data_9H1M
# 
_entry.id   9H1M 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.403 
_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   9H1M         pdb_00009h1m 10.2210/pdb9h1m/pdb 
WWPDB D_1292142090 ?            ?                   
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
_pdbx_audit_revision_history.part_number 
1 'Structure model' 1 0 2025-03-19 ? 
2 'Structure model' 1 1 2025-04-16 ? 
# 
_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_audit_revision_group.ordinal             1 
_pdbx_audit_revision_group.revision_ordinal    2 
_pdbx_audit_revision_group.data_content_type   'Structure model' 
_pdbx_audit_revision_group.group               'Database references' 
# 
_pdbx_audit_revision_category.ordinal             1 
_pdbx_audit_revision_category.revision_ordinal    2 
_pdbx_audit_revision_category.data_content_type   'Structure model' 
_pdbx_audit_revision_category.category            citation 
# 
loop_
_pdbx_audit_revision_item.ordinal 
_pdbx_audit_revision_item.revision_ordinal 
_pdbx_audit_revision_item.data_content_type 
_pdbx_audit_revision_item.item 
1 2 'Structure model' '_citation.journal_volume' 
2 2 'Structure model' '_citation.page_first'     
3 2 'Structure model' '_citation.page_last'      
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9H1M 
_pdbx_database_status.recvd_initial_deposition_date   2024-10-09 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBE 
_pdbx_database_status.process_site                    PDBE 
_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                 4 
_pdbx_contact_author.email              emma.raven@bristol.ac.uk 
_pdbx_contact_author.name_first         'Emma L.' 
_pdbx_contact_author.name_last          Raven 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-1643-8694 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Nesa, M.L.'    1 0000-0001-9403-9798 
'Mandal, S.K.'  2 0000-0002-7753-9974 
'Toelzer, C.'   3 0000-0001-9984-5940 
'Humer, D.'     4 0000-0003-0259-9697 
'Moody, P.C.E.' 5 0000-0003-1762-9238 
'Berger, I.'    6 0000-0001-7518-9045 
'Spadiut, O.'   7 0000-0003-0916-0644 
'Raven, E.L.'   8 0000-0002-1643-8694 
# 
_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                   GW 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            J.Biol.Inorg.Chem. 
_citation.journal_id_ASTM           JJBCFA 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           1432-1327 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            30 
_citation.language                  ? 
_citation.page_first                221 
_citation.page_last                 227 
_citation.title                     'Crystal structure of ferric recombinant horseradish peroxidase.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1007/s00775-025-02103-2 
_citation.pdbx_database_id_PubMed   40053124 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Nesa, M.L.'    1 ? 
primary 'Mandal, S.K.'  2 ? 
primary 'Toelzer, C.'   3 ? 
primary 'Humer, D.'     4 ? 
primary 'Moody, P.C.E.' 5 ? 
primary 'Berger, I.'    6 ? 
primary 'Spadiut, O.'   7 ? 
primary 'Raven, E.L.'   8 ? 
# 
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 'Peroxidase C1A'                  34079.344 1   1.11.1.7 ? ? ? 
2 non-polymer syn 'PROTOPORPHYRIN IX CONTAINING FE' 616.487   1   ?        ? ? ? 
3 non-polymer syn 'CALCIUM ION'                     40.078    2   ?        ? ? ? 
4 non-polymer syn 1,2-ETHANEDIOL                    62.068    5   ?        ? ? ? 
5 non-polymer syn 'DIHYDROGENPHOSPHATE ION'         96.987    1   ?        ? ? ? 
6 water       nat water                             18.015    140 ?        ? ? ? 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;MQLTPTFYDNSCPNVSNIVRDTIVNELRSDPRIAASILRLHFHDCFVNGCDASILLDNTTSFRTEKDAFGNANSARGFPV
IDRMKAAVESACPRTVSCADLLTIAAQQSVTLAGGPSWRVPLGRRDSLQAFLDLANANLPAPFFTLPQLKDSFRNVGLNR
SSDLVALSGGHTFGKNQCRFIMDRLYNFSNTGLPDPTLNTTYLQTLRGLCPLNGNLSALVDFDLRTPTIFDNKYYVNLEE
QKGLIQSDQELFSSPNATDTIPLVRSFANSTQTFFNAFVEAMDRMGNITPLTGTQGQIRLNCRVVNSNS
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MQLTPTFYDNSCPNVSNIVRDTIVNELRSDPRIAASILRLHFHDCFVNGCDASILLDNTTSFRTEKDAFGNANSARGFPV
IDRMKAAVESACPRTVSCADLLTIAAQQSVTLAGGPSWRVPLGRRDSLQAFLDLANANLPAPFFTLPQLKDSFRNVGLNR
SSDLVALSGGHTFGKNQCRFIMDRLYNFSNTGLPDPTLNTTYLQTLRGLCPLNGNLSALVDFDLRTPTIFDNKYYVNLEE
QKGLIQSDQELFSSPNATDTIPLVRSFANSTQTFFNAFVEAMDRMGNITPLTGTQGQIRLNCRVVNSNS
;
_entity_poly.pdbx_strand_id                 A 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'PROTOPORPHYRIN IX CONTAINING FE' HEM 
3 'CALCIUM ION'                     CA  
4 1,2-ETHANEDIOL                    EDO 
5 'DIHYDROGENPHOSPHATE ION'         2HP 
6 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   GLN n 
1 3   LEU n 
1 4   THR n 
1 5   PRO n 
1 6   THR n 
1 7   PHE n 
1 8   TYR n 
1 9   ASP n 
1 10  ASN n 
1 11  SER n 
1 12  CYS n 
1 13  PRO n 
1 14  ASN n 
1 15  VAL n 
1 16  SER n 
1 17  ASN n 
1 18  ILE n 
1 19  VAL n 
1 20  ARG n 
1 21  ASP n 
1 22  THR n 
1 23  ILE n 
1 24  VAL n 
1 25  ASN n 
1 26  GLU n 
1 27  LEU n 
1 28  ARG n 
1 29  SER n 
1 30  ASP n 
1 31  PRO n 
1 32  ARG n 
1 33  ILE n 
1 34  ALA n 
1 35  ALA n 
1 36  SER n 
1 37  ILE n 
1 38  LEU n 
1 39  ARG n 
1 40  LEU n 
1 41  HIS n 
1 42  PHE n 
1 43  HIS n 
1 44  ASP n 
1 45  CYS n 
1 46  PHE n 
1 47  VAL n 
1 48  ASN n 
1 49  GLY n 
1 50  CYS n 
1 51  ASP n 
1 52  ALA n 
1 53  SER n 
1 54  ILE n 
1 55  LEU n 
1 56  LEU n 
1 57  ASP n 
1 58  ASN n 
1 59  THR n 
1 60  THR n 
1 61  SER n 
1 62  PHE n 
1 63  ARG n 
1 64  THR n 
1 65  GLU n 
1 66  LYS n 
1 67  ASP n 
1 68  ALA n 
1 69  PHE n 
1 70  GLY n 
1 71  ASN n 
1 72  ALA n 
1 73  ASN n 
1 74  SER n 
1 75  ALA n 
1 76  ARG n 
1 77  GLY n 
1 78  PHE n 
1 79  PRO n 
1 80  VAL n 
1 81  ILE n 
1 82  ASP n 
1 83  ARG n 
1 84  MET n 
1 85  LYS n 
1 86  ALA n 
1 87  ALA n 
1 88  VAL n 
1 89  GLU n 
1 90  SER n 
1 91  ALA n 
1 92  CYS n 
1 93  PRO n 
1 94  ARG n 
1 95  THR n 
1 96  VAL n 
1 97  SER n 
1 98  CYS n 
1 99  ALA n 
1 100 ASP n 
1 101 LEU n 
1 102 LEU n 
1 103 THR n 
1 104 ILE n 
1 105 ALA n 
1 106 ALA n 
1 107 GLN n 
1 108 GLN n 
1 109 SER n 
1 110 VAL n 
1 111 THR n 
1 112 LEU n 
1 113 ALA n 
1 114 GLY n 
1 115 GLY n 
1 116 PRO n 
1 117 SER n 
1 118 TRP n 
1 119 ARG n 
1 120 VAL n 
1 121 PRO n 
1 122 LEU n 
1 123 GLY n 
1 124 ARG n 
1 125 ARG n 
1 126 ASP n 
1 127 SER n 
1 128 LEU n 
1 129 GLN n 
1 130 ALA n 
1 131 PHE n 
1 132 LEU n 
1 133 ASP n 
1 134 LEU n 
1 135 ALA n 
1 136 ASN n 
1 137 ALA n 
1 138 ASN n 
1 139 LEU n 
1 140 PRO n 
1 141 ALA n 
1 142 PRO n 
1 143 PHE n 
1 144 PHE n 
1 145 THR n 
1 146 LEU n 
1 147 PRO n 
1 148 GLN n 
1 149 LEU n 
1 150 LYS n 
1 151 ASP n 
1 152 SER n 
1 153 PHE n 
1 154 ARG n 
1 155 ASN n 
1 156 VAL n 
1 157 GLY n 
1 158 LEU n 
1 159 ASN n 
1 160 ARG n 
1 161 SER n 
1 162 SER n 
1 163 ASP n 
1 164 LEU n 
1 165 VAL n 
1 166 ALA n 
1 167 LEU n 
1 168 SER n 
1 169 GLY n 
1 170 GLY n 
1 171 HIS n 
1 172 THR n 
1 173 PHE n 
1 174 GLY n 
1 175 LYS n 
1 176 ASN n 
1 177 GLN n 
1 178 CYS n 
1 179 ARG n 
1 180 PHE n 
1 181 ILE n 
1 182 MET n 
1 183 ASP n 
1 184 ARG n 
1 185 LEU n 
1 186 TYR n 
1 187 ASN n 
1 188 PHE n 
1 189 SER n 
1 190 ASN n 
1 191 THR n 
1 192 GLY n 
1 193 LEU n 
1 194 PRO n 
1 195 ASP n 
1 196 PRO n 
1 197 THR n 
1 198 LEU n 
1 199 ASN n 
1 200 THR n 
1 201 THR n 
1 202 TYR n 
1 203 LEU n 
1 204 GLN n 
1 205 THR n 
1 206 LEU n 
1 207 ARG n 
1 208 GLY n 
1 209 LEU n 
1 210 CYS n 
1 211 PRO n 
1 212 LEU n 
1 213 ASN n 
1 214 GLY n 
1 215 ASN n 
1 216 LEU n 
1 217 SER n 
1 218 ALA n 
1 219 LEU n 
1 220 VAL n 
1 221 ASP n 
1 222 PHE n 
1 223 ASP n 
1 224 LEU n 
1 225 ARG n 
1 226 THR n 
1 227 PRO n 
1 228 THR n 
1 229 ILE n 
1 230 PHE n 
1 231 ASP n 
1 232 ASN n 
1 233 LYS n 
1 234 TYR n 
1 235 TYR n 
1 236 VAL n 
1 237 ASN n 
1 238 LEU n 
1 239 GLU n 
1 240 GLU n 
1 241 GLN n 
1 242 LYS n 
1 243 GLY n 
1 244 LEU n 
1 245 ILE n 
1 246 GLN n 
1 247 SER n 
1 248 ASP n 
1 249 GLN n 
1 250 GLU n 
1 251 LEU n 
1 252 PHE n 
1 253 SER n 
1 254 SER n 
1 255 PRO n 
1 256 ASN n 
1 257 ALA n 
1 258 THR n 
1 259 ASP n 
1 260 THR n 
1 261 ILE n 
1 262 PRO n 
1 263 LEU n 
1 264 VAL n 
1 265 ARG n 
1 266 SER n 
1 267 PHE n 
1 268 ALA n 
1 269 ASN n 
1 270 SER n 
1 271 THR n 
1 272 GLN n 
1 273 THR n 
1 274 PHE n 
1 275 PHE n 
1 276 ASN n 
1 277 ALA n 
1 278 PHE n 
1 279 VAL n 
1 280 GLU n 
1 281 ALA n 
1 282 MET n 
1 283 ASP n 
1 284 ARG n 
1 285 MET n 
1 286 GLY n 
1 287 ASN n 
1 288 ILE n 
1 289 THR n 
1 290 PRO n 
1 291 LEU n 
1 292 THR n 
1 293 GLY n 
1 294 THR n 
1 295 GLN n 
1 296 GLY n 
1 297 GLN n 
1 298 ILE n 
1 299 ARG n 
1 300 LEU n 
1 301 ASN n 
1 302 CYS n 
1 303 ARG n 
1 304 VAL n 
1 305 VAL n 
1 306 ASN n 
1 307 SER n 
1 308 ASN n 
1 309 SER 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                   309 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'PRXC1A, HPRC1' 
_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      'Armoracia rusticana' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     3704 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli BL21(DE3)' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     469008 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
2HP non-polymer         . 'DIHYDROGENPHOSPHATE ION'         ?                 'H2 O4 P -1'       96.987  
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 
CA  non-polymer         . 'CALCIUM ION'                     ?                 'Ca 2'             40.078  
CYS 'L-peptide linking' y CYSTEINE                          ?                 'C3 H7 N O2 S'     121.158 
EDO non-polymer         . 1,2-ETHANEDIOL                    'ETHYLENE GLYCOL' 'C2 H6 O2'         62.068  
GLN 'L-peptide linking' y GLUTAMINE                         ?                 'C5 H10 N2 O3'     146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'                   ?                 'C5 H9 N O4'       147.129 
GLY 'peptide linking'   y GLYCINE                           ?                 'C2 H5 N O2'       75.067  
HEM non-polymer         . 'PROTOPORPHYRIN IX CONTAINING FE' HEME              'C34 H32 Fe N4 O4' 616.487 
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   0   ?   ?   ?   A . n 
A 1 2   GLN 2   1   1   GLN GLN A . n 
A 1 3   LEU 3   2   2   LEU LEU A . n 
A 1 4   THR 4   3   3   THR THR A . n 
A 1 5   PRO 5   4   4   PRO PRO A . n 
A 1 6   THR 6   5   5   THR THR A . n 
A 1 7   PHE 7   6   6   PHE PHE A . n 
A 1 8   TYR 8   7   7   TYR TYR A . n 
A 1 9   ASP 9   8   8   ASP ASP A . n 
A 1 10  ASN 10  9   9   ASN ASN A . n 
A 1 11  SER 11  10  10  SER SER A . n 
A 1 12  CYS 12  11  11  CYS CYS A . n 
A 1 13  PRO 13  12  12  PRO PRO A . n 
A 1 14  ASN 14  13  13  ASN ASN A . n 
A 1 15  VAL 15  14  14  VAL VAL A . n 
A 1 16  SER 16  15  15  SER SER A . n 
A 1 17  ASN 17  16  16  ASN ASN A . n 
A 1 18  ILE 18  17  17  ILE ILE A . n 
A 1 19  VAL 19  18  18  VAL VAL A . n 
A 1 20  ARG 20  19  19  ARG ARG A . n 
A 1 21  ASP 21  20  20  ASP ASP A . n 
A 1 22  THR 22  21  21  THR THR A . n 
A 1 23  ILE 23  22  22  ILE ILE A . n 
A 1 24  VAL 24  23  23  VAL VAL A . n 
A 1 25  ASN 25  24  24  ASN ASN A . n 
A 1 26  GLU 26  25  25  GLU GLU A . n 
A 1 27  LEU 27  26  26  LEU LEU A . n 
A 1 28  ARG 28  27  27  ARG ARG A . n 
A 1 29  SER 29  28  28  SER SER A . n 
A 1 30  ASP 30  29  29  ASP ASP A . n 
A 1 31  PRO 31  30  30  PRO PRO A . n 
A 1 32  ARG 32  31  31  ARG ARG A . n 
A 1 33  ILE 33  32  32  ILE ILE A . n 
A 1 34  ALA 34  33  33  ALA ALA A . n 
A 1 35  ALA 35  34  34  ALA ALA A . n 
A 1 36  SER 36  35  35  SER SER A . n 
A 1 37  ILE 37  36  36  ILE ILE A . n 
A 1 38  LEU 38  37  37  LEU LEU A . n 
A 1 39  ARG 39  38  38  ARG ARG A . n 
A 1 40  LEU 40  39  39  LEU LEU A . n 
A 1 41  HIS 41  40  40  HIS HIS A . n 
A 1 42  PHE 42  41  41  PHE PHE A . n 
A 1 43  HIS 43  42  42  HIS HIS A . n 
A 1 44  ASP 44  43  43  ASP ASP A . n 
A 1 45  CYS 45  44  44  CYS CYS A . n 
A 1 46  PHE 46  45  45  PHE PHE A . n 
A 1 47  VAL 47  46  46  VAL VAL A . n 
A 1 48  ASN 48  47  47  ASN ASN A . n 
A 1 49  GLY 49  48  48  GLY GLY A . n 
A 1 50  CYS 50  49  49  CYS CYS A . n 
A 1 51  ASP 51  50  50  ASP ASP A . n 
A 1 52  ALA 52  51  51  ALA ALA A . n 
A 1 53  SER 53  52  52  SER SER A . n 
A 1 54  ILE 54  53  53  ILE ILE A . n 
A 1 55  LEU 55  54  54  LEU LEU A . n 
A 1 56  LEU 56  55  55  LEU LEU A . n 
A 1 57  ASP 57  56  56  ASP ASP A . n 
A 1 58  ASN 58  57  57  ASN ASN A . n 
A 1 59  THR 59  58  58  THR THR A . n 
A 1 60  THR 60  59  59  THR THR A . n 
A 1 61  SER 61  60  60  SER SER A . n 
A 1 62  PHE 62  61  61  PHE PHE A . n 
A 1 63  ARG 63  62  62  ARG ARG A . n 
A 1 64  THR 64  63  63  THR THR A . n 
A 1 65  GLU 65  64  64  GLU GLU A . n 
A 1 66  LYS 66  65  65  LYS LYS A . n 
A 1 67  ASP 67  66  66  ASP ASP A . n 
A 1 68  ALA 68  67  67  ALA ALA A . n 
A 1 69  PHE 69  68  68  PHE PHE A . n 
A 1 70  GLY 70  69  69  GLY GLY A . n 
A 1 71  ASN 71  70  70  ASN ASN A . n 
A 1 72  ALA 72  71  71  ALA ALA A . n 
A 1 73  ASN 73  72  72  ASN ASN A . n 
A 1 74  SER 74  73  73  SER SER A . n 
A 1 75  ALA 75  74  74  ALA ALA A . n 
A 1 76  ARG 76  75  75  ARG ARG A . n 
A 1 77  GLY 77  76  76  GLY GLY A . n 
A 1 78  PHE 78  77  77  PHE PHE A . n 
A 1 79  PRO 79  78  78  PRO PRO A . n 
A 1 80  VAL 80  79  79  VAL VAL A . n 
A 1 81  ILE 81  80  80  ILE ILE A . n 
A 1 82  ASP 82  81  81  ASP ASP A . n 
A 1 83  ARG 83  82  82  ARG ARG A . n 
A 1 84  MET 84  83  83  MET MET A . n 
A 1 85  LYS 85  84  84  LYS LYS A . n 
A 1 86  ALA 86  85  85  ALA ALA A . n 
A 1 87  ALA 87  86  86  ALA ALA A . n 
A 1 88  VAL 88  87  87  VAL VAL A . n 
A 1 89  GLU 89  88  88  GLU GLU A . n 
A 1 90  SER 90  89  89  SER SER A . n 
A 1 91  ALA 91  90  90  ALA ALA A . n 
A 1 92  CYS 92  91  91  CYS CYS A . n 
A 1 93  PRO 93  92  92  PRO PRO A . n 
A 1 94  ARG 94  93  93  ARG ARG A . n 
A 1 95  THR 95  94  94  THR THR A . n 
A 1 96  VAL 96  95  95  VAL VAL A . n 
A 1 97  SER 97  96  96  SER SER A . n 
A 1 98  CYS 98  97  97  CYS CYS A . n 
A 1 99  ALA 99  98  98  ALA ALA A . n 
A 1 100 ASP 100 99  99  ASP ASP A . n 
A 1 101 LEU 101 100 100 LEU LEU A . n 
A 1 102 LEU 102 101 101 LEU LEU A . n 
A 1 103 THR 103 102 102 THR THR A . n 
A 1 104 ILE 104 103 103 ILE ILE A . n 
A 1 105 ALA 105 104 104 ALA ALA A . n 
A 1 106 ALA 106 105 105 ALA ALA A . n 
A 1 107 GLN 107 106 106 GLN GLN A . n 
A 1 108 GLN 108 107 107 GLN GLN A . n 
A 1 109 SER 109 108 108 SER SER A . n 
A 1 110 VAL 110 109 109 VAL VAL A . n 
A 1 111 THR 111 110 110 THR THR A . n 
A 1 112 LEU 112 111 111 LEU LEU A . n 
A 1 113 ALA 113 112 112 ALA ALA A . n 
A 1 114 GLY 114 113 113 GLY GLY A . n 
A 1 115 GLY 115 114 114 GLY GLY A . n 
A 1 116 PRO 116 115 115 PRO PRO A . n 
A 1 117 SER 117 116 116 SER SER A . n 
A 1 118 TRP 118 117 117 TRP TRP A . n 
A 1 119 ARG 119 118 118 ARG ARG A . n 
A 1 120 VAL 120 119 119 VAL VAL A . n 
A 1 121 PRO 121 120 120 PRO PRO A . n 
A 1 122 LEU 122 121 121 LEU LEU A . n 
A 1 123 GLY 123 122 122 GLY GLY A . n 
A 1 124 ARG 124 123 123 ARG ARG A . n 
A 1 125 ARG 125 124 124 ARG ARG A . n 
A 1 126 ASP 126 125 125 ASP ASP A . n 
A 1 127 SER 127 126 126 SER SER A . n 
A 1 128 LEU 128 127 127 LEU LEU A . n 
A 1 129 GLN 129 128 128 GLN GLN A . n 
A 1 130 ALA 130 129 129 ALA ALA A . n 
A 1 131 PHE 131 130 130 PHE PHE A . n 
A 1 132 LEU 132 131 131 LEU LEU A . n 
A 1 133 ASP 133 132 132 ASP ASP A . n 
A 1 134 LEU 134 133 133 LEU LEU A . n 
A 1 135 ALA 135 134 134 ALA ALA A . n 
A 1 136 ASN 136 135 135 ASN ASN A . n 
A 1 137 ALA 137 136 136 ALA ALA A . n 
A 1 138 ASN 138 137 137 ASN ASN A . n 
A 1 139 LEU 139 138 138 LEU LEU A . n 
A 1 140 PRO 140 139 139 PRO PRO A . n 
A 1 141 ALA 141 140 140 ALA ALA A . n 
A 1 142 PRO 142 141 141 PRO PRO A . n 
A 1 143 PHE 143 142 142 PHE PHE A . n 
A 1 144 PHE 144 143 143 PHE PHE A . n 
A 1 145 THR 145 144 144 THR THR A . n 
A 1 146 LEU 146 145 145 LEU LEU A . n 
A 1 147 PRO 147 146 146 PRO PRO A . n 
A 1 148 GLN 148 147 147 GLN GLN A . n 
A 1 149 LEU 149 148 148 LEU LEU A . n 
A 1 150 LYS 150 149 149 LYS LYS A . n 
A 1 151 ASP 151 150 150 ASP ASP A . n 
A 1 152 SER 152 151 151 SER SER A . n 
A 1 153 PHE 153 152 152 PHE PHE A . n 
A 1 154 ARG 154 153 153 ARG ARG A . n 
A 1 155 ASN 155 154 154 ASN ASN A . n 
A 1 156 VAL 156 155 155 VAL VAL A . n 
A 1 157 GLY 157 156 156 GLY GLY A . n 
A 1 158 LEU 158 157 157 LEU LEU A . n 
A 1 159 ASN 159 158 158 ASN ASN A . n 
A 1 160 ARG 160 159 159 ARG ARG A . n 
A 1 161 SER 161 160 160 SER SER A . n 
A 1 162 SER 162 161 161 SER SER A . n 
A 1 163 ASP 163 162 162 ASP ASP A . n 
A 1 164 LEU 164 163 163 LEU LEU A . n 
A 1 165 VAL 165 164 164 VAL VAL A . n 
A 1 166 ALA 166 165 165 ALA ALA A . n 
A 1 167 LEU 167 166 166 LEU LEU A . n 
A 1 168 SER 168 167 167 SER SER A . n 
A 1 169 GLY 169 168 168 GLY GLY A . n 
A 1 170 GLY 170 169 169 GLY GLY A . n 
A 1 171 HIS 171 170 170 HIS HIS A . n 
A 1 172 THR 172 171 171 THR THR A . n 
A 1 173 PHE 173 172 172 PHE PHE A . n 
A 1 174 GLY 174 173 173 GLY GLY A . n 
A 1 175 LYS 175 174 174 LYS LYS A . n 
A 1 176 ASN 176 175 175 ASN ASN A . n 
A 1 177 GLN 177 176 176 GLN GLN A . n 
A 1 178 CYS 178 177 177 CYS CYS A . n 
A 1 179 ARG 179 178 178 ARG ARG A . n 
A 1 180 PHE 180 179 179 PHE PHE A . n 
A 1 181 ILE 181 180 180 ILE ILE A . n 
A 1 182 MET 182 181 181 MET MET A . n 
A 1 183 ASP 183 182 182 ASP ASP A . n 
A 1 184 ARG 184 183 183 ARG ARG A . n 
A 1 185 LEU 185 184 184 LEU LEU A . n 
A 1 186 TYR 186 185 185 TYR TYR A . n 
A 1 187 ASN 187 186 186 ASN ASN A . n 
A 1 188 PHE 188 187 187 PHE PHE A . n 
A 1 189 SER 189 188 188 SER SER A . n 
A 1 190 ASN 190 189 189 ASN ASN A . n 
A 1 191 THR 191 190 190 THR THR A . n 
A 1 192 GLY 192 191 191 GLY GLY A . n 
A 1 193 LEU 193 192 192 LEU LEU A . n 
A 1 194 PRO 194 193 193 PRO PRO A . n 
A 1 195 ASP 195 194 194 ASP ASP A . n 
A 1 196 PRO 196 195 195 PRO PRO A . n 
A 1 197 THR 197 196 196 THR THR A . n 
A 1 198 LEU 198 197 197 LEU LEU A . n 
A 1 199 ASN 199 198 198 ASN ASN A . n 
A 1 200 THR 200 199 199 THR THR A . n 
A 1 201 THR 201 200 200 THR THR A . n 
A 1 202 TYR 202 201 201 TYR TYR A . n 
A 1 203 LEU 203 202 202 LEU LEU A . n 
A 1 204 GLN 204 203 203 GLN GLN A . n 
A 1 205 THR 205 204 204 THR THR A . n 
A 1 206 LEU 206 205 205 LEU LEU A . n 
A 1 207 ARG 207 206 206 ARG ARG A . n 
A 1 208 GLY 208 207 207 GLY GLY A . n 
A 1 209 LEU 209 208 208 LEU LEU A . n 
A 1 210 CYS 210 209 209 CYS CYS A . n 
A 1 211 PRO 211 210 210 PRO PRO A . n 
A 1 212 LEU 212 211 211 LEU LEU A . n 
A 1 213 ASN 213 212 212 ASN ASN A . n 
A 1 214 GLY 214 213 213 GLY GLY A . n 
A 1 215 ASN 215 214 214 ASN ASN A . n 
A 1 216 LEU 216 215 215 LEU LEU A . n 
A 1 217 SER 217 216 216 SER SER A . n 
A 1 218 ALA 218 217 217 ALA ALA A . n 
A 1 219 LEU 219 218 218 LEU LEU A . n 
A 1 220 VAL 220 219 219 VAL VAL A . n 
A 1 221 ASP 221 220 220 ASP ASP A . n 
A 1 222 PHE 222 221 221 PHE PHE A . n 
A 1 223 ASP 223 222 222 ASP ASP A . n 
A 1 224 LEU 224 223 223 LEU LEU A . n 
A 1 225 ARG 225 224 224 ARG ARG A . n 
A 1 226 THR 226 225 225 THR THR A . n 
A 1 227 PRO 227 226 226 PRO PRO A . n 
A 1 228 THR 228 227 227 THR THR A . n 
A 1 229 ILE 229 228 228 ILE ILE A . n 
A 1 230 PHE 230 229 229 PHE PHE A . n 
A 1 231 ASP 231 230 230 ASP ASP A . n 
A 1 232 ASN 232 231 231 ASN ASN A . n 
A 1 233 LYS 233 232 232 LYS LYS A . n 
A 1 234 TYR 234 233 233 TYR TYR A . n 
A 1 235 TYR 235 234 234 TYR TYR A . n 
A 1 236 VAL 236 235 235 VAL VAL A . n 
A 1 237 ASN 237 236 236 ASN ASN A . n 
A 1 238 LEU 238 237 237 LEU LEU A . n 
A 1 239 GLU 239 238 238 GLU GLU A . n 
A 1 240 GLU 240 239 239 GLU GLU A . n 
A 1 241 GLN 241 240 240 GLN GLN A . n 
A 1 242 LYS 242 241 241 LYS LYS A . n 
A 1 243 GLY 243 242 242 GLY GLY A . n 
A 1 244 LEU 244 243 243 LEU LEU A . n 
A 1 245 ILE 245 244 244 ILE ILE A . n 
A 1 246 GLN 246 245 245 GLN GLN A . n 
A 1 247 SER 247 246 246 SER SER A . n 
A 1 248 ASP 248 247 247 ASP ASP A . n 
A 1 249 GLN 249 248 248 GLN GLN A . n 
A 1 250 GLU 250 249 249 GLU GLU A . n 
A 1 251 LEU 251 250 250 LEU LEU A . n 
A 1 252 PHE 252 251 251 PHE PHE A . n 
A 1 253 SER 253 252 252 SER SER A . n 
A 1 254 SER 254 253 253 SER SER A . n 
A 1 255 PRO 255 254 254 PRO PRO A . n 
A 1 256 ASN 256 255 255 ASN ASN A . n 
A 1 257 ALA 257 256 256 ALA ALA A . n 
A 1 258 THR 258 257 257 THR THR A . n 
A 1 259 ASP 259 258 258 ASP ASP A . n 
A 1 260 THR 260 259 259 THR THR A . n 
A 1 261 ILE 261 260 260 ILE ILE A . n 
A 1 262 PRO 262 261 261 PRO PRO A . n 
A 1 263 LEU 263 262 262 LEU LEU A . n 
A 1 264 VAL 264 263 263 VAL VAL A . n 
A 1 265 ARG 265 264 264 ARG ARG A . n 
A 1 266 SER 266 265 265 SER SER A . n 
A 1 267 PHE 267 266 266 PHE PHE A . n 
A 1 268 ALA 268 267 267 ALA ALA A . n 
A 1 269 ASN 269 268 268 ASN ASN A . n 
A 1 270 SER 270 269 269 SER SER A . n 
A 1 271 THR 271 270 270 THR THR A . n 
A 1 272 GLN 272 271 271 GLN GLN A . n 
A 1 273 THR 273 272 272 THR THR A . n 
A 1 274 PHE 274 273 273 PHE PHE A . n 
A 1 275 PHE 275 274 274 PHE PHE A . n 
A 1 276 ASN 276 275 275 ASN ASN A . n 
A 1 277 ALA 277 276 276 ALA ALA A . n 
A 1 278 PHE 278 277 277 PHE PHE A . n 
A 1 279 VAL 279 278 278 VAL VAL A . n 
A 1 280 GLU 280 279 279 GLU GLU A . n 
A 1 281 ALA 281 280 280 ALA ALA A . n 
A 1 282 MET 282 281 281 MET MET A . n 
A 1 283 ASP 283 282 282 ASP ASP A . n 
A 1 284 ARG 284 283 283 ARG ARG A . n 
A 1 285 MET 285 284 284 MET MET A . n 
A 1 286 GLY 286 285 285 GLY GLY A . n 
A 1 287 ASN 287 286 286 ASN ASN A . n 
A 1 288 ILE 288 287 287 ILE ILE A . n 
A 1 289 THR 289 288 288 THR THR A . n 
A 1 290 PRO 290 289 289 PRO PRO A . n 
A 1 291 LEU 291 290 290 LEU LEU A . n 
A 1 292 THR 292 291 291 THR THR A . n 
A 1 293 GLY 293 292 292 GLY GLY A . n 
A 1 294 THR 294 293 293 THR THR A . n 
A 1 295 GLN 295 294 294 GLN GLN A . n 
A 1 296 GLY 296 295 295 GLY GLY A . n 
A 1 297 GLN 297 296 296 GLN GLN A . n 
A 1 298 ILE 298 297 297 ILE ILE A . n 
A 1 299 ARG 299 298 298 ARG ARG A . n 
A 1 300 LEU 300 299 299 LEU LEU A . n 
A 1 301 ASN 301 300 300 ASN ASN A . n 
A 1 302 CYS 302 301 301 CYS CYS A . n 
A 1 303 ARG 303 302 302 ARG ARG A . n 
A 1 304 VAL 304 303 303 VAL VAL A . n 
A 1 305 VAL 305 304 304 VAL VAL A . n 
A 1 306 ASN 306 305 305 ASN ASN A . n 
A 1 307 SER 307 306 306 SER SER A . n 
A 1 308 ASN 308 307 ?   ?   ?   A . n 
A 1 309 SER 309 308 ?   ?   ?   A . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        HEM 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   HEM 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
B 2 HEM 1   401 350  HEM HEM A . 
C 3 CA  1   402 501  CA  CA  A . 
D 3 CA  1   403 502  CA  CA  A . 
E 4 EDO 1   404 505  EDO EDO A . 
F 4 EDO 1   405 600  EDO EDO A . 
G 5 2HP 1   406 800  2HP 2HP A . 
H 4 EDO 1   407 900  EDO EDO A . 
I 4 EDO 1   408 1000 EDO EDO A . 
J 4 EDO 1   409 1100 EDO EDO A . 
K 6 HOH 1   501 91   HOH HOH A . 
K 6 HOH 2   502 81   HOH HOH A . 
K 6 HOH 3   503 55   HOH HOH A . 
K 6 HOH 4   504 227  HOH HOH A . 
K 6 HOH 5   505 510  HOH HOH A . 
K 6 HOH 6   506 116  HOH HOH A . 
K 6 HOH 7   507 70   HOH HOH A . 
K 6 HOH 8   508 501  HOH HOH A . 
K 6 HOH 9   509 326  HOH HOH A . 
K 6 HOH 10  510 1    HOH HOH A . 
K 6 HOH 11  511 28   HOH HOH A . 
K 6 HOH 12  512 5    HOH HOH A . 
K 6 HOH 13  513 349  HOH HOH A . 
K 6 HOH 14  514 246  HOH HOH A . 
K 6 HOH 15  515 49   HOH HOH A . 
K 6 HOH 16  516 110  HOH HOH A . 
K 6 HOH 17  517 141  HOH HOH A . 
K 6 HOH 18  518 11   HOH HOH A . 
K 6 HOH 19  519 23   HOH HOH A . 
K 6 HOH 20  520 27   HOH HOH A . 
K 6 HOH 21  521 65   HOH HOH A . 
K 6 HOH 22  522 37   HOH HOH A . 
K 6 HOH 23  523 85   HOH HOH A . 
K 6 HOH 24  524 38   HOH HOH A . 
K 6 HOH 25  525 78   HOH HOH A . 
K 6 HOH 26  526 19   HOH HOH A . 
K 6 HOH 27  527 511  HOH HOH A . 
K 6 HOH 28  528 369  HOH HOH A . 
K 6 HOH 29  529 62   HOH HOH A . 
K 6 HOH 30  530 18   HOH HOH A . 
K 6 HOH 31  531 97   HOH HOH A . 
K 6 HOH 32  532 61   HOH HOH A . 
K 6 HOH 33  533 114  HOH HOH A . 
K 6 HOH 34  534 22   HOH HOH A . 
K 6 HOH 35  535 84   HOH HOH A . 
K 6 HOH 36  536 4    HOH HOH A . 
K 6 HOH 37  537 39   HOH HOH A . 
K 6 HOH 38  538 119  HOH HOH A . 
K 6 HOH 39  539 3    HOH HOH A . 
K 6 HOH 40  540 34   HOH HOH A . 
K 6 HOH 41  541 66   HOH HOH A . 
K 6 HOH 42  542 15   HOH HOH A . 
K 6 HOH 43  543 13   HOH HOH A . 
K 6 HOH 44  544 24   HOH HOH A . 
K 6 HOH 45  545 82   HOH HOH A . 
K 6 HOH 46  546 112  HOH HOH A . 
K 6 HOH 47  547 63   HOH HOH A . 
K 6 HOH 48  548 176  HOH HOH A . 
K 6 HOH 49  549 42   HOH HOH A . 
K 6 HOH 50  550 25   HOH HOH A . 
K 6 HOH 51  551 21   HOH HOH A . 
K 6 HOH 52  552 31   HOH HOH A . 
K 6 HOH 53  553 60   HOH HOH A . 
K 6 HOH 54  554 26   HOH HOH A . 
K 6 HOH 55  555 12   HOH HOH A . 
K 6 HOH 56  556 10   HOH HOH A . 
K 6 HOH 57  557 108  HOH HOH A . 
K 6 HOH 58  558 44   HOH HOH A . 
K 6 HOH 59  559 135  HOH HOH A . 
K 6 HOH 60  560 40   HOH HOH A . 
K 6 HOH 61  561 14   HOH HOH A . 
K 6 HOH 62  562 7    HOH HOH A . 
K 6 HOH 63  563 504  HOH HOH A . 
K 6 HOH 64  564 72   HOH HOH A . 
K 6 HOH 65  565 29   HOH HOH A . 
K 6 HOH 66  566 20   HOH HOH A . 
K 6 HOH 67  567 98   HOH HOH A . 
K 6 HOH 68  568 144  HOH HOH A . 
K 6 HOH 69  569 8    HOH HOH A . 
K 6 HOH 70  570 88   HOH HOH A . 
K 6 HOH 71  571 16   HOH HOH A . 
K 6 HOH 72  572 120  HOH HOH A . 
K 6 HOH 73  573 182  HOH HOH A . 
K 6 HOH 74  574 47   HOH HOH A . 
K 6 HOH 75  575 67   HOH HOH A . 
K 6 HOH 76  576 32   HOH HOH A . 
K 6 HOH 77  577 113  HOH HOH A . 
K 6 HOH 78  578 6    HOH HOH A . 
K 6 HOH 79  579 224  HOH HOH A . 
K 6 HOH 80  580 95   HOH HOH A . 
K 6 HOH 81  581 164  HOH HOH A . 
K 6 HOH 82  582 502  HOH HOH A . 
K 6 HOH 83  583 131  HOH HOH A . 
K 6 HOH 84  584 93   HOH HOH A . 
K 6 HOH 85  585 169  HOH HOH A . 
K 6 HOH 86  586 175  HOH HOH A . 
K 6 HOH 87  587 46   HOH HOH A . 
K 6 HOH 88  588 505  HOH HOH A . 
K 6 HOH 89  589 75   HOH HOH A . 
K 6 HOH 90  590 50   HOH HOH A . 
K 6 HOH 91  591 30   HOH HOH A . 
K 6 HOH 92  592 64   HOH HOH A . 
K 6 HOH 93  593 234  HOH HOH A . 
K 6 HOH 94  594 127  HOH HOH A . 
K 6 HOH 95  595 123  HOH HOH A . 
K 6 HOH 96  596 258  HOH HOH A . 
K 6 HOH 97  597 80   HOH HOH A . 
K 6 HOH 98  598 73   HOH HOH A . 
K 6 HOH 99  599 103  HOH HOH A . 
K 6 HOH 100 600 43   HOH HOH A . 
K 6 HOH 101 601 56   HOH HOH A . 
K 6 HOH 102 602 242  HOH HOH A . 
K 6 HOH 103 603 170  HOH HOH A . 
K 6 HOH 104 604 35   HOH HOH A . 
K 6 HOH 105 605 503  HOH HOH A . 
K 6 HOH 106 606 69   HOH HOH A . 
K 6 HOH 107 607 286  HOH HOH A . 
K 6 HOH 108 608 54   HOH HOH A . 
K 6 HOH 109 609 243  HOH HOH A . 
K 6 HOH 110 610 303  HOH HOH A . 
K 6 HOH 111 611 33   HOH HOH A . 
K 6 HOH 112 612 53   HOH HOH A . 
K 6 HOH 113 613 99   HOH HOH A . 
K 6 HOH 114 614 146  HOH HOH A . 
K 6 HOH 115 615 309  HOH HOH A . 
K 6 HOH 116 616 317  HOH HOH A . 
K 6 HOH 117 617 382  HOH HOH A . 
K 6 HOH 118 618 214  HOH HOH A . 
K 6 HOH 119 619 111  HOH HOH A . 
K 6 HOH 120 620 83   HOH HOH A . 
K 6 HOH 121 621 219  HOH HOH A . 
K 6 HOH 122 622 233  HOH HOH A . 
K 6 HOH 123 623 231  HOH HOH A . 
K 6 HOH 124 624 174  HOH HOH A . 
K 6 HOH 125 625 238  HOH HOH A . 
K 6 HOH 126 626 498  HOH HOH A . 
K 6 HOH 127 627 218  HOH HOH A . 
K 6 HOH 128 628 250  HOH HOH A . 
K 6 HOH 129 629 129  HOH HOH A . 
K 6 HOH 130 630 366  HOH HOH A . 
K 6 HOH 131 631 249  HOH HOH A . 
K 6 HOH 132 632 499  HOH HOH A . 
K 6 HOH 133 633 92   HOH HOH A . 
K 6 HOH 134 634 500  HOH HOH A . 
K 6 HOH 135 635 102  HOH HOH A . 
K 6 HOH 136 636 343  HOH HOH A . 
K 6 HOH 137 637 96   HOH HOH A . 
K 6 HOH 138 638 166  HOH HOH A . 
K 6 HOH 139 639 184  HOH HOH A . 
K 6 HOH 140 640 89   HOH HOH A . 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? 'data processing' ? ? ? ? ? ? ? ? ? ? ? autoPROC ? ? ? 1.0.5 1 
? 'model building'  ? ? ? ? ? ? ? ? ? ? ? Coot     ? ? ? 0.9.8 2 
? phasing           ? ? ? ? ? ? ? ? ? ? ? PHASER   ? ? ? .     3 
? refinement        ? ? ? ? ? ? ? ? ? ? ? PHENIX   ? ? ? 1.21  4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.00 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9H1M 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     40.157 
_cell.length_a_esd                 ? 
_cell.length_b                     67.061 
_cell.length_b_esd                 ? 
_cell.length_c                     117.178 
_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                         9H1M 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                19 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 21 21 21' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   9H1M 
_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             2.31 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          46.87 
_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              8.5 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    
'25% (w/v) PEG 1500, 100 mM SPG (2:7:7, succinic acid:sodium hydrogen phosphate:glycine buffer pH 8.5' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            277.15 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS PILATUS3 6M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2024-03-13 
_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   0.9999 
_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                        'DIAMOND BEAMLINE I24' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.9999 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   I24 
_diffrn_source.pdbx_synchrotron_site       Diamond 
# 
_reflns.B_iso_Wilson_estimate                          22.02 
_reflns.entry_id                                       9H1M 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.63 
_reflns.d_resolution_low                               58.20 
_reflns.details                                        ? 
_reflns.limit_h_max                                    ? 
_reflns.limit_h_min                                    ? 
_reflns.limit_k_max                                    ? 
_reflns.limit_k_min                                    ? 
_reflns.limit_l_max                                    ? 
_reflns.limit_l_min                                    ? 
_reflns.number_all                                     ? 
_reflns.number_obs                                     37103 
_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                           92.0 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                3.9 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          5.4 
_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                                   0.991 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.115 
_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                                    1.63 
_reflns_shell.d_res_low                                     1.66 
_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                             1850 
_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                               2.1 
_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                                  0.343 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          93.6 
_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                                 9H1M 
_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                            1.63 
_refine.ls_d_res_low                             58.20 
_refine.ls_extinction_coef                       ? 
_refine.ls_extinction_coef_esd                   ? 
_refine.ls_extinction_expression                 ? 
_refine.ls_extinction_method                     ? 
_refine.ls_goodness_of_fit_all                   ? 
_refine.ls_goodness_of_fit_all_esd               ? 
_refine.ls_goodness_of_fit_obs                   ? 
_refine.ls_goodness_of_fit_obs_esd               ? 
_refine.ls_hydrogen_treatment                    ? 
_refine.ls_matrix_type                           ? 
_refine.ls_number_constraints                    ? 
_refine.ls_number_parameters                     ? 
_refine.ls_number_reflns_all                     ? 
_refine.ls_number_reflns_obs                     36260 
_refine.ls_number_reflns_R_free                  1903 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    89.93 
_refine.ls_percent_reflns_R_free                 5.25 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1709 
_refine.ls_R_factor_R_free                       0.1893 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1698 
_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             1.11 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.90 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 20.85 
_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                       1.63 
_refine_hist.d_res_low                        58.20 
_refine_hist.number_atoms_solvent             140 
_refine_hist.number_atoms_total               2579 
_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        2369 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         70 
_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  ? 2491 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.876  ? 3396 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 13.381 ? 900  ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.042  ? 380  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.008  ? 448  ? 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' 1.63 1.67 . . 126 2206 82.00  . . . . 0.3162 . . . . . . . . . . . 0.3180 
'X-RAY DIFFRACTION' 1.67 1.72 . . 98  2000 75.00  . . . . 0.3037 . . . . . . . . . . . 0.3299 
'X-RAY DIFFRACTION' 1.72 1.77 . . 108 2275 84.00  . . . . 0.2383 . . . . . . . . . . . 0.2639 
'X-RAY DIFFRACTION' 1.77 1.82 . . 134 2665 98.00  . . . . 0.2196 . . . . . . . . . . . 0.2509 
'X-RAY DIFFRACTION' 1.82 1.89 . . 135 2207 83.00  . . . . 0.2221 . . . . . . . . . . . 0.2321 
'X-RAY DIFFRACTION' 1.89 1.96 . . 114 2112 78.00  . . . . 0.1995 . . . . . . . . . . . 0.2274 
'X-RAY DIFFRACTION' 1.97 2.05 . . 162 2659 99.00  . . . . 0.1597 . . . . . . . . . . . 0.2332 
'X-RAY DIFFRACTION' 2.05 2.16 . . 136 2333 87.00  . . . . 0.1468 . . . . . . . . . . . 0.1713 
'X-RAY DIFFRACTION' 2.16 2.30 . . 132 2521 92.00  . . . . 0.1399 . . . . . . . . . . . 0.1763 
'X-RAY DIFFRACTION' 2.30 2.48 . . 156 2724 100.00 . . . . 0.1437 . . . . . . . . . . . 0.1585 
'X-RAY DIFFRACTION' 2.48 2.72 . . 150 2537 93.00  . . . . 0.1525 . . . . . . . . . . . 0.1837 
'X-RAY DIFFRACTION' 2.73 3.12 . . 152 2764 99.00  . . . . 0.1626 . . . . . . . . . . . 0.1893 
'X-RAY DIFFRACTION' 3.12 3.93 . . 140 2441 88.00  . . . . 0.1641 . . . . . . . . . . . 0.2101 
# 
_struct.entry_id                     9H1M 
_struct.title                        'Recombinant ferric horseradish peroxidase C1A' 
_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        9H1M 
_struct_keywords.text            'Horseradish Peroxidase, Ferric, oxidoreductases, Heme, OXIDOREDUCTASE' 
_struct_keywords.pdbx_keywords   OXIDOREDUCTASE 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
D N N 3 ? 
E N N 4 ? 
F N N 4 ? 
G N N 5 ? 
H N N 4 ? 
I N N 4 ? 
J N N 4 ? 
K N N 6 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    PER1A_ARMRU 
_struct_ref.pdbx_db_accession          P00433 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;QLTPTFYDNSCPNVSNIVRDTIVNELRSDPRIAASILRLHFHDCFVNGCDASILLDNTTSFRTEKDAFGNANSARGFPVI
DRMKAAVESACPRTVSCADLLTIAAQQSVTLAGGPSWRVPLGRRDSLQAFLDLANANLPAPFFTLPQLKDSFRNVGLNRS
SDLVALSGGHTFGKNQCRFIMDRLYNFSNTGLPDPTLNTTYLQTLRGLCPLNGNLSALVDFDLRTPTIFDNKYYVNLEEQ
KGLIQSDQELFSSPNATDTIPLVRSFANSTQTFFNAFVEAMDRMGNITPLTGTQGQIRLNCRVVNSNS
;
_struct_ref.pdbx_align_begin           31 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              9H1M 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 2 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 309 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             P00433 
_struct_ref_seq.db_align_beg                  31 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  338 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       1 
_struct_ref_seq.pdbx_auth_seq_align_end       308 
# 
_struct_ref_seq_dif.align_id                     1 
_struct_ref_seq_dif.pdbx_pdb_id_code             9H1M 
_struct_ref_seq_dif.mon_id                       MET 
_struct_ref_seq_dif.pdbx_pdb_strand_id           A 
_struct_ref_seq_dif.seq_num                      1 
_struct_ref_seq_dif.pdbx_pdb_ins_code            ? 
_struct_ref_seq_dif.pdbx_seq_db_name             UNP 
_struct_ref_seq_dif.pdbx_seq_db_accession_code   P00433 
_struct_ref_seq_dif.db_mon_id                    ? 
_struct_ref_seq_dif.pdbx_seq_db_seq_num          ? 
_struct_ref_seq_dif.details                      'initiating methionine' 
_struct_ref_seq_dif.pdbx_auth_seq_num            0 
_struct_ref_seq_dif.pdbx_ordinal                 1 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 2510  ? 
1 MORE         -4    ? 
1 'SSA (A^2)'  12570 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G,H,I,J,K 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   none 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 ASN A 14  ? ARG A 28  ? ASN A 13  ARG A 27  1 ? 15 
HELX_P HELX_P2  AA2 ARG A 32  ? PHE A 46  ? ARG A 31  PHE A 45  1 ? 15 
HELX_P HELX_P3  AA3 ALA A 52  ? LEU A 56  ? ALA A 51  LEU A 55  5 ? 5  
HELX_P HELX_P4  AA4 THR A 64  ? ALA A 68  ? THR A 63  ALA A 67  5 ? 5  
HELX_P HELX_P5  AA5 GLY A 77  ? CYS A 92  ? GLY A 76  CYS A 91  1 ? 16 
HELX_P HELX_P6  AA6 SER A 97  ? ALA A 113 ? SER A 96  ALA A 112 1 ? 17 
HELX_P HELX_P7  AA7 PHE A 131 ? LEU A 139 ? PHE A 130 LEU A 138 1 ? 9  
HELX_P HELX_P8  AA8 THR A 145 ? VAL A 156 ? THR A 144 VAL A 155 1 ? 12 
HELX_P HELX_P9  AA9 ARG A 160 ? GLY A 169 ? ARG A 159 GLY A 168 1 ? 10 
HELX_P HELX_P10 AB1 GLY A 170 ? PHE A 173 ? GLY A 169 PHE A 172 5 ? 4  
HELX_P HELX_P11 AB2 ILE A 181 ? ASN A 187 ? ILE A 180 ASN A 186 1 ? 7  
HELX_P HELX_P12 AB3 PHE A 188 ? THR A 191 ? PHE A 187 THR A 190 5 ? 4  
HELX_P HELX_P13 AB4 ASN A 199 ? CYS A 210 ? ASN A 198 CYS A 209 1 ? 12 
HELX_P HELX_P14 AB5 ASN A 232 ? GLU A 240 ? ASN A 231 GLU A 239 1 ? 9  
HELX_P HELX_P15 AB6 ILE A 245 ? SER A 254 ? ILE A 244 SER A 253 1 ? 10 
HELX_P HELX_P16 AB7 THR A 260 ? SER A 270 ? THR A 259 SER A 269 1 ? 11 
HELX_P HELX_P17 AB8 SER A 270 ? GLY A 286 ? SER A 269 GLY A 285 1 ? 17 
# 
_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 
disulf1  disulf ? ? A CYS 12  SG  ? ? ? 1_555 A CYS 92  SG A ? A CYS 11  A CYS 91  1_555 ? ? ? ? ? ? ? 2.042 ? ? 
disulf2  disulf ? ? A CYS 12  SG  ? ? ? 1_555 A CYS 92  SG B ? A CYS 11  A CYS 91  1_555 ? ? ? ? ? ? ? 2.045 ? ? 
disulf3  disulf ? ? A CYS 45  SG  ? ? ? 1_555 A CYS 50  SG ? ? A CYS 44  A CYS 49  1_555 ? ? ? ? ? ? ? 2.049 ? ? 
disulf4  disulf ? ? A CYS 98  SG  ? ? ? 1_555 A CYS 302 SG ? ? A CYS 97  A CYS 301 1_555 ? ? ? ? ? ? ? 2.057 ? ? 
disulf5  disulf ? ? A CYS 178 SG  ? ? ? 1_555 A CYS 210 SG ? ? A CYS 177 A CYS 209 1_555 ? ? ? ? ? ? ? 2.041 ? ? 
metalc1  metalc ? ? A ASP 44  O   ? ? ? 1_555 C CA  .   CA ? ? A ASP 43  A CA  402 1_555 ? ? ? ? ? ? ? 2.356 ? ? 
metalc2  metalc ? ? A ASP 44  OD1 ? ? ? 1_555 C CA  .   CA ? ? A ASP 43  A CA  402 1_555 ? ? ? ? ? ? ? 2.381 ? ? 
metalc3  metalc ? ? A VAL 47  O   ? ? ? 1_555 C CA  .   CA ? ? A VAL 46  A CA  402 1_555 ? ? ? ? ? ? ? 2.312 ? ? 
metalc4  metalc ? ? A GLY 49  O   ? ? ? 1_555 C CA  .   CA ? ? A GLY 48  A CA  402 1_555 ? ? ? ? ? ? ? 2.485 ? ? 
metalc5  metalc ? ? A ASP 51  OD1 ? ? ? 1_555 C CA  .   CA ? ? A ASP 50  A CA  402 1_555 ? ? ? ? ? ? ? 2.354 ? ? 
metalc6  metalc ? ? A SER 53  OG  ? ? ? 1_555 C CA  .   CA ? ? A SER 52  A CA  402 1_555 ? ? ? ? ? ? ? 2.420 ? ? 
metalc7  metalc ? ? A HIS 171 NE2 ? ? ? 1_555 B HEM .   FE ? ? A HIS 170 A HEM 401 1_555 ? ? ? ? ? ? ? 2.034 ? ? 
metalc8  metalc ? ? A THR 172 O   ? ? ? 1_555 D CA  .   CA ? ? A THR 171 A CA  403 1_555 ? ? ? ? ? ? ? 2.313 ? ? 
metalc9  metalc ? ? A THR 172 OG1 ? ? ? 1_555 D CA  .   CA ? ? A THR 171 A CA  403 1_555 ? ? ? ? ? ? ? 2.507 ? ? 
metalc10 metalc ? ? A ASP 223 OD2 ? ? ? 1_555 D CA  .   CA ? ? A ASP 222 A CA  403 1_555 ? ? ? ? ? ? ? 2.205 ? ? 
metalc11 metalc ? ? A THR 226 O   ? ? ? 1_555 D CA  .   CA ? ? A THR 225 A CA  403 1_555 ? ? ? ? ? ? ? 2.375 ? ? 
metalc12 metalc ? ? A THR 226 OG1 ? ? ? 1_555 D CA  .   CA ? ? A THR 225 A CA  403 1_555 ? ? ? ? ? ? ? 2.439 ? ? 
metalc13 metalc ? ? A ILE 229 O   ? ? ? 1_555 D CA  .   CA ? ? A ILE 228 A CA  403 1_555 ? ? ? ? ? ? ? 2.387 ? ? 
metalc14 metalc ? ? A ASP 231 OD1 ? ? ? 1_555 D CA  .   CA ? ? A ASP 230 A CA  403 1_555 ? ? ? ? ? ? ? 2.435 ? ? 
metalc15 metalc ? ? C CA  .   CA  ? ? ? 1_555 K HOH .   O  ? ? A CA  402 A HOH 510 1_555 ? ? ? ? ? ? ? 2.433 ? ? 
# 
loop_
_struct_conn_type.id 
_struct_conn_type.criteria 
_struct_conn_type.reference 
disulf ? ? 
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  O   ? A ASP 44  ? A ASP 43  ? 1_555 CA ? C CA  . ? A CA  402 ? 1_555 OD1 ? A ASP 44  ? A ASP 43  ? 1_555 78.4  ? 
2  O   ? A ASP 44  ? A ASP 43  ? 1_555 CA ? C CA  . ? A CA  402 ? 1_555 O   ? A VAL 47  ? A VAL 46  ? 1_555 85.3  ? 
3  OD1 ? A ASP 44  ? A ASP 43  ? 1_555 CA ? C CA  . ? A CA  402 ? 1_555 O   ? A VAL 47  ? A VAL 46  ? 1_555 163.6 ? 
4  O   ? A ASP 44  ? A ASP 43  ? 1_555 CA ? C CA  . ? A CA  402 ? 1_555 O   ? A GLY 49  ? A GLY 48  ? 1_555 71.2  ? 
5  OD1 ? A ASP 44  ? A ASP 43  ? 1_555 CA ? C CA  . ? A CA  402 ? 1_555 O   ? A GLY 49  ? A GLY 48  ? 1_555 88.1  ? 
6  O   ? A VAL 47  ? A VAL 46  ? 1_555 CA ? C CA  . ? A CA  402 ? 1_555 O   ? A GLY 49  ? A GLY 48  ? 1_555 86.9  ? 
7  O   ? A ASP 44  ? A ASP 43  ? 1_555 CA ? C CA  . ? A CA  402 ? 1_555 OD1 ? A ASP 51  ? A ASP 50  ? 1_555 140.4 ? 
8  OD1 ? A ASP 44  ? A ASP 43  ? 1_555 CA ? C CA  . ? A CA  402 ? 1_555 OD1 ? A ASP 51  ? A ASP 50  ? 1_555 80.4  ? 
9  O   ? A VAL 47  ? A VAL 46  ? 1_555 CA ? C CA  . ? A CA  402 ? 1_555 OD1 ? A ASP 51  ? A ASP 50  ? 1_555 113.2 ? 
10 O   ? A GLY 49  ? A GLY 48  ? 1_555 CA ? C CA  . ? A CA  402 ? 1_555 OD1 ? A ASP 51  ? A ASP 50  ? 1_555 75.1  ? 
11 O   ? A ASP 44  ? A ASP 43  ? 1_555 CA ? C CA  . ? A CA  402 ? 1_555 OG  ? A SER 53  ? A SER 52  ? 1_555 141.3 ? 
12 OD1 ? A ASP 44  ? A ASP 43  ? 1_555 CA ? C CA  . ? A CA  402 ? 1_555 OG  ? A SER 53  ? A SER 52  ? 1_555 100.1 ? 
13 O   ? A VAL 47  ? A VAL 46  ? 1_555 CA ? C CA  . ? A CA  402 ? 1_555 OG  ? A SER 53  ? A SER 52  ? 1_555 92.5  ? 
14 O   ? A GLY 49  ? A GLY 48  ? 1_555 CA ? C CA  . ? A CA  402 ? 1_555 OG  ? A SER 53  ? A SER 52  ? 1_555 147.4 ? 
15 OD1 ? A ASP 51  ? A ASP 50  ? 1_555 CA ? C CA  . ? A CA  402 ? 1_555 OG  ? A SER 53  ? A SER 52  ? 1_555 75.3  ? 
16 O   ? A ASP 44  ? A ASP 43  ? 1_555 CA ? C CA  . ? A CA  402 ? 1_555 O   ? K HOH .   ? A HOH 510 ? 1_555 76.6  ? 
17 OD1 ? A ASP 44  ? A ASP 43  ? 1_555 CA ? C CA  . ? A CA  402 ? 1_555 O   ? K HOH .   ? A HOH 510 ? 1_555 84.8  ? 
18 O   ? A VAL 47  ? A VAL 46  ? 1_555 CA ? C CA  . ? A CA  402 ? 1_555 O   ? K HOH .   ? A HOH 510 ? 1_555 91.1  ? 
19 O   ? A GLY 49  ? A GLY 48  ? 1_555 CA ? C CA  . ? A CA  402 ? 1_555 O   ? K HOH .   ? A HOH 510 ? 1_555 147.7 ? 
20 OD1 ? A ASP 51  ? A ASP 50  ? 1_555 CA ? C CA  . ? A CA  402 ? 1_555 O   ? K HOH .   ? A HOH 510 ? 1_555 134.0 ? 
21 OG  ? A SER 53  ? A SER 52  ? 1_555 CA ? C CA  . ? A CA  402 ? 1_555 O   ? K HOH .   ? A HOH 510 ? 1_555 64.8  ? 
22 NE2 ? A HIS 171 ? A HIS 170 ? 1_555 FE ? B HEM . ? A HEM 401 ? 1_555 NA  ? B HEM .   ? A HEM 401 ? 1_555 97.2  ? 
23 NE2 ? A HIS 171 ? A HIS 170 ? 1_555 FE ? B HEM . ? A HEM 401 ? 1_555 NB  ? B HEM .   ? A HEM 401 ? 1_555 98.5  ? 
24 NA  ? B HEM .   ? A HEM 401 ? 1_555 FE ? B HEM . ? A HEM 401 ? 1_555 NB  ? B HEM .   ? A HEM 401 ? 1_555 88.4  ? 
25 NE2 ? A HIS 171 ? A HIS 170 ? 1_555 FE ? B HEM . ? A HEM 401 ? 1_555 NC  ? B HEM .   ? A HEM 401 ? 1_555 93.6  ? 
26 NA  ? B HEM .   ? A HEM 401 ? 1_555 FE ? B HEM . ? A HEM 401 ? 1_555 NC  ? B HEM .   ? A HEM 401 ? 1_555 169.2 ? 
27 NB  ? B HEM .   ? A HEM 401 ? 1_555 FE ? B HEM . ? A HEM 401 ? 1_555 NC  ? B HEM .   ? A HEM 401 ? 1_555 89.4  ? 
28 NE2 ? A HIS 171 ? A HIS 170 ? 1_555 FE ? B HEM . ? A HEM 401 ? 1_555 ND  ? B HEM .   ? A HEM 401 ? 1_555 97.9  ? 
29 NA  ? B HEM .   ? A HEM 401 ? 1_555 FE ? B HEM . ? A HEM 401 ? 1_555 ND  ? B HEM .   ? A HEM 401 ? 1_555 89.1  ? 
30 NB  ? B HEM .   ? A HEM 401 ? 1_555 FE ? B HEM . ? A HEM 401 ? 1_555 ND  ? B HEM .   ? A HEM 401 ? 1_555 163.6 ? 
31 NC  ? B HEM .   ? A HEM 401 ? 1_555 FE ? B HEM . ? A HEM 401 ? 1_555 ND  ? B HEM .   ? A HEM 401 ? 1_555 90.0  ? 
32 O   ? A THR 172 ? A THR 171 ? 1_555 CA ? D CA  . ? A CA  403 ? 1_555 OG1 ? A THR 172 ? A THR 171 ? 1_555 73.6  ? 
33 O   ? A THR 172 ? A THR 171 ? 1_555 CA ? D CA  . ? A CA  403 ? 1_555 OD2 ? A ASP 223 ? A ASP 222 ? 1_555 90.8  ? 
34 OG1 ? A THR 172 ? A THR 171 ? 1_555 CA ? D CA  . ? A CA  403 ? 1_555 OD2 ? A ASP 223 ? A ASP 222 ? 1_555 89.2  ? 
35 O   ? A THR 172 ? A THR 171 ? 1_555 CA ? D CA  . ? A CA  403 ? 1_555 O   ? A THR 226 ? A THR 225 ? 1_555 80.9  ? 
36 OG1 ? A THR 172 ? A THR 171 ? 1_555 CA ? D CA  . ? A CA  403 ? 1_555 O   ? A THR 226 ? A THR 225 ? 1_555 154.5 ? 
37 OD2 ? A ASP 223 ? A ASP 222 ? 1_555 CA ? D CA  . ? A CA  403 ? 1_555 O   ? A THR 226 ? A THR 225 ? 1_555 90.0  ? 
38 O   ? A THR 172 ? A THR 171 ? 1_555 CA ? D CA  . ? A CA  403 ? 1_555 OG1 ? A THR 226 ? A THR 225 ? 1_555 151.2 ? 
39 OG1 ? A THR 172 ? A THR 171 ? 1_555 CA ? D CA  . ? A CA  403 ? 1_555 OG1 ? A THR 226 ? A THR 225 ? 1_555 134.5 ? 
40 OD2 ? A ASP 223 ? A ASP 222 ? 1_555 CA ? D CA  . ? A CA  403 ? 1_555 OG1 ? A THR 226 ? A THR 225 ? 1_555 84.6  ? 
41 O   ? A THR 226 ? A THR 225 ? 1_555 CA ? D CA  . ? A CA  403 ? 1_555 OG1 ? A THR 226 ? A THR 225 ? 1_555 70.8  ? 
42 O   ? A THR 172 ? A THR 171 ? 1_555 CA ? D CA  . ? A CA  403 ? 1_555 O   ? A ILE 229 ? A ILE 228 ? 1_555 84.7  ? 
43 OG1 ? A THR 172 ? A THR 171 ? 1_555 CA ? D CA  . ? A CA  403 ? 1_555 O   ? A ILE 229 ? A ILE 228 ? 1_555 89.0  ? 
44 OD2 ? A ASP 223 ? A ASP 222 ? 1_555 CA ? D CA  . ? A CA  403 ? 1_555 O   ? A ILE 229 ? A ILE 228 ? 1_555 175.4 ? 
45 O   ? A THR 226 ? A THR 225 ? 1_555 CA ? D CA  . ? A CA  403 ? 1_555 O   ? A ILE 229 ? A ILE 228 ? 1_555 89.8  ? 
46 OG1 ? A THR 226 ? A THR 225 ? 1_555 CA ? D CA  . ? A CA  403 ? 1_555 O   ? A ILE 229 ? A ILE 228 ? 1_555 99.7  ? 
47 O   ? A THR 172 ? A THR 171 ? 1_555 CA ? D CA  . ? A CA  403 ? 1_555 OD1 ? A ASP 231 ? A ASP 230 ? 1_555 139.0 ? 
48 OG1 ? A THR 172 ? A THR 171 ? 1_555 CA ? D CA  . ? A CA  403 ? 1_555 OD1 ? A ASP 231 ? A ASP 230 ? 1_555 68.0  ? 
49 OD2 ? A ASP 223 ? A ASP 222 ? 1_555 CA ? D CA  . ? A CA  403 ? 1_555 OD1 ? A ASP 231 ? A ASP 230 ? 1_555 102.4 ? 
50 O   ? A THR 226 ? A THR 225 ? 1_555 CA ? D CA  . ? A CA  403 ? 1_555 OD1 ? A ASP 231 ? A ASP 230 ? 1_555 136.8 ? 
51 OG1 ? A THR 226 ? A THR 225 ? 1_555 CA ? D CA  . ? A CA  403 ? 1_555 OD1 ? A ASP 231 ? A ASP 230 ? 1_555 69.5  ? 
52 O   ? A ILE 229 ? A ILE 228 ? 1_555 CA ? D CA  . ? A CA  403 ? 1_555 OD1 ? A ASP 231 ? A ASP 230 ? 1_555 80.8  ? 
# 
loop_
_pdbx_modification_feature.ordinal 
_pdbx_modification_feature.label_comp_id 
_pdbx_modification_feature.label_asym_id 
_pdbx_modification_feature.label_seq_id 
_pdbx_modification_feature.label_alt_id 
_pdbx_modification_feature.modified_residue_label_comp_id 
_pdbx_modification_feature.modified_residue_label_asym_id 
_pdbx_modification_feature.modified_residue_label_seq_id 
_pdbx_modification_feature.modified_residue_label_alt_id 
_pdbx_modification_feature.auth_comp_id 
_pdbx_modification_feature.auth_asym_id 
_pdbx_modification_feature.auth_seq_id 
_pdbx_modification_feature.PDB_ins_code 
_pdbx_modification_feature.symmetry 
_pdbx_modification_feature.modified_residue_auth_comp_id 
_pdbx_modification_feature.modified_residue_auth_asym_id 
_pdbx_modification_feature.modified_residue_auth_seq_id 
_pdbx_modification_feature.modified_residue_PDB_ins_code 
_pdbx_modification_feature.modified_residue_symmetry 
_pdbx_modification_feature.comp_id_linking_atom 
_pdbx_modification_feature.modified_residue_id_linking_atom 
_pdbx_modification_feature.modified_residue_id 
_pdbx_modification_feature.ref_pcm_id 
_pdbx_modification_feature.ref_comp_id 
_pdbx_modification_feature.type 
_pdbx_modification_feature.category 
1 CYS A 12  ? CYS A 92  A CYS A 11  ? 1_555 CYS A 91  ? 1_555 SG SG . . . None 'Disulfide bridge' 
2 CYS A 12  ? CYS A 92  B CYS A 11  ? 1_555 CYS A 91  ? 1_555 SG SG . . . None 'Disulfide bridge' 
3 CYS A 45  ? CYS A 50  ? CYS A 44  ? 1_555 CYS A 49  ? 1_555 SG SG . . . None 'Disulfide bridge' 
4 CYS A 98  ? CYS A 302 ? CYS A 97  ? 1_555 CYS A 301 ? 1_555 SG SG . . . None 'Disulfide bridge' 
5 CYS A 178 ? CYS A 210 ? CYS A 177 ? 1_555 CYS A 209 ? 1_555 SG SG . . . None 'Disulfide bridge' 
# 
_struct_sheet.id               AA1 
_struct_sheet.type             ? 
_struct_sheet.number_strands   2 
_struct_sheet.details          ? 
# 
_struct_sheet_order.sheet_id     AA1 
_struct_sheet_order.range_id_1   1 
_struct_sheet_order.range_id_2   2 
_struct_sheet_order.offset       ? 
_struct_sheet_order.sense        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 LYS A 175 ? GLN A 177 ? LYS A 174 GLN A 176 
AA1 2 LEU A 219 ? ASP A 221 ? LEU A 218 ASP A 220 
# 
_pdbx_struct_sheet_hbond.sheet_id                AA1 
_pdbx_struct_sheet_hbond.range_id_1              1 
_pdbx_struct_sheet_hbond.range_id_2              2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id   N 
_pdbx_struct_sheet_hbond.range_1_label_comp_id   ASN 
_pdbx_struct_sheet_hbond.range_1_label_asym_id   A 
_pdbx_struct_sheet_hbond.range_1_label_seq_id    176 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code    ? 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id    N 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id    ASN 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id    A 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id     175 
_pdbx_struct_sheet_hbond.range_2_label_atom_id   O 
_pdbx_struct_sheet_hbond.range_2_label_comp_id   VAL 
_pdbx_struct_sheet_hbond.range_2_label_asym_id   A 
_pdbx_struct_sheet_hbond.range_2_label_seq_id    220 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code    ? 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id    O 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id    VAL 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id    A 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id     219 
# 
_pdbx_entry_details.entry_id                   9H1M 
_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 610 ? ? O A HOH 623 ? ? 2.04 
2 1 O A HOH 620 ? ? O A HOH 624 ? ? 2.05 
3 1 O A HOH 597 ? ? O A HOH 639 ? ? 2.14 
# 
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 CYS A 11  ? ? -158.26 67.79  
2 1 SER A 73  ? ? -156.74 -63.74 
3 1 THR A 94  ? ? -120.26 -52.25 
4 1 ASN A 186 ? ? -160.35 82.07  
5 1 THR A 288 ? ? 29.73   62.47  
# 
loop_
_pdbx_refine_tls.id 
_pdbx_refine_tls.pdbx_refine_id 
_pdbx_refine_tls.details 
_pdbx_refine_tls.method 
_pdbx_refine_tls.origin_x 
_pdbx_refine_tls.origin_y 
_pdbx_refine_tls.origin_z 
_pdbx_refine_tls.T[1][1] 
_pdbx_refine_tls.T[1][1]_esd 
_pdbx_refine_tls.T[1][2] 
_pdbx_refine_tls.T[1][2]_esd 
_pdbx_refine_tls.T[1][3] 
_pdbx_refine_tls.T[1][3]_esd 
_pdbx_refine_tls.T[2][2] 
_pdbx_refine_tls.T[2][2]_esd 
_pdbx_refine_tls.T[2][3] 
_pdbx_refine_tls.T[2][3]_esd 
_pdbx_refine_tls.T[3][3] 
_pdbx_refine_tls.T[3][3]_esd 
_pdbx_refine_tls.L[1][1] 
_pdbx_refine_tls.L[1][1]_esd 
_pdbx_refine_tls.L[1][2] 
_pdbx_refine_tls.L[1][2]_esd 
_pdbx_refine_tls.L[1][3] 
_pdbx_refine_tls.L[1][3]_esd 
_pdbx_refine_tls.L[2][2] 
_pdbx_refine_tls.L[2][2]_esd 
_pdbx_refine_tls.L[2][3] 
_pdbx_refine_tls.L[2][3]_esd 
_pdbx_refine_tls.L[3][3] 
_pdbx_refine_tls.L[3][3]_esd 
_pdbx_refine_tls.S[1][1] 
_pdbx_refine_tls.S[1][1]_esd 
_pdbx_refine_tls.S[1][2] 
_pdbx_refine_tls.S[1][2]_esd 
_pdbx_refine_tls.S[1][3] 
_pdbx_refine_tls.S[1][3]_esd 
_pdbx_refine_tls.S[2][1] 
_pdbx_refine_tls.S[2][1]_esd 
_pdbx_refine_tls.S[2][2] 
_pdbx_refine_tls.S[2][2]_esd 
_pdbx_refine_tls.S[2][3] 
_pdbx_refine_tls.S[2][3]_esd 
_pdbx_refine_tls.S[3][1] 
_pdbx_refine_tls.S[3][1]_esd 
_pdbx_refine_tls.S[3][2] 
_pdbx_refine_tls.S[3][2]_esd 
_pdbx_refine_tls.S[3][3] 
_pdbx_refine_tls.S[3][3]_esd 
1  'X-RAY DIFFRACTION' ? refined 10.9991 13.0905 33.6762 0.3012 ? -0.0013 ? 0.0002  ? 0.2656 ? -0.0445 ? 0.2375 ? 0.0903  ? 
-0.0464 ? -0.0819 ? 0.1670 ? -0.1271 ? 0.1683  ? 0.0342  ? 0.3302  ? -0.0393 ? -0.1796 ? -0.0404 ? -0.0061 ? 0.0999  ? 0.0347  ? 
0.0000  ? 
2  'X-RAY DIFFRACTION' ? refined 1.7643  23.0100 42.6938 0.2105 ? -0.0089 ? -0.0105 ? 0.2791 ? -0.0233 ? 0.2150 ? 0.0138  ? 0.0363 
? -0.0517 ? 0.1261 ? -0.0610 ? 0.1754  ? -0.0035 ? 0.2353  ? 0.0033  ? 0.0704  ? -0.0636 ? 0.0770  ? 0.1733  ? -0.0533 ? -0.0000 ? 
3  'X-RAY DIFFRACTION' ? refined 7.6717  16.2156 56.3181 0.2438 ? -0.0285 ? 0.0209  ? 0.2023 ? 0.0111  ? 0.2256 ? 0.1372  ? 
-0.0269 ? 0.0817  ? 0.1214 ? -0.0317 ? -0.0069 ? 0.0085  ? -0.1423 ? -0.0597 ? 0.0949  ? -0.1272 ? 0.0762  ? -0.0255 ? 0.0127  ? 
0.0001  ? 
4  'X-RAY DIFFRACTION' ? refined 4.2132  12.2928 44.3583 0.2581 ? -0.0128 ? -0.0085 ? 0.2404 ? -0.0121 ? 0.2490 ? 0.2349  ? 0.2570 
? 0.0560  ? 0.3651 ? -0.2986 ? 0.2625  ? -0.0938 ? 0.0756  ? -0.1583 ? 0.2220  ? -0.0746 ? 0.3247  ? 0.2540  ? -0.1773 ? -0.0000 ? 
5  'X-RAY DIFFRACTION' ? refined 11.8775 18.7070 40.3660 0.2458 ? 0.0015  ? -0.0052 ? 0.2524 ? 0.0165  ? 0.2172 ? -0.0301 ? 
-0.0522 ? 0.1205  ? 0.1989 ? -0.0136 ? 0.0585  ? -0.0176 ? 0.0258  ? -0.0812 ? -0.0252 ? -0.1099 ? -0.0605 ? 0.0840  ? 0.0466  ? 
0.0000  ? 
6  'X-RAY DIFFRACTION' ? refined 12.0738 34.0118 54.6606 0.2082 ? -0.0059 ? 0.0006  ? 0.2070 ? -0.0090 ? 0.2477 ? 0.0840  ? 
-0.0554 ? 0.0706  ? 0.1928 ? 0.0140  ? 0.0856  ? -0.0040 ? -0.0668 ? 0.0216  ? 0.2232  ? -0.0405 ? -0.0507 ? -0.0280 ? -0.0196 ? 
0.0000  ? 
7  'X-RAY DIFFRACTION' ? refined 0.1388  36.8894 47.4155 0.2023 ? 0.0065  ? 0.0034  ? 0.2415 ? -0.0128 ? 0.2547 ? 0.0437  ? 
-0.0300 ? 0.0190  ? 0.2193 ? -0.0911 ? -0.0295 ? -0.0297 ? -0.0083 ? 0.0590  ? 0.0276  ? 0.0078  ? 0.0794  ? 0.0180  ? 0.0440  ? 
-0.0000 ? 
8  'X-RAY DIFFRACTION' ? refined -9.1921 43.8735 50.7176 0.2247 ? 0.0031  ? 0.0210  ? 0.2643 ? 0.0053  ? 0.2771 ? 0.0420  ? 0.0794 
? 0.1001  ? 0.3263 ? -0.0927 ? 0.2044  ? 0.0196  ? 0.0381  ? 0.0166  ? 0.1498  ? 0.0132  ? 0.1013  ? -0.0511 ? -0.0104 ? -0.0000 ? 
9  'X-RAY DIFFRACTION' ? refined 4.9807  43.1270 40.3608 0.2289 ? 0.0031  ? -0.0082 ? 0.2310 ? 0.0157  ? 0.2321 ? 0.2428  ? 
-0.1488 ? 0.0647  ? 0.3472 ? -0.0092 ? 0.1471  ? 0.0211  ? 0.0179  ? 0.0732  ? -0.0704 ? -0.0585 ? 0.0624  ? -0.1191 ? -0.0191 ? 
0.0000  ? 
10 'X-RAY DIFFRACTION' ? refined 14.9806 31.6041 36.6703 0.2104 ? 0.0156  ? 0.0072  ? 0.2367 ? 0.0332  ? 0.1946 ? -0.0333 ? 0.0084 
? 0.0627  ? 0.1488 ? 0.0611  ? 0.0358  ? 0.0556  ? 0.0288  ? -0.0790 ? -0.1091 ? -0.0454 ? -0.1310 ? 0.2101  ? 0.1309  ? 0.0000  ? 
11 'X-RAY DIFFRACTION' ? refined 14.4591 9.6600  49.8666 0.2892 ? -0.0085 ? 0.0173  ? 0.2595 ? 0.0056  ? 0.2475 ? 0.0272  ? 
-0.0480 ? 0.0581  ? 0.0477 ? -0.0754 ? 0.1402  ? -0.0302 ? 0.0144  ? 0.0524  ? 0.1452  ? -0.0557 ? 0.0479  ? 0.1043  ? 0.0281  ? 
0.0000  ? 
# 
loop_
_pdbx_refine_tls_group.id 
_pdbx_refine_tls_group.pdbx_refine_id 
_pdbx_refine_tls_group.refine_tls_id 
_pdbx_refine_tls_group.beg_label_asym_id 
_pdbx_refine_tls_group.beg_label_seq_id 
_pdbx_refine_tls_group.beg_auth_asym_id 
_pdbx_refine_tls_group.beg_auth_seq_id 
_pdbx_refine_tls_group.beg_PDB_ins_code 
_pdbx_refine_tls_group.end_label_asym_id 
_pdbx_refine_tls_group.end_label_seq_id 
_pdbx_refine_tls_group.end_auth_asym_id 
_pdbx_refine_tls_group.end_auth_seq_id 
_pdbx_refine_tls_group.end_PDB_ins_code 
_pdbx_refine_tls_group.selection 
_pdbx_refine_tls_group.selection_details 
1  'X-RAY DIFFRACTION' 1  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 1 through 26 )
;
2  'X-RAY DIFFRACTION' 2  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 27 through 44 )
;
3  'X-RAY DIFFRACTION' 3  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 45 through 66 )
;
4  'X-RAY DIFFRACTION' 4  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 67 through 96 )
;
5  'X-RAY DIFFRACTION' 5  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 97 through 130 )
;
6  'X-RAY DIFFRACTION' 6  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 131 through 159 )
;
7  'X-RAY DIFFRACTION' 7  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 160 through 185 )
;
8  'X-RAY DIFFRACTION' 8  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 186 through 220 )
;
9  'X-RAY DIFFRACTION' 9  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 221 through 269 )
;
10 'X-RAY DIFFRACTION' 10 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 270 through 286 )
;
11 'X-RAY DIFFRACTION' 11 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 287 through 306 )
;
# 
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 MET 0   ? A MET 1   
2 1 Y 1 A ASN 307 ? A ASN 308 
3 1 Y 1 A SER 308 ? A SER 309 
# 
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 
2HP P    P  N N 1   
2HP O1   O  N N 2   
2HP O2   O  N N 3   
2HP O3   O  N N 4   
2HP O4   O  N N 5   
2HP HO3  H  N N 6   
2HP HO4  H  N N 7   
ALA N    N  N N 8   
ALA CA   C  N S 9   
ALA C    C  N N 10  
ALA O    O  N N 11  
ALA CB   C  N N 12  
ALA OXT  O  N N 13  
ALA H    H  N N 14  
ALA H2   H  N N 15  
ALA HA   H  N N 16  
ALA HB1  H  N N 17  
ALA HB2  H  N N 18  
ALA HB3  H  N N 19  
ALA HXT  H  N N 20  
ARG N    N  N N 21  
ARG CA   C  N S 22  
ARG C    C  N N 23  
ARG O    O  N N 24  
ARG CB   C  N N 25  
ARG CG   C  N N 26  
ARG CD   C  N N 27  
ARG NE   N  N N 28  
ARG CZ   C  N N 29  
ARG NH1  N  N N 30  
ARG NH2  N  N N 31  
ARG OXT  O  N N 32  
ARG H    H  N N 33  
ARG H2   H  N N 34  
ARG HA   H  N N 35  
ARG HB2  H  N N 36  
ARG HB3  H  N N 37  
ARG HG2  H  N N 38  
ARG HG3  H  N N 39  
ARG HD2  H  N N 40  
ARG HD3  H  N N 41  
ARG HE   H  N N 42  
ARG HH11 H  N N 43  
ARG HH12 H  N N 44  
ARG HH21 H  N N 45  
ARG HH22 H  N N 46  
ARG HXT  H  N N 47  
ASN N    N  N N 48  
ASN CA   C  N S 49  
ASN C    C  N N 50  
ASN O    O  N N 51  
ASN CB   C  N N 52  
ASN CG   C  N N 53  
ASN OD1  O  N N 54  
ASN ND2  N  N N 55  
ASN OXT  O  N N 56  
ASN H    H  N N 57  
ASN H2   H  N N 58  
ASN HA   H  N N 59  
ASN HB2  H  N N 60  
ASN HB3  H  N N 61  
ASN HD21 H  N N 62  
ASN HD22 H  N N 63  
ASN HXT  H  N N 64  
ASP N    N  N N 65  
ASP CA   C  N S 66  
ASP C    C  N N 67  
ASP O    O  N N 68  
ASP CB   C  N N 69  
ASP CG   C  N N 70  
ASP OD1  O  N N 71  
ASP OD2  O  N N 72  
ASP OXT  O  N N 73  
ASP H    H  N N 74  
ASP H2   H  N N 75  
ASP HA   H  N N 76  
ASP HB2  H  N N 77  
ASP HB3  H  N N 78  
ASP HD2  H  N N 79  
ASP HXT  H  N N 80  
CA  CA   CA N N 81  
CYS N    N  N N 82  
CYS CA   C  N R 83  
CYS C    C  N N 84  
CYS O    O  N N 85  
CYS CB   C  N N 86  
CYS SG   S  N N 87  
CYS OXT  O  N N 88  
CYS H    H  N N 89  
CYS H2   H  N N 90  
CYS HA   H  N N 91  
CYS HB2  H  N N 92  
CYS HB3  H  N N 93  
CYS HG   H  N N 94  
CYS HXT  H  N N 95  
EDO C1   C  N N 96  
EDO O1   O  N N 97  
EDO C2   C  N N 98  
EDO O2   O  N N 99  
EDO H11  H  N N 100 
EDO H12  H  N N 101 
EDO HO1  H  N N 102 
EDO H21  H  N N 103 
EDO H22  H  N N 104 
EDO HO2  H  N N 105 
GLN N    N  N N 106 
GLN CA   C  N S 107 
GLN C    C  N N 108 
GLN O    O  N N 109 
GLN CB   C  N N 110 
GLN CG   C  N N 111 
GLN CD   C  N N 112 
GLN OE1  O  N N 113 
GLN NE2  N  N N 114 
GLN OXT  O  N N 115 
GLN H    H  N N 116 
GLN H2   H  N N 117 
GLN HA   H  N N 118 
GLN HB2  H  N N 119 
GLN HB3  H  N N 120 
GLN HG2  H  N N 121 
GLN HG3  H  N N 122 
GLN HE21 H  N N 123 
GLN HE22 H  N N 124 
GLN HXT  H  N N 125 
GLU N    N  N N 126 
GLU CA   C  N S 127 
GLU C    C  N N 128 
GLU O    O  N N 129 
GLU CB   C  N N 130 
GLU CG   C  N N 131 
GLU CD   C  N N 132 
GLU OE1  O  N N 133 
GLU OE2  O  N N 134 
GLU OXT  O  N N 135 
GLU H    H  N N 136 
GLU H2   H  N N 137 
GLU HA   H  N N 138 
GLU HB2  H  N N 139 
GLU HB3  H  N N 140 
GLU HG2  H  N N 141 
GLU HG3  H  N N 142 
GLU HE2  H  N N 143 
GLU HXT  H  N N 144 
GLY N    N  N N 145 
GLY CA   C  N N 146 
GLY C    C  N N 147 
GLY O    O  N N 148 
GLY OXT  O  N N 149 
GLY H    H  N N 150 
GLY H2   H  N N 151 
GLY HA2  H  N N 152 
GLY HA3  H  N N 153 
GLY HXT  H  N N 154 
HEM CHA  C  N N 155 
HEM CHB  C  N N 156 
HEM CHC  C  N N 157 
HEM CHD  C  N N 158 
HEM C1A  C  Y N 159 
HEM C2A  C  Y N 160 
HEM C3A  C  Y N 161 
HEM C4A  C  Y N 162 
HEM CMA  C  N N 163 
HEM CAA  C  N N 164 
HEM CBA  C  N N 165 
HEM CGA  C  N N 166 
HEM O1A  O  N N 167 
HEM O2A  O  N N 168 
HEM C1B  C  N N 169 
HEM C2B  C  N N 170 
HEM C3B  C  N N 171 
HEM C4B  C  N N 172 
HEM CMB  C  N N 173 
HEM CAB  C  N N 174 
HEM CBB  C  N N 175 
HEM C1C  C  Y N 176 
HEM C2C  C  Y N 177 
HEM C3C  C  Y N 178 
HEM C4C  C  Y N 179 
HEM CMC  C  N N 180 
HEM CAC  C  N N 181 
HEM CBC  C  N N 182 
HEM C1D  C  N N 183 
HEM C2D  C  N N 184 
HEM C3D  C  N N 185 
HEM C4D  C  N N 186 
HEM CMD  C  N N 187 
HEM CAD  C  N N 188 
HEM CBD  C  N N 189 
HEM CGD  C  N N 190 
HEM O1D  O  N N 191 
HEM O2D  O  N N 192 
HEM NA   N  Y N 193 
HEM NB   N  N N 194 
HEM NC   N  Y N 195 
HEM ND   N  N N 196 
HEM FE   FE N N 197 
HEM HHB  H  N N 198 
HEM HHC  H  N N 199 
HEM HHD  H  N N 200 
HEM HMA  H  N N 201 
HEM HMAA H  N N 202 
HEM HMAB H  N N 203 
HEM HAA  H  N N 204 
HEM HAAA H  N N 205 
HEM HBA  H  N N 206 
HEM HBAA H  N N 207 
HEM HMB  H  N N 208 
HEM HMBA H  N N 209 
HEM HMBB H  N N 210 
HEM HAB  H  N N 211 
HEM HBB  H  N N 212 
HEM HBBA H  N N 213 
HEM HMC  H  N N 214 
HEM HMCA H  N N 215 
HEM HMCB H  N N 216 
HEM HAC  H  N N 217 
HEM HBC  H  N N 218 
HEM HBCA H  N N 219 
HEM HMD  H  N N 220 
HEM HMDA H  N N 221 
HEM HMDB H  N N 222 
HEM HAD  H  N N 223 
HEM HADA H  N N 224 
HEM HBD  H  N N 225 
HEM HBDA H  N N 226 
HEM H2A  H  N N 227 
HEM H2D  H  N N 228 
HEM HHA  H  N N 229 
HIS N    N  N N 230 
HIS CA   C  N S 231 
HIS C    C  N N 232 
HIS O    O  N N 233 
HIS CB   C  N N 234 
HIS CG   C  Y N 235 
HIS ND1  N  Y N 236 
HIS CD2  C  Y N 237 
HIS CE1  C  Y N 238 
HIS NE2  N  Y N 239 
HIS OXT  O  N N 240 
HIS H    H  N N 241 
HIS H2   H  N N 242 
HIS HA   H  N N 243 
HIS HB2  H  N N 244 
HIS HB3  H  N N 245 
HIS HD1  H  N N 246 
HIS HD2  H  N N 247 
HIS HE1  H  N N 248 
HIS HE2  H  N N 249 
HIS HXT  H  N N 250 
HOH O    O  N N 251 
HOH H1   H  N N 252 
HOH H2   H  N N 253 
ILE N    N  N N 254 
ILE CA   C  N S 255 
ILE C    C  N N 256 
ILE O    O  N N 257 
ILE CB   C  N S 258 
ILE CG1  C  N N 259 
ILE CG2  C  N N 260 
ILE CD1  C  N N 261 
ILE OXT  O  N N 262 
ILE H    H  N N 263 
ILE H2   H  N N 264 
ILE HA   H  N N 265 
ILE HB   H  N N 266 
ILE HG12 H  N N 267 
ILE HG13 H  N N 268 
ILE HG21 H  N N 269 
ILE HG22 H  N N 270 
ILE HG23 H  N N 271 
ILE HD11 H  N N 272 
ILE HD12 H  N N 273 
ILE HD13 H  N N 274 
ILE HXT  H  N N 275 
LEU N    N  N N 276 
LEU CA   C  N S 277 
LEU C    C  N N 278 
LEU O    O  N N 279 
LEU CB   C  N N 280 
LEU CG   C  N N 281 
LEU CD1  C  N N 282 
LEU CD2  C  N N 283 
LEU OXT  O  N N 284 
LEU H    H  N N 285 
LEU H2   H  N N 286 
LEU HA   H  N N 287 
LEU HB2  H  N N 288 
LEU HB3  H  N N 289 
LEU HG   H  N N 290 
LEU HD11 H  N N 291 
LEU HD12 H  N N 292 
LEU HD13 H  N N 293 
LEU HD21 H  N N 294 
LEU HD22 H  N N 295 
LEU HD23 H  N N 296 
LEU HXT  H  N N 297 
LYS N    N  N N 298 
LYS CA   C  N S 299 
LYS C    C  N N 300 
LYS O    O  N N 301 
LYS CB   C  N N 302 
LYS CG   C  N N 303 
LYS CD   C  N N 304 
LYS CE   C  N N 305 
LYS NZ   N  N N 306 
LYS OXT  O  N N 307 
LYS H    H  N N 308 
LYS H2   H  N N 309 
LYS HA   H  N N 310 
LYS HB2  H  N N 311 
LYS HB3  H  N N 312 
LYS HG2  H  N N 313 
LYS HG3  H  N N 314 
LYS HD2  H  N N 315 
LYS HD3  H  N N 316 
LYS HE2  H  N N 317 
LYS HE3  H  N N 318 
LYS HZ1  H  N N 319 
LYS HZ2  H  N N 320 
LYS HZ3  H  N N 321 
LYS HXT  H  N N 322 
MET N    N  N N 323 
MET CA   C  N S 324 
MET C    C  N N 325 
MET O    O  N N 326 
MET CB   C  N N 327 
MET CG   C  N N 328 
MET SD   S  N N 329 
MET CE   C  N N 330 
MET OXT  O  N N 331 
MET H    H  N N 332 
MET H2   H  N N 333 
MET HA   H  N N 334 
MET HB2  H  N N 335 
MET HB3  H  N N 336 
MET HG2  H  N N 337 
MET HG3  H  N N 338 
MET HE1  H  N N 339 
MET HE2  H  N N 340 
MET HE3  H  N N 341 
MET HXT  H  N N 342 
PHE N    N  N N 343 
PHE CA   C  N S 344 
PHE C    C  N N 345 
PHE O    O  N N 346 
PHE CB   C  N N 347 
PHE CG   C  Y N 348 
PHE CD1  C  Y N 349 
PHE CD2  C  Y N 350 
PHE CE1  C  Y N 351 
PHE CE2  C  Y N 352 
PHE CZ   C  Y N 353 
PHE OXT  O  N N 354 
PHE H    H  N N 355 
PHE H2   H  N N 356 
PHE HA   H  N N 357 
PHE HB2  H  N N 358 
PHE HB3  H  N N 359 
PHE HD1  H  N N 360 
PHE HD2  H  N N 361 
PHE HE1  H  N N 362 
PHE HE2  H  N N 363 
PHE HZ   H  N N 364 
PHE HXT  H  N N 365 
PRO N    N  N N 366 
PRO CA   C  N S 367 
PRO C    C  N N 368 
PRO O    O  N N 369 
PRO CB   C  N N 370 
PRO CG   C  N N 371 
PRO CD   C  N N 372 
PRO OXT  O  N N 373 
PRO H    H  N N 374 
PRO HA   H  N N 375 
PRO HB2  H  N N 376 
PRO HB3  H  N N 377 
PRO HG2  H  N N 378 
PRO HG3  H  N N 379 
PRO HD2  H  N N 380 
PRO HD3  H  N N 381 
PRO HXT  H  N N 382 
SER N    N  N N 383 
SER CA   C  N S 384 
SER C    C  N N 385 
SER O    O  N N 386 
SER CB   C  N N 387 
SER OG   O  N N 388 
SER OXT  O  N N 389 
SER H    H  N N 390 
SER H2   H  N N 391 
SER HA   H  N N 392 
SER HB2  H  N N 393 
SER HB3  H  N N 394 
SER HG   H  N N 395 
SER HXT  H  N N 396 
THR N    N  N N 397 
THR CA   C  N S 398 
THR C    C  N N 399 
THR O    O  N N 400 
THR CB   C  N R 401 
THR OG1  O  N N 402 
THR CG2  C  N N 403 
THR OXT  O  N N 404 
THR H    H  N N 405 
THR H2   H  N N 406 
THR HA   H  N N 407 
THR HB   H  N N 408 
THR HG1  H  N N 409 
THR HG21 H  N N 410 
THR HG22 H  N N 411 
THR HG23 H  N N 412 
THR HXT  H  N N 413 
TRP N    N  N N 414 
TRP CA   C  N S 415 
TRP C    C  N N 416 
TRP O    O  N N 417 
TRP CB   C  N N 418 
TRP CG   C  Y N 419 
TRP CD1  C  Y N 420 
TRP CD2  C  Y N 421 
TRP NE1  N  Y N 422 
TRP CE2  C  Y N 423 
TRP CE3  C  Y N 424 
TRP CZ2  C  Y N 425 
TRP CZ3  C  Y N 426 
TRP CH2  C  Y N 427 
TRP OXT  O  N N 428 
TRP H    H  N N 429 
TRP H2   H  N N 430 
TRP HA   H  N N 431 
TRP HB2  H  N N 432 
TRP HB3  H  N N 433 
TRP HD1  H  N N 434 
TRP HE1  H  N N 435 
TRP HE3  H  N N 436 
TRP HZ2  H  N N 437 
TRP HZ3  H  N N 438 
TRP HH2  H  N N 439 
TRP HXT  H  N N 440 
TYR N    N  N N 441 
TYR CA   C  N S 442 
TYR C    C  N N 443 
TYR O    O  N N 444 
TYR CB   C  N N 445 
TYR CG   C  Y N 446 
TYR CD1  C  Y N 447 
TYR CD2  C  Y N 448 
TYR CE1  C  Y N 449 
TYR CE2  C  Y N 450 
TYR CZ   C  Y N 451 
TYR OH   O  N N 452 
TYR OXT  O  N N 453 
TYR H    H  N N 454 
TYR H2   H  N N 455 
TYR HA   H  N N 456 
TYR HB2  H  N N 457 
TYR HB3  H  N N 458 
TYR HD1  H  N N 459 
TYR HD2  H  N N 460 
TYR HE1  H  N N 461 
TYR HE2  H  N N 462 
TYR HH   H  N N 463 
TYR HXT  H  N N 464 
VAL N    N  N N 465 
VAL CA   C  N S 466 
VAL C    C  N N 467 
VAL O    O  N N 468 
VAL CB   C  N N 469 
VAL CG1  C  N N 470 
VAL CG2  C  N N 471 
VAL OXT  O  N N 472 
VAL H    H  N N 473 
VAL H2   H  N N 474 
VAL HA   H  N N 475 
VAL HB   H  N N 476 
VAL HG11 H  N N 477 
VAL HG12 H  N N 478 
VAL HG13 H  N N 479 
VAL HG21 H  N N 480 
VAL HG22 H  N N 481 
VAL HG23 H  N N 482 
VAL HXT  H  N N 483 
# 
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 
2HP P   O1   doub N N 1   
2HP P   O2   sing N N 2   
2HP P   O3   sing N N 3   
2HP P   O4   sing N N 4   
2HP O3  HO3  sing N N 5   
2HP O4  HO4  sing N N 6   
ALA N   CA   sing N N 7   
ALA N   H    sing N N 8   
ALA N   H2   sing N N 9   
ALA CA  C    sing N N 10  
ALA CA  CB   sing N N 11  
ALA CA  HA   sing N N 12  
ALA C   O    doub N N 13  
ALA C   OXT  sing N N 14  
ALA CB  HB1  sing N N 15  
ALA CB  HB2  sing N N 16  
ALA CB  HB3  sing N N 17  
ALA OXT HXT  sing N N 18  
ARG N   CA   sing N N 19  
ARG N   H    sing N N 20  
ARG N   H2   sing N N 21  
ARG CA  C    sing N N 22  
ARG CA  CB   sing N N 23  
ARG CA  HA   sing N N 24  
ARG C   O    doub N N 25  
ARG C   OXT  sing N N 26  
ARG CB  CG   sing N N 27  
ARG CB  HB2  sing N N 28  
ARG CB  HB3  sing N N 29  
ARG CG  CD   sing N N 30  
ARG CG  HG2  sing N N 31  
ARG CG  HG3  sing N N 32  
ARG CD  NE   sing N N 33  
ARG CD  HD2  sing N N 34  
ARG CD  HD3  sing N N 35  
ARG NE  CZ   sing N N 36  
ARG NE  HE   sing N N 37  
ARG CZ  NH1  sing N N 38  
ARG CZ  NH2  doub N N 39  
ARG NH1 HH11 sing N N 40  
ARG NH1 HH12 sing N N 41  
ARG NH2 HH21 sing N N 42  
ARG NH2 HH22 sing N N 43  
ARG OXT HXT  sing N N 44  
ASN N   CA   sing N N 45  
ASN N   H    sing N N 46  
ASN N   H2   sing N N 47  
ASN CA  C    sing N N 48  
ASN CA  CB   sing N N 49  
ASN CA  HA   sing N N 50  
ASN C   O    doub N N 51  
ASN C   OXT  sing N N 52  
ASN CB  CG   sing N N 53  
ASN CB  HB2  sing N N 54  
ASN CB  HB3  sing N N 55  
ASN CG  OD1  doub N N 56  
ASN CG  ND2  sing N N 57  
ASN ND2 HD21 sing N N 58  
ASN ND2 HD22 sing N N 59  
ASN OXT HXT  sing N N 60  
ASP N   CA   sing N N 61  
ASP N   H    sing N N 62  
ASP N   H2   sing N N 63  
ASP CA  C    sing N N 64  
ASP CA  CB   sing N N 65  
ASP CA  HA   sing N N 66  
ASP C   O    doub N N 67  
ASP C   OXT  sing N N 68  
ASP CB  CG   sing N N 69  
ASP CB  HB2  sing N N 70  
ASP CB  HB3  sing N N 71  
ASP CG  OD1  doub N N 72  
ASP CG  OD2  sing N N 73  
ASP OD2 HD2  sing N N 74  
ASP OXT HXT  sing N N 75  
CYS N   CA   sing N N 76  
CYS N   H    sing N N 77  
CYS N   H2   sing N N 78  
CYS CA  C    sing N N 79  
CYS CA  CB   sing N N 80  
CYS CA  HA   sing N N 81  
CYS C   O    doub N N 82  
CYS C   OXT  sing N N 83  
CYS CB  SG   sing N N 84  
CYS CB  HB2  sing N N 85  
CYS CB  HB3  sing N N 86  
CYS SG  HG   sing N N 87  
CYS OXT HXT  sing N N 88  
EDO C1  O1   sing N N 89  
EDO C1  C2   sing N N 90  
EDO C1  H11  sing N N 91  
EDO C1  H12  sing N N 92  
EDO O1  HO1  sing N N 93  
EDO C2  O2   sing N N 94  
EDO C2  H21  sing N N 95  
EDO C2  H22  sing N N 96  
EDO O2  HO2  sing N N 97  
GLN N   CA   sing N N 98  
GLN N   H    sing N N 99  
GLN N   H2   sing N N 100 
GLN CA  C    sing N N 101 
GLN CA  CB   sing N N 102 
GLN CA  HA   sing N N 103 
GLN C   O    doub N N 104 
GLN C   OXT  sing N N 105 
GLN CB  CG   sing N N 106 
GLN CB  HB2  sing N N 107 
GLN CB  HB3  sing N N 108 
GLN CG  CD   sing N N 109 
GLN CG  HG2  sing N N 110 
GLN CG  HG3  sing N N 111 
GLN CD  OE1  doub N N 112 
GLN CD  NE2  sing N N 113 
GLN NE2 HE21 sing N N 114 
GLN NE2 HE22 sing N N 115 
GLN OXT HXT  sing N N 116 
GLU N   CA   sing N N 117 
GLU N   H    sing N N 118 
GLU N   H2   sing N N 119 
GLU CA  C    sing N N 120 
GLU CA  CB   sing N N 121 
GLU CA  HA   sing N N 122 
GLU C   O    doub N N 123 
GLU C   OXT  sing N N 124 
GLU CB  CG   sing N N 125 
GLU CB  HB2  sing N N 126 
GLU CB  HB3  sing N N 127 
GLU CG  CD   sing N N 128 
GLU CG  HG2  sing N N 129 
GLU CG  HG3  sing N N 130 
GLU CD  OE1  doub N N 131 
GLU CD  OE2  sing N N 132 
GLU OE2 HE2  sing N N 133 
GLU OXT HXT  sing N N 134 
GLY N   CA   sing N N 135 
GLY N   H    sing N N 136 
GLY N   H2   sing N N 137 
GLY CA  C    sing N N 138 
GLY CA  HA2  sing N N 139 
GLY CA  HA3  sing N N 140 
GLY C   O    doub N N 141 
GLY C   OXT  sing N N 142 
GLY OXT HXT  sing N N 143 
HEM CHA C1A  sing N N 144 
HEM CHA C4D  doub N N 145 
HEM CHA HHA  sing N N 146 
HEM CHB C4A  sing N N 147 
HEM CHB C1B  doub N N 148 
HEM CHB HHB  sing N N 149 
HEM CHC C4B  sing N N 150 
HEM CHC C1C  doub N N 151 
HEM CHC HHC  sing N N 152 
HEM CHD C4C  doub N N 153 
HEM CHD C1D  sing N N 154 
HEM CHD HHD  sing N N 155 
HEM C1A C2A  doub Y N 156 
HEM C1A NA   sing Y N 157 
HEM C2A C3A  sing Y N 158 
HEM C2A CAA  sing N N 159 
HEM C3A C4A  doub Y N 160 
HEM C3A CMA  sing N N 161 
HEM C4A NA   sing Y N 162 
HEM CMA HMA  sing N N 163 
HEM CMA HMAA sing N N 164 
HEM CMA HMAB sing N N 165 
HEM CAA CBA  sing N N 166 
HEM CAA HAA  sing N N 167 
HEM CAA HAAA sing N N 168 
HEM CBA CGA  sing N N 169 
HEM CBA HBA  sing N N 170 
HEM CBA HBAA sing N N 171 
HEM CGA O1A  doub N N 172 
HEM CGA O2A  sing N N 173 
HEM C1B C2B  sing N N 174 
HEM C1B NB   sing N N 175 
HEM C2B C3B  doub N N 176 
HEM C2B CMB  sing N N 177 
HEM C3B C4B  sing N N 178 
HEM C3B CAB  sing N N 179 
HEM C4B NB   doub N N 180 
HEM CMB HMB  sing N N 181 
HEM CMB HMBA sing N N 182 
HEM CMB HMBB sing N N 183 
HEM CAB CBB  doub N N 184 
HEM CAB HAB  sing N N 185 
HEM CBB HBB  sing N N 186 
HEM CBB HBBA sing N N 187 
HEM C1C C2C  sing Y N 188 
HEM C1C NC   sing Y N 189 
HEM C2C C3C  doub Y N 190 
HEM C2C CMC  sing N N 191 
HEM C3C C4C  sing Y N 192 
HEM C3C CAC  sing N N 193 
HEM C4C NC   sing Y N 194 
HEM CMC HMC  sing N N 195 
HEM CMC HMCA sing N N 196 
HEM CMC HMCB sing N N 197 
HEM CAC CBC  doub N N 198 
HEM CAC HAC  sing N N 199 
HEM CBC HBC  sing N N 200 
HEM CBC HBCA sing N N 201 
HEM C1D C2D  sing N N 202 
HEM C1D ND   doub N N 203 
HEM C2D C3D  doub N N 204 
HEM C2D CMD  sing N N 205 
HEM C3D C4D  sing N N 206 
HEM C3D CAD  sing N N 207 
HEM C4D ND   sing N N 208 
HEM CMD HMD  sing N N 209 
HEM CMD HMDA sing N N 210 
HEM CMD HMDB sing N N 211 
HEM CAD CBD  sing N N 212 
HEM CAD HAD  sing N N 213 
HEM CAD HADA sing N N 214 
HEM CBD CGD  sing N N 215 
HEM CBD HBD  sing N N 216 
HEM CBD HBDA sing N N 217 
HEM CGD O1D  doub N N 218 
HEM CGD O2D  sing N N 219 
HEM O2A H2A  sing N N 220 
HEM O2D H2D  sing N N 221 
HEM FE  NA   sing N N 222 
HEM FE  NB   sing N N 223 
HEM FE  NC   sing N N 224 
HEM FE  ND   sing N N 225 
HIS N   CA   sing N N 226 
HIS N   H    sing N N 227 
HIS N   H2   sing N N 228 
HIS CA  C    sing N N 229 
HIS CA  CB   sing N N 230 
HIS CA  HA   sing N N 231 
HIS C   O    doub N N 232 
HIS C   OXT  sing N N 233 
HIS CB  CG   sing N N 234 
HIS CB  HB2  sing N N 235 
HIS CB  HB3  sing N N 236 
HIS CG  ND1  sing Y N 237 
HIS CG  CD2  doub Y N 238 
HIS ND1 CE1  doub Y N 239 
HIS ND1 HD1  sing N N 240 
HIS CD2 NE2  sing Y N 241 
HIS CD2 HD2  sing N N 242 
HIS CE1 NE2  sing Y N 243 
HIS CE1 HE1  sing N N 244 
HIS NE2 HE2  sing N N 245 
HIS OXT HXT  sing N N 246 
HOH O   H1   sing N N 247 
HOH O   H2   sing N N 248 
ILE N   CA   sing N N 249 
ILE N   H    sing N N 250 
ILE N   H2   sing N N 251 
ILE CA  C    sing N N 252 
ILE CA  CB   sing N N 253 
ILE CA  HA   sing N N 254 
ILE C   O    doub N N 255 
ILE C   OXT  sing N N 256 
ILE CB  CG1  sing N N 257 
ILE CB  CG2  sing N N 258 
ILE CB  HB   sing N N 259 
ILE CG1 CD1  sing N N 260 
ILE CG1 HG12 sing N N 261 
ILE CG1 HG13 sing N N 262 
ILE CG2 HG21 sing N N 263 
ILE CG2 HG22 sing N N 264 
ILE CG2 HG23 sing N N 265 
ILE CD1 HD11 sing N N 266 
ILE CD1 HD12 sing N N 267 
ILE CD1 HD13 sing N N 268 
ILE OXT HXT  sing N N 269 
LEU N   CA   sing N N 270 
LEU N   H    sing N N 271 
LEU N   H2   sing N N 272 
LEU CA  C    sing N N 273 
LEU CA  CB   sing N N 274 
LEU CA  HA   sing N N 275 
LEU C   O    doub N N 276 
LEU C   OXT  sing N N 277 
LEU CB  CG   sing N N 278 
LEU CB  HB2  sing N N 279 
LEU CB  HB3  sing N N 280 
LEU CG  CD1  sing N N 281 
LEU CG  CD2  sing N N 282 
LEU CG  HG   sing N N 283 
LEU CD1 HD11 sing N N 284 
LEU CD1 HD12 sing N N 285 
LEU CD1 HD13 sing N N 286 
LEU CD2 HD21 sing N N 287 
LEU CD2 HD22 sing N N 288 
LEU CD2 HD23 sing N N 289 
LEU OXT HXT  sing N N 290 
LYS N   CA   sing N N 291 
LYS N   H    sing N N 292 
LYS N   H2   sing N N 293 
LYS CA  C    sing N N 294 
LYS CA  CB   sing N N 295 
LYS CA  HA   sing N N 296 
LYS C   O    doub N N 297 
LYS C   OXT  sing N N 298 
LYS CB  CG   sing N N 299 
LYS CB  HB2  sing N N 300 
LYS CB  HB3  sing N N 301 
LYS CG  CD   sing N N 302 
LYS CG  HG2  sing N N 303 
LYS CG  HG3  sing N N 304 
LYS CD  CE   sing N N 305 
LYS CD  HD2  sing N N 306 
LYS CD  HD3  sing N N 307 
LYS CE  NZ   sing N N 308 
LYS CE  HE2  sing N N 309 
LYS CE  HE3  sing N N 310 
LYS NZ  HZ1  sing N N 311 
LYS NZ  HZ2  sing N N 312 
LYS NZ  HZ3  sing N N 313 
LYS OXT HXT  sing N N 314 
MET N   CA   sing N N 315 
MET N   H    sing N N 316 
MET N   H2   sing N N 317 
MET CA  C    sing N N 318 
MET CA  CB   sing N N 319 
MET CA  HA   sing N N 320 
MET C   O    doub N N 321 
MET C   OXT  sing N N 322 
MET CB  CG   sing N N 323 
MET CB  HB2  sing N N 324 
MET CB  HB3  sing N N 325 
MET CG  SD   sing N N 326 
MET CG  HG2  sing N N 327 
MET CG  HG3  sing N N 328 
MET SD  CE   sing N N 329 
MET CE  HE1  sing N N 330 
MET CE  HE2  sing N N 331 
MET CE  HE3  sing N N 332 
MET OXT HXT  sing N N 333 
PHE N   CA   sing N N 334 
PHE N   H    sing N N 335 
PHE N   H2   sing N N 336 
PHE CA  C    sing N N 337 
PHE CA  CB   sing N N 338 
PHE CA  HA   sing N N 339 
PHE C   O    doub N N 340 
PHE C   OXT  sing N N 341 
PHE CB  CG   sing N N 342 
PHE CB  HB2  sing N N 343 
PHE CB  HB3  sing N N 344 
PHE CG  CD1  doub Y N 345 
PHE CG  CD2  sing Y N 346 
PHE CD1 CE1  sing Y N 347 
PHE CD1 HD1  sing N N 348 
PHE CD2 CE2  doub Y N 349 
PHE CD2 HD2  sing N N 350 
PHE CE1 CZ   doub Y N 351 
PHE CE1 HE1  sing N N 352 
PHE CE2 CZ   sing Y N 353 
PHE CE2 HE2  sing N N 354 
PHE CZ  HZ   sing N N 355 
PHE OXT HXT  sing N N 356 
PRO N   CA   sing N N 357 
PRO N   CD   sing N N 358 
PRO N   H    sing N N 359 
PRO CA  C    sing N N 360 
PRO CA  CB   sing N N 361 
PRO CA  HA   sing N N 362 
PRO C   O    doub N N 363 
PRO C   OXT  sing N N 364 
PRO CB  CG   sing N N 365 
PRO CB  HB2  sing N N 366 
PRO CB  HB3  sing N N 367 
PRO CG  CD   sing N N 368 
PRO CG  HG2  sing N N 369 
PRO CG  HG3  sing N N 370 
PRO CD  HD2  sing N N 371 
PRO CD  HD3  sing N N 372 
PRO OXT HXT  sing N N 373 
SER N   CA   sing N N 374 
SER N   H    sing N N 375 
SER N   H2   sing N N 376 
SER CA  C    sing N N 377 
SER CA  CB   sing N N 378 
SER CA  HA   sing N N 379 
SER C   O    doub N N 380 
SER C   OXT  sing N N 381 
SER CB  OG   sing N N 382 
SER CB  HB2  sing N N 383 
SER CB  HB3  sing N N 384 
SER OG  HG   sing N N 385 
SER OXT HXT  sing N N 386 
THR N   CA   sing N N 387 
THR N   H    sing N N 388 
THR N   H2   sing N N 389 
THR CA  C    sing N N 390 
THR CA  CB   sing N N 391 
THR CA  HA   sing N N 392 
THR C   O    doub N N 393 
THR C   OXT  sing N N 394 
THR CB  OG1  sing N N 395 
THR CB  CG2  sing N N 396 
THR CB  HB   sing N N 397 
THR OG1 HG1  sing N N 398 
THR CG2 HG21 sing N N 399 
THR CG2 HG22 sing N N 400 
THR CG2 HG23 sing N N 401 
THR OXT HXT  sing N N 402 
TRP N   CA   sing N N 403 
TRP N   H    sing N N 404 
TRP N   H2   sing N N 405 
TRP CA  C    sing N N 406 
TRP CA  CB   sing N N 407 
TRP CA  HA   sing N N 408 
TRP C   O    doub N N 409 
TRP C   OXT  sing N N 410 
TRP CB  CG   sing N N 411 
TRP CB  HB2  sing N N 412 
TRP CB  HB3  sing N N 413 
TRP CG  CD1  doub Y N 414 
TRP CG  CD2  sing Y N 415 
TRP CD1 NE1  sing Y N 416 
TRP CD1 HD1  sing N N 417 
TRP CD2 CE2  doub Y N 418 
TRP CD2 CE3  sing Y N 419 
TRP NE1 CE2  sing Y N 420 
TRP NE1 HE1  sing N N 421 
TRP CE2 CZ2  sing Y N 422 
TRP CE3 CZ3  doub Y N 423 
TRP CE3 HE3  sing N N 424 
TRP CZ2 CH2  doub Y N 425 
TRP CZ2 HZ2  sing N N 426 
TRP CZ3 CH2  sing Y N 427 
TRP CZ3 HZ3  sing N N 428 
TRP CH2 HH2  sing N N 429 
TRP OXT HXT  sing N N 430 
TYR N   CA   sing N N 431 
TYR N   H    sing N N 432 
TYR N   H2   sing N N 433 
TYR CA  C    sing N N 434 
TYR CA  CB   sing N N 435 
TYR CA  HA   sing N N 436 
TYR C   O    doub N N 437 
TYR C   OXT  sing N N 438 
TYR CB  CG   sing N N 439 
TYR CB  HB2  sing N N 440 
TYR CB  HB3  sing N N 441 
TYR CG  CD1  doub Y N 442 
TYR CG  CD2  sing Y N 443 
TYR CD1 CE1  sing Y N 444 
TYR CD1 HD1  sing N N 445 
TYR CD2 CE2  doub Y N 446 
TYR CD2 HD2  sing N N 447 
TYR CE1 CZ   doub Y N 448 
TYR CE1 HE1  sing N N 449 
TYR CE2 CZ   sing Y N 450 
TYR CE2 HE2  sing N N 451 
TYR CZ  OH   sing N N 452 
TYR OH  HH   sing N N 453 
TYR OXT HXT  sing N N 454 
VAL N   CA   sing N N 455 
VAL N   H    sing N N 456 
VAL N   H2   sing N N 457 
VAL CA  C    sing N N 458 
VAL CA  CB   sing N N 459 
VAL CA  HA   sing N N 460 
VAL C   O    doub N N 461 
VAL C   OXT  sing N N 462 
VAL CB  CG1  sing N N 463 
VAL CB  CG2  sing N N 464 
VAL CB  HB   sing N N 465 
VAL CG1 HG11 sing N N 466 
VAL CG1 HG12 sing N N 467 
VAL CG1 HG13 sing N N 468 
VAL CG2 HG21 sing N N 469 
VAL CG2 HG22 sing N N 470 
VAL CG2 HG23 sing N N 471 
VAL OXT HXT  sing N N 472 
# 
_pdbx_audit_support.funding_organization   'Leverhulme Trust' 
_pdbx_audit_support.country                'United Kingdom' 
_pdbx_audit_support.grant_number           2024-263/4 
_pdbx_audit_support.ordinal                1 
# 
_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   1GW2 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    9H1M 
_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]   0.024902 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.014912 
_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]   0.008534 
_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  
CA 
FE 
N  
O  
P  
S  
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N   . GLN A 1 2   ? 26.675  19.169 42.596 1.00 53.34 ? 1   GLN A N   1 
ATOM   2    C  CA  . GLN A 1 2   ? 26.981  18.085 41.620 1.00 36.22 ? 1   GLN A CA  1 
ATOM   3    C  C   . GLN A 1 2   ? 25.711  17.504 41.008 1.00 34.61 ? 1   GLN A C   1 
ATOM   4    O  O   . GLN A 1 2   ? 25.738  16.425 40.418 1.00 36.11 ? 1   GLN A O   1 
ATOM   5    C  CB  . GLN A 1 2   ? 27.781  16.968 42.290 1.00 37.27 ? 1   GLN A CB  1 
ATOM   6    C  CG  . GLN A 1 2   ? 27.125  16.406 43.536 1.00 43.76 ? 1   GLN A CG  1 
ATOM   7    C  CD  . GLN A 1 2   ? 27.699  15.063 43.937 1.00 53.47 ? 1   GLN A CD  1 
ATOM   8    O  OE1 . GLN A 1 2   ? 28.814  14.977 44.449 1.00 61.19 ? 1   GLN A OE1 1 
ATOM   9    N  NE2 . GLN A 1 2   ? 26.939  14.002 43.695 1.00 51.85 ? 1   GLN A NE2 1 
ATOM   10   N  N   . LEU A 1 3   ? 24.595  18.209 41.164 1.00 28.82 ? 2   LEU A N   1 
ATOM   11   C  CA  . LEU A 1 3   ? 23.401  17.862 40.413 1.00 26.92 ? 2   LEU A CA  1 
ATOM   12   C  C   . LEU A 1 3   ? 23.653  18.097 38.925 1.00 29.66 ? 2   LEU A C   1 
ATOM   13   O  O   . LEU A 1 3   ? 24.370  19.027 38.535 1.00 28.41 ? 2   LEU A O   1 
ATOM   14   C  CB  . LEU A 1 3   ? 22.205  18.686 40.884 1.00 25.28 ? 2   LEU A CB  1 
ATOM   15   C  CG  . LEU A 1 3   ? 21.809  18.575 42.361 1.00 21.44 ? 2   LEU A CG  1 
ATOM   16   C  CD1 . LEU A 1 3   ? 20.586  19.437 42.657 1.00 27.42 ? 2   LEU A CD1 1 
ATOM   17   C  CD2 . LEU A 1 3   ? 21.556  17.130 42.773 1.00 23.46 ? 2   LEU A CD2 1 
ATOM   18   N  N   . THR A 1 4   ? 23.074  17.235 38.090 1.00 24.91 ? 3   THR A N   1 
ATOM   19   C  CA  . THR A 1 4   ? 23.287  17.296 36.643 1.00 25.55 ? 3   THR A CA  1 
ATOM   20   C  C   . THR A 1 4   ? 21.989  17.040 35.894 1.00 24.35 ? 3   THR A C   1 
ATOM   21   O  O   . THR A 1 4   ? 21.191  16.189 36.313 1.00 24.60 ? 3   THR A O   1 
ATOM   22   C  CB  . THR A 1 4   ? 24.327  16.268 36.180 1.00 30.61 ? 3   THR A CB  1 
ATOM   23   O  OG1 . THR A 1 4   ? 24.393  16.259 34.750 1.00 34.84 ? 3   THR A OG1 1 
ATOM   24   C  CG2 . THR A 1 4   ? 23.943  14.871 36.660 1.00 30.42 ? 3   THR A CG2 1 
ATOM   25   N  N   . PRO A 1 5   ? 21.752  17.735 34.775 1.00 24.11 ? 4   PRO A N   1 
ATOM   26   C  CA  . PRO A 1 5   ? 20.499  17.499 34.037 1.00 25.68 ? 4   PRO A CA  1 
ATOM   27   C  C   . PRO A 1 5   ? 20.429  16.131 33.389 1.00 24.06 ? 4   PRO A C   1 
ATOM   28   O  O   . PRO A 1 5   ? 19.335  15.711 32.988 1.00 28.51 ? 4   PRO A O   1 
ATOM   29   C  CB  . PRO A 1 5   ? 20.483  18.612 32.978 1.00 31.10 ? 4   PRO A CB  1 
ATOM   30   C  CG  . PRO A 1 5   ? 21.553  19.585 33.382 1.00 37.48 ? 4   PRO A CG  1 
ATOM   31   C  CD  . PRO A 1 5   ? 22.568  18.797 34.163 1.00 29.82 ? 4   PRO A CD  1 
ATOM   32   N  N   . THR A 1 6   ? 21.555  15.434 33.254 1.00 25.18 ? 5   THR A N   1 
ATOM   33   C  CA  . THR A 1 6   ? 21.627  14.169 32.539 1.00 26.77 ? 5   THR A CA  1 
ATOM   34   C  C   . THR A 1 6   ? 21.495  12.957 33.457 1.00 27.75 ? 5   THR A C   1 
ATOM   35   O  O   . THR A 1 6   ? 21.696  11.825 33.004 1.00 27.13 ? 5   THR A O   1 
ATOM   36   C  CB  . THR A 1 6   ? 22.951  14.093 31.774 1.00 31.20 ? 5   THR A CB  1 
ATOM   37   O  OG1 . THR A 1 6   ? 24.040  14.270 32.691 1.00 33.04 ? 5   THR A OG1 1 
ATOM   38   C  CG2 . THR A 1 6   ? 23.015  15.181 30.716 1.00 31.15 ? 5   THR A CG2 1 
ATOM   39   N  N   . PHE A 1 7   ? 21.134  13.166 34.720 1.00 27.01 ? 6   PHE A N   1 
ATOM   40   C  CA  . PHE A 1 7   ? 21.267  12.109 35.719 1.00 23.05 ? 6   PHE A CA  1 
ATOM   41   C  C   . PHE A 1 7   ? 20.503  10.844 35.338 1.00 27.99 ? 6   PHE A C   1 
ATOM   42   O  O   . PHE A 1 7   ? 20.982  9.733  35.588 1.00 27.39 ? 6   PHE A O   1 
ATOM   43   C  CB  . PHE A 1 7   ? 20.791  12.619 37.083 1.00 22.31 ? 6   PHE A CB  1 
ATOM   44   C  CG  . PHE A 1 7   ? 21.082  11.665 38.212 1.00 26.24 ? 6   PHE A CG  1 
ATOM   45   C  CD1 . PHE A 1 7   ? 22.332  11.623 38.786 1.00 22.63 ? 6   PHE A CD1 1 
ATOM   46   C  CD2 . PHE A 1 7   ? 20.098  10.807 38.680 1.00 23.13 ? 6   PHE A CD2 1 
ATOM   47   C  CE1 . PHE A 1 7   ? 22.610  10.747 39.814 1.00 24.61 ? 6   PHE A CE1 1 
ATOM   48   C  CE2 . PHE A 1 7   ? 20.374  9.923  39.712 1.00 24.69 ? 6   PHE A CE2 1 
ATOM   49   C  CZ  . PHE A 1 7   ? 21.630  9.900  40.275 1.00 26.07 ? 6   PHE A CZ  1 
ATOM   50   N  N   . TYR A 1 8   ? 19.308  10.978 34.760 1.00 24.35 ? 7   TYR A N   1 
ATOM   51   C  CA  . TYR A 1 8   ? 18.500  9.814  34.414 1.00 24.29 ? 7   TYR A CA  1 
ATOM   52   C  C   . TYR A 1 8   ? 18.574  9.456  32.932 1.00 27.50 ? 7   TYR A C   1 
ATOM   53   O  O   . TYR A 1 8   ? 17.804  8.608  32.471 1.00 28.53 ? 7   TYR A O   1 
ATOM   54   C  CB  . TYR A 1 8   ? 17.038  10.033 34.821 1.00 24.58 ? 7   TYR A CB  1 
ATOM   55   C  CG  . TYR A 1 8   ? 16.864  10.222 36.307 1.00 22.99 ? 7   TYR A CG  1 
ATOM   56   C  CD1 . TYR A 1 8   ? 17.101  9.174  37.186 1.00 25.26 ? 7   TYR A CD1 1 
ATOM   57   C  CD2 . TYR A 1 8   ? 16.490  11.451 36.835 1.00 24.32 ? 7   TYR A CD2 1 
ATOM   58   C  CE1 . TYR A 1 8   ? 16.968  9.344  38.543 1.00 23.88 ? 7   TYR A CE1 1 
ATOM   59   C  CE2 . TYR A 1 8   ? 16.350  11.628 38.192 1.00 23.11 ? 7   TYR A CE2 1 
ATOM   60   C  CZ  . TYR A 1 8   ? 16.588  10.572 39.043 1.00 22.61 ? 7   TYR A CZ  1 
ATOM   61   O  OH  . TYR A 1 8   ? 16.458  10.737 40.396 1.00 24.05 ? 7   TYR A OH  1 
ATOM   62   N  N   . ASP A 1 9   ? 19.489  10.064 32.174 1.00 27.86 ? 8   ASP A N   1 
ATOM   63   C  CA  . ASP A 1 9   ? 19.463  9.868  30.729 1.00 30.64 ? 8   ASP A CA  1 
ATOM   64   C  C   . ASP A 1 9   ? 19.676  8.406  30.354 1.00 32.64 ? 8   ASP A C   1 
ATOM   65   O  O   . ASP A 1 9   ? 19.173  7.956  29.319 1.00 36.49 ? 8   ASP A O   1 
ATOM   66   C  CB  . ASP A 1 9   ? 20.501  10.775 30.063 1.00 33.42 ? 8   ASP A CB  1 
ATOM   67   C  CG  . ASP A 1 9   ? 20.031  12.225 29.975 1.00 36.78 ? 8   ASP A CG  1 
ATOM   68   O  OD1 . ASP A 1 9   ? 18.867  12.504 30.350 1.00 38.44 ? 8   ASP A OD1 1 
ATOM   69   O  OD2 . ASP A 1 9   ? 20.818  13.089 29.539 1.00 39.83 ? 8   ASP A OD2 1 
ATOM   70   N  N   . ASN A 1 10  ? 20.366  7.635  31.192 1.00 32.40 ? 9   ASN A N   1 
ATOM   71   C  CA  . ASN A 1 10  ? 20.506  6.208  30.930 1.00 33.69 ? 9   ASN A CA  1 
ATOM   72   C  C   . ASN A 1 10  ? 19.459  5.377  31.666 1.00 33.09 ? 9   ASN A C   1 
ATOM   73   O  O   . ASN A 1 10  ? 18.927  4.410  31.106 1.00 39.64 ? 9   ASN A O   1 
ATOM   74   C  CB  . ASN A 1 10  ? 21.911  5.742  31.315 1.00 33.96 ? 9   ASN A CB  1 
ATOM   75   C  CG  . ASN A 1 10  ? 22.976  6.288  30.390 1.00 33.17 ? 9   ASN A CG  1 
ATOM   76   O  OD1 . ASN A 1 10  ? 22.791  6.336  29.175 1.00 34.46 ? 9   ASN A OD1 1 
ATOM   77   N  ND2 . ASN A 1 10  ? 24.097  6.709  30.961 1.00 34.62 ? 9   ASN A ND2 1 
ATOM   78   N  N   . SER A 1 11  ? 19.130  5.750  32.898 1.00 31.81 ? 10  SER A N   1 
ATOM   79   C  CA  . SER A 1 11  ? 18.333  4.898  33.777 1.00 30.87 ? 10  SER A CA  1 
ATOM   80   C  C   . SER A 1 11  ? 16.829  5.132  33.671 1.00 34.56 ? 10  SER A C   1 
ATOM   81   O  O   . SER A 1 11  ? 16.050  4.226  33.988 1.00 33.05 ? 10  SER A O   1 
ATOM   82   C  CB  . SER A 1 11  ? 18.770  5.109  35.222 1.00 29.95 ? 10  SER A CB  1 
ATOM   83   O  OG  . SER A 1 11  ? 18.699  6.486  35.551 1.00 30.28 ? 10  SER A OG  1 
ATOM   84   N  N   . CYS A 1 12  ? 16.393  6.318  33.268 1.00 31.28 ? 11  CYS A N   1 
ATOM   85   C  CA  . CYS A 1 12  ? 14.968  6.569  33.101 1.00 30.59 ? 11  CYS A CA  1 
ATOM   86   C  C   . CYS A 1 12  ? 14.803  7.747  32.155 1.00 28.52 ? 11  CYS A C   1 
ATOM   87   O  O   . CYS A 1 12  ? 14.373  8.832  32.569 1.00 30.08 ? 11  CYS A O   1 
ATOM   88   C  CB  . CYS A 1 12  ? 14.285  6.858  34.438 1.00 31.68 ? 11  CYS A CB  1 
ATOM   89   S  SG  . CYS A 1 12  ? 12.491  6.600  34.387 1.00 34.85 ? 11  CYS A SG  1 
ATOM   90   N  N   . PRO A 1 13  ? 15.156  7.579  30.883 1.00 27.17 ? 12  PRO A N   1 
ATOM   91   C  CA  . PRO A 1 13  ? 15.210  8.745  29.983 1.00 33.24 ? 12  PRO A CA  1 
ATOM   92   C  C   . PRO A 1 13  ? 13.861  9.387  29.738 1.00 33.56 ? 12  PRO A C   1 
ATOM   93   O  O   . PRO A 1 13  ? 13.813  10.581 29.421 1.00 37.28 ? 12  PRO A O   1 
ATOM   94   C  CB  . PRO A 1 13  ? 15.807  8.174  28.689 1.00 33.09 ? 12  PRO A CB  1 
ATOM   95   C  CG  . PRO A 1 13  ? 15.573  6.686  28.768 1.00 40.67 ? 12  PRO A CG  1 
ATOM   96   C  CD  . PRO A 1 13  ? 15.606  6.337  30.233 1.00 36.84 ? 12  PRO A CD  1 
ATOM   97   N  N   . ASN A 1 14  ? 12.763  8.652  29.892 1.00 31.50 ? 13  ASN A N   1 
ATOM   98   C  CA  . ASN A 1 14  ? 11.441  9.198  29.631 1.00 36.72 ? 13  ASN A CA  1 
ATOM   99   C  C   . ASN A 1 14  ? 10.775  9.771  30.873 1.00 36.05 ? 13  ASN A C   1 
ATOM   100  O  O   . ASN A 1 14  ? 9.570   10.038 30.841 1.00 33.58 ? 13  ASN A O   1 
ATOM   101  C  CB  . ASN A 1 14  ? 10.532  8.126  29.033 1.00 39.66 ? 13  ASN A CB  1 
ATOM   102  C  CG  . ASN A 1 14  ? 11.095  7.526  27.771 1.00 56.68 ? 13  ASN A CG  1 
ATOM   103  O  OD1 . ASN A 1 14  ? 11.177  6.307  27.631 1.00 66.66 ? 13  ASN A OD1 1 
ATOM   104  N  ND2 . ASN A 1 14  ? 11.496  8.382  26.840 1.00 48.49 ? 13  ASN A ND2 1 
ATOM   105  N  N   . VAL A 1 15  ? 11.516  9.972  31.964 1.00 28.63 ? 14  VAL A N   1 
ATOM   106  C  CA  . VAL A 1 15  ? 10.862  10.409 33.193 1.00 29.00 ? 14  VAL A CA  1 
ATOM   107  C  C   . VAL A 1 15  ? 10.116  11.721 32.964 1.00 30.33 ? 14  VAL A C   1 
ATOM   108  O  O   . VAL A 1 15  ? 8.976   11.888 33.414 1.00 25.23 ? 14  VAL A O   1 
ATOM   109  C  CB  . VAL A 1 15  ? 11.885  10.524 34.338 1.00 27.73 ? 14  VAL A CB  1 
ATOM   110  C  CG1 . VAL A 1 15  ? 12.985  11.502 33.985 1.00 30.76 ? 14  VAL A CG1 1 
ATOM   111  C  CG2 . VAL A 1 15  ? 11.179  10.942 35.628 1.00 28.83 ? 14  VAL A CG2 1 
ATOM   112  N  N   . SER A 1 16  ? 10.732  12.665 32.245 1.00 30.83 ? 15  SER A N   1 
ATOM   113  C  CA  . SER A 1 16  ? 10.102  13.972 32.077 1.00 30.05 ? 15  SER A CA  1 
ATOM   114  C  C   . SER A 1 16  ? 8.794   13.875 31.307 1.00 30.90 ? 15  SER A C   1 
ATOM   115  O  O   . SER A 1 16  ? 7.871   14.658 31.550 1.00 27.59 ? 15  SER A O   1 
ATOM   116  C  CB  . SER A 1 16  ? 11.051  14.935 31.367 1.00 36.60 ? 15  SER A CB  1 
ATOM   117  O  OG  . SER A 1 16  ? 12.105  15.331 32.222 1.00 50.74 ? 15  SER A OG  1 
ATOM   118  N  N   . ASN A 1 17  ? 8.701   12.934 30.368 1.00 30.90 ? 16  ASN A N   1 
ATOM   119  C  CA  . ASN A 1 17  ? 7.477   12.776 29.586 1.00 27.99 ? 16  ASN A CA  1 
ATOM   120  C  C   . ASN A 1 17  ? 6.367   12.152 30.415 1.00 24.95 ? 16  ASN A C   1 
ATOM   121  O  O   . ASN A 1 17  ? 5.192   12.499 30.258 1.00 29.68 ? 16  ASN A O   1 
ATOM   122  C  CB  . ASN A 1 17  ? 7.772   11.925 28.351 1.00 29.65 ? 16  ASN A CB  1 
ATOM   123  C  CG  . ASN A 1 17  ? 8.806   12.557 27.449 1.00 39.94 ? 16  ASN A CG  1 
ATOM   124  O  OD1 . ASN A 1 17  ? 9.873   11.991 27.209 1.00 54.42 ? 16  ASN A OD1 1 
ATOM   125  N  ND2 . ASN A 1 17  ? 8.504   13.747 26.954 1.00 43.64 ? 16  ASN A ND2 1 
ATOM   126  N  N   . ILE A 1 18  ? 6.721   11.209 31.288 1.00 27.11 ? 17  ILE A N   1 
ATOM   127  C  CA  . ILE A 1 18  ? 5.737   10.616 32.182 1.00 25.84 ? 17  ILE A CA  1 
ATOM   128  C  C   . ILE A 1 18  ? 5.169   11.684 33.106 1.00 24.16 ? 17  ILE A C   1 
ATOM   129  O  O   . ILE A 1 18  ? 3.955   11.760 33.328 1.00 28.10 ? 17  ILE A O   1 
ATOM   130  C  CB  . ILE A 1 18  ? 6.370   9.460  32.980 1.00 27.19 ? 17  ILE A CB  1 
ATOM   131  C  CG1 . ILE A 1 18  ? 6.888   8.373  32.034 1.00 30.79 ? 17  ILE A CG1 1 
ATOM   132  C  CG2 . ILE A 1 18  ? 5.369   8.906  33.981 1.00 28.87 ? 17  ILE A CG2 1 
ATOM   133  C  CD1 . ILE A 1 18  ? 7.792   7.365  32.710 1.00 34.09 ? 17  ILE A CD1 1 
ATOM   134  N  N   . VAL A 1 19  ? 6.045   12.522 33.661 1.00 23.41 ? 18  VAL A N   1 
ATOM   135  C  CA  . VAL A 1 19  ? 5.606   13.609 34.528 1.00 23.33 ? 18  VAL A CA  1 
ATOM   136  C  C   . VAL A 1 19  ? 4.689   14.552 33.770 1.00 25.92 ? 18  VAL A C   1 
ATOM   137  O  O   . VAL A 1 19  ? 3.605   14.912 34.243 1.00 25.89 ? 18  VAL A O   1 
ATOM   138  C  CB  . VAL A 1 19  ? 6.827   14.354 35.098 1.00 21.59 ? 18  VAL A CB  1 
ATOM   139  C  CG1 . VAL A 1 19  ? 6.398   15.615 35.828 1.00 24.29 ? 18  VAL A CG1 1 
ATOM   140  C  CG2 . VAL A 1 19  ? 7.616   13.436 36.008 1.00 22.19 ? 18  VAL A CG2 1 
ATOM   141  N  N   . ARG A 1 20  ? 5.123   14.984 32.590 1.00 23.53 ? 19  ARG A N   1 
ATOM   142  C  CA  . ARG A 1 20  ? 4.315   15.910 31.808 1.00 27.75 ? 19  ARG A CA  1 
ATOM   143  C  C   . ARG A 1 20  ? 2.946   15.312 31.501 1.00 26.13 ? 19  ARG A C   1 
ATOM   144  O  O   . ARG A 1 20  ? 1.922   15.987 31.640 1.00 26.52 ? 19  ARG A O   1 
ATOM   145  C  CB  . ARG A 1 20  ? 5.053   16.278 30.523 1.00 26.85 ? 19  ARG A CB  1 
ATOM   146  C  CG  . ARG A 1 20  ? 4.303   17.274 29.677 1.00 32.50 ? 19  ARG A CG  1 
ATOM   147  C  CD  . ARG A 1 20  ? 5.023   17.595 28.383 1.00 30.65 ? 19  ARG A CD  1 
ATOM   148  N  NE  . ARG A 1 20  ? 4.182   18.420 27.525 1.00 37.82 ? 19  ARG A NE  1 
ATOM   149  C  CZ  . ARG A 1 20  ? 3.147   17.961 26.835 1.00 40.70 ? 19  ARG A CZ  1 
ATOM   150  N  NH1 . ARG A 1 20  ? 2.809   16.681 26.862 1.00 42.09 ? 19  ARG A NH1 1 
ATOM   151  N  NH2 . ARG A 1 20  ? 2.430   18.807 26.101 1.00 41.79 ? 19  ARG A NH2 1 
ATOM   152  N  N   . ASP A 1 21  ? 2.909   14.041 31.095 1.00 27.64 ? 20  ASP A N   1 
ATOM   153  C  CA  . ASP A 1 21  ? 1.635   13.414 30.766 1.00 27.93 ? 20  ASP A CA  1 
ATOM   154  C  C   . ASP A 1 21  ? 0.721   13.352 31.983 1.00 30.68 ? 20  ASP A C   1 
ATOM   155  O  O   . ASP A 1 21  ? -0.505  13.481 31.856 1.00 28.08 ? 20  ASP A O   1 
ATOM   156  C  CB  . ASP A 1 21  ? 1.864   12.011 30.202 1.00 31.60 ? 20  ASP A CB  1 
ATOM   157  C  CG  . ASP A 1 21  ? 2.277   12.027 28.741 1.00 41.61 ? 20  ASP A CG  1 
ATOM   158  O  OD1 . ASP A 1 21  ? 2.390   13.126 28.159 1.00 38.52 ? 20  ASP A OD1 1 
ATOM   159  O  OD2 . ASP A 1 21  ? 2.483   10.933 28.176 1.00 44.87 ? 20  ASP A OD2 1 
ATOM   160  N  N   . THR A 1 22  ? 1.291   13.147 33.171 1.00 27.55 ? 21  THR A N   1 
ATOM   161  C  CA  . THR A 1 22  ? 0.474   13.112 34.379 1.00 26.08 ? 21  THR A CA  1 
ATOM   162  C  C   . THR A 1 22  ? -0.149  14.474 34.650 1.00 26.96 ? 21  THR A C   1 
ATOM   163  O  O   . THR A 1 22  ? -1.342  14.577 34.964 1.00 30.52 ? 21  THR A O   1 
ATOM   164  C  CB  . THR A 1 22  ? 1.311   12.657 35.574 1.00 26.23 ? 21  THR A CB  1 
ATOM   165  O  OG1 . THR A 1 22  ? 1.874   11.364 35.308 1.00 29.90 ? 21  THR A OG1 1 
ATOM   166  C  CG2 . THR A 1 22  ? 0.456   12.582 36.837 1.00 30.17 ? 21  THR A CG2 1 
ATOM   167  N  N   . ILE A 1 23  ? 0.644   15.538 34.534 1.00 22.82 ? 22  ILE A N   1 
ATOM   168  C  CA  . ILE A 1 23  ? 0.118   16.871 34.799 1.00 23.68 ? 22  ILE A CA  1 
ATOM   169  C  C   . ILE A 1 23  ? -0.955  17.235 33.775 1.00 24.36 ? 22  ILE A C   1 
ATOM   170  O  O   . ILE A 1 23  ? -2.007  17.781 34.129 1.00 28.35 ? 22  ILE A O   1 
ATOM   171  C  CB  . ILE A 1 23  ? 1.257   17.904 34.821 1.00 24.86 ? 22  ILE A CB  1 
ATOM   172  C  CG1 . ILE A 1 23  ? 2.238   17.602 35.960 1.00 26.78 ? 22  ILE A CG1 1 
ATOM   173  C  CG2 . ILE A 1 23  ? 0.694   19.304 34.990 1.00 24.63 ? 22  ILE A CG2 1 
ATOM   174  C  CD1 . ILE A 1 23  ? 3.525   18.417 35.913 1.00 27.28 ? 22  ILE A CD1 1 
ATOM   175  N  N   . VAL A 1 24  ? -0.712  16.947 32.494 1.00 26.34 ? 23  VAL A N   1 
ATOM   176  C  CA  . VAL A 1 24  ? -1.683  17.285 31.453 1.00 27.17 ? 23  VAL A CA  1 
ATOM   177  C  C   . VAL A 1 24  ? -3.002  16.578 31.715 1.00 30.59 ? 23  VAL A C   1 
ATOM   178  O  O   . VAL A 1 24  ? -4.081  17.177 31.622 1.00 28.64 ? 23  VAL A O   1 
ATOM   179  C  CB  . VAL A 1 24  ? -1.133  16.933 30.060 1.00 25.79 ? 23  VAL A CB  1 
ATOM   180  C  CG1 . VAL A 1 24  ? -2.235  17.054 29.000 1.00 29.76 ? 23  VAL A CG1 1 
ATOM   181  C  CG2 . VAL A 1 24  ? 0.048   17.817 29.719 1.00 32.47 ? 23  VAL A CG2 1 
ATOM   182  N  N   . ASN A 1 25  ? -2.938  15.283 32.019 1.00 30.66 ? 24  ASN A N   1 
ATOM   183  C  CA  . ASN A 1 25  ? -4.162  14.560 32.337 1.00 34.16 ? 24  ASN A CA  1 
ATOM   184  C  C   . ASN A 1 25  ? -4.859  15.181 33.538 1.00 35.13 ? 24  ASN A C   1 
ATOM   185  O  O   . ASN A 1 25  ? -6.089  15.308 33.560 1.00 35.71 ? 24  ASN A O   1 
ATOM   186  C  CB  . ASN A 1 25  ? -3.856  13.096 32.616 1.00 36.43 ? 24  ASN A CB  1 
ATOM   187  C  CG  . ASN A 1 25  ? -5.110  12.277 32.774 1.00 45.54 ? 24  ASN A CG  1 
ATOM   188  O  OD1 . ASN A 1 25  ? -6.004  12.331 31.930 1.00 44.97 ? 24  ASN A OD1 1 
ATOM   189  N  ND2 . ASN A 1 25  ? -5.202  11.539 33.872 1.00 48.67 ? 24  ASN A ND2 1 
ATOM   190  N  N   . GLU A 1 26  ? -4.086  15.576 34.550 1.00 32.96 ? 25  GLU A N   1 
ATOM   191  C  CA  . GLU A 1 26  ? -4.686  16.170 35.736 1.00 31.18 ? 25  GLU A CA  1 
ATOM   192  C  C   . GLU A 1 26  ? -5.250  17.553 35.446 1.00 30.67 ? 25  GLU A C   1 
ATOM   193  O  O   . GLU A 1 26  ? -6.261  17.947 36.037 1.00 33.43 ? 25  GLU A O   1 
ATOM   194  C  CB  . GLU A 1 26  ? -3.651  16.242 36.858 1.00 30.59 ? 25  GLU A CB  1 
ATOM   195  C  CG  . GLU A 1 26  ? -4.228  16.650 38.193 1.00 38.26 ? 25  GLU A CG  1 
ATOM   196  C  CD  . GLU A 1 26  ? -5.221  15.639 38.724 1.00 48.52 ? 25  GLU A CD  1 
ATOM   197  O  OE1 . GLU A 1 26  ? -5.047  14.431 38.453 1.00 47.87 ? 25  GLU A OE1 1 
ATOM   198  O  OE2 . GLU A 1 26  ? -6.178  16.057 39.407 1.00 45.99 ? 25  GLU A OE2 1 
ATOM   199  N  N   . LEU A 1 27  ? -4.621  18.305 34.544 1.00 27.39 ? 26  LEU A N   1 
ATOM   200  C  CA  . LEU A 1 27  ? -5.144  19.620 34.217 1.00 25.92 ? 26  LEU A CA  1 
ATOM   201  C  C   . LEU A 1 27  ? -6.529  19.548 33.589 1.00 33.05 ? 26  LEU A C   1 
ATOM   202  O  O   . LEU A 1 27  ? -7.287  20.516 33.693 1.00 36.11 ? 26  LEU A O   1 
ATOM   203  C  CB  . LEU A 1 27  ? -4.191  20.343 33.275 1.00 29.02 ? 26  LEU A CB  1 
ATOM   204  C  CG  . LEU A 1 27  ? -2.980  20.987 33.942 1.00 28.47 ? 26  LEU A CG  1 
ATOM   205  C  CD1 . LEU A 1 27  ? -1.949  21.294 32.883 1.00 27.77 ? 26  LEU A CD1 1 
ATOM   206  C  CD2 . LEU A 1 27  ? -3.423  22.231 34.685 1.00 29.53 ? 26  LEU A CD2 1 
ATOM   207  N  N   . ARG A 1 28  ? -6.871  18.424 32.947 1.00 36.98 ? 27  ARG A N   1 
ATOM   208  C  CA  . ARG A 1 28  ? -8.200  18.284 32.360 1.00 38.10 ? 27  ARG A CA  1 
ATOM   209  C  C   . ARG A 1 28  ? -9.290  18.487 33.403 1.00 41.02 ? 27  ARG A C   1 
ATOM   210  O  O   . ARG A 1 28  ? -10.356 19.020 33.084 1.00 46.97 ? 27  ARG A O   1 
ATOM   211  C  CB  . ARG A 1 28  ? -8.328  16.911 31.699 1.00 34.77 ? 27  ARG A CB  1 
ATOM   212  C  CG  . ARG A 1 28  ? -7.572  16.789 30.377 1.00 46.16 ? 27  ARG A CG  1 
ATOM   213  C  CD  . ARG A 1 28  ? -7.275  15.340 29.977 1.00 42.61 ? 27  ARG A CD  1 
ATOM   214  N  NE  . ARG A 1 28  ? -6.681  15.285 28.645 1.00 52.57 ? 27  ARG A NE  1 
ATOM   215  C  CZ  . ARG A 1 28  ? -5.786  14.388 28.251 1.00 57.46 ? 27  ARG A CZ  1 
ATOM   216  N  NH1 . ARG A 1 28  ? -5.325  13.461 29.074 1.00 61.36 ? 27  ARG A NH1 1 
ATOM   217  N  NH2 . ARG A 1 28  ? -5.336  14.427 26.998 1.00 49.29 ? 27  ARG A NH2 1 
ATOM   218  N  N   . SER A 1 29  ? -9.039  18.091 34.653 1.00 36.82 ? 28  SER A N   1 
ATOM   219  C  CA  . SER A 1 29  ? -10.036 18.203 35.708 1.00 38.41 ? 28  SER A CA  1 
ATOM   220  C  C   . SER A 1 29  ? -9.722  19.263 36.751 1.00 39.62 ? 28  SER A C   1 
ATOM   221  O  O   . SER A 1 29  ? -10.647 19.737 37.416 1.00 39.55 ? 28  SER A O   1 
ATOM   222  C  CB  . SER A 1 29  ? -10.208 16.852 36.420 1.00 43.91 ? 28  SER A CB  1 
ATOM   223  O  OG  . SER A 1 29  ? -8.954  16.290 36.759 1.00 51.27 ? 28  SER A OG  1 
ATOM   224  N  N   . ASP A 1 30  ? -8.455  19.646 36.916 1.00 36.95 ? 29  ASP A N   1 
ATOM   225  C  CA  . ASP A 1 30  ? -8.047  20.622 37.928 1.00 33.29 ? 29  ASP A CA  1 
ATOM   226  C  C   . ASP A 1 30  ? -7.086  21.612 37.283 1.00 33.64 ? 29  ASP A C   1 
ATOM   227  O  O   . ASP A 1 30  ? -5.867  21.399 37.290 1.00 36.37 ? 29  ASP A O   1 
ATOM   228  C  CB  . ASP A 1 30  ? -7.402  19.929 39.128 1.00 35.62 ? 29  ASP A CB  1 
ATOM   229  C  CG  . ASP A 1 30  ? -6.787  20.909 40.113 1.00 37.62 ? 29  ASP A CG  1 
ATOM   230  O  OD1 . ASP A 1 30  ? -7.055  22.124 39.998 1.00 37.33 ? 29  ASP A OD1 1 
ATOM   231  O  OD2 . ASP A 1 30  ? -6.032  20.459 41.004 1.00 36.58 ? 29  ASP A OD2 1 
ATOM   232  N  N   . PRO A 1 31  ? -7.596  22.714 36.720 1.00 32.63 ? 30  PRO A N   1 
ATOM   233  C  CA  . PRO A 1 31  ? -6.701  23.664 36.032 1.00 28.64 ? 30  PRO A CA  1 
ATOM   234  C  C   . PRO A 1 31  ? -5.685  24.339 36.948 1.00 28.34 ? 30  PRO A C   1 
ATOM   235  O  O   . PRO A 1 31  ? -4.764  24.993 36.443 1.00 33.34 ? 30  PRO A O   1 
ATOM   236  C  CB  . PRO A 1 31  ? -7.670  24.693 35.429 1.00 36.84 ? 30  PRO A CB  1 
ATOM   237  C  CG  . PRO A 1 31  ? -8.936  24.561 36.228 1.00 39.95 ? 30  PRO A CG  1 
ATOM   238  C  CD  . PRO A 1 31  ? -9.015  23.115 36.631 1.00 38.16 ? 30  PRO A CD  1 
ATOM   239  N  N   . ARG A 1 32  ? -5.825  24.195 38.257 1.00 27.08 ? 31  ARG A N   1 
ATOM   240  C  CA  . ARG A 1 32  ? -4.942  24.821 39.236 1.00 29.96 ? 31  ARG A CA  1 
ATOM   241  C  C   . ARG A 1 32  ? -3.713  23.981 39.555 1.00 28.44 ? 31  ARG A C   1 
ATOM   242  O  O   . ARG A 1 32  ? -2.793  24.479 40.212 1.00 25.28 ? 31  ARG A O   1 
ATOM   243  C  CB  . ARG A 1 32  ? -5.748  25.075 40.511 1.00 25.83 ? 31  ARG A CB  1 
ATOM   244  C  CG  . ARG A 1 32  ? -5.161  26.025 41.526 1.00 30.88 ? 31  ARG A CG  1 
ATOM   245  C  CD  . ARG A 1 32  ? -6.101  26.092 42.730 1.00 33.74 ? 31  ARG A CD  1 
ATOM   246  N  NE  . ARG A 1 32  ? -5.426  26.578 43.923 1.00 29.93 ? 31  ARG A NE  1 
ATOM   247  C  CZ  . ARG A 1 32  ? -5.876  26.432 45.162 1.00 33.93 ? 31  ARG A CZ  1 
ATOM   248  N  NH1 . ARG A 1 32  ? -7.008  25.796 45.421 1.00 31.52 ? 31  ARG A NH1 1 
ATOM   249  N  NH2 . ARG A 1 32  ? -5.170  26.936 46.169 1.00 35.33 ? 31  ARG A NH2 1 
ATOM   250  N  N   . ILE A 1 33  ? -3.650  22.737 39.085 1.00 25.93 ? 32  ILE A N   1 
ATOM   251  C  CA  . ILE A 1 33  ? -2.658  21.821 39.631 1.00 29.47 ? 32  ILE A CA  1 
ATOM   252  C  C   . ILE A 1 33  ? -1.238  22.237 39.259 1.00 25.93 ? 32  ILE A C   1 
ATOM   253  O  O   . ILE A 1 33  ? -0.304  21.999 40.032 1.00 25.63 ? 32  ILE A O   1 
ATOM   254  C  CB  . ILE A 1 33  ? -2.975  20.383 39.180 1.00 30.28 ? 32  ILE A CB  1 
ATOM   255  C  CG1 . ILE A 1 33  ? -2.049  19.386 39.887 1.00 30.25 ? 32  ILE A CG1 1 
ATOM   256  C  CG2 . ILE A 1 33  ? -2.834  20.241 37.676 1.00 29.31 ? 32  ILE A CG2 1 
ATOM   257  C  CD1 . ILE A 1 33  ? -2.244  19.332 41.386 1.00 31.36 ? 32  ILE A CD1 1 
ATOM   258  N  N   . ALA A 1 34  ? -1.034  22.868 38.102 1.00 25.52 ? 33  ALA A N   1 
ATOM   259  C  CA  . ALA A 1 34  ? 0.321   23.290 37.756 1.00 23.18 ? 33  ALA A CA  1 
ATOM   260  C  C   . ALA A 1 34  ? 0.840   24.307 38.765 1.00 22.36 ? 33  ALA A C   1 
ATOM   261  O  O   . ALA A 1 34  ? 1.985   24.207 39.234 1.00 22.39 ? 33  ALA A O   1 
ATOM   262  C  CB  . ALA A 1 34  ? 0.365   23.862 36.339 1.00 26.13 ? 33  ALA A CB  1 
ATOM   263  N  N   . ALA A 1 35  ? 0.007   25.287 39.131 1.00 22.71 ? 34  ALA A N   1 
ATOM   264  C  CA  . ALA A 1 35  ? 0.427   26.252 40.143 1.00 22.39 ? 34  ALA A CA  1 
ATOM   265  C  C   . ALA A 1 35  ? 0.696   25.566 41.471 1.00 20.23 ? 34  ALA A C   1 
ATOM   266  O  O   . ALA A 1 35  ? 1.679   25.875 42.152 1.00 20.87 ? 34  ALA A O   1 
ATOM   267  C  CB  . ALA A 1 35  ? -0.652  27.328 40.309 1.00 24.64 ? 34  ALA A CB  1 
ATOM   268  N  N   . SER A 1 36  ? -0.174  24.627 41.856 1.00 22.66 ? 35  SER A N   1 
ATOM   269  C  CA  . SER A 1 36  ? -0.032  23.962 43.148 1.00 21.45 ? 35  SER A CA  1 
ATOM   270  C  C   . SER A 1 36  ? 1.253   23.152 43.210 1.00 19.35 ? 35  SER A C   1 
ATOM   271  O  O   . SER A 1 36  ? 1.893   23.075 44.262 1.00 21.93 ? 35  SER A O   1 
ATOM   272  C  CB  . SER A 1 36  ? -1.234  23.057 43.406 1.00 23.11 ? 35  SER A CB  1 
ATOM   273  O  OG  . SER A 1 36  ? -2.446  23.797 43.407 1.00 25.44 ? 35  SER A OG  1 
ATOM   274  N  N   . ILE A 1 37  ? 1.641   22.527 42.093 1.00 20.18 ? 36  ILE A N   1 
ATOM   275  C  CA  . ILE A 1 37  ? 2.857   21.715 42.096 1.00 20.09 ? 36  ILE A CA  1 
ATOM   276  C  C   . ILE A 1 37  ? 4.091   22.600 42.197 1.00 20.39 ? 36  ILE A C   1 
ATOM   277  O  O   . ILE A 1 37  ? 5.046   22.277 42.914 1.00 22.63 ? 36  ILE A O   1 
ATOM   278  C  CB  . ILE A 1 37  ? 2.909   20.804 40.858 1.00 24.78 ? 36  ILE A CB  1 
ATOM   279  C  CG1 . ILE A 1 37  ? 1.846   19.709 40.972 1.00 26.19 ? 36  ILE A CG1 1 
ATOM   280  C  CG2 . ILE A 1 37  ? 4.324   20.243 40.707 1.00 24.12 ? 36  ILE A CG2 1 
ATOM   281  C  CD1 . ILE A 1 37  ? 1.597   18.965 39.691 1.00 25.61 ? 36  ILE A CD1 1 
ATOM   282  N  N   . LEU A 1 38  ? 4.111   23.717 41.466 1.00 20.96 ? 37  LEU A N   1 
ATOM   283  C  CA  . LEU A 1 38  ? 5.221   24.651 41.624 1.00 19.86 ? 37  LEU A CA  1 
ATOM   284  C  C   . LEU A 1 38  ? 5.380   25.038 43.085 1.00 21.78 ? 37  LEU A C   1 
ATOM   285  O  O   . LEU A 1 38  ? 6.488   25.043 43.625 1.00 19.65 ? 37  LEU A O   1 
ATOM   286  C  CB  . LEU A 1 38  ? 5.004   25.898 40.766 1.00 19.59 ? 37  LEU A CB  1 
ATOM   287  C  CG  . LEU A 1 38  ? 6.060   27.000 40.928 1.00 17.72 ? 37  LEU A CG  1 
ATOM   288  C  CD1 . LEU A 1 38  ? 7.448   26.465 40.651 1.00 21.06 ? 37  LEU A CD1 1 
ATOM   289  C  CD2 . LEU A 1 38  ? 5.725   28.185 40.021 1.00 20.44 ? 37  LEU A CD2 1 
ATOM   290  N  N   . ARG A 1 39  ? 4.269   25.335 43.755 1.00 21.52 ? 38  ARG A N   1 
ATOM   291  C  CA  . ARG A 1 39  ? 4.363   25.749 45.147 1.00 19.56 ? 38  ARG A CA  1 
ATOM   292  C  C   . ARG A 1 39  ? 4.885   24.623 46.032 1.00 18.34 ? 38  ARG A C   1 
ATOM   293  O  O   . ARG A 1 39  ? 5.635   24.870 46.983 1.00 20.45 ? 38  ARG A O   1 
ATOM   294  C  CB  . ARG A 1 39  ? 3.013   26.235 45.638 1.00 20.50 ? 38  ARG A CB  1 
ATOM   295  C  CG  . ARG A 1 39  ? 3.106   26.928 46.960 1.00 21.25 ? 38  ARG A CG  1 
ATOM   296  C  CD  . ARG A 1 39  ? 1.777   27.478 47.346 1.00 21.39 ? 38  ARG A CD  1 
ATOM   297  N  NE  . ARG A 1 39  ? 1.840   28.140 48.639 1.00 21.97 ? 38  ARG A NE  1 
ATOM   298  C  CZ  . ARG A 1 39  ? 1.008   27.886 49.636 1.00 22.93 ? 38  ARG A CZ  1 
ATOM   299  N  NH1 . ARG A 1 39  ? 0.038   26.996 49.511 1.00 26.85 ? 38  ARG A NH1 1 
ATOM   300  N  NH2 . ARG A 1 39  ? 1.136   28.559 50.774 1.00 24.22 ? 38  ARG A NH2 1 
ATOM   301  N  N   . LEU A 1 40  ? 4.491   23.377 45.752 1.00 20.05 ? 39  LEU A N   1 
ATOM   302  C  CA  . LEU A 1 40  ? 4.977   22.261 46.564 1.00 22.02 ? 39  LEU A CA  1 
ATOM   303  C  C   . LEU A 1 40  ? 6.495   22.151 46.488 1.00 20.06 ? 39  LEU A C   1 
ATOM   304  O  O   . LEU A 1 40  ? 7.156   21.853 47.484 1.00 19.96 ? 39  LEU A O   1 
ATOM   305  C  CB  . LEU A 1 40  ? 4.354   20.941 46.108 1.00 21.40 ? 39  LEU A CB  1 
ATOM   306  C  CG  . LEU A 1 40  ? 2.890   20.610 46.374 1.00 26.06 ? 39  LEU A CG  1 
ATOM   307  C  CD1 . LEU A 1 40  ? 2.586   19.210 45.835 1.00 27.59 ? 39  LEU A CD1 1 
ATOM   308  C  CD2 . LEU A 1 40  ? 2.572   20.694 47.845 1.00 26.48 ? 39  LEU A CD2 1 
ATOM   309  N  N   . HIS A 1 41  ? 7.058   22.354 45.296 1.00 19.67 ? 40  HIS A N   1 
ATOM   310  C  CA  . HIS A 1 41  ? 8.508   22.321 45.126 1.00 21.60 ? 40  HIS A CA  1 
ATOM   311  C  C   . HIS A 1 41  ? 9.182   23.431 45.926 1.00 18.41 ? 40  HIS A C   1 
ATOM   312  O  O   . HIS A 1 41  ? 10.201  23.199 46.589 1.00 19.25 ? 40  HIS A O   1 
ATOM   313  C  CB  . HIS A 1 41  ? 8.829   22.424 43.639 1.00 20.86 ? 40  HIS A CB  1 
ATOM   314  C  CG  . HIS A 1 41  ? 10.292  22.450 43.330 1.00 18.34 ? 40  HIS A CG  1 
ATOM   315  N  ND1 . HIS A 1 41  ? 11.159  21.459 43.739 1.00 21.96 ? 40  HIS A ND1 1 
ATOM   316  C  CD2 . HIS A 1 41  ? 11.035  23.335 42.623 1.00 23.78 ? 40  HIS A CD2 1 
ATOM   317  C  CE1 . HIS A 1 41  ? 12.377  21.740 43.304 1.00 23.85 ? 40  HIS A CE1 1 
ATOM   318  N  NE2 . HIS A 1 41  ? 12.328  22.876 42.630 1.00 22.10 ? 40  HIS A NE2 1 
ATOM   319  N  N   . PHE A 1 42  ? 8.625   24.644 45.878 1.00 19.66 ? 41  PHE A N   1 
ATOM   320  C  CA  . PHE A 1 42  ? 9.116   25.756 46.699 1.00 18.59 ? 41  PHE A CA  1 
ATOM   321  C  C   . PHE A 1 42  ? 9.085   25.409 48.184 1.00 18.84 ? 41  PHE A C   1 
ATOM   322  O  O   . PHE A 1 42  ? 10.072  25.631 48.898 1.00 17.53 ? 41  PHE A O   1 
ATOM   323  C  CB  . PHE A 1 42  ? 8.280   26.997 46.335 1.00 21.45 ? 41  PHE A CB  1 
ATOM   324  C  CG  . PHE A 1 42  ? 8.188   28.057 47.393 1.00 20.74 ? 41  PHE A CG  1 
ATOM   325  C  CD1 . PHE A 1 42  ? 9.302   28.501 48.084 1.00 22.08 ? 41  PHE A CD1 1 
ATOM   326  C  CD2 . PHE A 1 42  ? 6.958   28.653 47.655 1.00 23.99 ? 41  PHE A CD2 1 
ATOM   327  C  CE1 . PHE A 1 42  ? 9.186   29.491 49.044 1.00 23.52 ? 41  PHE A CE1 1 
ATOM   328  C  CE2 . PHE A 1 42  ? 6.840   29.640 48.610 1.00 23.36 ? 41  PHE A CE2 1 
ATOM   329  C  CZ  . PHE A 1 42  ? 7.949   30.061 49.305 1.00 22.69 ? 41  PHE A CZ  1 
ATOM   330  N  N   . HIS A 1 43  ? 7.987   24.810 48.662 1.00 16.79 ? 42  HIS A N   1 
ATOM   331  C  CA  . HIS A 1 43  ? 7.909   24.461 50.075 1.00 18.95 ? 42  HIS A CA  1 
ATOM   332  C  C   . HIS A 1 43  ? 8.797   23.276 50.418 1.00 18.32 ? 42  HIS A C   1 
ATOM   333  O  O   . HIS A 1 43  ? 9.233   23.149 51.569 1.00 21.83 ? 42  HIS A O   1 
ATOM   334  C  CB  . HIS A 1 43  ? 6.476   24.148 50.478 1.00 17.90 ? 42  HIS A CB  1 
ATOM   335  C  CG  . HIS A 1 43  ? 5.629   25.363 50.677 1.00 20.81 ? 42  HIS A CG  1 
ATOM   336  N  ND1 . HIS A 1 43  ? 4.444   25.337 51.378 1.00 23.78 ? 42  HIS A ND1 1 
ATOM   337  C  CD2 . HIS A 1 43  ? 5.788   26.637 50.256 1.00 25.30 ? 42  HIS A CD2 1 
ATOM   338  C  CE1 . HIS A 1 43  ? 3.909   26.544 51.381 1.00 24.00 ? 42  HIS A CE1 1 
ATOM   339  N  NE2 . HIS A 1 43  ? 4.705   27.352 50.707 1.00 25.15 ? 42  HIS A NE2 1 
ATOM   340  N  N   . ASP A 1 44  ? 9.048   22.381 49.469 1.00 17.99 ? 43  ASP A N   1 
ATOM   341  C  CA  . ASP A 1 44  ? 10.068  21.363 49.700 1.00 17.45 ? 43  ASP A CA  1 
ATOM   342  C  C   . ASP A 1 44  ? 11.429  22.009 49.903 1.00 17.94 ? 43  ASP A C   1 
ATOM   343  O  O   . ASP A 1 44  ? 12.114  21.751 50.897 1.00 18.46 ? 43  ASP A O   1 
ATOM   344  C  CB  . ASP A 1 44  ? 10.120  20.379 48.525 1.00 19.58 ? 43  ASP A CB  1 
ATOM   345  C  CG  . ASP A 1 44  ? 10.992  19.180 48.823 1.00 22.84 ? 43  ASP A CG  1 
ATOM   346  O  OD1 . ASP A 1 44  ? 11.340  19.000 50.007 1.00 22.72 ? 43  ASP A OD1 1 
ATOM   347  O  OD2 . ASP A 1 44  ? 11.332  18.420 47.893 1.00 21.62 ? 43  ASP A OD2 1 
ATOM   348  N  N   . CYS A 1 45  ? 11.825  22.882 48.974 1.00 20.48 ? 44  CYS A N   1 
ATOM   349  C  CA  . CYS A 1 45  ? 13.208  23.349 48.936 1.00 20.70 ? 44  CYS A CA  1 
ATOM   350  C  C   . CYS A 1 45  ? 13.537  24.253 50.119 1.00 18.46 ? 44  CYS A C   1 
ATOM   351  O  O   . CYS A 1 45  ? 14.670  24.249 50.609 1.00 20.41 ? 44  CYS A O   1 
ATOM   352  C  CB  . CYS A 1 45  ? 13.465  24.065 47.616 1.00 19.89 ? 44  CYS A CB  1 
ATOM   353  S  SG  . CYS A 1 45  ? 13.381  22.961 46.197 1.00 22.76 ? 44  CYS A SG  1 
ATOM   354  N  N   . PHE A 1 46  ? 12.579  25.048 50.573 1.00 17.64 ? 45  PHE A N   1 
ATOM   355  C  CA  . PHE A 1 46  ? 12.822  25.967 51.679 1.00 20.24 ? 45  PHE A CA  1 
ATOM   356  C  C   . PHE A 1 46  ? 12.937  25.261 53.022 1.00 20.51 ? 45  PHE A C   1 
ATOM   357  O  O   . PHE A 1 46  ? 13.249  25.919 54.021 1.00 20.51 ? 45  PHE A O   1 
ATOM   358  C  CB  . PHE A 1 46  ? 11.712  27.018 51.747 1.00 19.76 ? 45  PHE A CB  1 
ATOM   359  C  CG  . PHE A 1 46  ? 12.062  28.314 51.081 1.00 18.73 ? 45  PHE A CG  1 
ATOM   360  C  CD1 . PHE A 1 46  ? 12.420  28.346 49.743 1.00 22.72 ? 45  PHE A CD1 1 
ATOM   361  C  CD2 . PHE A 1 46  ? 12.031  29.509 51.789 1.00 20.53 ? 45  PHE A CD2 1 
ATOM   362  C  CE1 . PHE A 1 46  ? 12.742  29.538 49.120 1.00 20.20 ? 45  PHE A CE1 1 
ATOM   363  C  CE2 . PHE A 1 46  ? 12.354  30.706 51.168 1.00 20.04 ? 45  PHE A CE2 1 
ATOM   364  C  CZ  . PHE A 1 46  ? 12.711  30.717 49.834 1.00 22.56 ? 45  PHE A CZ  1 
ATOM   365  N  N   . VAL A 1 47  ? 12.692  23.954 53.085 1.00 18.93 ? 46  VAL A N   1 
ATOM   366  C  CA  . VAL A 1 47  ? 12.723  23.221 54.342 1.00 20.97 ? 46  VAL A CA  1 
ATOM   367  C  C   . VAL A 1 47  ? 13.696  22.059 54.189 1.00 21.66 ? 46  VAL A C   1 
ATOM   368  O  O   . VAL A 1 47  ? 13.328  20.975 53.713 1.00 20.45 ? 46  VAL A O   1 
ATOM   369  C  CB  . VAL A 1 47  ? 11.338  22.737 54.764 1.00 20.41 ? 46  VAL A CB  1 
ATOM   370  C  CG1 . VAL A 1 47  ? 11.415  22.011 56.099 1.00 22.77 ? 46  VAL A CG1 1 
ATOM   371  C  CG2 . VAL A 1 47  ? 10.375  23.924 54.840 1.00 21.33 ? 46  VAL A CG2 1 
ATOM   372  N  N   . ASN A 1 48  ? 14.930  22.277 54.631 1.00 23.58 ? 47  ASN A N   1 
ATOM   373  C  CA  . ASN A 1 48  ? 16.017  21.305 54.597 1.00 22.58 ? 47  ASN A CA  1 
ATOM   374  C  C   . ASN A 1 48  ? 16.423  20.933 53.181 1.00 22.49 ? 47  ASN A C   1 
ATOM   375  O  O   . ASN A 1 48  ? 17.053  19.891 52.969 1.00 26.85 ? 47  ASN A O   1 
ATOM   376  C  CB  . ASN A 1 48  ? 15.652  20.043 55.383 1.00 23.60 ? 47  ASN A CB  1 
ATOM   377  C  CG  . ASN A 1 48  ? 16.872  19.242 55.786 1.00 29.89 ? 47  ASN A CG  1 
ATOM   378  O  OD1 . ASN A 1 48  ? 17.766  19.758 56.456 1.00 31.79 ? 47  ASN A OD1 1 
ATOM   379  N  ND2 . ASN A 1 48  ? 16.919  17.979 55.374 1.00 31.40 ? 47  ASN A ND2 1 
ATOM   380  N  N   . GLY A 1 49  ? 16.086  21.763 52.204 1.00 21.36 ? 48  GLY A N   1 
ATOM   381  C  CA  . GLY A 1 49  ? 16.446  21.496 50.830 1.00 23.57 ? 48  GLY A CA  1 
ATOM   382  C  C   . GLY A 1 49  ? 15.409  20.655 50.125 1.00 21.59 ? 48  GLY A C   1 
ATOM   383  O  O   . GLY A 1 49  ? 14.439  20.168 50.711 1.00 20.32 ? 48  GLY A O   1 
ATOM   384  N  N   . CYS A 1 50  ? 15.632  20.482 48.822 1.00 21.73 ? 49  CYS A N   1 
ATOM   385  C  CA  . CYS A 1 50  ? 14.718  19.737 47.960 1.00 22.20 ? 49  CYS A CA  1 
ATOM   386  C  C   . CYS A 1 50  ? 15.007  18.250 48.157 1.00 24.86 ? 49  CYS A C   1 
ATOM   387  O  O   . CYS A 1 50  ? 15.803  17.633 47.440 1.00 22.09 ? 49  CYS A O   1 
ATOM   388  C  CB  . CYS A 1 50  ? 14.872  20.182 46.505 1.00 24.44 ? 49  CYS A CB  1 
ATOM   389  S  SG  . CYS A 1 50  ? 15.178  21.978 46.238 1.00 27.80 ? 49  CYS A SG  1 
ATOM   390  N  N   . ASP A 1 51  ? 14.345  17.678 49.165 1.00 18.50 ? 50  ASP A N   1 
ATOM   391  C  CA  . ASP A 1 51  ? 14.575  16.318 49.626 1.00 19.44 ? 50  ASP A CA  1 
ATOM   392  C  C   . ASP A 1 51  ? 13.268  15.548 49.773 1.00 21.52 ? 50  ASP A C   1 
ATOM   393  O  O   . ASP A 1 51  ? 13.251  14.481 50.405 1.00 21.99 ? 50  ASP A O   1 
ATOM   394  C  CB  . ASP A 1 51  ? 15.307  16.336 50.971 1.00 20.22 ? 50  ASP A CB  1 
ATOM   395  C  CG  . ASP A 1 51  ? 14.518  17.071 52.057 1.00 21.64 ? 50  ASP A CG  1 
ATOM   396  O  OD1 . ASP A 1 51  ? 13.419  17.605 51.761 1.00 19.89 ? 50  ASP A OD1 1 
ATOM   397  O  OD2 . ASP A 1 51  ? 14.997  17.101 53.206 1.00 23.79 ? 50  ASP A OD2 1 
ATOM   398  N  N   . ALA A 1 52  ? 12.171  16.079 49.243 1.00 19.69 ? 51  ALA A N   1 
ATOM   399  C  CA  . ALA A 1 52  ? 10.852  15.473 49.331 1.00 22.17 ? 51  ALA A CA  1 
ATOM   400  C  C   . ALA A 1 52  ? 10.391  15.298 50.771 1.00 20.66 ? 51  ALA A C   1 
ATOM   401  O  O   . ALA A 1 52  ? 9.529   14.460 51.049 1.00 22.39 ? 51  ALA A O   1 
ATOM   402  C  CB  . ALA A 1 52  ? 10.818  14.123 48.602 1.00 22.03 ? 51  ALA A CB  1 
ATOM   403  N  N   . SER A 1 53  ? 10.951  16.071 51.701 1.00 18.36 ? 52  SER A N   1 
ATOM   404  C  CA  . SER A 1 53  ? 10.506  15.975 53.093 1.00 18.17 ? 52  SER A CA  1 
ATOM   405  C  C   . SER A 1 53  ? 9.029   16.321 53.205 1.00 20.66 ? 52  SER A C   1 
ATOM   406  O  O   . SER A 1 53  ? 8.314   15.746 54.027 1.00 23.22 ? 52  SER A O   1 
ATOM   407  C  CB  . SER A 1 53  ? 11.342  16.889 53.988 1.00 19.97 ? 52  SER A CB  1 
ATOM   408  O  OG  . SER A 1 53  ? 11.261  18.255 53.610 1.00 21.95 ? 52  SER A OG  1 
ATOM   409  N  N   . ILE A 1 54  ? 8.556   17.232 52.353 1.00 20.69 ? 53  ILE A N   1 
ATOM   410  C  CA  . ILE A 1 54  ? 7.181   17.704 52.440 1.00 20.81 ? 53  ILE A CA  1 
ATOM   411  C  C   . ILE A 1 54  ? 6.179   16.619 52.085 1.00 22.86 ? 53  ILE A C   1 
ATOM   412  O  O   . ILE A 1 54  ? 5.004   16.721 52.455 1.00 25.90 ? 53  ILE A O   1 
ATOM   413  C  CB  . ILE A 1 54  ? 6.986   18.926 51.533 1.00 19.01 ? 53  ILE A CB  1 
ATOM   414  C  CG1 . ILE A 1 54  ? 5.594   19.518 51.756 1.00 23.56 ? 53  ILE A CG1 1 
ATOM   415  C  CG2 . ILE A 1 54  ? 7.190   18.529 50.070 1.00 22.44 ? 53  ILE A CG2 1 
ATOM   416  C  CD1 . ILE A 1 54  ? 5.454   20.929 51.268 1.00 29.29 ? 53  ILE A CD1 1 
ATOM   417  N  N   . LEU A 1 55  ? 6.602   15.577 51.370 1.00 22.73 ? 54  LEU A N   1 
ATOM   418  C  CA  . LEU A 1 55  ? 5.662   14.548 50.934 1.00 21.41 ? 54  LEU A CA  1 
ATOM   419  C  C   . LEU A 1 55  ? 5.413   13.484 51.987 1.00 24.37 ? 54  LEU A C   1 
ATOM   420  O  O   . LEU A 1 55  ? 4.461   12.706 51.845 1.00 24.43 ? 54  LEU A O   1 
ATOM   421  C  CB  . LEU A 1 55  ? 6.192   13.897 49.652 1.00 18.53 ? 54  LEU A CB  1 
ATOM   422  C  CG  . LEU A 1 55  ? 6.402   14.815 48.451 1.00 22.13 ? 54  LEU A CG  1 
ATOM   423  C  CD1 . LEU A 1 55  ? 6.965   13.995 47.307 1.00 23.31 ? 54  LEU A CD1 1 
ATOM   424  C  CD2 . LEU A 1 55  ? 5.096   15.484 48.088 1.00 23.13 ? 54  LEU A CD2 1 
ATOM   425  N  N   . LEU A 1 56  ? 6.225   13.426 53.038 1.00 21.16 ? 55  LEU A N   1 
ATOM   426  C  CA  . LEU A 1 56  ? 6.055   12.395 54.057 1.00 20.96 ? 55  LEU A CA  1 
ATOM   427  C  C   . LEU A 1 56  ? 4.812   12.646 54.892 1.00 22.05 ? 55  LEU A C   1 
ATOM   428  O  O   . LEU A 1 56  ? 4.533   13.777 55.305 1.00 24.04 ? 55  LEU A O   1 
ATOM   429  C  CB  . LEU A 1 56  ? 7.272   12.347 54.976 1.00 22.50 ? 55  LEU A CB  1 
ATOM   430  C  CG  . LEU A 1 56  ? 8.562   11.881 54.310 1.00 21.41 ? 55  LEU A CG  1 
ATOM   431  C  CD1 . LEU A 1 56  ? 9.752   12.157 55.215 1.00 25.80 ? 55  LEU A CD1 1 
ATOM   432  C  CD2 . LEU A 1 56  ? 8.494   10.405 53.956 1.00 24.76 ? 55  LEU A CD2 1 
ATOM   433  N  N   . ASP A 1 57  ? 4.083   11.571 55.166 1.00 21.59 ? 56  ASP A N   1 
ATOM   434  C  CA  . ASP A 1 57  ? 2.950   11.609 56.076 1.00 25.76 ? 56  ASP A CA  1 
ATOM   435  C  C   . ASP A 1 57  ? 3.417   11.454 57.527 1.00 25.75 ? 56  ASP A C   1 
ATOM   436  O  O   . ASP A 1 57  ? 4.558   11.076 57.814 1.00 26.18 ? 56  ASP A O   1 
ATOM   437  C  CB  . ASP A 1 57  ? 1.950   10.508 55.723 1.00 25.30 ? 56  ASP A CB  1 
ATOM   438  C  CG  . ASP A 1 57  ? 1.069   10.865 54.527 1.00 35.72 ? 56  ASP A CG  1 
ATOM   439  O  OD1 . ASP A 1 57  ? 0.905   12.066 54.226 1.00 37.86 ? 56  ASP A OD1 1 
ATOM   440  O  OD2 . ASP A 1 57  ? 0.522   9.933  53.897 1.00 39.92 ? 56  ASP A OD2 1 
ATOM   441  N  N   . ASN A 1 58  ? 2.502   11.758 58.441 1.00 24.68 ? 57  ASN A N   1 
ATOM   442  C  CA  . ASN A 1 58  ? 2.742   11.623 59.874 1.00 25.19 ? 57  ASN A CA  1 
ATOM   443  C  C   . ASN A 1 58  ? 3.252   10.235 60.237 1.00 26.82 ? 57  ASN A C   1 
ATOM   444  O  O   . ASN A 1 58  ? 2.765   9.224  59.729 1.00 26.76 ? 57  ASN A O   1 
ATOM   445  C  CB  . ASN A 1 58  ? 1.426   11.859 60.620 1.00 28.64 ? 57  ASN A CB  1 
ATOM   446  C  CG  . ASN A 1 58  ? 1.476   13.023 61.575 1.00 31.52 ? 57  ASN A CG  1 
ATOM   447  O  OD1 . ASN A 1 58  ? 2.538   13.499 61.955 1.00 34.97 ? 57  ASN A OD1 1 
ATOM   448  N  ND2 . ASN A 1 58  ? 0.299   13.486 61.986 1.00 37.33 ? 57  ASN A ND2 1 
ATOM   449  N  N   . THR A 1 59  ? 4.200   10.188 61.163 1.00 27.61 ? 58  THR A N   1 
ATOM   450  C  CA  . THR A 1 59  ? 4.574   8.952  61.838 1.00 26.71 ? 58  THR A CA  1 
ATOM   451  C  C   . THR A 1 59  ? 4.619   9.228  63.330 1.00 30.03 ? 58  THR A C   1 
ATOM   452  O  O   . THR A 1 59  ? 4.515   10.376 63.772 1.00 29.35 ? 58  THR A O   1 
ATOM   453  C  CB  . THR A 1 59  ? 5.936   8.420  61.371 1.00 31.83 ? 58  THR A CB  1 
ATOM   454  O  OG1 . THR A 1 59  ? 6.967   9.093  62.095 1.00 33.16 ? 58  THR A OG1 1 
ATOM   455  C  CG2 . THR A 1 59  ? 6.118   8.646  59.887 1.00 29.77 ? 58  THR A CG2 1 
ATOM   456  N  N   . THR A 1 60  ? 4.804   8.172  64.123 1.00 30.46 ? 59  THR A N   1 
ATOM   457  C  CA  . THR A 1 60  ? 4.900   8.373  65.564 1.00 34.36 ? 59  THR A CA  1 
ATOM   458  C  C   . THR A 1 60  ? 6.243   8.952  65.990 1.00 31.23 ? 59  THR A C   1 
ATOM   459  O  O   . THR A 1 60  ? 6.403   9.281  67.171 1.00 40.38 ? 59  THR A O   1 
ATOM   460  C  CB  . THR A 1 60  ? 4.646   7.058  66.313 1.00 35.49 ? 59  THR A CB  1 
ATOM   461  O  OG1 . THR A 1 60  ? 5.702   6.131  66.045 1.00 32.15 ? 59  THR A OG1 1 
ATOM   462  C  CG2 . THR A 1 60  ? 3.314   6.449  65.893 1.00 35.19 ? 59  THR A CG2 1 
ATOM   463  N  N   . SER A 1 61  ? 7.204   9.094  65.072 1.00 34.60 ? 60  SER A N   1 
ATOM   464  C  CA  . SER A 1 61  ? 8.490   9.696  65.403 1.00 40.86 ? 60  SER A CA  1 
ATOM   465  C  C   . SER A 1 61  ? 8.723   11.068 64.779 1.00 35.90 ? 60  SER A C   1 
ATOM   466  O  O   . SER A 1 61  ? 9.656   11.760 65.199 1.00 43.44 ? 60  SER A O   1 
ATOM   467  C  CB  . SER A 1 61  ? 9.648   8.762  65.005 1.00 43.35 ? 60  SER A CB  1 
ATOM   468  O  OG  . SER A 1 61  ? 9.598   8.388  63.640 1.00 42.68 ? 60  SER A OG  1 
ATOM   469  N  N   . PHE A 1 62  ? 7.925   11.491 63.801 1.00 29.49 ? 61  PHE A N   1 
ATOM   470  C  CA  . PHE A 1 62  ? 7.995   12.881 63.371 1.00 28.70 ? 61  PHE A CA  1 
ATOM   471  C  C   . PHE A 1 62  ? 6.641   13.317 62.829 1.00 27.33 ? 61  PHE A C   1 
ATOM   472  O  O   . PHE A 1 62  ? 5.871   12.506 62.307 1.00 27.42 ? 61  PHE A O   1 
ATOM   473  C  CB  . PHE A 1 62  ? 9.099   13.132 62.322 1.00 28.76 ? 61  PHE A CB  1 
ATOM   474  C  CG  . PHE A 1 62  ? 8.990   12.277 61.092 1.00 28.18 ? 61  PHE A CG  1 
ATOM   475  C  CD1 . PHE A 1 62  ? 8.051   12.552 60.116 1.00 25.31 ? 61  PHE A CD1 1 
ATOM   476  C  CD2 . PHE A 1 62  ? 9.840   11.198 60.915 1.00 30.25 ? 61  PHE A CD2 1 
ATOM   477  C  CE1 . PHE A 1 62  ? 7.946   11.762 58.989 1.00 28.95 ? 61  PHE A CE1 1 
ATOM   478  C  CE2 . PHE A 1 62  ? 9.745   10.408 59.791 1.00 31.73 ? 61  PHE A CE2 1 
ATOM   479  C  CZ  . PHE A 1 62  ? 8.796   10.687 58.827 1.00 26.37 ? 61  PHE A CZ  1 
ATOM   480  N  N   . ARG A 1 63  ? 6.358   14.609 62.969 1.00 23.64 ? 62  ARG A N   1 
ATOM   481  C  CA  . ARG A 1 63  ? 5.149   15.190 62.404 1.00 22.72 ? 62  ARG A CA  1 
ATOM   482  C  C   . ARG A 1 63  ? 5.389   15.572 60.948 1.00 25.26 ? 62  ARG A C   1 
ATOM   483  O  O   . ARG A 1 63  ? 6.486   15.994 60.565 1.00 25.02 ? 62  ARG A O   1 
ATOM   484  C  CB  . ARG A 1 63  ? 4.709   16.430 63.184 1.00 26.91 ? 62  ARG A CB  1 
ATOM   485  C  CG  . ARG A 1 63  ? 4.250   16.179 64.617 1.00 27.19 ? 62  ARG A CG  1 
ATOM   486  C  CD  . ARG A 1 63  ? 3.116   15.168 64.710 1.00 23.01 ? 62  ARG A CD  1 
ATOM   487  N  NE  . ARG A 1 63  ? 3.643   13.815 64.825 1.00 26.29 ? 62  ARG A NE  1 
ATOM   488  C  CZ  . ARG A 1 63  ? 4.185   13.322 65.932 1.00 31.33 ? 62  ARG A CZ  1 
ATOM   489  N  NH1 . ARG A 1 63  ? 4.219   14.023 67.057 1.00 27.77 ? 62  ARG A NH1 1 
ATOM   490  N  NH2 . ARG A 1 63  ? 4.716   12.103 65.909 1.00 31.82 ? 62  ARG A NH2 1 
ATOM   491  N  N   . THR A 1 64  ? 4.339   15.436 60.148 1.00 24.51 ? 63  THR A N   1 
ATOM   492  C  CA  . THR A 1 64  ? 4.391   15.820 58.742 1.00 22.39 ? 63  THR A CA  1 
ATOM   493  C  C   . THR A 1 64  ? 4.480   17.335 58.597 1.00 23.00 ? 63  THR A C   1 
ATOM   494  O  O   . THR A 1 64  ? 3.905   18.092 59.389 1.00 24.62 ? 63  THR A O   1 
ATOM   495  C  CB  . THR A 1 64  ? 3.154   15.278 58.011 1.00 24.44 ? 63  THR A CB  1 
ATOM   496  O  OG1 . THR A 1 64  ? 3.153   15.735 56.653 1.00 25.16 ? 63  THR A OG1 1 
ATOM   497  C  CG2 . THR A 1 64  ? 1.847   15.699 58.699 1.00 25.24 ? 63  THR A CG2 1 
ATOM   498  N  N   . GLU A 1 65  ? 5.229   17.779 57.587 1.00 20.38 ? 64  GLU A N   1 
ATOM   499  C  CA  . GLU A 1 65  ? 5.242   19.196 57.254 1.00 21.16 ? 64  GLU A CA  1 
ATOM   500  C  C   . GLU A 1 65  ? 3.888   19.669 56.751 1.00 19.68 ? 64  GLU A C   1 
ATOM   501  O  O   . GLU A 1 65  ? 3.643   20.879 56.698 1.00 22.96 ? 64  GLU A O   1 
ATOM   502  C  CB  . GLU A 1 65  ? 6.322   19.471 56.208 1.00 20.19 ? 64  GLU A CB  1 
ATOM   503  C  CG  . GLU A 1 65  ? 7.710   19.215 56.742 1.00 23.28 ? 64  GLU A CG  1 
ATOM   504  C  CD  . GLU A 1 65  ? 8.792   19.318 55.694 1.00 26.76 ? 64  GLU A CD  1 
ATOM   505  O  OE1 . GLU A 1 65  ? 8.594   20.022 54.684 1.00 24.73 ? 64  GLU A OE1 1 
ATOM   506  O  OE2 . GLU A 1 65  ? 9.853   18.692 55.891 1.00 25.67 ? 64  GLU A OE2 1 
ATOM   507  N  N   . LYS A 1 66  ? 3.002   18.744 56.392 1.00 22.20 ? 65  LYS A N   1 
ATOM   508  C  CA  . LYS A 1 66  ? 1.687   19.139 55.908 1.00 23.81 ? 65  LYS A CA  1 
ATOM   509  C  C   . LYS A 1 66  ? 0.865   19.842 56.978 1.00 27.13 ? 65  LYS A C   1 
ATOM   510  O  O   . LYS A 1 66  ? -0.141  20.474 56.647 1.00 25.93 ? 65  LYS A O   1 
ATOM   511  C  CB  . LYS A 1 66  ? 0.926   17.919 55.385 1.00 24.38 ? 65  LYS A CB  1 
ATOM   512  C  CG  . LYS A 1 66  ? 1.623   17.208 54.238 1.00 25.76 ? 65  LYS A CG  1 
ATOM   513  C  CD  . LYS A 1 66  ? 0.905   15.923 53.865 1.00 29.76 ? 65  LYS A CD  1 
ATOM   514  C  CE  . LYS A 1 66  ? 1.565   15.252 52.670 1.00 32.88 ? 65  LYS A CE  1 
ATOM   515  N  NZ  . LYS A 1 66  ? 0.826   14.038 52.227 1.00 35.79 ? 65  LYS A NZ  1 
ATOM   516  N  N   . ASP A 1 67  ? 1.263   19.751 58.249 1.00 23.66 ? 66  ASP A N   1 
ATOM   517  C  CA  . ASP A 1 67  ? 0.580   20.459 59.321 1.00 24.79 ? 66  ASP A CA  1 
ATOM   518  C  C   . ASP A 1 67  ? 1.193   21.827 59.607 1.00 22.62 ? 66  ASP A C   1 
ATOM   519  O  O   . ASP A 1 67  ? 0.750   22.508 60.537 1.00 23.23 ? 66  ASP A O   1 
ATOM   520  C  CB  . ASP A 1 67  ? 0.579   19.601 60.599 1.00 30.69 ? 66  ASP A CB  1 
ATOM   521  C  CG  . ASP A 1 67  ? -0.319  18.368 60.479 1.00 45.58 ? 66  ASP A CG  1 
ATOM   522  O  OD1 . ASP A 1 67  ? -1.397  18.465 59.851 1.00 46.10 ? 66  ASP A OD1 1 
ATOM   523  O  OD2 . ASP A 1 67  ? 0.055   17.301 61.016 1.00 56.70 ? 66  ASP A OD2 1 
ATOM   524  N  N   . ALA A 1 68  ? 2.173   22.258 58.821 1.00 22.09 ? 67  ALA A N   1 
ATOM   525  C  CA  . ALA A 1 68  ? 2.769   23.569 59.007 1.00 22.58 ? 67  ALA A CA  1 
ATOM   526  C  C   . ALA A 1 68  ? 1.786   24.670 58.638 1.00 22.64 ? 67  ALA A C   1 
ATOM   527  O  O   . ALA A 1 68  ? 0.885   24.482 57.819 1.00 25.47 ? 67  ALA A O   1 
ATOM   528  C  CB  . ALA A 1 68  ? 4.036   23.712 58.169 1.00 22.11 ? 67  ALA A CB  1 
ATOM   529  N  N   . PHE A 1 69  ? 1.978   25.846 59.250 1.00 25.55 ? 68  PHE A N   1 
ATOM   530  C  CA  . PHE A 1 69  ? 1.086   26.970 58.975 1.00 23.73 ? 68  PHE A CA  1 
ATOM   531  C  C   . PHE A 1 69  ? 1.057   27.306 57.493 1.00 24.09 ? 68  PHE A C   1 
ATOM   532  O  O   . PHE A 1 69  ? 0.003   27.666 56.966 1.00 24.80 ? 68  PHE A O   1 
ATOM   533  C  CB  . PHE A 1 69  ? 1.508   28.172 59.812 1.00 27.79 ? 68  PHE A CB  1 
ATOM   534  C  CG  . PHE A 1 69  ? 1.432   27.919 61.287 1.00 26.79 ? 68  PHE A CG  1 
ATOM   535  C  CD1 . PHE A 1 69  ? 0.208   27.727 61.896 1.00 31.02 ? 68  PHE A CD1 1 
ATOM   536  C  CD2 . PHE A 1 69  ? 2.579   27.841 62.052 1.00 31.11 ? 68  PHE A CD2 1 
ATOM   537  C  CE1 . PHE A 1 69  ? 0.125   27.472 63.249 1.00 36.51 ? 68  PHE A CE1 1 
ATOM   538  C  CE2 . PHE A 1 69  ? 2.504   27.591 63.408 1.00 30.37 ? 68  PHE A CE2 1 
ATOM   539  C  CZ  . PHE A 1 69  ? 1.277   27.404 64.005 1.00 34.84 ? 68  PHE A CZ  1 
ATOM   540  N  N   . GLY A 1 70  ? 2.183   27.160 56.798 1.00 22.93 ? 69  GLY A N   1 
ATOM   541  C  CA  . GLY A 1 70  ? 2.216   27.462 55.379 1.00 23.38 ? 69  GLY A CA  1 
ATOM   542  C  C   . GLY A 1 70  ? 1.622   26.392 54.489 1.00 24.98 ? 69  GLY A C   1 
ATOM   543  O  O   . GLY A 1 70  ? 1.309   26.672 53.332 1.00 26.50 ? 69  GLY A O   1 
ATOM   544  N  N   . ASN A 1 71  ? 1.447   25.181 55.004 1.00 22.94 ? 70  ASN A N   1 
ATOM   545  C  CA  . ASN A 1 71  ? 0.980   24.048 54.218 1.00 21.64 ? 70  ASN A CA  1 
ATOM   546  C  C   . ASN A 1 71  ? -0.447  23.647 54.544 1.00 24.42 ? 70  ASN A C   1 
ATOM   547  O  O   . ASN A 1 71  ? -1.212  23.289 53.639 1.00 24.53 ? 70  ASN A O   1 
ATOM   548  C  CB  . ASN A 1 71  ? 1.876   22.831 54.445 1.00 23.19 ? 70  ASN A CB  1 
ATOM   549  C  CG  . ASN A 1 71  ? 3.208   22.965 53.771 1.00 21.16 ? 70  ASN A CG  1 
ATOM   550  O  OD1 . ASN A 1 71  ? 3.296   23.463 52.653 1.00 23.39 ? 70  ASN A OD1 1 
ATOM   551  N  ND2 . ASN A 1 71  ? 4.258   22.521 54.450 1.00 23.37 ? 70  ASN A ND2 1 
ATOM   552  N  N   . ALA A 1 72  ? -0.804  23.682 55.823 1.00 23.45 ? 71  ALA A N   1 
ATOM   553  C  CA  . ALA A 1 72  ? -2.095  23.172 56.261 1.00 26.21 ? 71  ALA A CA  1 
ATOM   554  C  C   . ALA A 1 72  ? -3.222  23.925 55.578 1.00 25.21 ? 71  ALA A C   1 
ATOM   555  O  O   . ALA A 1 72  ? -3.257  25.160 55.576 1.00 24.97 ? 71  ALA A O   1 
ATOM   556  C  CB  . ALA A 1 72  ? -2.216  23.290 57.780 1.00 24.76 ? 71  ALA A CB  1 
ATOM   557  N  N   . ASN A 1 73  ? -4.141  23.175 54.980 1.00 29.56 ? 72  ASN A N   1 
ATOM   558  C  CA  . ASN A 1 73  ? -5.295  23.772 54.319 1.00 29.83 ? 72  ASN A CA  1 
ATOM   559  C  C   . ASN A 1 73  ? -4.867  24.778 53.254 1.00 32.16 ? 72  ASN A C   1 
ATOM   560  O  O   . ASN A 1 73  ? -5.482  25.832 53.089 1.00 32.10 ? 72  ASN A O   1 
ATOM   561  C  CB  . ASN A 1 73  ? -6.204  24.433 55.352 1.00 33.87 ? 72  ASN A CB  1 
ATOM   562  C  CG  . ASN A 1 73  ? -7.542  24.794 54.784 1.00 36.95 ? 72  ASN A CG  1 
ATOM   563  O  OD1 . ASN A 1 73  ? -8.012  24.155 53.846 1.00 37.16 ? 72  ASN A OD1 1 
ATOM   564  N  ND2 . ASN A 1 73  ? -8.166  25.829 55.335 1.00 47.16 ? 72  ASN A ND2 1 
ATOM   565  N  N   . SER A 1 74  ? -3.804  24.438 52.517 1.00 22.40 ? 73  SER A N   1 
ATOM   566  C  CA  . SER A 1 74  ? -3.165  25.374 51.604 1.00 25.78 ? 73  SER A CA  1 
ATOM   567  C  C   . SER A 1 74  ? -2.403  24.617 50.517 1.00 25.04 ? 73  SER A C   1 
ATOM   568  O  O   . SER A 1 74  ? -2.747  24.709 49.333 1.00 25.35 ? 73  SER A O   1 
ATOM   569  C  CB  . SER A 1 74  ? -2.228  26.298 52.397 1.00 28.44 ? 73  SER A CB  1 
ATOM   570  O  OG  . SER A 1 74  ? -1.693  27.331 51.593 1.00 27.63 ? 73  SER A OG  1 
ATOM   571  N  N   . ALA A 1 75  ? -1.381  23.863 50.906 1.00 24.62 ? 74  ALA A N   1 
ATOM   572  C  CA  . ALA A 1 75  ? -0.653  23.031 49.955 1.00 23.94 ? 74  ALA A CA  1 
ATOM   573  C  C   . ALA A 1 75  ? -1.566  21.935 49.416 1.00 27.79 ? 74  ALA A C   1 
ATOM   574  O  O   . ALA A 1 75  ? -2.435  21.413 50.123 1.00 25.81 ? 74  ALA A O   1 
ATOM   575  C  CB  . ALA A 1 75  ? 0.577   22.412 50.616 1.00 24.14 ? 74  ALA A CB  1 
ATOM   576  N  N   . ARG A 1 76  ? -1.373  21.585 48.152 1.00 22.70 ? 75  ARG A N   1 
ATOM   577  C  CA  . ARG A 1 76  ? -2.259  20.618 47.521 1.00 23.26 ? 75  ARG A CA  1 
ATOM   578  C  C   . ARG A 1 76  ? -1.540  19.959 46.356 1.00 26.50 ? 75  ARG A C   1 
ATOM   579  O  O   . ARG A 1 76  ? -0.471  20.396 45.918 1.00 26.45 ? 75  ARG A O   1 
ATOM   580  C  CB  . ARG A 1 76  ? -3.554  21.289 47.057 1.00 27.85 ? 75  ARG A CB  1 
ATOM   581  C  CG  . ARG A 1 76  ? -3.327  22.391 46.032 1.00 25.62 ? 75  ARG A CG  1 
ATOM   582  C  CD  . ARG A 1 76  ? -4.576  23.220 45.788 1.00 26.97 ? 75  ARG A CD  1 
ATOM   583  N  NE  . ARG A 1 76  ? -5.696  22.410 45.327 1.00 29.39 ? 75  ARG A NE  1 
ATOM   584  C  CZ  . ARG A 1 76  ? -5.856  21.998 44.076 1.00 32.59 ? 75  ARG A CZ  1 
ATOM   585  N  NH1 . ARG A 1 76  ? -4.965  22.272 43.136 1.00 30.45 ? 75  ARG A NH1 1 
ATOM   586  N  NH2 . ARG A 1 76  ? -6.932  21.282 43.762 1.00 34.36 ? 75  ARG A NH2 1 
ATOM   587  N  N   . GLY A 1 77  ? -2.142  18.879 45.872 1.00 29.91 ? 76  GLY A N   1 
ATOM   588  C  CA  . GLY A 1 77  ? -1.608  18.141 44.749 1.00 29.79 ? 76  GLY A CA  1 
ATOM   589  C  C   . GLY A 1 77  ? -0.902  16.862 45.115 1.00 28.03 ? 76  GLY A C   1 
ATOM   590  O  O   . GLY A 1 77  ? -0.410  16.170 44.219 1.00 31.73 ? 76  GLY A O   1 
ATOM   591  N  N   . PHE A 1 78  ? -0.832  16.527 46.395 1.00 27.55 ? 77  PHE A N   1 
ATOM   592  C  CA  . PHE A 1 78  ? -0.122  15.323 46.805 1.00 26.67 ? 77  PHE A CA  1 
ATOM   593  C  C   . PHE A 1 78  ? -0.596  14.075 46.074 1.00 28.51 ? 77  PHE A C   1 
ATOM   594  O  O   . PHE A 1 78  ? 0.260   13.261 45.688 1.00 29.91 ? 77  PHE A O   1 
ATOM   595  C  CB  . PHE A 1 78  ? -0.256  15.180 48.323 1.00 29.68 ? 77  PHE A CB  1 
ATOM   596  C  CG  . PHE A 1 78  ? 0.305   16.353 49.081 1.00 27.45 ? 77  PHE A CG  1 
ATOM   597  C  CD1 . PHE A 1 78  ? 1.677   16.524 49.188 1.00 25.95 ? 77  PHE A CD1 1 
ATOM   598  C  CD2 . PHE A 1 78  ? -0.530  17.290 49.668 1.00 31.46 ? 77  PHE A CD2 1 
ATOM   599  C  CE1 . PHE A 1 78  ? 2.204   17.599 49.880 1.00 25.37 ? 77  PHE A CE1 1 
ATOM   600  C  CE2 . PHE A 1 78  ? -0.007  18.370 50.358 1.00 26.01 ? 77  PHE A CE2 1 
ATOM   601  C  CZ  . PHE A 1 78  ? 1.359   18.522 50.465 1.00 26.94 ? 77  PHE A CZ  1 
ATOM   602  N  N   . PRO A 1 79  ? -1.893  13.865 45.836 1.00 30.94 ? 78  PRO A N   1 
ATOM   603  C  CA  . PRO A 1 79  ? -2.306  12.650 45.110 1.00 31.41 ? 78  PRO A CA  1 
ATOM   604  C  C   . PRO A 1 79  ? -1.792  12.602 43.685 1.00 31.36 ? 78  PRO A C   1 
ATOM   605  O  O   . PRO A 1 79  ? -1.585  11.507 43.143 1.00 32.35 ? 78  PRO A O   1 
ATOM   606  C  CB  . PRO A 1 79  ? -3.841  12.710 45.159 1.00 36.20 ? 78  PRO A CB  1 
ATOM   607  C  CG  . PRO A 1 79  ? -4.157  13.604 46.334 1.00 35.16 ? 78  PRO A CG  1 
ATOM   608  C  CD  . PRO A 1 79  ? -3.047  14.624 46.359 1.00 31.22 ? 78  PRO A CD  1 
ATOM   609  N  N   . VAL A 1 80  ? -1.588  13.760 43.056 1.00 31.33 ? 79  VAL A N   1 
ATOM   610  C  CA  . VAL A 1 80  ? -1.025  13.787 41.711 1.00 31.63 ? 79  VAL A CA  1 
ATOM   611  C  C   . VAL A 1 80  ? 0.423   13.331 41.739 1.00 29.54 ? 79  VAL A C   1 
ATOM   612  O  O   . VAL A 1 80  ? 0.883   12.614 40.842 1.00 30.60 ? 79  VAL A O   1 
ATOM   613  C  CB  . VAL A 1 80  ? -1.152  15.195 41.108 1.00 28.64 ? 79  VAL A CB  1 
ATOM   614  C  CG1 . VAL A 1 80  ? -0.556  15.222 39.712 1.00 31.56 ? 79  VAL A CG1 1 
ATOM   615  C  CG2 . VAL A 1 80  ? -2.603  15.624 41.090 1.00 33.29 ? 79  VAL A CG2 1 
ATOM   616  N  N   . ILE A 1 81  ? 1.170   13.753 42.761 1.00 29.14 ? 80  ILE A N   1 
ATOM   617  C  CA  . ILE A 1 81  ? 2.545   13.304 42.904 1.00 26.42 ? 80  ILE A CA  1 
ATOM   618  C  C   . ILE A 1 81  ? 2.586   11.791 43.081 1.00 27.74 ? 80  ILE A C   1 
ATOM   619  O  O   . ILE A 1 81  ? 3.431   11.105 42.490 1.00 28.72 ? 80  ILE A O   1 
ATOM   620  C  CB  . ILE A 1 81  ? 3.226   14.042 44.068 1.00 28.74 ? 80  ILE A CB  1 
ATOM   621  C  CG1 . ILE A 1 81  ? 3.137   15.559 43.859 1.00 28.01 ? 80  ILE A CG1 1 
ATOM   622  C  CG2 . ILE A 1 81  ? 4.662   13.595 44.206 1.00 31.06 ? 80  ILE A CG2 1 
ATOM   623  C  CD1 . ILE A 1 81  ? 3.778   16.064 42.583 1.00 31.39 ? 80  ILE A CD1 1 
ATOM   624  N  N   . ASP A 1 82  ? 1.658   11.243 43.869 1.00 27.22 ? 81  ASP A N   1 
ATOM   625  C  CA  . ASP A 1 82  ? 1.578   9.793  44.032 1.00 30.53 ? 81  ASP A CA  1 
ATOM   626  C  C   . ASP A 1 82  ? 1.328   9.099  42.700 1.00 28.79 ? 81  ASP A C   1 
ATOM   627  O  O   . ASP A 1 82  ? 1.906   8.040  42.422 1.00 29.24 ? 81  ASP A O   1 
ATOM   628  C  CB  . ASP A 1 82  ? 0.454   9.411  44.993 1.00 32.19 ? 81  ASP A CB  1 
ATOM   629  C  CG  . ASP A 1 82  ? 0.741   9.792  46.418 1.00 40.70 ? 81  ASP A CG  1 
ATOM   630  O  OD1 . ASP A 1 82  ? 1.918   9.761  46.826 1.00 39.84 ? 81  ASP A OD1 1 
ATOM   631  O  OD2 . ASP A 1 82  ? -0.229  10.111 47.139 1.00 42.38 ? 81  ASP A OD2 1 
ATOM   632  N  N   . ARG A 1 83  ? 0.414   9.646  41.895 1.00 29.48 ? 82  ARG A N   1 
ATOM   633  C  CA  . ARG A 1 83  ? 0.107   9.041  40.606 1.00 32.42 ? 82  ARG A CA  1 
ATOM   634  C  C   . ARG A 1 83  ? 1.320   9.053  39.689 1.00 27.79 ? 82  ARG A C   1 
ATOM   635  O  O   . ARG A 1 83  ? 1.602   8.059  39.009 1.00 28.72 ? 82  ARG A O   1 
ATOM   636  C  CB  . ARG A 1 83  ? -1.068  9.768  39.948 1.00 33.37 ? 82  ARG A CB  1 
ATOM   637  C  CG  . ARG A 1 83  ? -2.428  9.221  40.342 1.00 44.08 ? 82  ARG A CG  1 
ATOM   638  C  CD  . ARG A 1 83  ? -3.573  10.008 39.721 1.00 45.74 ? 82  ARG A CD  1 
ATOM   639  N  NE  . ARG A 1 83  ? -4.129  10.962 40.671 1.00 47.77 ? 82  ARG A NE  1 
ATOM   640  C  CZ  . ARG A 1 83  ? -4.760  10.620 41.788 1.00 57.72 ? 82  ARG A CZ  1 
ATOM   641  N  NH1 . ARG A 1 83  ? -4.923  9.351  42.130 1.00 68.90 ? 82  ARG A NH1 1 
ATOM   642  N  NH2 . ARG A 1 83  ? -5.227  11.573 42.589 1.00 57.53 ? 82  ARG A NH2 1 
ATOM   643  N  N   . MET A 1 84  ? 2.055   10.165 39.646 1.00 27.82 ? 83  MET A N   1 
ATOM   644  C  CA  . MET A 1 84  ? 3.208   10.184 38.757 1.00 34.35 ? 83  MET A CA  1 
ATOM   645  C  C   . MET A 1 84  ? 4.343   9.328  39.307 1.00 28.92 ? 83  MET A C   1 
ATOM   646  O  O   . MET A 1 84  ? 5.056   8.689  38.525 1.00 27.47 ? 83  MET A O   1 
ATOM   647  C  CB  . MET A 1 84  ? 3.669   11.622 38.475 1.00 37.30 ? 83  MET A CB  1 
ATOM   648  C  CG  . MET A 1 84  ? 4.159   12.450 39.641 1.00 39.24 ? 83  MET A CG  1 
ATOM   649  S  SD  . MET A 1 84  ? 4.862   14.011 39.040 1.00 33.43 ? 83  MET A SD  1 
ATOM   650  C  CE  . MET A 1 84  ? 3.426   14.850 38.370 1.00 28.81 ? 83  MET A CE  1 
ATOM   651  N  N   . LYS A 1 85  ? 4.503   9.250  40.634 1.00 28.62 ? 84  LYS A N   1 
ATOM   652  C  CA  . LYS A 1 85  ? 5.505   8.334  41.183 1.00 27.12 ? 84  LYS A CA  1 
ATOM   653  C  C   . LYS A 1 85  ? 5.171   6.885  40.833 1.00 29.11 ? 84  LYS A C   1 
ATOM   654  O  O   . LYS A 1 85  ? 6.057   6.104  40.472 1.00 27.32 ? 84  LYS A O   1 
ATOM   655  C  CB  . LYS A 1 85  ? 5.609   8.506  42.700 1.00 28.22 ? 84  LYS A CB  1 
ATOM   656  C  CG  . LYS A 1 85  ? 6.556   7.524  43.387 1.00 29.97 ? 84  LYS A CG  1 
ATOM   657  C  CD  . LYS A 1 85  ? 8.017   7.737  42.993 1.00 29.09 ? 84  LYS A CD  1 
ATOM   658  C  CE  . LYS A 1 85  ? 8.924   6.821  43.812 1.00 30.31 ? 84  LYS A CE  1 
ATOM   659  N  NZ  . LYS A 1 85  ? 10.350  6.841  43.393 1.00 33.51 ? 84  LYS A NZ  1 
ATOM   660  N  N   . ALA A 1 86  ? 3.892   6.508  40.930 1.00 25.50 ? 85  ALA A N   1 
ATOM   661  C  CA  . ALA A 1 86  ? 3.501   5.147  40.588 1.00 26.64 ? 85  ALA A CA  1 
ATOM   662  C  C   . ALA A 1 86  ? 3.794   4.848  39.122 1.00 30.19 ? 85  ALA A C   1 
ATOM   663  O  O   . ALA A 1 86  ? 4.229   3.742  38.778 1.00 31.83 ? 85  ALA A O   1 
ATOM   664  C  CB  . ALA A 1 86  ? 2.019   4.930  40.890 1.00 32.62 ? 85  ALA A CB  1 
ATOM   665  N  N   . ALA A 1 87  ? 3.568   5.829  38.245 1.00 24.79 ? 86  ALA A N   1 
ATOM   666  C  CA  . ALA A 1 87  ? 3.812   5.629  36.821 1.00 31.89 ? 86  ALA A CA  1 
ATOM   667  C  C   . ALA A 1 87  ? 5.300   5.510  36.534 1.00 30.49 ? 86  ALA A C   1 
ATOM   668  O  O   . ALA A 1 87  ? 5.725   4.653  35.749 1.00 30.56 ? 86  ALA A O   1 
ATOM   669  C  CB  . ALA A 1 87  ? 3.209   6.781  36.023 1.00 28.98 ? 86  ALA A CB  1 
ATOM   670  N  N   . VAL A 1 88  ? 6.109   6.368  37.153 1.00 28.98 ? 87  VAL A N   1 
ATOM   671  C  CA  . VAL A 1 88  ? 7.547   6.265  36.954 1.00 30.01 ? 87  VAL A CA  1 
ATOM   672  C  C   . VAL A 1 88  ? 8.071   4.968  37.552 1.00 32.38 ? 87  VAL A C   1 
ATOM   673  O  O   . VAL A 1 88  ? 8.955   4.323  36.976 1.00 30.05 ? 87  VAL A O   1 
ATOM   674  C  CB  . VAL A 1 88  ? 8.261   7.498  37.531 1.00 33.20 ? 87  VAL A CB  1 
ATOM   675  C  CG1 . VAL A 1 88  ? 9.764   7.322  37.431 1.00 31.29 ? 87  VAL A CG1 1 
ATOM   676  C  CG2 . VAL A 1 88  ? 7.812   8.742  36.776 1.00 29.25 ? 87  VAL A CG2 1 
ATOM   677  N  N   . GLU A 1 89  ? 7.528   4.549  38.699 1.00 29.99 ? 88  GLU A N   1 
ATOM   678  C  CA  . GLU A 1 89  ? 7.971   3.282  39.275 1.00 32.33 ? 88  GLU A CA  1 
ATOM   679  C  C   . GLU A 1 89  ? 7.657   2.122  38.335 1.00 35.69 ? 88  GLU A C   1 
ATOM   680  O  O   . GLU A 1 89  ? 8.451   1.183  38.208 1.00 37.12 ? 88  GLU A O   1 
ATOM   681  C  CB  . GLU A 1 89  ? 7.337   3.059  40.648 1.00 34.33 ? 88  GLU A CB  1 
ATOM   682  C  CG  . GLU A 1 89  ? 8.026   3.825  41.785 1.00 35.66 ? 88  GLU A CG  1 
ATOM   683  C  CD  . GLU A 1 89  ? 9.499   3.456  41.973 1.00 40.41 ? 88  GLU A CD  1 
ATOM   684  O  OE1 . GLU A 1 89  ? 9.827   2.252  41.982 1.00 35.77 ? 88  GLU A OE1 1 
ATOM   685  O  OE2 . GLU A 1 89  ? 10.330  4.380  42.117 1.00 37.66 ? 88  GLU A OE2 1 
ATOM   686  N  N   . SER A 1 90  ? 6.514   2.174  37.651 1.00 34.82 ? 89  SER A N   1 
ATOM   687  C  CA  . SER A 1 90  ? 6.199   1.124  36.686 1.00 39.29 ? 89  SER A CA  1 
ATOM   688  C  C   . SER A 1 90  ? 7.213   1.100  35.551 1.00 39.57 ? 89  SER A C   1 
ATOM   689  O  O   . SER A 1 90  ? 7.585   0.027  35.063 1.00 42.49 ? 89  SER A O   1 
ATOM   690  C  CB  . SER A 1 90  ? 4.789   1.318  36.137 1.00 35.13 ? 89  SER A CB  1 
ATOM   691  O  OG  . SER A 1 90  ? 3.836   1.181  37.172 1.00 49.47 ? 89  SER A OG  1 
ATOM   692  N  N   . ALA A 1 91  ? 7.679   2.275  35.124 1.00 33.66 ? 90  ALA A N   1 
ATOM   693  C  CA  . ALA A 1 91  ? 8.532   2.374  33.945 1.00 40.98 ? 90  ALA A CA  1 
ATOM   694  C  C   . ALA A 1 91  ? 10.006  2.170  34.266 1.00 37.98 ? 90  ALA A C   1 
ATOM   695  O  O   . ALA A 1 91  ? 10.738  1.593  33.456 1.00 35.66 ? 90  ALA A O   1 
ATOM   696  C  CB  . ALA A 1 91  ? 8.335   3.734  33.270 1.00 37.72 ? 90  ALA A CB  1 
ATOM   697  N  N   A CYS A 1 92  ? 10.448  2.636  35.431 0.59 32.67 ? 91  CYS A N   1 
ATOM   698  N  N   B CYS A 1 92  ? 10.470  2.641  35.421 0.41 32.70 ? 91  CYS A N   1 
ATOM   699  C  CA  A CYS A 1 92  ? 11.846  2.532  35.849 0.59 33.21 ? 91  CYS A CA  1 
ATOM   700  C  CA  B CYS A 1 92  ? 11.869  2.493  35.828 0.41 33.22 ? 91  CYS A CA  1 
ATOM   701  C  C   A CYS A 1 92  ? 11.864  2.298  37.355 0.59 32.91 ? 91  CYS A C   1 
ATOM   702  C  C   B CYS A 1 92  ? 11.901  2.289  37.338 0.41 32.93 ? 91  CYS A C   1 
ATOM   703  O  O   A CYS A 1 92  ? 12.018  3.234  38.145 0.59 32.29 ? 91  CYS A O   1 
ATOM   704  O  O   B CYS A 1 92  ? 12.106  3.229  38.110 0.41 32.32 ? 91  CYS A O   1 
ATOM   705  C  CB  A CYS A 1 92  ? 12.631  3.798  35.494 0.59 34.20 ? 91  CYS A CB  1 
ATOM   706  C  CB  B CYS A 1 92  ? 12.706  3.701  35.388 0.41 34.18 ? 91  CYS A CB  1 
ATOM   707  S  SG  A CYS A 1 92  ? 12.216  4.626  33.943 0.59 42.30 ? 91  CYS A SG  1 
ATOM   708  S  SG  B CYS A 1 92  ? 12.136  5.327  35.948 0.41 31.59 ? 91  CYS A SG  1 
ATOM   709  N  N   . PRO A 1 93  ? 11.698  1.048  37.786 1.00 33.30 ? 92  PRO A N   1 
ATOM   710  C  CA  . PRO A 1 93  ? 11.582  0.805  39.236 1.00 34.97 ? 92  PRO A CA  1 
ATOM   711  C  C   . PRO A 1 93  ? 12.835  1.206  40.002 1.00 33.51 ? 92  PRO A C   1 
ATOM   712  O  O   . PRO A 1 93  ? 13.962  1.076  39.516 1.00 32.90 ? 92  PRO A O   1 
ATOM   713  C  CB  . PRO A 1 93  ? 11.329  -0.708 39.321 1.00 39.93 ? 92  PRO A CB  1 
ATOM   714  C  CG  . PRO A 1 93  ? 10.812  -1.107 37.956 1.00 39.03 ? 92  PRO A CG  1 
ATOM   715  C  CD  . PRO A 1 93  ? 11.492  -0.172 36.986 1.00 38.36 ? 92  PRO A CD  1 
ATOM   716  N  N   . ARG A 1 94  ? 12.616  1.717  41.214 1.00 30.76 ? 93  ARG A N   1 
ATOM   717  C  CA  . ARG A 1 94  ? 13.680  1.974  42.179 1.00 30.87 ? 93  ARG A CA  1 
ATOM   718  C  C   . ARG A 1 94  ? 14.752  2.904  41.621 1.00 29.20 ? 93  ARG A C   1 
ATOM   719  O  O   . ARG A 1 94  ? 15.927  2.773  41.957 1.00 31.60 ? 93  ARG A O   1 
ATOM   720  C  CB  . ARG A 1 94  ? 14.314  0.658  42.648 1.00 33.91 ? 93  ARG A CB  1 
ATOM   721  C  CG  . ARG A 1 94  ? 13.303  -0.333 43.228 1.00 40.49 ? 93  ARG A CG  1 
ATOM   722  C  CD  . ARG A 1 94  ? 13.868  -1.750 43.359 1.00 50.75 ? 93  ARG A CD  1 
ATOM   723  N  NE  . ARG A 1 94  ? 12.926  -2.736 42.840 1.00 66.70 ? 93  ARG A NE  1 
ATOM   724  C  CZ  . ARG A 1 94  ? 13.009  -3.290 41.637 1.00 64.78 ? 93  ARG A CZ  1 
ATOM   725  N  NH1 . ARG A 1 94  ? 14.037  -3.056 40.836 1.00 65.42 ? 93  ARG A NH1 1 
ATOM   726  N  NH2 . ARG A 1 94  ? 12.034  -4.096 41.224 1.00 61.44 ? 93  ARG A NH2 1 
ATOM   727  N  N   . THR A 1 95  ? 14.351  3.870  40.799 1.00 27.63 ? 94  THR A N   1 
ATOM   728  C  CA  . THR A 1 95  ? 15.305  4.692  40.061 1.00 28.24 ? 94  THR A CA  1 
ATOM   729  C  C   . THR A 1 95  ? 15.198  6.177  40.374 1.00 25.58 ? 94  THR A C   1 
ATOM   730  O  O   . THR A 1 95  ? 16.212  6.802  40.711 1.00 25.60 ? 94  THR A O   1 
ATOM   731  C  CB  . THR A 1 95  ? 15.115  4.454  38.553 1.00 29.51 ? 94  THR A CB  1 
ATOM   732  O  OG1 . THR A 1 95  ? 15.412  3.083  38.244 1.00 32.37 ? 94  THR A OG1 1 
ATOM   733  C  CG2 . THR A 1 95  ? 16.006  5.366  37.735 1.00 30.34 ? 94  THR A CG2 1 
ATOM   734  N  N   . VAL A 1 96  ? 14.006  6.769  40.282 1.00 23.52 ? 95  VAL A N   1 
ATOM   735  C  CA  . VAL A 1 96  ? 13.849  8.218  40.346 1.00 22.68 ? 95  VAL A CA  1 
ATOM   736  C  C   . VAL A 1 96  ? 13.389  8.618  41.740 1.00 25.73 ? 95  VAL A C   1 
ATOM   737  O  O   . VAL A 1 96  ? 12.369  8.121  42.236 1.00 24.43 ? 95  VAL A O   1 
ATOM   738  C  CB  . VAL A 1 96  ? 12.855  8.721  39.291 1.00 22.16 ? 95  VAL A CB  1 
ATOM   739  C  CG1 . VAL A 1 96  ? 12.824  10.241 39.291 1.00 26.04 ? 95  VAL A CG1 1 
ATOM   740  C  CG2 . VAL A 1 96  ? 13.199  8.178  37.915 1.00 22.01 ? 95  VAL A CG2 1 
ATOM   741  N  N   . SER A 1 97  ? 14.116  9.540  42.363 1.00 21.81 ? 96  SER A N   1 
ATOM   742  C  CA  . SER A 1 97  ? 13.745  9.995  43.696 1.00 21.97 ? 96  SER A CA  1 
ATOM   743  C  C   . SER A 1 97  ? 12.496  10.864 43.638 1.00 22.42 ? 96  SER A C   1 
ATOM   744  O  O   . SER A 1 97  ? 12.216  11.530 42.637 1.00 23.28 ? 96  SER A O   1 
ATOM   745  C  CB  . SER A 1 97  ? 14.887  10.786 44.328 1.00 22.99 ? 96  SER A CB  1 
ATOM   746  O  OG  . SER A 1 97  ? 15.069  12.016 43.649 1.00 24.79 ? 96  SER A OG  1 
ATOM   747  N  N   . CYS A 1 98  ? 11.739  10.854 44.736 1.00 25.37 ? 97  CYS A N   1 
ATOM   748  C  CA  . CYS A 1 98  ? 10.601  11.760 44.852 1.00 25.35 ? 97  CYS A CA  1 
ATOM   749  C  C   . CYS A 1 98  ? 11.049  13.213 44.795 1.00 22.77 ? 97  CYS A C   1 
ATOM   750  O  O   . CYS A 1 98  ? 10.338  14.061 44.250 1.00 23.49 ? 97  CYS A O   1 
ATOM   751  C  CB  . CYS A 1 98  ? 9.851   11.483 46.160 1.00 26.61 ? 97  CYS A CB  1 
ATOM   752  S  SG  . CYS A 1 98  ? 9.150   9.815  46.251 1.00 30.79 ? 97  CYS A SG  1 
ATOM   753  N  N   . ALA A 1 99  ? 12.232  13.514 45.332 1.00 22.13 ? 98  ALA A N   1 
ATOM   754  C  CA  . ALA A 1 99  ? 12.724  14.886 45.303 1.00 24.33 ? 98  ALA A CA  1 
ATOM   755  C  C   . ALA A 1 99  ? 12.942  15.361 43.874 1.00 20.73 ? 98  ALA A C   1 
ATOM   756  O  O   . ALA A 1 99  ? 12.592  16.495 43.529 1.00 22.13 ? 98  ALA A O   1 
ATOM   757  C  CB  . ALA A 1 99  ? 14.019  14.989 46.107 1.00 22.25 ? 98  ALA A CB  1 
ATOM   758  N  N   . ASP A 1 100 ? 13.539  14.512 43.029 1.00 19.51 ? 99  ASP A N   1 
ATOM   759  C  CA  . ASP A 1 100 ? 13.725  14.870 41.626 1.00 20.70 ? 99  ASP A CA  1 
ATOM   760  C  C   . ASP A 1 100 ? 12.394  14.910 40.889 1.00 19.54 ? 99  ASP A C   1 
ATOM   761  O  O   . ASP A 1 100 ? 12.176  15.762 40.019 1.00 21.61 ? 99  ASP A O   1 
ATOM   762  C  CB  . ASP A 1 100 ? 14.655  13.874 40.945 1.00 19.82 ? 99  ASP A CB  1 
ATOM   763  C  CG  . ASP A 1 100 ? 16.113  14.167 41.181 1.00 23.07 ? 99  ASP A CG  1 
ATOM   764  O  OD1 . ASP A 1 100 ? 16.453  15.257 41.697 1.00 21.21 ? 99  ASP A OD1 1 
ATOM   765  O  OD2 . ASP A 1 100 ? 16.923  13.288 40.839 1.00 21.97 ? 99  ASP A OD2 1 
ATOM   766  N  N   . LEU A 1 101 ? 11.494  13.983 41.214 1.00 21.60 ? 100 LEU A N   1 
ATOM   767  C  CA  . LEU A 1 101 ? 10.190  13.963 40.564 1.00 21.46 ? 100 LEU A CA  1 
ATOM   768  C  C   . LEU A 1 101 ? 9.454   15.281 40.781 1.00 20.63 ? 100 LEU A C   1 
ATOM   769  O  O   . LEU A 1 101 ? 8.876   15.834 39.845 1.00 22.40 ? 100 LEU A O   1 
ATOM   770  C  CB  . LEU A 1 101 ? 9.375   12.793 41.102 1.00 23.39 ? 100 LEU A CB  1 
ATOM   771  C  CG  . LEU A 1 101 ? 8.136   12.391 40.310 1.00 31.87 ? 100 LEU A CG  1 
ATOM   772  C  CD1 . LEU A 1 101 ? 8.553   11.853 38.958 1.00 36.92 ? 100 LEU A CD1 1 
ATOM   773  C  CD2 . LEU A 1 101 ? 7.352   11.378 41.122 1.00 34.76 ? 100 LEU A CD2 1 
ATOM   774  N  N   . LEU A 1 102 ? 9.487   15.805 42.006 1.00 21.75 ? 101 LEU A N   1 
ATOM   775  C  CA  . LEU A 1 102 ? 8.833   17.074 42.292 1.00 19.79 ? 101 LEU A CA  1 
ATOM   776  C  C   . LEU A 1 102 ? 9.506   18.226 41.561 1.00 24.12 ? 101 LEU A C   1 
ATOM   777  O  O   . LEU A 1 102 ? 8.829   19.159 41.101 1.00 20.88 ? 101 LEU A O   1 
ATOM   778  C  CB  . LEU A 1 102 ? 8.835   17.330 43.793 1.00 19.02 ? 101 LEU A CB  1 
ATOM   779  C  CG  . LEU A 1 102 ? 8.068   18.529 44.332 1.00 24.36 ? 101 LEU A CG  1 
ATOM   780  C  CD1 . LEU A 1 102 ? 6.673   18.607 43.777 1.00 26.39 ? 101 LEU A CD1 1 
ATOM   781  C  CD2 . LEU A 1 102 ? 8.065   18.405 45.858 1.00 23.05 ? 101 LEU A CD2 1 
ATOM   782  N  N   . THR A 1 103 ? 10.837  18.198 41.459 1.00 21.51 ? 102 THR A N   1 
ATOM   783  C  CA  . THR A 1 103 ? 11.536  19.250 40.730 1.00 22.02 ? 102 THR A CA  1 
ATOM   784  C  C   . THR A 1 103 ? 11.131  19.240 39.262 1.00 20.86 ? 102 THR A C   1 
ATOM   785  O  O   . THR A 1 103 ? 10.817  20.284 38.679 1.00 21.89 ? 102 THR A O   1 
ATOM   786  C  CB  . THR A 1 103 ? 13.047  19.065 40.866 1.00 19.52 ? 102 THR A CB  1 
ATOM   787  O  OG1 . THR A 1 103 ? 13.402  18.962 42.248 1.00 21.91 ? 102 THR A OG1 1 
ATOM   788  C  CG2 . THR A 1 103 ? 13.787  20.235 40.238 1.00 24.47 ? 102 THR A CG2 1 
ATOM   789  N  N   . ILE A 1 104 ? 11.128  18.052 38.654 1.00 21.42 ? 103 ILE A N   1 
ATOM   790  C  CA  . ILE A 1 104 ? 10.710  17.915 37.263 1.00 18.99 ? 103 ILE A CA  1 
ATOM   791  C  C   . ILE A 1 104 ? 9.269   18.378 37.100 1.00 20.54 ? 103 ILE A C   1 
ATOM   792  O  O   . ILE A 1 104 ? 8.931   19.080 36.141 1.00 23.14 ? 103 ILE A O   1 
ATOM   793  C  CB  . ILE A 1 104 ? 10.878  16.457 36.808 1.00 22.71 ? 103 ILE A CB  1 
ATOM   794  C  CG1 . ILE A 1 104 ? 12.348  16.049 36.850 1.00 21.72 ? 103 ILE A CG1 1 
ATOM   795  C  CG2 . ILE A 1 104 ? 10.298  16.265 35.410 1.00 23.66 ? 103 ILE A CG2 1 
ATOM   796  C  CD1 . ILE A 1 104 ? 12.568  14.565 36.670 1.00 25.17 ? 103 ILE A CD1 1 
ATOM   797  N  N   . ALA A 1 105 ? 8.395   17.983 38.033 1.00 21.47 ? 104 ALA A N   1 
ATOM   798  C  CA  . ALA A 1 105 ? 6.988   18.352 37.938 1.00 21.07 ? 104 ALA A CA  1 
ATOM   799  C  C   . ALA A 1 105 ? 6.809   19.861 38.024 1.00 20.62 ? 104 ALA A C   1 
ATOM   800  O  O   . ALA A 1 105 ? 5.990   20.437 37.302 1.00 22.86 ? 104 ALA A O   1 
ATOM   801  C  CB  . ALA A 1 105 ? 6.191   17.646 39.037 1.00 21.29 ? 104 ALA A CB  1 
ATOM   802  N  N   . ALA A 1 106 ? 7.575   20.523 38.893 1.00 21.31 ? 105 ALA A N   1 
ATOM   803  C  CA  . ALA A 1 106 ? 7.511   21.980 38.953 1.00 20.06 ? 105 ALA A CA  1 
ATOM   804  C  C   . ALA A 1 106 ? 7.914   22.602 37.622 1.00 20.81 ? 105 ALA A C   1 
ATOM   805  O  O   . ALA A 1 106 ? 7.238   23.502 37.109 1.00 20.15 ? 105 ALA A O   1 
ATOM   806  C  CB  . ALA A 1 106 ? 8.399   22.503 40.077 1.00 20.98 ? 105 ALA A CB  1 
ATOM   807  N  N   . GLN A 1 107 ? 9.017   22.138 37.039 1.00 21.24 ? 106 GLN A N   1 
ATOM   808  C  CA  . GLN A 1 107 ? 9.461   22.709 35.770 1.00 20.09 ? 106 GLN A CA  1 
ATOM   809  C  C   . GLN A 1 107 ? 8.425   22.471 34.677 1.00 23.04 ? 106 GLN A C   1 
ATOM   810  O  O   . GLN A 1 107 ? 8.084   23.384 33.919 1.00 21.76 ? 106 GLN A O   1 
ATOM   811  C  CB  . GLN A 1 107 ? 10.813  22.127 35.375 1.00 22.11 ? 106 GLN A CB  1 
ATOM   812  C  CG  . GLN A 1 107 ? 11.302  22.637 34.040 1.00 23.17 ? 106 GLN A CG  1 
ATOM   813  C  CD  . GLN A 1 107 ? 10.916  21.719 32.910 1.00 23.43 ? 106 GLN A CD  1 
ATOM   814  O  OE1 . GLN A 1 107 ? 11.173  20.513 32.972 1.00 26.08 ? 106 GLN A OE1 1 
ATOM   815  N  NE2 . GLN A 1 107 ? 10.292  22.269 31.873 1.00 26.09 ? 106 GLN A NE2 1 
ATOM   816  N  N   . GLN A 1 108 ? 7.907   21.243 34.590 1.00 21.25 ? 107 GLN A N   1 
ATOM   817  C  CA  . GLN A 1 108 ? 6.900   20.929 33.584 1.00 24.52 ? 107 GLN A CA  1 
ATOM   818  C  C   . GLN A 1 108 ? 5.632   21.742 33.799 1.00 23.51 ? 107 GLN A C   1 
ATOM   819  O  O   . GLN A 1 108 ? 4.981   22.147 32.829 1.00 24.71 ? 107 GLN A O   1 
ATOM   820  C  CB  . GLN A 1 108 ? 6.592   19.430 33.609 1.00 23.84 ? 107 GLN A CB  1 
ATOM   821  C  CG  . GLN A 1 108 ? 7.735   18.560 33.120 1.00 24.61 ? 107 GLN A CG  1 
ATOM   822  C  CD  . GLN A 1 108 ? 8.054   18.807 31.658 1.00 27.98 ? 107 GLN A CD  1 
ATOM   823  O  OE1 . GLN A 1 108 ? 7.171   18.778 30.809 1.00 29.75 ? 107 GLN A OE1 1 
ATOM   824  N  NE2 . GLN A 1 108 ? 9.322   19.068 31.360 1.00 31.40 ? 107 GLN A NE2 1 
ATOM   825  N  N   . SER A 1 109 ? 5.284   22.015 35.054 1.00 22.79 ? 108 SER A N   1 
ATOM   826  C  CA  . SER A 1 109 ? 4.105   22.825 35.343 1.00 24.06 ? 108 SER A CA  1 
ATOM   827  C  C   . SER A 1 109 ? 4.260   24.247 34.815 1.00 25.56 ? 108 SER A C   1 
ATOM   828  O  O   . SER A 1 109 ? 3.317   24.813 34.249 1.00 22.60 ? 108 SER A O   1 
ATOM   829  C  CB  . SER A 1 109 ? 3.852   22.845 36.847 1.00 23.22 ? 108 SER A CB  1 
ATOM   830  O  OG  . SER A 1 109 ? 3.478   21.555 37.297 1.00 24.54 ? 108 SER A OG  1 
ATOM   831  N  N   . VAL A 1 110 ? 5.434   24.846 35.008 1.00 22.57 ? 109 VAL A N   1 
ATOM   832  C  CA  . VAL A 1 110 ? 5.675   26.193 34.503 1.00 20.30 ? 109 VAL A CA  1 
ATOM   833  C  C   . VAL A 1 110 ? 5.604   26.208 32.985 1.00 20.95 ? 109 VAL A C   1 
ATOM   834  O  O   . VAL A 1 110 ? 4.957   27.075 32.378 1.00 21.85 ? 109 VAL A O   1 
ATOM   835  C  CB  . VAL A 1 110 ? 7.030   26.711 35.015 1.00 20.32 ? 109 VAL A CB  1 
ATOM   836  C  CG1 . VAL A 1 110 ? 7.447   27.967 34.276 1.00 23.86 ? 109 VAL A CG1 1 
ATOM   837  C  CG2 . VAL A 1 110 ? 6.952   26.934 36.522 1.00 20.95 ? 109 VAL A CG2 1 
ATOM   838  N  N   . THR A 1 111 ? 6.260   25.243 32.342 1.00 22.93 ? 110 THR A N   1 
ATOM   839  C  CA  . THR A 1 111 ? 6.267   25.201 30.886 1.00 22.23 ? 110 THR A CA  1 
ATOM   840  C  C   . THR A 1 111 ? 4.869   24.962 30.332 1.00 22.30 ? 110 THR A C   1 
ATOM   841  O  O   . THR A 1 111 ? 4.473   25.577 29.334 1.00 24.49 ? 110 THR A O   1 
ATOM   842  C  CB  . THR A 1 111 ? 7.230   24.109 30.417 1.00 22.70 ? 110 THR A CB  1 
ATOM   843  O  OG1 . THR A 1 111 ? 8.527   24.346 30.977 1.00 23.00 ? 110 THR A OG1 1 
ATOM   844  C  CG2 . THR A 1 111 ? 7.340   24.093 28.904 1.00 26.40 ? 110 THR A CG2 1 
ATOM   845  N  N   . LEU A 1 112 ? 4.098   24.083 30.971 1.00 20.49 ? 111 LEU A N   1 
ATOM   846  C  CA  . LEU A 1 112 ? 2.752   23.806 30.483 1.00 23.49 ? 111 LEU A CA  1 
ATOM   847  C  C   . LEU A 1 112 ? 1.866   25.043 30.538 1.00 23.94 ? 111 LEU A C   1 
ATOM   848  O  O   . LEU A 1 112 ? 0.938   25.169 29.733 1.00 27.55 ? 111 LEU A O   1 
ATOM   849  C  CB  . LEU A 1 112 ? 2.121   22.677 31.289 1.00 22.26 ? 111 LEU A CB  1 
ATOM   850  C  CG  . LEU A 1 112 ? 2.532   21.262 30.887 1.00 26.24 ? 111 LEU A CG  1 
ATOM   851  C  CD1 . LEU A 1 112 ? 2.118   20.324 32.016 1.00 26.26 ? 111 LEU A CD1 1 
ATOM   852  C  CD2 . LEU A 1 112 ? 1.927   20.832 29.571 1.00 31.55 ? 111 LEU A CD2 1 
ATOM   853  N  N   . ALA A 1 113 ? 2.119   25.956 31.470 1.00 21.67 ? 112 ALA A N   1 
ATOM   854  C  CA  . ALA A 1 113 ? 1.314   27.163 31.599 1.00 22.02 ? 112 ALA A CA  1 
ATOM   855  C  C   . ALA A 1 113 ? 1.841   28.310 30.750 1.00 22.80 ? 112 ALA A C   1 
ATOM   856  O  O   . ALA A 1 113 ? 1.387   29.447 30.918 1.00 25.06 ? 112 ALA A O   1 
ATOM   857  C  CB  . ALA A 1 113 ? 1.225   27.596 33.063 1.00 23.62 ? 112 ALA A CB  1 
ATOM   858  N  N   . GLY A 1 114 ? 2.784   28.045 29.854 1.00 23.02 ? 113 GLY A N   1 
ATOM   859  C  CA  . GLY A 1 114 ? 3.317   29.062 28.968 1.00 21.19 ? 113 GLY A CA  1 
ATOM   860  C  C   . GLY A 1 114 ? 4.672   29.597 29.357 1.00 23.93 ? 113 GLY A C   1 
ATOM   861  O  O   . GLY A 1 114 ? 5.190   30.492 28.677 1.00 26.85 ? 113 GLY A O   1 
ATOM   862  N  N   . GLY A 1 115 ? 5.269   29.087 30.424 1.00 22.59 ? 114 GLY A N   1 
ATOM   863  C  CA  . GLY A 1 115 ? 6.520   29.608 30.891 1.00 21.61 ? 114 GLY A CA  1 
ATOM   864  C  C   . GLY A 1 115 ? 7.706   29.034 30.151 1.00 23.72 ? 114 GLY A C   1 
ATOM   865  O  O   . GLY A 1 115 ? 7.575   28.301 29.165 1.00 25.02 ? 114 GLY A O   1 
ATOM   866  N  N   . PRO A 1 116 ? 8.904   29.368 30.626 1.00 25.46 ? 115 PRO A N   1 
ATOM   867  C  CA  . PRO A 1 116 ? 10.119  28.858 29.986 1.00 25.58 ? 115 PRO A CA  1 
ATOM   868  C  C   . PRO A 1 116 ? 10.241  27.348 30.120 1.00 23.61 ? 115 PRO A C   1 
ATOM   869  O  O   . PRO A 1 116 ? 9.652   26.709 30.996 1.00 24.20 ? 115 PRO A O   1 
ATOM   870  C  CB  . PRO A 1 116 ? 11.248  29.574 30.736 1.00 25.88 ? 115 PRO A CB  1 
ATOM   871  C  CG  . PRO A 1 116 ? 10.640  29.937 32.067 1.00 25.49 ? 115 PRO A CG  1 
ATOM   872  C  CD  . PRO A 1 116 ? 9.196   30.257 31.762 1.00 24.27 ? 115 PRO A CD  1 
ATOM   873  N  N   . SER A 1 117 ? 11.044  26.786 29.229 1.00 24.24 ? 116 SER A N   1 
ATOM   874  C  CA  . SER A 1 117 ? 11.333  25.366 29.187 1.00 24.78 ? 116 SER A CA  1 
ATOM   875  C  C   . SER A 1 117 ? 12.827  25.187 29.394 1.00 24.93 ? 116 SER A C   1 
ATOM   876  O  O   . SER A 1 117 ? 13.630  25.874 28.755 1.00 26.73 ? 116 SER A O   1 
ATOM   877  C  CB  . SER A 1 117 ? 10.893  24.772 27.849 1.00 27.46 ? 116 SER A CB  1 
ATOM   878  O  OG  . SER A 1 117 ? 11.141  23.382 27.811 1.00 33.72 ? 116 SER A OG  1 
ATOM   879  N  N   . TRP A 1 118 ? 13.197  24.282 30.294 1.00 24.10 ? 117 TRP A N   1 
ATOM   880  C  CA  . TRP A 1 118 ? 14.605  24.058 30.583 1.00 24.89 ? 117 TRP A CA  1 
ATOM   881  C  C   . TRP A 1 118 ? 14.749  22.696 31.242 1.00 23.88 ? 117 TRP A C   1 
ATOM   882  O  O   . TRP A 1 118 ? 13.771  22.112 31.722 1.00 26.80 ? 117 TRP A O   1 
ATOM   883  C  CB  . TRP A 1 118 ? 15.177  25.174 31.467 1.00 27.29 ? 117 TRP A CB  1 
ATOM   884  C  CG  . TRP A 1 118 ? 14.827  25.115 32.920 1.00 25.15 ? 117 TRP A CG  1 
ATOM   885  C  CD1 . TRP A 1 118 ? 15.636  24.692 33.934 1.00 27.57 ? 117 TRP A CD1 1 
ATOM   886  C  CD2 . TRP A 1 118 ? 13.594  25.513 33.532 1.00 22.96 ? 117 TRP A CD2 1 
ATOM   887  N  NE1 . TRP A 1 118 ? 14.984  24.800 35.137 1.00 27.81 ? 117 TRP A NE1 1 
ATOM   888  C  CE2 . TRP A 1 118 ? 13.728  25.298 34.916 1.00 27.16 ? 117 TRP A CE2 1 
ATOM   889  C  CE3 . TRP A 1 118 ? 12.390  26.027 33.046 1.00 26.34 ? 117 TRP A CE3 1 
ATOM   890  C  CZ2 . TRP A 1 118 ? 12.705  25.577 35.819 1.00 26.00 ? 117 TRP A CZ2 1 
ATOM   891  C  CZ3 . TRP A 1 118 ? 11.371  26.301 33.943 1.00 24.57 ? 117 TRP A CZ3 1 
ATOM   892  C  CH2 . TRP A 1 118 ? 11.537  26.074 35.317 1.00 23.44 ? 117 TRP A CH2 1 
ATOM   893  N  N   . ARG A 1 119 ? 15.977  22.182 31.211 1.00 24.99 ? 118 ARG A N   1 
ATOM   894  C  CA  . ARG A 1 119 ? 16.314  20.896 31.807 1.00 25.75 ? 118 ARG A CA  1 
ATOM   895  C  C   . ARG A 1 119 ? 16.813  21.146 33.225 1.00 24.45 ? 118 ARG A C   1 
ATOM   896  O  O   . ARG A 1 119 ? 17.857  21.774 33.422 1.00 26.88 ? 118 ARG A O   1 
ATOM   897  C  CB  . ARG A 1 119 ? 17.376  20.168 30.984 1.00 29.91 ? 118 ARG A CB  1 
ATOM   898  C  CG  . ARG A 1 119 ? 16.946  19.710 29.603 1.00 33.41 ? 118 ARG A CG  1 
ATOM   899  C  CD  . ARG A 1 119 ? 17.864  18.584 29.116 1.00 44.38 ? 118 ARG A CD  1 
ATOM   900  N  NE  . ARG A 1 119 ? 17.513  17.302 29.718 1.00 50.16 ? 118 ARG A NE  1 
ATOM   901  C  CZ  . ARG A 1 119 ? 18.310  16.242 29.771 1.00 41.80 ? 118 ARG A CZ  1 
ATOM   902  N  NH1 . ARG A 1 119 ? 19.556  16.288 29.330 1.00 49.04 ? 118 ARG A NH1 1 
ATOM   903  N  NH2 . ARG A 1 119 ? 17.844  15.107 30.286 1.00 44.73 ? 118 ARG A NH2 1 
ATOM   904  N  N   . VAL A 1 120 ? 16.075  20.654 34.215 1.00 24.19 ? 119 VAL A N   1 
ATOM   905  C  CA  . VAL A 1 120 ? 16.451  20.866 35.609 1.00 23.47 ? 119 VAL A CA  1 
ATOM   906  C  C   . VAL A 1 120 ? 17.643  19.985 35.963 1.00 20.04 ? 119 VAL A C   1 
ATOM   907  O  O   . VAL A 1 120 ? 17.760  18.863 35.448 1.00 23.33 ? 119 VAL A O   1 
ATOM   908  C  CB  . VAL A 1 120 ? 15.273  20.579 36.556 1.00 22.70 ? 119 VAL A CB  1 
ATOM   909  C  CG1 . VAL A 1 120 ? 14.091  21.478 36.225 1.00 24.85 ? 119 VAL A CG1 1 
ATOM   910  C  CG2 . VAL A 1 120 ? 14.870  19.105 36.485 1.00 24.87 ? 119 VAL A CG2 1 
ATOM   911  N  N   . PRO A 1 121 ? 18.545  20.448 36.824 1.00 23.32 ? 120 PRO A N   1 
ATOM   912  C  CA  . PRO A 1 121 ? 19.543  19.535 37.401 1.00 20.31 ? 120 PRO A CA  1 
ATOM   913  C  C   . PRO A 1 121 ? 18.850  18.450 38.212 1.00 23.61 ? 120 PRO A C   1 
ATOM   914  O  O   . PRO A 1 121 ? 17.799  18.676 38.813 1.00 25.82 ? 120 PRO A O   1 
ATOM   915  C  CB  . PRO A 1 121 ? 20.402  20.447 38.287 1.00 26.65 ? 120 PRO A CB  1 
ATOM   916  C  CG  . PRO A 1 121 ? 20.097  21.861 37.822 1.00 29.10 ? 120 PRO A CG  1 
ATOM   917  C  CD  . PRO A 1 121 ? 18.677  21.823 37.343 1.00 29.61 ? 120 PRO A CD  1 
ATOM   918  N  N   . LEU A 1 122 ? 19.443  17.254 38.209 1.00 22.99 ? 121 LEU A N   1 
ATOM   919  C  CA  . LEU A 1 122 ? 18.841  16.081 38.834 1.00 24.66 ? 121 LEU A CA  1 
ATOM   920  C  C   . LEU A 1 122 ? 19.910  15.317 39.608 1.00 22.99 ? 121 LEU A C   1 
ATOM   921  O  O   . LEU A 1 122 ? 21.103  15.598 39.496 1.00 24.73 ? 121 LEU A O   1 
ATOM   922  C  CB  . LEU A 1 122 ? 18.176  15.177 37.786 1.00 22.19 ? 121 LEU A CB  1 
ATOM   923  C  CG  . LEU A 1 122 ? 16.980  15.802 37.061 1.00 24.30 ? 121 LEU A CG  1 
ATOM   924  C  CD1 . LEU A 1 122 ? 16.644  15.049 35.789 1.00 29.52 ? 121 LEU A CD1 1 
ATOM   925  C  CD2 . LEU A 1 122 ? 15.792  15.842 38.010 1.00 25.80 ? 121 LEU A CD2 1 
ATOM   926  N  N   . GLY A 1 123 ? 19.472  14.334 40.389 1.00 20.33 ? 122 GLY A N   1 
ATOM   927  C  CA  . GLY A 1 123 ? 20.354  13.596 41.273 1.00 22.60 ? 122 GLY A CA  1 
ATOM   928  C  C   . GLY A 1 123 ? 20.057  13.752 42.753 1.00 20.35 ? 122 GLY A C   1 
ATOM   929  O  O   . GLY A 1 123 ? 20.817  13.226 43.579 1.00 24.14 ? 122 GLY A O   1 
ATOM   930  N  N   . ARG A 1 124 ? 18.994  14.455 43.117 1.00 20.13 ? 123 ARG A N   1 
ATOM   931  C  CA  . ARG A 1 124 ? 18.596  14.584 44.506 1.00 21.76 ? 123 ARG A CA  1 
ATOM   932  C  C   . ARG A 1 124 ? 18.113  13.248 45.053 1.00 21.95 ? 123 ARG A C   1 
ATOM   933  O  O   . ARG A 1 124 ? 17.568  12.412 44.329 1.00 23.81 ? 123 ARG A O   1 
ATOM   934  C  CB  . ARG A 1 124 ? 17.468  15.603 44.653 1.00 20.84 ? 123 ARG A CB  1 
ATOM   935  C  CG  . ARG A 1 124 ? 17.792  16.982 44.151 1.00 21.57 ? 123 ARG A CG  1 
ATOM   936  C  CD  . ARG A 1 124 ? 16.536  17.827 44.081 1.00 22.50 ? 123 ARG A CD  1 
ATOM   937  N  NE  . ARG A 1 124 ? 16.806  19.042 43.323 1.00 24.17 ? 123 ARG A NE  1 
ATOM   938  C  CZ  . ARG A 1 124 ? 16.884  19.088 42.001 1.00 23.21 ? 123 ARG A CZ  1 
ATOM   939  N  NH1 . ARG A 1 124 ? 16.634  18.020 41.258 1.00 23.39 ? 123 ARG A NH1 1 
ATOM   940  N  NH2 . ARG A 1 124 ? 17.227  20.226 41.411 1.00 24.30 ? 123 ARG A NH2 1 
ATOM   941  N  N   . ARG A 1 125 ? 18.286  13.065 46.354 1.00 20.06 ? 124 ARG A N   1 
ATOM   942  C  CA  . ARG A 1 125 ? 17.771  11.891 47.032 1.00 21.05 ? 124 ARG A CA  1 
ATOM   943  C  C   . ARG A 1 125 ? 16.805  12.311 48.133 1.00 21.33 ? 124 ARG A C   1 
ATOM   944  O  O   . ARG A 1 125 ? 16.707  13.487 48.494 1.00 20.76 ? 124 ARG A O   1 
ATOM   945  C  CB  . ARG A 1 125 ? 18.914  11.031 47.559 1.00 21.54 ? 124 ARG A CB  1 
ATOM   946  C  CG  . ARG A 1 125 ? 19.637  10.396 46.388 1.00 25.65 ? 124 ARG A CG  1 
ATOM   947  C  CD  . ARG A 1 125 ? 20.896  9.698  46.785 1.00 29.36 ? 124 ARG A CD  1 
ATOM   948  N  NE  . ARG A 1 125 ? 20.646  8.507  47.583 1.00 29.41 ? 124 ARG A NE  1 
ATOM   949  C  CZ  . ARG A 1 125 ? 20.453  7.295  47.085 1.00 28.57 ? 124 ARG A CZ  1 
ATOM   950  N  NH1 . ARG A 1 125 ? 20.337  7.094  45.784 1.00 29.95 ? 124 ARG A NH1 1 
ATOM   951  N  NH2 . ARG A 1 125 ? 20.394  6.257  47.915 1.00 28.58 ? 124 ARG A NH2 1 
ATOM   952  N  N   . ASP A 1 126 ? 16.067  11.321 48.627 1.00 21.17 ? 125 ASP A N   1 
ATOM   953  C  CA  . ASP A 1 126 ? 14.918  11.554 49.485 1.00 25.18 ? 125 ASP A CA  1 
ATOM   954  C  C   . ASP A 1 126 ? 15.306  11.477 50.957 1.00 23.87 ? 125 ASP A C   1 
ATOM   955  O  O   . ASP A 1 126 ? 16.074  10.603 51.374 1.00 24.16 ? 125 ASP A O   1 
ATOM   956  C  CB  . ASP A 1 126 ? 13.814  10.545 49.169 1.00 22.70 ? 125 ASP A CB  1 
ATOM   957  C  CG  . ASP A 1 126 ? 13.281  10.698 47.751 1.00 28.83 ? 125 ASP A CG  1 
ATOM   958  O  OD1 . ASP A 1 126 ? 13.226  11.846 47.270 1.00 25.10 ? 125 ASP A OD1 1 
ATOM   959  O  OD2 . ASP A 1 126 ? 12.917  9.681  47.116 1.00 27.85 ? 125 ASP A OD2 1 
ATOM   960  N  N   . SER A 1 127 ? 14.777  12.420 51.731 1.00 23.10 ? 126 SER A N   1 
ATOM   961  C  CA  . SER A 1 127 ? 15.047  12.514 53.154 1.00 23.24 ? 126 SER A CA  1 
ATOM   962  C  C   . SER A 1 127 ? 14.477  11.313 53.890 1.00 23.85 ? 126 SER A C   1 
ATOM   963  O  O   . SER A 1 127 ? 13.548  10.643 53.423 1.00 25.76 ? 126 SER A O   1 
ATOM   964  C  CB  . SER A 1 127 ? 14.435  13.780 53.735 1.00 26.37 ? 126 SER A CB  1 
ATOM   965  O  OG  . SER A 1 127 ? 13.021  13.675 53.687 1.00 32.68 ? 126 SER A OG  1 
ATOM   966  N  N   . LEU A 1 128 ? 15.025  11.059 55.079 1.00 23.88 ? 127 LEU A N   1 
ATOM   967  C  CA  . LEU A 1 128 ? 14.552  9.998  55.954 1.00 24.43 ? 127 LEU A CA  1 
ATOM   968  C  C   . LEU A 1 128 ? 13.606  10.517 57.032 1.00 22.44 ? 127 LEU A C   1 
ATOM   969  O  O   . LEU A 1 128 ? 13.186  9.745  57.901 1.00 28.37 ? 127 LEU A O   1 
ATOM   970  C  CB  . LEU A 1 128 ? 15.749  9.287  56.589 1.00 26.33 ? 127 LEU A CB  1 
ATOM   971  C  CG  . LEU A 1 128 ? 16.779  8.748  55.596 1.00 32.65 ? 127 LEU A CG  1 
ATOM   972  C  CD1 . LEU A 1 128 ? 17.994  8.174  56.291 1.00 32.84 ? 127 LEU A CD1 1 
ATOM   973  C  CD2 . LEU A 1 128 ? 16.112  7.693  54.714 1.00 31.85 ? 127 LEU A CD2 1 
ATOM   974  N  N   . GLN A 1 129 ? 13.243  11.798 56.980 1.00 23.74 ? 128 GLN A N   1 
ATOM   975  C  CA  . GLN A 1 129 ? 12.400  12.398 58.002 1.00 25.22 ? 128 GLN A CA  1 
ATOM   976  C  C   . GLN A 1 129 ? 11.807  13.686 57.449 1.00 24.33 ? 128 GLN A C   1 
ATOM   977  O  O   . GLN A 1 129 ? 12.237  14.197 56.413 1.00 22.07 ? 128 GLN A O   1 
ATOM   978  C  CB  . GLN A 1 129 ? 13.197  12.672 59.275 1.00 31.39 ? 128 GLN A CB  1 
ATOM   979  C  CG  . GLN A 1 129 ? 14.405  13.552 59.027 1.00 35.65 ? 128 GLN A CG  1 
ATOM   980  C  CD  . GLN A 1 129 ? 15.382  13.512 60.173 1.00 36.59 ? 128 GLN A CD  1 
ATOM   981  O  OE1 . GLN A 1 129 ? 14.998  13.289 61.319 1.00 41.71 ? 128 GLN A OE1 1 
ATOM   982  N  NE2 . GLN A 1 129 ? 16.656  13.716 59.866 1.00 36.96 ? 128 GLN A NE2 1 
ATOM   983  N  N   . ALA A 1 130 ? 10.798  14.194 58.148 1.00 25.17 ? 129 ALA A N   1 
ATOM   984  C  CA  . ALA A 1 130 ? 10.140  15.452 57.824 1.00 23.90 ? 129 ALA A CA  1 
ATOM   985  C  C   . ALA A 1 130 ? 10.422  16.461 58.929 1.00 22.65 ? 129 ALA A C   1 
ATOM   986  O  O   . ALA A 1 130 ? 10.776  16.095 60.048 1.00 24.01 ? 129 ALA A O   1 
ATOM   987  C  CB  . ALA A 1 130 ? 8.633   15.264 57.656 1.00 27.82 ? 129 ALA A CB  1 
ATOM   988  N  N   . PHE A 1 131 ? 10.227  17.748 58.610 1.00 24.49 ? 130 PHE A N   1 
ATOM   989  C  CA  . PHE A 1 131 ? 10.706  18.839 59.463 1.00 23.92 ? 130 PHE A CA  1 
ATOM   990  C  C   . PHE A 1 131 ? 9.611   19.880 59.685 1.00 22.33 ? 130 PHE A C   1 
ATOM   991  O  O   . PHE A 1 131 ? 9.677   20.988 59.145 1.00 22.67 ? 130 PHE A O   1 
ATOM   992  C  CB  . PHE A 1 131 ? 11.940  19.496 58.859 1.00 26.01 ? 130 PHE A CB  1 
ATOM   993  C  CG  . PHE A 1 131 ? 13.011  18.540 58.476 1.00 24.09 ? 130 PHE A CG  1 
ATOM   994  C  CD1 . PHE A 1 131 ? 13.940  18.135 59.406 1.00 27.33 ? 130 PHE A CD1 1 
ATOM   995  C  CD2 . PHE A 1 131 ? 13.088  18.047 57.187 1.00 28.02 ? 130 PHE A CD2 1 
ATOM   996  C  CE1 . PHE A 1 131 ? 14.936  17.253 59.065 1.00 32.73 ? 130 PHE A CE1 1 
ATOM   997  C  CE2 . PHE A 1 131 ? 14.084  17.162 56.838 1.00 25.55 ? 130 PHE A CE2 1 
ATOM   998  C  CZ  . PHE A 1 131 ? 15.009  16.764 57.776 1.00 29.13 ? 130 PHE A CZ  1 
ATOM   999  N  N   . LEU A 1 132 ? 8.643   19.554 60.546 1.00 23.07 ? 131 LEU A N   1 
ATOM   1000 C  CA  . LEU A 1 132 ? 7.513   20.454 60.751 1.00 22.18 ? 131 LEU A CA  1 
ATOM   1001 C  C   . LEU A 1 132 ? 7.948   21.771 61.390 1.00 23.77 ? 131 LEU A C   1 
ATOM   1002 O  O   . LEU A 1 132 ? 7.577   22.851 60.917 1.00 22.09 ? 131 LEU A O   1 
ATOM   1003 C  CB  . LEU A 1 132 ? 6.455   19.766 61.607 1.00 22.25 ? 131 LEU A CB  1 
ATOM   1004 C  CG  . LEU A 1 132 ? 5.305   20.672 62.062 1.00 24.18 ? 131 LEU A CG  1 
ATOM   1005 C  CD1 . LEU A 1 132 ? 4.679   21.402 60.893 1.00 22.97 ? 131 LEU A CD1 1 
ATOM   1006 C  CD2 . LEU A 1 132 ? 4.245   19.863 62.800 1.00 24.29 ? 131 LEU A CD2 1 
ATOM   1007 N  N   . ASP A 1 133 ? 8.709   21.707 62.488 1.00 23.81 ? 132 ASP A N   1 
ATOM   1008 C  CA  . ASP A 1 133 ? 9.147   22.945 63.125 1.00 22.65 ? 132 ASP A CA  1 
ATOM   1009 C  C   . ASP A 1 133 ? 9.959   23.798 62.155 1.00 25.98 ? 132 ASP A C   1 
ATOM   1010 O  O   . ASP A 1 133 ? 9.796   25.023 62.102 1.00 24.30 ? 132 ASP A O   1 
ATOM   1011 C  CB  . ASP A 1 133 ? 9.967   22.655 64.375 1.00 26.99 ? 132 ASP A CB  1 
ATOM   1012 C  CG  . ASP A 1 133 ? 9.133   22.091 65.507 1.00 33.04 ? 132 ASP A CG  1 
ATOM   1013 O  OD1 . ASP A 1 133 ? 7.938   22.440 65.613 1.00 28.73 ? 132 ASP A OD1 1 
ATOM   1014 O  OD2 . ASP A 1 133 ? 9.688   21.307 66.303 1.00 40.41 ? 132 ASP A OD2 1 
ATOM   1015 N  N   . LEU A 1 134 ? 10.841  23.170 61.381 1.00 22.84 ? 133 LEU A N   1 
ATOM   1016 C  CA  . LEU A 1 134 ? 11.632  23.925 60.420 1.00 23.61 ? 133 LEU A CA  1 
ATOM   1017 C  C   . LEU A 1 134 ? 10.742  24.554 59.355 1.00 25.39 ? 133 LEU A C   1 
ATOM   1018 O  O   . LEU A 1 134 ? 10.993  25.681 58.913 1.00 25.44 ? 133 LEU A O   1 
ATOM   1019 C  CB  . LEU A 1 134 ? 12.682  23.017 59.791 1.00 23.70 ? 133 LEU A CB  1 
ATOM   1020 C  CG  . LEU A 1 134 ? 13.737  23.735 58.957 1.00 25.58 ? 133 LEU A CG  1 
ATOM   1021 C  CD1 . LEU A 1 134 ? 14.532  24.729 59.776 1.00 27.54 ? 133 LEU A CD1 1 
ATOM   1022 C  CD2 . LEU A 1 134 ? 14.656  22.697 58.326 1.00 28.13 ? 133 LEU A CD2 1 
ATOM   1023 N  N   . ALA A 1 135 ? 9.681   23.854 58.939 1.00 22.41 ? 134 ALA A N   1 
ATOM   1024 C  CA  . ALA A 1 135 ? 8.751   24.458 57.994 1.00 21.38 ? 134 ALA A CA  1 
ATOM   1025 C  C   . ALA A 1 135 ? 8.094   25.693 58.592 1.00 24.20 ? 134 ALA A C   1 
ATOM   1026 O  O   . ALA A 1 135 ? 7.954   26.722 57.924 1.00 25.78 ? 134 ALA A O   1 
ATOM   1027 C  CB  . ALA A 1 135 ? 7.692   23.444 57.559 1.00 22.65 ? 134 ALA A CB  1 
ATOM   1028 N  N   . ASN A 1 136 ? 7.704   25.620 59.862 1.00 21.73 ? 135 ASN A N   1 
ATOM   1029 C  CA  . ASN A 1 136 ? 7.063   26.774 60.485 1.00 23.84 ? 135 ASN A CA  1 
ATOM   1030 C  C   . ASN A 1 136 ? 8.033   27.940 60.633 1.00 25.17 ? 135 ASN A C   1 
ATOM   1031 O  O   . ASN A 1 136 ? 7.609   29.102 60.626 1.00 29.00 ? 135 ASN A O   1 
ATOM   1032 C  CB  . ASN A 1 136 ? 6.478   26.371 61.837 1.00 21.73 ? 135 ASN A CB  1 
ATOM   1033 C  CG  . ASN A 1 136 ? 5.154   25.658 61.691 1.00 24.38 ? 135 ASN A CG  1 
ATOM   1034 O  OD1 . ASN A 1 136 ? 4.449   25.851 60.698 1.00 27.28 ? 135 ASN A OD1 1 
ATOM   1035 N  ND2 . ASN A 1 136 ? 4.803   24.833 62.671 1.00 28.04 ? 135 ASN A ND2 1 
ATOM   1036 N  N   . ALA A 1 137 ? 9.333   27.660 60.740 1.00 24.62 ? 136 ALA A N   1 
ATOM   1037 C  CA  . ALA A 1 137 ? 10.304  28.734 60.880 1.00 24.67 ? 136 ALA A CA  1 
ATOM   1038 C  C   . ALA A 1 137 ? 10.725  29.309 59.533 1.00 26.59 ? 136 ALA A C   1 
ATOM   1039 O  O   . ALA A 1 137 ? 11.001  30.511 59.434 1.00 26.76 ? 136 ALA A O   1 
ATOM   1040 C  CB  . ALA A 1 137 ? 11.539  28.237 61.629 1.00 27.89 ? 136 ALA A CB  1 
ATOM   1041 N  N   . ASN A 1 138 ? 10.786  28.486 58.495 1.00 22.10 ? 137 ASN A N   1 
ATOM   1042 C  CA  . ASN A 1 138 ? 11.449  28.904 57.268 1.00 22.44 ? 137 ASN A CA  1 
ATOM   1043 C  C   . ASN A 1 138 ? 10.512  29.462 56.209 1.00 26.05 ? 137 ASN A C   1 
ATOM   1044 O  O   . ASN A 1 138 ? 10.946  30.273 55.380 1.00 23.74 ? 137 ASN A O   1 
ATOM   1045 C  CB  . ASN A 1 138 ? 12.207  27.731 56.650 1.00 21.28 ? 137 ASN A CB  1 
ATOM   1046 C  CG  . ASN A 1 138 ? 13.507  27.461 57.338 1.00 23.76 ? 137 ASN A CG  1 
ATOM   1047 O  OD1 . ASN A 1 138 ? 13.779  27.980 58.415 1.00 24.06 ? 137 ASN A OD1 1 
ATOM   1048 N  ND2 . ASN A 1 138 ? 14.332  26.631 56.723 1.00 24.24 ? 137 ASN A ND2 1 
ATOM   1049 N  N   . LEU A 1 139 ? 9.268   29.046 56.179 1.00 23.69 ? 138 LEU A N   1 
ATOM   1050 C  CA  . LEU A 1 139 ? 8.407   29.478 55.086 1.00 23.37 ? 138 LEU A CA  1 
ATOM   1051 C  C   . LEU A 1 139 ? 7.985   30.928 55.308 1.00 22.93 ? 138 LEU A C   1 
ATOM   1052 O  O   . LEU A 1 139 ? 7.564   31.281 56.416 1.00 27.26 ? 138 LEU A O   1 
ATOM   1053 C  CB  . LEU A 1 139 ? 7.187   28.572 54.971 1.00 24.26 ? 138 LEU A CB  1 
ATOM   1054 C  CG  . LEU A 1 139 ? 7.474   27.121 54.574 1.00 22.35 ? 138 LEU A CG  1 
ATOM   1055 C  CD1 . LEU A 1 139 ? 6.216   26.270 54.643 1.00 26.52 ? 138 LEU A CD1 1 
ATOM   1056 C  CD2 . LEU A 1 139 ? 8.086   27.058 53.181 1.00 24.83 ? 138 LEU A CD2 1 
ATOM   1057 N  N   . PRO A 1 140 ? 8.117   31.797 54.304 1.00 24.56 ? 139 PRO A N   1 
ATOM   1058 C  CA  . PRO A 1 140 ? 7.727   33.197 54.492 1.00 25.47 ? 139 PRO A CA  1 
ATOM   1059 C  C   . PRO A 1 140 ? 6.214   33.334 54.537 1.00 26.52 ? 139 PRO A C   1 
ATOM   1060 O  O   . PRO A 1 140 ? 5.470   32.434 54.148 1.00 27.93 ? 139 PRO A O   1 
ATOM   1061 C  CB  . PRO A 1 140 ? 8.315   33.902 53.267 1.00 25.13 ? 139 PRO A CB  1 
ATOM   1062 C  CG  . PRO A 1 140 ? 8.308   32.848 52.211 1.00 30.37 ? 139 PRO A CG  1 
ATOM   1063 C  CD  . PRO A 1 140 ? 8.581   31.538 52.928 1.00 25.75 ? 139 PRO A CD  1 
ATOM   1064 N  N   . ALA A 1 141 ? 5.770   34.484 55.032 1.00 23.75 ? 140 ALA A N   1 
ATOM   1065 C  CA  . ALA A 1 141 ? 4.354   34.729 55.231 1.00 23.33 ? 140 ALA A CA  1 
ATOM   1066 C  C   . ALA A 1 141 ? 3.915   35.944 54.427 1.00 21.79 ? 140 ALA A C   1 
ATOM   1067 O  O   . ALA A 1 141 ? 4.717   36.836 54.142 1.00 21.61 ? 140 ALA A O   1 
ATOM   1068 C  CB  . ALA A 1 141 ? 4.029   34.947 56.713 1.00 25.54 ? 140 ALA A CB  1 
ATOM   1069 N  N   . PRO A 1 142 ? 2.641   36.003 54.039 1.00 21.52 ? 141 PRO A N   1 
ATOM   1070 C  CA  . PRO A 1 142 ? 2.200   37.093 53.146 1.00 26.78 ? 141 PRO A CA  1 
ATOM   1071 C  C   . PRO A 1 142 ? 2.203   38.469 53.797 1.00 26.99 ? 141 PRO A C   1 
ATOM   1072 O  O   . PRO A 1 142 ? 2.177   39.471 53.072 1.00 28.23 ? 141 PRO A O   1 
ATOM   1073 C  CB  . PRO A 1 142 ? 0.783   36.668 52.736 1.00 23.70 ? 141 PRO A CB  1 
ATOM   1074 C  CG  . PRO A 1 142 ? 0.353   35.644 53.759 1.00 24.82 ? 141 PRO A CG  1 
ATOM   1075 C  CD  . PRO A 1 142 ? 1.606   34.970 54.227 1.00 25.57 ? 141 PRO A CD  1 
ATOM   1076 N  N   . PHE A 1 143 ? 2.242   38.557 55.123 1.00 22.84 ? 142 PHE A N   1 
ATOM   1077 C  CA  . PHE A 1 143 ? 2.300   39.833 55.821 1.00 24.01 ? 142 PHE A CA  1 
ATOM   1078 C  C   . PHE A 1 143 ? 3.729   40.260 56.142 1.00 26.51 ? 142 PHE A C   1 
ATOM   1079 O  O   . PHE A 1 143 ? 3.927   41.234 56.877 1.00 27.00 ? 142 PHE A O   1 
ATOM   1080 C  CB  . PHE A 1 143 ? 1.470   39.755 57.100 1.00 24.61 ? 142 PHE A CB  1 
ATOM   1081 C  CG  . PHE A 1 143 ? 1.813   38.579 57.962 1.00 23.83 ? 142 PHE A CG  1 
ATOM   1082 C  CD1 . PHE A 1 143 ? 2.938   38.601 58.758 1.00 30.30 ? 142 PHE A CD1 1 
ATOM   1083 C  CD2 . PHE A 1 143 ? 1.020   37.444 57.954 1.00 27.27 ? 142 PHE A CD2 1 
ATOM   1084 C  CE1 . PHE A 1 143 ? 3.268   37.519 59.544 1.00 32.29 ? 142 PHE A CE1 1 
ATOM   1085 C  CE2 . PHE A 1 143 ? 1.342   36.357 58.741 1.00 31.49 ? 142 PHE A CE2 1 
ATOM   1086 C  CZ  . PHE A 1 143 ? 2.469   36.396 59.536 1.00 28.17 ? 142 PHE A CZ  1 
ATOM   1087 N  N   . PHE A 1 144 ? 4.727   39.555 55.612 1.00 23.63 ? 143 PHE A N   1 
ATOM   1088 C  CA  . PHE A 1 144 ? 6.111   39.957 55.819 1.00 23.24 ? 143 PHE A CA  1 
ATOM   1089 C  C   . PHE A 1 144 ? 6.388   41.276 55.111 1.00 24.05 ? 143 PHE A C   1 
ATOM   1090 O  O   . PHE A 1 144 ? 5.894   41.527 54.010 1.00 28.60 ? 143 PHE A O   1 
ATOM   1091 C  CB  . PHE A 1 144 ? 7.074   38.894 55.285 1.00 23.53 ? 143 PHE A CB  1 
ATOM   1092 C  CG  . PHE A 1 144 ? 7.389   37.775 56.250 1.00 24.78 ? 143 PHE A CG  1 
ATOM   1093 C  CD1 . PHE A 1 144 ? 6.683   37.610 57.432 1.00 25.00 ? 143 PHE A CD1 1 
ATOM   1094 C  CD2 . PHE A 1 144 ? 8.410   36.882 55.958 1.00 23.59 ? 143 PHE A CD2 1 
ATOM   1095 C  CE1 . PHE A 1 144 ? 6.990   36.574 58.300 1.00 27.13 ? 143 PHE A CE1 1 
ATOM   1096 C  CE2 . PHE A 1 144 ? 8.720   35.848 56.823 1.00 24.48 ? 143 PHE A CE2 1 
ATOM   1097 C  CZ  . PHE A 1 144 ? 8.011   35.697 57.998 1.00 24.29 ? 143 PHE A CZ  1 
ATOM   1098 N  N   . THR A 1 145 ? 7.197   42.122 55.742 1.00 24.15 ? 144 THR A N   1 
ATOM   1099 C  CA  . THR A 1 145 ? 7.729   43.286 55.058 1.00 25.08 ? 144 THR A CA  1 
ATOM   1100 C  C   . THR A 1 145 ? 8.889   42.862 54.160 1.00 23.19 ? 144 THR A C   1 
ATOM   1101 O  O   . THR A 1 145 ? 9.385   41.737 54.232 1.00 24.28 ? 144 THR A O   1 
ATOM   1102 C  CB  . THR A 1 145 ? 8.206   44.329 56.062 1.00 26.89 ? 144 THR A CB  1 
ATOM   1103 O  OG1 . THR A 1 145 ? 9.275   43.771 56.832 1.00 26.00 ? 144 THR A OG1 1 
ATOM   1104 C  CG2 . THR A 1 145 ? 7.060   44.744 56.968 1.00 31.53 ? 144 THR A CG2 1 
ATOM   1105 N  N   . LEU A 1 146 ? 9.342   43.780 53.318 1.00 22.82 ? 145 LEU A N   1 
ATOM   1106 C  CA  . LEU A 1 146 ? 10.408  43.427 52.384 1.00 23.35 ? 145 LEU A CA  1 
ATOM   1107 C  C   . LEU A 1 146 ? 11.667  42.946 53.094 1.00 23.37 ? 145 LEU A C   1 
ATOM   1108 O  O   . LEU A 1 146 ? 12.220  41.912 52.681 1.00 20.49 ? 145 LEU A O   1 
ATOM   1109 C  CB  . LEU A 1 146 ? 10.706  44.605 51.458 1.00 21.64 ? 145 LEU A CB  1 
ATOM   1110 C  CG  . LEU A 1 146 ? 11.754  44.278 50.397 1.00 20.05 ? 145 LEU A CG  1 
ATOM   1111 C  CD1 . LEU A 1 146 ? 11.396  43.030 49.601 1.00 22.23 ? 145 LEU A CD1 1 
ATOM   1112 C  CD2 . LEU A 1 146 ? 11.917  45.475 49.470 1.00 22.54 ? 145 LEU A CD2 1 
ATOM   1113 N  N   . PRO A 1 147 ? 12.177  43.611 54.138 1.00 21.70 ? 146 PRO A N   1 
ATOM   1114 C  CA  . PRO A 1 147 ? 13.366  43.052 54.811 1.00 23.41 ? 146 PRO A CA  1 
ATOM   1115 C  C   . PRO A 1 147 ? 13.121  41.672 55.394 1.00 22.68 ? 146 PRO A C   1 
ATOM   1116 O  O   . PRO A 1 147 ? 14.044  40.852 55.435 1.00 23.77 ? 146 PRO A O   1 
ATOM   1117 C  CB  . PRO A 1 147 ? 13.685  44.083 55.906 1.00 25.33 ? 146 PRO A CB  1 
ATOM   1118 C  CG  . PRO A 1 147 ? 12.972  45.325 55.523 1.00 27.45 ? 146 PRO A CG  1 
ATOM   1119 C  CD  . PRO A 1 147 ? 11.764  44.903 54.720 1.00 26.42 ? 146 PRO A CD  1 
ATOM   1120 N  N   . GLN A 1 148 ? 11.900  41.374 55.847 1.00 22.01 ? 147 GLN A N   1 
ATOM   1121 C  CA  . GLN A 1 148 ? 11.630  40.034 56.356 1.00 20.59 ? 147 GLN A CA  1 
ATOM   1122 C  C   . GLN A 1 148 ? 11.609  39.007 55.233 1.00 20.37 ? 147 GLN A C   1 
ATOM   1123 O  O   . GLN A 1 148 ? 12.069  37.872 55.414 1.00 22.72 ? 147 GLN A O   1 
ATOM   1124 C  CB  . GLN A 1 148 ? 10.304  39.994 57.106 1.00 22.35 ? 147 GLN A CB  1 
ATOM   1125 C  CG  . GLN A 1 148 ? 10.307  40.744 58.404 1.00 24.37 ? 147 GLN A CG  1 
ATOM   1126 C  CD  . GLN A 1 148 ? 8.931   40.842 59.001 1.00 33.99 ? 147 GLN A CD  1 
ATOM   1127 O  OE1 . GLN A 1 148 ? 8.044   41.479 58.437 1.00 29.54 ? 147 GLN A OE1 1 
ATOM   1128 N  NE2 . GLN A 1 148 ? 8.738   40.197 60.142 1.00 33.51 ? 147 GLN A NE2 1 
ATOM   1129 N  N   . LEU A 1 149 ? 11.042  39.367 54.084 1.00 21.28 ? 148 LEU A N   1 
ATOM   1130 C  CA  . LEU A 1 149 ? 11.090  38.476 52.925 1.00 19.13 ? 148 LEU A CA  1 
ATOM   1131 C  C   . LEU A 1 149 ? 12.524  38.205 52.517 1.00 19.20 ? 148 LEU A C   1 
ATOM   1132 O  O   . LEU A 1 149 ? 12.904  37.064 52.241 1.00 19.42 ? 148 LEU A O   1 
ATOM   1133 C  CB  . LEU A 1 149 ? 10.324  39.100 51.755 1.00 19.74 ? 148 LEU A CB  1 
ATOM   1134 C  CG  . LEU A 1 149 ? 8.821   39.283 51.918 1.00 21.96 ? 148 LEU A CG  1 
ATOM   1135 C  CD1 . LEU A 1 149 ? 8.260   40.153 50.817 1.00 25.76 ? 148 LEU A CD1 1 
ATOM   1136 C  CD2 . LEU A 1 149 ? 8.184   37.903 51.926 1.00 22.52 ? 148 LEU A CD2 1 
ATOM   1137 N  N   . LYS A 1 150 ? 13.332  39.261 52.446 1.00 20.95 ? 149 LYS A N   1 
ATOM   1138 C  CA  . LYS A 1 150 ? 14.737  39.092 52.096 1.00 20.40 ? 149 LYS A CA  1 
ATOM   1139 C  C   . LYS A 1 150 ? 15.429  38.168 53.087 1.00 19.60 ? 149 LYS A C   1 
ATOM   1140 O  O   . LYS A 1 150 ? 16.170  37.264 52.689 1.00 22.88 ? 149 LYS A O   1 
ATOM   1141 C  CB  . LYS A 1 150 ? 15.420  40.453 52.050 1.00 18.68 ? 149 LYS A CB  1 
ATOM   1142 C  CG  . LYS A 1 150 ? 15.049  41.266 50.829 1.00 19.48 ? 149 LYS A CG  1 
ATOM   1143 C  CD  . LYS A 1 150 ? 15.586  42.679 50.950 1.00 22.14 ? 149 LYS A CD  1 
ATOM   1144 C  CE  . LYS A 1 150 ? 15.364  43.473 49.670 1.00 25.98 ? 149 LYS A CE  1 
ATOM   1145 N  NZ  . LYS A 1 150 ? 15.982  44.827 49.792 1.00 27.87 ? 149 LYS A NZ  1 
ATOM   1146 N  N   . ASP A 1 151 ? 15.172  38.360 54.385 1.00 23.07 ? 150 ASP A N   1 
ATOM   1147 C  CA  . ASP A 1 151 ? 15.803  37.506 55.384 1.00 23.29 ? 150 ASP A CA  1 
ATOM   1148 C  C   . ASP A 1 151 ? 15.347  36.061 55.236 1.00 22.57 ? 150 ASP A C   1 
ATOM   1149 O  O   . ASP A 1 151 ? 16.146  35.130 55.413 1.00 22.94 ? 150 ASP A O   1 
ATOM   1150 C  CB  . ASP A 1 151 ? 15.513  38.042 56.782 1.00 27.55 ? 150 ASP A CB  1 
ATOM   1151 C  CG  . ASP A 1 151 ? 16.375  39.249 57.138 1.00 40.15 ? 150 ASP A CG  1 
ATOM   1152 O  OD1 . ASP A 1 151 ? 17.424  39.453 56.489 1.00 41.39 ? 150 ASP A OD1 1 
ATOM   1153 O  OD2 . ASP A 1 151 ? 16.004  39.992 58.070 1.00 42.66 ? 150 ASP A OD2 1 
ATOM   1154 N  N   . SER A 1 152 ? 14.075  35.851 54.890 1.00 22.12 ? 151 SER A N   1 
ATOM   1155 C  CA  . SER A 1 152 ? 13.578  34.492 54.691 1.00 21.54 ? 151 SER A CA  1 
ATOM   1156 C  C   . SER A 1 152 ? 14.317  33.783 53.563 1.00 20.57 ? 151 SER A C   1 
ATOM   1157 O  O   . SER A 1 152 ? 14.665  32.600 53.688 1.00 19.57 ? 151 SER A O   1 
ATOM   1158 C  CB  . SER A 1 152 ? 12.070  34.537 54.406 1.00 23.83 ? 151 SER A CB  1 
ATOM   1159 O  OG  . SER A 1 152 ? 11.559  33.243 54.164 1.00 35.85 ? 151 SER A OG  1 
ATOM   1160 N  N   . PHE A 1 153 ? 14.563  34.481 52.451 1.00 20.34 ? 152 PHE A N   1 
ATOM   1161 C  CA  . PHE A 1 153 ? 15.308  33.875 51.345 1.00 19.62 ? 152 PHE A CA  1 
ATOM   1162 C  C   . PHE A 1 153 ? 16.777  33.695 51.706 1.00 17.92 ? 152 PHE A C   1 
ATOM   1163 O  O   . PHE A 1 153 ? 17.376  32.657 51.400 1.00 20.69 ? 152 PHE A O   1 
ATOM   1164 C  CB  . PHE A 1 153 ? 15.139  34.729 50.083 1.00 19.09 ? 152 PHE A CB  1 
ATOM   1165 C  CG  . PHE A 1 153 ? 13.890  34.407 49.312 1.00 20.35 ? 152 PHE A CG  1 
ATOM   1166 C  CD1 . PHE A 1 153 ? 12.659  34.424 49.938 1.00 19.56 ? 152 PHE A CD1 1 
ATOM   1167 C  CD2 . PHE A 1 153 ? 13.951  34.062 47.968 1.00 23.72 ? 152 PHE A CD2 1 
ATOM   1168 C  CE1 . PHE A 1 153 ? 11.501  34.109 49.250 1.00 20.96 ? 152 PHE A CE1 1 
ATOM   1169 C  CE2 . PHE A 1 153 ? 12.792  33.750 47.268 1.00 21.09 ? 152 PHE A CE2 1 
ATOM   1170 C  CZ  . PHE A 1 153 ? 11.572  33.773 47.912 1.00 20.80 ? 152 PHE A CZ  1 
ATOM   1171 N  N   . ARG A 1 154 ? 17.372  34.690 52.375 1.00 19.53 ? 153 ARG A N   1 
ATOM   1172 C  CA  . ARG A 1 154 ? 18.770  34.581 52.779 1.00 20.53 ? 153 ARG A CA  1 
ATOM   1173 C  C   . ARG A 1 154 ? 18.977  33.400 53.713 1.00 20.65 ? 153 ARG A C   1 
ATOM   1174 O  O   . ARG A 1 154 ? 20.005  32.715 53.652 1.00 22.12 ? 153 ARG A O   1 
ATOM   1175 C  CB  . ARG A 1 154 ? 19.220  35.890 53.431 1.00 21.06 ? 153 ARG A CB  1 
ATOM   1176 C  CG  . ARG A 1 154 ? 19.250  37.038 52.436 1.00 21.40 ? 153 ARG A CG  1 
ATOM   1177 C  CD  . ARG A 1 154 ? 19.329  38.407 53.083 1.00 23.77 ? 153 ARG A CD  1 
ATOM   1178 N  NE  . ARG A 1 154 ? 19.147  39.447 52.077 1.00 23.93 ? 153 ARG A NE  1 
ATOM   1179 C  CZ  . ARG A 1 154 ? 19.157  40.750 52.326 1.00 21.40 ? 153 ARG A CZ  1 
ATOM   1180 N  NH1 . ARG A 1 154 ? 19.341  41.216 53.547 1.00 28.19 ? 153 ARG A NH1 1 
ATOM   1181 N  NH2 . ARG A 1 154 ? 18.970  41.602 51.321 1.00 28.00 ? 153 ARG A NH2 1 
ATOM   1182 N  N   . ASN A 1 155 ? 17.989  33.128 54.557 1.00 21.10 ? 154 ASN A N   1 
ATOM   1183 C  CA  . ASN A 1 155 ? 18.095  32.060 55.545 1.00 23.20 ? 154 ASN A CA  1 
ATOM   1184 C  C   . ASN A 1 155 ? 18.185  30.683 54.901 1.00 23.12 ? 154 ASN A C   1 
ATOM   1185 O  O   . ASN A 1 155 ? 18.757  29.765 55.497 1.00 26.88 ? 154 ASN A O   1 
ATOM   1186 C  CB  . ASN A 1 155 ? 16.894  32.135 56.483 1.00 24.13 ? 154 ASN A CB  1 
ATOM   1187 C  CG  . ASN A 1 155 ? 16.874  31.021 57.494 1.00 27.59 ? 154 ASN A CG  1 
ATOM   1188 O  OD1 . ASN A 1 155 ? 17.760  30.924 58.330 1.00 28.19 ? 154 ASN A OD1 1 
ATOM   1189 N  ND2 . ASN A 1 155 ? 15.851  30.181 57.428 1.00 29.93 ? 154 ASN A ND2 1 
ATOM   1190 N  N   . VAL A 1 156 ? 17.624  30.498 53.702 1.00 23.98 ? 155 VAL A N   1 
ATOM   1191 C  CA  . VAL A 1 156 ? 17.745  29.215 53.020 1.00 20.57 ? 155 VAL A CA  1 
ATOM   1192 C  C   . VAL A 1 156 ? 18.830  29.218 51.958 1.00 25.87 ? 155 VAL A C   1 
ATOM   1193 O  O   . VAL A 1 156 ? 19.011  28.205 51.270 1.00 29.70 ? 155 VAL A O   1 
ATOM   1194 C  CB  . VAL A 1 156 ? 16.395  28.779 52.407 1.00 22.19 ? 155 VAL A CB  1 
ATOM   1195 C  CG1 . VAL A 1 156 ? 15.360  28.679 53.506 1.00 22.84 ? 155 VAL A CG1 1 
ATOM   1196 C  CG2 . VAL A 1 156 ? 15.950  29.741 51.323 1.00 22.01 ? 155 VAL A CG2 1 
ATOM   1197 N  N   . GLY A 1 157 ? 19.558  30.320 51.801 1.00 25.54 ? 156 GLY A N   1 
ATOM   1198 C  CA  . GLY A 1 157 ? 20.693  30.366 50.903 1.00 24.46 ? 156 GLY A CA  1 
ATOM   1199 C  C   . GLY A 1 157 ? 20.481  31.109 49.606 1.00 26.83 ? 156 GLY A C   1 
ATOM   1200 O  O   . GLY A 1 157 ? 21.333  31.018 48.716 1.00 29.93 ? 156 GLY A O   1 
ATOM   1201 N  N   . LEU A 1 158 ? 19.373  31.830 49.461 1.00 21.80 ? 157 LEU A N   1 
ATOM   1202 C  CA  . LEU A 1 158 ? 19.111  32.644 48.278 1.00 22.44 ? 157 LEU A CA  1 
ATOM   1203 C  C   . LEU A 1 158 ? 19.369  34.094 48.674 1.00 21.64 ? 157 LEU A C   1 
ATOM   1204 O  O   . LEU A 1 158 ? 18.475  34.802 49.150 1.00 22.28 ? 157 LEU A O   1 
ATOM   1205 C  CB  . LEU A 1 158 ? 17.688  32.426 47.776 1.00 23.28 ? 157 LEU A CB  1 
ATOM   1206 C  CG  . LEU A 1 158 ? 17.410  30.985 47.348 1.00 22.47 ? 157 LEU A CG  1 
ATOM   1207 C  CD1 . LEU A 1 158 ? 15.935  30.785 47.095 1.00 26.78 ? 157 LEU A CD1 1 
ATOM   1208 C  CD2 . LEU A 1 158 ? 18.225  30.634 46.115 1.00 26.55 ? 157 LEU A CD2 1 
ATOM   1209 N  N   . ASN A 1 159 ? 20.608  34.534 48.464 1.00 20.80 ? 158 ASN A N   1 
ATOM   1210 C  CA  . ASN A 1 159 ? 21.032  35.845 48.934 1.00 21.40 ? 158 ASN A CA  1 
ATOM   1211 C  C   . ASN A 1 159 ? 20.576  36.997 48.052 1.00 24.22 ? 158 ASN A C   1 
ATOM   1212 O  O   . ASN A 1 159 ? 20.549  38.140 48.518 1.00 24.35 ? 158 ASN A O   1 
ATOM   1213 C  CB  . ASN A 1 159 ? 22.555  35.929 49.011 1.00 20.19 ? 158 ASN A CB  1 
ATOM   1214 C  CG  . ASN A 1 159 ? 23.119  35.341 50.271 1.00 22.31 ? 158 ASN A CG  1 
ATOM   1215 O  OD1 . ASN A 1 159 ? 22.389  34.840 51.125 1.00 23.41 ? 158 ASN A OD1 1 
ATOM   1216 N  ND2 . ASN A 1 159 ? 24.439  35.390 50.398 1.00 22.62 ? 158 ASN A ND2 1 
ATOM   1217 N  N   . ARG A 1 160 ? 20.259  36.741 46.792 1.00 22.49 ? 159 ARG A N   1 
ATOM   1218 C  CA  . ARG A 1 160 ? 20.166  37.809 45.807 1.00 22.57 ? 159 ARG A CA  1 
ATOM   1219 C  C   . ARG A 1 160 ? 18.750  38.349 45.714 1.00 22.33 ? 159 ARG A C   1 
ATOM   1220 O  O   . ARG A 1 160 ? 17.775  37.592 45.730 1.00 23.37 ? 159 ARG A O   1 
ATOM   1221 C  CB  . ARG A 1 160 ? 20.631  37.302 44.449 1.00 24.04 ? 159 ARG A CB  1 
ATOM   1222 C  CG  . ARG A 1 160 ? 21.976  36.629 44.549 1.00 25.11 ? 159 ARG A CG  1 
ATOM   1223 C  CD  . ARG A 1 160 ? 22.375  35.966 43.262 1.00 24.87 ? 159 ARG A CD  1 
ATOM   1224 N  NE  . ARG A 1 160 ? 23.645  35.264 43.404 1.00 24.26 ? 159 ARG A NE  1 
ATOM   1225 C  CZ  . ARG A 1 160 ? 24.199  34.537 42.445 1.00 29.67 ? 159 ARG A CZ  1 
ATOM   1226 N  NH1 . ARG A 1 160 ? 23.622  34.400 41.262 1.00 30.64 ? 159 ARG A NH1 1 
ATOM   1227 N  NH2 . ARG A 1 160 ? 25.355  33.927 42.681 1.00 26.03 ? 159 ARG A NH2 1 
ATOM   1228 N  N   . SER A 1 161 ? 18.643  39.674 45.622 1.00 21.93 ? 160 SER A N   1 
ATOM   1229 C  CA  . SER A 1 161 ? 17.327  40.260 45.411 1.00 27.51 ? 160 SER A CA  1 
ATOM   1230 C  C   . SER A 1 161 ? 16.696  39.718 44.141 1.00 23.00 ? 160 SER A C   1 
ATOM   1231 O  O   . SER A 1 161 ? 15.469  39.565 44.075 1.00 23.95 ? 160 SER A O   1 
ATOM   1232 C  CB  . SER A 1 161 ? 17.430  41.780 45.375 1.00 31.58 ? 160 SER A CB  1 
ATOM   1233 O  OG  . SER A 1 161 ? 17.664  42.270 46.686 1.00 36.16 ? 160 SER A OG  1 
ATOM   1234 N  N   . SER A 1 162 ? 17.513  39.380 43.139 1.00 25.29 ? 161 SER A N   1 
ATOM   1235 C  CA  . SER A 1 162 ? 16.980  38.797 41.911 1.00 25.04 ? 161 SER A CA  1 
ATOM   1236 C  C   . SER A 1 162 ? 16.319  37.446 42.175 1.00 23.80 ? 161 SER A C   1 
ATOM   1237 O  O   . SER A 1 162 ? 15.311  37.120 41.535 1.00 23.68 ? 161 SER A O   1 
ATOM   1238 C  CB  . SER A 1 162 ? 18.097  38.671 40.876 1.00 26.10 ? 161 SER A CB  1 
ATOM   1239 O  OG  . SER A 1 162 ? 19.170  37.887 41.362 1.00 29.40 ? 161 SER A OG  1 
ATOM   1240 N  N   . ASP A 1 163 ? 16.848  36.660 43.121 1.00 22.53 ? 162 ASP A N   1 
ATOM   1241 C  CA  . ASP A 1 163 ? 16.156  35.437 43.535 1.00 23.05 ? 162 ASP A CA  1 
ATOM   1242 C  C   . ASP A 1 163 ? 14.740  35.752 43.990 1.00 20.93 ? 162 ASP A C   1 
ATOM   1243 O  O   . ASP A 1 163 ? 13.767  35.130 43.542 1.00 21.39 ? 162 ASP A O   1 
ATOM   1244 C  CB  . ASP A 1 163 ? 16.877  34.746 44.697 1.00 25.10 ? 162 ASP A CB  1 
ATOM   1245 C  CG  . ASP A 1 163 ? 18.259  34.248 44.355 1.00 29.28 ? 162 ASP A CG  1 
ATOM   1246 O  OD1 . ASP A 1 163 ? 18.494  33.789 43.223 1.00 29.17 ? 162 ASP A OD1 1 
ATOM   1247 O  OD2 . ASP A 1 163 ? 19.114  34.288 45.271 1.00 26.53 ? 162 ASP A OD2 1 
ATOM   1248 N  N   . LEU A 1 164 ? 14.617  36.694 44.927 1.00 20.22 ? 163 LEU A N   1 
ATOM   1249 C  CA  . LEU A 1 164 ? 13.320  37.005 45.519 1.00 20.76 ? 163 LEU A CA  1 
ATOM   1250 C  C   . LEU A 1 164 ? 12.360  37.568 44.486 1.00 22.01 ? 163 LEU A C   1 
ATOM   1251 O  O   . LEU A 1 164 ? 11.194  37.152 44.414 1.00 22.08 ? 163 LEU A O   1 
ATOM   1252 C  CB  . LEU A 1 164 ? 13.503  37.992 46.669 1.00 19.80 ? 163 LEU A CB  1 
ATOM   1253 C  CG  . LEU A 1 164 ? 12.227  38.563 47.276 1.00 18.63 ? 163 LEU A CG  1 
ATOM   1254 C  CD1 . LEU A 1 164 ? 11.353  37.484 47.875 1.00 22.84 ? 163 LEU A CD1 1 
ATOM   1255 C  CD2 . LEU A 1 164 ? 12.604  39.614 48.318 1.00 23.69 ? 163 LEU A CD2 1 
ATOM   1256 N  N   . VAL A 1 165 ? 12.818  38.531 43.684 1.00 19.99 ? 164 VAL A N   1 
ATOM   1257 C  CA  . VAL A 1 165 ? 11.898  39.160 42.741 1.00 19.85 ? 164 VAL A CA  1 
ATOM   1258 C  C   . VAL A 1 165 ? 11.485  38.172 41.658 1.00 19.33 ? 164 VAL A C   1 
ATOM   1259 O  O   . VAL A 1 165 ? 10.308  38.103 41.280 1.00 19.84 ? 164 VAL A O   1 
ATOM   1260 C  CB  . VAL A 1 165 ? 12.519  40.435 42.143 1.00 20.20 ? 164 VAL A CB  1 
ATOM   1261 C  CG1 . VAL A 1 165 ? 11.561  41.056 41.146 1.00 20.69 ? 164 VAL A CG1 1 
ATOM   1262 C  CG2 . VAL A 1 165 ? 12.836  41.436 43.245 1.00 21.47 ? 164 VAL A CG2 1 
ATOM   1263 N  N   . ALA A 1 166 ? 12.430  37.379 41.157 1.00 18.87 ? 165 ALA A N   1 
ATOM   1264 C  CA  . ALA A 1 166 ? 12.089  36.450 40.079 1.00 20.23 ? 165 ALA A CA  1 
ATOM   1265 C  C   . ALA A 1 166 ? 11.191  35.326 40.586 1.00 18.22 ? 165 ALA A C   1 
ATOM   1266 O  O   . ALA A 1 166 ? 10.184  35.000 39.951 1.00 19.82 ? 165 ALA A O   1 
ATOM   1267 C  CB  . ALA A 1 166 ? 13.351  35.874 39.444 1.00 20.78 ? 165 ALA A CB  1 
ATOM   1268 N  N   . LEU A 1 167 ? 11.529  34.725 41.728 1.00 18.72 ? 166 LEU A N   1 
ATOM   1269 C  CA  . LEU A 1 167 ? 10.722  33.620 42.221 1.00 18.15 ? 166 LEU A CA  1 
ATOM   1270 C  C   . LEU A 1 167 ? 9.334   34.092 42.637 1.00 21.07 ? 166 LEU A C   1 
ATOM   1271 O  O   . LEU A 1 167 ? 8.367   33.329 42.534 1.00 20.37 ? 166 LEU A O   1 
ATOM   1272 C  CB  . LEU A 1 167 ? 11.449  32.924 43.367 1.00 19.42 ? 166 LEU A CB  1 
ATOM   1273 C  CG  . LEU A 1 167 ? 12.660  32.135 42.859 1.00 20.23 ? 166 LEU A CG  1 
ATOM   1274 C  CD1 . LEU A 1 167 ? 13.524  31.619 43.994 1.00 22.04 ? 166 LEU A CD1 1 
ATOM   1275 C  CD2 . LEU A 1 167 ? 12.228  30.972 41.968 1.00 22.75 ? 166 LEU A CD2 1 
ATOM   1276 N  N   . SER A 1 168 ? 9.202   35.349 43.069 1.00 20.28 ? 167 SER A N   1 
ATOM   1277 C  CA  . SER A 1 168 ? 7.871   35.857 43.396 1.00 21.57 ? 167 SER A CA  1 
ATOM   1278 C  C   . SER A 1 168 ? 6.973   35.871 42.171 1.00 20.10 ? 167 SER A C   1 
ATOM   1279 O  O   . SER A 1 168 ? 5.744   35.899 42.309 1.00 22.17 ? 167 SER A O   1 
ATOM   1280 C  CB  . SER A 1 168 ? 7.950   37.264 43.987 1.00 22.43 ? 167 SER A CB  1 
ATOM   1281 O  OG  . SER A 1 168 ? 8.608   37.265 45.241 1.00 24.22 ? 167 SER A OG  1 
ATOM   1282 N  N   . GLY A 1 169 ? 7.565   35.865 40.975 1.00 21.63 ? 168 GLY A N   1 
ATOM   1283 C  CA  . GLY A 1 169 ? 6.805   35.746 39.743 1.00 18.95 ? 168 GLY A CA  1 
ATOM   1284 C  C   . GLY A 1 169 ? 6.048   34.453 39.618 1.00 18.30 ? 168 GLY A C   1 
ATOM   1285 O  O   . GLY A 1 169 ? 5.215   34.318 38.711 1.00 21.73 ? 168 GLY A O   1 
ATOM   1286 N  N   . GLY A 1 170 ? 6.312   33.494 40.499 1.00 20.02 ? 169 GLY A N   1 
ATOM   1287 C  CA  . GLY A 1 170 ? 5.463   32.323 40.591 1.00 21.43 ? 169 GLY A CA  1 
ATOM   1288 C  C   . GLY A 1 170 ? 4.004   32.693 40.763 1.00 21.99 ? 169 GLY A C   1 
ATOM   1289 O  O   . GLY A 1 170 ? 3.113   31.916 40.397 1.00 22.75 ? 169 GLY A O   1 
ATOM   1290 N  N   . HIS A 1 171 ? 3.728   33.876 41.323 1.00 19.11 ? 170 HIS A N   1 
ATOM   1291 C  CA  . HIS A 1 171 ? 2.356   34.326 41.507 1.00 20.72 ? 170 HIS A CA  1 
ATOM   1292 C  C   . HIS A 1 171 ? 1.754   34.914 40.224 1.00 19.85 ? 170 HIS A C   1 
ATOM   1293 O  O   . HIS A 1 171 ? 0.725   35.597 40.281 1.00 23.15 ? 170 HIS A O   1 
ATOM   1294 C  CB  . HIS A 1 171 ? 2.260   35.343 42.648 1.00 20.40 ? 170 HIS A CB  1 
ATOM   1295 C  CG  . HIS A 1 171 ? 2.626   34.777 43.989 1.00 21.25 ? 170 HIS A CG  1 
ATOM   1296 N  ND1 . HIS A 1 171 ? 3.003   35.568 45.052 1.00 23.96 ? 170 HIS A ND1 1 
ATOM   1297 C  CD2 . HIS A 1 171 ? 2.673   33.499 44.437 1.00 21.23 ? 170 HIS A CD2 1 
ATOM   1298 C  CE1 . HIS A 1 171 ? 3.272   34.802 46.097 1.00 25.50 ? 170 HIS A CE1 1 
ATOM   1299 N  NE2 . HIS A 1 171 ? 3.086   33.539 45.754 1.00 19.43 ? 170 HIS A NE2 1 
ATOM   1300 N  N   . THR A 1 172 ? 2.386   34.672 39.069 1.00 19.71 ? 171 THR A N   1 
ATOM   1301 C  CA  . THR A 1 172 ? 1.757   34.986 37.795 1.00 21.25 ? 171 THR A CA  1 
ATOM   1302 C  C   . THR A 1 172 ? 0.635   34.010 37.457 1.00 22.41 ? 171 THR A C   1 
ATOM   1303 O  O   . THR A 1 172 ? -0.116  34.256 36.504 1.00 22.45 ? 171 THR A O   1 
ATOM   1304 C  CB  . THR A 1 172 ? 2.822   35.001 36.681 1.00 18.51 ? 171 THR A CB  1 
ATOM   1305 O  OG1 . THR A 1 172 ? 2.264   35.542 35.480 1.00 20.13 ? 171 THR A OG1 1 
ATOM   1306 C  CG2 . THR A 1 172 ? 3.345   33.607 36.403 1.00 21.52 ? 171 THR A CG2 1 
ATOM   1307 N  N   . PHE A 1 173 ? 0.484   32.926 38.219 1.00 20.55 ? 172 PHE A N   1 
ATOM   1308 C  CA  . PHE A 1 173 ? -0.678  32.057 38.110 1.00 21.94 ? 172 PHE A CA  1 
ATOM   1309 C  C   . PHE A 1 173 ? -1.017  31.554 39.512 1.00 23.98 ? 172 PHE A C   1 
ATOM   1310 O  O   . PHE A 1 173 ? -0.373  31.921 40.499 1.00 23.77 ? 172 PHE A O   1 
ATOM   1311 C  CB  . PHE A 1 173 ? -0.442  30.979 37.028 1.00 22.89 ? 172 PHE A CB  1 
ATOM   1312 C  CG  . PHE A 1 173 ? 0.658   29.980 37.303 1.00 21.62 ? 172 PHE A CG  1 
ATOM   1313 C  CD1 . PHE A 1 173 ? 1.465   30.034 38.428 1.00 23.66 ? 172 PHE A CD1 1 
ATOM   1314 C  CD2 . PHE A 1 173 ? 0.874   28.958 36.388 1.00 24.18 ? 172 PHE A CD2 1 
ATOM   1315 C  CE1 . PHE A 1 173 ? 2.452   29.074 38.625 1.00 23.16 ? 172 PHE A CE1 1 
ATOM   1316 C  CE2 . PHE A 1 173 ? 1.853   28.005 36.578 1.00 26.03 ? 172 PHE A CE2 1 
ATOM   1317 C  CZ  . PHE A 1 173 ? 2.644   28.060 37.697 1.00 21.05 ? 172 PHE A CZ  1 
ATOM   1318 N  N   . GLY A 1 174 ? -2.103  30.806 39.614 1.00 23.52 ? 173 GLY A N   1 
ATOM   1319 C  CA  . GLY A 1 174 ? -2.520  30.274 40.903 1.00 23.25 ? 173 GLY A CA  1 
ATOM   1320 C  C   . GLY A 1 174 ? -3.399  31.207 41.711 1.00 24.31 ? 173 GLY A C   1 
ATOM   1321 O  O   . GLY A 1 174 ? -3.733  32.332 41.320 1.00 23.81 ? 173 GLY A O   1 
ATOM   1322 N  N   . LYS A 1 175 ? -3.756  30.719 42.896 1.00 21.60 ? 174 LYS A N   1 
ATOM   1323 C  CA  . LYS A 1 175 ? -4.819  31.303 43.695 1.00 21.35 ? 174 LYS A CA  1 
ATOM   1324 C  C   . LYS A 1 175 ? -4.375  31.550 45.129 1.00 21.65 ? 174 LYS A C   1 
ATOM   1325 O  O   . LYS A 1 175 ? -3.485  30.885 45.657 1.00 21.63 ? 174 LYS A O   1 
ATOM   1326 C  CB  . LYS A 1 175 ? -6.056  30.398 43.741 1.00 24.39 ? 174 LYS A CB  1 
ATOM   1327 C  CG  . LYS A 1 175 ? -6.589  29.986 42.404 1.00 29.44 ? 174 LYS A CG  1 
ATOM   1328 C  CD  . LYS A 1 175 ? -7.639  30.971 41.942 1.00 31.23 ? 174 LYS A CD  1 
ATOM   1329 C  CE  . LYS A 1 175 ? -8.492  30.362 40.857 1.00 42.55 ? 174 LYS A CE  1 
ATOM   1330 N  NZ  . LYS A 1 175 ? -9.532  31.314 40.411 1.00 46.04 ? 174 LYS A NZ  1 
ATOM   1331 N  N   . ASN A 1 176 ? -5.069  32.492 45.762 1.00 21.66 ? 175 ASN A N   1 
ATOM   1332 C  CA  . ASN A 1 176 ? -4.827  32.913 47.130 1.00 22.55 ? 175 ASN A CA  1 
ATOM   1333 C  C   . ASN A 1 176 ? -6.145  33.029 47.880 1.00 24.98 ? 175 ASN A C   1 
ATOM   1334 O  O   . ASN A 1 176 ? -7.131  33.529 47.334 1.00 24.15 ? 175 ASN A O   1 
ATOM   1335 C  CB  . ASN A 1 176 ? -4.117  34.252 47.157 1.00 22.16 ? 175 ASN A CB  1 
ATOM   1336 C  CG  . ASN A 1 176 ? -4.029  34.827 48.545 1.00 25.43 ? 175 ASN A CG  1 
ATOM   1337 O  OD1 . ASN A 1 176 ? -3.291  34.323 49.385 1.00 27.21 ? 175 ASN A OD1 1 
ATOM   1338 N  ND2 . ASN A 1 176 ? -4.788  35.892 48.799 1.00 31.08 ? 175 ASN A ND2 1 
ATOM   1339 N  N   . GLN A 1 177 ? -6.157  32.594 49.135 1.00 20.95 ? 176 GLN A N   1 
ATOM   1340 C  CA  . GLN A 1 177 ? -7.368  32.667 49.940 1.00 21.88 ? 176 GLN A CA  1 
ATOM   1341 C  C   . GLN A 1 177 ? -7.593  34.079 50.458 1.00 21.71 ? 176 GLN A C   1 
ATOM   1342 O  O   . GLN A 1 177 ? -6.646  34.784 50.826 1.00 22.63 ? 176 GLN A O   1 
ATOM   1343 C  CB  . GLN A 1 177 ? -7.289  31.724 51.136 1.00 21.93 ? 176 GLN A CB  1 
ATOM   1344 C  CG  . GLN A 1 177 ? -7.217  30.273 50.782 1.00 24.62 ? 176 GLN A CG  1 
ATOM   1345 C  CD  . GLN A 1 177 ? -7.116  29.415 52.014 1.00 30.58 ? 176 GLN A CD  1 
ATOM   1346 O  OE1 . GLN A 1 177 ? -7.989  29.452 52.886 1.00 29.29 ? 176 GLN A OE1 1 
ATOM   1347 N  NE2 . GLN A 1 177 ? -6.036  28.655 52.118 1.00 31.22 ? 176 GLN A NE2 1 
ATOM   1348 N  N   . CYS A 1 178 ? -8.866  34.471 50.520 1.00 21.39 ? 177 CYS A N   1 
ATOM   1349 C  CA  . CYS A 1 178 ? -9.237  35.764 51.084 1.00 20.33 ? 177 CYS A CA  1 
ATOM   1350 C  C   . CYS A 1 178 ? -8.551  36.011 52.423 1.00 23.54 ? 177 CYS A C   1 
ATOM   1351 O  O   . CYS A 1 178 ? -8.180  37.149 52.738 1.00 22.42 ? 177 CYS A O   1 
ATOM   1352 C  CB  . CYS A 1 178 ? -10.755 35.839 51.268 1.00 22.97 ? 177 CYS A CB  1 
ATOM   1353 S  SG  . CYS A 1 178 ? -11.714 36.092 49.764 1.00 25.17 ? 177 CYS A SG  1 
ATOM   1354 N  N   . ARG A 1 179 ? -8.388  34.960 53.229 1.00 22.68 ? 178 ARG A N   1 
ATOM   1355 C  CA  . ARG A 1 179 ? -7.784  35.079 54.556 1.00 25.11 ? 178 ARG A CA  1 
ATOM   1356 C  C   . ARG A 1 179 ? -6.545  35.966 54.523 1.00 22.62 ? 178 ARG A C   1 
ATOM   1357 O  O   . ARG A 1 179 ? -6.342  36.795 55.418 1.00 26.17 ? 178 ARG A O   1 
ATOM   1358 C  CB  . ARG A 1 179 ? -7.421  33.693 55.108 1.00 25.72 ? 178 ARG A CB  1 
ATOM   1359 C  CG  . ARG A 1 179 ? -6.909  33.680 56.555 1.00 35.20 ? 178 ARG A CG  1 
ATOM   1360 C  CD  . ARG A 1 179 ? -6.650  32.254 57.063 1.00 35.29 ? 178 ARG A CD  1 
ATOM   1361 N  NE  . ARG A 1 179 ? -7.631  31.300 56.556 1.00 42.10 ? 178 ARG A NE  1 
ATOM   1362 C  CZ  . ARG A 1 179 ? -8.723  30.918 57.203 1.00 46.31 ? 178 ARG A CZ  1 
ATOM   1363 N  NH1 . ARG A 1 179 ? -8.986  31.341 58.428 1.00 41.15 ? 178 ARG A NH1 1 
ATOM   1364 N  NH2 . ARG A 1 179 ? -9.576  30.088 56.604 1.00 49.59 ? 178 ARG A NH2 1 
ATOM   1365 N  N   . PHE A 1 180 ? -5.727  35.827 53.498 1.00 22.08 ? 179 PHE A N   1 
ATOM   1366 C  CA  . PHE A 1 180 ? -4.395  36.429 53.515 1.00 24.39 ? 179 PHE A CA  1 
ATOM   1367 C  C   . PHE A 1 180 ? -4.363  37.847 52.977 1.00 25.51 ? 179 PHE A C   1 
ATOM   1368 O  O   . PHE A 1 180 ? -3.286  38.456 52.958 1.00 25.56 ? 179 PHE A O   1 
ATOM   1369 C  CB  . PHE A 1 180 ? -3.430  35.535 52.749 1.00 23.29 ? 179 PHE A CB  1 
ATOM   1370 C  CG  . PHE A 1 180 ? -3.427  34.119 53.247 1.00 23.58 ? 179 PHE A CG  1 
ATOM   1371 C  CD1 . PHE A 1 180 ? -3.131  33.851 54.571 1.00 31.30 ? 179 PHE A CD1 1 
ATOM   1372 C  CD2 . PHE A 1 180 ? -3.747  33.071 52.406 1.00 25.87 ? 179 PHE A CD2 1 
ATOM   1373 C  CE1 . PHE A 1 180 ? -3.141  32.559 55.050 1.00 30.76 ? 179 PHE A CE1 1 
ATOM   1374 C  CE2 . PHE A 1 180 ? -3.758  31.772 52.879 1.00 29.60 ? 179 PHE A CE2 1 
ATOM   1375 C  CZ  . PHE A 1 180 ? -3.454  31.519 54.203 1.00 31.59 ? 179 PHE A CZ  1 
ATOM   1376 N  N   . ILE A 1 181 ? -5.504  38.412 52.586 1.00 24.97 ? 180 ILE A N   1 
ATOM   1377 C  CA  . ILE A 1 181 ? -5.565  39.810 52.183 1.00 24.98 ? 180 ILE A CA  1 
ATOM   1378 C  C   . ILE A 1 181 ? -6.552  40.618 53.006 1.00 24.54 ? 180 ILE A C   1 
ATOM   1379 O  O   . ILE A 1 181 ? -6.653  41.833 52.805 1.00 23.75 ? 180 ILE A O   1 
ATOM   1380 C  CB  . ILE A 1 181 ? -5.887  39.956 50.680 1.00 23.37 ? 180 ILE A CB  1 
ATOM   1381 C  CG1 . ILE A 1 181 ? -7.204  39.276 50.321 1.00 22.42 ? 180 ILE A CG1 1 
ATOM   1382 C  CG2 . ILE A 1 181 ? -4.745  39.398 49.833 1.00 27.19 ? 180 ILE A CG2 1 
ATOM   1383 C  CD1 . ILE A 1 181 ? -7.744  39.712 48.971 1.00 24.16 ? 180 ILE A CD1 1 
ATOM   1384 N  N   . MET A 1 182 ? -7.261  39.991 53.953 1.00 25.93 ? 181 MET A N   1 
ATOM   1385 C  CA  . MET A 1 182 ? -8.285  40.711 54.707 1.00 26.85 ? 181 MET A CA  1 
ATOM   1386 C  C   . MET A 1 182 ? -7.710  41.947 55.386 1.00 24.49 ? 181 MET A C   1 
ATOM   1387 O  O   . MET A 1 182 ? -8.351  43.005 55.406 1.00 23.31 ? 181 MET A O   1 
ATOM   1388 C  CB  . MET A 1 182 ? -8.923  39.791 55.751 1.00 26.14 ? 181 MET A CB  1 
ATOM   1389 C  CG  . MET A 1 182 ? -9.697  38.619 55.176 1.00 26.47 ? 181 MET A CG  1 
ATOM   1390 S  SD  . MET A 1 182 ? -11.044 39.138 54.108 1.00 29.88 ? 181 MET A SD  1 
ATOM   1391 C  CE  . MET A 1 182 ? -12.260 39.629 55.327 1.00 30.39 ? 181 MET A CE  1 
ATOM   1392 N  N   . ASP A 1 183 ? -6.504  41.834 55.955 1.00 25.32 ? 182 ASP A N   1 
ATOM   1393 C  CA  . ASP A 1 183 ? -5.891  42.992 56.594 1.00 26.06 ? 182 ASP A CA  1 
ATOM   1394 C  C   . ASP A 1 183 ? -5.696  44.129 55.600 1.00 26.76 ? 182 ASP A C   1 
ATOM   1395 O  O   . ASP A 1 183 ? -5.989  45.291 55.908 1.00 23.93 ? 182 ASP A O   1 
ATOM   1396 C  CB  . ASP A 1 183 ? -4.556  42.596 57.243 1.00 27.62 ? 182 ASP A CB  1 
ATOM   1397 C  CG  . ASP A 1 183 ? -3.512  42.115 56.241 1.00 35.45 ? 182 ASP A CG  1 
ATOM   1398 O  OD1 . ASP A 1 183 ? -3.857  41.486 55.213 1.00 38.17 ? 182 ASP A OD1 1 
ATOM   1399 O  OD2 . ASP A 1 183 ? -2.316  42.359 56.500 1.00 44.34 ? 182 ASP A OD2 1 
ATOM   1400 N  N   . ARG A 1 184 ? -5.226  43.815 54.392 1.00 22.19 ? 183 ARG A N   1 
ATOM   1401 C  CA  . ARG A 1 184 ? -4.980  44.862 53.408 1.00 23.97 ? 183 ARG A CA  1 
ATOM   1402 C  C   . ARG A 1 184 ? -6.260  45.566 53.004 1.00 23.45 ? 183 ARG A C   1 
ATOM   1403 O  O   . ARG A 1 184 ? -6.231  46.736 52.608 1.00 21.88 ? 183 ARG A O   1 
ATOM   1404 C  CB  . ARG A 1 184 ? -4.320  44.282 52.163 1.00 24.62 ? 183 ARG A CB  1 
ATOM   1405 C  CG  . ARG A 1 184 ? -2.938  43.726 52.351 1.00 23.53 ? 183 ARG A CG  1 
ATOM   1406 C  CD  . ARG A 1 184 ? -2.314  43.484 50.987 1.00 23.36 ? 183 ARG A CD  1 
ATOM   1407 N  NE  . ARG A 1 184 ? -1.794  44.718 50.405 1.00 23.10 ? 183 ARG A NE  1 
ATOM   1408 C  CZ  . ARG A 1 184 ? -1.601  44.917 49.110 1.00 22.07 ? 183 ARG A CZ  1 
ATOM   1409 N  NH1 . ARG A 1 184 ? -1.945  44.009 48.213 1.00 22.64 ? 183 ARG A NH1 1 
ATOM   1410 N  NH2 . ARG A 1 184 ? -1.035  46.050 48.706 1.00 24.04 ? 183 ARG A NH2 1 
ATOM   1411 N  N   . LEU A 1 185 ? -7.386  44.866 53.061 1.00 22.84 ? 184 LEU A N   1 
ATOM   1412 C  CA  . LEU A 1 185 ? -8.645  45.431 52.605 1.00 21.71 ? 184 LEU A CA  1 
ATOM   1413 C  C   . LEU A 1 185 ? -9.361  46.226 53.682 1.00 22.33 ? 184 LEU A C   1 
ATOM   1414 O  O   . LEU A 1 185 ? -10.116 47.150 53.355 1.00 26.08 ? 184 LEU A O   1 
ATOM   1415 C  CB  . LEU A 1 185 ? -9.582  44.320 52.127 1.00 22.00 ? 184 LEU A CB  1 
ATOM   1416 C  CG  . LEU A 1 185 ? -9.067  43.356 51.060 1.00 22.10 ? 184 LEU A CG  1 
ATOM   1417 C  CD1 . LEU A 1 185 ? -10.190 42.443 50.593 1.00 24.78 ? 184 LEU A CD1 1 
ATOM   1418 C  CD2 . LEU A 1 185 ? -8.475  44.150 49.914 1.00 28.15 ? 184 LEU A CD2 1 
ATOM   1419 N  N   . TYR A 1 186 ? -9.155  45.887 54.955 1.00 22.84 ? 185 TYR A N   1 
ATOM   1420 C  CA  . TYR A 1 186 ? -10.024 46.431 55.995 1.00 23.68 ? 185 TYR A CA  1 
ATOM   1421 C  C   . TYR A 1 186 ? -9.301  46.941 57.231 1.00 27.89 ? 185 TYR A C   1 
ATOM   1422 O  O   . TYR A 1 186 ? -9.833  47.785 57.956 1.00 28.69 ? 185 TYR A O   1 
ATOM   1423 C  CB  . TYR A 1 186 ? -11.036 45.367 56.435 1.00 24.23 ? 185 TYR A CB  1 
ATOM   1424 C  CG  . TYR A 1 186 ? -11.877 44.844 55.309 1.00 23.39 ? 185 TYR A CG  1 
ATOM   1425 C  CD1 . TYR A 1 186 ? -12.744 45.688 54.640 1.00 24.66 ? 185 TYR A CD1 1 
ATOM   1426 C  CD2 . TYR A 1 186 ? -11.807 43.516 54.908 1.00 25.98 ? 185 TYR A CD2 1 
ATOM   1427 C  CE1 . TYR A 1 186 ? -13.516 45.238 53.598 1.00 24.70 ? 185 TYR A CE1 1 
ATOM   1428 C  CE2 . TYR A 1 186 ? -12.580 43.049 53.864 1.00 24.68 ? 185 TYR A CE2 1 
ATOM   1429 C  CZ  . TYR A 1 186 ? -13.430 43.921 53.216 1.00 23.64 ? 185 TYR A CZ  1 
ATOM   1430 O  OH  . TYR A 1 186 ? -14.212 43.473 52.176 1.00 23.44 ? 185 TYR A OH  1 
ATOM   1431 N  N   . ASN A 1 187 ? -8.108  46.428 57.502 1.00 24.36 ? 186 ASN A N   1 
ATOM   1432 C  CA  . ASN A 1 187 ? -7.436  46.782 58.745 1.00 26.13 ? 186 ASN A CA  1 
ATOM   1433 C  C   . ASN A 1 187 ? -5.957  46.485 58.599 1.00 25.75 ? 186 ASN A C   1 
ATOM   1434 O  O   . ASN A 1 187 ? -5.467  45.434 59.024 1.00 25.33 ? 186 ASN A O   1 
ATOM   1435 C  CB  . ASN A 1 187 ? -8.043  46.019 59.915 1.00 26.68 ? 186 ASN A CB  1 
ATOM   1436 C  CG  . ASN A 1 187 ? -7.350  46.322 61.230 1.00 26.32 ? 186 ASN A CG  1 
ATOM   1437 O  OD1 . ASN A 1 187 ? -6.641  47.326 61.365 1.00 27.19 ? 186 ASN A OD1 1 
ATOM   1438 N  ND2 . ASN A 1 187 ? -7.557  45.452 62.204 1.00 28.90 ? 186 ASN A ND2 1 
ATOM   1439 N  N   . PHE A 1 188 ? -5.244  47.407 57.985 1.00 22.68 ? 187 PHE A N   1 
ATOM   1440 C  CA  . PHE A 1 188 ? -3.845  47.194 57.671 1.00 25.21 ? 187 PHE A CA  1 
ATOM   1441 C  C   . PHE A 1 188 ? -2.992  47.745 58.799 1.00 24.96 ? 187 PHE A C   1 
ATOM   1442 O  O   . PHE A 1 188 ? -3.119  48.917 59.165 1.00 25.15 ? 187 PHE A O   1 
ATOM   1443 C  CB  . PHE A 1 188 ? -3.476  47.860 56.358 1.00 23.28 ? 187 PHE A CB  1 
ATOM   1444 C  CG  . PHE A 1 188 ? -2.135  47.456 55.873 1.00 23.10 ? 187 PHE A CG  1 
ATOM   1445 C  CD1 . PHE A 1 188 ? -1.908  46.149 55.494 1.00 26.39 ? 187 PHE A CD1 1 
ATOM   1446 C  CD2 . PHE A 1 188 ? -1.104  48.368 55.818 1.00 29.35 ? 187 PHE A CD2 1 
ATOM   1447 C  CE1 . PHE A 1 188 ? -0.675  45.755 55.053 1.00 28.10 ? 187 PHE A CE1 1 
ATOM   1448 C  CE2 . PHE A 1 188 ? 0.138   47.987 55.374 1.00 28.38 ? 187 PHE A CE2 1 
ATOM   1449 C  CZ  . PHE A 1 188 ? 0.354   46.676 54.992 1.00 27.42 ? 187 PHE A CZ  1 
ATOM   1450 N  N   . SER A 1 189 ? -2.143  46.892 59.354 1.00 29.24 ? 188 SER A N   1 
ATOM   1451 C  CA  . SER A 1 189 ? -1.212  47.308 60.398 1.00 31.13 ? 188 SER A CA  1 
ATOM   1452 C  C   . SER A 1 189 ? -1.952  47.981 61.549 1.00 30.04 ? 188 SER A C   1 
ATOM   1453 O  O   . SER A 1 189 ? -1.486  48.970 62.118 1.00 29.75 ? 188 SER A O   1 
ATOM   1454 C  CB  . SER A 1 189 ? -0.143  48.236 59.820 1.00 35.57 ? 188 SER A CB  1 
ATOM   1455 O  OG  . SER A 1 189 ? 1.058   48.134 60.557 1.00 52.38 ? 188 SER A OG  1 
ATOM   1456 N  N   . ASN A 1 190 ? -3.126  47.443 61.882 1.00 27.06 ? 189 ASN A N   1 
ATOM   1457 C  CA  . ASN A 1 190 ? -3.901  47.896 63.039 1.00 26.85 ? 189 ASN A CA  1 
ATOM   1458 C  C   . ASN A 1 190 ? -4.351  49.348 62.896 1.00 30.72 ? 189 ASN A C   1 
ATOM   1459 O  O   . ASN A 1 190 ? -4.413  50.097 63.873 1.00 27.09 ? 189 ASN A O   1 
ATOM   1460 C  CB  . ASN A 1 190 ? -3.099  47.701 64.325 1.00 26.51 ? 189 ASN A CB  1 
ATOM   1461 C  CG  . ASN A 1 190 ? -2.741  46.250 64.558 1.00 30.62 ? 189 ASN A CG  1 
ATOM   1462 O  OD1 . ASN A 1 190 ? -1.568  45.871 64.518 1.00 36.90 ? 189 ASN A OD1 1 
ATOM   1463 N  ND2 . ASN A 1 190 ? -3.748  45.424 64.798 1.00 27.88 ? 189 ASN A ND2 1 
ATOM   1464 N  N   . THR A 1 191 ? -4.701  49.743 61.673 1.00 28.09 ? 190 THR A N   1 
ATOM   1465 C  CA  . THR A 1 191 ? -5.258  51.067 61.443 1.00 28.93 ? 190 THR A CA  1 
ATOM   1466 C  C   . THR A 1 191 ? -6.769  51.060 61.277 1.00 28.93 ? 190 THR A C   1 
ATOM   1467 O  O   . THR A 1 191 ? -7.384  52.129 61.316 1.00 34.51 ? 190 THR A O   1 
ATOM   1468 C  CB  . THR A 1 191 ? -4.624  51.706 60.201 1.00 33.12 ? 190 THR A CB  1 
ATOM   1469 O  OG1 . THR A 1 191 ? -4.894  50.905 59.043 1.00 28.46 ? 190 THR A OG1 1 
ATOM   1470 C  CG2 . THR A 1 191 ? -3.122  51.844 60.376 1.00 32.55 ? 190 THR A CG2 1 
ATOM   1471 N  N   . GLY A 1 192 ? -7.386  49.897 61.103 1.00 30.33 ? 191 GLY A N   1 
ATOM   1472 C  CA  . GLY A 1 192 ? -8.774  49.881 60.689 1.00 31.57 ? 191 GLY A CA  1 
ATOM   1473 C  C   . GLY A 1 192 ? -8.996  50.460 59.313 1.00 31.38 ? 191 GLY A C   1 
ATOM   1474 O  O   . GLY A 1 192 ? -10.134 50.780 58.957 1.00 30.74 ? 191 GLY A O   1 
ATOM   1475 N  N   . LEU A 1 193 ? -7.942  50.606 58.526 1.00 27.53 ? 192 LEU A N   1 
ATOM   1476 C  CA  . LEU A 1 193 ? -8.017  51.158 57.183 1.00 23.55 ? 192 LEU A CA  1 
ATOM   1477 C  C   . LEU A 1 193 ? -7.314  50.243 56.197 1.00 26.49 ? 192 LEU A C   1 
ATOM   1478 O  O   . LEU A 1 193 ? -6.466  49.428 56.585 1.00 23.40 ? 192 LEU A O   1 
ATOM   1479 C  CB  . LEU A 1 193 ? -7.367  52.549 57.115 1.00 25.26 ? 192 LEU A CB  1 
ATOM   1480 C  CG  . LEU A 1 193 ? -8.105  53.661 57.860 1.00 29.70 ? 192 LEU A CG  1 
ATOM   1481 C  CD1 . LEU A 1 193 ? -7.249  54.917 57.837 1.00 34.22 ? 192 LEU A CD1 1 
ATOM   1482 C  CD2 . LEU A 1 193 ? -9.463  53.915 57.242 1.00 36.66 ? 192 LEU A CD2 1 
ATOM   1483 N  N   . PRO A 1 194 ? -7.631  50.361 54.910 1.00 27.31 ? 193 PRO A N   1 
ATOM   1484 C  CA  . PRO A 1 194 ? -6.930  49.547 53.912 1.00 23.50 ? 193 PRO A CA  1 
ATOM   1485 C  C   . PRO A 1 194 ? -5.475  49.967 53.752 1.00 24.87 ? 193 PRO A C   1 
ATOM   1486 O  O   . PRO A 1 194 ? -5.054  51.064 54.127 1.00 24.90 ? 193 PRO A O   1 
ATOM   1487 C  CB  . PRO A 1 194 ? -7.721  49.781 52.620 1.00 26.65 ? 193 PRO A CB  1 
ATOM   1488 C  CG  . PRO A 1 194 ? -8.454  51.066 52.837 1.00 29.44 ? 193 PRO A CG  1 
ATOM   1489 C  CD  . PRO A 1 194 ? -8.725  51.150 54.320 1.00 29.61 ? 193 PRO A CD  1 
ATOM   1490 N  N   . ASP A 1 195 ? -4.699  49.040 53.210 1.00 24.31 ? 194 ASP A N   1 
ATOM   1491 C  CA  . ASP A 1 195 ? -3.319  49.280 52.828 1.00 25.03 ? 194 ASP A CA  1 
ATOM   1492 C  C   . ASP A 1 195 ? -3.267  50.429 51.825 1.00 25.03 ? 194 ASP A C   1 
ATOM   1493 O  O   . ASP A 1 195 ? -3.850  50.315 50.737 1.00 26.02 ? 194 ASP A O   1 
ATOM   1494 C  CB  . ASP A 1 195 ? -2.762  47.985 52.242 1.00 27.10 ? 194 ASP A CB  1 
ATOM   1495 C  CG  . ASP A 1 195 ? -1.299  48.069 51.873 1.00 27.31 ? 194 ASP A CG  1 
ATOM   1496 O  OD1 . ASP A 1 195 ? -0.731  49.179 51.867 1.00 28.25 ? 194 ASP A OD1 1 
ATOM   1497 O  OD2 . ASP A 1 195 ? -0.722  47.002 51.576 1.00 27.27 ? 194 ASP A OD2 1 
ATOM   1498 N  N   . PRO A 1 196 ? -2.614  51.551 52.150 1.00 24.31 ? 195 PRO A N   1 
ATOM   1499 C  CA  . PRO A 1 196 ? -2.579  52.675 51.204 1.00 30.87 ? 195 PRO A CA  1 
ATOM   1500 C  C   . PRO A 1 196 ? -1.802  52.381 49.928 1.00 28.53 ? 195 PRO A C   1 
ATOM   1501 O  O   . PRO A 1 196 ? -1.906  53.168 48.978 1.00 34.59 ? 195 PRO A O   1 
ATOM   1502 C  CB  . PRO A 1 196 ? -1.912  53.799 52.012 1.00 33.04 ? 195 PRO A CB  1 
ATOM   1503 C  CG  . PRO A 1 196 ? -1.126  53.098 53.067 1.00 32.23 ? 195 PRO A CG  1 
ATOM   1504 C  CD  . PRO A 1 196 ? -1.922  51.869 53.416 1.00 27.32 ? 195 PRO A CD  1 
ATOM   1505 N  N   . THR A 1 197 ? -1.044  51.289 49.860 1.00 25.80 ? 196 THR A N   1 
ATOM   1506 C  CA  . THR A 1 197 ? -0.340  50.959 48.624 1.00 26.64 ? 196 THR A CA  1 
ATOM   1507 C  C   . THR A 1 197 ? -1.185  50.129 47.671 1.00 30.15 ? 196 THR A C   1 
ATOM   1508 O  O   . THR A 1 197 ? -0.713  49.779 46.590 1.00 26.30 ? 196 THR A O   1 
ATOM   1509 C  CB  . THR A 1 197 ? 0.970   50.207 48.909 1.00 26.63 ? 196 THR A CB  1 
ATOM   1510 O  OG1 . THR A 1 197 ? 0.699   48.955 49.553 1.00 30.19 ? 196 THR A OG1 1 
ATOM   1511 C  CG2 . THR A 1 197 ? 1.899   51.058 49.766 1.00 31.00 ? 196 THR A CG2 1 
ATOM   1512 N  N   . LEU A 1 198 ? -2.417  49.798 48.040 1.00 29.52 ? 197 LEU A N   1 
ATOM   1513 C  CA  . LEU A 1 198 ? -3.292  49.030 47.168 1.00 23.14 ? 197 LEU A CA  1 
ATOM   1514 C  C   . LEU A 1 198 ? -4.128  49.983 46.330 1.00 25.21 ? 197 LEU A C   1 
ATOM   1515 O  O   . LEU A 1 198 ? -4.790  50.878 46.869 1.00 27.52 ? 197 LEU A O   1 
ATOM   1516 C  CB  . LEU A 1 198 ? -4.182  48.111 47.997 1.00 24.52 ? 197 LEU A CB  1 
ATOM   1517 C  CG  . LEU A 1 198 ? -5.213  47.217 47.316 1.00 28.08 ? 197 LEU A CG  1 
ATOM   1518 C  CD1 . LEU A 1 198 ? -4.585  46.337 46.262 1.00 26.82 ? 197 LEU A CD1 1 
ATOM   1519 C  CD2 . LEU A 1 198 ? -5.894  46.385 48.402 1.00 26.64 ? 197 LEU A CD2 1 
ATOM   1520 N  N   . ASN A 1 199 ? -4.068  49.818 45.011 1.00 25.41 ? 198 ASN A N   1 
ATOM   1521 C  CA  . ASN A 1 199 ? -4.858  50.662 44.125 1.00 26.06 ? 198 ASN A CA  1 
ATOM   1522 C  C   . ASN A 1 199 ? -6.318  50.658 44.566 1.00 24.73 ? 198 ASN A C   1 
ATOM   1523 O  O   . ASN A 1 199 ? -6.899  49.601 44.825 1.00 25.22 ? 198 ASN A O   1 
ATOM   1524 C  CB  . ASN A 1 199 ? -4.738  50.170 42.686 1.00 27.76 ? 198 ASN A CB  1 
ATOM   1525 C  CG  . ASN A 1 199 ? -5.649  50.923 41.750 1.00 26.48 ? 198 ASN A CG  1 
ATOM   1526 O  OD1 . ASN A 1 199 ? -6.801  50.540 41.553 1.00 28.13 ? 198 ASN A OD1 1 
ATOM   1527 N  ND2 . ASN A 1 199 ? -5.148  52.015 41.183 1.00 34.11 ? 198 ASN A ND2 1 
ATOM   1528 N  N   . THR A 1 200 ? -6.913  51.850 44.648 1.00 28.36 ? 199 THR A N   1 
ATOM   1529 C  CA  . THR A 1 200 ? -8.210  51.973 45.307 1.00 28.99 ? 199 THR A CA  1 
ATOM   1530 C  C   . THR A 1 200 ? -9.341  51.397 44.462 1.00 24.33 ? 199 THR A C   1 
ATOM   1531 O  O   . THR A 1 200 ? -10.368 50.984 45.013 1.00 27.57 ? 199 THR A O   1 
ATOM   1532 C  CB  . THR A 1 200 ? -8.499  53.436 45.654 1.00 31.67 ? 199 THR A CB  1 
ATOM   1533 O  OG1 . THR A 1 200 ? -8.311  54.257 44.498 1.00 37.06 ? 199 THR A OG1 1 
ATOM   1534 C  CG2 . THR A 1 200 ? -7.587  53.906 46.784 1.00 34.53 ? 199 THR A CG2 1 
ATOM   1535 N  N   . THR A 1 201 ? -9.186  51.366 43.138 1.00 29.12 ? 200 THR A N   1 
ATOM   1536 C  CA  . THR A 1 201 ? -10.170 50.669 42.318 1.00 29.49 ? 200 THR A CA  1 
ATOM   1537 C  C   . THR A 1 201 ? -10.062 49.159 42.505 1.00 25.40 ? 200 THR A C   1 
ATOM   1538 O  O   . THR A 1 201 ? -11.079 48.473 42.661 1.00 27.93 ? 200 THR A O   1 
ATOM   1539 C  CB  . THR A 1 201 ? -9.999  51.055 40.849 1.00 35.99 ? 200 THR A CB  1 
ATOM   1540 O  OG1 . THR A 1 201 ? -10.144 52.474 40.713 1.00 42.24 ? 200 THR A OG1 1 
ATOM   1541 C  CG2 . THR A 1 201 ? -11.045 50.359 39.990 1.00 32.24 ? 200 THR A CG2 1 
ATOM   1542 N  N   . TYR A 1 202 ? -8.835  48.630 42.517 1.00 24.82 ? 201 TYR A N   1 
ATOM   1543 C  CA  . TYR A 1 202 ? -8.643  47.206 42.770 1.00 24.55 ? 201 TYR A CA  1 
ATOM   1544 C  C   . TYR A 1 202 ? -9.122  46.840 44.169 1.00 24.53 ? 201 TYR A C   1 
ATOM   1545 O  O   . TYR A 1 202 ? -9.701  45.769 44.375 1.00 24.26 ? 201 TYR A O   1 
ATOM   1546 C  CB  . TYR A 1 202 ? -7.169  46.849 42.580 1.00 24.15 ? 201 TYR A CB  1 
ATOM   1547 C  CG  . TYR A 1 202 ? -6.855  45.367 42.468 1.00 23.98 ? 201 TYR A CG  1 
ATOM   1548 C  CD1 . TYR A 1 202 ? -7.719  44.496 41.816 1.00 30.47 ? 201 TYR A CD1 1 
ATOM   1549 C  CD2 . TYR A 1 202 ? -5.676  44.859 42.981 1.00 27.77 ? 201 TYR A CD2 1 
ATOM   1550 C  CE1 . TYR A 1 202 ? -7.417  43.145 41.707 1.00 30.21 ? 201 TYR A CE1 1 
ATOM   1551 C  CE2 . TYR A 1 202 ? -5.365  43.518 42.877 1.00 30.64 ? 201 TYR A CE2 1 
ATOM   1552 C  CZ  . TYR A 1 202 ? -6.239  42.668 42.239 1.00 31.90 ? 201 TYR A CZ  1 
ATOM   1553 O  OH  . TYR A 1 202 ? -5.920  41.326 42.131 1.00 37.13 ? 201 TYR A OH  1 
ATOM   1554 N  N   . LEU A 1 203 ? -8.900  47.727 45.140 1.00 23.95 ? 202 LEU A N   1 
ATOM   1555 C  CA  . LEU A 1 203 ? -9.425  47.527 46.485 1.00 22.64 ? 202 LEU A CA  1 
ATOM   1556 C  C   . LEU A 1 203 ? -10.915 47.214 46.455 1.00 24.47 ? 202 LEU A C   1 
ATOM   1557 O  O   . LEU A 1 203 ? -11.389 46.302 47.140 1.00 24.13 ? 202 LEU A O   1 
ATOM   1558 C  CB  . LEU A 1 203 ? -9.169  48.778 47.326 1.00 23.90 ? 202 LEU A CB  1 
ATOM   1559 C  CG  . LEU A 1 203 ? -9.850  48.906 48.688 1.00 25.57 ? 202 LEU A CG  1 
ATOM   1560 C  CD1 . LEU A 1 203 ? -9.370  47.832 49.636 1.00 27.65 ? 202 LEU A CD1 1 
ATOM   1561 C  CD2 . LEU A 1 203 ? -9.585  50.303 49.248 1.00 30.05 ? 202 LEU A CD2 1 
ATOM   1562 N  N   . GLN A 1 204 ? -11.677 47.980 45.680 1.00 24.60 ? 203 GLN A N   1 
ATOM   1563 C  CA  . GLN A 1 204 ? -13.116 47.751 45.636 1.00 28.95 ? 203 GLN A CA  1 
ATOM   1564 C  C   . GLN A 1 204 ? -13.430 46.388 45.032 1.00 23.43 ? 203 GLN A C   1 
ATOM   1565 O  O   . GLN A 1 204 ? -14.292 45.664 45.541 1.00 26.97 ? 203 GLN A O   1 
ATOM   1566 C  CB  . GLN A 1 204 ? -13.787 48.886 44.866 1.00 31.46 ? 203 GLN A CB  1 
ATOM   1567 C  CG  . GLN A 1 204 ? -13.717 50.220 45.615 1.00 34.21 ? 203 GLN A CG  1 
ATOM   1568 C  CD  . GLN A 1 204 ? -14.458 50.195 46.945 1.00 47.07 ? 203 GLN A CD  1 
ATOM   1569 O  OE1 . GLN A 1 204 ? -13.843 50.193 48.014 1.00 48.37 ? 203 GLN A OE1 1 
ATOM   1570 N  NE2 . GLN A 1 204 ? -15.783 50.183 46.884 1.00 55.62 ? 203 GLN A NE2 1 
ATOM   1571 N  N   . THR A 1 205 ? -12.707 46.003 43.980 1.00 24.12 ? 204 THR A N   1 
ATOM   1572 C  CA  . THR A 1 205 ? -12.898 44.684 43.385 1.00 25.12 ? 204 THR A CA  1 
ATOM   1573 C  C   . THR A 1 205 ? -12.641 43.584 44.409 1.00 27.54 ? 204 THR A C   1 
ATOM   1574 O  O   . THR A 1 205 ? -13.435 42.643 44.545 1.00 24.87 ? 204 THR A O   1 
ATOM   1575 C  CB  . THR A 1 205 ? -11.972 44.514 42.186 1.00 33.30 ? 204 THR A CB  1 
ATOM   1576 O  OG1 . THR A 1 205 ? -12.346 45.436 41.154 1.00 34.83 ? 204 THR A OG1 1 
ATOM   1577 C  CG2 . THR A 1 205 ? -12.020 43.083 41.667 1.00 32.50 ? 204 THR A CG2 1 
ATOM   1578 N  N   . LEU A 1 206 ? -11.522 43.682 45.126 1.00 23.39 ? 205 LEU A N   1 
ATOM   1579 C  CA  . LEU A 1 206 ? -11.161 42.650 46.097 1.00 23.49 ? 205 LEU A CA  1 
ATOM   1580 C  C   . LEU A 1 206 ? -12.140 42.604 47.259 1.00 22.84 ? 205 LEU A C   1 
ATOM   1581 O  O   . LEU A 1 206 ? -12.435 41.529 47.785 1.00 24.36 ? 205 LEU A O   1 
ATOM   1582 C  CB  . LEU A 1 206 ? -9.740  42.895 46.605 1.00 22.54 ? 205 LEU A CB  1 
ATOM   1583 C  CG  . LEU A 1 206 ? -8.651  42.699 45.550 1.00 22.39 ? 205 LEU A CG  1 
ATOM   1584 C  CD1 . LEU A 1 206 ? -7.274  43.104 46.041 1.00 23.72 ? 205 LEU A CD1 1 
ATOM   1585 C  CD2 . LEU A 1 206 ? -8.629  41.244 45.077 1.00 26.16 ? 205 LEU A CD2 1 
ATOM   1586 N  N   . ARG A 1 207 ? -12.630 43.763 47.699 1.00 21.99 ? 206 ARG A N   1 
ATOM   1587 C  CA  . ARG A 1 207 ? -13.661 43.760 48.730 1.00 23.97 ? 206 ARG A CA  1 
ATOM   1588 C  C   . ARG A 1 207 ? -14.913 43.037 48.252 1.00 25.02 ? 206 ARG A C   1 
ATOM   1589 O  O   . ARG A 1 207 ? -15.602 42.397 49.054 1.00 23.07 ? 206 ARG A O   1 
ATOM   1590 C  CB  . ARG A 1 207 ? -13.991 45.188 49.149 1.00 23.07 ? 206 ARG A CB  1 
ATOM   1591 C  CG  . ARG A 1 207 ? -12.928 45.801 50.046 1.00 24.46 ? 206 ARG A CG  1 
ATOM   1592 C  CD  . ARG A 1 207 ? -13.236 47.252 50.355 1.00 25.74 ? 206 ARG A CD  1 
ATOM   1593 N  NE  . ARG A 1 207 ? -12.473 47.735 51.498 1.00 27.93 ? 206 ARG A NE  1 
ATOM   1594 C  CZ  . ARG A 1 207 ? -12.517 48.982 51.948 1.00 36.09 ? 206 ARG A CZ  1 
ATOM   1595 N  NH1 . ARG A 1 207 ? -13.181 49.925 51.300 1.00 42.83 ? 206 ARG A NH1 1 
ATOM   1596 N  NH2 . ARG A 1 207 ? -11.900 49.285 53.085 1.00 29.90 ? 206 ARG A NH2 1 
ATOM   1597 N  N   . GLY A 1 208 ? -15.217 43.114 46.951 1.00 24.77 ? 207 GLY A N   1 
ATOM   1598 C  CA  . GLY A 1 208 ? -16.363 42.397 46.421 1.00 26.59 ? 207 GLY A CA  1 
ATOM   1599 C  C   . GLY A 1 208 ? -16.187 40.894 46.437 1.00 24.72 ? 207 GLY A C   1 
ATOM   1600 O  O   . GLY A 1 208 ? -17.166 40.152 46.575 1.00 28.25 ? 207 GLY A O   1 
ATOM   1601 N  N   . LEU A 1 209 ? -14.951 40.425 46.306 1.00 22.69 ? 208 LEU A N   1 
ATOM   1602 C  CA  . LEU A 1 209 ? -14.630 39.004 46.360 1.00 21.97 ? 208 LEU A CA  1 
ATOM   1603 C  C   . LEU A 1 209 ? -14.413 38.503 47.776 1.00 23.81 ? 208 LEU A C   1 
ATOM   1604 O  O   . LEU A 1 209 ? -14.657 37.322 48.061 1.00 21.71 ? 208 LEU A O   1 
ATOM   1605 C  CB  . LEU A 1 209 ? -13.359 38.737 45.556 1.00 22.60 ? 208 LEU A CB  1 
ATOM   1606 C  CG  . LEU A 1 209 ? -13.396 39.066 44.071 1.00 25.04 ? 208 LEU A CG  1 
ATOM   1607 C  CD1 . LEU A 1 209 ? -11.988 38.923 43.525 1.00 22.98 ? 208 LEU A CD1 1 
ATOM   1608 C  CD2 . LEU A 1 209 ? -14.389 38.160 43.382 1.00 26.98 ? 208 LEU A CD2 1 
ATOM   1609 N  N   . CYS A 1 210 ? -13.929 39.379 48.653 1.00 21.53 ? 209 CYS A N   1 
ATOM   1610 C  CA  . CYS A 1 210 ? -13.549 39.040 50.020 1.00 21.05 ? 209 CYS A CA  1 
ATOM   1611 C  C   . CYS A 1 210 ? -14.212 40.037 50.953 1.00 22.11 ? 209 CYS A C   1 
ATOM   1612 O  O   . CYS A 1 210 ? -13.548 40.911 51.529 1.00 23.79 ? 209 CYS A O   1 
ATOM   1613 C  CB  . CYS A 1 210 ? -12.031 39.065 50.190 1.00 21.16 ? 209 CYS A CB  1 
ATOM   1614 S  SG  . CYS A 1 210 ? -11.134 37.940 49.120 1.00 24.89 ? 209 CYS A SG  1 
ATOM   1615 N  N   . PRO A 1 211 ? -15.530 39.955 51.108 1.00 23.32 ? 210 PRO A N   1 
ATOM   1616 C  CA  . PRO A 1 211 ? -16.218 40.877 52.016 1.00 24.73 ? 210 PRO A CA  1 
ATOM   1617 C  C   . PRO A 1 211 ? -15.847 40.592 53.467 1.00 25.90 ? 210 PRO A C   1 
ATOM   1618 O  O   . PRO A 1 211 ? -15.377 39.509 53.824 1.00 26.47 ? 210 PRO A O   1 
ATOM   1619 C  CB  . PRO A 1 211 ? -17.702 40.601 51.748 1.00 28.48 ? 210 PRO A CB  1 
ATOM   1620 C  CG  . PRO A 1 211 ? -17.731 39.173 51.239 1.00 23.63 ? 210 PRO A CG  1 
ATOM   1621 C  CD  . PRO A 1 211 ? -16.454 39.010 50.449 1.00 21.68 ? 210 PRO A CD  1 
ATOM   1622 N  N   . LEU A 1 212 ? -16.021 41.609 54.308 1.00 30.12 ? 211 LEU A N   1 
ATOM   1623 C  CA  . LEU A 1 212 ? -15.896 41.391 55.739 1.00 39.19 ? 211 LEU A CA  1 
ATOM   1624 C  C   . LEU A 1 212 ? -17.023 40.460 56.170 1.00 38.41 ? 211 LEU A C   1 
ATOM   1625 O  O   . LEU A 1 212 ? -18.145 40.546 55.660 1.00 42.18 ? 211 LEU A O   1 
ATOM   1626 C  CB  . LEU A 1 212 ? -15.940 42.727 56.478 1.00 43.06 ? 211 LEU A CB  1 
ATOM   1627 C  CG  . LEU A 1 212 ? -15.099 42.854 57.751 1.00 42.99 ? 211 LEU A CG  1 
ATOM   1628 C  CD1 . LEU A 1 212 ? -13.660 42.403 57.610 1.00 42.69 ? 211 LEU A CD1 1 
ATOM   1629 C  CD2 . LEU A 1 212 ? -15.126 44.328 58.198 1.00 45.75 ? 211 LEU A CD2 1 
ATOM   1630 N  N   . ASN A 1 213 ? -16.701 39.521 57.056 1.00 40.54 ? 212 ASN A N   1 
ATOM   1631 C  CA  . ASN A 1 213 ? -17.588 38.424 57.434 1.00 37.37 ? 212 ASN A CA  1 
ATOM   1632 C  C   . ASN A 1 213 ? -17.809 37.430 56.302 1.00 33.69 ? 212 ASN A C   1 
ATOM   1633 O  O   . ASN A 1 213 ? -18.773 36.655 56.333 1.00 34.33 ? 212 ASN A O   1 
ATOM   1634 C  CB  . ASN A 1 213 ? -18.948 38.944 57.913 1.00 43.74 ? 212 ASN A CB  1 
ATOM   1635 C  CG  . ASN A 1 213 ? -18.834 39.800 59.146 1.00 51.43 ? 212 ASN A CG  1 
ATOM   1636 O  OD1 . ASN A 1 213 ? -17.854 39.714 59.887 1.00 59.04 ? 212 ASN A OD1 1 
ATOM   1637 N  ND2 . ASN A 1 213 ? -19.834 40.639 59.375 1.00 57.61 ? 212 ASN A ND2 1 
ATOM   1638 N  N   . GLY A 1 214 ? -16.952 37.455 55.288 1.00 32.58 ? 213 GLY A N   1 
ATOM   1639 C  CA  . GLY A 1 214 ? -17.042 36.511 54.200 1.00 27.57 ? 213 GLY A CA  1 
ATOM   1640 C  C   . GLY A 1 214 ? -16.317 35.218 54.515 1.00 27.41 ? 213 GLY A C   1 
ATOM   1641 O  O   . GLY A 1 214 ? -15.671 35.066 55.552 1.00 28.03 ? 213 GLY A O   1 
ATOM   1642 N  N   . ASN A 1 215 ? -16.462 34.271 53.602 1.00 23.62 ? 214 ASN A N   1 
ATOM   1643 C  CA  . ASN A 1 215 ? -15.715 33.027 53.656 1.00 23.43 ? 214 ASN A CA  1 
ATOM   1644 C  C   . ASN A 1 215 ? -14.233 33.308 53.439 1.00 25.30 ? 214 ASN A C   1 
ATOM   1645 O  O   . ASN A 1 215 ? -13.826 33.752 52.358 1.00 23.87 ? 214 ASN A O   1 
ATOM   1646 C  CB  . ASN A 1 215 ? -16.235 32.067 52.589 1.00 24.85 ? 214 ASN A CB  1 
ATOM   1647 C  CG  . ASN A 1 215 ? -15.400 30.813 52.481 1.00 26.64 ? 214 ASN A CG  1 
ATOM   1648 O  OD1 . ASN A 1 215 ? -14.703 30.436 53.424 1.00 30.65 ? 214 ASN A OD1 1 
ATOM   1649 N  ND2 . ASN A 1 215 ? -15.463 30.160 51.329 1.00 28.01 ? 214 ASN A ND2 1 
ATOM   1650 N  N   . LEU A 1 216 ? -13.424 33.045 54.463 1.00 25.25 ? 215 LEU A N   1 
ATOM   1651 C  CA  . LEU A 1 216 ? -11.997 33.325 54.361 1.00 22.60 ? 215 LEU A CA  1 
ATOM   1652 C  C   . LEU A 1 216 ? -11.273 32.362 53.436 1.00 23.99 ? 215 LEU A C   1 
ATOM   1653 O  O   . LEU A 1 216 ? -10.167 32.674 52.983 1.00 25.18 ? 215 LEU A O   1 
ATOM   1654 C  CB  . LEU A 1 216 ? -11.364 33.280 55.753 1.00 24.55 ? 215 LEU A CB  1 
ATOM   1655 C  CG  . LEU A 1 216 ? -11.908 34.301 56.751 1.00 26.61 ? 215 LEU A CG  1 
ATOM   1656 C  CD1 . LEU A 1 216 ? -11.140 34.195 58.055 1.00 35.33 ? 215 LEU A CD1 1 
ATOM   1657 C  CD2 . LEU A 1 216 ? -11.823 35.701 56.179 1.00 29.66 ? 215 LEU A CD2 1 
ATOM   1658 N  N   . SER A 1 217 ? -11.857 31.204 53.136 1.00 23.26 ? 216 SER A N   1 
ATOM   1659 C  CA  . SER A 1 217 ? -11.214 30.247 52.246 1.00 20.01 ? 216 SER A CA  1 
ATOM   1660 C  C   . SER A 1 217 ? -11.566 30.458 50.781 1.00 23.96 ? 216 SER A C   1 
ATOM   1661 O  O   . SER A 1 217 ? -11.102 29.689 49.935 1.00 26.05 ? 216 SER A O   1 
ATOM   1662 C  CB  . SER A 1 217 ? -11.575 28.816 52.646 1.00 31.63 ? 216 SER A CB  1 
ATOM   1663 O  OG  . SER A 1 217 ? -10.973 28.472 53.878 1.00 36.15 ? 216 SER A OG  1 
ATOM   1664 N  N   . ALA A 1 218 ? -12.376 31.465 50.455 1.00 24.12 ? 217 ALA A N   1 
ATOM   1665 C  CA  . ALA A 1 218 ? -12.637 31.773 49.056 1.00 23.83 ? 217 ALA A CA  1 
ATOM   1666 C  C   . ALA A 1 218 ? -11.338 32.163 48.359 1.00 20.49 ? 217 ALA A C   1 
ATOM   1667 O  O   . ALA A 1 218 ? -10.460 32.792 48.954 1.00 21.95 ? 217 ALA A O   1 
ATOM   1668 C  CB  . ALA A 1 218 ? -13.670 32.895 48.945 1.00 21.53 ? 217 ALA A CB  1 
ATOM   1669 N  N   . LEU A 1 219 ? -11.210 31.777 47.094 1.00 23.66 ? 218 LEU A N   1 
ATOM   1670 C  CA  . LEU A 1 219 ? -9.960  31.934 46.365 1.00 23.72 ? 218 LEU A CA  1 
ATOM   1671 C  C   . LEU A 1 219 ? -10.020 33.118 45.411 1.00 20.86 ? 218 LEU A C   1 
ATOM   1672 O  O   . LEU A 1 219 ? -11.045 33.371 44.769 1.00 25.17 ? 218 LEU A O   1 
ATOM   1673 C  CB  . LEU A 1 219 ? -9.622  30.663 45.583 1.00 26.93 ? 218 LEU A CB  1 
ATOM   1674 C  CG  . LEU A 1 219 ? -9.406  29.410 46.430 1.00 28.62 ? 218 LEU A CG  1 
ATOM   1675 C  CD1 . LEU A 1 219 ? -9.321  28.175 45.535 1.00 32.66 ? 218 LEU A CD1 1 
ATOM   1676 C  CD2 . LEU A 1 219 ? -8.152  29.506 47.284 1.00 28.95 ? 218 LEU A CD2 1 
ATOM   1677 N  N   . VAL A 1 220 ? -8.905  33.833 45.320 1.00 21.82 ? 219 VAL A N   1 
ATOM   1678 C  CA  . VAL A 1 220 ? -8.747  34.972 44.427 1.00 22.98 ? 219 VAL A CA  1 
ATOM   1679 C  C   . VAL A 1 220 ? -7.491  34.747 43.589 1.00 22.67 ? 219 VAL A C   1 
ATOM   1680 O  O   . VAL A 1 220 ? -6.481  34.237 44.093 1.00 23.66 ? 219 VAL A O   1 
ATOM   1681 C  CB  . VAL A 1 220 ? -8.636  36.296 45.213 1.00 24.57 ? 219 VAL A CB  1 
ATOM   1682 C  CG1 . VAL A 1 220 ? -8.290  37.431 44.271 1.00 28.40 ? 219 VAL A CG1 1 
ATOM   1683 C  CG2 . VAL A 1 220 ? -9.927  36.588 45.978 1.00 29.67 ? 219 VAL A CG2 1 
ATOM   1684 N  N   . ASP A 1 221 ? -7.548  35.138 42.315 1.00 25.01 ? 220 ASP A N   1 
ATOM   1685 C  CA  . ASP A 1 221 ? -6.391  34.979 41.436 1.00 20.93 ? 220 ASP A CA  1 
ATOM   1686 C  C   . ASP A 1 221 ? -5.260  35.918 41.836 1.00 21.61 ? 220 ASP A C   1 
ATOM   1687 O  O   . ASP A 1 221 ? -5.474  37.112 42.059 1.00 24.03 ? 220 ASP A O   1 
ATOM   1688 C  CB  . ASP A 1 221 ? -6.774  35.261 39.983 1.00 23.24 ? 220 ASP A CB  1 
ATOM   1689 C  CG  . ASP A 1 221 ? -7.732  34.240 39.419 1.00 32.84 ? 220 ASP A CG  1 
ATOM   1690 O  OD1 . ASP A 1 221 ? -7.488  33.037 39.615 1.00 33.59 ? 220 ASP A OD1 1 
ATOM   1691 O  OD2 . ASP A 1 221 ? -8.722  34.649 38.769 1.00 36.30 ? 220 ASP A OD2 1 
ATOM   1692 N  N   . PHE A 1 222 ? -4.031  35.384 41.883 1.00 21.98 ? 221 PHE A N   1 
ATOM   1693 C  CA  . PHE A 1 222 ? -2.871  36.224 42.153 1.00 23.39 ? 221 PHE A CA  1 
ATOM   1694 C  C   . PHE A 1 222 ? -2.667  37.277 41.070 1.00 25.19 ? 221 PHE A C   1 
ATOM   1695 O  O   . PHE A 1 222 ? -2.270  38.412 41.358 1.00 25.03 ? 221 PHE A O   1 
ATOM   1696 C  CB  . PHE A 1 222 ? -1.615  35.362 42.257 1.00 23.02 ? 221 PHE A CB  1 
ATOM   1697 C  CG  . PHE A 1 222 ? -1.264  34.963 43.654 1.00 21.39 ? 221 PHE A CG  1 
ATOM   1698 C  CD1 . PHE A 1 222 ? -0.781  35.903 44.543 1.00 25.20 ? 221 PHE A CD1 1 
ATOM   1699 C  CD2 . PHE A 1 222 ? -1.387  33.652 44.063 1.00 21.87 ? 221 PHE A CD2 1 
ATOM   1700 C  CE1 . PHE A 1 222 ? -0.446  35.540 45.824 1.00 24.99 ? 221 PHE A CE1 1 
ATOM   1701 C  CE2 . PHE A 1 222 ? -1.052  33.283 45.340 1.00 22.76 ? 221 PHE A CE2 1 
ATOM   1702 C  CZ  . PHE A 1 222 ? -0.582  34.229 46.224 1.00 23.31 ? 221 PHE A CZ  1 
ATOM   1703 N  N   . ASP A 1 223 ? -2.894  36.907 39.822 1.00 19.59 ? 222 ASP A N   1 
ATOM   1704 C  CA  . ASP A 1 223 ? -2.605  37.743 38.654 1.00 22.01 ? 222 ASP A CA  1 
ATOM   1705 C  C   . ASP A 1 223 ? -3.943  38.123 38.041 1.00 24.02 ? 222 ASP A C   1 
ATOM   1706 O  O   . ASP A 1 223 ? -4.581  37.301 37.385 1.00 23.93 ? 222 ASP A O   1 
ATOM   1707 C  CB  . ASP A 1 223 ? -1.718  36.991 37.663 1.00 22.24 ? 222 ASP A CB  1 
ATOM   1708 C  CG  . ASP A 1 223 ? -1.364  37.811 36.426 1.00 23.05 ? 222 ASP A CG  1 
ATOM   1709 O  OD1 . ASP A 1 223 ? -1.914  38.918 36.225 1.00 22.58 ? 222 ASP A OD1 1 
ATOM   1710 O  OD2 . ASP A 1 223 ? -0.525  37.328 35.638 1.00 24.79 ? 222 ASP A OD2 1 
ATOM   1711 N  N   . LEU A 1 224 ? -4.365  39.374 38.247 1.00 24.87 ? 223 LEU A N   1 
ATOM   1712 C  CA  . LEU A 1 224 ? -5.650  39.803 37.715 1.00 26.49 ? 223 LEU A CA  1 
ATOM   1713 C  C   . LEU A 1 224 ? -5.651  39.913 36.192 1.00 26.72 ? 223 LEU A C   1 
ATOM   1714 O  O   . LEU A 1 224 ? -6.725  39.989 35.588 1.00 26.94 ? 223 LEU A O   1 
ATOM   1715 C  CB  . LEU A 1 224 ? -6.055  41.144 38.326 1.00 28.64 ? 223 LEU A CB  1 
ATOM   1716 C  CG  . LEU A 1 224 ? -5.516  42.432 37.709 1.00 29.41 ? 223 LEU A CG  1 
ATOM   1717 C  CD1 . LEU A 1 224 ? -6.564  43.535 37.871 1.00 40.55 ? 223 LEU A CD1 1 
ATOM   1718 C  CD2 . LEU A 1 224 ? -4.228  42.838 38.370 1.00 31.34 ? 223 LEU A CD2 1 
ATOM   1719 N  N   . ARG A 1 225 ? -4.477  39.943 35.560 1.00 22.67 ? 224 ARG A N   1 
ATOM   1720 C  CA  . ARG A 1 225 ? -4.406  40.050 34.106 1.00 23.19 ? 224 ARG A CA  1 
ATOM   1721 C  C   . ARG A 1 225 ? -4.505  38.680 33.440 1.00 26.35 ? 224 ARG A C   1 
ATOM   1722 O  O   . ARG A 1 225 ? -5.437  38.429 32.664 1.00 27.43 ? 224 ARG A O   1 
ATOM   1723 C  CB  . ARG A 1 225 ? -3.121  40.773 33.693 1.00 23.30 ? 224 ARG A CB  1 
ATOM   1724 C  CG  . ARG A 1 225 ? -3.178  42.273 33.937 1.00 25.31 ? 224 ARG A CG  1 
ATOM   1725 C  CD  . ARG A 1 225 ? -1.876  42.968 33.573 1.00 28.65 ? 224 ARG A CD  1 
ATOM   1726 N  NE  . ARG A 1 225 ? -2.108  44.337 33.128 1.00 29.93 ? 224 ARG A NE  1 
ATOM   1727 C  CZ  . ARG A 1 225 ? -2.184  45.388 33.934 1.00 32.25 ? 224 ARG A CZ  1 
ATOM   1728 N  NH1 . ARG A 1 225 ? -2.029  45.271 35.244 1.00 29.94 ? 224 ARG A NH1 1 
ATOM   1729 N  NH2 . ARG A 1 225 ? -2.424  46.588 33.413 1.00 32.16 ? 224 ARG A NH2 1 
ATOM   1730 N  N   . THR A 1 226 ? -3.555  37.784 33.721 1.00 24.46 ? 225 THR A N   1 
ATOM   1731 C  CA  . THR A 1 226 ? -3.563  36.430 33.158 1.00 24.69 ? 225 THR A CA  1 
ATOM   1732 C  C   . THR A 1 226 ? -3.441  35.431 34.296 1.00 22.12 ? 225 THR A C   1 
ATOM   1733 O  O   . THR A 1 226 ? -2.360  34.887 34.552 1.00 20.78 ? 225 THR A O   1 
ATOM   1734 C  CB  . THR A 1 226 ? -2.458  36.238 32.121 1.00 23.35 ? 225 THR A CB  1 
ATOM   1735 O  OG1 . THR A 1 226 ? -1.179  36.574 32.673 1.00 21.82 ? 225 THR A OG1 1 
ATOM   1736 C  CG2 . THR A 1 226 ? -2.738  37.109 30.907 1.00 26.95 ? 225 THR A CG2 1 
ATOM   1737 N  N   . PRO A 1 227 ? -4.548  35.142 34.984 1.00 22.39 ? 226 PRO A N   1 
ATOM   1738 C  CA  . PRO A 1 227 ? -4.465  34.285 36.179 1.00 24.36 ? 226 PRO A CA  1 
ATOM   1739 C  C   . PRO A 1 227 ? -3.989  32.871 35.920 1.00 23.92 ? 226 PRO A C   1 
ATOM   1740 O  O   . PRO A 1 227 ? -3.548  32.215 36.867 1.00 26.49 ? 226 PRO A O   1 
ATOM   1741 C  CB  . PRO A 1 227 ? -5.910  34.286 36.714 1.00 27.21 ? 226 PRO A CB  1 
ATOM   1742 C  CG  . PRO A 1 227 ? -6.762  34.716 35.550 1.00 30.70 ? 226 PRO A CG  1 
ATOM   1743 C  CD  . PRO A 1 227 ? -5.903  35.691 34.789 1.00 27.49 ? 226 PRO A CD  1 
ATOM   1744 N  N   . THR A 1 228 ? -4.077  32.355 34.688 1.00 23.83 ? 227 THR A N   1 
ATOM   1745 C  CA  . THR A 1 228 ? -3.680  30.980 34.435 1.00 23.93 ? 227 THR A CA  1 
ATOM   1746 C  C   . THR A 1 228 ? -2.456  30.846 33.543 1.00 26.28 ? 227 THR A C   1 
ATOM   1747 O  O   . THR A 1 228 ? -1.989  29.719 33.330 1.00 30.41 ? 227 THR A O   1 
ATOM   1748 C  CB  . THR A 1 228 ? -4.831  30.193 33.792 1.00 29.96 ? 227 THR A CB  1 
ATOM   1749 O  OG1 . THR A 1 228 ? -5.035  30.659 32.457 1.00 27.68 ? 227 THR A OG1 1 
ATOM   1750 C  CG2 . THR A 1 228 ? -6.106  30.371 34.584 1.00 30.08 ? 227 THR A CG2 1 
ATOM   1751 N  N   . ILE A 1 229 ? -1.933  31.944 33.015 1.00 24.84 ? 228 ILE A N   1 
ATOM   1752 C  CA  . ILE A 1 229 ? -0.805  31.911 32.096 1.00 22.53 ? 228 ILE A CA  1 
ATOM   1753 C  C   . ILE A 1 229 ? 0.451   32.343 32.837 1.00 21.53 ? 228 ILE A C   1 
ATOM   1754 O  O   . ILE A 1 229 ? 0.461   33.380 33.517 1.00 22.27 ? 228 ILE A O   1 
ATOM   1755 C  CB  . ILE A 1 229 ? -1.046  32.810 30.877 1.00 25.93 ? 228 ILE A CB  1 
ATOM   1756 C  CG1 . ILE A 1 229 ? -2.243  32.291 30.076 1.00 25.10 ? 228 ILE A CG1 1 
ATOM   1757 C  CG2 . ILE A 1 229 ? 0.221   32.883 30.038 1.00 24.32 ? 228 ILE A CG2 1 
ATOM   1758 C  CD1 . ILE A 1 229 ? -2.726  33.261 29.037 1.00 34.77 ? 228 ILE A CD1 1 
ATOM   1759 N  N   . PHE A 1 230 ? 1.516   31.561 32.688 1.00 21.56 ? 229 PHE A N   1 
ATOM   1760 C  CA  . PHE A 1 230 ? 2.810   31.907 33.257 1.00 20.97 ? 229 PHE A CA  1 
ATOM   1761 C  C   . PHE A 1 230 ? 3.489   32.933 32.360 1.00 21.58 ? 229 PHE A C   1 
ATOM   1762 O  O   . PHE A 1 230 ? 4.016   32.596 31.292 1.00 22.51 ? 229 PHE A O   1 
ATOM   1763 C  CB  . PHE A 1 230 ? 3.680   30.671 33.423 1.00 21.86 ? 229 PHE A CB  1 
ATOM   1764 C  CG  . PHE A 1 230 ? 4.856   30.912 34.288 1.00 22.41 ? 229 PHE A CG  1 
ATOM   1765 C  CD1 . PHE A 1 230 ? 5.986   31.536 33.784 1.00 21.56 ? 229 PHE A CD1 1 
ATOM   1766 C  CD2 . PHE A 1 230 ? 4.821   30.578 35.629 1.00 20.44 ? 229 PHE A CD2 1 
ATOM   1767 C  CE1 . PHE A 1 230 ? 7.065   31.791 34.592 1.00 21.09 ? 229 PHE A CE1 1 
ATOM   1768 C  CE2 . PHE A 1 230 ? 5.893   30.836 36.446 1.00 22.82 ? 229 PHE A CE2 1 
ATOM   1769 C  CZ  . PHE A 1 230 ? 7.021   31.440 35.927 1.00 22.50 ? 229 PHE A CZ  1 
ATOM   1770 N  N   . ASP A 1 231 ? 3.491   34.193 32.794 1.00 22.61 ? 230 ASP A N   1 
ATOM   1771 C  CA  . ASP A 1 231 ? 4.015   35.305 32.009 1.00 22.13 ? 230 ASP A CA  1 
ATOM   1772 C  C   . ASP A 1 231 ? 4.453   36.402 32.978 1.00 21.25 ? 230 ASP A C   1 
ATOM   1773 O  O   . ASP A 1 231 ? 4.434   36.221 34.197 1.00 22.08 ? 230 ASP A O   1 
ATOM   1774 C  CB  . ASP A 1 231 ? 2.969   35.798 30.999 1.00 23.74 ? 230 ASP A CB  1 
ATOM   1775 C  CG  . ASP A 1 231 ? 1.639   36.157 31.653 1.00 22.78 ? 230 ASP A CG  1 
ATOM   1776 O  OD1 . ASP A 1 231 ? 1.569   36.236 32.896 1.00 21.56 ? 230 ASP A OD1 1 
ATOM   1777 O  OD2 . ASP A 1 231 ? 0.647   36.358 30.903 1.00 24.80 ? 230 ASP A OD2 1 
ATOM   1778 N  N   . ASN A 1 232 ? 4.851   37.552 32.439 1.00 24.04 ? 231 ASN A N   1 
ATOM   1779 C  CA  . ASN A 1 232 ? 5.400   38.611 33.283 1.00 23.73 ? 231 ASN A CA  1 
ATOM   1780 C  C   . ASN A 1 232 ? 4.350   39.611 33.754 1.00 21.69 ? 231 ASN A C   1 
ATOM   1781 O  O   . ASN A 1 232 ? 4.718   40.640 34.326 1.00 23.97 ? 231 ASN A O   1 
ATOM   1782 C  CB  . ASN A 1 232 ? 6.512   39.364 32.546 1.00 23.05 ? 231 ASN A CB  1 
ATOM   1783 C  CG  . ASN A 1 232 ? 5.979   40.331 31.508 1.00 26.21 ? 231 ASN A CG  1 
ATOM   1784 O  OD1 . ASN A 1 232 ? 4.846   40.196 31.033 1.00 26.53 ? 231 ASN A OD1 1 
ATOM   1785 N  ND2 . ASN A 1 232 ? 6.792   41.318 31.148 1.00 27.35 ? 231 ASN A ND2 1 
ATOM   1786 N  N   . LYS A 1 233 ? 3.060   39.347 33.523 1.00 23.10 ? 232 LYS A N   1 
ATOM   1787 C  CA  . LYS A 1 233 ? 2.037   40.313 33.911 1.00 22.15 ? 232 LYS A CA  1 
ATOM   1788 C  C   . LYS A 1 233 ? 2.015   40.553 35.414 1.00 21.30 ? 232 LYS A C   1 
ATOM   1789 O  O   . LYS A 1 233 ? 1.587   41.625 35.856 1.00 22.36 ? 232 LYS A O   1 
ATOM   1790 C  CB  . LYS A 1 233 ? 0.663   39.841 33.432 1.00 21.82 ? 232 LYS A CB  1 
ATOM   1791 C  CG  . LYS A 1 233 ? 0.554   39.690 31.922 1.00 26.85 ? 232 LYS A CG  1 
ATOM   1792 C  CD  . LYS A 1 233 ? 0.710   41.022 31.189 1.00 34.27 ? 232 LYS A CD  1 
ATOM   1793 C  CE  . LYS A 1 233 ? 0.714   40.818 29.674 1.00 40.45 ? 232 LYS A CE  1 
ATOM   1794 N  NZ  . LYS A 1 233 ? 2.020   40.272 29.207 1.00 55.45 ? 232 LYS A NZ  1 
ATOM   1795 N  N   . TYR A 1 234 ? 2.474   39.580 36.203 1.00 20.31 ? 233 TYR A N   1 
ATOM   1796 C  CA  . TYR A 1 234 ? 2.632   39.779 37.642 1.00 21.93 ? 233 TYR A CA  1 
ATOM   1797 C  C   . TYR A 1 234 ? 3.317   41.104 37.960 1.00 22.68 ? 233 TYR A C   1 
ATOM   1798 O  O   . TYR A 1 234 ? 2.881   41.838 38.852 1.00 22.54 ? 233 TYR A O   1 
ATOM   1799 C  CB  . TYR A 1 234 ? 3.418   38.602 38.228 1.00 21.83 ? 233 TYR A CB  1 
ATOM   1800 C  CG  . TYR A 1 234 ? 3.844   38.780 39.662 1.00 22.43 ? 233 TYR A CG  1 
ATOM   1801 C  CD1 . TYR A 1 234 ? 2.944   38.592 40.704 1.00 21.97 ? 233 TYR A CD1 1 
ATOM   1802 C  CD2 . TYR A 1 234 ? 5.147   39.122 39.979 1.00 22.69 ? 233 TYR A CD2 1 
ATOM   1803 C  CE1 . TYR A 1 234 ? 3.338   38.754 42.014 1.00 21.29 ? 233 TYR A CE1 1 
ATOM   1804 C  CE2 . TYR A 1 234 ? 5.549   39.287 41.283 1.00 24.50 ? 233 TYR A CE2 1 
ATOM   1805 C  CZ  . TYR A 1 234 ? 4.642   39.101 42.297 1.00 22.37 ? 233 TYR A CZ  1 
ATOM   1806 O  OH  . TYR A 1 234 ? 5.065   39.265 43.592 1.00 26.21 ? 233 TYR A OH  1 
ATOM   1807 N  N   . TYR A 1 235 ? 4.384   41.436 37.228 1.00 21.91 ? 234 TYR A N   1 
ATOM   1808 C  CA  . TYR A 1 235 ? 5.164   42.633 37.529 1.00 19.79 ? 234 TYR A CA  1 
ATOM   1809 C  C   . TYR A 1 235 ? 4.480   43.895 37.040 1.00 21.92 ? 234 TYR A C   1 
ATOM   1810 O  O   . TYR A 1 235 ? 4.606   44.951 37.672 1.00 23.52 ? 234 TYR A O   1 
ATOM   1811 C  CB  . TYR A 1 235 ? 6.554   42.493 36.913 1.00 19.10 ? 234 TYR A CB  1 
ATOM   1812 C  CG  . TYR A 1 235 ? 7.236   41.257 37.434 1.00 20.76 ? 234 TYR A CG  1 
ATOM   1813 C  CD1 . TYR A 1 235 ? 7.848   41.265 38.677 1.00 20.81 ? 234 TYR A CD1 1 
ATOM   1814 C  CD2 . TYR A 1 235 ? 7.235   40.074 36.707 1.00 18.36 ? 234 TYR A CD2 1 
ATOM   1815 C  CE1 . TYR A 1 235 ? 8.457   40.134 39.186 1.00 19.84 ? 234 TYR A CE1 1 
ATOM   1816 C  CE2 . TYR A 1 235 ? 7.849   38.934 37.211 1.00 18.64 ? 234 TYR A CE2 1 
ATOM   1817 C  CZ  . TYR A 1 235 ? 8.457   38.972 38.439 1.00 18.06 ? 234 TYR A CZ  1 
ATOM   1818 O  OH  . TYR A 1 235 ? 9.065   37.847 38.951 1.00 21.43 ? 234 TYR A OH  1 
ATOM   1819 N  N   . VAL A 1 236 ? 3.762   43.802 35.925 1.00 22.23 ? 235 VAL A N   1 
ATOM   1820 C  CA  . VAL A 1 236 ? 2.952   44.919 35.462 1.00 23.85 ? 235 VAL A CA  1 
ATOM   1821 C  C   . VAL A 1 236 ? 1.942   45.303 36.531 1.00 23.98 ? 235 VAL A C   1 
ATOM   1822 O  O   . VAL A 1 236 ? 1.751   46.488 36.825 1.00 25.39 ? 235 VAL A O   1 
ATOM   1823 C  CB  . VAL A 1 236 ? 2.284   44.555 34.125 1.00 26.14 ? 235 VAL A CB  1 
ATOM   1824 C  CG1 . VAL A 1 236 ? 1.467   45.707 33.610 1.00 30.29 ? 235 VAL A CG1 1 
ATOM   1825 C  CG2 . VAL A 1 236 ? 3.359   44.137 33.116 1.00 27.59 ? 235 VAL A CG2 1 
ATOM   1826 N  N   . ASN A 1 237 ? 1.316   44.305 37.160 1.00 23.57 ? 236 ASN A N   1 
ATOM   1827 C  CA  . ASN A 1 237 ? 0.376   44.581 38.240 1.00 23.66 ? 236 ASN A CA  1 
ATOM   1828 C  C   . ASN A 1 237 ? 1.050   45.359 39.364 1.00 23.09 ? 236 ASN A C   1 
ATOM   1829 O  O   . ASN A 1 237 ? 0.468   46.301 39.916 1.00 21.56 ? 236 ASN A O   1 
ATOM   1830 C  CB  . ASN A 1 237 ? -0.204  43.285 38.804 1.00 23.75 ? 236 ASN A CB  1 
ATOM   1831 C  CG  . ASN A 1 237 ? -0.932  42.454 37.766 1.00 25.72 ? 236 ASN A CG  1 
ATOM   1832 O  OD1 . ASN A 1 237 ? -1.412  42.966 36.753 1.00 25.60 ? 236 ASN A OD1 1 
ATOM   1833 N  ND2 . ASN A 1 237 ? -1.027  41.155 38.026 1.00 23.52 ? 236 ASN A ND2 1 
ATOM   1834 N  N   . LEU A 1 238 ? 2.273   44.965 39.734 1.00 21.62 ? 237 LEU A N   1 
ATOM   1835 C  CA  . LEU A 1 238 ? 2.942   45.628 40.849 1.00 23.09 ? 237 LEU A CA  1 
ATOM   1836 C  C   . LEU A 1 238 ? 3.160   47.101 40.551 1.00 23.59 ? 237 LEU A C   1 
ATOM   1837 O  O   . LEU A 1 238 ? 2.977   47.955 41.425 1.00 23.40 ? 237 LEU A O   1 
ATOM   1838 C  CB  . LEU A 1 238 ? 4.283   44.956 41.140 1.00 22.82 ? 237 LEU A CB  1 
ATOM   1839 C  CG  . LEU A 1 238 ? 4.291   43.470 41.479 1.00 22.17 ? 237 LEU A CG  1 
ATOM   1840 C  CD1 . LEU A 1 238 ? 5.681   43.105 42.024 1.00 23.74 ? 237 LEU A CD1 1 
ATOM   1841 C  CD2 . LEU A 1 238 ? 3.216   43.097 42.464 1.00 24.69 ? 237 LEU A CD2 1 
ATOM   1842 N  N   . GLU A 1 239 ? 3.544   47.419 39.316 1.00 25.11 ? 238 GLU A N   1 
ATOM   1843 C  CA  . GLU A 1 239 ? 3.788   48.808 38.953 1.00 25.71 ? 238 GLU A CA  1 
ATOM   1844 C  C   . GLU A 1 239 ? 2.526   49.654 39.032 1.00 25.18 ? 238 GLU A C   1 
ATOM   1845 O  O   . GLU A 1 239 ? 2.621   50.878 39.162 1.00 29.51 ? 238 GLU A O   1 
ATOM   1846 C  CB  . GLU A 1 239 ? 4.365   48.879 37.536 1.00 30.38 ? 238 GLU A CB  1 
ATOM   1847 C  CG  . GLU A 1 239 ? 5.745   48.270 37.376 1.00 32.07 ? 238 GLU A CG  1 
ATOM   1848 C  CD  . GLU A 1 239 ? 6.273   48.438 35.961 1.00 37.33 ? 238 GLU A CD  1 
ATOM   1849 O  OE1 . GLU A 1 239 ? 5.465   48.350 35.012 1.00 38.98 ? 238 GLU A OE1 1 
ATOM   1850 O  OE2 . GLU A 1 239 ? 7.483   48.674 35.800 1.00 39.09 ? 238 GLU A OE2 1 
ATOM   1851 N  N   . GLU A 1 240 ? 1.350   49.036 38.947 1.00 23.80 ? 239 GLU A N   1 
ATOM   1852 C  CA  . GLU A 1 240 ? 0.082   49.740 39.058 1.00 27.16 ? 239 GLU A CA  1 
ATOM   1853 C  C   . GLU A 1 240 ? -0.518  49.648 40.452 1.00 24.80 ? 239 GLU A C   1 
ATOM   1854 O  O   . GLU A 1 240 ? -1.692  50.003 40.639 1.00 21.68 ? 239 GLU A O   1 
ATOM   1855 C  CB  . GLU A 1 240 ? -0.915  49.188 38.043 1.00 29.58 ? 239 GLU A CB  1 
ATOM   1856 C  CG  . GLU A 1 240 ? -0.424  49.240 36.622 1.00 29.85 ? 239 GLU A CG  1 
ATOM   1857 C  CD  . GLU A 1 240 ? -1.466  48.737 35.659 1.00 38.77 ? 239 GLU A CD  1 
ATOM   1858 O  OE1 . GLU A 1 240 ? -2.440  48.114 36.128 1.00 35.50 ? 239 GLU A OE1 1 
ATOM   1859 O  OE2 . GLU A 1 240 ? -1.319  48.971 34.440 1.00 47.98 ? 239 GLU A OE2 1 
ATOM   1860 N  N   . GLN A 1 241 ? 0.253   49.173 41.432 1.00 23.67 ? 240 GLN A N   1 
ATOM   1861 C  CA  . GLN A 1 241 ? -0.210  49.023 42.811 1.00 24.05 ? 240 GLN A CA  1 
ATOM   1862 C  C   . GLN A 1 241 ? -1.311  47.967 42.912 1.00 24.56 ? 240 GLN A C   1 
ATOM   1863 O  O   . GLN A 1 241 ? -2.229  48.089 43.725 1.00 22.34 ? 240 GLN A O   1 
ATOM   1864 C  CB  . GLN A 1 241 ? -0.689  50.361 43.388 1.00 24.41 ? 240 GLN A CB  1 
ATOM   1865 C  CG  . GLN A 1 241 ? 0.314   51.503 43.278 1.00 27.11 ? 240 GLN A CG  1 
ATOM   1866 C  CD  . GLN A 1 241 ? 1.626   51.211 43.979 1.00 35.25 ? 240 GLN A CD  1 
ATOM   1867 O  OE1 . GLN A 1 241 ? 2.702   51.467 43.434 1.00 33.23 ? 240 GLN A OE1 1 
ATOM   1868 N  NE2 . GLN A 1 241 ? 1.548   50.678 45.195 1.00 35.29 ? 240 GLN A NE2 1 
ATOM   1869 N  N   . LYS A 1 242 ? -1.211  46.917 42.091 1.00 21.55 ? 241 LYS A N   1 
ATOM   1870 C  CA  . LYS A 1 242 ? -2.206  45.853 42.048 1.00 20.39 ? 241 LYS A CA  1 
ATOM   1871 C  C   . LYS A 1 242 ? -1.611  44.491 42.376 1.00 25.17 ? 241 LYS A C   1 
ATOM   1872 O  O   . LYS A 1 242 ? -2.155  43.458 41.966 1.00 24.68 ? 241 LYS A O   1 
ATOM   1873 C  CB  . LYS A 1 242 ? -2.894  45.820 40.682 1.00 25.14 ? 241 LYS A CB  1 
ATOM   1874 C  CG  . LYS A 1 242 ? -3.626  47.107 40.376 1.00 25.46 ? 241 LYS A CG  1 
ATOM   1875 C  CD  . LYS A 1 242 ? -4.202  47.136 38.982 1.00 30.16 ? 241 LYS A CD  1 
ATOM   1876 C  CE  . LYS A 1 242 ? -4.857  48.478 38.710 1.00 34.23 ? 241 LYS A CE  1 
ATOM   1877 N  NZ  . LYS A 1 242 ? -5.672  48.417 37.472 1.00 51.10 ? 241 LYS A NZ  1 
ATOM   1878 N  N   . GLY A 1 243 ? -0.495  44.461 43.098 1.00 22.41 ? 242 GLY A N   1 
ATOM   1879 C  CA  . GLY A 1 243 ? -0.088  43.221 43.736 1.00 22.59 ? 242 GLY A CA  1 
ATOM   1880 C  C   . GLY A 1 243 ? -1.146  42.777 44.729 1.00 25.47 ? 242 GLY A C   1 
ATOM   1881 O  O   . GLY A 1 243 ? -1.743  43.593 45.433 1.00 23.42 ? 242 GLY A O   1 
ATOM   1882 N  N   . LEU A 1 244 ? -1.392  41.471 44.772 1.00 22.23 ? 243 LEU A N   1 
ATOM   1883 C  CA  . LEU A 1 244 ? -2.510  40.974 45.562 1.00 23.07 ? 243 LEU A CA  1 
ATOM   1884 C  C   . LEU A 1 244 ? -2.172  40.921 47.048 1.00 21.21 ? 243 LEU A C   1 
ATOM   1885 O  O   . LEU A 1 244 ? -2.904  41.471 47.878 1.00 22.43 ? 243 LEU A O   1 
ATOM   1886 C  CB  . LEU A 1 244 ? -2.944  39.596 45.066 1.00 21.16 ? 243 LEU A CB  1 
ATOM   1887 C  CG  . LEU A 1 244 ? -4.083  38.959 45.865 1.00 24.34 ? 243 LEU A CG  1 
ATOM   1888 C  CD1 . LEU A 1 244 ? -5.359  39.763 45.707 1.00 25.13 ? 243 LEU A CD1 1 
ATOM   1889 C  CD2 . LEU A 1 244 ? -4.290  37.513 45.439 1.00 23.81 ? 243 LEU A CD2 1 
ATOM   1890 N  N   . ILE A 1 245 ? -1.091  40.239 47.418 1.00 22.57 ? 244 ILE A N   1 
ATOM   1891 C  CA  . ILE A 1 245 ? -0.740  40.130 48.821 1.00 21.73 ? 244 ILE A CA  1 
ATOM   1892 C  C   . ILE A 1 245 ? 0.335   41.155 49.150 1.00 19.90 ? 244 ILE A C   1 
ATOM   1893 O  O   . ILE A 1 245 ? 1.019   41.699 48.274 1.00 20.27 ? 244 ILE A O   1 
ATOM   1894 C  CB  . ILE A 1 245 ? -0.298  38.706 49.237 1.00 22.09 ? 244 ILE A CB  1 
ATOM   1895 C  CG1 . ILE A 1 245 ? 0.895   38.208 48.432 1.00 22.79 ? 244 ILE A CG1 1 
ATOM   1896 C  CG2 . ILE A 1 245 ? -1.481  37.740 49.108 1.00 24.08 ? 244 ILE A CG2 1 
ATOM   1897 C  CD1 . ILE A 1 245 ? 1.438   36.881 48.964 1.00 23.13 ? 244 ILE A CD1 1 
ATOM   1898 N  N   . GLN A 1 246 ? 0.456   41.456 50.443 1.00 20.07 ? 245 GLN A N   1 
ATOM   1899 C  CA  . GLN A 1 246 ? 1.389   42.492 50.878 1.00 24.46 ? 245 GLN A CA  1 
ATOM   1900 C  C   . GLN A 1 246 ? 2.794   42.201 50.385 1.00 20.74 ? 245 GLN A C   1 
ATOM   1901 O  O   . GLN A 1 246 ? 3.490   43.100 49.898 1.00 22.65 ? 245 GLN A O   1 
ATOM   1902 C  CB  . GLN A 1 246 ? 1.353   42.608 52.400 1.00 24.94 ? 245 GLN A CB  1 
ATOM   1903 C  CG  . GLN A 1 246 ? 2.479   43.427 52.986 1.00 25.33 ? 245 GLN A CG  1 
ATOM   1904 C  CD  . GLN A 1 246 ? 2.365   43.566 54.495 1.00 31.19 ? 245 GLN A CD  1 
ATOM   1905 O  OE1 . GLN A 1 246 ? 1.433   43.040 55.112 1.00 27.72 ? 245 GLN A OE1 1 
ATOM   1906 N  NE2 . GLN A 1 246 ? 3.309   44.277 55.098 1.00 29.69 ? 245 GLN A NE2 1 
ATOM   1907 N  N   . SER A 1 247 ? 3.229   40.948 50.489 1.00 22.34 ? 246 SER A N   1 
ATOM   1908 C  CA  . SER A 1 247 ? 4.591   40.609 50.087 1.00 20.38 ? 246 SER A CA  1 
ATOM   1909 C  C   . SER A 1 247 ? 4.822   40.765 48.592 1.00 21.31 ? 246 SER A C   1 
ATOM   1910 O  O   . SER A 1 247 ? 5.975   40.919 48.180 1.00 21.89 ? 246 SER A O   1 
ATOM   1911 C  CB  . SER A 1 247 ? 4.906   39.180 50.530 1.00 24.52 ? 246 SER A CB  1 
ATOM   1912 O  OG  . SER A 1 247 ? 3.890   38.296 50.102 1.00 25.61 ? 246 SER A OG  1 
ATOM   1913 N  N   . ASP A 1 248 ? 3.769   40.704 47.771 1.00 18.86 ? 247 ASP A N   1 
ATOM   1914 C  CA  . ASP A 1 248 ? 3.914   41.055 46.356 1.00 22.12 ? 247 ASP A CA  1 
ATOM   1915 C  C   . ASP A 1 248 ? 4.217   42.541 46.203 1.00 20.37 ? 247 ASP A C   1 
ATOM   1916 O  O   . ASP A 1 248 ? 5.200   42.931 45.563 1.00 21.81 ? 247 ASP A O   1 
ATOM   1917 C  CB  . ASP A 1 248 ? 2.634   40.731 45.569 1.00 22.06 ? 247 ASP A CB  1 
ATOM   1918 C  CG  . ASP A 1 248 ? 2.363   39.241 45.429 1.00 25.72 ? 247 ASP A CG  1 
ATOM   1919 O  OD1 . ASP A 1 248 ? 3.314   38.430 45.412 1.00 27.37 ? 247 ASP A OD1 1 
ATOM   1920 O  OD2 . ASP A 1 248 ? 1.164   38.891 45.295 1.00 22.73 ? 247 ASP A OD2 1 
ATOM   1921 N  N   . GLN A 1 249 ? 3.352   43.392 46.774 1.00 20.20 ? 248 GLN A N   1 
ATOM   1922 C  CA  . GLN A 1 249 ? 3.481   44.825 46.554 1.00 19.28 ? 248 GLN A CA  1 
ATOM   1923 C  C   . GLN A 1 249 ? 4.719   45.394 47.232 1.00 22.31 ? 248 GLN A C   1 
ATOM   1924 O  O   . GLN A 1 249 ? 5.254   46.412 46.774 1.00 21.76 ? 248 GLN A O   1 
ATOM   1925 C  CB  . GLN A 1 249 ? 2.224   45.549 47.041 1.00 20.52 ? 248 GLN A CB  1 
ATOM   1926 C  CG  . GLN A 1 249 ? 2.116   46.969 46.503 1.00 20.56 ? 248 GLN A CG  1 
ATOM   1927 C  CD  . GLN A 1 249 ? 2.138   47.028 44.985 1.00 24.43 ? 248 GLN A CD  1 
ATOM   1928 O  OE1 . GLN A 1 249 ? 1.423   46.289 44.309 1.00 27.13 ? 248 GLN A OE1 1 
ATOM   1929 N  NE2 . GLN A 1 249 ? 2.980   47.897 44.438 1.00 22.36 ? 248 GLN A NE2 1 
ATOM   1930 N  N   . GLU A 1 250 ? 5.189   44.757 48.308 1.00 20.72 ? 249 GLU A N   1 
ATOM   1931 C  CA  . GLU A 1 250 ? 6.399   45.232 48.985 1.00 25.32 ? 249 GLU A CA  1 
ATOM   1932 C  C   . GLU A 1 250 ? 7.587   45.321 48.032 1.00 23.55 ? 249 GLU A C   1 
ATOM   1933 O  O   . GLU A 1 250 ? 8.455   46.189 48.197 1.00 21.09 ? 249 GLU A O   1 
ATOM   1934 C  CB  . GLU A 1 250 ? 6.758   44.310 50.154 1.00 23.83 ? 249 GLU A CB  1 
ATOM   1935 C  CG  . GLU A 1 250 ? 5.782   44.329 51.329 1.00 31.41 ? 249 GLU A CG  1 
ATOM   1936 C  CD  . GLU A 1 250 ? 6.132   45.353 52.396 1.00 36.67 ? 249 GLU A CD  1 
ATOM   1937 O  OE1 . GLU A 1 250 ? 7.138   46.084 52.247 1.00 39.04 ? 249 GLU A OE1 1 
ATOM   1938 O  OE2 . GLU A 1 250 ? 5.399   45.425 53.406 1.00 33.05 ? 249 GLU A OE2 1 
ATOM   1939 N  N   . LEU A 1 251 ? 7.652   44.429 47.044 1.00 21.10 ? 250 LEU A N   1 
ATOM   1940 C  CA  . LEU A 1 251 ? 8.768   44.430 46.102 1.00 21.01 ? 250 LEU A CA  1 
ATOM   1941 C  C   . LEU A 1 251 ? 8.883   45.746 45.344 1.00 22.45 ? 250 LEU A C   1 
ATOM   1942 O  O   . LEU A 1 251 ? 9.959   46.088 44.842 1.00 25.05 ? 250 LEU A O   1 
ATOM   1943 C  CB  . LEU A 1 251 ? 8.598   43.291 45.098 1.00 20.67 ? 250 LEU A CB  1 
ATOM   1944 C  CG  . LEU A 1 251 ? 8.487   41.883 45.666 1.00 22.94 ? 250 LEU A CG  1 
ATOM   1945 C  CD1 . LEU A 1 251 ? 8.265   40.901 44.531 1.00 23.93 ? 250 LEU A CD1 1 
ATOM   1946 C  CD2 . LEU A 1 251 ? 9.732   41.532 46.449 1.00 22.62 ? 250 LEU A CD2 1 
ATOM   1947 N  N   . PHE A 1 252 ? 7.779   46.472 45.207 1.00 21.90 ? 251 PHE A N   1 
ATOM   1948 C  CA  . PHE A 1 252 ? 7.762   47.712 44.457 1.00 20.77 ? 251 PHE A CA  1 
ATOM   1949 C  C   . PHE A 1 252 ? 7.586   48.938 45.333 1.00 25.18 ? 251 PHE A C   1 
ATOM   1950 O  O   . PHE A 1 252 ? 8.067   50.013 44.973 1.00 25.96 ? 251 PHE A O   1 
ATOM   1951 C  CB  . PHE A 1 252 ? 6.638   47.672 43.414 1.00 23.33 ? 251 PHE A CB  1 
ATOM   1952 C  CG  . PHE A 1 252 ? 6.734   48.747 42.384 1.00 27.74 ? 251 PHE A CG  1 
ATOM   1953 C  CD1 . PHE A 1 252 ? 7.725   48.713 41.419 1.00 26.11 ? 251 PHE A CD1 1 
ATOM   1954 C  CD2 . PHE A 1 252 ? 5.835   49.797 42.380 1.00 30.86 ? 251 PHE A CD2 1 
ATOM   1955 C  CE1 . PHE A 1 252 ? 7.819   49.710 40.471 1.00 29.33 ? 251 PHE A CE1 1 
ATOM   1956 C  CE2 . PHE A 1 252 ? 5.922   50.794 41.435 1.00 31.44 ? 251 PHE A CE2 1 
ATOM   1957 C  CZ  . PHE A 1 252 ? 6.913   50.751 40.480 1.00 28.94 ? 251 PHE A CZ  1 
ATOM   1958 N  N   . SER A 1 253 ? 6.938   48.800 46.488 1.00 23.20 ? 252 SER A N   1 
ATOM   1959 C  CA  . SER A 1 253 ? 6.495   49.951 47.250 1.00 24.11 ? 252 SER A CA  1 
ATOM   1960 C  C   . SER A 1 253 ? 7.172   50.095 48.603 1.00 25.10 ? 252 SER A C   1 
ATOM   1961 O  O   . SER A 1 253 ? 6.962   51.113 49.271 1.00 28.27 ? 252 SER A O   1 
ATOM   1962 C  CB  . SER A 1 253 ? 4.973   49.880 47.459 1.00 24.93 ? 252 SER A CB  1 
ATOM   1963 O  OG  . SER A 1 253 ? 4.314   49.841 46.210 1.00 24.65 ? 252 SER A OG  1 
ATOM   1964 N  N   . SER A 1 254 ? 7.973   49.121 49.022 1.00 22.81 ? 253 SER A N   1 
ATOM   1965 C  CA  . SER A 1 254 ? 8.613   49.194 50.322 1.00 22.87 ? 253 SER A CA  1 
ATOM   1966 C  C   . SER A 1 254 ? 9.650   50.314 50.344 1.00 24.93 ? 253 SER A C   1 
ATOM   1967 O  O   . SER A 1 254 ? 10.317  50.570 49.340 1.00 25.75 ? 253 SER A O   1 
ATOM   1968 C  CB  . SER A 1 254 ? 9.295   47.868 50.645 1.00 23.98 ? 253 SER A CB  1 
ATOM   1969 O  OG  . SER A 1 254 ? 10.141  47.999 51.780 1.00 24.97 ? 253 SER A OG  1 
ATOM   1970 N  N   . PRO A 1 255 ? 9.830   50.984 51.484 1.00 23.00 ? 254 PRO A N   1 
ATOM   1971 C  CA  . PRO A 1 255 ? 10.978  51.906 51.600 1.00 25.17 ? 254 PRO A CA  1 
ATOM   1972 C  C   . PRO A 1 255 ? 12.312  51.207 51.386 1.00 24.12 ? 254 PRO A C   1 
ATOM   1973 O  O   . PRO A 1 255 ? 13.322  51.878 51.145 1.00 24.24 ? 254 PRO A O   1 
ATOM   1974 C  CB  . PRO A 1 255 ? 10.857  52.456 53.028 1.00 26.92 ? 254 PRO A CB  1 
ATOM   1975 C  CG  . PRO A 1 255 ? 9.446   52.198 53.438 1.00 28.36 ? 254 PRO A CG  1 
ATOM   1976 C  CD  . PRO A 1 255 ? 9.006   50.957 52.708 1.00 27.85 ? 254 PRO A CD  1 
ATOM   1977 N  N   . ASN A 1 256 ? 12.337  49.881 51.474 1.00 23.73 ? 255 ASN A N   1 
ATOM   1978 C  CA  . ASN A 1 256 ? 13.541  49.072 51.325 1.00 22.19 ? 255 ASN A CA  1 
ATOM   1979 C  C   . ASN A 1 256 ? 13.686  48.514 49.915 1.00 25.53 ? 255 ASN A C   1 
ATOM   1980 O  O   . ASN A 1 256 ? 14.542  47.652 49.682 1.00 21.97 ? 255 ASN A O   1 
ATOM   1981 C  CB  . ASN A 1 256 ? 13.499  47.940 52.356 1.00 23.55 ? 255 ASN A CB  1 
ATOM   1982 C  CG  . ASN A 1 256 ? 14.764  47.111 52.384 1.00 26.73 ? 255 ASN A CG  1 
ATOM   1983 O  OD1 . ASN A 1 256 ? 14.720  45.895 52.199 1.00 27.82 ? 255 ASN A OD1 1 
ATOM   1984 N  ND2 . ASN A 1 256 ? 15.892  47.762 52.609 1.00 25.16 ? 255 ASN A ND2 1 
ATOM   1985 N  N   . ALA A 1 257 ? 12.894  49.002 48.961 1.00 23.14 ? 256 ALA A N   1 
ATOM   1986 C  CA  . ALA A 1 257 ? 12.834  48.413 47.627 1.00 21.28 ? 256 ALA A CA  1 
ATOM   1987 C  C   . ALA A 1 257 ? 13.757  49.082 46.620 1.00 21.25 ? 256 ALA A C   1 
ATOM   1988 O  O   . ALA A 1 257 ? 13.578  48.895 45.411 1.00 22.20 ? 256 ALA A O   1 
ATOM   1989 C  CB  . ALA A 1 257 ? 11.393  48.445 47.107 1.00 22.77 ? 256 ALA A CB  1 
ATOM   1990 N  N   . THR A 1 258 ? 14.760  49.838 47.069 1.00 23.05 ? 257 THR A N   1 
ATOM   1991 C  CA  . THR A 1 258 ? 15.667  50.458 46.106 1.00 27.17 ? 257 THR A CA  1 
ATOM   1992 C  C   . THR A 1 258 ? 16.295  49.413 45.188 1.00 23.43 ? 257 THR A C   1 
ATOM   1993 O  O   . THR A 1 258 ? 16.506  49.670 44.000 1.00 25.12 ? 257 THR A O   1 
ATOM   1994 C  CB  . THR A 1 258 ? 16.754  51.255 46.826 1.00 28.37 ? 257 THR A CB  1 
ATOM   1995 O  OG1 . THR A 1 258 ? 16.180  52.447 47.380 1.00 30.37 ? 257 THR A OG1 1 
ATOM   1996 C  CG2 . THR A 1 258 ? 17.861  51.628 45.850 1.00 32.96 ? 257 THR A CG2 1 
ATOM   1997 N  N   . ASP A 1 259 ? 16.590  48.223 45.713 1.00 25.60 ? 258 ASP A N   1 
ATOM   1998 C  CA  . ASP A 1 259 ? 17.212  47.200 44.882 1.00 27.19 ? 258 ASP A CA  1 
ATOM   1999 C  C   . ASP A 1 259 ? 16.208  46.297 44.183 1.00 28.84 ? 258 ASP A C   1 
ATOM   2000 O  O   . ASP A 1 259 ? 16.574  45.627 43.215 1.00 31.65 ? 258 ASP A O   1 
ATOM   2001 C  CB  . ASP A 1 259 ? 18.180  46.347 45.711 1.00 30.39 ? 258 ASP A CB  1 
ATOM   2002 C  CG  . ASP A 1 259 ? 17.514  45.661 46.881 1.00 38.05 ? 258 ASP A CG  1 
ATOM   2003 O  OD1 . ASP A 1 259 ? 16.402  46.075 47.266 1.00 36.38 ? 258 ASP A OD1 1 
ATOM   2004 O  OD2 . ASP A 1 259 ? 18.115  44.709 47.423 1.00 44.36 ? 258 ASP A OD2 1 
ATOM   2005 N  N   . THR A 1 260 ? 14.948  46.265 44.627 1.00 24.84 ? 259 THR A N   1 
ATOM   2006 C  CA  . THR A 1 260 ? 13.964  45.425 43.955 1.00 21.04 ? 259 THR A CA  1 
ATOM   2007 C  C   . THR A 1 260 ? 13.159  46.158 42.893 1.00 23.36 ? 259 THR A C   1 
ATOM   2008 O  O   . THR A 1 260 ? 12.750  45.533 41.911 1.00 22.89 ? 259 THR A O   1 
ATOM   2009 C  CB  . THR A 1 260 ? 13.000  44.801 44.979 1.00 24.73 ? 259 THR A CB  1 
ATOM   2010 O  OG1 . THR A 1 260 ? 12.455  45.812 45.835 1.00 27.78 ? 259 THR A OG1 1 
ATOM   2011 C  CG2 . THR A 1 260 ? 13.735  43.764 45.825 1.00 23.48 ? 259 THR A CG2 1 
ATOM   2012 N  N   . ILE A 1 261 ? 12.937  47.468 43.058 1.00 25.34 ? 260 ILE A N   1 
ATOM   2013 C  CA  . ILE A 1 261 ? 12.209  48.241 42.050 1.00 25.48 ? 260 ILE A CA  1 
ATOM   2014 C  C   . ILE A 1 261 ? 12.798  48.067 40.651 1.00 25.49 ? 260 ILE A C   1 
ATOM   2015 O  O   . ILE A 1 261 ? 12.037  47.819 39.710 1.00 24.80 ? 260 ILE A O   1 
ATOM   2016 C  CB  . ILE A 1 261 ? 12.122  49.712 42.474 1.00 27.46 ? 260 ILE A CB  1 
ATOM   2017 C  CG1 . ILE A 1 261 ? 11.075  49.879 43.575 1.00 24.53 ? 260 ILE A CG1 1 
ATOM   2018 C  CG2 . ILE A 1 261 ? 11.777  50.598 41.281 1.00 30.88 ? 260 ILE A CG2 1 
ATOM   2019 C  CD1 . ILE A 1 261 ? 11.237  51.129 44.418 1.00 26.35 ? 260 ILE A CD1 1 
ATOM   2020 N  N   . PRO A 1 262 ? 14.107  48.226 40.443 1.00 25.17 ? 261 PRO A N   1 
ATOM   2021 C  CA  . PRO A 1 262 ? 14.641  48.053 39.079 1.00 26.72 ? 261 PRO A CA  1 
ATOM   2022 C  C   . PRO A 1 262 ? 14.423  46.650 38.532 1.00 24.73 ? 261 PRO A C   1 
ATOM   2023 O  O   . PRO A 1 262 ? 14.231  46.488 37.323 1.00 24.21 ? 261 PRO A O   1 
ATOM   2024 C  CB  . PRO A 1 262 ? 16.134  48.388 39.226 1.00 24.22 ? 261 PRO A CB  1 
ATOM   2025 C  CG  . PRO A 1 262 ? 16.420  48.359 40.699 1.00 25.05 ? 261 PRO A CG  1 
ATOM   2026 C  CD  . PRO A 1 262 ? 15.130  48.646 41.414 1.00 25.96 ? 261 PRO A CD  1 
ATOM   2027 N  N   . LEU A 1 263 ? 14.434  45.630 39.390 1.00 22.71 ? 262 LEU A N   1 
ATOM   2028 C  CA  . LEU A 1 263 ? 14.164  44.274 38.927 1.00 22.76 ? 262 LEU A CA  1 
ATOM   2029 C  C   . LEU A 1 263 ? 12.707  44.123 38.504 1.00 23.75 ? 262 LEU A C   1 
ATOM   2030 O  O   . LEU A 1 263 ? 12.418  43.568 37.437 1.00 23.03 ? 262 LEU A O   1 
ATOM   2031 C  CB  . LEU A 1 263 ? 14.516  43.266 40.021 1.00 21.45 ? 262 LEU A CB  1 
ATOM   2032 C  CG  . LEU A 1 263 ? 16.005  43.110 40.325 1.00 24.20 ? 262 LEU A CG  1 
ATOM   2033 C  CD1 . LEU A 1 263 ? 16.236  42.361 41.615 1.00 25.97 ? 262 LEU A CD1 1 
ATOM   2034 C  CD2 . LEU A 1 263 ? 16.671  42.372 39.176 1.00 27.68 ? 262 LEU A CD2 1 
ATOM   2035 N  N   . VAL A 1 264 ? 11.777  44.617 39.326 1.00 21.54 ? 263 VAL A N   1 
ATOM   2036 C  CA  . VAL A 1 264 ? 10.361  44.578 38.957 1.00 18.97 ? 263 VAL A CA  1 
ATOM   2037 C  C   . VAL A 1 264 ? 10.153  45.267 37.616 1.00 21.44 ? 263 VAL A C   1 
ATOM   2038 O  O   . VAL A 1 264 ? 9.481   44.741 36.723 1.00 22.74 ? 263 VAL A O   1 
ATOM   2039 C  CB  . VAL A 1 264 ? 9.492   45.222 40.053 1.00 21.14 ? 263 VAL A CB  1 
ATOM   2040 C  CG1 . VAL A 1 264 ? 8.054   45.424 39.542 1.00 22.17 ? 263 VAL A CG1 1 
ATOM   2041 C  CG2 . VAL A 1 264 ? 9.502   44.387 41.337 1.00 20.83 ? 263 VAL A CG2 1 
ATOM   2042 N  N   . ARG A 1 265 ? 10.745  46.452 37.449 1.00 21.31 ? 264 ARG A N   1 
ATOM   2043 C  CA  . ARG A 1 265 ? 10.579  47.181 36.195 1.00 24.68 ? 264 ARG A CA  1 
ATOM   2044 C  C   . ARG A 1 265 ? 11.179  46.417 35.023 1.00 23.86 ? 264 ARG A C   1 
ATOM   2045 O  O   . ARG A 1 265 ? 10.587  46.371 33.941 1.00 25.71 ? 264 ARG A O   1 
ATOM   2046 C  CB  . ARG A 1 265 ? 11.212  48.566 36.305 1.00 24.21 ? 264 ARG A CB  1 
ATOM   2047 C  CG  . ARG A 1 265 ? 10.439  49.507 37.195 1.00 29.44 ? 264 ARG A CG  1 
ATOM   2048 C  CD  . ARG A 1 265 ? 11.031  50.900 37.167 1.00 31.84 ? 264 ARG A CD  1 
ATOM   2049 N  NE  . ARG A 1 265 ? 10.149  51.858 37.823 1.00 39.51 ? 264 ARG A NE  1 
ATOM   2050 C  CZ  . ARG A 1 265 ? 10.570  52.905 38.519 1.00 44.33 ? 264 ARG A CZ  1 
ATOM   2051 N  NH1 . ARG A 1 265 ? 11.860  53.143 38.696 1.00 43.09 ? 264 ARG A NH1 1 
ATOM   2052 N  NH2 . ARG A 1 265 ? 9.675   53.727 39.059 1.00 44.12 ? 264 ARG A NH2 1 
ATOM   2053 N  N   . SER A 1 266 ? 12.353  45.820 35.208 1.00 22.74 ? 265 SER A N   1 
ATOM   2054 C  CA  . SER A 1 266 ? 12.982  45.121 34.095 1.00 22.86 ? 265 SER A CA  1 
ATOM   2055 C  C   . SER A 1 266 ? 12.181  43.887 33.707 1.00 25.34 ? 265 SER A C   1 
ATOM   2056 O  O   . SER A 1 266 ? 12.086  43.552 32.521 1.00 24.87 ? 265 SER A O   1 
ATOM   2057 C  CB  . SER A 1 266 ? 14.420  44.735 34.448 1.00 25.77 ? 265 SER A CB  1 
ATOM   2058 O  OG  . SER A 1 266 ? 14.443  43.566 35.242 1.00 36.49 ? 265 SER A OG  1 
ATOM   2059 N  N   . PHE A 1 267 ? 11.594  43.200 34.691 1.00 23.32 ? 266 PHE A N   1 
ATOM   2060 C  CA  . PHE A 1 267 ? 10.782  42.025 34.396 1.00 20.60 ? 266 PHE A CA  1 
ATOM   2061 C  C   . PHE A 1 267 ? 9.436   42.409 33.785 1.00 24.55 ? 266 PHE A C   1 
ATOM   2062 O  O   . PHE A 1 267 ? 8.902   41.667 32.951 1.00 25.22 ? 266 PHE A O   1 
ATOM   2063 C  CB  . PHE A 1 267 ? 10.552  41.194 35.665 1.00 20.47 ? 266 PHE A CB  1 
ATOM   2064 C  CG  . PHE A 1 267 ? 11.811  40.620 36.278 1.00 22.44 ? 266 PHE A CG  1 
ATOM   2065 C  CD1 . PHE A 1 267 ? 13.017  40.610 35.587 1.00 23.87 ? 266 PHE A CD1 1 
ATOM   2066 C  CD2 . PHE A 1 267 ? 11.787  40.080 37.551 1.00 20.98 ? 266 PHE A CD2 1 
ATOM   2067 C  CE1 . PHE A 1 267 ? 14.157  40.078 36.167 1.00 20.94 ? 266 PHE A CE1 1 
ATOM   2068 C  CE2 . PHE A 1 267 ? 12.925  39.551 38.127 1.00 23.56 ? 266 PHE A CE2 1 
ATOM   2069 C  CZ  . PHE A 1 267 ? 14.111  39.549 37.431 1.00 21.65 ? 266 PHE A CZ  1 
ATOM   2070 N  N   . ALA A 1 268 ? 8.875   43.550 34.191 1.00 23.53 ? 267 ALA A N   1 
ATOM   2071 C  CA  . ALA A 1 268 ? 7.672   44.057 33.539 1.00 23.82 ? 267 ALA A CA  1 
ATOM   2072 C  C   . ALA A 1 268 ? 7.958   44.467 32.098 1.00 26.96 ? 267 ALA A C   1 
ATOM   2073 O  O   . ALA A 1 268 ? 7.072   44.391 31.241 1.00 31.09 ? 267 ALA A O   1 
ATOM   2074 C  CB  . ALA A 1 268 ? 7.108   45.247 34.313 1.00 25.07 ? 267 ALA A CB  1 
ATOM   2075 N  N   . ASN A 1 269 ? 9.181   44.901 31.817 1.00 24.15 ? 268 ASN A N   1 
ATOM   2076 C  CA  . ASN A 1 269 ? 9.495   45.418 30.495 1.00 27.04 ? 268 ASN A CA  1 
ATOM   2077 C  C   . ASN A 1 269 ? 9.878   44.338 29.501 1.00 30.06 ? 268 ASN A C   1 
ATOM   2078 O  O   . ASN A 1 269 ? 9.736   44.556 28.295 1.00 34.16 ? 268 ASN A O   1 
ATOM   2079 C  CB  . ASN A 1 269 ? 10.632  46.431 30.578 1.00 28.37 ? 268 ASN A CB  1 
ATOM   2080 C  CG  . ASN A 1 269 ? 10.191  47.738 31.182 1.00 38.93 ? 268 ASN A CG  1 
ATOM   2081 O  OD1 . ASN A 1 269 ? 8.995   48.034 31.236 1.00 45.82 ? 268 ASN A OD1 1 
ATOM   2082 N  ND2 . ASN A 1 269 ? 11.147  48.533 31.640 1.00 41.08 ? 268 ASN A ND2 1 
ATOM   2083 N  N   . SER A 1 270 ? 10.351  43.186 29.963 1.00 26.74 ? 269 SER A N   1 
ATOM   2084 C  CA  . SER A 1 270 ? 10.819  42.150 29.053 1.00 26.42 ? 269 SER A CA  1 
ATOM   2085 C  C   . SER A 1 270 ? 10.479  40.782 29.610 1.00 24.40 ? 269 SER A C   1 
ATOM   2086 O  O   . SER A 1 270 ? 11.012  40.382 30.649 1.00 23.76 ? 269 SER A O   1 
ATOM   2087 C  CB  . SER A 1 270 ? 12.331  42.250 28.827 1.00 28.97 ? 269 SER A CB  1 
ATOM   2088 O  OG  . SER A 1 270 ? 12.805  41.069 28.206 1.00 27.61 ? 269 SER A OG  1 
ATOM   2089 N  N   . THR A 1 271 ? 9.620   40.056 28.898 1.00 24.49 ? 270 THR A N   1 
ATOM   2090 C  CA  . THR A 1 271 ? 9.331   38.682 29.287 1.00 28.28 ? 270 THR A CA  1 
ATOM   2091 C  C   . THR A 1 271 ? 10.598  37.839 29.272 1.00 25.56 ? 270 THR A C   1 
ATOM   2092 O  O   . THR A 1 271 ? 10.805  36.998 30.156 1.00 25.23 ? 270 THR A O   1 
ATOM   2093 C  CB  . THR A 1 271 ? 8.288   38.075 28.362 1.00 29.68 ? 270 THR A CB  1 
ATOM   2094 O  OG1 . THR A 1 271 ? 7.056   38.796 28.500 1.00 30.82 ? 270 THR A OG1 1 
ATOM   2095 C  CG2 . THR A 1 271 ? 8.078   36.609 28.709 1.00 34.29 ? 270 THR A CG2 1 
ATOM   2096 N  N   . GLN A 1 272 ? 11.449  38.043 28.270 1.00 25.05 ? 271 GLN A N   1 
ATOM   2097 C  CA  . GLN A 1 272 ? 12.681  37.270 28.190 1.00 25.77 ? 271 GLN A CA  1 
ATOM   2098 C  C   . GLN A 1 272 ? 13.551  37.503 29.419 1.00 26.54 ? 271 GLN A C   1 
ATOM   2099 O  O   . GLN A 1 272 ? 14.149  36.564 29.952 1.00 24.43 ? 271 GLN A O   1 
ATOM   2100 C  CB  . GLN A 1 272 ? 13.441  37.635 26.919 1.00 28.68 ? 271 GLN A CB  1 
ATOM   2101 C  CG  . GLN A 1 272 ? 14.532  36.648 26.570 1.00 39.54 ? 271 GLN A CG  1 
ATOM   2102 C  CD  . GLN A 1 272 ? 13.984  35.340 26.031 1.00 49.97 ? 271 GLN A CD  1 
ATOM   2103 O  OE1 . GLN A 1 272 ? 13.304  34.594 26.737 1.00 51.59 ? 271 GLN A OE1 1 
ATOM   2104 N  NE2 . GLN A 1 272 ? 14.275  35.057 24.768 1.00 73.70 ? 271 GLN A NE2 1 
ATOM   2105 N  N   . THR A 1 273 ? 13.639  38.751 29.879 1.00 24.88 ? 272 THR A N   1 
ATOM   2106 C  CA  . THR A 1 273 ? 14.416  39.040 31.075 1.00 24.02 ? 272 THR A CA  1 
ATOM   2107 C  C   . THR A 1 273 ? 13.853  38.292 32.280 1.00 23.25 ? 272 THR A C   1 
ATOM   2108 O  O   . THR A 1 273 ? 14.600  37.665 33.036 1.00 24.71 ? 272 THR A O   1 
ATOM   2109 C  CB  . THR A 1 273 ? 14.437  40.547 31.336 1.00 24.36 ? 272 THR A CB  1 
ATOM   2110 O  OG1 . THR A 1 273 ? 15.002  41.220 30.204 1.00 26.58 ? 272 THR A OG1 1 
ATOM   2111 C  CG2 . THR A 1 273 ? 15.265  40.873 32.571 1.00 27.66 ? 272 THR A CG2 1 
ATOM   2112 N  N   . PHE A 1 274 ? 12.532  38.327 32.455 1.00 21.51 ? 273 PHE A N   1 
ATOM   2113 C  CA  . PHE A 1 274 ? 11.908  37.598 33.554 1.00 21.92 ? 273 PHE A CA  1 
ATOM   2114 C  C   . PHE A 1 274 ? 12.156  36.097 33.421 1.00 20.18 ? 273 PHE A C   1 
ATOM   2115 O  O   . PHE A 1 274 ? 12.569  35.440 34.380 1.00 19.35 ? 273 PHE A O   1 
ATOM   2116 C  CB  . PHE A 1 274 ? 10.408  37.900 33.609 1.00 23.51 ? 273 PHE A CB  1 
ATOM   2117 C  CG  . PHE A 1 274 ? 9.630   36.955 34.481 1.00 18.56 ? 273 PHE A CG  1 
ATOM   2118 C  CD1 . PHE A 1 274 ? 10.069  36.660 35.764 1.00 18.42 ? 273 PHE A CD1 1 
ATOM   2119 C  CD2 . PHE A 1 274 ? 8.463   36.370 34.027 1.00 19.93 ? 273 PHE A CD2 1 
ATOM   2120 C  CE1 . PHE A 1 274 ? 9.362   35.789 36.564 1.00 18.88 ? 273 PHE A CE1 1 
ATOM   2121 C  CE2 . PHE A 1 274 ? 7.755   35.498 34.822 1.00 19.96 ? 273 PHE A CE2 1 
ATOM   2122 C  CZ  . PHE A 1 274 ? 8.201   35.209 36.095 1.00 22.06 ? 273 PHE A CZ  1 
ATOM   2123 N  N   . PHE A 1 275 ? 11.905  35.533 32.236 1.00 18.95 ? 274 PHE A N   1 
ATOM   2124 C  CA  . PHE A 1 275 ? 12.039  34.088 32.081 1.00 21.86 ? 274 PHE A CA  1 
ATOM   2125 C  C   . PHE A 1 275 ? 13.473  33.636 32.344 1.00 21.20 ? 274 PHE A C   1 
ATOM   2126 O  O   . PHE A 1 275 ? 13.696  32.596 32.974 1.00 22.40 ? 274 PHE A O   1 
ATOM   2127 C  CB  . PHE A 1 275 ? 11.601  33.647 30.690 1.00 22.48 ? 274 PHE A CB  1 
ATOM   2128 C  CG  . PHE A 1 275 ? 10.107  33.515 30.518 1.00 22.30 ? 274 PHE A CG  1 
ATOM   2129 C  CD1 . PHE A 1 275 ? 9.214   33.990 31.474 1.00 21.93 ? 274 PHE A CD1 1 
ATOM   2130 C  CD2 . PHE A 1 275 ? 9.597   32.904 29.391 1.00 24.86 ? 274 PHE A CD2 1 
ATOM   2131 C  CE1 . PHE A 1 275 ? 7.846   33.856 31.287 1.00 24.11 ? 274 PHE A CE1 1 
ATOM   2132 C  CE2 . PHE A 1 275 ? 8.239   32.769 29.202 1.00 23.81 ? 274 PHE A CE2 1 
ATOM   2133 C  CZ  . PHE A 1 275 ? 7.363   33.242 30.148 1.00 26.20 ? 274 PHE A CZ  1 
ATOM   2134 N  N   . ASN A 1 276 ? 14.455  34.396 31.863 1.00 20.59 ? 275 ASN A N   1 
ATOM   2135 C  CA  . ASN A 1 276 ? 15.847  34.048 32.134 1.00 21.77 ? 275 ASN A CA  1 
ATOM   2136 C  C   . ASN A 1 276 ? 16.126  34.068 33.628 1.00 22.80 ? 275 ASN A C   1 
ATOM   2137 O  O   . ASN A 1 276 ? 16.774  33.162 34.162 1.00 24.17 ? 275 ASN A O   1 
ATOM   2138 C  CB  . ASN A 1 276 ? 16.789  35.007 31.406 1.00 24.64 ? 275 ASN A CB  1 
ATOM   2139 C  CG  . ASN A 1 276 ? 16.879  34.723 29.923 1.00 25.32 ? 275 ASN A CG  1 
ATOM   2140 O  OD1 . ASN A 1 276 ? 16.437  33.672 29.453 1.00 31.09 ? 275 ASN A OD1 1 
ATOM   2141 N  ND2 . ASN A 1 276 ? 17.464  35.650 29.179 1.00 31.94 ? 275 ASN A ND2 1 
ATOM   2142 N  N   . ALA A 1 277 ? 15.627  35.092 34.323 1.00 23.47 ? 276 ALA A N   1 
ATOM   2143 C  CA  . ALA A 1 277 ? 15.880  35.223 35.750 1.00 22.11 ? 276 ALA A CA  1 
ATOM   2144 C  C   . ALA A 1 277 ? 15.118  34.176 36.551 1.00 19.16 ? 276 ALA A C   1 
ATOM   2145 O  O   . ALA A 1 277 ? 15.614  33.707 37.582 1.00 21.71 ? 276 ALA A O   1 
ATOM   2146 C  CB  . ALA A 1 277 ? 15.505  36.631 36.206 1.00 22.18 ? 276 ALA A CB  1 
ATOM   2147 N  N   . PHE A 1 278 ? 13.927  33.793 36.085 1.00 17.92 ? 277 PHE A N   1 
ATOM   2148 C  CA  . PHE A 1 278 ? 13.148  32.764 36.757 1.00 18.71 ? 277 PHE A CA  1 
ATOM   2149 C  C   . PHE A 1 278 ? 13.837  31.403 36.669 1.00 20.13 ? 277 PHE A C   1 
ATOM   2150 O  O   . PHE A 1 278 ? 13.927  30.682 37.671 1.00 21.23 ? 277 PHE A O   1 
ATOM   2151 C  CB  . PHE A 1 278 ? 11.728  32.698 36.165 1.00 20.24 ? 277 PHE A CB  1 
ATOM   2152 C  CG  . PHE A 1 278 ? 10.827  31.766 36.900 1.00 17.01 ? 277 PHE A CG  1 
ATOM   2153 C  CD1 . PHE A 1 278 ? 10.218  32.162 38.078 1.00 19.14 ? 277 PHE A CD1 1 
ATOM   2154 C  CD2 . PHE A 1 278 ? 10.622  30.471 36.452 1.00 20.14 ? 277 PHE A CD2 1 
ATOM   2155 C  CE1 . PHE A 1 278 ? 9.415   31.297 38.787 1.00 20.67 ? 277 PHE A CE1 1 
ATOM   2156 C  CE2 . PHE A 1 278 ? 9.821   29.600 37.154 1.00 19.53 ? 277 PHE A CE2 1 
ATOM   2157 C  CZ  . PHE A 1 278 ? 9.218   30.011 38.325 1.00 21.56 ? 277 PHE A CZ  1 
ATOM   2158 N  N   . VAL A 1 279 ? 14.332  31.034 35.487 1.00 20.99 ? 278 VAL A N   1 
ATOM   2159 C  CA  . VAL A 1 279 ? 15.057  29.771 35.358 1.00 20.89 ? 278 VAL A CA  1 
ATOM   2160 C  C   . VAL A 1 279 ? 16.294  29.774 36.248 1.00 22.62 ? 278 VAL A C   1 
ATOM   2161 O  O   . VAL A 1 279 ? 16.564  28.808 36.970 1.00 19.20 ? 278 VAL A O   1 
ATOM   2162 C  CB  . VAL A 1 279 ? 15.421  29.505 33.887 1.00 21.52 ? 278 VAL A CB  1 
ATOM   2163 C  CG1 . VAL A 1 279 ? 16.298  28.261 33.777 1.00 22.93 ? 278 VAL A CG1 1 
ATOM   2164 C  CG2 . VAL A 1 279 ? 14.156  29.357 33.050 1.00 23.43 ? 278 VAL A CG2 1 
ATOM   2165 N  N   . GLU A 1 280 ? 17.065  30.860 36.207 1.00 20.95 ? 279 GLU A N   1 
ATOM   2166 C  CA  . GLU A 1 280 ? 18.256  30.950 37.040 1.00 23.58 ? 279 GLU A CA  1 
ATOM   2167 C  C   . GLU A 1 280 ? 17.904  30.790 38.518 1.00 21.71 ? 279 GLU A C   1 
ATOM   2168 O  O   . GLU A 1 280 ? 18.567  30.049 39.256 1.00 22.30 ? 279 GLU A O   1 
ATOM   2169 C  CB  . GLU A 1 280 ? 18.959  32.287 36.808 1.00 26.05 ? 279 GLU A CB  1 
ATOM   2170 C  CG  . GLU A 1 280 ? 19.680  32.412 35.481 1.00 46.36 ? 279 GLU A CG  1 
ATOM   2171 C  CD  . GLU A 1 280 ? 20.323  33.775 35.309 1.00 70.11 ? 279 GLU A CD  1 
ATOM   2172 O  OE1 . GLU A 1 280 ? 20.137  34.635 36.198 1.00 69.75 ? 279 GLU A OE1 1 
ATOM   2173 O  OE2 . GLU A 1 280 ? 21.013  33.988 34.291 1.00 74.17 ? 279 GLU A OE2 1 
ATOM   2174 N  N   . ALA A 1 281 ? 16.851  31.479 38.965 1.00 21.13 ? 280 ALA A N   1 
ATOM   2175 C  CA  . ALA A 1 281 ? 16.484  31.447 40.371 1.00 21.03 ? 280 ALA A CA  1 
ATOM   2176 C  C   . ALA A 1 281 ? 15.880  30.102 40.750 1.00 19.64 ? 280 ALA A C   1 
ATOM   2177 O  O   . ALA A 1 281 ? 16.094  29.610 41.867 1.00 20.08 ? 280 ALA A O   1 
ATOM   2178 C  CB  . ALA A 1 281 ? 15.508  32.582 40.675 1.00 19.70 ? 280 ALA A CB  1 
ATOM   2179 N  N   . MET A 1 282 ? 15.117  29.493 39.841 1.00 20.58 ? 281 MET A N   1 
ATOM   2180 C  CA  . MET A 1 282 ? 14.576  28.162 40.103 1.00 20.37 ? 281 MET A CA  1 
ATOM   2181 C  C   . MET A 1 282 ? 15.683  27.132 40.259 1.00 23.17 ? 281 MET A C   1 
ATOM   2182 O  O   . MET A 1 282 ? 15.600  26.248 41.116 1.00 22.73 ? 281 MET A O   1 
ATOM   2183 C  CB  . MET A 1 282 ? 13.634  27.746 38.976 1.00 23.91 ? 281 MET A CB  1 
ATOM   2184 C  CG  . MET A 1 282 ? 12.260  28.371 39.051 1.00 25.61 ? 281 MET A CG  1 
ATOM   2185 S  SD  . MET A 1 282 ? 11.255  27.624 40.343 1.00 27.01 ? 281 MET A SD  1 
ATOM   2186 C  CE  . MET A 1 282 ? 10.865  26.046 39.585 1.00 24.73 ? 281 MET A CE  1 
ATOM   2187 N  N   . ASP A 1 283 ? 16.715  27.207 39.415 1.00 22.18 ? 282 ASP A N   1 
ATOM   2188 C  CA  . ASP A 1 283 ? 17.808  26.246 39.518 1.00 21.81 ? 282 ASP A CA  1 
ATOM   2189 C  C   . ASP A 1 283 ? 18.602  26.452 40.812 1.00 21.53 ? 282 ASP A C   1 
ATOM   2190 O  O   . ASP A 1 283 ? 19.072  25.478 41.407 1.00 22.13 ? 282 ASP A O   1 
ATOM   2191 C  CB  . ASP A 1 283 ? 18.692  26.345 38.276 1.00 23.79 ? 282 ASP A CB  1 
ATOM   2192 C  CG  . ASP A 1 283 ? 18.077  25.635 37.066 1.00 27.77 ? 282 ASP A CG  1 
ATOM   2193 O  OD1 . ASP A 1 283 ? 17.067  24.911 37.249 1.00 26.12 ? 282 ASP A OD1 1 
ATOM   2194 O  OD2 . ASP A 1 283 ? 18.587  25.802 35.935 1.00 30.90 ? 282 ASP A OD2 1 
ATOM   2195 N  N   . ARG A 1 284 ? 18.731  27.701 41.280 1.00 19.66 ? 283 ARG A N   1 
ATOM   2196 C  CA  . ARG A 1 284 ? 19.367  27.949 42.565 1.00 20.73 ? 283 ARG A CA  1 
ATOM   2197 C  C   . ARG A 1 284 ? 18.513  27.417 43.710 1.00 22.36 ? 283 ARG A C   1 
ATOM   2198 O  O   . ARG A 1 284 ? 19.024  26.783 44.639 1.00 22.60 ? 283 ARG A O   1 
ATOM   2199 C  CB  . ARG A 1 284 ? 19.631  29.446 42.737 1.00 23.29 ? 283 ARG A CB  1 
ATOM   2200 C  CG  . ARG A 1 284 ? 20.807  29.947 41.898 1.00 21.15 ? 283 ARG A CG  1 
ATOM   2201 C  CD  . ARG A 1 284 ? 20.878  31.463 41.795 1.00 24.41 ? 283 ARG A CD  1 
ATOM   2202 N  NE  . ARG A 1 284 ? 20.791  32.114 43.091 1.00 25.45 ? 283 ARG A NE  1 
ATOM   2203 C  CZ  . ARG A 1 284 ? 21.739  32.084 44.018 1.00 27.10 ? 283 ARG A CZ  1 
ATOM   2204 N  NH1 . ARG A 1 284 ? 22.882  31.448 43.818 1.00 29.50 ? 283 ARG A NH1 1 
ATOM   2205 N  NH2 . ARG A 1 284 ? 21.529  32.697 45.180 1.00 29.87 ? 283 ARG A NH2 1 
ATOM   2206 N  N   . MET A 1 285 ? 17.205  27.660 43.654 1.00 21.52 ? 284 MET A N   1 
ATOM   2207 C  CA  . MET A 1 285 ? 16.312  27.104 44.659 1.00 19.68 ? 284 MET A CA  1 
ATOM   2208 C  C   . MET A 1 285 ? 16.368  25.584 44.649 1.00 22.54 ? 284 MET A C   1 
ATOM   2209 O  O   . MET A 1 285 ? 16.401  24.947 45.711 1.00 21.96 ? 284 MET A O   1 
ATOM   2210 C  CB  . MET A 1 285 ? 14.891  27.591 44.430 1.00 18.97 ? 284 MET A CB  1 
ATOM   2211 C  CG  . MET A 1 285 ? 13.949  27.112 45.495 1.00 20.74 ? 284 MET A CG  1 
ATOM   2212 S  SD  . MET A 1 285 ? 12.273  27.734 45.357 1.00 24.90 ? 284 MET A SD  1 
ATOM   2213 C  CE  . MET A 1 285 ? 11.663  26.797 43.961 1.00 26.08 ? 284 MET A CE  1 
ATOM   2214 N  N   . GLY A 1 286 ? 16.386  24.983 43.458 1.00 21.78 ? 285 GLY A N   1 
ATOM   2215 C  CA  . GLY A 1 286 ? 16.524  23.542 43.356 1.00 23.40 ? 285 GLY A CA  1 
ATOM   2216 C  C   . GLY A 1 286 ? 17.848  23.008 43.844 1.00 24.98 ? 285 GLY A C   1 
ATOM   2217 O  O   . GLY A 1 286 ? 17.984  21.790 44.012 1.00 25.56 ? 285 GLY A O   1 
ATOM   2218 N  N   . ASN A 1 287 ? 18.814  23.885 44.097 1.00 21.87 ? 286 ASN A N   1 
ATOM   2219 C  CA  . ASN A 1 287 ? 20.135  23.490 44.550 1.00 22.82 ? 286 ASN A CA  1 
ATOM   2220 C  C   . ASN A 1 287 ? 20.327  23.686 46.048 1.00 23.96 ? 286 ASN A C   1 
ATOM   2221 O  O   . ASN A 1 287 ? 21.453  23.570 46.539 1.00 25.11 ? 286 ASN A O   1 
ATOM   2222 C  CB  . ASN A 1 287 ? 21.193  24.289 43.798 1.00 24.46 ? 286 ASN A CB  1 
ATOM   2223 C  CG  . ASN A 1 287 ? 22.544  23.633 43.846 1.00 31.59 ? 286 ASN A CG  1 
ATOM   2224 O  OD1 . ASN A 1 287 ? 22.652  22.417 43.689 1.00 34.37 ? 286 ASN A OD1 1 
ATOM   2225 N  ND2 . ASN A 1 287 ? 23.580  24.424 44.086 1.00 36.30 ? 286 ASN A ND2 1 
ATOM   2226 N  N   . ILE A 1 288 ? 19.255  23.974 46.782 1.00 21.00 ? 287 ILE A N   1 
ATOM   2227 C  CA  . ILE A 1 288 ? 19.364  24.180 48.219 1.00 22.50 ? 287 ILE A CA  1 
ATOM   2228 C  C   . ILE A 1 288 ? 19.573  22.832 48.896 1.00 22.23 ? 287 ILE A C   1 
ATOM   2229 O  O   . ILE A 1 288 ? 18.719  21.940 48.812 1.00 22.94 ? 287 ILE A O   1 
ATOM   2230 C  CB  . ILE A 1 288 ? 18.126  24.903 48.761 1.00 22.74 ? 287 ILE A CB  1 
ATOM   2231 C  CG1 . ILE A 1 288 ? 18.063  26.327 48.198 1.00 24.28 ? 287 ILE A CG1 1 
ATOM   2232 C  CG2 . ILE A 1 288 ? 18.164  24.951 50.272 1.00 22.99 ? 287 ILE A CG2 1 
ATOM   2233 C  CD1 . ILE A 1 288 ? 16.765  27.048 48.461 1.00 27.78 ? 287 ILE A CD1 1 
ATOM   2234 N  N   . THR A 1 289 ? 20.728  22.684 49.554 1.00 23.59 ? 288 THR A N   1 
ATOM   2235 C  CA  . THR A 1 289 ? 21.180  21.571 50.380 1.00 25.84 ? 288 THR A CA  1 
ATOM   2236 C  C   . THR A 1 289 ? 20.632  20.201 49.998 1.00 24.70 ? 288 THR A C   1 
ATOM   2237 O  O   . THR A 1 289 ? 19.990  19.540 50.827 1.00 25.24 ? 288 THR A O   1 
ATOM   2238 C  CB  . THR A 1 289 ? 20.834  21.842 51.850 1.00 30.23 ? 288 THR A CB  1 
ATOM   2239 O  OG1 . THR A 1 289 ? 19.412  21.967 52.016 1.00 28.76 ? 288 THR A OG1 1 
ATOM   2240 C  CG2 . THR A 1 289 ? 21.496  23.130 52.342 1.00 26.54 ? 288 THR A CG2 1 
ATOM   2241 N  N   . PRO A 1 290 ? 20.928  19.708 48.801 1.00 23.53 ? 289 PRO A N   1 
ATOM   2242 C  CA  . PRO A 1 290 ? 20.428  18.388 48.412 1.00 21.62 ? 289 PRO A CA  1 
ATOM   2243 C  C   . PRO A 1 290 ? 21.222  17.249 49.029 1.00 24.12 ? 289 PRO A C   1 
ATOM   2244 O  O   . PRO A 1 290 ? 22.416  17.363 49.311 1.00 25.24 ? 289 PRO A O   1 
ATOM   2245 C  CB  . PRO A 1 290 ? 20.578  18.393 46.885 1.00 23.74 ? 289 PRO A CB  1 
ATOM   2246 C  CG  . PRO A 1 290 ? 21.762  19.285 46.641 1.00 25.29 ? 289 PRO A CG  1 
ATOM   2247 C  CD  . PRO A 1 290 ? 21.662  20.374 47.706 1.00 27.48 ? 289 PRO A CD  1 
ATOM   2248 N  N   . LEU A 1 291 ? 20.517  16.146 49.253 1.00 22.17 ? 290 LEU A N   1 
ATOM   2249 C  CA  . LEU A 1 291 ? 21.147  14.854 49.477 1.00 23.27 ? 290 LEU A CA  1 
ATOM   2250 C  C   . LEU A 1 291 ? 21.511  14.240 48.129 1.00 24.33 ? 290 LEU A C   1 
ATOM   2251 O  O   . LEU A 1 291 ? 20.705  14.250 47.195 1.00 22.26 ? 290 LEU A O   1 
ATOM   2252 C  CB  . LEU A 1 291 ? 20.200  13.930 50.234 1.00 21.83 ? 290 LEU A CB  1 
ATOM   2253 C  CG  . LEU A 1 291 ? 19.632  14.504 51.536 1.00 29.56 ? 290 LEU A CG  1 
ATOM   2254 C  CD1 . LEU A 1 291 ? 18.632  13.537 52.146 1.00 26.16 ? 290 LEU A CD1 1 
ATOM   2255 C  CD2 . LEU A 1 291 ? 20.752  14.824 52.504 1.00 30.74 ? 290 LEU A CD2 1 
ATOM   2256 N  N   . THR A 1 292 ? 22.728  13.718 48.023 1.00 23.40 ? 291 THR A N   1 
ATOM   2257 C  CA  . THR A 1 292 ? 23.189  13.153 46.761 1.00 24.39 ? 291 THR A CA  1 
ATOM   2258 C  C   . THR A 1 292 ? 23.979  11.877 47.025 1.00 26.68 ? 291 THR A C   1 
ATOM   2259 O  O   . THR A 1 292 ? 24.249  11.510 48.167 1.00 24.81 ? 291 THR A O   1 
ATOM   2260 C  CB  . THR A 1 292 ? 24.062  14.142 45.965 1.00 31.44 ? 291 THR A CB  1 
ATOM   2261 O  OG1 . THR A 1 292 ? 25.216  14.501 46.736 1.00 29.47 ? 291 THR A OG1 1 
ATOM   2262 C  CG2 . THR A 1 292 ? 23.281  15.401 45.586 1.00 31.63 ? 291 THR A CG2 1 
ATOM   2263 N  N   . GLY A 1 293 ? 24.359  11.203 45.941 1.00 26.90 ? 292 GLY A N   1 
ATOM   2264 C  CA  . GLY A 1 293 ? 25.184  10.014 46.049 1.00 28.81 ? 292 GLY A CA  1 
ATOM   2265 C  C   . GLY A 1 293 ? 24.477  8.862  46.733 1.00 26.88 ? 292 GLY A C   1 
ATOM   2266 O  O   . GLY A 1 293 ? 23.480  8.346  46.219 1.00 30.23 ? 292 GLY A O   1 
ATOM   2267 N  N   . THR A 1 294 ? 24.988  8.442  47.887 1.00 25.17 ? 293 THR A N   1 
ATOM   2268 C  CA  . THR A 1 294 ? 24.375  7.394  48.693 1.00 25.46 ? 293 THR A CA  1 
ATOM   2269 C  C   . THR A 1 294 ? 23.661  7.951  49.922 1.00 27.40 ? 293 THR A C   1 
ATOM   2270 O  O   . THR A 1 294 ? 23.199  7.176  50.766 1.00 31.56 ? 293 THR A O   1 
ATOM   2271 C  CB  . THR A 1 294 ? 25.431  6.380  49.121 1.00 32.43 ? 293 THR A CB  1 
ATOM   2272 O  OG1 . THR A 1 294 ? 26.475  7.061  49.820 1.00 33.31 ? 293 THR A OG1 1 
ATOM   2273 C  CG2 . THR A 1 294 ? 26.013  5.667  47.909 1.00 38.50 ? 293 THR A CG2 1 
ATOM   2274 N  N   . GLN A 1 295 ? 23.588  9.274  50.045 1.00 25.55 ? 294 GLN A N   1 
ATOM   2275 C  CA  . GLN A 1 295 ? 22.846  9.918  51.116 1.00 24.63 ? 294 GLN A CA  1 
ATOM   2276 C  C   . GLN A 1 295 ? 21.344  9.778  50.867 1.00 25.06 ? 294 GLN A C   1 
ATOM   2277 O  O   . GLN A 1 295 ? 20.886  9.807  49.727 1.00 25.12 ? 294 GLN A O   1 
ATOM   2278 C  CB  . GLN A 1 295 ? 23.225  11.398 51.195 1.00 22.68 ? 294 GLN A CB  1 
ATOM   2279 C  CG  . GLN A 1 295 ? 24.729  11.669 51.320 1.00 26.14 ? 294 GLN A CG  1 
ATOM   2280 C  CD  . GLN A 1 295 ? 25.095  13.127 51.076 1.00 27.64 ? 294 GLN A CD  1 
ATOM   2281 O  OE1 . GLN A 1 295 ? 24.268  13.924 50.636 1.00 25.57 ? 294 GLN A OE1 1 
ATOM   2282 N  NE2 . GLN A 1 295 ? 26.342  13.481 51.363 1.00 28.04 ? 294 GLN A NE2 1 
ATOM   2283 N  N   . GLY A 1 296 ? 20.580  9.629  51.942 1.00 26.33 ? 295 GLY A N   1 
ATOM   2284 C  CA  . GLY A 1 296 ? 19.137  9.504  51.723 1.00 26.21 ? 295 GLY A CA  1 
ATOM   2285 C  C   . GLY A 1 296 ? 18.845  8.252  50.913 1.00 27.70 ? 295 GLY A C   1 
ATOM   2286 O  O   . GLY A 1 296 ? 19.686  7.369  50.742 1.00 28.56 ? 295 GLY A O   1 
ATOM   2287 N  N   . GLN A 1 297 ? 17.622  8.179  50.395 1.00 23.44 ? 296 GLN A N   1 
ATOM   2288 C  CA  . GLN A 1 297 ? 17.234  6.998  49.638 1.00 25.61 ? 296 GLN A CA  1 
ATOM   2289 C  C   . GLN A 1 297 ? 16.439  7.377  48.398 1.00 26.55 ? 296 GLN A C   1 
ATOM   2290 O  O   . GLN A 1 297 ? 16.125  8.546  48.152 1.00 25.44 ? 296 GLN A O   1 
ATOM   2291 C  CB  . GLN A 1 297 ? 16.431  6.015  50.508 1.00 32.33 ? 296 GLN A CB  1 
ATOM   2292 C  CG  . GLN A 1 297 ? 15.421  6.680  51.435 1.00 35.02 ? 296 GLN A CG  1 
ATOM   2293 C  CD  . GLN A 1 297 ? 14.576  5.691  52.218 1.00 29.56 ? 296 GLN A CD  1 
ATOM   2294 O  OE1 . GLN A 1 297 ? 13.360  5.824  52.283 1.00 27.83 ? 296 GLN A OE1 1 
ATOM   2295 N  NE2 . GLN A 1 297 ? 15.226  4.705  52.834 1.00 30.10 ? 296 GLN A NE2 1 
ATOM   2296 N  N   . ILE A 1 298 ? 16.171  6.364  47.576 1.00 25.12 ? 297 ILE A N   1 
ATOM   2297 C  CA  . ILE A 1 298 ? 15.177  6.461  46.517 1.00 25.21 ? 297 ILE A CA  1 
ATOM   2298 C  C   . ILE A 1 298 ? 13.881  5.959  47.138 1.00 25.23 ? 297 ILE A C   1 
ATOM   2299 O  O   . ILE A 1 298 ? 13.674  4.755  47.303 1.00 26.79 ? 297 ILE A O   1 
ATOM   2300 C  CB  . ILE A 1 298 ? 15.569  5.669  45.270 1.00 27.66 ? 297 ILE A CB  1 
ATOM   2301 C  CG1 . ILE A 1 298 ? 16.898  6.182  44.711 1.00 31.76 ? 297 ILE A CG1 1 
ATOM   2302 C  CG2 . ILE A 1 298 ? 14.455  5.772  44.230 1.00 27.70 ? 297 ILE A CG2 1 
ATOM   2303 C  CD1 . ILE A 1 298 ? 16.933  7.672  44.422 1.00 32.91 ? 297 ILE A CD1 1 
ATOM   2304 N  N   . ARG A 1 299 ? 13.032  6.893  47.542 1.00 24.95 ? 298 ARG A N   1 
ATOM   2305 C  CA  . ARG A 1 299 ? 11.777  6.531  48.176 1.00 25.22 ? 298 ARG A CA  1 
ATOM   2306 C  C   . ARG A 1 299 ? 10.861  5.888  47.151 1.00 28.57 ? 298 ARG A C   1 
ATOM   2307 O  O   . ARG A 1 299 ? 10.723  6.388  46.033 1.00 30.97 ? 298 ARG A O   1 
ATOM   2308 C  CB  . ARG A 1 299 ? 11.132  7.774  48.778 1.00 28.06 ? 298 ARG A CB  1 
ATOM   2309 C  CG  . ARG A 1 299 ? 10.289  7.498  49.991 1.00 26.47 ? 298 ARG A CG  1 
ATOM   2310 C  CD  . ARG A 1 299 ? 9.626   8.779  50.451 1.00 27.19 ? 298 ARG A CD  1 
ATOM   2311 N  NE  . ARG A 1 299 ? 10.579  9.689  51.081 1.00 24.12 ? 298 ARG A NE  1 
ATOM   2312 C  CZ  . ARG A 1 299 ? 10.405  10.999 51.174 1.00 23.87 ? 298 ARG A CZ  1 
ATOM   2313 N  NH1 . ARG A 1 299 ? 9.324   11.590 50.688 1.00 21.64 ? 298 ARG A NH1 1 
ATOM   2314 N  NH2 . ARG A 1 299 ? 11.342  11.738 51.763 1.00 21.74 ? 298 ARG A NH2 1 
ATOM   2315 N  N   . LEU A 1 300 ? 10.262  4.758  47.517 1.00 26.80 ? 299 LEU A N   1 
ATOM   2316 C  CA  . LEU A 1 300 ? 9.414   4.036  46.578 1.00 32.02 ? 299 LEU A CA  1 
ATOM   2317 C  C   . LEU A 1 300 ? 7.963   4.485  46.646 1.00 33.20 ? 299 LEU A C   1 
ATOM   2318 O  O   . LEU A 1 300 ? 7.288   4.523  45.612 1.00 33.71 ? 299 LEU A O   1 
ATOM   2319 C  CB  . LEU A 1 300 ? 9.510   2.536  46.843 1.00 35.45 ? 299 LEU A CB  1 
ATOM   2320 C  CG  . LEU A 1 300 ? 10.923  1.976  46.662 1.00 37.92 ? 299 LEU A CG  1 
ATOM   2321 C  CD1 . LEU A 1 300 ? 10.898  0.457  46.742 1.00 40.18 ? 299 LEU A CD1 1 
ATOM   2322 C  CD2 . LEU A 1 300 ? 11.549  2.430  45.349 1.00 43.73 ? 299 LEU A CD2 1 
ATOM   2323 N  N   . ASN A 1 301 ? 7.488   4.823  47.841 1.00 27.58 ? 300 ASN A N   1 
ATOM   2324 C  CA  . ASN A 1 301 ? 6.189   5.445  48.073 1.00 28.07 ? 300 ASN A CA  1 
ATOM   2325 C  C   . ASN A 1 301 ? 6.482   6.811  48.667 1.00 33.07 ? 300 ASN A C   1 
ATOM   2326 O  O   . ASN A 1 301 ? 7.110   6.902  49.728 1.00 26.56 ? 300 ASN A O   1 
ATOM   2327 C  CB  . ASN A 1 301 ? 5.347   4.608  49.034 1.00 29.42 ? 300 ASN A CB  1 
ATOM   2328 C  CG  . ASN A 1 301 ? 3.996   5.233  49.327 1.00 32.44 ? 300 ASN A CG  1 
ATOM   2329 O  OD1 . ASN A 1 301 ? 3.859   6.452  49.432 1.00 30.83 ? 300 ASN A OD1 1 
ATOM   2330 N  ND2 . ASN A 1 301 ? 2.986   4.389  49.468 1.00 46.30 ? 300 ASN A ND2 1 
ATOM   2331 N  N   . CYS A 1 302 ? 6.054   7.876  47.990 1.00 28.17 ? 301 CYS A N   1 
ATOM   2332 C  CA  . CYS A 1 302 ? 6.538   9.183  48.411 1.00 31.68 ? 301 CYS A CA  1 
ATOM   2333 C  C   . CYS A 1 302 ? 6.020   9.577  49.795 1.00 27.73 ? 301 CYS A C   1 
ATOM   2334 O  O   . CYS A 1 302 ? 6.610   10.462 50.423 1.00 26.36 ? 301 CYS A O   1 
ATOM   2335 C  CB  . CYS A 1 302 ? 6.199   10.232 47.346 1.00 43.89 ? 301 CYS A CB  1 
ATOM   2336 S  SG  . CYS A 1 302 ? 7.162   10.033 45.770 1.00 65.23 ? 301 CYS A SG  1 
ATOM   2337 N  N   . ARG A 1 303 ? 4.998   8.896  50.324 1.00 26.76 ? 302 ARG A N   1 
ATOM   2338 C  CA  . ARG A 1 303 ? 4.457   9.257  51.630 1.00 26.11 ? 302 ARG A CA  1 
ATOM   2339 C  C   . ARG A 1 303 ? 5.188   8.620  52.805 1.00 24.03 ? 302 ARG A C   1 
ATOM   2340 O  O   . ARG A 1 303 ? 4.954   9.028  53.946 1.00 26.86 ? 302 ARG A O   1 
ATOM   2341 C  CB  . ARG A 1 303 ? 2.973   8.886  51.717 1.00 30.06 ? 302 ARG A CB  1 
ATOM   2342 C  CG  . ARG A 1 303 ? 2.108   9.724  50.812 1.00 30.25 ? 302 ARG A CG  1 
ATOM   2343 C  CD  . ARG A 1 303 ? 0.671   9.238  50.736 1.00 38.22 ? 302 ARG A CD  1 
ATOM   2344 N  NE  . ARG A 1 303 ? -0.076  10.033 49.767 1.00 35.50 ? 302 ARG A NE  1 
ATOM   2345 C  CZ  . ARG A 1 303 ? -0.720  11.154 50.056 1.00 38.62 ? 302 ARG A CZ  1 
ATOM   2346 N  NH1 . ARG A 1 303 ? -0.783  11.615 51.295 1.00 38.10 ? 302 ARG A NH1 1 
ATOM   2347 N  NH2 . ARG A 1 303 ? -1.314  11.832 49.079 1.00 36.29 ? 302 ARG A NH2 1 
ATOM   2348 N  N   . VAL A 1 304 ? 6.051   7.633  52.581 1.00 22.56 ? 303 VAL A N   1 
ATOM   2349 C  CA  . VAL A 1 304 ? 6.651   6.904  53.687 1.00 25.99 ? 303 VAL A CA  1 
ATOM   2350 C  C   . VAL A 1 304 ? 8.083   6.531  53.330 1.00 24.01 ? 303 VAL A C   1 
ATOM   2351 O  O   . VAL A 1 304 ? 8.433   6.361  52.160 1.00 24.16 ? 303 VAL A O   1 
ATOM   2352 C  CB  . VAL A 1 304 ? 5.823   5.649  54.052 1.00 30.39 ? 303 VAL A CB  1 
ATOM   2353 C  CG1 . VAL A 1 304 ? 4.372   6.027  54.345 1.00 35.73 ? 303 VAL A CG1 1 
ATOM   2354 C  CG2 . VAL A 1 304 ? 5.897   4.614  52.941 1.00 29.74 ? 303 VAL A CG2 1 
ATOM   2355 N  N   . VAL A 1 305 ? 8.914   6.419  54.365 1.00 27.51 ? 304 VAL A N   1 
ATOM   2356 C  CA  . VAL A 1 305 ? 10.277  5.939  54.199 1.00 26.17 ? 304 VAL A CA  1 
ATOM   2357 C  C   . VAL A 1 305 ? 10.259  4.454  53.860 1.00 28.43 ? 304 VAL A C   1 
ATOM   2358 O  O   . VAL A 1 305 ? 9.355   3.711  54.265 1.00 27.11 ? 304 VAL A O   1 
ATOM   2359 C  CB  . VAL A 1 305 ? 11.069  6.222  55.489 1.00 33.52 ? 304 VAL A CB  1 
ATOM   2360 C  CG1 . VAL A 1 305 ? 12.355  5.441  55.504 1.00 38.43 ? 304 VAL A CG1 1 
ATOM   2361 C  CG2 . VAL A 1 305 ? 11.337  7.720  55.615 1.00 28.41 ? 304 VAL A CG2 1 
ATOM   2362 N  N   . ASN A 1 306 ? 11.261  4.016  53.100 1.00 25.09 ? 305 ASN A N   1 
ATOM   2363 C  CA  . ASN A 1 306 ? 11.326  2.621  52.684 1.00 26.63 ? 305 ASN A CA  1 
ATOM   2364 C  C   . ASN A 1 306 ? 11.517  1.713  53.895 1.00 33.71 ? 305 ASN A C   1 
ATOM   2365 O  O   . ASN A 1 306 ? 12.148  2.085  54.888 1.00 32.30 ? 305 ASN A O   1 
ATOM   2366 C  CB  . ASN A 1 306 ? 12.479  2.389  51.702 1.00 29.35 ? 305 ASN A CB  1 
ATOM   2367 C  CG  . ASN A 1 306 ? 12.335  3.175  50.407 1.00 27.87 ? 305 ASN A CG  1 
ATOM   2368 O  OD1 . ASN A 1 306 ? 11.253  3.647  50.047 1.00 25.69 ? 305 ASN A OD1 1 
ATOM   2369 N  ND2 . ASN A 1 306 ? 13.443  3.311  49.691 1.00 29.14 ? 305 ASN A ND2 1 
ATOM   2370 N  N   . SER A 1 307 ? 10.982  0.501  53.801 1.00 35.14 ? 306 SER A N   1 
ATOM   2371 C  CA  . SER A 1 307 ? 11.138  -0.465 54.885 1.00 42.95 ? 306 SER A CA  1 
ATOM   2372 C  C   . SER A 1 307 ? 11.205  -1.894 54.363 1.00 41.51 ? 306 SER A C   1 
ATOM   2373 O  O   . SER A 1 307 ? 11.010  -2.137 53.174 1.00 45.18 ? 306 SER A O   1 
ATOM   2374 C  CB  . SER A 1 307 ? 9.986   -0.326 55.881 1.00 46.14 ? 306 SER A CB  1 
ATOM   2375 O  OG  . SER A 1 307 ? 8.749   -0.240 55.197 1.00 56.84 ? 306 SER A OG  1 
HETATM 2376 C  CHA . HEM B 2 .   ? 0.349   30.637 46.700 1.00 20.38 ? 401 HEM A CHA 1 
HETATM 2377 C  CHB . HEM B 2 .   ? 2.716   33.386 49.883 1.00 21.25 ? 401 HEM A CHB 1 
HETATM 2378 C  CHC . HEM B 2 .   ? 6.775   32.807 47.349 1.00 20.79 ? 401 HEM A CHC 1 
HETATM 2379 C  CHD . HEM B 2 .   ? 4.416   30.057 44.182 1.00 19.76 ? 401 HEM A CHD 1 
HETATM 2380 C  C1A . HEM B 2 .   ? 0.622   31.414 47.791 1.00 19.01 ? 401 HEM A C1A 1 
HETATM 2381 C  C2A . HEM B 2 .   ? -0.322  31.804 48.810 1.00 19.65 ? 401 HEM A C2A 1 
HETATM 2382 C  C3A . HEM B 2 .   ? 0.337   32.570 49.691 1.00 18.99 ? 401 HEM A C3A 1 
HETATM 2383 C  C4A . HEM B 2 .   ? 1.714   32.685 49.251 1.00 19.31 ? 401 HEM A C4A 1 
HETATM 2384 C  CMA . HEM B 2 .   ? -0.239  33.228 50.960 1.00 22.34 ? 401 HEM A CMA 1 
HETATM 2385 C  CAA . HEM B 2 .   ? -1.806  31.384 48.856 1.00 19.88 ? 401 HEM A CAA 1 
HETATM 2386 C  CBA . HEM B 2 .   ? -1.898  30.065 49.620 1.00 23.37 ? 401 HEM A CBA 1 
HETATM 2387 C  CGA . HEM B 2 .   ? -3.328  29.726 49.975 1.00 30.81 ? 401 HEM A CGA 1 
HETATM 2388 O  O1A . HEM B 2 .   ? -3.561  28.662 50.601 1.00 29.08 ? 401 HEM A O1A 1 
HETATM 2389 O  O2A . HEM B 2 .   ? -4.238  30.523 49.644 1.00 27.60 ? 401 HEM A O2A 1 
HETATM 2390 C  C1B . HEM B 2 .   ? 4.011   33.516 49.434 1.00 19.06 ? 401 HEM A C1B 1 
HETATM 2391 C  C2B . HEM B 2 .   ? 5.029   34.359 50.005 1.00 20.59 ? 401 HEM A C2B 1 
HETATM 2392 C  C3B . HEM B 2 .   ? 6.153   34.227 49.294 1.00 20.50 ? 401 HEM A C3B 1 
HETATM 2393 C  C4B . HEM B 2 .   ? 5.888   33.251 48.268 1.00 20.67 ? 401 HEM A C4B 1 
HETATM 2394 C  CMB . HEM B 2 .   ? 4.837   35.304 51.203 1.00 22.28 ? 401 HEM A CMB 1 
HETATM 2395 C  CAB . HEM B 2 .   ? 7.476   34.961 49.569 1.00 19.80 ? 401 HEM A CAB 1 
HETATM 2396 C  CBB . HEM B 2 .   ? 8.212   35.416 48.549 1.00 21.95 ? 401 HEM A CBB 1 
HETATM 2397 C  C1C . HEM B 2 .   ? 6.492   31.928 46.350 1.00 20.29 ? 401 HEM A C1C 1 
HETATM 2398 C  C2C . HEM B 2 .   ? 7.474   31.268 45.536 1.00 20.75 ? 401 HEM A C2C 1 
HETATM 2399 C  C3C . HEM B 2 .   ? 6.815   30.478 44.671 1.00 20.02 ? 401 HEM A C3C 1 
HETATM 2400 C  C4C . HEM B 2 .   ? 5.412   30.666 44.899 1.00 20.33 ? 401 HEM A C4C 1 
HETATM 2401 C  CMC . HEM B 2 .   ? 8.994   31.438 45.714 1.00 18.54 ? 401 HEM A CMC 1 
HETATM 2402 C  CAC . HEM B 2 .   ? 7.338   29.567 43.554 1.00 18.52 ? 401 HEM A CAC 1 
HETATM 2403 C  CBC . HEM B 2 .   ? 8.416   29.904 42.838 1.00 22.10 ? 401 HEM A CBC 1 
HETATM 2404 C  C1D . HEM B 2 .   ? 3.106   30.046 44.542 1.00 18.86 ? 401 HEM A C1D 1 
HETATM 2405 C  C2D . HEM B 2 .   ? 2.019   29.529 43.757 1.00 19.63 ? 401 HEM A C2D 1 
HETATM 2406 C  C3D . HEM B 2 .   ? 0.885   29.689 44.453 1.00 19.77 ? 401 HEM A C3D 1 
HETATM 2407 C  C4D . HEM B 2 .   ? 1.227   30.325 45.705 1.00 19.49 ? 401 HEM A C4D 1 
HETATM 2408 C  CMD . HEM B 2 .   ? 2.191   28.907 42.354 1.00 18.00 ? 401 HEM A CMD 1 
HETATM 2409 C  CAD . HEM B 2 .   ? -0.545  29.276 44.020 1.00 18.74 ? 401 HEM A CAD 1 
HETATM 2410 C  CBD . HEM B 2 .   ? -0.767  27.839 44.479 1.00 19.24 ? 401 HEM A CBD 1 
HETATM 2411 C  CGD . HEM B 2 .   ? -2.155  27.303 44.194 1.00 21.59 ? 401 HEM A CGD 1 
HETATM 2412 O  O1D . HEM B 2 .   ? -2.420  26.139 44.605 1.00 22.90 ? 401 HEM A O1D 1 
HETATM 2413 O  O2D . HEM B 2 .   ? -2.989  28.011 43.577 1.00 21.50 ? 401 HEM A O2D 1 
HETATM 2414 N  NA  . HEM B 2 .   ? 1.853   31.963 48.091 1.00 19.83 ? 401 HEM A NA  1 
HETATM 2415 N  NB  . HEM B 2 .   ? 4.572   32.837 48.376 1.00 17.63 ? 401 HEM A NB  1 
HETATM 2416 N  NC  . HEM B 2 .   ? 5.238   31.553 45.928 1.00 20.70 ? 401 HEM A NC  1 
HETATM 2417 N  ND  . HEM B 2 .   ? 2.606   30.522 45.734 1.00 18.98 ? 401 HEM A ND  1 
HETATM 2418 FE FE  . HEM B 2 .   ? 3.526   31.903 46.880 1.00 19.45 ? 401 HEM A FE  1 
HETATM 2419 CA CA  . CA  C 3 .   ? 12.384  19.702 52.029 1.00 19.13 ? 402 CA  A CA  1 
HETATM 2420 CA CA  . CA  D 3 .   ? -0.059  35.474 34.539 1.00 20.90 ? 403 CA  A CA  1 
HETATM 2421 C  C1  . EDO E 4 .   ? -3.464  54.025 46.311 1.00 39.06 ? 404 EDO A C1  1 
HETATM 2422 O  O1  . EDO E 4 .   ? -2.261  53.667 45.617 1.00 44.27 ? 404 EDO A O1  1 
HETATM 2423 C  C2  . EDO E 4 .   ? -4.393  54.813 45.396 1.00 40.36 ? 404 EDO A C2  1 
HETATM 2424 O  O2  . EDO E 4 .   ? -4.883  53.976 44.340 1.00 39.46 ? 404 EDO A O2  1 
HETATM 2425 C  C1  . EDO F 4 .   ? 16.886  25.277 54.492 1.00 29.98 ? 405 EDO A C1  1 
HETATM 2426 O  O1  . EDO F 4 .   ? 16.298  24.497 55.540 1.00 23.60 ? 405 EDO A O1  1 
HETATM 2427 C  C2  . EDO F 4 .   ? 17.778  24.409 53.609 1.00 31.42 ? 405 EDO A C2  1 
HETATM 2428 O  O2  . EDO F 4 .   ? 18.684  23.614 54.384 1.00 35.15 ? 405 EDO A O2  1 
HETATM 2429 P  P   . 2HP G 5 .   ? 25.710  29.821 45.865 1.00 42.91 ? 406 2HP A P   1 
HETATM 2430 O  O1  . 2HP G 5 .   ? 27.208  29.983 45.782 1.00 33.09 ? 406 2HP A O1  1 
HETATM 2431 O  O2  . 2HP G 5 .   ? 25.238  29.030 44.670 1.00 45.35 ? 406 2HP A O2  1 
HETATM 2432 O  O3  . 2HP G 5 .   ? 25.319  29.101 47.135 1.00 35.41 ? 406 2HP A O3  1 
HETATM 2433 O  O4  . 2HP G 5 .   ? 25.080  31.194 45.855 1.00 40.61 ? 406 2HP A O4  1 
HETATM 2434 C  C1  . EDO H 4 .   ? 22.049  27.835 47.635 1.00 40.00 ? 407 EDO A C1  1 
HETATM 2435 O  O1  . EDO H 4 .   ? 23.228  27.031 47.514 1.00 43.30 ? 407 EDO A O1  1 
HETATM 2436 C  C2  . EDO H 4 .   ? 21.766  28.485 46.284 1.00 35.98 ? 407 EDO A C2  1 
HETATM 2437 O  O2  . EDO H 4 .   ? 21.719  27.466 45.280 1.00 37.35 ? 407 EDO A O2  1 
HETATM 2438 C  C1  . EDO I 4 .   ? -2.986  27.811 36.349 1.00 31.12 ? 408 EDO A C1  1 
HETATM 2439 O  O1  . EDO I 4 .   ? -3.231  28.552 37.552 1.00 38.22 ? 408 EDO A O1  1 
HETATM 2440 C  C2  . EDO I 4 .   ? -1.923  26.752 36.622 1.00 30.55 ? 408 EDO A C2  1 
HETATM 2441 O  O2  . EDO I 4 .   ? -2.507  25.606 37.254 1.00 32.50 ? 408 EDO A O2  1 
HETATM 2442 C  C1  . EDO J 4 .   ? 4.349   30.684 51.419 1.00 28.98 ? 409 EDO A C1  1 
HETATM 2443 O  O1  . EDO J 4 .   ? 3.785   29.897 50.362 1.00 25.26 ? 409 EDO A O1  1 
HETATM 2444 C  C2  . EDO J 4 .   ? 3.261   31.031 52.429 1.00 35.71 ? 409 EDO A C2  1 
HETATM 2445 O  O2  . EDO J 4 .   ? 2.696   29.835 52.980 1.00 38.30 ? 409 EDO A O2  1 
HETATM 2446 O  O   . HOH K 6 .   ? 8.607   46.899 53.811 1.00 32.37 ? 501 HOH A O   1 
HETATM 2447 O  O   . HOH K 6 .   ? -0.943  41.575 54.801 1.00 28.73 ? 502 HOH A O   1 
HETATM 2448 O  O   . HOH K 6 .   ? 21.825  4.596  27.913 1.00 34.10 ? 503 HOH A O   1 
HETATM 2449 O  O   . HOH K 6 .   ? -5.444  28.447 38.626 1.00 37.97 ? 504 HOH A O   1 
HETATM 2450 O  O   . HOH K 6 .   ? 23.786  30.766 48.685 1.00 31.52 ? 505 HOH A O   1 
HETATM 2451 O  O   . HOH K 6 .   ? 5.201   37.507 29.491 1.00 34.54 ? 506 HOH A O   1 
HETATM 2452 O  O   . HOH K 6 .   ? -15.058 36.144 57.719 1.00 35.19 ? 507 HOH A O   1 
HETATM 2453 O  O   . HOH K 6 .   ? -19.189 41.081 45.440 1.00 35.84 ? 508 HOH A O   1 
HETATM 2454 O  O   . HOH K 6 .   ? -9.828  32.935 37.234 1.00 42.80 ? 509 HOH A O   1 
HETATM 2455 O  O   . HOH K 6 .   ? 10.150  20.414 52.677 1.00 20.55 ? 510 HOH A O   1 
HETATM 2456 O  O   . HOH K 6 .   ? 23.014  11.878 43.446 1.00 26.44 ? 511 HOH A O   1 
HETATM 2457 O  O   . HOH K 6 .   ? 8.736   4.176  50.330 1.00 27.66 ? 512 HOH A O   1 
HETATM 2458 O  O   . HOH K 6 .   ? 16.343  2.258  35.959 1.00 42.36 ? 513 HOH A O   1 
HETATM 2459 O  O   . HOH K 6 .   ? -5.584  17.923 41.426 1.00 39.74 ? 514 HOH A O   1 
HETATM 2460 O  O   . HOH K 6 .   ? -3.847  44.799 60.970 1.00 30.99 ? 515 HOH A O   1 
HETATM 2461 O  O   . HOH K 6 .   ? 18.830  34.907 40.887 1.00 32.51 ? 516 HOH A O   1 
HETATM 2462 O  O   . HOH K 6 .   ? 24.577  20.782 42.959 1.00 40.07 ? 517 HOH A O   1 
HETATM 2463 O  O   . HOH K 6 .   ? 8.602   17.017 61.752 1.00 24.49 ? 518 HOH A O   1 
HETATM 2464 O  O   . HOH K 6 .   ? 5.794   27.182 27.554 1.00 28.23 ? 519 HOH A O   1 
HETATM 2465 O  O   . HOH K 6 .   ? 11.707  5.175  39.924 1.00 29.60 ? 520 HOH A O   1 
HETATM 2466 O  O   . HOH K 6 .   ? 4.810   52.159 44.889 1.00 35.97 ? 521 HOH A O   1 
HETATM 2467 O  O   . HOH K 6 .   ? 21.237  7.674  33.929 1.00 30.48 ? 522 HOH A O   1 
HETATM 2468 O  O   . HOH K 6 .   ? 18.691  22.921 40.769 1.00 29.61 ? 523 HOH A O   1 
HETATM 2469 O  O   . HOH K 6 .   ? -3.387  33.869 39.172 1.00 29.04 ? 524 HOH A O   1 
HETATM 2470 O  O   . HOH K 6 .   ? -15.417 41.977 42.884 1.00 32.61 ? 525 HOH A O   1 
HETATM 2471 O  O   . HOH K 6 .   ? 12.780  8.441  52.118 1.00 31.03 ? 526 HOH A O   1 
HETATM 2472 O  O   . HOH K 6 .   ? -13.697 33.422 45.139 1.00 27.26 ? 527 HOH A O   1 
HETATM 2473 O  O   . HOH K 6 .   ? 26.307  31.987 41.089 1.00 42.87 ? 528 HOH A O   1 
HETATM 2474 O  O   . HOH K 6 .   ? 13.346  12.793 30.871 1.00 40.11 ? 529 HOH A O   1 
HETATM 2475 O  O   . HOH K 6 .   ? 4.681   37.350 47.709 1.00 24.89 ? 530 HOH A O   1 
HETATM 2476 O  O   . HOH K 6 .   ? 7.140   23.274 68.050 1.00 35.56 ? 531 HOH A O   1 
HETATM 2477 O  O   . HOH K 6 .   ? -11.364 32.109 42.230 1.00 36.42 ? 532 HOH A O   1 
HETATM 2478 O  O   . HOH K 6 .   ? 4.905   21.017 27.709 1.00 39.06 ? 533 HOH A O   1 
HETATM 2479 O  O   . HOH K 6 .   ? 15.514  51.171 49.724 1.00 27.73 ? 534 HOH A O   1 
HETATM 2480 O  O   . HOH K 6 .   ? -5.903  51.433 49.355 1.00 32.28 ? 535 HOH A O   1 
HETATM 2481 O  O   . HOH K 6 .   ? 6.125   16.104 55.594 1.00 25.64 ? 536 HOH A O   1 
HETATM 2482 O  O   . HOH K 6 .   ? -15.123 27.996 54.551 1.00 33.87 ? 537 HOH A O   1 
HETATM 2483 O  O   . HOH K 6 .   ? -4.732  26.727 48.847 1.00 38.07 ? 538 HOH A O   1 
HETATM 2484 O  O   . HOH K 6 .   ? 17.842  15.988 48.186 1.00 22.87 ? 539 HOH A O   1 
HETATM 2485 O  O   . HOH K 6 .   ? 2.295   13.163 50.106 1.00 31.21 ? 540 HOH A O   1 
HETATM 2486 O  O   . HOH K 6 .   ? 19.137  18.134 53.002 1.00 35.72 ? 541 HOH A O   1 
HETATM 2487 O  O   . HOH K 6 .   ? 13.565  30.994 55.617 1.00 26.55 ? 542 HOH A O   1 
HETATM 2488 O  O   . HOH K 6 .   ? -1.301  25.565 47.027 1.00 24.67 ? 543 HOH A O   1 
HETATM 2489 O  O   . HOH K 6 .   ? 14.073  23.902 40.796 1.00 23.62 ? 544 HOH A O   1 
HETATM 2490 O  O   . HOH K 6 .   ? 5.913   8.992  56.673 1.00 31.05 ? 545 HOH A O   1 
HETATM 2491 O  O   . HOH K 6 .   ? 2.816   52.862 41.038 1.00 36.28 ? 546 HOH A O   1 
HETATM 2492 O  O   . HOH K 6 .   ? 18.493  10.507 42.594 1.00 27.65 ? 547 HOH A O   1 
HETATM 2493 O  O   . HOH K 6 .   ? 9.982   21.230 29.056 1.00 34.93 ? 548 HOH A O   1 
HETATM 2494 O  O   . HOH K 6 .   ? -4.996  33.383 32.112 1.00 29.32 ? 549 HOH A O   1 
HETATM 2495 O  O   . HOH K 6 .   ? -1.369  40.326 52.342 1.00 26.25 ? 550 HOH A O   1 
HETATM 2496 O  O   . HOH K 6 .   ? 13.518  19.106 33.254 1.00 29.11 ? 551 HOH A O   1 
HETATM 2497 O  O   . HOH K 6 .   ? 17.121  17.397 33.211 1.00 26.69 ? 552 HOH A O   1 
HETATM 2498 O  O   . HOH K 6 .   ? -5.019  39.273 56.363 1.00 30.49 ? 553 HOH A O   1 
HETATM 2499 O  O   . HOH K 6 .   ? 24.871  16.110 49.072 1.00 28.09 ? 554 HOH A O   1 
HETATM 2500 O  O   . HOH K 6 .   ? 11.641  18.975 45.212 1.00 23.88 ? 555 HOH A O   1 
HETATM 2501 O  O   . HOH K 6 .   ? -0.159  39.445 42.939 1.00 23.62 ? 556 HOH A O   1 
HETATM 2502 O  O   . HOH K 6 .   ? 0.524   36.445 28.146 1.00 36.48 ? 557 HOH A O   1 
HETATM 2503 O  O   . HOH K 6 .   ? 18.080  20.570 46.497 1.00 32.12 ? 558 HOH A O   1 
HETATM 2504 O  O   . HOH K 6 .   ? -3.775  51.664 56.629 1.00 32.52 ? 559 HOH A O   1 
HETATM 2505 O  O   . HOH K 6 .   ? 13.604  54.389 52.277 1.00 30.06 ? 560 HOH A O   1 
HETATM 2506 O  O   . HOH K 6 .   ? -3.228  40.999 41.097 1.00 25.13 ? 561 HOH A O   1 
HETATM 2507 O  O   . HOH K 6 .   ? -1.170  46.260 45.936 1.00 22.49 ? 562 HOH A O   1 
HETATM 2508 O  O   . HOH K 6 .   ? -6.362  46.724 35.373 1.00 46.24 ? 563 HOH A O   1 
HETATM 2509 O  O   . HOH K 6 .   ? -1.723  44.040 58.641 1.00 33.78 ? 564 HOH A O   1 
HETATM 2510 O  O   . HOH K 6 .   ? 23.134  33.287 47.381 1.00 25.72 ? 565 HOH A O   1 
HETATM 2511 O  O   . HOH K 6 .   ? 0.572   23.379 46.700 1.00 21.98 ? 566 HOH A O   1 
HETATM 2512 O  O   . HOH K 6 .   ? 19.982  40.595 42.679 1.00 32.32 ? 567 HOH A O   1 
HETATM 2513 O  O   . HOH K 6 .   ? -7.206  39.069 41.082 1.00 35.30 ? 568 HOH A O   1 
HETATM 2514 O  O   . HOH K 6 .   ? 1.751   24.190 62.528 1.00 26.43 ? 569 HOH A O   1 
HETATM 2515 O  O   . HOH K 6 .   ? 21.055  29.184 38.316 1.00 30.30 ? 570 HOH A O   1 
HETATM 2516 O  O   . HOH K 6 .   ? 6.546   24.774 64.945 1.00 26.63 ? 571 HOH A O   1 
HETATM 2517 O  O   . HOH K 6 .   ? -14.062 37.259 52.794 1.00 31.81 ? 572 HOH A O   1 
HETATM 2518 O  O   . HOH K 6 .   ? 27.338  12.795 47.403 1.00 40.26 ? 573 HOH A O   1 
HETATM 2519 O  O   . HOH K 6 .   ? 17.350  38.083 33.384 1.00 27.71 ? 574 HOH A O   1 
HETATM 2520 O  O   . HOH K 6 .   ? 7.273   38.505 47.541 1.00 26.58 ? 575 HOH A O   1 
HETATM 2521 O  O   . HOH K 6 .   ? 18.263  13.105 33.240 1.00 27.77 ? 576 HOH A O   1 
HETATM 2522 O  O   . HOH K 6 .   ? 7.318   5.886  68.337 1.00 35.50 ? 577 HOH A O   1 
HETATM 2523 O  O   . HOH K 6 .   ? 7.234   22.346 53.843 1.00 22.32 ? 578 HOH A O   1 
HETATM 2524 O  O   . HOH K 6 .   ? 17.320  48.118 48.984 1.00 36.97 ? 579 HOH A O   1 
HETATM 2525 O  O   . HOH K 6 .   ? 2.870   6.128  44.275 1.00 35.84 ? 580 HOH A O   1 
HETATM 2526 O  O   . HOH K 6 .   ? 2.405   12.447 47.585 1.00 33.35 ? 581 HOH A O   1 
HETATM 2527 O  O   . HOH K 6 .   ? 10.965  39.579 25.935 1.00 32.64 ? 582 HOH A O   1 
HETATM 2528 O  O   . HOH K 6 .   ? 3.966   7.985  45.984 1.00 37.88 ? 583 HOH A O   1 
HETATM 2529 O  O   . HOH K 6 .   ? 22.915  9.165  43.558 1.00 34.60 ? 584 HOH A O   1 
HETATM 2530 O  O   . HOH K 6 .   ? 17.674  11.789 55.832 1.00 36.38 ? 585 HOH A O   1 
HETATM 2531 O  O   . HOH K 6 .   ? 22.116  4.555  50.343 1.00 39.36 ? 586 HOH A O   1 
HETATM 2532 O  O   . HOH K 6 .   ? 17.523  35.375 38.924 1.00 28.13 ? 587 HOH A O   1 
HETATM 2533 O  O   . HOH K 6 .   ? -15.302 35.239 46.195 1.00 23.88 ? 588 HOH A O   1 
HETATM 2534 O  O   . HOH K 6 .   ? 24.266  30.276 41.591 1.00 33.45 ? 589 HOH A O   1 
HETATM 2535 O  O   . HOH K 6 .   ? 1.005   43.673 57.883 1.00 34.77 ? 590 HOH A O   1 
HETATM 2536 O  O   . HOH K 6 .   ? 4.780   27.393 58.024 1.00 27.53 ? 591 HOH A O   1 
HETATM 2537 O  O   . HOH K 6 .   ? 7.958   16.386 64.588 1.00 32.91 ? 592 HOH A O   1 
HETATM 2538 O  O   . HOH K 6 .   ? 0.043   12.705 57.257 1.00 36.46 ? 593 HOH A O   1 
HETATM 2539 O  O   . HOH K 6 .   ? -3.062  12.434 35.857 1.00 37.78 ? 594 HOH A O   1 
HETATM 2540 O  O   . HOH K 6 .   ? 16.818  37.085 48.509 1.00 31.70 ? 595 HOH A O   1 
HETATM 2541 O  O   . HOH K 6 .   ? 3.896   1.367  40.396 1.00 42.77 ? 596 HOH A O   1 
HETATM 2542 O  O   . HOH K 6 .   ? 3.796   33.207 28.467 1.00 32.37 ? 597 HOH A O   1 
HETATM 2543 O  O   . HOH K 6 .   ? 18.034  23.514 29.660 1.00 33.84 ? 598 HOH A O   1 
HETATM 2544 O  O   . HOH K 6 .   ? -5.739  30.879 38.770 1.00 35.21 ? 599 HOH A O   1 
HETATM 2545 O  O   . HOH K 6 .   ? -10.132 36.013 41.307 1.00 32.25 ? 600 HOH A O   1 
HETATM 2546 O  O   . HOH K 6 .   ? 17.426  3.793  48.142 1.00 36.13 ? 601 HOH A O   1 
HETATM 2547 O  O   . HOH K 6 .   ? 5.911   29.759 58.345 1.00 36.60 ? 602 HOH A O   1 
HETATM 2548 O  O   . HOH K 6 .   ? 15.843  1.894  50.569 1.00 40.87 ? 603 HOH A O   1 
HETATM 2549 O  O   . HOH K 6 .   ? 0.577   40.753 40.438 1.00 26.21 ? 604 HOH A O   1 
HETATM 2550 O  O   . HOH K 6 .   ? 17.918  35.602 26.289 1.00 39.57 ? 605 HOH A O   1 
HETATM 2551 O  O   . HOH K 6 .   ? -7.384  26.446 58.088 1.00 34.36 ? 606 HOH A O   1 
HETATM 2552 O  O   . HOH K 6 .   ? 14.165  51.361 38.408 1.00 40.48 ? 607 HOH A O   1 
HETATM 2553 O  O   . HOH K 6 .   ? -14.462 31.672 56.832 1.00 27.60 ? 608 HOH A O   1 
HETATM 2554 O  O   . HOH K 6 .   ? 4.782   4.330  44.106 1.00 39.75 ? 609 HOH A O   1 
HETATM 2555 O  O   . HOH K 6 .   ? -3.119  20.988 52.944 1.00 39.19 ? 610 HOH A O   1 
HETATM 2556 O  O   . HOH K 6 .   ? 7.883   7.194  57.007 1.00 29.71 ? 611 HOH A O   1 
HETATM 2557 O  O   . HOH K 6 .   ? 9.505   19.155 63.725 1.00 32.19 ? 612 HOH A O   1 
HETATM 2558 O  O   . HOH K 6 .   ? 16.211  22.970 39.301 1.00 30.17 ? 613 HOH A O   1 
HETATM 2559 O  O   . HOH K 6 .   ? 23.225  24.152 48.930 1.00 37.37 ? 614 HOH A O   1 
HETATM 2560 O  O   . HOH K 6 .   ? 14.932  2.238  46.339 1.00 41.10 ? 615 HOH A O   1 
HETATM 2561 O  O   . HOH K 6 .   ? 21.561  22.799 40.940 1.00 40.17 ? 616 HOH A O   1 
HETATM 2562 O  O   . HOH K 6 .   ? 3.869   4.029  33.459 1.00 41.08 ? 617 HOH A O   1 
HETATM 2563 O  O   . HOH K 6 .   ? 11.792  20.395 62.118 1.00 30.08 ? 618 HOH A O   1 
HETATM 2564 O  O   . HOH K 6 .   ? 20.275  8.690  43.184 1.00 28.65 ? 619 HOH A O   1 
HETATM 2565 O  O   . HOH K 6 .   ? -2.173  14.497 51.734 1.00 38.47 ? 620 HOH A O   1 
HETATM 2566 O  O   . HOH K 6 .   ? -17.705 43.903 53.124 1.00 34.03 ? 621 HOH A O   1 
HETATM 2567 O  O   . HOH K 6 .   ? 11.823  23.229 38.832 1.00 32.23 ? 622 HOH A O   1 
HETATM 2568 O  O   . HOH K 6 .   ? -1.672  19.977 53.969 1.00 41.62 ? 623 HOH A O   1 
HETATM 2569 O  O   . HOH K 6 .   ? -3.365  13.966 50.152 1.00 39.10 ? 624 HOH A O   1 
HETATM 2570 O  O   . HOH K 6 .   ? 19.641  4.176  50.604 1.00 40.01 ? 625 HOH A O   1 
HETATM 2571 O  O   . HOH K 6 .   ? -10.389 53.223 61.330 1.00 37.67 ? 626 HOH A O   1 
HETATM 2572 O  O   . HOH K 6 .   ? 3.334   47.215 50.147 1.00 35.44 ? 627 HOH A O   1 
HETATM 2573 O  O   . HOH K 6 .   ? 14.908  16.985 32.605 1.00 41.30 ? 628 HOH A O   1 
HETATM 2574 O  O   . HOH K 6 .   ? -13.035 29.296 56.305 1.00 38.63 ? 629 HOH A O   1 
HETATM 2575 O  O   . HOH K 6 .   ? 18.098  3.034  52.108 1.00 42.72 ? 630 HOH A O   1 
HETATM 2576 O  O   . HOH K 6 .   ? 17.745  49.831 50.601 1.00 35.09 ? 631 HOH A O   1 
HETATM 2577 O  O   . HOH K 6 .   ? 11.759  53.283 47.724 1.00 41.20 ? 632 HOH A O   1 
HETATM 2578 O  O   . HOH K 6 .   ? -10.303 26.755 57.952 1.00 30.87 ? 633 HOH A O   1 
HETATM 2579 O  O   . HOH K 6 .   ? 12.276  36.666 58.741 1.00 42.29 ? 634 HOH A O   1 
HETATM 2580 O  O   . HOH K 6 .   ? 0.339   5.583  44.809 1.00 44.50 ? 635 HOH A O   1 
HETATM 2581 O  O   . HOH K 6 .   ? -7.660  27.757 38.049 1.00 41.52 ? 636 HOH A O   1 
HETATM 2582 O  O   . HOH K 6 .   ? 7.612   1.838  50.946 1.00 41.42 ? 637 HOH A O   1 
HETATM 2583 O  O   . HOH K 6 .   ? -6.284  53.849 50.428 1.00 42.68 ? 638 HOH A O   1 
HETATM 2584 O  O   . HOH K 6 .   ? 4.506   35.109 27.788 1.00 38.38 ? 639 HOH A O   1 
HETATM 2585 O  O   . HOH K 6 .   ? -9.602  38.943 40.334 1.00 39.70 ? 640 HOH A O   1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1    N N   . GLN A 2   ? 0.6810 0.6502 0.6954 0.0002  0.0407  0.0130  1   GLN A N   
2    C CA  . GLN A 2   ? 0.4650 0.4379 0.4734 0.0041  0.0424  0.0077  1   GLN A CA  
3    C C   . GLN A 2   ? 0.4475 0.4182 0.4493 0.0046  0.0397  0.0022  1   GLN A C   
4    O O   . GLN A 2   ? 0.4680 0.4391 0.4649 0.0073  0.0403  -0.0035 1   GLN A O   
5    C CB  . GLN A 2   ? 0.4784 0.4479 0.4899 0.0057  0.0438  0.0037  1   GLN A CB  
6    C CG  . GLN A 2   ? 0.5626 0.5221 0.5781 0.0036  0.0409  0.0000  1   GLN A CG  
7    C CD  . GLN A 2   ? 0.6864 0.6424 0.7028 0.0059  0.0422  -0.0055 1   GLN A CD  
8    O OE1 . GLN A 2   ? 0.7822 0.7393 0.8033 0.0066  0.0445  -0.0036 1   GLN A OE1 
9    N NE2 . GLN A 2   ? 0.6687 0.6207 0.6806 0.0072  0.0407  -0.0125 1   GLN A NE2 
10   N N   . LEU A 3   ? 0.3750 0.3432 0.3769 0.0019  0.0367  0.0041  2   LEU A N   
11   C CA  . LEU A 3   ? 0.3532 0.3211 0.3486 0.0022  0.0342  0.0001  2   LEU A CA  
12   C C   . LEU A 3   ? 0.3872 0.3643 0.3756 0.0048  0.0362  0.0012  2   LEU A C   
13   O O   . LEU A 3   ? 0.3689 0.3524 0.3581 0.0051  0.0386  0.0071  2   LEU A O   
14   C CB  . LEU A 3   ? 0.3330 0.2970 0.3303 -0.0011 0.0309  0.0028  2   LEU A CB  
15   C CG  . LEU A 3   ? 0.2854 0.2399 0.2894 -0.0039 0.0288  0.0022  2   LEU A CG  
16   C CD1 . LEU A 3   ? 0.3618 0.3133 0.3668 -0.0068 0.0258  0.0053  2   LEU A CD1 
17   C CD2 . LEU A 3   ? 0.3132 0.2614 0.3167 -0.0028 0.0276  -0.0055 2   LEU A CD2 
18   N N   . THR A 4   ? 0.3292 0.3068 0.3105 0.0067  0.0351  -0.0047 3   THR A N   
19   C CA  . THR A 4   ? 0.3371 0.3228 0.3108 0.0095  0.0368  -0.0046 3   THR A CA  
20   C C   . THR A 4   ? 0.3242 0.3097 0.2911 0.0093  0.0337  -0.0083 3   THR A C   
21   O O   . THR A 4   ? 0.3298 0.3088 0.2963 0.0084  0.0309  -0.0139 3   THR A O   
22   C CB  . THR A 4   ? 0.4016 0.3894 0.3722 0.0132  0.0400  -0.0085 3   THR A CB  
23   O OG1 . THR A 4   ? 0.4554 0.4504 0.4177 0.0159  0.0414  -0.0091 3   THR A OG1 
24   C CG2 . THR A 4   ? 0.4019 0.3822 0.3717 0.0136  0.0384  -0.0165 3   THR A CG2 
25   N N   . PRO A 5   ? 0.3206 0.3133 0.2822 0.0101  0.0340  -0.0053 4   PRO A N   
26   C CA  . PRO A 5   ? 0.3426 0.3356 0.2977 0.0098  0.0307  -0.0088 4   PRO A CA  
27   C C   . PRO A 5   ? 0.3247 0.3166 0.2728 0.0123  0.0305  -0.0167 4   PRO A C   
28   O O   . PRO A 5   ? 0.3832 0.3734 0.3266 0.0117  0.0273  -0.0208 4   PRO A O   
29   C CB  . PRO A 5   ? 0.4095 0.4113 0.3607 0.0105  0.0318  -0.0031 4   PRO A CB  
30   C CG  . PRO A 5   ? 0.4873 0.4922 0.4445 0.0102  0.0350  0.0040  4   PRO A CG  
31   C CD  . PRO A 5   ? 0.3902 0.3911 0.3517 0.0111  0.0371  0.0015  4   PRO A CD  
32   N N   . THR A 6   ? 0.3389 0.3317 0.2861 0.0152  0.0339  -0.0189 5   THR A N   
33   C CA  . THR A 6   ? 0.3618 0.3539 0.3015 0.0180  0.0344  -0.0262 5   THR A CA  
34   C C   . THR A 6   ? 0.3762 0.3595 0.3186 0.0175  0.0332  -0.0326 5   THR A C   
35   O O   . THR A 6   ? 0.3707 0.3525 0.3077 0.0200  0.0341  -0.0387 5   THR A O   
36   C CB  . THR A 6   ? 0.4168 0.4153 0.3534 0.0218  0.0391  -0.0247 5   THR A CB  
37   O OG1 . THR A 6   ? 0.4378 0.4353 0.3823 0.0218  0.0418  -0.0214 5   THR A OG1 
38   C CG2 . THR A 6   ? 0.4144 0.4218 0.3471 0.0226  0.0402  -0.0191 5   THR A CG2 
39   N N   . PHE A 7   ? 0.3662 0.3434 0.3166 0.0145  0.0313  -0.0313 6   PHE A N   
40   C CA  . PHE A 7   ? 0.3175 0.2865 0.2717 0.0144  0.0310  -0.0363 6   PHE A CA  
41   C C   . PHE A 7   ? 0.3836 0.3482 0.3316 0.0151  0.0289  -0.0447 6   PHE A C   
42   O O   . PHE A 7   ? 0.3776 0.3381 0.3250 0.0168  0.0303  -0.0499 6   PHE A O   
43   C CB  . PHE A 7   ? 0.3072 0.2702 0.2702 0.0108  0.0288  -0.0335 6   PHE A CB  
44   C CG  . PHE A 7   ? 0.3580 0.3131 0.3260 0.0107  0.0290  -0.0376 6   PHE A CG  
45   C CD1 . PHE A 7   ? 0.3105 0.2659 0.2834 0.0119  0.0323  -0.0355 6   PHE A CD1 
46   C CD2 . PHE A 7   ? 0.3211 0.2687 0.2890 0.0094  0.0258  -0.0435 6   PHE A CD2 
47   C CE1 . PHE A 7   ? 0.3364 0.2848 0.3138 0.0119  0.0325  -0.0391 6   PHE A CE1 
48   C CE2 . PHE A 7   ? 0.3418 0.2821 0.3142 0.0094  0.0262  -0.0471 6   PHE A CE2 
49   C CZ  . PHE A 7   ? 0.3576 0.2983 0.3347 0.0107  0.0295  -0.0449 6   PHE A CZ  
50   N N   . TYR A 8   ? 0.3389 0.3041 0.2823 0.0137  0.0254  -0.0462 7   TYR A N   
51   C CA  . TYR A 8   ? 0.3415 0.3023 0.2791 0.0139  0.0230  -0.0540 7   TYR A CA  
52   C C   . TYR A 8   ? 0.3838 0.3503 0.3109 0.0167  0.0239  -0.0569 7   TYR A C   
53   O O   . TYR A 8   ? 0.3996 0.3634 0.3208 0.0166  0.0215  -0.0631 7   TYR A O   
54   C CB  . TYR A 8   ? 0.3457 0.3027 0.2853 0.0104  0.0181  -0.0546 7   TYR A CB  
55   C CG  . TYR A 8   ? 0.3247 0.2748 0.2740 0.0078  0.0171  -0.0527 7   TYR A CG  
56   C CD1 . TYR A 8   ? 0.3549 0.2975 0.3075 0.0081  0.0174  -0.0576 7   TYR A CD1 
57   C CD2 . TYR A 8   ? 0.3393 0.2904 0.2942 0.0052  0.0159  -0.0461 7   TYR A CD2 
58   C CE1 . TYR A 8   ? 0.3366 0.2729 0.2978 0.0059  0.0165  -0.0559 7   TYR A CE1 
59   C CE2 . TYR A 8   ? 0.3234 0.2680 0.2867 0.0030  0.0150  -0.0444 7   TYR A CE2 
60   C CZ  . TYR A 8   ? 0.3185 0.2557 0.2849 0.0033  0.0153  -0.0493 7   TYR A CZ  
61   O OH  . TYR A 8   ? 0.3362 0.2668 0.3108 0.0012  0.0144  -0.0477 7   TYR A OH  
62   N N   . ASP A 9   ? 0.3866 0.3608 0.3112 0.0190  0.0273  -0.0526 8   ASP A N   
63   C CA  . ASP A 9   ? 0.4234 0.4032 0.3376 0.0215  0.0279  -0.0547 8   ASP A CA  
64   C C   . ASP A 9   ? 0.4522 0.4280 0.3600 0.0240  0.0288  -0.0629 8   ASP A C   
65   O O   . ASP A 9   ? 0.5034 0.4808 0.4021 0.0250  0.0275  -0.0669 8   ASP A O   
66   C CB  . ASP A 9   ? 0.4560 0.4445 0.3693 0.0238  0.0318  -0.0483 8   ASP A CB  
67   C CG  . ASP A 9   ? 0.4959 0.4895 0.4120 0.0216  0.0304  -0.0410 8   ASP A CG  
68   O OD1 . ASP A 9   ? 0.5172 0.5080 0.4354 0.0185  0.0264  -0.0410 8   ASP A OD1 
69   O OD2 . ASP A 9   ? 0.5322 0.5326 0.4486 0.0230  0.0335  -0.0351 8   ASP A OD2 
70   N N   . ASN A 10  ? 0.4495 0.4198 0.3616 0.0248  0.0308  -0.0654 9   ASN A N   
71   C CA  . ASN A 10  ? 0.4694 0.4350 0.3758 0.0270  0.0317  -0.0734 9   ASN A CA  
72   C C   . ASN A 10  ? 0.4641 0.4209 0.3723 0.0244  0.0278  -0.0793 9   ASN A C   
73   O O   . ASN A 10  ? 0.5505 0.5042 0.4515 0.0250  0.0263  -0.0861 9   ASN A O   
74   C CB  . ASN A 10  ? 0.4721 0.4370 0.3812 0.0300  0.0366  -0.0731 9   ASN A CB  
75   C CG  . ASN A 10  ? 0.4604 0.4338 0.3659 0.0333  0.0407  -0.0687 9   ASN A CG  
76   O OD1 . ASN A 10  ? 0.4783 0.4563 0.3749 0.0349  0.0408  -0.0697 9   ASN A OD1 
77   N ND2 . ASN A 10  ? 0.4759 0.4515 0.3881 0.0343  0.0442  -0.0638 9   ASN A ND2 
78   N N   . SER A 11  ? 0.4462 0.3987 0.3638 0.0215  0.0260  -0.0768 10  SER A N   
79   C CA  . SER A 11  ? 0.4363 0.3798 0.3569 0.0194  0.0231  -0.0821 10  SER A CA  
80   C C   . SER A 11  ? 0.4838 0.4260 0.4034 0.0161  0.0179  -0.0832 10  SER A C   
81   O O   . SER A 11  ? 0.4671 0.4026 0.3860 0.0148  0.0153  -0.0891 10  SER A O   
82   C CB  . SER A 11  ? 0.4225 0.3616 0.3538 0.0181  0.0240  -0.0791 10  SER A CB  
83   O OG  . SER A 11  ? 0.4234 0.3666 0.3605 0.0161  0.0234  -0.0713 10  SER A OG  
84   N N   . CYS A 12  ? 0.4402 0.3884 0.3599 0.0146  0.0164  -0.0775 11  CYS A N   
85   C CA  . CYS A 12  ? 0.4321 0.3797 0.3506 0.0116  0.0116  -0.0781 11  CYS A CA  
86   C C   . CYS A 12  ? 0.4040 0.3606 0.3190 0.0116  0.0113  -0.0724 11  CYS A C   
87   O O   . CYS A 12  ? 0.4214 0.3799 0.3418 0.0094  0.0099  -0.0664 11  CYS A O   
88   C CB  . CYS A 12  ? 0.4447 0.3863 0.3727 0.0083  0.0090  -0.0762 11  CYS A CB  
89   S SG  . CYS A 12  ? 0.4866 0.4247 0.4131 0.0049  0.0030  -0.0798 11  CYS A SG  
90   N N   . PRO A 13  ? 0.3880 0.3502 0.2940 0.0143  0.0128  -0.0739 12  PRO A N   
91   C CA  . PRO A 13  ? 0.4629 0.4342 0.3658 0.0148  0.0134  -0.0678 12  PRO A CA  
92   C C   . PRO A 13  ? 0.4666 0.4398 0.3688 0.0119  0.0089  -0.0659 12  PRO A C   
93   O O   . PRO A 13  ? 0.5112 0.4908 0.4144 0.0115  0.0091  -0.0593 12  PRO A O   
94   C CB  . PRO A 13  ? 0.4631 0.4386 0.3556 0.0184  0.0158  -0.0712 12  PRO A CB  
95   C CG  . PRO A 13  ? 0.5629 0.5311 0.4514 0.0189  0.0148  -0.0801 12  PRO A CG  
96   C CD  . PRO A 13  ? 0.5138 0.4741 0.4119 0.0171  0.0145  -0.0809 12  PRO A CD  
97   N N   . ASN A 14  ? 0.4426 0.4107 0.3436 0.0098  0.0048  -0.0713 13  ASN A N   
98   C CA  . ASN A 14  ? 0.5083 0.4784 0.4086 0.0071  0.0004  -0.0697 13  ASN A CA  
99   C C   . ASN A 14  ? 0.4979 0.4637 0.4082 0.0038  -0.0018 -0.0660 13  ASN A C   
100  O O   . ASN A 14  ? 0.4665 0.4323 0.3772 0.0013  -0.0058 -0.0656 13  ASN A O   
101  C CB  . ASN A 14  ? 0.5488 0.5162 0.4420 0.0065  -0.0031 -0.0774 13  ASN A CB  
102  C CG  . ASN A 14  ? 0.7667 0.7378 0.6492 0.0097  -0.0013 -0.0815 13  ASN A CG  
103  O OD1 . ASN A 14  ? 0.8962 0.8625 0.7741 0.0106  -0.0013 -0.0887 13  ASN A OD1 
104  N ND2 . ASN A 14  ? 0.6616 0.6411 0.5397 0.0114  0.0005  -0.0767 13  ASN A ND2 
105  N N   . VAL A 15  ? 0.4025 0.3646 0.3207 0.0037  0.0007  -0.0633 14  VAL A N   
106  C CA  . VAL A 15  ? 0.4059 0.3628 0.3332 0.0007  -0.0014 -0.0605 14  VAL A CA  
107  C C   . VAL A 15  ? 0.4205 0.3826 0.3492 -0.0012 -0.0032 -0.0537 14  VAL A C   
108  O O   . VAL A 15  ? 0.3559 0.3151 0.2878 -0.0039 -0.0068 -0.0532 14  VAL A O   
109  C CB  . VAL A 15  ? 0.3886 0.3414 0.3237 0.0011  0.0019  -0.0580 14  VAL A CB  
110  C CG1 . VAL A 15  ? 0.4245 0.3842 0.3599 0.0029  0.0058  -0.0516 14  VAL A CG1 
111  C CG2 . VAL A 15  ? 0.4015 0.3484 0.3456 -0.0021 -0.0003 -0.0553 14  VAL A CG2 
112  N N   . SER A 16  ? 0.4250 0.3950 0.3512 0.0004  -0.0007 -0.0482 15  SER A N   
113  C CA  . SER A 16  ? 0.4130 0.3878 0.3409 -0.0013 -0.0020 -0.0412 15  SER A CA  
114  C C   . SER A 16  ? 0.4246 0.4020 0.3473 -0.0025 -0.0063 -0.0432 15  SER A C   
115  O O   . SER A 16  ? 0.3815 0.3595 0.3074 -0.0048 -0.0087 -0.0390 15  SER A O   
116  C CB  . SER A 16  ? 0.4940 0.4770 0.4197 0.0009  0.0016  -0.0353 15  SER A CB  
117  O OG  . SER A 16  ? 0.6715 0.6525 0.6038 0.0012  0.0050  -0.0316 15  SER A OG  
118  N N   . ASN A 17  ? 0.4270 0.4057 0.3414 -0.0011 -0.0072 -0.0495 16  ASN A N   
119  C CA  . ASN A 17  ? 0.3911 0.3724 0.3000 -0.0023 -0.0114 -0.0518 16  ASN A CA  
120  C C   . ASN A 17  ? 0.3537 0.3276 0.2669 -0.0053 -0.0154 -0.0555 16  ASN A C   
121  O O   . ASN A 17  ? 0.4130 0.3884 0.3264 -0.0074 -0.0191 -0.0541 16  ASN A O   
122  C CB  . ASN A 17  ? 0.4145 0.3990 0.3129 0.0001  -0.0110 -0.0576 16  ASN A CB  
123  C CG  . ASN A 17  ? 0.5438 0.5361 0.4375 0.0032  -0.0071 -0.0538 16  ASN A CG  
124  O OD1 . ASN A 17  ? 0.7284 0.7204 0.6190 0.0059  -0.0037 -0.0565 16  ASN A OD1 
125  N ND2 . ASN A 17  ? 0.5884 0.5878 0.4817 0.0029  -0.0073 -0.0472 16  ASN A ND2 
126  N N   . ILE A 18  ? 0.3824 0.3484 0.2993 -0.0053 -0.0147 -0.0603 17  ILE A N   
127  C CA  . ILE A 18  ? 0.3672 0.3255 0.2890 -0.0081 -0.0182 -0.0636 17  ILE A CA  
128  C C   . ILE A 18  ? 0.3435 0.3006 0.2739 -0.0104 -0.0192 -0.0567 17  ILE A C   
129  O O   . ILE A 18  ? 0.3932 0.3487 0.3257 -0.0129 -0.0230 -0.0565 17  ILE A O   
130  C CB  . ILE A 18  ? 0.3863 0.3364 0.3105 -0.0073 -0.0166 -0.0694 17  ILE A CB  
131  C CG1 . ILE A 18  ? 0.4345 0.3855 0.3498 -0.0049 -0.0155 -0.0763 17  ILE A CG1 
132  C CG2 . ILE A 18  ? 0.4083 0.3504 0.3384 -0.0101 -0.0199 -0.0723 17  ILE A CG2 
133  C CD1 . ILE A 18  ? 0.4779 0.4220 0.3951 -0.0033 -0.0127 -0.0811 17  ILE A CD1 
134  N N   . VAL A 19  ? 0.3322 0.2899 0.2674 -0.0097 -0.0157 -0.0510 18  VAL A N   
135  C CA  . VAL A 19  ? 0.3291 0.2854 0.2720 -0.0118 -0.0162 -0.0441 18  VAL A CA  
136  C C   . VAL A 19  ? 0.3605 0.3237 0.3008 -0.0128 -0.0185 -0.0394 18  VAL A C   
137  O O   . VAL A 19  ? 0.3594 0.3205 0.3038 -0.0152 -0.0214 -0.0372 18  VAL A O   
138  C CB  . VAL A 19  ? 0.3055 0.2620 0.2529 -0.0107 -0.0119 -0.0388 18  VAL A CB  
139  C CG1 . VAL A 19  ? 0.3377 0.2936 0.2917 -0.0127 -0.0122 -0.0311 18  VAL A CG1 
140  C CG2 . VAL A 19  ? 0.3143 0.2635 0.2654 -0.0100 -0.0101 -0.0431 18  VAL A CG2 
141  N N   . ARG A 20  ? 0.3297 0.3012 0.2633 -0.0109 -0.0170 -0.0376 19  ARG A N   
142  C CA  . ARG A 20  ? 0.3815 0.3603 0.3124 -0.0116 -0.0188 -0.0328 19  ARG A CA  
143  C C   . ARG A 20  ? 0.3621 0.3401 0.2905 -0.0134 -0.0238 -0.0369 19  ARG A C   
144  O O   . ARG A 20  ? 0.3657 0.3449 0.2969 -0.0154 -0.0263 -0.0329 19  ARG A O   
145  C CB  . ARG A 20  ? 0.3698 0.3574 0.2930 -0.0088 -0.0164 -0.0313 19  ARG A CB  
146  C CG  . ARG A 20  ? 0.4397 0.4352 0.3599 -0.0092 -0.0179 -0.0261 19  ARG A CG  
147  C CD  . ARG A 20  ? 0.4160 0.4202 0.3283 -0.0064 -0.0155 -0.0248 19  ARG A CD  
148  N NE  . ARG A 20  ? 0.5054 0.5171 0.4142 -0.0068 -0.0175 -0.0206 19  ARG A NE  
149  C CZ  . ARG A 20  ? 0.5430 0.5569 0.4467 -0.0076 -0.0215 -0.0240 19  ARG A CZ  
150  N NH1 . ARG A 20  ? 0.5629 0.5720 0.4641 -0.0083 -0.0240 -0.0320 19  ARG A NH1 
151  N NH2 . ARG A 20  ? 0.5553 0.5763 0.4563 -0.0079 -0.0231 -0.0194 19  ARG A NH2 
152  N N   . ASP A 21  ? 0.3837 0.3595 0.3070 -0.0129 -0.0252 -0.0449 20  ASP A N   
153  C CA  . ASP A 21  ? 0.3884 0.3635 0.3091 -0.0148 -0.0300 -0.0492 20  ASP A CA  
154  C C   . ASP A 21  ? 0.4228 0.3908 0.3520 -0.0177 -0.0325 -0.0486 20  ASP A C   
155  O O   . ASP A 21  ? 0.3893 0.3585 0.3191 -0.0197 -0.0364 -0.0479 20  ASP A O   
156  C CB  . ASP A 21  ? 0.4380 0.4110 0.3519 -0.0137 -0.0306 -0.0581 20  ASP A CB  
157  C CG  . ASP A 21  ? 0.5655 0.5465 0.4692 -0.0114 -0.0298 -0.0592 20  ASP A CG  
158  O OD1 . ASP A 21  ? 0.5243 0.5129 0.4265 -0.0105 -0.0286 -0.0529 20  ASP A OD1 
159  O OD2 . ASP A 21  ? 0.6094 0.5891 0.5065 -0.0103 -0.0301 -0.0663 20  ASP A OD2 
160  N N   . THR A 22  ? 0.3834 0.3439 0.3194 -0.0178 -0.0304 -0.0488 21  THR A N   
161  C CA  . THR A 22  ? 0.3645 0.3178 0.3086 -0.0203 -0.0325 -0.0481 21  THR A CA  
162  C C   . THR A 22  ? 0.3732 0.3293 0.3218 -0.0216 -0.0330 -0.0396 21  THR A C   
163  O O   . THR A 22  ? 0.4178 0.3723 0.3696 -0.0239 -0.0364 -0.0386 21  THR A O   
164  C CB  . THR A 22  ? 0.3673 0.3123 0.3173 -0.0198 -0.0298 -0.0498 21  THR A CB  
165  O OG1 . THR A 22  ? 0.4160 0.3582 0.3616 -0.0184 -0.0292 -0.0577 21  THR A OG1 
166  C CG2 . THR A 22  ? 0.4170 0.3541 0.3752 -0.0223 -0.0319 -0.0492 21  THR A CG2 
167  N N   . ILE A 23  ? 0.3192 0.2796 0.2683 -0.0203 -0.0296 -0.0334 22  ILE A N   
168  C CA  . ILE A 23  ? 0.3279 0.2907 0.2810 -0.0215 -0.0297 -0.0252 22  ILE A CA  
169  C C   . ILE A 23  ? 0.3356 0.3058 0.2841 -0.0222 -0.0329 -0.0235 22  ILE A C   
170  O O   . ILE A 23  ? 0.3850 0.3546 0.3374 -0.0241 -0.0352 -0.0197 22  ILE A O   
171  C CB  . ILE A 23  ? 0.3415 0.3075 0.2955 -0.0200 -0.0252 -0.0191 22  ILE A CB  
172  C CG1 . ILE A 23  ? 0.3666 0.3250 0.3261 -0.0197 -0.0224 -0.0201 22  ILE A CG1 
173  C CG2 . ILE A 23  ? 0.3365 0.3053 0.2939 -0.0211 -0.0252 -0.0105 22  ILE A CG2 
174  C CD1 . ILE A 23  ? 0.3716 0.3333 0.3315 -0.0180 -0.0180 -0.0153 22  ILE A CD1 
175  N N   . VAL A 24  ? 0.3612 0.3383 0.3013 -0.0206 -0.0330 -0.0263 23  VAL A N   
176  C CA  . VAL A 24  ? 0.3708 0.3554 0.3060 -0.0211 -0.0361 -0.0248 23  VAL A CA  
177  C C   . VAL A 24  ? 0.4148 0.3959 0.3518 -0.0236 -0.0409 -0.0286 23  VAL A C   
178  O O   . VAL A 24  ? 0.3885 0.3725 0.3272 -0.0252 -0.0435 -0.0245 23  VAL A O   
179  C CB  . VAL A 24  ? 0.3542 0.3460 0.2796 -0.0188 -0.0354 -0.0281 23  VAL A CB  
180  C CG1 . VAL A 24  ? 0.4040 0.4029 0.3239 -0.0196 -0.0393 -0.0279 23  VAL A CG1 
181  C CG2 . VAL A 24  ? 0.4377 0.4343 0.3616 -0.0164 -0.0308 -0.0231 23  VAL A CG2 
182  N N   . ASN A 25  ? 0.4178 0.3927 0.3544 -0.0240 -0.0421 -0.0363 24  ASN A N   
183  C CA  . ASN A 25  ? 0.4628 0.4337 0.4016 -0.0264 -0.0466 -0.0401 24  ASN A CA  
184  C C   . ASN A 25  ? 0.4736 0.4395 0.4218 -0.0284 -0.0472 -0.0349 24  ASN A C   
185  O O   . ASN A 25  ? 0.4799 0.4467 0.4302 -0.0304 -0.0508 -0.0335 24  ASN A O   
186  C CB  . ASN A 25  ? 0.4942 0.4582 0.4318 -0.0264 -0.0471 -0.0490 24  ASN A CB  
187  C CG  . ASN A 25  ? 0.6103 0.5709 0.5492 -0.0290 -0.0519 -0.0534 24  ASN A CG  
188  O OD1 . ASN A 25  ? 0.6024 0.5688 0.5373 -0.0300 -0.0553 -0.0535 24  ASN A OD1 
189  N ND2 . ASN A 25  ? 0.6510 0.6025 0.5958 -0.0300 -0.0521 -0.0569 24  ASN A ND2 
190  N N   . GLU A 26  ? 0.4459 0.4065 0.3999 -0.0278 -0.0437 -0.0320 25  GLU A N   
191  C CA  . GLU A 26  ? 0.4224 0.3775 0.3849 -0.0296 -0.0440 -0.0271 25  GLU A CA  
192  C C   . GLU A 26  ? 0.4136 0.3749 0.3770 -0.0299 -0.0441 -0.0186 25  GLU A C   
193  O O   . GLU A 26  ? 0.4475 0.4065 0.4162 -0.0317 -0.0461 -0.0151 25  GLU A O   
194  C CB  . GLU A 26  ? 0.4155 0.3635 0.3833 -0.0288 -0.0403 -0.0262 25  GLU A CB  
195  C CG  . GLU A 26  ? 0.5121 0.4527 0.4887 -0.0305 -0.0406 -0.0224 25  GLU A CG  
196  C CD  . GLU A 26  ? 0.6432 0.5777 0.6228 -0.0324 -0.0442 -0.0275 25  GLU A CD  
197  O OE1 . GLU A 26  ? 0.6366 0.5693 0.6130 -0.0321 -0.0453 -0.0352 25  GLU A OE1 
198  O OE2 . GLU A 26  ? 0.6102 0.5417 0.5954 -0.0340 -0.0459 -0.0238 25  GLU A OE2 
199  N N   . LEU A 27  ? 0.3710 0.3402 0.3295 -0.0282 -0.0419 -0.0150 26  LEU A N   
200  C CA  . LEU A 27  ? 0.3502 0.3253 0.3092 -0.0284 -0.0418 -0.0069 26  LEU A CA  
201  C C   . LEU A 27  ? 0.4397 0.4195 0.3968 -0.0299 -0.0462 -0.0069 26  LEU A C   
202  O O   . LEU A 27  ? 0.4765 0.4588 0.4366 -0.0307 -0.0469 -0.0003 26  LEU A O   
203  C CB  . LEU A 27  ? 0.3888 0.3718 0.3422 -0.0262 -0.0385 -0.0037 26  LEU A CB  
204  C CG  . LEU A 27  ? 0.3816 0.3616 0.3384 -0.0250 -0.0338 0.0001  26  LEU A CG  
205  C CD1 . LEU A 27  ? 0.3724 0.3600 0.3227 -0.0226 -0.0310 0.0009  26  LEU A CD1 
206  C CD2 . LEU A 27  ? 0.3936 0.3720 0.3566 -0.0262 -0.0329 0.0084  26  LEU A CD2 
207  N N   . ARG A 28  ? 0.4081 0.5697 0.4272 -0.0345 -0.0105 -0.0597 27  ARG A N   
208  C CA  . ARG A 28  ? 0.4179 0.5886 0.4413 -0.0389 -0.0103 -0.0628 27  ARG A CA  
209  C C   . ARG A 28  ? 0.4555 0.6206 0.4824 -0.0430 -0.0079 -0.0641 27  ARG A C   
210  O O   . ARG A 28  ? 0.5247 0.7004 0.5597 -0.0455 -0.0083 -0.0636 27  ARG A O   
211  C CB  . ARG A 28  ? 0.3794 0.5475 0.3941 -0.0413 -0.0095 -0.0688 27  ARG A CB  
212  C CG  . ARG A 28  ? 0.5210 0.6990 0.5341 -0.0381 -0.0120 -0.0677 27  ARG A CG  
213  C CD  . ARG A 28  ? 0.4823 0.6527 0.4840 -0.0392 -0.0107 -0.0733 27  ARG A CD  
214  N NE  . ARG A 28  ? 0.6052 0.7863 0.6061 -0.0364 -0.0131 -0.0723 27  ARG A NE  
215  C CZ  . ARG A 28  ? 0.6721 0.8475 0.6637 -0.0343 -0.0129 -0.0743 27  ARG A CZ  
216  N NH1 . ARG A 28  ? 0.7301 0.8891 0.7123 -0.0344 -0.0104 -0.0775 27  ARG A NH1 
217  N NH2 . ARG A 28  ? 0.5649 0.7511 0.5567 -0.0320 -0.0151 -0.0731 27  ARG A NH2 
218  N N   . SER A 29  ? 0.4096 0.5584 0.4309 -0.0435 -0.0055 -0.0655 28  SER A N   
219  C CA  . SER A 29  ? 0.4313 0.5733 0.4550 -0.0473 -0.0030 -0.0670 28  SER A CA  
220  C C   . SER A 29  ? 0.4467 0.5838 0.4749 -0.0452 -0.0027 -0.0621 28  SER A C   
221  O O   . SER A 29  ? 0.4443 0.5806 0.4778 -0.0479 -0.0012 -0.0618 28  SER A O   
222  C CB  . SER A 29  ? 0.5098 0.6356 0.5231 -0.0506 0.0001  -0.0733 28  SER A CB  
223  O OG  . SER A 29  ? 0.6098 0.7241 0.6141 -0.0474 0.0003  -0.0734 28  SER A OG  
224  N N   . ASP A 30  ? 0.4146 0.5485 0.4408 -0.0404 -0.0041 -0.0581 29  ASP A N   
225  C CA  . ASP A 30  ? 0.3690 0.4974 0.3985 -0.0383 -0.0039 -0.0533 29  ASP A CA  
226  C C   . ASP A 30  ? 0.3684 0.5071 0.4027 -0.0332 -0.0071 -0.0471 29  ASP A C   
227  O O   . ASP A 30  ? 0.4064 0.5401 0.4352 -0.0297 -0.0081 -0.0457 29  ASP A O   
228  C CB  . ASP A 30  ? 0.4080 0.5172 0.4282 -0.0381 -0.0017 -0.0552 29  ASP A CB  
229  C CG  . ASP A 30  ? 0.4345 0.5378 0.4572 -0.0355 -0.0019 -0.0499 29  ASP A CG  
230  O OD1 . ASP A 30  ? 0.4245 0.5375 0.4564 -0.0345 -0.0032 -0.0453 29  ASP A OD1 
231  O OD2 . ASP A 30  ? 0.4286 0.5173 0.4438 -0.0344 -0.0008 -0.0505 29  ASP A OD2 
232  N N   . PRO A 31  ? 0.3474 0.5005 0.3918 -0.0328 -0.0088 -0.0433 30  PRO A N   
233  C CA  . PRO A 31  ? 0.2918 0.4554 0.3408 -0.0280 -0.0120 -0.0374 30  PRO A CA  
234  C C   . PRO A 31  ? 0.2911 0.4463 0.3393 -0.0246 -0.0122 -0.0328 30  PRO A C   
235  O O   . PRO A 31  ? 0.3515 0.5134 0.4019 -0.0205 -0.0147 -0.0281 30  PRO A O   
236  C CB  . PRO A 31  ? 0.3868 0.5661 0.4470 -0.0290 -0.0132 -0.0347 30  PRO A CB  
237  C CG  . PRO A 31  ? 0.4272 0.6012 0.4894 -0.0337 -0.0104 -0.0377 30  PRO A CG  
238  C CD  . PRO A 31  ? 0.4122 0.5733 0.4644 -0.0366 -0.0080 -0.0442 30  PRO A CD  
239  N N   . ARG A 32  ? 0.2810 0.4219 0.3260 -0.0263 -0.0098 -0.0338 31  ARG A N   
240  C CA  . ARG A 32  ? 0.3209 0.4526 0.3648 -0.0236 -0.0098 -0.0296 31  ARG A CA  
241  C C   . ARG A 32  ? 0.3089 0.4290 0.3429 -0.0213 -0.0098 -0.0307 31  ARG A C   
242  O O   . ARG A 32  ? 0.2714 0.3852 0.3041 -0.0185 -0.0104 -0.0268 31  ARG A O   
243  C CB  . ARG A 32  ? 0.2715 0.3932 0.3167 -0.0268 -0.0071 -0.0303 31  ARG A CB  
244  C CG  . ARG A 32  ? 0.3374 0.4520 0.3840 -0.0248 -0.0071 -0.0253 31  ARG A CG  
245  C CD  . ARG A 32  ? 0.3768 0.4811 0.4239 -0.0285 -0.0040 -0.0270 31  ARG A CD  
246  N NE  . ARG A 32  ? 0.3335 0.4255 0.3781 -0.0271 -0.0033 -0.0238 31  ARG A NE  
247  C CZ  . ARG A 32  ? 0.3896 0.4682 0.4314 -0.0298 -0.0005 -0.0255 31  ARG A CZ  
248  N NH1 . ARG A 32  ? 0.3604 0.4355 0.4016 -0.0341 0.0021  -0.0305 31  ARG A NH1 
249  N NH2 . ARG A 32  ? 0.4116 0.4798 0.4512 -0.0283 -0.0003 -0.0222 31  ARG A NH2 
250  N N   . ILE A 33  ? 0.2804 0.3977 0.3073 -0.0223 -0.0091 -0.0358 32  ILE A N   
251  C CA  . ILE A 33  ? 0.3332 0.4365 0.3499 -0.0208 -0.0083 -0.0376 32  ILE A CA  
252  C C   . ILE A 33  ? 0.2876 0.3941 0.3036 -0.0155 -0.0109 -0.0329 32  ILE A C   
253  O O   . ILE A 33  ? 0.2896 0.3844 0.2998 -0.0136 -0.0105 -0.0319 32  ILE A O   
254  C CB  . ILE A 33  ? 0.3472 0.4468 0.3564 -0.0232 -0.0068 -0.0443 32  ILE A CB  
255  C CG1 . ILE A 33  ? 0.3559 0.4394 0.3542 -0.0220 -0.0055 -0.0466 32  ILE A CG1 
256  C CG2 . ILE A 33  ? 0.3296 0.4437 0.3405 -0.0217 -0.0090 -0.0444 32  ILE A CG2 
257  C CD1 . ILE A 33  ? 0.3762 0.4440 0.3715 -0.0240 -0.0030 -0.0473 32  ILE A CD1 
258  N N   . ALA A 34  ? 0.2752 0.3973 0.2972 -0.0131 -0.0136 -0.0297 33  ALA A N   
259  C CA  . ALA A 34  ? 0.2447 0.3699 0.2662 -0.0081 -0.0160 -0.0250 33  ALA A CA  
260  C C   . ALA A 34  ? 0.2351 0.3550 0.2594 -0.0064 -0.0164 -0.0197 33  ALA A C   
261  O O   . ALA A 34  ? 0.2398 0.3518 0.2593 -0.0035 -0.0169 -0.0176 33  ALA A O   
262  C CB  . ALA A 34  ? 0.2739 0.4172 0.3018 -0.0061 -0.0187 -0.0224 33  ALA A CB  
263  N N   . ALA A 35  ? 0.2358 0.3595 0.2677 -0.0082 -0.0161 -0.0175 34  ALA A N   
264  C CA  . ALA A 35  ? 0.2330 0.3507 0.2671 -0.0070 -0.0163 -0.0127 34  ALA A CA  
265  C C   . ALA A 35  ? 0.2145 0.3135 0.2406 -0.0083 -0.0139 -0.0150 34  ALA A C   
266  O O   . ALA A 35  ? 0.2260 0.3176 0.2495 -0.0058 -0.0145 -0.0117 34  ALA A O   
267  C CB  . ALA A 35  ? 0.2562 0.3806 0.2994 -0.0091 -0.0159 -0.0105 34  ALA A CB  
268  N N   . SER A 36  ? 0.2494 0.3405 0.2713 -0.0122 -0.0112 -0.0209 35  SER A N   
269  C CA  . SER A 36  ? 0.2427 0.3156 0.2569 -0.0138 -0.0088 -0.0234 35  SER A CA  
270  C C   . SER A 36  ? 0.2215 0.2865 0.2271 -0.0108 -0.0093 -0.0239 35  SER A C   
271  O O   . SER A 36  ? 0.2601 0.3121 0.2608 -0.0101 -0.0086 -0.0228 35  SER A O   
272  C CB  . SER A 36  ? 0.2665 0.3337 0.2779 -0.0186 -0.0058 -0.0298 35  SER A CB  
273  O OG  . SER A 36  ? 0.2908 0.3652 0.3105 -0.0214 -0.0051 -0.0293 35  SER A OG  
274  N N   . ILE A 37  ? 0.2304 0.3027 0.2338 -0.0091 -0.0106 -0.0255 36  ILE A N   
275  C CA  . ILE A 37  ? 0.2343 0.2994 0.2294 -0.0061 -0.0110 -0.0260 36  ILE A CA  
276  C C   . ILE A 37  ? 0.2368 0.3041 0.2340 -0.0016 -0.0135 -0.0195 36  ILE A C   
277  O O   . ILE A 37  ? 0.2709 0.3272 0.2620 0.0003  -0.0133 -0.0186 36  ILE A O   
278  C CB  . ILE A 37  ? 0.2925 0.3647 0.2845 -0.0054 -0.0114 -0.0296 36  ILE A CB  
279  C CG1 . ILE A 37  ? 0.3139 0.3798 0.3012 -0.0100 -0.0086 -0.0366 36  ILE A CG1 
280  C CG2 . ILE A 37  ? 0.2879 0.3556 0.2730 -0.0013 -0.0124 -0.0285 36  ILE A CG2 
281  C CD1 . ILE A 37  ? 0.3041 0.3790 0.2900 -0.0103 -0.0090 -0.0401 36  ILE A CD1 
282  N N   . LEU A 38  ? 0.2362 0.3180 0.2420 0.0001  -0.0158 -0.0149 37  LEU A N   
283  C CA  . LEU A 38  ? 0.2208 0.3047 0.2290 0.0040  -0.0182 -0.0085 37  LEU A CA  
284  C C   . LEU A 38  ? 0.2502 0.3207 0.2567 0.0031  -0.0170 -0.0066 37  LEU A C   
285  O O   . LEU A 38  ? 0.2270 0.2902 0.2294 0.0057  -0.0178 -0.0039 37  LEU A O   
286  C CB  . LEU A 38  ? 0.2085 0.3091 0.2267 0.0053  -0.0205 -0.0039 37  LEU A CB  
287  C CG  . LEU A 38  ? 0.1827 0.2864 0.2043 0.0090  -0.0229 0.0030  37  LEU A CG  
288  C CD1 . LEU A 38  ? 0.2275 0.3291 0.2435 0.0129  -0.0243 0.0042  37  LEU A CD1 
289  C CD2 . LEU A 38  ? 0.2082 0.3287 0.2397 0.0100  -0.0250 0.0071  37  LEU A CD2 
290  N N   . ARG A 39  ? 0.2472 0.3139 0.2565 -0.0006 -0.0151 -0.0080 38  ARG A N   
291  C CA  . ARG A 39  ? 0.2273 0.2812 0.2350 -0.0017 -0.0140 -0.0062 38  ARG A CA  
292  C C   . ARG A 39  ? 0.2208 0.2579 0.2183 -0.0021 -0.0122 -0.0095 38  ARG A C   
293  O O   . ARG A 39  ? 0.2518 0.2789 0.2461 -0.0009 -0.0124 -0.0067 38  ARG A O   
294  C CB  . ARG A 39  ? 0.2376 0.2910 0.2502 -0.0057 -0.0120 -0.0074 38  ARG A CB  
295  C CG  . ARG A 39  ? 0.2508 0.2933 0.2633 -0.0065 -0.0111 -0.0044 38  ARG A CG  
296  C CD  . ARG A 39  ? 0.2504 0.2938 0.2685 -0.0101 -0.0092 -0.0052 38  ARG A CD  
297  N NE  . ARG A 39  ? 0.2617 0.2940 0.2792 -0.0110 -0.0082 -0.0025 38  ARG A NE  
298  C CZ  . ARG A 39  ? 0.2783 0.2994 0.2937 -0.0147 -0.0052 -0.0055 38  ARG A CZ  
299  N NH1 . ARG A 39  ? 0.3290 0.3485 0.3427 -0.0179 -0.0030 -0.0113 38  ARG A NH1 
300  N NH2 . ARG A 39  ? 0.2979 0.3094 0.3129 -0.0152 -0.0045 -0.0026 38  ARG A NH2 
301  N N   . LEU A 40  ? 0.2456 0.2790 0.2374 -0.0038 -0.0105 -0.0155 39  LEU A N   
302  C CA  . LEU A 40  ? 0.2792 0.2965 0.2609 -0.0041 -0.0088 -0.0189 39  LEU A CA  
303  C C   . LEU A 40  ? 0.2563 0.2718 0.2340 0.0005  -0.0108 -0.0155 39  LEU A C   
304  O O   . LEU A 40  ? 0.2615 0.2637 0.2332 0.0010  -0.0102 -0.0151 39  LEU A O   
305  C CB  . LEU A 40  ? 0.2738 0.2889 0.2502 -0.0064 -0.0068 -0.0257 39  LEU A CB  
306  C CG  . LEU A 40  ? 0.3335 0.3460 0.3108 -0.0115 -0.0041 -0.0306 39  LEU A CG  
307  C CD1 . LEU A 40  ? 0.3559 0.3659 0.3265 -0.0130 -0.0026 -0.0370 39  LEU A CD1 
308  C CD2 . LEU A 40  ? 0.3446 0.3422 0.3193 -0.0140 -0.0019 -0.0311 39  LEU A CD2 
309  N N   . HIS A 41  ? 0.2459 0.2747 0.2267 0.0037  -0.0132 -0.0133 40  HIS A N   
310  C CA  . HIS A 41  ? 0.2714 0.3001 0.2492 0.0083  -0.0152 -0.0098 40  HIS A CA  
311  C C   . HIS A 41  ? 0.2309 0.2570 0.2117 0.0098  -0.0168 -0.0036 40  HIS A C   
312  O O   . HIS A 41  ? 0.2464 0.2632 0.2219 0.0119  -0.0172 -0.0018 40  HIS A O   
313  C CB  . HIS A 41  ? 0.2554 0.3001 0.2370 0.0111  -0.0174 -0.0086 40  HIS A CB  
314  C CG  . HIS A 41  ? 0.2235 0.2702 0.2030 0.0159  -0.0196 -0.0047 40  HIS A CG  
315  N ND1 . HIS A 41  ? 0.2760 0.3116 0.2468 0.0176  -0.0188 -0.0063 40  HIS A ND1 
316  C CD2 . HIS A 41  ? 0.2866 0.3453 0.2716 0.0194  -0.0224 0.0007  40  HIS A CD2 
317  C CE1 . HIS A 41  ? 0.2981 0.3389 0.2693 0.0220  -0.0211 -0.0019 40  HIS A CE1 
318  N NE2 . HIS A 41  ? 0.2684 0.3232 0.2482 0.0231  -0.0234 0.0024  40  HIS A NE2 
319  N N   . PHE A 42  ? 0.2412 0.2755 0.2304 0.0089  -0.0176 -0.0002 41  PHE A N   
320  C CA  . PHE A 42  ? 0.2277 0.2590 0.2198 0.0098  -0.0188 0.0055  41  PHE A CA  
321  C C   . PHE A 42  ? 0.2389 0.2521 0.2248 0.0075  -0.0167 0.0041  41  PHE A C   
322  O O   . PHE A 42  ? 0.2258 0.2317 0.2087 0.0094  -0.0177 0.0075  41  PHE A O   
323  C CB  . PHE A 42  ? 0.2567 0.2997 0.2586 0.0085  -0.0195 0.0083  41  PHE A CB  
324  C CG  . PHE A 42  ? 0.2487 0.2859 0.2534 0.0074  -0.0194 0.0123  41  PHE A CG  
325  C CD1 . PHE A 42  ? 0.2686 0.2995 0.2710 0.0096  -0.0208 0.0169  41  PHE A CD1 
326  C CD2 . PHE A 42  ? 0.2876 0.3264 0.2976 0.0041  -0.0179 0.0117  41  PHE A CD2 
327  C CE1 . PHE A 42  ? 0.2878 0.3133 0.2926 0.0084  -0.0207 0.0205  41  PHE A CE1 
328  C CE2 . PHE A 42  ? 0.2806 0.3141 0.2931 0.0031  -0.0176 0.0153  41  PHE A CE2 
329  C CZ  . PHE A 42  ? 0.2752 0.3019 0.2850 0.0052  -0.0190 0.0197  41  PHE A CZ  
330  N N   . HIS A 43  ? 0.2162 0.2219 0.1998 0.0035  -0.0138 -0.0011 42  HIS A N   
331  C CA  . HIS A 43  ? 0.2514 0.2397 0.2289 0.0013  -0.0117 -0.0027 42  HIS A CA  
332  C C   . HIS A 43  ? 0.2504 0.2273 0.2182 0.0028  -0.0112 -0.0051 42  HIS A C   
333  O O   . HIS A 43  ? 0.3012 0.2644 0.2637 0.0024  -0.0105 -0.0044 42  HIS A O   
334  C CB  . HIS A 43  ? 0.2396 0.2232 0.2174 -0.0035 -0.0086 -0.0076 42  HIS A CB  
335  C CG  . HIS A 43  ? 0.2719 0.2610 0.2579 -0.0054 -0.0085 -0.0049 42  HIS A CG  
336  N ND1 . HIS A 43  ? 0.3115 0.2940 0.2980 -0.0096 -0.0057 -0.0079 42  HIS A ND1 
337  C CD2 . HIS A 43  ? 0.3223 0.3228 0.3162 -0.0036 -0.0107 0.0007  42  HIS A CD2 
338  C CE1 . HIS A 43  ? 0.3092 0.2989 0.3038 -0.0103 -0.0061 -0.0043 42  HIS A CE1 
339  N NE2 . HIS A 43  ? 0.3186 0.3192 0.3177 -0.0067 -0.0092 0.0009  42  HIS A NE2 
340  N N   . ASP A 44  ? 0.2456 0.2275 0.2106 0.0044  -0.0114 -0.0080 43  ASP A N   
341  C CA  . ASP A 44  ? 0.2447 0.2173 0.2009 0.0067  -0.0113 -0.0093 43  ASP A CA  
342  C C   . ASP A 44  ? 0.2506 0.2239 0.2073 0.0107  -0.0140 -0.0031 43  ASP A C   
343  O O   . ASP A 44  ? 0.2633 0.2239 0.2142 0.0112  -0.0138 -0.0021 43  ASP A O   
344  C CB  . ASP A 44  ? 0.2703 0.2496 0.2240 0.0080  -0.0112 -0.0131 43  ASP A CB  
345  C CG  . ASP A 44  ? 0.3187 0.2867 0.2625 0.0099  -0.0104 -0.0155 43  ASP A CG  
346  O OD1 . ASP A 44  ? 0.3236 0.2776 0.2623 0.0093  -0.0096 -0.0151 43  ASP A OD1 
347  O OD2 . ASP A 44  ? 0.3025 0.2754 0.2435 0.0119  -0.0106 -0.0176 43  ASP A OD2 
348  N N   . CYS A 45  ? 0.2754 0.2636 0.2391 0.0133  -0.0167 0.0014  44  CYS A N   
349  C CA  . CYS A 45  ? 0.2773 0.2679 0.2412 0.0175  -0.0194 0.0070  44  CYS A CA  
350  C C   . CYS A 45  ? 0.2513 0.2342 0.2161 0.0170  -0.0200 0.0115  44  CYS A C   
351  O O   . CYS A 45  ? 0.2790 0.2562 0.2403 0.0194  -0.0213 0.0147  44  CYS A O   
352  C CB  . CYS A 45  ? 0.2586 0.2674 0.2299 0.0203  -0.0219 0.0104  44  CYS A CB  
353  S SG  . CYS A 45  ? 0.2928 0.3102 0.2619 0.0217  -0.0216 0.0058  44  CYS A SG  
354  N N   . PHE A 46  ? 0.2527 0.1987 0.2190 -0.0197 -0.0127 0.0079  45  PHE A N   
355  C CA  . PHE A 46  ? 0.2873 0.2340 0.2477 -0.0226 -0.0141 0.0077  45  PHE A CA  
356  C C   . PHE A 46  ? 0.2910 0.2399 0.2483 -0.0255 -0.0112 0.0106  45  PHE A C   
357  O O   . PHE A 46  ? 0.2925 0.2422 0.2445 -0.0280 -0.0122 0.0112  45  PHE A O   
358  C CB  . PHE A 46  ? 0.2816 0.2269 0.2422 -0.0227 -0.0149 0.0003  45  PHE A CB  
359  C CG  . PHE A 46  ? 0.2694 0.2132 0.2290 -0.0218 -0.0194 -0.0012 45  PHE A CG  
360  C CD1 . PHE A 46  ? 0.3193 0.2618 0.2823 -0.0190 -0.0214 -0.0003 45  PHE A CD1 
361  C CD2 . PHE A 46  ? 0.2937 0.2374 0.2491 -0.0237 -0.0216 -0.0036 45  PHE A CD2 
362  C CE1 . PHE A 46  ? 0.2880 0.2292 0.2503 -0.0182 -0.0256 -0.0015 45  PHE A CE1 
363  C CE2 . PHE A 46  ? 0.2881 0.2304 0.2429 -0.0229 -0.0259 -0.0050 45  PHE A CE2 
364  C CZ  . PHE A 46  ? 0.3193 0.2604 0.2776 -0.0202 -0.0279 -0.0038 45  PHE A CZ  
365  N N   . VAL A 47  ? 0.2696 0.2195 0.2300 -0.0251 -0.0076 0.0124  46  VAL A N   
366  C CA  . VAL A 47  ? 0.2956 0.2477 0.2534 -0.0278 -0.0046 0.0151  46  VAL A CA  
367  C C   . VAL A 47  ? 0.3036 0.2570 0.2625 -0.0276 -0.0037 0.0221  46  VAL A C   
368  O O   . VAL A 47  ? 0.2866 0.2400 0.2503 -0.0260 -0.0012 0.0225  46  VAL A O   
369  C CB  . VAL A 47  ? 0.2876 0.2399 0.2482 -0.0281 -0.0007 0.0102  46  VAL A CB  
370  C CG1 . VAL A 47  ? 0.3176 0.2724 0.2753 -0.0310 0.0023  0.0133  46  VAL A CG1 
371  C CG2 . VAL A 47  ? 0.2999 0.2508 0.2597 -0.0281 -0.0018 0.0031  46  VAL A CG2 
372  N N   . ASN A 48  ? 0.3290 0.2834 0.2834 -0.0291 -0.0058 0.0276  47  ASN A N   
373  C CA  . ASN A 48  ? 0.3160 0.2716 0.2705 -0.0293 -0.0054 0.0347  47  ASN A CA  
374  C C   . ASN A 48  ? 0.3135 0.2681 0.2727 -0.0260 -0.0066 0.0363  47  ASN A C   
375  O O   . ASN A 48  ? 0.3678 0.3234 0.3290 -0.0254 -0.0055 0.0412  47  ASN A O   
376  C CB  . ASN A 48  ? 0.3279 0.2853 0.2836 -0.0307 -0.0012 0.0365  47  ASN A CB  
377  C CG  . ASN A 48  ? 0.4075 0.3666 0.3615 -0.0320 -0.0011 0.0441  47  ASN A CG  
378  O OD1 . ASN A 48  ? 0.4330 0.3928 0.3818 -0.0341 -0.0031 0.0476  47  ASN A OD1 
379  N ND2 . ASN A 48  ? 0.4249 0.3847 0.3835 -0.0307 0.0011  0.0468  47  ASN A ND2 
380  N N   . GLY A 49  ? 0.2993 0.2519 0.2603 -0.0238 -0.0089 0.0322  48  GLY A N   
381  C CA  . GLY A 49  ? 0.3263 0.2779 0.2914 -0.0205 -0.0102 0.0334  48  GLY A CA  
382  C C   . GLY A 49  ? 0.2995 0.2503 0.2707 -0.0181 -0.0075 0.0298  48  GLY A C   
383  O O   . GLY A 49  ? 0.2828 0.2339 0.2554 -0.0190 -0.0044 0.0268  48  GLY A O   
384  N N   . CYS A 50  ? 0.3004 0.2500 0.2753 -0.0150 -0.0087 0.0301  49  CYS A N   
385  C CA  . CYS A 50  ? 0.3047 0.2531 0.2857 -0.0122 -0.0067 0.0267  49  CYS A CA  
386  C C   . CYS A 50  ? 0.3370 0.2870 0.3205 -0.0122 -0.0039 0.0311  49  CYS A C   
387  O O   . CYS A 50  ? 0.3013 0.2515 0.2866 -0.0104 -0.0044 0.0353  49  CYS A O   
388  C CB  . CYS A 50  ? 0.3328 0.2794 0.3163 -0.0088 -0.0094 0.0253  49  CYS A CB  
389  S SG  . CYS A 50  ? 0.3771 0.3225 0.3567 -0.0091 -0.0140 0.0232  49  CYS A SG  
390  N N   . ASP A 51  ? 0.2561 0.2071 0.2396 -0.0143 -0.0007 0.0301  50  ASP A N   
391  C CA  . ASP A 51  ? 0.2668 0.2196 0.2522 -0.0150 0.0021  0.0344  50  ASP A CA  
392  C C   . ASP A 51  ? 0.2917 0.2444 0.2817 -0.0146 0.0056  0.0303  50  ASP A C   
393  O O   . ASP A 51  ? 0.2966 0.2509 0.2879 -0.0158 0.0083  0.0331  50  ASP A O   
394  C CB  . ASP A 51  ? 0.2778 0.2328 0.2577 -0.0187 0.0025  0.0389  50  ASP A CB  
395  C CG  . ASP A 51  ? 0.2969 0.2521 0.2732 -0.0213 0.0033  0.0349  50  ASP A CG  
396  O OD1 . ASP A 51  ? 0.2746 0.2283 0.2528 -0.0203 0.0036  0.0286  50  ASP A OD1 
397  O OD2 . ASP A 51  ? 0.3251 0.2820 0.2968 -0.0244 0.0038  0.0381  50  ASP A OD2 
398  N N   . ALA A 52  ? 0.2683 0.2190 0.2608 -0.0130 0.0055  0.0238  51  ALA A N   
399  C CA  . ALA A 52  ? 0.2984 0.2486 0.2954 -0.0125 0.0086  0.0193  51  ALA A CA  
400  C C   . ALA A 52  ? 0.2794 0.2316 0.2741 -0.0159 0.0114  0.0192  51  ALA A C   
401  O O   . ALA A 52  ? 0.2999 0.2525 0.2984 -0.0160 0.0145  0.0176  51  ALA A O   
402  C CB  . ALA A 52  ? 0.2947 0.2448 0.2977 -0.0101 0.0102  0.0212  51  ALA A CB  
403  N N   . SER A 53  ? 0.2520 0.2052 0.2403 -0.0187 0.0102  0.0209  52  SER A N   
404  C CA  . SER A 53  ? 0.2499 0.2050 0.2354 -0.0219 0.0128  0.0206  52  SER A CA  
405  C C   . SER A 53  ? 0.2810 0.2351 0.2688 -0.0217 0.0145  0.0135  52  SER A C   
406  O O   . SER A 53  ? 0.3126 0.2681 0.3014 -0.0232 0.0178  0.0126  52  SER A O   
407  C CB  . SER A 53  ? 0.2748 0.2309 0.2529 -0.0247 0.0108  0.0231  52  SER A CB  
408  O OG  . SER A 53  ? 0.3014 0.2558 0.2771 -0.0241 0.0077  0.0192  52  SER A OG  
409  N N   . ILE A 54  ? 0.2818 0.2336 0.2709 -0.0197 0.0124  0.0085  53  ILE A N   
410  C CA  . ILE A 54  ? 0.2830 0.2337 0.2741 -0.0195 0.0137  0.0015  53  ILE A CA  
411  C C   . ILE A 54  ? 0.3068 0.2571 0.3048 -0.0179 0.0168  -0.0007 53  ILE A C   
412  O O   . ILE A 54  ? 0.3447 0.2948 0.3446 -0.0183 0.0189  -0.0056 53  ILE A O   
413  C CB  . ILE A 54  ? 0.2610 0.2091 0.2521 -0.0177 0.0103  -0.0031 53  ILE A CB  
414  C CG1 . ILE A 54  ? 0.3185 0.2655 0.3111 -0.0179 0.0115  -0.0104 53  ILE A CG1 
415  C CG2 . ILE A 54  ? 0.3035 0.2497 0.2993 -0.0141 0.0089  -0.0027 53  ILE A CG2 
416  C CD1 . ILE A 54  ? 0.3923 0.3373 0.3831 -0.0172 0.0082  -0.0147 53  ILE A CD1 
417  N N   . LEU A 55  ? 0.3038 0.2540 0.3058 -0.0160 0.0171  0.0028  54  LEU A N   
418  C CA  . LEU A 55  ? 0.2850 0.2346 0.2939 -0.0142 0.0197  0.0006  54  LEU A CA  
419  C C   . LEU A 55  ? 0.3213 0.2734 0.3312 -0.0163 0.0235  0.0033  54  LEU A C   
420  O O   . LEU A 55  ? 0.3203 0.2722 0.3359 -0.0153 0.0260  0.0010  54  LEU A O   
421  C CB  . LEU A 55  ? 0.2476 0.1959 0.2607 -0.0109 0.0183  0.0029  54  LEU A CB  
422  C CG  . LEU A 55  ? 0.2941 0.2398 0.3071 -0.0083 0.0148  0.0004  54  LEU A CG  
423  C CD1 . LEU A 55  ? 0.3080 0.2529 0.3249 -0.0053 0.0139  0.0033  54  LEU A CD1 
424  C CD2 . LEU A 55  ? 0.3065 0.2501 0.3222 -0.0072 0.0148  -0.0070 54  LEU A CD2 
425  N N   . LEU A 56  ? 0.2816 0.2361 0.2862 -0.0192 0.0239  0.0081  55  LEU A N   
426  C CA  . LEU A 56  ? 0.2780 0.2351 0.2834 -0.0214 0.0273  0.0111  55  LEU A CA  
427  C C   . LEU A 56  ? 0.2915 0.2492 0.2970 -0.0230 0.0300  0.0063  55  LEU A C   
428  O O   . LEU A 56  ? 0.3183 0.2756 0.3196 -0.0241 0.0291  0.0028  55  LEU A O   
429  C CB  . LEU A 56  ? 0.2988 0.2582 0.2980 -0.0242 0.0268  0.0174  55  LEU A CB  
430  C CG  . LEU A 56  ? 0.2850 0.2444 0.2843 -0.0230 0.0247  0.0231  55  LEU A CG  
431  C CD1 . LEU A 56  ? 0.3421 0.3034 0.3347 -0.0258 0.0236  0.0286  55  LEU A CD1 
432  C CD2 . LEU A 56  ? 0.3250 0.2851 0.3306 -0.0216 0.0268  0.0259  55  LEU A CD2 
433  N N   . ASP A 57  ? 0.2836 0.2425 0.2941 -0.0230 0.0334  0.0063  56  ASP A N   
434  C CA  . ASP A 57  ? 0.3360 0.2960 0.3468 -0.0248 0.0365  0.0027  56  ASP A CA  
435  C C   . ASP A 57  ? 0.3367 0.2999 0.3419 -0.0285 0.0382  0.0069  56  ASP A C   
436  O O   . ASP A 57  ? 0.3427 0.3073 0.3449 -0.0296 0.0374  0.0129  56  ASP A O   
437  C CB  . ASP A 57  ? 0.3275 0.2873 0.3465 -0.0232 0.0393  0.0010  56  ASP A CB  
438  C CG  . ASP A 57  ? 0.4588 0.4154 0.4831 -0.0199 0.0382  -0.0050 56  ASP A CG  
439  O OD1 . ASP A 57  ? 0.4874 0.4422 0.5090 -0.0195 0.0361  -0.0092 56  ASP A OD1 
440  O OD2 . ASP A 57  ? 0.5099 0.4657 0.5412 -0.0179 0.0395  -0.0057 56  ASP A OD2 
441  N N   . ASN A 58  ? 0.3231 0.2875 0.3271 -0.0303 0.0407  0.0035  57  ASN A N   
442  C CA  . ASN A 58  ? 0.3303 0.2978 0.3290 -0.0338 0.0427  0.0067  57  ASN A CA  
443  C C   . ASN A 58  ? 0.3495 0.3193 0.3504 -0.0348 0.0447  0.0130  57  ASN A C   
444  O O   . ASN A 58  ? 0.3465 0.3161 0.3544 -0.0331 0.0463  0.0132  57  ASN A O   
445  C CB  . ASN A 58  ? 0.3734 0.3418 0.3728 -0.0350 0.0458  0.0016  57  ASN A CB  
446  C CG  . ASN A 58  ? 0.4121 0.3814 0.4039 -0.0374 0.0452  -0.0003 57  ASN A CG  
447  O OD1 . ASN A 58  ? 0.4578 0.4276 0.4433 -0.0388 0.0431  0.0031  57  ASN A OD1 
448  N ND2 . ASN A 58  ? 0.4855 0.4550 0.4779 -0.0377 0.0472  -0.0059 57  ASN A ND2 
449  N N   . THR A 59  ? 0.3607 0.3326 0.3556 -0.0375 0.0445  0.0182  58  THR A N   
450  C CA  . THR A 59  ? 0.3481 0.3227 0.3441 -0.0391 0.0468  0.0240  58  THR A CA  
451  C C   . THR A 59  ? 0.3914 0.3688 0.3808 -0.0428 0.0485  0.0255  58  THR A C   
452  O O   . THR A 59  ? 0.3849 0.3618 0.3686 -0.0438 0.0475  0.0224  58  THR A O   
453  C CB  . THR A 59  ? 0.4131 0.3876 0.4087 -0.0387 0.0446  0.0303  58  THR A CB  
454  O OG1 . THR A 59  ? 0.4323 0.4076 0.4198 -0.0410 0.0427  0.0337  58  THR A OG1 
455  C CG2 . THR A 59  ? 0.3868 0.3583 0.3862 -0.0351 0.0417  0.0284  58  THR A CG2 
456  N N   . THR A 60  ? 0.3958 0.3759 0.3857 -0.0448 0.0511  0.0303  59  THR A N   
457  C CA  . THR A 60  ? 0.4464 0.4292 0.4298 -0.0483 0.0527  0.0322  59  THR A CA  
458  C C   . THR A 60  ? 0.4094 0.3924 0.3850 -0.0500 0.0498  0.0364  59  THR A C   
459  O O   . THR A 60  ? 0.5267 0.5116 0.4959 -0.0529 0.0507  0.0377  59  THR A O   
460  C CB  . THR A 60  ? 0.4588 0.4445 0.4452 -0.0499 0.0564  0.0361  59  THR A CB  
461  O OG1 . THR A 60  ? 0.4157 0.4019 0.4038 -0.0499 0.0553  0.0426  59  THR A OG1 
462  C CG2 . THR A 60  ? 0.4523 0.4379 0.4470 -0.0482 0.0592  0.0321  59  THR A CG2 
463  N N   . SER A 61  ? 0.4526 0.4336 0.4284 -0.0484 0.0464  0.0386  60  SER A N   
464  C CA  . SER A 61  ? 0.5342 0.5152 0.5030 -0.0498 0.0434  0.0425  60  SER A CA  
465  C C   . SER A 61  ? 0.4734 0.4518 0.4389 -0.0485 0.0398  0.0388  60  SER A C   
466  O O   . SER A 61  ? 0.5710 0.5494 0.5301 -0.0500 0.0373  0.0413  60  SER A O   
467  C CB  . SER A 61  ? 0.5650 0.5463 0.5357 -0.0495 0.0422  0.0494  60  SER A CB  
468  O OG  . SER A 61  ? 0.5551 0.5343 0.5324 -0.0461 0.0411  0.0484  60  SER A OG  
469  N N   . PHE A 62  ? 0.3915 0.3676 0.3614 -0.0458 0.0393  0.0331  61  PHE A N   
470  C CA  . PHE A 62  ? 0.3834 0.3573 0.3499 -0.0448 0.0361  0.0290  61  PHE A CA  
471  C C   . PHE A 62  ? 0.3651 0.3374 0.3359 -0.0429 0.0371  0.0216  61  PHE A C   
472  O O   . PHE A 62  ? 0.3640 0.3361 0.3417 -0.0412 0.0392  0.0200  61  PHE A O   
473  C CB  . PHE A 62  ? 0.3848 0.3567 0.3514 -0.0430 0.0321  0.0317  61  PHE A CB  
474  C CG  . PHE A 62  ? 0.3752 0.3459 0.3496 -0.0399 0.0323  0.0321  61  PHE A CG  
475  C CD1 . PHE A 62  ? 0.3379 0.3064 0.3173 -0.0371 0.0322  0.0263  61  PHE A CD1 
476  C CD2 . PHE A 62  ? 0.4004 0.3720 0.3768 -0.0398 0.0324  0.0383  61  PHE A CD2 
477  C CE1 . PHE A 62  ? 0.3822 0.3495 0.3684 -0.0342 0.0322  0.0266  61  PHE A CE1 
478  C CE2 . PHE A 62  ? 0.4173 0.3878 0.4007 -0.0369 0.0325  0.0386  61  PHE A CE2 
479  C CZ  . PHE A 62  ? 0.3485 0.3168 0.3367 -0.0341 0.0324  0.0327  61  PHE A CZ  
480  N N   . ARG A 63  ? 0.3201 0.2913 0.2869 -0.0432 0.0354  0.0170  62  ARG A N   
481  C CA  . ARG A 63  ? 0.3078 0.2772 0.2782 -0.0413 0.0358  0.0097  62  ARG A CA  
482  C C   . ARG A 63  ? 0.3398 0.3062 0.3137 -0.0381 0.0325  0.0080  62  ARG A C   
483  O O   . ARG A 63  ? 0.3381 0.3037 0.3090 -0.0378 0.0292  0.0111  62  ARG A O   
484  C CB  . ARG A 63  ? 0.3627 0.3323 0.3275 -0.0429 0.0353  0.0052  62  ARG A CB  
485  C CG  . ARG A 63  ? 0.3665 0.3389 0.3278 -0.0458 0.0388  0.0055  62  ARG A CG  
486  C CD  . ARG A 63  ? 0.3110 0.2846 0.2786 -0.0454 0.0431  0.0039  62  ARG A CD  
487  N NE  . ARG A 63  ? 0.3512 0.3265 0.3213 -0.0459 0.0447  0.0101  62  ARG A NE  
488  C CZ  . ARG A 63  ? 0.4155 0.3935 0.3813 -0.0487 0.0462  0.0151  62  ARG A CZ  
489  N NH1 . ARG A 63  ? 0.3722 0.3518 0.3311 -0.0512 0.0465  0.0145  62  ARG A NH1 
490  N NH2 . ARG A 63  ? 0.4203 0.3996 0.3890 -0.0489 0.0473  0.0209  62  ARG A NH2 
491  N N   . THR A 64  ? 0.3288 0.2935 0.3090 -0.0358 0.0335  0.0031  63  THR A N   
492  C CA  . THR A 64  ? 0.3017 0.2635 0.2855 -0.0326 0.0307  0.0008  63  THR A CA  
493  C C   . THR A 64  ? 0.3115 0.2717 0.2910 -0.0326 0.0274  -0.0031 63  THR A C   
494  O O   . THR A 64  ? 0.3329 0.2936 0.3090 -0.0342 0.0280  -0.0067 63  THR A O   
495  C CB  . THR A 64  ? 0.3255 0.2860 0.3172 -0.0303 0.0327  -0.0038 63  THR A CB  
496  O OG1 . THR A 64  ? 0.3345 0.2920 0.3293 -0.0272 0.0298  -0.0065 63  THR A OG1 
497  C CG2 . THR A 64  ? 0.3354 0.2964 0.3274 -0.0313 0.0352  -0.0096 63  THR A CG2 
498  N N   . GLU A 65  ? 0.2788 0.2371 0.2584 -0.0307 0.0237  -0.0021 64  GLU A N   
499  C CA  . GLU A 65  ? 0.2903 0.2467 0.2669 -0.0302 0.0204  -0.0060 64  GLU A CA  
500  C C   . GLU A 65  ? 0.2707 0.2252 0.2516 -0.0286 0.0210  -0.0135 64  GLU A C   
501  O O   . GLU A 65  ? 0.3135 0.2667 0.2920 -0.0287 0.0188  -0.0178 64  GLU A O   
502  C CB  . GLU A 65  ? 0.2787 0.2335 0.2551 -0.0284 0.0165  -0.0030 64  GLU A CB  
503  C CG  . GLU A 65  ? 0.3187 0.2753 0.2904 -0.0302 0.0154  0.0042  64  GLU A CG  
504  C CD  . GLU A 65  ? 0.3631 0.3184 0.3353 -0.0283 0.0121  0.0077  64  GLU A CD  
505  O OE1 . GLU A 65  ? 0.3375 0.2906 0.3116 -0.0260 0.0096  0.0043  64  GLU A OE1 
506  O OE2 . GLU A 65  ? 0.3494 0.3060 0.3199 -0.0291 0.0118  0.0141  64  GLU A OE2 
507  N N   . LYS A 66  ? 0.3007 0.2549 0.2879 -0.0272 0.0239  -0.0153 65  LYS A N   
508  C CA  . LYS A 66  ? 0.3202 0.2725 0.3119 -0.0256 0.0246  -0.0224 65  LYS A CA  
509  C C   . LYS A 66  ? 0.3629 0.3163 0.3516 -0.0278 0.0262  -0.0267 65  LYS A C   
510  O O   . LYS A 66  ? 0.3474 0.2991 0.3386 -0.0268 0.0261  -0.0330 65  LYS A O   
511  C CB  . LYS A 66  ? 0.3250 0.2771 0.3243 -0.0238 0.0274  -0.0229 65  LYS A CB  
512  C CG  . LYS A 66  ? 0.3416 0.2925 0.3446 -0.0213 0.0259  -0.0193 65  LYS A CG  
513  C CD  . LYS A 66  ? 0.3899 0.3407 0.4001 -0.0197 0.0288  -0.0195 65  LYS A CD  
514  C CE  . LYS A 66  ? 0.4287 0.3781 0.4425 -0.0170 0.0271  -0.0164 65  LYS A CE  
515  N NZ  . LYS A 66  ? 0.4631 0.4121 0.4845 -0.0152 0.0297  -0.0169 65  LYS A NZ  
516  N N   . ASP A 67  ? 0.3198 0.2760 0.3031 -0.0308 0.0276  -0.0235 66  ASP A N   
517  C CA  . ASP A 67  ? 0.3349 0.2923 0.3145 -0.0329 0.0290  -0.0274 66  ASP A CA  
518  C C   . ASP A 67  ? 0.3099 0.2667 0.2829 -0.0340 0.0254  -0.0283 66  ASP A C   
519  O O   . ASP A 67  ? 0.3186 0.2764 0.2877 -0.0358 0.0262  -0.0314 66  ASP A O   
520  C CB  . ASP A 67  ? 0.4094 0.3701 0.3868 -0.0355 0.0328  -0.0238 66  ASP A CB  
521  C CG  . ASP A 67  ? 0.5954 0.5567 0.5796 -0.0347 0.0368  -0.0241 66  ASP A CG  
522  O OD1 . ASP A 67  ? 0.6007 0.5604 0.5905 -0.0328 0.0375  -0.0295 66  ASP A OD1 
523  O OD2 . ASP A 67  ? 0.7354 0.6990 0.7198 -0.0359 0.0390  -0.0190 66  ASP A OD2 
524  N N   . ALA A 68  ? 0.3529 0.2449 0.2415 0.0042  0.0505  0.0198  67  ALA A N   
525  C CA  . ALA A 68  ? 0.3625 0.2538 0.2418 0.0099  0.0431  0.0236  67  ALA A CA  
526  C C   . ALA A 68  ? 0.3513 0.2593 0.2497 0.0121  0.0430  0.0181  67  ALA A C   
527  O O   . ALA A 68  ? 0.3738 0.2985 0.2952 0.0106  0.0439  0.0122  67  ALA A O   
528  C CB  . ALA A 68  ? 0.3573 0.2520 0.2307 0.0145  0.0287  0.0289  67  ALA A CB  
529  N N   . PHE A 69  ? 0.3931 0.2961 0.2817 0.0158  0.0416  0.0204  68  PHE A N   
530  C CA  . PHE A 69  ? 0.3594 0.2770 0.2652 0.0184  0.0416  0.0156  68  PHE A CA  
531  C C   . PHE A 69  ? 0.3496 0.2896 0.2763 0.0215  0.0300  0.0134  68  PHE A C   
532  O O   . PHE A 69  ? 0.3454 0.3019 0.2949 0.0212  0.0318  0.0077  68  PHE A O   
533  C CB  . PHE A 69  ? 0.4199 0.3270 0.3090 0.0223  0.0403  0.0192  68  PHE A CB  
534  C CG  . PHE A 69  ? 0.4211 0.3066 0.2902 0.0187  0.0524  0.0209  68  PHE A CG  
535  C CD1 . PHE A 69  ? 0.4719 0.3569 0.3499 0.0150  0.0663  0.0153  68  PHE A CD1 
536  C CD2 . PHE A 69  ? 0.4915 0.3574 0.3331 0.0189  0.0499  0.0283  68  PHE A CD2 
537  C CE1 . PHE A 69  ? 0.5542 0.4195 0.4136 0.0113  0.0777  0.0167  68  PHE A CE1 
538  C CE2 . PHE A 69  ? 0.4951 0.3410 0.3179 0.0150  0.0609  0.0299  68  PHE A CE2 
539  C CZ  . PHE A 69  ? 0.5489 0.3944 0.3804 0.0112  0.0748  0.0240  68  PHE A CZ  
540  N N   . GLY A 70  ? 0.3367 0.2780 0.2564 0.0241  0.0181  0.0180  69  GLY A N   
541  C CA  . GLY A 70  ? 0.3293 0.2915 0.2675 0.0268  0.0066  0.0161  69  GLY A CA  
542  C C   . GLY A 70  ? 0.3397 0.3134 0.2961 0.0225  0.0084  0.0112  69  GLY A C   
543  O O   . GLY A 70  ? 0.3460 0.3390 0.3217 0.0234  0.0011  0.0082  69  GLY A O   
544  N N   . ASN A 71  ? 0.3197 0.2818 0.2700 0.0174  0.0180  0.0106  70  ASN A N   
545  C CA  . ASN A 71  ? 0.2959 0.2660 0.2604 0.0129  0.0198  0.0065  70  ASN A CA  
546  C C   . ASN A 71  ? 0.3247 0.2986 0.3045 0.0075  0.0322  0.0004  70  ASN A C   
547  O O   . ASN A 71  ? 0.3139 0.3034 0.3146 0.0046  0.0317  -0.0045 70  ASN A O   
548  C CB  . ASN A 71  ? 0.3264 0.2809 0.2737 0.0108  0.0208  0.0104  70  ASN A CB  
549  C CG  . ASN A 71  ? 0.3037 0.2587 0.2415 0.0154  0.0078  0.0157  70  ASN A CG  
550  O OD1 . ASN A 71  ? 0.3222 0.2939 0.2727 0.0182  -0.0022 0.0144  70  ASN A OD1 
551  N ND2 . ASN A 71  ? 0.3453 0.2820 0.2606 0.0161  0.0079  0.0222  70  ASN A ND2 
552  N N   . ALA A 72  ? 0.3205 0.2805 0.2898 0.0058  0.0434  0.0008  71  ALA A N   
553  C CA  . ALA A 72  ? 0.3511 0.3124 0.3325 0.0003  0.0563  -0.0043 71  ALA A CA  
554  C C   . ALA A 72  ? 0.3224 0.3051 0.3304 0.0009  0.0557  -0.0096 71  ALA A C   
555  O O   . ALA A 72  ? 0.3162 0.3052 0.3275 0.0056  0.0516  -0.0092 71  ALA A O   
556  C CB  . ALA A 72  ? 0.3445 0.2873 0.3088 -0.0008 0.0676  -0.0025 71  ALA A CB  
557  N N   . ASN A 73  ? 0.3674 0.3613 0.3945 -0.0041 0.0594  -0.0142 72  ASN A N   
558  C CA  . ASN A 73  ? 0.3549 0.3696 0.4090 -0.0046 0.0594  -0.0189 72  ASN A CA  
559  C C   . ASN A 73  ? 0.3762 0.4065 0.4394 0.0007  0.0453  -0.0182 72  ASN A C   
560  O O   . ASN A 73  ? 0.3663 0.4092 0.4441 0.0033  0.0440  -0.0200 72  ASN A O   
561  C CB  . ASN A 73  ? 0.4059 0.4179 0.4632 -0.0044 0.0707  -0.0206 72  ASN A CB  
562  C CG  . ASN A 73  ? 0.4284 0.4607 0.5148 -0.0061 0.0734  -0.0255 72  ASN A CG  
563  O OD1 . ASN A 73  ? 0.4211 0.4664 0.5244 -0.0101 0.0708  -0.0280 72  ASN A OD1 
564  N ND2 . ASN A 73  ? 0.5546 0.5900 0.6474 -0.0032 0.0786  -0.0266 72  ASN A ND2 
565  N N   . SER A 74  ? 0.2555 0.2853 0.3104 0.0022  0.0346  -0.0155 73  SER A N   
566  C CA  . SER A 74  ? 0.2929 0.3348 0.3517 0.0075  0.0205  -0.0137 73  SER A CA  
567  C C   . SER A 74  ? 0.2826 0.3286 0.3403 0.0066  0.0109  -0.0129 73  SER A C   
568  O O   . SER A 74  ? 0.2741 0.3385 0.3505 0.0056  0.0037  -0.0156 73  SER A O   
569  C CB  . SER A 74  ? 0.3379 0.3671 0.3757 0.0135  0.0173  -0.0086 73  SER A CB  
570  O OG  . SER A 74  ? 0.3221 0.3635 0.3644 0.0187  0.0040  -0.0068 73  SER A OG  
571  N N   . ALA A 75  ? 0.2901 0.3192 0.3263 0.0069  0.0109  -0.0090 74  ALA A N   
572  C CA  . ALA A 75  ? 0.2815 0.3125 0.3155 0.0060  0.0034  -0.0082 74  ALA A CA  
573  C C   . ALA A 75  ? 0.3231 0.3605 0.3725 -0.0009 0.0090  -0.0136 74  ALA A C   
574  O O   . ALA A 75  ? 0.2988 0.3306 0.3514 -0.0055 0.0206  -0.0161 74  ALA A O   
575  C CB  . ALA A 75  ? 0.2997 0.3099 0.3077 0.0075  0.0038  -0.0026 74  ALA A CB  
576  N N   . ARG A 76  ? 0.2515 0.3007 0.3103 -0.0020 0.0005  -0.0152 75  ARG A N   
577  C CA  . ARG A 76  ? 0.2509 0.3076 0.3251 -0.0088 0.0044  -0.0204 75  ARG A CA  
578  C C   . ARG A 76  ? 0.2910 0.3516 0.3641 -0.0094 -0.0045 -0.0206 75  ARG A C   
579  O O   . ARG A 76  ? 0.2932 0.3545 0.3574 -0.0042 -0.0145 -0.0171 75  ARG A O   
580  C CB  . ARG A 76  ? 0.2939 0.3704 0.3937 -0.0111 0.0049  -0.0247 75  ARG A CB  
581  C CG  . ARG A 76  ? 0.2558 0.3506 0.3669 -0.0071 -0.0081 -0.0244 75  ARG A CG  
582  C CD  . ARG A 76  ? 0.2588 0.3717 0.3943 -0.0085 -0.0071 -0.0277 75  ARG A CD  
583  N NE  . ARG A 76  ? 0.2806 0.4021 0.4340 -0.0161 -0.0017 -0.0323 75  ARG A NE  
584  C CZ  . ARG A 76  ? 0.3126 0.4472 0.4785 -0.0200 -0.0088 -0.0348 75  ARG A CZ  
585  N NH1 . ARG A 76  ? 0.2844 0.4253 0.4471 -0.0170 -0.0211 -0.0333 75  ARG A NH1 
586  N NH2 . ARG A 76  ? 0.3275 0.4689 0.5092 -0.0273 -0.0033 -0.0386 75  ARG A NH2 
587  N N   . GLY A 77  ? 0.3306 0.3932 0.4125 -0.0159 -0.0006 -0.0246 76  GLY A N   
588  C CA  . GLY A 77  ? 0.3281 0.3939 0.4099 -0.0174 -0.0076 -0.0258 76  GLY A CA  
589  C C   . GLY A 77  ? 0.3182 0.3648 0.3822 -0.0188 -0.0029 -0.0242 76  GLY A C   
590  O O   . GLY A 77  ? 0.3652 0.4126 0.4277 -0.0200 -0.0079 -0.0252 76  GLY A O   
591  N N   . PHE A 78  ? 0.3224 0.3515 0.3728 -0.0189 0.0066  -0.0217 77  PHE A N   
592  C CA  . PHE A 78  ? 0.3233 0.3335 0.3566 -0.0201 0.0111  -0.0196 77  PHE A CA  
593  C C   . PHE A 78  ? 0.3436 0.3549 0.3847 -0.0268 0.0135  -0.0243 77  PHE A C   
594  O O   . PHE A 78  ? 0.3677 0.3704 0.3983 -0.0262 0.0109  -0.0230 77  PHE A O   
595  C CB  . PHE A 78  ? 0.3712 0.3645 0.3921 -0.0207 0.0219  -0.0169 77  PHE A CB  
596  C CG  . PHE A 78  ? 0.3477 0.3373 0.3579 -0.0144 0.0195  -0.0119 77  PHE A CG  
597  C CD1 . PHE A 78  ? 0.3378 0.3181 0.3302 -0.0088 0.0129  -0.0059 77  PHE A CD1 
598  C CD2 . PHE A 78  ? 0.3938 0.3894 0.4121 -0.0141 0.0237  -0.0131 77  PHE A CD2 
599  C CE1 . PHE A 78  ? 0.3352 0.3116 0.3170 -0.0035 0.0103  -0.0011 77  PHE A CE1 
600  C CE2 . PHE A 78  ? 0.3298 0.3211 0.3375 -0.0085 0.0214  -0.0088 77  PHE A CE2 
601  C CZ  . PHE A 78  ? 0.3509 0.3325 0.3400 -0.0034 0.0145  -0.0027 77  PHE A CZ  
602  N N   . PRO A 79  ? 0.3651 0.3865 0.4241 -0.0330 0.0183  -0.0294 78  PRO A N   
603  C CA  . PRO A 79  ? 0.3690 0.3905 0.4341 -0.0397 0.0201  -0.0337 78  PRO A CA  
604  C C   . PRO A 79  ? 0.3633 0.3953 0.4328 -0.0389 0.0092  -0.0354 78  PRO A C   
605  O O   . PRO A 79  ? 0.3790 0.4051 0.4452 -0.0424 0.0095  -0.0374 78  PRO A O   
606  C CB  . PRO A 79  ? 0.4191 0.4520 0.5041 -0.0461 0.0263  -0.0381 78  PRO A CB  
607  C CG  . PRO A 79  ? 0.4072 0.4379 0.4907 -0.0431 0.0321  -0.0357 78  PRO A CG  
608  C CD  . PRO A 79  ? 0.3610 0.3914 0.4337 -0.0347 0.0237  -0.0312 78  PRO A CD  
609  N N   . VAL A 80  ? 0.3554 0.4027 0.4323 -0.0346 -0.0004 -0.0347 79  VAL A N   
610  C CA  . VAL A 80  ? 0.3547 0.4122 0.4347 -0.0335 -0.0113 -0.0359 79  VAL A CA  
611  C C   . VAL A 80  ? 0.3398 0.3830 0.3994 -0.0284 -0.0144 -0.0318 79  VAL A C   
612  O O   . VAL A 80  ? 0.3543 0.3968 0.4115 -0.0297 -0.0183 -0.0335 79  VAL A O   
613  C CB  . VAL A 80  ? 0.3060 0.3833 0.3987 -0.0300 -0.0209 -0.0356 79  VAL A CB  
614  C CG1 . VAL A 80  ? 0.3385 0.4266 0.4340 -0.0293 -0.0322 -0.0367 79  VAL A CG1 
615  C CG2 . VAL A 80  ? 0.3531 0.4447 0.4671 -0.0350 -0.0173 -0.0392 79  VAL A CG2 
616  N N   . ILE A 81  ? 0.3437 0.3751 0.3882 -0.0226 -0.0128 -0.0261 80  ILE A N   
617  C CA  . ILE A 81  ? 0.3206 0.3376 0.3457 -0.0178 -0.0152 -0.0213 80  ILE A CA  
618  C C   . ILE A 81  ? 0.3451 0.3463 0.3626 -0.0224 -0.0074 -0.0228 80  ILE A C   
619  O O   . ILE A 81  ? 0.3622 0.3576 0.3716 -0.0210 -0.0108 -0.0221 80  ILE A O   
620  C CB  . ILE A 81  ? 0.3582 0.3651 0.3689 -0.0118 -0.0143 -0.0146 80  ILE A CB  
621  C CG1 . ILE A 81  ? 0.3409 0.3636 0.3597 -0.0074 -0.0222 -0.0135 80  ILE A CG1 
622  C CG2 . ILE A 81  ? 0.3987 0.3913 0.3901 -0.0069 -0.0172 -0.0088 80  ILE A CG2 
623  C CD1 . ILE A 81  ? 0.3775 0.4144 0.4008 -0.0040 -0.0349 -0.0133 80  ILE A CD1 
624  N N   . ASP A 82  ? 0.3398 0.3341 0.3602 -0.0279 0.0030  -0.0249 81  ASP A N   
625  C CA  . ASP A 82  ? 0.3886 0.3684 0.4031 -0.0329 0.0105  -0.0267 81  ASP A CA  
626  C C   . ASP A 82  ? 0.3607 0.3485 0.3847 -0.0373 0.0067  -0.0322 81  ASP A C   
627  O O   . ASP A 82  ? 0.3733 0.3496 0.3882 -0.0382 0.0078  -0.0324 81  ASP A O   
628  C CB  . ASP A 82  ? 0.4098 0.3842 0.4289 -0.0389 0.0218  -0.0286 81  ASP A CB  
629  C CG  . ASP A 82  ? 0.5261 0.4879 0.5325 -0.0357 0.0275  -0.0233 81  ASP A CG  
630  O OD1 . ASP A 82  ? 0.5249 0.4744 0.5143 -0.0305 0.0254  -0.0177 81  ASP A OD1 
631  O OD2 . ASP A 82  ? 0.5443 0.5083 0.5576 -0.0387 0.0343  -0.0247 81  ASP A OD2 
632  N N   . ARG A 83  ? 0.3570 0.3638 0.3994 -0.0407 0.0028  -0.0367 82  ARG A N   
633  C CA  . ARG A 83  ? 0.3883 0.4034 0.4399 -0.0457 -0.0012 -0.0420 82  ARG A CA  
634  C C   . ARG A 83  ? 0.3323 0.3481 0.3756 -0.0406 -0.0103 -0.0406 82  ARG A C   
635  O O   . ARG A 83  ? 0.3473 0.3572 0.3867 -0.0433 -0.0105 -0.0432 82  ARG A O   
636  C CB  . ARG A 83  ? 0.3861 0.4226 0.4594 -0.0500 -0.0046 -0.0462 82  ARG A CB  
637  C CG  . ARG A 83  ? 0.5177 0.5546 0.6024 -0.0582 0.0045  -0.0498 82  ARG A CG  
638  C CD  . ARG A 83  ? 0.5240 0.5828 0.6310 -0.0621 0.0009  -0.0530 82  ARG A CD  
639  N NE  . ARG A 83  ? 0.5462 0.6096 0.6594 -0.0598 0.0049  -0.0508 82  ARG A NE  
640  C CZ  . ARG A 83  ? 0.6757 0.7298 0.7877 -0.0624 0.0157  -0.0503 82  ARG A CZ  
641  N NH1 . ARG A 83  ? 0.8242 0.8641 0.9294 -0.0674 0.0233  -0.0517 82  ARG A NH1 
642  N NH2 . ARG A 83  ? 0.6698 0.7287 0.7873 -0.0598 0.0189  -0.0485 82  ARG A NH2 
643  N N   . MET A 84  ? 0.3313 0.3541 0.3716 -0.0334 -0.0180 -0.0365 83  MET A N   
644  C CA  . MET A 84  ? 0.4161 0.4403 0.4489 -0.0286 -0.0267 -0.0348 83  MET A CA  
645  C C   . MET A 84  ? 0.3608 0.3641 0.3739 -0.0247 -0.0230 -0.0305 83  MET A C   
646  O O   . MET A 84  ? 0.3455 0.3453 0.3529 -0.0238 -0.0261 -0.0312 83  MET A O   
647  C CB  . MET A 84  ? 0.4476 0.4863 0.4834 -0.0222 -0.0368 -0.0315 83  MET A CB  
648  C CG  . MET A 84  ? 0.4775 0.5098 0.5038 -0.0159 -0.0359 -0.0250 83  MET A CG  
649  S SD  . MET A 84  ? 0.3973 0.4466 0.4262 -0.0085 -0.0495 -0.0213 83  MET A SD  
650  C CE  . MET A 84  ? 0.3227 0.3955 0.3766 -0.0137 -0.0528 -0.0271 83  MET A CE  
651  N N   . LYS A 85  ? 0.3652 0.3542 0.3680 -0.0229 -0.0159 -0.0260 84  LYS A N   
652  C CA  . LYS A 85  ? 0.3590 0.3275 0.3441 -0.0202 -0.0118 -0.0217 84  LYS A CA  
653  C C   . LYS A 85  ? 0.3873 0.3463 0.3725 -0.0264 -0.0056 -0.0265 84  LYS A C   
654  O O   . LYS A 85  ? 0.3713 0.3202 0.3465 -0.0243 -0.0063 -0.0253 84  LYS A O   
655  C CB  . LYS A 85  ? 0.3808 0.3360 0.3556 -0.0184 -0.0050 -0.0163 84  LYS A CB  
656  C CG  . LYS A 85  ? 0.4160 0.3494 0.3732 -0.0164 -0.0001 -0.0113 84  LYS A CG  
657  C CD  . LYS A 85  ? 0.4094 0.3404 0.3553 -0.0087 -0.0079 -0.0055 84  LYS A CD  
658  C CE  . LYS A 85  ? 0.4378 0.3470 0.3669 -0.0067 -0.0025 0.0004  84  LYS A CE  
659  N NZ  . LYS A 85  ? 0.4829 0.3888 0.4017 0.0004  -0.0092 0.0061  84  LYS A NZ  
660  N N   . ALA A 86  ? 0.3369 0.2988 0.3332 -0.0341 0.0004  -0.0318 85  ALA A N   
661  C CA  . ALA A 86  ? 0.3542 0.3072 0.3509 -0.0406 0.0060  -0.0365 85  ALA A CA  
662  C C   . ALA A 86  ? 0.3954 0.3560 0.3957 -0.0414 -0.0010 -0.0407 85  ALA A C   
663  O O   . ALA A 86  ? 0.4227 0.3713 0.4154 -0.0427 0.0014  -0.0421 85  ALA A O   
664  C CB  . ALA A 86  ? 0.4241 0.3815 0.4338 -0.0490 0.0128  -0.0412 85  ALA A CB  
665  N N   . ALA A 87  ? 0.3166 0.2971 0.3284 -0.0407 -0.0095 -0.0426 86  ALA A N   
666  C CA  . ALA A 87  ? 0.4025 0.3915 0.4179 -0.0418 -0.0166 -0.0467 86  ALA A CA  
667  C C   . ALA A 87  ? 0.3920 0.3734 0.3930 -0.0341 -0.0211 -0.0425 86  ALA A C   
668  O O   . ALA A 87  ? 0.3963 0.3720 0.3927 -0.0352 -0.0216 -0.0452 86  ALA A O   
669  C CB  . ALA A 87  ? 0.3524 0.3649 0.3838 -0.0430 -0.0250 -0.0491 86  ALA A CB  
670  N N   . VAL A 88  ? 0.3755 0.3565 0.3693 -0.0263 -0.0243 -0.0357 87  VAL A N   
671  C CA  . VAL A 88  ? 0.3954 0.3691 0.3756 -0.0188 -0.0284 -0.0308 87  VAL A CA  
672  C C   . VAL A 88  ? 0.4374 0.3885 0.4043 -0.0188 -0.0201 -0.0289 87  VAL A C   
673  O O   . VAL A 88  ? 0.4129 0.3570 0.3718 -0.0160 -0.0214 -0.0284 87  VAL A O   
674  C CB  . VAL A 88  ? 0.4359 0.4142 0.4113 -0.0110 -0.0340 -0.0234 87  VAL A CB  
675  C CG1 . VAL A 88  ? 0.4195 0.3890 0.3805 -0.0034 -0.0375 -0.0174 87  VAL A CG1 
676  C CG2 . VAL A 88  ? 0.3737 0.3748 0.3628 -0.0109 -0.0431 -0.0255 87  VAL A CG2 
677  N N   . GLU A 89  ? 0.4119 0.3513 0.3764 -0.0220 -0.0112 -0.0279 88  GLU A N   
678  C CA  . GLU A 89  ? 0.4526 0.3705 0.4052 -0.0225 -0.0033 -0.0261 88  GLU A CA  
679  C C   . GLU A 89  ? 0.4955 0.4097 0.4509 -0.0281 -0.0010 -0.0330 88  GLU A C   
680  O O   . GLU A 89  ? 0.5217 0.4217 0.4668 -0.0261 0.0014  -0.0318 88  GLU A O   
681  C CB  . GLU A 89  ? 0.4822 0.3894 0.4327 -0.0259 0.0057  -0.0242 88  GLU A CB  
682  C CG  . GLU A 89  ? 0.5041 0.4060 0.4448 -0.0196 0.0054  -0.0157 88  GLU A CG  
683  C CD  . GLU A 89  ? 0.5739 0.4623 0.4992 -0.0127 0.0039  -0.0086 88  GLU A CD  
684  O OE1 . GLU A 89  ? 0.5222 0.3958 0.4409 -0.0141 0.0089  -0.0089 88  GLU A OE1 
685  O OE2 . GLU A 89  ? 0.5395 0.4321 0.4594 -0.0059 -0.0025 -0.0025 88  GLU A OE2 
686  N N   . SER A 90  ? 0.4757 0.4024 0.4447 -0.0353 -0.0018 -0.0402 89  SER A N   
687  C CA  . SER A 90  ? 0.5327 0.4563 0.5040 -0.0411 -0.0003 -0.0469 89  SER A CA  
688  C C   . SER A 90  ? 0.5368 0.4635 0.5033 -0.0364 -0.0073 -0.0473 89  SER A C   
689  O O   . SER A 90  ? 0.5798 0.4948 0.5397 -0.0376 -0.0046 -0.0499 89  SER A O   
690  C CB  . SER A 90  ? 0.4696 0.4080 0.4572 -0.0498 -0.0010 -0.0537 89  SER A CB  
691  O OG  . SER A 90  ? 0.6512 0.5855 0.6430 -0.0545 0.0065  -0.0536 89  SER A OG  
692  N N   . ALA A 91  ? 0.4559 0.3977 0.4253 -0.0310 -0.0162 -0.0447 90  ALA A N   
693  C CA  . ALA A 91  ? 0.5475 0.4955 0.5142 -0.0271 -0.0236 -0.0455 90  ALA A CA  
694  C C   . ALA A 91  ? 0.5186 0.4541 0.4704 -0.0181 -0.0238 -0.0386 90  ALA A C   
695  O O   . ALA A 91  ? 0.4926 0.4237 0.4386 -0.0159 -0.0252 -0.0399 90  ALA A O   
696  C CB  . ALA A 91  ? 0.4949 0.4660 0.4724 -0.0258 -0.0337 -0.0459 90  ALA A CB  
697  N N   A CYS A 92  ? 0.4553 0.3849 0.4009 -0.0129 -0.0223 -0.0310 91  CYS A N   
698  N N   B CYS A 92  ? 0.4558 0.3854 0.4013 -0.0128 -0.0224 -0.0310 91  CYS A N   
699  C CA  A CYS A 92  ? 0.4706 0.3888 0.4025 -0.0044 -0.0228 -0.0231 91  CYS A CA  
700  C CA  B CYS A 92  ? 0.4709 0.3887 0.4026 -0.0044 -0.0227 -0.0231 91  CYS A CA  
701  C C   A CYS A 92  ? 0.4744 0.3773 0.3989 -0.0038 -0.0155 -0.0173 91  CYS A C   
702  C C   B CYS A 92  ? 0.4747 0.3775 0.3990 -0.0036 -0.0156 -0.0172 91  CYS A C   
703  O O   A CYS A 92  ? 0.4658 0.3723 0.3888 -0.0003 -0.0177 -0.0116 91  CYS A O   
704  O O   B CYS A 92  ? 0.4664 0.3727 0.3888 0.0001  -0.0180 -0.0113 91  CYS A O   
705  C CB  A CYS A 92  ? 0.4784 0.4110 0.4102 0.0029  -0.0331 -0.0181 91  CYS A CB  
706  C CB  B CYS A 92  ? 0.4784 0.4105 0.4098 0.0030  -0.0331 -0.0183 91  CYS A CB  
707  S SG  A CYS A 92  ? 0.5683 0.5258 0.5133 0.0008  -0.0434 -0.0245 91  CYS A SG  
708  S SG  B CYS A 92  ? 0.4373 0.3861 0.3770 0.0039  -0.0388 -0.0155 91  CYS A SG  
709  N N   . PRO A 93  ? 0.4868 0.3722 0.4063 -0.0075 -0.0066 -0.0188 92  PRO A N   
710  C CA  . PRO A 93  ? 0.5147 0.3861 0.4280 -0.0083 0.0007  -0.0138 92  PRO A CA  
711  C C   . PRO A 93  ? 0.5027 0.3665 0.4040 0.0000  -0.0013 -0.0034 92  PRO A C   
712  O O   . PRO A 93  ? 0.4981 0.3593 0.3927 0.0062  -0.0051 0.0003  92  PRO A O   
713  C CB  . PRO A 93  ? 0.5844 0.4386 0.4943 -0.0134 0.0095  -0.0174 92  PRO A CB  
714  C CG  . PRO A 93  ? 0.5675 0.4301 0.4855 -0.0180 0.0073  -0.0264 92  PRO A CG  
715  C CD  . PRO A 93  ? 0.5531 0.4313 0.4731 -0.0121 -0.0027 -0.0255 92  PRO A CD  
716  N N   . ARG A 94  ? 0.4699 0.3303 0.3683 0.0000  0.0012  0.0014  93  ARG A N   
717  C CA  . ARG A 94  ? 0.4790 0.3290 0.3648 0.0062  0.0008  0.0117  93  ARG A CA  
718  C C   . ARG A 94  ? 0.4554 0.3156 0.3383 0.0143  -0.0092 0.0170  93  ARG A C   
719  O O   . ARG A 94  ? 0.4926 0.3432 0.3647 0.0203  -0.0105 0.0252  93  ARG A O   
720  C CB  . ARG A 94  ? 0.5281 0.3567 0.4036 0.0065  0.0077  0.0152  93  ARG A CB  
721  C CG  . ARG A 94  ? 0.6145 0.4320 0.4921 -0.0017 0.0176  0.0104  93  ARG A CG  
722  C CD  . ARG A 94  ? 0.7535 0.5514 0.6231 -0.0019 0.0238  0.0120  93  ARG A CD  
723  N NE  . ARG A 94  ? 0.9542 0.7494 0.8306 -0.0093 0.0292  0.0029  93  ARG A NE  
724  C CZ  . ARG A 94  ? 0.9280 0.7257 0.8078 -0.0097 0.0276  -0.0030 93  ARG A CZ  
725  N NH1 . ARG A 94  ? 0.9358 0.7376 0.8125 -0.0028 0.0214  -0.0008 93  ARG A NH1 
726  N NH2 . ARG A 94  ? 0.8842 0.6799 0.7702 -0.0173 0.0322  -0.0114 93  ARG A NH2 
727  N N   . THR A 95  ? 0.4257 0.3054 0.3185 0.0145  -0.0165 0.0129  94  THR A N   
728  C CA  . THR A 95  ? 0.4301 0.3212 0.3216 0.0216  -0.0265 0.0168  94  THR A CA  
729  C C   . THR A 95  ? 0.3910 0.2956 0.2853 0.0241  -0.0334 0.0201  94  THR A C   
730  O O   . THR A 95  ? 0.3944 0.2981 0.2802 0.0307  -0.0387 0.0286  94  THR A O   
731  C CB  . THR A 95  ? 0.4394 0.3422 0.3396 0.0200  -0.0305 0.0089  94  THR A CB  
732  O OG1 . THR A 95  ? 0.4819 0.3706 0.3775 0.0188  -0.0245 0.0066  94  THR A OG1 
733  C CG2 . THR A 95  ? 0.4454 0.3620 0.3455 0.0268  -0.0412 0.0124  94  THR A CG2 
734  N N   . VAL A 96  ? 0.3570 0.2739 0.2630 0.0192  -0.0337 0.0140  95  VAL A N   
735  C CA  . VAL A 96  ? 0.3397 0.2718 0.2505 0.0216  -0.0411 0.0159  95  VAL A CA  
736  C C   . VAL A 96  ? 0.3820 0.3066 0.2889 0.0201  -0.0358 0.0193  95  VAL A C   
737  O O   . VAL A 96  ? 0.3657 0.2854 0.2772 0.0138  -0.0277 0.0146  95  VAL A O   
738  C CB  . VAL A 96  ? 0.3209 0.2728 0.2481 0.0175  -0.0455 0.0074  95  VAL A CB  
739  C CG1 . VAL A 96  ? 0.3633 0.3309 0.2952 0.0209  -0.0540 0.0100  95  VAL A CG1 
740  C CG2 . VAL A 96  ? 0.3161 0.2738 0.2465 0.0176  -0.0494 0.0031  95  VAL A CG2 
741  N N   . SER A 97  ? 0.3353 0.2594 0.2339 0.0257  -0.0406 0.0273  96  SER A N   
742  C CA  . SER A 97  ? 0.3415 0.2582 0.2350 0.0244  -0.0360 0.0308  96  SER A CA  
743  C C   . SER A 97  ? 0.3378 0.2691 0.2449 0.0207  -0.0364 0.0247  96  SER A C   
744  O O   . SER A 97  ? 0.3390 0.2881 0.2575 0.0213  -0.0436 0.0207  96  SER A O   
745  C CB  . SER A 97  ? 0.3603 0.2725 0.2406 0.0311  -0.0417 0.0412  96  SER A CB  
746  O OG  . SER A 97  ? 0.3755 0.3052 0.2614 0.0351  -0.0522 0.0417  96  SER A OG  
747  N N   . CYS A 98  ? 0.3370 0.3182 0.3088 -0.0003 0.0083  0.0183  97  CYS A N   
748  C CA  . CYS A 98  ? 0.3368 0.3194 0.3070 -0.0029 0.0061  0.0146  97  CYS A CA  
749  C C   . CYS A 98  ? 0.3020 0.2897 0.2735 -0.0030 0.0031  0.0169  97  CYS A C   
750  O O   . CYS A 98  ? 0.3108 0.3005 0.2810 -0.0037 0.0016  0.0137  97  CYS A O   
751  C CB  . CYS A 98  ? 0.3539 0.3339 0.3231 -0.0061 0.0055  0.0134  97  CYS A CB  
752  S SG  . CYS A 98  ? 0.4095 0.3834 0.3769 -0.0064 0.0087  0.0102  97  CYS A SG  
753  N N   . ALA A 99  ? 0.2924 0.2822 0.2664 -0.0022 0.0022  0.0223  98  ALA A N   
754  C CA  . ALA A 99  ? 0.3182 0.3128 0.2936 -0.0023 -0.0009 0.0249  98  ALA A CA  
755  C C   . ALA A 99  ? 0.2717 0.2690 0.2472 0.0000  -0.0004 0.0241  98  ALA A C   
756  O O   . ALA A 99  ? 0.2885 0.2889 0.2634 -0.0008 -0.0029 0.0228  98  ALA A O   
757  C CB  . ALA A 99  ? 0.2903 0.2862 0.2688 -0.0017 -0.0018 0.0311  98  ALA A CB  
758  N N   . ASP A 100 ? 0.2564 0.2524 0.2324 0.0029  0.0026  0.0248  99  ASP A N   
759  C CA  . ASP A 100 ? 0.2710 0.2689 0.2466 0.0053  0.0034  0.0239  99  ASP A CA  
760  C C   . ASP A 100 ? 0.2580 0.2541 0.2302 0.0045  0.0036  0.0176  99  ASP A C   
761  O O   . ASP A 100 ? 0.2838 0.2821 0.2550 0.0050  0.0024  0.0159  99  ASP A O   
762  C CB  . ASP A 100 ? 0.2599 0.2564 0.2366 0.0087  0.0068  0.0261  99  ASP A CB  
763  C CG  . ASP A 100 ? 0.2987 0.2986 0.2793 0.0103  0.0064  0.0324  99  ASP A CG  
764  O OD1 . ASP A 100 ? 0.2734 0.2769 0.2557 0.0090  0.0034  0.0351  99  ASP A OD1 
765  O OD2 . ASP A 100 ? 0.2847 0.2834 0.2666 0.0130  0.0091  0.0347  99  ASP A OD2 
766  N N   . LEU A 101 ? 0.2862 0.2780 0.2566 0.0033  0.0049  0.0140  100 LEU A N   
767  C CA  . LEU A 101 ? 0.2861 0.2758 0.2536 0.0024  0.0050  0.0079  100 LEU A CA  
768  C C   . LEU A 101 ? 0.2748 0.2674 0.2415 -0.0001 0.0016  0.0058  100 LEU A C   
769  O O   . LEU A 101 ? 0.2976 0.2908 0.2626 0.0002  0.0008  0.0024  100 LEU A O   
770  C CB  . LEU A 101 ? 0.3126 0.2974 0.2788 0.0011  0.0067  0.0050  100 LEU A CB  
771  C CG  . LEU A 101 ? 0.4220 0.4035 0.3854 0.0009  0.0076  -0.0010 100 LEU A CG  
772  C CD1 . LEU A 101 ? 0.4868 0.4668 0.4493 0.0045  0.0099  -0.0015 100 LEU A CD1 
773  C CD2 . LEU A 101 ? 0.4602 0.4376 0.4229 -0.0011 0.0087  -0.0032 100 LEU A CD2 
774  N N   . LEU A 102 ? 0.2881 0.2824 0.2558 -0.0025 -0.0007 0.0079  101 LEU A N   
775  C CA  . LEU A 102 ? 0.2626 0.2597 0.2296 -0.0048 -0.0042 0.0061  101 LEU A CA  
776  C C   . LEU A 102 ? 0.3158 0.3173 0.2835 -0.0035 -0.0062 0.0082  101 LEU A C   
777  O O   . LEU A 102 ? 0.2746 0.2779 0.2408 -0.0044 -0.0084 0.0051  101 LEU A O   
778  C CB  . LEU A 102 ? 0.2523 0.2500 0.2202 -0.0073 -0.0061 0.0084  101 LEU A CB  
779  C CG  . LEU A 102 ? 0.3195 0.3196 0.2864 -0.0100 -0.0097 0.0066  101 LEU A CG  
780  C CD1 . LEU A 102 ? 0.3465 0.3452 0.3109 -0.0113 -0.0098 0.0001  101 LEU A CD1 
781  C CD2 . LEU A 102 ? 0.3031 0.3023 0.2704 -0.0122 -0.0107 0.0087  101 LEU A CD2 
782  N N   . THR A 103 ? 0.2812 0.2847 0.2514 -0.0013 -0.0055 0.0135  102 THR A N   
783  C CA  . THR A 103 ? 0.2860 0.2936 0.2571 0.0000  -0.0072 0.0158  102 THR A CA  
784  C C   . THR A 103 ? 0.2723 0.2792 0.2412 0.0018  -0.0058 0.0120  102 THR A C   
785  O O   . THR A 103 ? 0.2849 0.2942 0.2526 0.0014  -0.0081 0.0103  102 THR A O   
786  C CB  . THR A 103 ? 0.2525 0.2620 0.2270 0.0022  -0.0062 0.0222  102 THR A CB  
787  O OG1 . THR A 103 ? 0.2823 0.2917 0.2586 0.0006  -0.0074 0.0256  102 THR A OG1 
788  C CG2 . THR A 103 ? 0.3132 0.3275 0.2890 0.0032  -0.0082 0.0250  102 THR A CG2 
789  N N   . ILE A 104 ? 0.2809 0.2841 0.2490 0.0038  -0.0022 0.0107  103 ILE A N   
790  C CA  . ILE A 104 ? 0.2515 0.2530 0.2171 0.0057  -0.0008 0.0069  103 ILE A CA  
791  C C   . ILE A 104 ? 0.2724 0.2727 0.2352 0.0034  -0.0026 0.0008  103 ILE A C   
792  O O   . ILE A 104 ? 0.3058 0.3068 0.2668 0.0039  -0.0038 -0.0018 103 ILE A O   
793  C CB  . ILE A 104 ? 0.3001 0.2973 0.2653 0.0081  0.0032  0.0064  103 ILE A CB  
794  C CG1 . ILE A 104 ? 0.2862 0.2849 0.2542 0.0106  0.0051  0.0123  103 ILE A CG1 
795  C CG2 . ILE A 104 ? 0.3141 0.3087 0.2761 0.0099  0.0046  0.0019  103 ILE A CG2 
796  C CD1 . ILE A 104 ? 0.3313 0.3258 0.2991 0.0127  0.0088  0.0123  103 ILE A CD1 
797  N N   . ALA A 105 ? 0.2851 0.2832 0.2475 0.0009  -0.0030 -0.0016 104 ALA A N   
798  C CA  . ALA A 105 ? 0.2812 0.2780 0.2413 -0.0014 -0.0047 -0.0074 104 ALA A CA  
799  C C   . ALA A 105 ? 0.2742 0.2752 0.2340 -0.0030 -0.0086 -0.0076 104 ALA A C   
800  O O   . ALA A 105 ? 0.3033 0.3042 0.2610 -0.0035 -0.0101 -0.0120 104 ALA A O   
801  C CB  . ALA A 105 ? 0.2848 0.2790 0.2450 -0.0038 -0.0042 -0.0092 104 ALA A CB  
802  N N   . ALA A 106 ? 0.2810 0.2857 0.2429 -0.0038 -0.0106 -0.0030 105 ALA A N   
803  C CA  . ALA A 106 ? 0.2640 0.2727 0.2256 -0.0052 -0.0146 -0.0027 105 ALA A CA  
804  C C   . ALA A 106 ? 0.2732 0.2837 0.2340 -0.0031 -0.0149 -0.0029 105 ALA A C   
805  O O   . ALA A 106 ? 0.2652 0.2766 0.2239 -0.0040 -0.0174 -0.0063 105 ALA A O   
806  C CB  . ALA A 106 ? 0.2737 0.2857 0.2378 -0.0060 -0.0166 0.0029  105 ALA A CB  
807  N N   . GLN A 107 ? 0.2781 0.2887 0.2402 -0.0002 -0.0125 0.0009  106 GLN A N   
808  C CA  . GLN A 107 ? 0.2633 0.2755 0.2245 0.0019  -0.0125 0.0011  106 GLN A CA  
809  C C   . GLN A 107 ? 0.3030 0.3116 0.2607 0.0025  -0.0116 -0.0051 106 GLN A C   
810  O O   . GLN A 107 ? 0.2871 0.2968 0.2427 0.0023  -0.0137 -0.0075 106 GLN A O   
811  C CB  . GLN A 107 ? 0.2879 0.3008 0.2513 0.0051  -0.0096 0.0062  106 GLN A CB  
812  C CG  . GLN A 107 ? 0.3013 0.3155 0.2637 0.0074  -0.0092 0.0065  106 GLN A CG  
813  C CD  . GLN A 107 ? 0.3070 0.3167 0.2667 0.0098  -0.0058 0.0029  106 GLN A CD  
814  O OE1 . GLN A 107 ? 0.3413 0.3480 0.3016 0.0113  -0.0025 0.0036  106 GLN A OE1 
815  N NE2 . GLN A 107 ? 0.3420 0.3507 0.2985 0.0101  -0.0068 -0.0012 106 GLN A NE2 
816  N N   . GLN A 108 ? 0.2822 0.2862 0.2390 0.0030  -0.0087 -0.0078 107 GLN A N   
817  C CA  . GLN A 108 ? 0.3260 0.3260 0.2795 0.0036  -0.0078 -0.0137 107 GLN A CA  
818  C C   . GLN A 108 ? 0.3138 0.3140 0.2656 0.0006  -0.0112 -0.0187 107 GLN A C   
819  O O   . GLN A 108 ? 0.3303 0.3291 0.2795 0.0009  -0.0121 -0.0230 107 GLN A O   
820  C CB  . GLN A 108 ? 0.3192 0.3142 0.2724 0.0046  -0.0044 -0.0153 107 GLN A CB  
821  C CG  . GLN A 108 ? 0.3290 0.3230 0.2832 0.0080  -0.0009 -0.0114 107 GLN A CG  
822  C CD  . GLN A 108 ? 0.3725 0.3660 0.3246 0.0109  0.0000  -0.0122 107 GLN A CD  
823  O OE1 . GLN A 108 ? 0.3971 0.3872 0.3460 0.0112  -0.0001 -0.0172 107 GLN A OE1 
824  N NE2 . GLN A 108 ? 0.4143 0.4108 0.3680 0.0131  0.0009  -0.0071 107 GLN A NE2 
825  N N   . SER A 109 ? 0.3036 0.3055 0.2569 -0.0022 -0.0131 -0.0182 108 SER A N   
826  C CA  . SER A 109 ? 0.3199 0.3224 0.2717 -0.0051 -0.0163 -0.0227 108 SER A CA  
827  C C   . SER A 109 ? 0.3381 0.3441 0.2888 -0.0052 -0.0198 -0.0227 108 SER A C   
828  O O   . SER A 109 ? 0.3017 0.3069 0.2501 -0.0062 -0.0217 -0.0277 108 SER A O   
829  C CB  . SER A 109 ? 0.3082 0.3121 0.2618 -0.0078 -0.0175 -0.0214 108 SER A CB  
830  O OG  . SER A 109 ? 0.3261 0.3262 0.2802 -0.0080 -0.0145 -0.0225 108 SER A OG  
831  N N   . VAL A 110 ? 0.2983 0.3084 0.2508 -0.0045 -0.0208 -0.0172 109 VAL A N   
832  C CA  . VAL A 110 ? 0.2687 0.2823 0.2203 -0.0046 -0.0241 -0.0167 109 VAL A CA  
833  C C   . VAL A 110 ? 0.2785 0.2900 0.2275 -0.0024 -0.0230 -0.0194 109 VAL A C   
834  O O   . VAL A 110 ? 0.2907 0.3024 0.2371 -0.0032 -0.0257 -0.0232 109 VAL A O   
835  C CB  . VAL A 110 ? 0.2666 0.2846 0.2209 -0.0040 -0.0251 -0.0097 109 VAL A CB  
836  C CG1 . VAL A 110 ? 0.3106 0.3320 0.2640 -0.0035 -0.0279 -0.0087 109 VAL A CG1 
837  C CG2 . VAL A 110 ? 0.2733 0.2932 0.2295 -0.0065 -0.0272 -0.0077 109 VAL A CG2 
838  N N   . THR A 111 ? 0.3043 0.3135 0.2536 0.0005  -0.0191 -0.0176 110 THR A N   
839  C CA  . THR A 111 ? 0.2971 0.3039 0.2436 0.0029  -0.0178 -0.0199 110 THR A CA  
840  C C   . THR A 111 ? 0.3006 0.3029 0.2440 0.0021  -0.0181 -0.0271 110 THR A C   
841  O O   . THR A 111 ? 0.3296 0.3308 0.2700 0.0026  -0.0195 -0.0304 110 THR A O   
842  C CB  . THR A 111 ? 0.3033 0.3084 0.2509 0.0062  -0.0134 -0.0165 110 THR A CB  
843  O OG1 . THR A 111 ? 0.3044 0.3139 0.2554 0.0068  -0.0132 -0.0098 110 THR A OG1 
844  C CG2 . THR A 111 ? 0.3519 0.3546 0.2965 0.0090  -0.0119 -0.0183 110 THR A CG2 
845  N N   . LEU A 112 ? 0.2784 0.2777 0.2223 0.0009  -0.0169 -0.0296 111 LEU A N   
846  C CA  . LEU A 112 ? 0.3188 0.3137 0.2601 0.0001  -0.0172 -0.0363 111 LEU A CA  
847  C C   . LEU A 112 ? 0.3243 0.3210 0.2642 -0.0025 -0.0215 -0.0401 111 LEU A C   
848  O O   . LEU A 112 ? 0.3721 0.3656 0.3093 -0.0026 -0.0224 -0.0456 111 LEU A O   
849  C CB  . LEU A 112 ? 0.3037 0.2957 0.2463 -0.0011 -0.0152 -0.0378 111 LEU A CB  
850  C CG  . LEU A 112 ? 0.3555 0.3435 0.2982 0.0016  -0.0109 -0.0367 111 LEU A CG  
851  C CD1 . LEU A 112 ? 0.3555 0.3421 0.3003 -0.0001 -0.0096 -0.0367 111 LEU A CD1 
852  C CD2 . LEU A 112 ? 0.4255 0.4083 0.3650 0.0036  -0.0098 -0.0414 111 LEU A CD2 
853  N N   . ALA A 113 ? 0.2935 0.2950 0.2350 -0.0045 -0.0244 -0.0375 112 ALA A N   
854  C CA  . ALA A 113 ? 0.2976 0.3012 0.2378 -0.0070 -0.0287 -0.0409 112 ALA A CA  
855  C C   . ALA A 113 ? 0.3072 0.3132 0.2456 -0.0061 -0.0312 -0.0399 112 ALA A C   
856  O O   . ALA A 113 ? 0.3354 0.3439 0.2729 -0.0081 -0.0353 -0.0417 112 ALA A O   
857  C CB  . ALA A 113 ? 0.3159 0.3231 0.2583 -0.0097 -0.0309 -0.0388 112 ALA A CB  
858  N N   . GLY A 114 ? 0.3104 0.3158 0.2483 -0.0032 -0.0289 -0.0371 113 GLY A N   
859  C CA  . GLY A 114 ? 0.2872 0.2946 0.2234 -0.0022 -0.0308 -0.0361 113 GLY A CA  
860  C C   . GLY A 114 ? 0.3194 0.3319 0.2580 -0.0015 -0.0313 -0.0291 113 GLY A C   
861  O O   . GLY A 114 ? 0.3560 0.3707 0.2935 -0.0008 -0.0330 -0.0277 113 GLY A O   
862  N N   . GLY A 115 ? 0.3005 0.3150 0.2427 -0.0018 -0.0300 -0.0247 114 GLY A N   
863  C CA  . GLY A 115 ? 0.2856 0.3049 0.2305 -0.0014 -0.0308 -0.0180 114 GLY A CA  
864  C C   . GLY A 115 ? 0.3120 0.3312 0.2580 0.0019  -0.0271 -0.0138 114 GLY A C   
865  O O   . GLY A 115 ? 0.3305 0.3457 0.2745 0.0041  -0.0240 -0.0161 114 GLY A O   
866  N N   . PRO A 116 ? 0.3316 0.3551 0.2808 0.0023  -0.0274 -0.0074 115 PRO A N   
867  C CA  . PRO A 116 ? 0.3325 0.3564 0.2832 0.0055  -0.0239 -0.0028 115 PRO A CA  
868  C C   . PRO A 116 ? 0.3083 0.3287 0.2601 0.0072  -0.0193 -0.0025 115 PRO A C   
869  O O   . PRO A 116 ? 0.3161 0.3347 0.2687 0.0057  -0.0189 -0.0041 115 PRO A O   
870  C CB  . PRO A 116 ? 0.3331 0.3626 0.2877 0.0050  -0.0259 0.0038  115 PRO A CB  
871  C CG  . PRO A 116 ? 0.3274 0.3581 0.2828 0.0018  -0.0292 0.0031  115 PRO A CG  
872  C CD  . PRO A 116 ? 0.3142 0.3422 0.2657 0.0001  -0.0312 -0.0040 115 PRO A CD  
873  N N   . SER A 117 ? 0.3166 0.3360 0.2685 0.0104  -0.0158 -0.0003 116 SER A N   
874  C CA  . SER A 117 ? 0.3242 0.3404 0.2771 0.0126  -0.0113 0.0005  116 SER A CA  
875  C C   . SER A 117 ? 0.3236 0.3432 0.2804 0.0146  -0.0095 0.0075  116 SER A C   
876  O O   . SER A 117 ? 0.3452 0.3678 0.3025 0.0159  -0.0097 0.0105  116 SER A O   
877  C CB  . SER A 117 ? 0.3610 0.3722 0.3100 0.0151  -0.0087 -0.0037 116 SER A CB  
878  O OG  . SER A 117 ? 0.4412 0.4490 0.3908 0.0173  -0.0046 -0.0031 116 SER A OG  
879  N N   . TRP A 118 ? 0.3123 0.3315 0.2721 0.0146  -0.0076 0.0102  117 TRP A N   
880  C CA  . TRP A 118 ? 0.3199 0.3422 0.2838 0.0164  -0.0059 0.0168  117 TRP A CA  
881  C C   . TRP A 118 ? 0.3075 0.3269 0.2730 0.0171  -0.0029 0.0178  117 TRP A C   
882  O O   . TRP A 118 ? 0.3462 0.3621 0.3101 0.0155  -0.0029 0.0138  117 TRP A O   
883  C CB  . TRP A 118 ? 0.3474 0.3751 0.3145 0.0143  -0.0097 0.0212  117 TRP A CB  
884  C CG  . TRP A 118 ? 0.3196 0.3475 0.2884 0.0115  -0.0118 0.0217  117 TRP A CG  
885  C CD1 . TRP A 118 ? 0.3486 0.3778 0.3213 0.0115  -0.0113 0.0265  117 TRP A CD1 
886  C CD2 . TRP A 118 ? 0.2930 0.3197 0.2596 0.0084  -0.0148 0.0172  117 TRP A CD2 
887  N NE1 . TRP A 118 ? 0.3518 0.3805 0.3245 0.0086  -0.0137 0.0254  117 TRP A NE1 
888  C CE2 . TRP A 118 ? 0.3452 0.3725 0.3143 0.0066  -0.0158 0.0197  117 TRP A CE2 
889  C CE3 . TRP A 118 ? 0.3376 0.3627 0.3003 0.0070  -0.0167 0.0112  117 TRP A CE3 
890  C CZ2 . TRP A 118 ? 0.3312 0.3577 0.2990 0.0036  -0.0185 0.0165  117 TRP A CZ2 
891  C CZ3 . TRP A 118 ? 0.3159 0.3403 0.2775 0.0039  -0.0194 0.0081  117 TRP A CZ3 
892  C CH2 . TRP A 118 ? 0.3005 0.3257 0.2647 0.0023  -0.0202 0.0108  117 TRP A CH2 
893  N N   . ARG A 119 ? 0.3199 0.3408 0.2886 0.0195  -0.0003 0.0229  118 ARG A N   
894  C CA  . ARG A 119 ? 0.3298 0.3483 0.3004 0.0205  0.0026  0.0246  118 ARG A CA  
895  C C   . ARG A 119 ? 0.3109 0.3324 0.2855 0.0184  0.0004  0.0288  118 ARG A C   
896  O O   . ARG A 119 ? 0.3392 0.3650 0.3172 0.0188  -0.0006 0.0341  118 ARG A O   
897  C CB  . ARG A 119 ? 0.3822 0.4005 0.3539 0.0245  0.0066  0.0277  118 ARG A CB  
898  C CG  . ARG A 119 ? 0.4292 0.4437 0.3967 0.0271  0.0092  0.0237  118 ARG A CG  
899  C CD  . ARG A 119 ? 0.5682 0.5811 0.5368 0.0309  0.0136  0.0265  118 ARG A CD  
900  N NE  . ARG A 119 ? 0.6429 0.6516 0.6113 0.0308  0.0154  0.0250  118 ARG A NE  
901  C CZ  . ARG A 119 ? 0.5367 0.5444 0.5070 0.0333  0.0186  0.0279  118 ARG A CZ  
902  N NH1 . ARG A 119 ? 0.6266 0.6373 0.5995 0.0361  0.0205  0.0327  118 ARG A NH1 
903  N NH2 . ARG A 119 ? 0.5756 0.5790 0.5450 0.0330  0.0198  0.0259  118 ARG A NH2 
904  N N   . VAL A 120 ? 0.3087 0.3275 0.2828 0.0161  -0.0002 0.0267  119 VAL A N   
905  C CA  . VAL A 120 ? 0.2979 0.3188 0.2752 0.0140  -0.0024 0.0304  119 VAL A CA  
906  C C   . VAL A 120 ? 0.2532 0.2741 0.2341 0.0161  0.0002  0.0355  119 VAL A C   
907  O O   . VAL A 120 ? 0.2961 0.3139 0.2763 0.0184  0.0039  0.0346  119 VAL A O   
908  C CB  . VAL A 120 ? 0.2898 0.3076 0.2652 0.0110  -0.0037 0.0264  119 VAL A CB  
909  C CG1 . VAL A 120 ? 0.3181 0.3360 0.2902 0.0090  -0.0065 0.0213  119 VAL A CG1 
910  C CG2 . VAL A 120 ? 0.3194 0.3322 0.2935 0.0121  -0.0001 0.0238  119 VAL A CG2 
911  N N   . PRO A 121 ? 0.2924 0.3167 0.2772 0.0155  -0.0016 0.0408  120 PRO A N   
912  C CA  . PRO A 121 ? 0.2533 0.2769 0.2416 0.0169  0.0005  0.0452  120 PRO A CA  
913  C C   . PRO A 121 ? 0.2972 0.3161 0.2840 0.0156  0.0017  0.0426  120 PRO A C   
914  O O   . PRO A 121 ? 0.3264 0.3437 0.3109 0.0128  -0.0004 0.0391  120 PRO A O   
915  C CB  . PRO A 121 ? 0.3307 0.3586 0.3231 0.0157  -0.0027 0.0507  120 PRO A CB  
916  C CG  . PRO A 121 ? 0.3610 0.3924 0.3521 0.0145  -0.0060 0.0498  120 PRO A CG  
917  C CD  . PRO A 121 ? 0.3701 0.3986 0.3563 0.0133  -0.0060 0.0430  120 PRO A CD  
918  N N   . LEU A 122 ? 0.2896 0.3061 0.2777 0.0177  0.0050  0.0442  121 LEU A N   
919  C CA  . LEU A 122 ? 0.3129 0.3245 0.2994 0.0169  0.0065  0.0417  121 LEU A CA  
920  C C   . LEU A 122 ? 0.2908 0.3019 0.2808 0.0179  0.0077  0.0465  121 LEU A C   
921  O O   . LEU A 122 ? 0.3104 0.3248 0.3042 0.0196  0.0078  0.0515  121 LEU A O   
922  C CB  . LEU A 122 ? 0.2841 0.2918 0.2671 0.0187  0.0097  0.0370  121 LEU A CB  
923  C CG  . LEU A 122 ? 0.3123 0.3195 0.2914 0.0176  0.0085  0.0315  121 LEU A CG  
924  C CD1 . LEU A 122 ? 0.3805 0.3844 0.3567 0.0202  0.0116  0.0280  121 LEU A CD1 
925  C CD2 . LEU A 122 ? 0.3327 0.3377 0.3100 0.0140  0.0064  0.0279  121 LEU A CD2 
926  N N   . GLY A 123 ? 0.2589 0.2658 0.2479 0.0168  0.0086  0.0450  122 GLY A N   
927  C CA  . GLY A 123 ? 0.2870 0.2927 0.2789 0.0172  0.0093  0.0491  122 GLY A CA  
928  C C   . GLY A 123 ? 0.2589 0.2633 0.2511 0.0140  0.0067  0.0499  122 GLY A C   
929  O O   . GLY A 123 ? 0.3065 0.3097 0.3011 0.0142  0.0068  0.0535  122 GLY A O   
930  N N   . ARG A 124 ? 0.2569 0.2613 0.2466 0.0111  0.0042  0.0466  123 ARG A N   
931  C CA  . ARG A 124 ? 0.2782 0.2810 0.2676 0.0081  0.0019  0.0469  123 ARG A CA  
932  C C   . ARG A 124 ? 0.2830 0.2803 0.2705 0.0075  0.0041  0.0447  123 ARG A C   
933  O O   . ARG A 124 ? 0.3082 0.3029 0.2935 0.0085  0.0068  0.0411  123 ARG A O   
934  C CB  . ARG A 124 ? 0.2670 0.2710 0.2538 0.0054  -0.0010 0.0433  123 ARG A CB  
935  C CG  . ARG A 124 ? 0.2742 0.2832 0.2621 0.0056  -0.0036 0.0449  123 ARG A CG  
936  C CD  . ARG A 124 ? 0.2867 0.2965 0.2716 0.0032  -0.0059 0.0403  123 ARG A CD  
937  N NE  . ARG A 124 ? 0.3062 0.3205 0.2916 0.0038  -0.0079 0.0412  123 ARG A NE  
938  C CZ  . ARG A 124 ? 0.2938 0.3093 0.2787 0.0059  -0.0062 0.0398  123 ARG A CZ  
939  N NH1 . ARG A 124 ? 0.2977 0.3100 0.2811 0.0077  -0.0026 0.0370  123 ARG A NH1 
940  N NH2 . ARG A 124 ? 0.3060 0.3257 0.2916 0.0064  -0.0083 0.0412  123 ARG A NH2 
941  N N   . ARG A 125 ? 0.2595 0.2550 0.2478 0.0057  0.0028  0.0469  124 ARG A N   
942  C CA  . ARG A 125 ? 0.2743 0.2646 0.2607 0.0046  0.0044  0.0449  124 ARG A CA  
943  C C   . ARG A 125 ? 0.2791 0.2679 0.2633 0.0010  0.0020  0.0429  124 ARG A C   
944  O O   . ARG A 125 ? 0.2708 0.2626 0.2553 -0.0005 -0.0011 0.0438  124 ARG A O   
945  C CB  . ARG A 125 ? 0.2804 0.2688 0.2693 0.0061  0.0056  0.0493  124 ARG A CB  
946  C CG  . ARG A 125 ? 0.3317 0.3208 0.3220 0.0097  0.0086  0.0501  124 ARG A CG  
947  C CD  . ARG A 125 ? 0.3780 0.3661 0.3714 0.0115  0.0096  0.0548  124 ARG A CD  
948  N NE  . ARG A 125 ? 0.3809 0.3636 0.3727 0.0105  0.0107  0.0538  124 ARG A NE  
949  C CZ  . ARG A 125 ? 0.3721 0.3513 0.3622 0.0120  0.0137  0.0515  124 ARG A CZ  
950  N NH1 . ARG A 125 ? 0.3894 0.3697 0.3787 0.0144  0.0159  0.0494  124 ARG A NH1 
951  N NH2 . ARG A 125 ? 0.3742 0.3486 0.3632 0.0111  0.0144  0.0514  124 ARG A NH2 
952  N N   . ASP A 126 ? 0.2794 0.2636 0.2612 -0.0004 0.0036  0.0401  125 ASP A N   
953  C CA  . ASP A 126 ? 0.3317 0.3141 0.3109 -0.0037 0.0022  0.0370  125 ASP A CA  
954  C C   . ASP A 126 ? 0.3157 0.2960 0.2954 -0.0054 0.0006  0.0403  125 ASP A C   
955  O O   . ASP A 126 ? 0.3199 0.2974 0.3007 -0.0044 0.0019  0.0431  125 ASP A O   
956  C CB  . ASP A 126 ? 0.3025 0.2810 0.2789 -0.0044 0.0047  0.0318  125 ASP A CB  
957  C CG  . ASP A 126 ? 0.3800 0.3601 0.3554 -0.0029 0.0059  0.0280  125 ASP A CG  
958  O OD1 . ASP A 126 ? 0.3313 0.3154 0.3070 -0.0029 0.0040  0.0279  125 ASP A OD1 
959  O OD2 . ASP A 126 ? 0.3690 0.3461 0.3431 -0.0018 0.0086  0.0253  125 ASP A OD2 
960  N N   . SER A 127 ? 0.3059 0.2872 0.2845 -0.0078 -0.0023 0.0400  126 SER A N   
961  C CA  . SER A 127 ? 0.3084 0.2876 0.2869 -0.0095 -0.0042 0.0429  126 SER A CA  
962  C C   . SER A 127 ? 0.3188 0.2923 0.2950 -0.0110 -0.0021 0.0409  126 SER A C   
963  O O   . SER A 127 ? 0.3442 0.3159 0.3184 -0.0115 0.0002  0.0365  126 SER A O   
964  C CB  . SER A 127 ? 0.3478 0.3291 0.3250 -0.0117 -0.0076 0.0422  126 SER A CB  
965  O OG  . SER A 127 ? 0.4292 0.4093 0.4033 -0.0137 -0.0068 0.0368  126 SER A OG  
966  N N   . LEU A 128 ? 0.3201 0.2908 0.2965 -0.0118 -0.0031 0.0443  127 LEU A N   
967  C CA  . LEU A 128 ? 0.3298 0.2948 0.3038 -0.0134 -0.0015 0.0430  127 LEU A CA  
968  C C   . LEU A 128 ? 0.3060 0.2696 0.2772 -0.0166 -0.0033 0.0414  127 LEU A C   
969  O O   . LEU A 128 ? 0.3833 0.3422 0.3523 -0.0183 -0.0023 0.0405  127 LEU A O   
970  C CB  . LEU A 128 ? 0.3543 0.3163 0.3299 -0.0123 -0.0013 0.0476  127 LEU A CB  
971  C CG  . LEU A 128 ? 0.4328 0.3962 0.4115 -0.0090 0.0005  0.0496  127 LEU A CG  
972  C CD1 . LEU A 128 ? 0.4356 0.3962 0.4162 -0.0080 0.0003  0.0544  127 LEU A CD1 
973  C CD2 . LEU A 128 ? 0.4239 0.3855 0.4010 -0.0084 0.0040  0.0454  127 LEU A CD2 
974  N N   . GLN A 129 ? 0.3212 0.2887 0.2922 -0.0174 -0.0059 0.0408  128 GLN A N   
975  C CA  . GLN A 129 ? 0.3411 0.3076 0.3095 -0.0201 -0.0079 0.0395  128 GLN A CA  
976  C C   . GLN A 129 ? 0.3282 0.2997 0.2965 -0.0205 -0.0101 0.0374  128 GLN A C   
977  O O   . GLN A 129 ? 0.2976 0.2731 0.2679 -0.0187 -0.0105 0.0379  128 GLN A O   
978  C CB  . GLN A 129 ? 0.4200 0.3843 0.3885 -0.0205 -0.0103 0.0443  128 GLN A CB  
979  C CG  . GLN A 129 ? 0.4716 0.4396 0.4433 -0.0186 -0.0130 0.0490  128 GLN A CG  
980  C CD  . GLN A 129 ? 0.4844 0.4492 0.4567 -0.0185 -0.0149 0.0541  128 GLN A CD  
981  O OE1 . GLN A 129 ? 0.5515 0.5121 0.5211 -0.0204 -0.0154 0.0540  128 GLN A OE1 
982  N NE2 . GLN A 129 ? 0.4872 0.4540 0.4631 -0.0163 -0.0160 0.0585  128 GLN A NE2 
983  N N   . ALA A 130 ? 0.3399 0.3109 0.3055 -0.0229 -0.0114 0.0349  129 ALA A N   
984  C CA  . ALA A 130 ? 0.3226 0.2978 0.2875 -0.0237 -0.0138 0.0327  129 ALA A CA  
985  C C   . ALA A 130 ? 0.3070 0.2826 0.2711 -0.0247 -0.0177 0.0359  129 ALA A C   
986  O O   . ALA A 130 ? 0.3259 0.2976 0.2890 -0.0253 -0.0180 0.0386  129 ALA A O   
987  C CB  . ALA A 130 ? 0.3733 0.3480 0.3359 -0.0257 -0.0123 0.0268  129 ALA A CB  
988  N N   . PHE A 131 ? 0.3288 0.3087 0.2929 -0.0247 -0.0207 0.0355  130 PHE A N   
989  C CA  . PHE A 131 ? 0.3214 0.3024 0.2852 -0.0251 -0.0249 0.0391  130 PHE A CA  
990  C C   . PHE A 131 ? 0.3014 0.2845 0.2626 -0.0269 -0.0273 0.0358  130 PHE A C   
991  O O   . PHE A 131 ? 0.3040 0.2914 0.2658 -0.0263 -0.0301 0.0359  130 PHE A O   
992  C CB  . PHE A 131 ? 0.3456 0.3302 0.3127 -0.0228 -0.0270 0.0434  130 PHE A CB  
993  C CG  . PHE A 131 ? 0.3207 0.3040 0.2907 -0.0208 -0.0246 0.0464  130 PHE A CG  
994  C CD1 . PHE A 131 ? 0.3626 0.3425 0.3334 -0.0204 -0.0252 0.0510  130 PHE A CD1 
995  C CD2 . PHE A 131 ? 0.3692 0.3544 0.3410 -0.0192 -0.0218 0.0446  130 PHE A CD2 
996  C CE1 . PHE A 131 ? 0.4304 0.4091 0.4040 -0.0185 -0.0230 0.0537  130 PHE A CE1 
997  C CE2 . PHE A 131 ? 0.3375 0.3215 0.3118 -0.0172 -0.0196 0.0474  130 PHE A CE2 
998  C CZ  . PHE A 131 ? 0.3835 0.3644 0.3589 -0.0169 -0.0202 0.0519  130 PHE A CZ  
999  N N   . LEU A 132 ? 0.3031 0.2800 0.2934 -0.0155 0.0194  0.0041  131 LEU A N   
1000 C CA  . LEU A 132 ? 0.2928 0.2697 0.2802 -0.0150 0.0238  0.0015  131 LEU A CA  
1001 C C   . LEU A 132 ? 0.3163 0.2887 0.2981 -0.0148 0.0211  0.0002  131 LEU A C   
1002 O O   . LEU A 132 ? 0.2930 0.2682 0.2782 -0.0138 0.0225  -0.0018 131 LEU A O   
1003 C CB  . LEU A 132 ? 0.2976 0.2710 0.2770 -0.0160 0.0284  0.0014  131 LEU A CB  
1004 C CG  . LEU A 132 ? 0.3241 0.2962 0.2985 -0.0156 0.0329  -0.0012 131 LEU A CG  
1005 C CD1 . LEU A 132 ? 0.3031 0.2825 0.2871 -0.0142 0.0356  -0.0031 131 LEU A CD1 
1006 C CD2 . LEU A 132 ? 0.3285 0.2980 0.2963 -0.0166 0.0378  -0.0011 131 LEU A CD2 
1007 N N   . ASP A 133 ? 0.3223 0.2873 0.2952 -0.0157 0.0174  0.0011  132 ASP A N   
1008 C CA  . ASP A 133 ? 0.3110 0.2713 0.2784 -0.0154 0.0145  -0.0002 132 ASP A CA  
1009 C C   . ASP A 133 ? 0.3486 0.3134 0.3252 -0.0144 0.0110  -0.0004 132 ASP A C   
1010 O O   . ASP A 133 ? 0.3273 0.2921 0.3039 -0.0137 0.0110  -0.0023 132 ASP A O   
1011 C CB  . ASP A 133 ? 0.3722 0.3241 0.3294 -0.0164 0.0103  0.0011  132 ASP A CB  
1012 C CG  . ASP A 133 ? 0.4543 0.4004 0.4004 -0.0173 0.0138  0.0010  132 ASP A CG  
1013 O OD1 . ASP A 133 ? 0.4003 0.3473 0.3442 -0.0169 0.0190  -0.0008 132 ASP A OD1 
1014 O OD2 . ASP A 133 ? 0.5518 0.4924 0.4913 -0.0183 0.0112  0.0028  132 ASP A OD2 
1015 N N   . LEU A 134 ? 0.3049 0.2736 0.2895 -0.0145 0.0079  0.0015  133 LEU A N   
1016 C CA  . LEU A 134 ? 0.3099 0.2833 0.3037 -0.0136 0.0048  0.0015  133 LEU A CA  
1017 C C   . LEU A 134 ? 0.3276 0.3078 0.3291 -0.0124 0.0089  -0.0002 133 LEU A C   
1018 O O   . LEU A 134 ? 0.3264 0.3083 0.3317 -0.0116 0.0076  -0.0013 133 LEU A O   
1019 C CB  . LEU A 134 ? 0.3077 0.2842 0.3085 -0.0138 0.0012  0.0040  133 LEU A CB  
1020 C CG  . LEU A 134 ? 0.3274 0.3077 0.3368 -0.0131 -0.0029 0.0044  133 LEU A CG  
1021 C CD1 . LEU A 134 ? 0.3561 0.3305 0.3598 -0.0135 -0.0075 0.0040  133 LEU A CD1 
1022 C CD2 . LEU A 134 ? 0.3562 0.3399 0.3725 -0.0132 -0.0058 0.0069  133 LEU A CD2 
1023 N N   . ALA A 135 ? 0.2879 0.2718 0.2917 -0.0122 0.0140  -0.0006 134 ALA A N   
1024 C CA  . ALA A 135 ? 0.2706 0.2605 0.2812 -0.0110 0.0181  -0.0024 134 ALA A CA  
1025 C C   . ALA A 135 ? 0.3094 0.2961 0.3140 -0.0107 0.0198  -0.0050 134 ALA A C   
1026 O O   . ALA A 135 ? 0.3267 0.3167 0.3363 -0.0096 0.0202  -0.0064 134 ALA A O   
1027 C CB  . ALA A 135 ? 0.2844 0.2783 0.2978 -0.0110 0.0232  -0.0024 134 ALA A CB  
1028 N N   . ASN A 136 ? 0.2840 0.2640 0.2775 -0.0115 0.0209  -0.0055 135 ASN A N   
1029 C CA  . ASN A 136 ? 0.3141 0.2906 0.3013 -0.0110 0.0226  -0.0080 135 ASN A CA  
1030 C C   . ASN A 136 ? 0.3319 0.3058 0.3185 -0.0107 0.0176  -0.0084 135 ASN A C   
1031 O O   . ASN A 136 ? 0.3809 0.3545 0.3666 -0.0099 0.0186  -0.0106 135 ASN A O   
1032 C CB  . ASN A 136 ? 0.2936 0.2633 0.2688 -0.0119 0.0248  -0.0082 135 ASN A CB  
1033 C CG  . ASN A 136 ? 0.3259 0.2986 0.3016 -0.0120 0.0311  -0.0088 135 ASN A CG  
1034 O OD1 . ASN A 136 ? 0.3579 0.3370 0.3416 -0.0111 0.0343  -0.0100 135 ASN A OD1 
1035 N ND2 . ASN A 136 ? 0.3768 0.3447 0.3440 -0.0131 0.0328  -0.0080 135 ASN A ND2 
1036 N N   . ALA A 137 ? 0.3254 0.2974 0.3126 -0.0113 0.0122  -0.0064 136 ALA A N   
1037 C CA  . ALA A 137 ? 0.3270 0.2964 0.3140 -0.0111 0.0072  -0.0066 136 ALA A CA  
1038 C C   . ALA A 137 ? 0.3450 0.3215 0.3439 -0.0102 0.0059  -0.0065 136 ALA A C   
1039 O O   . ALA A 137 ? 0.3470 0.3229 0.3469 -0.0097 0.0039  -0.0077 136 ALA A O   
1040 C CB  . ALA A 137 ? 0.3710 0.3351 0.3535 -0.0122 0.0017  -0.0045 136 ALA A CB  
1041 N N   . ASN A 138 ? 0.2830 0.2659 0.2909 -0.0100 0.0070  -0.0052 137 ASN A N   
1042 C CA  . ASN A 138 ? 0.2816 0.2706 0.3004 -0.0093 0.0049  -0.0045 137 ASN A CA  
1043 C C   . ASN A 138 ? 0.3228 0.3181 0.3487 -0.0080 0.0091  -0.0062 137 ASN A C   
1044 O O   . ASN A 138 ? 0.2901 0.2890 0.3230 -0.0072 0.0074  -0.0064 137 ASN A O   
1045 C CB  . ASN A 138 ? 0.2636 0.2562 0.2888 -0.0095 0.0030  -0.0019 137 ASN A CB  
1046 C CG  . ASN A 138 ? 0.2977 0.2857 0.3196 -0.0105 -0.0026 -0.0001 137 ASN A CG  
1047 O OD1 . ASN A 138 ? 0.3066 0.2878 0.3200 -0.0111 -0.0050 -0.0006 137 ASN A OD1 
1048 N ND2 . ASN A 138 ? 0.3004 0.2919 0.3288 -0.0106 -0.0050 0.0021  137 ASN A ND2 
1049 N N   . LEU A 139 ? 0.2930 0.2898 0.3175 -0.0077 0.0143  -0.0074 138 LEU A N   
1050 C CA  . LEU A 139 ? 0.2842 0.2874 0.3162 -0.0064 0.0181  -0.0090 138 LEU A CA  
1051 C C   . LEU A 139 ? 0.2803 0.2816 0.3095 -0.0057 0.0187  -0.0114 138 LEU A C   
1052 O O   . LEU A 139 ? 0.3402 0.3356 0.3600 -0.0061 0.0194  -0.0127 138 LEU A O   
1053 C CB  . LEU A 139 ? 0.2948 0.3004 0.3267 -0.0063 0.0236  -0.0095 138 LEU A CB  
1054 C CG  . LEU A 139 ? 0.2683 0.2767 0.3042 -0.0068 0.0236  -0.0072 138 LEU A CG  
1055 C CD1 . LEU A 139 ? 0.3211 0.3308 0.3556 -0.0068 0.0289  -0.0079 138 LEU A CD1 
1056 C CD2 . LEU A 139 ? 0.2936 0.3089 0.3410 -0.0058 0.0219  -0.0061 138 LEU A CD2 
1057 N N   . PRO A 140 ? 0.2968 0.3026 0.3337 -0.0047 0.0181  -0.0121 139 PRO A N   
1058 C CA  . PRO A 140 ? 0.3098 0.3137 0.3443 -0.0040 0.0184  -0.0145 139 PRO A CA  
1059 C C   . PRO A 140 ? 0.3235 0.3284 0.3559 -0.0033 0.0241  -0.0169 139 PRO A C   
1060 O O   . PRO A 140 ? 0.3392 0.3477 0.3742 -0.0031 0.0279  -0.0168 139 PRO A O   
1061 C CB  . PRO A 140 ? 0.3004 0.3096 0.3449 -0.0032 0.0163  -0.0141 139 PRO A CB  
1062 C CG  . PRO A 140 ? 0.3619 0.3775 0.4147 -0.0028 0.0179  -0.0125 139 PRO A CG  
1063 C CD  . PRO A 140 ? 0.3058 0.3187 0.3540 -0.0040 0.0174  -0.0107 139 PRO A CD  
1064 N N   . ALA A 141 ? 0.2910 0.2927 0.3186 -0.0028 0.0246  -0.0193 140 ALA A N   
1065 C CA  . ALA A 141 ? 0.2866 0.2886 0.3112 -0.0021 0.0298  -0.0218 140 ALA A CA  
1066 C C   . ALA A 141 ? 0.2643 0.2696 0.2941 -0.0007 0.0307  -0.0239 140 ALA A C   
1067 O O   . ALA A 141 ? 0.2613 0.2662 0.2936 -0.0005 0.0269  -0.0237 140 ALA A O   
1068 C CB  . ALA A 141 ? 0.3212 0.3156 0.3335 -0.0027 0.0303  -0.0230 140 ALA A CB  
1069 N N   . PRO A 142 ? 0.2592 0.2678 0.2909 0.0003  0.0358  -0.0259 141 PRO A N   
1070 C CA  . PRO A 142 ? 0.3225 0.3348 0.3601 0.0017  0.0367  -0.0279 141 PRO A CA  
1071 C C   . PRO A 142 ? 0.3287 0.3362 0.3606 0.0021  0.0350  -0.0299 141 PRO A C   
1072 O O   . PRO A 142 ? 0.3420 0.3518 0.3789 0.0032  0.0343  -0.0311 141 PRO A O   
1073 C CB  . PRO A 142 ? 0.2813 0.2977 0.3214 0.0026  0.0426  -0.0296 141 PRO A CB  
1074 C CG  . PRO A 142 ? 0.2990 0.3121 0.3318 0.0015  0.0450  -0.0291 141 PRO A CG  
1075 C CD  . PRO A 142 ? 0.3105 0.3205 0.3407 0.0001  0.0407  -0.0262 141 PRO A CD  
1076 N N   . PHE A 143 ? 0.2818 0.2825 0.3034 0.0014  0.0343  -0.0304 142 PHE A N   
1077 C CA  . PHE A 143 ? 0.3004 0.2959 0.3159 0.0017  0.0323  -0.0323 142 PHE A CA  
1078 C C   . PHE A 143 ? 0.3339 0.3254 0.3479 0.0009  0.0261  -0.0307 142 PHE A C   
1079 O O   . PHE A 143 ? 0.3438 0.3301 0.3517 0.0010  0.0237  -0.0320 142 PHE A O   
1080 C CB  . PHE A 143 ? 0.3134 0.3036 0.3181 0.0016  0.0352  -0.0341 142 PHE A CB  
1081 C CG  . PHE A 143 ? 0.3067 0.2934 0.3053 0.0002  0.0349  -0.0321 142 PHE A CG  
1082 C CD1 . PHE A 143 ? 0.3924 0.3734 0.3854 -0.0008 0.0300  -0.0306 142 PHE A CD1 
1083 C CD2 . PHE A 143 ? 0.3494 0.3385 0.3482 -0.0002 0.0394  -0.0317 142 PHE A CD2 
1084 C CE1 . PHE A 143 ? 0.4207 0.3983 0.4080 -0.0021 0.0295  -0.0287 142 PHE A CE1 
1085 C CE2 . PHE A 143 ? 0.4059 0.3916 0.3991 -0.0015 0.0390  -0.0297 142 PHE A CE2 
1086 C CZ  . PHE A 143 ? 0.3676 0.3476 0.3550 -0.0024 0.0341  -0.0283 142 PHE A CZ  
1087 N N   . PHE A 144 ? 0.2947 0.2888 0.3143 0.0001  0.0232  -0.0279 143 PHE A N   
1088 C CA  . PHE A 144 ? 0.2909 0.2819 0.3103 -0.0006 0.0172  -0.0262 143 PHE A CA  
1089 C C   . PHE A 144 ? 0.2988 0.2915 0.3236 0.0002  0.0150  -0.0271 143 PHE A C   
1090 O O   . PHE A 144 ? 0.3518 0.3503 0.3843 0.0012  0.0174  -0.0278 143 PHE A O   
1091 C CB  . PHE A 144 ? 0.2915 0.2857 0.3168 -0.0015 0.0149  -0.0230 143 PHE A CB  
1092 C CG  . PHE A 144 ? 0.3110 0.3011 0.3296 -0.0027 0.0143  -0.0214 143 PHE A CG  
1093 C CD1 . PHE A 144 ? 0.3190 0.3037 0.3272 -0.0030 0.0165  -0.0228 143 PHE A CD1 
1094 C CD2 . PHE A 144 ? 0.2940 0.2857 0.3166 -0.0036 0.0113  -0.0186 143 PHE A CD2 
1095 C CE1 . PHE A 144 ? 0.3494 0.3302 0.3513 -0.0042 0.0158  -0.0212 143 PHE A CE1 
1096 C CE2 . PHE A 144 ? 0.3086 0.2964 0.3251 -0.0047 0.0105  -0.0171 143 PHE A CE2 
1097 C CZ  . PHE A 144 ? 0.3115 0.2938 0.3175 -0.0050 0.0127  -0.0184 143 PHE A CZ  
1098 N N   . THR A 145 ? 0.3032 0.2906 0.3238 -0.0002 0.0104  -0.0272 144 THR A N   
1099 C CA  . THR A 145 ? 0.3126 0.3014 0.3389 0.0003  0.0074  -0.0274 144 THR A CA  
1100 C C   . THR A 145 ? 0.2842 0.2773 0.3195 -0.0003 0.0042  -0.0244 144 THR A C   
1101 O O   . THR A 145 ? 0.2976 0.2915 0.3336 -0.0012 0.0036  -0.0223 144 THR A O   
1102 C CB  . THR A 145 ? 0.3404 0.3220 0.3593 0.0000  0.0033  -0.0285 144 THR A CB  
1103 O OG1 . THR A 145 ? 0.3320 0.3092 0.3468 -0.0014 -0.0008 -0.0264 144 THR A OG1 
1104 C CG2 . THR A 145 ? 0.4037 0.3809 0.4134 0.0007  0.0066  -0.0315 144 THR A CG2 
1105 N N   . LEU A 146 ? 0.2764 0.2722 0.3186 0.0001  0.0020  -0.0243 145 LEU A N   
1106 C CA  . LEU A 146 ? 0.2785 0.2789 0.3297 -0.0004 -0.0007 -0.0215 145 LEU A CA  
1107 C C   . LEU A 146 ? 0.2809 0.2775 0.3294 -0.0018 -0.0055 -0.0192 145 LEU A C   
1108 O O   . LEU A 146 ? 0.2419 0.2417 0.2949 -0.0023 -0.0059 -0.0168 145 LEU A O   
1109 C CB  . LEU A 146 ? 0.2536 0.2567 0.3119 0.0003  -0.0023 -0.0217 145 LEU A CB  
1110 C CG  . LEU A 146 ? 0.2284 0.2369 0.2966 -0.0001 -0.0047 -0.0188 145 LEU A CG  
1111 C CD1 . LEU A 146 ? 0.2522 0.2667 0.3258 0.0004  -0.0011 -0.0176 145 LEU A CD1 
1112 C CD2 . LEU A 146 ? 0.2568 0.2680 0.3317 0.0006  -0.0057 -0.0192 145 LEU A CD2 
1113 N N   . PRO A 147 ? 0.2644 0.2541 0.3059 -0.0025 -0.0093 -0.0197 146 PRO A N   
1114 C CA  . PRO A 147 ? 0.2882 0.2743 0.3272 -0.0038 -0.0139 -0.0175 146 PRO A CA  
1115 C C   . PRO A 147 ? 0.2809 0.2659 0.3151 -0.0043 -0.0119 -0.0166 146 PRO A C   
1116 O O   . PRO A 147 ? 0.2939 0.2793 0.3300 -0.0052 -0.0146 -0.0142 146 PRO A O   
1117 C CB  . PRO A 147 ? 0.3176 0.2960 0.3486 -0.0042 -0.0177 -0.0188 146 PRO A CB  
1118 C CG  . PRO A 147 ? 0.3440 0.3231 0.3761 -0.0031 -0.0161 -0.0212 146 PRO A CG  
1119 C CD  . PRO A 147 ? 0.3277 0.3126 0.3635 -0.0020 -0.0100 -0.0223 146 PRO A CD  
1120 N N   . GLN A 148 ? 0.2748 0.2586 0.3029 -0.0038 -0.0073 -0.0185 147 GLN A N   
1121 C CA  . GLN A 148 ? 0.2584 0.2414 0.2824 -0.0044 -0.0051 -0.0176 147 GLN A CA  
1122 C C   . GLN A 148 ? 0.2501 0.2406 0.2831 -0.0042 -0.0029 -0.0159 147 GLN A C   
1123 O O   . GLN A 148 ? 0.2801 0.2705 0.3128 -0.0050 -0.0036 -0.0139 147 GLN A O   
1124 C CB  . GLN A 148 ? 0.2846 0.2646 0.3001 -0.0039 -0.0005 -0.0201 147 GLN A CB  
1125 C CG  . GLN A 148 ? 0.3165 0.2883 0.3213 -0.0041 -0.0025 -0.0217 147 GLN A CG  
1126 C CD  . GLN A 148 ? 0.4414 0.4111 0.4389 -0.0033 0.0025  -0.0243 147 GLN A CD  
1127 O OE1 . GLN A 148 ? 0.3830 0.3560 0.3835 -0.0022 0.0058  -0.0263 147 GLN A OE1 
1128 N NE2 . GLN A 148 ? 0.4403 0.4047 0.4282 -0.0039 0.0031  -0.0243 147 GLN A NE2 
1129 N N   . LEU A 149 ? 0.2570 0.2536 0.2978 -0.0031 0.0000  -0.0166 148 LEU A N   
1130 C CA  . LEU A 149 ? 0.2244 0.2282 0.2743 -0.0028 0.0018  -0.0149 148 LEU A CA  
1131 C C   . LEU A 149 ? 0.2228 0.2282 0.2785 -0.0035 -0.0029 -0.0121 148 LEU A C   
1132 O O   . LEU A 149 ? 0.2236 0.2316 0.2824 -0.0039 -0.0030 -0.0102 148 LEU A O   
1133 C CB  . LEU A 149 ? 0.2278 0.2375 0.2849 -0.0014 0.0051  -0.0164 148 LEU A CB  
1134 C CG  . LEU A 149 ? 0.2571 0.2667 0.3105 -0.0005 0.0103  -0.0191 148 LEU A CG  
1135 C CD1 . LEU A 149 ? 0.3014 0.3158 0.3617 0.0009  0.0123  -0.0206 148 LEU A CD1 
1136 C CD2 . LEU A 149 ? 0.2637 0.2755 0.3166 -0.0006 0.0141  -0.0186 148 LEU A CD2 
1137 N N   . LYS A 150 ? 0.2448 0.2488 0.3025 -0.0037 -0.0069 -0.0119 149 LYS A N   
1138 C CA  . LYS A 150 ? 0.2355 0.2409 0.2989 -0.0044 -0.0116 -0.0093 149 LYS A CA  
1139 C C   . LYS A 150 ? 0.2287 0.2296 0.2864 -0.0056 -0.0144 -0.0078 149 LYS A C   
1140 O O   . LYS A 150 ? 0.2677 0.2716 0.3302 -0.0060 -0.0159 -0.0055 149 LYS A O   
1141 C CB  . LYS A 150 ? 0.2137 0.2173 0.2788 -0.0045 -0.0155 -0.0096 149 LYS A CB  
1142 C CG  . LYS A 150 ? 0.2193 0.2285 0.2924 -0.0034 -0.0136 -0.0103 149 LYS A CG  
1143 C CD  . LYS A 150 ? 0.2538 0.2602 0.3271 -0.0036 -0.0173 -0.0109 149 LYS A CD  
1144 C CE  . LYS A 150 ? 0.2978 0.3098 0.3796 -0.0026 -0.0158 -0.0112 149 LYS A CE  
1145 N NZ  . LYS A 150 ? 0.3225 0.3315 0.4048 -0.0029 -0.0198 -0.0115 149 LYS A NZ  
1146 N N   . ASP A 151 ? 0.2785 0.2722 0.3257 -0.0061 -0.0151 -0.0091 150 ASP A N   
1147 C CA  . ASP A 151 ? 0.2851 0.2739 0.3260 -0.0073 -0.0179 -0.0077 150 ASP A CA  
1148 C C   . ASP A 151 ? 0.2750 0.2664 0.3161 -0.0073 -0.0145 -0.0067 150 ASP A C   
1149 O O   . ASP A 151 ? 0.2797 0.2707 0.3214 -0.0081 -0.0170 -0.0046 150 ASP A O   
1150 C CB  . ASP A 151 ? 0.3457 0.3261 0.3748 -0.0076 -0.0189 -0.0095 150 ASP A CB  
1151 C CG  . ASP A 151 ? 0.5070 0.4834 0.5352 -0.0079 -0.0241 -0.0098 150 ASP A CG  
1152 O OD1 . ASP A 151 ? 0.5191 0.4984 0.5551 -0.0083 -0.0277 -0.0080 150 ASP A OD1 
1153 O OD2 . ASP A 151 ? 0.5436 0.5139 0.5633 -0.0079 -0.0245 -0.0117 150 ASP A OD2 
1154 N N   . SER A 152 ? 0.2683 0.2627 0.3095 -0.0065 -0.0090 -0.0082 151 SER A N   
1155 C CA  . SER A 152 ? 0.2598 0.2569 0.3017 -0.0065 -0.0057 -0.0073 151 SER A CA  
1156 C C   . SER A 152 ? 0.2419 0.2455 0.2941 -0.0063 -0.0068 -0.0050 151 SER A C   
1157 O O   . SER A 152 ? 0.2291 0.2330 0.2813 -0.0069 -0.0073 -0.0033 151 SER A O   
1158 C CB  . SER A 152 ? 0.2881 0.2877 0.3294 -0.0056 0.0004  -0.0095 151 SER A CB  
1159 O OG  . SER A 152 ? 0.4390 0.4415 0.4816 -0.0056 0.0037  -0.0087 151 SER A OG  
1160 N N   . PHE A 153 ? 0.2342 0.2431 0.2953 -0.0055 -0.0072 -0.0049 152 PHE A N   
1161 C CA  . PHE A 153 ? 0.2197 0.2349 0.2907 -0.0053 -0.0083 -0.0027 152 PHE A CA  
1162 C C   . PHE A 153 ? 0.1988 0.2117 0.2704 -0.0063 -0.0140 -0.0005 152 PHE A C   
1163 O O   . PHE A 153 ? 0.2318 0.2472 0.3072 -0.0065 -0.0151 0.0016  152 PHE A O   
1164 C CB  . PHE A 153 ? 0.2082 0.2292 0.2879 -0.0041 -0.0070 -0.0032 152 PHE A CB  
1165 C CG  . PHE A 153 ? 0.2215 0.2474 0.3043 -0.0029 -0.0014 -0.0045 152 PHE A CG  
1166 C CD1 . PHE A 153 ? 0.2147 0.2378 0.2906 -0.0027 0.0024  -0.0067 152 PHE A CD1 
1167 C CD2 . PHE A 153 ? 0.2586 0.2917 0.3511 -0.0018 0.0000  -0.0036 152 PHE A CD2 
1168 C CE1 . PHE A 153 ? 0.2300 0.2575 0.3089 -0.0016 0.0074  -0.0080 152 PHE A CE1 
1169 C CE2 . PHE A 153 ? 0.2229 0.2602 0.3181 -0.0007 0.0049  -0.0048 152 PHE A CE2 
1170 C CZ  . PHE A 153 ? 0.2224 0.2569 0.3110 -0.0006 0.0085  -0.0070 152 PHE A CZ  
1171 N N   . ARG A 154 ? 0.2221 0.2301 0.2900 -0.0069 -0.0178 -0.0009 153 ARG A N   
1172 C CA  . ARG A 154 ? 0.2354 0.2409 0.3038 -0.0079 -0.0235 0.0011  153 ARG A CA  
1173 C C   . ARG A 154 ? 0.2405 0.2418 0.3023 -0.0088 -0.0245 0.0021  153 ARG A C   
1174 O O   . ARG A 154 ? 0.2578 0.2598 0.3228 -0.0093 -0.0279 0.0043  153 ARG A O   
1175 C CB  . ARG A 154 ? 0.2451 0.2454 0.3097 -0.0084 -0.0272 0.0001  153 ARG A CB  
1176 C CG  . ARG A 154 ? 0.2454 0.2501 0.3177 -0.0077 -0.0270 -0.0004 153 ARG A CG  
1177 C CD  . ARG A 154 ? 0.2787 0.2780 0.3463 -0.0079 -0.0294 -0.0019 153 ARG A CD  
1178 N NE  . ARG A 154 ? 0.2770 0.2807 0.3516 -0.0071 -0.0284 -0.0026 153 ARG A NE  
1179 C CZ  . ARG A 154 ? 0.2465 0.2472 0.3193 -0.0071 -0.0301 -0.0040 153 ARG A CZ  
1180 N NH1 . ARG A 154 ? 0.3380 0.3311 0.4020 -0.0078 -0.0331 -0.0050 153 ARG A NH1 
1181 N NH2 . ARG A 154 ? 0.3264 0.3314 0.4060 -0.0064 -0.0289 -0.0044 153 ARG A NH2 
1182 N N   . ASN A 155 ? 0.2506 0.2477 0.3034 -0.0089 -0.0216 0.0006  154 ASN A N   
1183 C CA  . ASN A 155 ? 0.2813 0.2736 0.3266 -0.0098 -0.0224 0.0014  154 ASN A CA  
1184 C C   . ASN A 155 ? 0.2769 0.2740 0.3275 -0.0097 -0.0209 0.0032  154 ASN A C   
1185 O O   . ASN A 155 ? 0.3265 0.3207 0.3739 -0.0104 -0.0233 0.0047  154 ASN A O   
1186 C CB  . ASN A 155 ? 0.2982 0.2855 0.3332 -0.0098 -0.0187 -0.0007 154 ASN A CB  
1187 C CG  . ASN A 155 ? 0.3464 0.3288 0.3733 -0.0107 -0.0189 0.0001  154 ASN A CG  
1188 O OD1 . ASN A 155 ? 0.3573 0.3343 0.3794 -0.0115 -0.0234 0.0011  154 ASN A OD1 
1189 N ND2 . ASN A 155 ? 0.3759 0.3600 0.4012 -0.0105 -0.0141 -0.0003 154 ASN A ND2 
1190 N N   . VAL A 156 ? 0.2827 0.2870 0.3413 -0.0086 -0.0172 0.0031  155 VAL A N   
1191 C CA  . VAL A 156 ? 0.2361 0.2453 0.3004 -0.0084 -0.0161 0.0048  155 VAL A CA  
1192 C C   . VAL A 156 ? 0.2978 0.3126 0.3726 -0.0080 -0.0190 0.0067  155 VAL A C   
1193 O O   . VAL A 156 ? 0.3429 0.3623 0.4234 -0.0075 -0.0183 0.0081  155 VAL A O   
1194 C CB  . VAL A 156 ? 0.2546 0.2680 0.3206 -0.0075 -0.0101 0.0036  155 VAL A CB  
1195 C CG1 . VAL A 156 ? 0.2682 0.2760 0.3237 -0.0080 -0.0072 0.0020  155 VAL A CG1 
1196 C CG2 . VAL A 156 ? 0.2481 0.2668 0.3212 -0.0063 -0.0078 0.0024  155 VAL A CG2 
1197 N N   . GLY A 157 ? 0.2927 0.3074 0.3704 -0.0080 -0.0222 0.0067  156 GLY A N   
1198 C CA  . GLY A 157 ? 0.2741 0.2937 0.3615 -0.0078 -0.0253 0.0086  156 GLY A CA  
1199 C C   . GLY A 157 ? 0.2990 0.3252 0.3953 -0.0066 -0.0232 0.0083  156 GLY A C   
1200 O O   . GLY A 157 ? 0.3337 0.3649 0.4387 -0.0062 -0.0250 0.0100  156 GLY A O   
1201 N N   . LEU A 158 ? 0.2358 0.2622 0.3303 -0.0060 -0.0195 0.0061  157 LEU A N   
1202 C CA  . LEU A 158 ? 0.2395 0.2715 0.3417 -0.0048 -0.0176 0.0055  157 LEU A CA  
1203 C C   . LEU A 158 ? 0.2312 0.2597 0.3313 -0.0052 -0.0200 0.0045  157 LEU A C   
1204 O O   . LEU A 158 ? 0.2424 0.2676 0.3367 -0.0051 -0.0179 0.0023  157 LEU A O   
1205 C CB  . LEU A 158 ? 0.2490 0.2840 0.3513 -0.0037 -0.0118 0.0038  157 LEU A CB  
1206 C CG  . LEU A 158 ? 0.2368 0.2754 0.3416 -0.0033 -0.0095 0.0048  157 LEU A CG  
1207 C CD1 . LEU A 158 ? 0.2914 0.3316 0.3946 -0.0024 -0.0039 0.0029  157 LEU A CD1 
1208 C CD2 . LEU A 158 ? 0.2828 0.3281 0.3980 -0.0025 -0.0106 0.0068  157 LEU A CD2 
1209 N N   . ASN A 159 ? 0.2187 0.2478 0.3236 -0.0057 -0.0244 0.0061  158 ASN A N   
1210 C CA  . ASN A 159 ? 0.2284 0.2536 0.3312 -0.0063 -0.0275 0.0054  158 ASN A CA  
1211 C C   . ASN A 159 ? 0.2613 0.2899 0.3690 -0.0054 -0.0256 0.0043  158 ASN A C   
1212 O O   . ASN A 159 ? 0.2655 0.2901 0.3698 -0.0058 -0.0272 0.0030  158 ASN A O   
1213 C CB  . ASN A 159 ? 0.2119 0.2366 0.3186 -0.0072 -0.0331 0.0077  158 ASN A CB  
1214 C CG  . ASN A 159 ? 0.2433 0.2617 0.3426 -0.0084 -0.0367 0.0082  158 ASN A CG  
1215 O OD1 . ASN A 159 ? 0.2614 0.2755 0.3523 -0.0086 -0.0349 0.0071  158 ASN A OD1 
1216 N ND2 . ASN A 159 ? 0.2463 0.2641 0.3490 -0.0093 -0.0417 0.0101  158 ASN A ND2 
1217 N N   . ARG A 160 ? 0.2344 0.2700 0.3499 -0.0042 -0.0225 0.0047  159 ARG A N   
1218 C CA  . ARG A 160 ? 0.2321 0.2715 0.3540 -0.0034 -0.0217 0.0044  159 ARG A CA  
1219 C C   . ARG A 160 ? 0.2302 0.2693 0.3488 -0.0025 -0.0172 0.0016  159 ARG A C   
1220 O O   . ARG A 160 ? 0.2440 0.2839 0.3600 -0.0019 -0.0134 0.0006  159 ARG A O   
1221 C CB  . ARG A 160 ? 0.2447 0.2918 0.3769 -0.0025 -0.0209 0.0063  159 ARG A CB  
1222 C CG  . ARG A 160 ? 0.2569 0.3047 0.3925 -0.0034 -0.0249 0.0089  159 ARG A CG  
1223 C CD  . ARG A 160 ? 0.2482 0.3034 0.3933 -0.0023 -0.0238 0.0108  159 ARG A CD  
1224 N NE  . ARG A 160 ? 0.2393 0.2951 0.3874 -0.0031 -0.0276 0.0132  159 ARG A NE  
1225 C CZ  . ARG A 160 ? 0.3031 0.3650 0.4591 -0.0023 -0.0274 0.0151  159 ARG A CZ  
1226 N NH1 . ARG A 160 ? 0.3116 0.3794 0.4732 -0.0007 -0.0236 0.0150  159 ARG A NH1 
1227 N NH2 . ARG A 160 ? 0.2564 0.3182 0.4146 -0.0030 -0.0311 0.0172  159 ARG A NH2 
1228 N N   . SER A 161 ? 0.2435 0.3116 0.2779 0.0104  -0.0097 0.0034  160 SER A N   
1229 C CA  . SER A 161 ? 0.3138 0.3809 0.3507 0.0094  -0.0100 0.0020  160 SER A CA  
1230 C C   . SER A 161 ? 0.2568 0.3237 0.2932 0.0093  -0.0093 0.0028  160 SER A C   
1231 O O   . SER A 161 ? 0.2694 0.3345 0.3061 0.0089  -0.0087 0.0014  160 SER A O   
1232 C CB  . SER A 161 ? 0.3631 0.4316 0.4050 0.0085  -0.0122 0.0021  160 SER A CB  
1233 O OG  . SER A 161 ? 0.4214 0.4892 0.4634 0.0085  -0.0128 0.0007  160 SER A OG  
1234 N N   . SER A 162 ? 0.2857 0.3539 0.3212 0.0098  -0.0093 0.0050  161 SER A N   
1235 C CA  . SER A 162 ? 0.2832 0.3507 0.3175 0.0098  -0.0086 0.0058  161 SER A CA  
1236 C C   . SER A 162 ? 0.2696 0.3349 0.2997 0.0104  -0.0067 0.0047  161 SER A C   
1237 O O   . SER A 162 ? 0.2686 0.3325 0.2985 0.0100  -0.0064 0.0042  161 SER A O   
1238 C CB  . SER A 162 ? 0.2962 0.3655 0.3300 0.0103  -0.0088 0.0085  161 SER A CB  
1239 O OG  . SER A 162 ? 0.3389 0.4085 0.3695 0.0114  -0.0078 0.0093  161 SER A OG  
1240 N N   . ASP A 163 ? 0.2548 0.3197 0.2817 0.0112  -0.0055 0.0042  162 ASP A N   
1241 C CA  . ASP A 163 ? 0.2632 0.3261 0.2865 0.0118  -0.0036 0.0029  162 ASP A CA  
1242 C C   . ASP A 163 ? 0.2364 0.2975 0.2615 0.0110  -0.0036 0.0007  162 ASP A C   
1243 O O   . ASP A 163 ? 0.2430 0.3024 0.2673 0.0110  -0.0028 0.0002  162 ASP A O   
1244 C CB  . ASP A 163 ? 0.2903 0.3530 0.3105 0.0126  -0.0025 0.0024  162 ASP A CB  
1245 C CG  . ASP A 163 ? 0.3434 0.4077 0.3615 0.0134  -0.0022 0.0045  162 ASP A CG  
1246 O OD1 . ASP A 163 ? 0.3422 0.4069 0.3593 0.0137  -0.0019 0.0061  162 ASP A OD1 
1247 O OD2 . ASP A 163 ? 0.3085 0.3735 0.3261 0.0138  -0.0023 0.0045  162 ASP A OD2 
1248 N N   . LEU A 164 ? 0.2265 0.2877 0.2542 0.0106  -0.0043 -0.0005 163 LEU A N   
1249 C CA  . LEU A 164 ? 0.2333 0.2927 0.2628 0.0100  -0.0040 -0.0025 163 LEU A CA  
1250 C C   . LEU A 164 ? 0.2481 0.3072 0.2810 0.0090  -0.0049 -0.0023 163 LEU A C   
1251 O O   . LEU A 164 ? 0.2495 0.3068 0.2826 0.0088  -0.0041 -0.0033 163 LEU A O   
1252 C CB  . LEU A 164 ? 0.2205 0.2800 0.2518 0.0097  -0.0048 -0.0037 163 LEU A CB  
1253 C CG  . LEU A 164 ? 0.2054 0.2631 0.2392 0.0091  -0.0045 -0.0057 163 LEU A CG  
1254 C CD1 . LEU A 164 ? 0.2606 0.3159 0.2915 0.0098  -0.0024 -0.0071 163 LEU A CD1 
1255 C CD2 . LEU A 164 ? 0.2690 0.3269 0.3043 0.0089  -0.0055 -0.0067 163 LEU A CD2 
1256 N N   . VAL A 165 ? 0.2209 0.2819 0.2568 0.0083  -0.0067 -0.0010 164 VAL A N   
1257 C CA  . VAL A 165 ? 0.2180 0.2787 0.2574 0.0073  -0.0078 -0.0008 164 VAL A CA  
1258 C C   . VAL A 165 ? 0.2126 0.2722 0.2496 0.0075  -0.0071 0.0001  164 VAL A C   
1259 O O   . VAL A 165 ? 0.2192 0.2771 0.2576 0.0069  -0.0072 -0.0005 164 VAL A O   
1260 C CB  . VAL A 165 ? 0.2204 0.2834 0.2636 0.0065  -0.0098 0.0005  164 VAL A CB  
1261 C CG1 . VAL A 165 ? 0.2254 0.2882 0.2722 0.0054  -0.0109 0.0008  164 VAL A CG1 
1262 C CG2 . VAL A 165 ? 0.2354 0.2993 0.2810 0.0063  -0.0106 -0.0005 164 VAL A CG2 
1263 N N   . ALA A 166 ? 0.2077 0.2680 0.2412 0.0084  -0.0066 0.0016  165 ALA A N   
1264 C CA  . ALA A 166 ? 0.2262 0.2852 0.2571 0.0086  -0.0061 0.0025  165 ALA A CA  
1265 C C   . ALA A 166 ? 0.2024 0.2590 0.2308 0.0091  -0.0045 0.0010  165 ALA A C   
1266 O O   . ALA A 166 ? 0.2233 0.2780 0.2519 0.0087  -0.0047 0.0009  165 ALA A O   
1267 C CB  . ALA A 166 ? 0.2340 0.2941 0.2615 0.0096  -0.0057 0.0045  165 ALA A CB  
1268 N N   . LEU A 167 ? 0.2097 0.2661 0.2357 0.0099  -0.0031 0.0001  166 LEU A N   
1269 C CA  . LEU A 167 ? 0.2039 0.2582 0.2276 0.0105  -0.0015 -0.0012 166 LEU A CA  
1270 C C   . LEU A 167 ? 0.2403 0.2930 0.2674 0.0096  -0.0016 -0.0028 166 LEU A C   
1271 O O   . LEU A 167 ? 0.2323 0.2830 0.2588 0.0098  -0.0008 -0.0034 166 LEU A O   
1272 C CB  . LEU A 167 ? 0.2210 0.2756 0.2414 0.0115  0.0000  -0.0017 166 LEU A CB  
1273 C CG  . LEU A 167 ? 0.2322 0.2879 0.2488 0.0124  0.0005  -0.0001 166 LEU A CG  
1274 C CD1 . LEU A 167 ? 0.2557 0.3120 0.2696 0.0133  0.0017  -0.0004 166 LEU A CD1 
1275 C CD2 . LEU A 167 ? 0.2655 0.3197 0.2792 0.0129  0.0013  0.0005  166 LEU A CD2 
1276 N N   . SER A 168 ? 0.2287 0.2822 0.2597 0.0088  -0.0026 -0.0034 167 SER A N   
1277 C CA  . SER A 168 ? 0.2443 0.2963 0.2790 0.0080  -0.0027 -0.0047 167 SER A CA  
1278 C C   . SER A 168 ? 0.2253 0.2762 0.2620 0.0072  -0.0037 -0.0040 167 SER A C   
1279 O O   . SER A 168 ? 0.2513 0.3004 0.2905 0.0067  -0.0034 -0.0050 167 SER A O   
1280 C CB  . SER A 168 ? 0.2536 0.3066 0.2921 0.0073  -0.0037 -0.0054 167 SER A CB  
1281 O OG  . SER A 168 ? 0.2768 0.3301 0.3134 0.0080  -0.0028 -0.0063 167 SER A OG  
1282 N N   . GLY A 169 ? 0.2448 0.2966 0.2805 0.0070  -0.0048 -0.0023 168 GLY A N   
1283 C CA  . GLY A 169 ? 0.2110 0.2615 0.2477 0.0063  -0.0058 -0.0015 168 GLY A CA  
1284 C C   . GLY A 169 ? 0.2043 0.2524 0.2384 0.0069  -0.0047 -0.0019 168 GLY A C   
1285 O O   . GLY A 169 ? 0.2481 0.2945 0.2833 0.0063  -0.0057 -0.0014 168 GLY A O   
1286 N N   . GLY A 170 ? 0.2274 0.2751 0.2582 0.0080  -0.0029 -0.0026 169 GLY A N   
1287 C CA  . GLY A 170 ? 0.2467 0.2920 0.2757 0.0086  -0.0018 -0.0032 169 GLY A CA  
1288 C C   . GLY A 170 ? 0.2529 0.2964 0.2863 0.0077  -0.0020 -0.0042 169 GLY A C   
1289 O O   . GLY A 170 ? 0.2633 0.3046 0.2965 0.0077  -0.0019 -0.0042 169 GLY A O   
1290 N N   . HIS A 171 ? 0.2147 0.2589 0.2523 0.0069  -0.0025 -0.0049 170 HIS A N   
1291 C CA  . HIS A 171 ? 0.2342 0.2767 0.2764 0.0060  -0.0026 -0.0057 170 HIS A CA  
1292 C C   . HIS A 171 ? 0.2222 0.2642 0.2677 0.0046  -0.0048 -0.0047 170 HIS A C   
1293 O O   . HIS A 171 ? 0.2628 0.3038 0.3131 0.0036  -0.0054 -0.0052 170 HIS A O   
1294 C CB  . HIS A 171 ? 0.2288 0.2721 0.2742 0.0057  -0.0021 -0.0070 170 HIS A CB  
1295 C CG  . HIS A 171 ? 0.2407 0.2838 0.2831 0.0070  0.0000  -0.0082 170 HIS A CG  
1296 N ND1 . HIS A 171 ? 0.2744 0.3184 0.3176 0.0071  0.0005  -0.0092 170 HIS A ND1 
1297 C CD2 . HIS A 171 ? 0.2420 0.2841 0.2805 0.0082  0.0017  -0.0085 170 HIS A CD2 
1298 C CE1 . HIS A 171 ? 0.2952 0.3386 0.3350 0.0083  0.0024  -0.0101 170 HIS A CE1 
1299 N NE2 . HIS A 171 ? 0.2197 0.2621 0.2567 0.0090  0.0032  -0.0097 170 HIS A NE2 
1300 N N   . THR A 172 ? 0.2211 0.2635 0.2641 0.0046  -0.0060 -0.0033 171 THR A N   
1301 C CA  . THR A 172 ? 0.2403 0.2816 0.2854 0.0035  -0.0080 -0.0022 171 THR A CA  
1302 C C   . THR A 172 ? 0.2562 0.2943 0.3010 0.0035  -0.0079 -0.0023 171 THR A C   
1303 O O   . THR A 172 ? 0.2564 0.2931 0.3036 0.0024  -0.0097 -0.0016 171 THR A O   
1304 C CB  . THR A 172 ? 0.2063 0.2487 0.2482 0.0036  -0.0092 -0.0006 171 THR A CB  
1305 O OG1 . THR A 172 ? 0.2264 0.2679 0.2707 0.0024  -0.0113 0.0004  171 THR A OG1 
1306 C CG2 . THR A 172 ? 0.2468 0.2882 0.2827 0.0050  -0.0081 -0.0001 171 THR A CG2 
1307 N N   . PHE A 173 ? 0.2338 0.2709 0.2761 0.0046  -0.0061 -0.0031 172 PHE A N   
1308 C CA  . PHE A 173 ? 0.2521 0.2863 0.2951 0.0047  -0.0059 -0.0033 172 PHE A CA  
1309 C C   . PHE A 173 ? 0.2780 0.3119 0.3212 0.0056  -0.0035 -0.0047 172 PHE A C   
1310 O O   . PHE A 173 ? 0.2749 0.3106 0.3175 0.0061  -0.0022 -0.0055 172 PHE A O   
1311 C CB  . PHE A 173 ? 0.2662 0.2989 0.3046 0.0052  -0.0066 -0.0022 172 PHE A CB  
1312 C CG  . PHE A 173 ? 0.2518 0.2855 0.2843 0.0068  -0.0051 -0.0021 172 PHE A CG  
1313 C CD1 . PHE A 173 ? 0.2773 0.3132 0.3085 0.0076  -0.0033 -0.0029 172 PHE A CD1 
1314 C CD2 . PHE A 173 ? 0.2861 0.3183 0.3142 0.0073  -0.0055 -0.0012 172 PHE A CD2 
1315 C CE1 . PHE A 173 ? 0.2725 0.3091 0.2984 0.0089  -0.0019 -0.0027 172 PHE A CE1 
1316 C CE2 . PHE A 173 ? 0.3112 0.3441 0.3339 0.0087  -0.0041 -0.0010 172 PHE A CE2 
1317 C CZ  . PHE A 173 ? 0.2476 0.2828 0.2694 0.0095  -0.0023 -0.0017 172 PHE A CZ  
1318 N N   . GLY A 174 ? 0.2725 0.3040 0.3170 0.0058  -0.0030 -0.0050 173 GLY A N   
1319 C CA  . GLY A 174 ? 0.2693 0.3002 0.3141 0.0068  -0.0006 -0.0062 173 GLY A CA  
1320 C C   . GLY A 174 ? 0.2809 0.3115 0.3313 0.0061  0.0000  -0.0071 173 GLY A C   
1321 O O   . GLY A 174 ? 0.2731 0.3039 0.3276 0.0048  -0.0015 -0.0069 173 GLY A O   
1322 N N   . LYS A 175 ? 0.2468 0.2766 0.2972 0.0071  0.0023  -0.0082 174 LYS A N   
1323 C CA  . LYS A 175 ? 0.2423 0.2709 0.2978 0.0067  0.0033  -0.0090 174 LYS A CA  
1324 C C   . LYS A 175 ? 0.2463 0.2758 0.3005 0.0077  0.0056  -0.0103 174 LYS A C   
1325 O O   . LYS A 175 ? 0.2474 0.2779 0.2967 0.0089  0.0068  -0.0107 174 LYS A O   
1326 C CB  . LYS A 175 ? 0.2810 0.3069 0.3387 0.0071  0.0041  -0.0088 174 LYS A CB  
1327 C CG  . LYS A 175 ? 0.3451 0.3695 0.4038 0.0063  0.0018  -0.0075 174 LYS A CG  
1328 C CD  . LYS A 175 ? 0.3661 0.3893 0.4313 0.0047  0.0003  -0.0071 174 LYS A CD  
1329 C CE  . LYS A 175 ? 0.5097 0.5305 0.5766 0.0040  -0.0016 -0.0059 174 LYS A CE  
1330 N NZ  . LYS A 175 ? 0.5521 0.5717 0.6256 0.0024  -0.0031 -0.0054 174 LYS A NZ  
1331 N N   . ASN A 176 ? 0.2451 0.2740 0.3038 0.0072  0.0062  -0.0110 175 ASN A N   
1332 C CA  . ASN A 176 ? 0.2565 0.2857 0.3146 0.0079  0.0083  -0.0124 175 ASN A CA  
1333 C C   . ASN A 176 ? 0.2866 0.3134 0.3491 0.0081  0.0101  -0.0130 175 ASN A C   
1334 O O   . ASN A 176 ? 0.2746 0.3003 0.3425 0.0069  0.0091  -0.0124 175 ASN A O   
1335 C CB  . ASN A 176 ? 0.2506 0.2817 0.3095 0.0071  0.0071  -0.0126 175 ASN A CB  
1336 C CG  . ASN A 176 ? 0.2921 0.3230 0.3509 0.0077  0.0090  -0.0141 175 ASN A CG  
1337 O OD1 . ASN A 176 ? 0.3162 0.3473 0.3704 0.0089  0.0104  -0.0148 175 ASN A OD1 
1338 N ND2 . ASN A 176 ? 0.3624 0.3924 0.4261 0.0068  0.0090  -0.0145 175 ASN A ND2 
1339 N N   . GLN A 177 ? 0.2365 0.2625 0.2970 0.0094  0.0127  -0.0140 176 GLN A N   
1340 C CA  . GLN A 177 ? 0.2478 0.2713 0.3122 0.0098  0.0148  -0.0145 176 GLN A CA  
1341 C C   . GLN A 177 ? 0.2445 0.2679 0.3123 0.0091  0.0149  -0.0153 176 GLN A C   
1342 O O   . GLN A 177 ? 0.2566 0.2815 0.3219 0.0090  0.0145  -0.0160 176 GLN A O   
1343 C CB  . GLN A 177 ? 0.2501 0.2726 0.3107 0.0117  0.0176  -0.0154 176 GLN A CB  
1344 C CG  . GLN A 177 ? 0.2851 0.3074 0.3428 0.0125  0.0179  -0.0148 176 GLN A CG  
1345 C CD  . GLN A 177 ? 0.3621 0.3836 0.4163 0.0143  0.0208  -0.0157 176 GLN A CD  
1346 O OE1 . GLN A 177 ? 0.3456 0.3651 0.4023 0.0150  0.0230  -0.0162 176 GLN A OE1 
1347 N NE2 . GLN A 177 ? 0.3716 0.3946 0.4201 0.0152  0.0209  -0.0158 176 GLN A NE2 
1348 N N   . CYS A 178 ? 0.2393 0.2607 0.3129 0.0085  0.0156  -0.0151 177 CYS A N   
1349 C CA  . CYS A 178 ? 0.2247 0.2455 0.3020 0.0079  0.0161  -0.0158 177 CYS A CA  
1350 C C   . CYS A 178 ? 0.2668 0.2875 0.3399 0.0092  0.0181  -0.0173 177 CYS A C   
1351 O O   . CYS A 178 ? 0.2523 0.2737 0.3259 0.0086  0.0176  -0.0180 177 CYS A O   
1352 C CB  . CYS A 178 ? 0.2571 0.2752 0.3405 0.0078  0.0175  -0.0155 177 CYS A CB  
1353 S SG  . CYS A 178 ? 0.2828 0.3007 0.3730 0.0058  0.0147  -0.0138 177 CYS A SG  
1354 N N   . ARG A 179 ? 0.2577 0.2775 0.3265 0.0108  0.0203  -0.0179 178 ARG A N   
1355 C CA  . ARG A 179 ? 0.2901 0.3093 0.3545 0.0121  0.0223  -0.0193 178 ARG A CA  
1356 C C   . ARG A 179 ? 0.2588 0.2802 0.3205 0.0115  0.0204  -0.0198 178 ARG A C   
1357 O O   . ARG A 179 ? 0.3042 0.3249 0.3652 0.0118  0.0212  -0.0209 178 ARG A O   
1358 C CB  . ARG A 179 ? 0.2997 0.3186 0.3589 0.0138  0.0240  -0.0195 178 ARG A CB  
1359 C CG  . ARG A 179 ? 0.4217 0.4395 0.4762 0.0153  0.0263  -0.0210 178 ARG A CG  
1360 C CD  . ARG A 179 ? 0.4245 0.4420 0.4744 0.0169  0.0281  -0.0211 178 ARG A CD  
1361 N NE  . ARG A 179 ? 0.5100 0.5266 0.5629 0.0171  0.0287  -0.0200 178 ARG A NE  
1362 C CZ  . ARG A 179 ? 0.5634 0.5775 0.6188 0.0181  0.0313  -0.0201 178 ARG A CZ  
1363 N NH1 . ARG A 179 ? 0.4990 0.5109 0.5536 0.0191  0.0338  -0.0212 178 ARG A NH1 
1364 N NH2 . ARG A 179 ? 0.6041 0.6176 0.6627 0.0181  0.0314  -0.0190 178 ARG A NH2 
1365 N N   . PHE A 180 ? 0.2516 0.2756 0.3119 0.0108  0.0179  -0.0189 179 PHE A N   
1366 C CA  . PHE A 180 ? 0.2811 0.3073 0.3381 0.0105  0.0163  -0.0192 179 PHE A CA  
1367 C C   . PHE A 180 ? 0.2936 0.3210 0.3547 0.0089  0.0142  -0.0191 179 PHE A C   
1368 O O   . PHE A 180 ? 0.2943 0.3235 0.3532 0.0086  0.0127  -0.0192 179 PHE A O   
1369 C CB  . PHE A 180 ? 0.2678 0.2962 0.3208 0.0107  0.0150  -0.0183 179 PHE A CB  
1370 C CG  . PHE A 180 ? 0.2732 0.3006 0.3222 0.0122  0.0170  -0.0184 179 PHE A CG  
1371 C CD1 . PHE A 180 ? 0.3725 0.3988 0.4178 0.0135  0.0191  -0.0197 179 PHE A CD1 
1372 C CD2 . PHE A 180 ? 0.3021 0.3296 0.3512 0.0122  0.0167  -0.0174 179 PHE A CD2 
1373 C CE1 . PHE A 180 ? 0.3671 0.3926 0.4090 0.0149  0.0210  -0.0198 179 PHE A CE1 
1374 C CE2 . PHE A 180 ? 0.3508 0.3774 0.3965 0.0136  0.0185  -0.0175 179 PHE A CE2 
1375 C CZ  . PHE A 180 ? 0.3774 0.4032 0.4196 0.0150  0.0207  -0.0187 179 PHE A CZ  
1376 N N   . ILE A 181 ? 0.2852 0.3115 0.3522 0.0079  0.0141  -0.0187 180 ILE A N   
1377 C CA  . ILE A 181 ? 0.2836 0.3108 0.3548 0.0065  0.0123  -0.0186 180 ILE A CA  
1378 C C   . ILE A 181 ? 0.2774 0.3023 0.3526 0.0064  0.0140  -0.0196 180 ILE A C   
1379 O O   . ILE A 181 ? 0.2659 0.2914 0.3449 0.0052  0.0127  -0.0196 180 ILE A O   
1380 C CB  . ILE A 181 ? 0.2614 0.2900 0.3366 0.0049  0.0098  -0.0171 180 ILE A CB  
1381 C CG1 . ILE A 181 ? 0.2488 0.2754 0.3277 0.0048  0.0107  -0.0164 180 ILE A CG1 
1382 C CG2 . ILE A 181 ? 0.3103 0.3414 0.3815 0.0049  0.0079  -0.0162 180 ILE A CG2 
1383 C CD1 . ILE A 181 ? 0.2689 0.2961 0.3528 0.0030  0.0082  -0.0151 180 ILE A CD1 
1384 N N   . MET A 182 ? 0.2961 0.3183 0.3706 0.0077  0.0169  -0.0202 181 MET A N   
1385 C CA  . MET A 182 ? 0.3074 0.3271 0.3858 0.0077  0.0188  -0.0209 181 MET A CA  
1386 C C   . MET A 182 ? 0.2777 0.2975 0.3553 0.0075  0.0185  -0.0221 181 MET A C   
1387 O O   . MET A 182 ? 0.2614 0.2804 0.3438 0.0066  0.0184  -0.0223 181 MET A O   
1388 C CB  . MET A 182 ? 0.3000 0.3167 0.3765 0.0095  0.0223  -0.0215 181 MET A CB  
1389 C CG  . MET A 182 ? 0.3038 0.3199 0.3821 0.0097  0.0228  -0.0203 181 MET A CG  
1390 S SD  . MET A 182 ? 0.3442 0.3598 0.4314 0.0080  0.0216  -0.0189 181 MET A SD  
1391 C CE  . MET A 182 ? 0.3506 0.3625 0.4416 0.0088  0.0252  -0.0197 181 MET A CE  
1392 N N   . ASP A 183 ? 0.2900 0.3106 0.3616 0.0084  0.0182  -0.0229 182 ASP A N   
1393 C CA  . ASP A 183 ? 0.2997 0.3203 0.3702 0.0082  0.0176  -0.0240 182 ASP A CA  
1394 C C   . ASP A 183 ? 0.3061 0.3293 0.3812 0.0063  0.0146  -0.0233 182 ASP A C   
1395 O O   . ASP A 183 ? 0.2695 0.2920 0.3477 0.0057  0.0144  -0.0240 182 ASP A O   
1396 C CB  . ASP A 183 ? 0.3215 0.3429 0.3850 0.0093  0.0173  -0.0247 182 ASP A CB  
1397 C CG  . ASP A 183 ? 0.4203 0.4450 0.4817 0.0088  0.0148  -0.0236 182 ASP A CG  
1398 O OD1 . ASP A 183 ? 0.4537 0.4796 0.5171 0.0083  0.0142  -0.0223 182 ASP A OD1 
1399 O OD2 . ASP A 183 ? 0.5336 0.5597 0.5913 0.0090  0.0135  -0.0239 182 ASP A OD2 
1400 N N   . ARG A 184 ? 0.2472 0.2732 0.3228 0.0055  0.0123  -0.0220 183 ARG A N   
1401 C CA  . ARG A 184 ? 0.2676 0.2961 0.3472 0.0038  0.0094  -0.0212 183 ARG A CA  
1402 C C   . ARG A 184 ? 0.2589 0.2864 0.3457 0.0025  0.0095  -0.0209 183 ARG A C   
1403 O O   . ARG A 184 ? 0.2373 0.2661 0.3280 0.0012  0.0078  -0.0207 183 ARG A O   
1404 C CB  . ARG A 184 ? 0.2752 0.3065 0.3538 0.0032  0.0072  -0.0197 183 ARG A CB  
1405 C CG  . ARG A 184 ? 0.2630 0.2958 0.3354 0.0041  0.0066  -0.0198 183 ARG A CG  
1406 C CD  . ARG A 184 ? 0.2598 0.2955 0.3322 0.0033  0.0042  -0.0182 183 ARG A CD  
1407 N NE  . ARG A 184 ? 0.2548 0.2928 0.3302 0.0021  0.0017  -0.0177 183 ARG A NE  
1408 C CZ  . ARG A 184 ? 0.2402 0.2804 0.3178 0.0009  -0.0005 -0.0163 183 ARG A CZ  
1409 N NH1 . ARG A 184 ? 0.2476 0.2876 0.3249 0.0008  -0.0007 -0.0152 183 ARG A NH1 
1410 N NH2 . ARG A 184 ? 0.2636 0.3060 0.3437 -0.0001 -0.0026 -0.0159 183 ARG A NH2 
1411 N N   . LEU A 185 ? 0.2512 0.2765 0.3400 0.0029  0.0114  -0.0206 184 LEU A N   
1412 C CA  . LEU A 185 ? 0.2349 0.2591 0.3308 0.0017  0.0115  -0.0200 184 LEU A CA  
1413 C C   . LEU A 185 ? 0.2429 0.2645 0.3412 0.0020  0.0137  -0.0212 184 LEU A C   
1414 O O   . LEU A 185 ? 0.2884 0.3098 0.3928 0.0007  0.0132  -0.0208 184 LEU A O   
1415 C CB  . LEU A 185 ? 0.2384 0.2613 0.3360 0.0018  0.0124  -0.0189 184 LEU A CB  
1416 C CG  . LEU A 185 ? 0.2399 0.2647 0.3351 0.0017  0.0105  -0.0177 184 LEU A CG  
1417 C CD1 . LEU A 185 ? 0.2735 0.2964 0.3716 0.0016  0.0113  -0.0167 184 LEU A CD1 
1418 C CD2 . LEU A 185 ? 0.3150 0.3426 0.4119 0.0000  0.0072  -0.0169 184 LEU A CD2 
1419 N N   . TYR A 186 ? 0.2515 0.2710 0.3451 0.0037  0.0162  -0.0225 185 TYR A N   
1420 C CA  . TYR A 186 ? 0.2625 0.2788 0.3582 0.0043  0.0189  -0.0235 185 TYR A CA  
1421 C C   . TYR A 186 ? 0.3180 0.3330 0.4087 0.0054  0.0199  -0.0252 185 TYR A C   
1422 O O   . TYR A 186 ? 0.3282 0.3409 0.4209 0.0055  0.0213  -0.0261 185 TYR A O   
1423 C CB  . TYR A 186 ? 0.2703 0.2838 0.3664 0.0055  0.0219  -0.0232 185 TYR A CB  
1424 C CG  . TYR A 186 ? 0.2579 0.2719 0.3590 0.0045  0.0211  -0.0215 185 TYR A CG  
1425 C CD1 . TYR A 186 ? 0.2714 0.2855 0.3800 0.0028  0.0201  -0.0207 185 TYR A CD1 
1426 C CD2 . TYR A 186 ? 0.2913 0.3057 0.3900 0.0051  0.0211  -0.0207 185 TYR A CD2 
1427 C CE1 . TYR A 186 ? 0.2703 0.2847 0.3836 0.0018  0.0190  -0.0191 185 TYR A CE1 
1428 C CE2 . TYR A 186 ? 0.2733 0.2880 0.3765 0.0042  0.0200  -0.0192 185 TYR A CE2 
1429 C CZ  . TYR A 186 ? 0.2577 0.2723 0.3682 0.0025  0.0189  -0.0184 185 TYR A CZ  
1430 O OH  . TYR A 186 ? 0.2536 0.2682 0.3687 0.0015  0.0177  -0.0168 185 TYR A OH  
1431 N N   . ASN A 187 ? 0.3123 0.2967 0.3165 0.0009  0.0319  0.0042  186 ASN A N   
1432 C CA  . ASN A 187 ? 0.3424 0.3154 0.3350 -0.0004 0.0320  0.0038  186 ASN A CA  
1433 C C   . ASN A 187 ? 0.3383 0.3124 0.3278 -0.0023 0.0263  0.0031  186 ASN A C   
1434 O O   . ASN A 187 ? 0.3340 0.3070 0.3213 -0.0034 0.0243  0.0021  186 ASN A O   
1435 C CB  . ASN A 187 ? 0.3534 0.3191 0.3413 -0.0005 0.0354  0.0033  186 ASN A CB  
1436 C CG  . ASN A 187 ? 0.3571 0.3103 0.3325 -0.0020 0.0353  0.0028  186 ASN A CG  
1437 O OD1 . ASN A 187 ? 0.3716 0.3203 0.3414 -0.0027 0.0338  0.0031  186 ASN A OD1 
1438 N ND2 . ASN A 187 ? 0.3934 0.3406 0.3639 -0.0027 0.0369  0.0021  186 ASN A ND2 
1439 N N   . PHE A 188 ? 0.2984 0.2750 0.2882 -0.0028 0.0237  0.0036  187 PHE A N   
1440 C CA  . PHE A 188 ? 0.3300 0.3094 0.3184 -0.0045 0.0183  0.0032  187 PHE A CA  
1441 C C   . PHE A 188 ? 0.3342 0.3026 0.3114 -0.0062 0.0172  0.0032  187 PHE A C   
1442 O O   . PHE A 188 ? 0.3405 0.3024 0.3126 -0.0061 0.0189  0.0040  187 PHE A O   
1443 C CB  . PHE A 188 ? 0.3005 0.2889 0.2953 -0.0043 0.0158  0.0038  187 PHE A CB  
1444 C CG  . PHE A 188 ? 0.2963 0.2898 0.2918 -0.0058 0.0106  0.0033  187 PHE A CG  
1445 C CD1 . PHE A 188 ? 0.3342 0.3340 0.3345 -0.0057 0.0086  0.0023  187 PHE A CD1 
1446 C CD2 . PHE A 188 ? 0.3773 0.3692 0.3689 -0.0072 0.0077  0.0040  187 PHE A CD2 
1447 C CE1 . PHE A 188 ? 0.3539 0.3586 0.3552 -0.0069 0.0040  0.0018  187 PHE A CE1 
1448 C CE2 . PHE A 188 ? 0.3628 0.3599 0.3556 -0.0085 0.0031  0.0036  187 PHE A CE2 
1449 C CZ  . PHE A 188 ? 0.3468 0.3503 0.3446 -0.0083 0.0014  0.0025  187 PHE A CZ  
1450 N N   . SER A 189 ? 0.3906 0.3565 0.3638 -0.0077 0.0143  0.0023  188 SER A N   
1451 C CA  . SER A 189 ? 0.4216 0.3772 0.3842 -0.0096 0.0123  0.0025  188 SER A CA  
1452 C C   . SER A 189 ? 0.4147 0.3581 0.3687 -0.0094 0.0169  0.0028  188 SER A C   
1453 O O   . SER A 189 ? 0.4165 0.3516 0.3624 -0.0104 0.0164  0.0035  188 SER A O   
1454 C CB  . SER A 189 ? 0.4770 0.4352 0.4393 -0.0108 0.0085  0.0033  188 SER A CB  
1455 O OG  . SER A 189 ? 0.6943 0.6465 0.6493 -0.0130 0.0046  0.0033  188 SER A OG  
1456 N N   . ASN A 190 ? 0.3768 0.3189 0.3324 -0.0080 0.0213  0.0024  189 ASN A N   
1457 C CA  . ASN A 190 ? 0.3808 0.3113 0.3283 -0.0076 0.0262  0.0025  189 ASN A CA  
1458 C C   . ASN A 190 ? 0.4312 0.3587 0.3772 -0.0065 0.0289  0.0036  189 ASN A C   
1459 O O   . ASN A 190 ? 0.3924 0.3084 0.3287 -0.0068 0.0311  0.0038  189 ASN A O   
1460 C CB  . ASN A 190 ? 0.3843 0.3030 0.3199 -0.0098 0.0245  0.0021  189 ASN A CB  
1461 C CG  . ASN A 190 ? 0.4354 0.3559 0.3720 -0.0109 0.0220  0.0011  189 ASN A CG  
1462 O OD1 . ASN A 190 ? 0.5151 0.4367 0.4503 -0.0126 0.0169  0.0008  189 ASN A OD1 
1463 N ND2 . ASN A 190 ? 0.3997 0.3208 0.3388 -0.0099 0.0256  0.0006  189 ASN A ND2 
1464 N N   . THR A 191 ? 0.3913 0.3290 0.3469 -0.0050 0.0288  0.0042  190 THR A N   
1465 C CA  . THR A 191 ? 0.4026 0.3384 0.3582 -0.0037 0.0315  0.0052  190 THR A CA  
1466 C C   . THR A 191 ? 0.3997 0.3380 0.3615 -0.0011 0.0371  0.0054  190 THR A C   
1467 O O   . THR A 191 ? 0.4719 0.4067 0.4326 0.0003  0.0402  0.0062  190 THR A O   
1468 C CB  . THR A 191 ? 0.4508 0.3954 0.4122 -0.0040 0.0275  0.0059  190 THR A CB  
1469 O OG1 . THR A 191 ? 0.3836 0.3411 0.3565 -0.0032 0.0264  0.0057  190 THR A OG1 
1470 C CG2 . THR A 191 ? 0.4464 0.3885 0.4018 -0.0065 0.0222  0.0059  190 THR A CG2 
1471 N N   . GLY A 192 ? 0.4134 0.3574 0.3816 -0.0005 0.0383  0.0049  191 GLY A N   
1472 C CA  . GLY A 192 ? 0.4247 0.3735 0.4011 0.0019  0.0428  0.0055  191 GLY A CA  
1473 C C   . GLY A 192 ? 0.4158 0.3748 0.4018 0.0030  0.0415  0.0064  191 GLY A C   
1474 O O   . GLY A 192 ? 0.4045 0.3665 0.3969 0.0050  0.0452  0.0072  191 GLY A O   
1475 N N   . LEU A 193 ? 0.3647 0.3291 0.3522 0.0017  0.0363  0.0064  192 LEU A N   
1476 C CA  . LEU A 193 ? 0.3083 0.2821 0.3042 0.0023  0.0345  0.0072  192 LEU A CA  
1477 C C   . LEU A 193 ? 0.3401 0.3241 0.3423 0.0013  0.0298  0.0067  192 LEU A C   
1478 O O   . LEU A 193 ? 0.3025 0.2854 0.3011 -0.0002 0.0271  0.0058  192 LEU A O   
1479 C CB  . LEU A 193 ? 0.3332 0.3028 0.3238 0.0017  0.0329  0.0079  192 LEU A CB  
1480 C CG  . LEU A 193 ? 0.3943 0.3545 0.3796 0.0031  0.0374  0.0085  192 LEU A CG  
1481 C CD1 . LEU A 193 ? 0.4554 0.4108 0.4342 0.0020  0.0348  0.0091  192 LEU A CD1 
1482 C CD2 . LEU A 193 ? 0.4777 0.4431 0.4721 0.0056  0.0411  0.0094  192 LEU A CD2 
1483 N N   . PRO A 194 ? 0.3440 0.3380 0.3555 0.0020  0.0287  0.0073  193 PRO A N   
1484 C CA  . PRO A 194 ? 0.2908 0.2944 0.3079 0.0011  0.0243  0.0068  193 PRO A CA  
1485 C C   . PRO A 194 ? 0.3096 0.3131 0.3221 -0.0008 0.0197  0.0066  193 PRO A C   
1486 O O   . PRO A 194 ? 0.3141 0.3116 0.3205 -0.0014 0.0195  0.0072  193 PRO A O   
1487 C CB  . PRO A 194 ? 0.3242 0.3371 0.3514 0.0023  0.0246  0.0078  193 PRO A CB  
1488 C CG  . PRO A 194 ? 0.3615 0.3695 0.3874 0.0035  0.0278  0.0089  193 PRO A CG  
1489 C CD  . PRO A 194 ? 0.3702 0.3670 0.3878 0.0038  0.0315  0.0085  193 PRO A CD  
1490 N N   . ASP A 195 ? 0.2994 0.3094 0.3148 -0.0018 0.0161  0.0058  194 ASP A N   
1491 C CA  . ASP A 195 ? 0.3084 0.3209 0.3218 -0.0035 0.0115  0.0057  194 ASP A CA  
1492 C C   . ASP A 195 ? 0.3058 0.3229 0.3225 -0.0035 0.0105  0.0068  194 ASP A C   
1493 O O   . ASP A 195 ? 0.3129 0.3381 0.3377 -0.0026 0.0107  0.0071  194 ASP A O   
1494 C CB  . ASP A 195 ? 0.3304 0.3506 0.3485 -0.0038 0.0085  0.0046  194 ASP A CB  
1495 C CG  . ASP A 195 ? 0.3325 0.3560 0.3492 -0.0055 0.0039  0.0043  194 ASP A CG  
1496 O OD1 . ASP A 195 ? 0.3464 0.3675 0.3595 -0.0065 0.0028  0.0053  194 ASP A OD1 
1497 O OD2 . ASP A 195 ? 0.3294 0.3579 0.3488 -0.0058 0.0015  0.0033  194 ASP A OD2 
1498 N N   . PRO A 196 ? 0.3004 0.3122 0.3109 -0.0047 0.0094  0.0076  195 PRO A N   
1499 C CA  . PRO A 196 ? 0.3813 0.3970 0.3946 -0.0048 0.0084  0.0087  195 PRO A CA  
1500 C C   . PRO A 196 ? 0.3460 0.3725 0.3653 -0.0058 0.0045  0.0087  195 PRO A C   
1501 O O   . PRO A 196 ? 0.4202 0.4513 0.4430 -0.0059 0.0037  0.0096  195 PRO A O   
1502 C CB  . PRO A 196 ? 0.4150 0.4214 0.4189 -0.0061 0.0076  0.0094  195 PRO A CB  
1503 C CG  . PRO A 196 ? 0.4089 0.4096 0.4063 -0.0073 0.0064  0.0086  195 PRO A CG  
1504 C CD  . PRO A 196 ? 0.3455 0.3467 0.3458 -0.0059 0.0090  0.0075  195 PRO A CD  
1505 N N   . THR A 197 ? 0.3098 0.3402 0.3301 -0.0065 0.0021  0.0076  196 THR A N   
1506 C CA  . THR A 197 ? 0.3151 0.3559 0.3413 -0.0072 -0.0012 0.0074  196 THR A CA  
1507 C C   . THR A 197 ? 0.3541 0.4029 0.3887 -0.0058 -0.0003 0.0069  196 THR A C   
1508 O O   . THR A 197 ? 0.3008 0.3582 0.3404 -0.0062 -0.0027 0.0066  196 THR A O   
1509 C CB  . THR A 197 ? 0.3154 0.3573 0.3392 -0.0085 -0.0045 0.0065  196 THR A CB  
1510 O OG1 . THR A 197 ? 0.3611 0.4011 0.3847 -0.0077 -0.0035 0.0052  196 THR A OG1 
1511 C CG2 . THR A 197 ? 0.3760 0.4104 0.3916 -0.0103 -0.0061 0.0072  196 THR A CG2 
1512 N N   . LEU A 198 ? 0.3463 0.3925 0.3827 -0.0042 0.0031  0.0069  197 LEU A N   
1513 C CA  . LEU A 198 ? 0.2605 0.3138 0.3049 -0.0030 0.0039  0.0067  197 LEU A CA  
1514 C C   . LEU A 198 ? 0.2843 0.3404 0.3332 -0.0024 0.0051  0.0080  197 LEU A C   
1515 O O   . LEU A 198 ? 0.3163 0.3664 0.3629 -0.0017 0.0077  0.0090  197 LEU A O   
1516 C CB  . LEU A 198 ? 0.2794 0.3287 0.3237 -0.0018 0.0068  0.0061  197 LEU A CB  
1517 C CG  . LEU A 198 ? 0.3199 0.3751 0.3718 -0.0005 0.0079  0.0060  197 LEU A CG  
1518 C CD1 . LEU A 198 ? 0.2996 0.3635 0.3560 -0.0010 0.0046  0.0051  197 LEU A CD1 
1519 C CD2 . LEU A 198 ? 0.3042 0.3539 0.3542 0.0003  0.0107  0.0054  197 LEU A CD2 
1520 N N   . ASN A 199 ? 0.2819 0.3467 0.3369 -0.0026 0.0031  0.0082  198 ASN A N   
1521 C CA  . ASN A 199 ? 0.2874 0.3554 0.3472 -0.0022 0.0037  0.0096  198 ASN A CA  
1522 C C   . ASN A 199 ? 0.2708 0.3354 0.3332 -0.0004 0.0076  0.0102  198 ASN A C   
1523 O O   . ASN A 199 ? 0.2760 0.3412 0.3410 0.0005  0.0089  0.0096  198 ASN A O   
1524 C CB  . ASN A 199 ? 0.3037 0.3813 0.3698 -0.0027 0.0012  0.0094  198 ASN A CB  
1525 C CG  . ASN A 199 ? 0.2847 0.3655 0.3561 -0.0023 0.0017  0.0109  198 ASN A CG  
1526 O OD1 . ASN A 199 ? 0.3034 0.3854 0.3799 -0.0011 0.0035  0.0114  198 ASN A OD1 
1527 N ND2 . ASN A 199 ? 0.3814 0.4633 0.4516 -0.0035 0.0000  0.0118  198 ASN A ND2 
1528 N N   . THR A 200 ? 0.3182 0.3793 0.3802 0.0001  0.0093  0.0115  199 THR A N   
1529 C CA  . THR A 200 ? 0.3271 0.3836 0.3906 0.0019  0.0135  0.0122  199 THR A CA  
1530 C C   . THR A 200 ? 0.2629 0.3259 0.3355 0.0030  0.0142  0.0128  199 THR A C   
1531 O O   . THR A 200 ? 0.3040 0.3647 0.3789 0.0044  0.0175  0.0131  199 THR A O   
1532 C CB  . THR A 200 ? 0.3641 0.4147 0.4244 0.0024  0.0151  0.0133  199 THR A CB  
1533 O OG1 . THR A 200 ? 0.4298 0.4853 0.4932 0.0016  0.0126  0.0143  199 THR A OG1 
1534 C CG2 . THR A 200 ? 0.4065 0.4486 0.4569 0.0015  0.0151  0.0127  199 THR A CG2 
1535 N N   . THR A 201 ? 0.3194 0.3901 0.3971 0.0022  0.0113  0.0132  200 THR A N   
1536 C CA  . THR A 201 ? 0.3193 0.3960 0.4052 0.0029  0.0115  0.0138  200 THR A CA  
1537 C C   . THR A 201 ? 0.2665 0.3453 0.3532 0.0029  0.0111  0.0125  200 THR A C   
1538 O O   . THR A 201 ? 0.2969 0.3763 0.3879 0.0039  0.0130  0.0129  200 THR A O   
1539 C CB  . THR A 201 ? 0.3978 0.4815 0.4881 0.0019  0.0083  0.0145  200 THR A CB  
1540 O OG1 . THR A 201 ? 0.4780 0.5593 0.5675 0.0018  0.0086  0.0158  200 THR A OG1 
1541 C CG2 . THR A 201 ? 0.3457 0.4351 0.4443 0.0024  0.0082  0.0153  200 THR A CG2 
1542 N N   . TYR A 202 ? 0.2601 0.3401 0.3428 0.0017  0.0085  0.0110  201 TYR A N   
1543 C CA  . TYR A 202 ? 0.2563 0.3375 0.3389 0.0018  0.0079  0.0097  201 TYR A CA  
1544 C C   . TYR A 202 ? 0.2596 0.3337 0.3388 0.0027  0.0112  0.0094  201 TYR A C   
1545 O O   . TYR A 202 ? 0.2551 0.3299 0.3367 0.0032  0.0121  0.0090  201 TYR A O   
1546 C CB  . TYR A 202 ? 0.2519 0.3352 0.3306 0.0005  0.0046  0.0082  201 TYR A CB  
1547 C CG  . TYR A 202 ? 0.2483 0.3347 0.3280 0.0005  0.0031  0.0068  201 TYR A CG  
1548 C CD1 . TYR A 202 ? 0.3272 0.4179 0.4128 0.0011  0.0031  0.0069  201 TYR A CD1 
1549 C CD2 . TYR A 202 ? 0.2985 0.3834 0.3732 -0.0001 0.0014  0.0053  201 TYR A CD2 
1550 C CE1 . TYR A 202 ? 0.3230 0.4161 0.4090 0.0012  0.0015  0.0056  201 TYR A CE1 
1551 C CE2 . TYR A 202 ? 0.3337 0.4213 0.4093 0.0000  -0.0002 0.0039  201 TYR A CE2 
1552 C CZ  . TYR A 202 ? 0.3466 0.4380 0.4276 0.0007  -0.0001 0.0040  201 TYR A CZ  
1553 O OH  . TYR A 202 ? 0.4119 0.5055 0.4933 0.0009  -0.0018 0.0025  201 TYR A OH  
1554 N N   . LEU A 203 ? 0.2566 0.3235 0.3298 0.0027  0.0130  0.0095  202 LEU A N   
1555 C CA  . LEU A 203 ? 0.2438 0.3032 0.3133 0.0036  0.0166  0.0093  202 LEU A CA  
1556 C C   . LEU A 203 ? 0.2645 0.3249 0.3402 0.0050  0.0197  0.0104  202 LEU A C   
1557 O O   . LEU A 203 ? 0.2610 0.3193 0.3366 0.0054  0.0216  0.0100  202 LEU A O   
1558 C CB  . LEU A 203 ? 0.2646 0.3161 0.3273 0.0036  0.0183  0.0097  202 LEU A CB  
1559 C CG  . LEU A 203 ? 0.2902 0.3329 0.3486 0.0046  0.0226  0.0098  202 LEU A CG  
1560 C CD1 . LEU A 203 ? 0.3195 0.3583 0.3728 0.0040  0.0225  0.0084  202 LEU A CD1 
1561 C CD2 . LEU A 203 ? 0.3513 0.3869 0.4034 0.0046  0.0238  0.0104  202 LEU A CD2 
1562 N N   . GLN A 204 ? 0.2631 0.3269 0.3446 0.0057  0.0203  0.0119  203 GLN A N   
1563 C CA  . GLN A 204 ? 0.3155 0.3806 0.4038 0.0070  0.0233  0.0132  203 GLN A CA  
1564 C C   . GLN A 204 ? 0.2417 0.3129 0.3354 0.0067  0.0217  0.0130  203 GLN A C   
1565 O O   . GLN A 204 ? 0.2862 0.3564 0.3822 0.0075  0.0241  0.0133  203 GLN A O   
1566 C CB  . GLN A 204 ? 0.3448 0.4123 0.4382 0.0077  0.0237  0.0149  203 GLN A CB  
1567 C CG  . GLN A 204 ? 0.3838 0.4441 0.4719 0.0084  0.0261  0.0153  203 GLN A CG  
1568 C CD  . GLN A 204 ? 0.5499 0.6030 0.6354 0.0098  0.0310  0.0154  203 GLN A CD  
1569 O OE1 . GLN A 204 ? 0.5714 0.6176 0.6486 0.0095  0.0321  0.0143  203 GLN A OE1 
1570 N NE2 . GLN A 204 ? 0.6554 0.7100 0.7478 0.0113  0.0340  0.0168  203 GLN A NE2 
1571 N N   . THR A 205 ? 0.2480 0.3252 0.3432 0.0056  0.0176  0.0124  204 THR A N   
1572 C CA  . THR A 205 ? 0.2576 0.3400 0.3569 0.0053  0.0156  0.0120  204 THR A CA  
1573 C C   . THR A 205 ? 0.2909 0.3695 0.3859 0.0053  0.0164  0.0106  204 THR A C   
1574 O O   . THR A 205 ? 0.2557 0.3352 0.3541 0.0056  0.0174  0.0109  204 THR A O   
1575 C CB  . THR A 205 ? 0.3590 0.4474 0.4590 0.0042  0.0113  0.0112  204 THR A CB  
1576 O OG1 . THR A 205 ? 0.3756 0.4678 0.4801 0.0041  0.0104  0.0127  204 THR A OG1 
1577 C CG2 . THR A 205 ? 0.3464 0.4392 0.4492 0.0039  0.0092  0.0105  204 THR A CG2 
1578 N N   . LEU A 206 ? 0.2424 0.3166 0.3298 0.0047  0.0157  0.0091  205 LEU A N   
1579 C CA  . LEU A 206 ? 0.2465 0.3167 0.3292 0.0044  0.0159  0.0077  205 LEU A CA  
1580 C C   . LEU A 206 ? 0.2407 0.3048 0.3223 0.0052  0.0203  0.0084  205 LEU A C   
1581 O O   . LEU A 206 ? 0.2605 0.3233 0.3417 0.0052  0.0209  0.0079  205 LEU A O   
1582 C CB  . LEU A 206 ? 0.2382 0.3049 0.3133 0.0035  0.0140  0.0063  205 LEU A CB  
1583 C CG  . LEU A 206 ? 0.2339 0.3068 0.3098 0.0026  0.0097  0.0054  205 LEU A CG  
1584 C CD1 . LEU A 206 ? 0.2542 0.3238 0.3232 0.0017  0.0080  0.0044  205 LEU A CD1 
1585 C CD2 . LEU A 206 ? 0.2793 0.3565 0.3581 0.0026  0.0076  0.0044  205 LEU A CD2 
1586 N N   . ARG A 207 ? 0.2315 0.2916 0.3122 0.0060  0.0235  0.0095  206 ARG A N   
1587 C CA  . ARG A 207 ? 0.2586 0.3134 0.3389 0.0069  0.0281  0.0102  206 ARG A CA  
1588 C C   . ARG A 207 ? 0.2673 0.3271 0.3561 0.0076  0.0293  0.0114  206 ARG A C   
1589 O O   . ARG A 207 ? 0.2437 0.3005 0.3323 0.0079  0.0321  0.0116  206 ARG A O   
1590 C CB  . ARG A 207 ? 0.2494 0.2994 0.3277 0.0079  0.0313  0.0112  206 ARG A CB  
1591 C CG  . ARG A 207 ? 0.2728 0.3153 0.3412 0.0072  0.0311  0.0100  206 ARG A CG  
1592 C CD  . ARG A 207 ? 0.2914 0.3290 0.3577 0.0081  0.0338  0.0110  206 ARG A CD  
1593 N NE  . ARG A 207 ? 0.3256 0.3540 0.3815 0.0076  0.0347  0.0101  206 ARG A NE  
1594 C CZ  . ARG A 207 ? 0.4324 0.4548 0.4841 0.0082  0.0367  0.0106  206 ARG A CZ  
1595 N NH1 . ARG A 207 ? 0.5152 0.5402 0.5720 0.0094  0.0378  0.0120  206 ARG A NH1 
1596 N NH2 . ARG A 207 ? 0.3604 0.3736 0.4021 0.0076  0.0376  0.0098  206 ARG A NH2 
1597 N N   . GLY A 208 ? 0.2592 0.3265 0.3553 0.0076  0.0270  0.0124  207 GLY A N   
1598 C CA  . GLY A 208 ? 0.2780 0.3502 0.3823 0.0079  0.0275  0.0138  207 GLY A CA  
1599 C C   . GLY A 208 ? 0.2537 0.3276 0.3577 0.0071  0.0254  0.0128  207 GLY A C   
1600 O O   . GLY A 208 ? 0.2967 0.3717 0.4050 0.0073  0.0269  0.0137  207 GLY A O   
1601 N N   . LEU A 209 ? 0.2297 0.3037 0.3286 0.0061  0.0220  0.0109  208 LEU A N   
1602 C CA  . LEU A 209 ? 0.2207 0.2956 0.3184 0.0054  0.0197  0.0096  208 LEU A CA  
1603 C C   . LEU A 209 ? 0.2487 0.3164 0.3396 0.0052  0.0217  0.0086  208 LEU A C   
1604 O O   . LEU A 209 ? 0.2221 0.2895 0.3131 0.0048  0.0212  0.0082  208 LEU A O   
1605 C CB  . LEU A 209 ? 0.2282 0.3066 0.3237 0.0047  0.0151  0.0080  208 LEU A CB  
1606 C CG  . LEU A 209 ? 0.2548 0.3404 0.3561 0.0046  0.0125  0.0088  208 LEU A CG  
1607 C CD1 . LEU A 209 ? 0.2292 0.3170 0.3268 0.0039  0.0087  0.0070  208 LEU A CD1 
1608 C CD2 . LEU A 209 ? 0.2757 0.3658 0.3836 0.0046  0.0117  0.0098  208 LEU A CD2 
1609 N N   . CYS A 210 ? 0.2239 0.2854 0.3085 0.0053  0.0236  0.0081  209 CYS A N   
1610 C CA  . CYS A 210 ? 0.2231 0.2768 0.2999 0.0049  0.0252  0.0070  209 CYS A CA  
1611 C C   . CYS A 210 ? 0.2395 0.2869 0.3139 0.0057  0.0301  0.0080  209 CYS A C   
1612 O O   . CYS A 210 ? 0.2646 0.3067 0.3327 0.0056  0.0307  0.0075  209 CYS A O   
1613 C CB  . CYS A 210 ? 0.2275 0.2790 0.2973 0.0040  0.0219  0.0052  209 CYS A CB  
1614 S SG  . CYS A 210 ? 0.2717 0.3301 0.3438 0.0034  0.0163  0.0038  209 CYS A SG  
1615 N N   . PRO A 211 ? 0.2528 0.3009 0.3324 0.0065  0.0337  0.0095  210 PRO A N   
1616 C CA  . PRO A 211 ? 0.2733 0.3154 0.3509 0.0075  0.0388  0.0104  210 PRO A CA  
1617 C C   . PRO A 211 ? 0.2944 0.3272 0.3624 0.0068  0.0409  0.0093  210 PRO A C   
1618 O O   . PRO A 211 ? 0.3032 0.3347 0.3678 0.0057  0.0389  0.0081  210 PRO A O   
1619 C CB  . PRO A 211 ? 0.3165 0.3627 0.4029 0.0084  0.0417  0.0124  210 PRO A CB  
1620 C CG  . PRO A 211 ? 0.2522 0.3034 0.3421 0.0074  0.0385  0.0121  210 PRO A CG  
1621 C CD  . PRO A 211 ? 0.2273 0.2816 0.3149 0.0065  0.0331  0.0106  210 PRO A CD  
1622 N N   . LEU A 212 ? 0.3518 0.3777 0.4151 0.0076  0.0447  0.0095  211 LEU A N   
1623 C CA  . LEU A 212 ? 0.4727 0.4892 0.5271 0.0070  0.0475  0.0087  211 LEU A CA  
1624 C C   . LEU A 212 ? 0.4615 0.4785 0.5196 0.0071  0.0506  0.0095  211 LEU A C   
1625 O O   . LEU A 212 ? 0.5046 0.5267 0.5712 0.0082  0.0529  0.0112  211 LEU A O   
1626 C CB  . LEU A 212 ? 0.5262 0.5351 0.5748 0.0079  0.0512  0.0090  211 LEU A CB  
1627 C CG  . LEU A 212 ? 0.5330 0.5312 0.5693 0.0068  0.0517  0.0076  211 LEU A CG  
1628 C CD1 . LEU A 212 ? 0.5308 0.5289 0.5622 0.0051  0.0460  0.0061  211 LEU A CD1 
1629 C CD2 . LEU A 212 ? 0.5717 0.5634 0.6033 0.0078  0.0547  0.0080  211 LEU A CD2 
1630 N N   . ASN A 213 ? 0.4923 0.5041 0.5440 0.0058  0.0504  0.0084  212 ASN A N   
1631 C CA  . ASN A 213 ? 0.4511 0.4635 0.5055 0.0054  0.0523  0.0090  212 ASN A CA  
1632 C C   . ASN A 213 ? 0.3984 0.4203 0.4614 0.0050  0.0485  0.0094  212 ASN A C   
1633 O O   . ASN A 213 ? 0.4040 0.4284 0.4719 0.0049  0.0502  0.0105  212 ASN A O   
1634 C CB  . ASN A 213 ? 0.5310 0.5419 0.5890 0.0068  0.0587  0.0107  212 ASN A CB  
1635 C CG  . ASN A 213 ? 0.6349 0.6355 0.6836 0.0071  0.0630  0.0102  212 ASN A CG  
1636 O OD1 . ASN A 213 ? 0.7371 0.7304 0.7759 0.0059  0.0614  0.0086  212 ASN A OD1 
1637 N ND2 . ASN A 213 ? 0.7125 0.7121 0.7644 0.0088  0.0683  0.0116  212 ASN A ND2 
1638 N N   . GLY A 214 ? 0.3820 0.4091 0.4468 0.0049  0.0436  0.0087  213 GLY A N   
1639 C CA  . GLY A 214 ? 0.3136 0.3488 0.3853 0.0045  0.0397  0.0089  213 GLY A CA  
1640 C C   . GLY A 214 ? 0.3137 0.3471 0.3806 0.0030  0.0362  0.0072  213 GLY A C   
1641 O O   . GLY A 214 ? 0.3269 0.3529 0.3852 0.0022  0.0365  0.0060  213 GLY A O   
1642 N N   . ASN A 215 ? 0.2615 0.3016 0.3342 0.0027  0.0329  0.0074  214 ASN A N   
1643 C CA  . ASN A 215 ? 0.2605 0.3001 0.3296 0.0016  0.0288  0.0058  214 ASN A CA  
1644 C C   . ASN A 215 ? 0.2862 0.3250 0.3502 0.0014  0.0250  0.0039  214 ASN A C   
1645 O O   . ASN A 215 ? 0.2647 0.3094 0.3326 0.0019  0.0226  0.0039  214 ASN A O   
1646 C CB  . ASN A 215 ? 0.2735 0.3205 0.3501 0.0015  0.0261  0.0065  214 ASN A CB  
1647 C CG  . ASN A 215 ? 0.2973 0.3443 0.3706 0.0006  0.0214  0.0047  214 ASN A CG  
1648 O OD1 . ASN A 215 ? 0.3527 0.3934 0.4184 -0.0002 0.0209  0.0032  214 ASN A OD1 
1649 N ND2 . ASN A 215 ? 0.3105 0.3643 0.3893 0.0006  0.0179  0.0048  214 ASN A ND2 
1650 N N   . LEU A 216 ? 0.2908 0.3225 0.3462 0.0005  0.0245  0.0024  215 LEU A N   
1651 C CA  . LEU A 216 ? 0.2591 0.2898 0.3098 0.0002  0.0209  0.0008  215 LEU A CA  
1652 C C   . LEU A 216 ? 0.2740 0.3105 0.3271 0.0001  0.0158  -0.0004 215 LEU A C   
1653 O O   . LEU A 216 ? 0.2888 0.3272 0.3406 0.0002  0.0127  -0.0014 215 LEU A O   
1654 C CB  . LEU A 216 ? 0.2903 0.3114 0.3312 -0.0008 0.0216  -0.0002 215 LEU A CB  
1655 C CG  . LEU A 216 ? 0.3202 0.3341 0.3568 -0.0007 0.0267  0.0007  215 LEU A CG  
1656 C CD1 . LEU A 216 ? 0.4374 0.4414 0.4635 -0.0020 0.0265  -0.0005 215 LEU A CD1 
1657 C CD2 . LEU A 216 ? 0.3572 0.3736 0.3961 0.0003  0.0277  0.0015  215 LEU A CD2 
1658 N N   . SER A 217 ? 0.2626 0.3020 0.3193 -0.0001 0.0147  -0.0002 216 SER A N   
1659 C CA  . SER A 217 ? 0.2190 0.2635 0.2778 -0.0001 0.0098  -0.0014 216 SER A CA  
1660 C C   . SER A 217 ? 0.2635 0.3166 0.3303 0.0008  0.0086  -0.0006 216 SER A C   
1661 O O   . SER A 217 ? 0.2878 0.3454 0.3565 0.0009  0.0048  -0.0016 216 SER A O   
1662 C CB  . SER A 217 ? 0.3672 0.4097 0.4250 -0.0008 0.0086  -0.0018 216 SER A CB  
1663 O OG  . SER A 217 ? 0.4297 0.4644 0.4795 -0.0017 0.0085  -0.0030 216 SER A OG  
1664 N N   . ALA A 218 ? 0.2633 0.3187 0.3346 0.0013  0.0116  0.0011  217 ALA A N   
1665 C CA  . ALA A 218 ? 0.2546 0.3178 0.3330 0.0020  0.0102  0.0020  217 ALA A CA  
1666 C C   . ALA A 218 ? 0.2119 0.2780 0.2886 0.0022  0.0070  0.0006  217 ALA A C   
1667 O O   . ALA A 218 ? 0.2334 0.2958 0.3049 0.0020  0.0071  -0.0003 217 ALA A O   
1668 C CB  . ALA A 218 ? 0.2236 0.2879 0.3065 0.0025  0.0141  0.0041  217 ALA A CB  
1669 N N   . LEU A 219 ? 0.2483 0.3211 0.3296 0.0024  0.0039  0.0004  218 LEU A N   
1670 C CA  . LEU A 219 ? 0.2484 0.3245 0.3284 0.0026  0.0007  -0.0011 218 LEU A CA  
1671 C C   . LEU A 219 ? 0.2093 0.2901 0.2933 0.0029  0.0011  0.0000  218 LEU A C   
1672 O O   . LEU A 219 ? 0.2609 0.3450 0.3505 0.0030  0.0022  0.0017  218 LEU A O   
1673 C CB  . LEU A 219 ? 0.2874 0.3673 0.3687 0.0027  -0.0031 -0.0023 218 LEU A CB  
1674 C CG  . LEU A 219 ? 0.3116 0.3870 0.3888 0.0024  -0.0044 -0.0036 218 LEU A CG  
1675 C CD1 . LEU A 219 ? 0.3608 0.4401 0.4401 0.0026  -0.0079 -0.0045 218 LEU A CD1 
1676 C CD2 . LEU A 219 ? 0.3195 0.3905 0.3901 0.0022  -0.0053 -0.0052 218 LEU A CD2 
1677 N N   . VAL A 220 ? 0.2224 0.3035 0.3033 0.0028  -0.0001 -0.0009 219 VAL A N   
1678 C CA  . VAL A 220 ? 0.2348 0.3200 0.3184 0.0029  -0.0001 -0.0001 219 VAL A CA  
1679 C C   . VAL A 220 ? 0.2296 0.3193 0.3125 0.0028  -0.0038 -0.0016 219 VAL A C   
1680 O O   . VAL A 220 ? 0.2443 0.3319 0.3228 0.0027  -0.0054 -0.0032 219 VAL A O   
1681 C CB  . VAL A 220 ? 0.2574 0.3381 0.3378 0.0027  0.0025  0.0007  219 VAL A CB  
1682 C CG1 . VAL A 220 ? 0.3038 0.3887 0.3863 0.0026  0.0018  0.0013  219 VAL A CG1 
1683 C CG2 . VAL A 220 ? 0.3231 0.3996 0.4046 0.0030  0.0065  0.0022  219 VAL A CG2 
1684 N N   . ASP A 221 ? 0.2558 0.3515 0.3429 0.0028  -0.0050 -0.0010 220 ASP A N   
1685 C CA  . ASP A 221 ? 0.2028 0.3031 0.2894 0.0027  -0.0080 -0.0024 220 ASP A CA  
1686 C C   . ASP A 221 ? 0.2132 0.3122 0.2958 0.0023  -0.0082 -0.0029 220 ASP A C   
1687 O O   . ASP A 221 ? 0.2444 0.3417 0.3267 0.0020  -0.0063 -0.0016 220 ASP A O   
1688 C CB  . ASP A 221 ? 0.2282 0.3348 0.3198 0.0026  -0.0091 -0.0016 220 ASP A CB  
1689 C CG  . ASP A 221 ? 0.3480 0.4565 0.4434 0.0029  -0.0098 -0.0012 220 ASP A CG  
1690 O OD1 . ASP A 221 ? 0.3582 0.4659 0.4520 0.0032  -0.0113 -0.0025 220 ASP A OD1 
1691 O OD2 . ASP A 221 ? 0.3895 0.5003 0.4895 0.0027  -0.0091 0.0006  220 ASP A OD2 
1692 N N   . PHE A 222 ? 0.2451 0.2897 0.3005 0.0139  -0.0148 -0.0007 221 PHE A N   
1693 C CA  . PHE A 222 ? 0.2666 0.3071 0.3149 0.0121  -0.0130 0.0009  221 PHE A CA  
1694 C C   . PHE A 222 ? 0.2937 0.3278 0.3358 0.0140  -0.0152 0.0017  221 PHE A C   
1695 O O   . PHE A 222 ? 0.2942 0.3243 0.3324 0.0137  -0.0143 0.0023  221 PHE A O   
1696 C CB  . PHE A 222 ? 0.2625 0.3045 0.3078 0.0092  -0.0114 0.0025  221 PHE A CB  
1697 C CG  . PHE A 222 ? 0.2398 0.2854 0.2874 0.0065  -0.0080 0.0025  221 PHE A CG  
1698 C CD1 . PHE A 222 ? 0.2898 0.3332 0.3345 0.0053  -0.0059 0.0026  221 PHE A CD1 
1699 C CD2 . PHE A 222 ? 0.2425 0.2935 0.2949 0.0053  -0.0072 0.0023  221 PHE A CD2 
1700 C CE1 . PHE A 222 ? 0.2856 0.3321 0.3317 0.0030  -0.0030 0.0025  221 PHE A CE1 
1701 C CE2 . PHE A 222 ? 0.2522 0.3063 0.3062 0.0030  -0.0041 0.0024  221 PHE A CE2 
1702 C CZ  . PHE A 222 ? 0.2611 0.3129 0.3117 0.0020  -0.0020 0.0025  221 PHE A CZ  
1703 N N   . ASP A 223 ? 0.2234 0.2565 0.2644 0.0160  -0.0182 0.0019  222 ASP A N   
1704 C CA  . ASP A 223 ? 0.2583 0.2853 0.2926 0.0179  -0.0203 0.0032  222 ASP A CA  
1705 C C   . ASP A 223 ? 0.2830 0.3090 0.3205 0.0216  -0.0236 0.0014  222 ASP A C   
1706 O O   . ASP A 223 ? 0.2801 0.3084 0.3207 0.0233  -0.0262 0.0004  222 ASP A O   
1707 C CB  . ASP A 223 ? 0.2630 0.2894 0.2926 0.0175  -0.0212 0.0049  222 ASP A CB  
1708 C CG  . ASP A 223 ? 0.2778 0.2980 0.3000 0.0195  -0.0230 0.0065  222 ASP A CG  
1709 O OD1 . ASP A 223 ? 0.2736 0.2898 0.2945 0.0215  -0.0242 0.0062  222 ASP A OD1 
1710 O OD2 . ASP A 223 ? 0.3018 0.3210 0.3192 0.0192  -0.0232 0.0082  222 ASP A OD2 
1711 N N   . LEU A 224 ? 0.2953 0.3177 0.3319 0.0229  -0.0238 0.0010  223 LEU A N   
1712 C CA  . LEU A 224 ? 0.3151 0.3365 0.3549 0.0266  -0.0269 -0.0007 223 LEU A CA  
1713 C C   . LEU A 224 ? 0.3211 0.3383 0.3558 0.0293  -0.0305 0.0002  223 LEU A C   
1714 O O   . LEU A 224 ? 0.3230 0.3399 0.3605 0.0325  -0.0338 -0.0014 223 LEU A O   
1715 C CB  . LEU A 224 ? 0.3434 0.3616 0.3832 0.0274  -0.0261 -0.0014 223 LEU A CB  
1716 C CG  . LEU A 224 ? 0.3582 0.3689 0.3904 0.0283  -0.0269 0.0003  223 LEU A CG  
1717 C CD1 . LEU A 224 ? 0.4994 0.5076 0.5339 0.0311  -0.0282 -0.0013 223 LEU A CD1 
1718 C CD2 . LEU A 224 ? 0.3849 0.3936 0.4124 0.0249  -0.0236 0.0021  223 LEU A CD2 
1719 N N   . ARG A 225 ? 0.2735 0.2873 0.3005 0.0282  -0.0299 0.0026  224 ARG A N   
1720 C CA  . ARG A 225 ? 0.2835 0.2931 0.3046 0.0310  -0.0330 0.0037  224 ARG A CA  
1721 C C   . ARG A 225 ? 0.3218 0.3349 0.3444 0.0317  -0.0350 0.0031  224 ARG A C   
1722 O O   . ARG A 225 ? 0.3349 0.3480 0.3594 0.0349  -0.0388 0.0015  224 ARG A O   
1723 C CB  . ARG A 225 ? 0.2896 0.2938 0.3018 0.0297  -0.0314 0.0068  224 ARG A CB  
1724 C CG  . ARG A 225 ? 0.3176 0.3165 0.3274 0.0302  -0.0308 0.0075  224 ARG A CG  
1725 C CD  . ARG A 225 ? 0.3643 0.3580 0.3661 0.0287  -0.0290 0.0108  224 ARG A CD  
1726 N NE  . ARG A 225 ? 0.3841 0.3712 0.3821 0.0307  -0.0302 0.0117  224 ARG A NE  
1727 C CZ  . ARG A 225 ? 0.4138 0.3986 0.4130 0.0299  -0.0289 0.0114  224 ARG A CZ  
1728 N NH1 . ARG A 225 ? 0.3819 0.3702 0.3856 0.0270  -0.0264 0.0101  224 ARG A NH1 
1729 N NH2 . ARG A 225 ? 0.4160 0.3944 0.4115 0.0320  -0.0304 0.0123  224 ARG A NH2 
1730 N N   . THR A 226 ? 0.2972 0.3132 0.3190 0.0288  -0.0327 0.0041  225 THR A N   
1731 C CA  . THR A 226 ? 0.2985 0.3178 0.3217 0.0292  -0.0344 0.0034  225 THR A CA  
1732 C C   . THR A 226 ? 0.2617 0.2874 0.2915 0.0260  -0.0318 0.0026  225 THR A C   
1733 O O   . THR A 226 ? 0.2451 0.2720 0.2724 0.0233  -0.0294 0.0041  225 THR A O   
1734 C CB  . THR A 226 ? 0.2856 0.3017 0.3001 0.0294  -0.0345 0.0058  225 THR A CB  
1735 O OG1 . THR A 226 ? 0.2677 0.2829 0.2783 0.0261  -0.0305 0.0081  225 THR A OG1 
1736 C CG2 . THR A 226 ? 0.3353 0.3453 0.3434 0.0332  -0.0374 0.0065  225 THR A CG2 
1737 N N   . PRO A 227 ? 0.2608 0.2907 0.2994 0.0263  -0.0323 0.0003  226 PRO A N   
1738 C CA  . PRO A 227 ? 0.2817 0.3174 0.3265 0.0233  -0.0295 -0.0002 226 PRO A CA  
1739 C C   . PRO A 227 ? 0.2747 0.3137 0.3205 0.0221  -0.0298 0.0000  226 PRO A C   
1740 O O   . PRO A 227 ? 0.3050 0.3479 0.3536 0.0191  -0.0269 0.0003  226 PRO A O   
1741 C CB  . PRO A 227 ? 0.3136 0.3526 0.3676 0.0247  -0.0305 -0.0026 226 PRO A CB  
1742 C CG  . PRO A 227 ? 0.3591 0.3950 0.4124 0.0287  -0.0350 -0.0037 226 PRO A CG  
1743 C CD  . PRO A 227 ? 0.3240 0.3533 0.3670 0.0294  -0.0351 -0.0017 226 PRO A CD  
1744 N N   . THR A 228 ? 0.2748 0.3124 0.3181 0.0244  -0.0332 -0.0003 227 THR A N   
1745 C CA  . THR A 228 ? 0.2746 0.3154 0.3192 0.0234  -0.0337 -0.0004 227 THR A CA  
1746 C C   . THR A 228 ? 0.3086 0.3460 0.3439 0.0235  -0.0337 0.0015  227 THR A C   
1747 O O   . THR A 228 ? 0.3600 0.3997 0.3956 0.0227  -0.0339 0.0016  227 THR A O   
1748 C CB  . THR A 228 ? 0.3483 0.3912 0.3989 0.0261  -0.0381 -0.0029 227 THR A CB  
1749 O OG1 . THR A 228 ? 0.3230 0.3610 0.3678 0.0297  -0.0418 -0.0031 227 THR A OG1 
1750 C CG2 . THR A 228 ? 0.3455 0.3917 0.4057 0.0264  -0.0382 -0.0047 227 THR A CG2 
1751 N N   . ILE A 229 ? 0.2947 0.3268 0.3223 0.0244  -0.0333 0.0032  228 ILE A N   
1752 C CA  . ILE A 229 ? 0.2695 0.2983 0.2883 0.0247  -0.0331 0.0054  228 ILE A CA  
1753 C C   . ILE A 229 ? 0.2581 0.2864 0.2735 0.0213  -0.0286 0.0078  228 ILE A C   
1754 O O   . ILE A 229 ? 0.2681 0.2948 0.2834 0.0201  -0.0267 0.0084  228 ILE A O   
1755 C CB  . ILE A 229 ? 0.3167 0.3396 0.3287 0.0284  -0.0358 0.0060  228 ILE A CB  
1756 C CG1 . ILE A 229 ? 0.3050 0.3283 0.3202 0.0321  -0.0407 0.0034  228 ILE A CG1 
1757 C CG2 . ILE A 229 ? 0.3008 0.3201 0.3033 0.0285  -0.0346 0.0086  228 ILE A CG2 
1758 C CD1 . ILE A 229 ? 0.4312 0.4489 0.4409 0.0359  -0.0436 0.0036  228 ILE A CD1 
1759 N N   . PHE A 230 ? 0.2591 0.2886 0.2715 0.0197  -0.0271 0.0091  229 PHE A N   
1760 C CA  . PHE A 230 ? 0.2529 0.2820 0.2618 0.0165  -0.0232 0.0115  229 PHE A CA  
1761 C C   . PHE A 230 ? 0.2653 0.2887 0.2658 0.0177  -0.0229 0.0139  229 PHE A C   
1762 O O   . PHE A 230 ? 0.2796 0.3011 0.2744 0.0193  -0.0238 0.0151  229 PHE A O   
1763 C CB  . PHE A 230 ? 0.2628 0.2956 0.2723 0.0144  -0.0218 0.0120  229 PHE A CB  
1764 C CG  . PHE A 230 ? 0.2699 0.3035 0.2781 0.0108  -0.0179 0.0139  229 PHE A CG  
1765 C CD1 . PHE A 230 ? 0.2625 0.2926 0.2639 0.0103  -0.0162 0.0166  229 PHE A CD1 
1766 C CD2 . PHE A 230 ? 0.2417 0.2793 0.2557 0.0079  -0.0159 0.0131  229 PHE A CD2 
1767 C CE1 . PHE A 230 ? 0.2565 0.2873 0.2573 0.0069  -0.0129 0.0182  229 PHE A CE1 
1768 C CE2 . PHE A 230 ? 0.2720 0.3101 0.2848 0.0047  -0.0126 0.0147  229 PHE A CE2 
1769 C CZ  . PHE A 230 ? 0.2712 0.3059 0.2776 0.0041  -0.0112 0.0172  229 PHE A CZ  
1770 N N   . ASP A 231 ? 0.2798 0.3001 0.2793 0.0170  -0.0216 0.0148  230 ASP A N   
1771 C CA  . ASP A 231 ? 0.2781 0.2925 0.2702 0.0182  -0.0213 0.0172  230 ASP A CA  
1772 C C   . ASP A 231 ? 0.2674 0.2801 0.2599 0.0155  -0.0186 0.0183  230 ASP A C   
1773 O O   . ASP A 231 ? 0.2750 0.2912 0.2728 0.0129  -0.0169 0.0172  230 ASP A O   
1774 C CB  . ASP A 231 ? 0.3004 0.3111 0.2904 0.0225  -0.0250 0.0163  230 ASP A CB  
1775 C CG  . ASP A 231 ? 0.2858 0.2976 0.2823 0.0233  -0.0267 0.0137  230 ASP A CG  
1776 O OD1 . ASP A 231 ? 0.2675 0.2822 0.2694 0.0207  -0.0246 0.0129  230 ASP A OD1 
1777 O OD2 . ASP A 231 ? 0.3121 0.3219 0.3084 0.0269  -0.0301 0.0124  230 ASP A OD2 
1778 N N   . ASN A 232 ? 0.3064 0.3135 0.2933 0.0162  -0.0182 0.0205  231 ASN A N   
1779 C CA  . ASN A 232 ? 0.3032 0.3083 0.2903 0.0135  -0.0157 0.0217  231 ASN A CA  
1780 C C   . ASN A 232 ? 0.2772 0.2801 0.2670 0.0147  -0.0169 0.0201  231 ASN A C   
1781 O O   . ASN A 232 ? 0.3072 0.3072 0.2963 0.0131  -0.0154 0.0210  231 ASN A O   
1782 C CB  . ASN A 232 ? 0.2984 0.2987 0.2786 0.0132  -0.0141 0.0253  231 ASN A CB  
1783 C CG  . ASN A 232 ? 0.3421 0.3364 0.3175 0.0166  -0.0162 0.0263  231 ASN A CG  
1784 O OD1 . ASN A 232 ? 0.3459 0.3399 0.3221 0.0198  -0.0193 0.0244  231 ASN A OD1 
1785 N ND2 . ASN A 232 ? 0.3598 0.3492 0.3303 0.0159  -0.0146 0.0294  231 ASN A ND2 
1786 N N   . LYS A 233 ? 0.2936 0.2975 0.2865 0.0176  -0.0198 0.0176  232 LYS A N   
1787 C CA  . LYS A 233 ? 0.2814 0.2833 0.2770 0.0191  -0.0211 0.0161  232 LYS A CA  
1788 C C   . LYS A 233 ? 0.2681 0.2725 0.2688 0.0163  -0.0188 0.0148  232 LYS A C   
1789 O O   . LYS A 233 ? 0.2822 0.2837 0.2836 0.0167  -0.0189 0.0142  232 LYS A O   
1790 C CB  . LYS A 233 ? 0.2755 0.2790 0.2746 0.0225  -0.0246 0.0135  232 LYS A CB  
1791 C CG  . LYS A 233 ? 0.3421 0.3424 0.3357 0.0259  -0.0274 0.0145  232 LYS A CG  
1792 C CD  . LYS A 233 ? 0.4406 0.4338 0.4277 0.0277  -0.0280 0.0166  232 LYS A CD  
1793 C CE  . LYS A 233 ? 0.5222 0.5121 0.5028 0.0311  -0.0305 0.0178  232 LYS A CE  
1794 N NZ  . LYS A 233 ? 0.7138 0.7039 0.6891 0.0296  -0.0283 0.0204  232 LYS A NZ  
1795 N N   . TYR A 234 ? 0.2528 0.2623 0.2567 0.0135  -0.0169 0.0143  233 TYR A N   
1796 C CA  . TYR A 234 ? 0.2712 0.2830 0.2789 0.0108  -0.0145 0.0134  233 TYR A CA  
1797 C C   . TYR A 234 ? 0.2836 0.2904 0.2878 0.0094  -0.0130 0.0148  233 TYR A C   
1798 O O   . TYR A 234 ? 0.2813 0.2873 0.2878 0.0091  -0.0125 0.0134  233 TYR A O   
1799 C CB  . TYR A 234 ? 0.2676 0.2845 0.2771 0.0079  -0.0124 0.0136  233 TYR A CB  
1800 C CG  . TYR A 234 ? 0.2739 0.2927 0.2858 0.0048  -0.0098 0.0131  233 TYR A CG  
1801 C CD1 . TYR A 234 ? 0.2650 0.2872 0.2825 0.0049  -0.0094 0.0107  233 TYR A CD1 
1802 C CD2 . TYR A 234 ? 0.2787 0.2959 0.2874 0.0020  -0.0077 0.0150  233 TYR A CD2 
1803 C CE1 . TYR A 234 ? 0.2554 0.2791 0.2744 0.0024  -0.0070 0.0102  233 TYR A CE1 
1804 C CE2 . TYR A 234 ? 0.3005 0.3192 0.3110 -0.0006 -0.0056 0.0144  233 TYR A CE2 
1805 C CZ  . TYR A 234 ? 0.2710 0.2928 0.2863 -0.0003 -0.0053 0.0120  233 TYR A CZ  
1806 O OH  . TYR A 234 ? 0.3188 0.3419 0.3353 -0.0026 -0.0033 0.0114  233 TYR A OH  
1807 N N   . TYR A 235 ? 0.2769 0.2802 0.2755 0.0086  -0.0124 0.0177  234 TYR A N   
1808 C CA  . TYR A 235 ? 0.2525 0.2511 0.2482 0.0069  -0.0110 0.0193  234 TYR A CA  
1809 C C   . TYR A 235 ? 0.2821 0.2749 0.2758 0.0095  -0.0128 0.0194  234 TYR A C   
1810 O O   . TYR A 235 ? 0.3035 0.2930 0.2972 0.0085  -0.0121 0.0193  234 TYR A O   
1811 C CB  . TYR A 235 ? 0.2457 0.2430 0.2369 0.0050  -0.0094 0.0226  234 TYR A CB  
1812 C CG  . TYR A 235 ? 0.2642 0.2672 0.2575 0.0026  -0.0077 0.0224  234 TYR A CG  
1813 C CD1 . TYR A 235 ? 0.2632 0.2683 0.2591 -0.0007 -0.0057 0.0219  234 TYR A CD1 
1814 C CD2 . TYR A 235 ? 0.2329 0.2391 0.2257 0.0036  -0.0084 0.0226  234 TYR A CD2 
1815 C CE1 . TYR A 235 ? 0.2485 0.2589 0.2464 -0.0029 -0.0043 0.0218  234 TYR A CE1 
1816 C CE2 . TYR A 235 ? 0.2340 0.2454 0.2290 0.0014  -0.0069 0.0224  234 TYR A CE2 
1817 C CZ  . TYR A 235 ? 0.2251 0.2386 0.2227 -0.0019 -0.0048 0.0221  234 TYR A CZ  
1818 O OH  . TYR A 235 ? 0.2654 0.2838 0.2650 -0.0040 -0.0035 0.0220  234 TYR A OH  
1819 N N   . VAL A 236 ? 0.2872 0.2784 0.2791 0.0129  -0.0152 0.0195  235 VAL A N   
1820 C CA  . VAL A 236 ? 0.3099 0.2959 0.3003 0.0158  -0.0173 0.0192  235 VAL A CA  
1821 C C   . VAL A 236 ? 0.3093 0.2967 0.3052 0.0162  -0.0177 0.0161  235 VAL A C   
1822 O O   . VAL A 236 ? 0.3288 0.3118 0.3241 0.0166  -0.0179 0.0160  235 VAL A O   
1823 C CB  . VAL A 236 ? 0.3401 0.3251 0.3279 0.0196  -0.0201 0.0194  235 VAL A CB  
1824 C CG1 . VAL A 236 ? 0.3951 0.3745 0.3811 0.0227  -0.0225 0.0193  235 VAL A CG1 
1825 C CG2 . VAL A 236 ? 0.3609 0.3446 0.3428 0.0191  -0.0193 0.0225  235 VAL A CG2 
1826 N N   . ASN A 237 ? 0.3002 0.2937 0.3015 0.0161  -0.0176 0.0137  236 ASN A N   
1827 C CA  . ASN A 237 ? 0.2988 0.2944 0.3057 0.0165  -0.0175 0.0108  236 ASN A CA  
1828 C C   . ASN A 237 ? 0.2923 0.2862 0.2988 0.0138  -0.0152 0.0109  236 ASN A C   
1829 O O   . ASN A 237 ? 0.2733 0.2648 0.2812 0.0148  -0.0155 0.0094  236 ASN A O   
1830 C CB  . ASN A 237 ? 0.2955 0.2984 0.3084 0.0162  -0.0172 0.0087  236 ASN A CB  
1831 C CG  . ASN A 237 ? 0.3194 0.3242 0.3335 0.0189  -0.0198 0.0082  236 ASN A CG  
1832 O OD1 . ASN A 237 ? 0.3201 0.3210 0.3316 0.0218  -0.0224 0.0086  236 ASN A OD1 
1833 N ND2 . ASN A 237 ? 0.2884 0.2991 0.3064 0.0179  -0.0194 0.0073  236 ASN A ND2 
1834 N N   . LEU A 238 ? 0.2738 0.2690 0.2787 0.0104  -0.0129 0.0124  237 LEU A N   
1835 C CA  . LEU A 238 ? 0.2928 0.2867 0.2977 0.0078  -0.0110 0.0123  237 LEU A CA  
1836 C C   . LEU A 238 ? 0.3029 0.2895 0.3042 0.0083  -0.0117 0.0134  237 LEU A C   
1837 O O   . LEU A 238 ? 0.3007 0.2851 0.3031 0.0080  -0.0113 0.0120  237 LEU A O   
1838 C CB  . LEU A 238 ? 0.2891 0.2854 0.2927 0.0042  -0.0088 0.0140  237 LEU A CB  
1839 C CG  . LEU A 238 ? 0.2775 0.2807 0.2842 0.0032  -0.0079 0.0132  237 LEU A CG  
1840 C CD1 . LEU A 238 ? 0.2973 0.3020 0.3028 -0.0006 -0.0057 0.0146  237 LEU A CD1 
1841 C CD2 . LEU A 238 ? 0.3062 0.3136 0.3182 0.0040  -0.0077 0.0102  237 LEU A CD2 
1842 N N   . GLU A 239 ? 0.3249 0.3074 0.3218 0.0092  -0.0127 0.0161  238 GLU A N   
1843 C CA  . GLU A 239 ? 0.3361 0.3113 0.3296 0.0097  -0.0133 0.0176  238 GLU A CA  
1844 C C   . GLU A 239 ? 0.3297 0.3021 0.3248 0.0128  -0.0153 0.0155  238 GLU A C   
1845 O O   . GLU A 239 ? 0.3870 0.3538 0.3805 0.0129  -0.0157 0.0159  238 GLU A O   
1846 C CB  . GLU A 239 ? 0.3981 0.3699 0.3864 0.0104  -0.0138 0.0211  238 GLU A CB  
1847 C CG  . GLU A 239 ? 0.4196 0.3931 0.4058 0.0073  -0.0116 0.0237  238 GLU A CG  
1848 C CD  . GLU A 239 ? 0.4893 0.4590 0.4700 0.0084  -0.0119 0.0272  238 GLU A CD  
1849 O OE1 . GLU A 239 ? 0.5114 0.4798 0.4901 0.0119  -0.0140 0.0272  238 GLU A OE1 
1850 O OE2 . GLU A 239 ? 0.5130 0.4809 0.4913 0.0059  -0.0100 0.0301  238 GLU A OE2 
1851 N N   . GLU A 240 ? 0.3099 0.2861 0.3083 0.0154  -0.0167 0.0132  239 GLU A N   
1852 C CA  . GLU A 240 ? 0.3523 0.3267 0.3530 0.0186  -0.0186 0.0110  239 GLU A CA  
1853 C C   . GLU A 240 ? 0.3194 0.2977 0.3254 0.0182  -0.0175 0.0077  239 GLU A C   
1854 O O   . GLU A 240 ? 0.2787 0.2571 0.2879 0.0210  -0.0188 0.0054  239 GLU A O   
1855 C CB  . GLU A 240 ? 0.3822 0.3581 0.3838 0.0221  -0.0212 0.0105  239 GLU A CB  
1856 C CG  . GLU A 240 ? 0.3889 0.3608 0.3846 0.0232  -0.0224 0.0135  239 GLU A CG  
1857 C CD  . GLU A 240 ? 0.5012 0.4744 0.4977 0.0269  -0.0254 0.0126  239 GLU A CD  
1858 O OE1 . GLU A 240 ? 0.4561 0.4343 0.4584 0.0280  -0.0261 0.0098  239 GLU A OE1 
1859 O OE2 . GLU A 240 ? 0.6209 0.5899 0.6122 0.0288  -0.0270 0.0147  239 GLU A OE2 
1860 N N   . GLN A 241 ? 0.3036 0.2851 0.3106 0.0149  -0.0150 0.0075  240 GLN A N   
1861 C CA  . GLN A 241 ? 0.3056 0.2910 0.3170 0.0144  -0.0135 0.0047  240 GLN A CA  
1862 C C   . GLN A 241 ? 0.3082 0.3001 0.3248 0.0162  -0.0138 0.0027  240 GLN A C   
1863 O O   . GLN A 241 ? 0.2779 0.2721 0.2987 0.0176  -0.0134 0.0001  240 GLN A O   
1864 C CB  . GLN A 241 ? 0.3118 0.2925 0.3232 0.0158  -0.0141 0.0030  240 GLN A CB  
1865 C CG  . GLN A 241 ? 0.3499 0.3236 0.3567 0.0142  -0.0141 0.0048  240 GLN A CG  
1866 C CD  . GLN A 241 ? 0.4530 0.4278 0.4585 0.0102  -0.0120 0.0058  240 GLN A CD  
1867 O OE1 . GLN A 241 ? 0.4297 0.4012 0.4317 0.0081  -0.0118 0.0086  240 GLN A OE1 
1868 N NE2 . GLN A 241 ? 0.4510 0.4305 0.4592 0.0090  -0.0103 0.0037  240 GLN A NE2 
1869 N N   . LYS A 242 ? 0.2690 0.2640 0.2857 0.0162  -0.0144 0.0039  241 LYS A N   
1870 C CA  . LYS A 242 ? 0.2505 0.2515 0.2726 0.0177  -0.0150 0.0023  241 LYS A CA  
1871 C C   . LYS A 242 ? 0.3087 0.3154 0.3323 0.0151  -0.0133 0.0028  241 LYS A C   
1872 O O   . LYS A 242 ? 0.2999 0.3110 0.3269 0.0161  -0.0141 0.0023  241 LYS A O   
1873 C CB  . LYS A 242 ? 0.3115 0.3108 0.3331 0.0209  -0.0182 0.0027  241 LYS A CB  
1874 C CG  . LYS A 242 ? 0.3176 0.3115 0.3383 0.0238  -0.0201 0.0020  241 LYS A CG  
1875 C CD  . LYS A 242 ? 0.3785 0.3700 0.3976 0.0270  -0.0235 0.0026  241 LYS A CD  
1876 C CE  . LYS A 242 ? 0.4323 0.4181 0.4503 0.0299  -0.0254 0.0021  241 LYS A CE  
1877 N NZ  . LYS A 242 ? 0.6465 0.6309 0.6642 0.0335  -0.0289 0.0021  241 LYS A NZ  
1878 N N   . GLY A 243 ? 0.2744 0.2813 0.2958 0.0119  -0.0109 0.0038  242 GLY A N   
1879 C CA  . GLY A 243 ? 0.2739 0.2867 0.2977 0.0096  -0.0090 0.0037  242 GLY A CA  
1880 C C   . GLY A 243 ? 0.3066 0.3244 0.3365 0.0105  -0.0080 0.0012  242 GLY A C   
1881 O O   . GLY A 243 ? 0.2808 0.2972 0.3120 0.0116  -0.0076 -0.0005 242 GLY A O   
1882 N N   . LEU A 244 ? 0.2625 0.2860 0.2963 0.0100  -0.0076 0.0010  243 LEU A N   
1883 C CA  . LEU A 244 ? 0.2692 0.2978 0.3096 0.0111  -0.0067 -0.0011 243 LEU A CA  
1884 C C   . LEU A 244 ? 0.2447 0.2756 0.2857 0.0091  -0.0035 -0.0018 243 LEU A C   
1885 O O   . LEU A 244 ? 0.2592 0.2905 0.3026 0.0104  -0.0025 -0.0036 243 LEU A O   
1886 C CB  . LEU A 244 ? 0.2418 0.2756 0.2867 0.0114  -0.0075 -0.0011 243 LEU A CB  
1887 C CG  . LEU A 244 ? 0.2776 0.3172 0.3302 0.0123  -0.0063 -0.0029 243 LEU A CG  
1888 C CD1 . LEU A 244 ? 0.2868 0.3252 0.3428 0.0156  -0.0078 -0.0047 243 LEU A CD1 
1889 C CD2 . LEU A 244 ? 0.2678 0.3123 0.3247 0.0118  -0.0070 -0.0026 243 LEU A CD2 
1890 N N   . ILE A 245 ? 0.2620 0.2946 0.3009 0.0061  -0.0019 -0.0005 244 ILE A N   
1891 C CA  . ILE A 245 ? 0.2506 0.2853 0.2896 0.0043  0.0009  -0.0012 244 ILE A CA  
1892 C C   . ILE A 245 ? 0.2311 0.2606 0.2642 0.0027  0.0012  -0.0006 244 ILE A C   
1893 O O   . ILE A 245 ? 0.2386 0.2637 0.2678 0.0023  -0.0003 0.0009  244 ILE A O   
1894 C CB  . ILE A 245 ? 0.2527 0.2929 0.2937 0.0021  0.0025  -0.0003 244 ILE A CB  
1895 C CG1 . ILE A 245 ? 0.2632 0.3024 0.3005 0.0001  0.0017  0.0018  244 ILE A CG1 
1896 C CG2 . ILE A 245 ? 0.2739 0.3193 0.3218 0.0037  0.0023  -0.0012 244 ILE A CG2 
1897 C CD1 . ILE A 245 ? 0.2652 0.3094 0.3041 -0.0022 0.0034  0.0026  244 ILE A CD1 
1898 N N   . GLN A 246 ? 0.2333 0.2632 0.2659 0.0020  0.0032  -0.0018 245 GLN A N   
1899 C CA  . GLN A 246 ? 0.2923 0.3172 0.3200 0.0006  0.0033  -0.0017 245 GLN A CA  
1900 C C   . GLN A 246 ? 0.2467 0.2704 0.2709 -0.0023 0.0030  0.0006  245 GLN A C   
1901 O O   . GLN A 246 ? 0.2739 0.2924 0.2944 -0.0029 0.0018  0.0016  245 GLN A O   
1902 C CB  . GLN A 246 ? 0.2978 0.3243 0.3255 0.0002  0.0055  -0.0034 245 GLN A CB  
1903 C CG  . GLN A 246 ? 0.3058 0.3279 0.3286 -0.0017 0.0055  -0.0034 245 GLN A CG  
1904 C CD  . GLN A 246 ? 0.3799 0.4031 0.4022 -0.0016 0.0075  -0.0054 245 GLN A CD  
1905 O OE1 . GLN A 246 ? 0.3333 0.3609 0.3589 -0.0001 0.0091  -0.0066 245 GLN A OE1 
1906 N NE2 . GLN A 246 ? 0.3635 0.3829 0.3817 -0.0032 0.0073  -0.0058 245 GLN A NE2 
1907 N N   . SER A 247 ? 0.2650 0.2934 0.2904 -0.0040 0.0040  0.0016  246 SER A N   
1908 C CA  . SER A 247 ? 0.2414 0.2691 0.2637 -0.0067 0.0040  0.0038  246 SER A CA  
1909 C C   . SER A 247 ? 0.2548 0.2796 0.2754 -0.0061 0.0021  0.0056  246 SER A C   
1910 O O   . SER A 247 ? 0.2639 0.2865 0.2813 -0.0081 0.0020  0.0075  246 SER A O   
1911 C CB  . SER A 247 ? 0.2913 0.3248 0.3156 -0.0083 0.0055  0.0043  246 SER A CB  
1912 O OG  . SER A 247 ? 0.3024 0.3398 0.3310 -0.0066 0.0052  0.0039  246 SER A OG  
1913 N N   . ASP A 248 ? 0.2229 0.2480 0.2456 -0.0035 0.0007  0.0052  247 ASP A N   
1914 C CA  . ASP A 248 ? 0.2662 0.2877 0.2864 -0.0024 -0.0013 0.0068  247 ASP A CA  
1915 C C   . ASP A 248 ? 0.2476 0.2624 0.2641 -0.0022 -0.0020 0.0072  247 ASP A C   
1916 O O   . ASP A 248 ? 0.2681 0.2795 0.2810 -0.0034 -0.0023 0.0093  247 ASP A O   
1917 C CB  . ASP A 248 ? 0.2640 0.2869 0.2873 0.0007  -0.0030 0.0059  247 ASP A CB  
1918 C CG  . ASP A 248 ? 0.3072 0.3359 0.3342 0.0006  -0.0028 0.0059  247 ASP A CG  
1919 O OD1 . ASP A 248 ? 0.3278 0.3586 0.3536 -0.0017 -0.0019 0.0072  247 ASP A OD1 
1920 O OD2 . ASP A 248 ? 0.2669 0.2982 0.2984 0.0028  -0.0038 0.0044  247 ASP A OD2 
1921 N N   . GLN A 249 ? 0.2456 0.2586 0.2635 -0.0004 -0.0023 0.0052  248 GLN A N   
1922 C CA  . GLN A 249 ? 0.2372 0.2436 0.2520 0.0003  -0.0034 0.0054  248 GLN A CA  
1923 C C   . GLN A 249 ? 0.2774 0.2810 0.2893 -0.0027 -0.0023 0.0061  248 GLN A C   
1924 O O   . GLN A 249 ? 0.2733 0.2713 0.2822 -0.0031 -0.0032 0.0073  248 GLN A O   
1925 C CB  . GLN A 249 ? 0.2523 0.2577 0.2695 0.0030  -0.0039 0.0028  248 GLN A CB  
1926 C CG  . GLN A 249 ? 0.2561 0.2545 0.2706 0.0045  -0.0056 0.0031  248 GLN A CG  
1927 C CD  . GLN A 249 ? 0.3067 0.3024 0.3190 0.0057  -0.0075 0.0053  248 GLN A CD  
1928 O OE1 . GLN A 249 ? 0.3393 0.3379 0.3537 0.0076  -0.0084 0.0052  248 GLN A OE1 
1929 N NE2 . GLN A 249 ? 0.2838 0.2737 0.2920 0.0048  -0.0080 0.0073  248 GLN A NE2 
1930 N N   . GLU A 250 ? 0.2557 0.2631 0.2686 -0.0047 -0.0006 0.0053  249 GLU A N   
1931 C CA  . GLU A 250 ? 0.3155 0.3207 0.3260 -0.0076 0.0001  0.0058  249 GLU A CA  
1932 C C   . GLU A 250 ? 0.2947 0.2974 0.3025 -0.0096 -0.0003 0.0089  249 GLU A C   
1933 O O   . GLU A 250 ? 0.2658 0.2641 0.2715 -0.0113 -0.0005 0.0097  249 GLU A O   
1934 C CB  . GLU A 250 ? 0.2945 0.3048 0.3063 -0.0094 0.0019  0.0049  249 GLU A CB  
1935 C CG  . GLU A 250 ? 0.3891 0.4015 0.4029 -0.0078 0.0028  0.0020  249 GLU A CG  
1936 C CD  . GLU A 250 ? 0.4576 0.4663 0.4693 -0.0083 0.0029  0.0003  249 GLU A CD  
1937 O OE1 . GLU A 250 ? 0.4900 0.4942 0.4990 -0.0102 0.0020  0.0014  249 GLU A OE1 
1938 O OE2 . GLU A 250 ? 0.4109 0.4211 0.4236 -0.0069 0.0038  -0.0020 249 GLU A OE2 
1939 N N   . LEU A 251 ? 0.2628 0.2680 0.2708 -0.0093 -0.0004 0.0106  250 LEU A N   
1940 C CA  . LEU A 251 ? 0.2632 0.2665 0.2685 -0.0110 -0.0004 0.0137  250 LEU A CA  
1941 C C   . LEU A 251 ? 0.2846 0.2811 0.2873 -0.0102 -0.0016 0.0150  250 LEU A C   
1942 O O   . LEU A 251 ? 0.3191 0.3129 0.3197 -0.0120 -0.0013 0.0176  250 LEU A O   
1943 C CB  . LEU A 251 ? 0.2576 0.2644 0.2632 -0.0100 -0.0005 0.0149  250 LEU A CB  
1944 C CG  . LEU A 251 ? 0.2831 0.2967 0.2916 -0.0107 0.0005  0.0140  250 LEU A CG  
1945 C CD1 . LEU A 251 ? 0.2949 0.3109 0.3035 -0.0094 -0.0001 0.0151  250 LEU A CD1 
1946 C CD2 . LEU A 251 ? 0.2787 0.2940 0.2869 -0.0140 0.0020  0.0147  250 LEU A CD2 
1947 N N   . PHE A 252 ? 0.2785 0.2722 0.2815 -0.0074 -0.0029 0.0136  251 PHE A N   
1948 C CA  . PHE A 252 ? 0.2672 0.2542 0.2677 -0.0063 -0.0042 0.0149  251 PHE A CA  
1949 C C   . PHE A 252 ? 0.3245 0.3071 0.3251 -0.0063 -0.0047 0.0131  251 PHE A C   
1950 O O   . PHE A 252 ? 0.3370 0.3137 0.3355 -0.0068 -0.0053 0.0145  251 PHE A O   
1951 C CB  . PHE A 252 ? 0.2999 0.2862 0.3001 -0.0027 -0.0058 0.0149  251 PHE A CB  
1952 C CG  . PHE A 252 ? 0.3591 0.3388 0.3560 -0.0015 -0.0070 0.0170  251 PHE A CG  
1953 C CD1 . PHE A 252 ? 0.3402 0.3180 0.3340 -0.0027 -0.0065 0.0204  251 PHE A CD1 
1954 C CD2 . PHE A 252 ? 0.4001 0.3754 0.3970 0.0009  -0.0086 0.0156  251 PHE A CD2 
1955 C CE1 . PHE A 252 ? 0.3842 0.3556 0.3746 -0.0016 -0.0075 0.0226  251 PHE A CE1 
1956 C CE2 . PHE A 252 ? 0.4107 0.3795 0.4044 0.0021  -0.0098 0.0177  251 PHE A CE2 
1957 C CZ  . PHE A 252 ? 0.3808 0.3477 0.3712 0.0008  -0.0092 0.0213  251 PHE A CZ  
1958 N N   . SER A 253 ? 0.2977 0.2830 0.3007 -0.0057 -0.0043 0.0100  252 SER A N   
1959 C CA  . SER A 253 ? 0.3106 0.2918 0.3136 -0.0048 -0.0050 0.0078  252 SER A CA  
1960 C C   . SER A 253 ? 0.3229 0.3045 0.3261 -0.0071 -0.0041 0.0062  252 SER A C   
1961 O O   . SER A 253 ? 0.3646 0.3422 0.3674 -0.0065 -0.0048 0.0043  252 SER A O   
1962 C CB  . SER A 253 ? 0.3195 0.3027 0.3250 -0.0013 -0.0055 0.0051  252 SER A CB  
1963 O OG  . SER A 253 ? 0.3163 0.2985 0.3216 0.0011  -0.0068 0.0063  252 SER A OG  
1964 N N   . SER A 254 ? 0.2922 0.2784 0.2959 -0.0096 -0.0027 0.0068  253 SER A N   
1965 C CA  . SER A 254 ? 0.2928 0.2796 0.2964 -0.0117 -0.0020 0.0053  253 SER A CA  
1966 C C   . SER A 254 ? 0.3215 0.3022 0.3234 -0.0138 -0.0030 0.0063  253 SER A C   
1967 O O   . SER A 254 ? 0.3331 0.3111 0.3340 -0.0149 -0.0033 0.0092  253 SER A O   
1968 C CB  . SER A 254 ? 0.3046 0.2974 0.3090 -0.0139 -0.0005 0.0061  253 SER A CB  
1969 O OG  . SER A 254 ? 0.3175 0.3102 0.3213 -0.0162 -0.0001 0.0050  253 SER A OG  
1970 N N   . PRO A 255 ? 0.2980 0.2763 0.2995 -0.0143 -0.0034 0.0039  254 PRO A N   
1971 C CA  . PRO A 255 ? 0.3275 0.3006 0.3280 -0.0169 -0.0044 0.0049  254 PRO A CA  
1972 C C   . PRO A 255 ? 0.3133 0.2890 0.3141 -0.0204 -0.0036 0.0074  254 PRO A C   
1973 O O   . PRO A 255 ? 0.3161 0.2880 0.3169 -0.0227 -0.0042 0.0092  254 PRO A O   
1974 C CB  . PRO A 255 ? 0.3505 0.3220 0.3505 -0.0167 -0.0050 0.0013  254 PRO A CB  
1975 C CG  . PRO A 255 ? 0.3676 0.3418 0.3680 -0.0132 -0.0044 -0.0013 254 PRO A CG  
1976 C CD  . PRO A 255 ? 0.3588 0.3389 0.3606 -0.0126 -0.0030 0.0003  254 PRO A CD  
1977 N N   . ASN A 256 ? 0.3058 0.2881 0.3075 -0.0208 -0.0021 0.0078  255 ASN A N   
1978 C CA  . ASN A 256 ? 0.2852 0.2707 0.2873 -0.0238 -0.0012 0.0100  255 ASN A CA  
1979 C C   . ASN A 256 ? 0.3270 0.3140 0.3291 -0.0237 -0.0005 0.0133  255 ASN A C   
1980 O O   . ASN A 256 ? 0.2805 0.2712 0.2832 -0.0256 0.0005  0.0151  255 ASN A O   
1981 C CB  . ASN A 256 ? 0.3001 0.2917 0.3029 -0.0241 -0.0001 0.0082  255 ASN A CB  
1982 C CG  . ASN A 256 ? 0.3391 0.3342 0.3426 -0.0272 0.0007  0.0101  255 ASN A CG  
1983 O OD1 . ASN A 256 ? 0.3507 0.3513 0.3550 -0.0272 0.0019  0.0109  255 ASN A OD1 
1984 N ND2 . ASN A 256 ? 0.3201 0.3121 0.3237 -0.0298 -0.0001 0.0108  255 ASN A ND2 
1985 N N   . ALA A 257 ? 0.2980 0.2821 0.2993 -0.0213 -0.0011 0.0140  256 ALA A N   
1986 C CA  . ALA A 257 ? 0.2741 0.2597 0.2748 -0.0204 -0.0006 0.0167  256 ALA A CA  
1987 C C   . ALA A 257 ? 0.2756 0.2568 0.2750 -0.0218 -0.0007 0.0202  256 ALA A C   
1988 O O   . ALA A 257 ? 0.2883 0.2690 0.2862 -0.0205 -0.0005 0.0225  256 ALA A O   
1989 C CB  . ALA A 257 ? 0.2932 0.2785 0.2936 -0.0167 -0.0014 0.0156  256 ALA A CB  
1990 N N   . THR A 258 ? 0.2993 0.2773 0.2992 -0.0245 -0.0009 0.0208  257 THR A N   
1991 C CA  . THR A 258 ? 0.3530 0.3270 0.3522 -0.0260 -0.0006 0.0245  257 THR A CA  
1992 C C   . THR A 258 ? 0.3044 0.2825 0.3031 -0.0267 0.0010  0.0274  257 THR A C   
1993 O O   . THR A 258 ? 0.3272 0.3030 0.3243 -0.0262 0.0014  0.0305  257 THR A O   
1994 C CB  . THR A 258 ? 0.3686 0.3396 0.3695 -0.0292 -0.0011 0.0246  257 THR A CB  
1995 O OG1 . THR A 258 ? 0.3960 0.3614 0.3967 -0.0282 -0.0028 0.0224  257 THR A OG1 
1996 C CG2 . THR A 258 ? 0.4276 0.3960 0.4286 -0.0313 -0.0002 0.0288  257 THR A CG2 
1997 N N   . ASP A 259 ? 0.3295 0.3138 0.3295 -0.0278 0.0019  0.0266  258 ASP A N   
1998 C CA  . ASP A 259 ? 0.3484 0.3367 0.3480 -0.0284 0.0034  0.0292  258 ASP A CA  
1999 C C   . ASP A 259 ? 0.3687 0.3601 0.3669 -0.0253 0.0034  0.0288  258 ASP A C   
2000 O O   . ASP A 259 ? 0.4041 0.3974 0.4010 -0.0250 0.0044  0.0311  258 ASP A O   
2001 C CB  . ASP A 259 ? 0.3865 0.3798 0.3883 -0.0312 0.0043  0.0288  258 ASP A CB  
2002 C CG  . ASP A 259 ? 0.4819 0.4792 0.4848 -0.0306 0.0039  0.0252  258 ASP A CG  
2003 O OD1 . ASP A 259 ? 0.4614 0.4570 0.4638 -0.0284 0.0029  0.0228  258 ASP A OD1 
2004 O OD2 . ASP A 259 ? 0.5597 0.5618 0.5639 -0.0322 0.0047  0.0250  258 ASP A OD2 
2005 N N   . THR A 260 ? 0.3178 0.3097 0.3162 -0.0229 0.0024  0.0259  259 THR A N   
2006 C CA  . THR A 260 ? 0.2690 0.2638 0.2668 -0.0201 0.0021  0.0254  259 THR A CA  
2007 C C   . THR A 260 ? 0.3006 0.2908 0.2962 -0.0171 0.0009  0.0262  259 THR A C   
2008 O O   . THR A 260 ? 0.2946 0.2862 0.2887 -0.0151 0.0007  0.0272  259 THR A O   
2009 C CB  . THR A 260 ? 0.3135 0.3124 0.3136 -0.0190 0.0018  0.0219  259 THR A CB  
2010 O OG1 . THR A 260 ? 0.3531 0.3486 0.3538 -0.0185 0.0010  0.0196  259 THR A OG1 
2011 C CG2 . THR A 260 ? 0.2953 0.2995 0.2972 -0.0214 0.0030  0.0214  259 THR A CG2 
2012 N N   . ILE A 261 ? 0.3278 0.3123 0.3228 -0.0168 0.0000  0.0259  260 ILE A N   
2013 C CA  . ILE A 261 ? 0.3319 0.3116 0.3245 -0.0140 -0.0013 0.0269  260 ILE A CA  
2014 C C   . ILE A 261 ? 0.3336 0.3120 0.3231 -0.0136 -0.0006 0.0306  260 ILE A C   
2015 O O   . ILE A 261 ? 0.3256 0.3037 0.3131 -0.0106 -0.0015 0.0310  260 ILE A O   
2016 C CB  . ILE A 261 ? 0.3592 0.3325 0.3517 -0.0142 -0.0023 0.0263  260 ILE A CB  
2017 C CG1 . ILE A 261 ? 0.3210 0.2952 0.3157 -0.0128 -0.0032 0.0223  260 ILE A CG1 
2018 C CG2 . ILE A 261 ? 0.4054 0.3729 0.3950 -0.0119 -0.0032 0.0285  260 ILE A CG2 
2019 C CD1 . ILE A 261 ? 0.3455 0.3148 0.3408 -0.0138 -0.0040 0.0210  260 ILE A CD1 
2020 N N   . PRO A 262 ? 0.3299 0.3074 0.3190 -0.0164 0.0009  0.0335  261 PRO A N   
2021 C CA  . PRO A 262 ? 0.3511 0.3275 0.3369 -0.0157 0.0018  0.0372  261 PRO A CA  
2022 C C   . PRO A 262 ? 0.3243 0.3061 0.3092 -0.0142 0.0021  0.0371  261 PRO A C   
2023 O O   . PRO A 262 ? 0.3193 0.2999 0.3007 -0.0119 0.0020  0.0390  261 PRO A O   
2024 C CB  . PRO A 262 ? 0.3193 0.2949 0.3061 -0.0194 0.0036  0.0399  261 PRO A CB  
2025 C CG  . PRO A 262 ? 0.3278 0.3056 0.3185 -0.0221 0.0035  0.0373  261 PRO A CG  
2026 C CD  . PRO A 262 ? 0.3393 0.3163 0.3307 -0.0200 0.0017  0.0335  261 PRO A CD  
2027 N N   . LEU A 263 ? 0.2958 0.2835 0.2836 -0.0154 0.0025  0.0348  262 LEU A N   
2028 C CA  . LEU A 263 ? 0.2948 0.2876 0.2823 -0.0140 0.0026  0.0344  262 LEU A CA  
2029 C C   . LEU A 263 ? 0.3077 0.3002 0.2945 -0.0102 0.0005  0.0324  262 LEU A C   
2030 O O   . LEU A 263 ? 0.2992 0.2923 0.2835 -0.0079 -0.0001 0.0333  262 LEU A O   
2031 C CB  . LEU A 263 ? 0.2751 0.2738 0.2661 -0.0163 0.0034  0.0325  262 LEU A CB  
2032 C CG  . LEU A 263 ? 0.3091 0.3093 0.3010 -0.0198 0.0053  0.0345  262 LEU A CG  
2033 C CD1 . LEU A 263 ? 0.3288 0.3339 0.3242 -0.0219 0.0057  0.0323  262 LEU A CD1 
2034 C CD2 . LEU A 263 ? 0.3535 0.3554 0.3430 -0.0193 0.0065  0.0373  262 LEU A CD2 
2035 N N   . VAL A 264 ? 0.2792 0.2709 0.2683 -0.0095 -0.0007 0.0296  263 VAL A N   
2036 C CA  . VAL A 264 ? 0.2468 0.2381 0.2360 -0.0059 -0.0027 0.0276  263 VAL A CA  
2037 C C   . VAL A 264 ? 0.2812 0.2673 0.2661 -0.0034 -0.0038 0.0299  263 VAL A C   
2038 O O   . VAL A 264 ? 0.2980 0.2847 0.2813 -0.0005 -0.0052 0.0297  263 VAL A O   
2039 C CB  . VAL A 264 ? 0.2734 0.2640 0.2657 -0.0056 -0.0036 0.0246  263 VAL A CB  
2040 C CG1 . VAL A 264 ? 0.2869 0.2762 0.2793 -0.0017 -0.0058 0.0230  263 VAL A CG1 
2041 C CG2 . VAL A 264 ? 0.2663 0.2626 0.2626 -0.0074 -0.0025 0.0223  263 VAL A CG2 
2042 N N   . ARG A 265 ? 0.2821 0.2627 0.2650 -0.0044 -0.0033 0.0320  264 ARG A N   
2043 C CA  . ARG A 265 ? 0.3282 0.3032 0.3065 -0.0019 -0.0042 0.0345  264 ARG A CA  
2044 C C   . ARG A 265 ? 0.3186 0.2949 0.2931 -0.0012 -0.0033 0.0372  264 ARG A C   
2045 O O   . ARG A 265 ? 0.3438 0.3181 0.3148 0.0022  -0.0048 0.0379  264 ARG A O   
2046 C CB  . ARG A 265 ? 0.3246 0.2935 0.3019 -0.0035 -0.0036 0.0365  264 ARG A CB  
2047 C CG  . ARG A 265 ? 0.3910 0.3571 0.3707 -0.0032 -0.0050 0.0339  264 ARG A CG  
2048 C CD  . ARG A 265 ? 0.4239 0.3833 0.4025 -0.0045 -0.0047 0.0360  264 ARG A CD  
2049 N NE  . ARG A 265 ? 0.5217 0.4776 0.5019 -0.0033 -0.0064 0.0335  264 ARG A NE  
2050 C CZ  . ARG A 265 ? 0.5836 0.5355 0.5652 -0.0053 -0.0063 0.0334  264 ARG A CZ  
2051 N NH1 . ARG A 265 ? 0.5681 0.5190 0.5500 -0.0088 -0.0047 0.0357  264 ARG A NH1 
2052 N NH2 . ARG A 265 ? 0.5816 0.5303 0.5643 -0.0037 -0.0080 0.0308  264 ARG A NH2 
2053 N N   . SER A 266 ? 0.3032 0.2826 0.2783 -0.0040 -0.0011 0.0387  265 SER A N   
2054 C CA  . SER A 266 ? 0.3056 0.2861 0.2769 -0.0032 -0.0001 0.0414  265 SER A CA  
2055 C C   . SER A 266 ? 0.3356 0.3204 0.3069 -0.0006 -0.0016 0.0392  265 SER A C   
2056 O O   . SER A 266 ? 0.3314 0.3152 0.2982 0.0021  -0.0021 0.0407  265 SER A O   
2057 C CB  . SER A 266 ? 0.3410 0.3243 0.3137 -0.0069 0.0027  0.0433  265 SER A CB  
2058 O OG  . SER A 266 ? 0.4735 0.4632 0.4498 -0.0082 0.0029  0.0409  265 SER A OG  
2059 N N   . PHE A 267 ? 0.3069 0.2963 0.2828 -0.0012 -0.0023 0.0359  266 PHE A N   
2060 C CA  . PHE A 267 ? 0.2708 0.2643 0.2476 0.0011  -0.0039 0.0337  266 PHE A CA  
2061 C C   . PHE A 267 ? 0.3222 0.3129 0.2978 0.0050  -0.0068 0.0323  266 PHE A C   
2062 O O   . PHE A 267 ? 0.3308 0.3227 0.3048 0.0078  -0.0085 0.0317  266 PHE A O   
2063 C CB  . PHE A 267 ? 0.2652 0.2646 0.2478 -0.0009 -0.0036 0.0308  266 PHE A CB  
2064 C CG  . PHE A 267 ? 0.2886 0.2914 0.2726 -0.0045 -0.0012 0.0318  266 PHE A CG  
2065 C CD1 . PHE A 267 ? 0.3081 0.3099 0.2888 -0.0055 0.0006  0.0351  266 PHE A CD1 
2066 C CD2 . PHE A 267 ? 0.2671 0.2743 0.2558 -0.0067 -0.0006 0.0296  266 PHE A CD2 
2067 C CE1 . PHE A 267 ? 0.2694 0.2746 0.2518 -0.0088 0.0027  0.0359  266 PHE A CE1 
2068 C CE2 . PHE A 267 ? 0.2983 0.3086 0.2882 -0.0098 0.0015  0.0305  266 PHE A CE2 
2069 C CZ  . PHE A 267 ? 0.2754 0.2848 0.2624 -0.0109 0.0030  0.0336  266 PHE A CZ  
2070 N N   . ALA A 268 ? 0.3102 0.2971 0.2868 0.0054  -0.0076 0.0315  267 ALA A N   
2071 C CA  . ALA A 268 ? 0.3154 0.2989 0.2906 0.0092  -0.0104 0.0305  267 ALA A CA  
2072 C C   . ALA A 268 ? 0.3592 0.3378 0.3276 0.0116  -0.0109 0.0337  267 ALA A C   
2073 O O   . ALA A 268 ? 0.4127 0.3898 0.3789 0.0153  -0.0135 0.0330  267 ALA A O   
2074 C CB  . ALA A 268 ? 0.3317 0.3119 0.3091 0.0090  -0.0110 0.0292  267 ALA A CB  
2075 N N   . ASN A 269 ? 0.3254 0.3015 0.2906 0.0096  -0.0085 0.0371  268 ASN A N   
2076 C CA  . ASN A 269 ? 0.3660 0.3370 0.3245 0.0118  -0.0085 0.0405  268 ASN A CA  
2077 C C   . ASN A 269 ? 0.4047 0.3781 0.3593 0.0134  -0.0082 0.0417  268 ASN A C   
2078 O O   . ASN A 269 ? 0.4599 0.4295 0.4085 0.0166  -0.0092 0.0436  268 ASN A O   
2079 C CB  . ASN A 269 ? 0.3846 0.3516 0.3416 0.0091  -0.0058 0.0440  268 ASN A CB  
2080 C CG  . ASN A 269 ? 0.5193 0.4817 0.4781 0.0086  -0.0067 0.0434  268 ASN A CG  
2081 O OD1 . ASN A 269 ? 0.6067 0.5677 0.5664 0.0112  -0.0093 0.0410  268 ASN A OD1 
2082 N ND2 . ASN A 269 ? 0.5471 0.5070 0.5068 0.0054  -0.0045 0.0455  268 ASN A ND2 
2083 N N   . SER A 270 ? 0.3597 0.3390 0.3171 0.0114  -0.0070 0.0406  269 SER A N   
2084 C CA  . SER A 270 ? 0.3562 0.3377 0.3099 0.0128  -0.0066 0.0417  269 SER A CA  
2085 C C   . SER A 270 ? 0.3269 0.3151 0.2853 0.0123  -0.0075 0.0385  269 SER A C   
2086 O O   . SER A 270 ? 0.3159 0.3080 0.2788 0.0088  -0.0057 0.0378  269 SER A O   
2087 C CB  . SER A 270 ? 0.3894 0.3706 0.3406 0.0103  -0.0030 0.0455  269 SER A CB  
2088 O OG  . SER A 270 ? 0.3718 0.3565 0.3207 0.0112  -0.0024 0.0460  269 SER A OG  
2089 N N   . THR A 271 ? 0.3109 0.3451 0.2745 -0.0099 0.0202  0.0215  270 THR A N   
2090 C CA  . THR A 271 ? 0.3635 0.3885 0.3223 -0.0082 0.0177  0.0214  270 THR A CA  
2091 C C   . THR A 271 ? 0.3285 0.3536 0.2890 -0.0018 0.0200  0.0222  270 THR A C   
2092 O O   . THR A 271 ? 0.3243 0.3480 0.2863 -0.0006 0.0180  0.0234  270 THR A O   
2093 C CB  . THR A 271 ? 0.3894 0.4013 0.3371 -0.0088 0.0166  0.0189  270 THR A CB  
2094 O OG1 . THR A 271 ? 0.4043 0.4160 0.3509 -0.0150 0.0139  0.0180  270 THR A OG1 
2095 C CG2 . THR A 271 ? 0.4526 0.4550 0.3953 -0.0067 0.0142  0.0187  270 THR A CG2 
2096 N N   . GLN A 272 ? 0.3218 0.3482 0.2819 0.0023  0.0243  0.0216  271 GLN A N   
2097 C CA  . GLN A 272 ? 0.3301 0.3569 0.2920 0.0085  0.0268  0.0222  271 GLN A CA  
2098 C C   . GLN A 272 ? 0.3329 0.3703 0.3053 0.0090  0.0264  0.0247  271 GLN A C   
2099 O O   . GLN A 272 ? 0.3062 0.3421 0.2800 0.0124  0.0257  0.0255  271 GLN A O   
2100 C CB  . GLN A 272 ? 0.3671 0.3949 0.3276 0.0123  0.0317  0.0211  271 GLN A CB  
2101 C CG  . GLN A 272 ? 0.5059 0.5308 0.4656 0.0191  0.0343  0.0210  271 GLN A CG  
2102 C CD  . GLN A 272 ? 0.6461 0.6571 0.5954 0.0213  0.0330  0.0194  271 GLN A CD  
2103 O OE1 . GLN A 272 ? 0.6693 0.6748 0.6161 0.0196  0.0290  0.0196  271 GLN A OE1 
2104 N NE2 . GLN A 272 ? 0.9506 0.9558 0.8939 0.0251  0.0362  0.0177  271 GLN A NE2 
2105 N N   . THR A 273 ? 0.3057 0.3540 0.2858 0.0055  0.0266  0.0260  272 THR A N   
2106 C CA  . THR A 273 ? 0.2879 0.3465 0.2781 0.0056  0.0260  0.0284  272 THR A CA  
2107 C C   . THR A 273 ? 0.2795 0.3345 0.2696 0.0034  0.0214  0.0294  272 THR A C   
2108 O O   . THR A 273 ? 0.2960 0.3528 0.2901 0.0063  0.0208  0.0308  272 THR A O   
2109 C CB  . THR A 273 ? 0.2859 0.3561 0.2835 0.0017  0.0267  0.0295  272 THR A CB  
2110 O OG1 . THR A 273 ? 0.3131 0.3863 0.3106 0.0038  0.0311  0.0285  272 THR A OG1 
2111 C CG2 . THR A 273 ? 0.3206 0.4015 0.3289 0.0018  0.0261  0.0321  272 THR A CG2 
2112 N N   . PHE A 274 ? 0.2607 0.3105 0.2460 -0.0016 0.0181  0.0286  273 PHE A N   
2113 C CA  . PHE A 274 ? 0.2676 0.3133 0.2520 -0.0039 0.0138  0.0294  273 PHE A CA  
2114 C C   . PHE A 274 ? 0.2509 0.2865 0.2293 0.0007  0.0133  0.0288  273 PHE A C   
2115 O O   . PHE A 274 ? 0.2392 0.2753 0.2206 0.0020  0.0115  0.0302  273 PHE A O   
2116 C CB  . PHE A 274 ? 0.2909 0.3320 0.2705 -0.0100 0.0107  0.0283  273 PHE A CB  
2117 C CG  . PHE A 274 ? 0.2318 0.2657 0.2079 -0.0121 0.0065  0.0285  273 PHE A CG  
2118 C CD1 . PHE A 274 ? 0.2266 0.2646 0.2085 -0.0121 0.0045  0.0306  273 PHE A CD1 
2119 C CD2 . PHE A 274 ? 0.2558 0.2786 0.2228 -0.0142 0.0044  0.0265  273 PHE A CD2 
2120 C CE1 . PHE A 274 ? 0.2360 0.2671 0.2144 -0.0142 0.0007  0.0307  273 PHE A CE1 
2121 C CE2 . PHE A 274 ? 0.2595 0.2756 0.2232 -0.0162 0.0007  0.0267  273 PHE A CE2 
2122 C CZ  . PHE A 274 ? 0.2828 0.3031 0.2522 -0.0162 -0.0012 0.0288  273 PHE A CZ  
2123 N N   . PHE A 275 ? 0.2413 0.2677 0.2112 0.0031  0.0148  0.0267  274 PHE A N   
2124 C CA  . PHE A 275 ? 0.2836 0.2998 0.2472 0.0072  0.0140  0.0260  274 PHE A CA  
2125 C C   . PHE A 275 ? 0.2720 0.2925 0.2409 0.0129  0.0161  0.0272  274 PHE A C   
2126 O O   . PHE A 275 ? 0.2889 0.3052 0.2570 0.0151  0.0140  0.0278  274 PHE A O   
2127 C CB  . PHE A 275 ? 0.2982 0.3041 0.2518 0.0092  0.0156  0.0235  274 PHE A CB  
2128 C CG  . PHE A 275 ? 0.3012 0.2986 0.2473 0.0045  0.0125  0.0221  274 PHE A CG  
2129 C CD1 . PHE A 275 ? 0.2948 0.2949 0.2436 -0.0015 0.0090  0.0228  274 PHE A CD1 
2130 C CD2 . PHE A 275 ? 0.3406 0.3269 0.2769 0.0062  0.0131  0.0199  274 PHE A CD2 
2131 C CE1 . PHE A 275 ? 0.3274 0.3195 0.2693 -0.0057 0.0063  0.0213  274 PHE A CE1 
2132 C CE2 . PHE A 275 ? 0.3323 0.3105 0.2617 0.0020  0.0103  0.0184  274 PHE A CE2 
2133 C CZ  . PHE A 275 ? 0.3607 0.3418 0.2930 -0.0039 0.0069  0.0191  274 PHE A CZ  
2134 N N   . ASN A 276 ? 0.2596 0.2886 0.2341 0.0155  0.0200  0.0275  275 ASN A N   
2135 C CA  . ASN A 276 ? 0.2709 0.3049 0.2515 0.0208  0.0221  0.0287  275 ASN A CA  
2136 C C   . ASN A 276 ? 0.2792 0.3196 0.2676 0.0192  0.0192  0.0309  275 ASN A C   
2137 O O   . ASN A 276 ? 0.2967 0.3353 0.2863 0.0228  0.0183  0.0316  275 ASN A O   
2138 C CB  . ASN A 276 ? 0.3025 0.3454 0.2885 0.0230  0.0268  0.0287  275 ASN A CB  
2139 C CG  . ASN A 276 ? 0.3158 0.3518 0.2943 0.0265  0.0302  0.0265  275 ASN A CG  
2140 O OD1 . ASN A 276 ? 0.3955 0.4203 0.3654 0.0282  0.0292  0.0251  275 ASN A OD1 
2141 N ND2 . ASN A 276 ? 0.3964 0.4391 0.3781 0.0274  0.0343  0.0262  275 ASN A ND2 
2142 N N   . ALA A 277 ? 0.2837 0.3312 0.2770 0.0139  0.0176  0.0321  276 ALA A N   
2143 C CA  . ALA A 277 ? 0.2617 0.3158 0.2626 0.0121  0.0150  0.0344  276 ALA A CA  
2144 C C   . ALA A 277 ? 0.2289 0.2743 0.2248 0.0104  0.0105  0.0345  276 ALA A C   
2145 O O   . ALA A 277 ? 0.2592 0.3064 0.2593 0.0115  0.0086  0.0360  276 ALA A O   
2146 C CB  . ALA A 277 ? 0.2572 0.3211 0.2644 0.0067  0.0146  0.0355  276 ALA A CB  
2147 N N   . PHE A 278 ? 0.2193 0.2551 0.2064 0.0077  0.0088  0.0328  277 PHE A N   
2148 C CA  . PHE A 278 ? 0.2342 0.2610 0.2158 0.0061  0.0048  0.0327  277 PHE A CA  
2149 C C   . PHE A 278 ? 0.2557 0.2753 0.2338 0.0118  0.0048  0.0324  277 PHE A C   
2150 O O   . PHE A 278 ? 0.2700 0.2875 0.2489 0.0120  0.0019  0.0335  277 PHE A O   
2151 C CB  . PHE A 278 ? 0.2594 0.2775 0.2322 0.0021  0.0032  0.0308  277 PHE A CB  
2152 C CG  . PHE A 278 ? 0.2231 0.2325 0.1907 -0.0005 -0.0011 0.0308  277 PHE A CG  
2153 C CD1 . PHE A 278 ? 0.2476 0.2606 0.2189 -0.0058 -0.0042 0.0321  277 PHE A CD1 
2154 C CD2 . PHE A 278 ? 0.2695 0.2671 0.2285 0.0025  -0.0019 0.0294  277 PHE A CD2 
2155 C CE1 . PHE A 278 ? 0.2712 0.2763 0.2378 -0.0081 -0.0081 0.0320  277 PHE A CE1 
2156 C CE2 . PHE A 278 ? 0.2660 0.2557 0.2203 0.0002  -0.0058 0.0294  277 PHE A CE2 
2157 C CZ  . PHE A 278 ? 0.2893 0.2827 0.2473 -0.0052 -0.0089 0.0307  277 PHE A CZ  
2158 N N   . VAL A 279 ? 0.2693 0.2851 0.2433 0.0166  0.0080  0.0309  278 VAL A N   
2159 C CA  . VAL A 279 ? 0.2710 0.2805 0.2421 0.0224  0.0082  0.0306  278 VAL A CA  
2160 C C   . VAL A 279 ? 0.2871 0.3048 0.2673 0.0253  0.0085  0.0325  278 VAL A C   
2161 O O   . VAL A 279 ? 0.2454 0.2592 0.2251 0.0273  0.0060  0.0331  278 VAL A O   
2162 C CB  . VAL A 279 ? 0.2823 0.2872 0.2481 0.0269  0.0119  0.0287  278 VAL A CB  
2163 C CG1 . VAL A 279 ? 0.3026 0.3022 0.2663 0.0333  0.0124  0.0284  278 VAL A CG1 
2164 C CG2 . VAL A 279 ? 0.3130 0.3083 0.2689 0.0242  0.0111  0.0267  278 VAL A CG2 
2165 N N   . GLU A 280 ? 0.2594 0.2886 0.2481 0.0257  0.0113  0.0334  279 GLU A N   
2166 C CA  . GLU A 280 ? 0.2867 0.3243 0.2848 0.0285  0.0117  0.0352  279 GLU A CA  
2167 C C   . GLU A 280 ? 0.2617 0.3002 0.2628 0.0250  0.0073  0.0370  279 GLU A C   
2168 O O   . GLU A 280 ? 0.2687 0.3065 0.2721 0.0278  0.0057  0.0379  279 GLU A O   
2169 C CB  . GLU A 280 ? 0.3110 0.3611 0.3177 0.0283  0.0152  0.0360  279 GLU A CB  
2170 C CG  . GLU A 280 ? 0.5683 0.6190 0.5740 0.0329  0.0201  0.0345  279 GLU A CG  
2171 C CD  . GLU A 280 ? 0.8621 0.9253 0.8764 0.0323  0.0234  0.0354  279 GLU A CD  
2172 O OE1 . GLU A 280 ? 0.8528 0.9238 0.8735 0.0281  0.0218  0.0371  279 GLU A OE1 
2173 O OE2 . GLU A 280 ? 0.9129 0.9779 0.9275 0.0359  0.0276  0.0344  279 GLU A OE2 
2174 N N   . ALA A 281 ? 0.2540 0.2940 0.2548 0.0187  0.0051  0.0374  280 ALA A N   
2175 C CA  . ALA A 281 ? 0.2512 0.2927 0.2551 0.0150  0.0011  0.0392  280 ALA A CA  
2176 C C   . ALA A 281 ? 0.2402 0.2698 0.2362 0.0150  -0.0024 0.0386  280 ALA A C   
2177 O O   . ALA A 281 ? 0.2451 0.2743 0.2434 0.0149  -0.0053 0.0399  280 ALA A O   
2178 C CB  . ALA A 281 ? 0.2321 0.2784 0.2379 0.0083  0.0000  0.0396  280 ALA A CB  
2179 N N   . MET A 282 ? 0.2587 0.2782 0.2451 0.0151  -0.0024 0.0366  281 MET A N   
2180 C CA  . MET A 282 ? 0.2626 0.2703 0.2411 0.0156  -0.0056 0.0359  281 MET A CA  
2181 C C   . MET A 282 ? 0.2987 0.3039 0.2778 0.0218  -0.0054 0.0362  281 MET A C   
2182 O O   . MET A 282 ? 0.2956 0.2955 0.2726 0.0218  -0.0088 0.0368  281 MET A O   
2183 C CB  . MET A 282 ? 0.3141 0.3118 0.2824 0.0151  -0.0052 0.0336  281 MET A CB  
2184 C CG  . MET A 282 ? 0.3371 0.3335 0.3026 0.0084  -0.0069 0.0332  281 MET A CG  
2185 S SD  . MET A 282 ? 0.3582 0.3478 0.3202 0.0038  -0.0123 0.0339  281 MET A SD  
2186 C CE  . MET A 282 ? 0.3385 0.3126 0.2885 0.0072  -0.0134 0.0319  281 MET A CE  
2187 N N   . ASP A 283 ? 0.2842 0.2927 0.2657 0.0270  -0.0016 0.0356  282 ASP A N   
2188 C CA  . ASP A 283 ? 0.2800 0.2864 0.2624 0.0331  -0.0013 0.0357  282 ASP A CA  
2189 C C   . ASP A 283 ? 0.2707 0.2850 0.2622 0.0333  -0.0029 0.0378  282 ASP A C   
2190 O O   . ASP A 283 ? 0.2799 0.2900 0.2708 0.0362  -0.0050 0.0382  282 ASP A O   
2191 C CB  . ASP A 283 ? 0.3042 0.3126 0.2871 0.0385  0.0033  0.0344  282 ASP A CB  
2192 C CG  . ASP A 283 ? 0.3618 0.3592 0.3340 0.0400  0.0042  0.0321  282 ASP A CG  
2193 O OD1 . ASP A 283 ? 0.3467 0.3344 0.3112 0.0376  0.0010  0.0316  282 ASP A OD1 
2194 O OD2 . ASP A 283 ? 0.4015 0.3997 0.3729 0.0436  0.0082  0.0309  282 ASP A OD2 
2195 N N   . ARG A 284 ? 0.2406 0.2659 0.2404 0.0302  -0.0021 0.0393  283 ARG A N   
2196 C CA  . ARG A 284 ? 0.2490 0.2815 0.2573 0.0298  -0.0039 0.0414  283 ARG A CA  
2197 C C   . ARG A 284 ? 0.2727 0.2993 0.2776 0.0256  -0.0088 0.0423  283 ARG A C   
2198 O O   . ARG A 284 ? 0.2754 0.3010 0.2824 0.0273  -0.0112 0.0433  283 ARG A O   
2199 C CB  . ARG A 284 ? 0.2741 0.3194 0.2916 0.0271  -0.0019 0.0427  283 ARG A CB  
2200 C CG  . ARG A 284 ? 0.2426 0.2954 0.2657 0.0319  0.0028  0.0424  283 ARG A CG  
2201 C CD  . ARG A 284 ? 0.2775 0.3419 0.3079 0.0290  0.0051  0.0433  283 ARG A CD  
2202 N NE  . ARG A 284 ? 0.2861 0.3575 0.3234 0.0250  0.0025  0.0455  283 ARG A NE  
2203 C CZ  . ARG A 284 ? 0.3025 0.3796 0.3475 0.0271  0.0016  0.0472  283 ARG A CZ  
2204 N NH1 . ARG A 284 ? 0.3322 0.4092 0.3795 0.0332  0.0031  0.0468  283 ARG A NH1 
2205 N NH2 . ARG A 284 ? 0.3339 0.4167 0.3844 0.0230  -0.0009 0.0491  283 ARG A NH2 
2206 N N   . MET A 285 ? 0.2651 0.2878 0.2647 0.0201  -0.0103 0.0418  284 MET A N   
2207 C CA  . MET A 285 ? 0.2453 0.2616 0.2408 0.0160  -0.0148 0.0423  284 MET A CA  
2208 C C   . MET A 285 ? 0.2878 0.2926 0.2759 0.0195  -0.0168 0.0414  284 MET A C   
2209 O O   . MET A 285 ? 0.2816 0.2832 0.2695 0.0190  -0.0202 0.0425  284 MET A O   
2210 C CB  . MET A 285 ? 0.2389 0.2525 0.2296 0.0099  -0.0157 0.0416  284 MET A CB  
2211 C CG  . MET A 285 ? 0.2644 0.2722 0.2515 0.0053  -0.0201 0.0422  284 MET A CG  
2212 S SD  . MET A 285 ? 0.3195 0.3248 0.3019 -0.0022 -0.0214 0.0413  284 MET A SD  
2213 C CE  . MET A 285 ? 0.3424 0.3353 0.3134 0.0001  -0.0205 0.0385  284 MET A CE  
2214 N N   . GLY A 286 ? 0.2826 0.2808 0.2642 0.0232  -0.0148 0.0395  285 GLY A N   
2215 C CA  . GLY A 286 ? 0.3090 0.2964 0.2836 0.0270  -0.0165 0.0386  285 GLY A CA  
2216 C C   . GLY A 286 ? 0.3265 0.3164 0.3061 0.0324  -0.0166 0.0394  285 GLY A C   
2217 O O   . GLY A 286 ? 0.3386 0.3197 0.3129 0.0353  -0.0187 0.0389  285 GLY A O   
2218 N N   . ASN A 287 ? 0.2801 0.2814 0.2697 0.0338  -0.0145 0.0406  286 ASN A N   
2219 C CA  . ASN A 287 ? 0.2890 0.2937 0.2845 0.0389  -0.0144 0.0414  286 ASN A CA  
2220 C C   . ASN A 287 ? 0.2999 0.3090 0.3015 0.0365  -0.0176 0.0435  286 ASN A C   
2221 O O   . ASN A 287 ? 0.3108 0.3244 0.3189 0.0402  -0.0176 0.0444  286 ASN A O   
2222 C CB  . ASN A 287 ? 0.3040 0.3185 0.3069 0.0427  -0.0097 0.0412  286 ASN A CB  
2223 C CG  . ASN A 287 ? 0.3927 0.4082 0.3995 0.0493  -0.0089 0.0411  286 ASN A CG  
2224 O OD1 . ASN A 287 ? 0.4330 0.4393 0.4336 0.0527  -0.0103 0.0401  286 ASN A OD1 
2225 N ND2 . ASN A 287 ? 0.4452 0.4717 0.4622 0.0511  -0.0068 0.0422  286 ASN A ND2 
2226 N N   . ILE A 288 ? 0.2391 0.2782 0.2805 -0.0086 -0.0308 0.0262  287 ILE A N   
2227 C CA  . ILE A 288 ? 0.2633 0.2939 0.2975 -0.0092 -0.0308 0.0250  287 ILE A CA  
2228 C C   . ILE A 288 ? 0.2660 0.2891 0.2897 -0.0082 -0.0275 0.0244  287 ILE A C   
2229 O O   . ILE A 288 ? 0.2768 0.2970 0.2978 -0.0086 -0.0229 0.0217  287 ILE A O   
2230 C CB  . ILE A 288 ? 0.2670 0.2941 0.3028 -0.0114 -0.0289 0.0210  287 ILE A CB  
2231 C CG1 . ILE A 288 ? 0.2809 0.3150 0.3265 -0.0122 -0.0328 0.0219  287 ILE A CG1 
2232 C CG2 . ILE A 288 ? 0.2762 0.2939 0.3035 -0.0118 -0.0283 0.0195  287 ILE A CG2 
2233 C CD1 . ILE A 288 ? 0.3249 0.3571 0.3735 -0.0142 -0.0308 0.0181  287 ILE A CD1 
2234 N N   . THR A 289 ? 0.2860 0.3063 0.3040 -0.0068 -0.0300 0.0271  288 THR A N   
2235 C CA  . THR A 289 ? 0.3205 0.3334 0.3280 -0.0057 -0.0279 0.0271  288 THR A CA  
2236 C C   . THR A 289 ? 0.3080 0.3189 0.3116 -0.0053 -0.0231 0.0254  288 THR A C   
2237 O O   . THR A 289 ? 0.3198 0.3227 0.3164 -0.0060 -0.0191 0.0224  288 THR A O   
2238 C CB  . THR A 289 ? 0.3813 0.3851 0.3822 -0.0069 -0.0268 0.0246  288 THR A CB  
2239 O OG1 . THR A 289 ? 0.3632 0.3642 0.3654 -0.0088 -0.0230 0.0203  288 THR A OG1 
2240 C CG2 . THR A 289 ? 0.3335 0.3382 0.3368 -0.0072 -0.0319 0.0264  288 THR A CG2 
2241 N N   . PRO A 290 ? 0.2897 0.3071 0.2971 -0.0040 -0.0234 0.0274  289 PRO A N   
2242 C CA  . PRO A 290 ? 0.2676 0.2828 0.2711 -0.0035 -0.0189 0.0259  289 PRO A CA  
2243 C C   . PRO A 290 ? 0.3046 0.3138 0.2979 -0.0017 -0.0179 0.0271  289 PRO A C   
2244 O O   . PRO A 290 ? 0.3194 0.3292 0.3103 -0.0001 -0.0213 0.0304  289 PRO A O   
2245 C CB  . PRO A 290 ? 0.2886 0.3134 0.3001 -0.0025 -0.0203 0.0280  289 PRO A CB  
2246 C CG  . PRO A 290 ? 0.3046 0.3356 0.3207 -0.0013 -0.0258 0.0321  289 PRO A CG  
2247 C CD  . PRO A 290 ? 0.3336 0.3610 0.3496 -0.0029 -0.0277 0.0311  289 PRO A CD  
2248 N N   . LEU A 291 ? 0.2839 0.2873 0.2711 -0.0020 -0.0132 0.0244  290 LEU A N   
2249 C CA  . LEU A 291 ? 0.3023 0.3012 0.2807 -0.0001 -0.0117 0.0255  290 LEU A CA  
2250 C C   . LEU A 291 ? 0.3124 0.3180 0.2941 0.0017  -0.0121 0.0278  290 LEU A C   
2251 O O   . LEU A 291 ? 0.2827 0.2927 0.2704 0.0009  -0.0107 0.0264  290 LEU A O   
2252 C CB  . LEU A 291 ? 0.2895 0.2795 0.2603 -0.0014 -0.0065 0.0217  290 LEU A CB  
2253 C CG  . LEU A 291 ? 0.3908 0.3740 0.3585 -0.0033 -0.0055 0.0190  290 LEU A CG  
2254 C CD1 . LEU A 291 ? 0.3526 0.3278 0.3134 -0.0045 -0.0001 0.0153  290 LEU A CD1 
2255 C CD2 . LEU A 291 ? 0.4085 0.3884 0.3711 -0.0022 -0.0086 0.0212  290 LEU A CD2 
2256 N N   . THR A 292 ? 0.3016 0.3082 0.2794 0.0042  -0.0141 0.0312  291 THR A N   
2257 C CA  . THR A 292 ? 0.3110 0.3241 0.2916 0.0063  -0.0149 0.0337  291 THR A CA  
2258 C C   . THR A 292 ? 0.3448 0.3532 0.3157 0.0087  -0.0138 0.0352  291 THR A C   
2259 O O   . THR A 292 ? 0.3264 0.3272 0.2890 0.0088  -0.0129 0.0346  291 THR A O   
2260 C CB  . THR A 292 ? 0.3942 0.4171 0.3833 0.0075  -0.0199 0.0376  291 THR A CB  
2261 O OG1 . THR A 292 ? 0.3708 0.3925 0.3565 0.0085  -0.0233 0.0405  291 THR A OG1 
2262 C CG2 . THR A 292 ? 0.3915 0.4195 0.3906 0.0052  -0.0211 0.0362  291 THR A CG2 
2263 N N   . GLY A 293 ? 0.3456 0.3588 0.3176 0.0109  -0.0139 0.0372  292 GLY A N   
2264 C CA  . GLY A 293 ? 0.3739 0.3836 0.3372 0.0135  -0.0133 0.0390  292 GLY A CA  
2265 C C   . GLY A 293 ? 0.3557 0.3556 0.3098 0.0128  -0.0085 0.0357  292 GLY A C   
2266 O O   . GLY A 293 ? 0.3983 0.3972 0.3532 0.0117  -0.0053 0.0330  292 GLY A O   
2267 N N   . THR A 294 ? 0.3396 0.3321 0.2848 0.0133  -0.0080 0.0358  293 THR A N   
2268 C CA  . THR A 294 ? 0.3497 0.3323 0.2855 0.0125  -0.0037 0.0327  293 THR A CA  
2269 C C   . THR A 294 ? 0.3770 0.3533 0.3110 0.0097  -0.0022 0.0296  293 THR A C   
2270 O O   . THR A 294 ? 0.4351 0.4028 0.3611 0.0090  0.0012  0.0271  293 THR A O   
2271 C CB  . THR A 294 ? 0.4426 0.4208 0.3687 0.0152  -0.0038 0.0349  293 THR A CB  
2272 O OG1 . THR A 294 ? 0.4538 0.4326 0.3791 0.0160  -0.0073 0.0375  293 THR A OG1 
2273 C CG2 . THR A 294 ? 0.5175 0.5010 0.4443 0.0181  -0.0045 0.0375  293 THR A CG2 
2274 N N   . GLN A 295 ? 0.3498 0.3302 0.2910 0.0083  -0.0048 0.0298  294 GLN A N   
2275 C CA  . GLN A 295 ? 0.3401 0.3152 0.2806 0.0058  -0.0036 0.0268  294 GLN A CA  
2276 C C   . GLN A 295 ? 0.3451 0.3188 0.2882 0.0034  0.0003  0.0228  294 GLN A C   
2277 O O   . GLN A 295 ? 0.3416 0.3213 0.2914 0.0032  0.0006  0.0227  294 GLN A O   
2278 C CB  . GLN A 295 ? 0.3111 0.2916 0.2589 0.0052  -0.0079 0.0284  294 GLN A CB  
2279 C CG  . GLN A 295 ? 0.3544 0.3376 0.3010 0.0074  -0.0124 0.0327  294 GLN A CG  
2280 C CD  . GLN A 295 ? 0.3681 0.3585 0.3237 0.0069  -0.0170 0.0347  294 GLN A CD  
2281 O OE1 . GLN A 295 ? 0.3381 0.3322 0.3013 0.0050  -0.0170 0.0331  294 GLN A OE1 
2282 N NE2 . GLN A 295 ? 0.3729 0.3650 0.3273 0.0084  -0.0209 0.0383  294 GLN A NE2 
2283 N N   . GLY A 296 ? 0.3656 0.3314 0.3035 0.0015  0.0034  0.0195  295 GLY A N   
2284 C CA  . GLY A 296 ? 0.3635 0.3281 0.3041 -0.0009 0.0072  0.0158  295 GLY A CA  
2285 C C   . GLY A 296 ? 0.3834 0.3477 0.3215 -0.0001 0.0100  0.0155  295 GLY A C   
2286 O O   . GLY A 296 ? 0.3964 0.3595 0.3290 0.0021  0.0096  0.0176  295 GLY A O   
2287 N N   . GLN A 297 ? 0.3276 0.2930 0.2699 -0.0021 0.0128  0.0127  296 GLN A N   
2288 C CA  . GLN A 297 ? 0.3561 0.3208 0.2961 -0.0017 0.0155  0.0121  296 GLN A CA  
2289 C C   . GLN A 297 ? 0.3623 0.3344 0.3119 -0.0028 0.0157  0.0113  296 GLN A C   
2290 O O   . GLN A 297 ? 0.3438 0.3213 0.3017 -0.0039 0.0139  0.0111  296 GLN A O   
2291 C CB  . GLN A 297 ? 0.4473 0.4024 0.3787 -0.0032 0.0202  0.0090  296 GLN A CB  
2292 C CG  . GLN A 297 ? 0.4822 0.4337 0.4146 -0.0059 0.0222  0.0058  296 GLN A CG  
2293 C CD  . GLN A 297 ? 0.4188 0.3614 0.3431 -0.0075 0.0269  0.0029  296 GLN A CD  
2294 O OE1 . GLN A 297 ? 0.3963 0.3380 0.3232 -0.0099 0.0297  0.0000  296 GLN A OE1 
2295 N NE2 . GLN A 297 ? 0.4311 0.3671 0.3456 -0.0060 0.0277  0.0036  296 GLN A NE2 
2296 N N   . ILE A 298 ? 0.3448 0.3170 0.2929 -0.0022 0.0176  0.0111  297 ILE A N   
2297 C CA  . ILE A 298 ? 0.3418 0.3189 0.2973 -0.0036 0.0189  0.0096  297 ILE A CA  
2298 C C   . ILE A 298 ? 0.3454 0.3158 0.2974 -0.0064 0.0235  0.0057  297 ILE A C   
2299 O O   . ILE A 298 ? 0.3698 0.3341 0.3142 -0.0063 0.0264  0.0048  297 ILE A O   
2300 C CB  . ILE A 298 ? 0.3712 0.3523 0.3274 -0.0015 0.0184  0.0115  297 ILE A CB  
2301 C CG1 . ILE A 298 ? 0.4197 0.4077 0.3793 0.0013  0.0138  0.0155  297 ILE A CG1 
2302 C CG2 . ILE A 298 ? 0.3677 0.3534 0.3314 -0.0032 0.0199  0.0096  297 ILE A CG2 
2303 C CD1 . ILE A 298 ? 0.4283 0.4240 0.3981 0.0006  0.0106  0.0164  297 ILE A CD1 
2304 N N   . ARG A 299 ? 0.3400 0.3111 0.2969 -0.0088 0.0242  0.0036  298 ARG A N   
2305 C CA  . ARG A 299 ? 0.3463 0.3115 0.3004 -0.0114 0.0285  0.0000  298 ARG A CA  
2306 C C   . ARG A 299 ? 0.3870 0.3543 0.3440 -0.0125 0.0309  -0.0014 298 ARG A C   
2307 O O   . ARG A 299 ? 0.4120 0.3871 0.3776 -0.0124 0.0293  -0.0007 298 ARG A O   
2308 C CB  . ARG A 299 ? 0.3802 0.3466 0.3394 -0.0134 0.0284  -0.0018 298 ARG A CB  
2309 C CG  . ARG A 299 ? 0.3648 0.3230 0.3180 -0.0155 0.0321  -0.0048 298 ARG A CG  
2310 C CD  . ARG A 299 ? 0.3712 0.3315 0.3304 -0.0172 0.0318  -0.0064 298 ARG A CD  
2311 N NE  . ARG A 299 ? 0.3322 0.2929 0.2912 -0.0160 0.0282  -0.0046 298 ARG A NE  
2312 C CZ  . ARG A 299 ? 0.3255 0.2901 0.2912 -0.0167 0.0261  -0.0049 298 ARG A CZ  
2313 N NH1 . ARG A 299 ? 0.2934 0.2622 0.2666 -0.0186 0.0273  -0.0068 298 ARG A NH1 
2314 N NH2 . ARG A 299 ? 0.2989 0.2634 0.2638 -0.0155 0.0227  -0.0031 298 ARG A NH2 
2315 N N   . LEU A 300 ? 0.3693 0.3296 0.3192 -0.0135 0.0347  -0.0033 299 LEU A N   
2316 C CA  . LEU A 300 ? 0.4344 0.3959 0.3862 -0.0146 0.0370  -0.0045 299 LEU A CA  
2317 C C   . LEU A 300 ? 0.4474 0.4095 0.4044 -0.0178 0.0398  -0.0076 299 LEU A C   
2318 O O   . LEU A 300 ? 0.4500 0.4172 0.4135 -0.0188 0.0402  -0.0083 299 LEU A O   
2319 C CB  . LEU A 300 ? 0.4839 0.4376 0.4255 -0.0140 0.0395  -0.0048 299 LEU A CB  
2320 C CG  . LEU A 300 ? 0.5172 0.4704 0.4534 -0.0106 0.0370  -0.0017 299 LEU A CG  
2321 C CD1 . LEU A 300 ? 0.5514 0.4973 0.4780 -0.0101 0.0395  -0.0021 299 LEU A CD1 
2322 C CD2 . LEU A 300 ? 0.5851 0.5475 0.5289 -0.0086 0.0335  0.0009  299 LEU A CD2 
2323 N N   . ASN A 301 ? 0.3788 0.3361 0.3331 -0.0194 0.0415  -0.0095 300 ASN A N   
2324 C CA  . ASN A 301 ? 0.3831 0.3413 0.3423 -0.0223 0.0439  -0.0123 300 ASN A CA  
2325 C C   . ASN A 301 ? 0.4442 0.4049 0.4075 -0.0222 0.0414  -0.0120 300 ASN A C   
2326 O O   . ASN A 301 ? 0.3654 0.3212 0.3227 -0.0213 0.0408  -0.0115 300 ASN A O   
2327 C CB  . ASN A 301 ? 0.4055 0.3551 0.3572 -0.0243 0.0482  -0.0148 300 ASN A CB  
2328 C CG  . ASN A 301 ? 0.4419 0.3924 0.3984 -0.0272 0.0508  -0.0176 300 ASN A CG  
2329 O OD1 . ASN A 301 ? 0.4179 0.3727 0.3808 -0.0276 0.0492  -0.0179 300 ASN A OD1 
2330 N ND2 . ASN A 301 ? 0.6199 0.5661 0.5732 -0.0293 0.0547  -0.0197 300 ASN A ND2 
2331 N N   . CYS A 302 ? 0.3763 0.3445 0.3496 -0.0230 0.0400  -0.0122 301 CYS A N   
2332 C CA  . CYS A 302 ? 0.4184 0.3896 0.3957 -0.0224 0.0369  -0.0114 301 CYS A CA  
2333 C C   . CYS A 302 ? 0.3717 0.3369 0.3451 -0.0238 0.0388  -0.0135 301 CYS A C   
2334 O O   . CYS A 302 ? 0.3542 0.3195 0.3280 -0.0230 0.0362  -0.0127 301 CYS A O   
2335 C CB  . CYS A 302 ? 0.5661 0.5467 0.5550 -0.0229 0.0348  -0.0111 301 CYS A CB  
2336 S SG  . CYS A 302 ? 0.8320 0.8205 0.8259 -0.0205 0.0313  -0.0078 301 CYS A SG  
2337 N N   . ARG A 303 ? 0.3626 0.3223 0.3318 -0.0258 0.0431  -0.0161 302 ARG A N   
2338 C CA  . ARG A 303 ? 0.3575 0.3116 0.3230 -0.0270 0.0451  -0.0182 302 ARG A CA  
2339 C C   . ARG A 303 ? 0.3375 0.2832 0.2922 -0.0259 0.0456  -0.0176 302 ARG A C   
2340 O O   . ARG A 303 ? 0.3759 0.3172 0.3274 -0.0265 0.0465  -0.0190 302 ARG A O   
2341 C CB  . ARG A 303 ? 0.4079 0.3603 0.3741 -0.0297 0.0496  -0.0211 302 ARG A CB  
2342 C CG  . ARG A 303 ? 0.4041 0.3642 0.3809 -0.0311 0.0494  -0.0221 302 ARG A CG  
2343 C CD  . ARG A 303 ? 0.5051 0.4641 0.4828 -0.0337 0.0539  -0.0247 302 ARG A CD  
2344 N NE  . ARG A 303 ? 0.4646 0.4316 0.4527 -0.0349 0.0534  -0.0254 302 ARG A NE  
2345 C CZ  . ARG A 303 ? 0.5014 0.4710 0.4949 -0.0359 0.0534  -0.0267 302 ARG A CZ  
2346 N NH1 . ARG A 303 ? 0.4977 0.4627 0.4872 -0.0360 0.0540  -0.0277 302 ARG A NH1 
2347 N NH2 . ARG A 303 ? 0.4662 0.4434 0.4693 -0.0368 0.0528  -0.0271 302 ARG A NH2 
2348 N N   . VAL A 304 ? 0.3216 0.2650 0.2707 -0.0242 0.0449  -0.0158 303 VAL A N   
2349 C CA  . VAL A 304 ? 0.3714 0.3065 0.3099 -0.0233 0.0458  -0.0155 303 VAL A CA  
2350 C C   . VAL A 304 ? 0.3470 0.2829 0.2825 -0.0205 0.0425  -0.0124 303 VAL A C   
2351 O O   . VAL A 304 ? 0.3456 0.2872 0.2854 -0.0195 0.0408  -0.0107 303 VAL A O   
2352 C CB  . VAL A 304 ? 0.4315 0.3599 0.3632 -0.0248 0.0505  -0.0175 303 VAL A CB  
2353 C CG1 . VAL A 304 ? 0.4980 0.4263 0.4332 -0.0276 0.0538  -0.0205 303 VAL A CG1 
2354 C CG2 . VAL A 304 ? 0.4228 0.3529 0.3544 -0.0244 0.0510  -0.0166 303 VAL A CG2 
2355 N N   . VAL A 305 ? 0.3956 0.3260 0.3237 -0.0192 0.0417  -0.0115 304 VAL A N   
2356 C CA  . VAL A 305 ? 0.3802 0.3102 0.3039 -0.0165 0.0390  -0.0085 304 VAL A CA  
2357 C C   . VAL A 305 ? 0.4123 0.3384 0.3297 -0.0161 0.0414  -0.0085 304 VAL A C   
2358 O O   . VAL A 305 ? 0.3987 0.3194 0.3118 -0.0178 0.0453  -0.0108 304 VAL A O   
2359 C CB  . VAL A 305 ? 0.4773 0.4018 0.3945 -0.0154 0.0376  -0.0078 304 VAL A CB  
2360 C CG1 . VAL A 305 ? 0.5425 0.4648 0.4531 -0.0128 0.0359  -0.0051 304 VAL A CG1 
2361 C CG2 . VAL A 305 ? 0.4086 0.3380 0.3327 -0.0154 0.0342  -0.0071 304 VAL A CG2 
2362 N N   . ASN A 306 ? 0.3692 0.2981 0.2860 -0.0137 0.0390  -0.0058 305 ASN A N   
2363 C CA  . ASN A 306 ? 0.3919 0.3173 0.3026 -0.0130 0.0409  -0.0055 305 ASN A CA  
2364 C C   . ASN A 306 ? 0.4887 0.4042 0.3880 -0.0128 0.0432  -0.0063 305 ASN A C   
2365 O O   . ASN A 306 ? 0.4732 0.3855 0.3686 -0.0120 0.0420  -0.0056 305 ASN A O   
2366 C CB  . ASN A 306 ? 0.4243 0.3546 0.3361 -0.0101 0.0376  -0.0022 305 ASN A CB  
2367 C CG  . ASN A 306 ? 0.3986 0.3388 0.3215 -0.0100 0.0353  -0.0013 305 ASN A CG  
2368 O OD1 . ASN A 306 ? 0.3678 0.3111 0.2973 -0.0123 0.0367  -0.0034 305 ASN A OD1 
2369 N ND2 . ASN A 306 ? 0.4123 0.3577 0.3373 -0.0074 0.0317  0.0018  305 ASN A ND2 
2370 N N   . SER A 307 ? 0.5102 0.4209 0.4040 -0.0135 0.0465  -0.0075 306 SER A N   
2371 C CA  . SER A 307 ? 0.6161 0.5172 0.4987 -0.0134 0.0488  -0.0082 306 SER A CA  
2372 C C   . SER A 307 ? 0.6010 0.4986 0.4776 -0.0127 0.0505  -0.0079 306 SER A C   
2373 O O   . SER A 307 ? 0.6444 0.5467 0.5254 -0.0125 0.0500  -0.0074 306 SER A O   
2374 C CB  . SER A 307 ? 0.6586 0.5547 0.5397 -0.0163 0.0524  -0.0113 306 SER A CB  
2375 O OG  . SER A 307 ? 0.7908 0.6904 0.6783 -0.0186 0.0545  -0.0132 306 SER A OG  
# 
