data_8XPF
# 
_entry.id   8XPF 
# 
_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   8XPF         pdb_00008xpf 10.2210/pdb8xpf/pdb 
WWPDB D_1300043960 ?            ?                   
# 
_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       2025-01-15 
# 
_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                        8XPF 
_pdbx_database_status.recvd_initial_deposition_date   2024-01-03 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBJ 
_pdbx_database_status.process_site                    PDBJ 
_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              hmge@nju.edu.cn 
_pdbx_contact_author.name_first         Ge 
_pdbx_contact_author.name_last          Huiming 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-8241-0630 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Zhang, B.' 1 ? 
'Shi, J.'   2 ? 
'Zhang, Y.' 3 ? 
'Ge, H.M.'  4 ? 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   ? 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'To Be Published' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            0353 
_citation.journal_id_ISSN           ? 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     'Biosynthesis of Collinodins' 
_citation.year                      ? 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      ? 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Shi, J.'  1 ? 
primary 'Ge, H.M.' 2 ? 
# 
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 '2OG-Fe(II) oxygenase' 34838.051 1   ? ? ? ? 
2 polymer     syn 'small peptide'        1637.748  1   ? ? ? ? 
3 non-polymer syn '2-OXOGLUTARIC ACID'   146.098   1   ? ? ? ? 
4 non-polymer syn 'FE (III) ION'         55.845    2   ? ? ? ? 
5 water       nat water                  18.015    394 ? ? ? ? 
# 
loop_
_entity_poly.entity_id 
_entity_poly.type 
_entity_poly.nstd_linkage 
_entity_poly.nstd_monomer 
_entity_poly.pdbx_seq_one_letter_code 
_entity_poly.pdbx_seq_one_letter_code_can 
_entity_poly.pdbx_strand_id 
_entity_poly.pdbx_target_identifier 
1 'polypeptide(L)' no no 
;MDSKSIAAELATRGYALVPDFLTGDALTEAVAAIETYFPDPEADDSTADDVAALKHAVPFPFTSNALNRHPLDLRVISVV
EELLGTTDLRMTSSFIQAKYGTAYGESKDQRLHNDAWAASSLVHPRADGVYQRVYGILYLTDVTEDTAPTYVVDRAAHLG
VPLLTPEGTGAYSKEAYPELYERERPVVVSKGSLLLFVGDIVHRGSAYHGHLGRRLALFFNIHGAQARWTDKHLWSLRPA
HPDWGTFRDLMIELEPRQRHLLGFPPPGDDYWTEETIKHLSEMYPGIDVEPYLPARVASKLAAALEHHHHHH
;
;MDSKSIAAELATRGYALVPDFLTGDALTEAVAAIETYFPDPEADDSTADDVAALKHAVPFPFTSNALNRHPLDLRVISVV
EELLGTTDLRMTSSFIQAKYGTAYGESKDQRLHNDAWAASSLVHPRADGVYQRVYGILYLTDVTEDTAPTYVVDRAAHLG
VPLLTPEGTGAYSKEAYPELYERERPVVVSKGSLLLFVGDIVHRGSAYHGHLGRRLALFFNIHGAQARWTDKHLWSLRPA
HPDWGTFRDLMIELEPRQRHLLGFPPPGDDYWTEETIKHLSEMYPGIDVEPYLPARVASKLAAALEHHHHHH
;
A ? 
2 'polypeptide(L)' no no WYGWASNDGEGVAII WYGWASNDGEGVAII C ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
3 '2-OXOGLUTARIC ACID' AKG 
4 'FE (III) ION'       FE  
5 water                HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   ASP n 
1 3   SER n 
1 4   LYS n 
1 5   SER n 
1 6   ILE n 
1 7   ALA n 
1 8   ALA n 
1 9   GLU n 
1 10  LEU n 
1 11  ALA n 
1 12  THR n 
1 13  ARG n 
1 14  GLY n 
1 15  TYR n 
1 16  ALA n 
1 17  LEU n 
1 18  VAL n 
1 19  PRO n 
1 20  ASP n 
1 21  PHE n 
1 22  LEU n 
1 23  THR n 
1 24  GLY n 
1 25  ASP n 
1 26  ALA n 
1 27  LEU n 
1 28  THR n 
1 29  GLU n 
1 30  ALA n 
1 31  VAL n 
1 32  ALA n 
1 33  ALA n 
1 34  ILE n 
1 35  GLU n 
1 36  THR n 
1 37  TYR n 
1 38  PHE n 
1 39  PRO n 
1 40  ASP n 
1 41  PRO n 
1 42  GLU n 
1 43  ALA n 
1 44  ASP n 
1 45  ASP n 
1 46  SER n 
1 47  THR n 
1 48  ALA n 
1 49  ASP n 
1 50  ASP n 
1 51  VAL n 
1 52  ALA n 
1 53  ALA n 
1 54  LEU n 
1 55  LYS n 
1 56  HIS n 
1 57  ALA n 
1 58  VAL n 
1 59  PRO n 
1 60  PHE n 
1 61  PRO n 
1 62  PHE n 
1 63  THR n 
1 64  SER n 
1 65  ASN n 
1 66  ALA n 
1 67  LEU n 
1 68  ASN n 
1 69  ARG n 
1 70  HIS n 
1 71  PRO n 
1 72  LEU n 
1 73  ASP n 
1 74  LEU n 
1 75  ARG n 
1 76  VAL n 
1 77  ILE n 
1 78  SER n 
1 79  VAL n 
1 80  VAL n 
1 81  GLU n 
1 82  GLU n 
1 83  LEU n 
1 84  LEU n 
1 85  GLY n 
1 86  THR n 
1 87  THR n 
1 88  ASP n 
1 89  LEU n 
1 90  ARG n 
1 91  MET n 
1 92  THR n 
1 93  SER n 
1 94  SER n 
1 95  PHE n 
1 96  ILE n 
1 97  GLN n 
1 98  ALA n 
1 99  LYS n 
1 100 TYR n 
1 101 GLY n 
1 102 THR n 
1 103 ALA n 
1 104 TYR n 
1 105 GLY n 
1 106 GLU n 
1 107 SER n 
1 108 LYS n 
1 109 ASP n 
1 110 GLN n 
1 111 ARG n 
1 112 LEU n 
1 113 HIS n 
1 114 ASN n 
1 115 ASP n 
1 116 ALA n 
1 117 TRP n 
1 118 ALA n 
1 119 ALA n 
1 120 SER n 
1 121 SER n 
1 122 LEU n 
1 123 VAL n 
1 124 HIS n 
1 125 PRO n 
1 126 ARG n 
1 127 ALA n 
1 128 ASP n 
1 129 GLY n 
1 130 VAL n 
1 131 TYR n 
1 132 GLN n 
1 133 ARG n 
1 134 VAL n 
1 135 TYR n 
1 136 GLY n 
1 137 ILE n 
1 138 LEU n 
1 139 TYR n 
1 140 LEU n 
1 141 THR n 
1 142 ASP n 
1 143 VAL n 
1 144 THR n 
1 145 GLU n 
1 146 ASP n 
1 147 THR n 
1 148 ALA n 
1 149 PRO n 
1 150 THR n 
1 151 TYR n 
1 152 VAL n 
1 153 VAL n 
1 154 ASP n 
1 155 ARG n 
1 156 ALA n 
1 157 ALA n 
1 158 HIS n 
1 159 LEU n 
1 160 GLY n 
1 161 VAL n 
1 162 PRO n 
1 163 LEU n 
1 164 LEU n 
1 165 THR n 
1 166 PRO n 
1 167 GLU n 
1 168 GLY n 
1 169 THR n 
1 170 GLY n 
1 171 ALA n 
1 172 TYR n 
1 173 SER n 
1 174 LYS n 
1 175 GLU n 
1 176 ALA n 
1 177 TYR n 
1 178 PRO n 
1 179 GLU n 
1 180 LEU n 
1 181 TYR n 
1 182 GLU n 
1 183 ARG n 
1 184 GLU n 
1 185 ARG n 
1 186 PRO n 
1 187 VAL n 
1 188 VAL n 
1 189 VAL n 
1 190 SER n 
1 191 LYS n 
1 192 GLY n 
1 193 SER n 
1 194 LEU n 
1 195 LEU n 
1 196 LEU n 
1 197 PHE n 
1 198 VAL n 
1 199 GLY n 
1 200 ASP n 
1 201 ILE n 
1 202 VAL n 
1 203 HIS n 
1 204 ARG n 
1 205 GLY n 
1 206 SER n 
1 207 ALA n 
1 208 TYR n 
1 209 HIS n 
1 210 GLY n 
1 211 HIS n 
1 212 LEU n 
1 213 GLY n 
1 214 ARG n 
1 215 ARG n 
1 216 LEU n 
1 217 ALA n 
1 218 LEU n 
1 219 PHE n 
1 220 PHE n 
1 221 ASN n 
1 222 ILE n 
1 223 HIS n 
1 224 GLY n 
1 225 ALA n 
1 226 GLN n 
1 227 ALA n 
1 228 ARG n 
1 229 TRP n 
1 230 THR n 
1 231 ASP n 
1 232 LYS n 
1 233 HIS n 
1 234 LEU n 
1 235 TRP n 
1 236 SER n 
1 237 LEU n 
1 238 ARG n 
1 239 PRO n 
1 240 ALA n 
1 241 HIS n 
1 242 PRO n 
1 243 ASP n 
1 244 TRP n 
1 245 GLY n 
1 246 THR n 
1 247 PHE n 
1 248 ARG n 
1 249 ASP n 
1 250 LEU n 
1 251 MET n 
1 252 ILE n 
1 253 GLU n 
1 254 LEU n 
1 255 GLU n 
1 256 PRO n 
1 257 ARG n 
1 258 GLN n 
1 259 ARG n 
1 260 HIS n 
1 261 LEU n 
1 262 LEU n 
1 263 GLY n 
1 264 PHE n 
1 265 PRO n 
1 266 PRO n 
1 267 PRO n 
1 268 GLY n 
1 269 ASP n 
1 270 ASP n 
1 271 TYR n 
1 272 TRP n 
1 273 THR n 
1 274 GLU n 
1 275 GLU n 
1 276 THR n 
1 277 ILE n 
1 278 LYS n 
1 279 HIS n 
1 280 LEU n 
1 281 SER n 
1 282 GLU n 
1 283 MET n 
1 284 TYR n 
1 285 PRO n 
1 286 GLY n 
1 287 ILE n 
1 288 ASP n 
1 289 VAL n 
1 290 GLU n 
1 291 PRO n 
1 292 TYR n 
1 293 LEU n 
1 294 PRO n 
1 295 ALA n 
1 296 ARG n 
1 297 VAL n 
1 298 ALA n 
1 299 SER n 
1 300 LYS n 
1 301 LEU n 
1 302 ALA n 
1 303 ALA n 
1 304 ALA n 
1 305 LEU n 
1 306 GLU n 
1 307 HIS n 
1 308 HIS n 
1 309 HIS n 
1 310 HIS n 
1 311 HIS n 
1 312 HIS n 
2 1   TRP n 
2 2   TYR n 
2 3   GLY n 
2 4   TRP n 
2 5   ALA n 
2 6   SER n 
2 7   ASN n 
2 8   ASP n 
2 9   GLY n 
2 10  GLU n 
2 11  GLY n 
2 12  VAL n 
2 13  ALA n 
2 14  ILE n 
2 15  ILE 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                   312 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 ? 
_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      'Streptomyces collinus' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     42684 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      
;Escherichia coli 'BL21-Gold(DE3)pLysS AG'
;
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     866768 
_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                   ? 
# 
_pdbx_entity_src_syn.entity_id              2 
_pdbx_entity_src_syn.pdbx_src_id            1 
_pdbx_entity_src_syn.pdbx_alt_source_flag   sample 
_pdbx_entity_src_syn.pdbx_beg_seq_num       1 
_pdbx_entity_src_syn.pdbx_end_seq_num       15 
_pdbx_entity_src_syn.organism_scientific    'synthetic construct' 
_pdbx_entity_src_syn.organism_common_name   ? 
_pdbx_entity_src_syn.ncbi_taxonomy_id       32630 
_pdbx_entity_src_syn.details                ? 
# 
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 
AKG non-polymer         . '2-OXOGLUTARIC ACID' ? 'C5 H6 O5'       146.098 
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 
FE  non-polymer         . 'FE (III) ION'       ? 'Fe 3'           55.845  
GLN 'L-peptide linking' y GLUTAMINE            ? 'C5 H10 N2 O3'   146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'      ? 'C5 H9 N O4'     147.129 
GLY 'peptide linking'   y GLYCINE              ? 'C2 H5 N O2'     75.067  
HIS 'L-peptide linking' y HISTIDINE            ? 'C6 H10 N3 O2 1' 156.162 
HOH non-polymer         . WATER                ? 'H2 O'           18.015  
ILE 'L-peptide linking' y ISOLEUCINE           ? 'C6 H13 N O2'    131.173 
LEU 'L-peptide linking' y LEUCINE              ? 'C6 H13 N O2'    131.173 
LYS 'L-peptide linking' y LYSINE               ? 'C6 H15 N2 O2 1' 147.195 
MET 'L-peptide linking' y METHIONINE           ? 'C5 H11 N O2 S'  149.211 
PHE 'L-peptide linking' y PHENYLALANINE        ? 'C9 H11 N O2'    165.189 
PRO 'L-peptide linking' y PROLINE              ? 'C5 H9 N O2'     115.130 
SER 'L-peptide linking' y SERINE               ? 'C3 H7 N O3'     105.093 
THR 'L-peptide linking' y THREONINE            ? 'C4 H9 N O3'     119.119 
TRP 'L-peptide linking' y TRYPTOPHAN           ? 'C11 H12 N2 O2'  204.225 
TYR 'L-peptide linking' y TYROSINE             ? 'C9 H11 N O3'    181.189 
VAL 'L-peptide linking' y VALINE               ? 'C5 H11 N O2'    117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   MET 1   1   1   MET MET A . n 
A 1 2   ASP 2   2   2   ASP ASP A . n 
A 1 3   SER 3   3   3   SER SER A . n 
A 1 4   LYS 4   4   4   LYS LYS A . n 
A 1 5   SER 5   5   5   SER SER A . n 
A 1 6   ILE 6   6   6   ILE ILE A . n 
A 1 7   ALA 7   7   7   ALA ALA A . n 
A 1 8   ALA 8   8   8   ALA ALA A . n 
A 1 9   GLU 9   9   9   GLU GLU A . n 
A 1 10  LEU 10  10  10  LEU LEU A . n 
A 1 11  ALA 11  11  11  ALA ALA A . n 
A 1 12  THR 12  12  12  THR THR A . n 
A 1 13  ARG 13  13  13  ARG ARG A . n 
A 1 14  GLY 14  14  14  GLY GLY A . n 
A 1 15  TYR 15  15  15  TYR TYR A . n 
A 1 16  ALA 16  16  16  ALA ALA A . n 
A 1 17  LEU 17  17  17  LEU LEU A . n 
A 1 18  VAL 18  18  18  VAL VAL A . n 
A 1 19  PRO 19  19  19  PRO PRO A . n 
A 1 20  ASP 20  20  20  ASP ASP A . n 
A 1 21  PHE 21  21  21  PHE PHE A . n 
A 1 22  LEU 22  22  22  LEU LEU A . n 
A 1 23  THR 23  23  23  THR THR A . n 
A 1 24  GLY 24  24  24  GLY GLY A . n 
A 1 25  ASP 25  25  25  ASP ASP A . n 
A 1 26  ALA 26  26  26  ALA ALA A . n 
A 1 27  LEU 27  27  27  LEU LEU A . n 
A 1 28  THR 28  28  28  THR THR A . n 
A 1 29  GLU 29  29  29  GLU GLU A . n 
A 1 30  ALA 30  30  30  ALA ALA A . n 
A 1 31  VAL 31  31  31  VAL VAL A . n 
A 1 32  ALA 32  32  32  ALA ALA A . n 
A 1 33  ALA 33  33  33  ALA ALA A . n 
A 1 34  ILE 34  34  34  ILE ILE A . n 
A 1 35  GLU 35  35  35  GLU GLU A . n 
A 1 36  THR 36  36  36  THR THR A . n 
A 1 37  TYR 37  37  37  TYR TYR A . n 
A 1 38  PHE 38  38  38  PHE PHE A . n 
A 1 39  PRO 39  39  39  PRO PRO A . n 
A 1 40  ASP 40  40  40  ASP ASP A . n 
A 1 41  PRO 41  41  41  PRO PRO A . n 
A 1 42  GLU 42  42  42  GLU GLU A . n 
A 1 43  ALA 43  43  ?   ?   ?   A . n 
A 1 44  ASP 44  44  ?   ?   ?   A . n 
A 1 45  ASP 45  45  ?   ?   ?   A . n 
A 1 46  SER 46  46  ?   ?   ?   A . n 
A 1 47  THR 47  47  ?   ?   ?   A . n 
A 1 48  ALA 48  48  ?   ?   ?   A . n 
A 1 49  ASP 49  49  ?   ?   ?   A . n 
A 1 50  ASP 50  50  ?   ?   ?   A . n 
A 1 51  VAL 51  51  51  VAL VAL A . n 
A 1 52  ALA 52  52  52  ALA ALA A . n 
A 1 53  ALA 53  53  53  ALA ALA A . n 
A 1 54  LEU 54  54  54  LEU LEU A . n 
A 1 55  LYS 55  55  55  LYS LYS A . n 
A 1 56  HIS 56  56  56  HIS HIS A . n 
A 1 57  ALA 57  57  57  ALA ALA A . n 
A 1 58  VAL 58  58  58  VAL VAL A . n 
A 1 59  PRO 59  59  59  PRO PRO A . n 
A 1 60  PHE 60  60  60  PHE PHE A . n 
A 1 61  PRO 61  61  61  PRO PRO A . n 
A 1 62  PHE 62  62  62  PHE PHE A . n 
A 1 63  THR 63  63  63  THR THR A . n 
A 1 64  SER 64  64  64  SER SER A . n 
A 1 65  ASN 65  65  65  ASN ASN A . n 
A 1 66  ALA 66  66  66  ALA ALA A . n 
A 1 67  LEU 67  67  67  LEU LEU A . n 
A 1 68  ASN 68  68  68  ASN ASN A . n 
A 1 69  ARG 69  69  69  ARG ARG A . n 
A 1 70  HIS 70  70  70  HIS HIS A . n 
A 1 71  PRO 71  71  71  PRO PRO A . n 
A 1 72  LEU 72  72  72  LEU LEU A . n 
A 1 73  ASP 73  73  73  ASP ASP A . n 
A 1 74  LEU 74  74  74  LEU LEU A . n 
A 1 75  ARG 75  75  75  ARG ARG A . n 
A 1 76  VAL 76  76  76  VAL VAL A . n 
A 1 77  ILE 77  77  77  ILE ILE A . n 
A 1 78  SER 78  78  78  SER SER A . n 
A 1 79  VAL 79  79  79  VAL VAL A . n 
A 1 80  VAL 80  80  80  VAL VAL A . n 
A 1 81  GLU 81  81  81  GLU GLU A . n 
A 1 82  GLU 82  82  82  GLU GLU A . n 
A 1 83  LEU 83  83  83  LEU LEU A . n 
A 1 84  LEU 84  84  84  LEU LEU A . n 
A 1 85  GLY 85  85  85  GLY GLY A . n 
A 1 86  THR 86  86  86  THR THR A . n 
A 1 87  THR 87  87  87  THR THR A . n 
A 1 88  ASP 88  88  88  ASP ASP A . n 
A 1 89  LEU 89  89  89  LEU LEU A . n 
A 1 90  ARG 90  90  90  ARG ARG A . n 
A 1 91  MET 91  91  91  MET MET A . n 
A 1 92  THR 92  92  92  THR THR A . n 
A 1 93  SER 93  93  93  SER SER A . n 
A 1 94  SER 94  94  94  SER SER A . n 
A 1 95  PHE 95  95  95  PHE PHE A . n 
A 1 96  ILE 96  96  96  ILE ILE A . n 
A 1 97  GLN 97  97  97  GLN GLN A . n 
A 1 98  ALA 98  98  98  ALA ALA A . n 
A 1 99  LYS 99  99  99  LYS LYS A . n 
A 1 100 TYR 100 100 100 TYR TYR A . n 
A 1 101 GLY 101 101 101 GLY GLY A . n 
A 1 102 THR 102 102 102 THR THR A . n 
A 1 103 ALA 103 103 103 ALA ALA A . n 
A 1 104 TYR 104 104 104 TYR TYR A . n 
A 1 105 GLY 105 105 105 GLY GLY A . n 
A 1 106 GLU 106 106 106 GLU GLU A . n 
A 1 107 SER 107 107 107 SER SER A . n 
A 1 108 LYS 108 108 108 LYS LYS A . n 
A 1 109 ASP 109 109 109 ASP ASP A . n 
A 1 110 GLN 110 110 110 GLN GLN A . n 
A 1 111 ARG 111 111 111 ARG ARG A . n 
A 1 112 LEU 112 112 112 LEU LEU A . n 
A 1 113 HIS 113 113 113 HIS HIS A . n 
A 1 114 ASN 114 114 114 ASN ASN A . n 
A 1 115 ASP 115 115 115 ASP ASP A . n 
A 1 116 ALA 116 116 116 ALA ALA A . n 
A 1 117 TRP 117 117 117 TRP TRP A . n 
A 1 118 ALA 118 118 118 ALA ALA A . n 
A 1 119 ALA 119 119 119 ALA ALA A . n 
A 1 120 SER 120 120 120 SER SER A . n 
A 1 121 SER 121 121 121 SER SER A . n 
A 1 122 LEU 122 122 122 LEU LEU A . n 
A 1 123 VAL 123 123 123 VAL VAL A . n 
A 1 124 HIS 124 124 124 HIS HIS A . n 
A 1 125 PRO 125 125 125 PRO PRO A . n 
A 1 126 ARG 126 126 126 ARG ARG A . n 
A 1 127 ALA 127 127 127 ALA ALA A . n 
A 1 128 ASP 128 128 128 ASP ASP A . n 
A 1 129 GLY 129 129 129 GLY GLY A . n 
A 1 130 VAL 130 130 130 VAL VAL A . n 
A 1 131 TYR 131 131 131 TYR TYR A . n 
A 1 132 GLN 132 132 132 GLN GLN A . n 
A 1 133 ARG 133 133 133 ARG ARG A . n 
A 1 134 VAL 134 134 134 VAL VAL A . n 
A 1 135 TYR 135 135 135 TYR TYR A . n 
A 1 136 GLY 136 136 136 GLY GLY A . n 
A 1 137 ILE 137 137 137 ILE ILE A . n 
A 1 138 LEU 138 138 138 LEU LEU A . n 
A 1 139 TYR 139 139 139 TYR TYR A . n 
A 1 140 LEU 140 140 140 LEU LEU A . n 
A 1 141 THR 141 141 141 THR THR A . n 
A 1 142 ASP 142 142 142 ASP ASP A . n 
A 1 143 VAL 143 143 143 VAL VAL A . n 
A 1 144 THR 144 144 144 THR THR A . n 
A 1 145 GLU 145 145 145 GLU GLU A . n 
A 1 146 ASP 146 146 146 ASP ASP A . n 
A 1 147 THR 147 147 147 THR THR A . n 
A 1 148 ALA 148 148 148 ALA ALA A . n 
A 1 149 PRO 149 149 149 PRO PRO A . n 
A 1 150 THR 150 150 150 THR THR A . n 
A 1 151 TYR 151 151 151 TYR TYR A . n 
A 1 152 VAL 152 152 152 VAL VAL A . n 
A 1 153 VAL 153 153 153 VAL VAL A . n 
A 1 154 ASP 154 154 154 ASP ASP A . n 
A 1 155 ARG 155 155 155 ARG ARG A . n 
A 1 156 ALA 156 156 156 ALA ALA A . n 
A 1 157 ALA 157 157 157 ALA ALA A . n 
A 1 158 HIS 158 158 158 HIS HIS A . n 
A 1 159 LEU 159 159 159 LEU LEU A . n 
A 1 160 GLY 160 160 160 GLY GLY A . n 
A 1 161 VAL 161 161 161 VAL VAL A . n 
A 1 162 PRO 162 162 162 PRO PRO A . n 
A 1 163 LEU 163 163 163 LEU LEU A . n 
A 1 164 LEU 164 164 164 LEU LEU A . n 
A 1 165 THR 165 165 165 THR THR A . n 
A 1 166 PRO 166 166 166 PRO PRO A . n 
A 1 167 GLU 167 167 167 GLU GLU A . n 
A 1 168 GLY 168 168 168 GLY GLY A . n 
A 1 169 THR 169 169 169 THR THR A . n 
A 1 170 GLY 170 170 170 GLY GLY A . n 
A 1 171 ALA 171 171 171 ALA ALA A . n 
A 1 172 TYR 172 172 172 TYR TYR A . n 
A 1 173 SER 173 173 173 SER SER A . n 
A 1 174 LYS 174 174 174 LYS LYS A . n 
A 1 175 GLU 175 175 175 GLU GLU A . n 
A 1 176 ALA 176 176 176 ALA ALA A . n 
A 1 177 TYR 177 177 177 TYR TYR A . n 
A 1 178 PRO 178 178 178 PRO PRO A . n 
A 1 179 GLU 179 179 179 GLU GLU A . n 
A 1 180 LEU 180 180 180 LEU LEU A . n 
A 1 181 TYR 181 181 181 TYR TYR A . n 
A 1 182 GLU 182 182 182 GLU GLU A . n 
A 1 183 ARG 183 183 183 ARG ARG A . n 
A 1 184 GLU 184 184 184 GLU GLU A . n 
A 1 185 ARG 185 185 185 ARG ARG A . n 
A 1 186 PRO 186 186 186 PRO PRO A . n 
A 1 187 VAL 187 187 187 VAL VAL A . n 
A 1 188 VAL 188 188 188 VAL VAL A . n 
A 1 189 VAL 189 189 189 VAL VAL A . n 
A 1 190 SER 190 190 190 SER SER A . n 
A 1 191 LYS 191 191 191 LYS LYS A . n 
A 1 192 GLY 192 192 192 GLY GLY A . n 
A 1 193 SER 193 193 193 SER SER A . n 
A 1 194 LEU 194 194 194 LEU LEU A . n 
A 1 195 LEU 195 195 195 LEU LEU A . n 
A 1 196 LEU 196 196 196 LEU LEU A . n 
A 1 197 PHE 197 197 197 PHE PHE A . n 
A 1 198 VAL 198 198 198 VAL VAL A . n 
A 1 199 GLY 199 199 199 GLY GLY A . n 
A 1 200 ASP 200 200 200 ASP ASP A . n 
A 1 201 ILE 201 201 201 ILE ILE A . n 
A 1 202 VAL 202 202 202 VAL VAL A . n 
A 1 203 HIS 203 203 203 HIS HIS A . n 
A 1 204 ARG 204 204 204 ARG ARG A . n 
A 1 205 GLY 205 205 205 GLY GLY A . n 
A 1 206 SER 206 206 206 SER SER A . n 
A 1 207 ALA 207 207 207 ALA ALA A . n 
A 1 208 TYR 208 208 208 TYR TYR A . n 
A 1 209 HIS 209 209 209 HIS HIS A . n 
A 1 210 GLY 210 210 210 GLY GLY A . n 
A 1 211 HIS 211 211 211 HIS HIS A . n 
A 1 212 LEU 212 212 212 LEU LEU A . n 
A 1 213 GLY 213 213 213 GLY GLY A . n 
A 1 214 ARG 214 214 214 ARG ARG A . n 
A 1 215 ARG 215 215 215 ARG ARG A . n 
A 1 216 LEU 216 216 216 LEU LEU A . n 
A 1 217 ALA 217 217 217 ALA ALA A . n 
A 1 218 LEU 218 218 218 LEU LEU A . n 
A 1 219 PHE 219 219 219 PHE PHE A . n 
A 1 220 PHE 220 220 220 PHE PHE A . n 
A 1 221 ASN 221 221 221 ASN ASN A . n 
A 1 222 ILE 222 222 222 ILE ILE A . n 
A 1 223 HIS 223 223 223 HIS HIS A . n 
A 1 224 GLY 224 224 224 GLY GLY A . n 
A 1 225 ALA 225 225 225 ALA ALA A . n 
A 1 226 GLN 226 226 226 GLN GLN A . n 
A 1 227 ALA 227 227 227 ALA ALA A . n 
A 1 228 ARG 228 228 228 ARG ARG A . n 
A 1 229 TRP 229 229 229 TRP TRP A . n 
A 1 230 THR 230 230 230 THR THR A . n 
A 1 231 ASP 231 231 231 ASP ASP A . n 
A 1 232 LYS 232 232 232 LYS LYS A . n 
A 1 233 HIS 233 233 233 HIS HIS A . n 
A 1 234 LEU 234 234 234 LEU LEU A . n 
A 1 235 TRP 235 235 235 TRP TRP A . n 
A 1 236 SER 236 236 236 SER SER A . n 
A 1 237 LEU 237 237 237 LEU LEU A . n 
A 1 238 ARG 238 238 238 ARG ARG A . n 
A 1 239 PRO 239 239 239 PRO PRO A . n 
A 1 240 ALA 240 240 240 ALA ALA A . n 
A 1 241 HIS 241 241 241 HIS HIS A . n 
A 1 242 PRO 242 242 242 PRO PRO A . n 
A 1 243 ASP 243 243 243 ASP ASP A . n 
A 1 244 TRP 244 244 244 TRP TRP A . n 
A 1 245 GLY 245 245 245 GLY GLY A . n 
A 1 246 THR 246 246 246 THR THR A . n 
A 1 247 PHE 247 247 247 PHE PHE A . n 
A 1 248 ARG 248 248 248 ARG ARG A . n 
A 1 249 ASP 249 249 249 ASP ASP A . n 
A 1 250 LEU 250 250 250 LEU LEU A . n 
A 1 251 MET 251 251 251 MET MET A . n 
A 1 252 ILE 252 252 252 ILE ILE A . n 
A 1 253 GLU 253 253 253 GLU GLU A . n 
A 1 254 LEU 254 254 254 LEU LEU A . n 
A 1 255 GLU 255 255 255 GLU GLU A . n 
A 1 256 PRO 256 256 256 PRO PRO A . n 
A 1 257 ARG 257 257 257 ARG ARG A . n 
A 1 258 GLN 258 258 258 GLN GLN A . n 
A 1 259 ARG 259 259 259 ARG ARG A . n 
A 1 260 HIS 260 260 260 HIS HIS A . n 
A 1 261 LEU 261 261 261 LEU LEU A . n 
A 1 262 LEU 262 262 262 LEU LEU A . n 
A 1 263 GLY 263 263 263 GLY GLY A . n 
A 1 264 PHE 264 264 264 PHE PHE A . n 
A 1 265 PRO 265 265 265 PRO PRO A . n 
A 1 266 PRO 266 266 266 PRO PRO A . n 
A 1 267 PRO 267 267 267 PRO PRO A . n 
A 1 268 GLY 268 268 268 GLY GLY A . n 
A 1 269 ASP 269 269 269 ASP ASP A . n 
A 1 270 ASP 270 270 270 ASP ASP A . n 
A 1 271 TYR 271 271 271 TYR TYR A . n 
A 1 272 TRP 272 272 272 TRP TRP A . n 
A 1 273 THR 273 273 273 THR THR A . n 
A 1 274 GLU 274 274 274 GLU GLU A . n 
A 1 275 GLU 275 275 275 GLU GLU A . n 
A 1 276 THR 276 276 276 THR THR A . n 
A 1 277 ILE 277 277 277 ILE ILE A . n 
A 1 278 LYS 278 278 278 LYS LYS A . n 
A 1 279 HIS 279 279 279 HIS HIS A . n 
A 1 280 LEU 280 280 280 LEU LEU A . n 
A 1 281 SER 281 281 281 SER SER A . n 
A 1 282 GLU 282 282 282 GLU GLU A . n 
A 1 283 MET 283 283 283 MET MET A . n 
A 1 284 TYR 284 284 284 TYR TYR A . n 
A 1 285 PRO 285 285 285 PRO PRO A . n 
A 1 286 GLY 286 286 286 GLY GLY A . n 
A 1 287 ILE 287 287 287 ILE ILE A . n 
A 1 288 ASP 288 288 288 ASP ASP A . n 
A 1 289 VAL 289 289 289 VAL VAL A . n 
A 1 290 GLU 290 290 290 GLU GLU A . n 
A 1 291 PRO 291 291 291 PRO PRO A . n 
A 1 292 TYR 292 292 292 TYR TYR A . n 
A 1 293 LEU 293 293 293 LEU LEU A . n 
A 1 294 PRO 294 294 294 PRO PRO A . n 
A 1 295 ALA 295 295 ?   ?   ?   A . n 
A 1 296 ARG 296 296 ?   ?   ?   A . n 
A 1 297 VAL 297 297 ?   ?   ?   A . n 
A 1 298 ALA 298 298 ?   ?   ?   A . n 
A 1 299 SER 299 299 ?   ?   ?   A . n 
A 1 300 LYS 300 300 ?   ?   ?   A . n 
A 1 301 LEU 301 301 ?   ?   ?   A . n 
A 1 302 ALA 302 302 ?   ?   ?   A . n 
A 1 303 ALA 303 303 ?   ?   ?   A . n 
A 1 304 ALA 304 304 ?   ?   ?   A . n 
A 1 305 LEU 305 305 ?   ?   ?   A . n 
A 1 306 GLU 306 306 ?   ?   ?   A . n 
A 1 307 HIS 307 307 ?   ?   ?   A . n 
A 1 308 HIS 308 308 ?   ?   ?   A . n 
A 1 309 HIS 309 309 ?   ?   ?   A . n 
A 1 310 HIS 310 310 ?   ?   ?   A . n 
A 1 311 HIS 311 311 ?   ?   ?   A . n 
A 1 312 HIS 312 312 ?   ?   ?   A . n 
B 2 1   TRP 1   15  15  TRP TRP C . n 
B 2 2   TYR 2   16  16  TYR TYR C . n 
B 2 3   GLY 3   17  17  GLY GLY C . n 
B 2 4   TRP 4   18  18  TRP TRP C . n 
B 2 5   ALA 5   19  19  ALA ALA C . n 
B 2 6   SER 6   20  20  SER SER C . n 
B 2 7   ASN 7   21  21  ASN ASN C . n 
B 2 8   ASP 8   22  22  ASP ASP C . n 
B 2 9   GLY 9   23  23  GLY GLY C . n 
B 2 10  GLU 10  24  24  GLU GLU C . n 
B 2 11  GLY 11  25  25  GLY GLY C . n 
B 2 12  VAL 12  26  26  VAL VAL C . n 
B 2 13  ALA 13  27  27  ALA ALA C . n 
B 2 14  ILE 14  28  28  ILE ILE C . n 
B 2 15  ILE 15  29  29  ILE ILE C . 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 AKG ? ? AKG ? ? 'SUBJECT OF INVESTIGATION' ? 
2 FE  ? ? FE  ? ? 'SUBJECT OF INVESTIGATION' ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
C 3 AKG 1   401 401 AKG AKG A . 
D 4 FE  1   402 402 FE  FE  A . 
E 4 FE  1   403 403 FE  FE  A . 
F 5 HOH 1   501 503 HOH HOH A . 
F 5 HOH 2   502 501 HOH HOH A . 
F 5 HOH 3   503 502 HOH HOH A . 
F 5 HOH 4   504 507 HOH HOH A . 
F 5 HOH 5   505 505 HOH HOH A . 
F 5 HOH 6   506 570 HOH HOH A . 
F 5 HOH 7   507 506 HOH HOH A . 
F 5 HOH 8   508 509 HOH HOH A . 
F 5 HOH 9   509 508 HOH HOH A . 
F 5 HOH 10  510 510 HOH HOH A . 
F 5 HOH 11  511 512 HOH HOH A . 
F 5 HOH 12  512 504 HOH HOH A . 
F 5 HOH 13  513 595 HOH HOH A . 
F 5 HOH 14  514 515 HOH HOH A . 
F 5 HOH 15  515 520 HOH HOH A . 
F 5 HOH 16  516 523 HOH HOH A . 
F 5 HOH 17  517 533 HOH HOH A . 
F 5 HOH 18  518 555 HOH HOH A . 
F 5 HOH 19  519 592 HOH HOH A . 
F 5 HOH 20  520 541 HOH HOH A . 
F 5 HOH 21  521 571 HOH HOH A . 
F 5 HOH 22  522 553 HOH HOH A . 
F 5 HOH 23  523 536 HOH HOH A . 
F 5 HOH 24  524 540 HOH HOH A . 
F 5 HOH 25  525 527 HOH HOH A . 
F 5 HOH 26  526 529 HOH HOH A . 
F 5 HOH 27  527 519 HOH HOH A . 
F 5 HOH 28  528 618 HOH HOH A . 
F 5 HOH 29  529 538 HOH HOH A . 
F 5 HOH 30  530 521 HOH HOH A . 
F 5 HOH 31  531 518 HOH HOH A . 
F 5 HOH 32  532 544 HOH HOH A . 
F 5 HOH 33  533 581 HOH HOH A . 
F 5 HOH 34  534 603 HOH HOH A . 
F 5 HOH 35  535 590 HOH HOH A . 
F 5 HOH 36  536 517 HOH HOH A . 
F 5 HOH 37  537 543 HOH HOH A . 
F 5 HOH 38  538 597 HOH HOH A . 
F 5 HOH 39  539 651 HOH HOH A . 
F 5 HOH 40  540 530 HOH HOH A . 
F 5 HOH 41  541 516 HOH HOH A . 
F 5 HOH 42  542 577 HOH HOH A . 
F 5 HOH 43  543 524 HOH HOH A . 
F 5 HOH 44  544 537 HOH HOH A . 
F 5 HOH 45  545 549 HOH HOH A . 
F 5 HOH 46  546 551 HOH HOH A . 
F 5 HOH 47  547 525 HOH HOH A . 
F 5 HOH 48  548 526 HOH HOH A . 
F 5 HOH 49  549 602 HOH HOH A . 
F 5 HOH 50  550 545 HOH HOH A . 
F 5 HOH 51  551 572 HOH HOH A . 
F 5 HOH 52  552 562 HOH HOH A . 
F 5 HOH 53  553 646 HOH HOH A . 
F 5 HOH 54  554 534 HOH HOH A . 
F 5 HOH 55  555 563 HOH HOH A . 
F 5 HOH 56  556 688 HOH HOH A . 
F 5 HOH 57  557 567 HOH HOH A . 
F 5 HOH 58  558 569 HOH HOH A . 
F 5 HOH 59  559 539 HOH HOH A . 
F 5 HOH 60  560 542 HOH HOH A . 
F 5 HOH 61  561 547 HOH HOH A . 
F 5 HOH 62  562 634 HOH HOH A . 
F 5 HOH 63  563 556 HOH HOH A . 
F 5 HOH 64  564 558 HOH HOH A . 
F 5 HOH 65  565 535 HOH HOH A . 
F 5 HOH 66  566 557 HOH HOH A . 
F 5 HOH 67  567 103 HOH HOH A . 
F 5 HOH 68  568 588 HOH HOH A . 
F 5 HOH 69  569 531 HOH HOH A . 
F 5 HOH 70  570 548 HOH HOH A . 
F 5 HOH 71  571 565 HOH HOH A . 
F 5 HOH 72  572 589 HOH HOH A . 
F 5 HOH 73  573 636 HOH HOH A . 
F 5 HOH 74  574 532 HOH HOH A . 
F 5 HOH 75  575 599 HOH HOH A . 
F 5 HOH 76  576 522 HOH HOH A . 
F 5 HOH 77  577 511 HOH HOH A . 
F 5 HOH 78  578 578 HOH HOH A . 
F 5 HOH 79  579 598 HOH HOH A . 
F 5 HOH 80  580 514 HOH HOH A . 
F 5 HOH 81  581 513 HOH HOH A . 
F 5 HOH 82  582 586 HOH HOH A . 
F 5 HOH 83  583 584 HOH HOH A . 
F 5 HOH 84  584 604 HOH HOH A . 
F 5 HOH 85  585 559 HOH HOH A . 
F 5 HOH 86  586 579 HOH HOH A . 
F 5 HOH 87  587 587 HOH HOH A . 
F 5 HOH 88  588 528 HOH HOH A . 
F 5 HOH 89  589 561 HOH HOH A . 
F 5 HOH 90  590 594 HOH HOH A . 
F 5 HOH 91  591 568 HOH HOH A . 
F 5 HOH 92  592 573 HOH HOH A . 
F 5 HOH 93  593 576 HOH HOH A . 
F 5 HOH 94  594 606 HOH HOH A . 
F 5 HOH 95  595 640 HOH HOH A . 
F 5 HOH 96  596 733 HOH HOH A . 
F 5 HOH 97  597 583 HOH HOH A . 
F 5 HOH 98  598 614 HOH HOH A . 
F 5 HOH 99  599 585 HOH HOH A . 
F 5 HOH 100 600 605 HOH HOH A . 
F 5 HOH 101 601 560 HOH HOH A . 
F 5 HOH 102 602 591 HOH HOH A . 
F 5 HOH 103 603 574 HOH HOH A . 
F 5 HOH 104 604 582 HOH HOH A . 
F 5 HOH 105 605 609 HOH HOH A . 
F 5 HOH 106 606 697 HOH HOH A . 
F 5 HOH 107 607 575 HOH HOH A . 
F 5 HOH 108 608 739 HOH HOH A . 
F 5 HOH 109 609 610 HOH HOH A . 
F 5 HOH 110 610 639 HOH HOH A . 
F 5 HOH 111 611 617 HOH HOH A . 
F 5 HOH 112 612 743 HOH HOH A . 
F 5 HOH 113 613 608 HOH HOH A . 
F 5 HOH 114 614 593 HOH HOH A . 
F 5 HOH 115 615 616 HOH HOH A . 
F 5 HOH 116 616 620 HOH HOH A . 
F 5 HOH 117 617 550 HOH HOH A . 
F 5 HOH 118 618 601 HOH HOH A . 
F 5 HOH 119 619 566 HOH HOH A . 
F 5 HOH 120 620 596 HOH HOH A . 
F 5 HOH 121 621 580 HOH HOH A . 
F 5 HOH 122 622 619 HOH HOH A . 
F 5 HOH 123 623 546 HOH HOH A . 
F 5 HOH 124 624 600 HOH HOH A . 
F 5 HOH 125 625 650 HOH HOH A . 
F 5 HOH 126 626 655 HOH HOH A . 
F 5 HOH 127 627 564 HOH HOH A . 
F 5 HOH 128 628 631 HOH HOH A . 
F 5 HOH 129 629 662 HOH HOH A . 
F 5 HOH 130 630 661 HOH HOH A . 
F 5 HOH 131 631 613 HOH HOH A . 
F 5 HOH 132 632 611 HOH HOH A . 
F 5 HOH 133 633 623 HOH HOH A . 
F 5 HOH 134 634 625 HOH HOH A . 
F 5 HOH 135 635 694 HOH HOH A . 
F 5 HOH 136 636 632 HOH HOH A . 
F 5 HOH 137 637 626 HOH HOH A . 
F 5 HOH 138 638 629 HOH HOH A . 
F 5 HOH 139 639 638 HOH HOH A . 
F 5 HOH 140 640 627 HOH HOH A . 
F 5 HOH 141 641 552 HOH HOH A . 
F 5 HOH 142 642 630 HOH HOH A . 
F 5 HOH 143 643 633 HOH HOH A . 
F 5 HOH 144 644 621 HOH HOH A . 
F 5 HOH 145 645 624 HOH HOH A . 
F 5 HOH 146 646 635 HOH HOH A . 
F 5 HOH 147 647 649 HOH HOH A . 
F 5 HOH 148 648 607 HOH HOH A . 
F 5 HOH 149 649 653 HOH HOH A . 
F 5 HOH 150 650 644 HOH HOH A . 
F 5 HOH 151 651 643 HOH HOH A . 
F 5 HOH 152 652 656 HOH HOH A . 
F 5 HOH 153 653 622 HOH HOH A . 
F 5 HOH 154 654 705 HOH HOH A . 
F 5 HOH 155 655 652 HOH HOH A . 
F 5 HOH 156 656 637 HOH HOH A . 
F 5 HOH 157 657 642 HOH HOH A . 
F 5 HOH 158 658 641 HOH HOH A . 
F 5 HOH 159 659 685 HOH HOH A . 
F 5 HOH 160 660 680 HOH HOH A . 
F 5 HOH 161 661 699 HOH HOH A . 
F 5 HOH 162 662 696 HOH HOH A . 
F 5 HOH 163 663 660 HOH HOH A . 
F 5 HOH 164 664 691 HOH HOH A . 
F 5 HOH 165 665 654 HOH HOH A . 
F 5 HOH 166 666 647 HOH HOH A . 
F 5 HOH 167 667 704 HOH HOH A . 
F 5 HOH 168 668 615 HOH HOH A . 
F 5 HOH 169 669 692 HOH HOH A . 
F 5 HOH 170 670 668 HOH HOH A . 
F 5 HOH 171 671 684 HOH HOH A . 
F 5 HOH 172 672 663 HOH HOH A . 
F 5 HOH 173 673 678 HOH HOH A . 
F 5 HOH 174 674 706 HOH HOH A . 
F 5 HOH 175 675 693 HOH HOH A . 
F 5 HOH 176 676 713 HOH HOH A . 
F 5 HOH 177 677 762 HOH HOH A . 
F 5 HOH 178 678 667 HOH HOH A . 
F 5 HOH 179 679 671 HOH HOH A . 
F 5 HOH 180 680 720 HOH HOH A . 
F 5 HOH 181 681 645 HOH HOH A . 
F 5 HOH 182 682 687 HOH HOH A . 
F 5 HOH 183 683 665 HOH HOH A . 
F 5 HOH 184 684 670 HOH HOH A . 
F 5 HOH 185 685 676 HOH HOH A . 
F 5 HOH 186 686 648 HOH HOH A . 
F 5 HOH 187 687 664 HOH HOH A . 
F 5 HOH 188 688 681 HOH HOH A . 
F 5 HOH 189 689 659 HOH HOH A . 
F 5 HOH 190 690 672 HOH HOH A . 
F 5 HOH 191 691 675 HOH HOH A . 
F 5 HOH 192 692 716 HOH HOH A . 
F 5 HOH 193 693 723 HOH HOH A . 
F 5 HOH 194 694 695 HOH HOH A . 
F 5 HOH 195 695 708 HOH HOH A . 
F 5 HOH 196 696 682 HOH HOH A . 
F 5 HOH 197 697 718 HOH HOH A . 
F 5 HOH 198 698 658 HOH HOH A . 
F 5 HOH 199 699 554 HOH HOH A . 
F 5 HOH 200 700 709 HOH HOH A . 
F 5 HOH 201 701 755 HOH HOH A . 
F 5 HOH 202 702 683 HOH HOH A . 
F 5 HOH 203 703 677 HOH HOH A . 
F 5 HOH 204 704 740 HOH HOH A . 
F 5 HOH 205 705 673 HOH HOH A . 
F 5 HOH 206 706 698 HOH HOH A . 
F 5 HOH 207 707 746 HOH HOH A . 
F 5 HOH 208 708 674 HOH HOH A . 
F 5 HOH 209 709 722 HOH HOH A . 
F 5 HOH 210 710 679 HOH HOH A . 
F 5 HOH 211 711 669 HOH HOH A . 
F 5 HOH 212 712 689 HOH HOH A . 
F 5 HOH 213 713 702 HOH HOH A . 
F 5 HOH 214 714 612 HOH HOH A . 
F 5 HOH 215 715 666 HOH HOH A . 
F 5 HOH 216 716 710 HOH HOH A . 
F 5 HOH 217 717 750 HOH HOH A . 
F 5 HOH 218 718 690 HOH HOH A . 
F 5 HOH 219 719 628 HOH HOH A . 
F 5 HOH 220 720 703 HOH HOH A . 
F 5 HOH 221 721 712 HOH HOH A . 
F 5 HOH 222 722 700 HOH HOH A . 
F 5 HOH 223 723 707 HOH HOH A . 
F 5 HOH 224 724 756 HOH HOH A . 
F 5 HOH 225 725 741 HOH HOH A . 
F 5 HOH 226 726 715 HOH HOH A . 
F 5 HOH 227 727 734 HOH HOH A . 
F 5 HOH 228 728 714 HOH HOH A . 
F 5 HOH 229 729 701 HOH HOH A . 
F 5 HOH 230 730 717 HOH HOH A . 
F 5 HOH 231 731 657 HOH HOH A . 
F 5 HOH 232 732 711 HOH HOH A . 
F 5 HOH 233 733 735 HOH HOH A . 
F 5 HOH 234 734 727 HOH HOH A . 
F 5 HOH 235 735 719 HOH HOH A . 
F 5 HOH 236 736 729 HOH HOH A . 
F 5 HOH 237 737 742 HOH HOH A . 
F 5 HOH 238 738 104 HOH HOH A . 
F 5 HOH 239 739 745 HOH HOH A . 
F 5 HOH 240 740 725 HOH HOH A . 
F 5 HOH 241 741 728 HOH HOH A . 
F 5 HOH 242 742 724 HOH HOH A . 
F 5 HOH 243 743 726 HOH HOH A . 
F 5 HOH 244 744 747 HOH HOH A . 
F 5 HOH 245 745 686 HOH HOH A . 
F 5 HOH 246 746 759 HOH HOH A . 
F 5 HOH 247 747 766 HOH HOH A . 
F 5 HOH 248 748 736 HOH HOH A . 
F 5 HOH 249 749 778 HOH HOH A . 
F 5 HOH 250 750 748 HOH HOH A . 
F 5 HOH 251 751 730 HOH HOH A . 
F 5 HOH 252 752 737 HOH HOH A . 
F 5 HOH 253 753 753 HOH HOH A . 
F 5 HOH 254 754 754 HOH HOH A . 
F 5 HOH 255 755 752 HOH HOH A . 
F 5 HOH 256 756 795 HOH HOH A . 
F 5 HOH 257 757 761 HOH HOH A . 
F 5 HOH 258 758 738 HOH HOH A . 
F 5 HOH 259 759 751 HOH HOH A . 
F 5 HOH 260 760 763 HOH HOH A . 
F 5 HOH 261 761 757 HOH HOH A . 
F 5 HOH 262 762 758 HOH HOH A . 
F 5 HOH 263 763 731 HOH HOH A . 
F 5 HOH 264 764 744 HOH HOH A . 
F 5 HOH 265 765 765 HOH HOH A . 
F 5 HOH 266 766 770 HOH HOH A . 
F 5 HOH 267 767 721 HOH HOH A . 
F 5 HOH 268 768 764 HOH HOH A . 
F 5 HOH 269 769 782 HOH HOH A . 
F 5 HOH 270 770 772 HOH HOH A . 
F 5 HOH 271 771 767 HOH HOH A . 
F 5 HOH 272 772 774 HOH HOH A . 
F 5 HOH 273 773 768 HOH HOH A . 
F 5 HOH 274 774 807 HOH HOH A . 
F 5 HOH 275 775 760 HOH HOH A . 
F 5 HOH 276 776 749 HOH HOH A . 
F 5 HOH 277 777 769 HOH HOH A . 
F 5 HOH 278 778 775 HOH HOH A . 
F 5 HOH 279 779 777 HOH HOH A . 
F 5 HOH 280 780 771 HOH HOH A . 
F 5 HOH 281 781 773 HOH HOH A . 
F 5 HOH 282 782 776 HOH HOH A . 
F 5 HOH 283 783 784 HOH HOH A . 
F 5 HOH 284 784 780 HOH HOH A . 
F 5 HOH 285 785 779 HOH HOH A . 
F 5 HOH 286 786 799 HOH HOH A . 
F 5 HOH 287 787 785 HOH HOH A . 
F 5 HOH 288 788 790 HOH HOH A . 
F 5 HOH 289 789 787 HOH HOH A . 
F 5 HOH 290 790 788 HOH HOH A . 
F 5 HOH 291 791 789 HOH HOH A . 
F 5 HOH 292 792 797 HOH HOH A . 
F 5 HOH 293 793 791 HOH HOH A . 
F 5 HOH 294 794 786 HOH HOH A . 
F 5 HOH 295 795 794 HOH HOH A . 
F 5 HOH 296 796 802 HOH HOH A . 
F 5 HOH 297 797 809 HOH HOH A . 
F 5 HOH 298 798 804 HOH HOH A . 
F 5 HOH 299 799 798 HOH HOH A . 
F 5 HOH 300 800 783 HOH HOH A . 
F 5 HOH 301 801 801 HOH HOH A . 
F 5 HOH 302 802 806 HOH HOH A . 
F 5 HOH 303 803 796 HOH HOH A . 
F 5 HOH 304 804 808 HOH HOH A . 
F 5 HOH 305 805 803 HOH HOH A . 
F 5 HOH 306 806 815 HOH HOH A . 
F 5 HOH 307 807 800 HOH HOH A . 
F 5 HOH 308 808 781 HOH HOH A . 
F 5 HOH 309 809 828 HOH HOH A . 
F 5 HOH 310 810 812 HOH HOH A . 
F 5 HOH 311 811 814 HOH HOH A . 
F 5 HOH 312 812 829 HOH HOH A . 
F 5 HOH 313 813 792 HOH HOH A . 
F 5 HOH 314 814 810 HOH HOH A . 
F 5 HOH 315 815 813 HOH HOH A . 
F 5 HOH 316 816 819 HOH HOH A . 
F 5 HOH 317 817 817 HOH HOH A . 
F 5 HOH 318 818 820 HOH HOH A . 
F 5 HOH 319 819 805 HOH HOH A . 
F 5 HOH 320 820 826 HOH HOH A . 
F 5 HOH 321 821 825 HOH HOH A . 
F 5 HOH 322 822 827 HOH HOH A . 
F 5 HOH 323 823 824 HOH HOH A . 
F 5 HOH 324 824 854 HOH HOH A . 
F 5 HOH 325 825 821 HOH HOH A . 
F 5 HOH 326 826 111 HOH HOH A . 
F 5 HOH 327 827 811 HOH HOH A . 
F 5 HOH 328 828 832 HOH HOH A . 
F 5 HOH 329 829 818 HOH HOH A . 
F 5 HOH 330 830 831 HOH HOH A . 
F 5 HOH 331 831 823 HOH HOH A . 
F 5 HOH 332 832 793 HOH HOH A . 
F 5 HOH 333 833 834 HOH HOH A . 
F 5 HOH 334 834 837 HOH HOH A . 
F 5 HOH 335 835 836 HOH HOH A . 
F 5 HOH 336 836 841 HOH HOH A . 
F 5 HOH 337 837 848 HOH HOH A . 
F 5 HOH 338 838 838 HOH HOH A . 
F 5 HOH 339 839 822 HOH HOH A . 
F 5 HOH 340 840 840 HOH HOH A . 
F 5 HOH 341 841 835 HOH HOH A . 
F 5 HOH 342 842 844 HOH HOH A . 
F 5 HOH 343 843 816 HOH HOH A . 
F 5 HOH 344 844 842 HOH HOH A . 
F 5 HOH 345 845 847 HOH HOH A . 
F 5 HOH 346 846 845 HOH HOH A . 
F 5 HOH 347 847 833 HOH HOH A . 
F 5 HOH 348 848 850 HOH HOH A . 
F 5 HOH 349 849 839 HOH HOH A . 
F 5 HOH 350 850 843 HOH HOH A . 
F 5 HOH 351 851 852 HOH HOH A . 
F 5 HOH 352 852 849 HOH HOH A . 
F 5 HOH 353 853 851 HOH HOH A . 
F 5 HOH 354 854 830 HOH HOH A . 
F 5 HOH 355 855 853 HOH HOH A . 
F 5 HOH 356 856 856 HOH HOH A . 
F 5 HOH 357 857 858 HOH HOH A . 
F 5 HOH 358 858 857 HOH HOH A . 
F 5 HOH 359 859 855 HOH HOH A . 
F 5 HOH 360 860 846 HOH HOH A . 
F 5 HOH 361 861 869 HOH HOH A . 
F 5 HOH 362 862 864 HOH HOH A . 
F 5 HOH 363 863 859 HOH HOH A . 
F 5 HOH 364 864 860 HOH HOH A . 
F 5 HOH 365 865 865 HOH HOH A . 
F 5 HOH 366 866 863 HOH HOH A . 
F 5 HOH 367 867 866 HOH HOH A . 
F 5 HOH 368 868 862 HOH HOH A . 
F 5 HOH 369 869 861 HOH HOH A . 
F 5 HOH 370 870 868 HOH HOH A . 
F 5 HOH 371 871 867 HOH HOH A . 
F 5 HOH 372 872 872 HOH HOH A . 
F 5 HOH 373 873 870 HOH HOH A . 
F 5 HOH 374 874 871 HOH HOH A . 
F 5 HOH 375 875 873 HOH HOH A . 
F 5 HOH 376 876 875 HOH HOH A . 
F 5 HOH 377 877 874 HOH HOH A . 
F 5 HOH 378 878 876 HOH HOH A . 
G 5 HOH 1   101 107 HOH HOH C . 
G 5 HOH 2   102 101 HOH HOH C . 
G 5 HOH 3   103 102 HOH HOH C . 
G 5 HOH 4   104 105 HOH HOH C . 
G 5 HOH 5   105 732 HOH HOH C . 
G 5 HOH 6   106 109 HOH HOH C . 
G 5 HOH 7   107 106 HOH HOH C . 
G 5 HOH 8   108 110 HOH HOH C . 
G 5 HOH 9   109 114 HOH HOH C . 
G 5 HOH 10  110 112 HOH HOH C . 
G 5 HOH 11  111 113 HOH HOH C . 
G 5 HOH 12  112 116 HOH HOH C . 
G 5 HOH 13  113 115 HOH HOH C . 
G 5 HOH 14  114 117 HOH HOH C . 
G 5 HOH 15  115 118 HOH HOH C . 
G 5 HOH 16  116 108 HOH HOH C . 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX   ? ? ? '(1.20.1_4487: ???)' 1 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? XDS      ? ? ? .                    2 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? autoPROC ? ? ? .                    3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER   ? ? ? .                    4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   112.60 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     8XPF 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     121.363 
_cell.length_a_esd                 ? 
_cell.length_b                     61.010 
_cell.length_b_esd                 ? 
_cell.length_c                     56.346 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        4 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         8XPF 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                5 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'C 1 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                   8XPF 
_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             2.83 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          56.51 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              ? 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '0.01 M Cobalt (II) chloride hexahydrate, 0.1 M MES monohydrate pH 6.5, 1.8 M Ammonium sulfate' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            291.1500 
# 
_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         2022-09-02 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.97918 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'SSRF BEAMLINE BL10U2' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.97918 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   BL10U2 
_diffrn_source.pdbx_synchrotron_site       SSRF 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       8XPF 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.5 
_reflns.d_resolution_low                               53.58 
_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                                     58994 
_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                           96.5 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                4.1 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          13.7 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                ? 
_reflns.pdbx_Rpim_I_all                                ? 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   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                                    1.50 
_reflns_shell.d_res_low                                     1.58 
_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                             8822 
_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                                  0.64 
_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                                 8XPF 
_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                            1.50 
_refine.ls_d_res_low                             48.54 
_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                     58760 
_refine.ls_number_reflns_R_free                  2819 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    96.05 
_refine.ls_percent_reflns_R_free                 4.80 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1659 
_refine.ls_R_factor_R_free                       0.1838 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1650 
_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                          1.33 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       ML 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.10 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.90 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 18.61 
_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                            0.14 
_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                       1.50 
_refine_hist.d_res_low                        48.54 
_refine_hist.number_atoms_solvent             394 
_refine_hist.number_atoms_total               2787 
_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        2381 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         12 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.005  ? 2468 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.826  ? 3370 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 12.534 ? 881  ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.080  ? 364  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.008  ? 437  ? 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' 1.50 1.52  . . 143 2802 95.00  . . . . 0.2935 . . . . . . . . . . . 0.3206 
'X-RAY DIFFRACTION' 1.52 1.55  . . 149 2767 98.00  . . . . 0.2505 . . . . . . . . . . . 0.2574 
'X-RAY DIFFRACTION' 1.55 1.58  . . 145 2916 100.00 . . . . 0.1957 . . . . . . . . . . . 0.2145 
'X-RAY DIFFRACTION' 1.58 1.61  . . 146 2875 100.00 . . . . 0.1788 . . . . . . . . . . . 0.2149 
'X-RAY DIFFRACTION' 1.61 1.65  . . 146 2907 100.00 . . . . 0.1696 . . . . . . . . . . . 0.1917 
'X-RAY DIFFRACTION' 1.65 1.69  . . 146 2882 100.00 . . . . 0.1634 . . . . . . . . . . . 0.2090 
'X-RAY DIFFRACTION' 1.69 1.73  . . 149 2918 100.00 . . . . 0.1609 . . . . . . . . . . . 0.2180 
'X-RAY DIFFRACTION' 1.73 1.78  . . 136 2878 100.00 . . . . 0.1563 . . . . . . . . . . . 0.1687 
'X-RAY DIFFRACTION' 1.78 1.83  . . 129 2926 100.00 . . . . 0.1601 . . . . . . . . . . . 0.1713 
'X-RAY DIFFRACTION' 1.83 1.89  . . 149 2893 99.00  . . . . 0.1674 . . . . . . . . . . . 0.2092 
'X-RAY DIFFRACTION' 1.89 1.95  . . 117 2105 74.00  . . . . 0.1891 . . . . . . . . . . . 0.2003 
'X-RAY DIFFRACTION' 1.95 2.03  . . 146 2930 100.00 . . . . 0.1608 . . . . . . . . . . . 0.1695 
'X-RAY DIFFRACTION' 2.03 2.12  . . 165 2842 99.00  . . . . 0.1552 . . . . . . . . . . . 0.1967 
'X-RAY DIFFRACTION' 2.12 2.24  . . 164 2830 99.00  . . . . 0.1578 . . . . . . . . . . . 0.1796 
'X-RAY DIFFRACTION' 2.24 2.38  . . 118 2250 77.00  . . . . 0.1611 . . . . . . . . . . . 0.1724 
'X-RAY DIFFRACTION' 2.38 2.56  . . 111 2944 100.00 . . . . 0.1635 . . . . . . . . . . . 0.2011 
'X-RAY DIFFRACTION' 2.56 2.82  . . 125 2912 99.00  . . . . 0.1764 . . . . . . . . . . . 0.1971 
'X-RAY DIFFRACTION' 2.82 3.23  . . 163 2873 99.00  . . . . 0.1688 . . . . . . . . . . . 0.1721 
'X-RAY DIFFRACTION' 3.23 4.06  . . 142 2634 89.00  . . . . 0.1518 . . . . . . . . . . . 0.1710 
'X-RAY DIFFRACTION' 4.06 48.54 . . 130 2857 95.00  . . . . 0.1588 . . . . . . . . . . . 0.1701 
# 
_struct.entry_id                     8XPF 
_struct.title                        '2OG-Fe(II) oxygenase-ColD in complex with collinodins' 
_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        8XPF 
_struct_keywords.text            'Oxidase, METAL BINDING PROTEIN' 
_struct_keywords.pdbx_keywords   'METAL BINDING PROTEIN' 
# 
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 4 ? 
F N N 5 ? 
G N N 5 ? 
# 
loop_
_struct_ref.id 
_struct_ref.db_name 
_struct_ref.db_code 
_struct_ref.pdbx_db_accession 
_struct_ref.pdbx_db_isoform 
_struct_ref.entity_id 
_struct_ref.pdbx_seq_one_letter_code 
_struct_ref.pdbx_align_begin 
1 PDB 8XPF 8XPF ? 1 ? 1 
2 PDB 8XPF 8XPF ? 2 ? 1 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 8XPF A 1 ? 312 ? 8XPF 1  ? 312 ? 1  312 
2 2 8XPF C 1 ? 15  ? 8XPF 15 ? 29  ? 15 29  
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   tetrameric 
_pdbx_struct_assembly.oligomeric_count     4 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 6440  ? 
1 MORE         -44   ? 
1 'SSA (A^2)'  24060 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1,2 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G 
# 
_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 1.0  0.0 0.0 0.0 0.0 1.0 0.0 0.0 0.0 0.0 1.0  0.0 
2 'point symmetry operation' ?     ?     -1.0 0.0 0.0 0.0 0.0 1.0 0.0 0.0 0.0 0.0 -1.0 0.0 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 ASP A 2   ? GLY A 14  ? ASP A 2   GLY A 14  1 ? 13 
HELX_P HELX_P2  AA2 THR A 23  ? PHE A 38  ? THR A 23  PHE A 38  1 ? 16 
HELX_P HELX_P3  AA3 ALA A 52  ? HIS A 56  ? ALA A 52  HIS A 56  5 ? 5  
HELX_P HELX_P4  AA4 SER A 64  ? ARG A 69  ? SER A 64  ARG A 69  1 ? 6  
HELX_P HELX_P5  AA5 HIS A 70  ? LEU A 72  ? HIS A 70  LEU A 72  5 ? 3  
HELX_P HELX_P6  AA6 ASP A 73  ? GLY A 85  ? ASP A 73  GLY A 85  1 ? 13 
HELX_P HELX_P7  AA7 THR A 102 ? GLY A 105 ? THR A 102 GLY A 105 5 ? 4  
HELX_P HELX_P8  AA8 ASP A 128 ? GLN A 132 ? ASP A 128 GLN A 132 5 ? 5  
HELX_P HELX_P9  AA9 ALA A 156 ? GLY A 160 ? ALA A 156 GLY A 160 1 ? 5  
HELX_P HELX_P10 AB1 TYR A 177 ? GLU A 184 ? TYR A 177 GLU A 184 1 ? 8  
HELX_P HELX_P11 AB2 ASP A 243 ? LEU A 254 ? ASP A 243 LEU A 254 1 ? 12 
HELX_P HELX_P12 AB3 GLU A 255 ? HIS A 260 ? GLU A 255 HIS A 260 1 ? 6  
HELX_P HELX_P13 AB4 LEU A 261 ? GLY A 263 ? LEU A 261 GLY A 263 5 ? 3  
HELX_P HELX_P14 AB5 THR A 273 ? TYR A 284 ? THR A 273 TYR A 284 1 ? 12 
HELX_P HELX_P15 AB6 VAL A 289 ? LEU A 293 ? VAL A 289 LEU A 293 5 ? 5  
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
covale1 covale one ? B TRP 1   N   ? ? ? 1_555 B ASP 8 CG ? ? C TRP 15  C ASP 22  1_555 ? ? ? ? ? ? ? 1.460 ? ? 
metalc1 metalc ?   ? A HIS 113 NE2 ? ? ? 1_555 D FE  . FE ? ? A HIS 113 A FE  402 1_555 ? ? ? ? ? ? ? 2.175 ? ? 
metalc2 metalc ?   ? A ASP 115 OD2 ? ? ? 1_555 D FE  . FE ? ? A ASP 115 A FE  402 1_555 ? ? ? ? ? ? ? 1.980 ? ? 
metalc3 metalc ?   ? A ASP 146 OD1 ? ? ? 1_555 E FE  . FE ? ? A ASP 146 A FE  403 4_545 ? ? ? ? ? ? ? 2.017 ? ? 
metalc4 metalc ?   ? A HIS 158 NE2 ? ? ? 1_555 E FE  . FE ? ? A HIS 158 A FE  403 1_555 ? ? ? ? ? ? ? 2.038 ? ? 
metalc5 metalc ?   ? A HIS 203 NE2 ? ? ? 1_555 D FE  . FE ? ? A HIS 203 A FE  402 1_555 ? ? ? ? ? ? ? 2.148 ? ? 
metalc6 metalc ?   ? A HIS 209 ND1 ? ? ? 1_555 E FE  . FE ? ? A HIS 209 A FE  403 4_545 ? ? ? ? ? ? ? 2.192 ? ? 
metalc7 metalc ?   ? C AKG .   O1  ? ? ? 1_555 D FE  . FE ? ? A AKG 401 A FE  402 1_555 ? ? ? ? ? ? ? 2.173 ? ? 
metalc8 metalc ?   ? C AKG .   O5  ? ? ? 1_555 D FE  . FE ? ? A AKG 401 A FE  402 1_555 ? ? ? ? ? ? ? 2.148 ? ? 
# 
loop_
_struct_conn_type.id 
_struct_conn_type.criteria 
_struct_conn_type.reference 
covale ? ? 
metalc ? ? 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1  NE2 ? A HIS 113 ? A HIS 113 ? 1_555 FE ? D FE . ? A FE 402 ? 1_555 OD2 ? A ASP 115 ? A ASP 115 ? 1_555 94.9  ? 
2  NE2 ? A HIS 113 ? A HIS 113 ? 1_555 FE ? D FE . ? A FE 402 ? 1_555 NE2 ? A HIS 203 ? A HIS 203 ? 1_555 90.1  ? 
3  OD2 ? A ASP 115 ? A ASP 115 ? 1_555 FE ? D FE . ? A FE 402 ? 1_555 NE2 ? A HIS 203 ? A HIS 203 ? 1_555 83.1  ? 
4  NE2 ? A HIS 113 ? A HIS 113 ? 1_555 FE ? D FE . ? A FE 402 ? 1_555 O1  ? C AKG .   ? A AKG 401 ? 1_555 171.7 ? 
5  OD2 ? A ASP 115 ? A ASP 115 ? 1_555 FE ? D FE . ? A FE 402 ? 1_555 O1  ? C AKG .   ? A AKG 401 ? 1_555 91.7  ? 
6  NE2 ? A HIS 203 ? A HIS 203 ? 1_555 FE ? D FE . ? A FE 402 ? 1_555 O1  ? C AKG .   ? A AKG 401 ? 1_555 95.7  ? 
7  NE2 ? A HIS 113 ? A HIS 113 ? 1_555 FE ? D FE . ? A FE 402 ? 1_555 O5  ? C AKG .   ? A AKG 401 ? 1_555 93.9  ? 
8  OD2 ? A ASP 115 ? A ASP 115 ? 1_555 FE ? D FE . ? A FE 402 ? 1_555 O5  ? C AKG .   ? A AKG 401 ? 1_555 170.6 ? 
9  NE2 ? A HIS 203 ? A HIS 203 ? 1_555 FE ? D FE . ? A FE 402 ? 1_555 O5  ? C AKG .   ? A AKG 401 ? 1_555 93.6  ? 
10 O1  ? C AKG .   ? A AKG 401 ? 1_555 FE ? D FE . ? A FE 402 ? 1_555 O5  ? C AKG .   ? A AKG 401 ? 1_555 79.8  ? 
11 OD1 ? A ASP 146 ? A ASP 146 ? 1_555 FE ? E FE . ? A FE 403 ? 4_545 NE2 ? A HIS 158 ? A HIS 158 ? 1_555 91.3  ? 
12 OD1 ? A ASP 146 ? A ASP 146 ? 1_555 FE ? E FE . ? A FE 403 ? 4_545 ND1 ? A HIS 209 ? A HIS 209 ? 1_555 90.6  ? 
13 NE2 ? A HIS 158 ? A HIS 158 ? 1_555 FE ? E FE . ? A FE 403 ? 4_545 ND1 ? A HIS 209 ? A HIS 209 ? 1_555 65.7  ? 
# 
_pdbx_modification_feature.ordinal                            1 
_pdbx_modification_feature.label_comp_id                      TRP 
_pdbx_modification_feature.label_asym_id                      B 
_pdbx_modification_feature.label_seq_id                       1 
_pdbx_modification_feature.label_alt_id                       ? 
_pdbx_modification_feature.modified_residue_label_comp_id     ASP 
_pdbx_modification_feature.modified_residue_label_asym_id     B 
_pdbx_modification_feature.modified_residue_label_seq_id      8 
_pdbx_modification_feature.modified_residue_label_alt_id      ? 
_pdbx_modification_feature.auth_comp_id                       TRP 
_pdbx_modification_feature.auth_asym_id                       C 
_pdbx_modification_feature.auth_seq_id                        15 
_pdbx_modification_feature.PDB_ins_code                       ? 
_pdbx_modification_feature.symmetry                           1_555 
_pdbx_modification_feature.modified_residue_auth_comp_id      ASP 
_pdbx_modification_feature.modified_residue_auth_asym_id      C 
_pdbx_modification_feature.modified_residue_auth_seq_id       22 
_pdbx_modification_feature.modified_residue_PDB_ins_code      ? 
_pdbx_modification_feature.modified_residue_symmetry          1_555 
_pdbx_modification_feature.comp_id_linking_atom               N 
_pdbx_modification_feature.modified_residue_id_linking_atom   CG 
_pdbx_modification_feature.modified_residue_id                . 
_pdbx_modification_feature.ref_pcm_id                         . 
_pdbx_modification_feature.ref_comp_id                        . 
_pdbx_modification_feature.type                               None 
_pdbx_modification_feature.category                           'Isopeptide bond' 
# 
_struct_mon_prot_cis.pdbx_id                1 
_struct_mon_prot_cis.label_comp_id          PHE 
_struct_mon_prot_cis.label_seq_id           60 
_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            60 
_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    61 
_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     61 
_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       2.27 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 6 ? 
AA2 ? 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 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA1 3 4 ? anti-parallel 
AA1 4 5 ? anti-parallel 
AA1 5 6 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA2 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 TYR A 15  ? VAL A 18  ? TYR A 15  VAL A 18  
AA1 2 LEU A 194 ? VAL A 198 ? LEU A 194 VAL A 198 
AA1 3 VAL A 134 ? TYR A 139 ? VAL A 134 TYR A 139 
AA1 4 ARG A 214 ? GLY A 224 ? ARG A 214 GLY A 224 
AA1 5 LEU A 89  ? TYR A 100 ? LEU A 89  TYR A 100 
AA1 6 VAL A 58  ? PRO A 59  ? VAL A 58  PRO A 59  
AA2 1 ARG A 185 ? VAL A 187 ? ARG A 185 VAL A 187 
AA2 2 THR A 150 ? ARG A 155 ? THR A 150 ARG A 155 
AA2 3 ILE A 201 ? ARG A 204 ? ILE A 201 ARG A 204 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N VAL A 18  ? N VAL A 18  O LEU A 194 ? O LEU A 194 
AA1 2 3 O PHE A 197 ? O PHE A 197 N TYR A 135 ? N TYR A 135 
AA1 3 4 N LEU A 138 ? N LEU A 138 O LEU A 218 ? O LEU A 218 
AA1 4 5 O PHE A 219 ? O PHE A 219 N PHE A 95  ? N PHE A 95  
AA1 5 6 O ILE A 96  ? O ILE A 96  N VAL A 58  ? N VAL A 58  
AA2 1 2 O VAL A 187 ? O VAL A 187 N THR A 150 ? N THR A 150 
AA2 2 3 N TYR A 151 ? N TYR A 151 O ARG A 204 ? O ARG A 204 
# 
_pdbx_entry_details.entry_id                   8XPF 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   Y 
# 
loop_
_pdbx_validate_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 769 ? ? O A HOH 853 ? ? 1.94 
2  1 O   A HOH 735 ? ? O A HOH 796 ? ? 1.99 
3  1 OG  A SER 190 ? ? O A HOH 501 ? ? 2.01 
4  1 O   A HOH 724 ? ? O A HOH 792 ? ? 2.02 
5  1 FE  A FE  403 ? ? O A HOH 540 ? ? 2.05 
6  1 O   A HOH 832 ? ? O A HOH 873 ? ? 2.07 
7  1 O   A HOH 711 ? ? O A HOH 849 ? ? 2.07 
8  1 O   A HOH 839 ? ? O A HOH 862 ? ? 2.08 
9  1 FE  A FE  402 ? ? O A HOH 665 ? ? 2.12 
10 1 OE1 A GLU 255 ? ? O A HOH 502 ? ? 2.13 
11 1 O   A HOH 580 ? ? O A HOH 789 ? ? 2.17 
# 
loop_
_pdbx_validate_symm_contact.id 
_pdbx_validate_symm_contact.PDB_model_num 
_pdbx_validate_symm_contact.auth_atom_id_1 
_pdbx_validate_symm_contact.auth_asym_id_1 
_pdbx_validate_symm_contact.auth_comp_id_1 
_pdbx_validate_symm_contact.auth_seq_id_1 
_pdbx_validate_symm_contact.PDB_ins_code_1 
_pdbx_validate_symm_contact.label_alt_id_1 
_pdbx_validate_symm_contact.site_symmetry_1 
_pdbx_validate_symm_contact.auth_atom_id_2 
_pdbx_validate_symm_contact.auth_asym_id_2 
_pdbx_validate_symm_contact.auth_comp_id_2 
_pdbx_validate_symm_contact.auth_seq_id_2 
_pdbx_validate_symm_contact.PDB_ins_code_2 
_pdbx_validate_symm_contact.label_alt_id_2 
_pdbx_validate_symm_contact.site_symmetry_2 
_pdbx_validate_symm_contact.dist 
1 1 FE A FE  403 ? ? 1_555 O A HOH 542 ? ? 4_555 1.88 
2 1 FE A FE  403 ? ? 1_555 O A HOH 623 ? ? 4_555 2.17 
3 1 O  A HOH 743 ? ? 1_555 O C HOH 109 ? ? 2_555 2.18 
# 
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 VAL A 153 ? ? -117.90 -86.61  
2 1 TRP C 18  ? ? -141.46 -5.90   
3 1 SER C 20  ? ? 61.87   -142.02 
4 1 GLU C 24  ? ? -126.74 -69.86  
# 
_pdbx_refine_tls.id               1 
_pdbx_refine_tls.pdbx_refine_id   'X-RAY DIFFRACTION' 
_pdbx_refine_tls.details          ? 
_pdbx_refine_tls.method           refined 
_pdbx_refine_tls.origin_x         12.9894 
_pdbx_refine_tls.origin_y         -10.2364 
_pdbx_refine_tls.origin_z         6.8799 
_pdbx_refine_tls.T[1][1]          0.1448 
_pdbx_refine_tls.T[1][1]_esd      ? 
_pdbx_refine_tls.T[1][2]          -0.0103 
_pdbx_refine_tls.T[1][2]_esd      ? 
_pdbx_refine_tls.T[1][3]          -0.0168 
_pdbx_refine_tls.T[1][3]_esd      ? 
_pdbx_refine_tls.T[2][2]          0.1572 
_pdbx_refine_tls.T[2][2]_esd      ? 
_pdbx_refine_tls.T[2][3]          -0.0119 
_pdbx_refine_tls.T[2][3]_esd      ? 
_pdbx_refine_tls.T[3][3]          0.1409 
_pdbx_refine_tls.T[3][3]_esd      ? 
_pdbx_refine_tls.L[1][1]          1.8037 
_pdbx_refine_tls.L[1][1]_esd      ? 
_pdbx_refine_tls.L[1][2]          -0.2661 
_pdbx_refine_tls.L[1][2]_esd      ? 
_pdbx_refine_tls.L[1][3]          -0.5880 
_pdbx_refine_tls.L[1][3]_esd      ? 
_pdbx_refine_tls.L[2][2]          0.6809 
_pdbx_refine_tls.L[2][2]_esd      ? 
_pdbx_refine_tls.L[2][3]          0.0378 
_pdbx_refine_tls.L[2][3]_esd      ? 
_pdbx_refine_tls.L[3][3]          1.1679 
_pdbx_refine_tls.L[3][3]_esd      ? 
_pdbx_refine_tls.S[1][1]          -0.0492 
_pdbx_refine_tls.S[1][1]_esd      ? 
_pdbx_refine_tls.S[1][2]          -0.2331 
_pdbx_refine_tls.S[1][2]_esd      ? 
_pdbx_refine_tls.S[1][3]          -0.0857 
_pdbx_refine_tls.S[1][3]_esd      ? 
_pdbx_refine_tls.S[2][1]          0.0473 
_pdbx_refine_tls.S[2][1]_esd      ? 
_pdbx_refine_tls.S[2][2]          0.0411 
_pdbx_refine_tls.S[2][2]_esd      ? 
_pdbx_refine_tls.S[2][3]          -0.0564 
_pdbx_refine_tls.S[2][3]_esd      ? 
_pdbx_refine_tls.S[3][1]          -0.0014 
_pdbx_refine_tls.S[3][1]_esd      ? 
_pdbx_refine_tls.S[3][2]          0.1589 
_pdbx_refine_tls.S[3][2]_esd      ? 
_pdbx_refine_tls.S[3][3]          0.0079 
_pdbx_refine_tls.S[3][3]_esd      ? 
# 
_pdbx_refine_tls_group.id                  1 
_pdbx_refine_tls_group.pdbx_refine_id      'X-RAY DIFFRACTION' 
_pdbx_refine_tls_group.refine_tls_id       1 
_pdbx_refine_tls_group.beg_label_asym_id   ? 
_pdbx_refine_tls_group.beg_label_seq_id    ? 
_pdbx_refine_tls_group.beg_auth_asym_id    ? 
_pdbx_refine_tls_group.beg_auth_seq_id     ? 
_pdbx_refine_tls_group.beg_PDB_ins_code    ? 
_pdbx_refine_tls_group.end_label_asym_id   ? 
_pdbx_refine_tls_group.end_label_seq_id    ? 
_pdbx_refine_tls_group.end_auth_asym_id    ? 
_pdbx_refine_tls_group.end_auth_seq_id     ? 
_pdbx_refine_tls_group.end_PDB_ins_code    ? 
_pdbx_refine_tls_group.selection           ? 
_pdbx_refine_tls_group.selection_details   ALL 
# 
loop_
_pdbx_distant_solvent_atoms.id 
_pdbx_distant_solvent_atoms.PDB_model_num 
_pdbx_distant_solvent_atoms.auth_atom_id 
_pdbx_distant_solvent_atoms.label_alt_id 
_pdbx_distant_solvent_atoms.auth_asym_id 
_pdbx_distant_solvent_atoms.auth_comp_id 
_pdbx_distant_solvent_atoms.auth_seq_id 
_pdbx_distant_solvent_atoms.PDB_ins_code 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance 
1 1 O ? A HOH 877 ? 6.04 . 
2 1 O ? A HOH 878 ? 6.75 . 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A ALA 43  ? A ALA 43  
2  1 Y 1 A ASP 44  ? A ASP 44  
3  1 Y 1 A ASP 45  ? A ASP 45  
4  1 Y 1 A SER 46  ? A SER 46  
5  1 Y 1 A THR 47  ? A THR 47  
6  1 Y 1 A ALA 48  ? A ALA 48  
7  1 Y 1 A ASP 49  ? A ASP 49  
8  1 Y 1 A ASP 50  ? A ASP 50  
9  1 Y 1 A ALA 295 ? A ALA 295 
10 1 Y 1 A ARG 296 ? A ARG 296 
11 1 Y 1 A VAL 297 ? A VAL 297 
12 1 Y 1 A ALA 298 ? A ALA 298 
13 1 Y 1 A SER 299 ? A SER 299 
14 1 Y 1 A LYS 300 ? A LYS 300 
15 1 Y 1 A LEU 301 ? A LEU 301 
16 1 Y 1 A ALA 302 ? A ALA 302 
17 1 Y 1 A ALA 303 ? A ALA 303 
18 1 Y 1 A ALA 304 ? A ALA 304 
19 1 Y 1 A LEU 305 ? A LEU 305 
20 1 Y 1 A GLU 306 ? A GLU 306 
21 1 Y 1 A HIS 307 ? A HIS 307 
22 1 Y 1 A HIS 308 ? A HIS 308 
23 1 Y 1 A HIS 309 ? A HIS 309 
24 1 Y 1 A HIS 310 ? A HIS 310 
25 1 Y 1 A HIS 311 ? A HIS 311 
26 1 Y 1 A HIS 312 ? A HIS 312 
# 
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 
AKG C1   C  N N 1   
AKG O1   O  N N 2   
AKG O2   O  N N 3   
AKG C2   C  N N 4   
AKG O5   O  N N 5   
AKG C3   C  N N 6   
AKG C4   C  N N 7   
AKG C5   C  N N 8   
AKG O3   O  N N 9   
AKG O4   O  N N 10  
AKG HO2  H  N N 11  
AKG H31  H  N N 12  
AKG H32  H  N N 13  
AKG H41  H  N N 14  
AKG H42  H  N N 15  
AKG HO4  H  N N 16  
ALA N    N  N N 17  
ALA CA   C  N S 18  
ALA C    C  N N 19  
ALA O    O  N N 20  
ALA CB   C  N N 21  
ALA OXT  O  N N 22  
ALA H    H  N N 23  
ALA H2   H  N N 24  
ALA HA   H  N N 25  
ALA HB1  H  N N 26  
ALA HB2  H  N N 27  
ALA HB3  H  N N 28  
ALA HXT  H  N N 29  
ARG N    N  N N 30  
ARG CA   C  N S 31  
ARG C    C  N N 32  
ARG O    O  N N 33  
ARG CB   C  N N 34  
ARG CG   C  N N 35  
ARG CD   C  N N 36  
ARG NE   N  N N 37  
ARG CZ   C  N N 38  
ARG NH1  N  N N 39  
ARG NH2  N  N N 40  
ARG OXT  O  N N 41  
ARG H    H  N N 42  
ARG H2   H  N N 43  
ARG HA   H  N N 44  
ARG HB2  H  N N 45  
ARG HB3  H  N N 46  
ARG HG2  H  N N 47  
ARG HG3  H  N N 48  
ARG HD2  H  N N 49  
ARG HD3  H  N N 50  
ARG HE   H  N N 51  
ARG HH11 H  N N 52  
ARG HH12 H  N N 53  
ARG HH21 H  N N 54  
ARG HH22 H  N N 55  
ARG HXT  H  N N 56  
ASN N    N  N N 57  
ASN CA   C  N S 58  
ASN C    C  N N 59  
ASN O    O  N N 60  
ASN CB   C  N N 61  
ASN CG   C  N N 62  
ASN OD1  O  N N 63  
ASN ND2  N  N N 64  
ASN OXT  O  N N 65  
ASN H    H  N N 66  
ASN H2   H  N N 67  
ASN HA   H  N N 68  
ASN HB2  H  N N 69  
ASN HB3  H  N N 70  
ASN HD21 H  N N 71  
ASN HD22 H  N N 72  
ASN HXT  H  N N 73  
ASP N    N  N N 74  
ASP CA   C  N S 75  
ASP C    C  N N 76  
ASP O    O  N N 77  
ASP CB   C  N N 78  
ASP CG   C  N N 79  
ASP OD1  O  N N 80  
ASP OD2  O  N N 81  
ASP OXT  O  N N 82  
ASP H    H  N N 83  
ASP H2   H  N N 84  
ASP HA   H  N N 85  
ASP HB2  H  N N 86  
ASP HB3  H  N N 87  
ASP HD2  H  N N 88  
ASP HXT  H  N N 89  
FE  FE   FE N N 90  
GLN N    N  N N 91  
GLN CA   C  N S 92  
GLN C    C  N N 93  
GLN O    O  N N 94  
GLN CB   C  N N 95  
GLN CG   C  N N 96  
GLN CD   C  N N 97  
GLN OE1  O  N N 98  
GLN NE2  N  N N 99  
GLN OXT  O  N N 100 
GLN H    H  N N 101 
GLN H2   H  N N 102 
GLN HA   H  N N 103 
GLN HB2  H  N N 104 
GLN HB3  H  N N 105 
GLN HG2  H  N N 106 
GLN HG3  H  N N 107 
GLN HE21 H  N N 108 
GLN HE22 H  N N 109 
GLN HXT  H  N N 110 
GLU N    N  N N 111 
GLU CA   C  N S 112 
GLU C    C  N N 113 
GLU O    O  N N 114 
GLU CB   C  N N 115 
GLU CG   C  N N 116 
GLU CD   C  N N 117 
GLU OE1  O  N N 118 
GLU OE2  O  N N 119 
GLU OXT  O  N N 120 
GLU H    H  N N 121 
GLU H2   H  N N 122 
GLU HA   H  N N 123 
GLU HB2  H  N N 124 
GLU HB3  H  N N 125 
GLU HG2  H  N N 126 
GLU HG3  H  N N 127 
GLU HE2  H  N N 128 
GLU HXT  H  N N 129 
GLY N    N  N N 130 
GLY CA   C  N N 131 
GLY C    C  N N 132 
GLY O    O  N N 133 
GLY OXT  O  N N 134 
GLY H    H  N N 135 
GLY H2   H  N N 136 
GLY HA2  H  N N 137 
GLY HA3  H  N N 138 
GLY HXT  H  N N 139 
HIS N    N  N N 140 
HIS CA   C  N S 141 
HIS C    C  N N 142 
HIS O    O  N N 143 
HIS CB   C  N N 144 
HIS CG   C  Y N 145 
HIS ND1  N  Y N 146 
HIS CD2  C  Y N 147 
HIS CE1  C  Y N 148 
HIS NE2  N  Y N 149 
HIS OXT  O  N N 150 
HIS H    H  N N 151 
HIS H2   H  N N 152 
HIS HA   H  N N 153 
HIS HB2  H  N N 154 
HIS HB3  H  N N 155 
HIS HD1  H  N N 156 
HIS HD2  H  N N 157 
HIS HE1  H  N N 158 
HIS HE2  H  N N 159 
HIS HXT  H  N N 160 
HOH O    O  N N 161 
HOH H1   H  N N 162 
HOH H2   H  N N 163 
ILE N    N  N N 164 
ILE CA   C  N S 165 
ILE C    C  N N 166 
ILE O    O  N N 167 
ILE CB   C  N S 168 
ILE CG1  C  N N 169 
ILE CG2  C  N N 170 
ILE CD1  C  N N 171 
ILE OXT  O  N N 172 
ILE H    H  N N 173 
ILE H2   H  N N 174 
ILE HA   H  N N 175 
ILE HB   H  N N 176 
ILE HG12 H  N N 177 
ILE HG13 H  N N 178 
ILE HG21 H  N N 179 
ILE HG22 H  N N 180 
ILE HG23 H  N N 181 
ILE HD11 H  N N 182 
ILE HD12 H  N N 183 
ILE HD13 H  N N 184 
ILE HXT  H  N N 185 
LEU N    N  N N 186 
LEU CA   C  N S 187 
LEU C    C  N N 188 
LEU O    O  N N 189 
LEU CB   C  N N 190 
LEU CG   C  N N 191 
LEU CD1  C  N N 192 
LEU CD2  C  N N 193 
LEU OXT  O  N N 194 
LEU H    H  N N 195 
LEU H2   H  N N 196 
LEU HA   H  N N 197 
LEU HB2  H  N N 198 
LEU HB3  H  N N 199 
LEU HG   H  N N 200 
LEU HD11 H  N N 201 
LEU HD12 H  N N 202 
LEU HD13 H  N N 203 
LEU HD21 H  N N 204 
LEU HD22 H  N N 205 
LEU HD23 H  N N 206 
LEU HXT  H  N N 207 
LYS N    N  N N 208 
LYS CA   C  N S 209 
LYS C    C  N N 210 
LYS O    O  N N 211 
LYS CB   C  N N 212 
LYS CG   C  N N 213 
LYS CD   C  N N 214 
LYS CE   C  N N 215 
LYS NZ   N  N N 216 
LYS OXT  O  N N 217 
LYS H    H  N N 218 
LYS H2   H  N N 219 
LYS HA   H  N N 220 
LYS HB2  H  N N 221 
LYS HB3  H  N N 222 
LYS HG2  H  N N 223 
LYS HG3  H  N N 224 
LYS HD2  H  N N 225 
LYS HD3  H  N N 226 
LYS HE2  H  N N 227 
LYS HE3  H  N N 228 
LYS HZ1  H  N N 229 
LYS HZ2  H  N N 230 
LYS HZ3  H  N N 231 
LYS HXT  H  N N 232 
MET N    N  N N 233 
MET CA   C  N S 234 
MET C    C  N N 235 
MET O    O  N N 236 
MET CB   C  N N 237 
MET CG   C  N N 238 
MET SD   S  N N 239 
MET CE   C  N N 240 
MET OXT  O  N N 241 
MET H    H  N N 242 
MET H2   H  N N 243 
MET HA   H  N N 244 
MET HB2  H  N N 245 
MET HB3  H  N N 246 
MET HG2  H  N N 247 
MET HG3  H  N N 248 
MET HE1  H  N N 249 
MET HE2  H  N N 250 
MET HE3  H  N N 251 
MET HXT  H  N N 252 
PHE N    N  N N 253 
PHE CA   C  N S 254 
PHE C    C  N N 255 
PHE O    O  N N 256 
PHE CB   C  N N 257 
PHE CG   C  Y N 258 
PHE CD1  C  Y N 259 
PHE CD2  C  Y N 260 
PHE CE1  C  Y N 261 
PHE CE2  C  Y N 262 
PHE CZ   C  Y N 263 
PHE OXT  O  N N 264 
PHE H    H  N N 265 
PHE H2   H  N N 266 
PHE HA   H  N N 267 
PHE HB2  H  N N 268 
PHE HB3  H  N N 269 
PHE HD1  H  N N 270 
PHE HD2  H  N N 271 
PHE HE1  H  N N 272 
PHE HE2  H  N N 273 
PHE HZ   H  N N 274 
PHE HXT  H  N N 275 
PRO N    N  N N 276 
PRO CA   C  N S 277 
PRO C    C  N N 278 
PRO O    O  N N 279 
PRO CB   C  N N 280 
PRO CG   C  N N 281 
PRO CD   C  N N 282 
PRO OXT  O  N N 283 
PRO H    H  N N 284 
PRO HA   H  N N 285 
PRO HB2  H  N N 286 
PRO HB3  H  N N 287 
PRO HG2  H  N N 288 
PRO HG3  H  N N 289 
PRO HD2  H  N N 290 
PRO HD3  H  N N 291 
PRO HXT  H  N N 292 
SER N    N  N N 293 
SER CA   C  N S 294 
SER C    C  N N 295 
SER O    O  N N 296 
SER CB   C  N N 297 
SER OG   O  N N 298 
SER OXT  O  N N 299 
SER H    H  N N 300 
SER H2   H  N N 301 
SER HA   H  N N 302 
SER HB2  H  N N 303 
SER HB3  H  N N 304 
SER HG   H  N N 305 
SER HXT  H  N N 306 
THR N    N  N N 307 
THR CA   C  N S 308 
THR C    C  N N 309 
THR O    O  N N 310 
THR CB   C  N R 311 
THR OG1  O  N N 312 
THR CG2  C  N N 313 
THR OXT  O  N N 314 
THR H    H  N N 315 
THR H2   H  N N 316 
THR HA   H  N N 317 
THR HB   H  N N 318 
THR HG1  H  N N 319 
THR HG21 H  N N 320 
THR HG22 H  N N 321 
THR HG23 H  N N 322 
THR HXT  H  N N 323 
TRP N    N  N N 324 
TRP CA   C  N S 325 
TRP C    C  N N 326 
TRP O    O  N N 327 
TRP CB   C  N N 328 
TRP CG   C  Y N 329 
TRP CD1  C  Y N 330 
TRP CD2  C  Y N 331 
TRP NE1  N  Y N 332 
TRP CE2  C  Y N 333 
TRP CE3  C  Y N 334 
TRP CZ2  C  Y N 335 
TRP CZ3  C  Y N 336 
TRP CH2  C  Y N 337 
TRP OXT  O  N N 338 
TRP H    H  N N 339 
TRP H2   H  N N 340 
TRP HA   H  N N 341 
TRP HB2  H  N N 342 
TRP HB3  H  N N 343 
TRP HD1  H  N N 344 
TRP HE1  H  N N 345 
TRP HE3  H  N N 346 
TRP HZ2  H  N N 347 
TRP HZ3  H  N N 348 
TRP HH2  H  N N 349 
TRP HXT  H  N N 350 
TYR N    N  N N 351 
TYR CA   C  N S 352 
TYR C    C  N N 353 
TYR O    O  N N 354 
TYR CB   C  N N 355 
TYR CG   C  Y N 356 
TYR CD1  C  Y N 357 
TYR CD2  C  Y N 358 
TYR CE1  C  Y N 359 
TYR CE2  C  Y N 360 
TYR CZ   C  Y N 361 
TYR OH   O  N N 362 
TYR OXT  O  N N 363 
TYR H    H  N N 364 
TYR H2   H  N N 365 
TYR HA   H  N N 366 
TYR HB2  H  N N 367 
TYR HB3  H  N N 368 
TYR HD1  H  N N 369 
TYR HD2  H  N N 370 
TYR HE1  H  N N 371 
TYR HE2  H  N N 372 
TYR HH   H  N N 373 
TYR HXT  H  N N 374 
VAL N    N  N N 375 
VAL CA   C  N S 376 
VAL C    C  N N 377 
VAL O    O  N N 378 
VAL CB   C  N N 379 
VAL CG1  C  N N 380 
VAL CG2  C  N N 381 
VAL OXT  O  N N 382 
VAL H    H  N N 383 
VAL H2   H  N N 384 
VAL HA   H  N N 385 
VAL HB   H  N N 386 
VAL HG11 H  N N 387 
VAL HG12 H  N N 388 
VAL HG13 H  N N 389 
VAL HG21 H  N N 390 
VAL HG22 H  N N 391 
VAL HG23 H  N N 392 
VAL HXT  H  N N 393 
# 
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 
AKG C1  O1   doub N N 1   
AKG C1  O2   sing N N 2   
AKG C1  C2   sing N N 3   
AKG O2  HO2  sing N N 4   
AKG C2  O5   doub N N 5   
AKG C2  C3   sing N N 6   
AKG C3  C4   sing N N 7   
AKG C3  H31  sing N N 8   
AKG C3  H32  sing N N 9   
AKG C4  C5   sing N N 10  
AKG C4  H41  sing N N 11  
AKG C4  H42  sing N N 12  
AKG C5  O3   doub N N 13  
AKG C5  O4   sing N N 14  
AKG O4  HO4  sing N N 15  
ALA N   CA   sing N N 16  
ALA N   H    sing N N 17  
ALA N   H2   sing N N 18  
ALA CA  C    sing N N 19  
ALA CA  CB   sing N N 20  
ALA CA  HA   sing N N 21  
ALA C   O    doub N N 22  
ALA C   OXT  sing N N 23  
ALA CB  HB1  sing N N 24  
ALA CB  HB2  sing N N 25  
ALA CB  HB3  sing N N 26  
ALA OXT HXT  sing N N 27  
ARG N   CA   sing N N 28  
ARG N   H    sing N N 29  
ARG N   H2   sing N N 30  
ARG CA  C    sing N N 31  
ARG CA  CB   sing N N 32  
ARG CA  HA   sing N N 33  
ARG C   O    doub N N 34  
ARG C   OXT  sing N N 35  
ARG CB  CG   sing N N 36  
ARG CB  HB2  sing N N 37  
ARG CB  HB3  sing N N 38  
ARG CG  CD   sing N N 39  
ARG CG  HG2  sing N N 40  
ARG CG  HG3  sing N N 41  
ARG CD  NE   sing N N 42  
ARG CD  HD2  sing N N 43  
ARG CD  HD3  sing N N 44  
ARG NE  CZ   sing N N 45  
ARG NE  HE   sing N N 46  
ARG CZ  NH1  sing N N 47  
ARG CZ  NH2  doub N N 48  
ARG NH1 HH11 sing N N 49  
ARG NH1 HH12 sing N N 50  
ARG NH2 HH21 sing N N 51  
ARG NH2 HH22 sing N N 52  
ARG OXT HXT  sing N N 53  
ASN N   CA   sing N N 54  
ASN N   H    sing N N 55  
ASN N   H2   sing N N 56  
ASN CA  C    sing N N 57  
ASN CA  CB   sing N N 58  
ASN CA  HA   sing N N 59  
ASN C   O    doub N N 60  
ASN C   OXT  sing N N 61  
ASN CB  CG   sing N N 62  
ASN CB  HB2  sing N N 63  
ASN CB  HB3  sing N N 64  
ASN CG  OD1  doub N N 65  
ASN CG  ND2  sing N N 66  
ASN ND2 HD21 sing N N 67  
ASN ND2 HD22 sing N N 68  
ASN OXT HXT  sing N N 69  
ASP N   CA   sing N N 70  
ASP N   H    sing N N 71  
ASP N   H2   sing N N 72  
ASP CA  C    sing N N 73  
ASP CA  CB   sing N N 74  
ASP CA  HA   sing N N 75  
ASP C   O    doub N N 76  
ASP C   OXT  sing N N 77  
ASP CB  CG   sing N N 78  
ASP CB  HB2  sing N N 79  
ASP CB  HB3  sing N N 80  
ASP CG  OD1  doub N N 81  
ASP CG  OD2  sing N N 82  
ASP OD2 HD2  sing N N 83  
ASP OXT HXT  sing N N 84  
GLN N   CA   sing N N 85  
GLN N   H    sing N N 86  
GLN N   H2   sing N N 87  
GLN CA  C    sing N N 88  
GLN CA  CB   sing N N 89  
GLN CA  HA   sing N N 90  
GLN C   O    doub N N 91  
GLN C   OXT  sing N N 92  
GLN CB  CG   sing N N 93  
GLN CB  HB2  sing N N 94  
GLN CB  HB3  sing N N 95  
GLN CG  CD   sing N N 96  
GLN CG  HG2  sing N N 97  
GLN CG  HG3  sing N N 98  
GLN CD  OE1  doub N N 99  
GLN CD  NE2  sing N N 100 
GLN NE2 HE21 sing N N 101 
GLN NE2 HE22 sing N N 102 
GLN OXT HXT  sing N N 103 
GLU N   CA   sing N N 104 
GLU N   H    sing N N 105 
GLU N   H2   sing N N 106 
GLU CA  C    sing N N 107 
GLU CA  CB   sing N N 108 
GLU CA  HA   sing N N 109 
GLU C   O    doub N N 110 
GLU C   OXT  sing N N 111 
GLU CB  CG   sing N N 112 
GLU CB  HB2  sing N N 113 
GLU CB  HB3  sing N N 114 
GLU CG  CD   sing N N 115 
GLU CG  HG2  sing N N 116 
GLU CG  HG3  sing N N 117 
GLU CD  OE1  doub N N 118 
GLU CD  OE2  sing N N 119 
GLU OE2 HE2  sing N N 120 
GLU OXT HXT  sing N N 121 
GLY N   CA   sing N N 122 
GLY N   H    sing N N 123 
GLY N   H2   sing N N 124 
GLY CA  C    sing N N 125 
GLY CA  HA2  sing N N 126 
GLY CA  HA3  sing N N 127 
GLY C   O    doub N N 128 
GLY C   OXT  sing N N 129 
GLY OXT HXT  sing N N 130 
HIS N   CA   sing N N 131 
HIS N   H    sing N N 132 
HIS N   H2   sing N N 133 
HIS CA  C    sing N N 134 
HIS CA  CB   sing N N 135 
HIS CA  HA   sing N N 136 
HIS C   O    doub N N 137 
HIS C   OXT  sing N N 138 
HIS CB  CG   sing N N 139 
HIS CB  HB2  sing N N 140 
HIS CB  HB3  sing N N 141 
HIS CG  ND1  sing Y N 142 
HIS CG  CD2  doub Y N 143 
HIS ND1 CE1  doub Y N 144 
HIS ND1 HD1  sing N N 145 
HIS CD2 NE2  sing Y N 146 
HIS CD2 HD2  sing N N 147 
HIS CE1 NE2  sing Y N 148 
HIS CE1 HE1  sing N N 149 
HIS NE2 HE2  sing N N 150 
HIS OXT HXT  sing N N 151 
HOH O   H1   sing N N 152 
HOH O   H2   sing N N 153 
ILE N   CA   sing N N 154 
ILE N   H    sing N N 155 
ILE N   H2   sing N N 156 
ILE CA  C    sing N N 157 
ILE CA  CB   sing N N 158 
ILE CA  HA   sing N N 159 
ILE C   O    doub N N 160 
ILE C   OXT  sing N N 161 
ILE CB  CG1  sing N N 162 
ILE CB  CG2  sing N N 163 
ILE CB  HB   sing N N 164 
ILE CG1 CD1  sing N N 165 
ILE CG1 HG12 sing N N 166 
ILE CG1 HG13 sing N N 167 
ILE CG2 HG21 sing N N 168 
ILE CG2 HG22 sing N N 169 
ILE CG2 HG23 sing N N 170 
ILE CD1 HD11 sing N N 171 
ILE CD1 HD12 sing N N 172 
ILE CD1 HD13 sing N N 173 
ILE OXT HXT  sing N N 174 
LEU N   CA   sing N N 175 
LEU N   H    sing N N 176 
LEU N   H2   sing N N 177 
LEU CA  C    sing N N 178 
LEU CA  CB   sing N N 179 
LEU CA  HA   sing N N 180 
LEU C   O    doub N N 181 
LEU C   OXT  sing N N 182 
LEU CB  CG   sing N N 183 
LEU CB  HB2  sing N N 184 
LEU CB  HB3  sing N N 185 
LEU CG  CD1  sing N N 186 
LEU CG  CD2  sing N N 187 
LEU CG  HG   sing N N 188 
LEU CD1 HD11 sing N N 189 
LEU CD1 HD12 sing N N 190 
LEU CD1 HD13 sing N N 191 
LEU CD2 HD21 sing N N 192 
LEU CD2 HD22 sing N N 193 
LEU CD2 HD23 sing N N 194 
LEU OXT HXT  sing N N 195 
LYS N   CA   sing N N 196 
LYS N   H    sing N N 197 
LYS N   H2   sing N N 198 
LYS CA  C    sing N N 199 
LYS CA  CB   sing N N 200 
LYS CA  HA   sing N N 201 
LYS C   O    doub N N 202 
LYS C   OXT  sing N N 203 
LYS CB  CG   sing N N 204 
LYS CB  HB2  sing N N 205 
LYS CB  HB3  sing N N 206 
LYS CG  CD   sing N N 207 
LYS CG  HG2  sing N N 208 
LYS CG  HG3  sing N N 209 
LYS CD  CE   sing N N 210 
LYS CD  HD2  sing N N 211 
LYS CD  HD3  sing N N 212 
LYS CE  NZ   sing N N 213 
LYS CE  HE2  sing N N 214 
LYS CE  HE3  sing N N 215 
LYS NZ  HZ1  sing N N 216 
LYS NZ  HZ2  sing N N 217 
LYS NZ  HZ3  sing N N 218 
LYS OXT HXT  sing N N 219 
MET N   CA   sing N N 220 
MET N   H    sing N N 221 
MET N   H2   sing N N 222 
MET CA  C    sing N N 223 
MET CA  CB   sing N N 224 
MET CA  HA   sing N N 225 
MET C   O    doub N N 226 
MET C   OXT  sing N N 227 
MET CB  CG   sing N N 228 
MET CB  HB2  sing N N 229 
MET CB  HB3  sing N N 230 
MET CG  SD   sing N N 231 
MET CG  HG2  sing N N 232 
MET CG  HG3  sing N N 233 
MET SD  CE   sing N N 234 
MET CE  HE1  sing N N 235 
MET CE  HE2  sing N N 236 
MET CE  HE3  sing N N 237 
MET OXT HXT  sing N N 238 
PHE N   CA   sing N N 239 
PHE N   H    sing N N 240 
PHE N   H2   sing N N 241 
PHE CA  C    sing N N 242 
PHE CA  CB   sing N N 243 
PHE CA  HA   sing N N 244 
PHE C   O    doub N N 245 
PHE C   OXT  sing N N 246 
PHE CB  CG   sing N N 247 
PHE CB  HB2  sing N N 248 
PHE CB  HB3  sing N N 249 
PHE CG  CD1  doub Y N 250 
PHE CG  CD2  sing Y N 251 
PHE CD1 CE1  sing Y N 252 
PHE CD1 HD1  sing N N 253 
PHE CD2 CE2  doub Y N 254 
PHE CD2 HD2  sing N N 255 
PHE CE1 CZ   doub Y N 256 
PHE CE1 HE1  sing N N 257 
PHE CE2 CZ   sing Y N 258 
PHE CE2 HE2  sing N N 259 
PHE CZ  HZ   sing N N 260 
PHE OXT HXT  sing N N 261 
PRO N   CA   sing N N 262 
PRO N   CD   sing N N 263 
PRO N   H    sing N N 264 
PRO CA  C    sing N N 265 
PRO CA  CB   sing N N 266 
PRO CA  HA   sing N N 267 
PRO C   O    doub N N 268 
PRO C   OXT  sing N N 269 
PRO CB  CG   sing N N 270 
PRO CB  HB2  sing N N 271 
PRO CB  HB3  sing N N 272 
PRO CG  CD   sing N N 273 
PRO CG  HG2  sing N N 274 
PRO CG  HG3  sing N N 275 
PRO CD  HD2  sing N N 276 
PRO CD  HD3  sing N N 277 
PRO OXT HXT  sing N N 278 
SER N   CA   sing N N 279 
SER N   H    sing N N 280 
SER N   H2   sing N N 281 
SER CA  C    sing N N 282 
SER CA  CB   sing N N 283 
SER CA  HA   sing N N 284 
SER C   O    doub N N 285 
SER C   OXT  sing N N 286 
SER CB  OG   sing N N 287 
SER CB  HB2  sing N N 288 
SER CB  HB3  sing N N 289 
SER OG  HG   sing N N 290 
SER OXT HXT  sing N N 291 
THR N   CA   sing N N 292 
THR N   H    sing N N 293 
THR N   H2   sing N N 294 
THR CA  C    sing N N 295 
THR CA  CB   sing N N 296 
THR CA  HA   sing N N 297 
THR C   O    doub N N 298 
THR C   OXT  sing N N 299 
THR CB  OG1  sing N N 300 
THR CB  CG2  sing N N 301 
THR CB  HB   sing N N 302 
THR OG1 HG1  sing N N 303 
THR CG2 HG21 sing N N 304 
THR CG2 HG22 sing N N 305 
THR CG2 HG23 sing N N 306 
THR OXT HXT  sing N N 307 
TRP N   CA   sing N N 308 
TRP N   H    sing N N 309 
TRP N   H2   sing N N 310 
TRP CA  C    sing N N 311 
TRP CA  CB   sing N N 312 
TRP CA  HA   sing N N 313 
TRP C   O    doub N N 314 
TRP C   OXT  sing N N 315 
TRP CB  CG   sing N N 316 
TRP CB  HB2  sing N N 317 
TRP CB  HB3  sing N N 318 
TRP CG  CD1  doub Y N 319 
TRP CG  CD2  sing Y N 320 
TRP CD1 NE1  sing Y N 321 
TRP CD1 HD1  sing N N 322 
TRP CD2 CE2  doub Y N 323 
TRP CD2 CE3  sing Y N 324 
TRP NE1 CE2  sing Y N 325 
TRP NE1 HE1  sing N N 326 
TRP CE2 CZ2  sing Y N 327 
TRP CE3 CZ3  doub Y N 328 
TRP CE3 HE3  sing N N 329 
TRP CZ2 CH2  doub Y N 330 
TRP CZ2 HZ2  sing N N 331 
TRP CZ3 CH2  sing Y N 332 
TRP CZ3 HZ3  sing N N 333 
TRP CH2 HH2  sing N N 334 
TRP OXT HXT  sing N N 335 
TYR N   CA   sing N N 336 
TYR N   H    sing N N 337 
TYR N   H2   sing N N 338 
TYR CA  C    sing N N 339 
TYR CA  CB   sing N N 340 
TYR CA  HA   sing N N 341 
TYR C   O    doub N N 342 
TYR C   OXT  sing N N 343 
TYR CB  CG   sing N N 344 
TYR CB  HB2  sing N N 345 
TYR CB  HB3  sing N N 346 
TYR CG  CD1  doub Y N 347 
TYR CG  CD2  sing Y N 348 
TYR CD1 CE1  sing Y N 349 
TYR CD1 HD1  sing N N 350 
TYR CD2 CE2  doub Y N 351 
TYR CD2 HD2  sing N N 352 
TYR CE1 CZ   doub Y N 353 
TYR CE1 HE1  sing N N 354 
TYR CE2 CZ   sing Y N 355 
TYR CE2 HE2  sing N N 356 
TYR CZ  OH   sing N N 357 
TYR OH  HH   sing N N 358 
TYR OXT HXT  sing N N 359 
VAL N   CA   sing N N 360 
VAL N   H    sing N N 361 
VAL N   H2   sing N N 362 
VAL CA  C    sing N N 363 
VAL CA  CB   sing N N 364 
VAL CA  HA   sing N N 365 
VAL C   O    doub N N 366 
VAL C   OXT  sing N N 367 
VAL CB  CG1  sing N N 368 
VAL CB  CG2  sing N N 369 
VAL CB  HB   sing N N 370 
VAL CG1 HG11 sing N N 371 
VAL CG1 HG12 sing N N 372 
VAL CG1 HG13 sing N N 373 
VAL CG2 HG21 sing N N 374 
VAL CG2 HG22 sing N N 375 
VAL CG2 HG23 sing N N 376 
VAL OXT HXT  sing N N 377 
# 
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 '81925033, 22193071, 81991522, 81991524, 22107048, and 22377052' 1 
'Ministry of Science and Technology (MoST, China)'    China '2022YFC2804100, 2022YFC2303100, and 2018YFA0902000'             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   8XP6 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    8XPF 
_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]   0.008240 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.003430 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.016391 
_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]   0.019224 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C  
FE 
H  
N  
O  
S  
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N    . MET A 1 1   ? 24.128  -0.187  18.503  1.00 52.32  ?  1   MET A N    1 
ATOM   2    C  CA   . MET A 1 1   ? 24.037  0.050   17.063  1.00 45.95  ?  1   MET A CA   1 
ATOM   3    C  C    . MET A 1 1   ? 24.063  1.538   16.726  1.00 41.81  ?  1   MET A C    1 
ATOM   4    O  O    . MET A 1 1   ? 23.343  2.337   17.322  1.00 46.73  ?  1   MET A O    1 
ATOM   5    C  CB   . MET A 1 1   ? 22.776  -0.596  16.485  1.00 38.84  ?  1   MET A CB   1 
ATOM   6    C  CG   . MET A 1 1   ? 22.872  -2.101  16.353  1.00 41.28  ?  1   MET A CG   1 
ATOM   7    S  SD   . MET A 1 1   ? 21.300  -2.892  15.975  1.00 39.66  ?  1   MET A SD   1 
ATOM   8    C  CE   . MET A 1 1   ? 20.934  -2.253  14.343  1.00 33.81  ?  1   MET A CE   1 
ATOM   9    N  N    . ASP A 1 2   ? 24.898  1.891   15.756  1.00 38.50  ?  2   ASP A N    1 
ATOM   10   C  CA   . ASP A 1 2   ? 25.029  3.252   15.246  1.00 37.55  ?  2   ASP A CA   1 
ATOM   11   C  C    . ASP A 1 2   ? 24.327  3.255   13.893  1.00 36.21  ?  2   ASP A C    1 
ATOM   12   O  O    . ASP A 1 2   ? 24.871  2.752   12.907  1.00 33.77  ?  2   ASP A O    1 
ATOM   13   C  CB   . ASP A 1 2   ? 26.512  3.599   15.110  1.00 39.74  ?  2   ASP A CB   1 
ATOM   14   C  CG   . ASP A 1 2   ? 26.755  5.018   14.605  1.00 42.87  ?  2   ASP A CG   1 
ATOM   15   O  OD1  . ASP A 1 2   ? 25.877  5.592   13.928  1.00 39.79  ?  2   ASP A OD1  1 
ATOM   16   O  OD2  . ASP A 1 2   ? 27.848  5.559   14.888  1.00 48.86  -1 2   ASP A OD2  1 
ATOM   17   N  N    . SER A 1 3   ? 23.117  3.823   13.850  1.00 31.05  ?  3   SER A N    1 
ATOM   18   C  CA   . SER A 1 3   ? 22.296  3.743   12.643  1.00 31.50  ?  3   SER A CA   1 
ATOM   19   C  C    . SER A 1 3   ? 23.014  4.325   11.434  1.00 32.38  ?  3   SER A C    1 
ATOM   20   O  O    . SER A 1 3   ? 23.009  3.729   10.351  1.00 30.98  ?  3   SER A O    1 
ATOM   21   C  CB   . SER A 1 3   ? 20.971  4.469   12.860  1.00 33.64  ?  3   SER A CB   1 
ATOM   22   O  OG   . SER A 1 3   ? 20.190  3.786   13.813  1.00 37.89  ?  3   SER A OG   1 
ATOM   23   N  N    . LYS A 1 4   ? 23.601  5.511   11.588  1.00 33.13  ?  4   LYS A N    1 
ATOM   24   C  CA   . LYS A 1 4   ? 24.249  6.155   10.450  1.00 32.81  ?  4   LYS A CA   1 
ATOM   25   C  C    . LYS A 1 4   ? 25.458  5.358   9.981   1.00 35.81  ?  4   LYS A C    1 
ATOM   26   O  O    . LYS A 1 4   ? 25.711  5.253   8.775   1.00 35.25  ?  4   LYS A O    1 
ATOM   27   C  CB   . LYS A 1 4   ? 24.625  7.595   10.800  1.00 38.23  ?  4   LYS A CB   1 
ATOM   28   C  CG   . LYS A 1 4   ? 23.421  8.511   10.936  1.00 41.59  ?  4   LYS A CG   1 
ATOM   29   C  CD   . LYS A 1 4   ? 23.848  9.948   11.178  1.00 42.71  ?  4   LYS A CD   1 
ATOM   30   C  CE   . LYS A 1 4   ? 22.633  10.856  11.262  1.00 48.12  ?  4   LYS A CE   1 
ATOM   31   N  NZ   . LYS A 1 4   ? 21.734  10.677  10.084  1.00 49.27  ?  4   LYS A NZ   1 
ATOM   32   N  N    . SER A 1 5   ? 26.202  4.773   10.916  1.00 30.89  ?  5   SER A N    1 
ATOM   33   C  CA   . SER A 1 5   ? 27.352  3.957   10.545  1.00 33.59  ?  5   SER A CA   1 
ATOM   34   C  C    . SER A 1 5   ? 26.916  2.703   9.796   1.00 31.73  ?  5   SER A C    1 
ATOM   35   O  O    . SER A 1 5   ? 27.485  2.352   8.752   1.00 30.09  ?  5   SER A O    1 
ATOM   36   C  CB   . SER A 1 5   ? 28.133  3.589   11.806  1.00 36.70  ?  5   SER A CB   1 
ATOM   37   O  OG   . SER A 1 5   ? 29.285  2.840   11.487  1.00 38.77  ?  5   SER A OG   1 
ATOM   38   N  N    . ILE A 1 6   ? 25.903  2.013   10.314  1.00 28.88  ?  6   ILE A N    1 
ATOM   39   C  CA   . ILE A 1 6   ? 25.429  0.802   9.656   1.00 26.14  ?  6   ILE A CA   1 
ATOM   40   C  C    . ILE A 1 6   ? 24.869  1.129   8.282   1.00 27.69  ?  6   ILE A C    1 
ATOM   41   O  O    . ILE A 1 6   ? 25.130  0.415   7.310   1.00 26.09  ?  6   ILE A O    1 
ATOM   42   C  CB   . ILE A 1 6   ? 24.397  0.076   10.537  1.00 24.57  ?  6   ILE A CB   1 
ATOM   43   C  CG1  . ILE A 1 6   ? 25.061  -0.390  11.832  1.00 30.48  ?  6   ILE A CG1  1 
ATOM   44   C  CG2  . ILE A 1 6   ? 23.815  -1.098  9.789   1.00 24.12  ?  6   ILE A CG2  1 
ATOM   45   C  CD1  . ILE A 1 6   ? 24.080  -0.804  12.907  1.00 30.59  ?  6   ILE A CD1  1 
ATOM   46   N  N    . ALA A 1 7   ? 24.082  2.205   8.180   1.00 27.70  ?  7   ALA A N    1 
ATOM   47   C  CA   . ALA A 1 7   ? 23.516  2.569   6.885   1.00 26.86  ?  7   ALA A CA   1 
ATOM   48   C  C    . ALA A 1 7   ? 24.604  2.922   5.877   1.00 29.77  ?  7   ALA A C    1 
ATOM   49   O  O    . ALA A 1 7   ? 24.457  2.634   4.684   1.00 27.38  ?  7   ALA A O    1 
ATOM   50   C  CB   . ALA A 1 7   ? 22.514  3.718   7.041   1.00 32.19  ?  7   ALA A CB   1 
ATOM   51   N  N    . ALA A 1 8   ? 25.706  3.524   6.336   1.00 28.00  ?  8   ALA A N    1 
ATOM   52   C  CA   . ALA A 1 8   ? 26.822  3.817   5.442   1.00 27.31  ?  8   ALA A CA   1 
ATOM   53   C  C    . ALA A 1 8   ? 27.482  2.538   4.945   1.00 29.62  ?  8   ALA A C    1 
ATOM   54   O  O    . ALA A 1 8   ? 27.864  2.451   3.774   1.00 27.97  ?  8   ALA A O    1 
ATOM   55   C  CB   . ALA A 1 8   ? 27.847  4.715   6.142   1.00 27.90  ?  8   ALA A CB   1 
ATOM   56   N  N    . GLU A 1 9   ? 27.650  1.541   5.819   1.00 29.55  ?  9   GLU A N    1 
ATOM   57   C  CA   . GLU A 1 9   ? 28.207  0.269   5.370   1.00 29.29  ?  9   GLU A CA   1 
ATOM   58   C  C    . GLU A 1 9   ? 27.275  -0.417  4.380   1.00 27.68  ?  9   GLU A C    1 
ATOM   59   O  O    . GLU A 1 9   ? 27.727  -0.979  3.377   1.00 25.92  ?  9   GLU A O    1 
ATOM   60   C  CB   . GLU A 1 9   ? 28.527  -0.645  6.557   1.00 34.11  ?  9   GLU A CB   1 
ATOM   61   C  CG   . GLU A 1 9   ? 29.784  -0.269  7.337   1.00 46.86  ?  9   GLU A CG   1 
ATOM   62   C  CD   . GLU A 1 9   ? 31.070  -0.840  6.723   1.00 47.99  ?  9   GLU A CD   1 
ATOM   63   O  OE1  . GLU A 1 9   ? 30.993  -1.876  6.021   1.00 50.83  ?  9   GLU A OE1  1 
ATOM   64   O  OE2  . GLU A 1 9   ? 32.158  -0.255  6.944   1.00 57.02  -1 9   GLU A OE2  1 
ATOM   65   N  N    . LEU A 1 10  ? 25.966  -0.381  4.635   1.00 25.00  ?  10  LEU A N    1 
ATOM   66   C  CA   . LEU A 1 10  ? 25.033  -0.942  3.666   1.00 22.75  ?  10  LEU A CA   1 
ATOM   67   C  C    . LEU A 1 10  ? 25.160  -0.244  2.320   1.00 23.09  ?  10  LEU A C    1 
ATOM   68   O  O    . LEU A 1 10  ? 25.140  -0.898  1.270   1.00 23.72  ?  10  LEU A O    1 
ATOM   69   C  CB   . LEU A 1 10  ? 23.599  -0.835  4.183   1.00 23.61  ?  10  LEU A CB   1 
ATOM   70   C  CG   . LEU A 1 10  ? 23.258  -1.720  5.377   1.00 25.04  ?  10  LEU A CG   1 
ATOM   71   C  CD1  . LEU A 1 10  ? 21.865  -1.359  5.915   1.00 27.41  ?  10  LEU A CD1  1 
ATOM   72   C  CD2  . LEU A 1 10  ? 23.274  -3.176  4.981   1.00 24.53  ?  10  LEU A CD2  1 
ATOM   73   N  N    . ALA A 1 11  ? 25.297  1.084   2.328   1.00 24.89  ?  11  ALA A N    1 
ATOM   74   C  CA   . ALA A 1 11  ? 25.360  1.806   1.062   1.00 25.61  ?  11  ALA A CA   1 
ATOM   75   C  C    . ALA A 1 11  ? 26.636  1.485   0.292   1.00 23.96  ?  11  ALA A C    1 
ATOM   76   O  O    . ALA A 1 11  ? 26.606  1.386   -0.942  1.00 26.35  ?  11  ALA A O    1 
ATOM   77   C  CB   . ALA A 1 11  ? 25.204  3.308   1.285   1.00 28.66  ?  11  ALA A CB   1 
ATOM   78   N  N    . THR A 1 12  ? 27.762  1.314   0.994   1.00 24.37  ?  12  THR A N    1 
ATOM   79   C  CA   . THR A 1 12  ? 29.055  1.115   0.346   1.00 27.15  ?  12  THR A CA   1 
ATOM   80   C  C    . THR A 1 12  ? 29.331  -0.339  -0.014  1.00 28.63  ?  12  THR A C    1 
ATOM   81   O  O    . THR A 1 12  ? 29.819  -0.618  -1.118  1.00 28.20  ?  12  THR A O    1 
ATOM   82   C  CB   . THR A 1 12  ? 30.178  1.636   1.246   1.00 26.67  ?  12  THR A CB   1 
ATOM   83   O  OG1  . THR A 1 12  ? 30.023  3.048   1.414   1.00 31.58  ?  12  THR A OG1  1 
ATOM   84   C  CG2  . THR A 1 12  ? 31.551  1.331   0.624   1.00 29.04  ?  12  THR A CG2  1 
ATOM   85   N  N    . ARG A 1 13  ? 29.042  -1.269  0.900   1.00 24.63  ?  13  ARG A N    1 
ATOM   86   C  CA   . ARG A 1 13  ? 29.378  -2.670  0.718   1.00 25.65  ?  13  ARG A CA   1 
ATOM   87   C  C    . ARG A 1 13  ? 28.165  -3.547  0.467   1.00 22.93  ?  13  ARG A C    1 
ATOM   88   O  O    . ARG A 1 13  ? 28.326  -4.694  0.043   1.00 23.27  ?  13  ARG A O    1 
ATOM   89   C  CB   . ARG A 1 13  ? 30.117  -3.213  1.952   1.00 29.66  ?  13  ARG A CB   1 
ATOM   90   C  CG   . ARG A 1 13  ? 31.392  -2.481  2.296   1.00 39.63  ?  13  ARG A CG   1 
ATOM   91   C  CD   . ARG A 1 13  ? 32.284  -3.334  3.189   1.00 44.82  ?  13  ARG A CD   1 
ATOM   92   N  NE   . ARG A 1 13  ? 33.690  -2.999  3.002   1.00 55.45  ?  13  ARG A NE   1 
ATOM   93   C  CZ   . ARG A 1 13  ? 34.281  -1.943  3.541   1.00 56.90  ?  13  ARG A CZ   1 
ATOM   94   N  NH1  . ARG A 1 13  ? 33.618  -1.104  4.321   1.00 58.02  ?  13  ARG A NH1  1 
ATOM   95   N  NH2  . ARG A 1 13  ? 35.569  -1.719  3.289   1.00 59.41  ?  13  ARG A NH2  1 
ATOM   96   N  N    . GLY A 1 14  ? 26.961  -3.050  0.745   1.00 21.23  ?  14  GLY A N    1 
ATOM   97   C  CA   . GLY A 1 14  ? 25.756  -3.821  0.561   1.00 19.98  ?  14  GLY A CA   1 
ATOM   98   C  C    . GLY A 1 14  ? 25.306  -4.634  1.759   1.00 19.33  ?  14  GLY A C    1 
ATOM   99   O  O    . GLY A 1 14  ? 24.182  -5.137  1.746   1.00 20.03  ?  14  GLY A O    1 
ATOM   100  N  N    . TYR A 1 15  ? 26.122  -4.761  2.801   1.00 19.01  ?  15  TYR A N    1 
ATOM   101  C  CA   . TYR A 1 15  ? 25.758  -5.583  3.950   1.00 19.41  ?  15  TYR A CA   1 
ATOM   102  C  C    . TYR A 1 15  ? 26.514  -5.097  5.174   1.00 19.98  ?  15  TYR A C    1 
ATOM   103  O  O    . TYR A 1 15  ? 27.576  -4.470  5.072   1.00 22.35  ?  15  TYR A O    1 
ATOM   104  C  CB   . TYR A 1 15  ? 26.057  -7.074  3.702   1.00 20.28  ?  15  TYR A CB   1 
ATOM   105  C  CG   . TYR A 1 15  ? 27.524  -7.430  3.734   1.00 23.19  ?  15  TYR A CG   1 
ATOM   106  C  CD1  . TYR A 1 15  ? 28.340  -7.191  2.635   1.00 21.70  ?  15  TYR A CD1  1 
ATOM   107  C  CD2  . TYR A 1 15  ? 28.093  -7.994  4.871   1.00 24.35  ?  15  TYR A CD2  1 
ATOM   108  C  CE1  . TYR A 1 15  ? 29.703  -7.516  2.666   1.00 23.76  ?  15  TYR A CE1  1 
ATOM   109  C  CE2  . TYR A 1 15  ? 29.448  -8.314  4.917   1.00 26.12  ?  15  TYR A CE2  1 
ATOM   110  C  CZ   . TYR A 1 15  ? 30.241  -8.076  3.810   1.00 25.48  ?  15  TYR A CZ   1 
ATOM   111  O  OH   . TYR A 1 15  ? 31.591  -8.389  3.842   1.00 32.40  ?  15  TYR A OH   1 
ATOM   112  N  N    . ALA A 1 16  ? 25.966  -5.429  6.340   1.00 20.38  ?  16  ALA A N    1 
ATOM   113  C  CA   . ALA A 1 16  ? 26.623  -5.165  7.608   1.00 23.47  ?  16  ALA A CA   1 
ATOM   114  C  C    . ALA A 1 16  ? 26.201  -6.252  8.581   1.00 22.22  ?  16  ALA A C    1 
ATOM   115  O  O    . ALA A 1 16  ? 25.014  -6.569  8.667   1.00 22.00  ?  16  ALA A O    1 
ATOM   116  C  CB   . ALA A 1 16  ? 26.225  -3.787  8.144   1.00 25.24  ?  16  ALA A CB   1 
ATOM   117  N  N    . LEU A 1 17  ? 27.162  -6.830  9.288   1.00 24.55  ?  17  LEU A N    1 
ATOM   118  C  CA   . LEU A 1 17  ? 26.889  -7.818  10.323  1.00 26.00  ?  17  LEU A CA   1 
ATOM   119  C  C    . LEU A 1 17  ? 26.917  -7.133  11.686  1.00 24.41  ?  17  LEU A C    1 
ATOM   120  O  O    . LEU A 1 17  ? 27.922  -6.511  12.051  1.00 29.74  ?  17  LEU A O    1 
ATOM   121  C  CB   . LEU A 1 17  ? 27.936  -8.931  10.265  1.00 24.55  ?  17  LEU A CB   1 
ATOM   122  C  CG   . LEU A 1 17  ? 27.735  -10.023 11.313  1.00 29.93  ?  17  LEU A CG   1 
ATOM   123  C  CD1  . LEU A 1 17  ? 26.432  -10.772 11.035  1.00 26.14  ?  17  LEU A CD1  1 
ATOM   124  C  CD2  . LEU A 1 17  ? 28.928  -10.969 11.365  1.00 34.13  ?  17  LEU A CD2  1 
ATOM   125  N  N    . VAL A 1 18  ? 25.825  -7.258  12.438  1.00 24.87  ?  18  VAL A N    1 
ATOM   126  C  CA   . VAL A 1 18  ? 25.709  -6.684  13.777  1.00 28.16  ?  18  VAL A CA   1 
ATOM   127  C  C    . VAL A 1 18  ? 25.848  -7.807  14.797  1.00 26.92  ?  18  VAL A C    1 
ATOM   128  O  O    . VAL A 1 18  ? 24.889  -8.564  15.009  1.00 27.70  ?  18  VAL A O    1 
ATOM   129  C  CB   . VAL A 1 18  ? 24.362  -5.968  13.971  1.00 28.23  ?  18  VAL A CB   1 
ATOM   130  C  CG1  . VAL A 1 18  ? 24.286  -5.345  15.371  1.00 30.13  ?  18  VAL A CG1  1 
ATOM   131  C  CG2  . VAL A 1 18  ? 24.111  -4.932  12.871  1.00 31.26  ?  18  VAL A CG2  1 
ATOM   132  N  N    . PRO A 1 19  ? 26.994  -7.957  15.453  1.00 28.73  ?  19  PRO A N    1 
ATOM   133  C  CA   . PRO A 1 19  ? 27.104  -8.985  16.487  1.00 31.85  ?  19  PRO A CA   1 
ATOM   134  C  C    . PRO A 1 19  ? 26.266  -8.597  17.694  1.00 31.16  ?  19  PRO A C    1 
ATOM   135  O  O    . PRO A 1 19  ? 26.054  -7.416  17.979  1.00 35.18  ?  19  PRO A O    1 
ATOM   136  C  CB   . PRO A 1 19  ? 28.600  -8.993  16.826  1.00 34.76  ?  19  PRO A CB   1 
ATOM   137  C  CG   . PRO A 1 19  ? 29.067  -7.608  16.489  1.00 38.67  ?  19  PRO A CG   1 
ATOM   138  C  CD   . PRO A 1 19  ? 28.226  -7.161  15.315  1.00 32.48  ?  19  PRO A CD   1 
ATOM   139  N  N    . ASP A 1 20  ? 25.742  -9.607  18.380  1.00 32.96  ?  20  ASP A N    1 
ATOM   140  C  CA   . ASP A 1 20  ? 25.089  -9.390  19.672  1.00 30.87  ?  20  ASP A CA   1 
ATOM   141  C  C    . ASP A 1 20  ? 23.878  -8.464  19.551  1.00 31.78  ?  20  ASP A C    1 
ATOM   142  O  O    . ASP A 1 20  ? 23.585  -7.660  20.440  1.00 33.92  ?  20  ASP A O    1 
ATOM   143  C  CB   . ASP A 1 20  ? 26.084  -8.894  20.723  1.00 37.07  ?  20  ASP A CB   1 
ATOM   144  C  CG   . ASP A 1 20  ? 27.175  -9.902  21.002  1.00 42.70  ?  20  ASP A CG   1 
ATOM   145  O  OD1  . ASP A 1 20  ? 26.841  -11.070 21.307  1.00 42.96  ?  20  ASP A OD1  1 
ATOM   146  O  OD2  . ASP A 1 20  ? 28.365  -9.533  20.905  1.00 49.46  -1 20  ASP A OD2  1 
ATOM   147  N  N    . PHE A 1 21  ? 23.166  -8.576  18.431  1.00 27.17  ?  21  PHE A N    1 
ATOM   148  C  CA   . PHE A 1 21  ? 21.922  -7.838  18.276  1.00 25.74  ?  21  PHE A CA   1 
ATOM   149  C  C    . PHE A 1 21  ? 20.931  -8.232  19.363  1.00 30.10  ?  21  PHE A C    1 
ATOM   150  O  O    . PHE A 1 21  ? 20.240  -7.376  19.928  1.00 28.95  ?  21  PHE A O    1 
ATOM   151  C  CB   . PHE A 1 21  ? 21.350  -8.101  16.880  1.00 25.91  ?  21  PHE A CB   1 
ATOM   152  C  CG   . PHE A 1 21  ? 19.999  -7.485  16.640  1.00 25.17  ?  21  PHE A CG   1 
ATOM   153  C  CD1  . PHE A 1 21  ? 19.873  -6.134  16.357  1.00 26.28  ?  21  PHE A CD1  1 
ATOM   154  C  CD2  . PHE A 1 21  ? 18.865  -8.266  16.667  1.00 24.67  ?  21  PHE A CD2  1 
ATOM   155  C  CE1  . PHE A 1 21  ? 18.632  -5.577  16.117  1.00 26.34  ?  21  PHE A CE1  1 
ATOM   156  C  CE2  . PHE A 1 21  ? 17.610  -7.710  16.427  1.00 26.79  ?  21  PHE A CE2  1 
ATOM   157  C  CZ   . PHE A 1 21  ? 17.506  -6.361  16.153  1.00 26.30  ?  21  PHE A CZ   1 
ATOM   158  N  N    . LEU A 1 22  ? 20.848  -9.524  19.667  1.00 27.38  ?  22  LEU A N    1 
ATOM   159  C  CA   . LEU A 1 22  ? 20.161  -10.020 20.850  1.00 28.35  ?  22  LEU A CA   1 
ATOM   160  C  C    . LEU A 1 22  ? 21.192  -10.589 21.810  1.00 32.35  ?  22  LEU A C    1 
ATOM   161  O  O    . LEU A 1 22  ? 22.126  -11.282 21.390  1.00 33.49  ?  22  LEU A O    1 
ATOM   162  C  CB   . LEU A 1 22  ? 19.175  -11.134 20.499  1.00 30.32  ?  22  LEU A CB   1 
ATOM   163  C  CG   . LEU A 1 22  ? 17.994  -10.788 19.592  1.00 29.88  ?  22  LEU A CG   1 
ATOM   164  C  CD1  . LEU A 1 22  ? 17.005  -11.947 19.563  1.00 30.56  ?  22  LEU A CD1  1 
ATOM   165  C  CD2  . LEU A 1 22  ? 17.307  -9.493  20.018  1.00 30.47  ?  22  LEU A CD2  1 
ATOM   166  N  N    . THR A 1 23  ? 21.022  -10.288 23.098  1.00 31.74  ?  23  THR A N    1 
ATOM   167  C  CA   . THR A 1 23  ? 21.850  -10.841 24.161  1.00 33.69  ?  23  THR A CA   1 
ATOM   168  C  C    . THR A 1 23  ? 20.952  -11.172 25.342  1.00 33.22  ?  23  THR A C    1 
ATOM   169  O  O    . THR A 1 23  ? 19.770  -10.829 25.360  1.00 33.39  ?  23  THR A O    1 
ATOM   170  C  CB   . THR A 1 23  ? 22.926  -9.846  24.629  1.00 40.79  ?  23  THR A CB   1 
ATOM   171  O  OG1  . THR A 1 23  ? 22.291  -8.674  25.160  1.00 43.36  ?  23  THR A OG1  1 
ATOM   172  C  CG2  . THR A 1 23  ? 23.855  -9.457  23.481  1.00 38.02  ?  23  THR A CG2  1 
ATOM   173  N  N    . GLY A 1 24  ? 21.525  -11.845 26.336  1.00 35.95  ?  24  GLY A N    1 
ATOM   174  C  CA   . GLY A 1 24  ? 20.816  -12.077 27.578  1.00 38.65  ?  24  GLY A CA   1 
ATOM   175  C  C    . GLY A 1 24  ? 19.533  -12.869 27.400  1.00 37.94  ?  24  GLY A C    1 
ATOM   176  O  O    . GLY A 1 24  ? 19.414  -13.754 26.541  1.00 36.68  ?  24  GLY A O    1 
ATOM   177  N  N    . ASP A 1 25  ? 18.542  -12.535 28.233  1.00 36.32  ?  25  ASP A N    1 
ATOM   178  C  CA   . ASP A 1 25  ? 17.271  -13.251 28.192  1.00 37.77  ?  25  ASP A CA   1 
ATOM   179  C  C    . ASP A 1 25  ? 16.569  -13.104 26.849  1.00 34.97  ?  25  ASP A C    1 
ATOM   180  O  O    . ASP A 1 25  ? 15.868  -14.024 26.416  1.00 36.45  ?  25  ASP A O    1 
ATOM   181  C  CB   . ASP A 1 25  ? 16.343  -12.772 29.309  1.00 43.30  ?  25  ASP A CB   1 
ATOM   182  C  CG   . ASP A 1 25  ? 16.906  -13.032 30.686  1.00 45.61  ?  25  ASP A CG   1 
ATOM   183  O  OD1  . ASP A 1 25  ? 17.766  -13.930 30.821  1.00 49.18  ?  25  ASP A OD1  1 
ATOM   184  O  OD2  . ASP A 1 25  ? 16.479  -12.339 31.636  1.00 50.63  -1 25  ASP A OD2  1 
ATOM   185  N  N    . ALA A 1 26  ? 16.711  -11.956 26.185  1.00 32.43  ?  26  ALA A N    1 
ATOM   186  C  CA   . ALA A 1 26  ? 16.076  -11.809 24.880  1.00 30.49  ?  26  ALA A CA   1 
ATOM   187  C  C    . ALA A 1 26  ? 16.579  -12.866 23.903  1.00 31.74  ?  26  ALA A C    1 
ATOM   188  O  O    . ALA A 1 26  ? 15.793  -13.449 23.146  1.00 29.53  ?  26  ALA A O    1 
ATOM   189  C  CB   . ALA A 1 26  ? 16.289  -10.397 24.337  1.00 34.73  ?  26  ALA A CB   1 
ATOM   190  N  N    . LEU A 1 27  ? 17.889  -13.131 23.905  1.00 30.48  ?  27  LEU A N    1 
ATOM   191  C  CA   . LEU A 1 27  ? 18.416  -14.177 23.037  1.00 29.78  ?  27  LEU A CA   1 
ATOM   192  C  C    . LEU A 1 27  ? 17.884  -15.541 23.458  1.00 28.39  ?  27  LEU A C    1 
ATOM   193  O  O    . LEU A 1 27  ? 17.382  -16.308 22.628  1.00 29.06  ?  27  LEU A O    1 
ATOM   194  C  CB   . LEU A 1 27  ? 19.948  -14.148 23.056  1.00 28.61  ?  27  LEU A CB   1 
ATOM   195  C  CG   . LEU A 1 27  ? 20.652  -15.254 22.273  1.00 29.72  ?  27  LEU A CG   1 
ATOM   196  C  CD1  . LEU A 1 27  ? 20.195  -15.235 20.818  1.00 27.75  ?  27  LEU A CD1  1 
ATOM   197  C  CD2  . LEU A 1 27  ? 22.174  -15.116 22.365  1.00 32.97  ?  27  LEU A CD2  1 
ATOM   198  N  N    . THR A 1 28  ? 17.957  -15.846 24.754  1.00 31.64  ?  28  THR A N    1 
ATOM   199  C  CA   . THR A 1 28  ? 17.490  -17.141 25.241  1.00 30.10  ?  28  THR A CA   1 
ATOM   200  C  C    . THR A 1 28  ? 16.022  -17.368 24.900  1.00 30.80  ?  28  THR A C    1 
ATOM   201  O  O    . THR A 1 28  ? 15.633  -18.470 24.496  1.00 30.39  ?  28  THR A O    1 
ATOM   202  C  CB   . THR A 1 28  ? 17.738  -17.232 26.747  1.00 37.43  ?  28  THR A CB   1 
ATOM   203  O  OG1  . THR A 1 28  ? 19.149  -17.183 26.984  1.00 43.43  ?  28  THR A OG1  1 
ATOM   204  C  CG2  . THR A 1 28  ? 17.187  -18.523 27.320  1.00 38.86  ?  28  THR A CG2  1 
ATOM   205  N  N    . GLU A 1 29  ? 15.194  -16.334 25.040  1.00 29.39  ?  29  GLU A N    1 
ATOM   206  C  CA   . GLU A 1 29  ? 13.771  -16.488 24.754  1.00 29.77  ?  29  GLU A CA   1 
ATOM   207  C  C    . GLU A 1 29  ? 13.520  -16.681 23.267  1.00 28.90  ?  29  GLU A C    1 
ATOM   208  O  O    . GLU A 1 29  ? 12.634  -17.453 22.877  1.00 27.54  ?  29  GLU A O    1 
ATOM   209  C  CB   . GLU A 1 29  ? 12.997  -15.284 25.288  1.00 30.01  ?  29  GLU A CB   1 
ATOM   210  C  CG   . GLU A 1 29  ? 12.926  -15.265 26.808  1.00 32.41  ?  29  GLU A CG   1 
ATOM   211  C  CD   . GLU A 1 29  ? 12.711  -13.877 27.371  1.00 42.35  ?  29  GLU A CD   1 
ATOM   212  O  OE1  . GLU A 1 29  ? 12.468  -12.942 26.583  1.00 46.62  ?  29  GLU A OE1  1 
ATOM   213  O  OE2  . GLU A 1 29  ? 12.788  -13.720 28.608  1.00 47.74  -1 29  GLU A OE2  1 
ATOM   214  N  N    . ALA A 1 30  ? 14.285  -15.983 22.422  1.00 25.95  ?  30  ALA A N    1 
ATOM   215  C  CA   . ALA A 1 30  ? 14.114  -16.145 20.983  1.00 25.66  ?  30  ALA A CA   1 
ATOM   216  C  C    . ALA A 1 30  ? 14.533  -17.540 20.543  1.00 26.26  ?  30  ALA A C    1 
ATOM   217  O  O    . ALA A 1 30  ? 13.861  -18.161 19.706  1.00 24.78  ?  30  ALA A O    1 
ATOM   218  C  CB   . ALA A 1 30  ? 14.896  -15.068 20.232  1.00 24.32  ?  30  ALA A CB   1 
ATOM   219  N  N    . VAL A 1 31  ? 15.630  -18.054 21.108  1.00 26.06  ?  31  VAL A N    1 
ATOM   220  C  CA   . VAL A 1 31  ? 16.066  -19.408 20.779  1.00 28.76  ?  31  VAL A CA   1 
ATOM   221  C  C    . VAL A 1 31  ? 15.002  -20.414 21.187  1.00 28.81  ?  31  VAL A C    1 
ATOM   222  O  O    . VAL A 1 31  ? 14.632  -21.306 20.414  1.00 29.55  ?  31  VAL A O    1 
ATOM   223  C  CB   . VAL A 1 31  ? 17.424  -19.717 21.436  1.00 29.29  ?  31  VAL A CB   1 
ATOM   224  C  CG1  . VAL A 1 31  ? 17.787  -21.183 21.243  1.00 32.28  ?  31  VAL A CG1  1 
ATOM   225  C  CG2  . VAL A 1 31  ? 18.512  -18.813 20.878  1.00 29.79  ?  31  VAL A CG2  1 
ATOM   226  N  N    . ALA A 1 32  ? 14.486  -20.282 22.412  1.00 29.13  ?  32  ALA A N    1 
ATOM   227  C  CA   . ALA A 1 32  ? 13.457  -21.205 22.869  1.00 31.72  ?  32  ALA A CA   1 
ATOM   228  C  C    . ALA A 1 32  ? 12.246  -21.149 21.951  1.00 29.25  ?  32  ALA A C    1 
ATOM   229  O  O    . ALA A 1 32  ? 11.668  -22.186 21.609  1.00 32.56  ?  32  ALA A O    1 
ATOM   230  C  CB   . ALA A 1 32  ? 13.053  -20.871 24.305  1.00 34.17  ?  32  ALA A CB   1 
ATOM   231  N  N    . ALA A 1 33  ? 11.863  -19.943 21.528  1.00 26.90  ?  33  ALA A N    1 
ATOM   232  C  CA   . ALA A 1 33  ? 10.674  -19.783 20.697  1.00 27.11  ?  33  ALA A CA   1 
ATOM   233  C  C    . ALA A 1 33  ? 10.838  -20.493 19.360  1.00 27.94  ?  33  ALA A C    1 
ATOM   234  O  O    . ALA A 1 33  ? 9.947   -21.232 18.925  1.00 28.37  ?  33  ALA A O    1 
ATOM   235  C  CB   . ALA A 1 33  ? 10.378  -18.297 20.491  1.00 26.55  ?  33  ALA A CB   1 
ATOM   236  N  N    . ILE A 1 34  ? 11.969  -20.272 18.681  1.00 26.22  ?  34  ILE A N    1 
ATOM   237  C  CA   . ILE A 1 34  ? 12.158  -20.923 17.389  1.00 26.12  ?  34  ILE A CA   1 
ATOM   238  C  C    . ILE A 1 34  ? 12.296  -22.432 17.550  1.00 27.39  ?  34  ILE A C    1 
ATOM   239  O  O    . ILE A 1 34  ? 11.911  -23.194 16.655  1.00 27.40  ?  34  ILE A O    1 
ATOM   240  C  CB   . ILE A 1 34  ? 13.306  -20.281 16.590  1.00 25.16  ?  34  ILE A CB   1 
ATOM   241  C  CG1  . ILE A 1 34  ? 13.200  -20.669 15.110  1.00 25.84  ?  34  ILE A CG1  1 
ATOM   242  C  CG2  . ILE A 1 34  ? 14.659  -20.685 17.170  1.00 26.12  ?  34  ILE A CG2  1 
ATOM   243  C  CD1  . ILE A 1 34  ? 14.020  -19.780 14.176  1.00 24.45  ?  34  ILE A CD1  1 
ATOM   244  N  N    . GLU A 1 35  ? 12.806  -22.893 18.694  1.00 29.42  ?  35  GLU A N    1 
ATOM   245  C  CA   . GLU A 1 35  ? 12.915  -24.328 18.931  1.00 30.38  ?  35  GLU A CA   1 
ATOM   246  C  C    . GLU A 1 35  ? 11.561  -25.001 19.141  1.00 33.81  ?  35  GLU A C    1 
ATOM   247  O  O    . GLU A 1 35  ? 11.457  -26.217 18.935  1.00 36.44  ?  35  GLU A O    1 
ATOM   248  C  CB   . GLU A 1 35  ? 13.891  -24.613 20.077  1.00 33.40  ?  35  GLU A CB   1 
ATOM   249  C  CG   . GLU A 1 35  ? 15.324  -24.219 19.705  1.00 32.21  ?  35  GLU A CG   1 
ATOM   250  C  CD   . GLU A 1 35  ? 16.383  -24.762 20.646  1.00 41.11  ?  35  GLU A CD   1 
ATOM   251  O  OE1  . GLU A 1 35  ? 16.216  -24.670 21.876  1.00 45.31  ?  35  GLU A OE1  1 
ATOM   252  O  OE2  . GLU A 1 35  ? 17.399  -25.286 20.148  1.00 48.96  -1 35  GLU A OE2  1 
ATOM   253  N  N    . THR A 1 36  ? 10.520  -24.252 19.537  1.00 31.20  ?  36  THR A N    1 
ATOM   254  C  CA   . THR A 1 36  ? 9.183   -24.843 19.542  1.00 34.33  ?  36  THR A CA   1 
ATOM   255  C  C    . THR A 1 36  ? 8.775   -25.288 18.143  1.00 32.48  ?  36  THR A C    1 
ATOM   256  O  O    . THR A 1 36  ? 8.005   -26.243 17.993  1.00 35.98  ?  36  THR A O    1 
ATOM   257  C  CB   . THR A 1 36  ? 8.117   -23.908 20.149  1.00 34.11  ?  36  THR A CB   1 
ATOM   258  O  OG1  . THR A 1 36  ? 7.902   -22.763 19.311  1.00 31.99  ?  36  THR A OG1  1 
ATOM   259  C  CG2  . THR A 1 36  ? 8.491   -23.456 21.561  1.00 33.82  ?  36  THR A CG2  1 
ATOM   260  N  N    . TYR A 1 37  ? 9.294   -24.630 17.109  1.00 29.54  ?  37  TYR A N    1 
ATOM   261  C  CA   . TYR A 1 37  ? 8.964   -25.006 15.742  1.00 28.30  ?  37  TYR A CA   1 
ATOM   262  C  C    . TYR A 1 37  ? 9.955   -26.007 15.171  1.00 30.95  ?  37  TYR A C    1 
ATOM   263  O  O    . TYR A 1 37  ? 9.565   -26.930 14.446  1.00 31.78  ?  37  TYR A O    1 
ATOM   264  C  CB   . TYR A 1 37  ? 9.014   -23.777 14.844  1.00 28.02  ?  37  TYR A CB   1 
ATOM   265  C  CG   . TYR A 1 37  ? 7.923   -22.749 15.009  1.00 25.69  ?  37  TYR A CG   1 
ATOM   266  C  CD1  . TYR A 1 37  ? 6.763   -22.818 14.245  1.00 26.18  ?  37  TYR A CD1  1 
ATOM   267  C  CD2  . TYR A 1 37  ? 8.080   -21.670 15.871  1.00 25.11  ?  37  TYR A CD2  1 
ATOM   268  C  CE1  . TYR A 1 37  ? 5.779   -21.857 14.356  1.00 25.15  ?  37  TYR A CE1  1 
ATOM   269  C  CE2  . TYR A 1 37  ? 7.106   -20.697 15.983  1.00 25.98  ?  37  TYR A CE2  1 
ATOM   270  C  CZ   . TYR A 1 37  ? 5.961   -20.795 15.218  1.00 25.76  ?  37  TYR A CZ   1 
ATOM   271  O  OH   . TYR A 1 37  ? 4.987   -19.826 15.307  1.00 25.55  ?  37  TYR A OH   1 
ATOM   272  N  N    . PHE A 1 38  ? 11.237  -25.835 15.470  1.00 30.40  ?  38  PHE A N    1 
ATOM   273  C  CA   . PHE A 1 38  ? 12.295  -26.663 14.897  1.00 29.14  ?  38  PHE A CA   1 
ATOM   274  C  C    . PHE A 1 38  ? 13.130  -27.221 16.037  1.00 33.40  ?  38  PHE A C    1 
ATOM   275  O  O    . PHE A 1 38  ? 14.200  -26.686 16.361  1.00 34.78  ?  38  PHE A O    1 
ATOM   276  C  CB   . PHE A 1 38  ? 13.148  -25.857 13.919  1.00 29.29  ?  38  PHE A CB   1 
ATOM   277  C  CG   . PHE A 1 38  ? 12.344  -25.054 12.932  1.00 25.51  ?  38  PHE A CG   1 
ATOM   278  C  CD1  . PHE A 1 38  ? 11.515  -25.685 12.020  1.00 26.62  ?  38  PHE A CD1  1 
ATOM   279  C  CD2  . PHE A 1 38  ? 12.410  -23.676 12.922  1.00 23.07  ?  38  PHE A CD2  1 
ATOM   280  C  CE1  . PHE A 1 38  ? 10.786  -24.951 11.107  1.00 26.95  ?  38  PHE A CE1  1 
ATOM   281  C  CE2  . PHE A 1 38  ? 11.684  -22.946 12.019  1.00 23.27  ?  38  PHE A CE2  1 
ATOM   282  C  CZ   . PHE A 1 38  ? 10.872  -23.586 11.109  1.00 25.44  ?  38  PHE A CZ   1 
ATOM   283  N  N    . PRO A 1 39  ? 12.676  -28.299 16.666  1.00 34.70  ?  39  PRO A N    1 
ATOM   284  C  CA   . PRO A 1 39  ? 13.405  -28.846 17.817  1.00 37.97  ?  39  PRO A CA   1 
ATOM   285  C  C    . PRO A 1 39  ? 14.734  -29.461 17.399  1.00 39.74  ?  39  PRO A C    1 
ATOM   286  O  O    . PRO A 1 39  ? 15.009  -29.709 16.223  1.00 40.73  ?  39  PRO A O    1 
ATOM   287  C  CB   . PRO A 1 39  ? 12.453  -29.903 18.385  1.00 40.87  ?  39  PRO A CB   1 
ATOM   288  C  CG   . PRO A 1 39  ? 11.512  -30.225 17.260  1.00 42.45  ?  39  PRO A CG   1 
ATOM   289  C  CD   . PRO A 1 39  ? 11.397  -28.989 16.425  1.00 37.41  ?  39  PRO A CD   1 
ATOM   290  N  N    . ASP A 1 40  ? 15.574  -29.695 18.398  1.00 41.80  ?  40  ASP A N    1 
ATOM   291  C  CA   . ASP A 1 40  ? 16.875  -30.317 18.186  1.00 48.48  ?  40  ASP A CA   1 
ATOM   292  C  C    . ASP A 1 40  ? 16.660  -31.718 17.626  1.00 49.53  ?  40  ASP A C    1 
ATOM   293  O  O    . ASP A 1 40  ? 16.153  -32.595 18.336  1.00 48.85  ?  40  ASP A O    1 
ATOM   294  C  CB   . ASP A 1 40  ? 17.631  -30.387 19.513  1.00 50.23  ?  40  ASP A CB   1 
ATOM   295  C  CG   . ASP A 1 40  ? 19.074  -30.810 19.342  1.00 57.98  ?  40  ASP A CG   1 
ATOM   296  O  OD1  . ASP A 1 40  ? 19.521  -30.954 18.184  1.00 56.43  ?  40  ASP A OD1  1 
ATOM   297  O  OD2  . ASP A 1 40  ? 19.760  -30.998 20.369  1.00 64.34  -1 40  ASP A OD2  1 
ATOM   298  N  N    . PRO A 1 41  ? 17.014  -31.968 16.361  1.00 47.14  ?  41  PRO A N    1 
ATOM   299  C  CA   . PRO A 1 41  ? 16.741  -33.286 15.766  1.00 49.07  ?  41  PRO A CA   1 
ATOM   300  C  C    . PRO A 1 41  ? 17.509  -34.423 16.416  1.00 53.40  ?  41  PRO A C    1 
ATOM   301  O  O    . PRO A 1 41  ? 17.184  -35.591 16.160  1.00 54.31  ?  41  PRO A O    1 
ATOM   302  C  CB   . PRO A 1 41  ? 17.142  -33.103 14.297  1.00 45.84  ?  41  PRO A CB   1 
ATOM   303  C  CG   . PRO A 1 41  ? 18.149  -31.997 14.318  1.00 45.51  ?  41  PRO A CG   1 
ATOM   304  C  CD   . PRO A 1 41  ? 17.713  -31.070 15.425  1.00 43.45  ?  41  PRO A CD   1 
ATOM   305  N  N    . GLU A 1 42  ? 18.507  -34.126 17.239  1.00 52.82  ?  42  GLU A N    1 
ATOM   306  C  CA   . GLU A 1 42  ? 19.209  -35.159 17.986  1.00 62.41  ?  42  GLU A CA   1 
ATOM   307  C  C    . GLU A 1 42  ? 18.243  -35.890 18.917  1.00 68.54  ?  42  GLU A C    1 
ATOM   308  O  O    . GLU A 1 42  ? 18.399  -37.083 19.183  1.00 67.02  ?  42  GLU A O    1 
ATOM   309  C  CB   . GLU A 1 42  ? 20.365  -34.545 18.782  1.00 67.07  ?  42  GLU A CB   1 
ATOM   310  C  CG   . GLU A 1 42  ? 20.406  -34.935 20.257  1.00 72.74  ?  42  GLU A CG   1 
ATOM   311  C  CD   . GLU A 1 42  ? 19.538  -34.043 21.131  1.00 74.20  ?  42  GLU A CD   1 
ATOM   312  O  OE1  . GLU A 1 42  ? 18.362  -33.810 20.776  1.00 70.58  ?  42  GLU A OE1  1 
ATOM   313  O  OE2  . GLU A 1 42  ? 20.039  -33.571 22.174  1.00 78.07  -1 42  GLU A OE2  1 
ATOM   314  N  N    . VAL A 1 51  ? 11.147  -34.715 9.451   1.00 63.97  ?  51  VAL A N    1 
ATOM   315  C  CA   . VAL A 1 51  ? 11.897  -33.476 9.267   1.00 55.37  ?  51  VAL A CA   1 
ATOM   316  C  C    . VAL A 1 51  ? 11.581  -32.818 7.925   1.00 52.64  ?  51  VAL A C    1 
ATOM   317  O  O    . VAL A 1 51  ? 11.869  -31.638 7.720   1.00 48.31  ?  51  VAL A O    1 
ATOM   318  C  CB   . VAL A 1 51  ? 13.415  -33.696 9.473   1.00 57.49  ?  51  VAL A CB   1 
ATOM   319  C  CG1  . VAL A 1 51  ? 14.224  -32.651 8.718   1.00 48.42  ?  51  VAL A CG1  1 
ATOM   320  C  CG2  . VAL A 1 51  ? 13.757  -33.668 10.963  1.00 52.84  ?  51  VAL A CG2  1 
ATOM   321  N  N    . ALA A 1 52  ? 10.969  -33.582 7.017   1.00 53.98  ?  52  ALA A N    1 
ATOM   322  C  CA   . ALA A 1 52  ? 10.627  -33.051 5.699   1.00 49.47  ?  52  ALA A CA   1 
ATOM   323  C  C    . ALA A 1 52  ? 9.805   -31.770 5.813   1.00 47.56  ?  52  ALA A C    1 
ATOM   324  O  O    . ALA A 1 52  ? 10.165  -30.726 5.255   1.00 46.48  ?  52  ALA A O    1 
ATOM   325  C  CB   . ALA A 1 52  ? 9.877   -34.112 4.890   1.00 55.05  ?  52  ALA A CB   1 
ATOM   326  N  N    . ALA A 1 53  ? 8.683   -31.838 6.533   1.00 47.31  ?  53  ALA A N    1 
ATOM   327  C  CA   . ALA A 1 53  ? 7.858   -30.650 6.728   1.00 47.99  ?  53  ALA A CA   1 
ATOM   328  C  C    . ALA A 1 53  ? 8.607   -29.564 7.488   1.00 42.49  ?  53  ALA A C    1 
ATOM   329  O  O    . ALA A 1 53  ? 8.342   -28.371 7.287   1.00 38.23  ?  53  ALA A O    1 
ATOM   330  C  CB   . ALA A 1 53  ? 6.562   -31.022 7.451   1.00 44.36  ?  53  ALA A CB   1 
ATOM   331  N  N    . LEU A 1 54  ? 9.559   -29.949 8.347   1.00 39.89  ?  54  LEU A N    1 
ATOM   332  C  CA   . LEU A 1 54  ? 10.313  -28.970 9.124   1.00 38.17  ?  54  LEU A CA   1 
ATOM   333  C  C    . LEU A 1 54  ? 11.326  -28.188 8.292   1.00 34.36  ?  54  LEU A C    1 
ATOM   334  O  O    . LEU A 1 54  ? 11.930  -27.245 8.815   1.00 32.61  ?  54  LEU A O    1 
ATOM   335  C  CB   . LEU A 1 54  ? 10.991  -29.630 10.326  1.00 38.58  ?  54  LEU A CB   1 
ATOM   336  C  CG   . LEU A 1 54  ? 10.054  -30.202 11.394  1.00 42.64  ?  54  LEU A CG   1 
ATOM   337  C  CD1  . LEU A 1 54  ? 10.848  -30.665 12.608  1.00 43.43  ?  54  LEU A CD1  1 
ATOM   338  C  CD2  . LEU A 1 54  ? 8.983   -29.195 11.795  1.00 43.82  ?  54  LEU A CD2  1 
ATOM   339  N  N    . LYS A 1 55  ? 11.523  -28.541 7.022   1.00 31.88  ?  55  LYS A N    1 
ATOM   340  C  CA   . LYS A 1 55  ? 12.353  -27.730 6.141   1.00 31.58  ?  55  LYS A CA   1 
ATOM   341  C  C    . LYS A 1 55  ? 11.629  -26.501 5.596   1.00 28.99  ?  55  LYS A C    1 
ATOM   342  O  O    . LYS A 1 55  ? 12.276  -25.629 5.012   1.00 28.21  ?  55  LYS A O    1 
ATOM   343  C  CB   . LYS A 1 55  ? 12.895  -28.575 4.982   1.00 33.88  ?  55  LYS A CB   1 
ATOM   344  C  CG   . LYS A 1 55  ? 13.809  -29.717 5.416   1.00 38.34  ?  55  LYS A CG   1 
ATOM   345  C  CD   . LYS A 1 55  ? 14.357  -30.465 4.214   1.00 39.03  ?  55  LYS A CD   1 
ATOM   346  C  CE   . LYS A 1 55  ? 15.251  -31.627 4.648   1.00 42.02  ?  55  LYS A CE   1 
ATOM   347  N  NZ   . LYS A 1 55  ? 15.698  -32.440 3.481   1.00 43.63  ?  55  LYS A NZ   1 
ATOM   348  N  N    . HIS A 1 56  ? 10.315  -26.388 5.783   1.00 28.64  ?  56  HIS A N    1 
ATOM   349  C  CA   . HIS A 1 56  ? 9.588   -25.261 5.212   1.00 28.03  ?  56  HIS A CA   1 
ATOM   350  C  C    . HIS A 1 56  ? 9.639   -24.050 6.133   1.00 24.14  ?  56  HIS A C    1 
ATOM   351  O  O    . HIS A 1 56  ? 9.488   -24.173 7.351   1.00 27.45  ?  56  HIS A O    1 
ATOM   352  C  CB   . HIS A 1 56  ? 8.137   -25.651 4.936   1.00 29.94  ?  56  HIS A CB   1 
ATOM   353  C  CG   . HIS A 1 56  ? 7.975   -26.524 3.732   1.00 37.07  ?  56  HIS A CG   1 
ATOM   354  N  ND1  . HIS A 1 56  ? 7.526   -26.041 2.521   1.00 37.35  ?  56  HIS A ND1  1 
ATOM   355  C  CD2  . HIS A 1 56  ? 8.223   -27.842 3.545   1.00 42.26  ?  56  HIS A CD2  1 
ATOM   356  C  CE1  . HIS A 1 56  ? 7.494   -27.029 1.643   1.00 43.98  ?  56  HIS A CE1  1 
ATOM   357  N  NE2  . HIS A 1 56  ? 7.912   -28.132 2.239   1.00 42.89  ?  56  HIS A NE2  1 
ATOM   358  N  N    . ALA A 1 57  ? 9.856   -22.882 5.534   1.00 25.20  ?  57  ALA A N    1 
ATOM   359  C  CA   . ALA A 1 57  ? 9.788   -21.630 6.272   1.00 21.93  ?  57  ALA A CA   1 
ATOM   360  C  C    . ALA A 1 57  ? 8.369   -21.431 6.795   1.00 22.76  ?  57  ALA A C    1 
ATOM   361  O  O    . ALA A 1 57  ? 7.397   -21.793 6.129   1.00 25.29  ?  57  ALA A O    1 
ATOM   362  C  CB   . ALA A 1 57  ? 10.131  -20.483 5.324   1.00 24.31  ?  57  ALA A CB   1 
ATOM   363  N  N    . VAL A 1 58  ? 8.259   -20.858 7.986   1.00 18.05  ?  58  VAL A N    1 
ATOM   364  C  CA   . VAL A 1 58  ? 6.983   -20.548 8.634   1.00 17.32  ?  58  VAL A CA   1 
ATOM   365  C  C    . VAL A 1 58  ? 6.833   -19.034 8.667   1.00 17.66  ?  58  VAL A C    1 
ATOM   366  O  O    . VAL A 1 58  ? 7.725   -18.349 9.176   1.00 16.79  ?  58  VAL A O    1 
ATOM   367  C  CB   . VAL A 1 58  ? 6.947   -21.113 10.062  1.00 19.41  ?  58  VAL A CB   1 
ATOM   368  C  CG1  . VAL A 1 58  ? 5.699   -20.654 10.799  1.00 23.84  ?  58  VAL A CG1  1 
ATOM   369  C  CG2  . VAL A 1 58  ? 7.055   -22.634 10.015  1.00 23.86  ?  58  VAL A CG2  1 
ATOM   370  N  N    . PRO A 1 59  ? 5.738   -18.478 8.156   1.00 16.94  ?  59  PRO A N    1 
ATOM   371  C  CA   . PRO A 1 59  ? 5.600   -17.023 8.066   1.00 17.57  ?  59  PRO A CA   1 
ATOM   372  C  C    . PRO A 1 59  ? 5.097   -16.381 9.356   1.00 17.56  ?  59  PRO A C    1 
ATOM   373  O  O    . PRO A 1 59  ? 4.399   -16.998 10.169  1.00 19.52  ?  59  PRO A O    1 
ATOM   374  C  CB   . PRO A 1 59  ? 4.565   -16.846 6.943   1.00 18.07  ?  59  PRO A CB   1 
ATOM   375  C  CG   . PRO A 1 59  ? 3.714   -18.079 7.036   1.00 19.75  ?  59  PRO A CG   1 
ATOM   376  C  CD   . PRO A 1 59  ? 4.679   -19.196 7.419   1.00 21.17  ?  59  PRO A CD   1 
ATOM   377  N  N    . PHE A 1 60  ? 5.453   -15.101 9.499   1.00 17.32  ?  60  PHE A N    1 
ATOM   378  C  CA   . PHE A 1 60  ? 4.917   -14.226 10.544  1.00 17.61  ?  60  PHE A CA   1 
ATOM   379  C  C    . PHE A 1 60  ? 3.399   -14.114 10.376  1.00 17.31  ?  60  PHE A C    1 
ATOM   380  O  O    . PHE A 1 60  ? 2.897   -14.163 9.250   1.00 18.67  ?  60  PHE A O    1 
ATOM   381  C  CB   . PHE A 1 60  ? 5.590   -12.860 10.356  1.00 17.37  ?  60  PHE A CB   1 
ATOM   382  C  CG   . PHE A 1 60  ? 5.072   -11.740 11.241  1.00 18.90  ?  60  PHE A CG   1 
ATOM   383  C  CD1  . PHE A 1 60  ? 3.869   -11.106 10.953  1.00 19.46  ?  60  PHE A CD1  1 
ATOM   384  C  CD2  . PHE A 1 60  ? 5.862   -11.239 12.265  1.00 20.84  ?  60  PHE A CD2  1 
ATOM   385  C  CE1  . PHE A 1 60  ? 3.422   -10.047 11.744  1.00 20.71  ?  60  PHE A CE1  1 
ATOM   386  C  CE2  . PHE A 1 60  ? 5.429   -10.182 13.052  1.00 20.23  ?  60  PHE A CE2  1 
ATOM   387  C  CZ   . PHE A 1 60  ? 4.204   -9.587  12.784  1.00 21.33  ?  60  PHE A CZ   1 
ATOM   388  N  N    . PRO A 1 61  ? 2.637   -13.982 11.474  1.00 17.32  ?  61  PRO A N    1 
ATOM   389  C  CA   . PRO A 1 61  ? 3.059   -13.881 12.871  1.00 17.69  ?  61  PRO A CA   1 
ATOM   390  C  C    . PRO A 1 61  ? 3.267   -15.248 13.506  1.00 19.23  ?  61  PRO A C    1 
ATOM   391  O  O    . PRO A 1 61  ? 2.610   -16.251 13.189  1.00 20.21  ?  61  PRO A O    1 
ATOM   392  C  CB   . PRO A 1 61  ? 1.873   -13.142 13.533  1.00 19.34  ?  61  PRO A CB   1 
ATOM   393  C  CG   . PRO A 1 61  ? 0.690   -13.572 12.741  1.00 20.34  ?  61  PRO A CG   1 
ATOM   394  C  CD   . PRO A 1 61  ? 1.198   -13.675 11.319  1.00 19.12  ?  61  PRO A CD   1 
ATOM   395  N  N    . PHE A 1 62  ? 4.205   -15.286 14.448  1.00 18.88  ?  62  PHE A N    1 
ATOM   396  C  CA   . PHE A 1 62  ? 4.586   -16.500 15.147  1.00 21.20  ?  62  PHE A CA   1 
ATOM   397  C  C    . PHE A 1 62  ? 3.818   -16.644 16.456  1.00 22.87  ?  62  PHE A C    1 
ATOM   398  O  O    . PHE A 1 62  ? 3.093   -15.745 16.892  1.00 23.14  ?  62  PHE A O    1 
ATOM   399  C  CB   . PHE A 1 62  ? 6.096   -16.485 15.389  1.00 20.74  ?  62  PHE A CB   1 
ATOM   400  C  CG   . PHE A 1 62  ? 6.879   -16.072 14.179  1.00 19.52  ?  62  PHE A CG   1 
ATOM   401  C  CD1  . PHE A 1 62  ? 6.889   -16.876 13.045  1.00 19.60  ?  62  PHE A CD1  1 
ATOM   402  C  CD2  . PHE A 1 62  ? 7.532   -14.855 14.140  1.00 19.84  ?  62  PHE A CD2  1 
ATOM   403  C  CE1  . PHE A 1 62  ? 7.564   -16.489 11.901  1.00 17.04  ?  62  PHE A CE1  1 
ATOM   404  C  CE2  . PHE A 1 62  ? 8.238   -14.456 12.989  1.00 19.25  ?  62  PHE A CE2  1 
ATOM   405  C  CZ   . PHE A 1 62  ? 8.239   -15.276 11.867  1.00 19.56  ?  62  PHE A CZ   1 
ATOM   406  N  N    . THR A 1 63  ? 3.963   -17.810 17.073  1.00 22.79  ?  63  THR A N    1 
ATOM   407  C  CA   . THR A 1 63  ? 3.270   -18.083 18.329  1.00 23.40  ?  63  THR A CA   1 
ATOM   408  C  C    . THR A 1 63  ? 3.947   -17.446 19.535  1.00 24.28  ?  63  THR A C    1 
ATOM   409  O  O    . THR A 1 63  ? 3.425   -17.574 20.652  1.00 28.12  ?  63  THR A O    1 
ATOM   410  C  CB   . THR A 1 63  ? 3.129   -19.593 18.552  1.00 29.11  ?  63  THR A CB   1 
ATOM   411  O  OG1  . THR A 1 63  ? 4.419   -20.203 18.497  1.00 29.65  ?  63  THR A OG1  1 
ATOM   412  C  CG2  . THR A 1 63  ? 2.231   -20.212 17.495  1.00 31.58  ?  63  THR A CG2  1 
ATOM   413  N  N    . SER A 1 64  ? 5.062   -16.750 19.345  1.00 23.50  ?  64  SER A N    1 
ATOM   414  C  CA   . SER A 1 64  ? 5.755   -16.086 20.434  1.00 25.04  ?  64  SER A CA   1 
ATOM   415  C  C    . SER A 1 64  ? 6.189   -14.700 19.991  1.00 23.13  ?  64  SER A C    1 
ATOM   416  O  O    . SER A 1 64  ? 6.727   -14.523 18.890  1.00 21.79  ?  64  SER A O    1 
ATOM   417  C  CB   . SER A 1 64  ? 7.002   -16.874 20.844  1.00 28.47  ?  64  SER A CB   1 
ATOM   418  O  OG   . SER A 1 64  ? 7.837   -16.109 21.699  1.00 29.62  ?  64  SER A OG   1 
ATOM   419  N  N    . ASN A 1 65  ? 5.995   -13.724 20.872  1.00 23.31  ?  65  ASN A N    1 
ATOM   420  C  CA   . ASN A 1 65  ? 6.489   -12.383 20.602  1.00 21.17  ?  65  ASN A CA   1 
ATOM   421  C  C    . ASN A 1 65  ? 7.993   -12.241 20.798  1.00 22.56  ?  65  ASN A C    1 
ATOM   422  O  O    . ASN A 1 65  ? 8.555   -11.231 20.361  1.00 23.72  ?  65  ASN A O    1 
ATOM   423  C  CB   . ASN A 1 65  ? 5.685   -11.353 21.399  1.00 22.52  ?  65  ASN A CB   1 
ATOM   424  C  CG   . ASN A 1 65  ? 4.283   -11.200 20.842  1.00 21.69  ?  65  ASN A CG   1 
ATOM   425  O  OD1  . ASN A 1 65  ? 4.091   -11.293 19.630  1.00 20.93  ?  65  ASN A OD1  1 
ATOM   426  N  ND2  . ASN A 1 65  ? 3.305   -11.024 21.708  1.00 22.45  ?  65  ASN A ND2  1 
ATOM   427  N  N    . ALA A 1 66  ? 8.647   -13.230 21.415  1.00 23.56  ?  66  ALA A N    1 
ATOM   428  C  CA   . ALA A 1 66  ? 10.105  -13.312 21.371  1.00 23.62  ?  66  ALA A CA   1 
ATOM   429  C  C    . ALA A 1 66  ? 10.627  -13.531 19.956  1.00 24.57  ?  66  ALA A C    1 
ATOM   430  O  O    . ALA A 1 66  ? 11.846  -13.494 19.744  1.00 26.42  ?  66  ALA A O    1 
ATOM   431  C  CB   . ALA A 1 66  ? 10.591  -14.422 22.303  1.00 26.12  ?  66  ALA A CB   1 
ATOM   432  N  N    . LEU A 1 67  ? 9.750   -13.785 18.994  1.00 21.46  ?  67  LEU A N    1 
ATOM   433  C  CA   . LEU A 1 67  ? 10.097  -13.751 17.577  1.00 21.39  ?  67  LEU A CA   1 
ATOM   434  C  C    . LEU A 1 67  ? 9.425   -12.604 16.845  1.00 21.86  ?  67  LEU A C    1 
ATOM   435  O  O    . LEU A 1 67  ? 10.075  -11.908 16.071  1.00 22.24  ?  67  LEU A O    1 
ATOM   436  C  CB   . LEU A 1 67  ? 9.721   -15.078 16.904  1.00 22.34  ?  67  LEU A CB   1 
ATOM   437  C  CG   . LEU A 1 67  ? 10.482  -16.311 17.415  1.00 22.15  ?  67  LEU A CG   1 
ATOM   438  C  CD1  . LEU A 1 67  ? 9.811   -17.603 16.953  1.00 25.69  ?  67  LEU A CD1  1 
ATOM   439  C  CD2  . LEU A 1 67  ? 11.956  -16.275 16.982  1.00 26.53  ?  67  LEU A CD2  1 
ATOM   440  N  N    . ASN A 1 68  ? 8.140   -12.358 17.122  1.00 21.45  ?  68  ASN A N    1 
ATOM   441  C  CA   . ASN A 1 68  ? 7.395   -11.346 16.382  1.00 19.60  ?  68  ASN A CA   1 
ATOM   442  C  C    . ASN A 1 68  ? 7.979   -9.950  16.537  1.00 20.48  ?  68  ASN A C    1 
ATOM   443  O  O    . ASN A 1 68  ? 7.872   -9.136  15.613  1.00 21.78  ?  68  ASN A O    1 
ATOM   444  C  CB   . ASN A 1 68  ? 5.937   -11.312 16.836  1.00 19.37  ?  68  ASN A CB   1 
ATOM   445  C  CG   . ASN A 1 68  ? 5.160   -12.520 16.381  1.00 20.49  ?  68  ASN A CG   1 
ATOM   446  O  OD1  . ASN A 1 68  ? 5.363   -13.019 15.280  1.00 20.04  ?  68  ASN A OD1  1 
ATOM   447  N  ND2  . ASN A 1 68  ? 4.251   -12.990 17.230  1.00 21.94  ?  68  ASN A ND2  1 
ATOM   448  N  N    . ARG A 1 69  ? 8.539   -9.625  17.700  1.00 21.87  ?  69  ARG A N    1 
ATOM   449  C  CA   . ARG A 1 69  ? 8.924   -8.236  17.915  1.00 22.85  ?  69  ARG A CA   1 
ATOM   450  C  C    . ARG A 1 69  ? 10.185  -7.849  17.149  1.00 23.30  ?  69  ARG A C    1 
ATOM   451  O  O    . ARG A 1 69  ? 10.411  -6.659  16.913  1.00 24.95  ?  69  ARG A O    1 
ATOM   452  C  CB   . ARG A 1 69  ? 9.072   -7.931  19.408  1.00 25.87  ?  69  ARG A CB   1 
ATOM   453  C  CG   . ARG A 1 69  ? 10.299  -8.536  20.072  1.00 25.75  ?  69  ARG A CG   1 
ATOM   454  C  CD   . ARG A 1 69  ? 10.434  -7.976  21.475  1.00 26.92  ?  69  ARG A CD   1 
ATOM   455  N  NE   . ARG A 1 69  ? 9.216   -8.239  22.233  1.00 29.84  ?  69  ARG A NE   1 
ATOM   456  C  CZ   . ARG A 1 69  ? 9.054   -9.282  23.033  1.00 28.63  ?  69  ARG A CZ   1 
ATOM   457  N  NH1  . ARG A 1 69  ? 10.049  -10.118 23.286  1.00 30.52  ?  69  ARG A NH1  1 
ATOM   458  N  NH2  . ARG A 1 69  ? 7.864   -9.491  23.594  1.00 28.93  ?  69  ARG A NH2  1 
ATOM   459  N  N    . HIS A 1 70  ? 11.001  -8.812  16.749  1.00 21.58  ?  70  HIS A N    1 
ATOM   460  C  CA   . HIS A 1 70  ? 12.337  -8.466  16.265  1.00 23.12  ?  70  HIS A CA   1 
ATOM   461  C  C    . HIS A 1 70  ? 12.406  -7.790  14.899  1.00 21.30  ?  70  HIS A C    1 
ATOM   462  O  O    . HIS A 1 70  ? 13.215  -6.871  14.728  1.00 22.39  ?  70  HIS A O    1 
ATOM   463  C  CB   . HIS A 1 70  ? 13.271  -9.667  16.365  1.00 25.08  ?  70  HIS A CB   1 
ATOM   464  C  CG   . HIS A 1 70  ? 13.405  -10.172 17.760  1.00 26.53  ?  70  HIS A CG   1 
ATOM   465  N  ND1  . HIS A 1 70  ? 13.744  -9.350  18.814  1.00 28.83  ?  70  HIS A ND1  1 
ATOM   466  C  CD2  . HIS A 1 70  ? 13.173  -11.395 18.293  1.00 30.00  ?  70  HIS A CD2  1 
ATOM   467  C  CE1  . HIS A 1 70  ? 13.760  -10.056 19.930  1.00 29.36  ?  70  HIS A CE1  1 
ATOM   468  N  NE2  . HIS A 1 70  ? 13.419  -11.299 19.640  1.00 29.85  ?  70  HIS A NE2  1 
ATOM   469  N  N    . PRO A 1 71  ? 11.606  -8.186  13.910  1.00 20.92  ?  71  PRO A N    1 
ATOM   470  C  CA   . PRO A 1 71  ? 11.624  -7.442  12.641  1.00 22.28  ?  71  PRO A CA   1 
ATOM   471  C  C    . PRO A 1 71  ? 11.239  -5.985  12.810  1.00 23.98  ?  71  PRO A C    1 
ATOM   472  O  O    . PRO A 1 71  ? 11.548  -5.165  11.938  1.00 26.26  ?  71  PRO A O    1 
ATOM   473  C  CB   . PRO A 1 71  ? 10.604  -8.188  11.772  1.00 20.98  ?  71  PRO A CB   1 
ATOM   474  C  CG   . PRO A 1 71  ? 10.546  -9.556  12.352  1.00 24.95  ?  71  PRO A CG   1 
ATOM   475  C  CD   . PRO A 1 71  ? 10.720  -9.360  13.847  1.00 22.50  ?  71  PRO A CD   1 
ATOM   476  N  N    . LEU A 1 72  ? 10.563  -5.640  13.903  1.00 20.23  ?  72  LEU A N    1 
ATOM   477  C  CA   . LEU A 1 72  ? 10.122  -4.280  14.157  1.00 24.18  ?  72  LEU A CA   1 
ATOM   478  C  C    . LEU A 1 72  ? 10.990  -3.565  15.182  1.00 23.75  ?  72  LEU A C    1 
ATOM   479  O  O    . LEU A 1 72  ? 10.611  -2.497  15.664  1.00 24.98  ?  72  LEU A O    1 
ATOM   480  C  CB   . LEU A 1 72  ? 8.665   -4.300  14.615  1.00 22.29  ?  72  LEU A CB   1 
ATOM   481  C  CG   . LEU A 1 72  ? 7.754   -5.066  13.658  1.00 22.32  ?  72  LEU A CG   1 
ATOM   482  C  CD1  . LEU A 1 72  ? 6.345   -5.134  14.248  1.00 24.13  ?  72  LEU A CD1  1 
ATOM   483  C  CD2  . LEU A 1 72  ? 7.739   -4.408  12.276  1.00 27.84  ?  72  LEU A CD2  1 
ATOM   484  N  N    . ASP A 1 73  ? 12.151  -4.122  15.516  1.00 21.42  ?  73  ASP A N    1 
ATOM   485  C  CA   . ASP A 1 73  ? 13.032  -3.516  16.510  1.00 22.92  ?  73  ASP A CA   1 
ATOM   486  C  C    . ASP A 1 73  ? 13.331  -2.073  16.118  1.00 23.93  ?  73  ASP A C    1 
ATOM   487  O  O    . ASP A 1 73  ? 13.617  -1.781  14.953  1.00 22.12  ?  73  ASP A O    1 
ATOM   488  C  CB   . ASP A 1 73  ? 14.322  -4.347  16.549  1.00 24.91  ?  73  ASP A CB   1 
ATOM   489  C  CG   . ASP A 1 73  ? 15.270  -3.956  17.677  1.00 26.98  ?  73  ASP A CG   1 
ATOM   490  O  OD1  . ASP A 1 73  ? 15.820  -2.828  17.659  1.00 30.19  ?  73  ASP A OD1  1 
ATOM   491  O  OD2  . ASP A 1 73  ? 15.475  -4.794  18.585  1.00 29.28  -1 73  ASP A OD2  1 
ATOM   492  N  N    . LEU A 1 74  ? 13.242  -1.165  17.093  1.00 25.28  ?  74  LEU A N    1 
ATOM   493  C  CA   . LEU A 1 74  ? 13.490  0.246   16.810  1.00 24.76  ?  74  LEU A CA   1 
ATOM   494  C  C    . LEU A 1 74  ? 14.865  0.474   16.188  1.00 28.26  ?  74  LEU A C    1 
ATOM   495  O  O    . LEU A 1 74  ? 15.042  1.410   15.402  1.00 26.17  ?  74  LEU A O    1 
ATOM   496  C  CB   . LEU A 1 74  ? 13.326  1.072   18.090  1.00 28.47  ?  74  LEU A CB   1 
ATOM   497  C  CG   . LEU A 1 74  ? 11.930  1.127   18.700  1.00 31.80  ?  74  LEU A CG   1 
ATOM   498  C  CD1  . LEU A 1 74  ? 11.969  1.920   20.000  1.00 33.83  ?  74  LEU A CD1  1 
ATOM   499  C  CD2  . LEU A 1 74  ? 10.960  1.757   17.709  1.00 29.35  ?  74  LEU A CD2  1 
ATOM   500  N  N    . ARG A 1 75  ? 15.852  -0.354  16.533  1.00 23.82  ?  75  ARG A N    1 
ATOM   501  C  CA   . ARG A 1 75  ? 17.191  -0.176  15.975  1.00 26.24  ?  75  ARG A CA   1 
ATOM   502  C  C    . ARG A 1 75  ? 17.217  -0.522  14.493  1.00 25.98  ?  75  ARG A C    1 
ATOM   503  O  O    . ARG A 1 75  ? 17.957  0.098   13.713  1.00 24.04  ?  75  ARG A O    1 
ATOM   504  C  CB   . ARG A 1 75  ? 18.168  -1.069  16.727  1.00 26.23  ?  75  ARG A CB   1 
ATOM   505  C  CG   . ARG A 1 75  ? 18.322  -0.701  18.199  1.00 29.79  ?  75  ARG A CG   1 
ATOM   506  C  CD   . ARG A 1 75  ? 19.168  -1.738  18.909  1.00 32.04  ?  75  ARG A CD   1 
ATOM   507  N  NE   . ARG A 1 75  ? 18.483  -3.024  18.958  1.00 29.69  ?  75  ARG A NE   1 
ATOM   508  C  CZ   . ARG A 1 75  ? 19.046  -4.154  19.360  1.00 27.25  ?  75  ARG A CZ   1 
ATOM   509  N  NH1  . ARG A 1 75  ? 20.312  -4.195  19.743  1.00 32.09  ?  75  ARG A NH1  1 
ATOM   510  N  NH2  . ARG A 1 75  ? 18.318  -5.268  19.384  1.00 28.67  ?  75  ARG A NH2  1 
ATOM   511  N  N    . VAL A 1 76  ? 16.451  -1.538  14.099  1.00 22.83  ?  76  VAL A N    1 
ATOM   512  C  CA   . VAL A 1 76  ? 16.341  -1.894  12.685  1.00 22.54  ?  76  VAL A CA   1 
ATOM   513  C  C    . VAL A 1 76  ? 15.633  -0.785  11.926  1.00 22.55  ?  76  VAL A C    1 
ATOM   514  O  O    . VAL A 1 76  ? 16.090  -0.333  10.873  1.00 21.71  ?  76  VAL A O    1 
ATOM   515  C  CB   . VAL A 1 76  ? 15.613  -3.243  12.547  1.00 23.70  ?  76  VAL A CB   1 
ATOM   516  C  CG1  . VAL A 1 76  ? 15.218  -3.525  11.092  1.00 22.18  ?  76  VAL A CG1  1 
ATOM   517  C  CG2  . VAL A 1 76  ? 16.490  -4.363  13.108  1.00 25.65  ?  76  VAL A CG2  1 
ATOM   518  N  N    . ILE A 1 77  ? 14.512  -0.308  12.466  1.00 21.62  ?  77  ILE A N    1 
ATOM   519  C  CA   . ILE A 1 77  ? 13.788  0.773   11.808  1.00 21.49  ?  77  ILE A CA   1 
ATOM   520  C  C    . ILE A 1 77  ? 14.701  1.969   11.593  1.00 24.59  ?  77  ILE A C    1 
ATOM   521  O  O    . ILE A 1 77  ? 14.713  2.576   10.514  1.00 23.62  ?  77  ILE A O    1 
ATOM   522  C  CB   . ILE A 1 77  ? 12.528  1.123   12.623  1.00 23.50  ?  77  ILE A CB   1 
ATOM   523  C  CG1  . ILE A 1 77  ? 11.582  -0.074  12.599  1.00 23.60  ?  77  ILE A CG1  1 
ATOM   524  C  CG2  . ILE A 1 77  ? 11.844  2.357   12.065  1.00 26.12  ?  77  ILE A CG2  1 
ATOM   525  C  CD1  . ILE A 1 77  ? 10.376  0.054   13.523  1.00 23.75  ?  77  ILE A CD1  1 
ATOM   526  N  N    A SER A 1 78  ? 15.495  2.318   12.606  0.56 23.49  ?  78  SER A N    1 
ATOM   527  N  N    B SER A 1 78  ? 15.496  2.313   12.610  0.44 23.49  ?  78  SER A N    1 
ATOM   528  C  CA   A SER A 1 78  ? 16.366  3.480   12.486  0.56 25.15  ?  78  SER A CA   1 
ATOM   529  C  CA   B SER A 1 78  ? 16.379  3.469   12.513  0.44 25.17  ?  78  SER A CA   1 
ATOM   530  C  C    A SER A 1 78  ? 17.358  3.318   11.341  0.56 24.46  ?  78  SER A C    1 
ATOM   531  C  C    B SER A 1 78  ? 17.364  3.318   11.359  0.44 24.47  ?  78  SER A C    1 
ATOM   532  O  O    A SER A 1 78  ? 17.601  4.267   10.589  0.56 25.28  ?  78  SER A O    1 
ATOM   533  O  O    B SER A 1 78  ? 17.611  4.277   10.620  0.44 25.24  ?  78  SER A O    1 
ATOM   534  C  CB   A SER A 1 78  ? 17.081  3.736   13.809  0.56 27.04  ?  78  SER A CB   1 
ATOM   535  C  CB   B SER A 1 78  ? 17.115  3.667   13.838  0.44 27.07  ?  78  SER A CB   1 
ATOM   536  O  OG   A SER A 1 78  ? 16.147  4.130   14.792  0.56 30.01  ?  78  SER A OG   1 
ATOM   537  O  OG   B SER A 1 78  ? 17.793  4.910   13.872  0.44 28.78  ?  78  SER A OG   1 
ATOM   538  N  N    . VAL A 1 79  ? 17.934  2.123   11.188  1.00 23.38  ?  79  VAL A N    1 
ATOM   539  C  CA   . VAL A 1 79  ? 18.856  1.886   10.074  1.00 22.26  ?  79  VAL A CA   1 
ATOM   540  C  C    . VAL A 1 79  ? 18.147  2.090   8.745   1.00 22.88  ?  79  VAL A C    1 
ATOM   541  O  O    . VAL A 1 79  ? 18.656  2.766   7.844   1.00 23.81  ?  79  VAL A O    1 
ATOM   542  C  CB   . VAL A 1 79  ? 19.457  0.473   10.150  1.00 22.00  ?  79  VAL A CB   1 
ATOM   543  C  CG1  . VAL A 1 79  ? 20.173  0.142   8.822   1.00 24.08  ?  79  VAL A CG1  1 
ATOM   544  C  CG2  . VAL A 1 79  ? 20.436  0.365   11.298  1.00 24.48  ?  79  VAL A CG2  1 
ATOM   545  N  N    . VAL A 1 80  ? 16.984  1.463   8.581   1.00 20.92  ?  80  VAL A N    1 
ATOM   546  C  CA   . VAL A 1 80  ? 16.299  1.514   7.295   1.00 21.06  ?  80  VAL A CA   1 
ATOM   547  C  C    . VAL A 1 80  ? 15.888  2.941   6.963   1.00 23.88  ?  80  VAL A C    1 
ATOM   548  O  O    . VAL A 1 80  ? 16.015  3.393   5.814   1.00 22.56  ?  80  VAL A O    1 
ATOM   549  C  CB   . VAL A 1 80  ? 15.104  0.547   7.300   1.00 20.32  ?  80  VAL A CB   1 
ATOM   550  C  CG1  . VAL A 1 80  ? 14.361  0.608   5.967   1.00 22.45  ?  80  VAL A CG1  1 
ATOM   551  C  CG2  . VAL A 1 80  ? 15.586  -0.858  7.580   1.00 23.51  ?  80  VAL A CG2  1 
ATOM   552  N  N    . GLU A 1 81  ? 15.413  3.681   7.968   1.00 22.26  ?  81  GLU A N    1 
ATOM   553  C  CA   . GLU A 1 81  ? 15.039  5.076   7.761   1.00 26.38  ?  81  GLU A CA   1 
ATOM   554  C  C    . GLU A 1 81  ? 16.220  5.891   7.260   1.00 27.27  ?  81  GLU A C    1 
ATOM   555  O  O    . GLU A 1 81  ? 16.067  6.738   6.375   1.00 27.19  ?  81  GLU A O    1 
ATOM   556  C  CB   . GLU A 1 81  ? 14.519  5.681   9.067   1.00 26.81  ?  81  GLU A CB   1 
ATOM   557  C  CG   . GLU A 1 81  ? 13.169  5.161   9.508   1.00 28.67  ?  81  GLU A CG   1 
ATOM   558  C  CD   . GLU A 1 81  ? 12.678  5.849   10.767  1.00 32.07  ?  81  GLU A CD   1 
ATOM   559  O  OE1  . GLU A 1 81  ? 13.469  6.588   11.389  1.00 34.67  ?  81  GLU A OE1  1 
ATOM   560  O  OE2  . GLU A 1 81  ? 11.500  5.644   11.139  1.00 35.44  -1 81  GLU A OE2  1 
ATOM   561  N  N    . GLU A 1 82  ? 17.406  5.660   7.829   1.00 26.86  ?  82  GLU A N    1 
ATOM   562  C  CA   . GLU A 1 82  ? 18.592  6.387   7.391   1.00 26.43  ?  82  GLU A CA   1 
ATOM   563  C  C    . GLU A 1 82  ? 18.988  6.012   5.967   1.00 27.22  ?  82  GLU A C    1 
ATOM   564  O  O    . GLU A 1 82  ? 19.336  6.886   5.168   1.00 28.97  ?  82  GLU A O    1 
ATOM   565  C  CB   . GLU A 1 82  ? 19.746  6.129   8.356   1.00 29.80  ?  82  GLU A CB   1 
ATOM   566  C  CG   . GLU A 1 82  ? 21.048  6.772   7.938   1.00 34.09  ?  82  GLU A CG   1 
ATOM   567  C  CD   . GLU A 1 82  ? 21.069  8.276   8.161   1.00 44.04  ?  82  GLU A CD   1 
ATOM   568  O  OE1  . GLU A 1 82  ? 20.115  8.811   8.771   1.00 43.80  ?  82  GLU A OE1  1 
ATOM   569  O  OE2  . GLU A 1 82  ? 22.050  8.918   7.725   1.00 50.48  -1 82  GLU A OE2  1 
ATOM   570  N  N    . LEU A 1 83  ? 18.943  4.720   5.630   1.00 23.34  ?  83  LEU A N    1 
ATOM   571  C  CA   . LEU A 1 83  ? 19.370  4.300   4.299   1.00 22.54  ?  83  LEU A CA   1 
ATOM   572  C  C    . LEU A 1 83  ? 18.402  4.769   3.220   1.00 23.61  ?  83  LEU A C    1 
ATOM   573  O  O    . LEU A 1 83  ? 18.834  5.260   2.171   1.00 26.73  ?  83  LEU A O    1 
ATOM   574  C  CB   . LEU A 1 83  ? 19.552  2.786   4.250   1.00 21.20  ?  83  LEU A CB   1 
ATOM   575  C  CG   . LEU A 1 83  ? 20.008  2.215   2.904   1.00 20.67  ?  83  LEU A CG   1 
ATOM   576  C  CD1  . LEU A 1 83  ? 21.468  2.591   2.683   1.00 24.48  ?  83  LEU A CD1  1 
ATOM   577  C  CD2  . LEU A 1 83  ? 19.848  0.726   2.896   1.00 24.19  ?  83  LEU A CD2  1 
ATOM   578  N  N    . LEU A 1 84  ? 17.093  4.631   3.455   1.00 23.51  ?  84  LEU A N    1 
ATOM   579  C  CA   . LEU A 1 84  ? 16.102  4.964   2.436   1.00 23.99  ?  84  LEU A CA   1 
ATOM   580  C  C    . LEU A 1 84  ? 15.754  6.443   2.406   1.00 25.92  ?  84  LEU A C    1 
ATOM   581  O  O    . LEU A 1 84  ? 15.280  6.933   1.376   1.00 27.46  ?  84  LEU A O    1 
ATOM   582  C  CB   . LEU A 1 84  ? 14.812  4.174   2.666   1.00 22.29  ?  84  LEU A CB   1 
ATOM   583  C  CG   . LEU A 1 84  ? 14.725  2.788   2.015   1.00 21.74  ?  84  LEU A CG   1 
ATOM   584  C  CD1  . LEU A 1 84  ? 15.851  1.871   2.479   1.00 23.13  ?  84  LEU A CD1  1 
ATOM   585  C  CD2  . LEU A 1 84  ? 13.361  2.145   2.301   1.00 20.58  ?  84  LEU A CD2  1 
ATOM   586  N  N    . GLY A 1 85  ? 15.954  7.156   3.505   1.00 24.53  ?  85  GLY A N    1 
ATOM   587  C  CA   . GLY A 1 85  ? 15.583  8.554   3.538   1.00 27.57  ?  85  GLY A CA   1 
ATOM   588  C  C    . GLY A 1 85  ? 14.110  8.813   3.735   1.00 28.68  ?  85  GLY A C    1 
ATOM   589  O  O    . GLY A 1 85  ? 13.629  9.887   3.356   1.00 31.44  ?  85  GLY A O    1 
ATOM   590  N  N    . THR A 1 86  ? 13.383  7.869   4.330   1.00 27.42  ?  86  THR A N    1 
ATOM   591  C  CA   . THR A 1 86  ? 11.968  8.038   4.625   1.00 27.98  ?  86  THR A CA   1 
ATOM   592  C  C    . THR A 1 86  ? 11.609  7.256   5.880   1.00 29.49  ?  86  THR A C    1 
ATOM   593  O  O    . THR A 1 86  ? 12.240  6.246   6.213   1.00 27.41  ?  86  THR A O    1 
ATOM   594  C  CB   . THR A 1 86  ? 11.073  7.573   3.464   1.00 27.94  ?  86  THR A CB   1 
ATOM   595  O  OG1  . THR A 1 86  ? 9.697   7.773   3.816   1.00 28.10  ?  86  THR A OG1  1 
ATOM   596  C  CG2  . THR A 1 86  ? 11.285  6.085   3.165   1.00 26.83  ?  86  THR A CG2  1 
ATOM   597  N  N    . THR A 1 87  ? 10.579  7.733   6.571   1.00 26.82  ?  87  THR A N    1 
ATOM   598  C  CA   . THR A 1 87  ? 9.994   6.984   7.673   1.00 26.96  ?  87  THR A CA   1 
ATOM   599  C  C    . THR A 1 87  ? 8.777   6.166   7.255   1.00 26.42  ?  87  THR A C    1 
ATOM   600  O  O    . THR A 1 87  ? 8.255   5.408   8.074   1.00 25.71  ?  87  THR A O    1 
ATOM   601  C  CB   . THR A 1 87  ? 9.601   7.924   8.818   1.00 27.27  ?  87  THR A CB   1 
ATOM   602  O  OG1  . THR A 1 87  ? 8.600   8.841   8.360   1.00 31.54  ?  87  THR A OG1  1 
ATOM   603  C  CG2  . THR A 1 87  ? 10.811  8.709   9.313   1.00 32.31  ?  87  THR A CG2  1 
ATOM   604  N  N    . ASP A 1 88  ? 8.314   6.286   6.011   1.00 24.53  ?  88  ASP A N    1 
ATOM   605  C  CA   . ASP A 1 88  ? 7.091   5.597   5.588   1.00 22.83  ?  88  ASP A CA   1 
ATOM   606  C  C    . ASP A 1 88  ? 7.462   4.191   5.128   1.00 25.08  ?  88  ASP A C    1 
ATOM   607  O  O    . ASP A 1 88  ? 7.556   3.900   3.934   1.00 24.83  ?  88  ASP A O    1 
ATOM   608  C  CB   . ASP A 1 88  ? 6.390   6.389   4.491   1.00 26.50  ?  88  ASP A CB   1 
ATOM   609  C  CG   . ASP A 1 88  ? 4.916   6.016   4.340   1.00 27.96  ?  88  ASP A CG   1 
ATOM   610  O  OD1  . ASP A 1 88  ? 4.403   5.204   5.146   1.00 27.83  ?  88  ASP A OD1  1 
ATOM   611  O  OD2  . ASP A 1 88  ? 4.264   6.532   3.403   1.00 30.74  -1 88  ASP A OD2  1 
ATOM   612  N  N    . LEU A 1 89  ? 7.674   3.306   6.099   1.00 19.45  ?  89  LEU A N    1 
ATOM   613  C  CA   . LEU A 1 89  ? 8.198   1.969   5.847   1.00 20.10  ?  89  LEU A CA   1 
ATOM   614  C  C    . LEU A 1 89  ? 7.122   0.915   6.059   1.00 18.60  ?  89  LEU A C    1 
ATOM   615  O  O    . LEU A 1 89  ? 6.158   1.117   6.809   1.00 17.98  ?  89  LEU A O    1 
ATOM   616  C  CB   . LEU A 1 89  ? 9.365   1.660   6.786   1.00 19.31  ?  89  LEU A CB   1 
ATOM   617  C  CG   . LEU A 1 89  ? 10.520  2.645   6.690   1.00 20.61  ?  89  LEU A CG   1 
ATOM   618  C  CD1  . LEU A 1 89  ? 11.575  2.264   7.708   1.00 23.12  ?  89  LEU A CD1  1 
ATOM   619  C  CD2  . LEU A 1 89  ? 11.091  2.640   5.265   1.00 20.29  ?  89  LEU A CD2  1 
ATOM   620  N  N    . ARG A 1 90  ? 7.319   -0.232  5.410   1.00 17.57  ?  90  ARG A N    1 
ATOM   621  C  CA   . ARG A 1 90  ? 6.470   -1.397  5.611   1.00 16.71  ?  90  ARG A CA   1 
ATOM   622  C  C    . ARG A 1 90  ? 7.317   -2.654  5.729   1.00 18.83  ?  90  ARG A C    1 
ATOM   623  O  O    . ARG A 1 90  ? 8.340   -2.795  5.047   1.00 16.22  ?  90  ARG A O    1 
ATOM   624  C  CB   . ARG A 1 90  ? 5.512   -1.611  4.433   1.00 18.40  ?  90  ARG A CB   1 
ATOM   625  C  CG   . ARG A 1 90  ? 4.521   -0.501  4.163   1.00 19.32  ?  90  ARG A CG   1 
ATOM   626  C  CD   . ARG A 1 90  ? 3.508   -0.309  5.304   1.00 19.51  ?  90  ARG A CD   1 
ATOM   627  N  NE   . ARG A 1 90  ? 2.538   0.707   4.905   1.00 19.87  ?  90  ARG A NE   1 
ATOM   628  C  CZ   . ARG A 1 90  ? 2.766   2.013   4.958   1.00 20.32  ?  90  ARG A CZ   1 
ATOM   629  N  NH1  . ARG A 1 90  ? 3.837   2.507   5.554   1.00 20.79  ?  90  ARG A NH1  1 
ATOM   630  N  NH2  . ARG A 1 90  ? 1.910   2.848   4.368   1.00 24.15  ?  90  ARG A NH2  1 
ATOM   631  N  N    . MET A 1 91  ? 6.870   -3.581  6.570   1.00 16.16  ?  91  MET A N    1 
ATOM   632  C  CA   . MET A 1 91  ? 7.458   -4.915  6.618   1.00 15.09  ?  91  MET A CA   1 
ATOM   633  C  C    . MET A 1 91  ? 6.943   -5.714  5.423   1.00 15.89  ?  91  MET A C    1 
ATOM   634  O  O    . MET A 1 91  ? 5.738   -5.984  5.314   1.00 19.44  ?  91  MET A O    1 
ATOM   635  C  CB   . MET A 1 91  ? 7.119   -5.616  7.931   1.00 18.69  ?  91  MET A CB   1 
ATOM   636  C  CG   . MET A 1 91  ? 7.891   -6.944  8.093   1.00 19.63  ?  91  MET A CG   1 
ATOM   637  S  SD   . MET A 1 91  ? 7.488   -7.803  9.633   1.00 22.96  ?  91  MET A SD   1 
ATOM   638  C  CE   . MET A 1 91  ? 5.963   -8.564  9.101   1.00 20.51  ?  91  MET A CE   1 
ATOM   639  N  N    . THR A 1 92  ? 7.864   -6.083  4.522   1.00 15.62  ?  92  THR A N    1 
ATOM   640  C  CA   . THR A 1 92  ? 7.527   -6.811  3.303   1.00 15.10  ?  92  THR A CA   1 
ATOM   641  C  C    . THR A 1 92  ? 7.252   -8.286  3.577   1.00 17.34  ?  92  THR A C    1 
ATOM   642  O  O    . THR A 1 92  ? 6.410   -8.901  2.917   1.00 18.03  ?  92  THR A O    1 
ATOM   643  C  CB   . THR A 1 92  ? 8.718   -6.740  2.353   1.00 14.59  ?  92  THR A CB   1 
ATOM   644  O  OG1  . THR A 1 92  ? 9.318   -5.441  2.426   1.00 16.72  ?  92  THR A OG1  1 
ATOM   645  C  CG2  . THR A 1 92  ? 8.279   -7.040  0.925   1.00 17.07  ?  92  THR A CG2  1 
ATOM   646  N  N    . SER A 1 93  ? 8.008   -8.873  4.502   1.00 15.61  ?  93  SER A N    1 
ATOM   647  C  CA   . SER A 1 93  ? 7.980   -10.303 4.740   1.00 16.86  ?  93  SER A CA   1 
ATOM   648  C  C    . SER A 1 93  ? 8.681   -10.573 6.058   1.00 16.68  ?  93  SER A C    1 
ATOM   649  O  O    . SER A 1 93  ? 9.594   -9.839  6.458   1.00 16.73  ?  93  SER A O    1 
ATOM   650  C  CB   . SER A 1 93  ? 8.748   -11.029 3.621   1.00 20.41  ?  93  SER A CB   1 
ATOM   651  O  OG   . SER A 1 93  ? 8.755   -12.430 3.827   1.00 27.03  ?  93  SER A OG   1 
ATOM   652  N  N    . SER A 1 94  ? 8.252   -11.641 6.728   1.00 16.15  ?  94  SER A N    1 
ATOM   653  C  CA   . SER A 1 94  ? 9.034   -12.185 7.828   1.00 16.58  ?  94  SER A CA   1 
ATOM   654  C  C    . SER A 1 94  ? 8.697   -13.660 7.955   1.00 16.08  ?  94  SER A C    1 
ATOM   655  O  O    . SER A 1 94  ? 7.547   -14.062 7.752   1.00 16.97  ?  94  SER A O    1 
ATOM   656  C  CB   . SER A 1 94  ? 8.805   -11.436 9.145   1.00 17.39  ?  94  SER A CB   1 
ATOM   657  O  OG   . SER A 1 94  ? 9.535   -12.047 10.194  1.00 19.53  ?  94  SER A OG   1 
ATOM   658  N  N    . PHE A 1 95  ? 9.716   -14.471 8.253   1.00 14.95  ?  95  PHE A N    1 
ATOM   659  C  CA   . PHE A 1 95  ? 9.506   -15.901 8.408   1.00 15.43  ?  95  PHE A CA   1 
ATOM   660  C  C    . PHE A 1 95  ? 10.659  -16.466 9.222   1.00 15.84  ?  95  PHE A C    1 
ATOM   661  O  O    . PHE A 1 95  ? 11.703  -15.824 9.384   1.00 17.94  ?  95  PHE A O    1 
ATOM   662  C  CB   . PHE A 1 95  ? 9.382   -16.626 7.049   1.00 16.55  ?  95  PHE A CB   1 
ATOM   663  C  CG   . PHE A 1 95  ? 10.590  -16.485 6.156   1.00 19.41  ?  95  PHE A CG   1 
ATOM   664  C  CD1  . PHE A 1 95  ? 11.606  -17.419 6.216   1.00 19.37  ?  95  PHE A CD1  1 
ATOM   665  C  CD2  . PHE A 1 95  ? 10.688  -15.437 5.251   1.00 18.87  ?  95  PHE A CD2  1 
ATOM   666  C  CE1  . PHE A 1 95  ? 12.728  -17.309 5.382   1.00 20.17  ?  95  PHE A CE1  1 
ATOM   667  C  CE2  . PHE A 1 95  ? 11.821  -15.313 4.422   1.00 20.38  ?  95  PHE A CE2  1 
ATOM   668  C  CZ   . PHE A 1 95  ? 12.821  -16.257 4.504   1.00 20.13  ?  95  PHE A CZ   1 
ATOM   669  N  N    . ILE A 1 96  ? 10.457  -17.666 9.735   1.00 15.80  ?  96  ILE A N    1 
ATOM   670  C  CA   . ILE A 1 96  ? 11.527  -18.414 10.390  1.00 17.92  ?  96  ILE A CA   1 
ATOM   671  C  C    . ILE A 1 96  ? 11.815  -19.646 9.553   1.00 18.87  ?  96  ILE A C    1 
ATOM   672  O  O    . ILE A 1 96  ? 10.930  -20.174 8.874   1.00 18.75  ?  96  ILE A O    1 
ATOM   673  C  CB   . ILE A 1 96  ? 11.204  -18.800 11.848  1.00 18.03  ?  96  ILE A CB   1 
ATOM   674  C  CG1  . ILE A 1 96  ? 9.864   -19.548 11.928  1.00 18.10  ?  96  ILE A CG1  1 
ATOM   675  C  CG2  . ILE A 1 96  ? 11.201  -17.570 12.725  1.00 20.24  ?  96  ILE A CG2  1 
ATOM   676  C  CD1  . ILE A 1 96  ? 9.492   -20.021 13.341  1.00 19.49  ?  96  ILE A CD1  1 
ATOM   677  N  N    . GLN A 1 97  ? 13.064  -20.113 9.593   1.00 18.93  ?  97  GLN A N    1 
ATOM   678  C  CA   . GLN A 1 97  ? 13.400  -21.302 8.829   1.00 20.69  ?  97  GLN A CA   1 
ATOM   679  C  C    . GLN A 1 97  ? 14.572  -22.013 9.485   1.00 23.14  ?  97  GLN A C    1 
ATOM   680  O  O    . GLN A 1 97  ? 15.455  -21.378 10.070  1.00 22.54  ?  97  GLN A O    1 
ATOM   681  C  CB   . GLN A 1 97  ? 13.752  -20.962 7.372   1.00 23.76  ?  97  GLN A CB   1 
ATOM   682  C  CG   . GLN A 1 97  ? 13.759  -22.176 6.433   1.00 27.10  ?  97  GLN A CG   1 
ATOM   683  C  CD   . GLN A 1 97  ? 13.917  -21.791 4.969   1.00 30.27  ?  97  GLN A CD   1 
ATOM   684  O  OE1  . GLN A 1 97  ? 14.695  -20.888 4.625   1.00 34.30  ?  97  GLN A OE1  1 
ATOM   685  N  NE2  . GLN A 1 97  ? 13.195  -22.497 4.092   1.00 29.96  ?  97  GLN A NE2  1 
ATOM   686  N  N    . ALA A 1 98  ? 14.546  -23.337 9.406   1.00 21.47  ?  98  ALA A N    1 
ATOM   687  C  CA   . ALA A 1 98  ? 15.674  -24.176 9.787   1.00 23.56  ?  98  ALA A CA   1 
ATOM   688  C  C    . ALA A 1 98  ? 16.265  -24.785 8.526   1.00 26.48  ?  98  ALA A C    1 
ATOM   689  O  O    . ALA A 1 98  ? 15.533  -25.172 7.611   1.00 27.18  ?  98  ALA A O    1 
ATOM   690  C  CB   . ALA A 1 98  ? 15.224  -25.301 10.729  1.00 26.13  ?  98  ALA A CB   1 
ATOM   691  N  N    . LYS A 1 99  ? 17.592  -24.865 8.471   1.00 23.27  ?  99  LYS A N    1 
ATOM   692  C  CA   . LYS A 1 99  ? 18.283  -25.534 7.376   1.00 25.95  ?  99  LYS A CA   1 
ATOM   693  C  C    . LYS A 1 99  ? 19.055  -26.699 7.973   1.00 23.99  ?  99  LYS A C    1 
ATOM   694  O  O    . LYS A 1 99  ? 19.949  -26.495 8.802   1.00 26.08  ?  99  LYS A O    1 
ATOM   695  C  CB   . LYS A 1 99  ? 19.232  -24.581 6.652   1.00 26.88  ?  99  LYS A CB   1 
ATOM   696  C  CG   . LYS A 1 99  ? 19.802  -25.186 5.396   1.00 31.06  ?  99  LYS A CG   1 
ATOM   697  C  CD   . LYS A 1 99  ? 20.634  -24.195 4.627   1.00 38.68  ?  99  LYS A CD   1 
ATOM   698  C  CE   . LYS A 1 99  ? 19.767  -23.216 3.877   1.00 40.23  ?  99  LYS A CE   1 
ATOM   699  N  NZ   . LYS A 1 99  ? 20.581  -22.505 2.840   1.00 31.34  ?  99  LYS A NZ   1 
ATOM   700  N  N    . TYR A 1 100 ? 18.705  -27.913 7.565   1.00 25.24  ?  100 TYR A N    1 
ATOM   701  C  CA   . TYR A 1 100 ? 19.177  -29.117 8.230   1.00 27.76  ?  100 TYR A CA   1 
ATOM   702  C  C    . TYR A 1 100 ? 20.426  -29.699 7.570   1.00 26.51  ?  100 TYR A C    1 
ATOM   703  O  O    . TYR A 1 100 ? 20.658  -29.531 6.370   1.00 28.45  ?  100 TYR A O    1 
ATOM   704  C  CB   . TYR A 1 100 ? 18.070  -30.176 8.250   1.00 31.51  ?  100 TYR A CB   1 
ATOM   705  C  CG   . TYR A 1 100 ? 16.981  -29.882 9.246   1.00 27.40  ?  100 TYR A CG   1 
ATOM   706  C  CD1  . TYR A 1 100 ? 15.964  -28.993 8.938   1.00 28.42  ?  100 TYR A CD1  1 
ATOM   707  C  CD2  . TYR A 1 100 ? 16.982  -30.476 10.502  1.00 29.79  ?  100 TYR A CD2  1 
ATOM   708  C  CE1  . TYR A 1 100 ? 14.973  -28.711 9.851   1.00 28.78  ?  100 TYR A CE1  1 
ATOM   709  C  CE2  . TYR A 1 100 ? 15.989  -30.198 11.422  1.00 32.62  ?  100 TYR A CE2  1 
ATOM   710  C  CZ   . TYR A 1 100 ? 14.993  -29.308 11.084  1.00 32.77  ?  100 TYR A CZ   1 
ATOM   711  O  OH   . TYR A 1 100 ? 13.994  -29.017 11.987  1.00 34.12  ?  100 TYR A OH   1 
ATOM   712  N  N    . GLY A 1 101 ? 21.210  -30.413 8.371   1.00 26.68  ?  101 GLY A N    1 
ATOM   713  C  CA   . GLY A 1 101 ? 22.420  -31.069 7.900   1.00 27.76  ?  101 GLY A CA   1 
ATOM   714  C  C    . GLY A 1 101 ? 22.142  -32.254 6.985   1.00 32.76  ?  101 GLY A C    1 
ATOM   715  O  O    . GLY A 1 101 ? 21.000  -32.637 6.724   1.00 31.98  ?  101 GLY A O    1 
ATOM   716  N  N    . THR A 1 102 ? 23.238  -32.864 6.506   1.00 28.70  ?  102 THR A N    1 
ATOM   717  C  CA   . THR A 1 102 ? 23.153  -33.899 5.478   1.00 31.93  ?  102 THR A CA   1 
ATOM   718  C  C    . THR A 1 102 ? 22.499  -35.183 5.967   1.00 32.48  ?  102 THR A C    1 
ATOM   719  O  O    . THR A 1 102 ? 22.033  -35.968 5.138   1.00 36.59  ?  102 THR A O    1 
ATOM   720  C  CB   . THR A 1 102 ? 24.540  -34.216 4.902   1.00 29.88  ?  102 THR A CB   1 
ATOM   721  O  OG1  . THR A 1 102 ? 25.344  -34.843 5.905   1.00 31.91  ?  102 THR A OG1  1 
ATOM   722  C  CG2  . THR A 1 102 ? 25.234  -32.943 4.419   1.00 33.53  ?  102 THR A CG2  1 
ATOM   723  N  N    . ALA A 1 103 ? 22.466  -35.431 7.279   1.00 33.03  ?  103 ALA A N    1 
ATOM   724  C  CA   . ALA A 1 103 ? 21.778  -36.612 7.790   1.00 35.26  ?  103 ALA A CA   1 
ATOM   725  C  C    . ALA A 1 103 ? 20.291  -36.598 7.457   1.00 34.22  ?  103 ALA A C    1 
ATOM   726  O  O    . ALA A 1 103 ? 19.641  -37.647 7.520   1.00 39.37  ?  103 ALA A O    1 
ATOM   727  C  CB   . ALA A 1 103 ? 21.949  -36.701 9.305   1.00 36.21  ?  103 ALA A CB   1 
ATOM   728  N  N    . TYR A 1 104 ? 19.740  -35.441 7.100   1.00 35.84  ?  104 TYR A N    1 
ATOM   729  C  CA   . TYR A 1 104 ? 18.310  -35.302 6.867   1.00 36.59  ?  104 TYR A CA   1 
ATOM   730  C  C    . TYR A 1 104 ? 17.972  -35.081 5.394   1.00 39.87  ?  104 TYR A C    1 
ATOM   731  O  O    . TYR A 1 104 ? 16.871  -34.626 5.076   1.00 40.12  ?  104 TYR A O    1 
ATOM   732  C  CB   . TYR A 1 104 ? 17.755  -34.188 7.760   1.00 34.28  ?  104 TYR A CB   1 
ATOM   733  C  CG   . TYR A 1 104 ? 18.287  -34.291 9.177   1.00 35.10  ?  104 TYR A CG   1 
ATOM   734  C  CD1  . TYR A 1 104 ? 17.771  -35.221 10.072  1.00 41.13  ?  104 TYR A CD1  1 
ATOM   735  C  CD2  . TYR A 1 104 ? 19.342  -33.489 9.603   1.00 38.50  ?  104 TYR A CD2  1 
ATOM   736  C  CE1  . TYR A 1 104 ? 18.274  -35.332 11.362  1.00 43.13  ?  104 TYR A CE1  1 
ATOM   737  C  CE2  . TYR A 1 104 ? 19.847  -33.594 10.887  1.00 37.41  ?  104 TYR A CE2  1 
ATOM   738  C  CZ   . TYR A 1 104 ? 19.315  -34.507 11.759  1.00 43.73  ?  104 TYR A CZ   1 
ATOM   739  O  OH   . TYR A 1 104 ? 19.828  -34.611 13.035  1.00 52.33  ?  104 TYR A OH   1 
ATOM   740  N  N    . GLY A 1 105 ? 18.888  -35.399 4.491   1.00 37.65  ?  105 GLY A N    1 
ATOM   741  C  CA   . GLY A 1 105 ? 18.655  -35.268 3.067   1.00 38.21  ?  105 GLY A CA   1 
ATOM   742  C  C    . GLY A 1 105 ? 19.636  -34.313 2.412   1.00 46.75  ?  105 GLY A C    1 
ATOM   743  O  O    . GLY A 1 105 ? 20.324  -33.530 3.064   1.00 47.35  ?  105 GLY A O    1 
ATOM   744  N  N    . GLU A 1 106 ? 19.673  -34.395 1.082   1.00 50.79  ?  106 GLU A N    1 
ATOM   745  C  CA   . GLU A 1 106 ? 20.610  -33.597 0.297   1.00 57.69  ?  106 GLU A CA   1 
ATOM   746  C  C    . GLU A 1 106 ? 20.335  -32.105 0.447   1.00 56.91  ?  106 GLU A C    1 
ATOM   747  O  O    . GLU A 1 106 ? 19.209  -31.639 0.241   1.00 55.55  ?  106 GLU A O    1 
ATOM   748  C  CB   . GLU A 1 106 ? 20.528  -33.999 -1.177  1.00 64.51  ?  106 GLU A CB   1 
ATOM   749  C  CG   . GLU A 1 106 ? 21.306  -35.260 -1.516  1.00 71.97  ?  106 GLU A CG   1 
ATOM   750  C  CD   . GLU A 1 106 ? 20.901  -35.861 -2.851  1.00 82.25  ?  106 GLU A CD   1 
ATOM   751  O  OE1  . GLU A 1 106 ? 19.698  -35.813 -3.188  1.00 83.87  ?  106 GLU A OE1  1 
ATOM   752  O  OE2  . GLU A 1 106 ? 21.786  -36.382 -3.564  1.00 85.31  -1 106 GLU A OE2  1 
ATOM   753  N  N    . SER A 1 107 ? 21.380  -31.357 0.794   1.00 53.80  ?  107 SER A N    1 
ATOM   754  C  CA   . SER A 1 107 ? 21.329  -29.908 0.952   1.00 53.71  ?  107 SER A CA   1 
ATOM   755  C  C    . SER A 1 107 ? 22.087  -29.271 -0.205  1.00 54.92  ?  107 SER A C    1 
ATOM   756  O  O    . SER A 1 107 ? 23.222  -29.663 -0.498  1.00 51.18  ?  107 SER A O    1 
ATOM   757  C  CB   . SER A 1 107 ? 21.975  -29.502 2.282   1.00 48.64  ?  107 SER A CB   1 
ATOM   758  O  OG   . SER A 1 107 ? 22.005  -28.097 2.459   1.00 43.74  ?  107 SER A OG   1 
ATOM   759  N  N    . LYS A 1 108 ? 21.464  -28.291 -0.855  1.00 53.87  ?  108 LYS A N    1 
ATOM   760  C  CA   . LYS A 1 108 ? 22.017  -27.682 -2.056  1.00 51.96  ?  108 LYS A CA   1 
ATOM   761  C  C    . LYS A 1 108 ? 22.273  -26.195 -1.839  1.00 48.79  ?  108 LYS A C    1 
ATOM   762  O  O    . LYS A 1 108 ? 21.673  -25.556 -0.969  1.00 44.67  ?  108 LYS A O    1 
ATOM   763  C  CB   . LYS A 1 108 ? 21.083  -27.884 -3.260  1.00 58.29  ?  108 LYS A CB   1 
ATOM   764  C  CG   . LYS A 1 108 ? 19.743  -28.521 -2.912  1.00 60.51  ?  108 LYS A CG   1 
ATOM   765  C  CD   . LYS A 1 108 ? 18.831  -27.545 -2.187  1.00 60.42  ?  108 LYS A CD   1 
ATOM   766  C  CE   . LYS A 1 108 ? 17.572  -28.235 -1.690  1.00 61.91  ?  108 LYS A CE   1 
ATOM   767  N  NZ   . LYS A 1 108 ? 16.536  -27.255 -1.266  1.00 61.57  ?  108 LYS A NZ   1 
ATOM   768  N  N    . ASP A 1 109 ? 23.192  -25.656 -2.639  1.00 49.32  ?  109 ASP A N    1 
ATOM   769  C  CA   . ASP A 1 109 ? 23.473  -24.228 -2.655  1.00 41.52  ?  109 ASP A CA   1 
ATOM   770  C  C    . ASP A 1 109 ? 22.510  -23.535 -3.610  1.00 44.39  ?  109 ASP A C    1 
ATOM   771  O  O    . ASP A 1 109 ? 22.219  -24.050 -4.695  1.00 46.59  ?  109 ASP A O    1 
ATOM   772  C  CB   . ASP A 1 109 ? 24.905  -23.975 -3.135  1.00 41.11  ?  109 ASP A CB   1 
ATOM   773  C  CG   . ASP A 1 109 ? 25.942  -24.692 -2.293  1.00 44.83  ?  109 ASP A CG   1 
ATOM   774  O  OD1  . ASP A 1 109 ? 26.234  -25.869 -2.597  1.00 54.59  ?  109 ASP A OD1  1 
ATOM   775  O  OD2  . ASP A 1 109 ? 26.468  -24.083 -1.330  1.00 32.44  -1 109 ASP A OD2  1 
ATOM   776  N  N    . GLN A 1 110 ? 22.008  -22.373 -3.195  1.00 36.53  ?  110 GLN A N    1 
ATOM   777  C  CA   . GLN A 1 110 ? 21.262  -21.503 -4.092  1.00 34.14  ?  110 GLN A CA   1 
ATOM   778  C  C    . GLN A 1 110 ? 22.218  -20.873 -5.100  1.00 29.31  ?  110 GLN A C    1 
ATOM   779  O  O    . GLN A 1 110 ? 23.417  -20.746 -4.855  1.00 32.64  ?  110 GLN A O    1 
ATOM   780  C  CB   . GLN A 1 110 ? 20.637  -20.348 -3.305  1.00 33.58  ?  110 GLN A CB   1 
ATOM   781  C  CG   . GLN A 1 110 ? 19.539  -20.711 -2.315  1.00 39.37  ?  110 GLN A CG   1 
ATOM   782  C  CD   . GLN A 1 110 ? 18.921  -19.474 -1.648  1.00 33.70  ?  110 GLN A CD   1 
ATOM   783  O  OE1  . GLN A 1 110 ? 19.553  -18.416 -1.545  1.00 27.91  ?  110 GLN A OE1  1 
ATOM   784  N  NE2  . GLN A 1 110 ? 17.677  -19.608 -1.195  1.00 39.23  ?  110 GLN A NE2  1 
ATOM   785  N  N    . ARG A 1 111 ? 21.671  -20.442 -6.234  1.00 25.97  ?  111 ARG A N    1 
ATOM   786  C  CA   . ARG A 1 111 ? 22.438  -19.573 -7.117  1.00 24.37  ?  111 ARG A CA   1 
ATOM   787  C  C    . ARG A 1 111 ? 22.546  -18.170 -6.518  1.00 21.88  ?  111 ARG A C    1 
ATOM   788  O  O    . ARG A 1 111 ? 21.662  -17.708 -5.786  1.00 20.24  ?  111 ARG A O    1 
ATOM   789  C  CB   . ARG A 1 111 ? 21.770  -19.483 -8.492  1.00 25.18  ?  111 ARG A CB   1 
ATOM   790  C  CG   . ARG A 1 111 ? 21.886  -20.749 -9.334  1.00 35.73  ?  111 ARG A CG   1 
ATOM   791  C  CD   . ARG A 1 111 ? 21.514  -20.479 -10.793 1.00 36.90  ?  111 ARG A CD   1 
ATOM   792  N  NE   . ARG A 1 111 ? 20.131  -20.027 -10.889 1.00 41.21  ?  111 ARG A NE   1 
ATOM   793  C  CZ   . ARG A 1 111 ? 19.593  -19.484 -11.973 1.00 38.42  ?  111 ARG A CZ   1 
ATOM   794  N  NH1  . ARG A 1 111 ? 20.299  -19.316 -13.084 1.00 39.58  ?  111 ARG A NH1  1 
ATOM   795  N  NH2  . ARG A 1 111 ? 18.319  -19.094 -11.938 1.00 39.90  ?  111 ARG A NH2  1 
ATOM   796  N  N    . LEU A 1 112 ? 23.659  -17.494 -6.820  1.00 20.35  ?  112 LEU A N    1 
ATOM   797  C  CA   . LEU A 1 112 ? 23.760  -16.078 -6.490  1.00 18.73  ?  112 LEU A CA   1 
ATOM   798  C  C    . LEU A 1 112 ? 22.618  -15.324 -7.162  1.00 19.80  ?  112 LEU A C    1 
ATOM   799  O  O    . LEU A 1 112 ? 22.232  -15.629 -8.294  1.00 19.71  ?  112 LEU A O    1 
ATOM   800  C  CB   . LEU A 1 112 ? 25.098  -15.511 -6.967  1.00 19.88  ?  112 LEU A CB   1 
ATOM   801  C  CG   . LEU A 1 112 ? 26.323  -15.888 -6.127  1.00 19.86  ?  112 LEU A CG   1 
ATOM   802  C  CD1  . LEU A 1 112 ? 27.600  -15.439 -6.795  1.00 21.51  ?  112 LEU A CD1  1 
ATOM   803  C  CD2  . LEU A 1 112 ? 26.218  -15.292 -4.719  1.00 21.61  ?  112 LEU A CD2  1 
ATOM   804  N  N    . HIS A 1 113 ? 22.088  -14.326 -6.467  1.00 18.09  ?  113 HIS A N    1 
ATOM   805  C  CA   . HIS A 1 113 ? 20.922  -13.600 -6.956  1.00 17.02  ?  113 HIS A CA   1 
ATOM   806  C  C    . HIS A 1 113 ? 20.841  -12.270 -6.225  1.00 18.10  ?  113 HIS A C    1 
ATOM   807  O  O    . HIS A 1 113 ? 21.536  -12.036 -5.231  1.00 18.28  ?  113 HIS A O    1 
ATOM   808  C  CB   . HIS A 1 113 ? 19.638  -14.407 -6.714  1.00 18.33  ?  113 HIS A CB   1 
ATOM   809  C  CG   . HIS A 1 113 ? 19.340  -14.643 -5.261  1.00 18.34  ?  113 HIS A CG   1 
ATOM   810  N  ND1  . HIS A 1 113 ? 19.874  -15.707 -4.561  1.00 20.15  ?  113 HIS A ND1  1 
ATOM   811  C  CD2  . HIS A 1 113 ? 18.590  -13.944 -4.375  1.00 19.40  ?  113 HIS A CD2  1 
ATOM   812  C  CE1  . HIS A 1 113 ? 19.443  -15.660 -3.307  1.00 20.19  ?  113 HIS A CE1  1 
ATOM   813  N  NE2  . HIS A 1 113 ? 18.675  -14.594 -3.167  1.00 19.91  ?  113 HIS A NE2  1 
ATOM   814  N  N    . ASN A 1 114 ? 19.978  -11.391 -6.731  1.00 18.16  ?  114 ASN A N    1 
ATOM   815  C  CA   . ASN A 1 114 ? 19.560  -10.215 -5.983  1.00 16.85  ?  114 ASN A CA   1 
ATOM   816  C  C    . ASN A 1 114 ? 18.113  -10.395 -5.539  1.00 17.62  ?  114 ASN A C    1 
ATOM   817  O  O    . ASN A 1 114 ? 17.368  -11.219 -6.082  1.00 18.57  ?  114 ASN A O    1 
ATOM   818  C  CB   . ASN A 1 114 ? 19.718  -8.912  -6.793  1.00 19.00  ?  114 ASN A CB   1 
ATOM   819  C  CG   . ASN A 1 114 ? 18.687  -8.774  -7.913  1.00 18.56  ?  114 ASN A CG   1 
ATOM   820  O  OD1  . ASN A 1 114 ? 17.511  -8.517  -7.660  1.00 17.92  ?  114 ASN A OD1  1 
ATOM   821  N  ND2  . ASN A 1 114 ? 19.127  -8.931  -9.155  1.00 17.88  ?  114 ASN A ND2  1 
ATOM   822  N  N    . ASP A 1 115 ? 17.755  -9.651  -4.497  1.00 16.76  ?  115 ASP A N    1 
ATOM   823  C  CA   . ASP A 1 115 ? 16.374  -9.611  -4.027  1.00 16.67  ?  115 ASP A CA   1 
ATOM   824  C  C    . ASP A 1 115 ? 15.875  -8.177  -4.132  1.00 18.04  ?  115 ASP A C    1 
ATOM   825  O  O    . ASP A 1 115 ? 15.328  -7.611  -3.180  1.00 17.78  ?  115 ASP A O    1 
ATOM   826  C  CB   . ASP A 1 115 ? 16.271  -10.131 -2.587  1.00 19.24  ?  115 ASP A CB   1 
ATOM   827  C  CG   . ASP A 1 115 ? 16.367  -11.633 -2.502  1.00 22.05  ?  115 ASP A CG   1 
ATOM   828  O  OD1  . ASP A 1 115 ? 15.472  -12.333 -3.031  1.00 24.74  ?  115 ASP A OD1  1 
ATOM   829  O  OD2  . ASP A 1 115 ? 17.349  -12.129 -1.925  1.00 21.17  -1 115 ASP A OD2  1 
ATOM   830  N  N    . ALA A 1 116 ? 16.096  -7.568  -5.284  1.00 17.21  ?  116 ALA A N    1 
ATOM   831  C  CA   . ALA A 1 116 ? 15.741  -6.175  -5.482  1.00 17.92  ?  116 ALA A CA   1 
ATOM   832  C  C    . ALA A 1 116 ? 14.306  -6.004  -5.935  1.00 17.33  ?  116 ALA A C    1 
ATOM   833  O  O    . ALA A 1 116 ? 13.818  -4.871  -5.951  1.00 17.84  ?  116 ALA A O    1 
ATOM   834  C  CB   . ALA A 1 116 ? 16.654  -5.568  -6.543  1.00 18.74  ?  116 ALA A CB   1 
ATOM   835  N  N    . TRP A 1 117 ? 13.638  -7.099  -6.295  1.00 17.51  ?  117 TRP A N    1 
ATOM   836  C  CA   . TRP A 1 117 ? 12.348  -7.082  -6.976  1.00 16.51  ?  117 TRP A CA   1 
ATOM   837  C  C    . TRP A 1 117 ? 11.179  -7.284  -6.018  1.00 18.02  ?  117 TRP A C    1 
ATOM   838  O  O    . TRP A 1 117 ? 11.257  -8.050  -5.054  1.00 19.94  ?  117 TRP A O    1 
ATOM   839  C  CB   . TRP A 1 117 ? 12.304  -8.222  -7.997  1.00 17.33  ?  117 TRP A CB   1 
ATOM   840  C  CG   . TRP A 1 117 ? 13.175  -7.996  -9.172  1.00 17.91  ?  117 TRP A CG   1 
ATOM   841  C  CD1  . TRP A 1 117 ? 14.529  -8.233  -9.267  1.00 19.46  ?  117 TRP A CD1  1 
ATOM   842  C  CD2  . TRP A 1 117 ? 12.771  -7.453  -10.424 1.00 17.45  ?  117 TRP A CD2  1 
ATOM   843  N  NE1  . TRP A 1 117 ? 14.972  -7.872  -10.512 1.00 19.31  ?  117 TRP A NE1  1 
ATOM   844  C  CE2  . TRP A 1 117 ? 13.918  -7.392  -11.245 1.00 20.12  ?  117 TRP A CE2  1 
ATOM   845  C  CE3  . TRP A 1 117 ? 11.540  -7.002  -10.937 1.00 19.66  ?  117 TRP A CE3  1 
ATOM   846  C  CZ2  . TRP A 1 117 ? 13.871  -6.909  -12.549 1.00 21.09  ?  117 TRP A CZ2  1 
ATOM   847  C  CZ3  . TRP A 1 117 ? 11.499  -6.525  -12.234 1.00 19.63  ?  117 TRP A CZ3  1 
ATOM   848  C  CH2  . TRP A 1 117 ? 12.656  -6.479  -13.022 1.00 22.70  ?  117 TRP A CH2  1 
ATOM   849  N  N    . ALA A 1 118 ? 10.061  -6.649  -6.349  1.00 16.66  ?  118 ALA A N    1 
ATOM   850  C  CA   . ALA A 1 118 ? 8.791   -7.064  -5.773  1.00 16.34  ?  118 ALA A CA   1 
ATOM   851  C  C    . ALA A 1 118 ? 8.380   -8.421  -6.344  1.00 19.26  ?  118 ALA A C    1 
ATOM   852  O  O    . ALA A 1 118 ? 8.808   -8.831  -7.424  1.00 18.34  ?  118 ALA A O    1 
ATOM   853  C  CB   . ALA A 1 118 ? 7.724   -6.025  -6.107  1.00 18.37  ?  118 ALA A CB   1 
ATOM   854  N  N    . ALA A 1 119 ? 7.488   -9.104  -5.617  1.00 19.24  ?  119 ALA A N    1 
ATOM   855  C  CA   . ALA A 1 119 ? 7.113   -10.472 -5.971  1.00 20.36  ?  119 ALA A CA   1 
ATOM   856  C  C    . ALA A 1 119 ? 6.499   -10.570 -7.362  1.00 18.53  ?  119 ALA A C    1 
ATOM   857  O  O    . ALA A 1 119 ? 6.708   -11.565 -8.066  1.00 20.14  ?  119 ALA A O    1 
ATOM   858  C  CB   . ALA A 1 119 ? 6.135   -11.031 -4.934  1.00 21.03  ?  119 ALA A CB   1 
ATOM   859  N  N    . SER A 1 120 ? 5.722   -9.570  -7.764  1.00 19.10  ?  120 SER A N    1 
ATOM   860  C  CA   . SER A 1 120 ? 5.037   -9.585  -9.050  1.00 20.10  ?  120 SER A CA   1 
ATOM   861  C  C    . SER A 1 120 ? 5.911   -9.094  -10.194 1.00 18.95  ?  120 SER A C    1 
ATOM   862  O  O    . SER A 1 120 ? 5.475   -9.136  -11.347 1.00 19.93  ?  120 SER A O    1 
ATOM   863  C  CB   . SER A 1 120 ? 3.842   -8.640  -8.989  1.00 21.46  ?  120 SER A CB   1 
ATOM   864  O  OG   . SER A 1 120 ? 4.326   -7.317  -8.803  1.00 22.19  ?  120 SER A OG   1 
ATOM   865  N  N    . SER A 1 121 ? 7.105   -8.586  -9.900  1.00 18.54  ?  121 SER A N    1 
ATOM   866  C  CA   . SER A 1 121 ? 7.956   -7.979  -10.924 1.00 18.76  ?  121 SER A CA   1 
ATOM   867  C  C    . SER A 1 121 ? 7.248   -6.870  -11.695 1.00 18.51  ?  121 SER A C    1 
ATOM   868  O  O    . SER A 1 121 ? 7.547   -6.664  -12.864 1.00 19.72  ?  121 SER A O    1 
ATOM   869  C  CB   . SER A 1 121 ? 8.512   -9.015  -11.910 1.00 20.96  ?  121 SER A CB   1 
ATOM   870  O  OG   . SER A 1 121 ? 9.211   -10.026 -11.212 1.00 23.37  ?  121 SER A OG   1 
ATOM   871  N  N    . LEU A 1 122 ? 6.307   -6.136  -11.082 1.00 16.89  ?  122 LEU A N    1 
ATOM   872  C  CA   . LEU A 1 122 ? 5.427   -5.277  -11.872 1.00 16.56  ?  122 LEU A CA   1 
ATOM   873  C  C    . LEU A 1 122 ? 6.220   -4.211  -12.625 1.00 16.85  ?  122 LEU A C    1 
ATOM   874  O  O    . LEU A 1 122 ? 5.939   -3.916  -13.794 1.00 18.58  ?  122 LEU A O    1 
ATOM   875  C  CB   . LEU A 1 122 ? 4.355   -4.632  -10.983 1.00 17.80  ?  122 LEU A CB   1 
ATOM   876  C  CG   . LEU A 1 122 ? 3.252   -3.884  -11.747 1.00 19.65  ?  122 LEU A CG   1 
ATOM   877  C  CD1  . LEU A 1 122 ? 2.330   -4.880  -12.406 1.00 24.59  ?  122 LEU A CD1  1 
ATOM   878  C  CD2  . LEU A 1 122 ? 2.434   -2.968  -10.823 1.00 19.83  ?  122 LEU A CD2  1 
ATOM   879  N  N    . VAL A 1 123 ? 7.166   -3.575  -11.943 1.00 17.12  ?  123 VAL A N    1 
ATOM   880  C  CA   . VAL A 1 123 ? 8.103   -2.660  -12.594 1.00 17.71  ?  123 VAL A CA   1 
ATOM   881  C  C    . VAL A 1 123 ? 9.517   -2.972  -12.127 1.00 18.28  ?  123 VAL A C    1 
ATOM   882  O  O    . VAL A 1 123 ? 9.741   -3.577  -11.077 1.00 18.60  ?  123 VAL A O    1 
ATOM   883  C  CB   . VAL A 1 123 ? 7.784   -1.163  -12.359 1.00 18.23  ?  123 VAL A CB   1 
ATOM   884  C  CG1  . VAL A 1 123 ? 6.410   -0.795  -12.934 1.00 20.10  ?  123 VAL A CG1  1 
ATOM   885  C  CG2  . VAL A 1 123 ? 7.865   -0.811  -10.864 1.00 18.38  ?  123 VAL A CG2  1 
ATOM   886  N  N    . HIS A 1 124 ? 10.474  -2.513  -12.921 1.00 18.35  ?  124 HIS A N    1 
ATOM   887  C  CA   . HIS A 1 124 ? 11.872  -2.774  -12.644 1.00 17.74  ?  124 HIS A CA   1 
ATOM   888  C  C    . HIS A 1 124 ? 12.283  -2.059  -11.356 1.00 18.24  ?  124 HIS A C    1 
ATOM   889  O  O    . HIS A 1 124 ? 11.847  -0.930  -11.101 1.00 19.67  ?  124 HIS A O    1 
ATOM   890  C  CB   . HIS A 1 124 ? 12.688  -2.228  -13.816 1.00 18.28  ?  124 HIS A CB   1 
ATOM   891  C  CG   . HIS A 1 124 ? 14.118  -2.662  -13.841 1.00 19.25  ?  124 HIS A CG   1 
ATOM   892  N  ND1  . HIS A 1 124 ? 15.064  -2.144  -12.984 1.00 20.51  ?  124 HIS A ND1  1 
ATOM   893  C  CD2  . HIS A 1 124 ? 14.775  -3.533  -14.647 1.00 19.64  ?  124 HIS A CD2  1 
ATOM   894  C  CE1  . HIS A 1 124 ? 16.243  -2.680  -13.257 1.00 21.52  ?  124 HIS A CE1  1 
ATOM   895  N  NE2  . HIS A 1 124 ? 16.095  -3.522  -14.263 1.00 22.30  ?  124 HIS A NE2  1 
ATOM   896  N  N    . PRO A 1 125 ? 13.147  -2.661  -10.552 1.00 17.28  ?  125 PRO A N    1 
ATOM   897  C  CA   . PRO A 1 125 ? 13.585  -2.005  -9.315  1.00 17.69  ?  125 PRO A CA   1 
ATOM   898  C  C    . PRO A 1 125 ? 14.434  -0.767  -9.573  1.00 17.65  ?  125 PRO A C    1 
ATOM   899  O  O    . PRO A 1 125 ? 15.041  -0.580  -10.634 1.00 20.90  ?  125 PRO A O    1 
ATOM   900  C  CB   . PRO A 1 125 ? 14.423  -3.081  -8.612  1.00 17.16  ?  125 PRO A CB   1 
ATOM   901  C  CG   . PRO A 1 125 ? 14.106  -4.367  -9.289  1.00 20.82  ?  125 PRO A CG   1 
ATOM   902  C  CD   . PRO A 1 125 ? 13.672  -4.028  -10.689 1.00 19.68  ?  125 PRO A CD   1 
ATOM   903  N  N    . ARG A 1 126 ? 14.499  0.069   -8.541  1.00 19.44  ?  126 ARG A N    1 
ATOM   904  C  CA   . ARG A 1 126 ? 15.526  1.092   -8.389  1.00 19.07  ?  126 ARG A CA   1 
ATOM   905  C  C    . ARG A 1 126 ? 16.318  0.793   -7.125  1.00 21.58  ?  126 ARG A C    1 
ATOM   906  O  O    . ARG A 1 126 ? 15.761  0.344   -6.124  1.00 24.87  ?  126 ARG A O    1 
ATOM   907  C  CB   . ARG A 1 126 ? 14.913  2.484   -8.301  1.00 22.03  ?  126 ARG A CB   1 
ATOM   908  C  CG   . ARG A 1 126 ? 14.538  3.040   -9.651  1.00 22.39  ?  126 ARG A CG   1 
ATOM   909  C  CD   . ARG A 1 126 ? 13.743  4.328   -9.530  1.00 23.48  ?  126 ARG A CD   1 
ATOM   910  N  NE   . ARG A 1 126 ? 14.478  5.405   -8.871  1.00 24.25  ?  126 ARG A NE   1 
ATOM   911  C  CZ   . ARG A 1 126 ? 14.040  6.655   -8.789  1.00 26.51  ?  126 ARG A CZ   1 
ATOM   912  N  NH1  . ARG A 1 126 ? 12.903  7.030   -9.358  1.00 26.32  ?  126 ARG A NH1  1 
ATOM   913  N  NH2  . ARG A 1 126 ? 14.755  7.552   -8.113  1.00 29.32  ?  126 ARG A NH2  1 
ATOM   914  N  N    . ALA A 1 127 ? 17.627  1.004   -7.179  1.00 21.57  ?  127 ALA A N    1 
ATOM   915  C  CA   . ALA A 1 127 ? 18.485  0.705   -6.045  1.00 22.37  ?  127 ALA A CA   1 
ATOM   916  C  C    . ALA A 1 127 ? 18.842  1.946   -5.243  1.00 23.31  ?  127 ALA A C    1 
ATOM   917  O  O    . ALA A 1 127 ? 19.791  1.911   -4.455  1.00 28.95  ?  127 ALA A O    1 
ATOM   918  C  CB   . ALA A 1 127 ? 19.751  -0.021  -6.514  1.00 26.89  ?  127 ALA A CB   1 
ATOM   919  N  N    . ASP A 1 128 ? 18.107  3.043   -5.417  1.00 22.68  ?  128 ASP A N    1 
ATOM   920  C  CA   . ASP A 1 128 ? 18.432  4.302   -4.771  1.00 23.55  ?  128 ASP A CA   1 
ATOM   921  C  C    . ASP A 1 128 ? 17.284  4.775   -3.891  1.00 24.32  ?  128 ASP A C    1 
ATOM   922  O  O    . ASP A 1 128 ? 16.114  4.446   -4.128  1.00 23.53  ?  128 ASP A O    1 
ATOM   923  C  CB   . ASP A 1 128 ? 18.751  5.400   -5.809  1.00 25.47  ?  128 ASP A CB   1 
ATOM   924  C  CG   . ASP A 1 128 ? 17.547  5.757   -6.679  1.00 31.64  ?  128 ASP A CG   1 
ATOM   925  O  OD1  . ASP A 1 128 ? 17.097  4.897   -7.462  1.00 26.74  ?  128 ASP A OD1  1 
ATOM   926  O  OD2  . ASP A 1 128 ? 17.053  6.899   -6.579  1.00 36.69  -1 128 ASP A OD2  1 
ATOM   927  N  N    . GLY A 1 129 ? 17.644  5.549   -2.868  1.00 23.68  ?  129 GLY A N    1 
ATOM   928  C  CA   . GLY A 1 129 ? 16.656  6.253   -2.065  1.00 23.93  ?  129 GLY A CA   1 
ATOM   929  C  C    . GLY A 1 129 ? 15.555  5.364   -1.540  1.00 20.81  ?  129 GLY A C    1 
ATOM   930  O  O    . GLY A 1 129 ? 15.794  4.273   -1.009  1.00 21.45  ?  129 GLY A O    1 
ATOM   931  N  N    . VAL A 1 130 ? 14.320  5.844   -1.676  1.00 21.81  ?  130 VAL A N    1 
ATOM   932  C  CA   . VAL A 1 130 ? 13.196  5.161   -1.057  1.00 21.54  ?  130 VAL A CA   1 
ATOM   933  C  C    . VAL A 1 130 ? 12.834  3.836   -1.713  1.00 21.69  ?  130 VAL A C    1 
ATOM   934  O  O    . VAL A 1 130 ? 11.961  3.141   -1.196  1.00 20.75  ?  130 VAL A O    1 
ATOM   935  C  CB   . VAL A 1 130 ? 11.965  6.087   -1.020  1.00 23.55  ?  130 VAL A CB   1 
ATOM   936  C  CG1  . VAL A 1 130 ? 12.307  7.401   -0.320  1.00 26.31  ?  130 VAL A CG1  1 
ATOM   937  C  CG2  . VAL A 1 130 ? 11.433  6.326   -2.437  1.00 24.93  ?  130 VAL A CG2  1 
ATOM   938  N  N    . TYR A 1 131 ? 13.474  3.461   -2.825  1.00 19.87  ?  131 TYR A N    1 
ATOM   939  C  CA   . TYR A 1 131 ? 13.178  2.228   -3.552  1.00 18.91  ?  131 TYR A CA   1 
ATOM   940  C  C    . TYR A 1 131 ? 14.072  1.073   -3.122  1.00 16.99  ?  131 TYR A C    1 
ATOM   941  O  O    . TYR A 1 131 ? 13.869  -0.053  -3.576  1.00 18.70  ?  131 TYR A O    1 
ATOM   942  C  CB   . TYR A 1 131 ? 13.281  2.492   -5.070  1.00 19.72  ?  131 TYR A CB   1 
ATOM   943  C  CG   . TYR A 1 131 ? 12.441  3.689   -5.453  1.00 19.38  ?  131 TYR A CG   1 
ATOM   944  C  CD1  . TYR A 1 131 ? 11.055  3.587   -5.521  1.00 19.69  ?  131 TYR A CD1  1 
ATOM   945  C  CD2  . TYR A 1 131 ? 13.022  4.928   -5.692  1.00 22.17  ?  131 TYR A CD2  1 
ATOM   946  C  CE1  . TYR A 1 131 ? 10.272  4.688   -5.831  1.00 23.24  ?  131 TYR A CE1  1 
ATOM   947  C  CE2  . TYR A 1 131 ? 12.245  6.031   -6.000  1.00 23.37  ?  131 TYR A CE2  1 
ATOM   948  C  CZ   . TYR A 1 131 ? 10.866  5.903   -6.062  1.00 23.31  ?  131 TYR A CZ   1 
ATOM   949  O  OH   . TYR A 1 131 ? 10.077  6.996   -6.362  1.00 27.66  ?  131 TYR A OH   1 
ATOM   950  N  N    . GLN A 1 132 ? 15.021  1.322   -2.224  1.00 19.21  ?  132 GLN A N    1 
ATOM   951  C  CA   . GLN A 1 132 ? 15.851  0.248   -1.700  1.00 20.00  ?  132 GLN A CA   1 
ATOM   952  C  C    . GLN A 1 132 ? 15.053  -0.673  -0.779  1.00 20.41  ?  132 GLN A C    1 
ATOM   953  O  O    . GLN A 1 132 ? 14.114  -0.253  -0.096  1.00 20.96  ?  132 GLN A O    1 
ATOM   954  C  CB   . GLN A 1 132 ? 17.017  0.849   -0.926  1.00 20.04  ?  132 GLN A CB   1 
ATOM   955  C  CG   . GLN A 1 132 ? 17.964  1.628   -1.810  1.00 22.86  ?  132 GLN A CG   1 
ATOM   956  C  CD   . GLN A 1 132 ? 19.012  2.355   -1.005  1.00 22.89  ?  132 GLN A CD   1 
ATOM   957  O  OE1  . GLN A 1 132 ? 20.160  1.913   -0.901  1.00 24.20  ?  132 GLN A OE1  1 
ATOM   958  N  NE2  . GLN A 1 132 ? 18.630  3.492   -0.437  1.00 24.21  ?  132 GLN A NE2  1 
ATOM   959  N  N    . ARG A 1 133 ? 15.455  -1.937  -0.749  1.00 17.89  ?  133 ARG A N    1 
ATOM   960  C  CA   . ARG A 1 133 ? 14.890  -2.934  0.156   1.00 15.84  ?  133 ARG A CA   1 
ATOM   961  C  C    . ARG A 1 133 ? 15.958  -3.347  1.154   1.00 18.39  ?  133 ARG A C    1 
ATOM   962  O  O    . ARG A 1 133 ? 17.128  -3.475  0.793   1.00 19.47  ?  133 ARG A O    1 
ATOM   963  C  CB   . ARG A 1 133 ? 14.427  -4.157  -0.633  1.00 16.83  ?  133 ARG A CB   1 
ATOM   964  C  CG   . ARG A 1 133 ? 13.275  -3.844  -1.585  1.00 18.91  ?  133 ARG A CG   1 
ATOM   965  C  CD   . ARG A 1 133 ? 13.144  -4.808  -2.759  1.00 18.28  ?  133 ARG A CD   1 
ATOM   966  N  NE   . ARG A 1 133 ? 12.845  -6.175  -2.357  1.00 21.26  ?  133 ARG A NE   1 
ATOM   967  C  CZ   . ARG A 1 133 ? 11.620  -6.658  -2.181  1.00 20.08  ?  133 ARG A CZ   1 
ATOM   968  N  NH1  . ARG A 1 133 ? 10.542  -5.929  -2.436  1.00 20.72  ?  133 ARG A NH1  1 
ATOM   969  N  NH2  . ARG A 1 133 ? 11.465  -7.904  -1.741  1.00 23.27  ?  133 ARG A NH2  1 
ATOM   970  N  N    . VAL A 1 134 ? 15.584  -3.550  2.410   1.00 17.30  ?  134 VAL A N    1 
ATOM   971  C  CA   . VAL A 1 134 ? 16.551  -3.967  3.423   1.00 16.60  ?  134 VAL A CA   1 
ATOM   972  C  C    . VAL A 1 134 ? 16.126  -5.308  3.994   1.00 16.74  ?  134 VAL A C    1 
ATOM   973  O  O    . VAL A 1 134 ? 14.988  -5.459  4.451   1.00 17.68  ?  134 VAL A O    1 
ATOM   974  C  CB   . VAL A 1 134 ? 16.727  -2.930  4.542   1.00 18.37  ?  134 VAL A CB   1 
ATOM   975  C  CG1  . VAL A 1 134 ? 17.657  -3.499  5.620   1.00 21.55  ?  134 VAL A CG1  1 
ATOM   976  C  CG2  . VAL A 1 134 ? 17.270  -1.626  3.992   1.00 21.73  ?  134 VAL A CG2  1 
ATOM   977  N  N    . TYR A 1 135 ? 17.043  -6.271  3.976   1.00 16.86  ?  135 TYR A N    1 
ATOM   978  C  CA   . TYR A 1 135 ? 16.830  -7.626  4.470   1.00 17.53  ?  135 TYR A CA   1 
ATOM   979  C  C    . TYR A 1 135 ? 17.583  -7.827  5.770   1.00 17.85  ?  135 TYR A C    1 
ATOM   980  O  O    . TYR A 1 135 ? 18.672  -7.278  5.959   1.00 18.00  ?  135 TYR A O    1 
ATOM   981  C  CB   . TYR A 1 135 ? 17.355  -8.657  3.454   1.00 16.44  ?  135 TYR A CB   1 
ATOM   982  C  CG   . TYR A 1 135 ? 16.405  -8.851  2.310   1.00 17.40  ?  135 TYR A CG   1 
ATOM   983  C  CD1  . TYR A 1 135 ? 16.209  -7.846  1.367   1.00 16.65  ?  135 TYR A CD1  1 
ATOM   984  C  CD2  . TYR A 1 135 ? 15.662  -10.017 2.199   1.00 17.54  ?  135 TYR A CD2  1 
ATOM   985  C  CE1  . TYR A 1 135 ? 15.299  -8.005  0.343   1.00 18.97  ?  135 TYR A CE1  1 
ATOM   986  C  CE2  . TYR A 1 135 ? 14.765  -10.191 1.171   1.00 19.14  ?  135 TYR A CE2  1 
ATOM   987  C  CZ   . TYR A 1 135 ? 14.589  -9.180  0.254   1.00 18.15  ?  135 TYR A CZ   1 
ATOM   988  O  OH   . TYR A 1 135 ? 13.683  -9.377  -0.747  1.00 20.20  ?  135 TYR A OH   1 
ATOM   989  N  N    . GLY A 1 136 ? 17.005  -8.609  6.664   1.00 16.92  ?  136 GLY A N    1 
ATOM   990  C  CA   . GLY A 1 136 ? 17.700  -9.025  7.873   1.00 16.82  ?  136 GLY A CA   1 
ATOM   991  C  C    . GLY A 1 136 ? 17.631  -10.526 8.037   1.00 17.60  ?  136 GLY A C    1 
ATOM   992  O  O    . GLY A 1 136 ? 16.611  -11.147 7.736   1.00 17.87  ?  136 GLY A O    1 
ATOM   993  N  N    . ILE A 1 137 ? 18.712  -11.096 8.550   1.00 17.33  ?  137 ILE A N    1 
ATOM   994  C  CA   . ILE A 1 137 ? 18.727  -12.477 9.012   1.00 17.73  ?  137 ILE A CA   1 
ATOM   995  C  C    . ILE A 1 137 ? 19.276  -12.465 10.425  1.00 18.41  ?  137 ILE A C    1 
ATOM   996  O  O    . ILE A 1 137 ? 20.435  -12.087 10.639  1.00 19.90  ?  137 ILE A O    1 
ATOM   997  C  CB   . ILE A 1 137 ? 19.589  -13.385 8.121   1.00 18.30  ?  137 ILE A CB   1 
ATOM   998  C  CG1  . ILE A 1 137 ? 19.169  -13.238 6.660   1.00 18.67  ?  137 ILE A CG1  1 
ATOM   999  C  CG2  . ILE A 1 137 ? 19.444  -14.825 8.571   1.00 20.37  ?  137 ILE A CG2  1 
ATOM   1000 C  CD1  . ILE A 1 137 ? 20.014  -14.079 5.692   1.00 21.23  ?  137 ILE A CD1  1 
ATOM   1001 N  N    . LEU A 1 138 ? 18.441  -12.850 11.389  1.00 18.89  ?  138 LEU A N    1 
ATOM   1002 C  CA   . LEU A 1 138 ? 18.853  -12.948 12.777  1.00 18.63  ?  138 LEU A CA   1 
ATOM   1003 C  C    . LEU A 1 138 ? 19.173  -14.412 13.035  1.00 20.37  ?  138 LEU A C    1 
ATOM   1004 O  O    . LEU A 1 138 ? 18.276  -15.266 13.032  1.00 22.18  ?  138 LEU A O    1 
ATOM   1005 C  CB   . LEU A 1 138 ? 17.719  -12.464 13.670  1.00 21.09  ?  138 LEU A CB   1 
ATOM   1006 C  CG   . LEU A 1 138 ? 18.039  -12.042 15.105  1.00 25.71  ?  138 LEU A CG   1 
ATOM   1007 C  CD1  . LEU A 1 138 ? 16.727  -11.777 15.846  1.00 25.17  ?  138 LEU A CD1  1 
ATOM   1008 C  CD2  . LEU A 1 138 ? 18.894  -12.998 15.879  1.00 32.04  ?  138 LEU A CD2  1 
ATOM   1009 N  N    . TYR A 1 139 ? 20.444  -14.705 13.254  1.00 20.55  ?  139 TYR A N    1 
ATOM   1010 C  CA   . TYR A 1 139 ? 20.865  -16.081 13.423  1.00 20.37  ?  139 TYR A CA   1 
ATOM   1011 C  C    . TYR A 1 139 ? 20.648  -16.488 14.863  1.00 24.23  ?  139 TYR A C    1 
ATOM   1012 O  O    . TYR A 1 139 ? 21.095  -15.796 15.780  1.00 25.59  ?  139 TYR A O    1 
ATOM   1013 C  CB   . TYR A 1 139 ? 22.338  -16.215 13.064  1.00 22.97  ?  139 TYR A CB   1 
ATOM   1014 C  CG   . TYR A 1 139 ? 22.653  -15.803 11.638  1.00 22.96  ?  139 TYR A CG   1 
ATOM   1015 C  CD1  . TYR A 1 139 ? 22.319  -16.624 10.566  1.00 21.54  ?  139 TYR A CD1  1 
ATOM   1016 C  CD2  . TYR A 1 139 ? 23.266  -14.594 11.375  1.00 22.01  ?  139 TYR A CD2  1 
ATOM   1017 C  CE1  . TYR A 1 139 ? 22.620  -16.238 9.250   1.00 22.92  ?  139 TYR A CE1  1 
ATOM   1018 C  CE2  . TYR A 1 139 ? 23.583  -14.208 10.077  1.00 24.45  ?  139 TYR A CE2  1 
ATOM   1019 C  CZ   . TYR A 1 139 ? 23.245  -15.025 9.026   1.00 22.82  ?  139 TYR A CZ   1 
ATOM   1020 O  OH   . TYR A 1 139 ? 23.569  -14.622 7.742   1.00 25.42  ?  139 TYR A OH   1 
ATOM   1021 N  N    . LEU A 1 140 ? 19.964  -17.614 15.056  1.00 21.32  ?  140 LEU A N    1 
ATOM   1022 C  CA   . LEU A 1 140 ? 19.654  -18.133 16.381  1.00 22.75  ?  140 LEU A CA   1 
ATOM   1023 C  C    . LEU A 1 140 ? 20.420  -19.411 16.708  1.00 25.50  ?  140 LEU A C    1 
ATOM   1024 O  O    . LEU A 1 140 ? 20.134  -20.070 17.714  1.00 27.52  ?  140 LEU A O    1 
ATOM   1025 C  CB   . LEU A 1 140 ? 18.138  -18.291 16.520  1.00 23.24  ?  140 LEU A CB   1 
ATOM   1026 C  CG   . LEU A 1 140 ? 17.410  -16.939 16.494  1.00 22.62  ?  140 LEU A CG   1 
ATOM   1027 C  CD1  . LEU A 1 140 ? 15.881  -17.110 16.469  1.00 23.46  ?  140 LEU A CD1  1 
ATOM   1028 C  CD2  . LEU A 1 140 ? 17.832  -16.085 17.690  1.00 24.52  ?  140 LEU A CD2  1 
ATOM   1029 N  N    . THR A 1 141 ? 21.394  -19.764 15.875  1.00 24.84  ?  141 THR A N    1 
ATOM   1030 C  CA   . THR A 1 141 ? 22.426  -20.743 16.160  1.00 25.88  ?  141 THR A CA   1 
ATOM   1031 C  C    . THR A 1 141 ? 23.748  -20.126 15.721  1.00 26.67  ?  141 THR A C    1 
ATOM   1032 O  O    . THR A 1 141 ? 23.767  -19.201 14.905  1.00 26.72  ?  141 THR A O    1 
ATOM   1033 C  CB   . THR A 1 141 ? 22.203  -22.046 15.366  1.00 27.76  ?  141 THR A CB   1 
ATOM   1034 O  OG1  . THR A 1 141 ? 21.940  -21.743 13.987  1.00 26.29  ?  141 THR A OG1  1 
ATOM   1035 C  CG2  . THR A 1 141 ? 21.059  -22.863 15.940  1.00 29.14  ?  141 THR A CG2  1 
ATOM   1036 N  N    . ASP A 1 142 ? 24.854  -20.637 16.263  1.00 27.05  ?  142 ASP A N    1 
ATOM   1037 C  CA   . ASP A 1 142 ? 26.171  -20.220 15.789  1.00 28.82  ?  142 ASP A CA   1 
ATOM   1038 C  C    . ASP A 1 142 ? 26.354  -20.679 14.347  1.00 31.23  ?  142 ASP A C    1 
ATOM   1039 O  O    . ASP A 1 142 ? 26.103  -21.844 14.027  1.00 30.54  ?  142 ASP A O    1 
ATOM   1040 C  CB   . ASP A 1 142 ? 27.269  -20.841 16.653  1.00 30.24  ?  142 ASP A CB   1 
ATOM   1041 C  CG   . ASP A 1 142 ? 27.321  -20.263 18.057  1.00 37.52  ?  142 ASP A CG   1 
ATOM   1042 O  OD1  . ASP A 1 142 ? 26.905  -19.099 18.254  1.00 37.79  ?  142 ASP A OD1  1 
ATOM   1043 O  OD2  . ASP A 1 142 ? 27.790  -20.977 18.971  1.00 41.92  -1 142 ASP A OD2  1 
ATOM   1044 N  N    . VAL A 1 143 ? 26.789  -19.771 13.475  1.00 25.80  ?  143 VAL A N    1 
ATOM   1045 C  CA   . VAL A 1 143 ? 26.940  -20.064 12.053  1.00 26.20  ?  143 VAL A CA   1 
ATOM   1046 C  C    . VAL A 1 143 ? 28.424  -20.123 11.721  1.00 27.22  ?  143 VAL A C    1 
ATOM   1047 O  O    . VAL A 1 143 ? 29.133  -19.115 11.839  1.00 28.28  ?  143 VAL A O    1 
ATOM   1048 C  CB   . VAL A 1 143 ? 26.238  -19.024 11.174  1.00 25.14  ?  143 VAL A CB   1 
ATOM   1049 C  CG1  . VAL A 1 143 ? 26.436  -19.376 9.697   1.00 24.57  ?  143 VAL A CG1  1 
ATOM   1050 C  CG2  . VAL A 1 143 ? 24.770  -18.984 11.522  1.00 25.34  ?  143 VAL A CG2  1 
ATOM   1051 N  N    . THR A 1 144 ? 28.884  -21.294 11.294  1.00 26.64  ?  144 THR A N    1 
ATOM   1052 C  CA   . THR A 1 144 ? 30.249  -21.521 10.831  1.00 27.08  ?  144 THR A CA   1 
ATOM   1053 C  C    . THR A 1 144 ? 30.223  -21.854 9.345   1.00 26.61  ?  144 THR A C    1 
ATOM   1054 O  O    . THR A 1 144 ? 29.171  -21.928 8.713   1.00 25.17  ?  144 THR A O    1 
ATOM   1055 C  CB   . THR A 1 144 ? 30.893  -22.683 11.580  1.00 30.44  ?  144 THR A CB   1 
ATOM   1056 O  OG1  . THR A 1 144 ? 30.334  -23.918 11.103  1.00 32.75  ?  144 THR A OG1  1 
ATOM   1057 C  CG2  . THR A 1 144 ? 30.689  -22.553 13.085  1.00 31.45  ?  144 THR A CG2  1 
ATOM   1058 N  N    . GLU A 1 145 ? 31.411  -22.090 8.785   1.00 28.98  ?  145 GLU A N    1 
ATOM   1059 C  CA   . GLU A 1 145 ? 31.463  -22.440 7.372   1.00 29.03  ?  145 GLU A CA   1 
ATOM   1060 C  C    . GLU A 1 145 ? 30.797  -23.775 7.071   1.00 28.04  ?  145 GLU A C    1 
ATOM   1061 O  O    . GLU A 1 145 ? 30.471  -24.037 5.908   1.00 28.83  ?  145 GLU A O    1 
ATOM   1062 C  CB   . GLU A 1 145 ? 32.898  -22.405 6.843   1.00 33.69  ?  145 GLU A CB   1 
ATOM   1063 C  CG   . GLU A 1 145 ? 33.423  -20.988 6.653   1.00 39.26  ?  145 GLU A CG   1 
ATOM   1064 C  CD   . GLU A 1 145 ? 34.780  -20.953 5.974   1.00 41.85  ?  145 GLU A CD   1 
ATOM   1065 O  OE1  . GLU A 1 145 ? 35.402  -22.027 5.818   1.00 51.03  ?  145 GLU A OE1  1 
ATOM   1066 O  OE2  . GLU A 1 145 ? 35.229  -19.851 5.597   1.00 46.05  -1 145 GLU A OE2  1 
ATOM   1067 N  N    . ASP A 1 146 ? 30.543  -24.599 8.081   1.00 26.92  ?  146 ASP A N    1 
ATOM   1068 C  CA   . ASP A 1 146 ? 29.879  -25.879 7.872   1.00 25.58  ?  146 ASP A CA   1 
ATOM   1069 C  C    . ASP A 1 146 ? 28.412  -25.893 8.303   1.00 26.77  ?  146 ASP A C    1 
ATOM   1070 O  O    . ASP A 1 146 ? 27.801  -26.968 8.327   1.00 27.06  ?  146 ASP A O    1 
ATOM   1071 C  CB   . ASP A 1 146 ? 30.666  -27.004 8.539   1.00 27.29  ?  146 ASP A CB   1 
ATOM   1072 C  CG   . ASP A 1 146 ? 31.866  -27.413 7.721   1.00 28.04  ?  146 ASP A CG   1 
ATOM   1073 O  OD1  . ASP A 1 146 ? 31.774  -27.310 6.472   1.00 27.43  ?  146 ASP A OD1  1 
ATOM   1074 O  OD2  . ASP A 1 146 ? 32.883  -27.812 8.325   1.00 29.99  -1 146 ASP A OD2  1 
ATOM   1075 N  N    . THR A 1 147 ? 27.835  -24.745 8.632   1.00 24.53  ?  147 THR A N    1 
ATOM   1076 C  CA   . THR A 1 147 ? 26.419  -24.674 8.997   1.00 24.02  ?  147 THR A CA   1 
ATOM   1077 C  C    . THR A 1 147 ? 25.637  -23.731 8.084   1.00 23.68  ?  147 THR A C    1 
ATOM   1078 O  O    . THR A 1 147 ? 24.795  -22.953 8.539   1.00 23.99  ?  147 THR A O    1 
ATOM   1079 C  CB   . THR A 1 147 ? 26.208  -24.280 10.462  1.00 25.78  ?  147 THR A CB   1 
ATOM   1080 O  OG1  . THR A 1 147 ? 26.602  -22.916 10.662  1.00 27.27  ?  147 THR A OG1  1 
ATOM   1081 C  CG2  . THR A 1 147 ? 26.953  -25.193 11.405  1.00 27.69  ?  147 THR A CG2  1 
ATOM   1082 N  N    . ALA A 1 148 ? 25.907  -23.788 6.774   1.00 24.69  ?  148 ALA A N    1 
ATOM   1083 C  CA   . ALA A 1 148 ? 25.121  -23.082 5.765   1.00 22.85  ?  148 ALA A CA   1 
ATOM   1084 C  C    . ALA A 1 148 ? 25.191  -21.564 5.917   1.00 22.22  ?  148 ALA A C    1 
ATOM   1085 O  O    . ALA A 1 148 ? 24.152  -20.904 6.043   1.00 22.26  ?  148 ALA A O    1 
ATOM   1086 C  CB   . ALA A 1 148 ? 23.660  -23.549 5.771   1.00 23.67  ?  148 ALA A CB   1 
ATOM   1087 N  N    . PRO A 1 149 ? 26.380  -20.977 5.893   1.00 23.02  ?  149 PRO A N    1 
ATOM   1088 C  CA   . PRO A 1 149 ? 26.480  -19.519 5.980   1.00 23.56  ?  149 PRO A CA   1 
ATOM   1089 C  C    . PRO A 1 149 ? 25.882  -18.844 4.756   1.00 24.45  ?  149 PRO A C    1 
ATOM   1090 O  O    . PRO A 1 149 ? 25.883  -19.389 3.647   1.00 24.04  ?  149 PRO A O    1 
ATOM   1091 C  CB   . PRO A 1 149 ? 27.992  -19.281 6.032   1.00 23.70  ?  149 PRO A CB   1 
ATOM   1092 C  CG   . PRO A 1 149 ? 28.565  -20.436 5.283   1.00 24.13  ?  149 PRO A CG   1 
ATOM   1093 C  CD   . PRO A 1 149 ? 27.697  -21.605 5.707   1.00 24.74  ?  149 PRO A CD   1 
ATOM   1094 N  N    . THR A 1 150 ? 25.365  -17.637 4.979   1.00 22.06  ?  150 THR A N    1 
ATOM   1095 C  CA   . THR A 1 150 ? 25.033  -16.740 3.879   1.00 20.22  ?  150 THR A CA   1 
ATOM   1096 C  C    . THR A 1 150 ? 26.310  -16.322 3.163   1.00 21.00  ?  150 THR A C    1 
ATOM   1097 O  O    . THR A 1 150 ? 27.333  -16.054 3.798   1.00 25.17  ?  150 THR A O    1 
ATOM   1098 C  CB   . THR A 1 150 ? 24.368  -15.487 4.438   1.00 19.85  ?  150 THR A CB   1 
ATOM   1099 O  OG1  . THR A 1 150 ? 23.279  -15.864 5.298   1.00 21.39  ?  150 THR A OG1  1 
ATOM   1100 C  CG2  . THR A 1 150 ? 23.811  -14.629 3.317   1.00 22.67  ?  150 THR A CG2  1 
ATOM   1101 N  N    . TYR A 1 151 ? 26.270  -16.288 1.830   1.00 19.64  ?  151 TYR A N    1 
ATOM   1102 C  CA   . TYR A 1 151 ? 27.368  -15.749 1.034   1.00 20.75  ?  151 TYR A CA   1 
ATOM   1103 C  C    . TYR A 1 151 ? 26.966  -14.395 0.463   1.00 20.91  ?  151 TYR A C    1 
ATOM   1104 O  O    . TYR A 1 151 ? 25.820  -14.203 0.049   1.00 21.99  ?  151 TYR A O    1 
ATOM   1105 C  CB   . TYR A 1 151 ? 27.748  -16.685 -0.121  1.00 22.34  ?  151 TYR A CB   1 
ATOM   1106 C  CG   . TYR A 1 151 ? 28.675  -17.818 0.245   1.00 21.65  ?  151 TYR A CG   1 
ATOM   1107 C  CD1  . TYR A 1 151 ? 28.209  -18.910 0.966   1.00 23.36  ?  151 TYR A CD1  1 
ATOM   1108 C  CD2  . TYR A 1 151 ? 30.009  -17.804 -0.147  1.00 23.97  ?  151 TYR A CD2  1 
ATOM   1109 C  CE1  . TYR A 1 151 ? 29.049  -19.956 1.302   1.00 24.86  ?  151 TYR A CE1  1 
ATOM   1110 C  CE2  . TYR A 1 151 ? 30.848  -18.841 0.176   1.00 27.93  ?  151 TYR A CE2  1 
ATOM   1111 C  CZ   . TYR A 1 151 ? 30.365  -19.912 0.897   1.00 27.94  ?  151 TYR A CZ   1 
ATOM   1112 O  OH   . TYR A 1 151 ? 31.225  -20.944 1.213   1.00 33.77  ?  151 TYR A OH   1 
ATOM   1113 N  N    . VAL A 1 152 ? 27.912  -13.451 0.455   1.00 19.58  ?  152 VAL A N    1 
ATOM   1114 C  CA   . VAL A 1 152 ? 27.671  -12.119 -0.083  1.00 21.49  ?  152 VAL A CA   1 
ATOM   1115 C  C    . VAL A 1 152 ? 28.780  -11.757 -1.063  1.00 21.40  ?  152 VAL A C    1 
ATOM   1116 O  O    . VAL A 1 152 ? 29.902  -12.268 -0.979  1.00 22.27  ?  152 VAL A O    1 
ATOM   1117 C  CB   . VAL A 1 152 ? 27.558  -11.048 1.029   1.00 22.53  ?  152 VAL A CB   1 
ATOM   1118 C  CG1  . VAL A 1 152 ? 26.331  -11.299 1.883   1.00 22.30  ?  152 VAL A CG1  1 
ATOM   1119 C  CG2  . VAL A 1 152 ? 28.827  -11.028 1.891   1.00 24.66  ?  152 VAL A CG2  1 
ATOM   1120 N  N    . VAL A 1 153 ? 28.456  -10.880 -2.013  1.00 20.09  ?  153 VAL A N    1 
ATOM   1121 C  CA   . VAL A 1 153 ? 29.457  -10.319 -2.914  1.00 21.26  ?  153 VAL A CA   1 
ATOM   1122 C  C    . VAL A 1 153 ? 29.500  -8.808  -2.695  1.00 21.51  ?  153 VAL A C    1 
ATOM   1123 O  O    . VAL A 1 153 ? 30.289  -8.318  -1.880  1.00 25.47  ?  153 VAL A O    1 
ATOM   1124 C  CB   . VAL A 1 153 ? 29.208  -10.711 -4.384  1.00 22.04  ?  153 VAL A CB   1 
ATOM   1125 C  CG1  . VAL A 1 153 ? 30.417  -10.372 -5.238  1.00 24.34  ?  153 VAL A CG1  1 
ATOM   1126 C  CG2  . VAL A 1 153 ? 28.888  -12.200 -4.501  1.00 25.45  ?  153 VAL A CG2  1 
ATOM   1127 N  N    . ASP A 1 154 ? 28.640  -8.070  -3.389  1.00 20.44  ?  154 ASP A N    1 
ATOM   1128 C  CA   . ASP A 1 154 ? 28.580  -6.612  -3.316  1.00 20.31  ?  154 ASP A CA   1 
ATOM   1129 C  C    . ASP A 1 154 ? 27.303  -6.197  -4.034  1.00 21.02  ?  154 ASP A C    1 
ATOM   1130 O  O    . ASP A 1 154 ? 26.596  -7.032  -4.605  1.00 19.19  ?  154 ASP A O    1 
ATOM   1131 C  CB   . ASP A 1 154 ? 29.811  -6.011  -4.004  1.00 20.57  ?  154 ASP A CB   1 
ATOM   1132 C  CG   . ASP A 1 154 ? 30.115  -4.552  -3.593  1.00 24.39  ?  154 ASP A CG   1 
ATOM   1133 O  OD1  . ASP A 1 154 ? 29.237  -3.785  -3.134  1.00 23.94  ?  154 ASP A OD1  1 
ATOM   1134 O  OD2  . ASP A 1 154 ? 31.294  -4.157  -3.792  1.00 27.83  -1 154 ASP A OD2  1 
ATOM   1135 N  N    . ARG A 1 155 ? 27.015  -4.900  -4.016  1.00 19.47  ?  155 ARG A N    1 
ATOM   1136 C  CA   . ARG A 1 155 ? 25.827  -4.398  -4.690  1.00 19.37  ?  155 ARG A CA   1 
ATOM   1137 C  C    . ARG A 1 155 ? 25.950  -4.627  -6.189  1.00 19.52  ?  155 ARG A C    1 
ATOM   1138 O  O    . ARG A 1 155 ? 27.035  -4.503  -6.761  1.00 20.17  ?  155 ARG A O    1 
ATOM   1139 C  CB   . ARG A 1 155 ? 25.685  -2.903  -4.429  1.00 17.78  ?  155 ARG A CB   1 
ATOM   1140 C  CG   . ARG A 1 155 ? 25.621  -2.569  -2.939  1.00 20.17  ?  155 ARG A CG   1 
ATOM   1141 C  CD   . ARG A 1 155 ? 25.153  -1.142  -2.688  1.00 19.91  ?  155 ARG A CD   1 
ATOM   1142 N  NE   . ARG A 1 155 ? 23.709  -1.006  -2.865  1.00 21.56  ?  155 ARG A NE   1 
ATOM   1143 C  CZ   . ARG A 1 155 ? 23.000  0.027   -2.432  1.00 20.72  ?  155 ARG A CZ   1 
ATOM   1144 N  NH1  . ARG A 1 155 ? 23.579  1.052   -1.823  1.00 23.64  ?  155 ARG A NH1  1 
ATOM   1145 N  NH2  . ARG A 1 155 ? 21.678  0.027   -2.606  1.00 23.18  ?  155 ARG A NH2  1 
ATOM   1146 N  N    . ALA A 1 156 ? 24.820  -4.941  -6.828  1.00 18.93  ?  156 ALA A N    1 
ATOM   1147 C  CA   . ALA A 1 156 ? 24.841  -5.277  -8.252  1.00 18.03  ?  156 ALA A CA   1 
ATOM   1148 C  C    . ALA A 1 156 ? 25.461  -4.161  -9.086  1.00 20.52  ?  156 ALA A C    1 
ATOM   1149 O  O    . ALA A 1 156 ? 26.236  -4.433  -10.005 1.00 20.47  ?  156 ALA A O    1 
ATOM   1150 C  CB   . ALA A 1 156 ? 23.425  -5.580  -8.750  1.00 19.57  ?  156 ALA A CB   1 
ATOM   1151 N  N    . ALA A 1 157 ? 25.105  -2.902  -8.813  1.00 20.03  ?  157 ALA A N    1 
ATOM   1152 C  CA   . ALA A 1 157 ? 25.662  -1.813  -9.612  1.00 20.98  ?  157 ALA A CA   1 
ATOM   1153 C  C    . ALA A 1 157 ? 27.176  -1.741  -9.461  1.00 21.61  ?  157 ALA A C    1 
ATOM   1154 O  O    . ALA A 1 157 ? 27.891  -1.428  -10.420 1.00 25.73  ?  157 ALA A O    1 
ATOM   1155 C  CB   . ALA A 1 157 ? 25.018  -0.478  -9.239  1.00 24.12  ?  157 ALA A CB   1 
ATOM   1156 N  N    . HIS A 1 158 ? 27.687  -2.032  -8.264  1.00 20.77  ?  158 HIS A N    1 
ATOM   1157 C  CA   . HIS A 1 158 ? 29.129  -1.999  -8.042  1.00 22.12  ?  158 HIS A CA   1 
ATOM   1158 C  C    . HIS A 1 158 ? 29.847  -3.073  -8.852  1.00 22.38  ?  158 HIS A C    1 
ATOM   1159 O  O    . HIS A 1 158 ? 30.992  -2.881  -9.272  1.00 24.36  ?  158 HIS A O    1 
ATOM   1160 C  CB   . HIS A 1 158 ? 29.393  -2.175  -6.544  1.00 22.64  ?  158 HIS A CB   1 
ATOM   1161 C  CG   . HIS A 1 158 ? 28.885  -1.043  -5.699  1.00 22.17  ?  158 HIS A CG   1 
ATOM   1162 N  ND1  . HIS A 1 158 ? 28.937  -1.064  -4.321  1.00 22.08  ?  158 HIS A ND1  1 
ATOM   1163 C  CD2  . HIS A 1 158 ? 28.359  0.161   -6.037  1.00 22.70  ?  158 HIS A CD2  1 
ATOM   1164 C  CE1  . HIS A 1 158 ? 28.451  0.070   -3.846  1.00 24.50  ?  158 HIS A CE1  1 
ATOM   1165 N  NE2  . HIS A 1 158 ? 28.098  0.835   -4.864  1.00 21.99  ?  158 HIS A NE2  1 
ATOM   1166 N  N    . LEU A 1 159 ? 29.184  -4.197  -9.095  1.00 21.63  ?  159 LEU A N    1 
ATOM   1167 C  CA   . LEU A 1 159 ? 29.748  -5.316  -9.825  1.00 21.30  ?  159 LEU A CA   1 
ATOM   1168 C  C    . LEU A 1 159 ? 29.488  -5.215  -11.316 1.00 21.62  ?  159 LEU A C    1 
ATOM   1169 O  O    . LEU A 1 159 ? 29.997  -6.043  -12.077 1.00 26.59  ?  159 LEU A O    1 
ATOM   1170 C  CB   . LEU A 1 159 ? 29.156  -6.624  -9.277  1.00 21.92  ?  159 LEU A CB   1 
ATOM   1171 C  CG   . LEU A 1 159 ? 29.564  -6.878  -7.827  1.00 21.92  ?  159 LEU A CG   1 
ATOM   1172 C  CD1  . LEU A 1 159 ? 28.629  -7.870  -7.151  1.00 24.26  ?  159 LEU A CD1  1 
ATOM   1173 C  CD2  . LEU A 1 159 ? 31.010  -7.370  -7.768  1.00 26.12  ?  159 LEU A CD2  1 
ATOM   1174 N  N    . GLY A 1 160 ? 28.700  -4.230  -11.739 1.00 23.03  ?  160 GLY A N    1 
ATOM   1175 C  CA   . GLY A 1 160 ? 28.378  -4.078  -13.142 1.00 23.53  ?  160 GLY A CA   1 
ATOM   1176 C  C    . GLY A 1 160 ? 27.488  -5.169  -13.682 1.00 24.02  ?  160 GLY A C    1 
ATOM   1177 O  O    . GLY A 1 160 ? 27.609  -5.534  -14.860 1.00 28.00  ?  160 GLY A O    1 
ATOM   1178 N  N    . VAL A 1 161 ? 26.602  -5.706  -12.850 1.00 22.61  ?  161 VAL A N    1 
ATOM   1179 C  CA   . VAL A 1 161 ? 25.639  -6.698  -13.317 1.00 22.55  ?  161 VAL A CA   1 
ATOM   1180 C  C    . VAL A 1 161 ? 24.231  -6.134  -13.215 1.00 20.67  ?  161 VAL A C    1 
ATOM   1181 O  O    . VAL A 1 161 ? 23.926  -5.349  -12.296 1.00 21.67  ?  161 VAL A O    1 
ATOM   1182 C  CB   . VAL A 1 161 ? 25.787  -8.045  -12.594 1.00 19.16  ?  161 VAL A CB   1 
ATOM   1183 C  CG1  . VAL A 1 161 ? 27.200  -8.599  -12.830 1.00 23.26  ?  161 VAL A CG1  1 
ATOM   1184 C  CG2  . VAL A 1 161 ? 25.470  -7.923  -11.094 1.00 21.21  ?  161 VAL A CG2  1 
ATOM   1185 N  N    . PRO A 1 162 ? 23.342  -6.531  -14.113 1.00 20.83  ?  162 PRO A N    1 
ATOM   1186 C  CA   . PRO A 1 162 ? 21.985  -5.987  -14.115 1.00 20.29  ?  162 PRO A CA   1 
ATOM   1187 C  C    . PRO A 1 162 ? 21.118  -6.634  -13.043 1.00 21.36  ?  162 PRO A C    1 
ATOM   1188 O  O    . PRO A 1 162 ? 21.364  -7.751  -12.579 1.00 19.32  ?  162 PRO A O    1 
ATOM   1189 C  CB   . PRO A 1 162 ? 21.490  -6.381  -15.512 1.00 22.71  ?  162 PRO A CB   1 
ATOM   1190 C  CG   . PRO A 1 162 ? 22.116  -7.720  -15.731 1.00 20.19  ?  162 PRO A CG   1 
ATOM   1191 C  CD   . PRO A 1 162 ? 23.532  -7.533  -15.177 1.00 22.08  ?  162 PRO A CD   1 
ATOM   1192 N  N    . LEU A 1 163 ? 20.075  -5.902  -12.660 1.00 19.43  ?  163 LEU A N    1 
ATOM   1193 C  CA   . LEU A 1 163 ? 19.092  -6.459  -11.741 1.00 17.34  ?  163 LEU A CA   1 
ATOM   1194 C  C    . LEU A 1 163 ? 18.163  -7.459  -12.427 1.00 18.16  ?  163 LEU A C    1 
ATOM   1195 O  O    . LEU A 1 163 ? 17.606  -8.332  -11.747 1.00 18.26  ?  163 LEU A O    1 
ATOM   1196 C  CB   . LEU A 1 163 ? 18.286  -5.340  -11.087 1.00 19.35  ?  163 LEU A CB   1 
ATOM   1197 C  CG   . LEU A 1 163 ? 19.096  -4.443  -10.149 1.00 20.17  ?  163 LEU A CG   1 
ATOM   1198 C  CD1  . LEU A 1 163 ? 18.210  -3.369  -9.564  1.00 21.63  ?  163 LEU A CD1  1 
ATOM   1199 C  CD2  . LEU A 1 163 ? 19.751  -5.261  -9.042  1.00 20.77  ?  163 LEU A CD2  1 
ATOM   1200 N  N    . LEU A 1 164 ? 17.979  -7.340  -13.749 1.00 19.14  ?  164 LEU A N    1 
ATOM   1201 C  CA   . LEU A 1 164 ? 17.267  -8.320  -14.559 1.00 20.79  ?  164 LEU A CA   1 
ATOM   1202 C  C    . LEU A 1 164 ? 18.274  -8.941  -15.514 1.00 21.68  ?  164 LEU A C    1 
ATOM   1203 O  O    . LEU A 1 164 ? 18.830  -8.244  -16.371 1.00 22.35  ?  164 LEU A O    1 
ATOM   1204 C  CB   . LEU A 1 164 ? 16.153  -7.652  -15.361 1.00 22.88  ?  164 LEU A CB   1 
ATOM   1205 C  CG   . LEU A 1 164 ? 15.255  -8.597  -16.175 1.00 25.89  ?  164 LEU A CG   1 
ATOM   1206 C  CD1  . LEU A 1 164 ? 14.595  -9.638  -15.280 1.00 24.89  ?  164 LEU A CD1  1 
ATOM   1207 C  CD2  . LEU A 1 164 ? 14.206  -7.812  -16.938 1.00 31.73  ?  164 LEU A CD2  1 
ATOM   1208 N  N    . THR A 1 165 ? 18.501  -10.239 -15.374 1.00 21.83  ?  165 THR A N    1 
ATOM   1209 C  CA   . THR A 1 165 ? 19.478  -10.894 -16.224 1.00 22.25  ?  165 THR A CA   1 
ATOM   1210 C  C    . THR A 1 165 ? 18.844  -11.317 -17.540 1.00 25.76  ?  165 THR A C    1 
ATOM   1211 O  O    . THR A 1 165 ? 17.618  -11.339 -17.681 1.00 23.59  ?  165 THR A O    1 
ATOM   1212 C  CB   . THR A 1 165 ? 20.048  -12.119 -15.518 1.00 25.41  ?  165 THR A CB   1 
ATOM   1213 O  OG1  . THR A 1 165 ? 18.987  -13.032 -15.211 1.00 27.55  ?  165 THR A OG1  1 
ATOM   1214 C  CG2  . THR A 1 165 ? 20.782  -11.712 -14.229 1.00 25.20  ?  165 THR A CG2  1 
ATOM   1215 N  N    . PRO A 1 166 ? 19.654  -11.635 -18.541 1.00 24.91  ?  166 PRO A N    1 
ATOM   1216 C  CA   . PRO A 1 166 ? 19.083  -12.137 -19.796 1.00 24.74  ?  166 PRO A CA   1 
ATOM   1217 C  C    . PRO A 1 166 ? 18.160  -13.339 -19.621 1.00 28.96  ?  166 PRO A C    1 
ATOM   1218 O  O    . PRO A 1 166 ? 17.229  -13.507 -20.420 1.00 30.54  ?  166 PRO A O    1 
ATOM   1219 C  CB   . PRO A 1 166 ? 20.330  -12.446 -20.636 1.00 25.43  ?  166 PRO A CB   1 
ATOM   1220 C  CG   . PRO A 1 166 ? 21.353  -11.479 -20.130 1.00 26.79  ?  166 PRO A CG   1 
ATOM   1221 C  CD   . PRO A 1 166 ? 21.106  -11.412 -18.639 1.00 24.86  ?  166 PRO A CD   1 
ATOM   1222 N  N    . GLU A 1 167 ? 18.357  -14.160 -18.582 1.00 25.62  ?  167 GLU A N    1 
ATOM   1223 C  CA   . GLU A 1 167 ? 17.462  -15.295 -18.349 1.00 27.94  ?  167 GLU A CA   1 
ATOM   1224 C  C    . GLU A 1 167 ? 16.086  -14.873 -17.859 1.00 28.24  ?  167 GLU A C    1 
ATOM   1225 O  O    . GLU A 1 167 ? 15.189  -15.718 -17.795 1.00 27.88  ?  167 GLU A O    1 
ATOM   1226 C  CB   . GLU A 1 167 ? 18.083  -16.312 -17.376 1.00 31.36  ?  167 GLU A CB   1 
ATOM   1227 C  CG   . GLU A 1 167 ? 18.065  -15.917 -15.903 1.00 33.96  ?  167 GLU A CG   1 
ATOM   1228 C  CD   . GLU A 1 167 ? 18.443  -17.074 -14.963 1.00 36.23  ?  167 GLU A CD   1 
ATOM   1229 O  OE1  . GLU A 1 167 ? 19.435  -17.783 -15.239 1.00 38.46  ?  167 GLU A OE1  1 
ATOM   1230 O  OE2  . GLU A 1 167 ? 17.734  -17.277 -13.945 1.00 36.54  -1 167 GLU A OE2  1 
ATOM   1231 N  N    . GLY A 1 168 ? 15.894  -13.602 -17.523 1.00 25.07  ?  168 GLY A N    1 
ATOM   1232 C  CA   . GLY A 1 168 ? 14.594  -13.128 -17.085 1.00 25.84  ?  168 GLY A CA   1 
ATOM   1233 C  C    . GLY A 1 168 ? 14.338  -13.256 -15.604 1.00 23.58  ?  168 GLY A C    1 
ATOM   1234 O  O    . GLY A 1 168 ? 13.172  -13.300 -15.187 1.00 23.32  ?  168 GLY A O    1 
ATOM   1235 N  N    . THR A 1 169 ? 15.389  -13.290 -14.785 1.00 22.95  ?  169 THR A N    1 
ATOM   1236 C  CA   . THR A 1 169 ? 15.253  -13.369 -13.340 1.00 23.40  ?  169 THR A CA   1 
ATOM   1237 C  C    . THR A 1 169 ? 16.241  -12.401 -12.704 1.00 21.92  ?  169 THR A C    1 
ATOM   1238 O  O    . THR A 1 169 ? 16.958  -11.659 -13.389 1.00 23.29  ?  169 THR A O    1 
ATOM   1239 C  CB   . THR A 1 169 ? 15.549  -14.784 -12.828 1.00 27.19  ?  169 THR A CB   1 
ATOM   1240 O  OG1  . THR A 1 169 ? 16.932  -15.083 -13.038 1.00 27.85  ?  169 THR A OG1  1 
ATOM   1241 C  CG2  . THR A 1 169 ? 14.705  -15.823 -13.560 1.00 28.40  ?  169 THR A CG2  1 
ATOM   1242 N  N    . GLY A 1 170 ? 16.283  -12.415 -11.378 1.00 21.66  ?  170 GLY A N    1 
ATOM   1243 C  CA   . GLY A 1 170 ? 17.338  -11.716 -10.671 1.00 18.54  ?  170 GLY A CA   1 
ATOM   1244 C  C    . GLY A 1 170 ? 18.438  -12.647 -10.207 1.00 20.37  ?  170 GLY A C    1 
ATOM   1245 O  O    . GLY A 1 170 ? 19.162  -12.298 -9.277  1.00 20.91  ?  170 GLY A O    1 
ATOM   1246 N  N    . ALA A 1 171 ? 18.579  -13.817 -10.827 1.00 18.79  ?  171 ALA A N    1 
ATOM   1247 C  CA   . ALA A 1 171 ? 19.616  -14.792 -10.481 1.00 21.23  ?  171 ALA A CA   1 
ATOM   1248 C  C    . ALA A 1 171 ? 20.714  -14.835 -11.541 1.00 21.75  ?  171 ALA A C    1 
ATOM   1249 O  O    . ALA A 1 171 ? 20.468  -14.580 -12.725 1.00 22.18  ?  171 ALA A O    1 
ATOM   1250 C  CB   . ALA A 1 171 ? 19.039  -16.196 -10.317 1.00 22.05  ?  171 ALA A CB   1 
ATOM   1251 N  N    . TYR A 1 172 ? 21.934  -15.171 -11.102 1.00 20.24  ?  172 TYR A N    1 
ATOM   1252 C  CA   . TYR A 1 172 ? 23.148  -15.084 -11.917 1.00 20.07  ?  172 TYR A CA   1 
ATOM   1253 C  C    . TYR A 1 172 ? 23.731  -16.480 -12.070 1.00 24.39  ?  172 TYR A C    1 
ATOM   1254 O  O    . TYR A 1 172 ? 24.246  -17.046 -11.104 1.00 24.33  ?  172 TYR A O    1 
ATOM   1255 C  CB   . TYR A 1 172 ? 24.170  -14.151 -11.253 1.00 19.79  ?  172 TYR A CB   1 
ATOM   1256 C  CG   . TYR A 1 172 ? 23.588  -12.786 -10.991 1.00 18.23  ?  172 TYR A CG   1 
ATOM   1257 C  CD1  . TYR A 1 172 ? 23.515  -11.833 -12.004 1.00 19.68  ?  172 TYR A CD1  1 
ATOM   1258 C  CD2  . TYR A 1 172 ? 23.098  -12.448 -9.737  1.00 18.77  ?  172 TYR A CD2  1 
ATOM   1259 C  CE1  . TYR A 1 172 ? 22.945  -10.581 -11.775 1.00 19.01  ?  172 TYR A CE1  1 
ATOM   1260 C  CE2  . TYR A 1 172 ? 22.523  -11.210 -9.503  1.00 19.84  ?  172 TYR A CE2  1 
ATOM   1261 C  CZ   . TYR A 1 172 ? 22.445  -10.287 -10.518 1.00 19.46  ?  172 TYR A CZ   1 
ATOM   1262 O  OH   . TYR A 1 172 ? 21.867  -9.066  -10.260 1.00 19.46  ?  172 TYR A OH   1 
ATOM   1263 N  N    . SER A 1 173 ? 23.663  -17.030 -13.277 1.00 23.45  ?  173 SER A N    1 
ATOM   1264 C  CA   . SER A 1 173 ? 24.206  -18.359 -13.510 1.00 27.39  ?  173 SER A CA   1 
ATOM   1265 C  C    . SER A 1 173 ? 25.731  -18.344 -13.410 1.00 26.06  ?  173 SER A C    1 
ATOM   1266 O  O    . SER A 1 173 ? 26.389  -17.330 -13.664 1.00 25.44  ?  173 SER A O    1 
ATOM   1267 C  CB   . SER A 1 173 ? 23.789  -18.856 -14.893 1.00 29.77  ?  173 SER A CB   1 
ATOM   1268 O  OG   . SER A 1 173 ? 24.492  -18.154 -15.902 1.00 30.43  ?  173 SER A OG   1 
ATOM   1269 N  N    . LYS A 1 174 ? 26.295  -19.494 -13.030 1.00 28.29  ?  174 LYS A N    1 
ATOM   1270 C  CA   . LYS A 1 174 ? 27.748  -19.622 -12.996 1.00 29.37  ?  174 LYS A CA   1 
ATOM   1271 C  C    . LYS A 1 174 ? 28.364  -19.475 -14.382 1.00 29.57  ?  174 LYS A C    1 
ATOM   1272 O  O    . LYS A 1 174 ? 29.464  -18.939 -14.513 1.00 32.52  ?  174 LYS A O    1 
ATOM   1273 C  CB   . LYS A 1 174 ? 28.155  -20.962 -12.381 1.00 31.39  ?  174 LYS A CB   1 
ATOM   1274 C  CG   . LYS A 1 174 ? 27.705  -21.133 -10.944 1.00 32.78  ?  174 LYS A CG   1 
ATOM   1275 C  CD   . LYS A 1 174 ? 28.134  -22.481 -10.386 1.00 36.21  ?  174 LYS A CD   1 
ATOM   1276 C  CE   . LYS A 1 174 ? 27.688  -22.614 -8.936  1.00 36.18  ?  174 LYS A CE   1 
ATOM   1277 N  NZ   . LYS A 1 174 ? 27.954  -23.965 -8.370  1.00 44.51  ?  174 LYS A NZ   1 
ATOM   1278 N  N    . GLU A 1 175 ? 27.666  -19.922 -15.426 1.00 31.42  ?  175 GLU A N    1 
ATOM   1279 C  CA   . GLU A 1 175 ? 28.253  -19.842 -16.759 1.00 36.62  ?  175 GLU A CA   1 
ATOM   1280 C  C    . GLU A 1 175 ? 28.282  -18.405 -17.267 1.00 33.69  ?  175 GLU A C    1 
ATOM   1281 O  O    . GLU A 1 175 ? 29.249  -17.991 -17.916 1.00 36.75  ?  175 GLU A O    1 
ATOM   1282 C  CB   . GLU A 1 175 ? 27.517  -20.777 -17.720 1.00 39.68  ?  175 GLU A CB   1 
ATOM   1283 C  CG   . GLU A 1 175 ? 25.995  -20.694 -17.659 1.00 44.28  ?  175 GLU A CG   1 
ATOM   1284 C  CD   . GLU A 1 175 ? 25.353  -21.677 -16.668 1.00 49.09  ?  175 GLU A CD   1 
ATOM   1285 O  OE1  . GLU A 1 175 ? 25.807  -21.776 -15.494 1.00 39.15  ?  175 GLU A OE1  1 
ATOM   1286 O  OE2  . GLU A 1 175 ? 24.375  -22.352 -17.080 1.00 50.28  -1 175 GLU A OE2  1 
ATOM   1287 N  N    . ALA A 1 176 ? 27.249  -17.617 -16.952 1.00 32.13  ?  176 ALA A N    1 
ATOM   1288 C  CA   . ALA A 1 176 ? 27.179  -16.249 -17.451 1.00 34.10  ?  176 ALA A CA   1 
ATOM   1289 C  C    . ALA A 1 176 ? 27.895  -15.237 -16.567 1.00 30.39  ?  176 ALA A C    1 
ATOM   1290 O  O    . ALA A 1 176 ? 28.327  -14.197 -17.074 1.00 31.51  ?  176 ALA A O    1 
ATOM   1291 C  CB   . ALA A 1 176 ? 25.727  -15.819 -17.679 1.00 33.18  ?  176 ALA A CB   1 
ATOM   1292 N  N    . TYR A 1 177 ? 28.042  -15.510 -15.270 1.00 26.52  ?  177 TYR A N    1 
ATOM   1293 C  CA   . TYR A 1 177 ? 28.612  -14.545 -14.328 1.00 26.20  ?  177 TYR A CA   1 
ATOM   1294 C  C    . TYR A 1 177 ? 29.687  -15.201 -13.471 1.00 26.66  ?  177 TYR A C    1 
ATOM   1295 O  O    . TYR A 1 177 ? 29.605  -15.218 -12.241 1.00 25.61  ?  177 TYR A O    1 
ATOM   1296 C  CB   . TYR A 1 177 ? 27.502  -13.949 -13.464 1.00 23.71  ?  177 TYR A CB   1 
ATOM   1297 C  CG   . TYR A 1 177 ? 26.454  -13.226 -14.278 1.00 25.01  ?  177 TYR A CG   1 
ATOM   1298 C  CD1  . TYR A 1 177 ? 26.624  -11.892 -14.623 1.00 23.66  ?  177 TYR A CD1  1 
ATOM   1299 C  CD2  . TYR A 1 177 ? 25.304  -13.879 -14.711 1.00 25.89  ?  177 TYR A CD2  1 
ATOM   1300 C  CE1  . TYR A 1 177 ? 25.671  -11.219 -15.373 1.00 25.23  ?  177 TYR A CE1  1 
ATOM   1301 C  CE2  . TYR A 1 177 ? 24.343  -13.211 -15.451 1.00 24.76  ?  177 TYR A CE2  1 
ATOM   1302 C  CZ   . TYR A 1 177 ? 24.539  -11.882 -15.783 1.00 26.51  ?  177 TYR A CZ   1 
ATOM   1303 O  OH   . TYR A 1 177 ? 23.585  -11.202 -16.516 1.00 28.97  ?  177 TYR A OH   1 
ATOM   1304 N  N    . PRO A 1 178 ? 30.724  -15.746 -14.094 1.00 27.01  ?  178 PRO A N    1 
ATOM   1305 C  CA   . PRO A 1 178 ? 31.754  -16.436 -13.302 1.00 27.20  ?  178 PRO A CA   1 
ATOM   1306 C  C    . PRO A 1 178 ? 32.445  -15.554 -12.275 1.00 29.29  ?  178 PRO A C    1 
ATOM   1307 O  O    . PRO A 1 178 ? 32.825  -16.052 -11.208 1.00 27.59  ?  178 PRO A O    1 
ATOM   1308 C  CB   . PRO A 1 178 ? 32.735  -16.950 -14.367 1.00 29.24  ?  178 PRO A CB   1 
ATOM   1309 C  CG   . PRO A 1 178 ? 32.512  -16.051 -15.556 1.00 30.56  ?  178 PRO A CG   1 
ATOM   1310 C  CD   . PRO A 1 178 ? 31.033  -15.737 -15.534 1.00 26.73  ?  178 PRO A CD   1 
ATOM   1311 N  N    . GLU A 1 179 ? 32.644  -14.264 -12.564 1.00 28.81  ?  179 GLU A N    1 
ATOM   1312 C  CA   . GLU A 1 179 ? 33.378  -13.419 -11.626 1.00 33.28  ?  179 GLU A CA   1 
ATOM   1313 C  C    . GLU A 1 179 ? 32.629  -13.259 -10.312 1.00 29.97  ?  179 GLU A C    1 
ATOM   1314 O  O    . GLU A 1 179 ? 33.253  -13.079 -9.260  1.00 31.24  ?  179 GLU A O    1 
ATOM   1315 C  CB   . GLU A 1 179 ? 33.669  -12.049 -12.240 1.00 34.99  ?  179 GLU A CB   1 
ATOM   1316 C  CG   . GLU A 1 179 ? 34.608  -12.069 -13.434 1.00 47.40  ?  179 GLU A CG   1 
ATOM   1317 C  CD   . GLU A 1 179 ? 35.010  -10.665 -13.861 1.00 59.65  ?  179 GLU A CD   1 
ATOM   1318 O  OE1  . GLU A 1 179 ? 34.867  -9.728  -13.039 1.00 61.31  ?  179 GLU A OE1  1 
ATOM   1319 O  OE2  . GLU A 1 179 ? 35.459  -10.497 -15.016 1.00 65.29  -1 179 GLU A OE2  1 
ATOM   1320 N  N    . LEU A 1 180 ? 31.298  -13.323 -10.343 1.00 24.80  ?  180 LEU A N    1 
ATOM   1321 C  CA   . LEU A 1 180 ? 30.544  -13.212 -9.104  1.00 26.11  ?  180 LEU A CA   1 
ATOM   1322 C  C    . LEU A 1 180 ? 30.870  -14.365 -8.168  1.00 25.94  ?  180 LEU A C    1 
ATOM   1323 O  O    . LEU A 1 180 ? 31.043  -14.168 -6.961  1.00 25.53  ?  180 LEU A O    1 
ATOM   1324 C  CB   . LEU A 1 180 ? 29.052  -13.196 -9.420  1.00 21.78  ?  180 LEU A CB   1 
ATOM   1325 C  CG   . LEU A 1 180 ? 28.552  -12.052 -10.302 1.00 23.31  ?  180 LEU A CG   1 
ATOM   1326 C  CD1  . LEU A 1 180 ? 27.035  -12.146 -10.438 1.00 21.72  ?  180 LEU A CD1  1 
ATOM   1327 C  CD2  . LEU A 1 180 ? 28.964  -10.685 -9.759  1.00 28.20  ?  180 LEU A CD2  1 
ATOM   1328 N  N    . TYR A 1 181 ? 30.952  -15.578 -8.710  1.00 24.77  ?  181 TYR A N    1 
ATOM   1329 C  CA   . TYR A 1 181 ? 31.228  -16.757 -7.895  1.00 26.59  ?  181 TYR A CA   1 
ATOM   1330 C  C    . TYR A 1 181 ? 32.665  -16.782 -7.397  1.00 27.93  ?  181 TYR A C    1 
ATOM   1331 O  O    . TYR A 1 181 ? 32.943  -17.348 -6.335  1.00 29.34  ?  181 TYR A O    1 
ATOM   1332 C  CB   . TYR A 1 181 ? 30.861  -18.024 -8.675  1.00 25.66  ?  181 TYR A CB   1 
ATOM   1333 C  CG   . TYR A 1 181 ? 29.368  -18.154 -8.823  1.00 24.87  ?  181 TYR A CG   1 
ATOM   1334 C  CD1  . TYR A 1 181 ? 28.692  -17.540 -9.869  1.00 23.17  ?  181 TYR A CD1  1 
ATOM   1335 C  CD2  . TYR A 1 181 ? 28.632  -18.857 -7.889  1.00 25.20  ?  181 TYR A CD2  1 
ATOM   1336 C  CE1  . TYR A 1 181 ? 27.319  -17.638 -9.982  1.00 22.96  ?  181 TYR A CE1  1 
ATOM   1337 C  CE2  . TYR A 1 181 ? 27.253  -18.959 -7.987  1.00 24.07  ?  181 TYR A CE2  1 
ATOM   1338 C  CZ   . TYR A 1 181 ? 26.605  -18.351 -9.036  1.00 24.03  ?  181 TYR A CZ   1 
ATOM   1339 O  OH   . TYR A 1 181 ? 25.242  -18.465 -9.134  1.00 22.77  ?  181 TYR A OH   1 
ATOM   1340 N  N    . GLU A 1 182 ? 33.588  -16.158 -8.117  1.00 28.80  ?  182 GLU A N    1 
ATOM   1341 C  CA   . GLU A 1 182 ? 34.944  -16.111 -7.595  1.00 30.11  ?  182 GLU A CA   1 
ATOM   1342 C  C    . GLU A 1 182 ? 35.094  -15.105 -6.460  1.00 29.93  ?  182 GLU A C    1 
ATOM   1343 O  O    . GLU A 1 182 ? 35.962  -15.285 -5.599  1.00 33.33  ?  182 GLU A O    1 
ATOM   1344 C  CB   . GLU A 1 182 ? 35.942  -15.885 -8.732  1.00 34.16  ?  182 GLU A CB   1 
ATOM   1345 C  CG   . GLU A 1 182 ? 36.102  -17.131 -9.631  1.00 43.89  ?  182 GLU A CG   1 
ATOM   1346 C  CD   . GLU A 1 182 ? 35.947  -18.459 -8.856  1.00 47.61  ?  182 GLU A CD   1 
ATOM   1347 O  OE1  . GLU A 1 182 ? 36.962  -18.966 -8.318  1.00 50.61  ?  182 GLU A OE1  1 
ATOM   1348 O  OE2  . GLU A 1 182 ? 34.809  -18.993 -8.777  1.00 46.42  -1 182 GLU A OE2  1 
ATOM   1349 N  N    . ARG A 1 183 ? 34.234  -14.088 -6.408  1.00 27.37  ?  183 ARG A N    1 
ATOM   1350 C  CA   . ARG A 1 183 ? 34.330  -13.028 -5.414  1.00 27.99  ?  183 ARG A CA   1 
ATOM   1351 C  C    . ARG A 1 183 ? 33.452  -13.250 -4.184  1.00 27.25  ?  183 ARG A C    1 
ATOM   1352 O  O    . ARG A 1 183 ? 33.611  -12.522 -3.203  1.00 30.16  ?  183 ARG A O    1 
ATOM   1353 C  CB   . ARG A 1 183 ? 33.988  -11.671 -6.049  1.00 29.83  ?  183 ARG A CB   1 
ATOM   1354 C  CG   . ARG A 1 183 ? 35.030  -11.171 -7.046  1.00 34.81  ?  183 ARG A CG   1 
ATOM   1355 C  CD   . ARG A 1 183 ? 36.345  -10.836 -6.333  1.00 41.29  ?  183 ARG A CD   1 
ATOM   1356 N  NE   . ARG A 1 183 ? 37.358  -10.282 -7.224  1.00 51.05  ?  183 ARG A NE   1 
ATOM   1357 C  CZ   . ARG A 1 183 ? 38.440  -10.935 -7.626  1.00 49.27  ?  183 ARG A CZ   1 
ATOM   1358 N  NH1  . ARG A 1 183 ? 38.676  -12.180 -7.241  1.00 53.58  ?  183 ARG A NH1  1 
ATOM   1359 N  NH2  . ARG A 1 183 ? 39.309  -10.325 -8.431  1.00 52.96  ?  183 ARG A NH2  1 
ATOM   1360 N  N    . GLU A 1 184 ? 32.550  -14.229 -4.195  1.00 24.41  ?  184 GLU A N    1 
ATOM   1361 C  CA   . GLU A 1 184 ? 31.657  -14.403 -3.053  1.00 24.81  ?  184 GLU A CA   1 
ATOM   1362 C  C    . GLU A 1 184 ? 32.426  -14.848 -1.807  1.00 24.32  ?  184 GLU A C    1 
ATOM   1363 O  O    . GLU A 1 184 ? 33.468  -15.513 -1.887  1.00 28.35  ?  184 GLU A O    1 
ATOM   1364 C  CB   . GLU A 1 184 ? 30.561  -15.416 -3.387  1.00 23.55  ?  184 GLU A CB   1 
ATOM   1365 C  CG   . GLU A 1 184 ? 31.098  -16.824 -3.572  1.00 24.93  ?  184 GLU A CG   1 
ATOM   1366 C  CD   . GLU A 1 184 ? 30.011  -17.859 -3.825  1.00 28.25  ?  184 GLU A CD   1 
ATOM   1367 O  OE1  . GLU A 1 184 ? 28.822  -17.481 -3.922  1.00 28.74  ?  184 GLU A OE1  1 
ATOM   1368 O  OE2  . GLU A 1 184 ? 30.368  -19.055 -3.933  1.00 31.60  -1 184 GLU A OE2  1 
ATOM   1369 N  N    . ARG A 1 185 ? 31.898  -14.466 -0.637  1.00 24.96  ?  185 ARG A N    1 
ATOM   1370 C  CA   . ARG A 1 185 ? 32.524  -14.706 0.659   1.00 24.28  ?  185 ARG A CA   1 
ATOM   1371 C  C    . ARG A 1 185 ? 31.444  -15.107 1.652   1.00 26.46  ?  185 ARG A C    1 
ATOM   1372 O  O    . ARG A 1 185 ? 30.360  -14.504 1.665   1.00 24.68  ?  185 ARG A O    1 
ATOM   1373 C  CB   . ARG A 1 185 ? 33.194  -13.431 1.196   1.00 30.57  ?  185 ARG A CB   1 
ATOM   1374 C  CG   . ARG A 1 185 ? 34.316  -12.860 0.343   1.00 36.09  ?  185 ARG A CG   1 
ATOM   1375 C  CD   . ARG A 1 185 ? 35.521  -13.768 0.334   1.00 40.48  ?  185 ARG A CD   1 
ATOM   1376 N  NE   . ARG A 1 185 ? 35.614  -14.440 -0.952  1.00 48.24  ?  185 ARG A NE   1 
ATOM   1377 C  CZ   . ARG A 1 185 ? 36.692  -15.052 -1.415  1.00 44.60  ?  185 ARG A CZ   1 
ATOM   1378 N  NH1  . ARG A 1 185 ? 37.805  -15.128 -0.701  1.00 52.89  ?  185 ARG A NH1  1 
ATOM   1379 N  NH2  . ARG A 1 185 ? 36.651  -15.605 -2.624  1.00 49.28  ?  185 ARG A NH2  1 
ATOM   1380 N  N    . PRO A 1 186 ? 31.715  -16.076 2.516   1.00 25.86  ?  186 PRO A N    1 
ATOM   1381 C  CA   . PRO A 1 186 ? 30.726  -16.459 3.524   1.00 25.96  ?  186 PRO A CA   1 
ATOM   1382 C  C    . PRO A 1 186 ? 30.731  -15.504 4.705   1.00 27.67  ?  186 PRO A C    1 
ATOM   1383 O  O    . PRO A 1 186 ? 31.751  -14.896 5.046   1.00 29.93  ?  186 PRO A O    1 
ATOM   1384 C  CB   . PRO A 1 186 ? 31.204  -17.848 3.965   1.00 27.18  ?  186 PRO A CB   1 
ATOM   1385 C  CG   . PRO A 1 186 ? 32.688  -17.769 3.829   1.00 28.51  ?  186 PRO A CG   1 
ATOM   1386 C  CD   . PRO A 1 186 ? 32.941  -16.893 2.604   1.00 26.82  ?  186 PRO A CD   1 
ATOM   1387 N  N    . VAL A 1 187 ? 29.561  -15.386 5.328   1.00 26.75  ?  187 VAL A N    1 
ATOM   1388 C  CA   . VAL A 1 187 ? 29.372  -14.606 6.547   1.00 26.56  ?  187 VAL A CA   1 
ATOM   1389 C  C    . VAL A 1 187 ? 29.281  -15.591 7.709   1.00 28.31  ?  187 VAL A C    1 
ATOM   1390 O  O    . VAL A 1 187 ? 28.300  -16.329 7.830   1.00 31.84  ?  187 VAL A O    1 
ATOM   1391 C  CB   . VAL A 1 187 ? 28.106  -13.740 6.457   1.00 28.52  ?  187 VAL A CB   1 
ATOM   1392 C  CG1  . VAL A 1 187 ? 27.887  -12.964 7.758   1.00 33.12  ?  187 VAL A CG1  1 
ATOM   1393 C  CG2  . VAL A 1 187 ? 28.192  -12.788 5.259   1.00 32.19  ?  187 VAL A CG2  1 
ATOM   1394 N  N    . VAL A 1 188 ? 30.291  -15.627 8.577   1.00 29.50  ?  188 VAL A N    1 
ATOM   1395 C  CA   . VAL A 1 188 ? 30.178  -16.420 9.800   1.00 29.76  ?  188 VAL A CA   1 
ATOM   1396 C  C    . VAL A 1 188 ? 29.810  -15.498 10.951  1.00 32.63  ?  188 VAL A C    1 
ATOM   1397 O  O    . VAL A 1 188 ? 30.185  -14.320 10.974  1.00 32.76  ?  188 VAL A O    1 
ATOM   1398 C  CB   . VAL A 1 188 ? 31.434  -17.260 10.099  1.00 34.71  ?  188 VAL A CB   1 
ATOM   1399 C  CG1  . VAL A 1 188 ? 31.678  -18.246 8.962   1.00 35.96  ?  188 VAL A CG1  1 
ATOM   1400 C  CG2  . VAL A 1 188 ? 32.629  -16.360 10.290  1.00 35.34  ?  188 VAL A CG2  1 
ATOM   1401 N  N    . VAL A 1 189 ? 29.049  -16.024 11.906  1.00 29.49  ?  189 VAL A N    1 
ATOM   1402 C  CA   . VAL A 1 189 ? 28.391  -15.170 12.891  1.00 34.54  ?  189 VAL A CA   1 
ATOM   1403 C  C    . VAL A 1 189 ? 28.021  -16.009 14.100  1.00 31.97  ?  189 VAL A C    1 
ATOM   1404 O  O    . VAL A 1 189 ? 27.629  -17.171 13.970  1.00 32.79  ?  189 VAL A O    1 
ATOM   1405 C  CB   . VAL A 1 189 ? 27.129  -14.509 12.293  1.00 31.98  ?  189 VAL A CB   1 
ATOM   1406 C  CG1  . VAL A 1 189 ? 27.468  -13.690 11.057  1.00 41.18  ?  189 VAL A CG1  1 
ATOM   1407 C  CG2  . VAL A 1 189 ? 26.104  -15.572 11.961  1.00 38.12  ?  189 VAL A CG2  1 
ATOM   1408 N  N    . SER A 1 190 ? 28.105  -15.396 15.277  1.00 34.06  ?  190 SER A N    1 
ATOM   1409 C  CA   . SER A 1 190 ? 27.625  -16.028 16.493  1.00 33.46  ?  190 SER A CA   1 
ATOM   1410 C  C    . SER A 1 190 ? 26.107  -15.903 16.595  1.00 29.49  ?  190 SER A C    1 
ATOM   1411 O  O    . SER A 1 190 ? 25.485  -15.021 15.999  1.00 29.20  ?  190 SER A O    1 
ATOM   1412 C  CB   . SER A 1 190 ? 28.265  -15.381 17.724  1.00 43.75  ?  190 SER A CB   1 
ATOM   1413 O  OG   . SER A 1 190 ? 29.668  -15.601 17.765  1.00 54.66  ?  190 SER A OG   1 
ATOM   1414 N  N    . LYS A 1 191 ? 25.510  -16.803 17.370  1.00 29.84  ?  191 LYS A N    1 
ATOM   1415 C  CA   . LYS A 1 191 ? 24.077  -16.711 17.606  1.00 31.26  ?  191 LYS A CA   1 
ATOM   1416 C  C    . LYS A 1 191 ? 23.749  -15.363 18.233  1.00 27.93  ?  191 LYS A C    1 
ATOM   1417 O  O    . LYS A 1 191 ? 24.524  -14.822 19.028  1.00 30.41  ?  191 LYS A O    1 
ATOM   1418 C  CB   . LYS A 1 191 ? 23.596  -17.856 18.496  1.00 35.04  ?  191 LYS A CB   1 
ATOM   1419 C  CG   . LYS A 1 191 ? 24.076  -17.791 19.928  1.00 37.17  ?  191 LYS A CG   1 
ATOM   1420 C  CD   . LYS A 1 191 ? 23.373  -18.848 20.772  1.00 43.15  ?  191 LYS A CD   1 
ATOM   1421 C  CE   . LYS A 1 191 ? 24.029  -18.983 22.135  1.00 49.27  ?  191 LYS A CE   1 
ATOM   1422 N  NZ   . LYS A 1 191 ? 23.399  -20.052 22.957  1.00 55.36  ?  191 LYS A NZ   1 
ATOM   1423 N  N    . GLY A 1 192 ? 22.603  -14.810 17.847  1.00 26.29  ?  192 GLY A N    1 
ATOM   1424 C  CA   . GLY A 1 192 ? 22.230  -13.476 18.246  1.00 26.80  ?  192 GLY A CA   1 
ATOM   1425 C  C    . GLY A 1 192 ? 22.753  -12.368 17.357  1.00 26.42  ?  192 GLY A C    1 
ATOM   1426 O  O    . GLY A 1 192 ? 22.395  -11.210 17.578  1.00 27.50  ?  192 GLY A O    1 
ATOM   1427 N  N    . SER A 1 193 ? 23.591  -12.675 16.367  1.00 24.83  ?  193 SER A N    1 
ATOM   1428 C  CA   . SER A 1 193 ? 24.017  -11.678 15.392  1.00 22.84  ?  193 SER A CA   1 
ATOM   1429 C  C    . SER A 1 193 ? 22.934  -11.450 14.337  1.00 22.14  ?  193 SER A C    1 
ATOM   1430 O  O    . SER A 1 193 ? 22.154  -12.351 14.003  1.00 23.42  ?  193 SER A O    1 
ATOM   1431 C  CB   . SER A 1 193 ? 25.283  -12.139 14.672  1.00 26.24  ?  193 SER A CB   1 
ATOM   1432 O  OG   . SER A 1 193 ? 26.363  -12.298 15.578  1.00 31.27  ?  193 SER A OG   1 
ATOM   1433 N  N    . LEU A 1 194 ? 22.902  -10.233 13.796  1.00 21.67  ?  194 LEU A N    1 
ATOM   1434 C  CA   . LEU A 1 194 ? 21.957  -9.849  12.756  1.00 20.89  ?  194 LEU A CA   1 
ATOM   1435 C  C    . LEU A 1 194 ? 22.739  -9.437  11.517  1.00 20.81  ?  194 LEU A C    1 
ATOM   1436 O  O    . LEU A 1 194 ? 23.554  -8.509  11.577  1.00 22.14  ?  194 LEU A O    1 
ATOM   1437 C  CB   . LEU A 1 194 ? 21.091  -8.674  13.220  1.00 22.58  ?  194 LEU A CB   1 
ATOM   1438 C  CG   . LEU A 1 194 ? 20.145  -8.086  12.167  1.00 20.99  ?  194 LEU A CG   1 
ATOM   1439 C  CD1  . LEU A 1 194 ? 19.043  -9.059  11.832  1.00 19.02  ?  194 LEU A CD1  1 
ATOM   1440 C  CD2  . LEU A 1 194 ? 19.553  -6.770  12.661  1.00 24.17  ?  194 LEU A CD2  1 
ATOM   1441 N  N    . LEU A 1 195 ? 22.505  -10.127 10.405  1.00 20.16  ?  195 LEU A N    1 
ATOM   1442 C  CA   . LEU A 1 195 ? 23.030  -9.688  9.116   1.00 20.60  ?  195 LEU A CA   1 
ATOM   1443 C  C    . LEU A 1 195 ? 21.978  -8.803  8.466   1.00 19.52  ?  195 LEU A C    1 
ATOM   1444 O  O    . LEU A 1 195 ? 20.832  -9.228  8.283   1.00 20.79  ?  195 LEU A O    1 
ATOM   1445 C  CB   . LEU A 1 195 ? 23.346  -10.871 8.202   1.00 21.70  ?  195 LEU A CB   1 
ATOM   1446 C  CG   . LEU A 1 195 ? 23.838  -10.468 6.808   1.00 22.48  ?  195 LEU A CG   1 
ATOM   1447 C  CD1  . LEU A 1 195 ? 25.203  -9.799  6.898   1.00 21.84  ?  195 LEU A CD1  1 
ATOM   1448 C  CD2  . LEU A 1 195 ? 23.896  -11.697 5.893   1.00 23.16  ?  195 LEU A CD2  1 
ATOM   1449 N  N    . LEU A 1 196 ? 22.357  -7.578  8.135   1.00 18.65  ?  196 LEU A N    1 
ATOM   1450 C  CA   . LEU A 1 196 ? 21.522  -6.687  7.344   1.00 17.87  ?  196 LEU A CA   1 
ATOM   1451 C  C    . LEU A 1 196 ? 22.129  -6.562  5.956   1.00 19.43  ?  196 LEU A C    1 
ATOM   1452 O  O    . LEU A 1 196 ? 23.357  -6.484  5.816   1.00 18.94  ?  196 LEU A O    1 
ATOM   1453 C  CB   . LEU A 1 196 ? 21.495  -5.306  7.998   1.00 21.14  ?  196 LEU A CB   1 
ATOM   1454 C  CG   . LEU A 1 196 ? 20.676  -5.241  9.300   1.00 20.60  ?  196 LEU A CG   1 
ATOM   1455 C  CD1  . LEU A 1 196 ? 20.925  -3.916  10.007  1.00 26.56  ?  196 LEU A CD1  1 
ATOM   1456 C  CD2  . LEU A 1 196 ? 19.190  -5.440  9.032   1.00 22.26  ?  196 LEU A CD2  1 
ATOM   1457 N  N    . PHE A 1 197 ? 21.278  -6.536  4.934   1.00 18.31  ?  197 PHE A N    1 
ATOM   1458 C  CA   . PHE A 1 197 ? 21.781  -6.339  3.579   1.00 18.30  ?  197 PHE A CA   1 
ATOM   1459 C  C    . PHE A 1 197 ? 20.744  -5.647  2.712   1.00 19.17  ?  197 PHE A C    1 
ATOM   1460 O  O    . PHE A 1 197 ? 19.541  -5.698  2.981   1.00 18.29  ?  197 PHE A O    1 
ATOM   1461 C  CB   . PHE A 1 197 ? 22.328  -7.627  2.937   1.00 18.42  ?  197 PHE A CB   1 
ATOM   1462 C  CG   . PHE A 1 197 ? 21.316  -8.729  2.741   1.00 20.32  ?  197 PHE A CG   1 
ATOM   1463 C  CD1  . PHE A 1 197 ? 20.614  -8.837  1.554   1.00 17.60  ?  197 PHE A CD1  1 
ATOM   1464 C  CD2  . PHE A 1 197 ? 21.155  -9.715  3.703   1.00 20.55  ?  197 PHE A CD2  1 
ATOM   1465 C  CE1  . PHE A 1 197 ? 19.731  -9.894  1.350   1.00 19.15  ?  197 PHE A CE1  1 
ATOM   1466 C  CE2  . PHE A 1 197 ? 20.275  -10.762 3.509   1.00 20.25  ?  197 PHE A CE2  1 
ATOM   1467 C  CZ   . PHE A 1 197 ? 19.578  -10.861 2.334   1.00 19.53  ?  197 PHE A CZ   1 
ATOM   1468 N  N    . VAL A 1 198 ? 21.214  -4.993  1.674   1.00 19.08  ?  198 VAL A N    1 
ATOM   1469 C  CA   . VAL A 1 198 ? 20.306  -4.359  0.726   1.00 20.12  ?  198 VAL A CA   1 
ATOM   1470 C  C    . VAL A 1 198 ? 19.880  -5.375  -0.310  1.00 18.75  ?  198 VAL A C    1 
ATOM   1471 O  O    . VAL A 1 198 ? 20.640  -6.280  -0.687  1.00 19.84  ?  198 VAL A O    1 
ATOM   1472 C  CB   . VAL A 1 198 ? 20.893  -3.083  0.089   1.00 20.24  ?  198 VAL A CB   1 
ATOM   1473 C  CG1  . VAL A 1 198 ? 21.248  -2.106  1.150   1.00 23.43  ?  198 VAL A CG1  1 
ATOM   1474 C  CG2  . VAL A 1 198 ? 22.147  -3.403  -0.727  1.00 19.60  ?  198 VAL A CG2  1 
ATOM   1475 N  N    . GLY A 1 199 ? 18.639  -5.223  -0.792  1.00 16.79  ?  199 GLY A N    1 
ATOM   1476 C  CA   . GLY A 1 199 ? 18.094  -6.205  -1.703  1.00 18.02  ?  199 GLY A CA   1 
ATOM   1477 C  C    . GLY A 1 199 ? 18.873  -6.325  -2.994  1.00 17.73  ?  199 GLY A C    1 
ATOM   1478 O  O    . GLY A 1 199 ? 18.906  -7.392  -3.609  1.00 19.27  ?  199 GLY A O    1 
ATOM   1479 N  N    . ASP A 1 200 ? 19.533  -5.249  -3.407  1.00 18.40  ?  200 ASP A N    1 
ATOM   1480 C  CA   . ASP A 1 200 ? 20.285  -5.290  -4.649  1.00 18.07  ?  200 ASP A CA   1 
ATOM   1481 C  C    . ASP A 1 200 ? 21.685  -5.880  -4.485  1.00 17.26  ?  200 ASP A C    1 
ATOM   1482 O  O    . ASP A 1 200 ? 22.430  -5.930  -5.466  1.00 18.46  ?  200 ASP A O    1 
ATOM   1483 C  CB   . ASP A 1 200 ? 20.354  -3.889  -5.269  1.00 18.49  ?  200 ASP A CB   1 
ATOM   1484 C  CG   . ASP A 1 200 ? 20.977  -2.883  -4.337  1.00 19.45  ?  200 ASP A CG   1 
ATOM   1485 O  OD1  . ASP A 1 200 ? 20.269  -2.394  -3.432  1.00 20.59  ?  200 ASP A OD1  1 
ATOM   1486 O  OD2  . ASP A 1 200 ? 22.188  -2.634  -4.481  1.00 20.86  -1 200 ASP A OD2  1 
ATOM   1487 N  N    . ILE A 1 201 ? 22.062  -6.331  -3.288  1.00 18.81  ?  201 ILE A N    1 
ATOM   1488 C  CA   . ILE A 1 201 ? 23.309  -7.080  -3.140  1.00 16.19  ?  201 ILE A CA   1 
ATOM   1489 C  C    . ILE A 1 201 ? 23.188  -8.449  -3.801  1.00 18.25  ?  201 ILE A C    1 
ATOM   1490 O  O    . ILE A 1 201 ? 22.134  -9.103  -3.755  1.00 18.60  ?  201 ILE A O    1 
ATOM   1491 C  CB   . ILE A 1 201 ? 23.728  -7.214  -1.663  1.00 16.78  ?  201 ILE A CB   1 
ATOM   1492 C  CG1  . ILE A 1 201 ? 25.258  -7.355  -1.581  1.00 19.83  ?  201 ILE A CG1  1 
ATOM   1493 C  CG2  . ILE A 1 201 ? 23.061  -8.424  -0.997  1.00 19.68  ?  201 ILE A CG2  1 
ATOM   1494 C  CD1  . ILE A 1 201 ? 25.782  -7.641  -0.158  1.00 22.58  ?  201 ILE A CD1  1 
ATOM   1495 N  N    . VAL A 1 202 ? 24.285  -8.893  -4.401  1.00 17.15  ?  202 VAL A N    1 
ATOM   1496 C  CA   . VAL A 1 202 ? 24.397  -10.242 -4.937  1.00 17.08  ?  202 VAL A CA   1 
ATOM   1497 C  C    . VAL A 1 202 ? 24.807  -11.147 -3.788  1.00 18.81  ?  202 VAL A C    1 
ATOM   1498 O  O    . VAL A 1 202 ? 25.790  -10.875 -3.089  1.00 19.58  ?  202 VAL A O    1 
ATOM   1499 C  CB   . VAL A 1 202 ? 25.439  -10.276 -6.067  1.00 19.57  ?  202 VAL A CB   1 
ATOM   1500 C  CG1  . VAL A 1 202 ? 25.635  -11.702 -6.569  1.00 22.49  ?  202 VAL A CG1  1 
ATOM   1501 C  CG2  . VAL A 1 202 ? 25.025  -9.351  -7.203  1.00 21.03  ?  202 VAL A CG2  1 
ATOM   1502 N  N    . HIS A 1 203 ? 24.043  -12.215 -3.573  1.00 18.72  ?  203 HIS A N    1 
ATOM   1503 C  CA   . HIS A 1 203 ? 24.225  -13.044 -2.387  1.00 17.98  ?  203 HIS A CA   1 
ATOM   1504 C  C    . HIS A 1 203 ? 23.533  -14.377 -2.637  1.00 19.51  ?  203 HIS A C    1 
ATOM   1505 O  O    . HIS A 1 203 ? 22.803  -14.546 -3.619  1.00 19.81  ?  203 HIS A O    1 
ATOM   1506 C  CB   . HIS A 1 203 ? 23.590  -12.372 -1.161  1.00 17.15  ?  203 HIS A CB   1 
ATOM   1507 C  CG   . HIS A 1 203 ? 22.096  -12.312 -1.248  1.00 17.96  ?  203 HIS A CG   1 
ATOM   1508 N  ND1  . HIS A 1 203 ? 21.432  -11.366 -2.003  1.00 17.23  ?  203 HIS A ND1  1 
ATOM   1509 C  CD2  . HIS A 1 203 ? 21.141  -13.118 -0.727  1.00 20.69  ?  203 HIS A CD2  1 
ATOM   1510 C  CE1  . HIS A 1 203 ? 20.130  -11.582 -1.925  1.00 18.88  ?  203 HIS A CE1  1 
ATOM   1511 N  NE2  . HIS A 1 203 ? 19.931  -12.647 -1.170  1.00 19.84  ?  203 HIS A NE2  1 
ATOM   1512 N  N    . ARG A 1 204 ? 23.718  -15.306 -1.701  1.00 19.28  ?  204 ARG A N    1 
ATOM   1513 C  CA   . ARG A 1 204 ? 23.008  -16.578 -1.777  1.00 19.43  ?  204 ARG A CA   1 
ATOM   1514 C  C    . ARG A 1 204 ? 23.053  -17.262 -0.423  1.00 21.42  ?  204 ARG A C    1 
ATOM   1515 O  O    . ARG A 1 204 ? 23.930  -16.998 0.397   1.00 21.72  ?  204 ARG A O    1 
ATOM   1516 C  CB   . ARG A 1 204 ? 23.628  -17.511 -2.823  1.00 21.50  ?  204 ARG A CB   1 
ATOM   1517 C  CG   . ARG A 1 204 ? 25.039  -17.982 -2.470  1.00 20.93  ?  204 ARG A CG   1 
ATOM   1518 C  CD   . ARG A 1 204 ? 25.578  -18.928 -3.543  1.00 22.62  ?  204 ARG A CD   1 
ATOM   1519 N  NE   . ARG A 1 204 ? 26.936  -19.383 -3.261  1.00 24.04  ?  204 ARG A NE   1 
ATOM   1520 C  CZ   . ARG A 1 204 ? 27.218  -20.479 -2.571  1.00 25.90  ?  204 ARG A CZ   1 
ATOM   1521 N  NH1  . ARG A 1 204 ? 26.260  -21.246 -2.077  1.00 26.30  ?  204 ARG A NH1  1 
ATOM   1522 N  NH2  . ARG A 1 204 ? 28.489  -20.812 -2.372  1.00 29.07  ?  204 ARG A NH2  1 
ATOM   1523 N  N    . GLY A 1 205 ? 22.087  -18.159 -0.204  1.00 21.53  ?  205 GLY A N    1 
ATOM   1524 C  CA   . GLY A 1 205 ? 22.262  -19.187 0.800   1.00 22.22  ?  205 GLY A CA   1 
ATOM   1525 C  C    . GLY A 1 205 ? 23.172  -20.295 0.299   1.00 25.76  ?  205 GLY A C    1 
ATOM   1526 O  O    . GLY A 1 205 ? 23.499  -20.405 -0.886  1.00 25.01  ?  205 GLY A O    1 
ATOM   1527 N  N    . SER A 1 206 ? 23.613  -21.137 1.228   1.00 22.62  ?  206 SER A N    1 
ATOM   1528 C  CA   . SER A 1 206 ? 24.561  -22.187 0.897   1.00 25.38  ?  206 SER A CA   1 
ATOM   1529 C  C    . SER A 1 206 ? 24.143  -23.513 1.518   1.00 24.29  ?  206 SER A C    1 
ATOM   1530 O  O    . SER A 1 206 ? 23.276  -23.575 2.392   1.00 26.13  ?  206 SER A O    1 
ATOM   1531 C  CB   . SER A 1 206 ? 25.998  -21.824 1.303   1.00 25.40  ?  206 SER A CB   1 
ATOM   1532 O  OG   . SER A 1 206 ? 26.160  -21.828 2.719   1.00 26.06  ?  206 SER A OG   1 
ATOM   1533 N  N    . ALA A 1 207 ? 24.786  -24.578 1.040   1.00 27.86  ?  207 ALA A N    1 
ATOM   1534 C  CA   . ALA A 1 207 ? 24.526  -25.912 1.559   1.00 28.25  ?  207 ALA A CA   1 
ATOM   1535 C  C    . ALA A 1 207 ? 25.057  -26.031 2.982   1.00 25.39  ?  207 ALA A C    1 
ATOM   1536 O  O    . ALA A 1 207 ? 26.106  -25.481 3.322   1.00 27.45  ?  207 ALA A O    1 
ATOM   1537 C  CB   . ALA A 1 207 ? 25.201  -26.955 0.666   1.00 33.10  ?  207 ALA A CB   1 
ATOM   1538 N  N    . TYR A 1 208 ? 24.322  -26.751 3.820   1.00 26.57  ?  208 TYR A N    1 
ATOM   1539 C  CA   . TYR A 1 208 ? 24.790  -27.089 5.162   1.00 25.23  ?  208 TYR A CA   1 
ATOM   1540 C  C    . TYR A 1 208 ? 25.721  -28.291 5.040   1.00 26.99  ?  208 TYR A C    1 
ATOM   1541 O  O    . TYR A 1 208 ? 25.277  -29.402 4.724   1.00 27.64  ?  208 TYR A O    1 
ATOM   1542 C  CB   . TYR A 1 208 ? 23.573  -27.430 6.011   1.00 22.71  ?  208 TYR A CB   1 
ATOM   1543 C  CG   . TYR A 1 208 ? 23.807  -27.521 7.497   1.00 23.43  ?  208 TYR A CG   1 
ATOM   1544 C  CD1  . TYR A 1 208 ? 24.493  -28.594 8.049   1.00 25.46  ?  208 TYR A CD1  1 
ATOM   1545 C  CD2  . TYR A 1 208 ? 23.295  -26.547 8.358   1.00 24.39  ?  208 TYR A CD2  1 
ATOM   1546 C  CE1  . TYR A 1 208 ? 24.687  -28.691 9.423   1.00 28.94  ?  208 TYR A CE1  1 
ATOM   1547 C  CE2  . TYR A 1 208 ? 23.492  -26.636 9.728   1.00 25.76  ?  208 TYR A CE2  1 
ATOM   1548 C  CZ   . TYR A 1 208 ? 24.175  -27.706 10.255  1.00 28.06  ?  208 TYR A CZ   1 
ATOM   1549 O  OH   . TYR A 1 208 ? 24.366  -27.800 11.624  1.00 31.99  ?  208 TYR A OH   1 
ATOM   1550 N  N    . HIS A 1 209 ? 27.028  -28.083 5.271   1.00 25.20  ?  209 HIS A N    1 
ATOM   1551 C  CA   . HIS A 1 209 ? 27.986  -29.162 5.052   1.00 26.37  ?  209 HIS A CA   1 
ATOM   1552 C  C    . HIS A 1 209 ? 27.911  -30.216 6.147   1.00 27.40  ?  209 HIS A C    1 
ATOM   1553 O  O    . HIS A 1 209 ? 28.149  -31.404 5.894   1.00 29.46  ?  209 HIS A O    1 
ATOM   1554 C  CB   . HIS A 1 209 ? 29.415  -28.621 5.036   1.00 26.38  ?  209 HIS A CB   1 
ATOM   1555 C  CG   . HIS A 1 209 ? 29.762  -27.820 3.824   1.00 26.02  ?  209 HIS A CG   1 
ATOM   1556 N  ND1  . HIS A 1 209 ? 31.051  -27.403 3.567   1.00 28.86  ?  209 HIS A ND1  1 
ATOM   1557 C  CD2  . HIS A 1 209 ? 28.997  -27.344 2.814   1.00 29.28  ?  209 HIS A CD2  1 
ATOM   1558 C  CE1  . HIS A 1 209 ? 31.063  -26.704 2.445   1.00 29.09  ?  209 HIS A CE1  1 
ATOM   1559 N  NE2  . HIS A 1 209 ? 29.834  -26.662 1.965   1.00 29.03  ?  209 HIS A NE2  1 
ATOM   1560 N  N    . GLY A 1 210 ? 27.643  -29.792 7.377   1.00 27.35  ?  210 GLY A N    1 
ATOM   1561 C  CA   . GLY A 1 210 ? 27.654  -30.711 8.494   1.00 28.75  ?  210 GLY A CA   1 
ATOM   1562 C  C    . GLY A 1 210 ? 26.572  -31.765 8.385   1.00 29.19  ?  210 GLY A C    1 
ATOM   1563 O  O    . GLY A 1 210 ? 25.537  -31.587 7.740   1.00 28.87  ?  210 GLY A O    1 
ATOM   1564 N  N    . HIS A 1 211 ? 26.821  -32.870 9.074   1.00 32.22  ?  211 HIS A N    1 
ATOM   1565 C  CA   . HIS A 1 211 ? 25.953  -34.037 9.007   1.00 33.41  ?  211 HIS A CA   1 
ATOM   1566 C  C    . HIS A 1 211 ? 24.745  -33.879 9.923   1.00 31.39  ?  211 HIS A C    1 
ATOM   1567 O  O    . HIS A 1 211 ? 23.604  -34.106 9.504   1.00 34.93  ?  211 HIS A O    1 
ATOM   1568 C  CB   . HIS A 1 211 ? 26.772  -35.265 9.395   1.00 33.73  ?  211 HIS A CB   1 
ATOM   1569 C  CG   . HIS A 1 211 ? 26.086  -36.568 9.135   1.00 36.91  ?  211 HIS A CG   1 
ATOM   1570 N  ND1  . HIS A 1 211 ? 25.549  -36.898 7.908   1.00 39.45  ?  211 HIS A ND1  1 
ATOM   1571 C  CD2  . HIS A 1 211 ? 25.867  -37.632 9.941   1.00 36.84  ?  211 HIS A CD2  1 
ATOM   1572 C  CE1  . HIS A 1 211 ? 25.035  -38.115 7.971   1.00 38.75  ?  211 HIS A CE1  1 
ATOM   1573 N  NE2  . HIS A 1 211 ? 25.206  -38.577 9.196   1.00 42.12  ?  211 HIS A NE2  1 
ATOM   1574 N  N    . LEU A 1 212 ? 24.974  -33.450 11.157  1.00 32.69  ?  212 LEU A N    1 
ATOM   1575 C  CA   . LEU A 1 212 ? 23.920  -33.302 12.154  1.00 31.51  ?  212 LEU A CA   1 
ATOM   1576 C  C    . LEU A 1 212 ? 23.628  -31.828 12.414  1.00 32.51  ?  212 LEU A C    1 
ATOM   1577 O  O    . LEU A 1 212 ? 24.375  -30.931 12.016  1.00 36.44  ?  212 LEU A O    1 
ATOM   1578 C  CB   . LEU A 1 212 ? 24.322  -34.000 13.459  1.00 34.18  ?  212 LEU A CB   1 
ATOM   1579 C  CG   . LEU A 1 212 ? 24.601  -35.502 13.358  1.00 35.18  ?  212 LEU A CG   1 
ATOM   1580 C  CD1  . LEU A 1 212 ? 24.998  -36.084 14.705  1.00 37.87  ?  212 LEU A CD1  1 
ATOM   1581 C  CD2  . LEU A 1 212 ? 23.403  -36.241 12.771  1.00 40.48  ?  212 LEU A CD2  1 
ATOM   1582 N  N    . GLY A 1 213 ? 22.515  -31.584 13.094  1.00 32.54  ?  213 GLY A N    1 
ATOM   1583 C  CA   . GLY A 1 213 ? 22.164  -30.234 13.480  1.00 31.11  ?  213 GLY A CA   1 
ATOM   1584 C  C    . GLY A 1 213 ? 21.410  -29.479 12.408  1.00 32.14  ?  213 GLY A C    1 
ATOM   1585 O  O    . GLY A 1 213 ? 21.146  -29.958 11.302  1.00 31.91  ?  213 GLY A O    1 
ATOM   1586 N  N    . ARG A 1 214 ? 21.059  -28.247 12.753  1.00 28.98  ?  214 ARG A N    1 
ATOM   1587 C  CA   . ARG A 1 214 ? 20.374  -27.384 11.808  1.00 26.46  ?  214 ARG A CA   1 
ATOM   1588 C  C    . ARG A 1 214 ? 20.710  -25.937 12.137  1.00 27.16  ?  214 ARG A C    1 
ATOM   1589 O  O    . ARG A 1 214 ? 21.024  -25.608 13.282  1.00 30.83  ?  214 ARG A O    1 
ATOM   1590 C  CB   . ARG A 1 214 ? 18.851  -27.620 11.790  1.00 27.73  ?  214 ARG A CB   1 
ATOM   1591 C  CG   . ARG A 1 214 ? 18.083  -27.059 12.984  1.00 31.73  ?  214 ARG A CG   1 
ATOM   1592 C  CD   . ARG A 1 214 ? 18.173  -27.970 14.178  1.00 34.39  ?  214 ARG A CD   1 
ATOM   1593 N  NE   . ARG A 1 214 ? 17.318  -27.513 15.274  1.00 33.95  ?  214 ARG A NE   1 
ATOM   1594 C  CZ   . ARG A 1 214 ? 17.777  -26.916 16.365  1.00 39.54  ?  214 ARG A CZ   1 
ATOM   1595 N  NH1  . ARG A 1 214 ? 19.070  -26.658 16.519  1.00 41.08  ?  214 ARG A NH1  1 
ATOM   1596 N  NH2  . ARG A 1 214 ? 16.924  -26.587 17.333  1.00 34.35  ?  214 ARG A NH2  1 
ATOM   1597 N  N    . ARG A 1 215 ? 20.691  -25.089 11.113  1.00 23.67  ?  215 ARG A N    1 
ATOM   1598 C  CA   . ARG A 1 215 ? 20.799  -23.648 11.309  1.00 23.60  ?  215 ARG A CA   1 
ATOM   1599 C  C    . ARG A 1 215 ? 19.406  -23.091 11.574  1.00 26.14  ?  215 ARG A C    1 
ATOM   1600 O  O    . ARG A 1 215 ? 18.457  -23.431 10.862  1.00 25.47  ?  215 ARG A O    1 
ATOM   1601 C  CB   . ARG A 1 215 ? 21.390  -22.971 10.068  1.00 23.50  ?  215 ARG A CB   1 
ATOM   1602 C  CG   . ARG A 1 215 ? 21.713  -21.502 10.295  1.00 23.85  ?  215 ARG A CG   1 
ATOM   1603 C  CD   . ARG A 1 215 ? 22.087  -20.764 9.014   1.00 22.60  ?  215 ARG A CD   1 
ATOM   1604 N  NE   . ARG A 1 215 ? 20.921  -20.474 8.198   1.00 23.29  ?  215 ARG A NE   1 
ATOM   1605 C  CZ   . ARG A 1 215 ? 20.925  -19.672 7.145   1.00 23.46  ?  215 ARG A CZ   1 
ATOM   1606 N  NH1  . ARG A 1 215 ? 22.034  -19.074 6.736   1.00 22.02  ?  215 ARG A NH1  1 
ATOM   1607 N  NH2  . ARG A 1 215 ? 19.786  -19.463 6.487   1.00 26.51  ?  215 ARG A NH2  1 
ATOM   1608 N  N    . LEU A 1 216 ? 19.287  -22.234 12.587  1.00 21.65  ?  216 LEU A N    1 
ATOM   1609 C  CA   . LEU A 1 216 ? 18.025  -21.573 12.924  1.00 21.17  ?  216 LEU A CA   1 
ATOM   1610 C  C    . LEU A 1 216 ? 18.136  -20.082 12.650  1.00 20.43  ?  216 LEU A C    1 
ATOM   1611 O  O    . LEU A 1 216 ? 19.107  -19.443 13.072  1.00 21.72  ?  216 LEU A O    1 
ATOM   1612 C  CB   . LEU A 1 216 ? 17.715  -21.766 14.409  1.00 23.87  ?  216 LEU A CB   1 
ATOM   1613 C  CG   . LEU A 1 216 ? 17.566  -23.184 14.932  1.00 29.30  ?  216 LEU A CG   1 
ATOM   1614 C  CD1  . LEU A 1 216 ? 17.398  -23.162 16.447  1.00 29.72  ?  216 LEU A CD1  1 
ATOM   1615 C  CD2  . LEU A 1 216 ? 16.388  -23.863 14.261  1.00 28.96  ?  216 LEU A CD2  1 
ATOM   1616 N  N    . ALA A 1 217 ? 17.130  -19.516 11.982  1.00 18.08  ?  217 ALA A N    1 
ATOM   1617 C  CA   . ALA A 1 217 ? 17.201  -18.097 11.685  1.00 18.30  ?  217 ALA A CA   1 
ATOM   1618 C  C    . ALA A 1 217 ? 15.816  -17.500 11.549  1.00 18.03  ?  217 ALA A C    1 
ATOM   1619 O  O    . ALA A 1 217 ? 14.874  -18.155 11.099  1.00 19.44  ?  217 ALA A O    1 
ATOM   1620 C  CB   . ALA A 1 217 ? 17.986  -17.805 10.405  1.00 18.59  ?  217 ALA A CB   1 
ATOM   1621 N  N    . LEU A 1 218 ? 15.734  -16.228 11.903  1.00 18.10  ?  218 LEU A N    1 
ATOM   1622 C  CA   . LEU A 1 218 ? 14.560  -15.399 11.672  1.00 18.04  ?  218 LEU A CA   1 
ATOM   1623 C  C    . LEU A 1 218 ? 14.894  -14.415 10.551  1.00 18.61  ?  218 LEU A C    1 
ATOM   1624 O  O    . LEU A 1 218 ? 15.944  -13.754 10.581  1.00 19.23  ?  218 LEU A O    1 
ATOM   1625 C  CB   . LEU A 1 218 ? 14.203  -14.656 12.962  1.00 20.43  ?  218 LEU A CB   1 
ATOM   1626 C  CG   . LEU A 1 218 ? 13.203  -13.511 12.818  1.00 20.92  ?  218 LEU A CG   1 
ATOM   1627 C  CD1  . LEU A 1 218 ? 11.872  -14.071 12.372  1.00 24.25  ?  218 LEU A CD1  1 
ATOM   1628 C  CD2  . LEU A 1 218 ? 13.065  -12.769 14.144  1.00 28.78  ?  218 LEU A CD2  1 
ATOM   1629 N  N    . PHE A 1 219 ? 14.029  -14.350 9.545   1.00 16.29  ?  219 PHE A N    1 
ATOM   1630 C  CA   . PHE A 1 219 ? 14.257  -13.537 8.365   1.00 16.44  ?  219 PHE A CA   1 
ATOM   1631 C  C    . PHE A 1 219 ? 13.203  -12.449 8.314   1.00 16.81  ?  219 PHE A C    1 
ATOM   1632 O  O    . PHE A 1 219 ? 12.069  -12.672 8.733   1.00 17.41  ?  219 PHE A O    1 
ATOM   1633 C  CB   . PHE A 1 219 ? 14.072  -14.378 7.105   1.00 16.76  ?  219 PHE A CB   1 
ATOM   1634 C  CG   . PHE A 1 219 ? 15.066  -15.482 6.953   1.00 18.80  ?  219 PHE A CG   1 
ATOM   1635 C  CD1  . PHE A 1 219 ? 14.972  -16.623 7.732   1.00 20.30  ?  219 PHE A CD1  1 
ATOM   1636 C  CD2  . PHE A 1 219 ? 16.061  -15.396 5.991   1.00 21.78  ?  219 PHE A CD2  1 
ATOM   1637 C  CE1  . PHE A 1 219 ? 15.875  -17.664 7.578   1.00 24.38  ?  219 PHE A CE1  1 
ATOM   1638 C  CE2  . PHE A 1 219 ? 16.970  -16.435 5.828   1.00 25.39  ?  219 PHE A CE2  1 
ATOM   1639 C  CZ   . PHE A 1 219 ? 16.871  -17.569 6.623   1.00 24.91  ?  219 PHE A CZ   1 
ATOM   1640 N  N    . PHE A 1 220 ? 13.563  -11.289 7.767   1.00 16.96  ?  220 PHE A N    1 
ATOM   1641 C  CA   . PHE A 1 220 ? 12.569  -10.252 7.496   1.00 17.05  ?  220 PHE A CA   1 
ATOM   1642 C  C    . PHE A 1 220 ? 13.114  -9.320  6.427   1.00 17.69  ?  220 PHE A C    1 
ATOM   1643 O  O    . PHE A 1 220 ? 14.318  -9.291  6.157   1.00 17.37  ?  220 PHE A O    1 
ATOM   1644 C  CB   . PHE A 1 220 ? 12.196  -9.477  8.774   1.00 17.21  ?  220 PHE A CB   1 
ATOM   1645 C  CG   . PHE A 1 220 ? 13.348  -8.784  9.414   1.00 18.58  ?  220 PHE A CG   1 
ATOM   1646 C  CD1  . PHE A 1 220 ? 13.709  -7.500  9.030   1.00 20.45  ?  220 PHE A CD1  1 
ATOM   1647 C  CD2  . PHE A 1 220 ? 14.076  -9.417  10.412  1.00 19.97  ?  220 PHE A CD2  1 
ATOM   1648 C  CE1  . PHE A 1 220 ? 14.794  -6.853  9.622   1.00 23.13  ?  220 PHE A CE1  1 
ATOM   1649 C  CE2  . PHE A 1 220 ? 15.147  -8.773  11.018  1.00 22.98  ?  220 PHE A CE2  1 
ATOM   1650 C  CZ   . PHE A 1 220 ? 15.505  -7.489  10.620  1.00 22.52  ?  220 PHE A CZ   1 
ATOM   1651 N  N    . ASN A 1 221 ? 12.215  -8.567  5.804   1.00 17.40  ?  221 ASN A N    1 
ATOM   1652 C  CA   . ASN A 1 221 ? 12.644  -7.516  4.898   1.00 16.52  ?  221 ASN A CA   1 
ATOM   1653 C  C    . ASN A 1 221 ? 11.635  -6.384  4.932   1.00 16.32  ?  221 ASN A C    1 
ATOM   1654 O  O    . ASN A 1 221 ? 10.462  -6.587  5.279   1.00 16.72  ?  221 ASN A O    1 
ATOM   1655 C  CB   . ASN A 1 221 ? 13.070  -7.967  3.477   1.00 17.20  ?  221 ASN A CB   1 
ATOM   1656 C  CG   . ASN A 1 221 ? 12.072  -8.877  2.789   1.00 20.59  ?  221 ASN A CG   1 
ATOM   1657 O  OD1  . ASN A 1 221 ? 11.870  -10.041 3.183   1.00 22.54  ?  221 ASN A OD1  1 
ATOM   1658 N  ND2  . ASN A 1 221 ? 11.493  -8.387  1.707   1.00 18.38  ?  221 ASN A ND2  1 
ATOM   1659 N  N    . ILE A 1 222 ? 12.129  -5.189  4.618   1.00 16.50  ?  222 ILE A N    1 
ATOM   1660 C  CA   . ILE A 1 222 ? 11.401  -3.942  4.781   1.00 15.52  ?  222 ILE A CA   1 
ATOM   1661 C  C    . ILE A 1 222 ? 11.581  -3.132  3.510   1.00 17.70  ?  222 ILE A C    1 
ATOM   1662 O  O    . ILE A 1 222 ? 12.653  -3.155  2.885   1.00 17.88  ?  222 ILE A O    1 
ATOM   1663 C  CB   . ILE A 1 222 ? 11.941  -3.161  6.010   1.00 17.77  ?  222 ILE A CB   1 
ATOM   1664 C  CG1  . ILE A 1 222 ? 11.691  -3.969  7.292   1.00 21.06  ?  222 ILE A CG1  1 
ATOM   1665 C  CG2  . ILE A 1 222 ? 11.339  -1.725  6.106   1.00 18.71  ?  222 ILE A CG2  1 
ATOM   1666 C  CD1  . ILE A 1 222 ? 12.371  -3.398  8.531   1.00 21.80  ?  222 ILE A CD1  1 
ATOM   1667 N  N    . HIS A 1 223 ? 10.540  -2.386  3.141   1.00 16.83  ?  223 HIS A N    1 
ATOM   1668 C  CA   . HIS A 1 223 ? 10.583  -1.517  1.970   1.00 17.34  ?  223 HIS A CA   1 
ATOM   1669 C  C    . HIS A 1 223 ? 9.912   -0.190  2.313   1.00 17.58  ?  223 HIS A C    1 
ATOM   1670 O  O    . HIS A 1 223 ? 9.271   -0.047  3.363   1.00 18.02  ?  223 HIS A O    1 
ATOM   1671 C  CB   . HIS A 1 223 ? 9.947   -2.189  0.736   1.00 17.38  ?  223 HIS A CB   1 
ATOM   1672 C  CG   . HIS A 1 223 ? 8.453   -2.335  0.816   1.00 17.78  ?  223 HIS A CG   1 
ATOM   1673 N  ND1  . HIS A 1 223 ? 7.851   -3.422  1.409   1.00 17.83  ?  223 HIS A ND1  1 
ATOM   1674 C  CD2  . HIS A 1 223 ? 7.443   -1.541  0.372   1.00 17.35  ?  223 HIS A CD2  1 
ATOM   1675 C  CE1  . HIS A 1 223 ? 6.536   -3.292  1.335   1.00 18.54  ?  223 HIS A CE1  1 
ATOM   1676 N  NE2  . HIS A 1 223 ? 6.261   -2.152  0.723   1.00 19.17  ?  223 HIS A NE2  1 
ATOM   1677 N  N    . GLY A 1 224 ? 10.086  0.786   1.426   1.00 17.34  ?  224 GLY A N    1 
ATOM   1678 C  CA   . GLY A 1 224 ? 9.406   2.073   1.542   1.00 17.59  ?  224 GLY A CA   1 
ATOM   1679 C  C    . GLY A 1 224 ? 8.070   2.044   0.815   1.00 17.72  ?  224 GLY A C    1 
ATOM   1680 O  O    . GLY A 1 224 ? 7.951   1.496   -0.281  1.00 18.71  ?  224 GLY A O    1 
ATOM   1681 N  N    . ALA A 1 225 ? 7.050   2.626   1.463   1.00 18.90  ?  225 ALA A N    1 
ATOM   1682 C  CA   . ALA A 1 225 ? 5.700   2.623   0.909   1.00 19.89  ?  225 ALA A CA   1 
ATOM   1683 C  C    . ALA A 1 225 ? 5.617   3.340   -0.433  1.00 20.87  ?  225 ALA A C    1 
ATOM   1684 O  O    . ALA A 1 225 ? 4.701   3.066   -1.223  1.00 21.99  ?  225 ALA A O    1 
ATOM   1685 C  CB   . ALA A 1 225 ? 4.743   3.257   1.931   1.00 19.53  ?  225 ALA A CB   1 
ATOM   1686 N  N    . GLN A 1 226 ? 6.570   4.225   -0.724  1.00 20.36  ?  226 GLN A N    1 
ATOM   1687 C  CA   . GLN A 1 226 ? 6.606   4.858   -2.036  1.00 23.28  ?  226 GLN A CA   1 
ATOM   1688 C  C    . GLN A 1 226 ? 6.707   3.831   -3.160  1.00 21.05  ?  226 GLN A C    1 
ATOM   1689 O  O    . GLN A 1 226 ? 6.241   4.092   -4.276  1.00 23.46  ?  226 GLN A O    1 
ATOM   1690 C  CB   . GLN A 1 226 ? 7.774   5.841   -2.104  1.00 25.08  ?  226 GLN A CB   1 
ATOM   1691 C  CG   . GLN A 1 226 ? 7.700   6.993   -1.116  1.00 27.75  ?  226 GLN A CG   1 
ATOM   1692 C  CD   . GLN A 1 226 ? 8.277   6.680   0.273   1.00 30.33  ?  226 GLN A CD   1 
ATOM   1693 O  OE1  . GLN A 1 226 ? 8.545   5.525   0.614   1.00 28.29  ?  226 GLN A OE1  1 
ATOM   1694 N  NE2  . GLN A 1 226 ? 8.483   7.734   1.078   1.00 30.12  ?  226 GLN A NE2  1 
ATOM   1695 N  N    . ALA A 1 227 ? 7.344   2.681   -2.908  1.00 19.72  ?  227 ALA A N    1 
ATOM   1696 C  CA   . ALA A 1 227 ? 7.410   1.597   -3.895  1.00 17.94  ?  227 ALA A CA   1 
ATOM   1697 C  C    . ALA A 1 227 ? 6.093   0.824   -3.860  1.00 19.29  ?  227 ALA A C    1 
ATOM   1698 O  O    . ALA A 1 227 ? 6.011   -0.325  -3.422  1.00 19.70  ?  227 ALA A O    1 
ATOM   1699 C  CB   . ALA A 1 227 ? 8.594   0.679   -3.616  1.00 19.40  ?  227 ALA A CB   1 
ATOM   1700 N  N    . ARG A 1 228 ? 5.044   1.493   -4.344  1.00 19.48  ?  228 ARG A N    1 
ATOM   1701 C  CA   . ARG A 1 228 ? 3.661   1.121   -4.046  1.00 18.60  ?  228 ARG A CA   1 
ATOM   1702 C  C    . ARG A 1 228 ? 3.222   -0.170  -4.719  1.00 20.84  ?  228 ARG A C    1 
ATOM   1703 O  O    . ARG A 1 228 ? 2.166   -0.716  -4.361  1.00 20.69  ?  228 ARG A O    1 
ATOM   1704 C  CB   . ARG A 1 228 ? 2.726   2.248   -4.476  1.00 21.72  ?  228 ARG A CB   1 
ATOM   1705 C  CG   . ARG A 1 228 ? 2.748   2.496   -5.982  1.00 18.52  ?  228 ARG A CG   1 
ATOM   1706 C  CD   . ARG A 1 228 ? 1.557   3.308   -6.415  1.00 22.11  ?  228 ARG A CD   1 
ATOM   1707 N  NE   . ARG A 1 228 ? 1.566   4.647   -5.841  1.00 21.50  ?  228 ARG A NE   1 
ATOM   1708 C  CZ   . ARG A 1 228 ? 0.531   5.469   -5.889  1.00 22.54  ?  228 ARG A CZ   1 
ATOM   1709 N  NH1  . ARG A 1 228 ? -0.614  5.105   -6.443  1.00 24.19  ?  228 ARG A NH1  1 
ATOM   1710 N  NH2  . ARG A 1 228 ? 0.639   6.684   -5.354  1.00 26.71  ?  228 ARG A NH2  1 
ATOM   1711 N  N    . TRP A 1 229 ? 3.978   -0.659  -5.691  1.00 17.60  ?  229 TRP A N    1 
ATOM   1712 C  CA   . TRP A 1 229 ? 3.644   -1.928  -6.310  1.00 17.62  ?  229 TRP A CA   1 
ATOM   1713 C  C    . TRP A 1 229 ? 4.116   -3.106  -5.471  1.00 18.12  ?  229 TRP A C    1 
ATOM   1714 O  O    . TRP A 1 229 ? 3.814   -4.253  -5.811  1.00 20.23  ?  229 TRP A O    1 
ATOM   1715 C  CB   . TRP A 1 229 ? 4.251   -1.984  -7.722  1.00 18.34  ?  229 TRP A CB   1 
ATOM   1716 C  CG   . TRP A 1 229 ? 5.758   -2.060  -7.697  1.00 17.55  ?  229 TRP A CG   1 
ATOM   1717 C  CD1  . TRP A 1 229 ? 6.514   -3.194  -7.718  1.00 19.69  ?  229 TRP A CD1  1 
ATOM   1718 C  CD2  . TRP A 1 229 ? 6.677   -0.966  -7.571  1.00 18.02  ?  229 TRP A CD2  1 
ATOM   1719 N  NE1  . TRP A 1 229 ? 7.854   -2.877  -7.629  1.00 18.93  ?  229 TRP A NE1  1 
ATOM   1720 C  CE2  . TRP A 1 229 ? 7.978   -1.516  -7.537  1.00 18.83  ?  229 TRP A CE2  1 
ATOM   1721 C  CE3  . TRP A 1 229 ? 6.526   0.418   -7.496  1.00 20.01  ?  229 TRP A CE3  1 
ATOM   1722 C  CZ2  . TRP A 1 229 ? 9.124   -0.724  -7.434  1.00 18.12  ?  229 TRP A CZ2  1 
ATOM   1723 C  CZ3  . TRP A 1 229 ? 7.667   1.206   -7.395  1.00 19.49  ?  229 TRP A CZ3  1 
ATOM   1724 C  CH2  . TRP A 1 229 ? 8.944   0.635   -7.365  1.00 18.92  ?  229 TRP A CH2  1 
ATOM   1725 N  N    . THR A 1 230 ? 4.884   -2.844  -4.416  1.00 17.08  ?  230 THR A N    1 
ATOM   1726 C  CA   . THR A 1 230 ? 5.371   -3.892  -3.526  1.00 17.83  ?  230 THR A CA   1 
ATOM   1727 C  C    . THR A 1 230 ? 4.306   -4.207  -2.487  1.00 20.93  ?  230 THR A C    1 
ATOM   1728 O  O    . THR A 1 230 ? 3.651   -3.307  -1.963  1.00 23.45  ?  230 THR A O    1 
ATOM   1729 C  CB   . THR A 1 230 ? 6.624   -3.389  -2.810  1.00 18.79  ?  230 THR A CB   1 
ATOM   1730 O  OG1  . THR A 1 230 ? 7.522   -2.853  -3.786  1.00 20.68  ?  230 THR A OG1  1 
ATOM   1731 C  CG2  . THR A 1 230 ? 7.328   -4.507  -2.061  1.00 18.36  ?  230 THR A CG2  1 
ATOM   1732 N  N    . ASP A 1 231 ? 4.182   -5.482  -2.164  1.00 23.23  ?  231 ASP A N    1 
ATOM   1733 C  CA   . ASP A 1 231 ? 3.236   -5.962  -1.168  1.00 22.69  ?  231 ASP A CA   1 
ATOM   1734 C  C    . ASP A 1 231 ? 3.864   -5.941  0.220   1.00 24.00  ?  231 ASP A C    1 
ATOM   1735 O  O    . ASP A 1 231 ? 5.027   -6.299  0.394   1.00 24.64  ?  231 ASP A O    1 
ATOM   1736 C  CB   . ASP A 1 231 ? 2.858   -7.401  -1.520  1.00 26.27  ?  231 ASP A CB   1 
ATOM   1737 C  CG   . ASP A 1 231 ? 2.343   -7.534  -2.943  1.00 30.28  ?  231 ASP A CG   1 
ATOM   1738 O  OD1  . ASP A 1 231 ? 1.200   -7.084  -3.196  1.00 32.65  ?  231 ASP A OD1  1 
ATOM   1739 O  OD2  . ASP A 1 231 ? 3.100   -8.052  -3.807  1.00 33.89  -1 231 ASP A OD2  1 
ATOM   1740 N  N    . LYS A 1 232 ? 3.094   -5.519  1.209   1.00 21.68  ?  232 LYS A N    1 
ATOM   1741 C  CA   . LYS A 1 232 ? 3.534   -5.784  2.566   1.00 24.27  ?  232 LYS A CA   1 
ATOM   1742 C  C    . LYS A 1 232 ? 3.208   -7.235  2.917   1.00 22.25  ?  232 LYS A C    1 
ATOM   1743 O  O    . LYS A 1 232 ? 2.533   -7.944  2.166   1.00 23.40  ?  232 LYS A O    1 
ATOM   1744 C  CB   . LYS A 1 232 ? 2.937   -4.778  3.543   1.00 32.87  ?  232 LYS A CB   1 
ATOM   1745 C  CG   . LYS A 1 232 ? 1.458   -4.839  3.654   1.00 31.59  ?  232 LYS A CG   1 
ATOM   1746 C  CD   . LYS A 1 232 ? 0.927   -3.643  4.460   1.00 31.18  ?  232 LYS A CD   1 
ATOM   1747 C  CE   . LYS A 1 232 ? -0.576  -3.742  4.561   1.00 29.27  ?  232 LYS A CE   1 
ATOM   1748 N  NZ   . LYS A 1 232 ? -0.962  -5.007  5.246   1.00 35.17  ?  232 LYS A NZ   1 
ATOM   1749 N  N    . HIS A 1 233 ? 3.730   -7.698  4.048   1.00 18.77  ?  233 HIS A N    1 
ATOM   1750 C  CA   . HIS A 1 233 ? 3.595   -9.111  4.382   1.00 18.35  ?  233 HIS A CA   1 
ATOM   1751 C  C    . HIS A 1 233 ? 2.119   -9.484  4.541   1.00 21.04  ?  233 HIS A C    1 
ATOM   1752 O  O    . HIS A 1 233 ? 1.364   -8.795  5.236   1.00 21.54  ?  233 HIS A O    1 
ATOM   1753 C  CB   . HIS A 1 233 ? 4.353   -9.393  5.680   1.00 17.88  ?  233 HIS A CB   1 
ATOM   1754 C  CG   . HIS A 1 233 ? 4.313   -10.830 6.096   1.00 19.91  ?  233 HIS A CG   1 
ATOM   1755 N  ND1  . HIS A 1 233 ? 4.824   -11.845 5.318   1.00 21.58  ?  233 HIS A ND1  1 
ATOM   1756 C  CD2  . HIS A 1 233 ? 3.798   -11.427 7.200   1.00 19.49  ?  233 HIS A CD2  1 
ATOM   1757 C  CE1  . HIS A 1 233 ? 4.640   -13.004 5.927   1.00 22.88  ?  233 HIS A CE1  1 
ATOM   1758 N  NE2  . HIS A 1 233 ? 4.009   -12.779 7.069   1.00 18.55  ?  233 HIS A NE2  1 
ATOM   1759 N  N    . LEU A 1 234 ? 1.716   -10.584 3.899   1.00 18.00  ?  234 LEU A N    1 
ATOM   1760 C  CA   . LEU A 1 234 ? 0.331   -11.047 3.925   1.00 20.92  ?  234 LEU A CA   1 
ATOM   1761 C  C    . LEU A 1 234 ? 0.170   -12.174 4.937   1.00 21.22  ?  234 LEU A C    1 
ATOM   1762 O  O    . LEU A 1 234 ? 0.910   -13.168 4.900   1.00 22.49  ?  234 LEU A O    1 
ATOM   1763 C  CB   . LEU A 1 234 ? -0.066  -11.551 2.537   1.00 23.36  ?  234 LEU A CB   1 
ATOM   1764 C  CG   . LEU A 1 234 ? -1.431  -12.218 2.371   1.00 28.60  ?  234 LEU A CG   1 
ATOM   1765 C  CD1  . LEU A 1 234 ? -2.518  -11.244 2.755   1.00 28.57  ?  234 LEU A CD1  1 
ATOM   1766 C  CD2  . LEU A 1 234 ? -1.619  -12.685 0.927   1.00 30.32  ?  234 LEU A CD2  1 
ATOM   1767 N  N    . TRP A 1 235 ? -0.823  -12.033 5.819   1.00 19.40  ?  235 TRP A N    1 
ATOM   1768 C  CA   . TRP A 1 235 ? -1.231  -13.111 6.706   1.00 19.74  ?  235 TRP A CA   1 
ATOM   1769 C  C    . TRP A 1 235 ? -2.718  -12.982 7.000   1.00 19.63  ?  235 TRP A C    1 
ATOM   1770 O  O    . TRP A 1 235 ? -3.312  -11.924 6.804   1.00 20.25  ?  235 TRP A O    1 
ATOM   1771 C  CB   . TRP A 1 235 ? -0.421  -13.128 8.011   1.00 22.55  ?  235 TRP A CB   1 
ATOM   1772 C  CG   . TRP A 1 235 ? -0.769  -12.057 9.017   1.00 20.75  ?  235 TRP A CG   1 
ATOM   1773 C  CD1  . TRP A 1 235 ? -1.659  -12.163 10.059  1.00 19.50  ?  235 TRP A CD1  1 
ATOM   1774 C  CD2  . TRP A 1 235 ? -0.218  -10.740 9.093   1.00 20.91  ?  235 TRP A CD2  1 
ATOM   1775 N  NE1  . TRP A 1 235 ? -1.676  -10.994 10.768  1.00 22.60  ?  235 TRP A NE1  1 
ATOM   1776 C  CE2  . TRP A 1 235 ? -0.798  -10.107 10.203  1.00 22.69  ?  235 TRP A CE2  1 
ATOM   1777 C  CE3  . TRP A 1 235 ? 0.740   -10.043 8.342   1.00 21.31  ?  235 TRP A CE3  1 
ATOM   1778 C  CZ2  . TRP A 1 235 ? -0.490  -8.795  10.564  1.00 22.60  ?  235 TRP A CZ2  1 
ATOM   1779 C  CZ3  . TRP A 1 235 ? 1.052   -8.743  8.704   1.00 20.71  ?  235 TRP A CZ3  1 
ATOM   1780 C  CH2  . TRP A 1 235 ? 0.431   -8.130  9.808   1.00 22.85  ?  235 TRP A CH2  1 
ATOM   1781 N  N    . SER A 1 236 ? -3.303  -14.076 7.468   1.00 18.86  ?  236 SER A N    1 
ATOM   1782 C  CA   . SER A 1 236 ? -4.722  -14.140 7.799   1.00 19.67  ?  236 SER A CA   1 
ATOM   1783 C  C    . SER A 1 236 ? -4.874  -14.427 9.284   1.00 24.12  ?  236 SER A C    1 
ATOM   1784 O  O    . SER A 1 236 ? -4.312  -15.404 9.792   1.00 24.49  ?  236 SER A O    1 
ATOM   1785 C  CB   . SER A 1 236 ? -5.402  -15.240 6.989   1.00 25.59  ?  236 SER A CB   1 
ATOM   1786 O  OG   . SER A 1 236 ? -5.408  -14.905 5.614   1.00 36.33  ?  236 SER A OG   1 
ATOM   1787 N  N    . LEU A 1 237 ? -5.637  -13.582 9.977   1.00 21.40  ?  237 LEU A N    1 
ATOM   1788 C  CA   . LEU A 1 237 ? -5.888  -13.793 11.395  1.00 21.47  ?  237 LEU A CA   1 
ATOM   1789 C  C    . LEU A 1 237 ? -7.161  -13.046 11.765  1.00 23.29  ?  237 LEU A C    1 
ATOM   1790 O  O    . LEU A 1 237 ? -7.474  -12.006 11.180  1.00 23.57  ?  237 LEU A O    1 
ATOM   1791 C  CB   . LEU A 1 237 ? -4.704  -13.285 12.227  1.00 23.83  ?  237 LEU A CB   1 
ATOM   1792 C  CG   . LEU A 1 237 ? -4.497  -13.903 13.612  1.00 27.99  ?  237 LEU A CG   1 
ATOM   1793 C  CD1  . LEU A 1 237 ? -4.328  -15.410 13.503  1.00 32.67  ?  237 LEU A CD1  1 
ATOM   1794 C  CD2  . LEU A 1 237 ? -3.278  -13.270 14.284  1.00 26.91  ?  237 LEU A CD2  1 
ATOM   1795 N  N    . ARG A 1 238 ? -7.895  -13.596 12.724  1.00 21.49  ?  238 ARG A N    1 
ATOM   1796 C  CA   . ARG A 1 238 ? -9.114  -13.011 13.263  1.00 21.52  ?  238 ARG A CA   1 
ATOM   1797 C  C    . ARG A 1 238 ? -9.094  -13.226 14.767  1.00 21.80  ?  238 ARG A C    1 
ATOM   1798 O  O    . ARG A 1 238 ? -8.419  -14.136 15.257  1.00 22.60  ?  238 ARG A O    1 
ATOM   1799 C  CB   . ARG A 1 238 ? -10.375 -13.664 12.679  1.00 24.20  ?  238 ARG A CB   1 
ATOM   1800 C  CG   . ARG A 1 238 ? -10.488 -13.560 11.168  1.00 31.09  ?  238 ARG A CG   1 
ATOM   1801 C  CD   . ARG A 1 238 ? -11.699 -14.327 10.668  1.00 33.71  ?  238 ARG A CD   1 
ATOM   1802 N  NE   . ARG A 1 238 ? -11.728 -15.718 11.110  1.00 38.26  ?  238 ARG A NE   1 
ATOM   1803 C  CZ   . ARG A 1 238 ? -12.692 -16.583 10.806  1.00 38.14  ?  238 ARG A CZ   1 
ATOM   1804 N  NH1  . ARG A 1 238 ? -13.730 -16.234 10.063  1.00 34.67  ?  238 ARG A NH1  1 
ATOM   1805 N  NH2  . ARG A 1 238 ? -12.608 -17.834 11.255  1.00 42.66  ?  238 ARG A NH2  1 
ATOM   1806 N  N    . PRO A 1 239 ? -9.834  -12.416 15.527  1.00 22.33  ?  239 PRO A N    1 
ATOM   1807 C  CA   . PRO A 1 239 ? -9.831  -12.597 16.989  1.00 22.75  ?  239 PRO A CA   1 
ATOM   1808 C  C    . PRO A 1 239 ? -10.215 -13.992 17.463  1.00 24.47  ?  239 PRO A C    1 
ATOM   1809 O  O    . PRO A 1 239 ? -9.753  -14.410 18.530  1.00 26.70  ?  239 PRO A O    1 
ATOM   1810 C  CB   . PRO A 1 239 ? -10.792 -11.506 17.482  1.00 24.95  ?  239 PRO A CB   1 
ATOM   1811 C  CG   . PRO A 1 239 ? -10.668 -10.433 16.439  1.00 24.57  ?  239 PRO A CG   1 
ATOM   1812 C  CD   . PRO A 1 239 ? -10.542 -11.184 15.134  1.00 25.38  ?  239 PRO A CD   1 
ATOM   1813 N  N    . ALA A 1 240 ? -11.033 -14.737 16.712  1.00 22.90  ?  240 ALA A N    1 
ATOM   1814 C  CA   . ALA A 1 240 ? -11.364 -16.108 17.095  1.00 25.84  ?  240 ALA A CA   1 
ATOM   1815 C  C    . ALA A 1 240 ? -10.172 -17.063 17.036  1.00 26.72  ?  240 ALA A C    1 
ATOM   1816 O  O    . ALA A 1 240 ? -10.223 -18.130 17.658  1.00 29.00  ?  240 ALA A O    1 
ATOM   1817 C  CB   . ALA A 1 240 ? -12.470 -16.646 16.189  1.00 28.85  ?  240 ALA A CB   1 
ATOM   1818 N  N    . HIS A 1 241 ? -9.119  -16.719 16.315  1.00 25.25  ?  241 HIS A N    1 
ATOM   1819 C  CA   . HIS A 1 241 ? -8.059  -17.685 16.053  1.00 27.14  ?  241 HIS A CA   1 
ATOM   1820 C  C    . HIS A 1 241 ? -7.218  -17.909 17.308  1.00 28.76  ?  241 HIS A C    1 
ATOM   1821 O  O    . HIS A 1 241 ? -6.949  -16.963 18.053  1.00 26.29  ?  241 HIS A O    1 
ATOM   1822 C  CB   . HIS A 1 241 ? -7.157  -17.158 14.941  1.00 29.84  ?  241 HIS A CB   1 
ATOM   1823 C  CG   . HIS A 1 241 ? -6.206  -18.176 14.396  1.00 36.67  ?  241 HIS A CG   1 
ATOM   1824 N  ND1  . HIS A 1 241 ? -5.016  -18.493 15.016  1.00 33.92  ?  241 HIS A ND1  1 
ATOM   1825 C  CD2  . HIS A 1 241 ? -6.263  -18.939 13.278  1.00 39.96  ?  241 HIS A CD2  1 
ATOM   1826 C  CE1  . HIS A 1 241 ? -4.383  -19.411 14.306  1.00 39.49  ?  241 HIS A CE1  1 
ATOM   1827 N  NE2  . HIS A 1 241 ? -5.119  -19.699 13.247  1.00 42.40  ?  241 HIS A NE2  1 
ATOM   1828 N  N    . PRO A 1 242 ? -6.746  -19.137 17.542  1.00 32.91  ?  242 PRO A N    1 
ATOM   1829 C  CA   . PRO A 1 242 ? -5.915  -19.385 18.736  1.00 33.85  ?  242 PRO A CA   1 
ATOM   1830 C  C    . PRO A 1 242 ? -4.660  -18.532 18.811  1.00 28.15  ?  242 PRO A C    1 
ATOM   1831 O  O    . PRO A 1 242 ? -4.197  -18.251 19.923  1.00 32.76  ?  242 PRO A O    1 
ATOM   1832 C  CB   . PRO A 1 242 ? -5.596  -20.888 18.657  1.00 36.66  ?  242 PRO A CB   1 
ATOM   1833 C  CG   . PRO A 1 242 ? -5.875  -21.273 17.227  1.00 40.64  ?  242 PRO A CG   1 
ATOM   1834 C  CD   . PRO A 1 242 ? -6.997  -20.365 16.774  1.00 36.24  ?  242 PRO A CD   1 
ATOM   1835 N  N    . ASP A 1 243 ? -4.103  -18.100 17.677  1.00 28.45  ?  243 ASP A N    1 
ATOM   1836 C  CA   . ASP A 1 243 ? -2.909  -17.256 17.660  1.00 27.58  ?  243 ASP A CA   1 
ATOM   1837 C  C    . ASP A 1 243 ? -3.214  -15.771 17.840  1.00 25.92  ?  243 ASP A C    1 
ATOM   1838 O  O    . ASP A 1 243 ? -2.282  -14.962 17.856  1.00 26.13  ?  243 ASP A O    1 
ATOM   1839 C  CB   . ASP A 1 243 ? -2.139  -17.440 16.348  1.00 32.70  ?  243 ASP A CB   1 
ATOM   1840 C  CG   . ASP A 1 243 ? -1.565  -18.836 16.185  1.00 37.75  ?  243 ASP A CG   1 
ATOM   1841 O  OD1  . ASP A 1 243 ? -1.609  -19.626 17.147  1.00 38.06  ?  243 ASP A OD1  1 
ATOM   1842 O  OD2  . ASP A 1 243 ? -1.067  -19.134 15.078  1.00 41.92  -1 243 ASP A OD2  1 
ATOM   1843 N  N    . TRP A 1 244 ? -4.485  -15.386 17.971  1.00 24.00  ?  244 TRP A N    1 
ATOM   1844 C  CA   . TRP A 1 244 ? -4.805  -13.965 18.052  1.00 24.62  ?  244 TRP A CA   1 
ATOM   1845 C  C    . TRP A 1 244 ? -4.257  -13.339 19.325  1.00 21.68  ?  244 TRP A C    1 
ATOM   1846 O  O    . TRP A 1 244 ? -3.741  -12.217 19.289  1.00 22.83  ?  244 TRP A O    1 
ATOM   1847 C  CB   . TRP A 1 244 ? -6.314  -13.749 17.988  1.00 24.37  ?  244 TRP A CB   1 
ATOM   1848 C  CG   . TRP A 1 244 ? -6.697  -12.311 18.188  1.00 24.64  ?  244 TRP A CG   1 
ATOM   1849 C  CD1  . TRP A 1 244 ? -7.206  -11.746 19.321  1.00 24.31  ?  244 TRP A CD1  1 
ATOM   1850 C  CD2  . TRP A 1 244 ? -6.576  -11.249 17.230  1.00 21.53  ?  244 TRP A CD2  1 
ATOM   1851 N  NE1  . TRP A 1 244 ? -7.430  -10.403 19.122  1.00 25.71  ?  244 TRP A NE1  1 
ATOM   1852 C  CE2  . TRP A 1 244 ? -7.060  -10.073 17.848  1.00 21.99  ?  244 TRP A CE2  1 
ATOM   1853 C  CE3  . TRP A 1 244 ? -6.133  -11.182 15.905  1.00 23.04  ?  244 TRP A CE3  1 
ATOM   1854 C  CZ2  . TRP A 1 244 ? -7.094  -8.837  17.185  1.00 21.75  ?  244 TRP A CZ2  1 
ATOM   1855 C  CZ3  . TRP A 1 244 ? -6.179  -9.952  15.247  1.00 24.23  ?  244 TRP A CZ3  1 
ATOM   1856 C  CH2  . TRP A 1 244 ? -6.661  -8.801  15.893  1.00 22.99  ?  244 TRP A CH2  1 
ATOM   1857 N  N    . GLY A 1 245 ? -4.381  -14.037 20.457  1.00 23.44  ?  245 GLY A N    1 
ATOM   1858 C  CA   . GLY A 1 245 ? -3.915  -13.477 21.719  1.00 25.73  ?  245 GLY A CA   1 
ATOM   1859 C  C    . GLY A 1 245 ? -2.484  -12.981 21.639  1.00 23.25  ?  245 GLY A C    1 
ATOM   1860 O  O    . GLY A 1 245 ? -2.165  -11.879 22.094  1.00 23.39  ?  245 GLY A O    1 
ATOM   1861 N  N    . THR A 1 246 ? -1.599  -13.786 21.048  1.00 23.04  ?  246 THR A N    1 
ATOM   1862 C  CA   . THR A 1 246 ? -0.208  -13.368 20.916  1.00 21.99  ?  246 THR A CA   1 
ATOM   1863 C  C    . THR A 1 246 ? -0.094  -12.105 20.071  1.00 20.59  ?  246 THR A C    1 
ATOM   1864 O  O    . THR A 1 246 ? 0.623   -11.159 20.428  1.00 21.09  ?  246 THR A O    1 
ATOM   1865 C  CB   . THR A 1 246 ? 0.604   -14.497 20.292  1.00 21.39  ?  246 THR A CB   1 
ATOM   1866 O  OG1  . THR A 1 246 ? 0.622   -15.608 21.187  1.00 26.09  ?  246 THR A OG1  1 
ATOM   1867 C  CG2  . THR A 1 246 ? 2.049   -14.039 20.025  1.00 25.06  ?  246 THR A CG2  1 
ATOM   1868 N  N    . PHE A 1 247 ? -0.804  -12.068 18.945  1.00 20.00  ?  247 PHE A N    1 
ATOM   1869 C  CA   . PHE A 1 247 ? -0.749  -10.896 18.078  1.00 19.93  ?  247 PHE A CA   1 
ATOM   1870 C  C    . PHE A 1 247 ? -1.356  -9.673  18.748  1.00 18.96  ?  247 PHE A C    1 
ATOM   1871 O  O    . PHE A 1 247 ? -0.818  -8.558  18.634  1.00 19.94  ?  247 PHE A O    1 
ATOM   1872 C  CB   . PHE A 1 247 ? -1.448  -11.162 16.747  1.00 20.34  ?  247 PHE A CB   1 
ATOM   1873 C  CG   . PHE A 1 247 ? -1.333  -10.012 15.806  1.00 19.41  ?  247 PHE A CG   1 
ATOM   1874 C  CD1  . PHE A 1 247 ? -0.181  -9.837  15.056  1.00 21.41  ?  247 PHE A CD1  1 
ATOM   1875 C  CD2  . PHE A 1 247 ? -2.347  -9.068  15.724  1.00 20.90  ?  247 PHE A CD2  1 
ATOM   1876 C  CE1  . PHE A 1 247 ? -0.052  -8.754  14.217  1.00 21.95  ?  247 PHE A CE1  1 
ATOM   1877 C  CE2  . PHE A 1 247 ? -2.227  -7.969  14.888  1.00 20.95  ?  247 PHE A CE2  1 
ATOM   1878 C  CZ   . PHE A 1 247 ? -1.080  -7.814  14.125  1.00 21.76  ?  247 PHE A CZ   1 
ATOM   1879 N  N    . ARG A 1 248 ? -2.487  -9.861  19.428  1.00 19.32  ?  248 ARG A N    1 
ATOM   1880 C  CA   . ARG A 1 248 ? -3.105  -8.779  20.184  1.00 21.13  ?  248 ARG A CA   1 
ATOM   1881 C  C    . ARG A 1 248 ? -2.122  -8.197  21.185  1.00 21.23  ?  248 ARG A C    1 
ATOM   1882 O  O    . ARG A 1 248 ? -1.957  -6.976  21.269  1.00 21.87  ?  248 ARG A O    1 
ATOM   1883 C  CB   . ARG A 1 248 ? -4.351  -9.324  20.881  1.00 20.87  ?  248 ARG A CB   1 
ATOM   1884 C  CG   . ARG A 1 248 ? -5.076  -8.342  21.795  1.00 22.03  ?  248 ARG A CG   1 
ATOM   1885 C  CD   . ARG A 1 248 ? -5.879  -9.138  22.834  1.00 25.58  ?  248 ARG A CD   1 
ATOM   1886 N  NE   . ARG A 1 248 ? -4.972  -9.896  23.694  1.00 28.37  ?  248 ARG A NE   1 
ATOM   1887 C  CZ   . ARG A 1 248 ? -5.249  -11.073 24.239  1.00 35.71  ?  248 ARG A CZ   1 
ATOM   1888 N  NH1  . ARG A 1 248 ? -6.412  -11.671 24.039  1.00 37.39  ?  248 ARG A NH1  1 
ATOM   1889 N  NH2  . ARG A 1 248 ? -4.327  -11.673 24.994  1.00 33.29  ?  248 ARG A NH2  1 
ATOM   1890 N  N    . ASP A 1 249 ? -1.418  -9.067  21.918  1.00 21.57  ?  249 ASP A N    1 
ATOM   1891 C  CA   . ASP A 1 249 ? -0.433  -8.606  22.895  1.00 23.07  ?  249 ASP A CA   1 
ATOM   1892 C  C    . ASP A 1 249 ? 0.730   -7.893  22.214  1.00 22.39  ?  249 ASP A C    1 
ATOM   1893 O  O    . ASP A 1 249 ? 1.268   -6.913  22.752  1.00 23.26  ?  249 ASP A O    1 
ATOM   1894 C  CB   . ASP A 1 249 ? 0.076   -9.791  23.718  1.00 23.70  ?  249 ASP A CB   1 
ATOM   1895 C  CG   . ASP A 1 249 ? -1.003  -10.380 24.626  1.00 28.26  ?  249 ASP A CG   1 
ATOM   1896 O  OD1  . ASP A 1 249 ? -2.094  -9.773  24.741  1.00 29.21  ?  249 ASP A OD1  1 
ATOM   1897 O  OD2  . ASP A 1 249 ? -0.759  -11.451 25.230  1.00 31.15  -1 249 ASP A OD2  1 
ATOM   1898 N  N    . LEU A 1 250 ? 1.128   -8.367  21.030  1.00 21.15  ?  250 LEU A N    1 
ATOM   1899 C  CA   . LEU A 1 250 ? 2.164   -7.674  20.273  1.00 22.28  ?  250 LEU A CA   1 
ATOM   1900 C  C    . LEU A 1 250 ? 1.735   -6.250  19.957  1.00 21.04  ?  250 LEU A C    1 
ATOM   1901 O  O    . LEU A 1 250 ? 2.494   -5.297  20.174  1.00 22.67  ?  250 LEU A O    1 
ATOM   1902 C  CB   . LEU A 1 250 ? 2.465   -8.429  18.980  1.00 20.47  ?  250 LEU A CB   1 
ATOM   1903 C  CG   . LEU A 1 250 ? 3.527   -7.756  18.099  1.00 21.45  ?  250 LEU A CG   1 
ATOM   1904 C  CD1  . LEU A 1 250 ? 4.940   -7.826  18.729  1.00 23.42  ?  250 LEU A CD1  1 
ATOM   1905 C  CD2  . LEU A 1 250 ? 3.496   -8.370  16.710  1.00 20.96  ?  250 LEU A CD2  1 
ATOM   1906 N  N    . MET A 1 251 ? 0.498   -6.082  19.470  1.00 19.89  ?  251 MET A N    1 
ATOM   1907 C  CA   . MET A 1 251 ? 0.041   -4.754  19.076  1.00 20.02  ?  251 MET A CA   1 
ATOM   1908 C  C    . MET A 1 251 ? 0.011   -3.802  20.261  1.00 23.34  ?  251 MET A C    1 
ATOM   1909 O  O    . MET A 1 251 ? 0.310   -2.610  20.121  1.00 23.30  ?  251 MET A O    1 
ATOM   1910 C  CB   . MET A 1 251 ? -1.349  -4.860  18.451  1.00 20.47  ?  251 MET A CB   1 
ATOM   1911 C  CG   . MET A 1 251 ? -1.322  -5.447  17.047  1.00 21.99  ?  251 MET A CG   1 
ATOM   1912 S  SD   . MET A 1 251 ? -0.431  -4.428  15.830  1.00 24.24  ?  251 MET A SD   1 
ATOM   1913 C  CE   . MET A 1 251 ? -1.660  -3.154  15.532  1.00 27.08  ?  251 MET A CE   1 
ATOM   1914 N  N    . ILE A 1 252 ? -0.368  -4.307  21.437  1.00 21.02  ?  252 ILE A N    1 
ATOM   1915 C  CA   . ILE A 1 252 ? -0.386  -3.480  22.638  1.00 23.03  ?  252 ILE A CA   1 
ATOM   1916 C  C    . ILE A 1 252 ? 1.025   -3.052  23.031  1.00 24.57  ?  252 ILE A C    1 
ATOM   1917 O  O    . ILE A 1 252 ? 1.243   -1.917  23.466  1.00 26.73  ?  252 ILE A O    1 
ATOM   1918 C  CB   . ILE A 1 252 ? -1.130  -4.225  23.766  1.00 22.51  ?  252 ILE A CB   1 
ATOM   1919 C  CG1  . ILE A 1 252 ? -2.592  -4.443  23.364  1.00 24.97  ?  252 ILE A CG1  1 
ATOM   1920 C  CG2  . ILE A 1 252 ? -1.028  -3.467  25.076  1.00 26.71  ?  252 ILE A CG2  1 
ATOM   1921 C  CD1  . ILE A 1 252 ? -3.313  -5.491  24.197  1.00 25.77  ?  252 ILE A CD1  1 
ATOM   1922 N  N    . GLU A 1 253 ? 2.006   -3.944  22.867  1.00 23.45  ?  253 GLU A N    1 
ATOM   1923 C  CA   . GLU A 1 253 ? 3.381   -3.654  23.266  1.00 27.29  ?  253 GLU A CA   1 
ATOM   1924 C  C    . GLU A 1 253 ? 4.070   -2.679  22.311  1.00 25.31  ?  253 GLU A C    1 
ATOM   1925 O  O    . GLU A 1 253 ? 4.889   -1.864  22.753  1.00 29.33  ?  253 GLU A O    1 
ATOM   1926 C  CB   . GLU A 1 253 ? 4.158   -4.970  23.320  1.00 29.85  ?  253 GLU A CB   1 
ATOM   1927 C  CG   . GLU A 1 253 ? 5.650   -4.850  23.208  1.00 37.32  ?  253 GLU A CG   1 
ATOM   1928 C  CD   . GLU A 1 253 ? 6.308   -6.194  22.925  1.00 37.42  ?  253 GLU A CD   1 
ATOM   1929 O  OE1  . GLU A 1 253 ? 5.862   -7.222  23.497  1.00 37.12  ?  253 GLU A OE1  1 
ATOM   1930 O  OE2  . GLU A 1 253 ? 7.252   -6.214  22.112  1.00 38.79  -1 253 GLU A OE2  1 
ATOM   1931 N  N    . LEU A 1 254 ? 3.762   -2.743  21.016  1.00 23.09  ?  254 LEU A N    1 
ATOM   1932 C  CA   . LEU A 1 254 ? 4.478   -1.943  20.028  1.00 24.58  ?  254 LEU A CA   1 
ATOM   1933 C  C    . LEU A 1 254 ? 4.197   -0.455  20.210  1.00 25.84  ?  254 LEU A C    1 
ATOM   1934 O  O    . LEU A 1 254 ? 3.127   -0.051  20.670  1.00 28.14  ?  254 LEU A O    1 
ATOM   1935 C  CB   . LEU A 1 254 ? 4.066   -2.352  18.608  1.00 22.59  ?  254 LEU A CB   1 
ATOM   1936 C  CG   . LEU A 1 254 ? 4.439   -3.761  18.122  1.00 22.06  ?  254 LEU A CG   1 
ATOM   1937 C  CD1  . LEU A 1 254 ? 3.817   -4.028  16.745  1.00 20.58  ?  254 LEU A CD1  1 
ATOM   1938 C  CD2  . LEU A 1 254 ? 5.959   -3.930  18.063  1.00 24.67  ?  254 LEU A CD2  1 
ATOM   1939 N  N    . GLU A 1 255 ? 5.177   0.367   19.827  1.00 23.96  ?  255 GLU A N    1 
ATOM   1940 C  CA   . GLU A 1 255 ? 4.978   1.805   19.777  1.00 26.04  ?  255 GLU A CA   1 
ATOM   1941 C  C    . GLU A 1 255 ? 4.404   2.187   18.419  1.00 24.52  ?  255 GLU A C    1 
ATOM   1942 O  O    . GLU A 1 255 ? 4.476   1.407   17.461  1.00 22.62  ?  255 GLU A O    1 
ATOM   1943 C  CB   . GLU A 1 255 ? 6.320   2.511   19.989  1.00 30.39  ?  255 GLU A CB   1 
ATOM   1944 C  CG   . GLU A 1 255 ? 7.004   2.110   21.294  1.00 38.37  ?  255 GLU A CG   1 
ATOM   1945 C  CD   . GLU A 1 255 ? 8.412   2.674   21.439  1.00 46.40  ?  255 GLU A CD   1 
ATOM   1946 O  OE1  . GLU A 1 255 ? 8.905   3.311   20.485  1.00 46.81  ?  255 GLU A OE1  1 
ATOM   1947 O  OE2  . GLU A 1 255 ? 9.024   2.481   22.514  1.00 52.06  -1 255 GLU A OE2  1 
ATOM   1948 N  N    . PRO A 1 256 ? 3.811   3.380   18.303  1.00 23.99  ?  256 PRO A N    1 
ATOM   1949 C  CA   . PRO A 1 256 ? 3.275   3.801   16.995  1.00 24.00  ?  256 PRO A CA   1 
ATOM   1950 C  C    . PRO A 1 256 ? 4.254   3.661   15.837  1.00 24.18  ?  256 PRO A C    1 
ATOM   1951 O  O    . PRO A 1 256 ? 3.860   3.203   14.755  1.00 21.59  ?  256 PRO A O    1 
ATOM   1952 C  CB   . PRO A 1 256 ? 2.854   5.254   17.250  1.00 24.38  ?  256 PRO A CB   1 
ATOM   1953 C  CG   . PRO A 1 256 ? 2.470   5.253   18.719  1.00 26.68  ?  256 PRO A CG   1 
ATOM   1954 C  CD   . PRO A 1 256 ? 3.466   4.327   19.380  1.00 28.57  ?  256 PRO A CD   1 
ATOM   1955 N  N    . ARG A 1 257 ? 5.526   4.019   16.039  1.00 24.21  ?  257 ARG A N    1 
ATOM   1956 C  CA   . ARG A 1 257 ? 6.498   3.933   14.952  1.00 23.94  ?  257 ARG A CA   1 
ATOM   1957 C  C    . ARG A 1 257 ? 6.658   2.501   14.452  1.00 23.15  ?  257 ARG A C    1 
ATOM   1958 O  O    . ARG A 1 257 ? 6.941   2.280   13.269  1.00 23.66  ?  257 ARG A O    1 
ATOM   1959 C  CB   . ARG A 1 257 ? 7.835   4.530   15.409  1.00 25.69  ?  257 ARG A CB   1 
ATOM   1960 C  CG   . ARG A 1 257 ? 8.807   4.824   14.277  1.00 37.57  ?  257 ARG A CG   1 
ATOM   1961 C  CD   . ARG A 1 257 ? 9.831   5.856   14.726  1.00 39.50  ?  257 ARG A CD   1 
ATOM   1962 N  NE   . ARG A 1 257 ? 10.918  5.237   15.469  1.00 47.57  ?  257 ARG A NE   1 
ATOM   1963 C  CZ   . ARG A 1 257 ? 12.160  5.120   15.019  1.00 43.78  ?  257 ARG A CZ   1 
ATOM   1964 N  NH1  . ARG A 1 257 ? 12.521  5.609   13.843  1.00 46.24  ?  257 ARG A NH1  1 
ATOM   1965 N  NH2  . ARG A 1 257 ? 13.067  4.506   15.773  1.00 46.50  ?  257 ARG A NH2  1 
ATOM   1966 N  N    . GLN A 1 258 ? 6.444   1.515   15.323  1.00 22.30  ?  258 GLN A N    1 
ATOM   1967 C  CA   . GLN A 1 258 ? 6.560   0.118   14.929  1.00 19.15  ?  258 GLN A CA   1 
ATOM   1968 C  C    . GLN A 1 258 ? 5.295   -0.385  14.251  1.00 21.40  ?  258 GLN A C    1 
ATOM   1969 O  O    . GLN A 1 258 ? 5.371   -1.098  13.247  1.00 20.54  ?  258 GLN A O    1 
ATOM   1970 C  CB   . GLN A 1 258 ? 6.893   -0.745  16.144  1.00 21.75  ?  258 GLN A CB   1 
ATOM   1971 C  CG   . GLN A 1 258 ? 8.184   -0.345  16.847  1.00 22.77  ?  258 GLN A CG   1 
ATOM   1972 C  CD   . GLN A 1 258 ? 8.364   -1.084  18.157  1.00 24.85  ?  258 GLN A CD   1 
ATOM   1973 O  OE1  . GLN A 1 258 ? 7.658   -0.818  19.142  1.00 25.73  ?  258 GLN A OE1  1 
ATOM   1974 N  NE2  . GLN A 1 258 ? 9.306   -2.025  18.180  1.00 25.13  ?  258 GLN A NE2  1 
ATOM   1975 N  N    . ARG A 1 259 ? 4.120   -0.037  14.787  1.00 20.07  ?  259 ARG A N    1 
ATOM   1976 C  CA   . ARG A 1 259 ? 2.881   -0.470  14.146  1.00 19.14  ?  259 ARG A CA   1 
ATOM   1977 C  C    . ARG A 1 259 ? 2.782   0.054   12.723  1.00 18.58  ?  259 ARG A C    1 
ATOM   1978 O  O    . ARG A 1 259 ? 2.141   -0.574  11.877  1.00 18.28  ?  259 ARG A O    1 
ATOM   1979 C  CB   . ARG A 1 259 ? 1.673   0.023   14.941  1.00 18.61  ?  259 ARG A CB   1 
ATOM   1980 C  CG   . ARG A 1 259 ? 1.627   -0.373  16.402  1.00 19.91  ?  259 ARG A CG   1 
ATOM   1981 C  CD   . ARG A 1 259 ? 0.208   -0.151  16.922  1.00 19.69  ?  259 ARG A CD   1 
ATOM   1982 N  NE   . ARG A 1 259 ? 0.155   -0.328  18.368  1.00 21.49  ?  259 ARG A NE   1 
ATOM   1983 C  CZ   . ARG A 1 259 ? 0.236   0.653   19.256  1.00 23.41  ?  259 ARG A CZ   1 
ATOM   1984 N  NH1  . ARG A 1 259 ? 0.332   1.921   18.884  1.00 25.75  ?  259 ARG A NH1  1 
ATOM   1985 N  NH2  . ARG A 1 259 ? 0.217   0.356   20.551  1.00 23.43  ?  259 ARG A NH2  1 
ATOM   1986 N  N    . HIS A 1 260 ? 3.389   1.213   12.455  1.00 19.95  ?  260 HIS A N    1 
ATOM   1987 C  CA   . HIS A 1 260 ? 3.348   1.797   11.123  1.00 19.57  ?  260 HIS A CA   1 
ATOM   1988 C  C    . HIS A 1 260 ? 3.819   0.810   10.059  1.00 18.85  ?  260 HIS A C    1 
ATOM   1989 O  O    . HIS A 1 260 ? 3.315   0.814   8.931   1.00 17.30  ?  260 HIS A O    1 
ATOM   1990 C  CB   . HIS A 1 260 ? 4.232   3.049   11.123  1.00 20.74  ?  260 HIS A CB   1 
ATOM   1991 C  CG   . HIS A 1 260 ? 4.039   3.924   9.927   1.00 21.94  ?  260 HIS A CG   1 
ATOM   1992 N  ND1  . HIS A 1 260 ? 3.112   4.943   9.894   1.00 24.38  ?  260 HIS A ND1  1 
ATOM   1993 C  CD2  . HIS A 1 260 ? 4.660   3.941   8.724   1.00 26.30  ?  260 HIS A CD2  1 
ATOM   1994 C  CE1  . HIS A 1 260 ? 3.167   5.549   8.722   1.00 26.65  ?  260 HIS A CE1  1 
ATOM   1995 N  NE2  . HIS A 1 260 ? 4.103   4.964   7.996   1.00 26.68  ?  260 HIS A NE2  1 
ATOM   1996 N  N    . LEU A 1 261 ? 4.787   -0.045  10.398  1.00 18.29  ?  261 LEU A N    1 
ATOM   1997 C  CA   . LEU A 1 261 ? 5.333   -0.970  9.412   1.00 18.49  ?  261 LEU A CA   1 
ATOM   1998 C  C    . LEU A 1 261 ? 4.347   -2.061  9.034   1.00 18.63  ?  261 LEU A C    1 
ATOM   1999 O  O    . LEU A 1 261 ? 4.528   -2.719  8.006   1.00 18.15  ?  261 LEU A O    1 
ATOM   2000 C  CB   . LEU A 1 261 ? 6.654   -1.582  9.888   1.00 19.78  ?  261 LEU A CB   1 
ATOM   2001 C  CG   . LEU A 1 261 ? 7.888   -0.757  9.509   1.00 20.70  ?  261 LEU A CG   1 
ATOM   2002 C  CD1  . LEU A 1 261 ? 7.886   0.589   10.218  1.00 22.70  ?  261 LEU A CD1  1 
ATOM   2003 C  CD2  . LEU A 1 261 ? 9.161   -1.538  9.836   1.00 22.78  ?  261 LEU A CD2  1 
ATOM   2004 N  N    . LEU A 1 262 ? 3.295   -2.252  9.824   1.00 17.90  ?  262 LEU A N    1 
ATOM   2005 C  CA   . LEU A 1 262 ? 2.240   -3.200  9.498   1.00 18.95  ?  262 LEU A CA   1 
ATOM   2006 C  C    . LEU A 1 262 ? 1.091   -2.555  8.727   1.00 19.95  ?  262 LEU A C    1 
ATOM   2007 O  O    . LEU A 1 262 ? 0.086   -3.221  8.454   1.00 19.67  ?  262 LEU A O    1 
ATOM   2008 C  CB   . LEU A 1 262 ? 1.726   -3.854  10.786  1.00 18.70  ?  262 LEU A CB   1 
ATOM   2009 C  CG   . LEU A 1 262 ? 2.810   -4.537  11.622  1.00 18.75  ?  262 LEU A CG   1 
ATOM   2010 C  CD1  . LEU A 1 262 ? 2.204   -5.208  12.851  1.00 22.70  ?  262 LEU A CD1  1 
ATOM   2011 C  CD2  . LEU A 1 262 ? 3.611   -5.551  10.801  1.00 23.51  ?  262 LEU A CD2  1 
ATOM   2012 N  N    . GLY A 1 263 ? 1.220   -1.284  8.360   1.00 16.86  ?  263 GLY A N    1 
ATOM   2013 C  CA   . GLY A 1 263 ? 0.134   -0.590  7.694   1.00 18.92  ?  263 GLY A CA   1 
ATOM   2014 C  C    . GLY A 1 263 ? -0.887  -0.015  8.641   1.00 17.55  ?  263 GLY A C    1 
ATOM   2015 O  O    . GLY A 1 263 ? -1.995  0.340   8.219   1.00 18.46  ?  263 GLY A O    1 
ATOM   2016 N  N    . PHE A 1 264 ? -0.546  0.106   9.915   1.00 17.83  ?  264 PHE A N    1 
ATOM   2017 C  CA   . PHE A 1 264 ? -1.477  0.688   10.874  1.00 18.62  ?  264 PHE A CA   1 
ATOM   2018 C  C    . PHE A 1 264 ? -1.731  2.154   10.512  1.00 20.05  ?  264 PHE A C    1 
ATOM   2019 O  O    . PHE A 1 264 ? -0.793  2.868   10.148  1.00 21.03  ?  264 PHE A O    1 
ATOM   2020 C  CB   . PHE A 1 264 ? -0.844  0.614   12.265  1.00 18.99  ?  264 PHE A CB   1 
ATOM   2021 C  CG   . PHE A 1 264 ? -1.814  0.746   13.396  1.00 20.06  ?  264 PHE A CG   1 
ATOM   2022 C  CD1  . PHE A 1 264 ? -2.601  -0.329  13.761  1.00 19.54  ?  264 PHE A CD1  1 
ATOM   2023 C  CD2  . PHE A 1 264 ? -1.909  1.922   14.127  1.00 19.41  ?  264 PHE A CD2  1 
ATOM   2024 C  CE1  . PHE A 1 264 ? -3.499  -0.231  14.817  1.00 20.48  ?  264 PHE A CE1  1 
ATOM   2025 C  CE2  . PHE A 1 264 ? -2.793  2.030   15.191  1.00 23.26  ?  264 PHE A CE2  1 
ATOM   2026 C  CZ   . PHE A 1 264 ? -3.593  0.949   15.541  1.00 22.09  ?  264 PHE A CZ   1 
ATOM   2027 N  N    . PRO A 1 265 ? -2.966  2.643   10.599  1.00 19.82  ?  265 PRO A N    1 
ATOM   2028 C  CA   . PRO A 1 265 ? -3.221  4.058   10.251  1.00 20.06  ?  265 PRO A CA   1 
ATOM   2029 C  C    . PRO A 1 265 ? -2.482  4.984   11.198  1.00 21.82  ?  265 PRO A C    1 
ATOM   2030 O  O    . PRO A 1 265 ? -2.597  4.854   12.424  1.00 21.65  ?  265 PRO A O    1 
ATOM   2031 C  CB   . PRO A 1 265 ? -4.744  4.199   10.429  1.00 19.75  ?  265 PRO A CB   1 
ATOM   2032 C  CG   . PRO A 1 265 ? -5.254  2.793   10.203  1.00 19.98  ?  265 PRO A CG   1 
ATOM   2033 C  CD   . PRO A 1 265 ? -4.227  1.934   10.894  1.00 20.03  ?  265 PRO A CD   1 
ATOM   2034 N  N    . PRO A 1 266 ? -1.733  5.948   10.678  1.00 20.85  ?  266 PRO A N    1 
ATOM   2035 C  CA   . PRO A 1 266 ? -0.884  6.765   11.546  1.00 22.77  ?  266 PRO A CA   1 
ATOM   2036 C  C    . PRO A 1 266 ? -1.684  7.815   12.295  1.00 25.31  ?  266 PRO A C    1 
ATOM   2037 O  O    . PRO A 1 266 ? -2.862  8.072   11.988  1.00 22.80  ?  266 PRO A O    1 
ATOM   2038 C  CB   . PRO A 1 266 ? 0.106   7.414   10.561  1.00 23.91  ?  266 PRO A CB   1 
ATOM   2039 C  CG   . PRO A 1 266 ? -0.631  7.459   9.270   1.00 26.39  ?  266 PRO A CG   1 
ATOM   2040 C  CD   . PRO A 1 266 ? -1.485  6.204   9.247   1.00 23.92  ?  266 PRO A CD   1 
ATOM   2041 N  N    . PRO A 1 267 ? -1.084  8.437   13.305  1.00 26.40  ?  267 PRO A N    1 
ATOM   2042 C  CA   . PRO A 1 267 ? -1.733  9.585   13.944  1.00 27.47  ?  267 PRO A CA   1 
ATOM   2043 C  C    . PRO A 1 267 ? -2.131  10.612  12.893  1.00 26.37  ?  267 PRO A C    1 
ATOM   2044 O  O    . PRO A 1 267 ? -1.381  10.886  11.950  1.00 28.77  ?  267 PRO A O    1 
ATOM   2045 C  CB   . PRO A 1 267 ? -0.643  10.128  14.875  1.00 27.80  ?  267 PRO A CB   1 
ATOM   2046 C  CG   . PRO A 1 267 ? 0.206   8.934   15.182  1.00 29.19  ?  267 PRO A CG   1 
ATOM   2047 C  CD   . PRO A 1 267 ? 0.206   8.095   13.929  1.00 26.10  ?  267 PRO A CD   1 
ATOM   2048 N  N    . GLY A 1 268 ? -3.332  11.161  13.048  1.00 26.18  ?  268 GLY A N    1 
ATOM   2049 C  CA   . GLY A 1 268 ? -3.880  12.123  12.114  1.00 30.64  ?  268 GLY A CA   1 
ATOM   2050 C  C    . GLY A 1 268 ? -4.560  11.530  10.898  1.00 27.71  ?  268 GLY A C    1 
ATOM   2051 O  O    . GLY A 1 268 ? -5.168  12.278  10.121  1.00 35.04  ?  268 GLY A O    1 
ATOM   2052 N  N    . ASP A 1 269 ? -4.486  10.220  10.706  1.00 27.22  ?  269 ASP A N    1 
ATOM   2053 C  CA   . ASP A 1 269 ? -5.125  9.604   9.554   1.00 27.47  ?  269 ASP A CA   1 
ATOM   2054 C  C    . ASP A 1 269 ? -6.642  9.768   9.641   1.00 25.82  ?  269 ASP A C    1 
ATOM   2055 O  O    . ASP A 1 269 ? -7.235  9.727   10.722  1.00 26.81  ?  269 ASP A O    1 
ATOM   2056 C  CB   . ASP A 1 269 ? -4.747  8.124   9.506   1.00 25.81  ?  269 ASP A CB   1 
ATOM   2057 C  CG   . ASP A 1 269 ? -5.114  7.461   8.195   1.00 27.88  ?  269 ASP A CG   1 
ATOM   2058 O  OD1  . ASP A 1 269 ? -6.258  6.990   8.059   1.00 24.84  ?  269 ASP A OD1  1 
ATOM   2059 O  OD2  . ASP A 1 269 ? -4.254  7.404   7.297   1.00 28.57  -1 269 ASP A OD2  1 
ATOM   2060 N  N    . ASP A 1 270 ? -7.272  9.951   8.474   1.00 27.09  ?  270 ASP A N    1 
ATOM   2061 C  CA   . ASP A 1 270 ? -8.725  10.095  8.419   1.00 28.76  ?  270 ASP A CA   1 
ATOM   2062 C  C    . ASP A 1 270 ? -9.463  8.892   9.001   1.00 25.87  ?  270 ASP A C    1 
ATOM   2063 O  O    . ASP A 1 270 ? -10.646 9.011   9.347   1.00 24.86  ?  270 ASP A O    1 
ATOM   2064 C  CB   . ASP A 1 270 ? -9.188  10.323  6.979   1.00 29.22  ?  270 ASP A CB   1 
ATOM   2065 C  CG   . ASP A 1 270 ? -9.144  11.784  6.574   1.00 40.20  ?  270 ASP A CG   1 
ATOM   2066 O  OD1  . ASP A 1 270 ? -9.460  12.645  7.421   1.00 50.21  ?  270 ASP A OD1  1 
ATOM   2067 O  OD2  . ASP A 1 270 ? -8.805  12.068  5.405   1.00 46.40  -1 270 ASP A OD2  1 
ATOM   2068 N  N    . TYR A 1 271 ? -8.805  7.739   9.105   1.00 24.64  ?  271 TYR A N    1 
ATOM   2069 C  CA   . TYR A 1 271 ? -9.472  6.567   9.661   1.00 23.96  ?  271 TYR A CA   1 
ATOM   2070 C  C    . TYR A 1 271 ? -9.939  6.805   11.094  1.00 22.41  ?  271 TYR A C    1 
ATOM   2071 O  O    . TYR A 1 271 ? -10.971 6.265   11.504  1.00 22.78  ?  271 TYR A O    1 
ATOM   2072 C  CB   . TYR A 1 271 ? -8.553  5.340   9.568   1.00 20.52  ?  271 TYR A CB   1 
ATOM   2073 C  CG   . TYR A 1 271 ? -9.067  4.133   10.324  1.00 19.38  ?  271 TYR A CG   1 
ATOM   2074 C  CD1  . TYR A 1 271 ? -9.969  3.256   9.729   1.00 21.40  ?  271 TYR A CD1  1 
ATOM   2075 C  CD2  . TYR A 1 271 ? -8.645  3.867   11.627  1.00 19.95  ?  271 TYR A CD2  1 
ATOM   2076 C  CE1  . TYR A 1 271 ? -10.451 2.150   10.418  1.00 20.09  ?  271 TYR A CE1  1 
ATOM   2077 C  CE2  . TYR A 1 271 ? -9.122  2.761   12.327  1.00 20.49  ?  271 TYR A CE2  1 
ATOM   2078 C  CZ   . TYR A 1 271 ? -10.016 1.906   11.720  1.00 21.86  ?  271 TYR A CZ   1 
ATOM   2079 O  OH   . TYR A 1 271 ? -10.514 0.821   12.422  1.00 20.92  ?  271 TYR A OH   1 
ATOM   2080 N  N    . TRP A 1 272 ? -9.212  7.620   11.856  1.00 22.07  ?  272 TRP A N    1 
ATOM   2081 C  CA   . TRP A 1 272 ? -9.469  7.768   13.287  1.00 24.16  ?  272 TRP A CA   1 
ATOM   2082 C  C    . TRP A 1 272 ? -10.680 8.656   13.549  1.00 26.74  ?  272 TRP A C    1 
ATOM   2083 O  O    . TRP A 1 272 ? -10.718 9.824   13.141  1.00 27.78  ?  272 TRP A O    1 
ATOM   2084 C  CB   . TRP A 1 272 ? -8.225  8.296   14.000  1.00 24.72  ?  272 TRP A CB   1 
ATOM   2085 C  CG   . TRP A 1 272 ? -7.085  7.346   13.868  1.00 21.26  ?  272 TRP A CG   1 
ATOM   2086 C  CD1  . TRP A 1 272 ? -5.895  7.567   13.221  1.00 21.52  ?  272 TRP A CD1  1 
ATOM   2087 C  CD2  . TRP A 1 272 ? -7.032  5.991   14.344  1.00 21.94  ?  272 TRP A CD2  1 
ATOM   2088 N  NE1  . TRP A 1 272 ? -5.102  6.443   13.290  1.00 24.01  ?  272 TRP A NE1  1 
ATOM   2089 C  CE2  . TRP A 1 272 ? -5.775  5.465   13.972  1.00 20.86  ?  272 TRP A CE2  1 
ATOM   2090 C  CE3  . TRP A 1 272 ? -7.915  5.182   15.072  1.00 22.35  ?  272 TRP A CE3  1 
ATOM   2091 C  CZ2  . TRP A 1 272 ? -5.385  4.162   14.279  1.00 20.55  ?  272 TRP A CZ2  1 
ATOM   2092 C  CZ3  . TRP A 1 272 ? -7.526  3.880   15.374  1.00 22.69  ?  272 TRP A CZ3  1 
ATOM   2093 C  CH2  . TRP A 1 272 ? -6.266  3.387   14.980  1.00 19.97  ?  272 TRP A CH2  1 
ATOM   2094 N  N    . THR A 1 273 ? -11.667 8.091   14.238  1.00 24.81  ?  273 THR A N    1 
ATOM   2095 C  CA   . THR A 1 273 ? -12.854 8.794   14.702  1.00 27.10  ?  273 THR A CA   1 
ATOM   2096 C  C    . THR A 1 273 ? -13.171 8.281   16.097  1.00 27.40  ?  273 THR A C    1 
ATOM   2097 O  O    . THR A 1 273 ? -12.558 7.328   16.581  1.00 26.95  ?  273 THR A O    1 
ATOM   2098 C  CB   . THR A 1 273 ? -14.063 8.493   13.811  1.00 29.80  ?  273 THR A CB   1 
ATOM   2099 O  OG1  . THR A 1 273 ? -14.392 7.102   13.924  1.00 29.26  ?  273 THR A OG1  1 
ATOM   2100 C  CG2  . THR A 1 273 ? -13.768 8.831   12.355  1.00 27.50  ?  273 THR A CG2  1 
ATOM   2101 N  N    . GLU A 1 274 ? -14.158 8.897   16.748  1.00 29.94  ?  274 GLU A N    1 
ATOM   2102 C  CA   . GLU A 1 274 ? -14.583 8.373   18.042  1.00 28.45  ?  274 GLU A CA   1 
ATOM   2103 C  C    . GLU A 1 274 ? -14.936 6.895   17.946  1.00 30.22  ?  274 GLU A C    1 
ATOM   2104 O  O    . GLU A 1 274 ? -14.569 6.098   18.820  1.00 31.01  ?  274 GLU A O    1 
ATOM   2105 C  CB   . GLU A 1 274 ? -15.771 9.169   18.578  1.00 36.40  ?  274 GLU A CB   1 
ATOM   2106 C  CG   . GLU A 1 274 ? -15.409 10.523  19.143  1.00 45.06  ?  274 GLU A CG   1 
ATOM   2107 C  CD   . GLU A 1 274 ? -16.543 11.125  19.949  1.00 53.34  ?  274 GLU A CD   1 
ATOM   2108 O  OE1  . GLU A 1 274 ? -17.643 10.525  19.973  1.00 52.11  ?  274 GLU A OE1  1 
ATOM   2109 O  OE2  . GLU A 1 274 ? -16.335 12.194  20.562  1.00 61.84  -1 274 GLU A OE2  1 
ATOM   2110 N  N    . GLU A 1 275 ? -15.621 6.501   16.869  1.00 28.42  ?  275 GLU A N    1 
ATOM   2111 C  CA   . GLU A 1 275 ? -16.025 5.106   16.736  1.00 27.54  ?  275 GLU A CA   1 
ATOM   2112 C  C    . GLU A 1 275 ? -14.834 4.178   16.515  1.00 26.08  ?  275 GLU A C    1 
ATOM   2113 O  O    . GLU A 1 275 ? -14.804 3.075   17.069  1.00 25.81  ?  275 GLU A O    1 
ATOM   2114 C  CB   . GLU A 1 275 ? -17.042 4.923   15.615  1.00 32.43  ?  275 GLU A CB   1 
ATOM   2115 C  CG   . GLU A 1 275 ? -17.440 3.457   15.449  1.00 40.15  ?  275 GLU A CG   1 
ATOM   2116 C  CD   . GLU A 1 275 ? -18.732 3.256   14.677  1.00 50.52  ?  275 GLU A CD   1 
ATOM   2117 O  OE1  . GLU A 1 275 ? -19.084 4.127   13.847  1.00 51.15  ?  275 GLU A OE1  1 
ATOM   2118 O  OE2  . GLU A 1 275 ? -19.397 2.220   14.913  1.00 54.22  -1 275 GLU A OE2  1 
ATOM   2119 N  N    . THR A 1 276 ? -13.871 4.563   15.670  1.00 23.76  ?  276 THR A N    1 
ATOM   2120 C  CA   . THR A 1 276 ? -12.757 3.640   15.457  1.00 21.61  ?  276 THR A CA   1 
ATOM   2121 C  C    . THR A 1 276 ? -11.778 3.628   16.620  1.00 23.95  ?  276 THR A C    1 
ATOM   2122 O  O    . THR A 1 276 ? -11.097 2.624   16.828  1.00 22.77  ?  276 THR A O    1 
ATOM   2123 C  CB   . THR A 1 276 ? -12.018 3.893   14.140  1.00 22.45  ?  276 THR A CB   1 
ATOM   2124 O  OG1  . THR A 1 276 ? -11.594 5.255   14.059  1.00 23.66  ?  276 THR A OG1  1 
ATOM   2125 C  CG2  . THR A 1 276 ? -12.899 3.541   12.949  1.00 24.21  ?  276 THR A CG2  1 
ATOM   2126 N  N    . ILE A 1 277 ? -11.687 4.712   17.396  1.00 25.00  ?  277 ILE A N    1 
ATOM   2127 C  CA   . ILE A 1 277 ? -10.901 4.629   18.622  1.00 25.05  ?  277 ILE A CA   1 
ATOM   2128 C  C    . ILE A 1 277 ? -11.543 3.628   19.577  1.00 26.16  ?  277 ILE A C    1 
ATOM   2129 O  O    . ILE A 1 277 ? -10.861 2.770   20.161  1.00 25.78  ?  277 ILE A O    1 
ATOM   2130 C  CB   . ILE A 1 277 ? -10.740 6.023   19.259  1.00 26.53  ?  277 ILE A CB   1 
ATOM   2131 C  CG1  . ILE A 1 277 ? -9.873  6.926   18.371  1.00 26.35  ?  277 ILE A CG1  1 
ATOM   2132 C  CG2  . ILE A 1 277 ? -10.142 5.895   20.660  1.00 30.13  ?  277 ILE A CG2  1 
ATOM   2133 C  CD1  . ILE A 1 277 ? -8.390  6.590   18.398  1.00 27.08  ?  277 ILE A CD1  1 
ATOM   2134 N  N    . LYS A 1 278 ? -12.872 3.687   19.706  1.00 26.28  ?  278 LYS A N    1 
ATOM   2135 C  CA   . LYS A 1 278 ? -13.588 2.726   20.540  1.00 26.60  ?  278 LYS A CA   1 
ATOM   2136 C  C    . LYS A 1 278 ? -13.338 1.301   20.065  1.00 26.28  ?  278 LYS A C    1 
ATOM   2137 O  O    . LYS A 1 278 ? -13.050 0.406   20.867  1.00 25.17  ?  278 LYS A O    1 
ATOM   2138 C  CB   . LYS A 1 278 ? -15.089 3.023   20.539  1.00 28.90  ?  278 LYS A CB   1 
ATOM   2139 C  CG   . LYS A 1 278 ? -15.903 1.966   21.286  1.00 36.70  ?  278 LYS A CG   1 
ATOM   2140 C  CD   . LYS A 1 278 ? -17.411 2.166   21.158  1.00 44.19  ?  278 LYS A CD   1 
ATOM   2141 C  CE   . LYS A 1 278 ? -18.050 1.018   20.372  1.00 44.84  ?  278 LYS A CE   1 
ATOM   2142 N  NZ   . LYS A 1 278 ? -19.539 0.999   20.531  1.00 55.49  ?  278 LYS A NZ   1 
ATOM   2143 N  N    . HIS A 1 279 ? -13.462 1.060   18.760  1.00 23.40  ?  279 HIS A N    1 
ATOM   2144 C  CA   . HIS A 1 279 ? -13.249 -0.298  18.276  1.00 24.28  ?  279 HIS A CA   1 
ATOM   2145 C  C    . HIS A 1 279 ? -11.809 -0.748  18.483  1.00 22.14  ?  279 HIS A C    1 
ATOM   2146 O  O    . HIS A 1 279 ? -11.550 -1.939  18.694  1.00 22.20  ?  279 HIS A O    1 
ATOM   2147 C  CB   . HIS A 1 279 ? -13.654 -0.419  16.801  1.00 23.25  ?  279 HIS A CB   1 
ATOM   2148 C  CG   . HIS A 1 279 ? -15.134 -0.463  16.580  1.00 25.28  ?  279 HIS A CG   1 
ATOM   2149 N  ND1  . HIS A 1 279 ? -15.988 -1.198  17.373  1.00 28.66  ?  279 HIS A ND1  1 
ATOM   2150 C  CD2  . HIS A 1 279 ? -15.911 0.139   15.649  1.00 31.12  ?  279 HIS A CD2  1 
ATOM   2151 C  CE1  . HIS A 1 279 ? -17.228 -1.045  16.942  1.00 34.12  ?  279 HIS A CE1  1 
ATOM   2152 N  NE2  . HIS A 1 279 ? -17.208 -0.241  15.894  1.00 31.34  ?  279 HIS A NE2  1 
ATOM   2153 N  N    . LEU A 1 280 ? -10.851 0.176   18.419  1.00 20.83  ?  280 LEU A N    1 
ATOM   2154 C  CA   . LEU A 1 280 ? -9.471  -0.215  18.661  1.00 20.79  ?  280 LEU A CA   1 
ATOM   2155 C  C    . LEU A 1 280 ? -9.292  -0.687  20.099  1.00 22.24  ?  280 LEU A C    1 
ATOM   2156 O  O    . LEU A 1 280 ? -8.660  -1.720  20.351  1.00 22.21  ?  280 LEU A O    1 
ATOM   2157 C  CB   . LEU A 1 280 ? -8.540  0.950   18.345  1.00 22.81  ?  280 LEU A CB   1 
ATOM   2158 C  CG   . LEU A 1 280 ? -7.048  0.625   18.377  1.00 20.18  ?  280 LEU A CG   1 
ATOM   2159 C  CD1  . LEU A 1 280 ? -6.651  -0.202  17.162  1.00 21.28  ?  280 LEU A CD1  1 
ATOM   2160 C  CD2  . LEU A 1 280 ? -6.250  1.917   18.444  1.00 25.49  ?  280 LEU A CD2  1 
ATOM   2161 N  N    . SER A 1 281 ? -9.848  0.059   21.058  1.00 24.64  ?  281 SER A N    1 
ATOM   2162 C  CA   . SER A 1 281 ? -9.760  -0.342  22.459  1.00 24.60  ?  281 SER A CA   1 
ATOM   2163 C  C    . SER A 1 281 ? -10.446 -1.674  22.709  1.00 26.48  ?  281 SER A C    1 
ATOM   2164 O  O    . SER A 1 281 ? -10.005 -2.443  23.573  1.00 28.86  ?  281 SER A O    1 
ATOM   2165 C  CB   . SER A 1 281 ? -10.343 0.744   23.363  1.00 29.58  ?  281 SER A CB   1 
ATOM   2166 O  OG   . SER A 1 281 ? -9.547  1.911   23.274  1.00 34.29  ?  281 SER A OG   1 
ATOM   2167 N  N    . GLU A 1 282 ? -11.534 -1.954  21.988  1.00 23.26  ?  282 GLU A N    1 
ATOM   2168 C  CA   . GLU A 1 282 ? -12.242 -3.219  22.169  1.00 24.14  ?  282 GLU A CA   1 
ATOM   2169 C  C    . GLU A 1 282 ? -11.401 -4.393  21.690  1.00 23.35  ?  282 GLU A C    1 
ATOM   2170 O  O    . GLU A 1 282 ? -11.323 -5.429  22.364  1.00 26.59  ?  282 GLU A O    1 
ATOM   2171 C  CB   . GLU A 1 282 ? -13.583 -3.189  21.427  1.00 25.18  ?  282 GLU A CB   1 
ATOM   2172 C  CG   . GLU A 1 282 ? -14.642 -2.276  21.995  1.00 32.78  ?  282 GLU A CG   1 
ATOM   2173 C  CD   . GLU A 1 282 ? -15.862 -2.172  21.080  1.00 36.58  ?  282 GLU A CD   1 
ATOM   2174 O  OE1  . GLU A 1 282 ? -15.723 -2.478  19.865  1.00 39.54  ?  282 GLU A OE1  1 
ATOM   2175 O  OE2  . GLU A 1 282 ? -16.938 -1.767  21.563  1.00 46.95  -1 282 GLU A OE2  1 
ATOM   2176 N  N    . MET A 1 283 ? -10.762 -4.250  20.528  1.00 20.97  ?  283 MET A N    1 
ATOM   2177 C  CA   . MET A 1 283 ? -9.978  -5.340  19.966  1.00 20.51  ?  283 MET A CA   1 
ATOM   2178 C  C    . MET A 1 283 ? -8.648  -5.527  20.678  1.00 20.71  ?  283 MET A C    1 
ATOM   2179 O  O    . MET A 1 283 ? -8.121  -6.642  20.707  1.00 20.78  ?  283 MET A O    1 
ATOM   2180 C  CB   . MET A 1 283 ? -9.732  -5.093  18.478  1.00 22.75  ?  283 MET A CB   1 
ATOM   2181 C  CG   . MET A 1 283 ? -10.975 -5.372  17.649  1.00 22.91  ?  283 MET A CG   1 
ATOM   2182 S  SD   . MET A 1 283 ? -10.713 -4.876  15.933  1.00 25.12  ?  283 MET A SD   1 
ATOM   2183 C  CE   . MET A 1 283 ? -9.279  -5.841  15.453  1.00 22.52  ?  283 MET A CE   1 
ATOM   2184 N  N    . TYR A 1 284 ? -8.083  -4.460  21.233  1.00 20.56  ?  284 TYR A N    1 
ATOM   2185 C  CA   . TYR A 1 284 ? -6.757  -4.506  21.844  1.00 19.80  ?  284 TYR A CA   1 
ATOM   2186 C  C    . TYR A 1 284 ? -6.845  -3.900  23.238  1.00 22.82  ?  284 TYR A C    1 
ATOM   2187 O  O    . TYR A 1 284 ? -6.319  -2.807  23.480  1.00 23.31  ?  284 TYR A O    1 
ATOM   2188 C  CB   . TYR A 1 284 ? -5.764  -3.725  20.985  1.00 19.68  ?  284 TYR A CB   1 
ATOM   2189 C  CG   . TYR A 1 284 ? -5.591  -4.235  19.559  1.00 17.57  ?  284 TYR A CG   1 
ATOM   2190 C  CD1  . TYR A 1 284 ? -4.905  -5.407  19.310  1.00 18.32  ?  284 TYR A CD1  1 
ATOM   2191 C  CD2  . TYR A 1 284 ? -6.086  -3.523  18.478  1.00 20.18  ?  284 TYR A CD2  1 
ATOM   2192 C  CE1  . TYR A 1 284 ? -4.716  -5.864  18.017  1.00 19.08  ?  284 TYR A CE1  1 
ATOM   2193 C  CE2  . TYR A 1 284 ? -5.906  -3.969  17.164  1.00 19.82  ?  284 TYR A CE2  1 
ATOM   2194 C  CZ   . TYR A 1 284 ? -5.205  -5.147  16.953  1.00 19.77  ?  284 TYR A CZ   1 
ATOM   2195 O  OH   . TYR A 1 284 ? -5.003  -5.636  15.678  1.00 18.67  ?  284 TYR A OH   1 
ATOM   2196 N  N    . PRO A 1 285 ? -7.513  -4.577  24.173  1.00 21.68  ?  285 PRO A N    1 
ATOM   2197 C  CA   . PRO A 1 285 ? -7.745  -3.978  25.497  1.00 23.22  ?  285 PRO A CA   1 
ATOM   2198 C  C    . PRO A 1 285 ? -6.432  -3.666  26.196  1.00 27.82  ?  285 PRO A C    1 
ATOM   2199 O  O    . PRO A 1 285 ? -5.564  -4.532  26.337  1.00 27.01  ?  285 PRO A O    1 
ATOM   2200 C  CB   . PRO A 1 285 ? -8.540  -5.058  26.244  1.00 26.06  ?  285 PRO A CB   1 
ATOM   2201 C  CG   . PRO A 1 285 ? -9.191  -5.867  25.145  1.00 24.08  ?  285 PRO A CG   1 
ATOM   2202 C  CD   . PRO A 1 285 ? -8.161  -5.895  24.048  1.00 24.08  ?  285 PRO A CD   1 
ATOM   2203 N  N    . GLY A 1 286 ? -6.291  -2.413  26.629  1.00 25.87  ?  286 GLY A N    1 
ATOM   2204 C  CA   . GLY A 1 286 ? -5.050  -1.930  27.194  1.00 29.30  ?  286 GLY A CA   1 
ATOM   2205 C  C    . GLY A 1 286 ? -4.179  -1.119  26.254  1.00 29.49  ?  286 GLY A C    1 
ATOM   2206 O  O    . GLY A 1 286 ? -3.213  -0.509  26.719  1.00 31.56  ?  286 GLY A O    1 
ATOM   2207 N  N    . ILE A 1 287 ? -4.490  -1.090  24.953  1.00 25.43  ?  287 ILE A N    1 
ATOM   2208 C  CA   . ILE A 1 287 ? -3.689  -0.313  24.010  1.00 22.93  ?  287 ILE A CA   1 
ATOM   2209 C  C    . ILE A 1 287 ? -3.753  1.184   24.346  1.00 25.90  ?  287 ILE A C    1 
ATOM   2210 O  O    . ILE A 1 287 ? -4.778  1.714   24.796  1.00 27.91  ?  287 ILE A O    1 
ATOM   2211 C  CB   . ILE A 1 287 ? -4.121  -0.590  22.557  1.00 22.76  ?  287 ILE A CB   1 
ATOM   2212 C  CG1  . ILE A 1 287 ? -3.042  -0.146  21.572  1.00 21.61  ?  287 ILE A CG1  1 
ATOM   2213 C  CG2  . ILE A 1 287 ? -5.436  0.120   22.239  1.00 23.37  ?  287 ILE A CG2  1 
ATOM   2214 C  CD1  . ILE A 1 287 ? -3.223  -0.722  20.178  1.00 24.11  ?  287 ILE A CD1  1 
ATOM   2215 N  N    . ASP A 1 288 ? -2.635  1.873   24.120  1.00 27.03  ?  288 ASP A N    1 
ATOM   2216 C  CA   . ASP A 1 288 ? -2.569  3.310   24.358  1.00 29.84  ?  288 ASP A CA   1 
ATOM   2217 C  C    . ASP A 1 288 ? -3.117  4.022   23.126  1.00 28.16  ?  288 ASP A C    1 
ATOM   2218 O  O    . ASP A 1 288 ? -2.490  4.009   22.065  1.00 27.60  ?  288 ASP A O    1 
ATOM   2219 C  CB   . ASP A 1 288 ? -1.120  3.712   24.623  1.00 33.20  ?  288 ASP A CB   1 
ATOM   2220 C  CG   . ASP A 1 288 ? -0.953  5.205   24.806  1.00 34.39  ?  288 ASP A CG   1 
ATOM   2221 O  OD1  . ASP A 1 288 ? -1.973  5.891   25.024  1.00 36.54  ?  288 ASP A OD1  1 
ATOM   2222 O  OD2  . ASP A 1 288 ? 0.200   5.691   24.730  1.00 39.67  -1 288 ASP A OD2  1 
ATOM   2223 N  N    . VAL A 1 289 ? -4.286  4.656   23.262  1.00 29.84  ?  289 VAL A N    1 
ATOM   2224 C  CA   . VAL A 1 289 ? -4.900  5.325   22.116  1.00 30.03  ?  289 VAL A CA   1 
ATOM   2225 C  C    . VAL A 1 289 ? -4.524  6.795   22.005  1.00 32.85  ?  289 VAL A C    1 
ATOM   2226 O  O    . VAL A 1 289 ? -4.832  7.423   20.980  1.00 31.88  ?  289 VAL A O    1 
ATOM   2227 C  CB   . VAL A 1 289 ? -6.437  5.175   22.113  1.00 30.40  ?  289 VAL A CB   1 
ATOM   2228 C  CG1  . VAL A 1 289 ? -6.830  3.708   22.211  1.00 31.17  ?  289 VAL A CG1  1 
ATOM   2229 C  CG2  . VAL A 1 289 ? -7.070  5.992   23.238  1.00 33.21  ?  289 VAL A CG2  1 
ATOM   2230 N  N    . GLU A 1 290 ? -3.862  7.360   23.012  1.00 35.00  ?  290 GLU A N    1 
ATOM   2231 C  CA   . GLU A 1 290 ? -3.563  8.790   23.010  1.00 35.44  ?  290 GLU A CA   1 
ATOM   2232 C  C    . GLU A 1 290 ? -2.880  9.281   21.739  1.00 34.18  ?  290 GLU A C    1 
ATOM   2233 O  O    . GLU A 1 290 ? -3.255  10.361  21.253  1.00 37.27  ?  290 GLU A O    1 
ATOM   2234 C  CB   . GLU A 1 290 ? -2.756  9.167   24.261  1.00 39.62  ?  290 GLU A CB   1 
ATOM   2235 C  CG   . GLU A 1 290 ? -2.664  10.663  24.493  1.00 46.10  ?  290 GLU A CG   1 
ATOM   2236 C  CD   . GLU A 1 290 ? -2.056  11.012  25.840  1.00 54.40  ?  290 GLU A CD   1 
ATOM   2237 O  OE1  . GLU A 1 290 ? -0.973  10.473  26.160  1.00 58.66  ?  290 GLU A OE1  1 
ATOM   2238 O  OE2  . GLU A 1 290 ? -2.666  11.817  26.579  1.00 61.40  -1 290 GLU A OE2  1 
ATOM   2239 N  N    . PRO A 1 291 ? -1.901  8.579   21.163  1.00 32.18  ?  291 PRO A N    1 
ATOM   2240 C  CA   . PRO A 1 291 ? -1.281  9.085   19.927  1.00 31.44  ?  291 PRO A CA   1 
ATOM   2241 C  C    . PRO A 1 291 ? -2.256  9.236   18.773  1.00 35.06  ?  291 PRO A C    1 
ATOM   2242 O  O    . PRO A 1 291 ? -1.968  9.992   17.836  1.00 34.90  ?  291 PRO A O    1 
ATOM   2243 C  CB   . PRO A 1 291 ? -0.192  8.047   19.616  1.00 32.19  ?  291 PRO A CB   1 
ATOM   2244 C  CG   . PRO A 1 291 ? 0.084   7.370   20.926  1.00 30.84  ?  291 PRO A CG   1 
ATOM   2245 C  CD   . PRO A 1 291 ? -1.244  7.353   21.647  1.00 33.03  ?  291 PRO A CD   1 
ATOM   2246 N  N    . TYR A 1 292 ? -3.404  8.554   18.811  1.00 29.08  ?  292 TYR A N    1 
ATOM   2247 C  CA   . TYR A 1 292 ? -4.314  8.502   17.674  1.00 29.33  ?  292 TYR A CA   1 
ATOM   2248 C  C    . TYR A 1 292 ? -5.596  9.296   17.878  1.00 31.40  ?  292 TYR A C    1 
ATOM   2249 O  O    . TYR A 1 292 ? -6.381  9.425   16.931  1.00 30.54  ?  292 TYR A O    1 
ATOM   2250 C  CB   . TYR A 1 292 ? -4.673  7.046   17.344  1.00 27.55  ?  292 TYR A CB   1 
ATOM   2251 C  CG   . TYR A 1 292 ? -3.453  6.165   17.155  1.00 24.33  ?  292 TYR A CG   1 
ATOM   2252 C  CD1  . TYR A 1 292 ? -2.762  6.150   15.952  1.00 22.56  ?  292 TYR A CD1  1 
ATOM   2253 C  CD2  . TYR A 1 292 ? -2.989  5.359   18.188  1.00 25.97  ?  292 TYR A CD2  1 
ATOM   2254 C  CE1  . TYR A 1 292 ? -1.634  5.350   15.776  1.00 23.96  ?  292 TYR A CE1  1 
ATOM   2255 C  CE2  . TYR A 1 292 ? -1.868  4.555   18.022  1.00 24.38  ?  292 TYR A CE2  1 
ATOM   2256 C  CZ   . TYR A 1 292 ? -1.202  4.559   16.812  1.00 23.83  ?  292 TYR A CZ   1 
ATOM   2257 O  OH   . TYR A 1 292 ? -0.099  3.769   16.649  1.00 24.49  ?  292 TYR A OH   1 
ATOM   2258 N  N    . LEU A 1 293 ? -5.829  9.818   19.073  1.00 33.32  ?  293 LEU A N    1 
ATOM   2259 C  CA   . LEU A 1 293 ? -7.057  10.550  19.341  1.00 37.22  ?  293 LEU A CA   1 
ATOM   2260 C  C    . LEU A 1 293 ? -7.181  11.732  18.387  1.00 43.32  ?  293 LEU A C    1 
ATOM   2261 O  O    . LEU A 1 293 ? -6.251  12.547  18.292  1.00 45.36  ?  293 LEU A O    1 
ATOM   2262 C  CB   . LEU A 1 293 ? -7.042  11.057  20.777  1.00 38.37  ?  293 LEU A CB   1 
ATOM   2263 C  CG   . LEU A 1 293 ? -7.175  9.979   21.848  1.00 41.15  ?  293 LEU A CG   1 
ATOM   2264 C  CD1  . LEU A 1 293 ? -7.079  10.597  23.229  1.00 39.82  ?  293 LEU A CD1  1 
ATOM   2265 C  CD2  . LEU A 1 293 ? -8.497  9.238   21.676  1.00 42.77  ?  293 LEU A CD2  1 
ATOM   2266 N  N    . PRO A 1 294 ? -8.300  11.864  17.662  1.00 44.05  ?  294 PRO A N    1 
ATOM   2267 C  CA   . PRO A 1 294 ? -8.512  12.990  16.745  1.00 47.78  ?  294 PRO A CA   1 
ATOM   2268 C  C    . PRO A 1 294 ? -8.422  14.330  17.474  1.00 53.97  ?  294 PRO A C    1 
ATOM   2269 O  O    . PRO A 1 294 ? -9.063  14.467  18.515  1.00 48.98  ?  294 PRO A O    1 
ATOM   2270 C  CB   . PRO A 1 294 ? -9.941  12.766  16.240  1.00 51.11  ?  294 PRO A CB   1 
ATOM   2271 C  CG   . PRO A 1 294 ? -10.179 11.297  16.405  1.00 45.94  ?  294 PRO A CG   1 
ATOM   2272 C  CD   . PRO A 1 294 ? -9.416  10.902  17.636  1.00 42.37  ?  294 PRO A CD   1 
ATOM   2273 N  N    . TRP B 2 1   ? 10.389  -23.194 -3.508  1.00 30.00  ?  15  TRP C N    1 
ATOM   2274 C  CA   . TRP B 2 1   ? 10.248  -24.405 -2.661  1.00 30.00  ?  15  TRP C CA   1 
ATOM   2275 C  C    . TRP B 2 1   ? 10.557  -24.074 -1.200  1.00 30.00  ?  15  TRP C C    1 
ATOM   2276 O  O    . TRP B 2 1   ? 11.116  -23.002 -0.966  1.00 30.00  ?  15  TRP C O    1 
ATOM   2277 C  CB   . TRP B 2 1   ? 11.172  -25.525 -3.154  1.00 30.00  ?  15  TRP C CB   1 
ATOM   2278 C  CG   . TRP B 2 1   ? 12.623  -25.185 -3.037  1.00 30.00  ?  15  TRP C CG   1 
ATOM   2279 C  CD1  . TRP B 2 1   ? 13.497  -25.627 -2.089  1.00 30.00  ?  15  TRP C CD1  1 
ATOM   2280 C  CD2  . TRP B 2 1   ? 13.371  -24.311 -3.896  1.00 30.00  ?  15  TRP C CD2  1 
ATOM   2281 N  NE1  . TRP B 2 1   ? 14.737  -25.092 -2.301  1.00 30.00  ?  15  TRP C NE1  1 
ATOM   2282 C  CE2  . TRP B 2 1   ? 14.691  -24.282 -3.404  1.00 30.00  ?  15  TRP C CE2  1 
ATOM   2283 C  CE3  . TRP B 2 1   ? 13.058  -23.558 -5.032  1.00 30.00  ?  15  TRP C CE3  1 
ATOM   2284 C  CZ2  . TRP B 2 1   ? 15.693  -23.528 -4.009  1.00 30.00  ?  15  TRP C CZ2  1 
ATOM   2285 C  CZ3  . TRP B 2 1   ? 14.048  -22.811 -5.629  1.00 30.00  ?  15  TRP C CZ3  1 
ATOM   2286 C  CH2  . TRP B 2 1   ? 15.348  -22.800 -5.124  1.00 30.00  ?  15  TRP C CH2  1 
ATOM   2287 N  N    . TYR B 2 2   ? 10.206  -24.957 -0.272  1.00 35.33  ?  16  TYR C N    1 
ATOM   2288 C  CA   . TYR B 2 2   ? 10.477  -24.823 1.184   1.00 36.83  ?  16  TYR C CA   1 
ATOM   2289 C  C    . TYR B 2 2   ? 9.894   -23.526 1.748   1.00 33.28  ?  16  TYR C C    1 
ATOM   2290 O  O    . TYR B 2 2   ? 10.436  -23.037 2.735   1.00 28.47  ?  16  TYR C O    1 
ATOM   2291 C  CB   . TYR B 2 2   ? 11.963  -24.946 1.491   1.00 36.73  ?  16  TYR C CB   1 
ATOM   2292 C  CG   . TYR B 2 2   ? 12.630  -26.244 1.119   1.00 39.82  ?  16  TYR C CG   1 
ATOM   2293 C  CD1  . TYR B 2 2   ? 11.949  -27.278 0.499   1.00 41.34  ?  16  TYR C CD1  1 
ATOM   2294 C  CD2  . TYR B 2 2   ? 13.975  -26.423 1.382   1.00 43.98  ?  16  TYR C CD2  1 
ATOM   2295 C  CE1  . TYR B 2 2   ? 12.588  -28.455 0.153   1.00 45.87  ?  16  TYR C CE1  1 
ATOM   2296 C  CE2  . TYR B 2 2   ? 14.629  -27.593 1.045   1.00 41.36  ?  16  TYR C CE2  1 
ATOM   2297 C  CZ   . TYR B 2 2   ? 13.932  -28.613 0.429   1.00 44.74  ?  16  TYR C CZ   1 
ATOM   2298 O  OH   . TYR B 2 2   ? 14.584  -29.771 0.096   1.00 52.10  ?  16  TYR C OH   1 
ATOM   2299 H  H    . TYR B 2 2   ? 9.749   -25.717 -0.468  1.00 42.39  ?  16  TYR C H    1 
ATOM   2300 H  HB2  . TYR B 2 2   ? 12.424  -24.222 1.034   1.00 44.08  ?  16  TYR C HB2  1 
ATOM   2301 H  HD1  . TYR B 2 2   ? 11.034  -27.183 0.308   1.00 49.60  ?  16  TYR C HD1  1 
ATOM   2302 H  HD2  . TYR B 2 2   ? 14.458  -25.730 1.798   1.00 52.78  ?  16  TYR C HD2  1 
ATOM   2303 H  HE1  . TYR B 2 2   ? 12.108  -29.149 -0.264  1.00 55.05  ?  16  TYR C HE1  1 
ATOM   2304 H  HE2  . TYR B 2 2   ? 15.547  -27.695 1.233   1.00 49.63  ?  16  TYR C HE2  1 
ATOM   2305 H  HH   . TYR B 2 2   ? 15.430  -29.755 -0.057  1.00 62.52  ?  16  TYR C HH   1 
ATOM   2306 N  N    . GLY B 2 3   ? 8.812   -23.039 1.158   1.00 29.87  ?  17  GLY C N    1 
ATOM   2307 C  CA   . GLY B 2 3   ? 8.132   -21.834 1.653   1.00 28.46  ?  17  GLY C CA   1 
ATOM   2308 C  C    . GLY B 2 3   ? 6.704   -22.105 2.070   1.00 28.43  ?  17  GLY C C    1 
ATOM   2309 O  O    . GLY B 2 3   ? 6.450   -23.204 2.562   1.00 29.40  ?  17  GLY C O    1 
ATOM   2310 H  H    . GLY B 2 3   ? 8.432   -23.423 0.424   1.00 35.84  ?  17  GLY C H    1 
ATOM   2311 H  HA2  . GLY B 2 3   ? 8.632   -21.472 2.425   1.00 34.15  ?  17  GLY C HA2  1 
ATOM   2312 H  HA3  . GLY B 2 3   ? 8.141   -21.157 0.950   1.00 34.15  ?  17  GLY C HA3  1 
ATOM   2313 N  N    . TRP B 2 4   ? 5.808   -21.145 1.859   1.00 27.02  ?  18  TRP C N    1 
ATOM   2314 C  CA   . TRP B 2 4   ? 4.401   -21.238 2.316   1.00 28.49  ?  18  TRP C CA   1 
ATOM   2315 C  C    . TRP B 2 4   ? 3.426   -20.653 1.297   1.00 28.28  ?  18  TRP C C    1 
ATOM   2316 O  O    . TRP B 2 4   ? 2.230   -20.781 1.534   1.00 32.66  ?  18  TRP C O    1 
ATOM   2317 C  CB   . TRP B 2 4   ? 4.275   -20.488 3.647   1.00 26.03  ?  18  TRP C CB   1 
ATOM   2318 C  CG   . TRP B 2 4   ? 4.454   -19.006 3.512   1.00 24.13  ?  18  TRP C CG   1 
ATOM   2319 C  CD1  . TRP B 2 4   ? 3.478   -18.085 3.272   1.00 23.80  ?  18  TRP C CD1  1 
ATOM   2320 C  CD2  . TRP B 2 4   ? 5.686   -18.269 3.584   1.00 23.12  ?  18  TRP C CD2  1 
ATOM   2321 N  NE1  . TRP B 2 4   ? 4.014   -16.829 3.199   1.00 23.83  ?  18  TRP C NE1  1 
ATOM   2322 C  CE2  . TRP B 2 4   ? 5.367   -16.910 3.383   1.00 23.69  ?  18  TRP C CE2  1 
ATOM   2323 C  CE3  . TRP B 2 4   ? 7.022   -18.620 3.797   1.00 24.64  ?  18  TRP C CE3  1 
ATOM   2324 C  CZ2  . TRP B 2 4   ? 6.335   -15.908 3.392   1.00 23.49  ?  18  TRP C CZ2  1 
ATOM   2325 C  CZ3  . TRP B 2 4   ? 7.978   -17.629 3.805   1.00 24.87  ?  18  TRP C CZ3  1 
ATOM   2326 C  CH2  . TRP B 2 4   ? 7.637   -16.293 3.609   1.00 25.51  ?  18  TRP C CH2  1 
ATOM   2327 H  H    . TRP B 2 4   ? 6.022   -20.347 1.480   1.00 32.43  ?  18  TRP C H    1 
ATOM   2328 H  HA   . TRP B 2 4   ? 4.183   -22.186 2.468   1.00 34.19  ?  18  TRP C HA   1 
ATOM   2329 H  HB2  . TRP B 2 4   ? 3.392   -20.673 4.026   1.00 31.23  ?  18  TRP C HB2  1 
ATOM   2330 H  HB3  . TRP B 2 4   ? 4.949   -20.838 4.265   1.00 31.23  ?  18  TRP C HB3  1 
ATOM   2331 H  HD1  . TRP B 2 4   ? 2.560   -18.280 3.175   1.00 28.56  ?  18  TRP C HD1  1 
ATOM   2332 H  HE3  . TRP B 2 4   ? 7.264   -19.524 3.929   1.00 29.57  ?  18  TRP C HE3  1 
ATOM   2333 H  HZ2  . TRP B 2 4   ? 6.104   -15.005 3.258   1.00 28.19  ?  18  TRP C HZ2  1 
ATOM   2334 H  HZ3  . TRP B 2 4   ? 8.883   -17.858 3.947   1.00 29.85  ?  18  TRP C HZ3  1 
ATOM   2335 H  HH2  . TRP B 2 4   ? 8.313   -15.639 3.618   1.00 30.62  ?  18  TRP C HH2  1 
ATOM   2336 N  N    . ALA B 2 5   ? 3.896   -20.038 0.216   1.00 31.09  ?  19  ALA C N    1 
ATOM   2337 C  CA   . ALA B 2 5   ? 3.008   -19.324 -0.724  1.00 35.80  ?  19  ALA C CA   1 
ATOM   2338 C  C    . ALA B 2 5   ? 3.476   -19.418 -2.167  1.00 38.25  ?  19  ALA C C    1 
ATOM   2339 O  O    . ALA B 2 5   ? 4.669   -19.359 -2.392  1.00 38.09  ?  19  ALA C O    1 
ATOM   2340 C  CB   . ALA B 2 5   ? 2.971   -17.882 -0.331  1.00 36.59  ?  19  ALA C CB   1 
ATOM   2341 H  H    . ALA B 2 5   ? 4.767   -20.035 -0.045  1.00 37.30  ?  19  ALA C H    1 
ATOM   2342 H  HA   . ALA B 2 5   ? 2.102   -19.701 -0.660  1.00 42.96  ?  19  ALA C HA   1 
ATOM   2343 H  HB1  . ALA B 2 5   ? 3.879   -17.550 -0.230  1.00 43.90  ?  19  ALA C HB1  1 
ATOM   2344 H  HB2  . ALA B 2 5   ? 2.514   -17.370 -1.018  1.00 43.90  ?  19  ALA C HB2  1 
ATOM   2345 H  HB3  . ALA B 2 5   ? 2.497   -17.788 0.513   1.00 43.90  ?  19  ALA C HB3  1 
ATOM   2346 N  N    . SER B 2 6   ? 2.542   -19.392 -3.103  1.00 37.52  ?  20  SER C N    1 
ATOM   2347 C  CA   . SER B 2 6   ? 2.861   -19.401 -4.544  1.00 41.26  ?  20  SER C CA   1 
ATOM   2348 C  C    . SER B 2 6   ? 3.595   -20.698 -4.866  1.00 45.62  ?  20  SER C C    1 
ATOM   2349 O  O    . SER B 2 6   ? 3.228   -21.723 -4.297  1.00 45.56  ?  20  SER C O    1 
ATOM   2350 C  CB   . SER B 2 6   ? 3.648   -18.167 -4.913  1.00 44.74  ?  20  SER C CB   1 
ATOM   2351 O  OG   . SER B 2 6   ? 3.702   -18.001 -6.318  1.00 48.21  ?  20  SER C OG   1 
ATOM   2352 H  H    . SER B 2 6   ? 1.649   -19.364 -2.934  1.00 45.02  ?  20  SER C H    1 
ATOM   2353 H  HA   . SER B 2 6   ? 2.005   -19.393 -5.050  1.00 49.51  ?  20  SER C HA   1 
ATOM   2354 H  HB2  . SER B 2 6   ? 3.227   -17.380 -4.504  1.00 53.68  ?  20  SER C HB2  1 
ATOM   2355 H  HB3  . SER B 2 6   ? 4.562   -18.244 -4.560  1.00 53.68  ?  20  SER C HB3  1 
ATOM   2356 H  HG   . SER B 2 6   ? 3.134   -18.517 -6.672  1.00 57.85  ?  20  SER C HG   1 
ATOM   2357 N  N    . ASN B 2 7   ? 4.585   -20.655 -5.742  1.00 47.04  ?  21  ASN C N    1 
ATOM   2358 C  CA   . ASN B 2 7   ? 5.334   -21.863 -6.155  1.00 52.86  ?  21  ASN C CA   1 
ATOM   2359 C  C    . ASN B 2 7   ? 6.707   -21.438 -6.664  1.00 53.94  ?  21  ASN C C    1 
ATOM   2360 O  O    . ASN B 2 7   ? 6.807   -20.369 -7.284  1.00 52.98  ?  21  ASN C O    1 
ATOM   2361 C  CB   . ASN B 2 7   ? 4.593   -22.683 -7.213  1.00 56.10  ?  21  ASN C CB   1 
ATOM   2362 C  CG   . ASN B 2 7   ? 4.678   -24.171 -6.963  1.00 62.06  ?  21  ASN C CG   1 
ATOM   2363 O  OD1  . ASN B 2 7   ? 3.717   -24.785 -6.506  1.00 63.92  ?  21  ASN C OD1  1 
ATOM   2364 N  ND2  . ASN B 2 7   ? 5.831   -24.754 -7.245  1.00 66.22  ?  21  ASN C ND2  1 
ATOM   2365 H  H    . ASN B 2 7   ? 4.860   -19.896 -6.156  1.00 56.44  ?  21  ASN C H    1 
ATOM   2366 H  HA   . ASN B 2 7   ? 5.450   -22.426 -5.368  1.00 63.43  ?  21  ASN C HA   1 
ATOM   2367 H  HB2  . ASN B 2 7   ? 3.653   -22.411 -7.222  1.00 67.32  ?  21  ASN C HB2  1 
ATOM   2368 H  HB3  . ASN B 2 7   ? 4.977   -22.484 -8.090  1.00 67.32  ?  21  ASN C HB3  1 
ATOM   2369 H  HD21 . ASN B 2 7   ? 6.491   -24.736 -6.656  1.00 79.47  ?  21  ASN C HD21 1 
ATOM   2370 H  HD22 . ASN B 2 7   ? 5.948   -25.152 -8.025  1.00 79.47  ?  21  ASN C HD22 1 
ATOM   2371 N  N    . ASP B 2 8   ? 7.707   -22.262 -6.405  1.00 30.00  ?  22  ASP C N    1 
ATOM   2372 C  CA   . ASP B 2 8   ? 9.091   -21.941 -6.820  1.00 30.00  ?  22  ASP C CA   1 
ATOM   2373 C  C    . ASP B 2 8   ? 9.464   -22.884 -7.966  1.00 30.00  ?  22  ASP C C    1 
ATOM   2374 O  O    . ASP B 2 8   ? 10.656  -22.981 -8.282  1.00 30.00  ?  22  ASP C O    1 
ATOM   2375 C  CB   . ASP B 2 8   ? 10.033  -22.086 -5.628  1.00 30.00  ?  22  ASP C CB   1 
ATOM   2376 C  CG   . ASP B 2 8   ? 9.774   -23.343 -4.824  1.00 30.00  ?  22  ASP C CG   1 
ATOM   2377 O  OD1  . ASP B 2 8   ? 9.162   -24.265 -5.381  1.00 30.00  ?  22  ASP C OD1  1 
ATOM   2378 N  N    . GLY B 2 9   ? 8.478   -23.578 -8.536  1.00 81.32  ?  23  GLY C N    1 
ATOM   2379 C  CA   . GLY B 2 9   ? 8.745   -24.562 -9.597  1.00 88.51  ?  23  GLY C CA   1 
ATOM   2380 C  C    . GLY B 2 9   ? 8.766   -25.976 -9.041  1.00 89.67  ?  23  GLY C C    1 
ATOM   2381 O  O    . GLY B 2 9   ? 8.885   -26.907 -9.847  1.00 95.07  ?  23  GLY C O    1 
ATOM   2382 H  H    . GLY B 2 9   ? 7.612   -23.515 -8.276  1.00 97.59  ?  23  GLY C H    1 
ATOM   2383 H  HA2  . GLY B 2 9   ? 8.040   -24.491 -10.287 1.00 106.21 ?  23  GLY C HA2  1 
ATOM   2384 H  HA3  . GLY B 2 9   ? 9.615   -24.361 -10.019 1.00 106.21 ?  23  GLY C HA3  1 
ATOM   2385 N  N    . GLU B 2 10  ? 8.672   -26.143 -7.723  1.00 80.63  ?  24  GLU C N    1 
ATOM   2386 C  CA   . GLU B 2 10  ? 8.627   -27.478 -7.074  1.00 82.84  ?  24  GLU C CA   1 
ATOM   2387 C  C    . GLU B 2 10  ? 7.394   -27.500 -6.181  1.00 78.29  ?  24  GLU C C    1 
ATOM   2388 O  O    . GLU B 2 10  ? 6.446   -28.217 -6.526  1.00 84.10  ?  24  GLU C O    1 
ATOM   2389 C  CB   . GLU B 2 10  ? 9.917   -27.741 -6.301  1.00 85.62  ?  24  GLU C CB   1 
ATOM   2390 C  CG   . GLU B 2 10  ? 11.152  -27.605 -7.168  1.00 86.56  ?  24  GLU C CG   1 
ATOM   2391 C  CD   . GLU B 2 10  ? 12.295  -28.545 -6.832  1.00 94.50  ?  24  GLU C CD   1 
ATOM   2392 O  OE1  . GLU B 2 10  ? 12.032  -29.740 -6.595  1.00 97.97  ?  24  GLU C OE1  1 
ATOM   2393 O  OE2  . GLU B 2 10  ? 13.450  -28.077 -6.818  1.00 93.68  -1 24  GLU C OE2  1 
ATOM   2394 H  H    . GLU B 2 10  ? 8.599   -25.449 -7.144  1.00 96.75  ?  24  GLU C H    1 
ATOM   2395 H  HA   . GLU B 2 10  ? 8.526   -28.164 -7.770  1.00 99.41  ?  24  GLU C HA   1 
ATOM   2396 H  HB2  . GLU B 2 10  ? 9.976   -27.106 -5.558  1.00 102.74 ?  24  GLU C HB2  1 
ATOM   2397 H  HB3  . GLU B 2 10  ? 9.882   -28.644 -5.927  1.00 102.74 ?  24  GLU C HB3  1 
ATOM   2398 H  HG2  . GLU B 2 10  ? 10.895  -27.756 -8.101  1.00 103.87 ?  24  GLU C HG2  1 
ATOM   2399 H  HG3  . GLU B 2 10  ? 11.483  -26.686 -7.102  1.00 103.87 ?  24  GLU C HG3  1 
ATOM   2400 N  N    . GLY B 2 11  ? 7.394   -26.747 -5.088  1.00 66.48  ?  25  GLY C N    1 
ATOM   2401 C  CA   . GLY B 2 11  ? 6.248   -26.602 -4.212  1.00 57.57  ?  25  GLY C CA   1 
ATOM   2402 C  C    . GLY B 2 11  ? 6.057   -25.163 -3.779  1.00 49.85  ?  25  GLY C C    1 
ATOM   2403 O  O    . GLY B 2 11  ? 6.452   -24.242 -4.500  1.00 51.45  ?  25  GLY C O    1 
ATOM   2404 H  H    . GLY B 2 11  ? 8.079   -26.290 -4.839  1.00 79.77  ?  25  GLY C H    1 
ATOM   2405 H  HA2  . GLY B 2 11  ? 5.448   -26.895 -4.674  1.00 69.08  ?  25  GLY C HA2  1 
ATOM   2406 H  HA3  . GLY B 2 11  ? 6.374   -27.149 -3.421  1.00 69.08  ?  25  GLY C HA3  1 
ATOM   2407 N  N    . VAL B 2 12  ? 5.475   -24.951 -2.597  1.00 39.91  ?  26  VAL C N    1 
ATOM   2408 C  CA   . VAL B 2 12  ? 5.214   -23.593 -2.132  1.00 38.88  ?  26  VAL C CA   1 
ATOM   2409 C  C    . VAL B 2 12  ? 6.529   -22.881 -1.847  1.00 36.61  ?  26  VAL C C    1 
ATOM   2410 O  O    . VAL B 2 12  ? 7.531   -23.501 -1.466  1.00 36.06  ?  26  VAL C O    1 
ATOM   2411 C  CB   . VAL B 2 12  ? 4.297   -23.601 -0.896  1.00 37.77  ?  26  VAL C CB   1 
ATOM   2412 C  CG1  . VAL B 2 12  ? 2.900   -24.009 -1.309  1.00 42.79  ?  26  VAL C CG1  1 
ATOM   2413 C  CG2  . VAL B 2 12  ? 4.856   -24.530 0.167   1.00 38.31  ?  26  VAL C CG2  1 
ATOM   2414 H  H    . VAL B 2 12  ? 5.227   -25.569 -2.053  1.00 47.89  ?  26  VAL C H    1 
ATOM   2415 H  HA   . VAL B 2 12  ? 4.754   -23.106 -2.834  1.00 46.66  ?  26  VAL C HA   1 
ATOM   2416 H  HB   . VAL B 2 12  ? 4.252   -22.713 -0.509  1.00 45.33  ?  26  VAL C HB   1 
ATOM   2417 H  HG11 . VAL B 2 12  ? 2.954   -24.805 -1.861  1.00 51.35  ?  26  VAL C HG11 1 
ATOM   2418 H  HG12 . VAL B 2 12  ? 2.377   -24.192 -0.513  1.00 51.35  ?  26  VAL C HG12 1 
ATOM   2419 H  HG13 . VAL B 2 12  ? 2.496   -23.285 -1.812  1.00 51.35  ?  26  VAL C HG13 1 
ATOM   2420 H  HG21 . VAL B 2 12  ? 5.807   -24.646 0.016   1.00 45.97  ?  26  VAL C HG21 1 
ATOM   2421 H  HG22 . VAL B 2 12  ? 4.705   -24.136 1.041   1.00 45.97  ?  26  VAL C HG22 1 
ATOM   2422 H  HG23 . VAL B 2 12  ? 4.405   -25.386 0.107   1.00 45.97  ?  26  VAL C HG23 1 
ATOM   2423 N  N    . ALA B 2 13  ? 6.522   -21.559 -2.007  1.00 32.82  ?  27  ALA C N    1 
ATOM   2424 C  CA   . ALA B 2 13  ? 7.753   -20.787 -2.024  1.00 32.86  ?  27  ALA C CA   1 
ATOM   2425 C  C    . ALA B 2 13  ? 7.771   -19.728 -0.930  1.00 30.53  ?  27  ALA C C    1 
ATOM   2426 O  O    . ALA B 2 13  ? 6.745   -19.377 -0.346  1.00 27.60  ?  27  ALA C O    1 
ATOM   2427 C  CB   . ALA B 2 13  ? 7.960   -20.085 -3.376  1.00 36.97  ?  27  ALA C CB   1 
ATOM   2428 H  H    . ALA B 2 13  ? 5.809   -21.088 -2.108  1.00 39.39  ?  27  ALA C H    1 
ATOM   2429 H  HA   . ALA B 2 13  ? 8.484   -21.404 -1.859  1.00 39.44  ?  27  ALA C HA   1 
ATOM   2430 H  HB1  . ALA B 2 13  ? 7.569   -20.629 -4.077  1.00 44.37  ?  27  ALA C HB1  1 
ATOM   2431 H  HB2  . ALA B 2 13  ? 8.911   -19.976 -3.533  1.00 44.37  ?  27  ALA C HB2  1 
ATOM   2432 H  HB3  . ALA B 2 13  ? 7.527   -19.217 -3.350  1.00 44.37  ?  27  ALA C HB3  1 
ATOM   2433 N  N    . ILE B 2 14  ? 8.969   -19.235 -0.646  1.00 27.49  ?  28  ILE C N    1 
ATOM   2434 C  CA   . ILE B 2 14  ? 9.149   -18.078 0.219   1.00 26.14  ?  28  ILE C CA   1 
ATOM   2435 C  C    . ILE B 2 14  ? 8.768   -16.825 -0.557  1.00 36.30  ?  28  ILE C C    1 
ATOM   2436 O  O    . ILE B 2 14  ? 9.124   -16.668 -1.732  1.00 36.38  ?  28  ILE C O    1 
ATOM   2437 C  CB   . ILE B 2 14  ? 10.604  -18.029 0.723   1.00 30.43  ?  28  ILE C CB   1 
ATOM   2438 C  CG1  . ILE B 2 14  ? 10.906  -19.306 1.518   1.00 31.97  ?  28  ILE C CG1  1 
ATOM   2439 C  CG2  . ILE B 2 14  ? 10.843  -16.777 1.541   1.00 31.63  ?  28  ILE C CG2  1 
ATOM   2440 C  CD1  . ILE B 2 14  ? 12.338  -19.428 1.982   1.00 36.44  ?  28  ILE C CD1  1 
ATOM   2441 H  H    . ILE B 2 14  ? 9.707   -19.559 -0.947  1.00 32.98  ?  28  ILE C H    1 
ATOM   2442 H  HA   . ILE B 2 14  ? 8.565   -18.141 0.992   1.00 31.37  ?  28  ILE C HA   1 
ATOM   2443 H  HB   . ILE B 2 14  ? 11.210  -17.992 -0.033  1.00 36.52  ?  28  ILE C HB   1 
ATOM   2444 H  HG12 . ILE B 2 14  ? 10.341  -19.321 2.306   1.00 38.36  ?  28  ILE C HG12 1 
ATOM   2445 H  HG13 . ILE B 2 14  ? 10.714  -20.073 0.956   1.00 38.36  ?  28  ILE C HG13 1 
ATOM   2446 H  HG21 . ILE B 2 14  ? 10.067  -16.200 1.469   1.00 37.95  ?  28  ILE C HG21 1 
ATOM   2447 H  HG22 . ILE B 2 14  ? 11.627  -16.320 1.197   1.00 37.95  ?  28  ILE C HG22 1 
ATOM   2448 H  HG23 . ILE B 2 14  ? 10.985  -17.026 2.467   1.00 37.95  ?  28  ILE C HG23 1 
ATOM   2449 H  HD11 . ILE B 2 14  ? 12.477  -20.316 2.347   1.00 43.73  ?  28  ILE C HD11 1 
ATOM   2450 H  HD12 . ILE B 2 14  ? 12.506  -18.760 2.665   1.00 43.73  ?  28  ILE C HD12 1 
ATOM   2451 H  HD13 . ILE B 2 14  ? 12.928  -19.284 1.226   1.00 43.73  ?  28  ILE C HD13 1 
ATOM   2452 N  N    . ILE B 2 15  ? 8.043   -15.926 0.101   1.00 32.47  ?  29  ILE C N    1 
ATOM   2453 C  CA   . ILE B 2 15  ? 7.597   -14.669 -0.495  1.00 35.98  ?  29  ILE C CA   1 
ATOM   2454 C  C    . ILE B 2 15  ? 7.757   -13.577 0.572   1.00 43.51  ?  29  ILE C C    1 
ATOM   2455 O  O    . ILE B 2 15  ? 8.596   -13.685 1.478   1.00 40.77  ?  29  ILE C O    1 
ATOM   2456 C  CB   . ILE B 2 15  ? 6.157   -14.784 -1.035  1.00 38.65  ?  29  ILE C CB   1 
ATOM   2457 C  CG1  . ILE B 2 15  ? 5.866   -13.629 -2.002  1.00 46.36  ?  29  ILE C CG1  1 
ATOM   2458 C  CG2  . ILE B 2 15  ? 5.152   -14.831 0.109   1.00 37.56  ?  29  ILE C CG2  1 
ATOM   2459 C  CD1  . ILE B 2 15  ? 5.691   -12.274 -1.333  1.00 44.74  ?  29  ILE C CD1  1 
ATOM   2460 H  H    . ILE B 2 15  ? 7.789   -16.022 0.917   1.00 38.97  ?  29  ILE C H    1 
ATOM   2461 H  HA   . ILE B 2 15  ? 8.136   -14.432 -1.266  1.00 43.18  ?  29  ILE C HA   1 
ATOM   2462 H  HB   . ILE B 2 15  ? 6.072   -15.616 -1.527  1.00 46.38  ?  29  ILE C HB   1 
ATOM   2463 H  HG12 . ILE B 2 15  ? 6.605   -13.554 -2.626  1.00 55.63  ?  29  ILE C HG12 1 
ATOM   2464 H  HG13 . ILE B 2 15  ? 5.046   -13.827 -2.482  1.00 55.63  ?  29  ILE C HG13 1 
ATOM   2465 H  HG21 . ILE B 2 15  ? 5.201   -13.999 0.606   1.00 45.07  ?  29  ILE C HG21 1 
ATOM   2466 H  HG22 . ILE B 2 15  ? 4.262   -14.945 -0.258  1.00 45.07  ?  29  ILE C HG22 1 
ATOM   2467 H  HG23 . ILE B 2 15  ? 5.370   -15.577 0.689   1.00 45.07  ?  29  ILE C HG23 1 
ATOM   2468 H  HD11 . ILE B 2 15  ? 5.420   -11.625 -2.001  1.00 53.68  ?  29  ILE C HD11 1 
ATOM   2469 H  HD12 . ILE B 2 15  ? 6.534   -12.007 -0.935  1.00 53.68  ?  29  ILE C HD12 1 
ATOM   2470 H  HD13 . ILE B 2 15  ? 5.009   -12.346 -0.647  1.00 53.68  ?  29  ILE C HD13 1 
HETATM 2471 C  C1   . AKG C 3 .   ? 17.898  -14.201 1.577   1.00 32.64  ?  401 AKG A C1   1 
HETATM 2472 O  O1   . AKG C 3 .   ? 17.500  -13.318 0.807   1.00 27.02  ?  401 AKG A O1   1 
HETATM 2473 O  O2   . AKG C 3 .   ? 17.697  -14.191 2.894   1.00 37.34  ?  401 AKG A O2   1 
HETATM 2474 C  C2   . AKG C 3 .   ? 18.659  -15.436 1.036   1.00 31.84  ?  401 AKG A C2   1 
HETATM 2475 O  O5   . AKG C 3 .   ? 18.993  -15.453 -0.143  1.00 26.38  ?  401 AKG A O5   1 
HETATM 2476 C  C3   . AKG C 3 .   ? 18.910  -16.599 1.970   1.00 31.30  ?  401 AKG A C3   1 
HETATM 2477 C  C4   . AKG C 3 .   ? 20.300  -16.594 2.583   1.00 27.56  ?  401 AKG A C4   1 
HETATM 2478 C  C5   . AKG C 3 .   ? 20.471  -17.623 3.676   1.00 26.95  ?  401 AKG A C5   1 
HETATM 2479 O  O3   . AKG C 3 .   ? 19.599  -18.408 3.989   1.00 31.74  ?  401 AKG A O3   1 
HETATM 2480 O  O4   . AKG C 3 .   ? 21.631  -17.583 4.260   1.00 26.07  ?  401 AKG A O4   1 
HETATM 2481 H  H31  . AKG C 3 .   ? 18.797  -17.423 1.471   1.00 37.56  ?  401 AKG A H31  1 
HETATM 2482 H  H32  . AKG C 3 .   ? 18.258  -16.563 2.687   1.00 37.56  ?  401 AKG A H32  1 
HETATM 2483 H  H41  . AKG C 3 .   ? 20.468  -15.715 2.957   1.00 33.07  ?  401 AKG A H41  1 
HETATM 2484 H  H42  . AKG C 3 .   ? 20.945  -16.777 1.883   1.00 33.07  ?  401 AKG A H42  1 
HETATM 2485 FE FE   . FE  D 4 .   ? 18.124  -13.807 -1.216  1.00 19.14  ?  402 FE  A FE   1 
HETATM 2486 FE FE   . FE  E 4 .   ? 27.834  2.855   -4.798  1.00 24.52  ?  403 FE  A FE   1 
HETATM 2487 O  O    . HOH F 5 .   ? 30.540  -17.252 18.502  1.00 53.26  ?  501 HOH A O    1 
HETATM 2488 O  O    . HOH F 5 .   ? 8.846   4.850   19.020  1.00 47.34  ?  502 HOH A O    1 
HETATM 2489 O  O    . HOH F 5 .   ? 14.040  -30.703 14.484  1.00 44.18  ?  503 HOH A O    1 
HETATM 2490 O  O    . HOH F 5 .   ? 21.626  -21.191 22.100  1.00 50.12  ?  504 HOH A O    1 
HETATM 2491 O  O    . HOH F 5 .   ? -0.030  -7.742  -1.378  1.00 36.12  ?  505 HOH A O    1 
HETATM 2492 O  O    . HOH F 5 .   ? 10.703  4.059   22.725  1.00 55.53  ?  506 HOH A O    1 
HETATM 2493 O  O    . HOH F 5 .   ? 2.448   -9.776  0.738   1.00 33.84  ?  507 HOH A O    1 
HETATM 2494 O  O    . HOH F 5 .   ? 18.201  -20.014 3.024   1.00 44.25  ?  508 HOH A O    1 
HETATM 2495 O  O    . HOH F 5 .   ? -0.786  -7.240  5.960   1.00 33.73  ?  509 HOH A O    1 
HETATM 2496 O  O    . HOH F 5 .   ? 21.365  -30.422 16.773  1.00 49.89  ?  510 HOH A O    1 
HETATM 2497 O  O    . HOH F 5 .   ? 32.908  -9.947  2.478   1.00 44.57  ?  511 HOH A O    1 
HETATM 2498 O  O    . HOH F 5 .   ? 28.568  0.671   12.425  1.00 43.01  ?  512 HOH A O    1 
HETATM 2499 O  O    . HOH F 5 .   ? 31.529  -13.383 12.874  1.00 48.36  ?  513 HOH A O    1 
HETATM 2500 O  O    . HOH F 5 .   ? 2.181   5.709   26.277  1.00 54.54  ?  514 HOH A O    1 
HETATM 2501 O  O    . HOH F 5 .   ? 25.944  -24.174 14.984  1.00 43.92  ?  515 HOH A O    1 
HETATM 2502 O  O    . HOH F 5 .   ? 24.579  -12.098 21.759  1.00 41.91  ?  516 HOH A O    1 
HETATM 2503 O  O    . HOH F 5 .   ? 20.225  1.484   14.865  1.00 33.76  ?  517 HOH A O    1 
HETATM 2504 O  O    . HOH F 5 .   ? 33.214  -27.965 10.836  1.00 41.39  ?  518 HOH A O    1 
HETATM 2505 O  O    . HOH F 5 .   ? 15.673  -19.246 2.942   1.00 42.56  ?  519 HOH A O    1 
HETATM 2506 O  O    . HOH F 5 .   ? 8.564   -4.385  20.919  1.00 37.68  ?  520 HOH A O    1 
HETATM 2507 O  O    . HOH F 5 .   ? 25.041  -20.684 24.810  1.00 57.37  ?  521 HOH A O    1 
HETATM 2508 O  O    . HOH F 5 .   ? 14.838  -18.109 -18.660 1.00 42.96  ?  522 HOH A O    1 
HETATM 2509 O  O    . HOH F 5 .   ? 33.436  -5.446  -3.195  1.00 43.98  ?  523 HOH A O    1 
HETATM 2510 O  O    . HOH F 5 .   ? -12.421 -7.686  22.918  1.00 36.26  ?  524 HOH A O    1 
HETATM 2511 O  O    . HOH F 5 .   ? 1.893   5.611   3.022   1.00 32.06  ?  525 HOH A O    1 
HETATM 2512 O  O    . HOH F 5 .   ? -9.316  -8.921  20.807  1.00 27.91  ?  526 HOH A O    1 
HETATM 2513 O  O    . HOH F 5 .   ? 25.747  -16.529 7.551   1.00 25.61  ?  527 HOH A O    1 
HETATM 2514 O  O    . HOH F 5 .   ? 30.230  -24.936 -9.089  1.00 44.89  ?  528 HOH A O    1 
HETATM 2515 O  O    . HOH F 5 .   ? 28.924  -12.493 15.347  1.00 37.71  ?  529 HOH A O    1 
HETATM 2516 O  O    . HOH F 5 .   ? 20.048  -27.879 4.486   1.00 37.57  ?  530 HOH A O    1 
HETATM 2517 O  O    . HOH F 5 .   ? 12.909  -11.766 -1.356  1.00 34.92  ?  531 HOH A O    1 
HETATM 2518 O  O    . HOH F 5 .   ? 22.701  -36.222 2.648   1.00 50.85  ?  532 HOH A O    1 
HETATM 2519 O  O    . HOH F 5 .   ? 31.519  -20.211 -15.456 1.00 45.69  ?  533 HOH A O    1 
HETATM 2520 O  O    . HOH F 5 .   ? 8.588   -32.820 8.934   1.00 54.06  ?  534 HOH A O    1 
HETATM 2521 O  O    . HOH F 5 .   ? 19.091  -21.115 1.227   1.00 44.44  ?  535 HOH A O    1 
HETATM 2522 O  O    . HOH F 5 .   ? 20.462  -18.976 -17.315 1.00 41.28  ?  536 HOH A O    1 
HETATM 2523 O  O    . HOH F 5 .   ? 2.986   -20.021 13.648  1.00 28.11  ?  537 HOH A O    1 
HETATM 2524 O  O    . HOH F 5 .   ? 25.771  -30.178 -0.681  1.00 49.97  ?  538 HOH A O    1 
HETATM 2525 O  O    . HOH F 5 .   ? 21.127  -23.098 -0.276  1.00 44.76  ?  539 HOH A O    1 
HETATM 2526 O  O    . HOH F 5 .   ? 26.606  2.773   -3.157  1.00 28.06  ?  540 HOH A O    1 
HETATM 2527 O  O    . HOH F 5 .   ? 4.395   -7.355  -5.968  1.00 32.25  ?  541 HOH A O    1 
HETATM 2528 O  O    . HOH F 5 .   ? 33.051  -25.778 4.775   1.00 30.89  ?  542 HOH A O    1 
HETATM 2529 O  O    . HOH F 5 .   ? -17.277 3.610   12.023  1.00 37.91  ?  543 HOH A O    1 
HETATM 2530 O  O    . HOH F 5 .   ? 3.430   -10.101 -12.677 1.00 24.45  ?  544 HOH A O    1 
HETATM 2531 O  O    . HOH F 5 .   ? -5.587  10.808  14.835  1.00 31.64  ?  545 HOH A O    1 
HETATM 2532 O  O    . HOH F 5 .   ? 15.090  -25.631 5.054   1.00 31.26  ?  546 HOH A O    1 
HETATM 2533 O  O    . HOH F 5 .   ? 13.907  -6.793  19.447  1.00 32.85  ?  547 HOH A O    1 
HETATM 2534 O  O    . HOH F 5 .   ? 1.367   -18.193 14.682  1.00 34.72  ?  548 HOH A O    1 
HETATM 2535 O  O    . HOH F 5 .   ? 15.150  -14.282 -4.785  1.00 36.76  ?  549 HOH A O    1 
HETATM 2536 O  O    . HOH F 5 .   ? 1.199   3.799   14.347  1.00 25.39  ?  550 HOH A O    1 
HETATM 2537 O  O    . HOH F 5 .   ? 30.512  -6.932  12.372  1.00 44.09  ?  551 HOH A O    1 
HETATM 2538 O  O    . HOH F 5 .   ? 24.623  -9.287  -18.014 1.00 33.94  ?  552 HOH A O    1 
HETATM 2539 O  O    . HOH F 5 .   ? 18.861  9.488   5.201   1.00 43.27  ?  553 HOH A O    1 
HETATM 2540 O  O    . HOH F 5 .   ? -3.086  -8.312  26.713  1.00 34.52  ?  554 HOH A O    1 
HETATM 2541 O  O    . HOH F 5 .   ? 5.967   -8.312  -1.051  1.00 31.05  ?  555 HOH A O    1 
HETATM 2542 O  O    . HOH F 5 .   ? 17.642  9.292   9.601   1.00 49.41  ?  556 HOH A O    1 
HETATM 2543 O  O    . HOH F 5 .   ? 9.662   4.108   9.999   1.00 30.04  ?  557 HOH A O    1 
HETATM 2544 O  O    . HOH F 5 .   ? 23.054  -18.028 -18.135 1.00 39.61  ?  558 HOH A O    1 
HETATM 2545 O  O    . HOH F 5 .   ? 7.516   6.960   -5.641  1.00 31.82  ?  559 HOH A O    1 
HETATM 2546 O  O    . HOH F 5 .   ? 11.683  0.501   -0.879  1.00 18.94  ?  560 HOH A O    1 
HETATM 2547 O  O    . HOH F 5 .   ? 16.536  8.752   -4.732  1.00 37.75  ?  561 HOH A O    1 
HETATM 2548 O  O    . HOH F 5 .   ? 19.202  -15.831 29.621  1.00 48.24  ?  562 HOH A O    1 
HETATM 2549 O  O    . HOH F 5 .   ? 13.254  -9.756  -4.558  1.00 32.14  ?  563 HOH A O    1 
HETATM 2550 O  O    . HOH F 5 .   ? 20.060  -8.157  -18.749 1.00 34.05  ?  564 HOH A O    1 
HETATM 2551 O  O    . HOH F 5 .   ? 1.503   -15.538 6.000   1.00 30.77  ?  565 HOH A O    1 
HETATM 2552 O  O    . HOH F 5 .   ? -4.100  5.932   5.063   1.00 26.99  ?  566 HOH A O    1 
HETATM 2553 O  O    . HOH F 5 .   ? 5.807   -10.524 0.869   1.00 34.98  ?  567 HOH A O    1 
HETATM 2554 O  O    . HOH F 5 .   ? -15.887 5.840   12.088  1.00 36.49  ?  568 HOH A O    1 
HETATM 2555 O  O    . HOH F 5 .   ? -8.831  11.458  12.151  1.00 37.81  ?  569 HOH A O    1 
HETATM 2556 O  O    . HOH F 5 .   ? 5.740   -7.652  -3.519  1.00 27.21  ?  570 HOH A O    1 
HETATM 2557 O  O    . HOH F 5 .   ? -2.685  9.533   6.815   1.00 34.78  ?  571 HOH A O    1 
HETATM 2558 O  O    . HOH F 5 .   ? 1.724   -12.484 25.173  1.00 42.11  ?  572 HOH A O    1 
HETATM 2559 O  O    . HOH F 5 .   ? 6.976   -26.911 13.711  1.00 43.21  ?  573 HOH A O    1 
HETATM 2560 O  O    . HOH F 5 .   ? 35.467  -24.640 6.483   1.00 41.48  ?  574 HOH A O    1 
HETATM 2561 O  O    . HOH F 5 .   ? -1.938  -5.163  7.757   1.00 34.44  ?  575 HOH A O    1 
HETATM 2562 O  O    . HOH F 5 .   ? 0.900   8.298   24.808  1.00 48.63  ?  576 HOH A O    1 
HETATM 2563 O  O    . HOH F 5 .   ? 33.763  -18.650 -11.248 1.00 38.19  ?  577 HOH A O    1 
HETATM 2564 O  O    . HOH F 5 .   ? 1.019   4.174   11.676  1.00 23.47  ?  578 HOH A O    1 
HETATM 2565 O  O    . HOH F 5 .   ? 8.678   -13.368 -7.605  1.00 32.62  ?  579 HOH A O    1 
HETATM 2566 O  O    . HOH F 5 .   ? 31.917  1.007   4.314   1.00 47.19  ?  580 HOH A O    1 
HETATM 2567 O  O    . HOH F 5 .   ? 19.759  -24.716 18.940  1.00 44.89  ?  581 HOH A O    1 
HETATM 2568 O  O    . HOH F 5 .   ? -2.278  -16.702 21.056  1.00 31.01  ?  582 HOH A O    1 
HETATM 2569 O  O    . HOH F 5 .   ? 25.541  -21.579 -6.326  1.00 34.76  ?  583 HOH A O    1 
HETATM 2570 O  O    . HOH F 5 .   ? 41.764  -9.357  -9.073  1.00 55.80  ?  584 HOH A O    1 
HETATM 2571 O  O    . HOH F 5 .   ? -7.470  1.437   25.044  1.00 31.51  ?  585 HOH A O    1 
HETATM 2572 O  O    . HOH F 5 .   ? 10.928  -4.926  18.942  1.00 39.41  ?  586 HOH A O    1 
HETATM 2573 O  O    . HOH F 5 .   ? 23.930  -22.893 12.536  1.00 27.78  ?  587 HOH A O    1 
HETATM 2574 O  O    . HOH F 5 .   ? 13.726  -12.275 -5.117  1.00 41.23  ?  588 HOH A O    1 
HETATM 2575 O  O    . HOH F 5 .   ? 3.666   -4.997  6.787   1.00 29.74  ?  589 HOH A O    1 
HETATM 2576 O  O    . HOH F 5 .   ? 15.609  9.177   -0.141  1.00 36.49  ?  590 HOH A O    1 
HETATM 2577 O  O    . HOH F 5 .   ? 27.978  -34.163 6.129   1.00 35.48  ?  591 HOH A O    1 
HETATM 2578 O  O    . HOH F 5 .   ? 2.096   -9.327  -6.003  1.00 26.86  ?  592 HOH A O    1 
HETATM 2579 O  O    . HOH F 5 .   ? -1.255  -11.584 27.912  1.00 42.48  ?  593 HOH A O    1 
HETATM 2580 O  O    . HOH F 5 .   ? 22.390  2.649   -4.857  1.00 29.87  ?  594 HOH A O    1 
HETATM 2581 O  O    . HOH F 5 .   ? -8.729  -16.136 20.384  1.00 34.22  ?  595 HOH A O    1 
HETATM 2582 O  O    . HOH F 5 .   ? 32.438  -9.753  6.054   1.00 41.59  ?  596 HOH A O    1 
HETATM 2583 O  O    . HOH F 5 .   ? -0.588  0.255   26.715  1.00 45.24  ?  597 HOH A O    1 
HETATM 2584 O  O    . HOH F 5 .   ? -3.969  12.862  19.765  1.00 49.09  ?  598 HOH A O    1 
HETATM 2585 O  O    . HOH F 5 .   ? 11.585  -3.344  -6.372  1.00 18.38  ?  599 HOH A O    1 
HETATM 2586 O  O    . HOH F 5 .   ? -5.534  -7.258  26.081  1.00 31.86  ?  600 HOH A O    1 
HETATM 2587 O  O    . HOH F 5 .   ? 18.976  -31.747 4.654   1.00 36.40  ?  601 HOH A O    1 
HETATM 2588 O  O    . HOH F 5 .   ? 30.734  -5.861  -0.585  1.00 28.18  ?  602 HOH A O    1 
HETATM 2589 O  O    . HOH F 5 .   ? 8.012   -25.930 8.865   1.00 31.84  ?  603 HOH A O    1 
HETATM 2590 O  O    . HOH F 5 .   ? 27.893  -25.279 5.404   1.00 23.85  ?  604 HOH A O    1 
HETATM 2591 O  O    . HOH F 5 .   ? 29.589  -4.563  -16.508 1.00 40.56  ?  605 HOH A O    1 
HETATM 2592 O  O    . HOH F 5 .   ? -5.104  13.189  7.523   1.00 50.46  ?  606 HOH A O    1 
HETATM 2593 O  O    . HOH F 5 .   ? 2.714   -19.017 10.987  1.00 30.72  ?  607 HOH A O    1 
HETATM 2594 O  O    . HOH F 5 .   ? 34.625  -19.178 -5.148  1.00 43.21  ?  608 HOH A O    1 
HETATM 2595 O  O    . HOH F 5 .   ? 17.030  -20.972 6.085   1.00 30.90  ?  609 HOH A O    1 
HETATM 2596 O  O    . HOH F 5 .   ? 1.375   10.929  11.900  1.00 38.08  ?  610 HOH A O    1 
HETATM 2597 O  O    . HOH F 5 .   ? 30.790  -22.667 3.321   1.00 40.13  ?  611 HOH A O    1 
HETATM 2598 O  O    . HOH F 5 .   ? 32.963  -19.563 -3.146  1.00 42.71  ?  612 HOH A O    1 
HETATM 2599 O  O    . HOH F 5 .   ? -12.030 11.255  10.170  1.00 39.40  ?  613 HOH A O    1 
HETATM 2600 O  O    . HOH F 5 .   ? 21.554  -15.815 -14.944 1.00 26.29  ?  614 HOH A O    1 
HETATM 2601 O  O    . HOH F 5 .   ? 26.803  -15.597 20.387  1.00 44.16  ?  615 HOH A O    1 
HETATM 2602 O  O    . HOH F 5 .   ? 22.609  -3.045  -11.522 1.00 25.92  ?  616 HOH A O    1 
HETATM 2603 O  O    . HOH F 5 .   ? 33.974  -20.680 1.089   1.00 43.18  ?  617 HOH A O    1 
HETATM 2604 O  O    . HOH F 5 .   ? -0.033  0.523   23.724  1.00 29.75  ?  618 HOH A O    1 
HETATM 2605 O  O    . HOH F 5 .   ? 0.105   3.504   21.253  1.00 28.68  ?  619 HOH A O    1 
HETATM 2606 O  O    . HOH F 5 .   ? -10.779 0.431   15.172  1.00 24.48  ?  620 HOH A O    1 
HETATM 2607 O  O    . HOH F 5 .   ? 7.572   4.289   11.473  1.00 33.33  ?  621 HOH A O    1 
HETATM 2608 O  O    . HOH F 5 .   ? 10.230  -3.406  -3.936  1.00 17.71  ?  622 HOH A O    1 
HETATM 2609 O  O    . HOH F 5 .   ? 34.560  -27.694 6.124   1.00 29.78  ?  623 HOH A O    1 
HETATM 2610 O  O    . HOH F 5 .   ? 23.151  -1.822  -6.948  1.00 21.27  ?  624 HOH A O    1 
HETATM 2611 O  O    . HOH F 5 .   ? 7.885   -1.694  21.765  1.00 40.44  ?  625 HOH A O    1 
HETATM 2612 O  O    . HOH F 5 .   ? -0.026  -17.989 19.918  1.00 35.78  ?  626 HOH A O    1 
HETATM 2613 O  O    . HOH F 5 .   ? 18.746  -10.495 30.105  1.00 49.00  ?  627 HOH A O    1 
HETATM 2614 O  O    . HOH F 5 .   ? 16.150  -9.898  -19.546 1.00 34.13  ?  628 HOH A O    1 
HETATM 2615 O  O    . HOH F 5 .   ? 30.391  -10.928 19.613  1.00 51.98  ?  629 HOH A O    1 
HETATM 2616 O  O    . HOH F 5 .   ? 23.893  -25.663 13.339  1.00 33.17  ?  630 HOH A O    1 
HETATM 2617 O  O    . HOH F 5 .   ? 4.961   -23.129 6.323   1.00 30.63  ?  631 HOH A O    1 
HETATM 2618 O  O    . HOH F 5 .   ? 18.328  -4.786  -15.346 1.00 22.04  ?  632 HOH A O    1 
HETATM 2619 O  O    . HOH F 5 .   ? 22.353  3.632   -0.875  1.00 27.48  ?  633 HOH A O    1 
HETATM 2620 O  O    . HOH F 5 .   ? 11.343  -1.117  -3.062  1.00 20.13  ?  634 HOH A O    1 
HETATM 2621 O  O    . HOH F 5 .   ? 5.235   -22.839 18.053  1.00 36.90  ?  635 HOH A O    1 
HETATM 2622 O  O    . HOH F 5 .   ? -11.001 4.155   24.089  1.00 43.22  ?  636 HOH A O    1 
HETATM 2623 O  O    . HOH F 5 .   ? 11.807  -5.500  1.151   1.00 19.01  ?  637 HOH A O    1 
HETATM 2624 O  O    . HOH F 5 .   ? 10.147  -4.469  -8.457  1.00 17.67  ?  638 HOH A O    1 
HETATM 2625 O  O    . HOH F 5 .   ? 11.570  -24.359 23.371  1.00 40.43  ?  639 HOH A O    1 
HETATM 2626 O  O    . HOH F 5 .   ? 13.540  -11.998 4.293   1.00 30.68  ?  640 HOH A O    1 
HETATM 2627 O  O    . HOH F 5 .   ? -1.657  -15.961 10.506  1.00 36.54  ?  641 HOH A O    1 
HETATM 2628 O  O    . HOH F 5 .   ? 32.047  -1.689  -2.445  1.00 31.96  ?  642 HOH A O    1 
HETATM 2629 O  O    . HOH F 5 .   ? 20.965  -22.167 19.387  1.00 36.04  ?  643 HOH A O    1 
HETATM 2630 O  O    . HOH F 5 .   ? 2.610   1.322   -0.535  1.00 30.06  ?  644 HOH A O    1 
HETATM 2631 O  O    . HOH F 5 .   ? 3.604   -1.409  0.109   1.00 29.04  ?  645 HOH A O    1 
HETATM 2632 O  O    . HOH F 5 .   ? 1.266   -6.534  25.539  1.00 29.56  ?  646 HOH A O    1 
HETATM 2633 O  O    . HOH F 5 .   ? 2.484   1.597   22.860  1.00 34.42  ?  647 HOH A O    1 
HETATM 2634 O  O    . HOH F 5 .   ? 14.991  4.437   17.831  1.00 45.72  ?  648 HOH A O    1 
HETATM 2635 O  O    . HOH F 5 .   ? 12.313  -24.457 8.095   1.00 30.57  ?  649 HOH A O    1 
HETATM 2636 O  O    . HOH F 5 .   ? 34.700  -1.149  7.791   1.00 65.75  ?  650 HOH A O    1 
HETATM 2637 O  O    . HOH F 5 .   ? 0.273   0.123   3.319   1.00 31.54  ?  651 HOH A O    1 
HETATM 2638 O  O    . HOH F 5 .   ? 27.275  -12.856 -19.330 1.00 43.40  ?  652 HOH A O    1 
HETATM 2639 O  O    . HOH F 5 .   ? 0.884   -17.253 11.186  1.00 35.62  ?  653 HOH A O    1 
HETATM 2640 O  O    . HOH F 5 .   ? 31.701  -12.894 9.060   1.00 41.68  ?  654 HOH A O    1 
HETATM 2641 O  O    . HOH F 5 .   ? 30.246  -5.050  5.848   1.00 34.76  ?  655 HOH A O    1 
HETATM 2642 O  O    . HOH F 5 .   ? 13.355  -12.234 22.338  1.00 31.01  ?  656 HOH A O    1 
HETATM 2643 O  O    . HOH F 5 .   ? 6.233   4.215   -7.118  1.00 30.36  ?  657 HOH A O    1 
HETATM 2644 O  O    . HOH F 5 .   ? 22.420  -20.446 3.833   1.00 23.70  ?  658 HOH A O    1 
HETATM 2645 O  O    . HOH F 5 .   ? 26.833  -0.545  -12.910 1.00 44.06  ?  659 HOH A O    1 
HETATM 2646 O  O    . HOH F 5 .   ? 15.844  -3.679  21.178  1.00 40.46  ?  660 HOH A O    1 
HETATM 2647 O  O    . HOH F 5 .   ? 31.021  -18.540 13.895  1.00 40.91  ?  661 HOH A O    1 
HETATM 2648 O  O    . HOH F 5 .   ? 9.262   10.573  3.486   1.00 43.37  ?  662 HOH A O    1 
HETATM 2649 O  O    . HOH F 5 .   ? 0.449   11.508  17.991  1.00 46.58  ?  663 HOH A O    1 
HETATM 2650 O  O    . HOH F 5 .   ? 11.529  -28.275 20.916  1.00 45.89  ?  664 HOH A O    1 
HETATM 2651 O  O    . HOH F 5 .   ? 16.254  -14.795 -1.298  1.00 27.94  ?  665 HOH A O    1 
HETATM 2652 O  O    . HOH F 5 .   ? -18.970 6.740   12.696  1.00 52.37  ?  666 HOH A O    1 
HETATM 2653 O  O    . HOH F 5 .   ? 17.488  7.016   11.427  1.00 41.38  ?  667 HOH A O    1 
HETATM 2654 O  O    . HOH F 5 .   ? 26.312  -12.408 18.446  1.00 38.49  ?  668 HOH A O    1 
HETATM 2655 O  O    . HOH F 5 .   ? 30.210  2.956   8.112   1.00 37.94  ?  669 HOH A O    1 
HETATM 2656 O  O    . HOH F 5 .   ? 10.404  -18.206 24.511  1.00 34.00  ?  670 HOH A O    1 
HETATM 2657 O  O    . HOH F 5 .   ? 21.941  -21.539 -13.862 1.00 40.32  ?  671 HOH A O    1 
HETATM 2658 O  O    . HOH F 5 .   ? -5.772  10.341  6.056   1.00 35.39  ?  672 HOH A O    1 
HETATM 2659 O  O    . HOH F 5 .   ? 21.540  -27.843 15.647  1.00 39.49  ?  673 HOH A O    1 
HETATM 2660 O  O    . HOH F 5 .   ? -12.099 12.338  12.945  1.00 48.43  ?  674 HOH A O    1 
HETATM 2661 O  O    . HOH F 5 .   ? 28.409  -23.620 2.790   1.00 33.89  ?  675 HOH A O    1 
HETATM 2662 O  O    . HOH F 5 .   ? -10.332 -12.863 20.889  1.00 44.23  ?  676 HOH A O    1 
HETATM 2663 O  O    . HOH F 5 .   ? 26.913  -0.045  15.048  1.00 44.68  ?  677 HOH A O    1 
HETATM 2664 O  O    . HOH F 5 .   ? -6.012  -16.327 21.104  1.00 33.21  ?  678 HOH A O    1 
HETATM 2665 O  O    . HOH F 5 .   ? 18.752  1.737   -9.734  1.00 31.69  ?  679 HOH A O    1 
HETATM 2666 O  O    . HOH F 5 .   ? 22.394  -1.697  20.248  1.00 49.74  ?  680 HOH A O    1 
HETATM 2667 O  O    . HOH F 5 .   ? 16.959  -20.998 24.968  1.00 40.12  ?  681 HOH A O    1 
HETATM 2668 O  O    . HOH F 5 .   ? 16.252  -13.584 -7.336  1.00 30.81  ?  682 HOH A O    1 
HETATM 2669 O  O    . HOH F 5 .   ? 2.411   -14.371 2.725   1.00 24.12  ?  683 HOH A O    1 
HETATM 2670 O  O    . HOH F 5 .   ? 1.197   2.629   8.044   1.00 20.28  ?  684 HOH A O    1 
HETATM 2671 O  O    . HOH F 5 .   ? 13.957  -15.819 30.244  1.00 52.68  ?  685 HOH A O    1 
HETATM 2672 O  O    . HOH F 5 .   ? 1.963   4.597   22.694  1.00 35.09  ?  686 HOH A O    1 
HETATM 2673 O  O    . HOH F 5 .   ? 14.558  -13.628 -9.377  1.00 28.34  ?  687 HOH A O    1 
HETATM 2674 O  O    . HOH F 5 .   ? 17.447  -2.685  -2.794  1.00 21.10  ?  688 HOH A O    1 
HETATM 2675 O  O    . HOH F 5 .   ? 14.736  -10.299 -6.908  1.00 28.83  ?  689 HOH A O    1 
HETATM 2676 O  O    . HOH F 5 .   ? 6.419   5.625   18.295  1.00 31.16  ?  690 HOH A O    1 
HETATM 2677 O  O    . HOH F 5 .   ? -8.385  -0.395  26.522  1.00 31.81  ?  691 HOH A O    1 
HETATM 2678 O  O    . HOH F 5 .   ? -4.745  2.460   27.612  1.00 44.73  ?  692 HOH A O    1 
HETATM 2679 O  O    . HOH F 5 .   ? 21.827  -15.362 26.231  1.00 41.01  ?  693 HOH A O    1 
HETATM 2680 O  O    . HOH F 5 .   ? -15.416 11.268  15.607  1.00 39.92  ?  694 HOH A O    1 
HETATM 2681 O  O    . HOH F 5 .   ? 24.458  7.115   6.904   1.00 44.23  ?  695 HOH A O    1 
HETATM 2682 O  O    . HOH F 5 .   ? 9.597   -1.812  -15.619 1.00 21.76  ?  696 HOH A O    1 
HETATM 2683 O  O    . HOH F 5 .   ? 2.185   -14.966 23.573  1.00 35.69  ?  697 HOH A O    1 
HETATM 2684 O  O    . HOH F 5 .   ? -1.222  -1.847  28.396  1.00 46.27  ?  698 HOH A O    1 
HETATM 2685 O  O    . HOH F 5 .   ? -12.516 -19.117 19.188  1.00 45.10  ?  699 HOH A O    1 
HETATM 2686 O  O    . HOH F 5 .   ? 6.015   -27.967 19.276  1.00 55.97  ?  700 HOH A O    1 
HETATM 2687 O  O    . HOH F 5 .   ? 15.430  9.408   7.399   1.00 47.37  ?  701 HOH A O    1 
HETATM 2688 O  O    . HOH F 5 .   ? 12.888  -0.818  -6.256  1.00 19.46  ?  702 HOH A O    1 
HETATM 2689 O  O    . HOH F 5 .   ? -2.251  7.524   -6.161  1.00 33.16  ?  703 HOH A O    1 
HETATM 2690 O  O    . HOH F 5 .   ? -13.740 -3.760  17.976  1.00 36.05  ?  704 HOH A O    1 
HETATM 2691 O  O    . HOH F 5 .   ? 30.871  -21.087 -5.994  1.00 47.68  ?  705 HOH A O    1 
HETATM 2692 O  O    . HOH F 5 .   ? -1.673  11.672  9.134   1.00 39.74  ?  706 HOH A O    1 
HETATM 2693 O  O    . HOH F 5 .   ? 31.877  -19.304 -17.976 1.00 45.51  ?  707 HOH A O    1 
HETATM 2694 O  O    . HOH F 5 .   ? -14.269 0.754   23.521  1.00 37.81  ?  708 HOH A O    1 
HETATM 2695 O  O    . HOH F 5 .   ? 31.582  -12.630 -14.770 1.00 38.14  ?  709 HOH A O    1 
HETATM 2696 O  O    . HOH F 5 .   ? 1.370   -6.280  6.781   1.00 34.42  ?  710 HOH A O    1 
HETATM 2697 O  O    . HOH F 5 .   ? 4.400   -17.847 23.427  1.00 47.51  ?  711 HOH A O    1 
HETATM 2698 O  O    . HOH F 5 .   ? 29.921  -6.226  8.407   1.00 34.60  ?  712 HOH A O    1 
HETATM 2699 O  O    . HOH F 5 .   ? 18.074  -21.202 8.544   1.00 25.41  ?  713 HOH A O    1 
HETATM 2700 O  O    . HOH F 5 .   ? -5.753  -17.989 9.699   1.00 45.15  ?  714 HOH A O    1 
HETATM 2701 O  O    . HOH F 5 .   ? -3.102  -5.021  27.909  1.00 44.61  ?  715 HOH A O    1 
HETATM 2702 O  O    . HOH F 5 .   ? 16.174  -11.962 4.922   1.00 28.62  ?  716 HOH A O    1 
HETATM 2703 O  O    . HOH F 5 .   ? 26.954  -7.725  -16.745 1.00 36.36  ?  717 HOH A O    1 
HETATM 2704 O  O    . HOH F 5 .   ? -1.400  -18.232 12.274  1.00 45.79  ?  718 HOH A O    1 
HETATM 2705 O  O    . HOH F 5 .   ? 12.970  -9.589  23.330  1.00 37.87  ?  719 HOH A O    1 
HETATM 2706 O  O    . HOH F 5 .   ? 3.766   -12.096 2.371   1.00 27.53  ?  720 HOH A O    1 
HETATM 2707 O  O    . HOH F 5 .   ? -17.284 8.393   15.294  1.00 40.03  ?  721 HOH A O    1 
HETATM 2708 O  O    . HOH F 5 .   ? 12.834  -2.097  19.885  1.00 33.72  ?  722 HOH A O    1 
HETATM 2709 O  O    . HOH F 5 .   ? 14.142  8.380   -3.224  1.00 30.09  ?  723 HOH A O    1 
HETATM 2710 O  O    . HOH F 5 .   ? 18.728  -20.843 -6.520  1.00 39.52  ?  724 HOH A O    1 
HETATM 2711 O  O    . HOH F 5 .   ? 19.251  -24.274 -4.923  1.00 52.48  ?  725 HOH A O    1 
HETATM 2712 O  O    . HOH F 5 .   ? 0.949   -16.331 8.591   1.00 29.64  ?  726 HOH A O    1 
HETATM 2713 O  O    . HOH F 5 .   ? 3.743   -10.944 24.665  1.00 32.68  ?  727 HOH A O    1 
HETATM 2714 O  O    . HOH F 5 .   ? 2.373   4.899   -1.655  1.00 36.28  ?  728 HOH A O    1 
HETATM 2715 O  O    . HOH F 5 .   ? 0.305   -14.589 16.394  1.00 30.22  ?  729 HOH A O    1 
HETATM 2716 O  O    . HOH F 5 .   ? 13.798  10.385  -8.283  1.00 42.84  ?  730 HOH A O    1 
HETATM 2717 O  O    . HOH F 5 .   ? 12.147  -10.327 -11.726 1.00 31.82  ?  731 HOH A O    1 
HETATM 2718 O  O    . HOH F 5 .   ? 26.292  -30.501 2.122   1.00 35.96  ?  732 HOH A O    1 
HETATM 2719 O  O    . HOH F 5 .   ? 11.411  -12.373 5.230   1.00 35.20  ?  733 HOH A O    1 
HETATM 2720 O  O    . HOH F 5 .   ? 20.195  -2.964  -13.288 1.00 28.49  ?  734 HOH A O    1 
HETATM 2721 O  O    . HOH F 5 .   ? -10.082 -18.105 12.873  1.00 40.09  ?  735 HOH A O    1 
HETATM 2722 O  O    . HOH F 5 .   ? 19.178  -7.922  23.444  1.00 39.05  ?  736 HOH A O    1 
HETATM 2723 O  O    . HOH F 5 .   ? 33.920  -21.329 10.302  1.00 36.18  ?  737 HOH A O    1 
HETATM 2724 O  O    . HOH F 5 .   ? 9.907   -10.450 0.149   1.00 29.32  ?  738 HOH A O    1 
HETATM 2725 O  O    . HOH F 5 .   ? -9.056  -10.733 22.883  1.00 38.04  ?  739 HOH A O    1 
HETATM 2726 O  O    . HOH F 5 .   ? 21.138  -14.675 -17.476 1.00 31.01  ?  740 HOH A O    1 
HETATM 2727 O  O    . HOH F 5 .   ? 31.153  -8.855  -11.923 1.00 36.76  ?  741 HOH A O    1 
HETATM 2728 O  O    . HOH F 5 .   ? 16.779  -28.002 5.209   1.00 32.30  ?  742 HOH A O    1 
HETATM 2729 O  O    . HOH F 5 .   ? -8.233  -13.999 4.909   1.00 40.72  ?  743 HOH A O    1 
HETATM 2730 O  O    . HOH F 5 .   ? 5.787   7.869   7.696   1.00 37.99  ?  744 HOH A O    1 
HETATM 2731 O  O    . HOH F 5 .   ? 21.229  -6.325  22.618  1.00 47.10  ?  745 HOH A O    1 
HETATM 2732 O  O    . HOH F 5 .   ? 24.399  -21.871 -12.591 1.00 35.48  ?  746 HOH A O    1 
HETATM 2733 O  O    . HOH F 5 .   ? 30.546  -0.497  -11.671 1.00 41.19  ?  747 HOH A O    1 
HETATM 2734 O  O    . HOH F 5 .   ? 9.671   10.618  5.971   1.00 41.85  ?  748 HOH A O    1 
HETATM 2735 O  O    . HOH F 5 .   ? 10.384  -11.318 -8.342  1.00 36.18  ?  749 HOH A O    1 
HETATM 2736 O  O    . HOH F 5 .   ? -5.201  4.891   26.198  1.00 36.79  ?  750 HOH A O    1 
HETATM 2737 O  O    . HOH F 5 .   ? 27.455  -30.761 12.087  1.00 48.37  ?  751 HOH A O    1 
HETATM 2738 O  O    . HOH F 5 .   ? 15.674  -2.535  -5.012  1.00 24.23  ?  752 HOH A O    1 
HETATM 2739 O  O    . HOH F 5 .   ? 32.497  -11.913 4.676   1.00 50.08  ?  753 HOH A O    1 
HETATM 2740 O  O    . HOH F 5 .   ? 24.280  -22.717 18.497  1.00 41.75  ?  754 HOH A O    1 
HETATM 2741 O  O    . HOH F 5 .   ? 21.494  -21.369 -16.459 1.00 44.85  ?  755 HOH A O    1 
HETATM 2742 O  O    . HOH F 5 .   ? 21.789  6.793   3.263   1.00 46.30  ?  756 HOH A O    1 
HETATM 2743 O  O    . HOH F 5 .   ? 2.900   7.032   -3.235  1.00 40.71  ?  757 HOH A O    1 
HETATM 2744 O  O    . HOH F 5 .   ? 24.224  -13.324 25.797  1.00 53.85  ?  758 HOH A O    1 
HETATM 2745 O  O    . HOH F 5 .   ? 18.967  8.751   -8.225  1.00 51.41  ?  759 HOH A O    1 
HETATM 2746 O  O    . HOH F 5 .   ? 5.412   -27.607 6.484   1.00 52.96  ?  760 HOH A O    1 
HETATM 2747 O  O    . HOH F 5 .   ? 27.932  -33.426 12.240  1.00 43.99  ?  761 HOH A O    1 
HETATM 2748 O  O    . HOH F 5 .   ? 34.366  -18.409 -1.007  1.00 45.18  ?  762 HOH A O    1 
HETATM 2749 O  O    . HOH F 5 .   ? 14.854  -28.745 21.329  1.00 48.07  ?  763 HOH A O    1 
HETATM 2750 O  O    . HOH F 5 .   ? 27.692  -22.618 -5.517  1.00 39.98  ?  764 HOH A O    1 
HETATM 2751 O  O    . HOH F 5 .   ? 23.564  5.605   4.030   1.00 41.64  ?  765 HOH A O    1 
HETATM 2752 O  O    . HOH F 5 .   ? 28.594  -28.406 11.074  1.00 41.70  ?  766 HOH A O    1 
HETATM 2753 O  O    . HOH F 5 .   ? 16.970  -11.822 -23.130 1.00 49.41  ?  767 HOH A O    1 
HETATM 2754 O  O    . HOH F 5 .   ? 8.339   -8.310  -2.397  1.00 24.23  ?  768 HOH A O    1 
HETATM 2755 O  O    . HOH F 5 .   ? -6.046  -14.525 25.500  1.00 51.06  ?  769 HOH A O    1 
HETATM 2756 O  O    . HOH F 5 .   ? 11.757  9.254   -4.737  1.00 35.72  ?  770 HOH A O    1 
HETATM 2757 O  O    . HOH F 5 .   ? 17.240  7.515   -10.220 1.00 46.03  ?  771 HOH A O    1 
HETATM 2758 O  O    . HOH F 5 .   ? 6.354   6.659   10.408  1.00 40.45  ?  772 HOH A O    1 
HETATM 2759 O  O    . HOH F 5 .   ? 0.349   2.092   1.579   1.00 38.52  ?  773 HOH A O    1 
HETATM 2760 O  O    . HOH F 5 .   ? 14.416  -13.712 1.876   1.00 39.41  ?  774 HOH A O    1 
HETATM 2761 O  O    . HOH F 5 .   ? 24.711  -23.572 -7.955  1.00 43.23  ?  775 HOH A O    1 
HETATM 2762 O  O    . HOH F 5 .   ? 15.468  -16.447 1.961   1.00 44.62  ?  776 HOH A O    1 
HETATM 2763 O  O    . HOH F 5 .   ? 16.841  2.968   17.828  1.00 41.95  ?  777 HOH A O    1 
HETATM 2764 O  O    . HOH F 5 .   ? 21.315  1.100   19.745  1.00 48.45  ?  778 HOH A O    1 
HETATM 2765 O  O    . HOH F 5 .   ? 11.056  5.671   18.777  1.00 43.04  ?  779 HOH A O    1 
HETATM 2766 O  O    . HOH F 5 .   ? 36.535  -8.204  -4.734  1.00 54.88  ?  780 HOH A O    1 
HETATM 2767 O  O    . HOH F 5 .   ? -7.977  -16.721 11.482  1.00 36.16  ?  781 HOH A O    1 
HETATM 2768 O  O    . HOH F 5 .   ? 14.117  9.594   10.012  1.00 49.91  ?  782 HOH A O    1 
HETATM 2769 O  O    . HOH F 5 .   ? 12.606  -4.861  20.397  1.00 41.87  ?  783 HOH A O    1 
HETATM 2770 O  O    . HOH F 5 .   ? -12.430 -13.408 20.361  1.00 44.59  ?  784 HOH A O    1 
HETATM 2771 O  O    . HOH F 5 .   ? 24.303  4.106   -3.170  1.00 35.56  ?  785 HOH A O    1 
HETATM 2772 O  O    . HOH F 5 .   ? 26.777  -37.944 4.865   1.00 53.54  ?  786 HOH A O    1 
HETATM 2773 O  O    . HOH F 5 .   ? 16.110  -17.348 -3.378  1.00 44.67  ?  787 HOH A O    1 
HETATM 2774 O  O    . HOH F 5 .   ? 31.527  -15.888 14.576  1.00 46.10  ?  788 HOH A O    1 
HETATM 2775 O  O    . HOH F 5 .   ? 31.074  2.794   5.208   1.00 42.08  ?  789 HOH A O    1 
HETATM 2776 O  O    . HOH F 5 .   ? 1.807   -1.665  26.968  1.00 53.64  ?  790 HOH A O    1 
HETATM 2777 O  O    . HOH F 5 .   ? 19.796  2.592   17.196  1.00 40.98  ?  791 HOH A O    1 
HETATM 2778 O  O    . HOH F 5 .   ? 17.836  -20.976 -8.327  1.00 50.86  ?  792 HOH A O    1 
HETATM 2779 O  O    . HOH F 5 .   ? 17.661  -5.249  -17.945 1.00 36.53  ?  793 HOH A O    1 
HETATM 2780 O  O    . HOH F 5 .   ? -13.606 -6.278  19.727  1.00 36.44  ?  794 HOH A O    1 
HETATM 2781 O  O    . HOH F 5 .   ? 28.790  7.084   9.315   1.00 47.66  ?  795 HOH A O    1 
HETATM 2782 O  O    . HOH F 5 .   ? -10.540 -19.436 14.286  1.00 49.08  ?  796 HOH A O    1 
HETATM 2783 O  O    . HOH F 5 .   ? -11.892 -20.782 15.749  1.00 52.21  ?  797 HOH A O    1 
HETATM 2784 O  O    . HOH F 5 .   ? 19.602  -16.775 -20.839 1.00 49.58  ?  798 HOH A O    1 
HETATM 2785 O  O    . HOH F 5 .   ? 8.944   -20.224 23.747  1.00 39.06  ?  799 HOH A O    1 
HETATM 2786 O  O    . HOH F 5 .   ? 6.434   9.923   3.250   1.00 45.58  ?  800 HOH A O    1 
HETATM 2787 O  O    . HOH F 5 .   ? 21.511  -1.962  -9.089  1.00 25.17  ?  801 HOH A O    1 
HETATM 2788 O  O    . HOH F 5 .   ? 16.562  -16.505 -6.186  1.00 42.48  ?  802 HOH A O    1 
HETATM 2789 O  O    . HOH F 5 .   ? -8.639  -15.924 8.945   1.00 38.89  ?  803 HOH A O    1 
HETATM 2790 O  O    . HOH F 5 .   ? 18.936  9.096   -3.223  1.00 45.02  ?  804 HOH A O    1 
HETATM 2791 O  O    . HOH F 5 .   ? -2.577  -16.227 23.800  1.00 44.25  ?  805 HOH A O    1 
HETATM 2792 O  O    . HOH F 5 .   ? 25.324  -18.906 -20.016 1.00 54.32  ?  806 HOH A O    1 
HETATM 2793 O  O    . HOH F 5 .   ? 23.949  0.857   -6.229  1.00 26.73  ?  807 HOH A O    1 
HETATM 2794 O  O    . HOH F 5 .   ? 16.068  -18.695 -8.817  1.00 56.05  ?  808 HOH A O    1 
HETATM 2795 O  O    . HOH F 5 .   ? 30.225  -19.226 16.214  1.00 45.64  ?  809 HOH A O    1 
HETATM 2796 O  O    . HOH F 5 .   ? 2.474   -4.318  26.743  1.00 38.05  ?  810 HOH A O    1 
HETATM 2797 O  O    . HOH F 5 .   ? 3.871   -23.612 20.363  1.00 46.13  ?  811 HOH A O    1 
HETATM 2798 O  O    . HOH F 5 .   ? 14.245  -7.449  22.214  1.00 42.45  ?  812 HOH A O    1 
HETATM 2799 O  O    . HOH F 5 .   ? 6.394   -12.850 25.076  1.00 51.14  ?  813 HOH A O    1 
HETATM 2800 O  O    . HOH F 5 .   ? 9.487   -22.975 24.825  1.00 46.64  ?  814 HOH A O    1 
HETATM 2801 O  O    . HOH F 5 .   ? 16.476  -24.333 2.826   1.00 38.19  ?  815 HOH A O    1 
HETATM 2802 O  O    . HOH F 5 .   ? 13.073  -11.675 -9.139  1.00 34.81  ?  816 HOH A O    1 
HETATM 2803 O  O    . HOH F 5 .   ? 16.664  -6.963  22.602  1.00 54.50  ?  817 HOH A O    1 
HETATM 2804 O  O    . HOH F 5 .   ? 2.245   -22.557 14.295  1.00 41.91  ?  818 HOH A O    1 
HETATM 2805 O  O    . HOH F 5 .   ? 11.085  -1.239  21.681  1.00 42.13  ?  819 HOH A O    1 
HETATM 2806 O  O    . HOH F 5 .   ? -0.928  -6.845  27.227  1.00 38.66  ?  820 HOH A O    1 
HETATM 2807 O  O    . HOH F 5 .   ? -8.053  3.462   26.669  1.00 51.14  ?  821 HOH A O    1 
HETATM 2808 O  O    . HOH F 5 .   ? -6.789  8.817   4.137   1.00 40.88  ?  822 HOH A O    1 
HETATM 2809 O  O    . HOH F 5 .   ? -12.006 -8.791  20.235  1.00 34.58  ?  823 HOH A O    1 
HETATM 2810 O  O    . HOH F 5 .   ? 12.560  -32.657 14.898  1.00 49.53  ?  824 HOH A O    1 
HETATM 2811 O  O    . HOH F 5 .   ? 9.018   -15.547 25.567  1.00 41.12  ?  825 HOH A O    1 
HETATM 2812 O  O    . HOH F 5 .   ? 9.088   -11.955 -3.163  1.00 43.30  ?  826 HOH A O    1 
HETATM 2813 O  O    . HOH F 5 .   ? 1.084   4.308   0.630   1.00 40.60  ?  827 HOH A O    1 
HETATM 2814 O  O    . HOH F 5 .   ? -20.264 -2.989  15.841  1.00 40.37  ?  828 HOH A O    1 
HETATM 2815 O  O    . HOH F 5 .   ? 21.935  -15.215 29.452  1.00 55.54  ?  829 HOH A O    1 
HETATM 2816 O  O    . HOH F 5 .   ? 15.691  11.112  -6.204  1.00 50.95  ?  830 HOH A O    1 
HETATM 2817 O  O    . HOH F 5 .   ? 6.711   -19.982 22.669  1.00 41.19  ?  831 HOH A O    1 
HETATM 2818 O  O    . HOH F 5 .   ? 6.834   -25.942 11.465  1.00 45.45  ?  832 HOH A O    1 
HETATM 2819 O  O    . HOH F 5 .   ? 1.368   -1.731  1.663   1.00 37.59  ?  833 HOH A O    1 
HETATM 2820 O  O    . HOH F 5 .   ? 28.844  0.985   16.826  1.00 54.92  ?  834 HOH A O    1 
HETATM 2821 O  O    . HOH F 5 .   ? -7.077  -11.652 28.182  1.00 53.16  ?  835 HOH A O    1 
HETATM 2822 O  O    . HOH F 5 .   ? 29.359  -9.228  -15.815 1.00 41.40  ?  836 HOH A O    1 
HETATM 2823 O  O    . HOH F 5 .   ? 1.531   -10.287 28.560  1.00 47.84  ?  837 HOH A O    1 
HETATM 2824 O  O    . HOH F 5 .   ? 30.065  -10.799 -13.490 1.00 37.34  ?  838 HOH A O    1 
HETATM 2825 O  O    . HOH F 5 .   ? 12.581  5.305   21.213  1.00 59.16  ?  839 HOH A O    1 
HETATM 2826 O  O    . HOH F 5 .   ? -3.002  -10.070 28.881  1.00 41.81  ?  840 HOH A O    1 
HETATM 2827 O  O    . HOH F 5 .   ? 22.146  -15.776 -19.640 1.00 42.22  ?  841 HOH A O    1 
HETATM 2828 O  O    . HOH F 5 .   ? 19.236  -8.300  -21.170 1.00 38.66  ?  842 HOH A O    1 
HETATM 2829 O  O    . HOH F 5 .   ? -14.119 -20.013 14.609  1.00 56.08  ?  843 HOH A O    1 
HETATM 2830 O  O    . HOH F 5 .   ? 16.217  1.385   20.428  1.00 42.90  ?  844 HOH A O    1 
HETATM 2831 O  O    . HOH F 5 .   ? 33.309  -19.391 12.756  1.00 44.82  ?  845 HOH A O    1 
HETATM 2832 O  O    . HOH F 5 .   ? 11.896  -14.267 -4.435  1.00 49.14  ?  846 HOH A O    1 
HETATM 2833 O  O    . HOH F 5 .   ? 22.945  5.876   0.948   1.00 42.75  ?  847 HOH A O    1 
HETATM 2834 O  O    . HOH F 5 .   ? 5.227   -25.421 8.003   1.00 40.72  ?  848 HOH A O    1 
HETATM 2835 O  O    . HOH F 5 .   ? 5.870   -18.891 24.450  1.00 50.74  ?  849 HOH A O    1 
HETATM 2836 O  O    . HOH F 5 .   ? 13.476  -10.495 -19.454 1.00 38.31  ?  850 HOH A O    1 
HETATM 2837 O  O    . HOH F 5 .   ? 3.294   9.287   10.519  1.00 46.71  ?  851 HOH A O    1 
HETATM 2838 O  O    . HOH F 5 .   ? 24.237  -0.903  -12.831 1.00 40.34  ?  852 HOH A O    1 
HETATM 2839 O  O    . HOH F 5 .   ? -5.677  -16.033 24.338  1.00 50.52  ?  853 HOH A O    1 
HETATM 2840 O  O    . HOH F 5 .   ? 0.855   -13.525 28.825  1.00 48.07  ?  854 HOH A O    1 
HETATM 2841 O  O    . HOH F 5 .   ? 3.830   6.475   22.238  1.00 43.76  ?  855 HOH A O    1 
HETATM 2842 O  O    . HOH F 5 .   ? 21.090  0.595   -10.077 1.00 35.82  ?  856 HOH A O    1 
HETATM 2843 O  O    . HOH F 5 .   ? 3.691   -24.164 15.980  1.00 50.04  ?  857 HOH A O    1 
HETATM 2844 O  O    . HOH F 5 .   ? 22.703  -7.764  -19.423 1.00 35.37  ?  858 HOH A O    1 
HETATM 2845 O  O    . HOH F 5 .   ? 11.260  -18.946 27.009  1.00 40.45  ?  859 HOH A O    1 
HETATM 2846 O  O    . HOH F 5 .   ? 35.330  -10.737 2.388   1.00 55.39  ?  860 HOH A O    1 
HETATM 2847 O  O    . HOH F 5 .   ? 19.387  -19.892 -19.496 1.00 48.31  ?  861 HOH A O    1 
HETATM 2848 O  O    . HOH F 5 .   ? 14.322  4.559   20.365  1.00 56.74  ?  862 HOH A O    1 
HETATM 2849 O  O    . HOH F 5 .   ? 30.967  -11.109 14.436  1.00 47.68  ?  863 HOH A O    1 
HETATM 2850 O  O    . HOH F 5 .   ? 26.827  -2.774  14.854  1.00 44.44  ?  864 HOH A O    1 
HETATM 2851 O  O    . HOH F 5 .   ? 2.588   -22.080 7.004   1.00 33.37  ?  865 HOH A O    1 
HETATM 2852 O  O    . HOH F 5 .   ? 1.977   -21.311 9.502   1.00 37.76  ?  866 HOH A O    1 
HETATM 2853 O  O    . HOH F 5 .   ? 19.070  1.322   21.200  1.00 47.43  ?  867 HOH A O    1 
HETATM 2854 O  O    . HOH F 5 .   ? 13.462  -4.540  23.075  1.00 50.75  ?  868 HOH A O    1 
HETATM 2855 O  O    . HOH F 5 .   ? 37.808  -28.069 8.850   1.00 41.62  ?  869 HOH A O    1 
HETATM 2856 O  O    . HOH F 5 .   ? 35.133  -8.941  7.364   1.00 58.72  ?  870 HOH A O    1 
HETATM 2857 O  O    . HOH F 5 .   ? 0.000   -8.352  29.366  1.00 51.21  ?  871 HOH A O    1 
HETATM 2858 O  O    . HOH F 5 .   ? 24.165  -14.200 -20.826 1.00 47.76  ?  872 HOH A O    1 
HETATM 2859 O  O    . HOH F 5 .   ? 5.113   -25.116 12.253  1.00 47.98  ?  873 HOH A O    1 
HETATM 2860 O  O    . HOH F 5 .   ? 3.220   8.800   17.797  1.00 47.14  ?  874 HOH A O    1 
HETATM 2861 O  O    . HOH F 5 .   ? 3.588   8.507   20.340  1.00 53.02  ?  875 HOH A O    1 
HETATM 2862 O  O    . HOH F 5 .   ? 32.424  -10.651 16.771  1.00 56.94  ?  876 HOH A O    1 
HETATM 2863 O  O    . HOH F 5 .   ? 7.213   -24.433 25.071  1.00 53.95  ?  877 HOH A O    1 
HETATM 2864 O  O    . HOH F 5 .   ? 35.710  -17.841 12.699  1.00 54.87  ?  878 HOH A O    1 
HETATM 2865 O  O    . HOH G 5 .   ? 0.664   -22.114 -3.739  1.00 41.44  ?  101 HOH C O    1 
HETATM 2866 O  O    . HOH G 5 .   ? 1.743   -16.509 -7.542  1.00 28.90  ?  102 HOH C O    1 
HETATM 2867 O  O    . HOH G 5 .   ? 8.563   -27.019 -1.171  1.00 47.15  ?  103 HOH C O    1 
HETATM 2868 O  O    . HOH G 5 .   ? 4.353   -24.469 4.041   1.00 40.73  ?  104 HOH C O    1 
HETATM 2869 O  O    . HOH G 5 .   ? 11.244  -12.565 1.803   1.00 32.80  ?  105 HOH C O    1 
HETATM 2870 O  O    . HOH G 5 .   ? 11.069  -20.069 -2.456  1.00 36.30  ?  106 HOH C O    1 
HETATM 2871 O  O    . HOH G 5 .   ? 7.769   -17.650 -6.484  1.00 44.75  ?  107 HOH C O    1 
HETATM 2872 O  O    . HOH G 5 .   ? 0.245   -18.571 2.058   1.00 36.38  ?  108 HOH C O    1 
HETATM 2873 O  O    . HOH G 5 .   ? 8.049   -16.138 -4.510  1.00 46.50  ?  109 HOH C O    1 
HETATM 2874 O  O    . HOH G 5 .   ? 13.696  -22.323 0.799   1.00 47.21  ?  110 HOH C O    1 
HETATM 2875 O  O    . HOH G 5 .   ? 7.329   -20.834 -10.463 1.00 58.33  ?  111 HOH C O    1 
HETATM 2876 O  O    . HOH G 5 .   ? 1.179   -20.754 -7.744  1.00 46.25  ?  112 HOH C O    1 
HETATM 2877 O  O    . HOH G 5 .   ? -0.327  -17.536 -5.286  1.00 39.19  ?  113 HOH C O    1 
HETATM 2878 O  O    . HOH G 5 .   ? 0.370   -16.004 1.305   1.00 31.19  ?  114 HOH C O    1 
HETATM 2879 O  O    . HOH G 5 .   ? -0.806  -20.255 -5.593  1.00 38.54  ?  115 HOH C O    1 
HETATM 2880 O  O    . HOH G 5 .   ? 4.166   -22.369 -11.349 1.00 60.35  ?  116 HOH C O    1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1    N  N   . MET A 1   ? 0.5846 0.8119 0.5914 -0.0604 -0.0553 -0.1231 1   MET A N   
2    C  CA  . MET A 1   ? 0.5090 0.7136 0.5233 -0.0656 -0.0511 -0.1214 1   MET A CA  
3    C  C   . MET A 1   ? 0.4609 0.6467 0.4812 -0.0760 -0.0457 -0.1329 1   MET A C   
4    O  O   . MET A 1   ? 0.5283 0.7045 0.5429 -0.0776 -0.0435 -0.1399 1   MET A O   
5    C  CB  . MET A 1   ? 0.4275 0.6144 0.4339 -0.0600 -0.0496 -0.1125 1   MET A CB  
6    C  CG  . MET A 1   ? 0.4545 0.6551 0.4589 -0.0508 -0.0536 -0.0995 1   MET A CG  
7    S  SD  . MET A 1   ? 0.4445 0.6239 0.4386 -0.0426 -0.0507 -0.0875 1   MET A SD  
8    C  CE  . MET A 1   ? 0.3793 0.5252 0.3800 -0.0489 -0.0436 -0.0874 1   MET A CE  
9    N  N   . ASP A 2   ? 0.4167 0.5973 0.4489 -0.0826 -0.0431 -0.1339 2   ASP A N   
10   C  CA  . ASP A 2   ? 0.4085 0.5700 0.4483 -0.0924 -0.0370 -0.1423 2   ASP A CA  
11   C  C   . ASP A 2   ? 0.4003 0.5350 0.4406 -0.0928 -0.0317 -0.1353 2   ASP A C   
12   O  O   . ASP A 2   ? 0.3670 0.5022 0.4141 -0.0934 -0.0311 -0.1290 2   ASP A O   
13   C  CB  . ASP A 2   ? 0.4268 0.6033 0.4797 -0.0993 -0.0372 -0.1474 2   ASP A CB  
14   C  CG  . ASP A 2   ? 0.4696 0.6275 0.5317 -0.1097 -0.0303 -0.1557 2   ASP A CG  
15   O  OD1 . ASP A 2   ? 0.4404 0.5709 0.5006 -0.1110 -0.0245 -0.1540 2   ASP A OD1 
16   O  OD2 . ASP A 2   ? 0.5378 0.7091 0.6095 -0.1163 -0.0305 -0.1635 2   ASP A OD2 
17   N  N   . SER A 3   ? 0.3447 0.4571 0.3781 -0.0920 -0.0278 -0.1364 3   SER A N   
18   C  CA  . SER A 3   ? 0.3589 0.4472 0.3909 -0.0908 -0.0232 -0.1290 3   SER A CA  
19   C  C   . SER A 3   ? 0.3701 0.4467 0.4136 -0.0978 -0.0176 -0.1279 3   SER A C   
20   O  O   . SER A 3   ? 0.3536 0.4244 0.3991 -0.0965 -0.0162 -0.1197 3   SER A O   
21   C  CB  . SER A 3   ? 0.3956 0.4627 0.4198 -0.0891 -0.0192 -0.1315 3   SER A CB  
22   O  OG  . SER A 3   ? 0.4499 0.5269 0.4628 -0.0819 -0.0237 -0.1305 3   SER A OG  
23   N  N   . LYS A 4   ? 0.3783 0.4509 0.4297 -0.1052 -0.0138 -0.1360 4   LYS A N   
24   C  CA  . LYS A 4   ? 0.3746 0.4350 0.4370 -0.1119 -0.0074 -0.1343 4   LYS A CA  
25   C  C   . LYS A 4   ? 0.4033 0.4834 0.4740 -0.1133 -0.0102 -0.1306 4   LYS A C   
26   O  O   . LYS A 4   ? 0.3973 0.4687 0.4734 -0.1151 -0.0059 -0.1239 4   LYS A O   
27   C  CB  . LYS A 4   ? 0.4434 0.4961 0.5130 -0.1198 -0.0025 -0.1443 4   LYS A CB  
28   C  CG  . LYS A 4   ? 0.4960 0.5244 0.5598 -0.1184 0.0026  -0.1465 4   LYS A CG  
29   C  CD  . LYS A 4   ? 0.5102 0.5297 0.5828 -0.1264 0.0084  -0.1561 4   LYS A CD  
30   C  CE  . LYS A 4   ? 0.5888 0.5833 0.6563 -0.1242 0.0141  -0.1576 4   LYS A CE  
31   N  NZ  . LYS A 4   ? 0.6119 0.5847 0.6755 -0.1189 0.0186  -0.1454 4   LYS A NZ  
32   N  N   . SER A 5   ? 0.3316 0.4390 0.4030 -0.1119 -0.0171 -0.1342 5   SER A N   
33   C  CA  . SER A 5   ? 0.3561 0.4845 0.4358 -0.1119 -0.0201 -0.1303 5   SER A CA  
34   C  C   . SER A 5   ? 0.3341 0.4619 0.4095 -0.1048 -0.0217 -0.1193 5   SER A C   
35   O  O   . SER A 5   ? 0.3106 0.4391 0.3936 -0.1062 -0.0191 -0.1139 5   SER A O   
36   C  CB  . SER A 5   ? 0.3853 0.5437 0.4655 -0.1102 -0.0273 -0.1358 5   SER A CB  
37   O  OG  . SER A 5   ? 0.4015 0.5812 0.4905 -0.1095 -0.0300 -0.1320 5   SER A OG  
38   N  N   . ILE A 6   ? 0.3021 0.4293 0.3657 -0.0971 -0.0256 -0.1160 6   ILE A N   
39   C  CA  . ILE A 6   ? 0.2692 0.3955 0.3287 -0.0901 -0.0271 -0.1059 6   ILE A CA  
40   C  C   . ILE A 6   ? 0.2985 0.3966 0.3572 -0.0904 -0.0194 -0.0988 6   ILE A C   
41   O  O   . ILE A 6   ? 0.2782 0.3744 0.3387 -0.0862 -0.0175 -0.0894 6   ILE A O   
42   C  CB  . ILE A 6   ? 0.2533 0.3810 0.2991 -0.0804 -0.0314 -0.1017 6   ILE A CB  
43   C  CG1 . ILE A 6   ? 0.3179 0.4765 0.3637 -0.0781 -0.0389 -0.1057 6   ILE A CG1 
44   C  CG2 . ILE A 6   ? 0.2529 0.3705 0.2931 -0.0702 -0.0303 -0.0872 6   ILE A CG2 
45   C  CD1 . ILE A 6   ? 0.3224 0.4846 0.3551 -0.0708 -0.0426 -0.1044 6   ILE A CD1 
46   N  N   . ALA A 7   ? 0.3067 0.3832 0.3625 -0.0947 -0.0146 -0.1032 7   ALA A N   
47   C  CA  . ALA A 7   ? 0.3049 0.3562 0.3593 -0.0940 -0.0074 -0.0955 7   ALA A CA  
48   C  C   . ALA A 7   ? 0.3376 0.3895 0.4039 -0.1007 -0.0023 -0.0944 7   ALA A C   
49   O  O   . ALA A 7   ? 0.3115 0.3525 0.3763 -0.0971 0.0019  -0.0846 7   ALA A O   
50   C  CB  . ALA A 7   ? 0.3812 0.4104 0.4314 -0.0966 -0.0028 -0.1002 7   ALA A CB  
51   N  N   . ALA A 8   ? 0.3066 0.3726 0.3847 -0.1100 -0.0025 -0.1041 8   ALA A N   
52   C  CA  . ALA A 8   ? 0.2927 0.3620 0.3831 -0.1161 0.0025  -0.1024 8   ALA A CA  
53   C  C   . ALA A 8   ? 0.3153 0.4022 0.4081 -0.1106 -0.0004 -0.0949 8   ALA A C   
54   O  O   . ALA A 8   ? 0.2948 0.3763 0.3915 -0.1105 0.0051  -0.0877 8   ALA A O   
55   C  CB  . ALA A 8   ? 0.2935 0.3732 0.3933 -0.1231 0.0026  -0.1113 8   ALA A CB  
56   N  N   . GLU A 9   ? 0.3083 0.4162 0.3981 -0.1042 -0.0085 -0.0952 9   GLU A N   
57   C  CA  . GLU A 9   ? 0.3001 0.4219 0.3911 -0.0963 -0.0107 -0.0864 9   GLU A CA  
58   C  C   . GLU A 9   ? 0.2898 0.3919 0.3702 -0.0872 -0.0076 -0.0749 9   GLU A C   
59   O  O   . GLU A 9   ? 0.2663 0.3691 0.3495 -0.0842 -0.0045 -0.0683 9   GLU A O   
60   C  CB  . GLU A 9   ? 0.3529 0.5002 0.4429 -0.0903 -0.0194 -0.0877 9   GLU A CB  
61   C  CG  . GLU A 9   ? 0.5005 0.6765 0.6035 -0.0979 -0.0233 -0.0978 9   GLU A CG  
62   C  CD  . GLU A 9   ? 0.5042 0.6992 0.6199 -0.0972 -0.0225 -0.0940 9   GLU A CD  
63   O  OE1 . GLU A 9   ? 0.5426 0.7339 0.6550 -0.0876 -0.0211 -0.0831 9   GLU A OE1 
64   O  OE2 . GLU A 9   ? 0.6101 0.8196 0.7369 -0.1040 -0.0223 -0.1002 9   GLU A OE2 
65   N  N   . LEU A 10  ? 0.2653 0.3508 0.3336 -0.0829 -0.0084 -0.0732 10  LEU A N   
66   C  CA  . LEU A 10  ? 0.2459 0.3136 0.3048 -0.0755 -0.0056 -0.0637 10  LEU A CA  
67   C  C   . LEU A 10  ? 0.2542 0.3074 0.3158 -0.0795 0.0022  -0.0604 10  LEU A C   
68   O  O   . LEU A 10  ? 0.2642 0.3138 0.3232 -0.0745 0.0047  -0.0530 10  LEU A O   
69   C  CB  . LEU A 10  ? 0.2654 0.3190 0.3128 -0.0715 -0.0073 -0.0632 10  LEU A CB  
70   C  CG  . LEU A 10  ? 0.2811 0.3470 0.3233 -0.0653 -0.0141 -0.0633 10  LEU A CG  
71   C  CD1 . LEU A 10  ? 0.3191 0.3711 0.3513 -0.0631 -0.0145 -0.0642 10  LEU A CD1 
72   C  CD2 . LEU A 10  ? 0.2737 0.3443 0.3140 -0.0565 -0.0156 -0.0547 10  LEU A CD2 
73   N  N   . ALA A 11  ? 0.2781 0.3228 0.3448 -0.0884 0.0066  -0.0657 11  ALA A N   
74   C  CA  . ALA A 11  ? 0.2915 0.3212 0.3602 -0.0917 0.0150  -0.0609 11  ALA A CA  
75   C  C   . ALA A 11  ? 0.2629 0.3060 0.3415 -0.0941 0.0181  -0.0584 11  ALA A C   
76   O  O   . ALA A 11  ? 0.2967 0.3319 0.3726 -0.0915 0.0235  -0.0507 11  ALA A O   
77   C  CB  . ALA A 11  ? 0.3334 0.3489 0.4066 -0.1005 0.0202  -0.0666 11  ALA A CB  
78   N  N   . THR A 12  ? 0.2571 0.3220 0.3468 -0.0987 0.0147  -0.0649 12  THR A N   
79   C  CA  . THR A 12  ? 0.2835 0.3633 0.3849 -0.1018 0.0180  -0.0635 12  THR A CA  
80   C  C   . THR A 12  ? 0.2989 0.3912 0.3976 -0.0918 0.0149  -0.0573 12  THR A C   
81   O  O   . THR A 12  ? 0.2924 0.3856 0.3935 -0.0901 0.0202  -0.0518 12  THR A O   
82   C  CB  . THR A 12  ? 0.2655 0.3657 0.3822 -0.1117 0.0158  -0.0739 12  THR A CB  
83   O  OG1 . THR A 12  ? 0.3306 0.4170 0.4520 -0.1223 0.0207  -0.0804 12  THR A OG1 
84   C  CG2 . THR A 12  ? 0.2846 0.4040 0.4148 -0.1143 0.0189  -0.0723 12  THR A CG2 
85   N  N   . ARG A 13  ? 0.2467 0.3486 0.3407 -0.0848 0.0072  -0.0581 13  ARG A N   
86   C  CA  . ARG A 13  ? 0.2558 0.3697 0.3492 -0.0752 0.0046  -0.0529 13  ARG A CA  
87   C  C   . ARG A 13  ? 0.2309 0.3298 0.3104 -0.0655 0.0032  -0.0469 13  ARG A C   
88   O  O   . ARG A 13  ? 0.2341 0.3373 0.3128 -0.0577 0.0031  -0.0422 13  ARG A O   
89   C  CB  . ARG A 13  ? 0.2956 0.4349 0.3963 -0.0735 -0.0026 -0.0568 13  ARG A CB  
90   C  CG  . ARG A 13  ? 0.4100 0.5696 0.5262 -0.0831 -0.0024 -0.0640 13  ARG A CG  
91   C  CD  . ARG A 13  ? 0.4633 0.6525 0.5871 -0.0782 -0.0091 -0.0650 13  ARG A CD  
92   N  NE  . ARG A 13  ? 0.5850 0.7963 0.7258 -0.0849 -0.0073 -0.0689 13  ARG A NE  
93   C  CZ  . ARG A 13  ? 0.5958 0.8188 0.7472 -0.0968 -0.0080 -0.0788 13  ARG A CZ  
94   N  NH1 . ARG A 13  ? 0.6147 0.8290 0.7609 -0.1030 -0.0105 -0.0863 13  ARG A NH1 
95   N  NH2 . ARG A 13  ? 0.6149 0.8591 0.7831 -0.1029 -0.0059 -0.0819 13  ARG A NH2 
96   N  N   . GLY A 14  ? 0.2183 0.3003 0.2881 -0.0660 0.0023  -0.0475 14  GLY A N   
97   C  CA  . GLY A 14  ? 0.2106 0.2797 0.2686 -0.0579 0.0008  -0.0426 14  GLY A CA  
98   C  C   . GLY A 14  ? 0.2015 0.2773 0.2559 -0.0522 -0.0057 -0.0427 14  GLY A C   
99   O  O   . GLY A 14  ? 0.2172 0.2813 0.2625 -0.0469 -0.0067 -0.0394 14  GLY A O   
100  N  N   . TYR A 15  ? 0.1886 0.2838 0.2499 -0.0531 -0.0100 -0.0461 15  TYR A N   
101  C  CA  . TYR A 15  ? 0.1921 0.2956 0.2496 -0.0465 -0.0157 -0.0446 15  TYR A CA  
102  C  C   . TYR A 15  ? 0.1904 0.3148 0.2538 -0.0507 -0.0204 -0.0511 15  TYR A C   
103  O  O   . TYR A 15  ? 0.2130 0.3496 0.2866 -0.0576 -0.0196 -0.0561 15  TYR A O   
104  C  CB  . TYR A 15  ? 0.2006 0.3102 0.2597 -0.0369 -0.0159 -0.0376 15  TYR A CB  
105  C  CG  . TYR A 15  ? 0.2262 0.3578 0.2972 -0.0360 -0.0164 -0.0376 15  TYR A CG  
106  C  CD1 . TYR A 15  ? 0.2045 0.3374 0.2827 -0.0394 -0.0115 -0.0382 15  TYR A CD1 
107  C  CD2 . TYR A 15  ? 0.2324 0.3852 0.3075 -0.0313 -0.0216 -0.0365 15  TYR A CD2 
108  C  CE1 . TYR A 15  ? 0.2191 0.3741 0.3096 -0.0384 -0.0118 -0.0383 15  TYR A CE1 
109  C  CE2 . TYR A 15  ? 0.2433 0.4189 0.3303 -0.0297 -0.0223 -0.0363 15  TYR A CE2 
110  C  CZ  . TYR A 15  ? 0.2322 0.4086 0.3273 -0.0334 -0.0174 -0.0374 15  TYR A CZ  
111  O  OH  . TYR A 15  ? 0.3075 0.5079 0.4155 -0.0318 -0.0178 -0.0372 15  TYR A OH  
112  N  N   . ALA A 16  ? 0.1957 0.3256 0.2530 -0.0466 -0.0252 -0.0509 16  ALA A N   
113  C  CA  . ALA A 16  ? 0.2258 0.3791 0.2868 -0.0486 -0.0308 -0.0567 16  ALA A CA  
114  C  C   . ALA A 16  ? 0.2092 0.3713 0.2637 -0.0384 -0.0351 -0.0502 16  ALA A C   
115  O  O   . ALA A 16  ? 0.2150 0.3611 0.2599 -0.0343 -0.0342 -0.0460 16  ALA A O   
116  C  CB  . ALA A 16  ? 0.2508 0.3987 0.3093 -0.0580 -0.0311 -0.0670 16  ALA A CB  
117  N  N   . LEU A 17  ? 0.2281 0.4163 0.2885 -0.0341 -0.0394 -0.0486 17  LEU A N   
118  C  CA  . LEU A 17  ? 0.2444 0.4441 0.2992 -0.0238 -0.0432 -0.0413 17  LEU A CA  
119  C  C   . LEU A 17  ? 0.2194 0.4378 0.2702 -0.0270 -0.0490 -0.0490 17  LEU A C   
120  O  O   . LEU A 17  ? 0.2772 0.5174 0.3356 -0.0330 -0.0524 -0.0573 17  LEU A O   
121  C  CB  . LEU A 17  ? 0.2171 0.4353 0.2806 -0.0151 -0.0441 -0.0334 17  LEU A CB  
122  C  CG  . LEU A 17  ? 0.2827 0.5132 0.3414 -0.0032 -0.0471 -0.0236 17  LEU A CG  
123  C  CD1 . LEU A 17  ? 0.2464 0.4504 0.2964 0.0024  -0.0429 -0.0154 17  LEU A CD1 
124  C  CD2 . LEU A 17  ? 0.3251 0.5776 0.3940 0.0056  -0.0482 -0.0163 17  LEU A CD2 
125  N  N   . VAL A 18  ? 0.2315 0.4429 0.2706 -0.0233 -0.0499 -0.0467 18  VAL A N   
126  C  CA  . VAL A 18  ? 0.2694 0.4983 0.3024 -0.0252 -0.0550 -0.0539 18  VAL A CA  
127  C  C   . VAL A 18  ? 0.2480 0.4981 0.2769 -0.0131 -0.0589 -0.0437 18  VAL A C   
128  O  O   . VAL A 18  ? 0.2646 0.5026 0.2853 -0.0054 -0.0567 -0.0339 18  VAL A O   
129  C  CB  . VAL A 18  ? 0.2809 0.4884 0.3031 -0.0289 -0.0528 -0.0586 18  VAL A CB  
130  C  CG1 . VAL A 18  ? 0.3008 0.5275 0.3163 -0.0309 -0.0577 -0.0676 18  VAL A CG1 
131  C  CG2 . VAL A 18  ? 0.3261 0.5097 0.3520 -0.0388 -0.0478 -0.0658 18  VAL A CG2 
132  N  N   . PRO A 19  ? 0.2583 0.5404 0.2929 -0.0109 -0.0642 -0.0449 19  PRO A N   
133  C  CA  . PRO A 19  ? 0.2922 0.5959 0.3220 0.0017  -0.0678 -0.0338 19  PRO A CA  
134  C  C   . PRO A 19  ? 0.2871 0.5939 0.3030 0.0021  -0.0695 -0.0371 19  PRO A C   
135  O  O   . PRO A 19  ? 0.3409 0.6423 0.3534 -0.0076 -0.0694 -0.0505 19  PRO A O   
136  C  CB  . PRO A 19  ? 0.3169 0.6478 0.3559 0.0023  -0.0709 -0.0359 19  PRO A CB  
137  C  CG  . PRO A 19  ? 0.3657 0.6932 0.4104 -0.0124 -0.0705 -0.0524 19  PRO A CG  
138  C  CD  . PRO A 19  ? 0.2959 0.5963 0.3419 -0.0198 -0.0669 -0.0561 19  PRO A CD  
139  N  N   . ASP A 20  ? 0.3112 0.6221 0.3192 0.0140  -0.0693 -0.0237 20  ASP A N   
140  C  CA  . ASP A 20  ? 0.2872 0.6036 0.2821 0.0163  -0.0696 -0.0246 20  ASP A CA  
141  C  C   . ASP A 20  ? 0.3082 0.6041 0.2952 0.0082  -0.0679 -0.0343 20  ASP A C   
142  O  O   . ASP A 20  ? 0.3365 0.6360 0.3163 0.0043  -0.0682 -0.0435 20  ASP A O   
143  C  CB  . ASP A 20  ? 0.3574 0.6986 0.3525 0.0148  -0.0725 -0.0321 20  ASP A CB  
144  C  CG  . ASP A 20  ? 0.4196 0.7823 0.4204 0.0248  -0.0738 -0.0209 20  ASP A CG  
145  O  OD1 . ASP A 20  ? 0.4239 0.7875 0.4208 0.0370  -0.0719 -0.0048 20  ASP A OD1 
146  O  OD2 . ASP A 20  ? 0.4973 0.8751 0.5070 0.0206  -0.0761 -0.0278 20  ASP A OD2 
147  N  N   . PHE A 21  ? 0.2584 0.5261 0.2479 0.0058  -0.0635 -0.0316 21  PHE A N   
148  C  CA  . PHE A 21  ? 0.2507 0.4943 0.2331 0.0000  -0.0598 -0.0378 21  PHE A CA  
149  C  C   . PHE A 21  ? 0.3087 0.5564 0.2784 0.0073  -0.0593 -0.0313 21  PHE A C   
150  O  O   . PHE A 21  ? 0.2975 0.5433 0.2590 0.0030  -0.0594 -0.0407 21  PHE A O   
151  C  CB  . PHE A 21  ? 0.2619 0.4733 0.2494 -0.0017 -0.0537 -0.0330 21  PHE A CB  
152  C  CG  . PHE A 21  ? 0.2628 0.4498 0.2439 -0.0059 -0.0497 -0.0369 21  PHE A CG  
153  C  CD1 . PHE A 21  ? 0.2798 0.4575 0.2612 -0.0159 -0.0492 -0.0507 21  PHE A CD1 
154  C  CD2 . PHE A 21  ? 0.2628 0.4359 0.2387 0.0004  -0.0459 -0.0264 21  PHE A CD2 
155  C  CE1 . PHE A 21  ? 0.2896 0.4454 0.2657 -0.0183 -0.0453 -0.0533 21  PHE A CE1 
156  C  CE2 . PHE A 21  ? 0.2981 0.4507 0.2690 -0.0029 -0.0423 -0.0298 21  PHE A CE2 
157  C  CZ  . PHE A 21  ? 0.2946 0.4392 0.2655 -0.0117 -0.0422 -0.0429 21  PHE A CZ  
158  N  N   . LEU A 22  ? 0.2730 0.5258 0.2414 0.0185  -0.0580 -0.0151 22  LEU A N   
159  C  CA  . LEU A 22  ? 0.2855 0.5492 0.2425 0.0269  -0.0577 -0.0067 22  LEU A CA  
160  C  C   . LEU A 22  ? 0.3259 0.6206 0.2826 0.0351  -0.0615 -0.0002 22  LEU A C   
161  O  O   . LEU A 22  ? 0.3350 0.6367 0.3009 0.0395  -0.0623 0.0069  22  LEU A O   
162  C  CB  . LEU A 22  ? 0.3178 0.5596 0.2748 0.0337  -0.0508 0.0090  22  LEU A CB  
163  C  CG  . LEU A 22  ? 0.3227 0.5320 0.2804 0.0272  -0.0455 0.0053  22  LEU A CG  
164  C  CD1 . LEU A 22  ? 0.3366 0.5310 0.2937 0.0343  -0.0392 0.0205  22  LEU A CD1 
165  C  CD2 . LEU A 22  ? 0.3335 0.5411 0.2831 0.0200  -0.0464 -0.0085 22  LEU A CD2 
166  N  N   . THR A 23  ? 0.3165 0.6251 0.2644 0.0369  -0.0615 -0.0029 23  THR A N   
167  C  CA  . THR A 23  ? 0.3330 0.6668 0.2803 0.0449  -0.0625 0.0038  23  THR A CA  
168  C  C   . THR A 23  ? 0.3292 0.6682 0.2647 0.0519  -0.0593 0.0113  23  THR A C   
169  O  O   . THR A 23  ? 0.3386 0.6631 0.2671 0.0493  -0.0568 0.0090  23  THR A O   
170  C  CB  . THR A 23  ? 0.4153 0.7686 0.3658 0.0378  -0.0670 -0.0119 23  THR A CB  
171  O  OG1 . THR A 23  ? 0.4513 0.8015 0.3948 0.0300  -0.0671 -0.0267 23  THR A OG1 
172  C  CG2 . THR A 23  ? 0.3776 0.7264 0.3406 0.0301  -0.0693 -0.0196 23  THR A CG2 
173  N  N   . GLY A 24  ? 0.3570 0.7179 0.2909 0.0611  -0.0591 0.0206  24  GLY A N   
174  C  CA  . GLY A 24  ? 0.3915 0.7621 0.3149 0.0675  -0.0562 0.0266  24  GLY A CA  
175  C  C   . GLY A 24  ? 0.3906 0.7411 0.3100 0.0729  -0.0498 0.0409  24  GLY A C   
176  O  O   . GLY A 24  ? 0.3780 0.7123 0.3035 0.0766  -0.0468 0.0531  24  GLY A O   
177  N  N   . ASP A 25  ? 0.3730 0.7245 0.2824 0.0731  -0.0473 0.0391  25  ASP A N   
178  C  CA  . ASP A 25  ? 0.3984 0.7327 0.3040 0.0779  -0.0406 0.0526  25  ASP A CA  
179  C  C   . ASP A 25  ? 0.3712 0.6774 0.2802 0.0715  -0.0394 0.0505  25  ASP A C   
180  O  O   . ASP A 25  ? 0.3947 0.6844 0.3060 0.0760  -0.0338 0.0650  25  ASP A O   
181  C  CB  . ASP A 25  ? 0.4696 0.8113 0.3642 0.0784  -0.0383 0.0489  25  ASP A CB  
182  C  CG  . ASP A 25  ? 0.4906 0.8612 0.3811 0.0860  -0.0388 0.0531  25  ASP A CG  
183  O  OD1 . ASP A 25  ? 0.5304 0.9122 0.4261 0.0936  -0.0385 0.0649  25  ASP A OD1 
184  O  OD2 . ASP A 25  ? 0.5530 0.9355 0.4351 0.0848  -0.0392 0.0445  25  ASP A OD2 
185  N  N   . ALA A 26  ? 0.3407 0.6406 0.2508 0.0609  -0.0440 0.0328  26  ALA A N   
186  C  CA  . ALA A 26  ? 0.3234 0.5985 0.2367 0.0553  -0.0430 0.0308  26  ALA A CA  
187  C  C   . ALA A 26  ? 0.3390 0.6039 0.2633 0.0593  -0.0418 0.0433  26  ALA A C   
188  O  O   . ALA A 26  ? 0.3177 0.5560 0.2483 0.0587  -0.0354 0.0504  26  ALA A O   
189  C  CB  . ALA A 26  ? 0.3783 0.6486 0.2927 0.0433  -0.0475 0.0096  26  ALA A CB  
190  N  N   . LEU A 27  ? 0.3156 0.5962 0.2464 0.0621  -0.0456 0.0444  27  LEU A N   
191  C  CA  . LEU A 27  ? 0.3059 0.5776 0.2480 0.0672  -0.0437 0.0565  27  LEU A CA  
192  C  C   . LEU A 27  ? 0.2902 0.5565 0.2320 0.0785  -0.0366 0.0776  27  LEU A C   
193  O  O   . LEU A 27  ? 0.3045 0.5448 0.2548 0.0788  -0.0301 0.0853  27  LEU A O   
194  C  CB  . LEU A 27  ? 0.2820 0.5736 0.2313 0.0682  -0.0486 0.0530  27  LEU A CB  
195  C  CG  . LEU A 27  ? 0.2938 0.5802 0.2551 0.0752  -0.0467 0.0656  27  LEU A CG  
196  C  CD1 . LEU A 27  ? 0.2769 0.5303 0.2472 0.0676  -0.0426 0.0611  27  LEU A CD1 
197  C  CD2 . LEU A 27  ? 0.3255 0.6332 0.2939 0.0755  -0.0511 0.0606  27  LEU A CD2 
198  N  N   . THR A 28  ? 0.3276 0.6109 0.2636 0.0849  -0.0346 0.0836  28  THR A N   
199  C  CA  . THR A 28  ? 0.3096 0.5874 0.2468 0.0950  -0.0265 0.1033  28  THR A CA  
200  C  C   . THR A 28  ? 0.3270 0.5811 0.2621 0.0931  -0.0202 0.1090  28  THR A C   
201  O  O   . THR A 28  ? 0.3252 0.5615 0.2680 0.0979  -0.0130 0.1236  28  THR A O   
202  C  CB  . THR A 28  ? 0.3965 0.6992 0.3265 0.1014  -0.0259 0.1068  28  THR A CB  
203  O  OG1 . THR A 28  ? 0.4641 0.7885 0.3978 0.1039  -0.0309 0.1036  28  THR A OG1 
204  C  CG2 . THR A 28  ? 0.4159 0.7131 0.3474 0.1114  -0.0166 0.1270  28  THR A CG2 
205  N  N   . GLU A 29  ? 0.3126 0.5655 0.2386 0.0858  -0.0223 0.0971  29  GLU A N   
206  C  CA  . GLU A 29  ? 0.3250 0.5559 0.2501 0.0830  -0.0156 0.1009  29  GLU A CA  
207  C  C   . GLU A 29  ? 0.3198 0.5196 0.2588 0.0754  -0.0127 0.0964  29  GLU A C   
208  O  O   . GLU A 29  ? 0.3073 0.4861 0.2529 0.0754  -0.0051 0.1050  29  GLU A O   
209  C  CB  . GLU A 29  ? 0.3300 0.5668 0.2435 0.0769  -0.0178 0.0872  29  GLU A CB  
210  C  CG  . GLU A 29  ? 0.3559 0.6152 0.2602 0.0827  -0.0167 0.0902  29  GLU A CG  
211  C  CD  . GLU A 29  ? 0.4814 0.7519 0.3759 0.0764  -0.0213 0.0716  29  GLU A CD  
212  O  OE1 . GLU A 29  ? 0.5394 0.7989 0.4329 0.0678  -0.0244 0.0577  29  GLU A OE1 
213  O  OE2 . GLU A 29  ? 0.5452 0.8352 0.4334 0.0802  -0.0213 0.0707  29  GLU A OE2 
214  N  N   . ALA A 30  ? 0.2816 0.4788 0.2254 0.0686  -0.0185 0.0827  30  ALA A N   
215  C  CA  . ALA A 30  ? 0.2830 0.4532 0.2387 0.0619  -0.0160 0.0782  30  ALA A CA  
216  C  C   . ALA A 30  ? 0.2901 0.4510 0.2568 0.0687  -0.0110 0.0924  30  ALA A C   
217  O  O   . ALA A 30  ? 0.2765 0.4132 0.2520 0.0660  -0.0051 0.0952  30  ALA A O   
218  C  CB  . ALA A 30  ? 0.2650 0.4364 0.2228 0.0537  -0.0226 0.0616  30  ALA A CB  
219  N  N   . VAL A 31  ? 0.2809 0.4615 0.2478 0.0779  -0.0132 0.1013  31  VAL A N   
220  C  CA  . VAL A 31  ? 0.3143 0.4862 0.2920 0.0860  -0.0076 0.1159  31  VAL A CA  
221  C  C   . VAL A 31  ? 0.3191 0.4774 0.2982 0.0907  0.0018  0.1310  31  VAL A C   
222  O  O   . VAL A 31  ? 0.3326 0.4670 0.3231 0.0901  0.0089  0.1361  31  VAL A O   
223  C  CB  . VAL A 31  ? 0.3122 0.5114 0.2893 0.0964  -0.0119 0.1237  31  VAL A CB  
224  C  CG1 . VAL A 31  ? 0.3495 0.5394 0.3377 0.1070  -0.0046 0.1413  31  VAL A CG1 
225  C  CG2 . VAL A 31  ? 0.3139 0.5247 0.2932 0.0906  -0.0202 0.1085  31  VAL A CG2 
226  N  N   . ALA A 32  ? 0.3217 0.4957 0.2895 0.0951  0.0025  0.1378  32  ALA A N   
227  C  CA  . ALA A 32  ? 0.3578 0.5204 0.3272 0.0994  0.0122  0.1530  32  ALA A CA  
228  C  C   . ALA A 32  ? 0.3336 0.4678 0.3100 0.0886  0.0170  0.1452  32  ALA A C   
229  O  O   . ALA A 32  ? 0.3786 0.4928 0.3656 0.0894  0.0258  0.1549  32  ALA A O   
230  C  CB  . ALA A 32  ? 0.3860 0.5708 0.3416 0.1036  0.0120  0.1572  32  ALA A CB  
231  N  N   . ALA A 33  ? 0.3059 0.4386 0.2775 0.0785  0.0114  0.1276  33  ALA A N   
232  C  CA  . ALA A 33  ? 0.3143 0.4242 0.2917 0.0689  0.0150  0.1200  33  ALA A CA  
233  C  C   . ALA A 33  ? 0.3276 0.4144 0.3196 0.0653  0.0180  0.1182  33  ALA A C   
234  O  O   . ALA A 33  ? 0.3362 0.4041 0.3374 0.0624  0.0253  0.1222  33  ALA A O   
235  C  CB  . ALA A 33  ? 0.3085 0.4225 0.2779 0.0604  0.0082  0.1020  33  ALA A CB  
236  N  N   . ILE A 34  ? 0.3041 0.3930 0.2990 0.0649  0.0128  0.1113  34  ILE A N   
237  C  CA  . ILE A 34  ? 0.3055 0.3736 0.3132 0.0617  0.0157  0.1085  34  ILE A CA  
238  C  C   . ILE A 34  ? 0.3213 0.3802 0.3391 0.0698  0.0243  0.1246  34  ILE A C   
239  O  O   . ILE A 34  ? 0.3248 0.3619 0.3543 0.0664  0.0301  0.1239  34  ILE A O   
240  C  CB  . ILE A 34  ? 0.2915 0.3644 0.3000 0.0591  0.0088  0.0972  34  ILE A CB  
241  C  CG1 . ILE A 34  ? 0.3040 0.3545 0.3233 0.0533  0.0115  0.0901  34  ILE A CG1 
242  C  CG2 . ILE A 34  ? 0.2977 0.3886 0.3063 0.0691  0.0067  0.1058  34  ILE A CG2 
243  C  CD1 . ILE A 34  ? 0.2857 0.3389 0.3044 0.0480  0.0050  0.0766  34  ILE A CD1 
244  N  N   . GLU A 35  ? 0.3430 0.4182 0.3567 0.0807  0.0257  0.1392  35  GLU A N   
245  C  CA  . GLU A 35  ? 0.3550 0.4206 0.3785 0.0896  0.0351  0.1566  35  GLU A CA  
246  C  C   . GLU A 35  ? 0.4024 0.4512 0.4309 0.0869  0.0447  0.1644  35  GLU A C   
247  O  O   . GLU A 35  ? 0.4374 0.4689 0.4785 0.0904  0.0541  0.1749  35  GLU A O   
248  C  CB  . GLU A 35  ? 0.3873 0.4772 0.4046 0.1032  0.0337  0.1714  35  GLU A CB  
249  C  CG  . GLU A 35  ? 0.3674 0.4718 0.3848 0.1061  0.0256  0.1647  35  GLU A CG  
250  C  CD  . GLU A 35  ? 0.4733 0.5998 0.4891 0.1196  0.0254  0.1786  35  GLU A CD  
251  O  OE1 . GLU A 35  ? 0.5236 0.6681 0.5299 0.1229  0.0254  0.1836  35  GLU A OE1 
252  O  OE2 . GLU A 35  ? 0.5700 0.6954 0.5947 0.1243  0.0258  0.1799  35  GLU A OE2 
253  N  N   . THR A 36  ? 0.3705 0.4238 0.3911 0.0807  0.0433  0.1592  36  THR A N   
254  C  CA  . THR A 36  ? 0.4133 0.4500 0.4412 0.0761  0.0524  0.1640  36  THR A CA  
255  C  C   . THR A 36  ? 0.3936 0.4046 0.4361 0.0668  0.0556  0.1540  36  THR A C   
256  O  O   . THR A 36  ? 0.4397 0.4332 0.4942 0.0646  0.0651  0.1603  36  THR A O   
257  C  CB  . THR A 36  ? 0.4107 0.4576 0.4280 0.0710  0.0502  0.1590  36  THR A CB  
258  O  OG1 . THR A 36  ? 0.3853 0.4307 0.3994 0.0612  0.0423  0.1395  36  THR A OG1 
259  C  CG2 . THR A 36  ? 0.4031 0.4770 0.4048 0.0799  0.0471  0.1675  36  THR A CG2 
260  N  N   . TYR A 37  ? 0.3571 0.3660 0.3992 0.0613  0.0481  0.1383  37  TYR A N   
261  C  CA  . TYR A 37  ? 0.3445 0.3320 0.3989 0.0530  0.0504  0.1277  37  TYR A CA  
262  C  C   . TYR A 37  ? 0.3783 0.3547 0.4432 0.0583  0.0543  0.1316  37  TYR A C   
263  O  O   . TYR A 37  ? 0.3911 0.3468 0.4696 0.0546  0.0615  0.1304  37  TYR A O   
264  C  CB  . TYR A 37  ? 0.3419 0.3328 0.3900 0.0449  0.0410  0.1093  37  TYR A CB  
265  C  CG  . TYR A 37  ? 0.3130 0.3096 0.3536 0.0379  0.0375  0.1016  37  TYR A CG  
266  C  CD1 . TYR A 37  ? 0.3211 0.3048 0.3690 0.0290  0.0400  0.0940  37  TYR A CD1 
267  C  CD2 . TYR A 37  ? 0.3039 0.3195 0.3305 0.0402  0.0314  0.1006  37  TYR A CD2 
268  C  CE1 . TYR A 37  ? 0.3080 0.2977 0.3498 0.0236  0.0368  0.0872  37  TYR A CE1 
269  C  CE2 . TYR A 37  ? 0.3158 0.3354 0.3360 0.0345  0.0287  0.0929  37  TYR A CE2 
270  C  CZ  . TYR A 37  ? 0.3147 0.3214 0.3427 0.0266  0.0315  0.0868  37  TYR A CZ  
271  O  OH  . TYR A 37  ? 0.3123 0.3238 0.3348 0.0219  0.0290  0.0797  37  TYR A OH  
272  N  N   . PHE A 38  ? 0.3683 0.3588 0.4280 0.0666  0.0497  0.1353  38  PHE A N   
273  C  CA  . PHE A 38  ? 0.3518 0.3343 0.4210 0.0726  0.0526  0.1380  38  PHE A CA  
274  C  C   . PHE A 38  ? 0.4018 0.3981 0.4691 0.0868  0.0551  0.1566  38  PHE A C   
275  O  O   . PHE A 38  ? 0.4149 0.4317 0.4749 0.0927  0.0479  0.1568  38  PHE A O   
276  C  CB  . PHE A 38  ? 0.3530 0.3407 0.4193 0.0687  0.0442  0.1228  38  PHE A CB  
277  C  CG  . PHE A 38  ? 0.3084 0.2883 0.3727 0.0559  0.0401  0.1056  38  PHE A CG  
278  C  CD1 . PHE A 38  ? 0.3261 0.2847 0.4007 0.0489  0.0459  0.0996  38  PHE A CD1 
279  C  CD2 . PHE A 38  ? 0.2765 0.2707 0.3292 0.0512  0.0310  0.0956  38  PHE A CD2 
280  C  CE1 . PHE A 38  ? 0.3323 0.2867 0.4049 0.0382  0.0417  0.0846  38  PHE A CE1 
281  C  CE2 . PHE A 38  ? 0.2820 0.2693 0.3330 0.0410  0.0278  0.0816  38  PHE A CE2 
282  C  CZ  . PHE A 38  ? 0.3125 0.2810 0.3730 0.0349  0.0329  0.0765  38  PHE A CZ  
283  N  N   . PRO A 39  ? 0.4192 0.4057 0.4936 0.0926  0.0654  0.1727  39  PRO A N   
284  C  CA  . PRO A 39  ? 0.4563 0.4590 0.5276 0.1053  0.0677  0.1887  39  PRO A CA  
285  C  C   . PRO A 39  ? 0.4761 0.4792 0.5547 0.1129  0.0682  0.1899  39  PRO A C   
286  O  O   . PRO A 39  ? 0.4911 0.4771 0.5795 0.1097  0.0695  0.1814  39  PRO A O   
287  C  CB  . PRO A 39  ? 0.4946 0.4849 0.5734 0.1045  0.0791  0.1978  39  PRO A CB  
288  C  CG  . PRO A 39  ? 0.5197 0.4822 0.6108 0.0932  0.0843  0.1878  39  PRO A CG  
289  C  CD  . PRO A 39  ? 0.4576 0.4214 0.5423 0.0855  0.0749  0.1737  39  PRO A CD  
290  N  N   . ASP A 40  ? 0.4968 0.5211 0.5704 0.1231  0.0673  0.2001  40  ASP A N   
291  C  CA  . ASP A 40  ? 0.5779 0.6062 0.6579 0.1315  0.0682  0.2033  40  ASP A CA  
292  C  C   . ASP A 40  ? 0.5951 0.5957 0.6911 0.1316  0.0806  0.2064  40  ASP A C   
293  O  O   . ASP A 40  ? 0.5869 0.5821 0.6869 0.1343  0.0895  0.2171  40  ASP A O   
294  C  CB  . ASP A 40  ? 0.5934 0.6502 0.6651 0.1421  0.0662  0.2149  40  ASP A CB  
295  C  CG  . ASP A 40  ? 0.6867 0.7533 0.7632 0.1509  0.0652  0.2176  40  ASP A CG  
296  O  OD1 . ASP A 40  ? 0.6687 0.7211 0.7542 0.1489  0.0654  0.2097  40  ASP A OD1 
297  O  OD2 . ASP A 40  ? 0.7613 0.8507 0.8328 0.1601  0.0645  0.2273  40  ASP A OD2 
298  N  N   . PRO A 41  ? 0.5674 0.5504 0.6733 0.1284  0.0818  0.1966  41  PRO A N   
299  C  CA  . PRO A 41  ? 0.5958 0.5517 0.7170 0.1268  0.0936  0.1966  41  PRO A CA  
300  C  C   . PRO A 41  ? 0.6475 0.6069 0.7744 0.1383  0.1011  0.2105  41  PRO A C   
301  O  O   . PRO A 41  ? 0.6620 0.6002 0.8013 0.1376  0.1121  0.2128  41  PRO A O   
302  C  CB  . PRO A 41  ? 0.5573 0.4995 0.6849 0.1218  0.0912  0.1813  41  PRO A CB  
303  C  CG  . PRO A 41  ? 0.5482 0.5148 0.6662 0.1263  0.0797  0.1788  41  PRO A CG  
304  C  CD  . PRO A 41  ? 0.5195 0.5078 0.6235 0.1263  0.0728  0.1844  41  PRO A CD  
305  N  N   . GLU A 42  ? 0.6342 0.6202 0.7528 0.1484  0.0958  0.2192  42  GLU A N   
306  C  CA  . GLU A 42  ? 0.7520 0.7442 0.8749 0.1602  0.1029  0.2341  42  GLU A CA  
307  C  C   . GLU A 42  ? 0.8310 0.8171 0.9561 0.1611  0.1124  0.2461  42  GLU A C   
308  O  O   . GLU A 42  ? 0.8116 0.7883 0.9465 0.1676  0.1230  0.2566  42  GLU A O   
309  C  CB  . GLU A 42  ? 0.8034 0.8297 0.9155 0.1698  0.0940  0.2400  42  GLU A CB  
310  C  CG  . GLU A 42  ? 0.8706 0.9161 0.9771 0.1791  0.0974  0.2566  42  GLU A CG  
311  C  CD  . GLU A 42  ? 0.8885 0.9491 0.9817 0.1748  0.0921  0.2567  42  GLU A CD  
312  O  OE1 . GLU A 42  ? 0.8481 0.8915 0.9421 0.1648  0.0936  0.2503  42  GLU A OE1 
313  O  OE2 . GLU A 42  ? 0.9312 1.0217 1.0133 0.1812  0.0863  0.2625  42  GLU A OE2 
314  N  N   . VAL A 51  ? 0.8095 0.6389 0.9821 0.0526  0.1132  0.1092  51  VAL A N   
315  C  CA  . VAL A 51  ? 0.7000 0.5428 0.8609 0.0562  0.1032  0.1072  51  VAL A CA  
316  C  C   . VAL A 51  ? 0.6674 0.5048 0.8277 0.0456  0.0978  0.0871  51  VAL A C   
317  O  O   . VAL A 51  ? 0.6120 0.4617 0.7618 0.0452  0.0887  0.0827  51  VAL A O   
318  C  CB  . VAL A 51  ? 0.7248 0.5754 0.8842 0.0695  0.1028  0.1156  51  VAL A CB  
319  C  CG1 . VAL A 51  ? 0.6093 0.4685 0.7620 0.0706  0.0940  0.1065  51  VAL A CG1 
320  C  CG2 . VAL A 51  ? 0.6626 0.5298 0.8153 0.0803  0.1028  0.1356  51  VAL A CG2 
321  N  N   . ALA A 52  ? 0.6859 0.5091 0.8559 0.0365  0.1025  0.0737  52  ALA A N   
322  C  CA  . ALA A 52  ? 0.6301 0.4506 0.7990 0.0263  0.0974  0.0537  52  ALA A CA  
323  C  C   . ALA A 52  ? 0.6056 0.4354 0.7659 0.0194  0.0897  0.0506  52  ALA A C   
324  O  O   . ALA A 52  ? 0.5914 0.4354 0.7394 0.0178  0.0799  0.0415  52  ALA A O   
325  C  CB  . ALA A 52  ? 0.7013 0.5088 0.8814 0.0171  0.1034  0.0408  52  ALA A CB  
326  N  N   . ALA A 53  ? 0.6015 0.4323 0.7636 0.0147  0.0918  0.0562  53  ALA A N   
327  C  CA  . ALA A 53  ? 0.6088 0.4542 0.7603 0.0084  0.0835  0.0530  53  ALA A CA  
328  C  C   . ALA A 53  ? 0.5379 0.4038 0.6728 0.0164  0.0750  0.0614  53  ALA A C   
329  O  O   . ALA A 53  ? 0.4831 0.3632 0.6061 0.0121  0.0657  0.0540  53  ALA A O   
330  C  CB  . ALA A 53  ? 0.5618 0.4028 0.7210 0.0030  0.0894  0.0596  53  ALA A CB  
331  N  N   . LEU A 54  ? 0.5044 0.3725 0.6388 0.0280  0.0781  0.0765  54  LEU A N   
332  C  CA  . LEU A 54  ? 0.4805 0.3698 0.6001 0.0353  0.0701  0.0837  54  LEU A CA  
333  C  C   . LEU A 54  ? 0.4316 0.3304 0.5434 0.0358  0.0618  0.0729  54  LEU A C   
334  O  O   . LEU A 54  ? 0.4072 0.3244 0.5074 0.0397  0.0543  0.0758  54  LEU A O   
335  C  CB  . LEU A 54  ? 0.4840 0.3763 0.6054 0.0480  0.0756  0.1035  54  LEU A CB  
336  C  CG  . LEU A 54  ? 0.5355 0.4233 0.6612 0.0491  0.0833  0.1177  54  LEU A CG  
337  C  CD1 . LEU A 54  ? 0.5435 0.4395 0.6674 0.0634  0.0871  0.1384  54  LEU A CD1 
338  C  CD2 . LEU A 54  ? 0.5497 0.4496 0.6655 0.0415  0.0776  0.1138  54  LEU A CD2 
339  N  N   . LYS A 55  ? 0.4019 0.2894 0.5201 0.0317  0.0632  0.0602  55  LYS A N   
340  C  CA  . LYS A 55  ? 0.3975 0.2944 0.5080 0.0309  0.0558  0.0493  55  LYS A CA  
341  C  C   . LYS A 55  ? 0.3652 0.2707 0.4655 0.0214  0.0475  0.0375  55  LYS A C   
342  O  O   . LYS A 55  ? 0.3547 0.2700 0.4470 0.0207  0.0410  0.0304  55  LYS A O   
343  C  CB  . LYS A 55  ? 0.4281 0.3110 0.5483 0.0310  0.0609  0.0404  55  LYS A CB  
344  C  CG  . LYS A 55  ? 0.4839 0.3585 0.6145 0.0421  0.0692  0.0519  55  LYS A CG  
345  C  CD  . LYS A 55  ? 0.4941 0.3552 0.6337 0.0423  0.0743  0.0412  55  LYS A CD  
346  C  CE  . LYS A 55  ? 0.5313 0.3828 0.6824 0.0545  0.0835  0.0532  55  LYS A CE  
347  N  NZ  . LYS A 55  ? 0.5536 0.3897 0.7147 0.0546  0.0900  0.0417  55  LYS A NZ  
348  N  N   . HIS A 56  ? 0.3614 0.2643 0.4623 0.0144  0.0479  0.0359  56  HIS A N   
349  C  CA  . HIS A 56  ? 0.3539 0.2648 0.4462 0.0065  0.0405  0.0251  56  HIS A CA  
350  C  C   . HIS A 56  ? 0.3035 0.2306 0.3831 0.0087  0.0339  0.0308  56  HIS A C   
351  O  O   . HIS A 56  ? 0.3444 0.2757 0.4230 0.0130  0.0358  0.0423  56  HIS A O   
352  C  CB  . HIS A 56  ? 0.3783 0.2812 0.4779 -0.0020 0.0436  0.0198  56  HIS A CB  
353  C  CG  . HIS A 56  ? 0.4697 0.3595 0.5795 -0.0072 0.0478  0.0081  56  HIS A CG  
354  N  ND1 . HIS A 56  ? 0.4731 0.3661 0.5799 -0.0144 0.0431  -0.0066 56  HIS A ND1 
355  C  CD2 . HIS A 56  ? 0.5362 0.4101 0.6593 -0.0059 0.0565  0.0086  56  HIS A CD2 
356  C  CE1 . HIS A 56  ? 0.5577 0.4386 0.6748 -0.0179 0.0482  -0.0158 56  HIS A CE1 
357  N  NE2 . HIS A 56  ? 0.5446 0.4126 0.6723 -0.0130 0.0567  -0.0073 56  HIS A NE2 
358  N  N   . ALA A 57  ? 0.3171 0.2532 0.3871 0.0058  0.0266  0.0224  57  ALA A N   
359  C  CA  . ALA A 57  ? 0.2749 0.2246 0.3336 0.0063  0.0206  0.0247  57  ALA A CA  
360  C  C   . ALA A 57  ? 0.2855 0.2355 0.3437 0.0022  0.0212  0.0261  57  ALA A C   
361  O  O   . ALA A 57  ? 0.3180 0.2606 0.3823 -0.0037 0.0232  0.0201  57  ALA A O   
362  C  CB  . ALA A 57  ? 0.3059 0.2612 0.3567 0.0027  0.0143  0.0146  57  ALA A CB  
363  N  N   . VAL A 58  ? 0.2248 0.1848 0.2762 0.0053  0.0195  0.0333  58  VAL A N   
364  C  CA  . VAL A 58  ? 0.2152 0.1780 0.2649 0.0026  0.0202  0.0354  58  VAL A CA  
365  C  C   . VAL A 58  ? 0.2198 0.1928 0.2582 0.0008  0.0134  0.0295  58  VAL A C   
366  O  O   . VAL A 58  ? 0.2084 0.1904 0.2389 0.0044  0.0097  0.0308  58  VAL A O   
367  C  CB  . VAL A 58  ? 0.2402 0.2069 0.2904 0.0085  0.0247  0.0489  58  VAL A CB  
368  C  CG1 . VAL A 58  ? 0.2955 0.2678 0.3426 0.0062  0.0254  0.0510  58  VAL A CG1 
369  C  CG2 . VAL A 58  ? 0.2965 0.2506 0.3595 0.0106  0.0328  0.0559  58  VAL A CG2 
370  N  N   . PRO A 59  ? 0.2111 0.1835 0.2490 -0.0046 0.0118  0.0229  59  PRO A N   
371  C  CA  . PRO A 59  ? 0.2199 0.1995 0.2480 -0.0058 0.0063  0.0172  59  PRO A CA  
372  C  C   . PRO A 59  ? 0.2190 0.2075 0.2406 -0.0034 0.0061  0.0218  59  PRO A C   
373  O  O   . PRO A 59  ? 0.2424 0.2319 0.2675 -0.0023 0.0104  0.0287  59  PRO A O   
374  C  CB  . PRO A 59  ? 0.2264 0.2023 0.2580 -0.0114 0.0054  0.0094  59  PRO A CB  
375  C  CG  . PRO A 59  ? 0.2456 0.2162 0.2885 -0.0137 0.0108  0.0123  59  PRO A CG  
376  C  CD  . PRO A 59  ? 0.2640 0.2286 0.3118 -0.0100 0.0151  0.0190  59  PRO A CD  
377  N  N   . PHE A 60  ? 0.2170 0.2116 0.2293 -0.0029 0.0015  0.0175  60  PHE A N   
378  C  CA  . PHE A 60  ? 0.2204 0.2232 0.2254 -0.0013 0.0008  0.0183  60  PHE A CA  
379  C  C   . PHE A 60  ? 0.2160 0.2174 0.2244 -0.0040 0.0028  0.0170  60  PHE A C   
380  O  O   . PHE A 60  ? 0.2334 0.2292 0.2467 -0.0077 0.0021  0.0122  60  PHE A O   
381  C  CB  . PHE A 60  ? 0.2191 0.2248 0.2159 -0.0019 -0.0039 0.0112  60  PHE A CB  
382  C  CG  . PHE A 60  ? 0.2388 0.2512 0.2279 -0.0010 -0.0048 0.0088  60  PHE A CG  
383  C  CD1 . PHE A 60  ? 0.2467 0.2566 0.2359 -0.0025 -0.0042 0.0055  60  PHE A CD1 
384  C  CD2 . PHE A 60  ? 0.2627 0.2843 0.2446 0.0015  -0.0065 0.0085  60  PHE A CD2 
385  C  CE1 . PHE A 60  ? 0.2632 0.2781 0.2456 -0.0010 -0.0043 0.0026  60  PHE A CE1 
386  C  CE2 . PHE A 60  ? 0.2556 0.2827 0.2303 0.0021  -0.0070 0.0044  60  PHE A CE2 
387  C  CZ  . PHE A 60  ? 0.2709 0.2936 0.2460 0.0010  -0.0055 0.0015  60  PHE A CZ  
388  N  N   . PRO A 61  ? 0.2147 0.2226 0.2206 -0.0019 0.0052  0.0213  61  PRO A N   
389  C  CA  . PRO A 61  ? 0.2188 0.2360 0.2175 0.0028  0.0061  0.0268  61  PRO A CA  
390  C  C   . PRO A 61  ? 0.2364 0.2540 0.2401 0.0057  0.0109  0.0376  61  PRO A C   
391  O  O   . PRO A 61  ? 0.2478 0.2586 0.2616 0.0037  0.0155  0.0417  61  PRO A O   
392  C  CB  . PRO A 61  ? 0.2389 0.2621 0.2338 0.0032  0.0076  0.0256  61  PRO A CB  
393  C  CG  . PRO A 61  ? 0.2501 0.2678 0.2550 -0.0006 0.0100  0.0250  61  PRO A CG  
394  C  CD  . PRO A 61  ? 0.2362 0.2450 0.2454 -0.0042 0.0067  0.0192  61  PRO A CD  
395  N  N   . PHE A 62  ? 0.2313 0.2576 0.2283 0.0108  0.0101  0.0425  62  PHE A N   
396  C  CA  . PHE A 62  ? 0.2591 0.2872 0.2594 0.0156  0.0145  0.0546  62  PHE A CA  
397  C  C   . PHE A 62  ? 0.2783 0.3160 0.2744 0.0193  0.0190  0.0631  62  PHE A C   
398  O  O   . PHE A 62  ? 0.2817 0.3260 0.2715 0.0185  0.0181  0.0586  62  PHE A O   
399  C  CB  . PHE A 62  ? 0.2525 0.2877 0.2480 0.0200  0.0108  0.0559  62  PHE A CB  
400  C  CG  . PHE A 62  ? 0.2384 0.2670 0.2362 0.0163  0.0061  0.0464  62  PHE A CG  
401  C  CD1 . PHE A 62  ? 0.2405 0.2555 0.2485 0.0136  0.0083  0.0457  62  PHE A CD1 
402  C  CD2 . PHE A 62  ? 0.2428 0.2783 0.2328 0.0150  0.0003  0.0376  62  PHE A CD2 
403  C  CE1 . PHE A 62  ? 0.2094 0.2193 0.2187 0.0104  0.0046  0.0372  62  PHE A CE1 
404  C  CE2 . PHE A 62  ? 0.2366 0.2659 0.2291 0.0113  -0.0031 0.0298  62  PHE A CE2 
405  C  CZ  . PHE A 62  ? 0.2415 0.2586 0.2430 0.0094  -0.0009 0.0299  62  PHE A CZ  
406  N  N   . THR A 63  ? 0.2758 0.3140 0.2761 0.0239  0.0246  0.0760  63  THR A N   
407  C  CA  . THR A 63  ? 0.2816 0.3293 0.2781 0.0281  0.0301  0.0863  63  THR A CA  
408  C  C   . THR A 63  ? 0.2914 0.3583 0.2729 0.0347  0.0267  0.0883  63  THR A C   
409  O  O   . THR A 63  ? 0.3382 0.4160 0.3141 0.0390  0.0309  0.0966  63  THR A O   
410  C  CB  . THR A 63  ? 0.3529 0.3931 0.3600 0.0308  0.0387  0.1010  63  THR A CB  
411  O  OG1 . THR A 63  ? 0.3597 0.3990 0.3677 0.0360  0.0377  0.1065  63  THR A OG1 
412  C  CG2 . THR A 63  ? 0.3848 0.4078 0.4073 0.0230  0.0430  0.0976  63  THR A CG2 
413  N  N   . SER A 64  ? 0.2816 0.3544 0.2568 0.0353  0.0193  0.0804  64  SER A N   
414  C  CA  . SER A 64  ? 0.2990 0.3918 0.2606 0.0404  0.0151  0.0796  64  SER A CA  
415  C  C   . SER A 64  ? 0.2760 0.3708 0.2319 0.0355  0.0076  0.0632  64  SER A C   
416  O  O   . SER A 64  ? 0.2606 0.3449 0.2224 0.0312  0.0042  0.0562  64  SER A O   
417  C  CB  . SER A 64  ? 0.3396 0.4413 0.3008 0.0476  0.0143  0.0896  64  SER A CB  
418  O  OG  . SER A 64  ? 0.3512 0.4744 0.3000 0.0512  0.0082  0.0854  64  SER A OG  
419  N  N   . ASN A 65  ? 0.2776 0.3860 0.2221 0.0364  0.0054  0.0570  65  ASN A N   
420  C  CA  . ASN A 65  ? 0.2515 0.3621 0.1908 0.0320  -0.0009 0.0415  65  ASN A CA  
421  C  C   . ASN A 65  ? 0.2659 0.3891 0.2020 0.0337  -0.0068 0.0388  65  ASN A C   
422  O  O   . ASN A 65  ? 0.2813 0.4036 0.2164 0.0287  -0.0117 0.0260  65  ASN A O   
423  C  CB  . ASN A 65  ? 0.2693 0.3877 0.1989 0.0318  -0.0003 0.0340  65  ASN A CB  
424  C  CG  . ASN A 65  ? 0.2616 0.3657 0.1969 0.0284  0.0042  0.0328  65  ASN A CG  
425  O  OD1 . ASN A 65  ? 0.2541 0.3423 0.1989 0.0239  0.0040  0.0306  65  ASN A OD1 
426  N  ND2 . ASN A 65  ? 0.2706 0.3821 0.2004 0.0311  0.0084  0.0346  65  ASN A ND2 
427  N  N   . ALA A 66  ? 0.2750 0.4099 0.2105 0.0406  -0.0061 0.0510  66  ALA A N   
428  C  CA  . ALA A 66  ? 0.2718 0.4177 0.2080 0.0425  -0.0115 0.0501  66  ALA A CA  
429  C  C   . ALA A 66  ? 0.2856 0.4144 0.2335 0.0380  -0.0125 0.0471  66  ALA A C   
430  O  O   . ALA A 66  ? 0.3057 0.4424 0.2558 0.0385  -0.0168 0.0448  66  ALA A O   
431  C  CB  . ALA A 66  ? 0.2989 0.4607 0.2329 0.0525  -0.0096 0.0662  66  ALA A CB  
432  N  N   . LEU A 67  ? 0.2508 0.3584 0.2063 0.0338  -0.0085 0.0471  67  LEU A N   
433  C  CA  . LEU A 67  ? 0.2521 0.3438 0.2167 0.0284  -0.0096 0.0413  67  LEU A CA  
434  C  C   . LEU A 67  ? 0.2621 0.3427 0.2258 0.0209  -0.0109 0.0288  67  LEU A C   
435  O  O   . LEU A 67  ? 0.2675 0.3444 0.2329 0.0165  -0.0144 0.0199  67  LEU A O   
436  C  CB  . LEU A 67  ? 0.2657 0.3422 0.2408 0.0299  -0.0040 0.0510  67  LEU A CB  
437  C  CG  . LEU A 67  ? 0.2600 0.3432 0.2386 0.0380  -0.0015 0.0645  67  LEU A CG  
438  C  CD1 . LEU A 67  ? 0.3069 0.3732 0.2961 0.0389  0.0060  0.0740  67  LEU A CD1 
439  C  CD2 . LEU A 67  ? 0.3124 0.4020 0.2938 0.0393  -0.0061 0.0616  67  LEU A CD2 
440  N  N   . ASN A 68  ? 0.2591 0.3355 0.2203 0.0200  -0.0077 0.0287  68  ASN A N   
441  C  CA  . ASN A 68  ? 0.2392 0.3046 0.2007 0.0143  -0.0082 0.0186  68  ASN A CA  
442  C  C   . ASN A 68  ? 0.2508 0.3215 0.2059 0.0113  -0.0126 0.0066  68  ASN A C   
443  O  O   . ASN A 68  ? 0.2701 0.3299 0.2274 0.0065  -0.0136 -0.0013 68  ASN A O   
444  C  CB  . ASN A 68  ? 0.2374 0.3011 0.1974 0.0150  -0.0039 0.0210  68  ASN A CB  
445  C  CG  . ASN A 68  ? 0.2516 0.3060 0.2209 0.0152  0.0010  0.0301  68  ASN A CG  
446  O  OD1 . ASN A 68  ? 0.2469 0.2902 0.2243 0.0125  0.0009  0.0299  68  ASN A OD1 
447  N  ND2 . ASN A 68  ? 0.2686 0.3278 0.2370 0.0181  0.0057  0.0376  68  ASN A ND2 
448  N  N   . ARG A 69  ? 0.2654 0.3531 0.2126 0.0139  -0.0149 0.0049  69  ARG A N   
449  C  CA  . ARG A 69  ? 0.2782 0.3700 0.2200 0.0100  -0.0181 -0.0084 69  ARG A CA  
450  C  C   . ARG A 69  ? 0.2828 0.3732 0.2294 0.0056  -0.0220 -0.0147 69  ARG A C   
451  O  O   . ARG A 69  ? 0.3052 0.3919 0.2510 0.0004  -0.0235 -0.0260 69  ARG A O   
452  C  CB  . ARG A 69  ? 0.3131 0.4253 0.2446 0.0134  -0.0195 -0.0108 69  ARG A CB  
453  C  CG  . ARG A 69  ? 0.3057 0.4375 0.2352 0.0172  -0.0232 -0.0063 69  ARG A CG  
454  C  CD  . ARG A 69  ? 0.3171 0.4706 0.2351 0.0195  -0.0254 -0.0120 69  ARG A CD  
455  N  NE  . ARG A 69  ? 0.3557 0.5108 0.2672 0.0241  -0.0206 -0.0059 69  ARG A NE  
456  C  CZ  . ARG A 69  ? 0.3376 0.5049 0.2454 0.0316  -0.0183 0.0078  69  ARG A CZ  
457  N  NH1 . ARG A 69  ? 0.3568 0.5372 0.2656 0.0364  -0.0208 0.0166  69  ARG A NH1 
458  N  NH2 . ARG A 69  ? 0.3431 0.5097 0.2465 0.0349  -0.0129 0.0135  69  ARG A NH2 
459  N  N   . HIS A 70  ? 0.2583 0.3509 0.2107 0.0075  -0.0230 -0.0075 70  HIS A N   
460  C  CA  . HIS A 70  ? 0.2750 0.3719 0.2315 0.0041  -0.0268 -0.0131 70  HIS A CA  
461  C  C   . HIS A 70  ? 0.2558 0.3356 0.2181 -0.0023 -0.0262 -0.0197 70  HIS A C   
462  O  O   . HIS A 70  ? 0.2683 0.3509 0.2317 -0.0072 -0.0285 -0.0288 70  HIS A O   
463  C  CB  . HIS A 70  ? 0.2950 0.4022 0.2558 0.0094  -0.0278 -0.0034 70  HIS A CB  
464  C  CG  . HIS A 70  ? 0.3088 0.4362 0.2630 0.0162  -0.0289 0.0031  70  HIS A CG  
465  N  ND1 . HIS A 70  ? 0.3344 0.4804 0.2806 0.0156  -0.0326 -0.0048 70  HIS A ND1 
466  C  CD2 . HIS A 70  ? 0.3513 0.4834 0.3053 0.0239  -0.0261 0.0169  70  HIS A CD2 
467  C  CE1 . HIS A 70  ? 0.3373 0.5007 0.2776 0.0232  -0.0327 0.0043  70  HIS A CE1 
468  N  NE2 . HIS A 70  ? 0.3448 0.4994 0.2899 0.0286  -0.0285 0.0183  70  HIS A NE2 
469  N  N   . PRO A 71  ? 0.2551 0.3182 0.2214 -0.0025 -0.0230 -0.0156 71  PRO A N   
470  C  CA  . PRO A 71  ? 0.2759 0.3247 0.2460 -0.0078 -0.0224 -0.0214 71  PRO A CA  
471  C  C   . PRO A 71  ? 0.3002 0.3447 0.2663 -0.0118 -0.0221 -0.0311 71  PRO A C   
472  O  O   . PRO A 71  ? 0.3312 0.3664 0.3001 -0.0163 -0.0217 -0.0364 71  PRO A O   
473  C  CB  . PRO A 71  ? 0.2627 0.2983 0.2363 -0.0064 -0.0194 -0.0153 71  PRO A CB  
474  C  CG  . PRO A 71  ? 0.3103 0.3521 0.2854 -0.0013 -0.0183 -0.0058 71  PRO A CG  
475  C  CD  . PRO A 71  ? 0.2763 0.3339 0.2447 0.0017  -0.0197 -0.0055 71  PRO A CD  
476  N  N   . LEU A 72  ? 0.2528 0.3032 0.2125 -0.0099 -0.0217 -0.0332 72  LEU A N   
477  C  CA  . LEU A 72  ? 0.3057 0.3511 0.2618 -0.0129 -0.0205 -0.0428 72  LEU A CA  
478  C  C   . LEU A 72  ? 0.2968 0.3562 0.2492 -0.0154 -0.0232 -0.0522 72  LEU A C   
479  O  O   . LEU A 72  ? 0.3145 0.3714 0.2631 -0.0174 -0.0219 -0.0613 72  LEU A O   
480  C  CB  . LEU A 72  ? 0.2843 0.3263 0.2362 -0.0091 -0.0175 -0.0402 72  LEU A CB  
481  C  CG  . LEU A 72  ? 0.2867 0.3178 0.2433 -0.0071 -0.0153 -0.0317 72  LEU A CG  
482  C  CD1 . LEU A 72  ? 0.3106 0.3420 0.2642 -0.0035 -0.0123 -0.0290 72  LEU A CD1 
483  C  CD2 . LEU A 72  ? 0.3602 0.3764 0.3213 -0.0105 -0.0145 -0.0344 72  LEU A CD2 
484  N  N   . ASP A 73  ? 0.2618 0.3363 0.2156 -0.0153 -0.0268 -0.0509 73  ASP A N   
485  C  CA  . ASP A 73  ? 0.2760 0.3681 0.2269 -0.0179 -0.0302 -0.0605 73  ASP A CA  
486  C  C   . ASP A 73  ? 0.2910 0.3732 0.2451 -0.0259 -0.0291 -0.0737 73  ASP A C   
487  O  O   . ASP A 73  ? 0.2704 0.3386 0.2315 -0.0298 -0.0274 -0.0735 73  ASP A O   
488  C  CB  . ASP A 73  ? 0.2943 0.4027 0.2494 -0.0167 -0.0343 -0.0559 73  ASP A CB  
489  C  CG  . ASP A 73  ? 0.3134 0.4462 0.2654 -0.0182 -0.0389 -0.0645 73  ASP A CG  
490  O  OD1 . ASP A 73  ? 0.3530 0.4865 0.3077 -0.0259 -0.0399 -0.0778 73  ASP A OD1 
491  O  OD2 . ASP A 73  ? 0.3377 0.4899 0.2850 -0.0118 -0.0415 -0.0578 73  ASP A OD2 
492  N  N   . LEU A 74  ? 0.3075 0.3966 0.2564 -0.0283 -0.0294 -0.0852 74  LEU A N   
493  C  CA  . LEU A 74  ? 0.3032 0.3812 0.2561 -0.0362 -0.0272 -0.0985 74  LEU A CA  
494  C  C   . LEU A 74  ? 0.3434 0.4246 0.3057 -0.0431 -0.0291 -0.1025 74  LEU A C   
495  O  O   . LEU A 74  ? 0.3201 0.3852 0.2890 -0.0494 -0.0256 -0.1080 74  LEU A O   
496  C  CB  . LEU A 74  ? 0.3491 0.4374 0.2952 -0.0378 -0.0275 -0.1120 74  LEU A CB  
497  C  CG  . LEU A 74  ? 0.3959 0.4794 0.3332 -0.0317 -0.0242 -0.1105 74  LEU A CG  
498  C  CD1 . LEU A 74  ? 0.4195 0.5163 0.3497 -0.0336 -0.0248 -0.1255 74  LEU A CD1 
499  C  CD2 . LEU A 74  ? 0.3725 0.4288 0.3137 -0.0318 -0.0182 -0.1086 74  LEU A CD2 
500  N  N   . ARG A 75  ? 0.2795 0.3821 0.2433 -0.0418 -0.0342 -0.0992 75  ARG A N   
501  C  CA  . ARG A 75  ? 0.3048 0.4134 0.2786 -0.0482 -0.0360 -0.1028 75  ARG A CA  
502  C  C   . ARG A 75  ? 0.3053 0.3959 0.2859 -0.0481 -0.0328 -0.0933 75  ARG A C   
503  O  O   . ARG A 75  ? 0.2800 0.3643 0.2692 -0.0550 -0.0310 -0.0976 75  ARG A O   
504  C  CB  . ARG A 75  ? 0.2951 0.4328 0.2687 -0.0449 -0.0422 -0.1000 75  ARG A CB  
505  C  CG  . ARG A 75  ? 0.3355 0.4934 0.3029 -0.0445 -0.0453 -0.1085 75  ARG A CG  
506  C  CD  . ARG A 75  ? 0.3550 0.5409 0.3215 -0.0383 -0.0507 -0.1013 75  ARG A CD  
507  N  NE  . ARG A 75  ? 0.3266 0.5153 0.2861 -0.0285 -0.0515 -0.0871 75  ARG A NE  
508  C  CZ  . ARG A 75  ? 0.2892 0.4978 0.2483 -0.0208 -0.0549 -0.0763 75  ARG A CZ  
509  N  NH1 . ARG A 75  ? 0.3415 0.5714 0.3063 -0.0215 -0.0587 -0.0787 75  ARG A NH1 
510  N  NH2 . ARG A 75  ? 0.3106 0.5134 0.2653 -0.0116 -0.0526 -0.0611 75  ARG A NH2 
511  N  N   . VAL A 76  ? 0.2688 0.3524 0.2460 -0.0405 -0.0318 -0.0806 76  VAL A N   
512  C  CA  . VAL A 76  ? 0.2690 0.3361 0.2512 -0.0400 -0.0288 -0.0724 76  VAL A CA  
513  C  C   . VAL A 76  ? 0.2764 0.3210 0.2592 -0.0438 -0.0237 -0.0762 76  VAL A C   
514  O  O   . VAL A 76  ? 0.2671 0.3015 0.2562 -0.0481 -0.0210 -0.0764 76  VAL A O   
515  C  CB  . VAL A 76  ? 0.2854 0.3511 0.2642 -0.0316 -0.0288 -0.0598 76  VAL A CB  
516  C  CG1 . VAL A 76  ? 0.2710 0.3186 0.2532 -0.0311 -0.0255 -0.0532 76  VAL A CG1 
517  C  CG2 . VAL A 76  ? 0.3028 0.3887 0.2830 -0.0273 -0.0327 -0.0542 76  VAL A CG2 
518  N  N   . ILE A 77  ? 0.2692 0.3066 0.2457 -0.0417 -0.0219 -0.0787 77  ILE A N   
519  C  CA  . ILE A 77  ? 0.2743 0.2907 0.2516 -0.0439 -0.0167 -0.0815 77  ILE A CA  
520  C  C   . ILE A 77  ? 0.3128 0.3245 0.2969 -0.0526 -0.0144 -0.0915 77  ILE A C   
521  O  O   . ILE A 77  ? 0.3044 0.2998 0.2932 -0.0552 -0.0100 -0.0897 77  ILE A O   
522  C  CB  . ILE A 77  ? 0.3035 0.3160 0.2734 -0.0399 -0.0151 -0.0840 77  ILE A CB  
523  C  CG1 . ILE A 77  ? 0.3054 0.3202 0.2710 -0.0322 -0.0161 -0.0726 77  ILE A CG1 
524  C  CG2 . ILE A 77  ? 0.3430 0.3347 0.3146 -0.0414 -0.0093 -0.0876 77  ILE A CG2 
525  C  CD1 . ILE A 77  ? 0.3093 0.3250 0.2679 -0.0276 -0.0147 -0.0738 77  ILE A CD1 
526  N  N   A SER A 78  ? 0.2935 0.3204 0.2786 -0.0574 -0.0172 -0.1022 78  SER A N   
527  N  N   B SER A 78  ? 0.2934 0.3205 0.2785 -0.0573 -0.0173 -0.1022 78  SER A N   
528  C  CA  A SER A 78  ? 0.3131 0.3363 0.3064 -0.0670 -0.0147 -0.1135 78  SER A CA  
529  C  CA  B SER A 78  ? 0.3131 0.3369 0.3063 -0.0670 -0.0149 -0.1136 78  SER A CA  
530  C  C   A SER A 78  ? 0.3018 0.3233 0.3043 -0.0710 -0.0137 -0.1085 78  SER A C   
531  C  C   B SER A 78  ? 0.3019 0.3236 0.3043 -0.0710 -0.0137 -0.1087 78  SER A C   
532  O  O   A SER A 78  ? 0.3150 0.3211 0.3243 -0.0769 -0.0082 -0.1112 78  SER A O   
533  O  O   B SER A 78  ? 0.3144 0.3209 0.3237 -0.0770 -0.0083 -0.1115 78  SER A O   
534  C  CB  A SER A 78  ? 0.3301 0.3741 0.3232 -0.0707 -0.0188 -0.1249 78  SER A CB  
535  C  CB  B SER A 78  ? 0.3301 0.3755 0.3230 -0.0705 -0.0192 -0.1247 78  SER A CB  
536  O  OG  A SER A 78  ? 0.3709 0.4134 0.3558 -0.0672 -0.0180 -0.1299 78  SER A OG  
537  O  OG  B SER A 78  ? 0.3510 0.3903 0.3521 -0.0776 -0.0156 -0.1328 78  SER A OG  
538  N  N   . VAL A 79  ? 0.2829 0.3196 0.2860 -0.0674 -0.0181 -0.1008 79  VAL A N   
539  C  CA  . VAL A 79  ? 0.2661 0.3022 0.2775 -0.0702 -0.0168 -0.0958 79  VAL A CA  
540  C  C   . VAL A 79  ? 0.2818 0.2949 0.2925 -0.0680 -0.0111 -0.0874 79  VAL A C   
541  O  O   . VAL A 79  ? 0.2946 0.2979 0.3121 -0.0733 -0.0064 -0.0875 79  VAL A O   
542  C  CB  . VAL A 79  ? 0.2565 0.3116 0.2680 -0.0648 -0.0219 -0.0882 79  VAL A CB  
543  C  CG1 . VAL A 79  ? 0.2816 0.3328 0.3004 -0.0658 -0.0194 -0.0815 79  VAL A CG1 
544  C  CG2 . VAL A 79  ? 0.2782 0.3594 0.2925 -0.0674 -0.0275 -0.0959 79  VAL A CG2 
545  N  N   . VAL A 80  ? 0.2621 0.2679 0.2648 -0.0600 -0.0114 -0.0793 80  VAL A N   
546  C  CA  . VAL A 80  ? 0.2701 0.2584 0.2716 -0.0570 -0.0072 -0.0709 80  VAL A CA  
547  C  C   . VAL A 80  ? 0.3115 0.2812 0.3146 -0.0605 -0.0010 -0.0746 80  VAL A C   
548  O  O   . VAL A 80  ? 0.2978 0.2554 0.3041 -0.0618 0.0037  -0.0700 80  VAL A O   
549  C  CB  . VAL A 80  ? 0.2637 0.2508 0.2577 -0.0485 -0.0092 -0.0631 80  VAL A CB  
550  C  CG1 . VAL A 80  ? 0.2961 0.2682 0.2886 -0.0453 -0.0056 -0.0554 80  VAL A CG1 
551  C  CG2 . VAL A 80  ? 0.2989 0.3018 0.2928 -0.0450 -0.0139 -0.0587 80  VAL A CG2 
552  N  N   . GLU A 81  ? 0.2926 0.2597 0.2936 -0.0618 -0.0005 -0.0830 81  GLU A N   
553  C  CA  . GLU A 81  ? 0.3502 0.2982 0.3538 -0.0649 0.0062  -0.0873 81  GLU A CA  
554  C  C   . GLU A 81  ? 0.3595 0.3034 0.3734 -0.0741 0.0105  -0.0917 81  GLU A C   
555  O  O   . GLU A 81  ? 0.3634 0.2890 0.3807 -0.0753 0.0174  -0.0881 81  GLU A O   
556  C  CB  . GLU A 81  ? 0.3565 0.3052 0.3569 -0.0655 0.0060  -0.0981 81  GLU A CB  
557  C  CG  . GLU A 81  ? 0.3831 0.3319 0.3742 -0.0565 0.0042  -0.0935 81  GLU A CG  
558  C  CD  . GLU A 81  ? 0.4272 0.3765 0.4149 -0.0569 0.0050  -0.1047 81  GLU A CD  
559  O  OE1 . GLU A 81  ? 0.4576 0.4100 0.4497 -0.0646 0.0058  -0.1172 81  GLU A OE1 
560  O  OE2 . GLU A 81  ? 0.4727 0.4202 0.4537 -0.0499 0.0051  -0.1017 81  GLU A OE2 
561  N  N   . GLU A 82  ? 0.3465 0.3080 0.3659 -0.0805 0.0067  -0.0991 82  GLU A N   
562  C  CA  . GLU A 82  ? 0.3377 0.2979 0.3687 -0.0903 0.0108  -0.1040 82  GLU A CA  
563  C  C   . GLU A 82  ? 0.3481 0.3040 0.3820 -0.0889 0.0137  -0.0921 82  GLU A C   
564  O  O   . GLU A 82  ? 0.3726 0.3147 0.4134 -0.0939 0.0209  -0.0907 82  GLU A O   
565  C  CB  . GLU A 82  ? 0.3706 0.3554 0.4063 -0.0948 0.0049  -0.1122 82  GLU A CB  
566  C  CG  . GLU A 82  ? 0.4198 0.4075 0.4678 -0.1028 0.0083  -0.1145 82  GLU A CG  
567  C  CD  . GLU A 82  ? 0.5490 0.5221 0.6023 -0.1077 0.0146  -0.1209 82  GLU A CD  
568  O  OE1 . GLU A 82  ? 0.5513 0.5140 0.5988 -0.1046 0.0158  -0.1246 82  GLU A OE1 
569  O  OE2 . GLU A 82  ? 0.6272 0.5996 0.6911 -0.1146 0.0187  -0.1224 82  GLU A OE2 
570  N  N   . LEU A 83  ? 0.2970 0.2641 0.3258 -0.0822 0.0087  -0.0836 83  LEU A N   
571  C  CA  . LEU A 83  ? 0.2867 0.2519 0.3176 -0.0807 0.0113  -0.0737 83  LEU A CA  
572  C  C   . LEU A 83  ? 0.3089 0.2534 0.3348 -0.0760 0.0172  -0.0647 83  LEU A C   
573  O  O   . LEU A 83  ? 0.3496 0.2859 0.3799 -0.0785 0.0232  -0.0597 83  LEU A O   
574  C  CB  . LEU A 83  ? 0.2656 0.2471 0.2927 -0.0746 0.0051  -0.0682 83  LEU A CB  
575  C  CG  . LEU A 83  ? 0.2584 0.2400 0.2870 -0.0725 0.0075  -0.0593 83  LEU A CG  
576  C  CD1 . LEU A 83  ? 0.2998 0.2905 0.3400 -0.0807 0.0100  -0.0631 83  LEU A CD1 
577  C  CD2 . LEU A 83  ? 0.3008 0.2936 0.3246 -0.0651 0.0021  -0.0542 83  LEU A CD2 
578  N  N   . LEU A 84  ? 0.3129 0.2503 0.3301 -0.0688 0.0157  -0.0619 84  LEU A N   
579  C  CA  . LEU A 84  ? 0.3260 0.2476 0.3381 -0.0628 0.0201  -0.0526 84  LEU A CA  
580  C  C   . LEU A 84  ? 0.3557 0.2581 0.3710 -0.0652 0.0276  -0.0544 84  LEU A C   
581  O  O   . LEU A 84  ? 0.3802 0.2694 0.3937 -0.0614 0.0331  -0.0455 84  LEU A O   
582  C  CB  . LEU A 84  ? 0.3068 0.2305 0.3097 -0.0540 0.0155  -0.0487 84  LEU A CB  
583  C  CG  . LEU A 84  ? 0.2977 0.2319 0.2964 -0.0490 0.0111  -0.0418 84  LEU A CG  
584  C  CD1 . LEU A 84  ? 0.3084 0.2592 0.3110 -0.0522 0.0067  -0.0454 84  LEU A CD1 
585  C  CD2 . LEU A 84  ? 0.2852 0.2201 0.2767 -0.0416 0.0075  -0.0389 84  LEU A CD2 
586  N  N   . GLY A 85  ? 0.3372 0.2378 0.3568 -0.0709 0.0283  -0.0657 85  GLY A N   
587  C  CA  . GLY A 85  ? 0.3813 0.2615 0.4047 -0.0730 0.0363  -0.0685 85  GLY A CA  
588  C  C   . GLY A 85  ? 0.4014 0.2708 0.4175 -0.0642 0.0372  -0.0654 85  GLY A C   
589  O  O   . GLY A 85  ? 0.4420 0.2921 0.4604 -0.0625 0.0449  -0.0626 85  GLY A O   
590  N  N   . THR A 86  ? 0.3840 0.2655 0.3923 -0.0583 0.0301  -0.0655 86  THR A N   
591  C  CA  . THR A 86  ? 0.3956 0.2700 0.3976 -0.0500 0.0305  -0.0633 86  THR A CA  
592  C  C   . THR A 86  ? 0.4113 0.3010 0.4083 -0.0485 0.0235  -0.0700 86  THR A C   
593  O  O   . THR A 86  ? 0.3796 0.2863 0.3755 -0.0506 0.0173  -0.0713 86  THR A O   
594  C  CB  . THR A 86  ? 0.3977 0.2698 0.3943 -0.0409 0.0304  -0.0494 86  THR A CB  
595  O  OG1 . THR A 86  ? 0.4028 0.2702 0.3949 -0.0331 0.0307  -0.0479 86  THR A OG1 
596  C  CG2 . THR A 86  ? 0.3789 0.2689 0.3715 -0.0394 0.0230  -0.0452 86  THR A CG2 
597  N  N   . THR A 87  ? 0.3805 0.2641 0.3743 -0.0441 0.0252  -0.0734 87  THR A N   
598  C  CA  . THR A 87  ? 0.3797 0.2772 0.3673 -0.0408 0.0196  -0.0772 87  THR A CA  
599  C  C   . THR A 87  ? 0.3737 0.2746 0.3556 -0.0316 0.0172  -0.0668 87  THR A C   
600  O  O   . THR A 87  ? 0.3622 0.2752 0.3396 -0.0286 0.0130  -0.0679 87  THR A O   
601  C  CB  . THR A 87  ? 0.3857 0.2775 0.3729 -0.0417 0.0228  -0.0889 87  THR A CB  
602  O  OG1 . THR A 87  ? 0.4458 0.3189 0.4338 -0.0359 0.0296  -0.0850 87  THR A OG1 
603  C  CG2 . THR A 87  ? 0.4478 0.3381 0.4416 -0.0521 0.0249  -0.1017 87  THR A CG2 
604  N  N   . ASP A 88  ? 0.3525 0.2446 0.3349 -0.0272 0.0197  -0.0566 88  ASP A N   
605  C  CA  . ASP A 88  ? 0.3309 0.2274 0.3091 -0.0190 0.0174  -0.0479 88  ASP A CA  
606  C  C   . ASP A 88  ? 0.3553 0.2657 0.3320 -0.0196 0.0115  -0.0430 88  ASP A C   
607  O  O   . ASP A 88  ? 0.3524 0.2620 0.3292 -0.0183 0.0114  -0.0357 88  ASP A O   
608  C  CB  . ASP A 88  ? 0.3815 0.2648 0.3606 -0.0132 0.0226  -0.0396 88  ASP A CB  
609  C  CG  . ASP A 88  ? 0.3994 0.2876 0.3755 -0.0043 0.0210  -0.0334 88  ASP A CG  
610  O  OD1 . ASP A 88  ? 0.3945 0.2945 0.3683 -0.0032 0.0168  -0.0360 88  ASP A OD1 
611  O  OD2 . ASP A 88  ? 0.4367 0.3181 0.4130 0.0018  0.0242  -0.0254 88  ASP A OD2 
612  N  N   . LEU A 89  ? 0.2802 0.2037 0.2553 -0.0213 0.0069  -0.0471 89  LEU A N   
613  C  CA  . LEU A 89  ? 0.2844 0.2200 0.2592 -0.0224 0.0020  -0.0436 89  LEU A CA  
614  C  C   . LEU A 89  ? 0.2636 0.2074 0.2358 -0.0173 -0.0010 -0.0392 89  LEU A C   
615  O  O   . LEU A 89  ? 0.2562 0.2006 0.2264 -0.0140 -0.0003 -0.0405 89  LEU A O   
616  C  CB  . LEU A 89  ? 0.2707 0.2162 0.2467 -0.0278 -0.0007 -0.0502 89  LEU A CB  
617  C  CG  . LEU A 89  ? 0.2875 0.2276 0.2680 -0.0345 0.0020  -0.0563 89  LEU A CG  
618  C  CD1 . LEU A 89  ? 0.3141 0.2686 0.2959 -0.0391 -0.0017 -0.0632 89  LEU A CD1 
619  C  CD2 . LEU A 89  ? 0.2843 0.2189 0.2680 -0.0358 0.0040  -0.0501 89  LEU A CD2 
620  N  N   . ARG A 90  ? 0.2481 0.1983 0.2211 -0.0171 -0.0039 -0.0344 90  ARG A N   
621  C  CA  . ARG A 90  ? 0.2348 0.1930 0.2072 -0.0139 -0.0064 -0.0307 90  ARG A CA  
622  C  C   . ARG A 90  ? 0.2582 0.2249 0.2323 -0.0159 -0.0094 -0.0296 90  ARG A C   
623  O  O   . ARG A 90  ? 0.2247 0.1909 0.2006 -0.0186 -0.0097 -0.0295 90  ARG A O   
624  C  CB  . ARG A 90  ? 0.2567 0.2129 0.2296 -0.0104 -0.0063 -0.0254 90  ARG A CB  
625  C  CG  . ARG A 90  ? 0.2709 0.2202 0.2429 -0.0064 -0.0034 -0.0241 90  ARG A CG  
626  C  CD  . ARG A 90  ? 0.2727 0.2246 0.2441 -0.0034 -0.0026 -0.0260 90  ARG A CD  
627  N  NE  . ARG A 90  ? 0.2793 0.2250 0.2508 0.0016  0.0005  -0.0240 90  ARG A NE  
628  C  CZ  . ARG A 90  ? 0.2889 0.2232 0.2599 0.0023  0.0046  -0.0262 90  ARG A CZ  
629  N  NH1 . ARG A 90  ? 0.2967 0.2258 0.2674 -0.0027 0.0059  -0.0323 90  ARG A NH1 
630  N  NH2 . ARG A 90  ? 0.3392 0.2674 0.3109 0.0080  0.0077  -0.0222 90  ARG A NH2 
631  N  N   . MET A 91  ? 0.2219 0.1962 0.1958 -0.0142 -0.0108 -0.0281 91  MET A N   
632  C  CA  . MET A 91  ? 0.2052 0.1863 0.1817 -0.0146 -0.0127 -0.0252 91  MET A CA  
633  C  C   . MET A 91  ? 0.2152 0.1939 0.1946 -0.0138 -0.0128 -0.0216 91  MET A C   
634  O  O   . MET A 91  ? 0.2598 0.2387 0.2400 -0.0119 -0.0124 -0.0197 91  MET A O   
635  C  CB  . MET A 91  ? 0.2484 0.2378 0.2239 -0.0125 -0.0132 -0.0235 91  MET A CB  
636  C  CG  . MET A 91  ? 0.2573 0.2529 0.2358 -0.0121 -0.0143 -0.0196 91  MET A CG  
637  S  SD  . MET A 91  ? 0.2965 0.3021 0.2736 -0.0085 -0.0139 -0.0150 91  MET A SD  
638  C  CE  . MET A 91  ? 0.2658 0.2664 0.2473 -0.0075 -0.0115 -0.0106 91  MET A CE  
639  N  N   . THR A 92  ? 0.2115 0.1893 0.1927 -0.0155 -0.0132 -0.0215 92  THR A N   
640  C  CA  . THR A 92  ? 0.2048 0.1811 0.1881 -0.0152 -0.0133 -0.0199 92  THR A CA  
641  C  C   . THR A 92  ? 0.2304 0.2103 0.2181 -0.0145 -0.0136 -0.0179 92  THR A C   
642  O  O   . THR A 92  ? 0.2385 0.2181 0.2286 -0.0144 -0.0135 -0.0176 92  THR A O   
643  C  CB  . THR A 92  ? 0.1986 0.1735 0.1822 -0.0170 -0.0130 -0.0209 92  THR A CB  
644  O  OG1 . THR A 92  ? 0.2274 0.1991 0.2088 -0.0186 -0.0119 -0.0226 92  THR A OG1 
645  C  CG2 . THR A 92  ? 0.2306 0.2041 0.2139 -0.0164 -0.0128 -0.0205 92  THR A CG2 
646  N  N   . SER A 93  ? 0.2067 0.1903 0.1959 -0.0141 -0.0136 -0.0164 93  SER A N   
647  C  CA  . SER A 93  ? 0.2204 0.2055 0.2147 -0.0130 -0.0127 -0.0133 93  SER A CA  
648  C  C   . SER A 93  ? 0.2162 0.2075 0.2102 -0.0110 -0.0128 -0.0102 93  SER A C   
649  O  O   . SER A 93  ? 0.2163 0.2118 0.2074 -0.0114 -0.0142 -0.0121 93  SER A O   
650  C  CB  . SER A 93  ? 0.2651 0.2477 0.2628 -0.0138 -0.0122 -0.0145 93  SER A CB  
651  O  OG  . SER A 93  ? 0.3471 0.3290 0.3509 -0.0125 -0.0103 -0.0117 93  SER A OG  
652  N  N   . SER A 94  ? 0.2079 0.2006 0.2052 -0.0089 -0.0110 -0.0054 94  SER A N   
653  C  CA  . SER A 94  ? 0.2109 0.2107 0.2085 -0.0057 -0.0108 -0.0006 94  SER A CA  
654  C  C   . SER A 94  ? 0.2032 0.2000 0.2076 -0.0035 -0.0073 0.0056  94  SER A C   
655  O  O   . SER A 94  ? 0.2150 0.2069 0.2227 -0.0050 -0.0052 0.0062  94  SER A O   
656  C  CB  . SER A 94  ? 0.2205 0.2284 0.2118 -0.0043 -0.0118 -0.0001 94  SER A CB  
657  O  OG  . SER A 94  ? 0.2446 0.2620 0.2356 -0.0003 -0.0118 0.0053  94  SER A OG  
658  N  N   . PHE A 95  ? 0.1869 0.1866 0.1946 -0.0001 -0.0064 0.0102  95  PHE A N   
659  C  CA  . PHE A 95  ? 0.1921 0.1869 0.2072 0.0026  -0.0019 0.0169  95  PHE A CA  
660  C  C   . PHE A 95  ? 0.1944 0.1971 0.2104 0.0086  -0.0015 0.0240  95  PHE A C   
661  O  O   . PHE A 95  ? 0.2192 0.2311 0.2315 0.0096  -0.0051 0.0219  95  PHE A O   
662  C  CB  . PHE A 95  ? 0.2076 0.1913 0.2300 -0.0002 0.0002  0.0127  95  PHE A CB  
663  C  CG  . PHE A 95  ? 0.2436 0.2274 0.2664 -0.0001 -0.0014 0.0084  95  PHE A CG  
664  C  CD1 . PHE A 95  ? 0.2414 0.2251 0.2697 0.0043  0.0010  0.0126  95  PHE A CD1 
665  C  CD2 . PHE A 95  ? 0.2383 0.2223 0.2562 -0.0039 -0.0045 0.0009  95  PHE A CD2 
666  C  CE1 . PHE A 95  ? 0.2507 0.2357 0.2800 0.0046  0.0000  0.0086  95  PHE A CE1 
667  C  CE2 . PHE A 95  ? 0.2569 0.2419 0.2755 -0.0039 -0.0052 -0.0025 95  PHE A CE2 
668  C  CZ  . PHE A 95  ? 0.2516 0.2375 0.2759 0.0002  -0.0030 0.0010  95  PHE A CZ  
669  N  N   . ILE A 96  ? 0.1930 0.1926 0.2149 0.0126  0.0033  0.0328  96  ILE A N   
670  C  CA  . ILE A 96  ? 0.2168 0.2229 0.2411 0.0198  0.0047  0.0414  96  ILE A CA  
671  C  C   . ILE A 96  ? 0.2295 0.2229 0.2646 0.0212  0.0097  0.0431  96  ILE A C   
672  O  O   . ILE A 96  ? 0.2304 0.2106 0.2713 0.0170  0.0133  0.0402  96  ILE A O   
673  C  CB  . ILE A 96  ? 0.2163 0.2308 0.2379 0.0254  0.0070  0.0527  96  ILE A CB  
674  C  CG1 . ILE A 96  ? 0.2193 0.2222 0.2464 0.0235  0.0131  0.0571  96  ILE A CG1 
675  C  CG2 . ILE A 96  ? 0.2430 0.2727 0.2533 0.0250  0.0017  0.0497  96  ILE A CG2 
676  C  CD1 . ILE A 96  ? 0.2351 0.2455 0.2599 0.0294  0.0169  0.0698  96  ILE A CD1 
677  N  N   . GLN A 97  ? 0.2276 0.2257 0.2659 0.0270  0.0100  0.0471  97  GLN A N   
678  C  CA  . GLN A 97  ? 0.2505 0.2360 0.2996 0.0293  0.0155  0.0484  97  GLN A CA  
679  C  C   . GLN A 97  ? 0.2777 0.2710 0.3306 0.0392  0.0174  0.0588  97  GLN A C   
680  O  O   . GLN A 97  ? 0.2661 0.2769 0.3135 0.0426  0.0124  0.0605  97  GLN A O   
681  C  CB  . GLN A 97  ? 0.2909 0.2707 0.3412 0.0241  0.0137  0.0363  97  GLN A CB  
682  C  CG  . GLN A 97  ? 0.3349 0.2988 0.3959 0.0244  0.0200  0.0342  97  GLN A CG  
683  C  CD  . GLN A 97  ? 0.3767 0.3364 0.4370 0.0189  0.0183  0.0216  97  GLN A CD  
684  O  OE1 . GLN A 97  ? 0.4264 0.3957 0.4810 0.0182  0.0137  0.0174  97  GLN A OE1 
685  N  NE2 . GLN A 97  ? 0.3754 0.3212 0.4416 0.0147  0.0223  0.0154  97  GLN A NE2 
686  N  N   . ALA A 98  ? 0.2573 0.2380 0.3204 0.0437  0.0249  0.0657  98  ALA A N   
687  C  CA  . ALA A 98  ? 0.2803 0.2653 0.3496 0.0542  0.0281  0.0758  98  ALA A CA  
688  C  C   . ALA A 98  ? 0.3184 0.2911 0.3968 0.0541  0.0316  0.0690  98  ALA A C   
689  O  O   . ALA A 98  ? 0.3313 0.2868 0.4146 0.0478  0.0354  0.0610  98  ALA A O   
690  C  CB  . ALA A 98  ? 0.3131 0.2914 0.3881 0.0612  0.0358  0.0909  98  ALA A CB  
691  N  N   . LYS A 99  ? 0.2733 0.2566 0.3541 0.0611  0.0304  0.0713  99  LYS A N   
692  C  CA  . LYS A 99  ? 0.3075 0.2808 0.3975 0.0630  0.0347  0.0661  99  LYS A CA  
693  C  C   . LYS A 99  ? 0.2796 0.2526 0.3791 0.0759  0.0411  0.0800  99  LYS A C   
694  O  O   . LYS A 99  ? 0.3003 0.2931 0.3977 0.0840  0.0377  0.0889  99  LYS A O   
695  C  CB  . LYS A 99  ? 0.3163 0.3028 0.4021 0.0602  0.0285  0.0564  99  LYS A CB  
696  C  CG  . LYS A 99  ? 0.3701 0.3461 0.4640 0.0610  0.0332  0.0491  99  LYS A CG  
697  C  CD  . LYS A 99  ? 0.4638 0.4525 0.5533 0.0572  0.0278  0.0396  99  LYS A CD  
698  C  CE  . LYS A 99  ? 0.4879 0.4721 0.5686 0.0456  0.0238  0.0279  99  LYS A CE  
699  N  NZ  . LYS A 99  ? 0.3734 0.3651 0.4522 0.0424  0.0214  0.0188  99  LYS A NZ  
700  N  N   . TYR A 100 ? 0.2992 0.2503 0.4096 0.0779  0.0505  0.0818  100 TYR A N   
701  C  CA  . TYR A 100 ? 0.3293 0.2755 0.4498 0.0904  0.0585  0.0971  100 TYR A CA  
702  C  C   . TYR A 100 ? 0.3107 0.2564 0.4404 0.0986  0.0621  0.0962  100 TYR A C   
703  O  O   . TYR A 100 ? 0.3367 0.2766 0.4678 0.0931  0.0617  0.0821  100 TYR A O   
704  C  CB  . TYR A 100 ? 0.3824 0.3031 0.5118 0.0882  0.0684  0.1006  100 TYR A CB  
705  C  CG  . TYR A 100 ? 0.3316 0.2550 0.4544 0.0846  0.0673  0.1079  100 TYR A CG  
706  C  CD1 . TYR A 100 ? 0.3471 0.2710 0.4618 0.0721  0.0617  0.0963  100 TYR A CD1 
707  C  CD2 . TYR A 100 ? 0.3602 0.2871 0.4848 0.0946  0.0720  0.1269  100 TYR A CD2 
708  C  CE1 . TYR A 100 ? 0.3523 0.2797 0.4614 0.0692  0.0611  0.1027  100 TYR A CE1 
709  C  CE2 . TYR A 100 ? 0.3969 0.3276 0.5150 0.0915  0.0715  0.1337  100 TYR A CE2 
710  C  CZ  . TYR A 100 ? 0.4011 0.3321 0.5117 0.0787  0.0660  0.1209  100 TYR A CZ  
711  O  OH  . TYR A 100 ? 0.4188 0.3543 0.5234 0.0759  0.0658  0.1272  100 TYR A OH  
712  N  N   . GLY A 101 ? 0.3084 0.2607 0.4444 0.1125  0.0661  0.1121  101 GLY A N   
713  C  CA  . GLY A 101 ? 0.3186 0.2714 0.4648 0.1228  0.0705  0.1140  101 GLY A CA  
714  C  C   . GLY A 101 ? 0.3876 0.3107 0.5462 0.1221  0.0818  0.1083  101 GLY A C   
715  O  O   . GLY A 101 ? 0.3842 0.2864 0.5443 0.1132  0.0863  0.1029  101 GLY A O   
716  N  N   . THR A 102 ? 0.3336 0.2579 0.4990 0.1291  0.0853  0.1073  102 THR A N   
717  C  CA  . THR A 102 ? 0.3797 0.2798 0.5537 0.1261  0.0943  0.0972  102 THR A CA  
718  C  C   . THR A 102 ? 0.3912 0.2723 0.5707 0.1257  0.1034  0.1046  102 THR A C   
719  O  O   . THR A 102 ? 0.4483 0.3076 0.6344 0.1195  0.1104  0.0941  102 THR A O   
720  C  CB  . THR A 102 ? 0.3492 0.2571 0.5289 0.1346  0.0960  0.0951  102 THR A CB  
721  O  OG1 . THR A 102 ? 0.3704 0.2897 0.5524 0.1465  0.0977  0.1118  102 THR A OG1 
722  C  CG2 . THR A 102 ? 0.3895 0.3189 0.5654 0.1348  0.0877  0.0880  102 THR A CG2 
723  N  N   . ALA A 103 ? 0.3959 0.2860 0.5732 0.1321  0.1039  0.1219  103 ALA A N   
724  C  CA  . ALA A 103 ? 0.4279 0.3007 0.6113 0.1315  0.1135  0.1297  103 ALA A CA  
725  C  C   . ALA A 103 ? 0.4206 0.2754 0.6044 0.1179  0.1155  0.1202  103 ALA A C   
726  O  O   . ALA A 103 ? 0.4890 0.3261 0.6810 0.1148  0.1245  0.1215  103 ALA A O   
727  C  CB  . ALA A 103 ? 0.4359 0.3252 0.6147 0.1405  0.1129  0.1498  103 ALA A CB  
728  N  N   . TYR A 104 ? 0.4419 0.3018 0.6182 0.1097  0.1075  0.1106  104 TYR A N   
729  C  CA  . TYR A 104 ? 0.4558 0.3027 0.6317 0.0968  0.1082  0.1022  104 TYR A CA  
730  C  C   . TYR A 104 ? 0.5007 0.3359 0.6784 0.0862  0.1071  0.0808  104 TYR A C   
731  O  O   . TYR A 104 ? 0.5064 0.3364 0.6816 0.0750  0.1046  0.0715  104 TYR A O   
732  C  CB  . TYR A 104 ? 0.4251 0.2871 0.5903 0.0954  0.1005  0.1094  104 TYR A CB  
733  C  CG  . TYR A 104 ? 0.4311 0.3105 0.5921 0.1069  0.1000  0.1293  104 TYR A CG  
734  C  CD1 . TYR A 104 ? 0.5082 0.3816 0.6731 0.1089  0.1077  0.1415  104 TYR A CD1 
735  C  CD2 . TYR A 104 ? 0.4685 0.3722 0.6220 0.1156  0.0919  0.1353  104 TYR A CD2 
736  C  CE1 . TYR A 104 ? 0.5292 0.4202 0.6893 0.1197  0.1075  0.1593  104 TYR A CE1 
737  C  CE2 . TYR A 104 ? 0.4501 0.3727 0.5987 0.1256  0.0908  0.1520  104 TYR A CE2 
738  C  CZ  . TYR A 104 ? 0.5313 0.4475 0.6826 0.1278  0.0986  0.1640  104 TYR A CZ  
739  O  OH  . TYR A 104 ? 0.6353 0.5718 0.7810 0.1380  0.0977  0.1802  104 TYR A OH  
740  N  N   . GLY A 105 ? 0.4721 0.3047 0.6537 0.0896  0.1089  0.0726  105 GLY A N   
741  C  CA  . GLY A 105 ? 0.4820 0.3057 0.6642 0.0804  0.1083  0.0520  105 GLY A CA  
742  C  C   . GLY A 105 ? 0.5873 0.4248 0.7642 0.0841  0.1021  0.0453  105 GLY A C   
743  O  O   . GLY A 105 ? 0.5904 0.4460 0.7628 0.0920  0.0966  0.0554  105 GLY A O   
744  N  N   . GLU A 106 ? 0.6406 0.4711 0.8182 0.0781  0.1031  0.0275  106 GLU A N   
745  C  CA  . GLU A 106 ? 0.7251 0.5680 0.8989 0.0811  0.0990  0.0194  106 GLU A CA  
746  C  C   . GLU A 106 ? 0.7134 0.5755 0.8735 0.0748  0.0876  0.0178  106 GLU A C   
747  O  O   . GLU A 106 ? 0.6992 0.5585 0.8529 0.0635  0.0836  0.0103  106 GLU A O   
748  C  CB  . GLU A 106 ? 0.8145 0.6476 0.9890 0.0741  0.1020  -0.0003 106 GLU A CB  
749  C  CG  . GLU A 106 ? 0.9091 0.7332 1.0921 0.0808  0.1101  -0.0004 106 GLU A CG  
750  C  CD  . GLU A 106 ? 1.0431 0.8551 1.2269 0.0721  0.1136  -0.0198 106 GLU A CD  
751  O  OE1 . GLU A 106 ? 1.0666 0.8722 1.2479 0.0603  0.1119  -0.0294 106 GLU A OE1 
752  O  OE2 . GLU A 106 ? 1.0812 0.8919 1.2681 0.0773  0.1178  -0.0254 106 GLU A OE2 
753  N  N   . SER A 107 ? 0.6685 0.5527 0.8229 0.0809  0.0814  0.0245  107 SER A N   
754  C  CA  . SER A 107 ? 0.6651 0.5704 0.8054 0.0745  0.0701  0.0229  107 SER A CA  
755  C  C   . SER A 107 ? 0.6785 0.5941 0.8140 0.0719  0.0671  0.0108  107 SER A C   
756  O  O   . SER A 107 ? 0.6275 0.5476 0.7695 0.0803  0.0708  0.0119  107 SER A O   
757  C  CB  . SER A 107 ? 0.5951 0.5197 0.7333 0.0826  0.0655  0.0391  107 SER A CB  
758  O  OG  . SER A 107 ? 0.5307 0.4749 0.6564 0.0763  0.0551  0.0367  107 SER A OG  
759  N  N   . LYS A 108 ? 0.6675 0.5874 0.7919 0.0609  0.0608  0.0002  108 LYS A N   
760  C  CA  . LYS A 108 ? 0.6424 0.5705 0.7614 0.0574  0.0588  -0.0114 108 LYS A CA  
761  C  C   . LYS A 108 ? 0.5991 0.5476 0.7070 0.0530  0.0495  -0.0098 108 LYS A C   
762  O  O   . LYS A 108 ? 0.5473 0.5005 0.6495 0.0496  0.0440  -0.0040 108 LYS A O   
763  C  CB  . LYS A 108 ? 0.7280 0.6428 0.8440 0.0486  0.0608  -0.0268 108 LYS A CB  
764  C  CG  . LYS A 108 ? 0.7606 0.6584 0.8802 0.0437  0.0632  -0.0275 108 LYS A CG  
765  C  CD  . LYS A 108 ? 0.7600 0.6651 0.8704 0.0372  0.0554  -0.0227 108 LYS A CD  
766  C  CE  . LYS A 108 ? 0.7820 0.6720 0.8981 0.0332  0.0586  -0.0212 108 LYS A CE  
767  N  NZ  . LYS A 108 ? 0.7786 0.6757 0.8852 0.0257  0.0513  -0.0201 108 LYS A NZ  
768  N  N   . ASP A 109 ? 0.6028 0.5629 0.7083 0.0531  0.0486  -0.0151 109 ASP A N   
769  C  CA  . ASP A 109 ? 0.5014 0.4786 0.5976 0.0477  0.0412  -0.0155 109 ASP A CA  
770  C  C   . ASP A 109 ? 0.5429 0.5152 0.6284 0.0377  0.0386  -0.0259 109 ASP A C   
771  O  O   . ASP A 109 ? 0.5741 0.5370 0.6593 0.0359  0.0427  -0.0357 109 ASP A O   
772  C  CB  . ASP A 109 ? 0.4900 0.4823 0.5897 0.0521  0.0425  -0.0161 109 ASP A CB  
773  C  CG  . ASP A 109 ? 0.5307 0.5308 0.6419 0.0634  0.0452  -0.0059 109 ASP A CG  
774  O  OD1 . ASP A 109 ? 0.6547 0.6445 0.7750 0.0708  0.0527  -0.0063 109 ASP A OD1 
775  O  OD2 . ASP A 109 ? 0.3681 0.3851 0.4795 0.0651  0.0400  0.0022  109 ASP A OD2 
776  N  N   . GLN A 110 ? 0.4440 0.4232 0.5207 0.0315  0.0319  -0.0240 110 GLN A N   
777  C  CA  . GLN A 110 ? 0.4175 0.3959 0.4838 0.0232  0.0289  -0.0319 110 GLN A CA  
778  C  C   . GLN A 110 ? 0.3538 0.3427 0.4170 0.0226  0.0298  -0.0364 110 GLN A C   
779  O  O   . GLN A 110 ? 0.3905 0.3907 0.4589 0.0268  0.0306  -0.0322 110 GLN A O   
780  C  CB  . GLN A 110 ? 0.4110 0.3947 0.4700 0.0181  0.0223  -0.0275 110 GLN A CB  
781  C  CG  . GLN A 110 ? 0.4869 0.4623 0.5466 0.0174  0.0209  -0.0231 110 GLN A CG  
782  C  CD  . GLN A 110 ? 0.4159 0.3971 0.4675 0.0125  0.0147  -0.0203 110 GLN A CD  
783  O  OE1 . GLN A 110 ? 0.3401 0.3323 0.3880 0.0108  0.0115  -0.0193 110 GLN A OE1 
784  N  NE2 . GLN A 110 ? 0.4890 0.4626 0.5388 0.0098  0.0136  -0.0195 110 GLN A NE2 
785  N  N   . ARG A 111 ? 0.3150 0.3019 0.3697 0.0173  0.0296  -0.0443 111 ARG A N   
786  C  CA  . ARG A 111 ? 0.2927 0.2907 0.3424 0.0157  0.0300  -0.0466 111 ARG A CA  
787  C  C   . ARG A 111 ? 0.2597 0.2667 0.3049 0.0114  0.0248  -0.0407 111 ARG A C   
788  O  O   . ARG A 111 ? 0.2413 0.2447 0.2829 0.0081  0.0204  -0.0378 111 ARG A O   
789  C  CB  . ARG A 111 ? 0.3072 0.3018 0.3477 0.0120  0.0312  -0.0559 111 ARG A CB  
790  C  CG  . ARG A 111 ? 0.4417 0.4299 0.4861 0.0155  0.0372  -0.0647 111 ARG A CG  
791  C  CD  . ARG A 111 ? 0.4590 0.4501 0.4928 0.0123  0.0382  -0.0741 111 ARG A CD  
792  N  NE  . ARG A 111 ? 0.5174 0.5053 0.5430 0.0065  0.0332  -0.0762 111 ARG A NE  
793  C  CZ  . ARG A 111 ? 0.4841 0.4774 0.4984 0.0034  0.0319  -0.0816 111 ARG A CZ  
794  N  NH1 . ARG A 111 ? 0.4977 0.4996 0.5066 0.0050  0.0355  -0.0856 111 ARG A NH1 
795  N  NH2 . ARG A 111 ? 0.5053 0.4969 0.5137 -0.0010 0.0270  -0.0825 111 ARG A NH2 
796  N  N   . LEU A 112 ? 0.2359 0.2549 0.2823 0.0113  0.0260  -0.0393 112 LEU A N   
797  C  CA  . LEU A 112 ? 0.2144 0.2407 0.2567 0.0058  0.0223  -0.0357 112 LEU A CA  
798  C  C   . LEU A 112 ? 0.2341 0.2535 0.2648 0.0005  0.0205  -0.0384 112 LEU A C   
799  O  O   . LEU A 112 ? 0.2359 0.2520 0.2611 0.0007  0.0230  -0.0437 112 LEU A O   
800  C  CB  . LEU A 112 ? 0.2232 0.2627 0.2694 0.0055  0.0252  -0.0350 112 LEU A CB  
801  C  CG  . LEU A 112 ? 0.2149 0.2665 0.2733 0.0099  0.0255  -0.0310 112 LEU A CG  
802  C  CD1 . LEU A 112 ? 0.2296 0.2949 0.2929 0.0094  0.0295  -0.0314 112 LEU A CD1 
803  C  CD2 . LEU A 112 ? 0.2347 0.2911 0.2952 0.0076  0.0197  -0.0262 112 LEU A CD2 
804  N  N   . HIS A 113 ? 0.2138 0.2325 0.2410 -0.0037 0.0163  -0.0349 113 HIS A N   
805  C  CA  . HIS A 113 ? 0.2057 0.2182 0.2228 -0.0075 0.0144  -0.0361 113 HIS A CA  
806  C  C   . HIS A 113 ? 0.2194 0.2335 0.2348 -0.0118 0.0114  -0.0319 113 HIS A C   
807  O  O   . HIS A 113 ? 0.2177 0.2375 0.2394 -0.0123 0.0100  -0.0293 113 HIS A O   
808  C  CB  . HIS A 113 ? 0.2260 0.2291 0.2414 -0.0066 0.0122  -0.0385 113 HIS A CB  
809  C  CG  . HIS A 113 ? 0.2253 0.2259 0.2456 -0.0059 0.0092  -0.0344 113 HIS A CG  
810  N  ND1 . HIS A 113 ? 0.2453 0.2462 0.2742 -0.0014 0.0105  -0.0326 113 HIS A ND1 
811  C  CD2 . HIS A 113 ? 0.2403 0.2390 0.2578 -0.0084 0.0053  -0.0314 113 HIS A CD2 
812  C  CE1 . HIS A 113 ? 0.2455 0.2455 0.2760 -0.0012 0.0074  -0.0281 113 HIS A CE1 
813  N  NE2 . HIS A 113 ? 0.2447 0.2435 0.2682 -0.0057 0.0042  -0.0279 113 HIS A NE2 
814  N  N   . ASN A 114 ? 0.2245 0.2341 0.2314 -0.0147 0.0106  -0.0317 114 ASN A N   
815  C  CA  . ASN A 114 ? 0.2094 0.2166 0.2143 -0.0183 0.0080  -0.0286 114 ASN A CA  
816  C  C   . ASN A 114 ? 0.2231 0.2228 0.2237 -0.0178 0.0044  -0.0289 114 ASN A C   
817  O  O   . ASN A 114 ? 0.2369 0.2335 0.2349 -0.0159 0.0042  -0.0317 114 ASN A O   
818  C  CB  . ASN A 114 ? 0.2383 0.2454 0.2382 -0.0215 0.0108  -0.0264 114 ASN A CB  
819  C  CG  . ASN A 114 ? 0.2375 0.2404 0.2273 -0.0201 0.0113  -0.0264 114 ASN A CG  
820  O  OD1 . ASN A 114 ? 0.2326 0.2302 0.2181 -0.0200 0.0084  -0.0259 114 ASN A OD1 
821  N  ND2 . ASN A 114 ? 0.2285 0.2360 0.2149 -0.0187 0.0152  -0.0272 114 ASN A ND2 
822  N  N   . ASP A 115 ? 0.2128 0.2105 0.2135 -0.0199 0.0018  -0.0268 115 ASP A N   
823  C  CA  . ASP A 115 ? 0.2150 0.2067 0.2118 -0.0196 -0.0011 -0.0265 115 ASP A CA  
824  C  C   . ASP A 115 ? 0.2354 0.2233 0.2269 -0.0220 -0.0011 -0.0246 115 ASP A C   
825  O  O   . ASP A 115 ? 0.2330 0.2181 0.2242 -0.0230 -0.0031 -0.0238 115 ASP A O   
826  C  CB  . ASP A 115 ? 0.2456 0.2382 0.2472 -0.0186 -0.0037 -0.0255 115 ASP A CB  
827  C  CG  . ASP A 115 ? 0.2795 0.2723 0.2860 -0.0152 -0.0031 -0.0262 115 ASP A CG  
828  O  OD1 . ASP A 115 ? 0.3157 0.3036 0.3208 -0.0143 -0.0028 -0.0282 115 ASP A OD1 
829  O  OD2 . ASP A 115 ? 0.2646 0.2628 0.2771 -0.0132 -0.0026 -0.0247 115 ASP A OD2 
830  N  N   . ALA A 116 ? 0.2261 0.2140 0.2136 -0.0225 0.0018  -0.0235 116 ALA A N   
831  C  CA  . ALA A 116 ? 0.2381 0.2212 0.2214 -0.0241 0.0033  -0.0203 116 ALA A CA  
832  C  C   . ALA A 116 ? 0.2342 0.2138 0.2106 -0.0214 0.0017  -0.0189 116 ALA A C   
833  O  O   . ALA A 116 ? 0.2434 0.2179 0.2167 -0.0214 0.0028  -0.0156 116 ALA A O   
834  C  CB  . ALA A 116 ? 0.2483 0.2334 0.2305 -0.0253 0.0081  -0.0179 116 ALA A CB  
835  N  N   . TRP A 117 ? 0.2359 0.2184 0.2109 -0.0191 -0.0006 -0.0218 117 TRP A N   
836  C  CA  . TRP A 117 ? 0.2250 0.2083 0.1939 -0.0166 -0.0023 -0.0215 117 TRP A CA  
837  C  C   . TRP A 117 ? 0.2442 0.2253 0.2151 -0.0163 -0.0058 -0.0223 117 TRP A C   
838  O  O   . TRP A 117 ? 0.2669 0.2472 0.2434 -0.0173 -0.0071 -0.0244 117 TRP A O   
839  C  CB  . TRP A 117 ? 0.2339 0.2234 0.2012 -0.0154 -0.0025 -0.0261 117 TRP A CB  
840  C  CG  . TRP A 117 ? 0.2412 0.2350 0.2042 -0.0146 0.0011  -0.0252 117 TRP A CG  
841  C  CD1 . TRP A 117 ? 0.2592 0.2543 0.2258 -0.0158 0.0044  -0.0259 117 TRP A CD1 
842  C  CD2 . TRP A 117 ? 0.2367 0.2355 0.1907 -0.0121 0.0022  -0.0228 117 TRP A CD2 
843  N  NE1 . TRP A 117 ? 0.2577 0.2578 0.2182 -0.0145 0.0079  -0.0242 117 TRP A NE1 
844  C  CE2 . TRP A 117 ? 0.2700 0.2725 0.2220 -0.0120 0.0066  -0.0220 117 TRP A CE2 
845  C  CE3 . TRP A 117 ? 0.2658 0.2680 0.2131 -0.0093 -0.0001 -0.0205 117 TRP A CE3 
846  C  CZ2 . TRP A 117 ? 0.2832 0.2922 0.2260 -0.0092 0.0091  -0.0187 117 TRP A CZ2 
847  C  CZ3 . TRP A 117 ? 0.2661 0.2756 0.2043 -0.0060 0.0018  -0.0171 117 TRP A CZ3 
848  C  CH2 . TRP A 117 ? 0.3049 0.3174 0.2404 -0.0060 0.0065  -0.0160 117 TRP A CH2 
849  N  N   . ALA A 118 ? 0.2284 0.2098 0.1948 -0.0141 -0.0069 -0.0199 118 ALA A N   
850  C  CA  . ALA A 118 ? 0.2233 0.2058 0.1917 -0.0134 -0.0101 -0.0214 118 ALA A CA  
851  C  C   . ALA A 118 ? 0.2577 0.2462 0.2279 -0.0139 -0.0120 -0.0270 118 ALA A C   
852  O  O   . ALA A 118 ? 0.2455 0.2384 0.2129 -0.0136 -0.0111 -0.0296 118 ALA A O   
853  C  CB  . ALA A 118 ? 0.2504 0.2336 0.2140 -0.0101 -0.0107 -0.0173 118 ALA A CB  
854  N  N   . ALA A 119 ? 0.2556 0.2445 0.2309 -0.0148 -0.0140 -0.0291 119 ALA A N   
855  C  CA  . ALA A 119 ? 0.2672 0.2596 0.2468 -0.0165 -0.0149 -0.0353 119 ALA A CA  
856  C  C   . ALA A 119 ? 0.2425 0.2441 0.2174 -0.0158 -0.0166 -0.0391 119 ALA A C   
857  O  O   . ALA A 119 ? 0.2614 0.2660 0.2378 -0.0173 -0.0162 -0.0457 119 ALA A O   
858  C  CB  . ALA A 119 ? 0.2737 0.2650 0.2602 -0.0179 -0.0161 -0.0357 119 ALA A CB  
859  N  N   . SER A 120 ? 0.2498 0.2568 0.2193 -0.0129 -0.0183 -0.0354 120 SER A N   
860  C  CA  . SER A 120 ? 0.2601 0.2794 0.2243 -0.0113 -0.0206 -0.0382 120 SER A CA  
861  C  C   . SER A 120 ? 0.2475 0.2698 0.2027 -0.0088 -0.0186 -0.0363 120 SER A C   
862  O  O   . SER A 120 ? 0.2578 0.2922 0.2071 -0.0068 -0.0204 -0.0386 120 SER A O   
863  C  CB  . SER A 120 ? 0.2760 0.3012 0.2381 -0.0077 -0.0229 -0.0331 120 SER A CB  
864  O  OG  . SER A 120 ? 0.2894 0.3074 0.2465 -0.0042 -0.0203 -0.0245 120 SER A OG  
865  N  N   . SER A 121 ? 0.2456 0.2589 0.1999 -0.0088 -0.0149 -0.0318 121 SER A N   
866  C  CA  . SER A 121 ? 0.2503 0.2660 0.1967 -0.0065 -0.0119 -0.0283 121 SER A CA  
867  C  C   . SER A 121 ? 0.2476 0.2700 0.1857 -0.0015 -0.0123 -0.0213 121 SER A C   
868  O  O   . SER A 121 ? 0.2630 0.2933 0.1931 0.0012  -0.0109 -0.0197 121 SER A O   
869  C  CB  . SER A 121 ? 0.2765 0.2991 0.2208 -0.0075 -0.0112 -0.0359 121 SER A CB  
870  O  OG  . SER A 121 ? 0.3065 0.3221 0.2593 -0.0110 -0.0099 -0.0412 121 SER A OG  
871  N  N   . LEU A 122 ? 0.2273 0.2475 0.1668 0.0007  -0.0139 -0.0165 122 LEU A N   
872  C  CA  . LEU A 122 ? 0.2225 0.2516 0.1550 0.0067  -0.0149 -0.0102 122 LEU A CA  
873  C  C   . LEU A 122 ? 0.2297 0.2559 0.1546 0.0104  -0.0098 -0.0011 122 LEU A C   
874  O  O   . LEU A 122 ? 0.2506 0.2884 0.1669 0.0154  -0.0099 0.0029  122 LEU A O   
875  C  CB  . LEU A 122 ? 0.2379 0.2638 0.1746 0.0090  -0.0165 -0.0062 122 LEU A CB  
876  C  CG  . LEU A 122 ? 0.2593 0.2970 0.1904 0.0164  -0.0182 0.0003  122 LEU A CG  
877  C  CD1 . LEU A 122 ? 0.3155 0.3722 0.2465 0.0161  -0.0241 -0.0074 122 LEU A CD1 
878  C  CD2 . LEU A 122 ? 0.2624 0.2932 0.1978 0.0198  -0.0176 0.0061  122 LEU A CD2 
879  N  N   . VAL A 123 ? 0.2368 0.2485 0.1653 0.0080  -0.0052 0.0027  123 VAL A N   
880  C  CA  . VAL A 123 ? 0.2474 0.2546 0.1710 0.0096  0.0009  0.0106  123 VAL A CA  
881  C  C   . VAL A 123 ? 0.2555 0.2546 0.1846 0.0035  0.0042  0.0070  123 VAL A C   
882  O  O   . VAL A 123 ? 0.2586 0.2527 0.1954 -0.0010 0.0022  0.0007  123 VAL A O   
883  C  CB  . VAL A 123 ? 0.2575 0.2547 0.1806 0.0136  0.0050  0.0213  123 VAL A CB  
884  C  CG1 . VAL A 123 ? 0.2795 0.2869 0.1971 0.0214  0.0021  0.0266  123 VAL A CG1 
885  C  CG2 . VAL A 123 ? 0.2612 0.2438 0.1935 0.0095  0.0056  0.0190  123 VAL A CG2 
886  N  N   . HIS A 124 ? 0.2576 0.2568 0.1828 0.0038  0.0096  0.0119  124 HIS A N   
887  C  CA  . HIS A 124 ? 0.2496 0.2443 0.1803 -0.0015 0.0131  0.0089  124 HIS A CA  
888  C  C   . HIS A 124 ? 0.2574 0.2386 0.1970 -0.0058 0.0149  0.0098  124 HIS A C   
889  O  O   . HIS A 124 ? 0.2784 0.2511 0.2180 -0.0042 0.0173  0.0161  124 HIS A O   
890  C  CB  . HIS A 124 ? 0.2572 0.2555 0.1819 0.0002  0.0195  0.0157  124 HIS A CB  
891  C  CG  . HIS A 124 ? 0.2676 0.2665 0.1972 -0.0044 0.0231  0.0122  124 HIS A CG  
892  N  ND1 . HIS A 124 ? 0.2836 0.2731 0.2227 -0.0097 0.0265  0.0128  124 HIS A ND1 
893  C  CD2 . HIS A 124 ? 0.2702 0.2792 0.1968 -0.0041 0.0241  0.0078  124 HIS A CD2 
894  C  CE1 . HIS A 124 ? 0.2935 0.2882 0.2359 -0.0124 0.0293  0.0097  124 HIS A CE1 
895  N  NE2 . HIS A 124 ? 0.3023 0.3080 0.2371 -0.0088 0.0282  0.0068  124 HIS A NE2 
896  N  N   . PRO A 125 ? 0.2433 0.2227 0.1907 -0.0109 0.0143  0.0036  125 PRO A N   
897  C  CA  . PRO A 125 ? 0.2490 0.2186 0.2045 -0.0154 0.0155  0.0031  125 PRO A CA  
898  C  C   . PRO A 125 ? 0.2501 0.2127 0.2077 -0.0178 0.0225  0.0091  125 PRO A C   
899  O  O   . PRO A 125 ? 0.2912 0.2575 0.2455 -0.0170 0.0272  0.0136  125 PRO A O   
900  C  CB  . PRO A 125 ? 0.2387 0.2123 0.2011 -0.0192 0.0130  -0.0042 125 PRO A CB  
901  C  CG  . PRO A 125 ? 0.2834 0.2658 0.2421 -0.0164 0.0100  -0.0082 125 PRO A CG  
902  C  CD  . PRO A 125 ? 0.2704 0.2576 0.2197 -0.0123 0.0120  -0.0037 125 PRO A CD  
903  N  N   . ARG A 126 ? 0.2740 0.2267 0.2378 -0.0213 0.0238  0.0086  126 ARG A N   
904  C  CA  . ARG A 126 ? 0.2696 0.2151 0.2399 -0.0266 0.0302  0.0106  126 ARG A CA  
905  C  C   . ARG A 126 ? 0.2977 0.2448 0.2775 -0.0330 0.0276  0.0023  126 ARG A C   
906  O  O   . ARG A 126 ? 0.3389 0.2866 0.3196 -0.0327 0.0222  -0.0029 126 ARG A O   
907  C  CB  . ARG A 126 ? 0.3118 0.2435 0.2818 -0.0253 0.0348  0.0165  126 ARG A CB  
908  C  CG  . ARG A 126 ? 0.3193 0.2498 0.2816 -0.0193 0.0399  0.0274  126 ARG A CG  
909  C  CD  . ARG A 126 ? 0.3380 0.2544 0.2999 -0.0160 0.0443  0.0342  126 ARG A CD  
910  N  NE  . ARG A 126 ? 0.3491 0.2514 0.3210 -0.0228 0.0508  0.0331  126 ARG A NE  
911  C  CZ  . ARG A 126 ? 0.3822 0.2689 0.3562 -0.0210 0.0571  0.0389  126 ARG A CZ  
912  N  NH1 . ARG A 126 ? 0.3832 0.2672 0.3497 -0.0116 0.0578  0.0478  126 ARG A NH1 
913  N  NH2 . ARG A 126 ? 0.4186 0.2925 0.4030 -0.0288 0.0629  0.0353  126 ARG A NH2 
914  N  N   . ALA A 127 ? 0.2942 0.2440 0.2812 -0.0387 0.0316  0.0012  127 ALA A N   
915  C  CA  . ALA A 127 ? 0.2996 0.2547 0.2958 -0.0445 0.0288  -0.0066 127 ALA A CA  
916  C  C   . ALA A 127 ? 0.3116 0.2582 0.3157 -0.0511 0.0322  -0.0093 127 ALA A C   
917  O  O   . ALA A 127 ? 0.3780 0.3311 0.3910 -0.0572 0.0312  -0.0157 127 ALA A O   
918  C  CB  . ALA A 127 ? 0.3511 0.3185 0.3520 -0.0464 0.0300  -0.0078 127 ALA A CB  
919  N  N   . ASP A 128 ? 0.3093 0.2417 0.3108 -0.0500 0.0365  -0.0049 128 ASP A N   
920  C  CA  . ASP A 128 ? 0.3212 0.2427 0.3308 -0.0566 0.0413  -0.0079 128 ASP A CA  
921  C  C   . ASP A 128 ? 0.3353 0.2467 0.3421 -0.0541 0.0391  -0.0108 128 ASP A C   
922  O  O   . ASP A 128 ? 0.3287 0.2385 0.3268 -0.0464 0.0362  -0.0067 128 ASP A O   
923  C  CB  . ASP A 128 ? 0.3485 0.2590 0.3602 -0.0581 0.0514  0.0006  128 ASP A CB  
924  C  CG  . ASP A 128 ? 0.4332 0.3343 0.4345 -0.0490 0.0539  0.0110  128 ASP A CG  
925  O  OD1 . ASP A 128 ? 0.3712 0.2815 0.3633 -0.0422 0.0504  0.0154  128 ASP A OD1 
926  O  OD2 . ASP A 128 ? 0.5019 0.3872 0.5048 -0.0485 0.0594  0.0144  128 ASP A OD2 
927  N  N   . GLY A 129 ? 0.3263 0.2323 0.3410 -0.0609 0.0406  -0.0186 129 GLY A N   
928  C  CA  . GLY A 129 ? 0.3340 0.2282 0.3472 -0.0592 0.0407  -0.0218 129 GLY A CA  
929  C  C   . GLY A 129 ? 0.2951 0.1956 0.2999 -0.0521 0.0330  -0.0228 129 GLY A C   
930  O  O   . GLY A 129 ? 0.2987 0.2135 0.3027 -0.0522 0.0262  -0.0271 129 GLY A O   
931  N  N   . VAL A 130 ? 0.3131 0.2031 0.3126 -0.0456 0.0345  -0.0183 130 VAL A N   
932  C  CA  . VAL A 130 ? 0.3099 0.2051 0.3032 -0.0396 0.0282  -0.0199 130 VAL A CA  
933  C  C   . VAL A 130 ? 0.3098 0.2175 0.2969 -0.0344 0.0227  -0.0152 130 VAL A C   
934  O  O   . VAL A 130 ? 0.2973 0.2105 0.2806 -0.0304 0.0176  -0.0167 130 VAL A O   
935  C  CB  . VAL A 130 ? 0.3408 0.2224 0.3315 -0.0338 0.0318  -0.0164 130 VAL A CB  
936  C  CG1 . VAL A 130 ? 0.3783 0.2454 0.3760 -0.0392 0.0381  -0.0225 130 VAL A CG1 
937  C  CG2 . VAL A 130 ? 0.3614 0.2386 0.3473 -0.0268 0.0355  -0.0042 130 VAL A CG2 
938  N  N   . TYR A 131 ? 0.2854 0.1978 0.2717 -0.0345 0.0241  -0.0102 131 TYR A N   
939  C  CA  . TYR A 131 ? 0.2715 0.1950 0.2521 -0.0300 0.0197  -0.0072 131 TYR A CA  
940  C  C   . TYR A 131 ? 0.2420 0.1777 0.2260 -0.0335 0.0153  -0.0127 131 TYR A C   
941  O  O   . TYR A 131 ? 0.2620 0.2060 0.2427 -0.0304 0.0118  -0.0119 131 TYR A O   
942  C  CB  . TYR A 131 ? 0.2834 0.2058 0.2600 -0.0270 0.0241  0.0014  131 TYR A CB  
943  C  CG  . TYR A 131 ? 0.2840 0.1944 0.2579 -0.0224 0.0291  0.0085  131 TYR A CG  
944  C  CD1 . TYR A 131 ? 0.2895 0.2007 0.2578 -0.0151 0.0261  0.0114  131 TYR A CD1 
945  C  CD2 . TYR A 131 ? 0.3220 0.2201 0.3002 -0.0254 0.0371  0.0122  131 TYR A CD2 
946  C  CE1 . TYR A 131 ? 0.3386 0.2395 0.3051 -0.0097 0.0307  0.0185  131 TYR A CE1 
947  C  CE2 . TYR A 131 ? 0.3419 0.2273 0.3185 -0.0203 0.0425  0.0196  131 TYR A CE2 
948  C  CZ  . TYR A 131 ? 0.3427 0.2299 0.3132 -0.0119 0.0391  0.0229  131 TYR A CZ  
949  O  OH  . TYR A 131 ? 0.4021 0.2776 0.3714 -0.0055 0.0445  0.0310  131 TYR A OH  
950  N  N   . GLN A 132 ? 0.2672 0.2045 0.2581 -0.0397 0.0155  -0.0187 132 GLN A N   
951  C  CA  . GLN A 132 ? 0.2718 0.2220 0.2663 -0.0418 0.0112  -0.0231 132 GLN A CA  
952  C  C   . GLN A 132 ? 0.2762 0.2316 0.2678 -0.0382 0.0053  -0.0255 132 GLN A C   
953  O  O   . GLN A 132 ? 0.2857 0.2358 0.2748 -0.0366 0.0044  -0.0268 132 GLN A O   
954  C  CB  . GLN A 132 ? 0.2684 0.2216 0.2713 -0.0492 0.0126  -0.0291 132 GLN A CB  
955  C  CG  . GLN A 132 ? 0.3036 0.2533 0.3116 -0.0539 0.0190  -0.0268 132 GLN A CG  
956  C  CD  . GLN A 132 ? 0.2997 0.2523 0.3177 -0.0625 0.0206  -0.0340 132 GLN A CD  
957  O  OE1 . GLN A 132 ? 0.3098 0.2752 0.3345 -0.0662 0.0195  -0.0369 132 GLN A OE1 
958  N  NE2 . GLN A 132 ? 0.3196 0.2607 0.3394 -0.0657 0.0234  -0.0377 132 GLN A NE2 
959  N  N   . ARG A 133 ? 0.2405 0.2061 0.2332 -0.0368 0.0020  -0.0260 133 ARG A N   
960  C  CA  . ARG A 133 ? 0.2131 0.1842 0.2046 -0.0338 -0.0027 -0.0273 133 ARG A CA  
961  C  C   . ARG A 133 ? 0.2400 0.2219 0.2370 -0.0362 -0.0050 -0.0309 133 ARG A C   
962  O  O   . ARG A 133 ? 0.2499 0.2380 0.2519 -0.0386 -0.0039 -0.0315 133 ARG A O   
963  C  CB  . ARG A 133 ? 0.2257 0.1990 0.2147 -0.0295 -0.0040 -0.0244 133 ARG A CB  
964  C  CG  . ARG A 133 ? 0.2561 0.2228 0.2394 -0.0265 -0.0028 -0.0212 133 ARG A CG  
965  C  CD  . ARG A 133 ? 0.2478 0.2179 0.2290 -0.0239 -0.0030 -0.0198 133 ARG A CD  
966  N  NE  . ARG A 133 ? 0.2834 0.2579 0.2666 -0.0222 -0.0059 -0.0216 133 ARG A NE  
967  C  CZ  . ARG A 133 ? 0.2692 0.2429 0.2509 -0.0201 -0.0080 -0.0216 133 ARG A CZ  
968  N  NH1 . ARG A 133 ? 0.2796 0.2502 0.2573 -0.0186 -0.0082 -0.0200 133 ARG A NH1 
969  N  NH2 . ARG A 133 ? 0.3075 0.2840 0.2928 -0.0193 -0.0095 -0.0229 133 ARG A NH2 
970  N  N   . VAL A 134 ? 0.2251 0.2111 0.2213 -0.0353 -0.0082 -0.0331 134 VAL A N   
971  C  CA  . VAL A 134 ? 0.2103 0.2095 0.2109 -0.0364 -0.0110 -0.0359 134 VAL A CA  
972  C  C   . VAL A 134 ? 0.2106 0.2156 0.2098 -0.0309 -0.0139 -0.0324 134 VAL A C   
973  O  O   . VAL A 134 ? 0.2254 0.2262 0.2202 -0.0283 -0.0147 -0.0311 134 VAL A O   
974  C  CB  . VAL A 134 ? 0.2316 0.2336 0.2328 -0.0406 -0.0118 -0.0423 134 VAL A CB  
975  C  CG1 . VAL A 134 ? 0.2648 0.2844 0.2695 -0.0407 -0.0157 -0.0447 134 VAL A CG1 
976  C  CG2 . VAL A 134 ? 0.2752 0.2702 0.2801 -0.0469 -0.0078 -0.0459 134 VAL A CG2 
977  N  N   . TYR A 135 ? 0.2074 0.2220 0.2113 -0.0291 -0.0148 -0.0305 135 TYR A N   
978  C  CA  . TYR A 135 ? 0.2141 0.2334 0.2184 -0.0235 -0.0164 -0.0261 135 TYR A CA  
979  C  C   . TYR A 135 ? 0.2123 0.2469 0.2189 -0.0222 -0.0194 -0.0264 135 TYR A C   
980  O  O   . TYR A 135 ? 0.2096 0.2541 0.2203 -0.0256 -0.0204 -0.0301 135 TYR A O   
981  C  CB  . TYR A 135 ? 0.1992 0.2179 0.2077 -0.0209 -0.0145 -0.0233 135 TYR A CB  
982  C  CG  . TYR A 135 ? 0.2164 0.2230 0.2216 -0.0204 -0.0123 -0.0226 135 TYR A CG  
983  C  CD1 . TYR A 135 ? 0.2102 0.2100 0.2124 -0.0238 -0.0105 -0.0246 135 TYR A CD1 
984  C  CD2 . TYR A 135 ? 0.2196 0.2220 0.2250 -0.0167 -0.0119 -0.0200 135 TYR A CD2 
985  C  CE1 . TYR A 135 ? 0.2435 0.2352 0.2418 -0.0228 -0.0092 -0.0239 135 TYR A CE1 
986  C  CE2 . TYR A 135 ? 0.2435 0.2374 0.2463 -0.0169 -0.0105 -0.0208 135 TYR A CE2 
987  C  CZ  . TYR A 135 ? 0.2337 0.2236 0.2324 -0.0196 -0.0096 -0.0227 135 TYR A CZ  
988  O  OH  . TYR A 135 ? 0.2625 0.2470 0.2580 -0.0191 -0.0089 -0.0233 135 TYR A OH  
989  N  N   . GLY A 136 ? 0.2004 0.2381 0.2046 -0.0175 -0.0207 -0.0223 136 GLY A N   
990  C  CA  . GLY A 136 ? 0.1931 0.2474 0.1987 -0.0143 -0.0236 -0.0204 136 GLY A CA  
991  C  C   . GLY A 136 ? 0.2017 0.2573 0.2098 -0.0071 -0.0225 -0.0120 136 GLY A C   
992  O  O   . GLY A 136 ? 0.2095 0.2533 0.2162 -0.0051 -0.0202 -0.0084 136 GLY A O   
993  N  N   . ILE A 137 ? 0.1917 0.2624 0.2044 -0.0031 -0.0241 -0.0087 137 ILE A N   
994  C  CA  . ILE A 137 ? 0.1948 0.2687 0.2101 0.0051  -0.0228 0.0006  137 ILE A CA  
995  C  C   . ILE A 137 ? 0.1971 0.2919 0.2106 0.0090  -0.0265 0.0034  137 ILE A C   
996  O  O   . ILE A 137 ? 0.2092 0.3206 0.2262 0.0082  -0.0296 0.0003  137 ILE A O   
997  C  CB  . ILE A 137 ? 0.1996 0.2722 0.2234 0.0086  -0.0201 0.0036  137 ILE A CB  
998  C  CG1 . ILE A 137 ? 0.2099 0.2652 0.2343 0.0040  -0.0170 -0.0010 137 ILE A CG1 
999  C  CG2 . ILE A 137 ? 0.2252 0.2966 0.2523 0.0172  -0.0174 0.0137  137 ILE A CG2 
1000 C  CD1 . ILE A 137 ? 0.2402 0.2940 0.2723 0.0071  -0.0139 0.0003  137 ILE A CD1 
1001 N  N   . LEU A 138 ? 0.2047 0.3003 0.2127 0.0131  -0.0262 0.0090  138 LEU A N   
1002 C  CA  . LEU A 138 ? 0.1955 0.3123 0.2000 0.0181  -0.0294 0.0130  138 LEU A CA  
1003 C  C   . LEU A 138 ? 0.2148 0.3350 0.2242 0.0282  -0.0267 0.0259  138 LEU A C   
1004 O  O   . LEU A 138 ? 0.2423 0.3489 0.2517 0.0317  -0.0222 0.0335  138 LEU A O   
1005 C  CB  . LEU A 138 ? 0.2302 0.3460 0.2251 0.0171  -0.0298 0.0119  138 LEU A CB  
1006 C  CG  . LEU A 138 ? 0.2831 0.4226 0.2711 0.0194  -0.0342 0.0109  138 LEU A CG  
1007 C  CD1 . LEU A 138 ? 0.2810 0.4157 0.2597 0.0195  -0.0326 0.0113  138 LEU A CD1 
1008 C  CD2 . LEU A 138 ? 0.3560 0.5155 0.3459 0.0289  -0.0356 0.0212  138 LEU A CD2 
1009 N  N   . TYR A 139 ? 0.2093 0.3475 0.2240 0.0328  -0.0291 0.0286  139 TYR A N   
1010 C  CA  . TYR A 139 ? 0.2041 0.3450 0.2249 0.0433  -0.0259 0.0414  139 TYR A CA  
1011 C  C   . TYR A 139 ? 0.2499 0.4064 0.2645 0.0513  -0.0269 0.0514  139 TYR A C   
1012 O  O   . TYR A 139 ? 0.2613 0.4408 0.2702 0.0511  -0.0326 0.0480  139 TYR A O   
1013 C  CB  . TYR A 139 ? 0.2290 0.3850 0.2586 0.0461  -0.0278 0.0409  139 TYR A CB  
1014 C  CG  . TYR A 139 ? 0.2313 0.3742 0.2668 0.0387  -0.0263 0.0316  139 TYR A CG  
1015 C  CD1 . TYR A 139 ? 0.2188 0.3400 0.2595 0.0399  -0.0203 0.0340  139 TYR A CD1 
1016 C  CD2 . TYR A 139 ? 0.2159 0.3685 0.2517 0.0303  -0.0304 0.0204  139 TYR A CD2 
1017 C  CE1 . TYR A 139 ? 0.2383 0.3497 0.2830 0.0337  -0.0188 0.0257  139 TYR A CE1 
1018 C  CE2 . TYR A 139 ? 0.2489 0.3906 0.2897 0.0240  -0.0283 0.0134  139 TYR A CE2 
1019 C  CZ  . TYR A 139 ? 0.2336 0.3556 0.2780 0.0261  -0.0228 0.0163  139 TYR A CZ  
1020 O  OH  . TYR A 139 ? 0.2681 0.3814 0.3161 0.0203  -0.0206 0.0095  139 TYR A OH  
1021 N  N   . LEU A 140 ? 0.2167 0.3610 0.2324 0.0581  -0.0210 0.0635  140 LEU A N   
1022 C  CA  . LEU A 140 ? 0.2326 0.3894 0.2424 0.0666  -0.0202 0.0756  140 LEU A CA  
1023 C  C   . LEU A 140 ? 0.2624 0.4270 0.2793 0.0796  -0.0169 0.0910  140 LEU A C   
1024 O  O   . LEU A 140 ? 0.2868 0.4588 0.3001 0.0884  -0.0144 0.1044  140 LEU A O   
1025 C  CB  . LEU A 140 ? 0.2467 0.3847 0.2518 0.0639  -0.0153 0.0780  140 LEU A CB  
1026 C  CG  . LEU A 140 ? 0.2423 0.3782 0.2388 0.0534  -0.0191 0.0642  140 LEU A CG  
1027 C  CD1 . LEU A 140 ? 0.2601 0.3771 0.2540 0.0505  -0.0139 0.0661  140 LEU A CD1 
1028 C  CD2 . LEU A 140 ? 0.2606 0.4236 0.2473 0.0543  -0.0255 0.0605  140 LEU A CD2 
1029 N  N   . THR A 141 ? 0.2510 0.4145 0.2782 0.0814  -0.0164 0.0899  141 THR A N   
1030 C  CA  . THR A 141 ? 0.2574 0.4338 0.2923 0.0940  -0.0148 0.1024  141 THR A CA  
1031 C  C   . THR A 141 ? 0.2594 0.4545 0.2996 0.0918  -0.0208 0.0934  141 THR A C   
1032 O  O   . THR A 141 ? 0.2621 0.4508 0.3024 0.0804  -0.0234 0.0788  141 THR A O   
1033 C  CB  . THR A 141 ? 0.2863 0.4363 0.3321 0.0990  -0.0053 0.1107  141 THR A CB  
1034 O  OG1 . THR A 141 ? 0.2735 0.4018 0.3237 0.0887  -0.0037 0.0976  141 THR A OG1 
1035 C  CG2 . THR A 141 ? 0.3097 0.4442 0.3532 0.1031  0.0018  0.1228  141 THR A CG2 
1036 N  N   . ASP A 142 ? 0.2546 0.4734 0.2997 0.1029  -0.0226 0.1027  142 ASP A N   
1037 C  CA  . ASP A 142 ? 0.2682 0.5055 0.3214 0.1017  -0.0273 0.0953  142 ASP A CA  
1038 C  C   . ASP A 142 ? 0.3032 0.5164 0.3671 0.0994  -0.0212 0.0917  142 ASP A C   
1039 O  O   . ASP A 142 ? 0.2986 0.4930 0.3686 0.1071  -0.0134 0.1017  142 ASP A O   
1040 C  CB  . ASP A 142 ? 0.2744 0.5426 0.3320 0.1160  -0.0297 0.1080  142 ASP A CB  
1041 C  CG  . ASP A 142 ? 0.3627 0.6554 0.4076 0.1149  -0.0355 0.1066  142 ASP A CG  
1042 O  OD1 . ASP A 142 ? 0.3666 0.6658 0.4036 0.1045  -0.0414 0.0942  142 ASP A OD1 
1043 O  OD2 . ASP A 142 ? 0.4153 0.7197 0.4578 0.1240  -0.0332 0.1171  142 ASP A OD2 
1044 N  N   . VAL A 143 ? 0.2333 0.4469 0.2999 0.0889  -0.0241 0.0773  143 VAL A N   
1045 C  CA  . VAL A 143 ? 0.2427 0.4352 0.3177 0.0857  -0.0187 0.0721  143 VAL A CA  
1046 C  C   . VAL A 143 ? 0.2449 0.4584 0.3310 0.0900  -0.0203 0.0715  143 VAL A C   
1047 O  O   . VAL A 143 ? 0.2508 0.4861 0.3375 0.0836  -0.0267 0.0627  143 VAL A O   
1048 C  CB  . VAL A 143 ? 0.2368 0.4118 0.3064 0.0709  -0.0194 0.0576  143 VAL A CB  
1049 C  CG1 . VAL A 143 ? 0.2335 0.3895 0.3107 0.0686  -0.0137 0.0527  143 VAL A CG1 
1050 C  CG2 . VAL A 143 ? 0.2489 0.4053 0.3086 0.0673  -0.0178 0.0585  143 VAL A CG2 
1051 N  N   . THR A 144 ? 0.2365 0.4432 0.3326 0.1006  -0.0139 0.0802  144 THR A N   
1052 C  CA  . THR A 144 ? 0.2323 0.4560 0.3407 0.1062  -0.0136 0.0804  144 THR A CA  
1053 C  C   . THR A 144 ? 0.2326 0.4314 0.3472 0.1027  -0.0064 0.0738  144 THR A C   
1054 O  O   . THR A 144 ? 0.2255 0.3959 0.3348 0.0964  -0.0024 0.0693  144 THR A O   
1055 C  CB  . THR A 144 ? 0.2676 0.5056 0.3834 0.1237  -0.0113 0.0970  144 THR A CB  
1056 O  OG1 . THR A 144 ? 0.3054 0.5134 0.4254 0.1310  -0.0013 0.1049  144 THR A OG1 
1057 C  CG2 . THR A 144 ? 0.2759 0.5356 0.3833 0.1289  -0.0171 0.1058  144 THR A CG2 
1058 N  N   . GLU A 145 ? 0.2545 0.4661 0.3807 0.1076  -0.0048 0.0733  145 GLU A N   
1059 C  CA  . GLU A 145 ? 0.2603 0.4506 0.3919 0.1053  0.0024  0.0668  145 GLU A CA  
1060 C  C   . GLU A 145 ? 0.2565 0.4184 0.3906 0.1134  0.0114  0.0738  145 GLU A C   
1061 O  O   . GLU A 145 ? 0.2737 0.4129 0.4090 0.1093  0.0173  0.0664  145 GLU A O   
1062 C  CB  . GLU A 145 ? 0.3082 0.5195 0.4522 0.1090  0.0028  0.0647  145 GLU A CB  
1063 C  CG  . GLU A 145 ? 0.3728 0.6034 0.5156 0.0964  -0.0037 0.0533  145 GLU A CG  
1064 C  CD  . GLU A 145 ? 0.3949 0.6443 0.5509 0.0987  -0.0020 0.0504  145 GLU A CD  
1065 O  OE1 . GLU A 145 ? 0.5070 0.7588 0.6731 0.1118  0.0033  0.0581  145 GLU A OE1 
1066 O  OE2 . GLU A 145 ? 0.4437 0.7053 0.6006 0.0875  -0.0052 0.0406  145 GLU A OE2 
1067 N  N   . ASP A 146 ? 0.2421 0.4042 0.3767 0.1242  0.0130  0.0875  146 ASP A N   
1068 C  CA  . ASP A 146 ? 0.2333 0.3670 0.3717 0.1313  0.0225  0.0946  146 ASP A CA  
1069 C  C   . ASP A 146 ? 0.2585 0.3718 0.3869 0.1253  0.0231  0.0960  146 ASP A C   
1070 O  O   . ASP A 146 ? 0.2683 0.3594 0.4006 0.1310  0.0311  0.1032  146 ASP A O   
1071 C  CB  . ASP A 146 ? 0.2480 0.3919 0.3971 0.1494  0.0269  0.1110  146 ASP A CB  
1072 C  CG  . ASP A 146 ? 0.2508 0.4016 0.4129 0.1564  0.0310  0.1089  146 ASP A CG  
1073 O  OD1 . ASP A 146 ? 0.2483 0.3824 0.4117 0.1487  0.0347  0.0963  146 ASP A OD1 
1074 O  OD2 . ASP A 146 ? 0.2669 0.4382 0.4343 0.1668  0.0300  0.1180  146 ASP A OD2 
1075 N  N   . THR A 147 ? 0.2317 0.3518 0.3486 0.1141  0.0156  0.0890  147 THR A N   
1076 C  CA  . THR A 147 ? 0.2343 0.3366 0.3419 0.1079  0.0162  0.0894  147 THR A CA  
1077 C  C   . THR A 147 ? 0.2370 0.3257 0.3371 0.0927  0.0139  0.0739  147 THR A C   
1078 O  O   . THR A 147 ? 0.2442 0.3330 0.3343 0.0849  0.0094  0.0708  147 THR A O   
1079 C  CB  . THR A 147 ? 0.2528 0.3746 0.3522 0.1106  0.0103  0.0980  147 THR A CB  
1080 O  OG1 . THR A 147 ? 0.2665 0.4105 0.3592 0.1023  0.0010  0.0884  147 THR A OG1 
1081 C  CG2 . THR A 147 ? 0.2695 0.4073 0.3752 0.1268  0.0122  0.1149  147 THR A CG2 
1082 N  N   . ALA A 148 ? 0.2519 0.3295 0.3566 0.0888  0.0173  0.0643  148 ALA A N   
1083 C  CA  . ALA A 148 ? 0.2358 0.2985 0.3340 0.0761  0.0166  0.0511  148 ALA A CA  
1084 C  C   . ALA A 148 ? 0.2256 0.3036 0.3151 0.0665  0.0084  0.0437  148 ALA A C   
1085 O  O   . ALA A 148 ? 0.2317 0.3020 0.3122 0.0584  0.0057  0.0395  148 ALA A O   
1086 C  CB  . ALA A 148 ? 0.2554 0.2944 0.3498 0.0725  0.0202  0.0514  148 ALA A CB  
1087 N  N   . PRO A 149 ? 0.2274 0.3268 0.3204 0.0668  0.0048  0.0415  149 PRO A N   
1088 C  CA  . PRO A 149 ? 0.2322 0.3443 0.3187 0.0567  -0.0019 0.0334  149 PRO A CA  
1089 C  C   . PRO A 149 ? 0.2507 0.3462 0.3322 0.0462  -0.0005 0.0226  149 PRO A C   
1090 O  O   . PRO A 149 ? 0.2489 0.3310 0.3336 0.0467  0.0048  0.0194  149 PRO A O   
1091 C  CB  . PRO A 149 ? 0.2227 0.3601 0.3178 0.0599  -0.0042 0.0335  149 PRO A CB  
1092 C  CG  . PRO A 149 ? 0.2271 0.3576 0.3320 0.0686  0.0028  0.0369  149 PRO A CG  
1093 C  CD  . PRO A 149 ? 0.2411 0.3536 0.3454 0.0761  0.0073  0.0456  149 PRO A CD  
1094 N  N   . THR A 150 ? 0.2226 0.3198 0.2958 0.0370  -0.0052 0.0170  150 THR A N   
1095 C  CA  . THR A 150 ? 0.2041 0.2914 0.2728 0.0274  -0.0047 0.0077  150 THR A CA  
1096 C  C   . THR A 150 ? 0.2075 0.3075 0.2829 0.0258  -0.0039 0.0036  150 THR A C   
1097 O  O   . THR A 150 ? 0.2513 0.3725 0.3325 0.0274  -0.0069 0.0052  150 THR A O   
1098 C  CB  . THR A 150 ? 0.2019 0.2905 0.2620 0.0193  -0.0095 0.0036  150 THR A CB  
1099 O  OG1 . THR A 150 ? 0.2258 0.3069 0.2802 0.0216  -0.0104 0.0082  150 THR A OG1 
1100 C  CG2 . THR A 150 ? 0.2438 0.3190 0.2985 0.0107  -0.0082 -0.0039 150 THR A CG2 
1101 N  N   . TYR A 151 ? 0.1941 0.2828 0.2691 0.0226  0.0004  -0.0015 151 TYR A N   
1102 C  CA  . TYR A 151 ? 0.2028 0.3024 0.2831 0.0197  0.0020  -0.0056 151 TYR A CA  
1103 C  C   . TYR A 151 ? 0.2089 0.3033 0.2822 0.0090  0.0010  -0.0119 151 TYR A C   
1104 O  O   . TYR A 151 ? 0.2312 0.3088 0.2957 0.0057  0.0015  -0.0140 151 TYR A O   
1105 C  CB  . TYR A 151 ? 0.2238 0.3164 0.3087 0.0248  0.0085  -0.0066 151 TYR A CB  
1106 C  CG  . TYR A 151 ? 0.2080 0.3108 0.3039 0.0356  0.0108  -0.0008 151 TYR A CG  
1107 C  CD1 . TYR A 151 ? 0.2316 0.3271 0.3289 0.0437  0.0116  0.0058  151 TYR A CD1 
1108 C  CD2 . TYR A 151 ? 0.2286 0.3482 0.3341 0.0381  0.0129  -0.0013 151 TYR A CD2 
1109 C  CE1 . TYR A 151 ? 0.2444 0.3481 0.3521 0.0548  0.0145  0.0125  151 TYR A CE1 
1110 C  CE2 . TYR A 151 ? 0.2720 0.4013 0.3880 0.0492  0.0153  0.0046  151 TYR A CE2 
1111 C  CZ  . TYR A 151 ? 0.2746 0.3955 0.3916 0.0578  0.0161  0.0117  151 TYR A CZ  
1112 O  OH  . TYR A 151 ? 0.3416 0.4718 0.4697 0.0701  0.0193  0.0188  151 TYR A OH  
1113 N  N   . VAL A 152 ? 0.1854 0.2949 0.2635 0.0038  0.0000  -0.0146 152 VAL A N   
1114 C  CA  . VAL A 152 ? 0.2129 0.3173 0.2862 -0.0061 0.0003  -0.0196 152 VAL A CA  
1115 C  C   . VAL A 152 ? 0.2064 0.3198 0.2868 -0.0089 0.0047  -0.0218 152 VAL A C   
1116 O  O   . VAL A 152 ? 0.2087 0.3382 0.2993 -0.0046 0.0057  -0.0203 152 VAL A O   
1117 C  CB  . VAL A 152 ? 0.2240 0.3359 0.2962 -0.0125 -0.0050 -0.0218 152 VAL A CB  
1118 C  CG1 . VAL A 152 ? 0.2273 0.3290 0.2909 -0.0102 -0.0084 -0.0198 152 VAL A CG1 
1119 C  CG2 . VAL A 152 ? 0.2389 0.3762 0.3218 -0.0115 -0.0081 -0.0217 152 VAL A CG2 
1120 N  N   . VAL A 153 ? 0.1950 0.2984 0.2700 -0.0155 0.0079  -0.0245 153 VAL A N   
1121 C  CA  . VAL A 153 ? 0.2050 0.3168 0.2861 -0.0196 0.0127  -0.0260 153 VAL A CA  
1122 C  C   . VAL A 153 ? 0.2077 0.3202 0.2892 -0.0301 0.0121  -0.0286 153 VAL A C   
1123 O  O   . VAL A 153 ? 0.2496 0.3778 0.3402 -0.0341 0.0095  -0.0307 153 VAL A O   
1124 C  CB  . VAL A 153 ? 0.2204 0.3213 0.2956 -0.0171 0.0188  -0.0260 153 VAL A CB  
1125 C  CG1 . VAL A 153 ? 0.2429 0.3561 0.3259 -0.0194 0.0246  -0.0264 153 VAL A CG1 
1126 C  CG2 . VAL A 153 ? 0.2659 0.3614 0.3398 -0.0076 0.0193  -0.0251 153 VAL A CG2 
1127 N  N   . ASP A 154 ? 0.2029 0.2989 0.2750 -0.0342 0.0146  -0.0288 154 ASP A N   
1128 C  CA  . ASP A 154 ? 0.2024 0.2946 0.2747 -0.0437 0.0157  -0.0306 154 ASP A CA  
1129 C  C   . ASP A 154 ? 0.2225 0.2942 0.2819 -0.0438 0.0177  -0.0288 154 ASP A C   
1130 O  O   . ASP A 154 ? 0.2047 0.2685 0.2560 -0.0376 0.0178  -0.0270 154 ASP A O   
1131 C  CB  . ASP A 154 ? 0.1987 0.3018 0.2811 -0.0491 0.0215  -0.0310 154 ASP A CB  
1132 C  CG  . ASP A 154 ? 0.2448 0.3487 0.3333 -0.0601 0.0226  -0.0342 154 ASP A CG  
1133 O  OD1 . ASP A 154 ? 0.2454 0.3364 0.3279 -0.0638 0.0209  -0.0356 154 ASP A OD1 
1134 O  OD2 . ASP A 154 ? 0.2795 0.3975 0.3803 -0.0654 0.0262  -0.0355 154 ASP A OD2 
1135 N  N   . ARG A 155 ? 0.2061 0.2698 0.2640 -0.0509 0.0194  -0.0294 155 ARG A N   
1136 C  CA  . ARG A 155 ? 0.2146 0.2605 0.2609 -0.0504 0.0214  -0.0266 155 ARG A CA  
1137 C  C   . ARG A 155 ? 0.2187 0.2626 0.2604 -0.0476 0.0273  -0.0227 155 ARG A C   
1138 O  O   . ARG A 155 ? 0.2214 0.2747 0.2702 -0.0498 0.0322  -0.0219 155 ARG A O   
1139 C  CB  . ARG A 155 ? 0.1967 0.2344 0.2446 -0.0583 0.0238  -0.0273 155 ARG A CB  
1140 C  CG  . ARG A 155 ? 0.2244 0.2655 0.2767 -0.0619 0.0183  -0.0329 155 ARG A CG  
1141 C  CD  . ARG A 155 ? 0.2254 0.2537 0.2772 -0.0686 0.0208  -0.0345 155 ARG A CD  
1142 N  NE  . ARG A 155 ? 0.2558 0.2676 0.2956 -0.0641 0.0201  -0.0314 155 ARG A NE  
1143 C  CZ  . ARG A 155 ? 0.2501 0.2494 0.2877 -0.0671 0.0210  -0.0329 155 ARG A CZ  
1144 N  NH1 . ARG A 155 ? 0.2842 0.2836 0.3305 -0.0754 0.0230  -0.0382 155 ARG A NH1 
1145 N  NH2 . ARG A 155 ? 0.2888 0.2758 0.3160 -0.0618 0.0200  -0.0296 155 ARG A NH2 
1146 N  N   . ALA A 156 ? 0.2187 0.2520 0.2486 -0.0428 0.0269  -0.0206 156 ALA A N   
1147 C  CA  . ALA A 156 ? 0.2094 0.2428 0.2330 -0.0391 0.0317  -0.0180 156 ALA A CA  
1148 C  C   . ALA A 156 ? 0.2403 0.2739 0.2654 -0.0438 0.0392  -0.0136 156 ALA A C   
1149 O  O   . ALA A 156 ? 0.2366 0.2783 0.2630 -0.0426 0.0444  -0.0123 156 ALA A O   
1150 C  CB  . ALA A 156 ? 0.2366 0.2599 0.2472 -0.0344 0.0295  -0.0170 156 ALA A CB  
1151 N  N   . ALA A 157 ? 0.2374 0.2614 0.2624 -0.0489 0.0408  -0.0112 157 ALA A N   
1152 C  CA  . ALA A 157 ? 0.2492 0.2714 0.2766 -0.0534 0.0491  -0.0059 157 ALA A CA  
1153 C  C   . ALA A 157 ? 0.2479 0.2836 0.2897 -0.0590 0.0528  -0.0080 157 ALA A C   
1154 O  O   . ALA A 157 ? 0.2977 0.3381 0.3417 -0.0604 0.0604  -0.0037 157 ALA A O   
1155 C  CB  . ALA A 157 ? 0.2940 0.3016 0.3207 -0.0578 0.0508  -0.0032 157 ALA A CB  
1156 N  N   . HIS A 158 ? 0.2311 0.2752 0.2831 -0.0619 0.0475  -0.0142 158 HIS A N   
1157 C  CA  . HIS A 158 ? 0.2376 0.2980 0.3048 -0.0670 0.0500  -0.0168 158 HIS A CA  
1158 C  C   . HIS A 158 ? 0.2364 0.3098 0.3043 -0.0611 0.0524  -0.0158 158 HIS A C   
1159 O  O   . HIS A 158 ? 0.2540 0.3396 0.3322 -0.0646 0.0581  -0.0150 158 HIS A O   
1160 C  CB  . HIS A 158 ? 0.2385 0.3073 0.3145 -0.0698 0.0424  -0.0237 158 HIS A CB  
1161 C  CG  . HIS A 158 ? 0.2357 0.2939 0.3129 -0.0767 0.0410  -0.0266 158 HIS A CG  
1162 N  ND1 . HIS A 158 ? 0.2305 0.2954 0.3130 -0.0793 0.0340  -0.0334 158 HIS A ND1 
1163 C  CD2 . HIS A 158 ? 0.2489 0.2907 0.3231 -0.0814 0.0461  -0.0239 158 HIS A CD2 
1164 C  CE1 . HIS A 158 ? 0.2652 0.3180 0.3477 -0.0856 0.0349  -0.0359 158 HIS A CE1 
1165 N  NE2 . HIS A 158 ? 0.2399 0.2776 0.3180 -0.0869 0.0425  -0.0300 158 HIS A NE2 
1166 N  N   . LEU A 159 ? 0.2309 0.3020 0.2890 -0.0524 0.0487  -0.0163 159 LEU A N   
1167 C  CA  . LEU A 159 ? 0.2233 0.3047 0.2815 -0.0459 0.0509  -0.0167 159 LEU A CA  
1168 C  C   . LEU A 159 ? 0.2323 0.3095 0.2796 -0.0430 0.0576  -0.0125 159 LEU A C   
1169 O  O   . LEU A 159 ? 0.2926 0.3785 0.3393 -0.0379 0.0609  -0.0134 159 LEU A O   
1170 C  CB  . LEU A 159 ? 0.2329 0.3127 0.2872 -0.0383 0.0441  -0.0203 159 LEU A CB  
1171 C  CG  . LEU A 159 ? 0.2267 0.3147 0.2916 -0.0394 0.0379  -0.0234 159 LEU A CG  
1172 C  CD1 . LEU A 159 ? 0.2606 0.3416 0.3196 -0.0331 0.0314  -0.0250 159 LEU A CD1 
1173 C  CD2 . LEU A 159 ? 0.2686 0.3763 0.3475 -0.0383 0.0401  -0.0244 159 LEU A CD2 
1174 N  N   . GLY A 160 ? 0.2573 0.3220 0.2958 -0.0455 0.0599  -0.0079 160 GLY A N   
1175 C  CA  . GLY A 160 ? 0.2684 0.3307 0.2950 -0.0420 0.0659  -0.0028 160 GLY A CA  
1176 C  C   . GLY A 160 ? 0.2796 0.3399 0.2931 -0.0337 0.0622  -0.0058 160 GLY A C   
1177 O  O   . GLY A 160 ? 0.3307 0.3966 0.3365 -0.0294 0.0668  -0.0049 160 GLY A O   
1178 N  N   . VAL A 161 ? 0.2649 0.3182 0.2762 -0.0317 0.0542  -0.0100 161 VAL A N   
1179 C  CA  . VAL A 161 ? 0.2688 0.3191 0.2690 -0.0252 0.0507  -0.0137 161 VAL A CA  
1180 C  C   . VAL A 161 ? 0.2522 0.2908 0.2425 -0.0251 0.0467  -0.0113 161 VAL A C   
1181 O  O   . VAL A 161 ? 0.2661 0.2971 0.2601 -0.0292 0.0442  -0.0093 161 VAL A O   
1182 C  CB  . VAL A 161 ? 0.2228 0.2758 0.2294 -0.0218 0.0460  -0.0206 161 VAL A CB  
1183 C  CG1 . VAL A 161 ? 0.2671 0.3331 0.2836 -0.0205 0.0507  -0.0223 161 VAL A CG1 
1184 C  CG2 . VAL A 161 ? 0.2483 0.2960 0.2616 -0.0245 0.0395  -0.0214 161 VAL A CG2 
1185 N  N   . PRO A 162 ? 0.2586 0.2964 0.2363 -0.0204 0.0459  -0.0121 162 PRO A N   
1186 C  CA  . PRO A 162 ? 0.2577 0.2871 0.2262 -0.0194 0.0423  -0.0093 162 PRO A CA  
1187 C  C   . PRO A 162 ? 0.2725 0.2957 0.2435 -0.0191 0.0346  -0.0145 162 PRO A C   
1188 O  O   . PRO A 162 ? 0.2441 0.2694 0.2207 -0.0180 0.0321  -0.0207 162 PRO A O   
1189 C  CB  . PRO A 162 ? 0.2906 0.3266 0.2459 -0.0142 0.0439  -0.0099 162 PRO A CB  
1190 C  CG  . PRO A 162 ? 0.2550 0.2984 0.2137 -0.0120 0.0443  -0.0183 162 PRO A CG  
1191 C  CD  . PRO A 162 ? 0.2736 0.3200 0.2454 -0.0155 0.0482  -0.0168 162 PRO A CD  
1192 N  N   . LEU A 163 ? 0.2521 0.2672 0.2191 -0.0197 0.0316  -0.0112 163 LEU A N   
1193 C  CA  . LEU A 163 ? 0.2270 0.2368 0.1950 -0.0191 0.0248  -0.0154 163 LEU A CA  
1194 C  C   . LEU A 163 ? 0.2389 0.2519 0.1994 -0.0150 0.0218  -0.0204 163 LEU A C   
1195 O  O   . LEU A 163 ? 0.2398 0.2503 0.2037 -0.0147 0.0173  -0.0256 163 LEU A O   
1196 C  CB  . LEU A 163 ? 0.2558 0.2567 0.2228 -0.0207 0.0231  -0.0107 163 LEU A CB  
1197 C  CG  . LEU A 163 ? 0.2645 0.2611 0.2406 -0.0259 0.0251  -0.0086 163 LEU A CG  
1198 C  CD1 . LEU A 163 ? 0.2870 0.2734 0.2615 -0.0270 0.0241  -0.0052 163 LEU A CD1 
1199 C  CD2 . LEU A 163 ? 0.2676 0.2679 0.2535 -0.0278 0.0219  -0.0142 163 LEU A CD2 
1200 N  N   . LEU A 164 ? 0.2524 0.2718 0.2030 -0.0121 0.0244  -0.0192 164 LEU A N   
1201 C  CA  . LEU A 164 ? 0.2735 0.2992 0.2171 -0.0088 0.0220  -0.0259 164 LEU A CA  
1202 C  C   . LEU A 164 ? 0.2824 0.3167 0.2245 -0.0072 0.0269  -0.0298 164 LEU A C   
1203 O  O   . LEU A 164 ? 0.2909 0.3308 0.2274 -0.0062 0.0321  -0.0242 164 LEU A O   
1204 C  CB  . LEU A 164 ? 0.3026 0.3321 0.2346 -0.0059 0.0205  -0.0218 164 LEU A CB  
1205 C  CG  . LEU A 164 ? 0.3402 0.3787 0.2649 -0.0033 0.0168  -0.0301 164 LEU A CG  
1206 C  CD1 . LEU A 164 ? 0.3266 0.3599 0.2592 -0.0055 0.0117  -0.0385 164 LEU A CD1 
1207 C  CD2 . LEU A 164 ? 0.4156 0.4610 0.3290 0.0004  0.0150  -0.0246 164 LEU A CD2 
1208 N  N   . THR A 165 ? 0.2824 0.3174 0.2297 -0.0067 0.0260  -0.0388 165 THR A N   
1209 C  CA  . THR A 165 ? 0.2854 0.3281 0.2321 -0.0047 0.0312  -0.0435 165 THR A CA  
1210 C  C   . THR A 165 ? 0.3308 0.3826 0.2653 -0.0017 0.0312  -0.0496 165 THR A C   
1211 O  O   . THR A 165 ? 0.3052 0.3576 0.2337 -0.0015 0.0262  -0.0519 165 THR A O   
1212 C  CB  . THR A 165 ? 0.3227 0.3616 0.2812 -0.0045 0.0312  -0.0504 165 THR A CB  
1213 O  OG1 . THR A 165 ? 0.3514 0.3849 0.3107 -0.0045 0.0265  -0.0577 165 THR A OG1 
1214 C  CG2 . THR A 165 ? 0.3178 0.3517 0.2880 -0.0069 0.0309  -0.0444 165 THR A CG2 
1215 N  N   . PRO A 166 ? 0.3184 0.3793 0.2487 0.0008  0.0367  -0.0528 166 PRO A N   
1216 C  CA  . PRO A 166 ? 0.3168 0.3884 0.2349 0.0037  0.0365  -0.0607 166 PRO A CA  
1217 C  C   . PRO A 166 ? 0.3704 0.4389 0.2909 0.0028  0.0315  -0.0735 166 PRO A C   
1218 O  O   . PRO A 166 ? 0.3909 0.4681 0.3014 0.0037  0.0284  -0.0793 166 PRO A O   
1219 C  CB  . PRO A 166 ? 0.3231 0.4034 0.2397 0.0062  0.0441  -0.0631 166 PRO A CB  
1220 C  CG  . PRO A 166 ? 0.3389 0.4164 0.2624 0.0046  0.0485  -0.0512 166 PRO A CG  
1221 C  CD  . PRO A 166 ? 0.3149 0.3791 0.2507 0.0010  0.0435  -0.0488 166 PRO A CD  
1222 N  N   . GLU A 167 ? 0.3274 0.3845 0.2614 0.0009  0.0306  -0.0775 167 GLU A N   
1223 C  CA  . GLU A 167 ? 0.3570 0.4092 0.2953 -0.0006 0.0268  -0.0888 167 GLU A CA  
1224 C  C   . GLU A 167 ? 0.3622 0.4119 0.2988 -0.0032 0.0200  -0.0862 167 GLU A C   
1225 O  O   . GLU A 167 ? 0.3574 0.4052 0.2969 -0.0052 0.0167  -0.0956 167 GLU A O   
1226 C  CB  . GLU A 167 ? 0.3992 0.4394 0.3528 -0.0009 0.0289  -0.0922 167 GLU A CB  
1227 C  CG  . GLU A 167 ? 0.4324 0.4623 0.3956 -0.0027 0.0261  -0.0827 167 GLU A CG  
1228 C  CD  . GLU A 167 ? 0.4600 0.4793 0.4373 -0.0021 0.0276  -0.0860 167 GLU A CD  
1229 O  OE1 . GLU A 167 ? 0.4864 0.5062 0.4688 0.0011  0.0329  -0.0900 167 GLU A OE1 
1230 O  OE2 . GLU A 167 ? 0.4647 0.4754 0.4482 -0.0040 0.0240  -0.0840 167 GLU A OE2 
1231 N  N   . GLY A 168 ? 0.3233 0.3729 0.2564 -0.0032 0.0182  -0.0742 168 GLY A N   
1232 C  CA  . GLY A 168 ? 0.3339 0.3822 0.2654 -0.0047 0.0122  -0.0711 168 GLY A CA  
1233 C  C   . GLY A 168 ? 0.3057 0.3410 0.2490 -0.0075 0.0097  -0.0682 168 GLY A C   
1234 O  O   . GLY A 168 ? 0.3026 0.3364 0.2471 -0.0090 0.0049  -0.0693 168 GLY A O   
1235 N  N   . THR A 169 ? 0.2975 0.3251 0.2494 -0.0078 0.0126  -0.0642 169 THR A N   
1236 C  CA  . THR A 169 ? 0.3033 0.3205 0.2652 -0.0097 0.0104  -0.0606 169 THR A CA  
1237 C  C   . THR A 169 ? 0.2843 0.2993 0.2491 -0.0100 0.0125  -0.0513 169 THR A C   
1238 O  O   . THR A 169 ? 0.3016 0.3219 0.2615 -0.0092 0.0160  -0.0473 169 THR A O   
1239 C  CB  . THR A 169 ? 0.3499 0.3608 0.3224 -0.0098 0.0118  -0.0675 169 THR A CB  
1240 O  OG1 . THR A 169 ? 0.3565 0.3689 0.3326 -0.0076 0.0169  -0.0677 169 THR A OG1 
1241 C  CG2 . THR A 169 ? 0.3650 0.3776 0.3363 -0.0106 0.0110  -0.0790 169 THR A CG2 
1242 N  N   . GLY A 170 ? 0.2807 0.2886 0.2538 -0.0113 0.0107  -0.0481 170 GLY A N   
1243 C  CA  . GLY A 170 ? 0.2397 0.2470 0.2178 -0.0122 0.0124  -0.0418 170 GLY A CA  
1244 C  C   . GLY A 170 ? 0.2594 0.2673 0.2473 -0.0108 0.0148  -0.0439 170 GLY A C   
1245 O  O   . GLY A 170 ? 0.2639 0.2722 0.2583 -0.0116 0.0147  -0.0397 170 GLY A O   
1246 N  N   . ALA A 171 ? 0.2387 0.2473 0.2280 -0.0084 0.0171  -0.0507 171 ALA A N   
1247 C  CA  . ALA A 171 ? 0.2662 0.2749 0.2654 -0.0055 0.0202  -0.0524 171 ALA A CA  
1248 C  C   . ALA A 171 ? 0.2705 0.2873 0.2685 -0.0034 0.0256  -0.0546 171 ALA A C   
1249 O  O   . ALA A 171 ? 0.2776 0.2987 0.2663 -0.0035 0.0272  -0.0576 171 ALA A O   
1250 C  CB  . ALA A 171 ? 0.2775 0.2789 0.2816 -0.0038 0.0203  -0.0587 171 ALA A CB  
1251 N  N   . TYR A 172 ? 0.2470 0.2675 0.2545 -0.0010 0.0285  -0.0527 172 TYR A N   
1252 C  CA  . TYR A 172 ? 0.2413 0.2713 0.2500 0.0009  0.0341  -0.0531 172 TYR A CA  
1253 C  C   . TYR A 172 ? 0.2937 0.3229 0.3100 0.0063  0.0381  -0.0589 172 TYR A C   
1254 O  O   . TYR A 172 ? 0.2897 0.3178 0.3169 0.0092  0.0379  -0.0562 172 TYR A O   
1255 C  CB  . TYR A 172 ? 0.2331 0.2706 0.2483 -0.0011 0.0343  -0.0458 172 TYR A CB  
1256 C  CG  . TYR A 172 ? 0.2160 0.2515 0.2252 -0.0065 0.0311  -0.0405 172 TYR A CG  
1257 C  CD1 . TYR A 172 ? 0.2363 0.2747 0.2366 -0.0087 0.0338  -0.0385 172 TYR A CD1 
1258 C  CD2 . TYR A 172 ? 0.2234 0.2540 0.2356 -0.0088 0.0259  -0.0374 172 TYR A CD2 
1259 C  CE1 . TYR A 172 ? 0.2307 0.2653 0.2262 -0.0128 0.0317  -0.0332 172 TYR A CE1 
1260 C  CE2 . TYR A 172 ? 0.2397 0.2671 0.2468 -0.0132 0.0236  -0.0335 172 TYR A CE2 
1261 C  CZ  . TYR A 172 ? 0.2372 0.2657 0.2365 -0.0151 0.0266  -0.0313 172 TYR A CZ  
1262 O  OH  . TYR A 172 ? 0.2402 0.2637 0.2354 -0.0188 0.0252  -0.0269 172 TYR A OH  
1263 N  N   . SER A 173 ? 0.2832 0.3137 0.2940 0.0083  0.0420  -0.0667 173 SER A N   
1264 C  CA  . SER A 173 ? 0.3314 0.3596 0.3497 0.0137  0.0469  -0.0735 173 SER A CA  
1265 C  C   . SER A 173 ? 0.3081 0.3464 0.3355 0.0176  0.0517  -0.0694 173 SER A C   
1266 O  O   . SER A 173 ? 0.2974 0.3464 0.3228 0.0154  0.0527  -0.0643 173 SER A O   
1267 C  CB  . SER A 173 ? 0.3644 0.3933 0.3734 0.0143  0.0502  -0.0844 173 SER A CB  
1268 O  OG  . SER A 173 ? 0.3710 0.4125 0.3728 0.0146  0.0540  -0.0835 173 SER A OG  
1269 N  N   . LYS A 174 ? 0.3337 0.3687 0.3724 0.0236  0.0550  -0.0715 174 LYS A N   
1270 C  CA  . LYS A 174 ? 0.3403 0.3867 0.3890 0.0286  0.0599  -0.0684 174 LYS A CA  
1271 C  C   . LYS A 174 ? 0.3415 0.3976 0.3844 0.0297  0.0662  -0.0737 174 LYS A C   
1272 O  O   . LYS A 174 ? 0.3728 0.4425 0.4202 0.0304  0.0693  -0.0692 174 LYS A O   
1273 C  CB  . LYS A 174 ? 0.3636 0.4037 0.4254 0.0363  0.0630  -0.0692 174 LYS A CB  
1274 C  CG  . LYS A 174 ? 0.3815 0.4145 0.4496 0.0365  0.0576  -0.0620 174 LYS A CG  
1275 C  CD  . LYS A 174 ? 0.4227 0.4492 0.5039 0.0454  0.0618  -0.0611 174 LYS A CD  
1276 C  CE  . LYS A 174 ? 0.4224 0.4435 0.5088 0.0460  0.0567  -0.0523 174 LYS A CE  
1277 N  NZ  . LYS A 174 ? 0.5266 0.5391 0.6253 0.0552  0.0614  -0.0498 174 LYS A NZ  
1278 N  N   . GLU A 175 ? 0.3700 0.4209 0.4029 0.0295  0.0683  -0.0836 175 GLU A N   
1279 C  CA  . GLU A 175 ? 0.4346 0.4961 0.4608 0.0314  0.0748  -0.0890 175 GLU A CA  
1280 C  C   . GLU A 175 ? 0.3974 0.4696 0.4131 0.0261  0.0737  -0.0824 175 GLU A C   
1281 O  O   . GLU A 175 ? 0.4319 0.5171 0.4475 0.0274  0.0793  -0.0803 175 GLU A O   
1282 C  CB  . GLU A 175 ? 0.4782 0.5327 0.4965 0.0328  0.0772  -0.1027 175 GLU A CB  
1283 C  CG  . GLU A 175 ? 0.5429 0.5876 0.5521 0.0273  0.0705  -0.1063 175 GLU A CG  
1284 C  CD  . GLU A 175 ? 0.6059 0.6342 0.6253 0.0277  0.0680  -0.1086 175 GLU A CD  
1285 O  OE1 . GLU A 175 ? 0.4772 0.5018 0.5086 0.0298  0.0669  -0.0999 175 GLU A OE1 
1286 O  OE2 . GLU A 175 ? 0.6249 0.6450 0.6404 0.0258  0.0673  -0.1192 175 GLU A OE2 
1287 N  N   . ALA A 176 ? 0.3820 0.4489 0.3899 0.0203  0.0671  -0.0784 176 ALA A N   
1288 C  CA  . ALA A 176 ? 0.4077 0.4823 0.4057 0.0159  0.0667  -0.0715 176 ALA A CA  
1289 C  C   . ALA A 176 ? 0.3562 0.4352 0.3631 0.0123  0.0656  -0.0606 176 ALA A C   
1290 O  O   . ALA A 176 ? 0.3690 0.4563 0.3721 0.0095  0.0687  -0.0547 176 ALA A O   
1291 C  CB  . ALA A 176 ? 0.4025 0.4706 0.3874 0.0122  0.0610  -0.0724 176 ALA A CB  
1292 N  N   . TYR A 177 ? 0.3049 0.3792 0.3237 0.0123  0.0616  -0.0578 177 TYR A N   
1293 C  CA  . TYR A 177 ? 0.2963 0.3756 0.3234 0.0081  0.0594  -0.0492 177 TYR A CA  
1294 C  C   . TYR A 177 ? 0.2945 0.3805 0.3378 0.0121  0.0602  -0.0481 177 TYR A C   
1295 O  O   . TYR A 177 ? 0.2796 0.3633 0.3302 0.0114  0.0550  -0.0448 177 TYR A O   
1296 C  CB  . TYR A 177 ? 0.2697 0.3384 0.2927 0.0034  0.0520  -0.0460 177 TYR A CB  
1297 C  CG  . TYR A 177 ? 0.2927 0.3566 0.3008 0.0003  0.0510  -0.0457 177 TYR A CG  
1298 C  CD1 . TYR A 177 ? 0.2758 0.3436 0.2796 -0.0041 0.0530  -0.0391 177 TYR A CD1 
1299 C  CD2 . TYR A 177 ? 0.3096 0.3657 0.3085 0.0021  0.0486  -0.0519 177 TYR A CD2 
1300 C  CE1 . TYR A 177 ? 0.3015 0.3657 0.2916 -0.0055 0.0524  -0.0373 177 TYR A CE1 
1301 C  CE2 . TYR A 177 ? 0.3001 0.3549 0.2856 0.0001  0.0472  -0.0512 177 TYR A CE2 
1302 C  CZ  . TYR A 177 ? 0.3226 0.3815 0.3033 -0.0030 0.0492  -0.0432 177 TYR A CZ  
1303 O  OH  . TYR A 177 ? 0.3584 0.4165 0.3258 -0.0036 0.0481  -0.0409 177 TYR A OH  
1304 N  N   . PRO A 178 ? 0.2937 0.3897 0.3428 0.0170  0.0668  -0.0506 178 PRO A N   
1305 C  CA  . PRO A 178 ? 0.2881 0.3922 0.3533 0.0223  0.0677  -0.0490 178 PRO A CA  
1306 C  C   . PRO A 178 ? 0.3073 0.4227 0.3830 0.0178  0.0642  -0.0418 178 PRO A C   
1307 O  O   . PRO A 178 ? 0.2808 0.4000 0.3676 0.0215  0.0611  -0.0394 178 PRO A O   
1308 C  CB  . PRO A 178 ? 0.3094 0.4240 0.3776 0.0277  0.0766  -0.0529 178 PRO A CB  
1309 C  CG  . PRO A 178 ? 0.3296 0.4470 0.3847 0.0228  0.0800  -0.0533 178 PRO A CG  
1310 C  CD  . PRO A 178 ? 0.2907 0.3930 0.3320 0.0185  0.0741  -0.0544 178 PRO A CD  
1311 N  N   . GLU A 179 ? 0.3000 0.4215 0.3730 0.0101  0.0651  -0.0383 179 GLU A N   
1312 C  CA  . GLU A 179 ? 0.3489 0.4822 0.4333 0.0048  0.0623  -0.0334 179 GLU A CA  
1313 C  C   . GLU A 179 ? 0.3097 0.4350 0.3940 0.0024  0.0537  -0.0317 179 GLU A C   
1314 O  O   . GLU A 179 ? 0.3183 0.4548 0.4139 0.0013  0.0501  -0.0293 179 GLU A O   
1315 C  CB  . GLU A 179 ? 0.3696 0.5080 0.4517 -0.0037 0.0661  -0.0303 179 GLU A CB  
1316 C  CG  . GLU A 179 ? 0.5222 0.6726 0.6064 -0.0019 0.0754  -0.0305 179 GLU A CG  
1317 C  CD  . GLU A 179 ? 0.6750 0.8313 0.7601 -0.0109 0.0798  -0.0257 179 GLU A CD  
1318 O  OE1 . GLU A 179 ? 0.6954 0.8495 0.7845 -0.0186 0.0756  -0.0230 179 GLU A OE1 
1319 O  OE2 . GLU A 179 ? 0.7455 0.9081 0.8273 -0.0104 0.0880  -0.0246 179 GLU A OE2 
1320 N  N   . LEU A 180 ? 0.2542 0.3622 0.3260 0.0017  0.0503  -0.0331 180 LEU A N   
1321 C  CA  . LEU A 180 ? 0.2733 0.3740 0.3446 -0.0001 0.0428  -0.0314 180 LEU A CA  
1322 C  C   . LEU A 180 ? 0.2668 0.3712 0.3476 0.0074  0.0404  -0.0307 180 LEU A C   
1323 O  O   . LEU A 180 ? 0.2574 0.3681 0.3445 0.0065  0.0352  -0.0277 180 LEU A O   
1324 C  CB  . LEU A 180 ? 0.2292 0.3120 0.2863 -0.0014 0.0404  -0.0333 180 LEU A CB  
1325 C  CG  . LEU A 180 ? 0.2537 0.3320 0.3001 -0.0074 0.0423  -0.0324 180 LEU A CG  
1326 C  CD1 . LEU A 180 ? 0.2427 0.3059 0.2766 -0.0075 0.0387  -0.0341 180 LEU A CD1 
1327 C  CD2 . LEU A 180 ? 0.3124 0.3959 0.3633 -0.0151 0.0413  -0.0284 180 LEU A CD2 
1328 N  N   . TYR A 181 ? 0.2529 0.3535 0.3348 0.0152  0.0444  -0.0335 181 TYR A N   
1329 C  CA  . TYR A 181 ? 0.2725 0.3742 0.3637 0.0237  0.0436  -0.0316 181 TYR A CA  
1330 C  C   . TYR A 181 ? 0.2774 0.4004 0.3833 0.0273  0.0445  -0.0280 181 TYR A C   
1331 O  O   . TYR A 181 ? 0.2906 0.4194 0.4047 0.0329  0.0414  -0.0237 181 TYR A O   
1332 C  CB  . TYR A 181 ? 0.2657 0.3548 0.3544 0.0306  0.0487  -0.0366 181 TYR A CB  
1333 C  CG  . TYR A 181 ? 0.2660 0.3360 0.3428 0.0274  0.0461  -0.0400 181 TYR A CG  
1334 C  CD1 . TYR A 181 ? 0.2504 0.3150 0.3148 0.0218  0.0469  -0.0445 181 TYR A CD1 
1335 C  CD2 . TYR A 181 ? 0.2732 0.3325 0.3517 0.0302  0.0428  -0.0379 181 TYR A CD2 
1336 C  CE1 . TYR A 181 ? 0.2560 0.3060 0.3105 0.0190  0.0440  -0.0477 181 TYR A CE1 
1337 C  CE2 . TYR A 181 ? 0.2673 0.3108 0.3364 0.0266  0.0405  -0.0410 181 TYR A CE2 
1338 C  CZ  . TYR A 181 ? 0.2719 0.3116 0.3295 0.0210  0.0408  -0.0463 181 TYR A CZ  
1339 O  OH  . TYR A 181 ? 0.2630 0.2898 0.3125 0.0178  0.0381  -0.0496 181 TYR A OH  
1340 N  N   . GLU A 182 ? 0.2826 0.4191 0.3925 0.0242  0.0487  -0.0289 182 GLU A N   
1341 C  CA  . GLU A 182 ? 0.2863 0.4459 0.4116 0.0266  0.0489  -0.0258 182 GLU A CA  
1342 C  C   . GLU A 182 ? 0.2789 0.4498 0.4084 0.0193  0.0419  -0.0230 182 GLU A C   
1343 O  O   . GLU A 182 ? 0.3115 0.5014 0.4535 0.0228  0.0392  -0.0200 182 GLU A O   
1344 C  CB  . GLU A 182 ? 0.3319 0.5038 0.4620 0.0262  0.0567  -0.0278 182 GLU A CB  
1345 C  CG  . GLU A 182 ? 0.4572 0.6234 0.5873 0.0363  0.0639  -0.0311 182 GLU A CG  
1346 C  CD  . GLU A 182 ? 0.5045 0.6643 0.6402 0.0471  0.0624  -0.0293 182 GLU A CD  
1347 O  OE1 . GLU A 182 ? 0.5323 0.7084 0.6824 0.0546  0.0632  -0.0255 182 GLU A OE1 
1348 O  OE2 . GLU A 182 ? 0.4994 0.6385 0.6259 0.0482  0.0607  -0.0312 182 GLU A OE2 
1349 N  N   . ARG A 183 ? 0.2535 0.4136 0.3729 0.0099  0.0387  -0.0242 183 ARG A N   
1350 C  CA  . ARG A 183 ? 0.2573 0.4263 0.3799 0.0018  0.0328  -0.0234 183 ARG A CA  
1351 C  C   . ARG A 183 ? 0.2519 0.4135 0.3697 0.0034  0.0254  -0.0218 183 ARG A C   
1352 O  O   . ARG A 183 ? 0.2842 0.4560 0.4055 -0.0018 0.0201  -0.0219 183 ARG A O   
1353 C  CB  . ARG A 183 ? 0.2853 0.4469 0.4012 -0.0094 0.0349  -0.0254 183 ARG A CB  
1354 C  CG  . ARG A 183 ? 0.3421 0.5157 0.4651 -0.0130 0.0422  -0.0258 183 ARG A CG  
1355 C  CD  . ARG A 183 ? 0.4095 0.6091 0.5502 -0.0158 0.0408  -0.0258 183 ARG A CD  
1356 N  NE  . ARG A 183 ? 0.5260 0.7384 0.6753 -0.0205 0.0483  -0.0260 183 ARG A NE  
1357 C  CZ  . ARG A 183 ? 0.4940 0.7237 0.6544 -0.0145 0.0528  -0.0254 183 ARG A CZ  
1358 N  NH1 . ARG A 183 ? 0.5451 0.7808 0.7098 -0.0029 0.0510  -0.0243 183 ARG A NH1 
1359 N  NH2 . ARG A 183 ? 0.5342 0.7757 0.7024 -0.0199 0.0601  -0.0253 183 ARG A NH2 
1360 N  N   . GLU A 184 ? 0.2240 0.3691 0.3344 0.0102  0.0253  -0.0207 184 GLU A N   
1361 C  CA  . GLU A 184 ? 0.2331 0.3709 0.3385 0.0113  0.0191  -0.0184 184 GLU A CA  
1362 C  C   . GLU A 184 ? 0.2169 0.3741 0.3329 0.0172  0.0149  -0.0140 184 GLU A C   
1363 O  O   . GLU A 184 ? 0.2596 0.4313 0.3865 0.0244  0.0175  -0.0117 184 GLU A O   
1364 C  CB  . GLU A 184 ? 0.2271 0.3436 0.3243 0.0168  0.0209  -0.0182 184 GLU A CB  
1365 C  CG  . GLU A 184 ? 0.2415 0.3592 0.3465 0.0279  0.0252  -0.0161 184 GLU A CG  
1366 C  CD  . GLU A 184 ? 0.2928 0.3888 0.3917 0.0323  0.0274  -0.0169 184 GLU A CD  
1367 O  OE1 . GLU A 184 ? 0.3074 0.3889 0.3957 0.0267  0.0252  -0.0192 184 GLU A OE1 
1368 O  OE2 . GLU A 184 ? 0.3337 0.4275 0.4395 0.0415  0.0318  -0.0154 184 GLU A OE2 
1369 N  N   . ARG A 185 ? 0.2258 0.3845 0.3380 0.0148  0.0084  -0.0126 185 ARG A N   
1370 C  CA  . ARG A 185 ? 0.2076 0.3873 0.3275 0.0197  0.0032  -0.0085 185 ARG A CA  
1371 C  C   . ARG A 185 ? 0.2416 0.4108 0.3531 0.0231  -0.0008 -0.0046 185 ARG A C   
1372 O  O   . ARG A 185 ? 0.2278 0.3812 0.3286 0.0165  -0.0023 -0.0075 185 ARG A O   
1373 C  CB  . ARG A 185 ? 0.2790 0.4787 0.4039 0.0101  -0.0012 -0.0129 185 ARG A CB  
1374 C  CG  . ARG A 185 ? 0.3412 0.5540 0.4761 0.0049  0.0028  -0.0167 185 ARG A CG  
1375 C  CD  . ARG A 185 ? 0.3853 0.6189 0.5337 0.0146  0.0046  -0.0127 185 ARG A CD  
1376 N  NE  . ARG A 185 ? 0.4876 0.7090 0.6362 0.0194  0.0126  -0.0122 185 ARG A NE  
1377 C  CZ  . ARG A 185 ? 0.4328 0.6688 0.5931 0.0262  0.0170  -0.0104 185 ARG A CZ  
1378 N  NH1 . ARG A 185 ? 0.5237 0.7885 0.6976 0.0298  0.0140  -0.0082 185 ARG A NH1 
1379 N  NH2 . ARG A 185 ? 0.4972 0.7199 0.6554 0.0298  0.0246  -0.0115 185 ARG A NH2 
1380 N  N   . PRO A 186 ? 0.2292 0.4079 0.3454 0.0335  -0.0024 0.0027  186 PRO A N   
1381 C  CA  . PRO A 186 ? 0.2358 0.4063 0.3443 0.0370  -0.0056 0.0076  186 PRO A CA  
1382 C  C   . PRO A 186 ? 0.2529 0.4400 0.3583 0.0316  -0.0130 0.0060  186 PRO A C   
1383 O  O   . PRO A 186 ? 0.2710 0.4823 0.3838 0.0287  -0.0165 0.0032  186 PRO A O   
1384 C  CB  . PRO A 186 ? 0.2466 0.4234 0.3628 0.0512  -0.0033 0.0173  186 PRO A CB  
1385 C  CG  . PRO A 186 ? 0.2507 0.4530 0.3795 0.0541  -0.0034 0.0171  186 PRO A CG  
1386 C  CD  . PRO A 186 ? 0.2307 0.4285 0.3598 0.0436  -0.0006 0.0077  186 PRO A CD  
1387 N  N   . VAL A 187 ? 0.2490 0.4236 0.3439 0.0300  -0.0153 0.0070  187 VAL A N   
1388 C  CA  . VAL A 187 ? 0.2437 0.4318 0.3336 0.0261  -0.0220 0.0053  187 VAL A CA  
1389 C  C   . VAL A 187 ? 0.2630 0.4606 0.3522 0.0375  -0.0240 0.0156  187 VAL A C   
1390 O  O   . VAL A 187 ? 0.3156 0.4950 0.3992 0.0422  -0.0212 0.0215  187 VAL A O   
1391 C  CB  . VAL A 187 ? 0.2790 0.4474 0.3574 0.0169  -0.0225 -0.0005 187 VAL A CB  
1392 C  CG1 . VAL A 187 ? 0.3345 0.5166 0.4075 0.0134  -0.0289 -0.0031 187 VAL A CG1 
1393 C  CG2 . VAL A 187 ? 0.3286 0.4871 0.4075 0.0069  -0.0197 -0.0087 187 VAL A CG2 
1394 N  N   . VAL A 188 ? 0.2661 0.4931 0.3616 0.0423  -0.0286 0.0185  188 VAL A N   
1395 C  CA  . VAL A 188 ? 0.2662 0.5052 0.3594 0.0534  -0.0310 0.0292  188 VAL A CA  
1396 C  C   . VAL A 188 ? 0.3009 0.5537 0.3851 0.0478  -0.0379 0.0247  188 VAL A C   
1397 O  O   . VAL A 188 ? 0.2985 0.5628 0.3833 0.0372  -0.0420 0.0135  188 VAL A O   
1398 C  CB  . VAL A 188 ? 0.3168 0.5805 0.4217 0.0655  -0.0313 0.0377  188 VAL A CB  
1399 C  CG1 . VAL A 188 ? 0.3356 0.5820 0.4487 0.0718  -0.0232 0.0418  188 VAL A CG1 
1400 C  CG2 . VAL A 188 ? 0.3117 0.6068 0.4243 0.0598  -0.0371 0.0299  188 VAL A CG2 
1401 N  N   . VAL A 189 ? 0.2644 0.5155 0.3404 0.0546  -0.0386 0.0330  189 VAL A N   
1402 C  CA  . VAL A 189 ? 0.3299 0.5876 0.3948 0.0488  -0.0438 0.0279  189 VAL A CA  
1403 C  C   . VAL A 189 ? 0.2963 0.5634 0.3551 0.0606  -0.0447 0.0407  189 VAL A C   
1404 O  O   . VAL A 189 ? 0.3113 0.5635 0.3713 0.0700  -0.0390 0.0528  189 VAL A O   
1405 C  CB  . VAL A 189 ? 0.3103 0.5379 0.3668 0.0387  -0.0409 0.0204  189 VAL A CB  
1406 C  CG1 . VAL A 189 ? 0.4284 0.6460 0.4903 0.0280  -0.0392 0.0096  189 VAL A CG1 
1407 C  CG2 . VAL A 189 ? 0.3978 0.5993 0.4514 0.0448  -0.0346 0.0299  189 VAL A CG2 
1408 N  N   . SER A 190 ? 0.3169 0.6082 0.3688 0.0596  -0.0513 0.0378  190 SER A N   
1409 C  CA  . SER A 190 ? 0.3090 0.6102 0.3523 0.0698  -0.0522 0.0495  190 SER A CA  
1410 C  C   . SER A 190 ? 0.2712 0.5461 0.3033 0.0659  -0.0486 0.0493  190 SER A C   
1411 O  O   . SER A 190 ? 0.2746 0.5313 0.3036 0.0542  -0.0480 0.0376  190 SER A O   
1412 C  CB  . SER A 190 ? 0.4292 0.7654 0.4676 0.0694  -0.0600 0.0445  190 SER A CB  
1413 O  OG  . SER A 190 ? 0.5579 0.9139 0.6052 0.0726  -0.0612 0.0450  190 SER A OG  
1414 N  N   . LYS A 191 ? 0.2779 0.5516 0.3044 0.0762  -0.0458 0.0634  191 LYS A N   
1415 C  CA  . LYS A 191 ? 0.3062 0.5591 0.3226 0.0730  -0.0424 0.0640  191 LYS A CA  
1416 C  C   . LYS A 191 ? 0.2636 0.5279 0.2698 0.0635  -0.0482 0.0503  191 LYS A C   
1417 O  O   . LYS A 191 ? 0.2857 0.5803 0.2895 0.0637  -0.0551 0.0454  191 LYS A O   
1418 C  CB  . LYS A 191 ? 0.3548 0.6094 0.3672 0.0859  -0.0383 0.0822  191 LYS A CB  
1419 C  CG  . LYS A 191 ? 0.3730 0.6617 0.3776 0.0934  -0.0436 0.0875  191 LYS A CG  
1420 C  CD  . LYS A 191 ? 0.4529 0.7345 0.4521 0.1033  -0.0364 0.1042  191 LYS A CD  
1421 C  CE  . LYS A 191 ? 0.5237 0.8315 0.5167 0.1092  -0.0375 0.1080  191 LYS A CE  
1422 N  NZ  . LYS A 191 ? 0.6040 0.9062 0.5931 0.1190  -0.0297 0.1250  191 LYS A NZ  
1423 N  N   . GLY A 192 ? 0.2526 0.4929 0.2534 0.0551  -0.0455 0.0434  192 GLY A N   
1424 C  CA  . GLY A 192 ? 0.2602 0.5053 0.2527 0.0453  -0.0496 0.0290  192 GLY A CA  
1425 C  C   . GLY A 192 ? 0.2549 0.4955 0.2534 0.0334  -0.0518 0.0134  192 GLY A C   
1426 O  O   . GLY A 192 ? 0.2706 0.5107 0.2635 0.0246  -0.0541 0.0008  192 GLY A O   
1427 N  N   . SER A 193 ? 0.2322 0.4692 0.2420 0.0330  -0.0506 0.0140  193 SER A N   
1428 C  CA  . SER A 193 ? 0.2076 0.4370 0.2234 0.0217  -0.0511 0.0009  193 SER A CA  
1429 C  C   . SER A 193 ? 0.2103 0.4063 0.2244 0.0159  -0.0456 -0.0016 193 SER A C   
1430 O  O   . SER A 193 ? 0.2329 0.4111 0.2460 0.0211  -0.0410 0.0075  193 SER A O   
1431 C  CB  . SER A 193 ? 0.2434 0.4818 0.2719 0.0240  -0.0510 0.0032  193 SER A CB  
1432 O  OG  . SER A 193 ? 0.2947 0.5670 0.3263 0.0293  -0.0565 0.0051  193 SER A OG  
1433 N  N   . LEU A 194 ? 0.2068 0.3949 0.2214 0.0050  -0.0460 -0.0140 194 LEU A N   
1434 C  CA  . LEU A 194 ? 0.2071 0.3666 0.2201 -0.0005 -0.0414 -0.0170 194 LEU A CA  
1435 C  C   . LEU A 194 ? 0.2050 0.3587 0.2269 -0.0066 -0.0397 -0.0221 194 LEU A C   
1436 O  O   . LEU A 194 ? 0.2165 0.3820 0.2426 -0.0135 -0.0421 -0.0311 194 LEU A O   
1437 C  CB  . LEU A 194 ? 0.2333 0.3865 0.2381 -0.0072 -0.0421 -0.0261 194 LEU A CB  
1438 C  CG  . LEU A 194 ? 0.2226 0.3489 0.2260 -0.0129 -0.0378 -0.0296 194 LEU A CG  
1439 C  CD1 . LEU A 194 ? 0.2041 0.3140 0.2044 -0.0071 -0.0342 -0.0201 194 LEU A CD1 
1440 C  CD2 . LEU A 194 ? 0.2661 0.3888 0.2635 -0.0195 -0.0384 -0.0398 194 LEU A CD2 
1441 N  N   . LEU A 195 ? 0.2015 0.3380 0.2265 -0.0043 -0.0352 -0.0167 195 LEU A N   
1442 C  CA  . LEU A 195 ? 0.2078 0.3359 0.2391 -0.0100 -0.0325 -0.0212 195 LEU A CA  
1443 C  C   . LEU A 195 ? 0.2032 0.3097 0.2288 -0.0166 -0.0298 -0.0262 195 LEU A C   
1444 O  O   . LEU A 195 ? 0.2262 0.3173 0.2462 -0.0138 -0.0278 -0.0223 195 LEU A O   
1445 C  CB  . LEU A 195 ? 0.2218 0.3437 0.2589 -0.0039 -0.0288 -0.0140 195 LEU A CB  
1446 C  CG  . LEU A 195 ? 0.2327 0.3464 0.2750 -0.0091 -0.0253 -0.0182 195 LEU A CG  
1447 C  CD1 . LEU A 195 ? 0.2153 0.3487 0.2659 -0.0137 -0.0273 -0.0234 195 LEU A CD1 
1448 C  CD2 . LEU A 195 ? 0.2431 0.3478 0.2891 -0.0027 -0.0210 -0.0122 195 LEU A CD2 
1449 N  N   . LEU A 196 ? 0.1917 0.2976 0.2194 -0.0251 -0.0296 -0.0345 196 LEU A N   
1450 C  CA  . LEU A 196 ? 0.1899 0.2754 0.2136 -0.0306 -0.0262 -0.0381 196 LEU A CA  
1451 C  C   . LEU A 196 ? 0.2099 0.2890 0.2395 -0.0335 -0.0222 -0.0380 196 LEU A C   
1452 O  O   . LEU A 196 ? 0.1964 0.2888 0.2343 -0.0358 -0.0225 -0.0399 196 LEU A O   
1453 C  CB  . LEU A 196 ? 0.2310 0.3187 0.2534 -0.0381 -0.0274 -0.0474 196 LEU A CB  
1454 C  CG  . LEU A 196 ? 0.2256 0.3171 0.2400 -0.0356 -0.0304 -0.0488 196 LEU A CG  
1455 C  CD1 . LEU A 196 ? 0.2991 0.3964 0.3138 -0.0434 -0.0317 -0.0601 196 LEU A CD1 
1456 C  CD2 . LEU A 196 ? 0.2555 0.3282 0.2622 -0.0322 -0.0279 -0.0443 196 LEU A CD2 
1457 N  N   . PHE A 197 ? 0.2033 0.2638 0.2285 -0.0333 -0.0187 -0.0357 197 PHE A N   
1458 C  CA  . PHE A 197 ? 0.2039 0.2586 0.2328 -0.0358 -0.0145 -0.0354 197 PHE A CA  
1459 C  C   . PHE A 197 ? 0.2232 0.2592 0.2458 -0.0380 -0.0112 -0.0352 197 PHE A C   
1460 O  O   . PHE A 197 ? 0.2174 0.2443 0.2332 -0.0356 -0.0121 -0.0340 197 PHE A O   
1461 C  CB  . PHE A 197 ? 0.2027 0.2617 0.2356 -0.0299 -0.0132 -0.0306 197 PHE A CB  
1462 C  CG  . PHE A 197 ? 0.2318 0.2807 0.2597 -0.0235 -0.0129 -0.0259 197 PHE A CG  
1463 C  CD1 . PHE A 197 ? 0.2032 0.2383 0.2270 -0.0234 -0.0097 -0.0252 197 PHE A CD1 
1464 C  CD2 . PHE A 197 ? 0.2326 0.2874 0.2608 -0.0176 -0.0153 -0.0220 197 PHE A CD2 
1465 C  CE1 . PHE A 197 ? 0.2265 0.2537 0.2474 -0.0185 -0.0093 -0.0224 197 PHE A CE1 
1466 C  CE2 . PHE A 197 ? 0.2329 0.2778 0.2586 -0.0126 -0.0140 -0.0179 197 PHE A CE2 
1467 C  CZ  . PHE A 197 ? 0.2295 0.2607 0.2521 -0.0136 -0.0111 -0.0189 197 PHE A CZ  
1468 N  N   . VAL A 198 ? 0.2228 0.2544 0.2478 -0.0420 -0.0072 -0.0358 198 VAL A N   
1469 C  CA  . VAL A 198 ? 0.2433 0.2589 0.2622 -0.0427 -0.0037 -0.0341 198 VAL A CA  
1470 C  C   . VAL A 198 ? 0.2286 0.2400 0.2437 -0.0373 -0.0025 -0.0298 198 VAL A C   
1471 O  O   . VAL A 198 ? 0.2385 0.2575 0.2577 -0.0348 -0.0020 -0.0287 198 VAL A O   
1472 C  CB  . VAL A 198 ? 0.2452 0.2565 0.2676 -0.0493 0.0011  -0.0356 198 VAL A CB  
1473 C  CG1 . VAL A 198 ? 0.2829 0.2975 0.3099 -0.0555 0.0001  -0.0417 198 VAL A CG1 
1474 C  CG2 . VAL A 198 ? 0.2317 0.2521 0.2610 -0.0505 0.0041  -0.0344 198 VAL A CG2 
1475 N  N   . GLY A 199 ? 0.2101 0.2100 0.2177 -0.0353 -0.0020 -0.0279 199 GLY A N   
1476 C  CA  . GLY A 199 ? 0.2280 0.2250 0.2318 -0.0308 -0.0015 -0.0255 199 GLY A CA  
1477 C  C   . GLY A 199 ? 0.2232 0.2225 0.2280 -0.0309 0.0024  -0.0246 199 GLY A C   
1478 O  O   . GLY A 199 ? 0.2421 0.2435 0.2466 -0.0273 0.0028  -0.0246 199 GLY A O   
1479 N  N   . ASP A 200 ? 0.2311 0.2302 0.2378 -0.0351 0.0059  -0.0241 200 ASP A N   
1480 C  CA  . ASP A 200 ? 0.2258 0.2279 0.2330 -0.0352 0.0105  -0.0224 200 ASP A CA  
1481 C  C   . ASP A 200 ? 0.2084 0.2229 0.2246 -0.0358 0.0112  -0.0241 200 ASP A C   
1482 O  O   . ASP A 200 ? 0.2216 0.2404 0.2394 -0.0358 0.0156  -0.0230 200 ASP A O   
1483 C  CB  . ASP A 200 ? 0.2337 0.2295 0.2393 -0.0391 0.0153  -0.0196 200 ASP A CB  
1484 C  CG  . ASP A 200 ? 0.2433 0.2394 0.2564 -0.0455 0.0160  -0.0219 200 ASP A CG  
1485 O  OD1 . ASP A 200 ? 0.2601 0.2502 0.2719 -0.0465 0.0133  -0.0238 200 ASP A OD1 
1486 O  OD2 . ASP A 200 ? 0.2560 0.2596 0.2771 -0.0496 0.0191  -0.0227 200 ASP A OD2 
1487 N  N   . ILE A 201 ? 0.2235 0.2454 0.2458 -0.0355 0.0073  -0.0263 201 ILE A N   
1488 C  CA  . ILE A 201 ? 0.1828 0.2183 0.2139 -0.0340 0.0076  -0.0270 201 ILE A CA  
1489 C  C   . ILE A 201 ? 0.2097 0.2447 0.2391 -0.0274 0.0085  -0.0262 201 ILE A C   
1490 O  O   . ILE A 201 ? 0.2186 0.2456 0.2423 -0.0239 0.0065  -0.0260 201 ILE A O   
1491 C  CB  . ILE A 201 ? 0.1848 0.2305 0.2222 -0.0344 0.0029  -0.0287 201 ILE A CB  
1492 C  CG1 . ILE A 201 ? 0.2141 0.2769 0.2626 -0.0355 0.0039  -0.0296 201 ILE A CG1 
1493 C  CG2 . ILE A 201 ? 0.2228 0.2673 0.2577 -0.0278 -0.0007 -0.0271 201 ILE A CG2 
1494 C  CD1 . ILE A 201 ? 0.2418 0.3195 0.2967 -0.0344 -0.0013 -0.0309 201 ILE A CD1 
1495 N  N   . VAL A 202 ? 0.1907 0.2349 0.2261 -0.0259 0.0118  -0.0263 202 VAL A N   
1496 C  CA  . VAL A 202 ? 0.1893 0.2342 0.2254 -0.0194 0.0134  -0.0268 202 VAL A CA  
1497 C  C   . VAL A 202 ? 0.2062 0.2584 0.2499 -0.0150 0.0103  -0.0258 202 VAL A C   
1498 O  O   . VAL A 202 ? 0.2089 0.2743 0.2608 -0.0162 0.0090  -0.0252 202 VAL A O   
1499 C  CB  . VAL A 202 ? 0.2173 0.2695 0.2567 -0.0191 0.0191  -0.0272 202 VAL A CB  
1500 C  CG1 . VAL A 202 ? 0.2534 0.3064 0.2946 -0.0120 0.0213  -0.0289 202 VAL A CG1 
1501 C  CG2 . VAL A 202 ? 0.2408 0.2867 0.2717 -0.0227 0.0227  -0.0265 202 VAL A CG2 
1502 N  N   . HIS A 203 ? 0.2084 0.2530 0.2499 -0.0099 0.0091  -0.0254 203 HIS A N   
1503 C  CA  . HIS A 203 ? 0.1954 0.2450 0.2429 -0.0050 0.0064  -0.0225 203 HIS A CA  
1504 C  C   . HIS A 203 ? 0.2187 0.2575 0.2652 0.0006  0.0082  -0.0224 203 HIS A C   
1505 O  O   . HIS A 203 ? 0.2278 0.2562 0.2685 -0.0004 0.0103  -0.0258 203 HIS A O   
1506 C  CB  . HIS A 203 ? 0.1860 0.2355 0.2302 -0.0080 0.0014  -0.0212 203 HIS A CB  
1507 C  CG  . HIS A 203 ? 0.2040 0.2388 0.2394 -0.0093 0.0003  -0.0217 203 HIS A CG  
1508 N  ND1 . HIS A 203 ? 0.1998 0.2268 0.2280 -0.0142 0.0010  -0.0240 203 HIS A ND1 
1509 C  CD2 . HIS A 203 ? 0.2418 0.2690 0.2753 -0.0061 -0.0008 -0.0199 203 HIS A CD2 
1510 C  CE1 . HIS A 203 ? 0.2261 0.2429 0.2484 -0.0137 -0.0004 -0.0240 203 HIS A CE1 
1511 N  NE2 . HIS A 203 ? 0.2372 0.2537 0.2630 -0.0094 -0.0013 -0.0219 203 HIS A NE2 
1512 N  N   . ARG A 204 ? 0.2128 0.2543 0.2653 0.0065  0.0074  -0.0184 204 ARG A N   
1513 C  CA  . ARG A 204 ? 0.2185 0.2479 0.2719 0.0113  0.0098  -0.0178 204 ARG A CA  
1514 C  C   . ARG A 204 ? 0.2409 0.2737 0.2994 0.0169  0.0082  -0.0108 204 ARG A C   
1515 O  O   . ARG A 204 ? 0.2382 0.2859 0.3011 0.0190  0.0058  -0.0069 204 ARG A O   
1516 C  CB  . ARG A 204 ? 0.2438 0.2710 0.3023 0.0157  0.0156  -0.0208 204 ARG A CB  
1517 C  CG  . ARG A 204 ? 0.2286 0.2691 0.2976 0.0222  0.0174  -0.0170 204 ARG A CG  
1518 C  CD  . ARG A 204 ? 0.2496 0.2864 0.3234 0.0271  0.0239  -0.0208 204 ARG A CD  
1519 N  NE  . ARG A 204 ? 0.2593 0.3099 0.3441 0.0342  0.0262  -0.0168 204 ARG A NE  
1520 C  CZ  . ARG A 204 ? 0.2803 0.3301 0.3735 0.0431  0.0282  -0.0111 204 ARG A CZ  
1521 N  NH1 . ARG A 204 ? 0.2906 0.3257 0.3830 0.0453  0.0288  -0.0086 204 ARG A NH1 
1522 N  NH2 . ARG A 204 ? 0.3122 0.3769 0.4156 0.0502  0.0301  -0.0072 204 ARG A NH2 
1523 N  N   . GLY A 205 ? 0.2466 0.2664 0.3049 0.0192  0.0098  -0.0092 205 GLY A N   
1524 C  CA  . GLY A 205 ? 0.2528 0.2734 0.3179 0.0269  0.0112  -0.0014 205 GLY A CA  
1525 C  C   . GLY A 205 ? 0.2948 0.3147 0.3694 0.0343  0.0168  -0.0005 205 GLY A C   
1526 O  O   . GLY A 205 ? 0.2861 0.3027 0.3615 0.0333  0.0202  -0.0071 205 GLY A O   
1527 N  N   . SER A 206 ? 0.2512 0.2751 0.3331 0.0428  0.0183  0.0083  206 SER A N   
1528 C  CA  . SER A 206 ? 0.2826 0.3069 0.3749 0.0516  0.0241  0.0106  206 SER A CA  
1529 C  C   . SER A 206 ? 0.2708 0.2825 0.3696 0.0594  0.0291  0.0184  206 SER A C   
1530 O  O   . SER A 206 ? 0.2968 0.3038 0.3924 0.0586  0.0275  0.0239  206 SER A O   
1531 C  CB  . SER A 206 ? 0.2733 0.3208 0.3711 0.0565  0.0217  0.0148  206 SER A CB  
1532 O  OG  . SER A 206 ? 0.2769 0.3373 0.3758 0.0614  0.0178  0.0247  206 SER A OG  
1533 N  N   . ALA A 207 ? 0.3147 0.3206 0.4234 0.0672  0.0360  0.0191  207 ALA A N   
1534 C  CA  . ALA A 207 ? 0.3213 0.3135 0.4385 0.0755  0.0425  0.0272  207 ALA A CA  
1535 C  C   . ALA A 207 ? 0.2789 0.2866 0.3991 0.0846  0.0402  0.0420  207 ALA A C   
1536 O  O   . ALA A 207 ? 0.2972 0.3274 0.4182 0.0880  0.0358  0.0450  207 ALA A O   
1537 C  CB  . ALA A 207 ? 0.3825 0.3651 0.5100 0.0823  0.0510  0.0237  207 ALA A CB  
1538 N  N   . TYR A 208 ? 0.2970 0.2938 0.4190 0.0883  0.0432  0.0512  208 TYR A N   
1539 C  CA  . TYR A 208 ? 0.2744 0.2849 0.3995 0.0990  0.0425  0.0670  208 TYR A CA  
1540 C  C   . TYR A 208 ? 0.2933 0.3005 0.4319 0.1124  0.0505  0.0744  208 TYR A C   
1541 O  O   . TYR A 208 ? 0.3067 0.2903 0.4531 0.1156  0.0596  0.0756  208 TYR A O   
1542 C  CB  . TYR A 208 ? 0.2475 0.2458 0.3693 0.0978  0.0441  0.0744  208 TYR A CB  
1543 C  CG  . TYR A 208 ? 0.2516 0.2665 0.3720 0.1069  0.0418  0.0905  208 TYR A CG  
1544 C  CD1 . TYR A 208 ? 0.2735 0.2901 0.4038 0.1214  0.0478  0.1049  208 TYR A CD1 
1545 C  CD2 . TYR A 208 ? 0.2631 0.2918 0.3719 0.1015  0.0341  0.0916  208 TYR A CD2 
1546 C  CE1 . TYR A 208 ? 0.3126 0.3465 0.4405 0.1307  0.0457  0.1207  208 TYR A CE1 
1547 C  CE2 . TYR A 208 ? 0.2756 0.3215 0.3818 0.1101  0.0319  0.1058  208 TYR A CE2 
1548 C  CZ  . TYR A 208 ? 0.3006 0.3498 0.4159 0.1246  0.0375  0.1206  208 TYR A CZ  
1549 O  OH  . TYR A 208 ? 0.3452 0.4137 0.4568 0.1341  0.0352  0.1357  208 TYR A OH  
1550 N  N   . HIS A 209 ? 0.2613 0.2923 0.4040 0.1203  0.0476  0.0788  209 HIS A N   
1551 C  CA  . HIS A 209 ? 0.2721 0.3014 0.4283 0.1337  0.0553  0.0851  209 HIS A CA  
1552 C  C   . HIS A 209 ? 0.2844 0.3096 0.4472 0.1470  0.0608  0.1033  209 HIS A C   
1553 O  O   . HIS A 209 ? 0.3125 0.3214 0.4854 0.1553  0.0702  0.1076  209 HIS A O   
1554 C  CB  . HIS A 209 ? 0.2611 0.3203 0.4209 0.1387  0.0505  0.0854  209 HIS A CB  
1555 C  CG  . HIS A 209 ? 0.2562 0.3188 0.4135 0.1287  0.0482  0.0696  209 HIS A CG  
1556 N  ND1 . HIS A 209 ? 0.2824 0.3691 0.4452 0.1320  0.0458  0.0679  209 HIS A ND1 
1557 C  CD2 . HIS A 209 ? 0.3054 0.3520 0.4553 0.1159  0.0483  0.0555  209 HIS A CD2 
1558 C  CE1 . HIS A 209 ? 0.2875 0.3716 0.4461 0.1214  0.0450  0.0539  209 HIS A CE1 
1559 N  NE2 . HIS A 209 ? 0.2975 0.3577 0.4479 0.1121  0.0463  0.0465  209 HIS A NE2 
1560 N  N   . GLY A 210 ? 0.2810 0.3217 0.4364 0.1482  0.0547  0.1135  210 GLY A N   
1561 C  CA  . GLY A 210 ? 0.2983 0.3388 0.4553 0.1585  0.0586  0.1305  210 GLY A CA  
1562 C  C   . GLY A 210 ? 0.3143 0.3211 0.4736 0.1557  0.0684  0.1322  210 GLY A C   
1563 O  O   . GLY A 210 ? 0.3171 0.3036 0.4760 0.1465  0.0704  0.1227  210 GLY A O   
1564 N  N   . HIS A 211 ? 0.3531 0.3557 0.5153 0.1635  0.0746  0.1446  211 HIS A N   
1565 C  CA  . HIS A 211 ? 0.3767 0.3491 0.5437 0.1614  0.0852  0.1470  211 HIS A CA  
1566 C  C   . HIS A 211 ? 0.3548 0.3234 0.5145 0.1565  0.0847  0.1538  211 HIS A C   
1567 O  O   . HIS A 211 ? 0.4068 0.3521 0.5682 0.1475  0.0892  0.1474  211 HIS A O   
1568 C  CB  . HIS A 211 ? 0.3787 0.3499 0.5529 0.1726  0.0927  0.1585  211 HIS A CB  
1569 C  CG  . HIS A 211 ? 0.4267 0.3667 0.6091 0.1708  0.1049  0.1592  211 HIS A CG  
1570 N  ND1 . HIS A 211 ? 0.4653 0.3799 0.6538 0.1623  0.1101  0.1440  211 HIS A ND1 
1571 C  CD2 . HIS A 211 ? 0.4274 0.3590 0.6135 0.1762  0.1131  0.1729  211 HIS A CD2 
1572 C  CE1 . HIS A 211 ? 0.4614 0.3534 0.6574 0.1619  0.1207  0.1476  211 HIS A CE1 
1573 N  NE2 . HIS A 211 ? 0.5013 0.4025 0.6966 0.1704  0.1231  0.1655  211 HIS A NE2 
1574 N  N   . LEU A 212 ? 0.3658 0.3589 0.5171 0.1617  0.0788  0.1657  212 LEU A N   
1575 C  CA  . LEU A 212 ? 0.3534 0.3468 0.4969 0.1584  0.0785  0.1734  212 LEU A CA  
1576 C  C   . LEU A 212 ? 0.3634 0.3764 0.4955 0.1528  0.0669  0.1682  212 LEU A C   
1577 O  O   . LEU A 212 ? 0.4078 0.4387 0.5382 0.1527  0.0588  0.1608  212 LEU A O   
1578 C  CB  . LEU A 212 ? 0.3834 0.3903 0.5248 0.1688  0.0817  0.1911  212 LEU A CB  
1579 C  CG  . LEU A 212 ? 0.3984 0.3869 0.5513 0.1755  0.0940  0.1987  212 LEU A CG  
1580 C  CD1 . LEU A 212 ? 0.4280 0.4328 0.5783 0.1865  0.0970  0.2171  212 LEU A CD1 
1581 C  CD2 . LEU A 212 ? 0.4743 0.4290 0.6348 0.1668  0.1037  0.1933  212 LEU A CD2 
1582 N  N   . GLY A 213 ? 0.3671 0.3771 0.4921 0.1479  0.0666  0.1719  213 GLY A N   
1583 C  CA  . GLY A 213 ? 0.3467 0.3753 0.4600 0.1430  0.0562  0.1680  213 GLY A CA  
1584 C  C   . GLY A 213 ? 0.3646 0.3787 0.4780 0.1313  0.0535  0.1526  213 GLY A C   
1585 O  O   . GLY A 213 ? 0.3668 0.3570 0.4886 0.1260  0.0593  0.1432  213 GLY A O   
1586 N  N   . ARG A 214 ? 0.3236 0.3538 0.4238 0.1227  0.0440  0.1450  214 ARG A N   
1587 C  CA  . ARG A 214 ? 0.2966 0.3169 0.3919 0.1074  0.0399  0.1265  214 ARG A CA  
1588 C  C   . ARG A 214 ? 0.3011 0.3467 0.3842 0.1020  0.0284  0.1184  214 ARG A C   
1589 O  O   . ARG A 214 ? 0.3423 0.4106 0.4187 0.1077  0.0239  0.1268  214 ARG A O   
1590 C  CB  . ARG A 214 ? 0.3201 0.3190 0.4146 0.0993  0.0448  0.1252  214 ARG A CB  
1591 C  CG  . ARG A 214 ? 0.3703 0.3815 0.4537 0.0981  0.0414  0.1316  214 ARG A CG  
1592 C  CD  . ARG A 214 ? 0.4017 0.4175 0.4874 0.1109  0.0474  0.1523  214 ARG A CD  
1593 N  NE  . ARG A 214 ? 0.3964 0.4223 0.4713 0.1095  0.0455  0.1583  214 ARG A NE  
1594 C  CZ  . ARG A 214 ? 0.4616 0.5154 0.5255 0.1154  0.0389  0.1646  214 ARG A CZ  
1595 N  NH1 . ARG A 214 ? 0.4741 0.5499 0.5370 0.1224  0.0330  0.1655  214 ARG A NH1 
1596 N  NH2 . ARG A 214 ? 0.3966 0.4579 0.4508 0.1143  0.0385  0.1699  214 ARG A NH2 
1597 N  N   . ARG A 215 ? 0.2588 0.3011 0.3395 0.0912  0.0241  0.1021  215 ARG A N   
1598 C  CA  . ARG A 215 ? 0.2554 0.3159 0.3254 0.0836  0.0145  0.0926  215 ARG A CA  
1599 C  C   . ARG A 215 ? 0.2934 0.3453 0.3547 0.0749  0.0135  0.0887  215 ARG A C   
1600 O  O   . ARG A 215 ? 0.2912 0.3211 0.3553 0.0691  0.0181  0.0842  215 ARG A O   
1601 C  CB  . ARG A 215 ? 0.2538 0.3137 0.3255 0.0763  0.0114  0.0783  215 ARG A CB  
1602 C  CG  . ARG A 215 ? 0.2547 0.3339 0.3177 0.0693  0.0025  0.0694  215 ARG A CG  
1603 C  CD  . ARG A 215 ? 0.2398 0.3150 0.3039 0.0607  0.0007  0.0558  215 ARG A CD  
1604 N  NE  . ARG A 215 ? 0.2568 0.3113 0.3169 0.0516  0.0024  0.0475  215 ARG A NE  
1605 C  CZ  . ARG A 215 ? 0.2610 0.3111 0.3191 0.0432  0.0007  0.0362  215 ARG A CZ  
1606 N  NH1 . ARG A 215 ? 0.2379 0.3009 0.2980 0.0420  -0.0020 0.0314  215 ARG A NH1 
1607 N  NH2 . ARG A 215 ? 0.3066 0.3399 0.3607 0.0362  0.0020  0.0300  215 ARG A NH2 
1608 N  N   . LEU A 216 ? 0.2338 0.3040 0.2848 0.0740  0.0074  0.0896  216 LEU A N   
1609 C  CA  . LEU A 216 ? 0.2323 0.2975 0.2745 0.0665  0.0061  0.0854  216 LEU A CA  
1610 C  C   . LEU A 216 ? 0.2225 0.2969 0.2569 0.0572  -0.0016 0.0714  216 LEU A C   
1611 O  O   . LEU A 216 ? 0.2327 0.3281 0.2643 0.0587  -0.0074 0.0692  216 LEU A O   
1612 C  CB  . LEU A 216 ? 0.2641 0.3429 0.2999 0.0734  0.0063  0.0978  216 LEU A CB  
1613 C  CG  . LEU A 216 ? 0.3331 0.4045 0.3756 0.0836  0.0146  0.1148  216 LEU A CG  
1614 C  CD1 . LEU A 216 ? 0.3351 0.4256 0.3686 0.0909  0.0136  0.1269  216 LEU A CD1 
1615 C  CD2 . LEU A 216 ? 0.3360 0.3791 0.3852 0.0783  0.0225  0.1140  216 LEU A CD2 
1616 N  N   . ALA A 217 ? 0.1986 0.2583 0.2301 0.0479  -0.0015 0.0620  217 ALA A N   
1617 C  CA  . ALA A 217 ? 0.2015 0.2674 0.2264 0.0396  -0.0076 0.0496  217 ALA A CA  
1618 C  C   . ALA A 217 ? 0.2038 0.2580 0.2231 0.0325  -0.0072 0.0441  217 ALA A C   
1619 O  O   . ALA A 217 ? 0.2260 0.2638 0.2489 0.0311  -0.0024 0.0458  217 ALA A O   
1620 C  CB  . ALA A 217 ? 0.2049 0.2667 0.2349 0.0356  -0.0085 0.0410  217 ALA A CB  
1621 N  N   . LEU A 218 ? 0.2044 0.2676 0.2157 0.0276  -0.0122 0.0366  218 LEU A N   
1622 C  CA  . LEU A 218 ? 0.2085 0.2623 0.2145 0.0208  -0.0125 0.0297  218 LEU A CA  
1623 C  C   . LEU A 218 ? 0.2174 0.2662 0.2235 0.0138  -0.0149 0.0187  218 LEU A C   
1624 O  O   . LEU A 218 ? 0.2217 0.2816 0.2275 0.0125  -0.0184 0.0142  218 LEU A O   
1625 C  CB  . LEU A 218 ? 0.2374 0.3045 0.2342 0.0213  -0.0153 0.0296  218 LEU A CB  
1626 C  CG  . LEU A 218 ? 0.2478 0.3083 0.2386 0.0148  -0.0163 0.0208  218 LEU A CG  
1627 C  CD1 . LEU A 218 ? 0.2944 0.3392 0.2879 0.0137  -0.0117 0.0238  218 LEU A CD1 
1628 C  CD2 . LEU A 218 ? 0.3454 0.4210 0.3271 0.0158  -0.0189 0.0193  218 LEU A CD2 
1629 N  N   . PHE A 219 ? 0.1928 0.2260 0.2001 0.0094  -0.0128 0.0147  219 PHE A N   
1630 C  CA  . PHE A 219 ? 0.1967 0.2239 0.2040 0.0038  -0.0141 0.0063  219 PHE A CA  
1631 C  C   . PHE A 219 ? 0.2051 0.2271 0.2063 -0.0010 -0.0151 0.0009  219 PHE A C   
1632 O  O   . PHE A 219 ? 0.2147 0.2327 0.2141 -0.0003 -0.0136 0.0035  219 PHE A O   
1633 C  CB  . PHE A 219 ? 0.2030 0.2175 0.2163 0.0033  -0.0107 0.0059  219 PHE A CB  
1634 C  CG  . PHE A 219 ? 0.2259 0.2423 0.2463 0.0083  -0.0085 0.0104  219 PHE A CG  
1635 C  CD1 . PHE A 219 ? 0.2433 0.2602 0.2677 0.0143  -0.0056 0.0192  219 PHE A CD1 
1636 C  CD2 . PHE A 219 ? 0.2622 0.2794 0.2859 0.0074  -0.0085 0.0064  219 PHE A CD2 
1637 C  CE1 . PHE A 219 ? 0.2924 0.3098 0.3243 0.0200  -0.0028 0.0241  219 PHE A CE1 
1638 C  CE2 . PHE A 219 ? 0.3049 0.3238 0.3360 0.0128  -0.0059 0.0104  219 PHE A CE2 
1639 C  CZ  . PHE A 219 ? 0.2975 0.3160 0.3328 0.0193  -0.0030 0.0192  219 PHE A CZ  
1640 N  N   . PHE A 220 ? 0.2079 0.2295 0.2068 -0.0055 -0.0169 -0.0061 220 PHE A N   
1641 C  CA  . PHE A 220 ? 0.2131 0.2273 0.2073 -0.0092 -0.0170 -0.0107 220 PHE A CA  
1642 C  C   . PHE A 220 ? 0.2226 0.2325 0.2170 -0.0135 -0.0171 -0.0162 220 PHE A C   
1643 O  O   . PHE A 220 ? 0.2157 0.2309 0.2133 -0.0144 -0.0177 -0.0174 220 PHE A O   
1644 C  CB  . PHE A 220 ? 0.2148 0.2359 0.2033 -0.0091 -0.0184 -0.0123 220 PHE A CB  
1645 C  CG  . PHE A 220 ? 0.2286 0.2612 0.2160 -0.0106 -0.0211 -0.0165 220 PHE A CG  
1646 C  CD1 . PHE A 220 ? 0.2535 0.2835 0.2402 -0.0159 -0.0216 -0.0240 220 PHE A CD1 
1647 C  CD2 . PHE A 220 ? 0.2412 0.2884 0.2291 -0.0068 -0.0229 -0.0127 220 PHE A CD2 
1648 C  CE1 . PHE A 220 ? 0.2832 0.3249 0.2706 -0.0185 -0.0240 -0.0293 220 PHE A CE1 
1649 C  CE2 . PHE A 220 ? 0.2748 0.3360 0.2623 -0.0086 -0.0260 -0.0176 220 PHE A CE2 
1650 C  CZ  . PHE A 220 ? 0.2699 0.3283 0.2576 -0.0151 -0.0266 -0.0267 220 PHE A CZ  
1651 N  N   . ASN A 221 ? 0.2229 0.2239 0.2143 -0.0157 -0.0163 -0.0187 221 ASN A N   
1652 C  CA  . ASN A 221 ? 0.2136 0.2100 0.2043 -0.0193 -0.0156 -0.0227 221 ASN A CA  
1653 C  C   . ASN A 221 ? 0.2148 0.2043 0.2011 -0.0205 -0.0149 -0.0249 221 ASN A C   
1654 O  O   . ASN A 221 ? 0.2211 0.2087 0.2055 -0.0183 -0.0148 -0.0233 221 ASN A O   
1655 C  CB  . ASN A 221 ? 0.2226 0.2151 0.2160 -0.0197 -0.0141 -0.0221 221 ASN A CB  
1656 C  CG  . ASN A 221 ? 0.2671 0.2545 0.2608 -0.0176 -0.0133 -0.0201 221 ASN A CG  
1657 O  OD1 . ASN A 221 ? 0.2903 0.2791 0.2870 -0.0153 -0.0132 -0.0175 221 ASN A OD1 
1658 N  ND2 . ASN A 221 ? 0.2419 0.2236 0.2328 -0.0186 -0.0125 -0.0212 221 ASN A ND2 
1659 N  N   . ILE A 222 ? 0.2184 0.2045 0.2042 -0.0238 -0.0138 -0.0285 222 ILE A N   
1660 C  CA  . ILE A 222 ? 0.2094 0.1883 0.1920 -0.0247 -0.0123 -0.0310 222 ILE A CA  
1661 C  C   . ILE A 222 ? 0.2398 0.2100 0.2227 -0.0264 -0.0095 -0.0305 222 ILE A C   
1662 O  O   . ILE A 222 ? 0.2406 0.2124 0.2264 -0.0290 -0.0087 -0.0307 222 ILE A O   
1663 C  CB  . ILE A 222 ? 0.2364 0.2201 0.2188 -0.0274 -0.0129 -0.0368 222 ILE A CB  
1664 C  CG1 . ILE A 222 ? 0.2753 0.2694 0.2557 -0.0245 -0.0155 -0.0360 222 ILE A CG1 
1665 C  CG2 . ILE A 222 ? 0.2523 0.2259 0.2326 -0.0288 -0.0101 -0.0408 222 ILE A CG2 
1666 C  CD1 . ILE A 222 ? 0.2817 0.2854 0.2612 -0.0269 -0.0171 -0.0423 222 ILE A CD1 
1667 N  N   . HIS A 223 ? 0.2325 0.1943 0.2126 -0.0245 -0.0076 -0.0293 223 HIS A N   
1668 C  CA  . HIS A 223 ? 0.2420 0.1953 0.2215 -0.0249 -0.0043 -0.0271 223 HIS A CA  
1669 C  C   . HIS A 223 ? 0.2487 0.1925 0.2268 -0.0242 -0.0013 -0.0284 223 HIS A C   
1670 O  O   . HIS A 223 ? 0.2544 0.1990 0.2314 -0.0229 -0.0021 -0.0312 223 HIS A O   
1671 C  CB  . HIS A 223 ? 0.2430 0.1970 0.2203 -0.0214 -0.0048 -0.0222 223 HIS A CB  
1672 C  CG  . HIS A 223 ? 0.2489 0.2029 0.2238 -0.0170 -0.0060 -0.0203 223 HIS A CG  
1673 N  ND1 . HIS A 223 ? 0.2470 0.2074 0.2230 -0.0158 -0.0088 -0.0207 223 HIS A ND1 
1674 C  CD2 . HIS A 223 ? 0.2458 0.1950 0.2183 -0.0134 -0.0044 -0.0174 223 HIS A CD2 
1675 C  CE1 . HIS A 223 ? 0.2563 0.2168 0.2312 -0.0124 -0.0091 -0.0190 223 HIS A CE1 
1676 N  NE2 . HIS A 223 ? 0.2672 0.2215 0.2398 -0.0104 -0.0067 -0.0170 223 HIS A NE2 
1677 N  N   . GLY A 224 ? 0.2486 0.1832 0.2269 -0.0246 0.0030  -0.0259 224 GLY A N   
1678 C  CA  . GLY A 224 ? 0.2558 0.1789 0.2337 -0.0227 0.0071  -0.0256 224 GLY A CA  
1679 C  C   . GLY A 224 ? 0.2591 0.1808 0.2332 -0.0156 0.0072  -0.0191 224 GLY A C   
1680 O  O   . GLY A 224 ? 0.2710 0.1970 0.2430 -0.0133 0.0060  -0.0139 224 GLY A O   
1681 N  N   . ALA A 225 ? 0.2757 0.1931 0.2492 -0.0119 0.0083  -0.0200 225 ALA A N   
1682 C  CA  . ALA A 225 ? 0.2886 0.2074 0.2598 -0.0047 0.0080  -0.0141 225 ALA A CA  
1683 C  C   . ALA A 225 ? 0.3035 0.2161 0.2732 -0.0009 0.0117  -0.0064 225 ALA A C   
1684 O  O   . ALA A 225 ? 0.3165 0.2353 0.2837 0.0049  0.0100  -0.0007 225 ALA A O   
1685 C  CB  . ALA A 225 ? 0.2852 0.2001 0.2569 -0.0013 0.0097  -0.0170 225 ALA A CB  
1686 N  N   . GLN A 226 ? 0.3001 0.2019 0.2716 -0.0042 0.0167  -0.0058 226 GLN A N   
1687 C  CA  . GLN A 226 ? 0.3395 0.2358 0.3091 -0.0005 0.0210  0.0031  226 GLN A CA  
1688 C  C   . GLN A 226 ? 0.3083 0.2176 0.2738 0.0007  0.0170  0.0073  226 GLN A C   
1689 O  O   . GLN A 226 ? 0.3396 0.2506 0.3013 0.0066  0.0185  0.0155  226 GLN A O   
1690 C  CB  . GLN A 226 ? 0.3653 0.2486 0.3391 -0.0061 0.0276  0.0025  226 GLN A CB  
1691 C  CG  . GLN A 226 ? 0.4024 0.2710 0.3809 -0.0078 0.0328  -0.0027 226 GLN A CG  
1692 C  CD  . GLN A 226 ? 0.4328 0.3050 0.4145 -0.0152 0.0296  -0.0150 226 GLN A CD  
1693 O  OE1 . GLN A 226 ? 0.4028 0.2890 0.3830 -0.0176 0.0232  -0.0185 226 GLN A OE1 
1694 N  NE2 . GLN A 226 ? 0.4328 0.2925 0.4191 -0.0186 0.0346  -0.0217 226 GLN A NE2 
1695 N  N   . ALA A 227 ? 0.2882 0.2069 0.2544 -0.0044 0.0124  0.0018  227 ALA A N   
1696 C  CA  . ALA A 227 ? 0.2628 0.1934 0.2255 -0.0035 0.0088  0.0037  227 ALA A CA  
1697 C  C   . ALA A 227 ? 0.2770 0.2177 0.2381 0.0009  0.0037  0.0034  227 ALA A C   
1698 O  O   . ALA A 227 ? 0.2791 0.2276 0.2418 -0.0015 -0.0006 -0.0016 227 ALA A O   
1699 C  CB  . ALA A 227 ? 0.2787 0.2142 0.2441 -0.0099 0.0068  -0.0019 227 ALA A CB  
1700 N  N   . ARG A 228 ? 0.2803 0.2209 0.2391 0.0077  0.0049  0.0092  228 ARG A N   
1701 C  CA  . ARG A 228 ? 0.2661 0.2150 0.2255 0.0120  0.0011  0.0088  228 ARG A CA  
1702 C  C   . ARG A 228 ? 0.2897 0.2541 0.2480 0.0119  -0.0044 0.0069  228 ARG A C   
1703 O  O   . ARG A 228 ? 0.2841 0.2569 0.2450 0.0133  -0.0078 0.0048  228 ARG A O   
1704 C  CB  . ARG A 228 ? 0.3071 0.2530 0.2650 0.0202  0.0042  0.0164  228 ARG A CB  
1705 C  CG  . ARG A 228 ? 0.2667 0.2179 0.2190 0.0250  0.0051  0.0244  228 ARG A CG  
1706 C  CD  . ARG A 228 ? 0.3116 0.2657 0.2626 0.0349  0.0064  0.0325  228 ARG A CD  
1707 N  NE  . ARG A 228 ? 0.3088 0.2454 0.2626 0.0379  0.0132  0.0363  228 ARG A NE  
1708 C  CZ  . ARG A 228 ? 0.3221 0.2575 0.2768 0.0469  0.0156  0.0428  228 ARG A CZ  
1709 N  NH1 . ARG A 228 ? 0.3376 0.2905 0.2909 0.0539  0.0110  0.0464  228 ARG A NH1 
1710 N  NH2 . ARG A 228 ? 0.3801 0.2969 0.3380 0.0491  0.0229  0.0452  228 ARG A NH2 
1711 N  N   . TRP A 229 ? 0.2483 0.2169 0.2034 0.0100  -0.0048 0.0070  229 TRP A N   
1712 C  CA  . TRP A 229 ? 0.2442 0.2265 0.1987 0.0089  -0.0096 0.0030  229 TRP A CA  
1713 C  C   . TRP A 229 ? 0.2490 0.2311 0.2085 0.0026  -0.0116 -0.0044 229 TRP A C   
1714 O  O   . TRP A 229 ? 0.2721 0.2633 0.2332 0.0009  -0.0149 -0.0088 229 TRP A O   
1715 C  CB  . TRP A 229 ? 0.2537 0.2414 0.2019 0.0100  -0.0088 0.0056  229 TRP A CB  
1716 C  CG  . TRP A 229 ? 0.2462 0.2261 0.1946 0.0051  -0.0055 0.0041  229 TRP A CG  
1717 C  CD1 . TRP A 229 ? 0.2715 0.2547 0.2218 0.0003  -0.0070 -0.0022 229 TRP A CD1 
1718 C  CD2 . TRP A 229 ? 0.2562 0.2241 0.2045 0.0042  0.0001  0.0086  229 TRP A CD2 
1719 N  NE1 . TRP A 229 ? 0.2641 0.2399 0.2153 -0.0029 -0.0031 -0.0015 229 TRP A NE1 
1720 C  CE2 . TRP A 229 ? 0.2662 0.2329 0.2165 -0.0013 0.0012  0.0047  229 TRP A CE2 
1721 C  CE3 . TRP A 229 ? 0.2849 0.2427 0.2327 0.0074  0.0048  0.0154  229 TRP A CE3 
1722 C  CZ2 . TRP A 229 ? 0.2595 0.2171 0.2117 -0.0044 0.0064  0.0069  229 TRP A CZ2 
1723 C  CZ3 . TRP A 229 ? 0.2815 0.2279 0.2312 0.0039  0.0105  0.0174  229 TRP A CZ3 
1724 C  CH2 . TRP A 229 ? 0.2732 0.2205 0.2252 -0.0023 0.0110  0.0130  229 TRP A CH2 
1725 N  N   . THR A 230 ? 0.2381 0.2104 0.2005 -0.0007 -0.0095 -0.0058 230 THR A N   
1726 C  CA  . THR A 230 ? 0.2460 0.2186 0.2130 -0.0054 -0.0110 -0.0111 230 THR A CA  
1727 C  C   . THR A 230 ? 0.2831 0.2581 0.2539 -0.0048 -0.0128 -0.0125 230 THR A C   
1728 O  O   . THR A 230 ? 0.3163 0.2881 0.2867 -0.0019 -0.0116 -0.0104 230 THR A O   
1729 C  CB  . THR A 230 ? 0.2605 0.2249 0.2286 -0.0087 -0.0083 -0.0118 230 THR A CB  
1730 O  OG1 . THR A 230 ? 0.2862 0.2480 0.2515 -0.0091 -0.0055 -0.0094 230 THR A OG1 
1731 C  CG2 . THR A 230 ? 0.2528 0.2196 0.2250 -0.0123 -0.0099 -0.0159 230 THR A CG2 
1732 N  N   . ASP A 231 ? 0.3093 0.2891 0.2842 -0.0074 -0.0148 -0.0160 231 ASP A N   
1733 C  CA  . ASP A 231 ? 0.3000 0.2827 0.2794 -0.0074 -0.0158 -0.0168 231 ASP A CA  
1734 C  C   . ASP A 231 ? 0.3178 0.2955 0.2984 -0.0091 -0.0144 -0.0173 231 ASP A C   
1735 O  O   . ASP A 231 ? 0.3266 0.3020 0.3075 -0.0115 -0.0140 -0.0183 231 ASP A O   
1736 C  CB  . ASP A 231 ? 0.3414 0.3308 0.3258 -0.0099 -0.0176 -0.0201 231 ASP A CB  
1737 C  CG  . ASP A 231 ? 0.3903 0.3874 0.3730 -0.0090 -0.0196 -0.0215 231 ASP A CG  
1738 O  OD1 . ASP A 231 ? 0.4179 0.4219 0.4007 -0.0061 -0.0210 -0.0202 231 ASP A OD1 
1739 O  OD2 . ASP A 231 ? 0.4363 0.4339 0.4173 -0.0106 -0.0197 -0.0241 231 ASP A OD2 
1740 N  N   . LYS A 232 ? 0.2882 0.2661 0.2696 -0.0074 -0.0137 -0.0165 232 LYS A N   
1741 C  CA  . LYS A 232 ? 0.3209 0.2980 0.3032 -0.0088 -0.0130 -0.0173 232 LYS A CA  
1742 C  C   . LYS A 232 ? 0.2919 0.2741 0.2795 -0.0103 -0.0136 -0.0169 232 LYS A C   
1743 O  O   . LYS A 232 ? 0.3040 0.2898 0.2952 -0.0110 -0.0145 -0.0173 232 LYS A O   
1744 C  CB  . LYS A 232 ? 0.4310 0.4065 0.4113 -0.0064 -0.0114 -0.0174 232 LYS A CB  
1745 C  CG  . LYS A 232 ? 0.4122 0.3930 0.3951 -0.0035 -0.0113 -0.0159 232 LYS A CG  
1746 C  CD  . LYS A 232 ? 0.4088 0.3867 0.3892 -0.0001 -0.0089 -0.0165 232 LYS A CD  
1747 C  CE  . LYS A 232 ? 0.3810 0.3661 0.3650 0.0032  -0.0085 -0.0146 232 LYS A CE  
1748 N  NZ  . LYS A 232 ? 0.4517 0.4443 0.4402 0.0010  -0.0088 -0.0140 232 LYS A NZ  
1749 N  N   . HIS A 233 ? 0.2474 0.2301 0.2355 -0.0110 -0.0128 -0.0161 233 HIS A N   
1750 C  CA  . HIS A 233 ? 0.2393 0.2248 0.2331 -0.0121 -0.0122 -0.0143 233 HIS A CA  
1751 C  C   . HIS A 233 ? 0.2705 0.2602 0.2688 -0.0118 -0.0114 -0.0132 233 HIS A C   
1752 O  O   . HIS A 233 ? 0.2765 0.2687 0.2731 -0.0098 -0.0106 -0.0124 233 HIS A O   
1753 C  CB  . HIS A 233 ? 0.2332 0.2203 0.2258 -0.0113 -0.0113 -0.0120 233 HIS A CB  
1754 C  CG  . HIS A 233 ? 0.2565 0.2451 0.2550 -0.0114 -0.0096 -0.0083 233 HIS A CG  
1755 N  ND1 . HIS A 233 ? 0.2770 0.2624 0.2805 -0.0129 -0.0091 -0.0086 233 HIS A ND1 
1756 C  CD2 . HIS A 233 ? 0.2493 0.2414 0.2499 -0.0101 -0.0073 -0.0038 233 HIS A CD2 
1757 C  CE1 . HIS A 233 ? 0.2916 0.2769 0.3007 -0.0124 -0.0064 -0.0043 233 HIS A CE1 
1758 N  NE2 . HIS A 233 ? 0.2359 0.2257 0.2434 -0.0108 -0.0052 -0.0008 233 HIS A NE2 
1759 N  N   . LEU A 234 ? 0.2293 0.2201 0.2343 -0.0142 -0.0112 -0.0140 234 LEU A N   
1760 C  CA  . LEU A 234 ? 0.2623 0.2586 0.2741 -0.0153 -0.0103 -0.0138 234 LEU A CA  
1761 C  C   . LEU A 234 ? 0.2640 0.2603 0.2821 -0.0166 -0.0068 -0.0100 234 LEU A C   
1762 O  O   . LEU A 234 ? 0.2804 0.2721 0.3019 -0.0180 -0.0054 -0.0092 234 LEU A O   
1763 C  CB  . LEU A 234 ? 0.2909 0.2897 0.3071 -0.0181 -0.0121 -0.0183 234 LEU A CB  
1764 C  CG  . LEU A 234 ? 0.3515 0.3579 0.3772 -0.0209 -0.0116 -0.0200 234 LEU A CG  
1765 C  CD1 . LEU A 234 ? 0.3491 0.3629 0.3737 -0.0178 -0.0121 -0.0181 234 LEU A CD1 
1766 C  CD2 . LEU A 234 ? 0.3710 0.3813 0.3998 -0.0240 -0.0141 -0.0264 234 LEU A CD2 
1767 N  N   . TRP A 235 ? 0.2385 0.2399 0.2586 -0.0155 -0.0048 -0.0071 235 TRP A N   
1768 C  CA  . TRP A 235 ? 0.2401 0.2426 0.2673 -0.0168 -0.0006 -0.0024 235 TRP A CA  
1769 C  C   . TRP A 235 ? 0.2341 0.2448 0.2670 -0.0174 0.0011  -0.0018 235 TRP A C   
1770 O  O   . TRP A 235 ? 0.2415 0.2571 0.2708 -0.0151 -0.0010 -0.0040 235 TRP A O   
1771 C  CB  . TRP A 235 ? 0.2780 0.2794 0.2994 -0.0134 0.0015  0.0033  235 TRP A CB  
1772 C  CG  . TRP A 235 ? 0.2557 0.2629 0.2696 -0.0097 0.0016  0.0044  235 TRP A CG  
1773 C  CD1 . TRP A 235 ? 0.2373 0.2508 0.2527 -0.0082 0.0053  0.0087  235 TRP A CD1 
1774 C  CD2 . TRP A 235 ? 0.2612 0.2678 0.2653 -0.0072 -0.0013 0.0008  235 TRP A CD2 
1775 N  NE1 . TRP A 235 ? 0.2784 0.2957 0.2847 -0.0045 0.0046  0.0072  235 TRP A NE1 
1776 C  CE2 . TRP A 235 ? 0.2833 0.2958 0.2832 -0.0041 0.0007  0.0021  235 TRP A CE2 
1777 C  CE3 . TRP A 235 ? 0.2695 0.2712 0.2688 -0.0075 -0.0046 -0.0035 235 TRP A CE3 
1778 C  CZ2 . TRP A 235 ? 0.2850 0.2974 0.2763 -0.0016 -0.0007 -0.0020 235 TRP A CZ2 
1779 C  CZ3 . TRP A 235 ? 0.2647 0.2660 0.2562 -0.0054 -0.0057 -0.0066 235 TRP A CZ3 
1780 C  CH2 . TRP A 235 ? 0.2915 0.2976 0.2792 -0.0026 -0.0038 -0.0064 235 TRP A CH2 
1781 N  N   . SER A 236 ? 0.2207 0.2326 0.2633 -0.0202 0.0055  0.0017  236 SER A N   
1782 C  CA  . SER A 236 ? 0.2253 0.2462 0.2758 -0.0216 0.0081  0.0028  236 SER A CA  
1783 C  C   . SER A 236 ? 0.2813 0.3041 0.3312 -0.0193 0.0136  0.0109  236 SER A C   
1784 O  O   . SER A 236 ? 0.2870 0.3041 0.3395 -0.0199 0.0173  0.0163  236 SER A O   
1785 C  CB  . SER A 236 ? 0.2951 0.3172 0.3599 -0.0284 0.0093  -0.0007 236 SER A CB  
1786 O  OG  . SER A 236 ? 0.4306 0.4547 0.4949 -0.0301 0.0039  -0.0087 236 SER A OG  
1787 N  N   . LEU A 237 ? 0.2452 0.2764 0.2916 -0.0159 0.0145  0.0122  237 LEU A N   
1788 C  CA  . LEU A 237 ? 0.2451 0.2806 0.2899 -0.0132 0.0200  0.0198  237 LEU A CA  
1789 C  C   . LEU A 237 ? 0.2638 0.3106 0.3103 -0.0112 0.0215  0.0191  237 LEU A C   
1790 O  O   . LEU A 237 ? 0.2676 0.3170 0.3109 -0.0091 0.0175  0.0135  237 LEU A O   
1791 C  CB  . LEU A 237 ? 0.2806 0.3133 0.3114 -0.0080 0.0189  0.0220  237 LEU A CB  
1792 C  CG  . LEU A 237 ? 0.3331 0.3692 0.3612 -0.0051 0.0243  0.0312  237 LEU A CG  
1793 C  CD1 . LEU A 237 ? 0.3909 0.4208 0.4297 -0.0086 0.0286  0.0376  237 LEU A CD1 
1794 C  CD2 . LEU A 237 ? 0.3241 0.3604 0.3379 -0.0003 0.0214  0.0311  237 LEU A CD2 
1795 N  N   . ARG A 238 ? 0.2371 0.2904 0.2890 -0.0113 0.0278  0.0256  238 ARG A N   
1796 C  CA  . ARG A 238 ? 0.2326 0.2981 0.2870 -0.0090 0.0308  0.0262  238 ARG A CA  
1797 C  C   . ARG A 238 ? 0.2365 0.3064 0.2853 -0.0053 0.0371  0.0344  238 ARG A C   
1798 O  O   . ARG A 238 ? 0.2486 0.3134 0.2967 -0.0060 0.0401  0.0410  238 ARG A O   
1799 C  CB  . ARG A 238 ? 0.2582 0.3313 0.3301 -0.0148 0.0330  0.0254  238 ARG A CB  
1800 C  CG  . ARG A 238 ? 0.3437 0.4160 0.4215 -0.0186 0.0267  0.0172  238 ARG A CG  
1801 C  CD  . ARG A 238 ? 0.3674 0.4496 0.4638 -0.0254 0.0288  0.0156  238 ARG A CD  
1802 N  NE  . ARG A 238 ? 0.4228 0.5007 0.5302 -0.0316 0.0355  0.0208  238 ARG A NE  
1803 C  CZ  . ARG A 238 ? 0.4130 0.4976 0.5385 -0.0393 0.0390  0.0196  238 ARG A CZ  
1804 N  NH1 . ARG A 238 ? 0.3612 0.4601 0.4961 -0.0417 0.0357  0.0131  238 ARG A NH1 
1805 N  NH2 . ARG A 238 ? 0.4693 0.5468 0.6047 -0.0447 0.0462  0.0252  238 ARG A NH2 
1806 N  N   . PRO A 239 ? 0.2413 0.3214 0.2858 -0.0006 0.0396  0.0345  239 PRO A N   
1807 C  CA  . PRO A 239 ? 0.2467 0.3333 0.2844 0.0035  0.0459  0.0421  239 PRO A CA  
1808 C  C   . PRO A 239 ? 0.2641 0.3526 0.3128 -0.0003 0.0534  0.0525  239 PRO A C   
1809 O  O   . PRO A 239 ? 0.2942 0.3845 0.3357 0.0031  0.0578  0.0608  239 PRO A O   
1810 C  CB  . PRO A 239 ? 0.2720 0.3698 0.3064 0.0084  0.0477  0.0387  239 PRO A CB  
1811 C  CG  . PRO A 239 ? 0.2696 0.3621 0.3017 0.0094  0.0407  0.0289  239 PRO A CG  
1812 C  CD  . PRO A 239 ? 0.2784 0.3641 0.3217 0.0027  0.0368  0.0275  239 PRO A CD  
1813 N  N   . ALA A 240 ? 0.2384 0.3271 0.3047 -0.0071 0.0554  0.0524  240 ALA A N   
1814 C  CA  . ALA A 240 ? 0.2716 0.3594 0.3506 -0.0118 0.0635  0.0619  240 ALA A CA  
1815 C  C   . ALA A 240 ? 0.2880 0.3618 0.3654 -0.0130 0.0638  0.0670  240 ALA A C   
1816 O  O   . ALA A 240 ? 0.3154 0.3870 0.3994 -0.0143 0.0718  0.0777  240 ALA A O   
1817 C  CB  . ALA A 240 ? 0.3018 0.3930 0.4013 -0.0203 0.0648  0.0580  240 ALA A CB  
1818 N  N   . HIS A 241 ? 0.2751 0.3396 0.3446 -0.0121 0.0561  0.0605  241 HIS A N   
1819 C  CA  . HIS A 241 ? 0.3029 0.3544 0.3740 -0.0136 0.0564  0.0642  241 HIS A CA  
1820 C  C   . HIS A 241 ? 0.3270 0.3795 0.3862 -0.0065 0.0599  0.0751  241 HIS A C   
1821 O  O   . HIS A 241 ? 0.2979 0.3590 0.3420 -0.0002 0.0574  0.0744  241 HIS A O   
1822 C  CB  . HIS A 241 ? 0.3416 0.3851 0.4071 -0.0141 0.0473  0.0541  241 HIS A CB  
1823 C  CG  . HIS A 241 ? 0.4311 0.4611 0.5013 -0.0166 0.0474  0.0556  241 HIS A CG  
1824 N  ND1 . HIS A 241 ? 0.4006 0.4260 0.4622 -0.0113 0.0481  0.0626  241 HIS A ND1 
1825 C  CD2 . HIS A 241 ? 0.4714 0.4925 0.5544 -0.0233 0.0471  0.0504  241 HIS A CD2 
1826 C  CE1 . HIS A 241 ? 0.4727 0.4859 0.5420 -0.0142 0.0486  0.0624  241 HIS A CE1 
1827 N  NE2 . HIS A 241 ? 0.5064 0.5161 0.5884 -0.0218 0.0482  0.0545  241 HIS A NE2 
1828 N  N   . PRO A 242 ? 0.3803 0.4245 0.4457 -0.0070 0.0655  0.0848  242 PRO A N   
1829 C  CA  . PRO A 242 ? 0.3950 0.4425 0.4487 0.0009  0.0686  0.0966  242 PRO A CA  
1830 C  C   . PRO A 242 ? 0.3278 0.3774 0.3644 0.0067  0.0601  0.0915  242 PRO A C   
1831 O  O   . PRO A 242 ? 0.3872 0.4470 0.4106 0.0138  0.0607  0.0976  242 PRO A O   
1832 C  CB  . PRO A 242 ? 0.4305 0.4654 0.4969 -0.0010 0.0758  0.1069  242 PRO A CB  
1833 C  CG  . PRO A 242 ? 0.4799 0.5026 0.5616 -0.0101 0.0736  0.0965  242 PRO A CG  
1834 C  CD  . PRO A 242 ? 0.4202 0.4524 0.5043 -0.0145 0.0700  0.0858  242 PRO A CD  
1835 N  N   . ASP A 243 ? 0.3341 0.3759 0.3708 0.0037  0.0524  0.0802  243 ASP A N   
1836 C  CA  . ASP A 243 ? 0.3273 0.3708 0.3498 0.0079  0.0446  0.0745  243 ASP A CA  
1837 C  C   . ASP A 243 ? 0.3070 0.3594 0.3185 0.0094  0.0396  0.0649  243 ASP A C   
1838 O  O   . ASP A 243 ? 0.3128 0.3669 0.3132 0.0119  0.0336  0.0590  243 ASP A O   
1839 C  CB  . ASP A 243 ? 0.3946 0.4256 0.4221 0.0040  0.0394  0.0672  243 ASP A CB  
1840 C  CG  . ASP A 243 ? 0.4589 0.4796 0.4958 0.0038  0.0440  0.0754  243 ASP A CG  
1841 O  OD1 . ASP A 243 ? 0.4615 0.4846 0.4998 0.0076  0.0509  0.0881  243 ASP A OD1 
1842 O  OD2 . ASP A 243 ? 0.5132 0.5234 0.5561 0.0003  0.0411  0.0694  243 ASP A OD2 
1843 N  N   . TRP A 244 ? 0.2795 0.3377 0.2947 0.0079  0.0425  0.0631  244 TRP A N   
1844 C  CA  . TRP A 244 ? 0.2883 0.3529 0.2944 0.0098  0.0385  0.0537  244 TRP A CA  
1845 C  C   . TRP A 244 ? 0.2528 0.3280 0.2430 0.0163  0.0383  0.0548  244 TRP A C   
1846 O  O   . TRP A 244 ? 0.2703 0.3464 0.2507 0.0179  0.0330  0.0455  244 TRP A O   
1847 C  CB  . TRP A 244 ? 0.2804 0.3506 0.2949 0.0078  0.0424  0.0525  244 TRP A CB  
1848 C  CG  . TRP A 244 ? 0.2847 0.3612 0.2904 0.0113  0.0398  0.0439  244 TRP A CG  
1849 C  CD1 . TRP A 244 ? 0.2793 0.3672 0.2770 0.0162  0.0436  0.0450  244 TRP A CD1 
1850 C  CD2 . TRP A 244 ? 0.2478 0.3185 0.2516 0.0105  0.0335  0.0331  244 TRP A CD2 
1851 N  NE1 . TRP A 244 ? 0.2987 0.3873 0.2908 0.0184  0.0403  0.0348  244 TRP A NE1 
1852 C  CE2 . TRP A 244 ? 0.2540 0.3318 0.2499 0.0151  0.0343  0.0282  244 TRP A CE2 
1853 C  CE3 . TRP A 244 ? 0.2689 0.3294 0.2771 0.0067  0.0280  0.0277  244 TRP A CE3 
1854 C  CZ2 . TRP A 244 ? 0.2534 0.3265 0.2464 0.0162  0.0301  0.0186  244 TRP A CZ2 
1855 C  CZ3 . TRP A 244 ? 0.2862 0.3438 0.2907 0.0079  0.0236  0.0189  244 TRP A CZ3 
1856 C  CH2 . TRP A 244 ? 0.2709 0.3340 0.2684 0.0127  0.0249  0.0149  244 TRP A CH2 
1857 N  N   . GLY A 245 ? 0.2730 0.3569 0.2607 0.0201  0.0445  0.0660  245 GLY A N   
1858 C  CA  . GLY A 245 ? 0.3029 0.4002 0.2744 0.0266  0.0443  0.0668  245 GLY A CA  
1859 C  C   . GLY A 245 ? 0.2751 0.3718 0.2365 0.0281  0.0367  0.0606  245 GLY A C   
1860 O  O   . GLY A 245 ? 0.2784 0.3823 0.2281 0.0304  0.0330  0.0515  245 GLY A O   
1861 N  N   . THR A 246 ? 0.2734 0.3617 0.2403 0.0267  0.0347  0.0648  246 THR A N   
1862 C  CA  . THR A 246 ? 0.2625 0.3514 0.2218 0.0279  0.0277  0.0592  246 THR A CA  
1863 C  C   . THR A 246 ? 0.2475 0.3297 0.2051 0.0238  0.0216  0.0441  246 THR A C   
1864 O  O   . THR A 246 ? 0.2552 0.3435 0.2027 0.0251  0.0171  0.0358  246 THR A O   
1865 C  CB  . THR A 246 ? 0.2552 0.3349 0.2229 0.0271  0.0275  0.0662  246 THR A CB  
1866 O  OG1 . THR A 246 ? 0.3124 0.3982 0.2806 0.0322  0.0336  0.0814  246 THR A OG1 
1867 C  CG2 . THR A 246 ? 0.3032 0.3842 0.2649 0.0278  0.0201  0.0598  246 THR A CG2 
1868 N  N   . PHE A 247 ? 0.2404 0.3108 0.2085 0.0190  0.0218  0.0404  247 PHE A N   
1869 C  CA  . PHE A 247 ? 0.2423 0.3057 0.2093 0.0160  0.0169  0.0281  247 PHE A CA  
1870 C  C   . PHE A 247 ? 0.2304 0.3006 0.1893 0.0184  0.0176  0.0210  247 PHE A C   
1871 O  O   . PHE A 247 ? 0.2456 0.3139 0.1980 0.0180  0.0137  0.0110  247 PHE A O   
1872 C  CB  . PHE A 247 ? 0.2471 0.2994 0.2264 0.0113  0.0170  0.0267  247 PHE A CB  
1873 C  CG  . PHE A 247 ? 0.2380 0.2833 0.2160 0.0093  0.0124  0.0162  247 PHE A CG  
1874 C  CD1 . PHE A 247 ? 0.2661 0.3045 0.2428 0.0073  0.0077  0.0121  247 PHE A CD1 
1875 C  CD2 . PHE A 247 ? 0.2567 0.3029 0.2345 0.0101  0.0134  0.0112  247 PHE A CD2 
1876 C  CE1 . PHE A 247 ? 0.2756 0.3073 0.2510 0.0057  0.0044  0.0038  247 PHE A CE1 
1877 C  CE2 . PHE A 247 ? 0.2601 0.2992 0.2367 0.0092  0.0100  0.0030  247 PHE A CE2 
1878 C  CZ  . PHE A 247 ? 0.2733 0.3048 0.2485 0.0068  0.0057  -0.0004 247 PHE A CZ  
1879 N  N   . ARG A 248 ? 0.2322 0.3097 0.1922 0.0206  0.0231  0.0257  248 ARG A N   
1880 C  CA  . ARG A 248 ? 0.2552 0.3403 0.2073 0.0238  0.0249  0.0192  248 ARG A CA  
1881 C  C   . ARG A 248 ? 0.2581 0.3524 0.1960 0.0268  0.0225  0.0143  248 ARG A C   
1882 O  O   . ARG A 248 ? 0.2687 0.3619 0.2003 0.0270  0.0203  0.0028  248 ARG A O   
1883 C  CB  . ARG A 248 ? 0.2477 0.3418 0.2033 0.0261  0.0322  0.0273  248 ARG A CB  
1884 C  CG  . ARG A 248 ? 0.2619 0.3658 0.2094 0.0305  0.0354  0.0218  248 ARG A CG  
1885 C  CD  . ARG A 248 ? 0.3024 0.4195 0.2500 0.0337  0.0430  0.0327  248 ARG A CD  
1886 N  NE  . ARG A 248 ? 0.3378 0.4630 0.2771 0.0363  0.0433  0.0409  248 ARG A NE  
1887 C  CZ  . ARG A 248 ? 0.4275 0.5588 0.3703 0.0378  0.0492  0.0550  248 ARG A CZ  
1888 N  NH1 . ARG A 248 ? 0.4450 0.5752 0.4002 0.0358  0.0555  0.0619  248 ARG A NH1 
1889 N  NH2 . ARG A 248 ? 0.3971 0.5362 0.3315 0.0415  0.0490  0.0628  248 ARG A NH2 
1890 N  N   . ASP A 249 ? 0.2610 0.3644 0.1943 0.0292  0.0227  0.0226  249 ASP A N   
1891 C  CA  . ASP A 249 ? 0.2801 0.3963 0.2000 0.0322  0.0196  0.0180  249 ASP A CA  
1892 C  C   . ASP A 249 ? 0.2742 0.3833 0.1933 0.0284  0.0127  0.0074  249 ASP A C   
1893 O  O   . ASP A 249 ? 0.2860 0.4018 0.1959 0.0285  0.0098  -0.0035 249 ASP A O   
1894 C  CB  . ASP A 249 ? 0.2852 0.4137 0.2017 0.0365  0.0213  0.0315  249 ASP A CB  
1895 C  CG  . ASP A 249 ? 0.3401 0.4784 0.2553 0.0408  0.0292  0.0422  249 ASP A CG  
1896 O  OD1 . ASP A 249 ? 0.3520 0.4902 0.2676 0.0407  0.0328  0.0375  249 ASP A OD1 
1897 O  OD2 . ASP A 249 ? 0.3744 0.5206 0.2886 0.0448  0.0323  0.0559  249 ASP A OD2 
1898 N  N   . LEU A 250 ? 0.2595 0.3556 0.1885 0.0246  0.0103  0.0099  250 LEU A N   
1899 C  CA  . LEU A 250 ? 0.2762 0.3648 0.2057 0.0206  0.0046  0.0004  250 LEU A CA  
1900 C  C   . LEU A 250 ? 0.2635 0.3444 0.1914 0.0183  0.0043  -0.0122 250 LEU A C   
1901 O  O   . LEU A 250 ? 0.2854 0.3680 0.2078 0.0166  0.0013  -0.0228 250 LEU A O   
1902 C  CB  . LEU A 250 ? 0.2539 0.3295 0.1944 0.0173  0.0032  0.0053  250 LEU A CB  
1903 C  CG  . LEU A 250 ? 0.2685 0.3364 0.2103 0.0131  -0.0019 -0.0033 250 LEU A CG  
1904 C  CD1 . LEU A 250 ? 0.2912 0.3712 0.2275 0.0140  -0.0059 -0.0046 250 LEU A CD1 
1905 C  CD2 . LEU A 250 ? 0.2633 0.3176 0.2156 0.0101  -0.0022 0.0003  250 LEU A CD2 
1906 N  N   . MET A 251 ? 0.2496 0.3227 0.1833 0.0185  0.0079  -0.0113 251 MET A N   
1907 C  CA  . MET A 251 ? 0.2543 0.3185 0.1878 0.0176  0.0083  -0.0217 251 MET A CA  
1908 C  C   . MET A 251 ? 0.2969 0.3700 0.2200 0.0201  0.0098  -0.0308 251 MET A C   
1909 O  O   . MET A 251 ? 0.2994 0.3657 0.2204 0.0184  0.0090  -0.0423 251 MET A O   
1910 C  CB  . MET A 251 ? 0.2592 0.3175 0.2009 0.0186  0.0120  -0.0175 251 MET A CB  
1911 C  CG  . MET A 251 ? 0.2786 0.3264 0.2306 0.0152  0.0098  -0.0130 251 MET A CG  
1912 S  SD  . MET A 251 ? 0.3115 0.3449 0.2645 0.0116  0.0055  -0.0214 251 MET A SD  
1913 C  CE  . MET A 251 ? 0.3491 0.3761 0.3038 0.0146  0.0088  -0.0266 251 MET A CE  
1914 N  N   . ILE A 252 ? 0.2646 0.3528 0.1813 0.0242  0.0127  -0.0261 252 ILE A N   
1915 C  CA  . ILE A 252 ? 0.2901 0.3895 0.1955 0.0269  0.0142  -0.0354 252 ILE A CA  
1916 C  C   . ILE A 252 ? 0.3098 0.4155 0.2081 0.0243  0.0090  -0.0444 252 ILE A C   
1917 O  O   . ILE A 252 ? 0.3390 0.4453 0.2315 0.0232  0.0088  -0.0583 252 ILE A O   
1918 C  CB  . ILE A 252 ? 0.2799 0.3957 0.1797 0.0324  0.0190  -0.0265 252 ILE A CB  
1919 C  CG1 . ILE A 252 ? 0.3099 0.4201 0.2185 0.0341  0.0246  -0.0201 252 ILE A CG1 
1920 C  CG2 . ILE A 252 ? 0.3326 0.4633 0.2188 0.0356  0.0202  -0.0364 252 ILE A CG2 
1921 C  CD1 . ILE A 252 ? 0.3159 0.4399 0.2235 0.0381  0.0299  -0.0074 252 ILE A CD1 
1922 N  N   . GLU A 253 ? 0.2937 0.4042 0.1933 0.0230  0.0048  -0.0373 253 GLU A N   
1923 C  CA  . GLU A 253 ? 0.3408 0.4612 0.2349 0.0207  -0.0006 -0.0449 253 GLU A CA  
1924 C  C   . GLU A 253 ? 0.3187 0.4242 0.2187 0.0141  -0.0036 -0.0562 253 GLU A C   
1925 O  O   . GLU A 253 ? 0.3692 0.4808 0.2646 0.0110  -0.0064 -0.0688 253 GLU A O   
1926 C  CB  . GLU A 253 ? 0.3695 0.4996 0.2650 0.0225  -0.0034 -0.0320 253 GLU A CB  
1927 C  CG  . GLU A 253 ? 0.4621 0.5986 0.3575 0.0192  -0.0097 -0.0373 253 GLU A CG  
1928 C  CD  . GLU A 253 ? 0.4604 0.6008 0.3606 0.0216  -0.0115 -0.0232 253 GLU A CD  
1929 O  OE1 . GLU A 253 ? 0.4545 0.6030 0.3526 0.0274  -0.0084 -0.0099 253 GLU A OE1 
1930 O  OE2 . GLU A 253 ? 0.4775 0.6121 0.3844 0.0178  -0.0153 -0.0250 253 GLU A OE2 
1931 N  N   . LEU A 254 ? 0.2934 0.3803 0.2035 0.0118  -0.0028 -0.0522 254 LEU A N   
1932 C  CA  . LEU A 254 ? 0.3150 0.3879 0.2309 0.0060  -0.0051 -0.0601 254 LEU A CA  
1933 C  C   . LEU A 254 ? 0.3344 0.3993 0.2481 0.0041  -0.0025 -0.0743 254 LEU A C   
1934 O  O   . LEU A 254 ? 0.3649 0.4288 0.2756 0.0079  0.0019  -0.0763 254 LEU A O   
1935 C  CB  . LEU A 254 ? 0.2919 0.3484 0.2178 0.0050  -0.0043 -0.0520 254 LEU A CB  
1936 C  CG  . LEU A 254 ? 0.2828 0.3419 0.2135 0.0055  -0.0063 -0.0397 254 LEU A CG  
1937 C  CD1 . LEU A 254 ? 0.2662 0.3099 0.2059 0.0044  -0.0051 -0.0342 254 LEU A CD1 
1938 C  CD2 . LEU A 254 ? 0.3137 0.3790 0.2447 0.0024  -0.0111 -0.0418 254 LEU A CD2 
1939 N  N   . GLU A 255 ? 0.3118 0.3703 0.2283 -0.0018 -0.0046 -0.0843 255 GLU A N   
1940 C  CA  . GLU A 255 ? 0.3421 0.3878 0.2593 -0.0043 -0.0012 -0.0974 255 GLU A CA  
1941 C  C   . GLU A 255 ? 0.3273 0.3510 0.2532 -0.0044 0.0019  -0.0927 255 GLU A C   
1942 O  O   . GLU A 255 ? 0.3029 0.3225 0.2341 -0.0044 0.0000  -0.0820 255 GLU A O   
1943 C  CB  . GLU A 255 ? 0.3960 0.4451 0.3136 -0.0116 -0.0042 -0.1103 255 GLU A CB  
1944 C  CG  . GLU A 255 ? 0.4914 0.5663 0.4003 -0.0114 -0.0084 -0.1151 255 GLU A CG  
1945 C  CD  . GLU A 255 ? 0.5900 0.6719 0.5012 -0.0192 -0.0125 -0.1276 255 GLU A CD  
1946 O  OE1 . GLU A 255 ? 0.5976 0.6632 0.5178 -0.0253 -0.0115 -0.1314 255 GLU A OE1 
1947 O  OE2 . GLU A 255 ? 0.6563 0.7602 0.5615 -0.0191 -0.0163 -0.1317 255 GLU A OE2 
1948 N  N   . PRO A 256 ? 0.3248 0.3344 0.2522 -0.0038 0.0069  -0.1005 256 PRO A N   
1949 C  CA  . PRO A 256 ? 0.3288 0.3188 0.2640 -0.0028 0.0098  -0.0950 256 PRO A CA  
1950 C  C   . PRO A 256 ? 0.3317 0.3138 0.2733 -0.0080 0.0071  -0.0912 256 PRO A C   
1951 O  O   . PRO A 256 ? 0.2996 0.2751 0.2457 -0.0060 0.0068  -0.0809 256 PRO A O   
1952 C  CB  . PRO A 256 ? 0.3380 0.3147 0.2735 -0.0020 0.0158  -0.1064 256 PRO A CB  
1953 C  CG  . PRO A 256 ? 0.3651 0.3568 0.2920 0.0007  0.0168  -0.1139 256 PRO A CG  
1954 C  CD  . PRO A 256 ? 0.3840 0.3958 0.3056 -0.0027 0.0105  -0.1136 256 PRO A CD  
1955 N  N   . ARG A 257 ? 0.3311 0.3156 0.2733 -0.0147 0.0049  -0.0997 257 ARG A N   
1956 C  CA  . ARG A 257 ? 0.3277 0.3055 0.2764 -0.0198 0.0030  -0.0964 257 ARG A CA  
1957 C  C   . ARG A 257 ? 0.3144 0.3014 0.2638 -0.0180 -0.0015 -0.0839 257 ARG A C   
1958 O  O   . ARG A 257 ? 0.3218 0.3007 0.2763 -0.0193 -0.0019 -0.0775 257 ARG A O   
1959 C  CB  . ARG A 257 ? 0.3479 0.3302 0.2980 -0.0277 0.0014  -0.1086 257 ARG A CB  
1960 C  CG  . ARG A 257 ? 0.4990 0.4711 0.4573 -0.0337 0.0016  -0.1073 257 ARG A CG  
1961 C  CD  . ARG A 257 ? 0.5224 0.4939 0.4845 -0.0423 0.0027  -0.1222 257 ARG A CD  
1962 N  NE  . ARG A 257 ? 0.6176 0.6117 0.5781 -0.0462 -0.0036 -0.1267 257 ARG A NE  
1963 C  CZ  . ARG A 257 ? 0.5656 0.5649 0.5328 -0.0526 -0.0061 -0.1276 257 ARG A CZ  
1964 N  NH1 . ARG A 257 ? 0.5996 0.5825 0.5750 -0.0564 -0.0025 -0.1247 257 ARG A NH1 
1965 N  NH2 . ARG A 257 ? 0.5928 0.6156 0.5584 -0.0546 -0.0122 -0.1309 257 ARG A NH2 
1966 N  N   . GLN A 258 ? 0.3000 0.3033 0.2442 -0.0147 -0.0042 -0.0801 258 GLN A N   
1967 C  CA  . GLN A 258 ? 0.2571 0.2677 0.2027 -0.0127 -0.0073 -0.0685 258 GLN A CA  
1968 C  C   . GLN A 258 ? 0.2872 0.2907 0.2352 -0.0081 -0.0051 -0.0590 258 GLN A C   
1969 O  O   . GLN A 258 ? 0.2760 0.2758 0.2286 -0.0083 -0.0064 -0.0514 258 GLN A O   
1970 C  CB  . GLN A 258 ? 0.2854 0.3159 0.2253 -0.0107 -0.0103 -0.0670 258 GLN A CB  
1971 C  CG  . GLN A 258 ? 0.2950 0.3374 0.2327 -0.0151 -0.0136 -0.0765 258 GLN A CG  
1972 C  CD  . GLN A 258 ? 0.3165 0.3809 0.2468 -0.0115 -0.0162 -0.0748 258 GLN A CD  
1973 O  OE1 . GLN A 258 ? 0.3278 0.3989 0.2508 -0.0083 -0.0144 -0.0783 258 GLN A OE1 
1974 N  NE2 . GLN A 258 ? 0.3155 0.3921 0.2473 -0.0111 -0.0202 -0.0687 258 GLN A NE2 
1975 N  N   . ARG A 259 ? 0.2714 0.2745 0.2166 -0.0039 -0.0018 -0.0598 259 ARG A N   
1976 C  CA  . ARG A 259 ? 0.2599 0.2586 0.2086 0.0002  0.0001  -0.0515 259 ARG A CA  
1977 C  C   . ARG A 259 ? 0.2558 0.2401 0.2102 -0.0007 0.0009  -0.0498 259 ARG A C   
1978 O  O   . ARG A 259 ? 0.2510 0.2340 0.2094 0.0011  0.0005  -0.0422 259 ARG A O   
1979 C  CB  . ARG A 259 ? 0.2535 0.2544 0.1993 0.0050  0.0041  -0.0538 259 ARG A CB  
1980 C  CG  . ARG A 259 ? 0.2671 0.2835 0.2058 0.0068  0.0043  -0.0555 259 ARG A CG  
1981 C  CD  . ARG A 259 ? 0.2639 0.2828 0.2016 0.0123  0.0090  -0.0546 259 ARG A CD  
1982 N  NE  . ARG A 259 ? 0.2844 0.3182 0.2138 0.0145  0.0101  -0.0574 259 ARG A NE  
1983 C  CZ  . ARG A 259 ? 0.3102 0.3462 0.2331 0.0152  0.0121  -0.0686 259 ARG A CZ  
1984 N  NH1 . ARG A 259 ? 0.3439 0.3660 0.2686 0.0138  0.0141  -0.0783 259 ARG A NH1 
1985 N  NH2 . ARG A 259 ? 0.3078 0.3604 0.2221 0.0176  0.0127  -0.0703 259 ARG A NH2 
1986 N  N   . HIS A 260 ? 0.2764 0.2503 0.2312 -0.0034 0.0024  -0.0567 260 HIS A N   
1987 C  CA  . HIS A 260 ? 0.2747 0.2348 0.2341 -0.0036 0.0039  -0.0540 260 HIS A CA  
1988 C  C   . HIS A 260 ? 0.2639 0.2258 0.2264 -0.0054 0.0005  -0.0466 260 HIS A C   
1989 O  O   . HIS A 260 ? 0.2453 0.2015 0.2107 -0.0034 0.0011  -0.0410 260 HIS A O   
1990 C  CB  . HIS A 260 ? 0.2928 0.2422 0.2530 -0.0079 0.0064  -0.0626 260 HIS A CB  
1991 C  CG  . HIS A 260 ? 0.3120 0.2454 0.2763 -0.0067 0.0101  -0.0595 260 HIS A CG  
1992 N  ND1 . HIS A 260 ? 0.3461 0.2688 0.3113 -0.0018 0.0152  -0.0605 260 HIS A ND1 
1993 C  CD2 . HIS A 260 ? 0.3683 0.2952 0.3359 -0.0090 0.0098  -0.0548 260 HIS A CD2 
1994 C  CE1 . HIS A 260 ? 0.3778 0.2880 0.3466 -0.0009 0.0180  -0.0556 260 HIS A CE1 
1995 N  NE2 . HIS A 260 ? 0.3770 0.2898 0.3468 -0.0054 0.0148  -0.0522 260 HIS A NE2 
1996 N  N   . LEU A 261 ? 0.2541 0.2250 0.2159 -0.0088 -0.0029 -0.0466 261 LEU A N   
1997 C  CA  . LEU A 261 ? 0.2551 0.2271 0.2202 -0.0105 -0.0055 -0.0407 261 LEU A CA  
1998 C  C   . LEU A 261 ? 0.2548 0.2310 0.2219 -0.0072 -0.0063 -0.0334 261 LEU A C   
1999 O  O   . LEU A 261 ? 0.2481 0.2231 0.2182 -0.0080 -0.0077 -0.0293 261 LEU A O   
2000 C  CB  . LEU A 261 ? 0.2686 0.2495 0.2336 -0.0140 -0.0085 -0.0424 261 LEU A CB  
2001 C  CG  . LEU A 261 ? 0.2811 0.2572 0.2480 -0.0191 -0.0083 -0.0479 261 LEU A CG  
2002 C  CD1 . LEU A 261 ? 0.3086 0.2799 0.2738 -0.0210 -0.0057 -0.0569 261 LEU A CD1 
2003 C  CD2 . LEU A 261 ? 0.3031 0.2909 0.2714 -0.0218 -0.0118 -0.0481 261 LEU A CD2 
2004 N  N   . LEU A 262 ? 0.2443 0.2257 0.2101 -0.0038 -0.0051 -0.0323 262 LEU A N   
2005 C  CA  . LEU A 262 ? 0.2549 0.2406 0.2244 -0.0016 -0.0052 -0.0261 262 LEU A CA  
2006 C  C   . LEU A 262 ? 0.2684 0.2494 0.2402 0.0016  -0.0035 -0.0248 262 LEU A C   
2007 O  O   . LEU A 262 ? 0.2617 0.2480 0.2376 0.0033  -0.0036 -0.0208 262 LEU A O   
2008 C  CB  . LEU A 262 ? 0.2489 0.2446 0.2169 0.0003  -0.0041 -0.0243 262 LEU A CB  
2009 C  CG  . LEU A 262 ? 0.2482 0.2510 0.2134 -0.0013 -0.0058 -0.0239 262 LEU A CG  
2010 C  CD1 . LEU A 262 ? 0.2954 0.3087 0.2586 0.0015  -0.0039 -0.0201 262 LEU A CD1 
2011 C  CD2 . LEU A 262 ? 0.3074 0.3090 0.2769 -0.0037 -0.0080 -0.0200 262 LEU A CD2 
2012 N  N   . GLY A 263 ? 0.2328 0.2047 0.2030 0.0026  -0.0018 -0.0280 263 GLY A N   
2013 C  CA  . GLY A 263 ? 0.2594 0.2277 0.2317 0.0072  0.0002  -0.0257 263 GLY A CA  
2014 C  C   . GLY A 263 ? 0.2416 0.2120 0.2133 0.0117  0.0034  -0.0276 263 GLY A C   
2015 O  O   . GLY A 263 ? 0.2518 0.2232 0.2265 0.0166  0.0049  -0.0247 263 GLY A O   
2016 N  N   . PHE A 264 ? 0.2456 0.2184 0.2134 0.0106  0.0046  -0.0326 264 PHE A N   
2017 C  CA  . PHE A 264 ? 0.2552 0.2305 0.2216 0.0151  0.0083  -0.0355 264 PHE A CA  
2018 C  C   . PHE A 264 ? 0.2774 0.2400 0.2442 0.0187  0.0123  -0.0386 264 PHE A C   
2019 O  O   . PHE A 264 ? 0.2939 0.2454 0.2597 0.0158  0.0128  -0.0421 264 PHE A O   
2020 C  CB  . PHE A 264 ? 0.2601 0.2410 0.2205 0.0129  0.0086  -0.0414 264 PHE A CB  
2021 C  CG  . PHE A 264 ? 0.2718 0.2605 0.2299 0.0173  0.0120  -0.0432 264 PHE A CG  
2022 C  CD1 . PHE A 264 ? 0.2605 0.2614 0.2204 0.0188  0.0120  -0.0369 264 PHE A CD1 
2023 C  CD2 . PHE A 264 ? 0.2665 0.2504 0.2207 0.0195  0.0159  -0.0517 264 PHE A CD2 
2024 C  CE1 . PHE A 264 ? 0.2703 0.2798 0.2281 0.0230  0.0158  -0.0379 264 PHE A CE1 
2025 C  CE2 . PHE A 264 ? 0.3134 0.3057 0.2648 0.0239  0.0195  -0.0539 264 PHE A CE2 
2026 C  CZ  . PHE A 264 ? 0.2935 0.2993 0.2464 0.0258  0.0194  -0.0465 264 PHE A CZ  
2027 N  N   . PRO A 265 ? 0.2735 0.2371 0.2427 0.0252  0.0156  -0.0372 265 PRO A N   
2028 C  CA  . PRO A 265 ? 0.2807 0.2306 0.2511 0.0299  0.0204  -0.0393 265 PRO A CA  
2029 C  C   . PRO A 265 ? 0.3074 0.2480 0.2736 0.0275  0.0238  -0.0498 265 PRO A C   
2030 O  O   . PRO A 265 ? 0.3041 0.2522 0.2663 0.0272  0.0248  -0.0557 265 PRO A O   
2031 C  CB  . PRO A 265 ? 0.2732 0.2302 0.2472 0.0379  0.0232  -0.0360 265 PRO A CB  
2032 C  CG  . PRO A 265 ? 0.2696 0.2428 0.2467 0.0363  0.0187  -0.0296 265 PRO A CG  
2033 C  CD  . PRO A 265 ? 0.2705 0.2475 0.2430 0.0290  0.0158  -0.0326 265 PRO A CD  
2034 N  N   . PRO A 266 ? 0.3001 0.2250 0.2672 0.0255  0.0262  -0.0527 266 PRO A N   
2035 C  CA  . PRO A 266 ? 0.3281 0.2447 0.2924 0.0210  0.0291  -0.0644 266 PRO A CA  
2036 C  C   . PRO A 266 ? 0.3626 0.2723 0.3269 0.0268  0.0358  -0.0711 266 PRO A C   
2037 O  O   . PRO A 266 ? 0.3300 0.2390 0.2974 0.0351  0.0389  -0.0654 266 PRO A O   
2038 C  CB  . PRO A 266 ? 0.3465 0.2478 0.3140 0.0167  0.0303  -0.0638 266 PRO A CB  
2039 C  CG  . PRO A 266 ? 0.3780 0.2754 0.3493 0.0230  0.0311  -0.0521 266 PRO A CG  
2040 C  CD  . PRO A 266 ? 0.3409 0.2565 0.3115 0.0260  0.0260  -0.0453 266 PRO A CD  
2041 N  N   . PRO A 267 ? 0.3786 0.2847 0.3398 0.0227  0.0383  -0.0840 267 PRO A N   
2042 C  CA  . PRO A 267 ? 0.3953 0.2913 0.3570 0.0278  0.0458  -0.0922 267 PRO A CA  
2043 C  C   . PRO A 267 ? 0.3857 0.2616 0.3545 0.0333  0.0519  -0.0867 267 PRO A C   
2044 O  O   . PRO A 267 ? 0.4188 0.2833 0.3911 0.0295  0.0518  -0.0829 267 PRO A O   
2045 C  CB  . PRO A 267 ? 0.4017 0.2945 0.3601 0.0197  0.0467  -0.1080 267 PRO A CB  
2046 C  CG  . PRO A 267 ? 0.4149 0.3259 0.3684 0.0130  0.0385  -0.1070 267 PRO A CG  
2047 C  CD  . PRO A 267 ? 0.3740 0.2866 0.3311 0.0135  0.0342  -0.0922 267 PRO A CD  
2048 N  N   . GLY A 268 ? 0.3836 0.2564 0.3547 0.0431  0.0574  -0.0852 268 GLY A N   
2049 C  CA  . GLY A 268 ? 0.4435 0.2991 0.4214 0.0508  0.0637  -0.0782 268 GLY A CA  
2050 C  C   . GLY A 268 ? 0.4029 0.2662 0.3839 0.0569  0.0600  -0.0618 268 GLY A C   
2051 O  O   . GLY A 268 ? 0.4974 0.3502 0.4837 0.0654  0.0649  -0.0541 268 GLY A O   
2052 N  N   . ASP A 269 ? 0.3914 0.2733 0.3697 0.0530  0.0518  -0.0564 269 ASP A N   
2053 C  CA  . ASP A 269 ? 0.3903 0.2816 0.3717 0.0577  0.0478  -0.0428 269 ASP A CA  
2054 C  C   . ASP A 269 ? 0.3653 0.2650 0.3508 0.0689  0.0506  -0.0379 269 ASP A C   
2055 O  O   . ASP A 269 ? 0.3758 0.2827 0.3602 0.0711  0.0528  -0.0440 269 ASP A O   
2056 C  CB  . ASP A 269 ? 0.3644 0.2734 0.3428 0.0506  0.0393  -0.0405 269 ASP A CB  
2057 C  CG  . ASP A 269 ? 0.3869 0.3043 0.3682 0.0528  0.0346  -0.0288 269 ASP A CG  
2058 O  OD1 . ASP A 269 ? 0.3426 0.2741 0.3272 0.0585  0.0331  -0.0234 269 ASP A OD1 
2059 O  OD2 . ASP A 269 ? 0.3979 0.3092 0.3784 0.0487  0.0325  -0.0255 269 ASP A OD2 
2060 N  N   . ASP A 270 ? 0.3796 0.2801 0.3697 0.0763  0.0506  -0.0265 270 ASP A N   
2061 C  CA  . ASP A 270 ? 0.3954 0.3067 0.3908 0.0876  0.0527  -0.0207 270 ASP A CA  
2062 C  C   . ASP A 270 ? 0.3506 0.2859 0.3465 0.0859  0.0477  -0.0210 270 ASP A C   
2063 O  O   . ASP A 270 ? 0.3328 0.2784 0.3334 0.0940  0.0504  -0.0193 270 ASP A O   
2064 C  CB  . ASP A 270 ? 0.3992 0.3122 0.3989 0.0952  0.0516  -0.0076 270 ASP A CB  
2065 C  CG  . ASP A 270 ? 0.5448 0.4355 0.5471 0.1034  0.0602  -0.0044 270 ASP A CG  
2066 O  OD1 . ASP A 270 ? 0.6747 0.5540 0.6789 0.1081  0.0677  -0.0109 270 ASP A OD1 
2067 O  OD2 . ASP A 270 ? 0.6253 0.5097 0.6279 0.1055  0.0599  0.0047  270 ASP A OD2 
2068 N  N   . TYR A 271 ? 0.3332 0.2776 0.3255 0.0760  0.0412  -0.0225 271 TYR A N   
2069 C  CA  . TYR A 271 ? 0.3170 0.2825 0.3107 0.0739  0.0376  -0.0220 271 TYR A CA  
2070 C  C   . TYR A 271 ? 0.2970 0.2656 0.2890 0.0761  0.0427  -0.0295 271 TYR A C   
2071 O  O   . TYR A 271 ? 0.2947 0.2802 0.2908 0.0793  0.0430  -0.0271 271 TYR A O   
2072 C  CB  . TYR A 271 ? 0.2728 0.2439 0.2629 0.0631  0.0310  -0.0224 271 TYR A CB  
2073 C  CG  . TYR A 271 ? 0.2519 0.2412 0.2433 0.0598  0.0288  -0.0224 271 TYR A CG  
2074 C  CD1 . TYR A 271 ? 0.2695 0.2754 0.2682 0.0606  0.0254  -0.0157 271 TYR A CD1 
2075 C  CD2 . TYR A 271 ? 0.2605 0.2512 0.2462 0.0558  0.0303  -0.0289 271 TYR A CD2 
2076 C  CE1 . TYR A 271 ? 0.2470 0.2682 0.2483 0.0570  0.0245  -0.0152 271 TYR A CE1 
2077 C  CE2 . TYR A 271 ? 0.2615 0.2685 0.2485 0.0534  0.0293  -0.0272 271 TYR A CE2 
2078 C  CZ  . TYR A 271 ? 0.2714 0.2924 0.2668 0.0537  0.0268  -0.0202 271 TYR A CZ  
2079 O  OH  . TYR A 271 ? 0.2537 0.2895 0.2518 0.0508  0.0271  -0.0180 271 TYR A OH  
2080 N  N   . TRP A 272 ? 0.2996 0.2531 0.2860 0.0745  0.0471  -0.0389 272 TRP A N   
2081 C  CA  . TRP A 272 ? 0.3258 0.2836 0.3083 0.0753  0.0514  -0.0478 272 TRP A CA  
2082 C  C   . TRP A 272 ? 0.3570 0.3144 0.3445 0.0867  0.0586  -0.0480 272 TRP A C   
2083 O  O   . TRP A 272 ? 0.3749 0.3154 0.3651 0.0927  0.0638  -0.0488 272 TRP A O   
2084 C  CB  . TRP A 272 ? 0.3400 0.2843 0.3148 0.0687  0.0528  -0.0595 272 TRP A CB  
2085 C  CG  . TRP A 272 ? 0.2964 0.2447 0.2669 0.0584  0.0458  -0.0590 272 TRP A CG  
2086 C  CD1 . TRP A 272 ? 0.3042 0.2398 0.2736 0.0521  0.0434  -0.0602 272 TRP A CD1 
2087 C  CD2 . TRP A 272 ? 0.2999 0.2661 0.2675 0.0537  0.0408  -0.0561 272 TRP A CD2 
2088 N  NE1 . TRP A 272 ? 0.3337 0.2790 0.2996 0.0442  0.0369  -0.0588 272 TRP A NE1 
2089 C  CE2 . TRP A 272 ? 0.2882 0.2514 0.2529 0.0452  0.0354  -0.0561 272 TRP A CE2 
2090 C  CE3 . TRP A 272 ? 0.2991 0.2833 0.2669 0.0559  0.0412  -0.0532 272 TRP A CE3 
2091 C  CZ2 . TRP A 272 ? 0.2807 0.2573 0.2429 0.0398  0.0304  -0.0529 272 TRP A CZ2 
2092 C  CZ3 . TRP A 272 ? 0.2999 0.2968 0.2653 0.0499  0.0365  -0.0496 272 TRP A CZ3 
2093 C  CH2 . TRP A 272 ? 0.2680 0.2604 0.2305 0.0423  0.0312  -0.0494 272 TRP A CH2 
2094 N  N   . THR A 273 ? 0.3258 0.3017 0.3152 0.0900  0.0597  -0.0467 273 THR A N   
2095 C  CA  . THR A 273 ? 0.3520 0.3316 0.3460 0.1009  0.0669  -0.0478 273 THR A CA  
2096 C  C   . THR A 273 ? 0.3526 0.3469 0.3417 0.0994  0.0693  -0.0538 273 THR A C   
2097 O  O   . THR A 273 ? 0.3462 0.3487 0.3292 0.0908  0.0649  -0.0548 273 THR A O   
2098 C  CB  . THR A 273 ? 0.3777 0.3719 0.3827 0.1081  0.0654  -0.0360 273 THR A CB  
2099 O  OG1 . THR A 273 ? 0.3629 0.3788 0.3699 0.1022  0.0600  -0.0312 273 THR A OG1 
2100 C  CG2 . THR A 273 ? 0.3507 0.3349 0.3594 0.1097  0.0620  -0.0283 273 THR A CG2 
2101 N  N   . GLU A 274 ? 0.3824 0.3810 0.3742 0.1087  0.0766  -0.0569 274 GLU A N   
2102 C  CA  . GLU A 274 ? 0.3594 0.3748 0.3467 0.1083  0.0795  -0.0611 274 GLU A CA  
2103 C  C   . GLU A 274 ? 0.3736 0.4106 0.3642 0.1030  0.0740  -0.0514 274 GLU A C   
2104 O  O   . GLU A 274 ? 0.3827 0.4295 0.3662 0.0969  0.0729  -0.0533 274 GLU A O   
2105 C  CB  . GLU A 274 ? 0.4571 0.4768 0.4491 0.1202  0.0885  -0.0638 274 GLU A CB  
2106 C  CG  . GLU A 274 ? 0.5753 0.5749 0.5618 0.1245  0.0958  -0.0770 274 GLU A CG  
2107 C  CD  . GLU A 274 ? 0.6768 0.6837 0.6662 0.1356  0.1053  -0.0814 274 GLU A CD  
2108 O  OE1 . GLU A 274 ? 0.6518 0.6799 0.6484 0.1404  0.1059  -0.0729 274 GLU A OE1 
2109 O  OE2 . GLU A 274 ? 0.7910 0.7827 0.7759 0.1394  0.1124  -0.0940 274 GLU A OE2 
2110 N  N   . GLU A 275 ? 0.3444 0.3893 0.3463 0.1050  0.0707  -0.0410 275 GLU A N   
2111 C  CA  . GLU A 275 ? 0.3248 0.3896 0.3322 0.0993  0.0662  -0.0328 275 GLU A CA  
2112 C  C   . GLU A 275 ? 0.3098 0.3701 0.3110 0.0879  0.0593  -0.0318 275 GLU A C   
2113 O  O   . GLU A 275 ? 0.3026 0.3753 0.3028 0.0820  0.0581  -0.0290 275 GLU A O   
2114 C  CB  . GLU A 275 ? 0.3783 0.4543 0.3996 0.1036  0.0639  -0.0236 275 GLU A CB  
2115 C  CG  . GLU A 275 ? 0.4671 0.5628 0.4957 0.0962  0.0596  -0.0167 275 GLU A CG  
2116 C  CD  . GLU A 275 ? 0.5871 0.7013 0.6311 0.1009  0.0587  -0.0096 275 GLU A CD  
2117 O  OE1 . GLU A 275 ? 0.5949 0.7053 0.6434 0.1090  0.0584  -0.0077 275 GLU A OE1 
2118 O  OE2 . GLU A 275 ? 0.6248 0.7582 0.6770 0.0965  0.0586  -0.0057 275 GLU A OE2 
2119 N  N   . THR A 276 ? 0.2871 0.3304 0.2853 0.0849  0.0550  -0.0330 276 THR A N   
2120 C  CA  . THR A 276 ? 0.2623 0.3030 0.2556 0.0746  0.0487  -0.0319 276 THR A CA  
2121 C  C   . THR A 276 ? 0.2974 0.3340 0.2787 0.0701  0.0498  -0.0397 276 THR A C   
2122 O  O   . THR A 276 ? 0.2821 0.3234 0.2598 0.0629  0.0459  -0.0376 276 THR A O   
2123 C  CB  . THR A 276 ? 0.2773 0.3042 0.2717 0.0721  0.0436  -0.0297 276 THR A CB  
2124 O  OG1 . THR A 276 ? 0.3000 0.3084 0.2906 0.0764  0.0472  -0.0356 276 THR A OG1 
2125 C  CG2 . THR A 276 ? 0.2926 0.3293 0.2980 0.0748  0.0406  -0.0210 276 THR A CG2 
2126 N  N   . ILE A 277 ? 0.3153 0.3440 0.2904 0.0745  0.0552  -0.0491 277 ILE A N   
2127 C  CA  . ILE A 277 ? 0.3194 0.3498 0.2828 0.0706  0.0561  -0.0572 277 ILE A CA  
2128 C  C   . ILE A 277 ? 0.3268 0.3782 0.2889 0.0709  0.0580  -0.0527 277 ILE A C   
2129 O  O   . ILE A 277 ? 0.3218 0.3805 0.2773 0.0653  0.0553  -0.0515 277 ILE A O   
2130 C  CB  . ILE A 277 ? 0.3440 0.3624 0.3017 0.0750  0.0619  -0.0700 277 ILE A CB  
2131 C  CG1 . ILE A 277 ? 0.3488 0.3448 0.3076 0.0728  0.0604  -0.0742 277 ILE A CG1 
2132 C  CG2 . ILE A 277 ? 0.3910 0.4174 0.3363 0.0719  0.0630  -0.0792 277 ILE A CG2 
2133 C  CD1 . ILE A 277 ? 0.3619 0.3532 0.3140 0.0629  0.0546  -0.0782 277 ILE A CD1 
2134 N  N   . LYS A 278 ? 0.3223 0.3843 0.2918 0.0776  0.0629  -0.0489 278 LYS A N   
2135 C  CA  . LYS A 278 ? 0.3194 0.4017 0.2897 0.0778  0.0658  -0.0432 278 LYS A CA  
2136 C  C   . LYS A 278 ? 0.3114 0.4006 0.2864 0.0701  0.0605  -0.0330 278 LYS A C   
2137 O  O   . LYS A 278 ? 0.2959 0.3949 0.2657 0.0665  0.0609  -0.0297 278 LYS A O   
2138 C  CB  . LYS A 278 ? 0.3414 0.4346 0.3220 0.0859  0.0718  -0.0401 278 LYS A CB  
2139 C  CG  . LYS A 278 ? 0.4319 0.5468 0.4159 0.0853  0.0754  -0.0327 278 LYS A CG  
2140 C  CD  . LYS A 278 ? 0.5179 0.6461 0.5149 0.0925  0.0808  -0.0287 278 LYS A CD  
2141 C  CE  . LYS A 278 ? 0.5170 0.6577 0.5289 0.0876  0.0775  -0.0177 278 LYS A CE  
2142 N  NZ  . LYS A 278 ? 0.6413 0.8010 0.6661 0.0934  0.0835  -0.0135 278 LYS A NZ  
2143 N  N   . HIS A 279 ? 0.2731 0.3577 0.2583 0.0679  0.0558  -0.0277 279 HIS A N   
2144 C  CA  . HIS A 279 ? 0.2807 0.3707 0.2713 0.0603  0.0513  -0.0194 279 HIS A CA  
2145 C  C   . HIS A 279 ? 0.2595 0.3415 0.2402 0.0539  0.0470  -0.0210 279 HIS A C   
2146 O  O   . HIS A 279 ? 0.2578 0.3462 0.2393 0.0488  0.0457  -0.0147 279 HIS A O   
2147 C  CB  . HIS A 279 ? 0.2642 0.3522 0.2669 0.0593  0.0468  -0.0151 279 HIS A CB  
2148 C  CG  . HIS A 279 ? 0.2807 0.3837 0.2963 0.0639  0.0500  -0.0108 279 HIS A CG  
2149 N  ND1 . HIS A 279 ? 0.3160 0.4359 0.3370 0.0635  0.0548  -0.0065 279 HIS A ND1 
2150 C  CD2 . HIS A 279 ? 0.3509 0.4558 0.3756 0.0692  0.0491  -0.0097 279 HIS A CD2 
2151 C  CE1 . HIS A 279 ? 0.3767 0.5090 0.4105 0.0678  0.0566  -0.0038 279 HIS A CE1 
2152 N  NE2 . HIS A 279 ? 0.3435 0.4677 0.3796 0.0717  0.0529  -0.0056 279 HIS A NE2 
2153 N  N   . LEU A 280 ? 0.2504 0.3183 0.2226 0.0540  0.0450  -0.0291 280 LEU A N   
2154 C  CA  . LEU A 280 ? 0.2546 0.3175 0.2180 0.0482  0.0409  -0.0311 280 LEU A CA  
2155 C  C   . LEU A 280 ? 0.2719 0.3473 0.2260 0.0485  0.0438  -0.0313 280 LEU A C   
2156 O  O   . LEU A 280 ? 0.2706 0.3511 0.2222 0.0443  0.0414  -0.0257 280 LEU A O   
2157 C  CB  . LEU A 280 ? 0.2874 0.3341 0.2451 0.0478  0.0390  -0.0406 280 LEU A CB  
2158 C  CG  . LEU A 280 ? 0.2580 0.2997 0.2088 0.0413  0.0339  -0.0430 280 LEU A CG  
2159 C  CD1 . LEU A 280 ? 0.2711 0.3084 0.2290 0.0365  0.0286  -0.0355 280 LEU A CD1 
2160 C  CD2 . LEU A 280 ? 0.3316 0.3602 0.2767 0.0410  0.0341  -0.0546 280 LEU A CD2 
2161 N  N   . SER A 281 ? 0.3021 0.3833 0.2507 0.0542  0.0494  -0.0373 281 SER A N   
2162 C  CA  . SER A 281 ? 0.3002 0.3959 0.2386 0.0555  0.0527  -0.0374 281 SER A CA  
2163 C  C   . SER A 281 ? 0.3173 0.4272 0.2617 0.0547  0.0552  -0.0244 281 SER A C   
2164 O  O   . SER A 281 ? 0.3464 0.4665 0.2835 0.0536  0.0559  -0.0198 281 SER A O   
2165 C  CB  . SER A 281 ? 0.3642 0.4636 0.2962 0.0622  0.0590  -0.0472 281 SER A CB  
2166 O  OG  . SER A 281 ? 0.4304 0.5159 0.3565 0.0617  0.0573  -0.0601 281 SER A OG  
2167 N  N   . GLU A 282 ? 0.2713 0.3830 0.2295 0.0553  0.0570  -0.0182 282 GLU A N   
2168 C  CA  . GLU A 282 ? 0.2753 0.3998 0.2419 0.0533  0.0601  -0.0064 282 GLU A CA  
2169 C  C   . GLU A 282 ? 0.2660 0.3860 0.2351 0.0463  0.0553  0.0009  282 GLU A C   
2170 O  O   . GLU A 282 ? 0.3045 0.4332 0.2726 0.0447  0.0581  0.0094  282 GLU A O   
2171 C  CB  . GLU A 282 ? 0.2818 0.4107 0.2643 0.0547  0.0624  -0.0031 282 GLU A CB  
2172 C  CG  . GLU A 282 ? 0.3752 0.5124 0.3580 0.0626  0.0689  -0.0074 282 GLU A CG  
2173 C  CD  . GLU A 282 ? 0.4162 0.5581 0.4157 0.0643  0.0697  -0.0045 282 GLU A CD  
2174 O  OE1 . GLU A 282 ? 0.4529 0.5882 0.4612 0.0600  0.0638  -0.0023 282 GLU A OE1 
2175 O  OE2 . GLU A 282 ? 0.5421 0.6957 0.5459 0.0704  0.0760  -0.0048 282 GLU A OE2 
2176 N  N   . MET A 283 ? 0.2393 0.3456 0.2119 0.0425  0.0488  -0.0018 283 MET A N   
2177 C  CA  . MET A 283 ? 0.2340 0.3352 0.2101 0.0363  0.0446  0.0042  283 MET A CA  
2178 C  C   . MET A 283 ? 0.2412 0.3412 0.2045 0.0356  0.0423  0.0034  283 MET A C   
2179 O  O   . MET A 283 ? 0.2413 0.3421 0.2062 0.0323  0.0414  0.0111  283 MET A O   
2180 C  CB  . MET A 283 ? 0.2642 0.3528 0.2474 0.0331  0.0387  0.0011  283 MET A CB  
2181 C  CG  . MET A 283 ? 0.2596 0.3530 0.2578 0.0323  0.0397  0.0046  283 MET A CG  
2182 S  SD  . MET A 283 ? 0.2898 0.3711 0.2935 0.0304  0.0328  0.0005  283 MET A SD  
2183 C  CE  . MET A 283 ? 0.2610 0.3325 0.2620 0.0234  0.0277  0.0024  283 MET A CE  
2184 N  N   . TYR A 284 ? 0.2439 0.3423 0.1951 0.0385  0.0413  -0.0062 284 TYR A N   
2185 C  CA  . TYR A 284 ? 0.2378 0.3372 0.1773 0.0375  0.0380  -0.0089 284 TYR A CA  
2186 C  C   . TYR A 284 ? 0.2763 0.3879 0.2029 0.0425  0.0418  -0.0145 284 TYR A C   
2187 O  O   . TYR A 284 ? 0.2865 0.3944 0.2050 0.0434  0.0401  -0.0266 284 TYR A O   
2188 C  CB  . TYR A 284 ? 0.2415 0.3265 0.1797 0.0344  0.0319  -0.0177 284 TYR A CB  
2189 C  CG  . TYR A 284 ? 0.2149 0.2885 0.1641 0.0299  0.0280  -0.0134 284 TYR A CG  
2190 C  CD1 . TYR A 284 ? 0.2235 0.2972 0.1753 0.0263  0.0254  -0.0058 284 TYR A CD1 
2191 C  CD2 . TYR A 284 ? 0.2490 0.3125 0.2053 0.0298  0.0270  -0.0170 284 TYR A CD2 
2192 C  CE1 . TYR A 284 ? 0.2333 0.2972 0.1944 0.0222  0.0220  -0.0034 284 TYR A CE1 
2193 C  CE2 . TYR A 284 ? 0.2444 0.2995 0.2092 0.0259  0.0232  -0.0137 284 TYR A CE2 
2194 C  CZ  . TYR A 284 ? 0.2429 0.2983 0.2098 0.0218  0.0207  -0.0076 284 TYR A CZ  
2195 O  OH  . TYR A 284 ? 0.2289 0.2767 0.2037 0.0179  0.0172  -0.0054 284 TYR A OH  
2196 N  N   . PRO A 285 ? 0.2576 0.3839 0.1823 0.0457  0.0475  -0.0064 285 PRO A N   
2197 C  CA  . PRO A 285 ? 0.2769 0.4167 0.1888 0.0512  0.0519  -0.0120 285 PRO A CA  
2198 C  C   . PRO A 285 ? 0.3383 0.4830 0.2357 0.0510  0.0475  -0.0194 285 PRO A C   
2199 O  O   . PRO A 285 ? 0.3275 0.4765 0.2221 0.0493  0.0442  -0.0121 285 PRO A O   
2200 C  CB  . PRO A 285 ? 0.3072 0.4621 0.2209 0.0537  0.0586  0.0017  285 PRO A CB  
2201 C  CG  . PRO A 285 ? 0.2789 0.4256 0.2105 0.0495  0.0591  0.0111  285 PRO A CG  
2202 C  CD  . PRO A 285 ? 0.2830 0.4141 0.2179 0.0443  0.0511  0.0080  285 PRO A CD  
2203 N  N   . GLY A 286 ? 0.3167 0.4608 0.2055 0.0529  0.0476  -0.0344 286 GLY A N   
2204 C  CA  . GLY A 286 ? 0.3627 0.5114 0.2393 0.0515  0.0428  -0.0449 286 GLY A CA  
2205 C  C   . GLY A 286 ? 0.3696 0.5006 0.2502 0.0460  0.0370  -0.0556 286 GLY A C   
2206 O  O   . GLY A 286 ? 0.3976 0.5320 0.2694 0.0441  0.0335  -0.0673 286 GLY A O   
2207 N  N   . ILE A 287 ? 0.3197 0.4332 0.2134 0.0434  0.0360  -0.0521 287 ILE A N   
2208 C  CA  . ILE A 287 ? 0.2923 0.3887 0.1901 0.0386  0.0314  -0.0609 287 ILE A CA  
2209 C  C   . ILE A 287 ? 0.3337 0.4234 0.2269 0.0397  0.0341  -0.0775 287 ILE A C   
2210 O  O   . ILE A 287 ? 0.3588 0.4505 0.2510 0.0448  0.0401  -0.0809 287 ILE A O   
2211 C  CB  . ILE A 287 ? 0.2906 0.3718 0.2022 0.0366  0.0304  -0.0530 287 ILE A CB  
2212 C  CG1 . ILE A 287 ? 0.2800 0.3463 0.1950 0.0311  0.0251  -0.0581 287 ILE A CG1 
2213 C  CG2 . ILE A 287 ? 0.2984 0.3733 0.2163 0.0409  0.0358  -0.0547 287 ILE A CG2 
2214 C  CD1 . ILE A 287 ? 0.3113 0.3670 0.2378 0.0288  0.0229  -0.0488 287 ILE A CD1 
2215 N  N   . ASP A 288 ? 0.3513 0.4329 0.2428 0.0346  0.0301  -0.0882 288 ASP A N   
2216 C  CA  . ASP A 288 ? 0.3909 0.4630 0.2799 0.0343  0.0330  -0.1050 288 ASP A CA  
2217 C  C   . ASP A 288 ? 0.3732 0.4228 0.2739 0.0348  0.0355  -0.1043 288 ASP A C   
2218 O  O   . ASP A 288 ? 0.3681 0.4051 0.2756 0.0302  0.0318  -0.1013 288 ASP A O   
2219 C  CB  . ASP A 288 ? 0.4345 0.5083 0.3185 0.0277  0.0279  -0.1167 288 ASP A CB  
2220 C  CG  . ASP A 288 ? 0.4539 0.5155 0.3372 0.0257  0.0313  -0.1354 288 ASP A CG  
2221 O  OD1 . ASP A 288 ? 0.4830 0.5385 0.3667 0.0310  0.0380  -0.1399 288 ASP A OD1 
2222 O  OD2 . ASP A 288 ? 0.5218 0.5800 0.4053 0.0188  0.0277  -0.1457 288 ASP A OD2 
2223 N  N   . VAL A 289 ? 0.3953 0.4407 0.2980 0.0410  0.0422  -0.1065 289 VAL A N   
2224 C  CA  . VAL A 289 ? 0.4003 0.4265 0.3141 0.0433  0.0449  -0.1041 289 VAL A CA  
2225 C  C   . VAL A 289 ? 0.4419 0.4497 0.3566 0.0422  0.0483  -0.1187 289 VAL A C   
2226 O  O   . VAL A 289 ? 0.4326 0.4225 0.3563 0.0440  0.0506  -0.1161 289 VAL A O   
2227 C  CB  . VAL A 289 ? 0.4017 0.4329 0.3205 0.0513  0.0503  -0.0964 289 VAL A CB  
2228 C  CG1 . VAL A 289 ? 0.4054 0.4536 0.3251 0.0513  0.0479  -0.0822 289 VAL A CG1 
2229 C  CG2 . VAL A 289 ? 0.4378 0.4738 0.3503 0.0572  0.0574  -0.1075 289 VAL A CG2 
2230 N  N   . GLU A 290 ? 0.4707 0.4824 0.3767 0.0394  0.0491  -0.1338 290 GLU A N   
2231 C  CA  . GLU A 290 ? 0.4818 0.4751 0.3897 0.0379  0.0537  -0.1494 290 GLU A CA  
2232 C  C   . GLU A 290 ? 0.4699 0.4415 0.3874 0.0329  0.0522  -0.1476 290 GLU A C   
2233 O  O   . GLU A 290 ? 0.5135 0.4648 0.4379 0.0357  0.0585  -0.1517 290 GLU A O   
2234 C  CB  . GLU A 290 ? 0.5347 0.5388 0.4319 0.0333  0.0530  -0.1670 290 GLU A CB  
2235 C  CG  . GLU A 290 ? 0.6225 0.6068 0.5225 0.0318  0.0579  -0.1790 290 GLU A CG  
2236 C  CD  . GLU A 290 ? 0.7268 0.7225 0.6176 0.0275  0.0557  -0.1897 290 GLU A CD  
2237 O  OE1 . GLU A 290 ? 0.7775 0.7869 0.6644 0.0206  0.0483  -0.1903 290 GLU A OE1 
2238 O  OE2 . GLU A 290 ? 0.8177 0.8097 0.7055 0.0315  0.0614  -0.1976 290 GLU A OE2 
2239 N  N   . PRO A 291 ? 0.4431 0.4174 0.3620 0.0261  0.0452  -0.1413 291 PRO A N   
2240 C  CA  . PRO A 291 ? 0.4375 0.3914 0.3655 0.0217  0.0447  -0.1392 291 PRO A CA  
2241 C  C   . PRO A 291 ? 0.4849 0.4255 0.4216 0.0284  0.0480  -0.1266 291 PRO A C   
2242 O  O   . PRO A 291 ? 0.4871 0.4081 0.4309 0.0271  0.0504  -0.1261 291 PRO A O   
2243 C  CB  . PRO A 291 ? 0.4438 0.4084 0.3707 0.0147  0.0363  -0.1328 291 PRO A CB  
2244 C  CG  . PRO A 291 ? 0.4223 0.4106 0.3387 0.0138  0.0329  -0.1375 291 PRO A CG  
2245 C  CD  . PRO A 291 ? 0.4490 0.4447 0.3612 0.0224  0.0379  -0.1364 291 PRO A CD  
2246 N  N   . TYR A 292 ? 0.4055 0.3572 0.3422 0.0356  0.0483  -0.1163 292 TYR A N   
2247 C  CA  . TYR A 292 ? 0.4082 0.3529 0.3534 0.0416  0.0496  -0.1034 292 TYR A CA  
2248 C  C   . TYR A 292 ? 0.4349 0.3749 0.3834 0.0515  0.0573  -0.1047 292 TYR A C   
2249 O  O   . TYR A 292 ? 0.4233 0.3578 0.3793 0.0576  0.0589  -0.0946 292 TYR A O   
2250 C  CB  . TYR A 292 ? 0.3797 0.3413 0.3256 0.0417  0.0439  -0.0897 292 TYR A CB  
2251 C  CG  . TYR A 292 ? 0.3380 0.3050 0.2812 0.0332  0.0367  -0.0875 292 TYR A CG  
2252 C  CD1 . TYR A 292 ? 0.3176 0.2738 0.2658 0.0292  0.0336  -0.0827 292 TYR A CD1 
2253 C  CD2 . TYR A 292 ? 0.3558 0.3396 0.2915 0.0300  0.0336  -0.0898 292 TYR A CD2 
2254 C  CE1 . TYR A 292 ? 0.3342 0.2957 0.2805 0.0221  0.0276  -0.0809 292 TYR A CE1 
2255 C  CE2 . TYR A 292 ? 0.3343 0.3235 0.2683 0.0235  0.0274  -0.0872 292 TYR A CE2 
2256 C  CZ  . TYR A 292 ? 0.3293 0.3071 0.2690 0.0195  0.0245  -0.0831 292 TYR A CZ  
2257 O  OH  . TYR A 292 ? 0.3360 0.3197 0.2747 0.0136  0.0189  -0.0807 292 TYR A OH  
2258 N  N   . LEU A 293 ? 0.4600 0.4033 0.4028 0.0537  0.0622  -0.1167 293 LEU A N   
2259 C  CA  . LEU A 293 ? 0.5094 0.4493 0.4554 0.0638  0.0701  -0.1184 293 LEU A CA  
2260 C  C   . LEU A 293 ? 0.5920 0.5071 0.5469 0.0679  0.0756  -0.1179 293 LEU A C   
2261 O  O   . LEU A 293 ? 0.6236 0.5211 0.5788 0.0624  0.0775  -0.1273 293 LEU A O   
2262 C  CB  . LEU A 293 ? 0.5251 0.4701 0.4626 0.0643  0.0748  -0.1345 293 LEU A CB  
2263 C  CG  . LEU A 293 ? 0.5547 0.5261 0.4827 0.0633  0.0715  -0.1336 293 LEU A CG  
2264 C  CD1 . LEU A 293 ? 0.5393 0.5160 0.4576 0.0638  0.0762  -0.1510 293 LEU A CD1 
2265 C  CD2 . LEU A 293 ? 0.5690 0.5542 0.5017 0.0709  0.0726  -0.1196 293 LEU A CD2 
2266 N  N   . PRO A 294 ? 0.5990 0.5127 0.5618 0.0775  0.0784  -0.1067 294 PRO A N   
2267 C  CA  . PRO A 294 ? 0.6510 0.5422 0.6223 0.0835  0.0843  -0.1039 294 PRO A CA  
2268 C  C   . PRO A 294 ? 0.7356 0.6083 0.7066 0.0858  0.0939  -0.1194 294 PRO A C   
2269 O  O   . PRO A 294 ? 0.6708 0.5521 0.6383 0.0905  0.0982  -0.1275 294 PRO A O   
2270 C  CB  . PRO A 294 ? 0.6873 0.5890 0.6656 0.0950  0.0857  -0.0908 294 PRO A CB  
2271 C  CG  . PRO A 294 ? 0.6143 0.5417 0.5897 0.0912  0.0779  -0.0836 294 PRO A CG  
2272 C  CD  . PRO A 294 ? 0.5700 0.5049 0.5349 0.0830  0.0761  -0.0953 294 PRO A CD  
2287 N  N   . TYR B 2   ? 0.4496 0.3533 0.5393 -0.0092 0.0343  -0.0272 16  TYR C N   
2288 C  CA  . TYR B 2   ? 0.4679 0.3743 0.5570 -0.0037 0.0347  -0.0125 16  TYR C CA  
2289 C  C   . TYR B 2   ? 0.4224 0.3414 0.5007 -0.0059 0.0277  -0.0096 16  TYR C C   
2290 O  O   . TYR B 2   ? 0.3606 0.2878 0.4333 -0.0010 0.0253  -0.0005 16  TYR C O   
2291 C  CB  . TYR B 2   ? 0.4659 0.3750 0.5548 0.0054  0.0360  -0.0047 16  TYR C CB  
2292 C  CG  . TYR B 2   ? 0.5055 0.4021 0.6054 0.0096  0.0436  -0.0060 16  TYR C CG  
2293 C  CD1 . TYR B 2   ? 0.5262 0.4078 0.6365 0.0049  0.0498  -0.0141 16  TYR C CD1 
2294 C  CD2 . TYR B 2   ? 0.5566 0.4572 0.6573 0.0184  0.0448  0.0003  16  TYR C CD2 
2295 C  CE1 . TYR B 2   ? 0.5845 0.4532 0.7054 0.0090  0.0576  -0.0162 16  TYR C CE1 
2296 C  CE2 . TYR B 2   ? 0.5237 0.4128 0.6348 0.0234  0.0523  -0.0006 16  TYR C CE2 
2297 C  CZ  . TYR B 2   ? 0.5689 0.4410 0.6900 0.0189  0.0590  -0.0089 16  TYR C CZ  
2298 O  OH  . TYR B 2   ? 0.6628 0.5220 0.7949 0.0242  0.0672  -0.0105 16  TYR C OH  
2306 N  N   . GLY B 3   ? 0.3792 0.3009 0.4548 -0.0129 0.0245  -0.0178 17  GLY C N   
2307 C  CA  . GLY B 3   ? 0.3609 0.2930 0.4275 -0.0146 0.0188  -0.0156 17  GLY C CA  
2308 C  C   . GLY B 3   ? 0.3591 0.2897 0.4313 -0.0194 0.0204  -0.0149 17  GLY C C   
2309 O  O   . GLY B 3   ? 0.3708 0.2925 0.4537 -0.0198 0.0267  -0.0111 17  GLY C O   
2313 N  N   . TRP B 4   ? 0.3405 0.2799 0.4064 -0.0229 0.0154  -0.0184 18  TRP C N   
2314 C  CA  . TRP B 4   ? 0.3568 0.2981 0.4276 -0.0270 0.0163  -0.0175 18  TRP C CA  
2315 C  C   . TRP B 4   ? 0.3523 0.3010 0.4213 -0.0325 0.0119  -0.0274 18  TRP C C   
2316 O  O   . TRP B 4   ? 0.4047 0.3567 0.4796 -0.0366 0.0126  -0.0281 18  TRP C O   
2317 C  CB  . TRP B 4   ? 0.3255 0.2734 0.3900 -0.0232 0.0151  -0.0074 18  TRP C CB  
2318 C  CG  . TRP B 4   ? 0.3026 0.2599 0.3543 -0.0217 0.0086  -0.0092 18  TRP C CG  
2319 C  CD1 . TRP B 4   ? 0.2974 0.2619 0.3452 -0.0242 0.0049  -0.0127 18  TRP C CD1 
2320 C  CD2 . TRP B 4   ? 0.2919 0.2521 0.3346 -0.0175 0.0055  -0.0075 18  TRP C CD2 
2321 N  NE1 . TRP B 4   ? 0.2997 0.2692 0.3365 -0.0215 0.0004  -0.0130 18  TRP C NE1 
2322 C  CE2 . TRP B 4   ? 0.2997 0.2668 0.3335 -0.0181 0.0007  -0.0104 18  TRP C CE2 
2323 C  CE3 . TRP B 4   ? 0.3120 0.2701 0.3543 -0.0132 0.0067  -0.0040 18  TRP C CE3 
2324 C  CZ2 . TRP B 4   ? 0.2989 0.2696 0.3242 -0.0156 -0.0025 -0.0102 18  TRP C CZ2 
2325 C  CZ3 . TRP B 4   ? 0.3157 0.2799 0.3495 -0.0108 0.0028  -0.0042 18  TRP C CZ3 
2326 C  CH2 . TRP B 4   ? 0.3247 0.2944 0.3503 -0.0125 -0.0015 -0.0075 18  TRP C CH2 
2336 N  N   . ALA B 5   ? 0.3890 0.3417 0.4504 -0.0324 0.0075  -0.0345 19  ALA C N   
2337 C  CA  . ALA B 5   ? 0.4467 0.4093 0.5044 -0.0358 0.0027  -0.0418 19  ALA C CA  
2338 C  C   . ALA B 5   ? 0.4782 0.4420 0.5332 -0.0372 0.0010  -0.0517 19  ALA C C   
2339 O  O   . ALA B 5   ? 0.4788 0.4376 0.5308 -0.0342 0.0023  -0.0518 19  ALA C O   
2340 C  CB  . ALA B 5   ? 0.4578 0.4284 0.5040 -0.0322 -0.0020 -0.0369 19  ALA C CB  
2346 N  N   . SER B 6   ? 0.4657 0.4384 0.5214 -0.0414 -0.0020 -0.0601 20  SER C N   
2347 C  CA  . SER B 6   ? 0.5129 0.4912 0.5635 -0.0424 -0.0046 -0.0700 20  SER C CA  
2348 C  C   . SER B 6   ? 0.5693 0.5370 0.6273 -0.0442 0.0005  -0.0765 20  SER C C   
2349 O  O   . SER B 6   ? 0.5672 0.5262 0.6378 -0.0476 0.0054  -0.0774 20  SER C O   
2350 C  CB  . SER B 6   ? 0.5599 0.5434 0.5964 -0.0371 -0.0083 -0.0657 20  SER C CB  
2351 O  OG  . SER B 6   ? 0.6035 0.5943 0.6339 -0.0375 -0.0105 -0.0739 20  SER C OG  
2357 N  N   . ASN B 7   ? 0.5893 0.5574 0.6405 -0.0418 0.0002  -0.0811 21  ASN C N   
2358 C  CA  . ASN B 7   ? 0.6640 0.6225 0.7220 -0.0429 0.0053  -0.0886 21  ASN C CA  
2359 C  C   . ASN B 7   ? 0.6808 0.6389 0.7298 -0.0374 0.0056  -0.0871 21  ASN C C   
2360 O  O   . ASN B 7   ? 0.6695 0.6370 0.7066 -0.0348 0.0013  -0.0844 21  ASN C O   
2361 C  CB  . ASN B 7   ? 0.7017 0.6654 0.7646 -0.0494 0.0049  -0.1040 21  ASN C CB  
2362 C  CG  . ASN B 7   ? 0.7769 0.7263 0.8548 -0.0532 0.0122  -0.1108 21  ASN C CG  
2363 O  OD1 . ASN B 7   ? 0.7987 0.7413 0.8888 -0.0571 0.0154  -0.1084 21  ASN C OD1 
2364 N  ND2 . ASN B 7   ? 0.8315 0.7756 0.9091 -0.0520 0.0155  -0.1189 21  ASN C ND2 
2378 N  N   . GLY B 9   ? 1.0297 0.9727 1.0874 -0.0364 0.0174  -0.1108 23  GLY C N   
2379 C  CA  . GLY B 9   ? 1.1209 1.0584 1.1836 -0.0376 0.0223  -0.1241 23  GLY C CA  
2380 C  C   . GLY B 9   ? 1.1358 1.0564 1.2148 -0.0393 0.0296  -0.1250 23  GLY C C   
2381 O  O   . GLY B 9   ? 1.2032 1.1225 1.2866 -0.0418 0.0325  -0.1340 23  GLY C O   
2385 N  N   . GLU B 10  ? 1.0223 0.9326 1.1086 -0.0368 0.0323  -0.1124 24  GLU C N   
2386 C  CA  . GLU B 10  ? 1.0506 0.9448 1.1523 -0.0374 0.0399  -0.1097 24  GLU C CA  
2387 C  C   . GLU B 10  ? 0.9909 0.8850 1.0986 -0.0424 0.0386  -0.1040 24  GLU C C   
2388 O  O   . GLU B 10  ? 1.0620 0.9574 1.1760 -0.0485 0.0395  -0.1101 24  GLU C O   
2389 C  CB  . GLU B 10  ? 1.0882 0.9703 1.1947 -0.0287 0.0457  -0.0986 24  GLU C CB  
2390 C  CG  . GLU B 10  ? 1.1009 0.9911 1.1968 -0.0219 0.0437  -0.0973 24  GLU C CG  
2391 C  CD  . GLU B 10  ? 1.2028 1.0807 1.3072 -0.0152 0.0519  -0.0974 24  GLU C CD  
2392 O  OE1 . GLU B 10  ? 1.2470 1.1141 1.3612 -0.0175 0.0579  -0.1049 24  GLU C OE1 
2393 O  OE2 . GLU B 10  ? 1.1922 1.0746 1.2927 -0.0074 0.0518  -0.0885 24  GLU C OE2 
2400 N  N   . GLY B 11  ? 0.8418 0.7381 0.9459 -0.0391 0.0361  -0.0904 25  GLY C N   
2401 C  CA  . GLY B 11  ? 0.7269 0.6247 0.8356 -0.0431 0.0351  -0.0842 25  GLY C CA  
2402 C  C   . GLY B 11  ? 0.6288 0.5412 0.7242 -0.0408 0.0273  -0.0757 25  GLY C C   
2403 O  O   . GLY B 11  ? 0.6496 0.5727 0.7327 -0.0390 0.0217  -0.0787 25  GLY C O   
2407 N  N   . VAL B 12  ? 0.5020 0.4145 0.5998 -0.0404 0.0275  -0.0648 26  VAL C N   
2408 C  CA  . VAL B 12  ? 0.4886 0.4139 0.5748 -0.0384 0.0207  -0.0577 26  VAL C CA  
2409 C  C   . VAL B 12  ? 0.4626 0.3900 0.5385 -0.0308 0.0188  -0.0502 26  VAL C C   
2410 O  O   . VAL B 12  ? 0.4571 0.3765 0.5366 -0.0259 0.0232  -0.0452 26  VAL C O   
2411 C  CB  . VAL B 12  ? 0.4729 0.3980 0.5643 -0.0395 0.0223  -0.0485 26  VAL C CB  
2412 C  CG1 . VAL B 12  ? 0.5324 0.4603 0.6331 -0.0480 0.0227  -0.0571 26  VAL C CG1 
2413 C  CG2 . VAL B 12  ? 0.4811 0.3937 0.5807 -0.0353 0.0297  -0.0379 26  VAL C CG2 
2423 N  N   . ALA B 13  ? 0.4149 0.3535 0.4786 -0.0297 0.0124  -0.0490 27  ALA C N   
2424 C  CA  . ALA B 13  ? 0.4173 0.3596 0.4718 -0.0244 0.0102  -0.0449 27  ALA C CA  
2425 C  C   . ALA B 13  ? 0.3880 0.3361 0.4357 -0.0216 0.0070  -0.0352 27  ALA C C   
2426 O  O   . ALA B 13  ? 0.3499 0.3010 0.3977 -0.0236 0.0056  -0.0326 27  ALA C O   
2427 C  CB  . ALA B 13  ? 0.4698 0.4196 0.5154 -0.0256 0.0064  -0.0532 27  ALA C CB  
2433 N  N   . ILE B 14  ? 0.3504 0.3009 0.3931 -0.0171 0.0061  -0.0306 28  ILE C N   
2434 C  CA  . ILE B 14  ? 0.3336 0.2908 0.3688 -0.0151 0.0026  -0.0241 28  ILE C CA  
2435 C  C   . ILE B 14  ? 0.4632 0.4265 0.4896 -0.0175 -0.0018 -0.0285 28  ILE C C   
2436 O  O   . ILE B 14  ? 0.4648 0.4294 0.4881 -0.0183 -0.0024 -0.0342 28  ILE C O   
2437 C  CB  . ILE B 14  ? 0.3875 0.3469 0.4219 -0.0103 0.0032  -0.0190 28  ILE C CB  
2438 C  CG1 . ILE B 14  ? 0.4058 0.3596 0.4492 -0.0065 0.0080  -0.0129 28  ILE C CG1 
2439 C  CG2 . ILE B 14  ? 0.4025 0.3698 0.4294 -0.0093 -0.0006 -0.0148 28  ILE C CG2 
2440 C  CD1 . ILE B 14  ? 0.4607 0.4187 0.5050 -0.0007 0.0087  -0.0076 28  ILE C CD1 
2452 N  N   . ILE B 15  ? 0.4148 0.3820 0.4369 -0.0179 -0.0043 -0.0253 29  ILE C N   
2453 C  CA  . ILE B 15  ? 0.4603 0.4322 0.4746 -0.0190 -0.0077 -0.0276 29  ILE C CA  
2454 C  C   . ILE B 15  ? 0.5565 0.5308 0.5657 -0.0172 -0.0092 -0.0225 29  ILE C C   
2455 O  O   . ILE B 15  ? 0.5214 0.4961 0.5314 -0.0152 -0.0085 -0.0186 29  ILE C O   
2456 C  CB  . ILE B 15  ? 0.4928 0.4671 0.5088 -0.0218 -0.0088 -0.0316 29  ILE C CB  
2457 C  CG1 . ILE B 15  ? 0.5912 0.5710 0.5992 -0.0216 -0.0120 -0.0339 29  ILE C CG1 
2458 C  CG2 . ILE B 15  ? 0.4775 0.4525 0.4971 -0.0221 -0.0084 -0.0274 29  ILE C CG2 
2459 C  CD1 . ILE B 15  ? 0.5722 0.5534 0.5743 -0.0195 -0.0135 -0.0291 29  ILE C CD1 
2471 C  C1  . AKG C .   ? 0.4016 0.4108 0.4277 -0.0026 -0.0053 -0.0128 401 AKG A C1  
2472 O  O1  . AKG C .   ? 0.3335 0.3388 0.3544 -0.0071 -0.0057 -0.0169 401 AKG A O1  
2473 O  O2  . AKG C .   ? 0.4596 0.4739 0.4853 -0.0008 -0.0076 -0.0086 401 AKG A O2  
2474 C  C2  . AKG C .   ? 0.3893 0.3979 0.4228 0.0022  -0.0016 -0.0119 401 AKG A C2  
2475 O  O5  . AKG C .   ? 0.3208 0.3270 0.3544 0.0011  0.0007  -0.0162 401 AKG A O5  
2476 C  C3  . AKG C .   ? 0.3797 0.3901 0.4196 0.0089  -0.0001 -0.0053 401 AKG A C3  
2477 C  C4  . AKG C .   ? 0.3255 0.3512 0.3705 0.0132  -0.0012 -0.0015 401 AKG A C4  
2478 C  C5  . AKG C .   ? 0.3147 0.3442 0.3649 0.0210  -0.0002 0.0072  401 AKG A C5  
2479 O  O3  . AKG C .   ? 0.3788 0.3978 0.4295 0.0231  0.0022  0.0109  401 AKG A O3  
2480 O  O4  . AKG C .   ? 0.2967 0.3425 0.3511 0.0252  -0.0019 0.0108  401 AKG A O4  
2485 FE FE  . FE  D .   ? 0.2344 0.2360 0.2568 -0.0071 -0.0011 -0.0220 402 FE  A FE  
2486 FE FE  . FE  E .   ? 0.2772 0.2940 0.3605 -0.0980 0.0507  -0.0305 403 FE  A FE  
2487 O  O   . HOH F .   ? 0.5346 0.9040 0.5850 0.0919  -0.0571 0.0658  501 HOH A O   
2488 O  O   . HOH F .   ? 0.6121 0.6412 0.5452 -0.0321 -0.0048 -0.1383 502 HOH A O   
2489 O  O   . HOH F .   ? 0.5428 0.4842 0.6516 0.0968  0.0803  0.1675  503 HOH A O   
2490 O  O   . HOH F .   ? 0.5518 0.8068 0.5457 0.1210  -0.0175 0.1397  504 HOH A O   
2491 O  O   . HOH F .   ? 0.4578 0.4638 0.4507 -0.0079 -0.0203 -0.0205 505 HOH A O   
2492 O  O   . HOH F .   ? 0.6971 0.7987 0.6141 -0.0315 -0.0180 -0.1494 506 HOH A O   
2493 O  O   . HOH F .   ? 0.4325 0.4221 0.4310 -0.0149 -0.0157 -0.0210 507 HOH A O   
2494 O  O   . HOH F .   ? 0.5447 0.5359 0.6008 0.0230  0.0102  0.0088  508 HOH A O   
2495 O  O   . HOH F .   ? 0.4291 0.4281 0.4246 -0.0043 -0.0087 -0.0119 509 HOH A O   
2496 O  O   . HOH F .   ? 0.5805 0.6426 0.6726 0.1515  0.0563  0.1962  510 HOH A O   
2497 O  O   . HOH F .   ? 0.4540 0.6647 0.5749 -0.0198 -0.0108 -0.0290 511 HOH A O   
2498 O  O   . HOH F .   ? 0.4523 0.6559 0.5258 -0.0914 -0.0408 -0.1200 512 HOH A O   
2499 O  O   . HOH F .   ? 0.4749 0.7996 0.5630 0.0358  -0.0553 0.0070  513 HOH A O   
2500 O  O   . HOH F .   ? 0.7048 0.7888 0.5786 0.0099  0.0183  -0.1573 514 HOH A O   
2501 O  O   . HOH F .   ? 0.4685 0.6541 0.5460 0.1318  -0.0014 0.1334  515 HOH A O   
2502 O  O   . HOH F .   ? 0.4247 0.7630 0.4048 0.0480  -0.0658 0.0136  516 HOH A O   
2503 O  O   . HOH F .   ? 0.3887 0.5035 0.3904 -0.0692 -0.0351 -0.1199 517 HOH A O   
2504 O  O   . HOH F .   ? 0.4049 0.6087 0.5590 0.1748  0.0213  0.1376  518 HOH A O   
2505 O  O   . HOH F .   ? 0.5309 0.5091 0.5770 0.0118  0.0075  0.0029  519 HOH A O   
2506 O  O   . HOH F .   ? 0.4658 0.5863 0.3797 0.0055  -0.0207 -0.0479 520 HOH A O   
2507 O  O   . HOH F .   ? 0.6150 0.9640 0.6008 0.1333  -0.0306 0.1355  521 HOH A O   
2508 O  O   . HOH F .   ? 0.5465 0.5939 0.4920 -0.0072 0.0192  -0.1233 522 HOH A O   
2509 O  O   . HOH F .   ? 0.4624 0.6230 0.5857 -0.0603 0.0233  -0.0374 523 HOH A O   
2510 O  O   . HOH F .   ? 0.4160 0.5617 0.4000 0.0404  0.0675  0.0310  524 HOH A O   
2511 O  O   . HOH F .   ? 0.4487 0.3472 0.4222 0.0152  0.0194  -0.0156 525 HOH A O   
2512 O  O   . HOH F .   ? 0.3218 0.4327 0.3059 0.0279  0.0496  0.0310  526 HOH A O   
2513 O  O   . HOH F .   ? 0.2570 0.3918 0.3244 0.0374  -0.0169 0.0214  527 HOH A O   
2514 O  O   . HOH F .   ? 0.5205 0.5486 0.6365 0.0705  0.0733  -0.0507 528 HOH A O   
2515 O  O   . HOH F .   ? 0.3545 0.6712 0.4073 0.0325  -0.0619 0.0038  529 HOH A O   
2516 O  O   . HOH F .   ? 0.4563 0.3971 0.5741 0.0717  0.0518  0.0521  530 HOH A O   
2517 O  O   . HOH F .   ? 0.4482 0.4297 0.4490 -0.0158 -0.0078 -0.0250 531 HOH A O   
2518 O  O   . HOH F .   ? 0.6318 0.4762 0.8240 0.1135  0.1138  0.0636  532 HOH A O   
2519 O  O   . HOH F .   ? 0.5297 0.6148 0.5916 0.0433  0.0834  -0.0752 533 HOH A O   
2520 O  O   . HOH F .   ? 0.6848 0.5197 0.8493 0.0279  0.1022  0.0897  534 HOH A O   
2521 O  O   . HOH F .   ? 0.5473 0.5286 0.6125 0.0256  0.0172  0.0008  535 HOH A O   
2522 O  O   . HOH F .   ? 0.5204 0.5509 0.4970 0.0064  0.0429  -0.1074 536 HOH A O   
2523 O  O   . HOH F .   ? 0.3454 0.3382 0.3845 0.0077  0.0323  0.0669  537 HOH A O   
2524 O  O   . HOH F .   ? 0.6009 0.5412 0.7565 0.1000  0.0762  0.0193  538 HOH A O   
2525 O  O   . HOH F .   ? 0.5474 0.5226 0.6307 0.0381  0.0295  -0.0029 539 HOH A O   
2526 O  O   . HOH F .   ? 0.3266 0.3371 0.4026 -0.0955 0.0401  -0.0388 540 HOH A O   
2527 O  O   . HOH F .   ? 0.4187 0.4185 0.3881 -0.0082 -0.0186 -0.0230 541 HOH A O   
2528 O  O   . HOH F .   ? 0.2842 0.4393 0.4500 0.1340  0.0301  0.0732  542 HOH A O   
2529 O  O   . HOH F .   ? 0.4365 0.5264 0.4777 0.0969  0.0453  -0.0051 543 HOH A O   
2530 O  O   . HOH F .   ? 0.3059 0.3688 0.2544 -0.0071 -0.0283 -0.0508 544 HOH A O   
2531 O  O   . HOH F .   ? 0.4459 0.3436 0.4129 0.0569  0.0616  -0.0889 545 HOH A O   
2532 O  O   . HOH F .   ? 0.3885 0.3192 0.4801 0.0362  0.0393  0.0373  546 HOH A O   
2533 O  O   . HOH F .   ? 0.3855 0.5395 0.3233 0.0040  -0.0371 -0.0330 547 HOH A O   
2534 O  O   . HOH F .   ? 0.4274 0.4387 0.4531 0.0065  0.0294  0.0621  548 HOH A O   
2535 O  O   . HOH F .   ? 0.4686 0.4520 0.4761 -0.0121 0.0012  -0.0366 549 HOH A O   
2536 O  O   . HOH F .   ? 0.3506 0.3147 0.2994 0.0065  0.0147  -0.0735 550 HOH A O   
2537 O  O   . HOH F .   ? 0.4329 0.7285 0.5137 -0.0315 -0.0588 -0.0589 551 HOH A O   
2538 O  O   . HOH F .   ? 0.4201 0.4911 0.3783 -0.0052 0.0595  -0.0268 552 HOH A O   
2539 O  O   . HOH F .   ? 0.5629 0.4700 0.6113 -0.0991 0.0346  -0.0964 553 HOH A O   
2540 O  O   . HOH F .   ? 0.4179 0.5815 0.3123 0.0484  0.0384  0.0266  554 HOH A O   
2541 O  O   . HOH F .   ? 0.4052 0.3845 0.3900 -0.0147 -0.0149 -0.0219 555 HOH A O   
2542 O  O   . HOH F .   ? 0.6354 0.5754 0.6667 -0.0935 0.0179  -0.1261 556 HOH A O   
2543 O  O   . HOH F .   ? 0.4074 0.3523 0.3816 -0.0354 0.0034  -0.0790 557 HOH A O   
2544 O  O   . HOH F .   ? 0.4934 0.5426 0.4691 0.0125  0.0537  -0.0973 558 HOH A O   
2545 O  O   . HOH F .   ? 0.4553 0.3340 0.4197 0.0080  0.0380  0.0318  559 HOH A O   
2546 O  O   . HOH F .   ? 0.2679 0.2041 0.2475 -0.0273 0.0064  -0.0190 560 HOH A O   
2547 O  O   . HOH F .   ? 0.5204 0.3787 0.5352 -0.0553 0.0645  0.0037  561 HOH A O   
2548 O  O   . HOH F .   ? 0.5150 0.8891 0.4288 0.1042  -0.0362 0.0885  562 HOH A O   
2549 O  O   . HOH F .   ? 0.4171 0.4003 0.4039 -0.0181 -0.0051 -0.0279 563 HOH A O   
2550 O  O   . HOH F .   ? 0.4372 0.4973 0.3593 -0.0011 0.0434  -0.0221 564 HOH A O   
2551 O  O   . HOH F .   ? 0.3838 0.3680 0.4174 -0.0190 0.0022  -0.0009 565 HOH A O   
2552 O  O   . HOH F .   ? 0.3722 0.2998 0.3535 0.0466  0.0225  -0.0108 566 HOH A O   
2553 O  O   . HOH F .   ? 0.4510 0.4308 0.4473 -0.0164 -0.0137 -0.0210 567 HOH A O   
2554 O  O   . HOH F .   ? 0.4378 0.4851 0.4635 0.1047  0.0512  -0.0132 568 HOH A O   
2555 O  O   . HOH F .   ? 0.5169 0.4143 0.5053 0.0873  0.0678  -0.0539 569 HOH A O   
2556 O  O   . HOH F .   ? 0.3574 0.3418 0.3347 -0.0125 -0.0156 -0.0224 570 HOH A O   
2557 O  O   . HOH F .   ? 0.4891 0.3619 0.4706 0.0457  0.0428  -0.0301 571 HOH A O   
2558 O  O   . HOH F .   ? 0.5122 0.6639 0.4238 0.0482  0.0241  0.0644  572 HOH A O   
2559 O  O   . HOH F .   ? 0.5387 0.4755 0.6277 0.0349  0.0669  0.1171  573 HOH A O   
2560 O  O   . HOH F .   ? 0.3869 0.6250 0.5643 0.1426  0.0143  0.0829  574 HOH A O   
2561 O  O   . HOH F .   ? 0.4396 0.4405 0.4283 0.0035  -0.0043 -0.0131 575 HOH A O   
2562 O  O   . HOH F .   ? 0.6433 0.6705 0.5339 0.0105  0.0327  -0.1724 576 HOH A O   
2563 O  O   . HOH F .   ? 0.4095 0.5294 0.5123 0.0411  0.0687  -0.0437 577 HOH A O   
2564 O  O   . HOH F .   ? 0.3299 0.2723 0.2894 0.0078  0.0155  -0.0606 578 HOH A O   
2565 O  O   . HOH F .   ? 0.4199 0.4130 0.4064 -0.0195 -0.0105 -0.0510 579 HOH A O   
2566 O  O   . HOH F .   ? 0.4972 0.6641 0.6318 -0.1165 -0.0036 -0.0949 580 HOH A O   
2567 O  O   . HOH F .   ? 0.5090 0.6542 0.5424 0.1272  0.0140  0.1670  581 HOH A O   
2568 O  O   . HOH F .   ? 0.3701 0.4472 0.3610 0.0255  0.0493  0.0919  582 HOH A O   
2569 O  O   . HOH F .   ? 0.4103 0.4213 0.4892 0.0361  0.0409  -0.0380 583 HOH A O   
2570 O  O   . HOH F .   ? 0.5452 0.8303 0.7445 -0.0297 0.0711  -0.0251 584 HOH A O   
2571 O  O   . HOH F .   ? 0.3983 0.4995 0.2995 0.0559  0.0521  -0.0689 585 HOH A O   
2572 O  O   . HOH F .   ? 0.4843 0.5970 0.4161 -0.0020 -0.0274 -0.0456 586 HOH A O   
2573 O  O   . HOH F .   ? 0.2854 0.4128 0.3573 0.0989  0.0014  0.0994  587 HOH A O   
2574 O  O   . HOH F .   ? 0.5292 0.5134 0.5241 -0.0158 -0.0029 -0.0345 588 HOH A O   
2575 O  O   . HOH F .   ? 0.3905 0.3718 0.3678 -0.0072 -0.0100 -0.0201 589 HOH A O   
2576 O  O   . HOH F .   ? 0.5025 0.3584 0.5255 -0.0651 0.0515  -0.0357 590 HOH A O   
2577 O  O   . HOH F .   ? 0.3988 0.3668 0.5826 0.1642  0.0889  0.1195  591 HOH A O   
2578 O  O   . HOH F .   ? 0.3406 0.3577 0.3222 -0.0121 -0.0241 -0.0332 592 HOH A O   
2579 O  O   . HOH F .   ? 0.5129 0.6977 0.4034 0.0576  0.0406  0.0673  593 HOH A O   
2580 O  O   . HOH F .   ? 0.3793 0.3436 0.4121 -0.0708 0.0404  -0.0180 594 HOH A O   
2581 O  O   . HOH F .   ? 0.3917 0.4824 0.4263 0.0080  0.0688  0.0839  595 HOH A O   
2582 O  O   . HOH F .   ? 0.4074 0.6513 0.5216 -0.0168 -0.0290 -0.0309 596 HOH A O   
2583 O  O   . HOH F .   ? 0.5733 0.7078 0.4376 0.0344  0.0215  -0.0862 597 HOH A O   
2584 O  O   . HOH F .   ? 0.6746 0.5732 0.6176 0.0434  0.0737  -0.1558 598 HOH A O   
2585 O  O   . HOH F .   ? 0.2559 0.2228 0.2197 -0.0160 0.0025  -0.0086 599 HOH A O   
2586 O  O   . HOH F .   ? 0.3833 0.5363 0.2909 0.0474  0.0467  0.0187  600 HOH A O   
2587 O  O   . HOH F .   ? 0.4505 0.3289 0.6037 0.0832  0.0823  0.0662  601 HOH A O   
2588 O  O   . HOH F .   ? 0.2777 0.4160 0.3771 -0.0534 0.0060  -0.0400 602 HOH A O   
2589 O  O   . HOH F .   ? 0.3994 0.3161 0.4941 0.0145  0.0507  0.0614  603 HOH A O   
2590 O  O   . HOH F .   ? 0.2337 0.3118 0.3609 0.1045  0.0281  0.0656  604 HOH A O   
2591 O  O   . HOH F .   ? 0.4815 0.5656 0.4938 -0.0331 0.0850  0.0048  605 HOH A O   
2592 O  O   . HOH F .   ? 0.6969 0.5296 0.6908 0.0742  0.0687  -0.0310 606 HOH A O   
2593 O  O   . HOH F .   ? 0.3807 0.3631 0.4235 -0.0040 0.0230  0.0417  607 HOH A O   
2594 O  O   . HOH F .   ? 0.4503 0.6020 0.5897 0.0533  0.0435  -0.0148 608 HOH A O   
2595 O  O   . HOH F .   ? 0.3743 0.3686 0.4311 0.0321  0.0115  0.0314  609 HOH A O   
2596 O  O   . HOH F .   ? 0.5387 0.3970 0.5113 0.0090  0.0476  -0.0950 610 HOH A O   
2597 O  O   . HOH F .   ? 0.4209 0.5499 0.5538 0.0892  0.0191  0.0399  611 HOH A O   
2598 O  O   . HOH F .   ? 0.4524 0.5868 0.5834 0.0547  0.0333  -0.0069 612 HOH A O   
2599 O  O   . HOH F .   ? 0.5204 0.4486 0.5279 0.1145  0.0670  -0.0231 613 HOH A O   
2600 O  O   . HOH F .   ? 0.3276 0.3601 0.3111 0.0022  0.0372  -0.0709 614 HOH A O   
2601 O  O   . HOH F .   ? 0.4411 0.7859 0.4508 0.0775  -0.0591 0.0547  615 HOH A O   
2602 O  O   . HOH F .   ? 0.3280 0.3380 0.3187 -0.0350 0.0437  -0.0007 616 HOH A O   
2603 O  O   . HOH F .   ? 0.4372 0.6162 0.5873 0.0775  0.0194  0.0206  617 HOH A O   
2604 O  O   . HOH F .   ? 0.3833 0.4739 0.2733 0.0246  0.0166  -0.0817 618 HOH A O   
2605 O  O   . HOH F .   ? 0.3821 0.4163 0.2912 0.0168  0.0202  -0.1026 619 HOH A O   
2606 O  O   . HOH F .   ? 0.2973 0.3466 0.2863 0.0515  0.0352  -0.0230 620 HOH A O   
2607 O  O   . HOH F .   ? 0.4516 0.3982 0.4165 -0.0257 0.0053  -0.0819 621 HOH A O   
2608 O  O   . HOH F .   ? 0.2472 0.2090 0.2166 -0.0164 -0.0027 -0.0129 622 HOH A O   
2609 O  O   . HOH F .   ? 0.2554 0.4342 0.4419 0.1670  0.0360  0.1011  623 HOH A O   
2610 O  O   . HOH F .   ? 0.2618 0.2645 0.2818 -0.0513 0.0323  -0.0139 624 HOH A O   
2611 O  O   . HOH F .   ? 0.5055 0.6205 0.4104 -0.0005 -0.0177 -0.0777 625 HOH A O   
2612 O  O   . HOH F .   ? 0.4342 0.4932 0.4322 0.0261  0.0442  0.0959  626 HOH A O   
2613 O  O   . HOH F .   ? 0.5264 0.9115 0.4237 0.0647  -0.0533 0.0098  627 HOH A O   
2614 O  O   . HOH F .   ? 0.4413 0.5122 0.3435 0.0039  0.0244  -0.0433 628 HOH A O   
2615 O  O   . HOH F .   ? 0.5160 0.9100 0.5490 0.0301  -0.0761 -0.0137 629 HOH A O   
2616 O  O   . HOH F .   ? 0.3546 0.4649 0.4409 0.1243  0.0175  0.1320  630 HOH A O   
2617 O  O   . HOH F .   ? 0.3834 0.3140 0.4662 -0.0132 0.0328  0.0207  631 HOH A O   
2618 O  O   . HOH F .   ? 0.2929 0.3138 0.2307 -0.0105 0.0353  0.0002  632 HOH A O   
2619 O  O   . HOH F .   ? 0.3431 0.3113 0.3897 -0.0841 0.0290  -0.0446 633 HOH A O   
2620 O  O   . HOH F .   ? 0.2814 0.2288 0.2546 -0.0214 0.0039  -0.0118 634 HOH A O   
2621 O  O   . HOH F .   ? 0.4518 0.4676 0.4824 0.0420  0.0502  0.1267  635 HOH A O   
2622 O  O   . HOH F .   ? 0.5458 0.6262 0.4702 0.0753  0.0704  -0.0783 636 HOH A O   
2623 O  O   . HOH F .   ? 0.2543 0.2284 0.2394 -0.0228 -0.0101 -0.0237 637 HOH A O   
2624 O  O   . HOH F .   ? 0.2455 0.2275 0.1984 -0.0091 -0.0012 -0.0088 638 HOH A O   
2625 O  O   . HOH F .   ? 0.4746 0.5948 0.4666 0.1084  0.0419  0.1912  639 HOH A O   
2626 O  O   . HOH F .   ? 0.3867 0.3864 0.3927 -0.0094 -0.0124 -0.0112 640 HOH A O   
2627 O  O   . HOH F .   ? 0.4479 0.4525 0.4878 -0.0140 0.0170  0.0234  641 HOH A O   
2628 O  O   . HOH F .   ? 0.3235 0.4482 0.4425 -0.0878 0.0264  -0.0468 642 HOH A O   
2629 O  O   . HOH F .   ? 0.3855 0.5816 0.4023 0.1167  -0.0079 0.1409  643 HOH A O   
2630 O  O   . HOH F .   ? 0.4109 0.3523 0.3790 0.0096  0.0011  -0.0030 644 HOH A O   
2631 O  O   . HOH F .   ? 0.3919 0.3487 0.3629 -0.0006 -0.0065 -0.0111 645 HOH A O   
2632 O  O   . HOH F .   ? 0.3614 0.5159 0.2458 0.0379  0.0126  -0.0064 646 HOH A O   
2633 O  O   . HOH F .   ? 0.4452 0.5234 0.3394 0.0115  0.0075  -0.0994 647 HOH A O   
2634 O  O   . HOH F .   ? 0.5682 0.6351 0.5339 -0.0592 -0.0211 -0.1425 648 HOH A O   
2635 O  O   . HOH F .   ? 0.3800 0.3253 0.4561 0.0309  0.0347  0.0559  649 HOH A O   
2636 O  O   . HOH F .   ? 0.6949 0.9625 0.8407 -0.0996 -0.0301 -0.1010 650 HOH A O   
2637 O  O   . HOH F .   ? 0.4220 0.3794 0.3969 0.0107  -0.0018 -0.0138 651 HOH A O   
2638 O  O   . HOH F .   ? 0.5275 0.6219 0.4997 0.0077  0.0728  -0.0517 652 HOH A O   
2639 O  O   . HOH F .   ? 0.4409 0.4360 0.4765 -0.0076 0.0191  0.0339  653 HOH A O   
2640 O  O   . HOH F .   ? 0.4042 0.6728 0.5064 0.0197  -0.0390 -0.0039 654 HOH A O   
2641 O  O   . HOH F .   ? 0.3441 0.5355 0.4412 -0.0577 -0.0252 -0.0596 655 HOH A O   
2642 O  O   . HOH F .   ? 0.3513 0.5478 0.2791 0.0448  -0.0283 0.0357  656 HOH A O   
2643 O  O   . HOH F .   ? 0.4271 0.3488 0.3778 0.0157  0.0212  0.0327  657 HOH A O   
2644 O  O   . HOH F .   ? 0.2648 0.2984 0.3373 0.0421  0.0097  0.0211  658 HOH A O   
2645 O  O   . HOH F .   ? 0.5423 0.5688 0.5628 -0.0535 0.0723  0.0124  659 HOH A O   
2646 O  O   . HOH F .   ? 0.4705 0.6654 0.4014 -0.0124 -0.0479 -0.0771 660 HOH A O   
2647 O  O   . HOH F .   ? 0.3847 0.6949 0.4749 0.0925  -0.0412 0.0668  661 HOH A O   
2648 O  O   . HOH F .   ? 0.6068 0.4333 0.6080 -0.0319 0.0486  -0.0480 662 HOH A O   
2649 O  O   . HOH F .   ? 0.6411 0.5406 0.5879 0.0094  0.0518  -0.1510 663 HOH A O   
2650 O  O   . HOH F .   ? 0.5526 0.5910 0.5999 0.1081  0.0705  0.2072  664 HOH A O   
2651 O  O   . HOH F .   ? 0.3509 0.3392 0.3716 -0.0069 -0.0008 -0.0233 665 HOH A O   
2652 O  O   . HOH F .   ? 0.6209 0.7011 0.6678 0.1285  0.0628  -0.0077 666 HOH A O   
2653 O  O   . HOH F .   ? 0.5240 0.5082 0.5399 -0.0858 0.0012  -0.1292 667 HOH A O   
2654 O  O   . HOH F .   ? 0.3748 0.6981 0.3893 0.0411  -0.0664 0.0110  668 HOH A O   
2655 O  O   . HOH F .   ? 0.3921 0.5468 0.5025 -0.1185 -0.0155 -0.1187 669 HOH A O   
2656 O  O   . HOH F .   ? 0.3924 0.5717 0.3278 0.0822  0.0084  0.1255  670 HOH A O   
2657 O  O   . HOH F .   ? 0.5038 0.5010 0.5273 0.0149  0.0488  -0.0987 671 HOH A O   
2658 O  O   . HOH F .   ? 0.4910 0.3730 0.4808 0.0724  0.0485  -0.0129 672 HOH A O   
2659 O  O   . HOH F .   ? 0.4453 0.5276 0.5276 0.1386  0.0360  0.1707  673 HOH A O   
2660 O  O   . HOH F .   ? 0.6412 0.5566 0.6421 0.1155  0.0806  -0.0490 674 HOH A O   
2661 O  O   . HOH F .   ? 0.3627 0.4400 0.4849 0.0843  0.0263  0.0368  675 HOH A O   
2662 O  O   . HOH F .   ? 0.5162 0.6306 0.5337 0.0166  0.0640  0.0626  676 HOH A O   
2663 O  O   . HOH F .   ? 0.4777 0.6966 0.5236 -0.0765 -0.0500 -0.1200 677 HOH A O   
2664 O  O   . HOH F .   ? 0.3887 0.4739 0.3992 0.0171  0.0621  0.0897  678 HOH A O   
2665 O  O   . HOH F .   ? 0.4231 0.3755 0.4055 -0.0374 0.0453  0.0155  679 HOH A O   
2666 O  O   . HOH F .   ? 0.5554 0.7976 0.5369 -0.0412 -0.0591 -0.1090 680 HOH A O   
2667 O  O   . HOH F .   ? 0.4420 0.6806 0.4018 0.1176  -0.0022 0.1539  681 HOH A O   
2668 O  O   . HOH F .   ? 0.3937 0.3856 0.3916 -0.0123 0.0055  -0.0420 682 HOH A O   
2669 O  O   . HOH F .   ? 0.3028 0.2856 0.3279 -0.0218 -0.0067 -0.0174 683 HOH A O   
2670 O  O   . HOH F .   ? 0.2873 0.2277 0.2555 0.0074  0.0085  -0.0373 684 HOH A O   
2671 O  O   . HOH F .   ? 0.5960 0.9169 0.4888 0.1008  -0.0159 0.1011  685 HOH A O   
2672 O  O   . HOH F .   ? 0.4629 0.5095 0.3609 0.0082  0.0166  -0.1291 686 HOH A O   
2673 O  O   . HOH F .   ? 0.3656 0.3608 0.3503 -0.0134 0.0042  -0.0507 687 HOH A O   
2674 O  O   . HOH F .   ? 0.2762 0.2519 0.2736 -0.0384 0.0070  -0.0223 688 HOH A O   
2675 O  O   . HOH F .   ? 0.3738 0.3641 0.3575 -0.0169 0.0004  -0.0319 689 HOH A O   
2676 O  O   . HOH F .   ? 0.4176 0.4146 0.3516 -0.0218 0.0063  -0.1308 690 HOH A O   
2677 O  O   . HOH F .   ? 0.3927 0.5276 0.2882 0.0606  0.0580  -0.0500 691 HOH A O   
2678 O  O   . HOH F .   ? 0.5702 0.6939 0.4353 0.0512  0.0460  -0.1005 692 HOH A O   
2679 O  O   . HOH F .   ? 0.4196 0.7758 0.3628 0.0900  -0.0481 0.0707  693 HOH A O   
2680 O  O   . HOH F .   ? 0.5119 0.4864 0.5186 0.1316  0.0886  -0.0529 694 HOH A O   
2681 O  O   . HOH F .   ? 0.5297 0.5439 0.6070 -0.1195 0.0117  -0.1168 695 HOH A O   
2682 O  O   . HOH F .   ? 0.3004 0.3227 0.2035 0.0170  0.0117  0.0250  696 HOH A O   
2683 O  O   . HOH F .   ? 0.4313 0.5547 0.3701 0.0459  0.0289  0.0860  697 HOH A O   
2684 O  O   . HOH F .   ? 0.5781 0.7505 0.4294 0.0448  0.0254  -0.0610 698 HOH A O   
2685 O  O   . HOH F .   ? 0.5055 0.5969 0.6110 -0.0180 0.0918  0.0947  699 HOH A O   
2686 O  O   . HOH F .   ? 0.6932 0.6705 0.7631 0.0653  0.0878  0.1872  700 HOH A O   
2687 O  O   . HOH F .   ? 0.6268 0.5227 0.6505 -0.0812 0.0289  -0.1047 701 HOH A O   
2688 O  O   . HOH F .   ? 0.2736 0.2249 0.2409 -0.0206 0.0125  -0.0018 702 HOH A O   
2689 O  O   . HOH F .   ? 0.4549 0.3918 0.4132 0.0742  0.0218  0.0620  703 HOH A O   
2690 O  O   . HOH F .   ? 0.4157 0.5283 0.4255 0.0452  0.0491  0.0010  704 HOH A O   
2691 O  O   . HOH F .   ? 0.5405 0.6185 0.6525 0.0539  0.0473  -0.0244 705 HOH A O   
2692 O  O   . HOH F .   ? 0.5620 0.4035 0.5444 0.0384  0.0563  -0.0586 706 HOH A O   
2693 O  O   . HOH F .   ? 0.5285 0.6310 0.5696 0.0405  0.0930  -0.0823 707 HOH A O   
2694 O  O   . HOH F .   ? 0.4509 0.5774 0.4081 0.0772  0.0758  -0.0347 708 HOH A O   
2695 O  O   . HOH F .   ? 0.4301 0.5436 0.4754 0.0017  0.0714  -0.0372 709 HOH A O   
2696 O  O   . HOH F .   ? 0.4443 0.4343 0.4291 -0.0047 -0.0090 -0.0147 710 HOH A O   
2697 O  O   . HOH F .   ? 0.5783 0.6962 0.5307 0.0570  0.0325  0.1169  711 HOH A O   
2698 O  O   . HOH F .   ? 0.3347 0.5572 0.4226 -0.0442 -0.0385 -0.0566 712 HOH A O   
2699 O  O   . HOH F .   ? 0.2962 0.3181 0.3514 0.0461  0.0090  0.0513  713 HOH A O   
2700 O  O   . HOH F .   ? 0.5391 0.5531 0.6231 -0.0316 0.0289  0.0208  714 HOH A O   
2701 O  O   . HOH F .   ? 0.5502 0.7245 0.4201 0.0510  0.0358  -0.0132 715 HOH A O   
2702 O  O   . HOH F .   ? 0.3521 0.3712 0.3640 -0.0071 -0.0143 -0.0102 716 HOH A O   
2703 O  O   . HOH F .   ? 0.4404 0.5155 0.4256 -0.0152 0.0672  -0.0147 717 HOH A O   
2704 O  O   . HOH F .   ? 0.5632 0.5632 0.6133 -0.0110 0.0302  0.0439  718 HOH A O   
2705 O  O   . HOH F .   ? 0.4388 0.6502 0.3499 0.0339  -0.0343 0.0042  719 HOH A O   
2706 O  O   . HOH F .   ? 0.3516 0.3348 0.3597 -0.0175 -0.0113 -0.0178 720 HOH A O   
2707 O  O   . HOH F .   ? 0.4876 0.5250 0.5083 0.1274  0.0771  -0.0327 721 HOH A O   
2708 O  O   . HOH F .   ? 0.4067 0.5382 0.3362 -0.0172 -0.0339 -0.0833 722 HOH A O   
2709 O  O   . HOH F .   ? 0.4279 0.2839 0.4317 -0.0437 0.0536  -0.0030 723 HOH A O   
2710 O  O   . HOH F .   ? 0.4961 0.4628 0.5426 0.0077  0.0262  -0.0535 724 HOH A O   
2711 O  O   . HOH F .   ? 0.6587 0.5989 0.7363 0.0219  0.0399  -0.0458 725 HOH A O   
2712 O  O   . HOH F .   ? 0.3670 0.3558 0.4034 -0.0146 0.0102  0.0149  726 HOH A O   
2713 O  O   . HOH F .   ? 0.3942 0.5499 0.2978 0.0436  0.0094  0.0410  727 HOH A O   
2714 O  O   . HOH F .   ? 0.5004 0.4109 0.4673 0.0218  0.0161  0.0109  728 HOH A O   
2715 O  O   . HOH F .   ? 0.3707 0.4119 0.3655 0.0108  0.0211  0.0481  729 HOH A O   
2716 O  O   . HOH F .   ? 0.6013 0.4349 0.5916 -0.0228 0.0811  0.0508  730 HOH A O   
2717 O  O   . HOH F .   ? 0.4146 0.4260 0.3684 -0.0114 -0.0010 -0.0411 731 HOH A O   
2718 O  O   . HOH F .   ? 0.4147 0.3751 0.5764 0.1178  0.0730  0.0541  732 HOH A O   
2719 O  O   . HOH F .   ? 0.4465 0.4408 0.4502 -0.0085 -0.0117 -0.0076 733 HOH A O   
2720 O  O   . HOH F .   ? 0.3716 0.3762 0.3348 -0.0235 0.0420  0.0065  734 HOH A O   
2721 O  O   . HOH F .   ? 0.4541 0.5069 0.5621 -0.0333 0.0500  0.0408  735 HOH A O   
2722 O  O   . HOH F .   ? 0.4215 0.7069 0.3555 0.0201  -0.0595 -0.0312 736 HOH A O   
2723 O  O   . HOH F .   ? 0.3145 0.6066 0.4536 0.1165  -0.0187 0.0778  737 HOH A O   
2724 O  O   . HOH F .   ? 0.3806 0.3586 0.3750 -0.0168 -0.0118 -0.0221 738 HOH A O   
2725 O  O   . HOH F .   ? 0.4468 0.5746 0.4238 0.0311  0.0602  0.0521  739 HOH A O   
2726 O  O   . HOH F .   ? 0.3901 0.4409 0.3471 0.0028  0.0404  -0.0726 740 HOH A O   
2727 O  O   . HOH F .   ? 0.4110 0.5169 0.4687 -0.0237 0.0589  -0.0225 741 HOH A O   
2728 O  O   . HOH F .   ? 0.3994 0.3150 0.5130 0.0550  0.0542  0.0517  742 HOH A O   
2729 O  O   . HOH F .   ? 0.4720 0.5258 0.5494 -0.0314 0.0007  -0.0143 743 HOH A O   
2730 O  O   . HOH F .   ? 0.5292 0.4064 0.5080 -0.0153 0.0275  -0.0651 744 HOH A O   
2731 O  O   . HOH F .   ? 0.5150 0.8070 0.4674 0.0029  -0.0647 -0.0559 745 HOH A O   
2732 O  O   . HOH F .   ? 0.4334 0.4369 0.4778 0.0258  0.0550  -0.0845 746 HOH A O   
2733 O  O   . HOH F .   ? 0.4790 0.5408 0.5451 -0.0713 0.0784  0.0021  747 HOH A O   
2734 O  O   . HOH F .   ? 0.5835 0.4207 0.5858 -0.0413 0.0440  -0.0738 748 HOH A O   
2735 O  O   . HOH F .   ? 0.4685 0.4637 0.4423 -0.0159 -0.0079 -0.0417 749 HOH A O   
2736 O  O   . HOH F .   ? 0.4790 0.5599 0.3590 0.0504  0.0511  -0.1207 750 HOH A O   
2737 O  O   . HOH F .   ? 0.5401 0.6213 0.6764 0.1691  0.0504  0.1637  751 HOH A O   
2738 O  O   . HOH F .   ? 0.3240 0.2902 0.3065 -0.0303 0.0099  -0.0135 752 HOH A O   
2739 O  O   . HOH F .   ? 0.5197 0.7469 0.6362 0.0013  -0.0203 -0.0167 753 HOH A O   
2740 O  O   . HOH F .   ? 0.4402 0.6674 0.4788 0.1285  -0.0133 0.1401  754 HOH A O   
2741 O  O   . HOH F .   ? 0.5635 0.5752 0.5654 0.0126  0.0515  -0.1170 755 HOH A O   
2742 O  O   . HOH F .   ? 0.5821 0.5351 0.6421 -0.1050 0.0278  -0.0830 756 HOH A O   
2743 O  O   . HOH F .   ? 0.5644 0.4521 0.5302 0.0289  0.0287  0.0262  757 HOH A O   
2744 O  O   . HOH F .   ? 0.5680 0.9561 0.5220 0.0725  -0.0622 0.0357  758 HOH A O   
2745 O  O   . HOH F .   ? 0.6888 0.5591 0.7056 -0.0584 0.0820  0.0289  759 HOH A O   
2746 O  O   . HOH F .   ? 0.6676 0.5506 0.7940 -0.0106 0.0616  0.0342  760 HOH A O   
2747 O  O   . HOH F .   ? 0.4896 0.5411 0.6408 0.1842  0.0704  0.1814  761 HOH A O   
2748 O  O   . HOH F .   ? 0.4638 0.6452 0.6078 0.0531  0.0212  0.0015  762 HOH A O   
2749 O  O   . HOH F .   ? 0.5691 0.6424 0.6147 0.1298  0.0622  0.2149  763 HOH A O   
2750 O  O   . HOH F .   ? 0.4640 0.4913 0.5638 0.0518  0.0464  -0.0280 764 HOH A O   
2751 O  O   . HOH F .   ? 0.5064 0.4997 0.5760 -0.1101 0.0182  -0.0908 765 HOH A O   
2752 O  O   . HOH F .   ? 0.4423 0.5643 0.5779 0.1601  0.0327  0.1416  766 HOH A O   
2753 O  O   . HOH F .   ? 0.6303 0.7414 0.5057 0.0121  0.0324  -0.0682 767 HOH A O   
2754 O  O   . HOH F .   ? 0.3205 0.2977 0.3023 -0.0163 -0.0127 -0.0233 768 HOH A O   
2755 O  O   . HOH F .   ? 0.6137 0.7536 0.5727 0.0407  0.0691  0.0981  769 HOH A O   
2756 O  O   . HOH F .   ? 0.5087 0.3495 0.4991 -0.0224 0.0593  0.0196  770 HOH A O   
2757 O  O   . HOH F .   ? 0.6251 0.5106 0.6131 -0.0362 0.0758  0.0468  771 HOH A O   
2758 O  O   . HOH F .   ? 0.5524 0.4614 0.5232 -0.0215 0.0182  -0.0828 772 HOH A O   
2759 O  O   . HOH F .   ? 0.5164 0.4586 0.4888 0.0177  0.0034  -0.0062 773 HOH A O   
2760 O  O   . HOH F .   ? 0.4972 0.4881 0.5121 -0.0080 -0.0074 -0.0142 774 HOH A O   
2761 O  O   . HOH F .   ? 0.5256 0.5107 0.6063 0.0391  0.0516  -0.0548 775 HOH A O   
2762 O  O   . HOH F .   ? 0.5592 0.5469 0.5891 0.0010  -0.0010 -0.0086 776 HOH A O   
2763 O  O   . HOH F .   ? 0.5073 0.6080 0.4785 -0.0596 -0.0304 -0.1349 777 HOH A O   
2764 O  O   . HOH F .   ? 0.5533 0.7497 0.5378 -0.0586 -0.0492 -0.1331 778 HOH A O   
2765 O  O   . HOH F .   ? 0.5524 0.5847 0.4982 -0.0455 -0.0082 -0.1486 779 HOH A O   
2766 O  O   . HOH F .   ? 0.5746 0.7856 0.7251 -0.0398 0.0331  -0.0310 780 HOH A O   
2767 O  O   . HOH F .   ? 0.4170 0.4568 0.5002 -0.0270 0.0340  0.0282  781 HOH A O   
2768 O  O   . HOH F .   ? 0.6589 0.5671 0.6704 -0.0753 0.0230  -0.1217 782 HOH A O   
2769 O  O   . HOH F .   ? 0.5051 0.6549 0.4308 -0.0014 -0.0348 -0.0525 783 HOH A O   
2770 O  O   . HOH F .   ? 0.5089 0.6327 0.5527 0.0101  0.0714  0.0652  784 HOH A O   
2771 O  O   . HOH F .   ? 0.4397 0.4118 0.4994 -0.0912 0.0434  -0.0340 785 HOH A O   
2772 O  O   . HOH F .   ? 0.6476 0.5329 0.8537 0.1610  0.1207  0.1123  786 HOH A O   
2773 O  O   . HOH F .   ? 0.5644 0.5397 0.5933 -0.0038 0.0074  -0.0338 787 HOH A O   
2774 O  O   . HOH F .   ? 0.4403 0.7869 0.5245 0.0686  -0.0556 0.0390  788 HOH A O   
2775 O  O   . HOH F .   ? 0.4437 0.5845 0.5707 -0.1241 -0.0017 -0.1050 789 HOH A O   
2776 O  O   . HOH F .   ? 0.6727 0.8328 0.5324 0.0313  0.0088  -0.0710 790 HOH A O   
2777 O  O   . HOH F .   ? 0.4790 0.6074 0.4706 -0.0687 -0.0362 -0.1349 791 HOH A O   
2778 O  O   . HOH F .   ? 0.6432 0.6082 0.6812 0.0026  0.0271  -0.0685 792 HOH A O   
2779 O  O   . HOH F .   ? 0.4773 0.5197 0.3909 -0.0008 0.0376  0.0009  793 HOH A O   
2780 O  O   . HOH F .   ? 0.4151 0.5444 0.4251 0.0374  0.0569  0.0170  794 HOH A O   
2781 O  O   . HOH F .   ? 0.5353 0.6339 0.6418 -0.1357 -0.0022 -0.1428 795 HOH A O   
2782 O  O   . HOH F .   ? 0.5647 0.6167 0.6835 -0.0349 0.0639  0.0565  796 HOH A O   
2783 O  O   . HOH F .   ? 0.5955 0.6543 0.7340 -0.0392 0.0819  0.0737  797 HOH A O   
2784 O  O   . HOH F .   ? 0.6276 0.6989 0.5575 0.0071  0.0421  -0.1081 798 HOH A O   
2785 O  O   . HOH F .   ? 0.4626 0.6017 0.4196 0.0822  0.0261  0.1469  799 HOH A O   
2786 O  O   . HOH F .   ? 0.6362 0.4698 0.6258 -0.0103 0.0443  -0.0341 800 HOH A O   
2787 O  O   . HOH F .   ? 0.3219 0.3146 0.3198 -0.0409 0.0356  -0.0042 801 HOH A O   
2788 O  O   . HOH F .   ? 0.5384 0.5203 0.5552 -0.0070 0.0092  -0.0454 802 HOH A O   
2789 O  O   . HOH F .   ? 0.4473 0.4936 0.5368 -0.0326 0.0222  0.0094  803 HOH A O   
2790 O  O   . HOH F .   ? 0.6016 0.4691 0.6400 -0.0783 0.0655  -0.0179 804 HOH A O   
2791 O  O   . HOH F .   ? 0.5348 0.6455 0.5011 0.0385  0.0558  0.1043  805 HOH A O   
2792 O  O   . HOH F .   ? 0.6735 0.7417 0.6487 0.0222  0.0703  -0.1078 806 HOH A O   
2793 O  O   . HOH F .   ? 0.3300 0.3206 0.3650 -0.0669 0.0410  -0.0146 807 HOH A O   
2794 O  O   . HOH F .   ? 0.7121 0.6882 0.7294 -0.0067 0.0164  -0.0673 808 HOH A O   
2795 O  O   . HOH F .   ? 0.4458 0.7706 0.5177 0.1057  -0.0435 0.0843  809 HOH A O   
2796 O  O   . HOH F .   ? 0.4694 0.6417 0.3345 0.0355  0.0058  -0.0380 810 HOH A O   
2797 O  O   . HOH F .   ? 0.5655 0.5954 0.5918 0.0505  0.0644  0.1541  811 HOH A O   
2798 O  O   . HOH F .   ? 0.4962 0.7010 0.4156 0.0165  -0.0417 -0.0267 812 HOH A O   
2799 O  O   . HOH F .   ? 0.6209 0.7970 0.5252 0.0537  0.0036  0.0620  813 HOH A O   
2800 O  O   . HOH F .   ? 0.5546 0.6922 0.5251 0.1016  0.0421  0.1859  814 HOH A O   
2801 O  O   . HOH F .   ? 0.4753 0.4170 0.5588 0.0308  0.0318  0.0157  815 HOH A O   
2802 O  O   . HOH F .   ? 0.4506 0.4468 0.4254 -0.0148 -0.0008 -0.0426 816 HOH A O   
2803 O  O   . HOH F .   ? 0.6349 0.8768 0.5590 0.0126  -0.0527 -0.0391 817 HOH A O   
2804 O  O   . HOH F .   ? 0.5181 0.4948 0.5795 0.0086  0.0498  0.0871  818 HOH A O   
2805 O  O   . HOH F .   ? 0.5171 0.6548 0.4288 -0.0122 -0.0294 -0.0932 819 HOH A O   
2806 O  O   . HOH F .   ? 0.4734 0.6470 0.3486 0.0475  0.0260  0.0040  820 HOH A O   
2807 O  O   . HOH F .   ? 0.6503 0.7555 0.5371 0.0644  0.0621  -0.0946 821 HOH A O   
2808 O  O   . HOH F .   ? 0.5490 0.4639 0.5403 0.0777  0.0369  0.0051  822 HOH A O   
2809 O  O   . HOH F .   ? 0.3940 0.5178 0.4020 0.0274  0.0569  0.0323  823 HOH A O   
2810 O  O   . HOH F .   ? 0.6140 0.5275 0.7403 0.0916  0.0992  0.1754  824 HOH A O   
2811 O  O   . HOH F .   ? 0.4845 0.6824 0.3954 0.0717  0.0022  0.0965  825 HOH A O   
2812 O  O   . HOH F .   ? 0.5572 0.5363 0.5517 -0.0181 -0.0109 -0.0318 826 HOH A O   
2813 O  O   . HOH F .   ? 0.5511 0.4694 0.5219 0.0217  0.0125  -0.0003 827 HOH A O   
2814 O  O   . HOH F .   ? 0.4240 0.6067 0.5030 0.0617  0.0578  0.0100  828 HOH A O   
2815 O  O   . HOH F .   ? 0.5918 1.0021 0.5162 0.1012  -0.0481 0.0731  829 HOH A O   
2816 O  O   . HOH F .   ? 0.6998 0.5212 0.7150 -0.0472 0.0848  0.0260  830 HOH A O   
2817 O  O   . HOH F .   ? 0.4966 0.6035 0.4651 0.0666  0.0334  0.1361  831 HOH A O   
2818 O  O   . HOH F .   ? 0.5692 0.4991 0.6586 0.0205  0.0565  0.0865  832 HOH A O   
2819 O  O   . HOH F .   ? 0.4956 0.4616 0.4708 0.0042  -0.0077 -0.0120 833 HOH A O   
2820 O  O   . HOH F .   ? 0.5905 0.8508 0.6454 -0.0839 -0.0547 -0.1378 834 HOH A O   
2821 O  O   . HOH F .   ? 0.6391 0.8223 0.5584 0.0549  0.0720  0.0787  835 HOH A O   
2822 O  O   . HOH F .   ? 0.4885 0.5821 0.5024 -0.0135 0.0703  -0.0228 836 HOH A O   
2823 O  O   . HOH F .   ? 0.5807 0.7886 0.4484 0.0596  0.0230  0.0464  837 HOH A O   
2824 O  O   . HOH F .   ? 0.4280 0.5243 0.4663 -0.0102 0.0609  -0.0297 838 HOH A O   
2825 O  O   . HOH F .   ? 0.7423 0.8240 0.6814 -0.0470 -0.0178 -0.1581 839 HOH A O   
2826 O  O   . HOH F .   ? 0.5038 0.7008 0.3838 0.0598  0.0473  0.0536  840 HOH A O   
2827 O  O   . HOH F .   ? 0.5298 0.5972 0.4772 0.0090  0.0507  -0.0873 841 HOH A O   
2828 O  O   . HOH F .   ? 0.4970 0.5798 0.3922 0.0072  0.0453  -0.0240 842 HOH A O   
2829 O  O   . HOH F .   ? 0.6292 0.7130 0.7886 -0.0487 0.0776  0.0576  843 HOH A O   
2830 O  O   . HOH F .   ? 0.5116 0.6576 0.4608 -0.0441 -0.0384 -0.1285 844 HOH A O   
2831 O  O   . HOH F .   ? 0.4171 0.7511 0.5346 0.1039  -0.0377 0.0708  845 HOH A O   
2832 O  O   . HOH F .   ? 0.6288 0.6059 0.6323 -0.0161 -0.0040 -0.0387 846 HOH A O   
2833 O  O   . HOH F .   ? 0.5335 0.4935 0.5973 -0.1023 0.0331  -0.0647 847 HOH A O   
2834 O  O   . HOH F .   ? 0.5110 0.4247 0.6117 -0.0051 0.0496  0.0442  848 HOH A O   
2835 O  O   . HOH F .   ? 0.6150 0.7509 0.5618 0.0705  0.0329  0.1357  849 HOH A O   
2836 O  O   . HOH F .   ? 0.4936 0.5708 0.3913 0.0038  0.0111  -0.0533 850 HOH A O   
2837 O  O   . HOH F .   ? 0.6430 0.5156 0.6160 -0.0032 0.0358  -0.0837 851 HOH A O   
2838 O  O   . HOH F .   ? 0.5084 0.5182 0.5061 -0.0430 0.0617  0.0129  852 HOH A O   
2839 O  O   . HOH F .   ? 0.6070 0.7266 0.5859 0.0343  0.0703  0.1071  853 HOH A O   
2840 O  O   . HOH F .   ? 0.5797 0.7834 0.4632 0.0684  0.0384  0.0937  854 HOH A O   
2841 O  O   . HOH F .   ? 0.5767 0.6038 0.4822 -0.0062 0.0156  -0.1548 855 HOH A O   
2842 O  O   . HOH F .   ? 0.4646 0.4380 0.4584 -0.0438 0.0478  0.0095  856 HOH A O   
2843 O  O   . HOH F .   ? 0.6208 0.5982 0.6823 0.0253  0.0599  0.1160  857 HOH A O   
2844 O  O   . HOH F .   ? 0.4475 0.5181 0.3783 -0.0026 0.0583  -0.0159 858 HOH A O   
2845 O  O   . HOH F .   ? 0.4635 0.6870 0.3866 0.1003  0.0099  0.1439  859 HOH A O   
2846 O  O   . HOH F .   ? 0.5674 0.8231 0.7140 -0.0125 -0.0098 -0.0263 860 HOH A O   
2847 O  O   . HOH F .   ? 0.6113 0.6534 0.5710 0.0056  0.0439  -0.1315 861 HOH A O   
2848 O  O   . HOH F .   ? 0.7041 0.7978 0.6540 -0.0526 -0.0238 -0.1520 862 HOH A O   
2849 O  O   . HOH F .   ? 0.4645 0.8084 0.5388 0.0166  -0.0659 -0.0157 863 HOH A O   
2850 O  O   . HOH F .   ? 0.4688 0.7101 0.5098 -0.0570 -0.0568 -0.0966 864 HOH A O   
2851 O  O   . HOH F .   ? 0.4142 0.3584 0.4951 -0.0206 0.0305  0.0200  865 HOH A O   
2852 O  O   . HOH F .   ? 0.4682 0.4280 0.5385 -0.0131 0.0325  0.0384  866 HOH A O   
2853 O  O   . HOH F .   ? 0.5503 0.7387 0.5131 -0.0501 -0.0465 -0.1349 867 HOH A O   
2854 O  O   . HOH F .   ? 0.6059 0.8088 0.5133 0.0033  -0.0420 -0.0629 868 HOH A O   
2855 O  O   . HOH F .   ? 0.3767 0.6376 0.5672 0.1868  0.0218  0.1248  869 HOH A O   
2856 O  O   . HOH F .   ? 0.5912 0.9073 0.7328 -0.0238 -0.0385 -0.0412 870 HOH A O   
2857 O  O   . HOH F .   ? 0.6254 0.8396 0.4809 0.0590  0.0274  0.0244  871 HOH A O   
2858 O  O   . HOH F .   ? 0.5952 0.6832 0.5362 0.0115  0.0629  -0.0724 872 HOH A O   
2859 O  O   . HOH F .   ? 0.5996 0.5401 0.6834 0.0141  0.0556  0.0868  873 HOH A O   
2860 O  O   . HOH F .   ? 0.6366 0.5771 0.5774 -0.0082 0.0295  -0.1407 874 HOH A O   
2861 O  O   . HOH F .   ? 0.7049 0.6804 0.6292 -0.0101 0.0257  -0.1604 875 HOH A O   
2862 O  O   . HOH F .   ? 0.5680 0.9590 0.6365 0.0185  -0.0737 -0.0216 876 HOH A O   
2863 O  O   . HOH F .   ? 0.6515 0.7595 0.6387 0.0973  0.0625  0.2020  877 HOH A O   
2864 O  O   . HOH F .   ? 0.5234 0.9072 0.6541 0.0898  -0.0469 0.0514  878 HOH A O   
2865 O  O   . HOH G .   ? 0.5064 0.4744 0.5939 -0.0578 0.0053  -0.0803 101 HOH C O   
2866 O  O   . HOH G .   ? 0.3526 0.3717 0.3736 -0.0379 -0.0201 -0.0785 102 HOH C O   
2867 O  O   . HOH G .   ? 0.5994 0.4807 0.7114 -0.0213 0.0446  -0.0438 103 HOH C O   
2868 O  O   . HOH G .   ? 0.5109 0.4247 0.6119 -0.0251 0.0367  -0.0004 104 HOH C O   
2869 O  O   . HOH G .   ? 0.4199 0.4012 0.4252 -0.0132 -0.0098 -0.0170 105 HOH C O   
2870 O  O   . HOH G .   ? 0.4627 0.4097 0.5069 -0.0136 0.0102  -0.0401 106 HOH C O   
2871 O  O   . HOH G .   ? 0.5688 0.5445 0.5870 -0.0269 -0.0041 -0.0661 107 HOH C O   
2872 O  O   . HOH G .   ? 0.4476 0.4225 0.5124 -0.0369 0.0045  -0.0259 108 HOH C O   
2873 O  O   . HOH G .   ? 0.5929 0.5668 0.6072 -0.0230 -0.0061 -0.0491 109 HOH C O   
2874 O  O   . HOH G .   ? 0.5966 0.5351 0.6619 0.0065  0.0217  -0.0108 110 HOH C O   
2875 O  O   . HOH G .   ? 0.7359 0.7187 0.7617 -0.0368 0.0011  -0.1116 111 HOH C O   
2876 O  O   . HOH G .   ? 0.5658 0.5672 0.6244 -0.0563 -0.0091 -0.1066 112 HOH C O   
2877 O  O   . HOH G .   ? 0.4759 0.4908 0.5223 -0.0455 -0.0166 -0.0742 113 HOH C O   
2878 O  O   . HOH G .   ? 0.3845 0.3724 0.4280 -0.0311 -0.0055 -0.0278 114 HOH C O   
2879 O  O   . HOH G .   ? 0.4624 0.4677 0.5344 -0.0588 -0.0093 -0.0915 115 HOH C O   
2880 O  O   . HOH G .   ? 0.7507 0.7485 0.7938 -0.0528 -0.0029 -0.1363 116 HOH C O   
# 
