data_9EDV
# 
_entry.id   9EDV 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.400 
_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   9EDV         pdb_00009edv 10.2210/pdb9edv/pdb 
WWPDB D_1000290027 ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2025-01-08 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9EDV 
_pdbx_database_status.recvd_initial_deposition_date   2024-11-18 
_pdbx_database_status.SG_entry                        Y 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_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           N 
# 
_pdbx_database_related.db_name        TargetTrack 
_pdbx_database_related.db_id          IDP97431 
_pdbx_database_related.content_type   unspecified 
_pdbx_database_related.details        . 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              alexei.savchenko@ucalgary.ca 
_pdbx_contact_author.name_first         Alexei 
_pdbx_contact_author.name_last          Savchenko 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-5256-9237 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Stogios, P.J.'                                                1 ? 
'Whitesell, L.'                                                2 ? 
'Cowen, L.E.'                                                  3 ? 
'Savchenko, A.'                                                4 ? 
'Joachimiak, A.'                                               5 ? 
'Satchell, K.J.F.'                                             6 ? 
'Center for Structural Biology of Infectious Diseases (CSBID)' 7 ? 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   ? 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'To Be Published' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            0353 
_citation.journal_id_ISSN           ? 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     
;Crystal structure of Yck2 from Candida albicans in complex with inhibitor 1e: 2-(4-fluorophenyl)-3-(pyridin-4-yl)imidazo[1,2-a]pyridine-7-carbonitrile
;
_citation.year                      ? 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      ? 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
_citation_author.citation_id        primary 
_citation_author.name               'Stogios, P.J.' 
_citation_author.ordinal            1 
_citation_author.identifier_ORCID   ? 
# 
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 'non-specific serine/threonine protein kinase'                             35397.254 1 2.7.11.1 ? ? ? 
2 non-polymer syn '2-(4-fluorophenyl)-3-(pyridin-4-yl)imidazo[1,2-a]pyridine-7-carbonitrile' 314.316   1 ?        ? ? ? 
3 non-polymer syn 'CHLORIDE ION'                                                             35.453    1 ?        ? ? ? 
# 
_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       
;SSVVGLHYKIGKKIGEGSFGVIFEGTNIINGVPVAIKFEPRKTEAPQLRDEYRTYKHLQGCDGIPNAYYFGQEGLHNILV
IDLLGPSLEDLFDWCGRRFSVKTVVQVAIQMLTLVEEVHRHDLIYRDIKPDNFLIGRRGATDENNVHLIDFGMAKQYRDP
RTKQHIPYREKKSLSGTARYMSINTHLGREQSRRDDLEALGHVFFYFLRGQLPWQGLKAPTNKQKYEKIGDKKRTTPAVT
LCDGLPQQFAEYLDSVRSLPFDAEPPYEEYRMLLLSVLDDLGQACDGDMDWMHLNGGRGWDATINKKPN
;
_entity_poly.pdbx_seq_one_letter_code_can   
;SSVVGLHYKIGKKIGEGSFGVIFEGTNIINGVPVAIKFEPRKTEAPQLRDEYRTYKHLQGCDGIPNAYYFGQEGLHNILV
IDLLGPSLEDLFDWCGRRFSVKTVVQVAIQMLTLVEEVHRHDLIYRDIKPDNFLIGRRGATDENNVHLIDFGMAKQYRDP
RTKQHIPYREKKSLSGTARYMSINTHLGREQSRRDDLEALGHVFFYFLRGQLPWQGLKAPTNKQKYEKIGDKKRTTPAVT
LCDGLPQQFAEYLDSVRSLPFDAEPPYEEYRMLLLSVLDDLGQACDGDMDWMHLNGGRGWDATINKKPN
;
_entity_poly.pdbx_strand_id                 A 
_entity_poly.pdbx_target_identifier         IDP97431 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 '2-(4-fluorophenyl)-3-(pyridin-4-yl)imidazo[1,2-a]pyridine-7-carbonitrile' A1BIQ 
3 'CHLORIDE ION'                                                             CL    
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   SER n 
1 2   SER n 
1 3   VAL n 
1 4   VAL n 
1 5   GLY n 
1 6   LEU n 
1 7   HIS n 
1 8   TYR n 
1 9   LYS n 
1 10  ILE n 
1 11  GLY n 
1 12  LYS n 
1 13  LYS n 
1 14  ILE n 
1 15  GLY n 
1 16  GLU n 
1 17  GLY n 
1 18  SER n 
1 19  PHE n 
1 20  GLY n 
1 21  VAL n 
1 22  ILE n 
1 23  PHE n 
1 24  GLU n 
1 25  GLY n 
1 26  THR n 
1 27  ASN n 
1 28  ILE n 
1 29  ILE n 
1 30  ASN n 
1 31  GLY n 
1 32  VAL n 
1 33  PRO n 
1 34  VAL n 
1 35  ALA n 
1 36  ILE n 
1 37  LYS n 
1 38  PHE n 
1 39  GLU n 
1 40  PRO n 
1 41  ARG n 
1 42  LYS n 
1 43  THR n 
1 44  GLU n 
1 45  ALA n 
1 46  PRO n 
1 47  GLN n 
1 48  LEU n 
1 49  ARG n 
1 50  ASP n 
1 51  GLU n 
1 52  TYR n 
1 53  ARG n 
1 54  THR n 
1 55  TYR n 
1 56  LYS n 
1 57  HIS n 
1 58  LEU n 
1 59  GLN n 
1 60  GLY n 
1 61  CYS n 
1 62  ASP n 
1 63  GLY n 
1 64  ILE n 
1 65  PRO n 
1 66  ASN n 
1 67  ALA n 
1 68  TYR n 
1 69  TYR n 
1 70  PHE n 
1 71  GLY n 
1 72  GLN n 
1 73  GLU n 
1 74  GLY n 
1 75  LEU n 
1 76  HIS n 
1 77  ASN n 
1 78  ILE n 
1 79  LEU n 
1 80  VAL n 
1 81  ILE n 
1 82  ASP n 
1 83  LEU n 
1 84  LEU n 
1 85  GLY n 
1 86  PRO n 
1 87  SER n 
1 88  LEU n 
1 89  GLU n 
1 90  ASP n 
1 91  LEU n 
1 92  PHE n 
1 93  ASP n 
1 94  TRP n 
1 95  CYS n 
1 96  GLY n 
1 97  ARG n 
1 98  ARG n 
1 99  PHE n 
1 100 SER n 
1 101 VAL n 
1 102 LYS n 
1 103 THR n 
1 104 VAL n 
1 105 VAL n 
1 106 GLN n 
1 107 VAL n 
1 108 ALA n 
1 109 ILE n 
1 110 GLN n 
1 111 MET n 
1 112 LEU n 
1 113 THR n 
1 114 LEU n 
1 115 VAL n 
1 116 GLU n 
1 117 GLU n 
1 118 VAL n 
1 119 HIS n 
1 120 ARG n 
1 121 HIS n 
1 122 ASP n 
1 123 LEU n 
1 124 ILE n 
1 125 TYR n 
1 126 ARG n 
1 127 ASP n 
1 128 ILE n 
1 129 LYS n 
1 130 PRO n 
1 131 ASP n 
1 132 ASN n 
1 133 PHE n 
1 134 LEU n 
1 135 ILE n 
1 136 GLY n 
1 137 ARG n 
1 138 ARG n 
1 139 GLY n 
1 140 ALA n 
1 141 THR n 
1 142 ASP n 
1 143 GLU n 
1 144 ASN n 
1 145 ASN n 
1 146 VAL n 
1 147 HIS n 
1 148 LEU n 
1 149 ILE n 
1 150 ASP n 
1 151 PHE n 
1 152 GLY n 
1 153 MET n 
1 154 ALA n 
1 155 LYS n 
1 156 GLN n 
1 157 TYR n 
1 158 ARG n 
1 159 ASP n 
1 160 PRO n 
1 161 ARG n 
1 162 THR n 
1 163 LYS n 
1 164 GLN n 
1 165 HIS n 
1 166 ILE n 
1 167 PRO n 
1 168 TYR n 
1 169 ARG n 
1 170 GLU n 
1 171 LYS n 
1 172 LYS n 
1 173 SER n 
1 174 LEU n 
1 175 SER n 
1 176 GLY n 
1 177 THR n 
1 178 ALA n 
1 179 ARG n 
1 180 TYR n 
1 181 MET n 
1 182 SER n 
1 183 ILE n 
1 184 ASN n 
1 185 THR n 
1 186 HIS n 
1 187 LEU n 
1 188 GLY n 
1 189 ARG n 
1 190 GLU n 
1 191 GLN n 
1 192 SER n 
1 193 ARG n 
1 194 ARG n 
1 195 ASP n 
1 196 ASP n 
1 197 LEU n 
1 198 GLU n 
1 199 ALA n 
1 200 LEU n 
1 201 GLY n 
1 202 HIS n 
1 203 VAL n 
1 204 PHE n 
1 205 PHE n 
1 206 TYR n 
1 207 PHE n 
1 208 LEU n 
1 209 ARG n 
1 210 GLY n 
1 211 GLN n 
1 212 LEU n 
1 213 PRO n 
1 214 TRP n 
1 215 GLN n 
1 216 GLY n 
1 217 LEU n 
1 218 LYS n 
1 219 ALA n 
1 220 PRO n 
1 221 THR n 
1 222 ASN n 
1 223 LYS n 
1 224 GLN n 
1 225 LYS n 
1 226 TYR n 
1 227 GLU n 
1 228 LYS n 
1 229 ILE n 
1 230 GLY n 
1 231 ASP n 
1 232 LYS n 
1 233 LYS n 
1 234 ARG n 
1 235 THR n 
1 236 THR n 
1 237 PRO n 
1 238 ALA n 
1 239 VAL n 
1 240 THR n 
1 241 LEU n 
1 242 CYS n 
1 243 ASP n 
1 244 GLY n 
1 245 LEU n 
1 246 PRO n 
1 247 GLN n 
1 248 GLN n 
1 249 PHE n 
1 250 ALA n 
1 251 GLU n 
1 252 TYR n 
1 253 LEU n 
1 254 ASP n 
1 255 SER n 
1 256 VAL n 
1 257 ARG n 
1 258 SER n 
1 259 LEU n 
1 260 PRO n 
1 261 PHE n 
1 262 ASP n 
1 263 ALA n 
1 264 GLU n 
1 265 PRO n 
1 266 PRO n 
1 267 TYR n 
1 268 GLU n 
1 269 GLU n 
1 270 TYR n 
1 271 ARG n 
1 272 MET n 
1 273 LEU n 
1 274 LEU n 
1 275 LEU n 
1 276 SER n 
1 277 VAL n 
1 278 LEU n 
1 279 ASP n 
1 280 ASP n 
1 281 LEU n 
1 282 GLY n 
1 283 GLN n 
1 284 ALA n 
1 285 CYS n 
1 286 ASP n 
1 287 GLY n 
1 288 ASP n 
1 289 MET n 
1 290 ASP n 
1 291 TRP n 
1 292 MET n 
1 293 HIS n 
1 294 LEU n 
1 295 ASN n 
1 296 GLY n 
1 297 GLY n 
1 298 ARG n 
1 299 GLY n 
1 300 TRP n 
1 301 ASP n 
1 302 ALA n 
1 303 THR n 
1 304 ILE n 
1 305 ASN n 
1 306 LYS n 
1 307 LYS n 
1 308 PRO n 
1 309 ASN 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                 FOB64_000203 
_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      'Candida albicans' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     5476 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     562 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               LOBSTR 
_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          plasmid 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       pMCSG53 
_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 
A1BIQ non-polymer         . '2-(4-fluorophenyl)-3-(pyridin-4-yl)imidazo[1,2-a]pyridine-7-carbonitrile' ? 'C19 H11 F N4'   314.316 
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 
CL    non-polymer         . 'CHLORIDE ION'                                                             ? 'Cl -1'          35.453  
CYS   'L-peptide linking' y CYSTEINE                                                                   ? 'C3 H7 N O2 S'   121.158 
GLN   'L-peptide linking' y GLUTAMINE                                                                  ? 'C5 H10 N2 O3'   146.144 
GLU   'L-peptide linking' y 'GLUTAMIC ACID'                                                            ? 'C5 H9 N O4'     147.129 
GLY   'peptide linking'   y GLYCINE                                                                    ? 'C2 H5 N O2'     75.067  
HIS   'L-peptide linking' y HISTIDINE                                                                  ? 'C6 H10 N3 O2 1' 156.162 
ILE   'L-peptide linking' y ISOLEUCINE                                                                 ? 'C6 H13 N O2'    131.173 
LEU   'L-peptide linking' y LEUCINE                                                                    ? 'C6 H13 N O2'    131.173 
LYS   'L-peptide linking' y LYSINE                                                                     ? 'C6 H15 N2 O2 1' 147.195 
MET   'L-peptide linking' y METHIONINE                                                                 ? 'C5 H11 N O2 S'  149.211 
PHE   'L-peptide linking' y PHENYLALANINE                                                              ? 'C9 H11 N O2'    165.189 
PRO   'L-peptide linking' y PROLINE                                                                    ? 'C5 H9 N O2'     115.130 
SER   'L-peptide linking' y SERINE                                                                     ? 'C3 H7 N O3'     105.093 
THR   'L-peptide linking' y THREONINE                                                                  ? 'C4 H9 N O3'     119.119 
TRP   'L-peptide linking' y TRYPTOPHAN                                                                 ? 'C11 H12 N2 O2'  204.225 
TYR   'L-peptide linking' y TYROSINE                                                                   ? 'C9 H11 N O3'    181.189 
VAL   'L-peptide linking' y VALINE                                                                     ? 'C5 H11 N O2'    117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   SER 1   37  37  SER SER A . n 
A 1 2   SER 2   38  38  SER SER A . n 
A 1 3   VAL 3   39  39  VAL VAL A . n 
A 1 4   VAL 4   40  40  VAL VAL A . n 
A 1 5   GLY 5   41  41  GLY GLY A . n 
A 1 6   LEU 6   42  42  LEU LEU A . n 
A 1 7   HIS 7   43  43  HIS HIS A . n 
A 1 8   TYR 8   44  44  TYR TYR A . n 
A 1 9   LYS 9   45  45  LYS LYS A . n 
A 1 10  ILE 10  46  46  ILE ILE A . n 
A 1 11  GLY 11  47  47  GLY GLY A . n 
A 1 12  LYS 12  48  48  LYS LYS A . n 
A 1 13  LYS 13  49  49  LYS LYS A . n 
A 1 14  ILE 14  50  50  ILE ILE A . n 
A 1 15  GLY 15  51  51  GLY GLY A . n 
A 1 16  GLU 16  52  52  GLU GLU A . n 
A 1 17  GLY 17  53  53  GLY GLY A . n 
A 1 18  SER 18  54  54  SER SER A . n 
A 1 19  PHE 19  55  55  PHE PHE A . n 
A 1 20  GLY 20  56  56  GLY GLY A . n 
A 1 21  VAL 21  57  57  VAL VAL A . n 
A 1 22  ILE 22  58  58  ILE ILE A . n 
A 1 23  PHE 23  59  59  PHE PHE A . n 
A 1 24  GLU 24  60  60  GLU GLU A . n 
A 1 25  GLY 25  61  61  GLY GLY A . n 
A 1 26  THR 26  62  62  THR THR A . n 
A 1 27  ASN 27  63  63  ASN ASN A . n 
A 1 28  ILE 28  64  64  ILE ILE A . n 
A 1 29  ILE 29  65  65  ILE ILE A . n 
A 1 30  ASN 30  66  66  ASN ASN A . n 
A 1 31  GLY 31  67  67  GLY GLY A . n 
A 1 32  VAL 32  68  68  VAL VAL A . n 
A 1 33  PRO 33  69  69  PRO PRO A . n 
A 1 34  VAL 34  70  70  VAL VAL A . n 
A 1 35  ALA 35  71  71  ALA ALA A . n 
A 1 36  ILE 36  72  72  ILE ILE A . n 
A 1 37  LYS 37  73  73  LYS LYS A . n 
A 1 38  PHE 38  74  74  PHE PHE A . n 
A 1 39  GLU 39  75  75  GLU GLU A . n 
A 1 40  PRO 40  76  76  PRO PRO A . n 
A 1 41  ARG 41  77  77  ARG ARG A . n 
A 1 42  LYS 42  78  78  LYS LYS A . n 
A 1 43  THR 43  79  79  THR THR A . n 
A 1 44  GLU 44  80  80  GLU GLU A . n 
A 1 45  ALA 45  81  81  ALA ALA A . n 
A 1 46  PRO 46  82  82  PRO PRO A . n 
A 1 47  GLN 47  83  83  GLN GLN A . n 
A 1 48  LEU 48  84  84  LEU LEU A . n 
A 1 49  ARG 49  85  85  ARG ARG A . n 
A 1 50  ASP 50  86  86  ASP ASP A . n 
A 1 51  GLU 51  87  87  GLU GLU A . n 
A 1 52  TYR 52  88  88  TYR TYR A . n 
A 1 53  ARG 53  89  89  ARG ARG A . n 
A 1 54  THR 54  90  90  THR THR A . n 
A 1 55  TYR 55  91  91  TYR TYR A . n 
A 1 56  LYS 56  92  92  LYS LYS A . n 
A 1 57  HIS 57  93  93  HIS HIS A . n 
A 1 58  LEU 58  94  94  LEU LEU A . n 
A 1 59  GLN 59  95  95  GLN GLN A . n 
A 1 60  GLY 60  96  96  GLY GLY A . n 
A 1 61  CYS 61  97  97  CYS CYS A . n 
A 1 62  ASP 62  98  98  ASP ASP A . n 
A 1 63  GLY 63  99  99  GLY GLY A . n 
A 1 64  ILE 64  100 100 ILE ILE A . n 
A 1 65  PRO 65  101 101 PRO PRO A . n 
A 1 66  ASN 66  102 102 ASN ASN A . n 
A 1 67  ALA 67  103 103 ALA ALA A . n 
A 1 68  TYR 68  104 104 TYR TYR A . n 
A 1 69  TYR 69  105 105 TYR TYR A . n 
A 1 70  PHE 70  106 106 PHE PHE A . n 
A 1 71  GLY 71  107 107 GLY GLY A . n 
A 1 72  GLN 72  108 108 GLN GLN A . n 
A 1 73  GLU 73  109 109 GLU GLU A . n 
A 1 74  GLY 74  110 110 GLY GLY A . n 
A 1 75  LEU 75  111 111 LEU LEU A . n 
A 1 76  HIS 76  112 112 HIS HIS A . n 
A 1 77  ASN 77  113 113 ASN ASN A . n 
A 1 78  ILE 78  114 114 ILE ILE A . n 
A 1 79  LEU 79  115 115 LEU LEU A . n 
A 1 80  VAL 80  116 116 VAL VAL A . n 
A 1 81  ILE 81  117 117 ILE ILE A . n 
A 1 82  ASP 82  118 118 ASP ASP A . n 
A 1 83  LEU 83  119 119 LEU LEU A . n 
A 1 84  LEU 84  120 120 LEU LEU A . n 
A 1 85  GLY 85  121 121 GLY GLY A . n 
A 1 86  PRO 86  122 122 PRO PRO A . n 
A 1 87  SER 87  123 123 SER SER A . n 
A 1 88  LEU 88  124 124 LEU LEU A . n 
A 1 89  GLU 89  125 125 GLU GLU A . n 
A 1 90  ASP 90  126 126 ASP ASP A . n 
A 1 91  LEU 91  127 127 LEU LEU A . n 
A 1 92  PHE 92  128 128 PHE PHE A . n 
A 1 93  ASP 93  129 129 ASP ASP A . n 
A 1 94  TRP 94  130 130 TRP TRP A . n 
A 1 95  CYS 95  131 131 CYS CYS A . n 
A 1 96  GLY 96  132 132 GLY GLY A . n 
A 1 97  ARG 97  133 133 ARG ARG A . n 
A 1 98  ARG 98  134 134 ARG ARG A . n 
A 1 99  PHE 99  135 135 PHE PHE A . n 
A 1 100 SER 100 136 136 SER SER A . n 
A 1 101 VAL 101 137 137 VAL VAL A . n 
A 1 102 LYS 102 138 138 LYS LYS A . n 
A 1 103 THR 103 139 139 THR THR A . n 
A 1 104 VAL 104 140 140 VAL VAL A . n 
A 1 105 VAL 105 141 141 VAL VAL A . n 
A 1 106 GLN 106 142 142 GLN GLN A . n 
A 1 107 VAL 107 143 143 VAL VAL A . n 
A 1 108 ALA 108 144 144 ALA ALA A . n 
A 1 109 ILE 109 145 145 ILE ILE A . n 
A 1 110 GLN 110 146 146 GLN GLN A . n 
A 1 111 MET 111 147 147 MET MET A . n 
A 1 112 LEU 112 148 148 LEU LEU A . n 
A 1 113 THR 113 149 149 THR THR A . n 
A 1 114 LEU 114 150 150 LEU LEU A . n 
A 1 115 VAL 115 151 151 VAL VAL A . n 
A 1 116 GLU 116 152 152 GLU GLU A . n 
A 1 117 GLU 117 153 153 GLU GLU A . n 
A 1 118 VAL 118 154 154 VAL VAL A . n 
A 1 119 HIS 119 155 155 HIS HIS A . n 
A 1 120 ARG 120 156 156 ARG ARG A . n 
A 1 121 HIS 121 157 157 HIS HIS A . n 
A 1 122 ASP 122 158 158 ASP ASP A . n 
A 1 123 LEU 123 159 159 LEU LEU A . n 
A 1 124 ILE 124 160 160 ILE ILE A . n 
A 1 125 TYR 125 161 161 TYR TYR A . n 
A 1 126 ARG 126 162 162 ARG ARG A . n 
A 1 127 ASP 127 163 163 ASP ASP A . n 
A 1 128 ILE 128 164 164 ILE ILE A . n 
A 1 129 LYS 129 165 165 LYS LYS A . n 
A 1 130 PRO 130 166 166 PRO PRO A . n 
A 1 131 ASP 131 167 167 ASP ASP A . n 
A 1 132 ASN 132 168 168 ASN ASN A . n 
A 1 133 PHE 133 169 169 PHE PHE A . n 
A 1 134 LEU 134 170 170 LEU LEU A . n 
A 1 135 ILE 135 171 171 ILE ILE A . n 
A 1 136 GLY 136 172 172 GLY GLY A . n 
A 1 137 ARG 137 173 173 ARG ARG A . n 
A 1 138 ARG 138 174 174 ARG ARG A . n 
A 1 139 GLY 139 175 175 GLY GLY A . n 
A 1 140 ALA 140 176 176 ALA ALA A . n 
A 1 141 THR 141 177 177 THR THR A . n 
A 1 142 ASP 142 178 178 ASP ASP A . n 
A 1 143 GLU 143 179 179 GLU GLU A . n 
A 1 144 ASN 144 180 180 ASN ASN A . n 
A 1 145 ASN 145 181 181 ASN ASN A . n 
A 1 146 VAL 146 182 182 VAL VAL A . n 
A 1 147 HIS 147 183 183 HIS HIS A . n 
A 1 148 LEU 148 184 184 LEU LEU A . n 
A 1 149 ILE 149 185 185 ILE ILE A . n 
A 1 150 ASP 150 186 186 ASP ASP A . n 
A 1 151 PHE 151 187 187 PHE PHE A . n 
A 1 152 GLY 152 188 188 GLY GLY A . n 
A 1 153 MET 153 189 189 MET MET A . n 
A 1 154 ALA 154 190 190 ALA ALA A . n 
A 1 155 LYS 155 191 191 LYS LYS A . n 
A 1 156 GLN 156 192 192 GLN GLN A . n 
A 1 157 TYR 157 193 193 TYR TYR A . n 
A 1 158 ARG 158 194 194 ARG ARG A . n 
A 1 159 ASP 159 195 195 ASP ASP A . n 
A 1 160 PRO 160 196 196 PRO PRO A . n 
A 1 161 ARG 161 197 197 ARG ARG A . n 
A 1 162 THR 162 198 198 THR THR A . n 
A 1 163 LYS 163 199 199 LYS LYS A . n 
A 1 164 GLN 164 200 200 GLN GLN A . n 
A 1 165 HIS 165 201 201 HIS HIS A . n 
A 1 166 ILE 166 202 202 ILE ILE A . n 
A 1 167 PRO 167 203 203 PRO PRO A . n 
A 1 168 TYR 168 204 204 TYR TYR A . n 
A 1 169 ARG 169 205 205 ARG ARG A . n 
A 1 170 GLU 170 206 206 GLU GLU A . n 
A 1 171 LYS 171 207 207 LYS LYS A . n 
A 1 172 LYS 172 208 208 LYS LYS A . n 
A 1 173 SER 173 209 209 SER SER A . n 
A 1 174 LEU 174 210 210 LEU LEU A . n 
A 1 175 SER 175 211 211 SER SER A . n 
A 1 176 GLY 176 212 212 GLY GLY A . n 
A 1 177 THR 177 213 213 THR THR A . n 
A 1 178 ALA 178 214 214 ALA ALA A . n 
A 1 179 ARG 179 215 215 ARG ARG A . n 
A 1 180 TYR 180 216 216 TYR TYR A . n 
A 1 181 MET 181 217 217 MET MET A . n 
A 1 182 SER 182 218 218 SER SER A . n 
A 1 183 ILE 183 219 219 ILE ILE A . n 
A 1 184 ASN 184 220 220 ASN ASN A . n 
A 1 185 THR 185 221 221 THR THR A . n 
A 1 186 HIS 186 222 222 HIS HIS A . n 
A 1 187 LEU 187 223 223 LEU LEU A . n 
A 1 188 GLY 188 224 224 GLY GLY A . n 
A 1 189 ARG 189 225 225 ARG ARG A . n 
A 1 190 GLU 190 226 226 GLU GLU A . n 
A 1 191 GLN 191 227 227 GLN GLN A . n 
A 1 192 SER 192 228 228 SER SER A . n 
A 1 193 ARG 193 229 229 ARG ARG A . n 
A 1 194 ARG 194 230 230 ARG ARG A . n 
A 1 195 ASP 195 231 231 ASP ASP A . n 
A 1 196 ASP 196 232 232 ASP ASP A . n 
A 1 197 LEU 197 233 233 LEU LEU A . n 
A 1 198 GLU 198 234 234 GLU GLU A . n 
A 1 199 ALA 199 235 235 ALA ALA A . n 
A 1 200 LEU 200 236 236 LEU LEU A . n 
A 1 201 GLY 201 237 237 GLY GLY A . n 
A 1 202 HIS 202 238 238 HIS HIS A . n 
A 1 203 VAL 203 239 239 VAL VAL A . n 
A 1 204 PHE 204 240 240 PHE PHE A . n 
A 1 205 PHE 205 241 241 PHE PHE A . n 
A 1 206 TYR 206 242 242 TYR TYR A . n 
A 1 207 PHE 207 243 243 PHE PHE A . n 
A 1 208 LEU 208 244 244 LEU LEU A . n 
A 1 209 ARG 209 245 245 ARG ARG A . n 
A 1 210 GLY 210 246 246 GLY GLY A . n 
A 1 211 GLN 211 247 247 GLN GLN A . n 
A 1 212 LEU 212 248 248 LEU LEU A . n 
A 1 213 PRO 213 249 249 PRO PRO A . n 
A 1 214 TRP 214 250 250 TRP TRP A . n 
A 1 215 GLN 215 251 251 GLN GLN A . n 
A 1 216 GLY 216 252 252 GLY GLY A . n 
A 1 217 LEU 217 253 253 LEU LEU A . n 
A 1 218 LYS 218 254 254 LYS LYS A . n 
A 1 219 ALA 219 255 255 ALA ALA A . n 
A 1 220 PRO 220 256 256 PRO PRO A . n 
A 1 221 THR 221 257 257 THR THR A . n 
A 1 222 ASN 222 258 258 ASN ASN A . n 
A 1 223 LYS 223 259 259 LYS LYS A . n 
A 1 224 GLN 224 260 260 GLN GLN A . n 
A 1 225 LYS 225 261 261 LYS LYS A . n 
A 1 226 TYR 226 262 262 TYR TYR A . n 
A 1 227 GLU 227 263 263 GLU GLU A . n 
A 1 228 LYS 228 264 264 LYS LYS A . n 
A 1 229 ILE 229 265 265 ILE ILE A . n 
A 1 230 GLY 230 266 266 GLY GLY A . n 
A 1 231 ASP 231 267 267 ASP ASP A . n 
A 1 232 LYS 232 268 268 LYS LYS A . n 
A 1 233 LYS 233 269 269 LYS LYS A . n 
A 1 234 ARG 234 270 270 ARG ARG A . n 
A 1 235 THR 235 271 271 THR THR A . n 
A 1 236 THR 236 272 272 THR THR A . n 
A 1 237 PRO 237 273 273 PRO PRO A . n 
A 1 238 ALA 238 274 274 ALA ALA A . n 
A 1 239 VAL 239 275 275 VAL VAL A . n 
A 1 240 THR 240 276 276 THR THR A . n 
A 1 241 LEU 241 277 277 LEU LEU A . n 
A 1 242 CYS 242 278 278 CYS CYS A . n 
A 1 243 ASP 243 279 279 ASP ASP A . n 
A 1 244 GLY 244 280 280 GLY GLY A . n 
A 1 245 LEU 245 281 281 LEU LEU A . n 
A 1 246 PRO 246 282 282 PRO PRO A . n 
A 1 247 GLN 247 283 283 GLN GLN A . n 
A 1 248 GLN 248 284 284 GLN GLN A . n 
A 1 249 PHE 249 285 285 PHE PHE A . n 
A 1 250 ALA 250 286 286 ALA ALA A . n 
A 1 251 GLU 251 287 287 GLU GLU A . n 
A 1 252 TYR 252 288 288 TYR TYR A . n 
A 1 253 LEU 253 289 289 LEU LEU A . n 
A 1 254 ASP 254 290 290 ASP ASP A . n 
A 1 255 SER 255 291 291 SER SER A . n 
A 1 256 VAL 256 292 292 VAL VAL A . n 
A 1 257 ARG 257 293 293 ARG ARG A . n 
A 1 258 SER 258 294 294 SER SER A . n 
A 1 259 LEU 259 295 295 LEU LEU A . n 
A 1 260 PRO 260 296 296 PRO PRO A . n 
A 1 261 PHE 261 297 297 PHE PHE A . n 
A 1 262 ASP 262 298 298 ASP ASP A . n 
A 1 263 ALA 263 299 299 ALA ALA A . n 
A 1 264 GLU 264 300 300 GLU GLU A . n 
A 1 265 PRO 265 301 301 PRO PRO A . n 
A 1 266 PRO 266 302 302 PRO PRO A . n 
A 1 267 TYR 267 303 303 TYR TYR A . n 
A 1 268 GLU 268 304 304 GLU GLU A . n 
A 1 269 GLU 269 305 305 GLU GLU A . n 
A 1 270 TYR 270 306 306 TYR TYR A . n 
A 1 271 ARG 271 307 307 ARG ARG A . n 
A 1 272 MET 272 308 308 MET MET A . n 
A 1 273 LEU 273 309 309 LEU LEU A . n 
A 1 274 LEU 274 310 310 LEU LEU A . n 
A 1 275 LEU 275 311 311 LEU LEU A . n 
A 1 276 SER 276 312 312 SER SER A . n 
A 1 277 VAL 277 313 313 VAL VAL A . n 
A 1 278 LEU 278 314 314 LEU LEU A . n 
A 1 279 ASP 279 315 315 ASP ASP A . n 
A 1 280 ASP 280 316 316 ASP ASP A . n 
A 1 281 LEU 281 317 317 LEU LEU A . n 
A 1 282 GLY 282 318 318 GLY GLY A . n 
A 1 283 GLN 283 319 319 GLN GLN A . n 
A 1 284 ALA 284 320 320 ALA ALA A . n 
A 1 285 CYS 285 321 321 CYS CYS A . n 
A 1 286 ASP 286 322 322 ASP ASP A . n 
A 1 287 GLY 287 323 323 GLY GLY A . n 
A 1 288 ASP 288 324 324 ASP ASP A . n 
A 1 289 MET 289 325 325 MET MET A . n 
A 1 290 ASP 290 326 326 ASP ASP A . n 
A 1 291 TRP 291 327 327 TRP TRP A . n 
A 1 292 MET 292 328 328 MET MET A . n 
A 1 293 HIS 293 329 329 HIS HIS A . n 
A 1 294 LEU 294 330 330 LEU LEU A . n 
A 1 295 ASN 295 331 331 ASN ASN A . n 
A 1 296 GLY 296 332 332 GLY GLY A . n 
A 1 297 GLY 297 333 333 GLY GLY A . n 
A 1 298 ARG 298 334 334 ARG ARG A . n 
A 1 299 GLY 299 335 335 GLY GLY A . n 
A 1 300 TRP 300 336 336 TRP TRP A . n 
A 1 301 ASP 301 337 337 ASP ASP A . n 
A 1 302 ALA 302 338 338 ALA ALA A . n 
A 1 303 THR 303 339 339 THR THR A . n 
A 1 304 ILE 304 340 340 ILE ILE A . n 
A 1 305 ASN 305 341 341 ASN ASN A . n 
A 1 306 LYS 306 342 342 LYS LYS A . n 
A 1 307 LYS 307 343 ?   ?   ?   A . n 
A 1 308 PRO 308 344 ?   ?   ?   A . n 
A 1 309 ASN 309 345 ?   ?   ?   A . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1BIQ 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1BIQ 
_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 A1BIQ 1 401 401 A1BIQ LIG A . 
C 3 CL    1 402 2   CL    CL  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 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX   ? ? ? 1.21.2_5419 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? autoPROC ? ? ? .           2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? autoPROC ? ? ? .           3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHENIX   ? ? ? .           4 
# 
_cell.angle_alpha                  90.000 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.000 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  120.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9EDV 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     91.990 
_cell.length_a_esd                 ? 
_cell.length_b                     91.990 
_cell.length_b_esd                 ? 
_cell.length_c                     117.960 
_cell.length_c_esd                 ? 
_cell.volume                       864463.445 
_cell.volume_esd                   ? 
_cell.Z_PDB                        9 
_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                         9EDV 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                146 
_symmetry.space_group_name_Hall            'R 3' 
_symmetry.space_group_name_H-M             'H 3' 
_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                   9EDV 
_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             2.71 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          54.67 
_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              7.5 
_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    '0.1 M Tris pH 8, 25 mM Magnesium chloride, 20% (w/v) PEG3350' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            298 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS EIGER X 9M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2023-06-28 
_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   1.18077 
_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                        'CLSI BEAMLINE 08ID-1' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        1.18077 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   08ID-1 
_diffrn_source.pdbx_synchrotron_site       CLSI 
# 
_reflns.B_iso_Wilson_estimate                          81.21 
_reflns.entry_id                                       9EDV 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.42 
_reflns.d_resolution_low                               29.18 
_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                                     14204 
_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                           99.9 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                10.0 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          15.1 
_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                                0.032 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.999 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.065 
_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                                    2.42 
_reflns_shell.d_res_low                                     2.48 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           0.7 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             1065 
_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                               10.2 
_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                               1.437 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.368 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          99.9 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  2.903 
_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                               118.90 
_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                                 9EDV 
_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                            2.42 
_refine.ls_d_res_low                             29.18 
_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                     14202 
_refine.ls_number_reflns_R_free                  625 
_refine.ls_number_reflns_R_work                  13577 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.97 
_refine.ls_percent_reflns_R_free                 4.40 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2393 
_refine.ls_R_factor_R_free                       0.2935 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2372 
_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                          1.96 
_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       'GeoStd + Monomer Library + CDL v1.2' 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.1000 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.9000 
_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                 37.0902 
_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                            0.3968 
_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                       2.42 
_refine_hist.d_res_low                        29.18 
_refine_hist.number_atoms_solvent             0 
_refine_hist.number_atoms_total               2494 
_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        2469 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         25 
_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' ? 0.0031  ? 2555 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.5867  ? 3453 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 0.0410  ? 358  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.0047  ? 451  ? f_plane_restr      ? ? 
'X-RAY DIFFRACTION' ? 16.0710 ? 956  ? f_dihedral_angle_d ? ? 
# 
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' 2.42 2.66  . . 200 3350 99.92  . . . . 0.4289 . . . . . . . . . . . 0.4901 
'X-RAY DIFFRACTION' 2.66 3.05  . . 155 3413 100.00 . . . . 0.2986 . . . . . . . . . . . 0.3205 
'X-RAY DIFFRACTION' 3.05 3.84  . . 145 3397 100.00 . . . . 0.2819 . . . . . . . . . . . 0.2828 
'X-RAY DIFFRACTION' 3.84 29.18 . . 125 3417 99.97  . . . . 0.2025 . . . . . . . . . . . 0.2700 
# 
_struct.entry_id                     9EDV 
_struct.title                        
;Crystal structure of Yck2 from Candida albicans in complex with inhibitor 1e: 2-(4-fluorophenyl)-3-(pyridin-4-yl)imidazo[1,2-a]pyridine-7-carbonitrile
;
_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        9EDV 
_struct_keywords.text            
;YCK2, KINASE, KINASE INHIBITOR, STRUCTURAL GENOMICS, NIAID, NATIONAL INSTITUTE OF ALLERGY AND INFECTIOUS DISEASES, Center for Structural Biology of Infectious Diseases, CSBID, TRANSFERASE, TRANSFERASE-INHIBITOR complex
;
_struct_keywords.pdbx_keywords   TRANSFERASE/INHIBITOR 
# 
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 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    A0A8H6C375_CANAX 
_struct_ref.pdbx_db_accession          A0A8H6C375 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;SSVVGLHYKIGKKIGEGSFGVIFEGTNIINGVPVAIKFEPRKTEAPQLRDEYRTYKHLQGCDGIPNAYYFGQEGLHNILV
IDLLGPSLEDLFDWCGRRFSVKTVVQVAIQMLTLVEEVHRHDLIYRDIKPDNFLIGRRGATDENNVHLIDFGMAKQYRDP
RTKQHIPYREKKSLSGTARYMSINTHLGREQSRRDDLEALGHVFFYFLRGQLPWQGLKAPTNKQKYEKIGDKKRTTPAVT
LCDGLPQQFAEYLDSVRSLPFDAEPPYEEYRMLLLSVLDDLGQACDGDMDWMHLNGGRGWDATINKKPN
;
_struct_ref.pdbx_align_begin           37 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              9EDV 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 1 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 309 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             A0A8H6C375 
_struct_ref_seq.db_align_beg                  37 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  345 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       37 
_struct_ref_seq.pdbx_auth_seq_align_end       345 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'gel filtration' 
_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 GLN A 47  ? LEU A 58  ? GLN A 83  LEU A 94  1 ? 12 
HELX_P HELX_P2  AA2 SER A 87  ? CYS A 95  ? SER A 123 CYS A 131 1 ? 9  
HELX_P HELX_P3  AA3 SER A 100 ? HIS A 121 ? SER A 136 HIS A 157 1 ? 22 
HELX_P HELX_P4  AA4 SER A 182 ? LEU A 187 ? SER A 218 LEU A 223 1 ? 6  
HELX_P HELX_P5  AA5 SER A 192 ? GLY A 210 ? SER A 228 GLY A 246 1 ? 19 
HELX_P HELX_P6  AA6 THR A 221 ? THR A 236 ? THR A 257 THR A 272 1 ? 16 
HELX_P HELX_P7  AA7 PRO A 237 ? CYS A 242 ? PRO A 273 CYS A 278 1 ? 6  
HELX_P HELX_P8  AA8 GLN A 247 ? SER A 258 ? GLN A 283 SER A 294 1 ? 12 
HELX_P HELX_P9  AA9 PRO A 266 ? LEU A 281 ? PRO A 302 LEU A 317 1 ? 16 
HELX_P HELX_P10 AB1 MET A 289 ? HIS A 293 ? MET A 325 HIS A 329 5 ? 5  
HELX_P HELX_P11 AB2 LEU A 294 ? ARG A 298 ? LEU A 330 ARG A 334 5 ? 5  
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 5 ? 
AA2 ? 2 ? 
AA3 ? 2 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA1 3 4 ? anti-parallel 
AA1 4 5 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA3 1 2 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 TYR A 8   ? LYS A 13  ? TYR A 44  LYS A 49  
AA1 2 VAL A 21  ? ASN A 27  ? VAL A 57  ASN A 63  
AA1 3 PRO A 33  ? PHE A 38  ? PRO A 69  PHE A 74  
AA1 4 HIS A 76  ? ASP A 82  ? HIS A 112 ASP A 118 
AA1 5 TYR A 69  ? GLU A 73  ? TYR A 105 GLU A 109 
AA2 1 LEU A 123 ? ILE A 124 ? LEU A 159 ILE A 160 
AA2 2 LYS A 155 ? GLN A 156 ? LYS A 191 GLN A 192 
AA3 1 PHE A 133 ? ILE A 135 ? PHE A 169 ILE A 171 
AA3 2 VAL A 146 ? LEU A 148 ? VAL A 182 LEU A 184 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N LYS A 12  ? N LYS A 48  O GLU A 24  ? O GLU A 60  
AA1 2 3 N VAL A 21  ? N VAL A 57  O PHE A 38  ? O PHE A 74  
AA1 3 4 N LYS A 37  ? N LYS A 73  O LEU A 79  ? O LEU A 115 
AA1 4 5 O VAL A 80  ? O VAL A 116 N TYR A 69  ? N TYR A 105 
AA2 1 2 N ILE A 124 ? N ILE A 160 O LYS A 155 ? O LYS A 191 
AA3 1 2 N LEU A 134 ? N LEU A 170 O HIS A 147 ? O HIS A 183 
# 
_pdbx_entry_details.entry_id                   9EDV 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_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 LEU A 42  ? ? 68.70   -38.12  
2 1 GLU A 52  ? ? -130.93 -105.04 
3 1 GLN A 83  ? ? -148.53 -30.26  
4 1 ARG A 162 ? ? 66.46   -0.13   
5 1 ASP A 186 ? ? 59.02   89.47   
6 1 LYS A 207 ? ? 60.97   67.04   
7 1 SER A 228 ? ? -147.91 -155.78 
8 1 TRP A 250 ? ? -92.53  36.27   
9 1 THR A 257 ? ? -112.73 -158.97 
# 
_pdbx_SG_project.id                    1 
_pdbx_SG_project.project_name          'NIAID, National Institute of Allergy and Infectious Diseases' 
_pdbx_SG_project.full_name_of_center   'Center for Structural Biology of Infectious Diseases' 
_pdbx_SG_project.initial_of_center     CSBID 
# 
loop_
_space_group_symop.id 
_space_group_symop.operation_xyz 
1 x,y,z                 
2 -y,x-y,z              
3 -x+y,-x,z             
4 x+1/3,y+2/3,z+2/3     
5 -y+1/3,x-y+2/3,z+2/3  
6 -x+y+1/3,-x+2/3,z+2/3 
7 x+2/3,y+1/3,z+1/3     
8 -y+2/3,x-y+1/3,z+1/3  
9 -x+y+2/3,-x+1/3,z+1/3 
# 
loop_
_pdbx_refine_tls.id 
_pdbx_refine_tls.pdbx_refine_id 
_pdbx_refine_tls.details 
_pdbx_refine_tls.method 
_pdbx_refine_tls.origin_x 
_pdbx_refine_tls.origin_y 
_pdbx_refine_tls.origin_z 
_pdbx_refine_tls.T[1][1] 
_pdbx_refine_tls.T[1][1]_esd 
_pdbx_refine_tls.T[1][2] 
_pdbx_refine_tls.T[1][2]_esd 
_pdbx_refine_tls.T[1][3] 
_pdbx_refine_tls.T[1][3]_esd 
_pdbx_refine_tls.T[2][2] 
_pdbx_refine_tls.T[2][2]_esd 
_pdbx_refine_tls.T[2][3] 
_pdbx_refine_tls.T[2][3]_esd 
_pdbx_refine_tls.T[3][3] 
_pdbx_refine_tls.T[3][3]_esd 
_pdbx_refine_tls.L[1][1] 
_pdbx_refine_tls.L[1][1]_esd 
_pdbx_refine_tls.L[1][2] 
_pdbx_refine_tls.L[1][2]_esd 
_pdbx_refine_tls.L[1][3] 
_pdbx_refine_tls.L[1][3]_esd 
_pdbx_refine_tls.L[2][2] 
_pdbx_refine_tls.L[2][2]_esd 
_pdbx_refine_tls.L[2][3] 
_pdbx_refine_tls.L[2][3]_esd 
_pdbx_refine_tls.L[3][3] 
_pdbx_refine_tls.L[3][3]_esd 
_pdbx_refine_tls.S[1][1] 
_pdbx_refine_tls.S[1][1]_esd 
_pdbx_refine_tls.S[1][2] 
_pdbx_refine_tls.S[1][2]_esd 
_pdbx_refine_tls.S[1][3] 
_pdbx_refine_tls.S[1][3]_esd 
_pdbx_refine_tls.S[2][1] 
_pdbx_refine_tls.S[2][1]_esd 
_pdbx_refine_tls.S[2][2] 
_pdbx_refine_tls.S[2][2]_esd 
_pdbx_refine_tls.S[2][3] 
_pdbx_refine_tls.S[2][3]_esd 
_pdbx_refine_tls.S[3][1] 
_pdbx_refine_tls.S[3][1]_esd 
_pdbx_refine_tls.S[3][2] 
_pdbx_refine_tls.S[3][2]_esd 
_pdbx_refine_tls.S[3][3] 
_pdbx_refine_tls.S[3][3]_esd 
1 'X-RAY DIFFRACTION' ? refined 23.4138084743 -8.59345490307 -14.3045397122 1.14566889283  ? 0.192500328129   ? -0.0763546386128 ? 
0.878876214648 ? 0.018633668428  ? 1.32837454332  ? 4.37414649304 ? 1.76345180782   ? 0.640284604356  ? 4.73354253764 ? 
-2.32672793162 ? 3.87953333166   ? -0.177267611306 ? 0.0199221950965 ? 0.845382917742  ? -0.917064226912 ? 0.11832789052   ? 
0.691101938335 ? -0.0555652252136 ? -0.635368396198 ? 0.0969281032542 ? 
2 'X-RAY DIFFRACTION' ? refined 18.221910784  -22.2076330926 -6.82146110628 0.678471402511 ? 0.06481869639    ? 0.0286590226075  ? 
0.854518468827 ? 0.0229247839177 ? 0.546251575275 ? 6.65236164089 ? -0.123325228291 ? -0.715648169055 ? 8.24899642696 ? 
0.497105011786 ? 0.0658599874076 ? 0.151838189409  ? 0.155624466289  ? 0.562682738174  ? 0.0443184109002 ? -0.144973634609 ? 
0.220653997714 ? -0.267705795545  ? -0.37452629634  ? 0.0180480345189 ? 
3 'X-RAY DIFFRACTION' ? refined 14.7301200051 -36.6032855149 -10.1872893216 0.578904113574 ? -0.0886804620562 ? 0.00299668935241 ? 
1.00351502892  ? 0.0267812941934 ? 0.644928265237 ? 5.1978097992  ? -0.127540666281 ? 0.527508127304  ? 7.82654175688 ? 
0.318168949857 ? 4.64227236047   ? 0.074848868358  ? 0.45766418203   ? -0.547023914202 ? -0.166680867125 ? -0.380599453104 ? 
0.247757094758 ? 0.1514109041     ? -0.631285562062 ? 0.303393493961  ? 
# 
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 A 1   A 37  ? A 57  A 93  ? ? 
;chain 'A' and (resid 37 through 93 )
;
2 'X-RAY DIFFRACTION' 2 A 58  A 94  ? A 173 A 209 ? ? 
;chain 'A' and (resid 94 through 209 )
;
3 'X-RAY DIFFRACTION' 3 A 174 A 210 ? A 306 A 342 ? ? 
;chain 'A' and (resid 210 through 342 )
;
# 
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 LYS 343 ? A LYS 307 
2 1 Y 1 A PRO 344 ? A PRO 308 
3 1 Y 1 A ASN 345 ? A ASN 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 
A1BIQ C10  C  Y N 1   
A1BIQ C15  C  Y N 2   
A1BIQ C17  C  Y N 3   
A1BIQ C20  C  N N 4   
A1BIQ C22  C  Y N 5   
A1BIQ C02  C  Y N 6   
A1BIQ C03  C  Y N 7   
A1BIQ C04  C  Y N 8   
A1BIQ C05  C  Y N 9   
A1BIQ C06  C  Y N 10  
A1BIQ C07  C  Y N 11  
A1BIQ C08  C  Y N 12  
A1BIQ C09  C  Y N 13  
A1BIQ C11  C  Y N 14  
A1BIQ C12  C  Y N 15  
A1BIQ C14  C  Y N 16  
A1BIQ C18  C  Y N 17  
A1BIQ C19  C  Y N 18  
A1BIQ C23  C  Y N 19  
A1BIQ F01  F  N N 20  
A1BIQ N13  N  Y N 21  
A1BIQ N16  N  Y N 22  
A1BIQ N21  N  N N 23  
A1BIQ N24  N  Y N 24  
A1BIQ H151 H  N N 25  
A1BIQ H171 H  N N 26  
A1BIQ H221 H  N N 27  
A1BIQ H031 H  N N 28  
A1BIQ H041 H  N N 29  
A1BIQ H051 H  N N 30  
A1BIQ H061 H  N N 31  
A1BIQ H111 H  N N 32  
A1BIQ H121 H  N N 33  
A1BIQ H141 H  N N 34  
A1BIQ H181 H  N N 35  
ALA   N    N  N N 36  
ALA   CA   C  N S 37  
ALA   C    C  N N 38  
ALA   O    O  N N 39  
ALA   CB   C  N N 40  
ALA   OXT  O  N N 41  
ALA   H    H  N N 42  
ALA   H2   H  N N 43  
ALA   HA   H  N N 44  
ALA   HB1  H  N N 45  
ALA   HB2  H  N N 46  
ALA   HB3  H  N N 47  
ALA   HXT  H  N N 48  
ARG   N    N  N N 49  
ARG   CA   C  N S 50  
ARG   C    C  N N 51  
ARG   O    O  N N 52  
ARG   CB   C  N N 53  
ARG   CG   C  N N 54  
ARG   CD   C  N N 55  
ARG   NE   N  N N 56  
ARG   CZ   C  N N 57  
ARG   NH1  N  N N 58  
ARG   NH2  N  N N 59  
ARG   OXT  O  N N 60  
ARG   H    H  N N 61  
ARG   H2   H  N N 62  
ARG   HA   H  N N 63  
ARG   HB2  H  N N 64  
ARG   HB3  H  N N 65  
ARG   HG2  H  N N 66  
ARG   HG3  H  N N 67  
ARG   HD2  H  N N 68  
ARG   HD3  H  N N 69  
ARG   HE   H  N N 70  
ARG   HH11 H  N N 71  
ARG   HH12 H  N N 72  
ARG   HH21 H  N N 73  
ARG   HH22 H  N N 74  
ARG   HXT  H  N N 75  
ASN   N    N  N N 76  
ASN   CA   C  N S 77  
ASN   C    C  N N 78  
ASN   O    O  N N 79  
ASN   CB   C  N N 80  
ASN   CG   C  N N 81  
ASN   OD1  O  N N 82  
ASN   ND2  N  N N 83  
ASN   OXT  O  N N 84  
ASN   H    H  N N 85  
ASN   H2   H  N N 86  
ASN   HA   H  N N 87  
ASN   HB2  H  N N 88  
ASN   HB3  H  N N 89  
ASN   HD21 H  N N 90  
ASN   HD22 H  N N 91  
ASN   HXT  H  N N 92  
ASP   N    N  N N 93  
ASP   CA   C  N S 94  
ASP   C    C  N N 95  
ASP   O    O  N N 96  
ASP   CB   C  N N 97  
ASP   CG   C  N N 98  
ASP   OD1  O  N N 99  
ASP   OD2  O  N N 100 
ASP   OXT  O  N N 101 
ASP   H    H  N N 102 
ASP   H2   H  N N 103 
ASP   HA   H  N N 104 
ASP   HB2  H  N N 105 
ASP   HB3  H  N N 106 
ASP   HD2  H  N N 107 
ASP   HXT  H  N N 108 
CL    CL   CL N N 109 
CYS   N    N  N N 110 
CYS   CA   C  N R 111 
CYS   C    C  N N 112 
CYS   O    O  N N 113 
CYS   CB   C  N N 114 
CYS   SG   S  N N 115 
CYS   OXT  O  N N 116 
CYS   H    H  N N 117 
CYS   H2   H  N N 118 
CYS   HA   H  N N 119 
CYS   HB2  H  N N 120 
CYS   HB3  H  N N 121 
CYS   HG   H  N N 122 
CYS   HXT  H  N N 123 
GLN   N    N  N N 124 
GLN   CA   C  N S 125 
GLN   C    C  N N 126 
GLN   O    O  N N 127 
GLN   CB   C  N N 128 
GLN   CG   C  N N 129 
GLN   CD   C  N N 130 
GLN   OE1  O  N N 131 
GLN   NE2  N  N N 132 
GLN   OXT  O  N N 133 
GLN   H    H  N N 134 
GLN   H2   H  N N 135 
GLN   HA   H  N N 136 
GLN   HB2  H  N N 137 
GLN   HB3  H  N N 138 
GLN   HG2  H  N N 139 
GLN   HG3  H  N N 140 
GLN   HE21 H  N N 141 
GLN   HE22 H  N N 142 
GLN   HXT  H  N N 143 
GLU   N    N  N N 144 
GLU   CA   C  N S 145 
GLU   C    C  N N 146 
GLU   O    O  N N 147 
GLU   CB   C  N N 148 
GLU   CG   C  N N 149 
GLU   CD   C  N N 150 
GLU   OE1  O  N N 151 
GLU   OE2  O  N N 152 
GLU   OXT  O  N N 153 
GLU   H    H  N N 154 
GLU   H2   H  N N 155 
GLU   HA   H  N N 156 
GLU   HB2  H  N N 157 
GLU   HB3  H  N N 158 
GLU   HG2  H  N N 159 
GLU   HG3  H  N N 160 
GLU   HE2  H  N N 161 
GLU   HXT  H  N N 162 
GLY   N    N  N N 163 
GLY   CA   C  N N 164 
GLY   C    C  N N 165 
GLY   O    O  N N 166 
GLY   OXT  O  N N 167 
GLY   H    H  N N 168 
GLY   H2   H  N N 169 
GLY   HA2  H  N N 170 
GLY   HA3  H  N N 171 
GLY   HXT  H  N N 172 
HIS   N    N  N N 173 
HIS   CA   C  N S 174 
HIS   C    C  N N 175 
HIS   O    O  N N 176 
HIS   CB   C  N N 177 
HIS   CG   C  Y N 178 
HIS   ND1  N  Y N 179 
HIS   CD2  C  Y N 180 
HIS   CE1  C  Y N 181 
HIS   NE2  N  Y N 182 
HIS   OXT  O  N N 183 
HIS   H    H  N N 184 
HIS   H2   H  N N 185 
HIS   HA   H  N N 186 
HIS   HB2  H  N N 187 
HIS   HB3  H  N N 188 
HIS   HD1  H  N N 189 
HIS   HD2  H  N N 190 
HIS   HE1  H  N N 191 
HIS   HE2  H  N N 192 
HIS   HXT  H  N N 193 
ILE   N    N  N N 194 
ILE   CA   C  N S 195 
ILE   C    C  N N 196 
ILE   O    O  N N 197 
ILE   CB   C  N S 198 
ILE   CG1  C  N N 199 
ILE   CG2  C  N N 200 
ILE   CD1  C  N N 201 
ILE   OXT  O  N N 202 
ILE   H    H  N N 203 
ILE   H2   H  N N 204 
ILE   HA   H  N N 205 
ILE   HB   H  N N 206 
ILE   HG12 H  N N 207 
ILE   HG13 H  N N 208 
ILE   HG21 H  N N 209 
ILE   HG22 H  N N 210 
ILE   HG23 H  N N 211 
ILE   HD11 H  N N 212 
ILE   HD12 H  N N 213 
ILE   HD13 H  N N 214 
ILE   HXT  H  N N 215 
LEU   N    N  N N 216 
LEU   CA   C  N S 217 
LEU   C    C  N N 218 
LEU   O    O  N N 219 
LEU   CB   C  N N 220 
LEU   CG   C  N N 221 
LEU   CD1  C  N N 222 
LEU   CD2  C  N N 223 
LEU   OXT  O  N N 224 
LEU   H    H  N N 225 
LEU   H2   H  N N 226 
LEU   HA   H  N N 227 
LEU   HB2  H  N N 228 
LEU   HB3  H  N N 229 
LEU   HG   H  N N 230 
LEU   HD11 H  N N 231 
LEU   HD12 H  N N 232 
LEU   HD13 H  N N 233 
LEU   HD21 H  N N 234 
LEU   HD22 H  N N 235 
LEU   HD23 H  N N 236 
LEU   HXT  H  N N 237 
LYS   N    N  N N 238 
LYS   CA   C  N S 239 
LYS   C    C  N N 240 
LYS   O    O  N N 241 
LYS   CB   C  N N 242 
LYS   CG   C  N N 243 
LYS   CD   C  N N 244 
LYS   CE   C  N N 245 
LYS   NZ   N  N N 246 
LYS   OXT  O  N N 247 
LYS   H    H  N N 248 
LYS   H2   H  N N 249 
LYS   HA   H  N N 250 
LYS   HB2  H  N N 251 
LYS   HB3  H  N N 252 
LYS   HG2  H  N N 253 
LYS   HG3  H  N N 254 
LYS   HD2  H  N N 255 
LYS   HD3  H  N N 256 
LYS   HE2  H  N N 257 
LYS   HE3  H  N N 258 
LYS   HZ1  H  N N 259 
LYS   HZ2  H  N N 260 
LYS   HZ3  H  N N 261 
LYS   HXT  H  N N 262 
MET   N    N  N N 263 
MET   CA   C  N S 264 
MET   C    C  N N 265 
MET   O    O  N N 266 
MET   CB   C  N N 267 
MET   CG   C  N N 268 
MET   SD   S  N N 269 
MET   CE   C  N N 270 
MET   OXT  O  N N 271 
MET   H    H  N N 272 
MET   H2   H  N N 273 
MET   HA   H  N N 274 
MET   HB2  H  N N 275 
MET   HB3  H  N N 276 
MET   HG2  H  N N 277 
MET   HG3  H  N N 278 
MET   HE1  H  N N 279 
MET   HE2  H  N N 280 
MET   HE3  H  N N 281 
MET   HXT  H  N N 282 
PHE   N    N  N N 283 
PHE   CA   C  N S 284 
PHE   C    C  N N 285 
PHE   O    O  N N 286 
PHE   CB   C  N N 287 
PHE   CG   C  Y N 288 
PHE   CD1  C  Y N 289 
PHE   CD2  C  Y N 290 
PHE   CE1  C  Y N 291 
PHE   CE2  C  Y N 292 
PHE   CZ   C  Y N 293 
PHE   OXT  O  N N 294 
PHE   H    H  N N 295 
PHE   H2   H  N N 296 
PHE   HA   H  N N 297 
PHE   HB2  H  N N 298 
PHE   HB3  H  N N 299 
PHE   HD1  H  N N 300 
PHE   HD2  H  N N 301 
PHE   HE1  H  N N 302 
PHE   HE2  H  N N 303 
PHE   HZ   H  N N 304 
PHE   HXT  H  N N 305 
PRO   N    N  N N 306 
PRO   CA   C  N S 307 
PRO   C    C  N N 308 
PRO   O    O  N N 309 
PRO   CB   C  N N 310 
PRO   CG   C  N N 311 
PRO   CD   C  N N 312 
PRO   OXT  O  N N 313 
PRO   H    H  N N 314 
PRO   HA   H  N N 315 
PRO   HB2  H  N N 316 
PRO   HB3  H  N N 317 
PRO   HG2  H  N N 318 
PRO   HG3  H  N N 319 
PRO   HD2  H  N N 320 
PRO   HD3  H  N N 321 
PRO   HXT  H  N N 322 
SER   N    N  N N 323 
SER   CA   C  N S 324 
SER   C    C  N N 325 
SER   O    O  N N 326 
SER   CB   C  N N 327 
SER   OG   O  N N 328 
SER   OXT  O  N N 329 
SER   H    H  N N 330 
SER   H2   H  N N 331 
SER   HA   H  N N 332 
SER   HB2  H  N N 333 
SER   HB3  H  N N 334 
SER   HG   H  N N 335 
SER   HXT  H  N N 336 
THR   N    N  N N 337 
THR   CA   C  N S 338 
THR   C    C  N N 339 
THR   O    O  N N 340 
THR   CB   C  N R 341 
THR   OG1  O  N N 342 
THR   CG2  C  N N 343 
THR   OXT  O  N N 344 
THR   H    H  N N 345 
THR   H2   H  N N 346 
THR   HA   H  N N 347 
THR   HB   H  N N 348 
THR   HG1  H  N N 349 
THR   HG21 H  N N 350 
THR   HG22 H  N N 351 
THR   HG23 H  N N 352 
THR   HXT  H  N N 353 
TRP   N    N  N N 354 
TRP   CA   C  N S 355 
TRP   C    C  N N 356 
TRP   O    O  N N 357 
TRP   CB   C  N N 358 
TRP   CG   C  Y N 359 
TRP   CD1  C  Y N 360 
TRP   CD2  C  Y N 361 
TRP   NE1  N  Y N 362 
TRP   CE2  C  Y N 363 
TRP   CE3  C  Y N 364 
TRP   CZ2  C  Y N 365 
TRP   CZ3  C  Y N 366 
TRP   CH2  C  Y N 367 
TRP   OXT  O  N N 368 
TRP   H    H  N N 369 
TRP   H2   H  N N 370 
TRP   HA   H  N N 371 
TRP   HB2  H  N N 372 
TRP   HB3  H  N N 373 
TRP   HD1  H  N N 374 
TRP   HE1  H  N N 375 
TRP   HE3  H  N N 376 
TRP   HZ2  H  N N 377 
TRP   HZ3  H  N N 378 
TRP   HH2  H  N N 379 
TRP   HXT  H  N N 380 
TYR   N    N  N N 381 
TYR   CA   C  N S 382 
TYR   C    C  N N 383 
TYR   O    O  N N 384 
TYR   CB   C  N N 385 
TYR   CG   C  Y N 386 
TYR   CD1  C  Y N 387 
TYR   CD2  C  Y N 388 
TYR   CE1  C  Y N 389 
TYR   CE2  C  Y N 390 
TYR   CZ   C  Y N 391 
TYR   OH   O  N N 392 
TYR   OXT  O  N N 393 
TYR   H    H  N N 394 
TYR   H2   H  N N 395 
TYR   HA   H  N N 396 
TYR   HB2  H  N N 397 
TYR   HB3  H  N N 398 
TYR   HD1  H  N N 399 
TYR   HD2  H  N N 400 
TYR   HE1  H  N N 401 
TYR   HE2  H  N N 402 
TYR   HH   H  N N 403 
TYR   HXT  H  N N 404 
VAL   N    N  N N 405 
VAL   CA   C  N S 406 
VAL   C    C  N N 407 
VAL   O    O  N N 408 
VAL   CB   C  N N 409 
VAL   CG1  C  N N 410 
VAL   CG2  C  N N 411 
VAL   OXT  O  N N 412 
VAL   H    H  N N 413 
VAL   H2   H  N N 414 
VAL   HA   H  N N 415 
VAL   HB   H  N N 416 
VAL   HG11 H  N N 417 
VAL   HG12 H  N N 418 
VAL   HG13 H  N N 419 
VAL   HG21 H  N N 420 
VAL   HG22 H  N N 421 
VAL   HG23 H  N N 422 
VAL   HXT  H  N N 423 
# 
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 
A1BIQ C02 F01  sing N N 1   
A1BIQ C04 C03  doub Y N 2   
A1BIQ C03 C02  sing Y N 3   
A1BIQ C05 C02  doub Y N 4   
A1BIQ C06 C05  sing Y N 5   
A1BIQ C07 C06  doub Y N 6   
A1BIQ C08 C07  sing N N 7   
A1BIQ C09 C08  doub Y N 8   
A1BIQ C11 C10  doub Y N 9   
A1BIQ C12 C11  sing Y N 10  
A1BIQ N13 C12  doub Y N 11  
A1BIQ C14 N13  sing Y N 12  
A1BIQ C15 C14  doub Y N 13  
A1BIQ C10 C09  sing N N 14  
A1BIQ N16 C09  sing Y N 15  
A1BIQ C17 N16  sing Y N 16  
A1BIQ C18 C17  doub Y N 17  
A1BIQ C19 C18  sing Y N 18  
A1BIQ N21 C20  trip N N 19  
A1BIQ C20 C19  sing N N 20  
A1BIQ C22 C19  doub Y N 21  
A1BIQ C23 C22  sing Y N 22  
A1BIQ N24 C23  doub Y N 23  
A1BIQ C04 C07  sing Y N 24  
A1BIQ C08 N24  sing Y N 25  
A1BIQ C10 C15  sing Y N 26  
A1BIQ N16 C23  sing Y N 27  
A1BIQ C15 H151 sing N N 28  
A1BIQ C17 H171 sing N N 29  
A1BIQ C22 H221 sing N N 30  
A1BIQ C03 H031 sing N N 31  
A1BIQ C04 H041 sing N N 32  
A1BIQ C05 H051 sing N N 33  
A1BIQ C06 H061 sing N N 34  
A1BIQ C11 H111 sing N N 35  
A1BIQ C12 H121 sing N N 36  
A1BIQ C14 H141 sing N N 37  
A1BIQ C18 H181 sing N N 38  
ALA   N   CA   sing N N 39  
ALA   N   H    sing N N 40  
ALA   N   H2   sing N N 41  
ALA   CA  C    sing N N 42  
ALA   CA  CB   sing N N 43  
ALA   CA  HA   sing N N 44  
ALA   C   O    doub N N 45  
ALA   C   OXT  sing N N 46  
ALA   CB  HB1  sing N N 47  
ALA   CB  HB2  sing N N 48  
ALA   CB  HB3  sing N N 49  
ALA   OXT HXT  sing N N 50  
ARG   N   CA   sing N N 51  
ARG   N   H    sing N N 52  
ARG   N   H2   sing N N 53  
ARG   CA  C    sing N N 54  
ARG   CA  CB   sing N N 55  
ARG   CA  HA   sing N N 56  
ARG   C   O    doub N N 57  
ARG   C   OXT  sing N N 58  
ARG   CB  CG   sing N N 59  
ARG   CB  HB2  sing N N 60  
ARG   CB  HB3  sing N N 61  
ARG   CG  CD   sing N N 62  
ARG   CG  HG2  sing N N 63  
ARG   CG  HG3  sing N N 64  
ARG   CD  NE   sing N N 65  
ARG   CD  HD2  sing N N 66  
ARG   CD  HD3  sing N N 67  
ARG   NE  CZ   sing N N 68  
ARG   NE  HE   sing N N 69  
ARG   CZ  NH1  sing N N 70  
ARG   CZ  NH2  doub N N 71  
ARG   NH1 HH11 sing N N 72  
ARG   NH1 HH12 sing N N 73  
ARG   NH2 HH21 sing N N 74  
ARG   NH2 HH22 sing N N 75  
ARG   OXT HXT  sing N N 76  
ASN   N   CA   sing N N 77  
ASN   N   H    sing N N 78  
ASN   N   H2   sing N N 79  
ASN   CA  C    sing N N 80  
ASN   CA  CB   sing N N 81  
ASN   CA  HA   sing N N 82  
ASN   C   O    doub N N 83  
ASN   C   OXT  sing N N 84  
ASN   CB  CG   sing N N 85  
ASN   CB  HB2  sing N N 86  
ASN   CB  HB3  sing N N 87  
ASN   CG  OD1  doub N N 88  
ASN   CG  ND2  sing N N 89  
ASN   ND2 HD21 sing N N 90  
ASN   ND2 HD22 sing N N 91  
ASN   OXT HXT  sing N N 92  
ASP   N   CA   sing N N 93  
ASP   N   H    sing N N 94  
ASP   N   H2   sing N N 95  
ASP   CA  C    sing N N 96  
ASP   CA  CB   sing N N 97  
ASP   CA  HA   sing N N 98  
ASP   C   O    doub N N 99  
ASP   C   OXT  sing N N 100 
ASP   CB  CG   sing N N 101 
ASP   CB  HB2  sing N N 102 
ASP   CB  HB3  sing N N 103 
ASP   CG  OD1  doub N N 104 
ASP   CG  OD2  sing N N 105 
ASP   OD2 HD2  sing N N 106 
ASP   OXT HXT  sing N N 107 
CYS   N   CA   sing N N 108 
CYS   N   H    sing N N 109 
CYS   N   H2   sing N N 110 
CYS   CA  C    sing N N 111 
CYS   CA  CB   sing N N 112 
CYS   CA  HA   sing N N 113 
CYS   C   O    doub N N 114 
CYS   C   OXT  sing N N 115 
CYS   CB  SG   sing N N 116 
CYS   CB  HB2  sing N N 117 
CYS   CB  HB3  sing N N 118 
CYS   SG  HG   sing N N 119 
CYS   OXT HXT  sing N N 120 
GLN   N   CA   sing N N 121 
GLN   N   H    sing N N 122 
GLN   N   H2   sing N N 123 
GLN   CA  C    sing N N 124 
GLN   CA  CB   sing N N 125 
GLN   CA  HA   sing N N 126 
GLN   C   O    doub N N 127 
GLN   C   OXT  sing N N 128 
GLN   CB  CG   sing N N 129 
GLN   CB  HB2  sing N N 130 
GLN   CB  HB3  sing N N 131 
GLN   CG  CD   sing N N 132 
GLN   CG  HG2  sing N N 133 
GLN   CG  HG3  sing N N 134 
GLN   CD  OE1  doub N N 135 
GLN   CD  NE2  sing N N 136 
GLN   NE2 HE21 sing N N 137 
GLN   NE2 HE22 sing N N 138 
GLN   OXT HXT  sing N N 139 
GLU   N   CA   sing N N 140 
GLU   N   H    sing N N 141 
GLU   N   H2   sing N N 142 
GLU   CA  C    sing N N 143 
GLU   CA  CB   sing N N 144 
GLU   CA  HA   sing N N 145 
GLU   C   O    doub N N 146 
GLU   C   OXT  sing N N 147 
GLU   CB  CG   sing N N 148 
GLU   CB  HB2  sing N N 149 
GLU   CB  HB3  sing N N 150 
GLU   CG  CD   sing N N 151 
GLU   CG  HG2  sing N N 152 
GLU   CG  HG3  sing N N 153 
GLU   CD  OE1  doub N N 154 
GLU   CD  OE2  sing N N 155 
GLU   OE2 HE2  sing N N 156 
GLU   OXT HXT  sing N N 157 
GLY   N   CA   sing N N 158 
GLY   N   H    sing N N 159 
GLY   N   H2   sing N N 160 
GLY   CA  C    sing N N 161 
GLY   CA  HA2  sing N N 162 
GLY   CA  HA3  sing N N 163 
GLY   C   O    doub N N 164 
GLY   C   OXT  sing N N 165 
GLY   OXT HXT  sing N N 166 
HIS   N   CA   sing N N 167 
HIS   N   H    sing N N 168 
HIS   N   H2   sing N N 169 
HIS   CA  C    sing N N 170 
HIS   CA  CB   sing N N 171 
HIS   CA  HA   sing N N 172 
HIS   C   O    doub N N 173 
HIS   C   OXT  sing N N 174 
HIS   CB  CG   sing N N 175 
HIS   CB  HB2  sing N N 176 
HIS   CB  HB3  sing N N 177 
HIS   CG  ND1  sing Y N 178 
HIS   CG  CD2  doub Y N 179 
HIS   ND1 CE1  doub Y N 180 
HIS   ND1 HD1  sing N N 181 
HIS   CD2 NE2  sing Y N 182 
HIS   CD2 HD2  sing N N 183 
HIS   CE1 NE2  sing Y N 184 
HIS   CE1 HE1  sing N N 185 
HIS   NE2 HE2  sing N N 186 
HIS   OXT HXT  sing N N 187 
ILE   N   CA   sing N N 188 
ILE   N   H    sing N N 189 
ILE   N   H2   sing N N 190 
ILE   CA  C    sing N N 191 
ILE   CA  CB   sing N N 192 
ILE   CA  HA   sing N N 193 
ILE   C   O    doub N N 194 
ILE   C   OXT  sing N N 195 
ILE   CB  CG1  sing N N 196 
ILE   CB  CG2  sing N N 197 
ILE   CB  HB   sing N N 198 
ILE   CG1 CD1  sing N N 199 
ILE   CG1 HG12 sing N N 200 
ILE   CG1 HG13 sing N N 201 
ILE   CG2 HG21 sing N N 202 
ILE   CG2 HG22 sing N N 203 
ILE   CG2 HG23 sing N N 204 
ILE   CD1 HD11 sing N N 205 
ILE   CD1 HD12 sing N N 206 
ILE   CD1 HD13 sing N N 207 
ILE   OXT HXT  sing N N 208 
LEU   N   CA   sing N N 209 
LEU   N   H    sing N N 210 
LEU   N   H2   sing N N 211 
LEU   CA  C    sing N N 212 
LEU   CA  CB   sing N N 213 
LEU   CA  HA   sing N N 214 
LEU   C   O    doub N N 215 
LEU   C   OXT  sing N N 216 
LEU   CB  CG   sing N N 217 
LEU   CB  HB2  sing N N 218 
LEU   CB  HB3  sing N N 219 
LEU   CG  CD1  sing N N 220 
LEU   CG  CD2  sing N N 221 
LEU   CG  HG   sing N N 222 
LEU   CD1 HD11 sing N N 223 
LEU   CD1 HD12 sing N N 224 
LEU   CD1 HD13 sing N N 225 
LEU   CD2 HD21 sing N N 226 
LEU   CD2 HD22 sing N N 227 
LEU   CD2 HD23 sing N N 228 
LEU   OXT HXT  sing N N 229 
LYS   N   CA   sing N N 230 
LYS   N   H    sing N N 231 
LYS   N   H2   sing N N 232 
LYS   CA  C    sing N N 233 
LYS   CA  CB   sing N N 234 
LYS   CA  HA   sing N N 235 
LYS   C   O    doub N N 236 
LYS   C   OXT  sing N N 237 
LYS   CB  CG   sing N N 238 
LYS   CB  HB2  sing N N 239 
LYS   CB  HB3  sing N N 240 
LYS   CG  CD   sing N N 241 
LYS   CG  HG2  sing N N 242 
LYS   CG  HG3  sing N N 243 
LYS   CD  CE   sing N N 244 
LYS   CD  HD2  sing N N 245 
LYS   CD  HD3  sing N N 246 
LYS   CE  NZ   sing N N 247 
LYS   CE  HE2  sing N N 248 
LYS   CE  HE3  sing N N 249 
LYS   NZ  HZ1  sing N N 250 
LYS   NZ  HZ2  sing N N 251 
LYS   NZ  HZ3  sing N N 252 
LYS   OXT HXT  sing N N 253 
MET   N   CA   sing N N 254 
MET   N   H    sing N N 255 
MET   N   H2   sing N N 256 
MET   CA  C    sing N N 257 
MET   CA  CB   sing N N 258 
MET   CA  HA   sing N N 259 
MET   C   O    doub N N 260 
MET   C   OXT  sing N N 261 
MET   CB  CG   sing N N 262 
MET   CB  HB2  sing N N 263 
MET   CB  HB3  sing N N 264 
MET   CG  SD   sing N N 265 
MET   CG  HG2  sing N N 266 
MET   CG  HG3  sing N N 267 
MET   SD  CE   sing N N 268 
MET   CE  HE1  sing N N 269 
MET   CE  HE2  sing N N 270 
MET   CE  HE3  sing N N 271 
MET   OXT HXT  sing N N 272 
PHE   N   CA   sing N N 273 
PHE   N   H    sing N N 274 
PHE   N   H2   sing N N 275 
PHE   CA  C    sing N N 276 
PHE   CA  CB   sing N N 277 
PHE   CA  HA   sing N N 278 
PHE   C   O    doub N N 279 
PHE   C   OXT  sing N N 280 
PHE   CB  CG   sing N N 281 
PHE   CB  HB2  sing N N 282 
PHE   CB  HB3  sing N N 283 
PHE   CG  CD1  doub Y N 284 
PHE   CG  CD2  sing Y N 285 
PHE   CD1 CE1  sing Y N 286 
PHE   CD1 HD1  sing N N 287 
PHE   CD2 CE2  doub Y N 288 
PHE   CD2 HD2  sing N N 289 
PHE   CE1 CZ   doub Y N 290 
PHE   CE1 HE1  sing N N 291 
PHE   CE2 CZ   sing Y N 292 
PHE   CE2 HE2  sing N N 293 
PHE   CZ  HZ   sing N N 294 
PHE   OXT HXT  sing N N 295 
PRO   N   CA   sing N N 296 
PRO   N   CD   sing N N 297 
PRO   N   H    sing N N 298 
PRO   CA  C    sing N N 299 
PRO   CA  CB   sing N N 300 
PRO   CA  HA   sing N N 301 
PRO   C   O    doub N N 302 
PRO   C   OXT  sing N N 303 
PRO   CB  CG   sing N N 304 
PRO   CB  HB2  sing N N 305 
PRO   CB  HB3  sing N N 306 
PRO   CG  CD   sing N N 307 
PRO   CG  HG2  sing N N 308 
PRO   CG  HG3  sing N N 309 
PRO   CD  HD2  sing N N 310 
PRO   CD  HD3  sing N N 311 
PRO   OXT HXT  sing N N 312 
SER   N   CA   sing N N 313 
SER   N   H    sing N N 314 
SER   N   H2   sing N N 315 
SER   CA  C    sing N N 316 
SER   CA  CB   sing N N 317 
SER   CA  HA   sing N N 318 
SER   C   O    doub N N 319 
SER   C   OXT  sing N N 320 
SER   CB  OG   sing N N 321 
SER   CB  HB2  sing N N 322 
SER   CB  HB3  sing N N 323 
SER   OG  HG   sing N N 324 
SER   OXT HXT  sing N N 325 
THR   N   CA   sing N N 326 
THR   N   H    sing N N 327 
THR   N   H2   sing N N 328 
THR   CA  C    sing N N 329 
THR   CA  CB   sing N N 330 
THR   CA  HA   sing N N 331 
THR   C   O    doub N N 332 
THR   C   OXT  sing N N 333 
THR   CB  OG1  sing N N 334 
THR   CB  CG2  sing N N 335 
THR   CB  HB   sing N N 336 
THR   OG1 HG1  sing N N 337 
THR   CG2 HG21 sing N N 338 
THR   CG2 HG22 sing N N 339 
THR   CG2 HG23 sing N N 340 
THR   OXT HXT  sing N N 341 
TRP   N   CA   sing N N 342 
TRP   N   H    sing N N 343 
TRP   N   H2   sing N N 344 
TRP   CA  C    sing N N 345 
TRP   CA  CB   sing N N 346 
TRP   CA  HA   sing N N 347 
TRP   C   O    doub N N 348 
TRP   C   OXT  sing N N 349 
TRP   CB  CG   sing N N 350 
TRP   CB  HB2  sing N N 351 
TRP   CB  HB3  sing N N 352 
TRP   CG  CD1  doub Y N 353 
TRP   CG  CD2  sing Y N 354 
TRP   CD1 NE1  sing Y N 355 
TRP   CD1 HD1  sing N N 356 
TRP   CD2 CE2  doub Y N 357 
TRP   CD2 CE3  sing Y N 358 
TRP   NE1 CE2  sing Y N 359 
TRP   NE1 HE1  sing N N 360 
TRP   CE2 CZ2  sing Y N 361 
TRP   CE3 CZ3  doub Y N 362 
TRP   CE3 HE3  sing N N 363 
TRP   CZ2 CH2  doub Y N 364 
TRP   CZ2 HZ2  sing N N 365 
TRP   CZ3 CH2  sing Y N 366 
TRP   CZ3 HZ3  sing N N 367 
TRP   CH2 HH2  sing N N 368 
TRP   OXT HXT  sing N N 369 
TYR   N   CA   sing N N 370 
TYR   N   H    sing N N 371 
TYR   N   H2   sing N N 372 
TYR   CA  C    sing N N 373 
TYR   CA  CB   sing N N 374 
TYR   CA  HA   sing N N 375 
TYR   C   O    doub N N 376 
TYR   C   OXT  sing N N 377 
TYR   CB  CG   sing N N 378 
TYR   CB  HB2  sing N N 379 
TYR   CB  HB3  sing N N 380 
TYR   CG  CD1  doub Y N 381 
TYR   CG  CD2  sing Y N 382 
TYR   CD1 CE1  sing Y N 383 
TYR   CD1 HD1  sing N N 384 
TYR   CD2 CE2  doub Y N 385 
TYR   CD2 HD2  sing N N 386 
TYR   CE1 CZ   doub Y N 387 
TYR   CE1 HE1  sing N N 388 
TYR   CE2 CZ   sing Y N 389 
TYR   CE2 HE2  sing N N 390 
TYR   CZ  OH   sing N N 391 
TYR   OH  HH   sing N N 392 
TYR   OXT HXT  sing N N 393 
VAL   N   CA   sing N N 394 
VAL   N   H    sing N N 395 
VAL   N   H2   sing N N 396 
VAL   CA  C    sing N N 397 
VAL   CA  CB   sing N N 398 
VAL   CA  HA   sing N N 399 
VAL   C   O    doub N N 400 
VAL   C   OXT  sing N N 401 
VAL   CB  CG1  sing N N 402 
VAL   CB  CG2  sing N N 403 
VAL   CB  HB   sing N N 404 
VAL   CG1 HG11 sing N N 405 
VAL   CG1 HG12 sing N N 406 
VAL   CG1 HG13 sing N N 407 
VAL   CG2 HG21 sing N N 408 
VAL   CG2 HG22 sing N N 409 
VAL   CG2 HG23 sing N N 410 
VAL   OXT HXT  sing N N 411 
# 
_pdbx_audit_support.funding_organization   
'National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID)' 
_pdbx_audit_support.country                'United States' 
_pdbx_audit_support.grant_number           75N93022C00035 
_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   6u6a 
_pdbx_initial_refinement_model.details          ? 
# 
_space_group.name_H-M_alt     'R 3 :H' 
_space_group.name_Hall        'R 3' 
_space_group.IT_number        146 
_space_group.crystal_system   trigonal 
_space_group.id               1 
# 
_atom_sites.entry_id                    9EDV 
_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]   0.010871 
_atom_sites.fract_transf_matrix[1][2]   0.006276 
_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]   0.012552 
_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]   0.008477 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
_atom_type.scat_dispersion_real 
_atom_type.scat_dispersion_imag 
_atom_type.scat_Cromer_Mann_a1 
_atom_type.scat_Cromer_Mann_a2 
_atom_type.scat_Cromer_Mann_a3 
_atom_type.scat_Cromer_Mann_a4 
_atom_type.scat_Cromer_Mann_b1 
_atom_type.scat_Cromer_Mann_b2 
_atom_type.scat_Cromer_Mann_b3 
_atom_type.scat_Cromer_Mann_b4 
_atom_type.scat_Cromer_Mann_c 
_atom_type.scat_source 
_atom_type.scat_dispersion_source 
C  ? ? 3.54356 2.42580 ? ? 25.62398 1.50364  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
CL ? ? 9.50761 7.44341 ? ? 1.04373  23.83732 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
F  ? ? 8.95735 ?       ? ? 7.27484  ?        ? ? 0.0 
;1-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
N  ? ? 4.01032 2.96436 ? ? 19.97189 1.75589  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
O  ? ? 4.49882 3.47563 ? ? 15.80542 1.70748  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
S  ? ? 9.55732 6.39887 ? ? 1.23737  29.19336 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
# 
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   . SER   A 1 1   ? 31.70500  3.83200   -21.88600 1.000 153.03833 ? 37  SER   A N   1 
ATOM   2    C  CA  . SER   A 1 1   ? 31.73500  3.42400   -20.48600 1.000 150.33140 ? 37  SER   A CA  1 
ATOM   3    C  C   . SER   A 1 1   ? 31.26900  1.97800   -20.34000 1.000 154.02448 ? 37  SER   A C   1 
ATOM   4    O  O   . SER   A 1 1   ? 30.07100  1.70700   -20.26500 1.000 150.82697 ? 37  SER   A O   1 
ATOM   5    C  CB  . SER   A 1 1   ? 30.86500  4.35500   -19.63900 1.000 153.54662 ? 37  SER   A CB  1 
ATOM   6    O  OG  . SER   A 1 1   ? 31.08700  4.14600   -18.25500 1.000 152.79622 ? 37  SER   A OG  1 
ATOM   7    N  N   . SER   A 1 2   ? 32.23000  1.05200   -20.30000 1.000 153.70730 ? 38  SER   A N   1 
ATOM   8    C  CA  . SER   A 1 2   ? 31.90200  -0.36900  -20.24900 1.000 148.66300 ? 38  SER   A CA  1 
ATOM   9    C  C   . SER   A 1 2   ? 31.49600  -0.82400  -18.85300 1.000 146.87303 ? 38  SER   A C   1 
ATOM   10   O  O   . SER   A 1 2   ? 30.70300  -1.76200  -18.72100 1.000 145.15913 ? 38  SER   A O   1 
ATOM   11   C  CB  . SER   A 1 2   ? 33.08900  -1.19800  -20.74200 1.000 151.09649 ? 38  SER   A CB  1 
ATOM   12   O  OG  . SER   A 1 2   ? 34.24000  -0.95800  -19.95000 1.000 151.81880 ? 38  SER   A OG  1 
ATOM   13   N  N   . VAL   A 1 3   ? 32.02700  -0.18500  -17.81000 1.000 152.07802 ? 39  VAL   A N   1 
ATOM   14   C  CA  . VAL   A 1 3   ? 31.70200  -0.57800  -16.44500 1.000 145.30479 ? 39  VAL   A CA  1 
ATOM   15   C  C   . VAL   A 1 3   ? 30.24300  -0.25300  -16.14900 1.000 145.18395 ? 39  VAL   A C   1 
ATOM   16   O  O   . VAL   A 1 3   ? 29.72700  0.80300   -16.54300 1.000 153.29216 ? 39  VAL   A O   1 
ATOM   17   C  CB  . VAL   A 1 3   ? 32.65300  0.11600   -15.45200 1.000 145.70555 ? 39  VAL   A CB  1 
ATOM   18   C  CG1 . VAL   A 1 3   ? 32.61800  1.62900   -15.63700 1.000 158.99647 ? 39  VAL   A CG1 1 
ATOM   19   C  CG2 . VAL   A 1 3   ? 32.31400  -0.26300  -14.01800 1.000 136.44011 ? 39  VAL   A CG2 1 
ATOM   20   N  N   . VAL   A 1 4   ? 29.55900  -1.17400  -15.47100 1.000 135.90871 ? 40  VAL   A N   1 
ATOM   21   C  CA  . VAL   A 1 4   ? 28.16300  -0.99300  -15.10000 1.000 130.28192 ? 40  VAL   A CA  1 
ATOM   22   C  C   . VAL   A 1 4   ? 28.03900  -1.11300  -13.58700 1.000 124.21804 ? 40  VAL   A C   1 
ATOM   23   O  O   . VAL   A 1 4   ? 28.91700  -1.64500  -12.90300 1.000 120.35649 ? 40  VAL   A O   1 
ATOM   24   C  CB  . VAL   A 1 4   ? 27.22900  -2.00300  -15.79900 1.000 130.54977 ? 40  VAL   A CB  1 
ATOM   25   C  CG1 . VAL   A 1 4   ? 27.57500  -2.12400  -17.27700 1.000 137.07872 ? 40  VAL   A CG1 1 
ATOM   26   C  CG2 . VAL   A 1 4   ? 27.29000  -3.36000  -15.11000 1.000 128.36981 ? 40  VAL   A CG2 1 
ATOM   27   N  N   . GLY   A 1 5   ? 26.92500  -0.60600  -13.06600 1.000 129.13099 ? 41  GLY   A N   1 
ATOM   28   C  CA  . GLY   A 1 5   ? 26.66800  -0.69800  -11.64400 1.000 118.06106 ? 41  GLY   A CA  1 
ATOM   29   C  C   . GLY   A 1 5   ? 27.61700  0.08200   -10.76900 1.000 112.58228 ? 41  GLY   A C   1 
ATOM   30   O  O   . GLY   A 1 5   ? 27.76200  -0.24700  -9.58900  1.000 110.59599 ? 41  GLY   A O   1 
ATOM   31   N  N   . LEU   A 1 6   ? 28.27900  1.10100   -11.32400 1.000 111.23125 ? 42  LEU   A N   1 
ATOM   32   C  CA  . LEU   A 1 6   ? 29.22300  1.95900   -10.61200 1.000 114.05403 ? 42  LEU   A CA  1 
ATOM   33   C  C   . LEU   A 1 6   ? 30.50000  1.21900   -10.22100 1.000 118.21012 ? 42  LEU   A C   1 
ATOM   34   O  O   . LEU   A 1 6   ? 31.59200  1.79200   -10.29100 1.000 120.53674 ? 42  LEU   A O   1 
ATOM   35   C  CB  . LEU   A 1 6   ? 28.57600  2.57300   -9.36400  1.000 118.94708 ? 42  LEU   A CB  1 
ATOM   36   C  CG  . LEU   A 1 6   ? 27.18700  3.20300   -9.49700  1.000 114.26333 ? 42  LEU   A CG  1 
ATOM   37   C  CD1 . LEU   A 1 6   ? 26.65700  3.58900   -8.12800  1.000 107.04111 ? 42  LEU   A CD1 1 
ATOM   38   C  CD2 . LEU   A 1 6   ? 27.21300  4.40600   -10.42700 1.000 118.43617 ? 42  LEU   A CD2 1 
ATOM   39   N  N   . HIS   A 1 7   ? 30.38500  -0.05300  -9.81800  1.000 110.86248 ? 43  HIS   A N   1 
ATOM   40   C  CA  . HIS   A 1 7   ? 31.50600  -0.77800  -9.23000  1.000 108.57945 ? 43  HIS   A CA  1 
ATOM   41   C  C   . HIS   A 1 7   ? 31.73000  -2.15200  -9.85800  1.000 109.95709 ? 43  HIS   A C   1 
ATOM   42   O  O   . HIS   A 1 7   ? 32.31500  -3.02600  -9.21000  1.000 111.11999 ? 43  HIS   A O   1 
ATOM   43   C  CB  . HIS   A 1 7   ? 31.30300  -0.94600  -7.71900  1.000 107.81496 ? 43  HIS   A CB  1 
ATOM   44   C  CG  . HIS   A 1 7   ? 31.38600  0.33200   -6.94200  1.000 113.26515 ? 43  HIS   A CG  1 
ATOM   45   N  ND1 . HIS   A 1 7   ? 30.92700  0.44100   -5.64600  1.000 117.16400 ? 43  HIS   A ND1 1 
ATOM   46   C  CD2 . HIS   A 1 7   ? 31.88500  1.54700   -7.26600  1.000 115.95914 ? 43  HIS   A CD2 1 
ATOM   47   C  CE1 . HIS   A 1 7   ? 31.13200  1.67000   -5.21000  1.000 112.85115 ? 43  HIS   A CE1 1 
ATOM   48   N  NE2 . HIS   A 1 7   ? 31.71300  2.36200   -6.17400  1.000 117.14433 ? 43  HIS   A NE2 1 
ATOM   49   N  N   . TYR   A 1 8   ? 31.28900  -2.38100  -11.09600 1.000 114.62378 ? 44  TYR   A N   1 
ATOM   50   C  CA  . TYR   A 1 8   ? 31.36600  -3.71800  -11.68700 1.000 110.49561 ? 44  TYR   A CA  1 
ATOM   51   C  C   . TYR   A 1 8   ? 31.75000  -3.61800  -13.15700 1.000 115.56578 ? 44  TYR   A C   1 
ATOM   52   O  O   . TYR   A 1 8   ? 30.95700  -3.15300  -13.98100 1.000 119.58303 ? 44  TYR   A O   1 
ATOM   53   C  CB  . TYR   A 1 8   ? 30.04600  -4.46900  -11.51000 1.000 106.97103 ? 44  TYR   A CB  1 
ATOM   54   C  CG  . TYR   A 1 8   ? 29.68900  -4.66500  -10.05500 1.000 107.20013 ? 44  TYR   A CG  1 
ATOM   55   C  CD1 . TYR   A 1 8   ? 30.32700  -5.63200  -9.29100  1.000 100.82841 ? 44  TYR   A CD1 1 
ATOM   56   C  CD2 . TYR   A 1 8   ? 28.73500  -3.86600  -9.44000  1.000 106.87979 ? 44  TYR   A CD2 1 
ATOM   57   C  CE1 . TYR   A 1 8   ? 30.01500  -5.80900  -7.95800  1.000 102.09647 ? 44  TYR   A CE1 1 
ATOM   58   C  CE2 . TYR   A 1 8   ? 28.41700  -4.03600  -8.10600  1.000 108.57142 ? 44  TYR   A CE2 1 
ATOM   59   C  CZ  . TYR   A 1 8   ? 29.06100  -5.00800  -7.37100  1.000 108.73368 ? 44  TYR   A CZ  1 
ATOM   60   O  OH  . TYR   A 1 8   ? 28.74900  -5.18000  -6.04300  1.000 112.75989 ? 44  TYR   A OH  1 
ATOM   61   N  N   . LYS   A 1 9   ? 32.95500  -4.08400  -13.48400 1.000 112.89537 ? 45  LYS   A N   1 
ATOM   62   C  CA  . LYS   A 1 9   ? 33.48400  -4.02900  -14.84000 1.000 113.53784 ? 45  LYS   A CA  1 
ATOM   63   C  C   . LYS   A 1 9   ? 33.08800  -5.28500  -15.60700 1.000 114.46201 ? 45  LYS   A C   1 
ATOM   64   O  O   . LYS   A 1 9   ? 33.21400  -6.40000  -15.09100 1.000 107.21992 ? 45  LYS   A O   1 
ATOM   65   C  CB  . LYS   A 1 9   ? 35.00600  -3.88200  -14.80700 1.000 113.94136 ? 45  LYS   A CB  1 
ATOM   66   C  CG  . LYS   A 1 9   ? 35.69800  -4.07600  -16.14900 1.000 116.47831 ? 45  LYS   A CG  1 
ATOM   67   C  CD  . LYS   A 1 9   ? 37.19900  -3.83700  -16.02600 1.000 112.97293 ? 45  LYS   A CD  1 
ATOM   68   C  CE  . LYS   A 1 9   ? 37.83100  -4.75800  -14.99000 1.000 102.79319 ? 45  LYS   A CE  1 
ATOM   69   N  NZ  . LYS   A 1 9   ? 39.24600  -4.39700  -14.68400 1.000 101.88604 ? 45  LYS   A NZ  1 
ATOM   70   N  N   . ILE   A 1 10  ? 32.61300  -5.09900  -16.83900 1.000 117.72687 ? 46  ILE   A N   1 
ATOM   71   C  CA  . ILE   A 1 10  ? 32.20600  -6.22700  -17.66900 1.000 117.76370 ? 46  ILE   A CA  1 
ATOM   72   C  C   . ILE   A 1 10  ? 33.43000  -7.04700  -18.05500 1.000 119.90065 ? 46  ILE   A C   1 
ATOM   73   O  O   . ILE   A 1 10  ? 34.45300  -6.50200  -18.49100 1.000 123.20134 ? 46  ILE   A O   1 
ATOM   74   C  CB  . ILE   A 1 10  ? 31.44500  -5.73000  -18.90700 1.000 121.99009 ? 46  ILE   A CB  1 
ATOM   75   C  CG1 . ILE   A 1 10  ? 29.96700  -5.52500  -18.57100 1.000 123.38207 ? 46  ILE   A CG1 1 
ATOM   76   C  CG2 . ILE   A 1 10  ? 31.61400  -6.69200  -20.07800 1.000 117.06788 ? 46  ILE   A CG2 1 
ATOM   77   C  CD1 . ILE   A 1 10  ? 29.18800  -4.84200  -19.66500 1.000 124.33980 ? 46  ILE   A CD1 1 
ATOM   78   N  N   . GLY   A 1 11  ? 33.33300  -8.36400  -17.88300 1.000 124.86582 ? 47  GLY   A N   1 
ATOM   79   C  CA  . GLY   A 1 11  ? 34.40200  -9.26500  -18.26200 1.000 125.98409 ? 47  GLY   A CA  1 
ATOM   80   C  C   . GLY   A 1 11  ? 34.01200  -10.16200 -19.41700 1.000 130.88031 ? 47  GLY   A C   1 
ATOM   81   O  O   . GLY   A 1 11  ? 33.71400  -9.68000  -20.51600 1.000 126.33755 ? 47  GLY   A O   1 
ATOM   82   N  N   . LYS   A 1 12  ? 33.99200  -11.46800 -19.17100 1.000 145.85033 ? 48  LYS   A N   1 
ATOM   83   C  CA  . LYS   A 1 12  ? 33.69300  -12.43500 -20.21600 1.000 147.91503 ? 48  LYS   A CA  1 
ATOM   84   C  C   . LYS   A 1 12  ? 32.18500  -12.64000 -20.35500 1.000 146.16620 ? 48  LYS   A C   1 
ATOM   85   O  O   . LYS   A 1 12  ? 31.42800  -12.51600 -19.39000 1.000 146.38443 ? 48  LYS   A O   1 
ATOM   86   C  CB  . LYS   A 1 12  ? 34.39400  -13.76500 -19.91900 1.000 152.02092 ? 48  LYS   A CB  1 
ATOM   87   C  CG  . LYS   A 1 12  ? 34.60700  -14.64100 -21.13800 1.000 156.29741 ? 48  LYS   A CG  1 
ATOM   88   C  CD  . LYS   A 1 12  ? 35.54600  -15.78500 -20.81700 1.000 157.52228 ? 48  LYS   A CD  1 
ATOM   89   C  CE  . LYS   A 1 12  ? 36.25300  -16.27000 -22.07000 1.000 167.74454 ? 48  LYS   A CE  1 
ATOM   90   N  NZ  . LYS   A 1 12  ? 35.29900  -16.73100 -23.11800 1.000 171.98232 ? 48  LYS   A NZ  1 
ATOM   91   N  N   . LYS   A 1 13  ? 31.74900  -12.93100 -21.57700 1.000 137.84739 ? 49  LYS   A N   1 
ATOM   92   C  CA  . LYS   A 1 13  ? 30.35900  -13.27000 -21.84500 1.000 132.90052 ? 49  LYS   A CA  1 
ATOM   93   C  C   . LYS   A 1 13  ? 30.21300  -14.77300 -21.67200 1.000 139.25385 ? 49  LYS   A C   1 
ATOM   94   O  O   . LYS   A 1 13  ? 30.90400  -15.55200 -22.34100 1.000 140.40161 ? 49  LYS   A O   1 
ATOM   95   C  CB  . LYS   A 1 13  ? 29.94700  -12.82500 -23.25300 1.000 125.64394 ? 49  LYS   A CB  1 
ATOM   96   C  CG  . LYS   A 1 13  ? 29.15400  -13.85100 -24.10400 1.000 129.03000 ? 49  LYS   A CG  1 
ATOM   97   C  CD  . LYS   A 1 13  ? 27.67800  -13.89900 -23.67900 1.000 134.29241 ? 49  LYS   A CD  1 
ATOM   98   C  CE  . LYS   A 1 13  ? 26.92900  -15.05300 -24.31400 1.000 144.07975 ? 49  LYS   A CE  1 
ATOM   99   N  NZ  . LYS   A 1 13  ? 27.38700  -16.28800 -23.64900 1.000 148.91626 ? 49  LYS   A NZ  1 
ATOM   100  N  N   . ILE   A 1 14  ? 29.31400  -15.17500 -20.77800 1.000 139.16146 ? 50  ILE   A N   1 
ATOM   101  C  CA  . ILE   A 1 14  ? 28.99700  -16.57400 -20.54900 1.000 141.40402 ? 50  ILE   A CA  1 
ATOM   102  C  C   . ILE   A 1 14  ? 27.51500  -16.85900 -20.70800 1.000 152.10267 ? 50  ILE   A C   1 
ATOM   103  O  O   . ILE   A 1 14  ? 27.10100  -18.01200 -20.55100 1.000 151.97260 ? 50  ILE   A O   1 
ATOM   104  C  CB  . ILE   A 1 14  ? 29.49100  -17.03700 -19.16200 1.000 134.41899 ? 50  ILE   A CB  1 
ATOM   105  C  CG1 . ILE   A 1 14  ? 28.54100  -16.57100 -18.05300 1.000 128.46176 ? 50  ILE   A CG1 1 
ATOM   106  C  CG2 . ILE   A 1 14  ? 30.92300  -16.53800 -18.90400 1.000 130.08101 ? 50  ILE   A CG2 1 
ATOM   107  C  CD1 . ILE   A 1 14  ? 28.87900  -17.16500 -16.67900 1.000 111.59970 ? 50  ILE   A CD1 1 
ATOM   108  N  N   . GLY   A 1 15  ? 26.71000  -15.84100 -21.04400 1.000 180.35218 ? 51  GLY   A N   1 
ATOM   109  C  CA  . GLY   A 1 15  ? 25.26100  -15.89200 -21.14300 1.000 180.15799 ? 51  GLY   A CA  1 
ATOM   110  C  C   . GLY   A 1 15  ? 24.64800  -17.16600 -21.65800 1.000 193.66250 ? 51  GLY   A C   1 
ATOM   111  O  O   . GLY   A 1 15  ? 24.99500  -17.65100 -22.73600 1.000 201.58124 ? 51  GLY   A O   1 
ATOM   112  N  N   . GLU   A 1 16  ? 23.75000  -17.72600 -20.85700 1.000 173.98739 ? 52  GLU   A N   1 
ATOM   113  C  CA  . GLU   A 1 16  ? 22.94500  -18.86900 -21.25900 1.000 175.78135 ? 52  GLU   A CA  1 
ATOM   114  C  C   . GLU   A 1 16  ? 21.47400  -18.61300 -20.95000 1.000 176.91115 ? 52  GLU   A C   1 
ATOM   115  O  O   . GLU   A 1 16  ? 20.80800  -17.85500 -21.66300 1.000 180.86575 ? 52  GLU   A O   1 
ATOM   116  C  CB  . GLU   A 1 16  ? 23.41600  -20.14000 -20.55100 1.000 166.85363 ? 52  GLU   A CB  1 
ATOM   117  C  CG  . GLU   A 1 16  ? 24.80100  -20.61800 -20.94500 1.000 172.14947 ? 52  GLU   A CG  1 
ATOM   118  C  CD  . GLU   A 1 16  ? 24.80300  -21.42600 -22.22900 1.000 177.15978 ? 52  GLU   A CD  1 
ATOM   119  O  OE1 . GLU   A 1 16  ? 24.53200  -20.84800 -23.30200 1.000 177.90514 ? 52  GLU   A OE1 1 
ATOM   120  O  OE2 . GLU   A 1 16  ? 25.07600  -22.64400 -22.16200 1.000 179.95929 ? 52  GLU   A OE2 1 
ATOM   121  N  N   . GLY   A 1 17  ? 20.96100  -19.25400 -19.90000 1.000 165.96786 ? 53  GLY   A N   1 
ATOM   122  C  CA  . GLY   A 1 17  ? 19.57700  -19.04600 -19.49900 1.000 169.28316 ? 53  GLY   A CA  1 
ATOM   123  C  C   . GLY   A 1 17  ? 18.61300  -19.36200 -20.62500 1.000 186.13127 ? 53  GLY   A C   1 
ATOM   124  O  O   . GLY   A 1 17  ? 18.83700  -20.26800 -21.43500 1.000 187.74229 ? 53  GLY   A O   1 
ATOM   125  N  N   . SER   A 1 18  ? 17.52000  -18.60900 -20.67900 1.000 188.56162 ? 54  SER   A N   1 
ATOM   126  C  CA  . SER   A 1 18  ? 16.59900  -18.65600 -21.81500 1.000 191.18263 ? 54  SER   A CA  1 
ATOM   127  C  C   . SER   A 1 18  ? 16.89300  -17.49600 -22.76400 1.000 197.41177 ? 54  SER   A C   1 
ATOM   128  O  O   . SER   A 1 18  ? 16.06000  -16.62400 -23.01600 1.000 198.52602 ? 54  SER   A O   1 
ATOM   129  C  CB  . SER   A 1 18  ? 15.15300  -18.63100 -21.32800 1.000 187.82688 ? 54  SER   A CB  1 
ATOM   130  O  OG  . SER   A 1 18  ? 14.90400  -19.70300 -20.43500 1.000 185.29313 ? 54  SER   A OG  1 
ATOM   131  N  N   . PHE   A 1 19  ? 18.12300  -17.50700 -23.27900 1.000 209.29400 ? 55  PHE   A N   1 
ATOM   132  C  CA  . PHE   A 1 19  ? 18.74000  -16.40900 -24.01800 1.000 210.32739 ? 55  PHE   A CA  1 
ATOM   133  C  C   . PHE   A 1 19  ? 18.91400  -15.15800 -23.16700 1.000 211.57615 ? 55  PHE   A C   1 
ATOM   134  O  O   . PHE   A 1 19  ? 19.23200  -14.08800 -23.70200 1.000 210.01474 ? 55  PHE   A O   1 
ATOM   135  C  CB  . PHE   A 1 19  ? 17.96700  -16.07400 -25.30200 1.000 206.91164 ? 55  PHE   A CB  1 
ATOM   136  C  CG  . PHE   A 1 19  ? 18.68700  -16.47000 -26.55900 1.000 206.13325 ? 55  PHE   A CG  1 
ATOM   137  C  CD1 . PHE   A 1 19  ? 18.73300  -17.79500 -26.95900 1.000 203.93224 ? 55  PHE   A CD1 1 
ATOM   138  C  CD2 . PHE   A 1 19  ? 19.32000  -15.51700 -27.34000 1.000 205.69220 ? 55  PHE   A CD2 1 
ATOM   139  C  CE1 . PHE   A 1 19  ? 19.39600  -18.16300 -28.11400 1.000 200.73100 ? 55  PHE   A CE1 1 
ATOM   140  C  CE2 . PHE   A 1 19  ? 19.98400  -15.87800 -28.49800 1.000 201.90348 ? 55  PHE   A CE2 1 
ATOM   141  C  CZ  . PHE   A 1 19  ? 20.02200  -17.20300 -28.88500 1.000 197.67884 ? 55  PHE   A CZ  1 
ATOM   142  N  N   . GLY   A 1 20  ? 18.71600  -15.26400 -21.85400 1.000 192.88856 ? 56  GLY   A N   1 
ATOM   143  C  CA  . GLY   A 1 20  ? 19.04000  -14.18300 -20.94800 1.000 179.04247 ? 56  GLY   A CA  1 
ATOM   144  C  C   . GLY   A 1 20  ? 20.52500  -13.89500 -20.97700 1.000 166.98384 ? 56  GLY   A C   1 
ATOM   145  O  O   . GLY   A 1 20  ? 21.34000  -14.81800 -20.90400 1.000 169.36773 ? 56  GLY   A O   1 
ATOM   146  N  N   . VAL   A 1 21  ? 20.89000  -12.62300 -21.09300 1.000 156.50168 ? 57  VAL   A N   1 
ATOM   147  C  CA  . VAL   A 1 21  ? 22.28400  -12.24600 -21.29800 1.000 152.69384 ? 57  VAL   A CA  1 
ATOM   148  C  C   . VAL   A 1 21  ? 23.00700  -12.26700 -19.95800 1.000 145.38770 ? 57  VAL   A C   1 
ATOM   149  O  O   . VAL   A 1 21  ? 22.70300  -11.46700 -19.06600 1.000 139.75280 ? 57  VAL   A O   1 
ATOM   150  C  CB  . VAL   A 1 21  ? 22.38600  -10.86900 -21.96300 1.000 151.59558 ? 57  VAL   A CB  1 
ATOM   151  C  CG1 . VAL   A 1 21  ? 23.73200  -10.70500 -22.64000 1.000 145.56228 ? 57  VAL   A CG1 1 
ATOM   152  C  CG2 . VAL   A 1 21  ? 21.25400  -10.68600 -22.96500 1.000 157.71483 ? 57  VAL   A CG2 1 
ATOM   153  N  N   . ILE   A 1 22  ? 23.96100  -13.18400 -19.81300 1.000 145.92525 ? 58  ILE   A N   1 
ATOM   154  C  CA  . ILE   A 1 22  ? 24.73700  -13.34700 -18.59100 1.000 135.35022 ? 58  ILE   A CA  1 
ATOM   155  C  C   . ILE   A 1 22  ? 26.19600  -13.05300 -18.90700 1.000 125.15296 ? 58  ILE   A C   1 
ATOM   156  O  O   . ILE   A 1 22  ? 26.71300  -13.47800 -19.94600 1.000 130.12531 ? 58  ILE   A O   1 
ATOM   157  C  CB  . ILE   A 1 22  ? 24.58600  -14.76400 -17.99900 1.000 136.67689 ? 58  ILE   A CB  1 
ATOM   158  C  CG1 . ILE   A 1 22  ? 23.18400  -15.31600 -18.27200 1.000 141.68229 ? 58  ILE   A CG1 1 
ATOM   159  C  CG2 . ILE   A 1 22  ? 24.92800  -14.75700 -16.52400 1.000 127.94902 ? 58  ILE   A CG2 1 
ATOM   160  C  CD1 . ILE   A 1 22  ? 22.08000  -14.67300 -17.45000 1.000 137.75615 ? 58  ILE   A CD1 1 
ATOM   161  N  N   . PHE   A 1 23  ? 26.86600  -12.33900 -18.00600 1.000 117.59806 ? 59  PHE   A N   1 
ATOM   162  C  CA  . PHE   A 1 23  ? 28.23700  -11.90600 -18.23200 1.000 121.93425 ? 59  PHE   A CA  1 
ATOM   163  C  C   . PHE   A 1 23  ? 29.08300  -12.11700 -16.98400 1.000 119.53231 ? 59  PHE   A C   1 
ATOM   164  O  O   . PHE   A 1 23  ? 28.58100  -12.09500 -15.85800 1.000 113.86231 ? 59  PHE   A O   1 
ATOM   165  C  CB  . PHE   A 1 23  ? 28.29400  -10.42500 -18.64300 1.000 121.58980 ? 59  PHE   A CB  1 
ATOM   166  C  CG  . PHE   A 1 23  ? 28.27900  -10.20500 -20.13000 1.000 121.59231 ? 59  PHE   A CG  1 
ATOM   167  C  CD1 . PHE   A 1 23  ? 27.14400  -10.47300 -20.87400 1.000 123.40811 ? 59  PHE   A CD1 1 
ATOM   168  C  CD2 . PHE   A 1 23  ? 29.40100  -9.71800  -20.78100 1.000 126.85498 ? 59  PHE   A CD2 1 
ATOM   169  C  CE1 . PHE   A 1 23  ? 27.13000  -10.26900 -22.24000 1.000 122.90629 ? 59  PHE   A CE1 1 
ATOM   170  C  CE2 . PHE   A 1 23  ? 29.39000  -9.50900  -22.14700 1.000 123.54805 ? 59  PHE   A CE2 1 
ATOM   171  C  CZ  . PHE   A 1 23  ? 28.25200  -9.78600  -22.87700 1.000 121.17169 ? 59  PHE   A CZ  1 
ATOM   172  N  N   . GLU   A 1 24  ? 30.37900  -12.32500 -17.20200 1.000 118.39958 ? 60  GLU   A N   1 
ATOM   173  C  CA  . GLU   A 1 24  ? 31.34300  -12.28400 -16.11400 1.000 114.15762 ? 60  GLU   A CA  1 
ATOM   174  C  C   . GLU   A 1 24  ? 31.68800  -10.83500 -15.80000 1.000 112.24671 ? 60  GLU   A C   1 
ATOM   175  O  O   . GLU   A 1 24  ? 31.75800  -9.99000  -16.69600 1.000 112.77933 ? 60  GLU   A O   1 
ATOM   176  C  CB  . GLU   A 1 24  ? 32.60800  -13.06600 -16.47800 1.000 118.41691 ? 60  GLU   A CB  1 
ATOM   177  C  CG  . GLU   A 1 24  ? 33.80200  -12.77700 -15.57500 1.000 119.90949 ? 60  GLU   A CG  1 
ATOM   178  C  CD  . GLU   A 1 24  ? 34.92400  -13.78100 -15.73700 1.000 125.85451 ? 60  GLU   A CD  1 
ATOM   179  O  OE1 . GLU   A 1 24  ? 34.79300  -14.69600 -16.57800 1.000 124.57804 ? 60  GLU   A OE1 1 
ATOM   180  O  OE2 . GLU   A 1 24  ? 35.93500  -13.65600 -15.01600 1.000 126.02547 ? 60  GLU   A OE2 1 
ATOM   181  N  N   . GLY   A 1 25  ? 31.87600  -10.54500 -14.51500 1.000 112.99926 ? 61  GLY   A N   1 
ATOM   182  C  CA  . GLY   A 1 25  ? 32.26800  -9.21900  -14.08000 1.000 109.74849 ? 61  GLY   A CA  1 
ATOM   183  C  C   . GLY   A 1 25  ? 33.23300  -9.29600  -12.92700 1.000 97.37315  ? 61  GLY   A C   1 
ATOM   184  O  O   . GLY   A 1 25  ? 33.54000  -10.37400 -12.41200 1.000 98.24773  ? 61  GLY   A O   1 
ATOM   185  N  N   . THR   A 1 26  ? 33.72400  -8.12600  -12.51300 1.000 99.38887  ? 62  THR   A N   1 
ATOM   186  C  CA  . THR   A 1 26  ? 34.61700  -8.03000  -11.37400 1.000 99.04157  ? 62  THR   A CA  1 
ATOM   187  C  C   . THR   A 1 26  ? 34.40000  -6.69300  -10.68700 1.000 93.69406  ? 62  THR   A C   1 
ATOM   188  O  O   . THR   A 1 26  ? 34.15800  -5.67700  -11.34600 1.000 94.67284  ? 62  THR   A O   1 
ATOM   189  C  CB  . THR   A 1 26  ? 36.08600  -8.18400  -11.78700 1.000 96.09057  ? 62  THR   A CB  1 
ATOM   190  O  OG1 . THR   A 1 26  ? 36.93800  -7.79900  -10.69900 1.000 94.30803  ? 62  THR   A OG1 1 
ATOM   191  C  CG2 . THR   A 1 26  ? 36.39300  -7.32700  -13.00200 1.000 103.77079 ? 62  THR   A CG2 1 
ATOM   192  N  N   . ASN   A 1 27  ? 34.48300  -6.70200  -9.36300  1.000 93.10937  ? 63  ASN   A N   1 
ATOM   193  C  CA  . ASN   A 1 27  ? 34.28700  -5.49200  -8.57400  1.000 98.96638  ? 63  ASN   A CA  1 
ATOM   194  C  C   . ASN   A 1 27  ? 35.61200  -4.74000  -8.48500  1.000 101.62463 ? 63  ASN   A C   1 
ATOM   195  O  O   . ASN   A 1 27  ? 36.56200  -5.21500  -7.85400  1.000 99.78902  ? 63  ASN   A O   1 
ATOM   196  C  CB  . ASN   A 1 27  ? 33.74400  -5.85300  -7.19400  1.000 91.30414  ? 63  ASN   A CB  1 
ATOM   197  C  CG  . ASN   A 1 27  ? 33.40900  -4.63600  -6.35800  1.000 96.66364  ? 63  ASN   A CG  1 
ATOM   198  O  OD1 . ASN   A 1 27  ? 34.28900  -3.85800  -5.99600  1.000 98.05240  ? 63  ASN   A OD1 1 
ATOM   199  N  ND2 . ASN   A 1 27  ? 32.13600  -4.48300  -6.01700  1.000 113.62214 ? 63  ASN   A ND2 1 
ATOM   200  N  N   . ILE   A 1 28  ? 35.67200  -3.55700  -9.10100  1.000 95.93348  ? 64  ILE   A N   1 
ATOM   201  C  CA  . ILE   A 1 28  ? 36.91600  -2.79700  -9.16300  1.000 99.42593  ? 64  ILE   A CA  1 
ATOM   202  C  C   . ILE   A 1 28  ? 37.34200  -2.23500  -7.81300  1.000 96.53590  ? 64  ILE   A C   1 
ATOM   203  O  O   . ILE   A 1 28  ? 38.47000  -1.75100  -7.67700  1.000 96.76166  ? 64  ILE   A O   1 
ATOM   204  C  CB  . ILE   A 1 28  ? 36.75900  -1.68500  -10.22100 1.000 97.54792  ? 64  ILE   A CB  1 
ATOM   205  C  CG1 . ILE   A 1 28  ? 36.17600  -2.26600  -11.50900 1.000 105.30293 ? 64  ILE   A CG1 1 
ATOM   206  C  CG2 . ILE   A 1 28  ? 38.09100  -1.02500  -10.54400 1.000 109.62088 ? 64  ILE   A CG2 1 
ATOM   207  C  CD1 . ILE   A 1 28  ? 34.71200  -1.91800  -11.71600 1.000 109.24813 ? 64  ILE   A CD1 1 
ATOM   208  N  N   . ILE   A 1 29  ? 36.47700  -2.29000  -6.80100  1.000 97.56706  ? 65  ILE   A N   1 
ATOM   209  C  CA  . ILE   A 1 29  ? 36.90300  -1.86900  -5.47000  1.000 100.26393 ? 65  ILE   A CA  1 
ATOM   210  C  C   . ILE   A 1 29  ? 37.71400  -2.96800  -4.78500  1.000 102.15083 ? 65  ILE   A C   1 
ATOM   211  O  O   . ILE   A 1 29  ? 38.65400  -2.67200  -4.03800  1.000 98.82741  ? 65  ILE   A O   1 
ATOM   212  C  CB  . ILE   A 1 29  ? 35.68900  -1.44900  -4.62000  1.000 108.16645 ? 65  ILE   A CB  1 
ATOM   213  C  CG1 . ILE   A 1 29  ? 34.90800  -0.33300  -5.31900  1.000 111.55175 ? 65  ILE   A CG1 1 
ATOM   214  C  CG2 . ILE   A 1 29  ? 36.11400  -0.99400  -3.22500  1.000 111.90968 ? 65  ILE   A CG2 1 
ATOM   215  C  CD1 . ILE   A 1 29  ? 35.68300  0.95900   -5.46700  1.000 109.37451 ? 65  ILE   A CD1 1 
ATOM   216  N  N   . ASN   A 1 30  ? 37.38400  -4.24500  -5.02500  1.000 102.78108 ? 66  ASN   A N   1 
ATOM   217  C  CA  . ASN   A 1 30  ? 38.09700  -5.33300  -4.36600  1.000 101.25470 ? 66  ASN   A CA  1 
ATOM   218  C  C   . ASN   A 1 30  ? 38.46300  -6.50600  -5.26900  1.000 95.59118  ? 66  ASN   A C   1 
ATOM   219  O  O   . ASN   A 1 30  ? 39.03300  -7.48000  -4.76900  1.000 98.65742  ? 66  ASN   A O   1 
ATOM   220  C  CB  . ASN   A 1 30  ? 37.28900  -5.85300  -3.16200  1.000 103.84187 ? 66  ASN   A CB  1 
ATOM   221  C  CG  . ASN   A 1 30  ? 35.90900  -6.32500  -3.54700  1.000 98.72936  ? 66  ASN   A CG  1 
ATOM   222  O  OD1 . ASN   A 1 30  ? 35.44500  -6.07400  -4.65600  1.000 96.89872  ? 66  ASN   A OD1 1 
ATOM   223  N  ND2 . ASN   A 1 30  ? 35.23600  -7.00500  -2.62600  1.000 102.76125 ? 66  ASN   A ND2 1 
ATOM   224  N  N   . GLY   A 1 31  ? 38.17000  -6.45300  -6.56700  1.000 97.31151  ? 67  GLY   A N   1 
ATOM   225  C  CA  . GLY   A 1 31  ? 38.60000  -7.49300  -7.48200  1.000 90.76578  ? 67  GLY   A CA  1 
ATOM   226  C  C   . GLY   A 1 31  ? 37.80700  -8.78300  -7.43900  1.000 97.11508  ? 67  GLY   A C   1 
ATOM   227  O  O   . GLY   A 1 31  ? 38.15400  -9.72400  -8.16500  1.000 94.30357  ? 67  GLY   A O   1 
ATOM   228  N  N   . VAL   A 1 32  ? 36.76200  -8.86000  -6.62700  1.000 99.62172  ? 68  VAL   A N   1 
ATOM   229  C  CA  . VAL   A 1 32  ? 35.97200  -10.09300 -6.52400  1.000 94.07838  ? 68  VAL   A CA  1 
ATOM   230  C  C   . VAL   A 1 32  ? 35.15400  -10.27800 -7.79900  1.000 88.96921  ? 68  VAL   A C   1 
ATOM   231  O  O   . VAL   A 1 32  ? 34.50200  -9.32300  -8.25700  1.000 85.79521  ? 68  VAL   A O   1 
ATOM   232  C  CB  . VAL   A 1 32  ? 35.06900  -10.04400 -5.28900  1.000 101.03223 ? 68  VAL   A CB  1 
ATOM   233  C  CG1 . VAL   A 1 32  ? 33.89700  -11.00400 -5.43800  1.000 96.31768  ? 68  VAL   A CG1 1 
ATOM   234  C  CG2 . VAL   A 1 32  ? 35.87100  -10.37600 -4.03800  1.000 100.44590 ? 68  VAL   A CG2 1 
ATOM   235  N  N   . PRO   A 1 33  ? 35.15600  -11.46400 -8.40500  1.000 99.52488  ? 69  PRO   A N   1 
ATOM   236  C  CA  . PRO   A 1 33  ? 34.35600  -11.67300 -9.61700  1.000 96.90562  ? 69  PRO   A CA  1 
ATOM   237  C  C   . PRO   A 1 33  ? 32.87100  -11.72900 -9.30000  1.000 95.05659  ? 69  PRO   A C   1 
ATOM   238  O  O   . PRO   A 1 33  ? 32.45900  -12.08200 -8.19200  1.000 96.73185  ? 69  PRO   A O   1 
ATOM   239  C  CB  . PRO   A 1 33  ? 34.85800  -13.02200 -10.15200 1.000 95.06730  ? 69  PRO   A CB  1 
ATOM   240  C  CG  . PRO   A 1 33  ? 36.10900  -13.33200 -9.37300  1.000 98.12828  ? 69  PRO   A CG  1 
ATOM   241  C  CD  . PRO   A 1 33  ? 35.94200  -12.65500 -8.05300  1.000 100.16736 ? 69  PRO   A CD  1 
ATOM   242  N  N   . VAL   A 1 34  ? 32.05900  -11.37200 -10.29600 1.000 88.74702  ? 70  VAL   A N   1 
ATOM   243  C  CA  . VAL   A 1 34  ? 30.60600  -11.36700 -10.17200 1.000 97.28136  ? 70  VAL   A CA  1 
ATOM   244  C  C   . VAL   A 1 34  ? 29.99700  -11.90600 -11.46300 1.000 99.52264  ? 70  VAL   A C   1 
ATOM   245  O  O   . VAL   A 1 34  ? 30.66800  -12.05000 -12.48500 1.000 98.62236  ? 70  VAL   A O   1 
ATOM   246  C  CB  . VAL   A 1 34  ? 30.04000  -9.96200  -9.86600  1.000 88.38916  ? 70  VAL   A CB  1 
ATOM   247  C  CG1 . VAL   A 1 34  ? 30.50800  -9.47600  -8.50000  1.000 94.02435  ? 70  VAL   A CG1 1 
ATOM   248  C  CG2 . VAL   A 1 34  ? 30.43700  -8.98000  -10.95300 1.000 86.76205  ? 70  VAL   A CG2 1 
ATOM   249  N  N   . ALA   A 1 35  ? 28.70200  -12.20500 -11.39600 1.000 96.16354  ? 71  ALA   A N   1 
ATOM   250  C  CA  . ALA   A 1 35  ? 27.93000  -12.68000 -12.54000 1.000 99.03843  ? 71  ALA   A CA  1 
ATOM   251  C  C   . ALA   A 1 35  ? 26.89200  -11.61700 -12.87800 1.000 100.46558 ? 71  ALA   A C   1 
ATOM   252  O  O   . ALA   A 1 35  ? 25.94700  -11.39900 -12.11200 1.000 106.33252 ? 71  ALA   A O   1 
ATOM   253  C  CB  . ALA   A 1 35  ? 27.27000  -14.02200 -12.23600 1.000 97.22706  ? 71  ALA   A CB  1 
ATOM   254  N  N   . ILE   A 1 36  ? 27.06700  -10.95900 -14.02100 1.000 106.11598 ? 72  ILE   A N   1 
ATOM   255  C  CA  . ILE   A 1 36  ? 26.21700  -9.85000  -14.43500 1.000 113.64257 ? 72  ILE   A CA  1 
ATOM   256  C  C   . ILE   A 1 36  ? 25.17200  -10.37000 -15.41100 1.000 114.59233 ? 72  ILE   A C   1 
ATOM   257  O  O   . ILE   A 1 36  ? 25.50700  -11.06200 -16.38100 1.000 119.09193 ? 72  ILE   A O   1 
ATOM   258  C  CB  . ILE   A 1 36  ? 27.04700  -8.72200  -15.07000 1.000 110.34985 ? 72  ILE   A CB  1 
ATOM   259  C  CG1 . ILE   A 1 36  ? 28.25300  -8.38300  -14.19300 1.000 108.81420 ? 72  ILE   A CG1 1 
ATOM   260  C  CG2 . ILE   A 1 36  ? 26.19200  -7.49000  -15.27100 1.000 114.93141 ? 72  ILE   A CG2 1 
ATOM   261  C  CD1 . ILE   A 1 36  ? 29.18500  -7.36300  -14.81700 1.000 106.90359 ? 72  ILE   A CD1 1 
ATOM   262  N  N   . LYS   A 1 37  ? 23.90900  -10.03700 -15.15900 1.000 117.48754 ? 73  LYS   A N   1 
ATOM   263  C  CA  . LYS   A 1 37  ? 22.79500  -10.46600 -15.99200 1.000 124.59085 ? 73  LYS   A CA  1 
ATOM   264  C  C   . LYS   A 1 37  ? 22.15100  -9.25300  -16.64600 1.000 136.78381 ? 73  LYS   A C   1 
ATOM   265  O  O   . LYS   A 1 37  ? 21.77500  -8.29800  -15.95500 1.000 127.89160 ? 73  LYS   A O   1 
ATOM   266  C  CB  . LYS   A 1 37  ? 21.75900  -11.23600 -15.17000 1.000 117.17421 ? 73  LYS   A CB  1 
ATOM   267  C  CG  . LYS   A 1 37  ? 20.57300  -11.73600 -15.97900 1.000 123.41114 ? 73  LYS   A CG  1 
ATOM   268  C  CD  . LYS   A 1 37  ? 19.67300  -12.62600 -15.13700 1.000 118.72794 ? 73  LYS   A CD  1 
ATOM   269  C  CE  . LYS   A 1 37  ? 18.52100  -13.19500 -15.95000 1.000 118.53139 ? 73  LYS   A CE  1 
ATOM   270  N  NZ  . LYS   A 1 37  ? 17.64500  -14.07500 -15.12500 1.000 115.66244 ? 73  LYS   A NZ  1 
ATOM   271  N  N   . PHE   A 1 38  ? 22.02900  -9.29200  -17.97000 1.000 139.07903 ? 74  PHE   A N   1 
ATOM   272  C  CA  . PHE   A 1 38  ? 21.40600  -8.21900  -18.72900 1.000 144.62029 ? 74  PHE   A CA  1 
ATOM   273  C  C   . PHE   A 1 38  ? 19.96400  -8.57800  -19.06700 1.000 158.70097 ? 74  PHE   A C   1 
ATOM   274  O  O   . PHE   A 1 38  ? 19.55200  -9.74000  -18.99900 1.000 154.39255 ? 74  PHE   A O   1 
ATOM   275  C  CB  . PHE   A 1 38  ? 22.17700  -7.92500  -20.01900 1.000 144.40104 ? 74  PHE   A CB  1 
ATOM   276  C  CG  . PHE   A 1 38  ? 23.48400  -7.20800  -19.81200 1.000 137.35248 ? 74  PHE   A CG  1 
ATOM   277  C  CD1 . PHE   A 1 38  ? 24.03200  -7.05200  -18.55100 1.000 129.57693 ? 74  PHE   A CD1 1 
ATOM   278  C  CD2 . PHE   A 1 38  ? 24.17100  -6.69600  -20.90000 1.000 137.68003 ? 74  PHE   A CD2 1 
ATOM   279  C  CE1 . PHE   A 1 38  ? 25.23700  -6.39200  -18.38700 1.000 131.97956 ? 74  PHE   A CE1 1 
ATOM   280  C  CE2 . PHE   A 1 38  ? 25.37000  -6.03600  -20.74000 1.000 138.39792 ? 74  PHE   A CE2 1 
ATOM   281  C  CZ  . PHE   A 1 38  ? 25.90300  -5.88600  -19.48000 1.000 137.89057 ? 74  PHE   A CZ  1 
ATOM   282  N  N   . GLU   A 1 39  ? 19.20200  -7.55600  -19.45500 1.000 198.83308 ? 75  GLU   A N   1 
ATOM   283  C  CA  . GLU   A 1 39  ? 17.80700  -7.71600  -19.84200 1.000 206.17572 ? 75  GLU   A CA  1 
ATOM   284  C  C   . GLU   A 1 39  ? 17.29200  -6.43200  -20.48000 1.000 209.57760 ? 75  GLU   A C   1 
ATOM   285  O  O   . GLU   A 1 39  ? 17.47200  -5.34500  -19.91700 1.000 207.73213 ? 75  GLU   A O   1 
ATOM   286  C  CB  . GLU   A 1 39  ? 16.94400  -8.08000  -18.63300 1.000 202.16729 ? 75  GLU   A CB  1 
ATOM   287  C  CG  . GLU   A 1 39  ? 15.52000  -8.46600  -18.98400 1.000 210.87255 ? 75  GLU   A CG  1 
ATOM   288  C  CD  . GLU   A 1 39  ? 14.55900  -8.23600  -17.83600 1.000 212.78701 ? 75  GLU   A CD  1 
ATOM   289  O  OE1 . GLU   A 1 39  ? 14.48500  -7.09200  -17.34100 1.000 210.15664 ? 75  GLU   A OE1 1 
ATOM   290  O  OE2 . GLU   A 1 39  ? 13.88200  -9.20000  -17.42100 1.000 217.44707 ? 75  GLU   A OE2 1 
ATOM   291  N  N   . PRO   A 1 40  ? 16.65100  -6.51100  -21.64500 1.000 181.28917 ? 76  PRO   A N   1 
ATOM   292  C  CA  . PRO   A 1 40  ? 16.08800  -5.30000  -22.25400 1.000 171.21183 ? 76  PRO   A CA  1 
ATOM   293  C  C   . PRO   A 1 40  ? 14.94800  -4.74300  -21.41700 1.000 170.36290 ? 76  PRO   A C   1 
ATOM   294  O  O   . PRO   A 1 40  ? 14.13000  -5.48800  -20.87200 1.000 174.42725 ? 76  PRO   A O   1 
ATOM   295  C  CB  . PRO   A 1 40  ? 15.59100  -5.78200  -23.62300 1.000 163.13648 ? 76  PRO   A CB  1 
ATOM   296  C  CG  . PRO   A 1 40  ? 16.29300  -7.08500  -23.86100 1.000 151.49283 ? 76  PRO   A CG  1 
ATOM   297  C  CD  . PRO   A 1 40  ? 16.48200  -7.69100  -22.50600 1.000 167.46151 ? 76  PRO   A CD  1 
ATOM   298  N  N   . ARG   A 1 41  ? 14.90600  -3.41300  -21.31300 1.000 153.18744 ? 77  ARG   A N   1 
ATOM   299  C  CA  . ARG   A 1 41  ? 13.83000  -2.76800  -20.56800 1.000 156.81769 ? 77  ARG   A CA  1 
ATOM   300  C  C   . ARG   A 1 41  ? 12.51700  -2.85800  -21.33000 1.000 158.12080 ? 77  ARG   A C   1 
ATOM   301  O  O   . ARG   A 1 41  ? 11.51300  -3.35000  -20.80300 1.000 157.68929 ? 77  ARG   A O   1 
ATOM   302  C  CB  . ARG   A 1 41  ? 14.18100  -1.30900  -20.28400 1.000 154.53899 ? 77  ARG   A CB  1 
ATOM   303  C  CG  . ARG   A 1 41  ? 15.66300  -1.03200  -20.22700 1.000 160.45509 ? 77  ARG   A CG  1 
ATOM   304  C  CD  . ARG   A 1 41  ? 15.92600  0.36800   -19.72300 1.000 162.24781 ? 77  ARG   A CD  1 
ATOM   305  N  NE  . ARG   A 1 41  ? 15.34500  0.54900   -18.40000 1.000 153.76809 ? 77  ARG   A NE  1 
ATOM   306  C  CZ  . ARG   A 1 41  ? 15.85200  0.03200   -17.28900 1.000 153.67277 ? 77  ARG   A CZ  1 
ATOM   307  N  NH1 . ARG   A 1 41  ? 16.95900  -0.69400  -17.30400 1.000 154.34025 ? 77  ARG   A NH1 1 
ATOM   308  N  NH2 . ARG   A 1 41  ? 15.22800  0.24200   -16.13400 1.000 153.92010 ? 77  ARG   A NH2 1 
ATOM   309  N  N   . LYS   A 1 42  ? 12.50600  -2.38000  -22.57500 1.000 154.24911 ? 78  LYS   A N   1 
ATOM   310  C  CA  . LYS   A 1 42  ? 11.32900  -2.48500  -23.43600 1.000 160.24601 ? 78  LYS   A CA  1 
ATOM   311  C  C   . LYS   A 1 42  ? 11.30300  -3.87300  -24.07500 1.000 171.84110 ? 78  LYS   A C   1 
ATOM   312  O  O   . LYS   A 1 42  ? 11.57300  -4.06700  -25.26200 1.000 177.13572 ? 78  LYS   A O   1 
ATOM   313  C  CB  . LYS   A 1 42  ? 11.32500  -1.37700  -24.48000 1.000 157.54115 ? 78  LYS   A CB  1 
ATOM   314  C  CG  . LYS   A 1 42  ? 10.82000  -0.04400  -23.95500 1.000 149.97208 ? 78  LYS   A CG  1 
ATOM   315  C  CD  . LYS   A 1 42  ? 9.42400   -0.18900  -23.36300 1.000 158.51517 ? 78  LYS   A CD  1 
ATOM   316  C  CE  . LYS   A 1 42  ? 8.42100   -0.66700  -24.40600 1.000 155.92765 ? 78  LYS   A CE  1 
ATOM   317  N  NZ  . LYS   A 1 42  ? 7.11100   -1.02500  -23.79500 1.000 155.42883 ? 78  LYS   A NZ  1 
ATOM   318  N  N   . THR   A 1 43  ? 10.97300  -4.85600  -23.24500 1.000 175.73747 ? 79  THR   A N   1 
ATOM   319  C  CA  . THR   A 1 43  ? 10.85600  -6.24400  -23.65900 1.000 181.49288 ? 79  THR   A CA  1 
ATOM   320  C  C   . THR   A 1 43  ? 9.42400   -6.71500  -23.45400 1.000 189.06234 ? 79  THR   A C   1 
ATOM   321  O  O   . THR   A 1 43  ? 8.59300   -6.02300  -22.86000 1.000 188.56095 ? 79  THR   A O   1 
ATOM   322  C  CB  . THR   A 1 43  ? 11.82400  -7.14300  -22.87800 1.000 184.42756 ? 79  THR   A CB  1 
ATOM   323  O  OG1 . THR   A 1 43  ? 11.77000  -8.47500  -23.40300 1.000 190.09518 ? 79  THR   A OG1 1 
ATOM   324  C  CG2 . THR   A 1 43  ? 11.44600  -7.17300  -21.40500 1.000 189.37167 ? 79  THR   A CG2 1 
ATOM   325  N  N   . GLU   A 1 44  ? 9.14100   -7.91200  -23.95800 1.000 195.00316 ? 80  GLU   A N   1 
ATOM   326  C  CA  . GLU   A 1 44  ? 7.82900   -8.52400  -23.80700 1.000 198.34597 ? 80  GLU   A CA  1 
ATOM   327  C  C   . GLU   A 1 44  ? 7.72500   -9.39800  -22.56500 1.000 201.85034 ? 80  GLU   A C   1 
ATOM   328  O  O   . GLU   A 1 44  ? 6.65400   -9.95700  -22.30600 1.000 204.23084 ? 80  GLU   A O   1 
ATOM   329  C  CB  . GLU   A 1 44  ? 7.48500   -9.35000  -25.05100 1.000 197.01566 ? 80  GLU   A CB  1 
ATOM   330  C  CG  . GLU   A 1 44  ? 8.43800   -10.50400 -25.32200 1.000 196.07215 ? 80  GLU   A CG  1 
ATOM   331  C  CD  . GLU   A 1 44  ? 9.15500   -10.37000 -26.65200 1.000 190.55213 ? 80  GLU   A CD  1 
ATOM   332  O  OE1 . GLU   A 1 44  ? 9.51100   -9.23300  -27.02600 1.000 186.63584 ? 80  GLU   A OE1 1 
ATOM   333  O  OE2 . GLU   A 1 44  ? 9.35500   -11.40100 -27.32700 1.000 186.98177 ? 80  GLU   A OE2 1 
ATOM   334  N  N   . ALA   A 1 45  ? 8.80000   -9.52600  -21.78800 1.000 215.51030 ? 81  ALA   A N   1 
ATOM   335  C  CA  . ALA   A 1 45  ? 8.80200   -10.36600 -20.59000 1.000 218.43825 ? 81  ALA   A CA  1 
ATOM   336  C  C   . ALA   A 1 45  ? 9.72000   -9.75700  -19.54600 1.000 224.61411 ? 81  ALA   A C   1 
ATOM   337  O  O   . ALA   A 1 45  ? 10.89700  -10.12500 -19.42900 1.000 227.37393 ? 81  ALA   A O   1 
ATOM   338  C  CB  . ALA   A 1 45  ? 9.22700   -11.79800 -20.91700 1.000 225.13703 ? 81  ALA   A CB  1 
ATOM   339  N  N   . PRO   A 1 46  ? 9.21800   -8.80500  -18.75600 1.000 193.93663 ? 82  PRO   A N   1 
ATOM   340  C  CA  . PRO   A 1 46  ? 10.01400  -8.25600  -17.65000 1.000 184.95437 ? 82  PRO   A CA  1 
ATOM   341  C  C   . PRO   A 1 46  ? 10.05300  -9.23200  -16.48100 1.000 175.30118 ? 82  PRO   A C   1 
ATOM   342  O  O   . PRO   A 1 46  ? 9.01400   -9.73000  -16.03900 1.000 167.54412 ? 82  PRO   A O   1 
ATOM   343  C  CB  . PRO   A 1 46  ? 9.27100   -6.96500  -17.27600 1.000 177.67457 ? 82  PRO   A CB  1 
ATOM   344  C  CG  . PRO   A 1 46  ? 8.30500   -6.71200  -18.41000 1.000 178.09349 ? 82  PRO   A CG  1 
ATOM   345  C  CD  . PRO   A 1 46  ? 7.96000   -8.06300  -18.94600 1.000 186.41718 ? 82  PRO   A CD  1 
ATOM   346  N  N   . GLN   A 1 47  ? 11.25800  -9.50200  -15.97600 1.000 166.67719 ? 83  GLN   A N   1 
ATOM   347  C  CA  . GLN   A 1 47  ? 11.41900  -10.47800 -14.90300 1.000 158.59883 ? 83  GLN   A CA  1 
ATOM   348  C  C   . GLN   A 1 47  ? 12.58100  -10.13000 -13.97900 1.000 155.27685 ? 83  GLN   A C   1 
ATOM   349  O  O   . GLN   A 1 47  ? 12.54800  -10.45500 -12.78800 1.000 146.72692 ? 83  GLN   A O   1 
ATOM   350  C  CB  . GLN   A 1 47  ? 11.62800  -11.87900 -15.48500 1.000 154.54115 ? 83  GLN   A CB  1 
ATOM   351  C  CG  . GLN   A 1 47  ? 12.98800  -12.07600 -16.14200 1.000 157.71011 ? 83  GLN   A CG  1 
ATOM   352  C  CD  . GLN   A 1 47  ? 13.17500  -13.46200 -16.72600 1.000 142.07323 ? 83  GLN   A CD  1 
ATOM   353  O  OE1 . GLN   A 1 47  ? 12.35500  -14.35600 -16.51600 1.000 140.62616 ? 83  GLN   A OE1 1 
ATOM   354  N  NE2 . GLN   A 1 47  ? 14.26000  -13.64500 -17.46900 1.000 127.17204 ? 83  GLN   A NE2 1 
ATOM   355  N  N   . LEU   A 1 48  ? 13.61200  -9.47300  -14.51900 1.000 155.06660 ? 84  LEU   A N   1 
ATOM   356  C  CA  . LEU   A 1 48  ? 14.83200  -9.23100  -13.75800 1.000 150.58688 ? 84  LEU   A CA  1 
ATOM   357  C  C   . LEU   A 1 48  ? 14.59600  -8.33500  -12.55000 1.000 140.37325 ? 84  LEU   A C   1 
ATOM   358  O  O   . LEU   A 1 48  ? 15.38900  -8.37000  -11.60400 1.000 137.23097 ? 84  LEU   A O   1 
ATOM   359  C  CB  . LEU   A 1 48  ? 15.90100  -8.61900  -14.66500 1.000 154.67932 ? 84  LEU   A CB  1 
ATOM   360  C  CG  . LEU   A 1 48  ? 17.33400  -8.69400  -14.13900 1.000 139.59796 ? 84  LEU   A CG  1 
ATOM   361  C  CD1 . LEU   A 1 48  ? 17.58400  -10.06800 -13.54700 1.000 129.77670 ? 84  LEU   A CD1 1 
ATOM   362  C  CD2 . LEU   A 1 48  ? 18.32200  -8.40400  -15.25700 1.000 140.01219 ? 84  LEU   A CD2 1 
ATOM   363  N  N   . ARG   A 1 49  ? 13.53200  -7.53200  -12.57100 1.000 141.41276 ? 85  ARG   A N   1 
ATOM   364  C  CA  . ARG   A 1 49  ? 13.18800  -6.70400  -11.42200 1.000 140.62062 ? 85  ARG   A CA  1 
ATOM   365  C  C   . ARG   A 1 49  ? 12.85400  -7.56600  -10.21000 1.000 133.42151 ? 85  ARG   A C   1 
ATOM   366  O  O   . ARG   A 1 49  ? 13.40500  -7.36800  -9.12100  1.000 128.19502 ? 85  ARG   A O   1 
ATOM   367  C  CB  . ARG   A 1 49  ? 12.01700  -5.79400  -11.79300 1.000 143.43892 ? 85  ARG   A CB  1 
ATOM   368  C  CG  . ARG   A 1 49  ? 11.51400  -4.89800  -10.68300 1.000 140.87458 ? 85  ARG   A CG  1 
ATOM   369  C  CD  . ARG   A 1 49  ? 10.24300  -4.20800  -11.13400 1.000 143.08186 ? 85  ARG   A CD  1 
ATOM   370  N  NE  . ARG   A 1 49  ? 10.45000  -3.43100  -12.34900 1.000 145.10287 ? 85  ARG   A NE  1 
ATOM   371  C  CZ  . ARG   A 1 49  ? 10.90300  -2.18600  -12.37100 1.000 150.17936 ? 85  ARG   A CZ  1 
ATOM   372  N  NH1 . ARG   A 1 49  ? 11.22000  -1.54300  -11.25700 1.000 151.05097 ? 85  ARG   A NH1 1 
ATOM   373  N  NH2 . ARG   A 1 49  ? 11.04300  -1.56900  -13.53900 1.000 155.03397 ? 85  ARG   A NH2 1 
ATOM   374  N  N   . ASP   A 1 50  ? 11.96700  -8.54700  -10.38900 1.000 133.53135 ? 86  ASP   A N   1 
ATOM   375  C  CA  . ASP   A 1 50  ? 11.51700  -9.36800  -9.27100  1.000 132.65915 ? 86  ASP   A CA  1 
ATOM   376  C  C   . ASP   A 1 50  ? 12.54900  -10.40800 -8.85800  1.000 134.50679 ? 86  ASP   A C   1 
ATOM   377  O  O   . ASP   A 1 50  ? 12.55600  -10.83500 -7.69800  1.000 131.90379 ? 86  ASP   A O   1 
ATOM   378  C  CB  . ASP   A 1 50  ? 10.19400  -10.04900 -9.62000  1.000 135.91397 ? 86  ASP   A CB  1 
ATOM   379  C  CG  . ASP   A 1 50  ? 9.02400   -9.08300  -9.61300  1.000 141.39888 ? 86  ASP   A CG  1 
ATOM   380  O  OD1 . ASP   A 1 50  ? 9.22100   -7.91100  -9.22500  1.000 136.05031 ? 86  ASP   A OD1 1 
ATOM   381  O  OD2 . ASP   A 1 50  ? 7.90800   -9.49600  -9.99700  1.000 149.95539 ? 86  ASP   A OD2 1 
ATOM   382  N  N   . GLU   A 1 51  ? 13.41700  -10.83600 -9.77800  1.000 134.68208 ? 87  GLU   A N   1 
ATOM   383  C  CA  . GLU   A 1 51  ? 14.48600  -11.75200 -9.39200  1.000 132.33587 ? 87  GLU   A CA  1 
ATOM   384  C  C   . GLU   A 1 51  ? 15.47800  -11.07800 -8.45500  1.000 127.65725 ? 87  GLU   A C   1 
ATOM   385  O  O   . GLU   A 1 51  ? 16.02700  -11.72900 -7.55800  1.000 123.57866 ? 87  GLU   A O   1 
ATOM   386  C  CB  . GLU   A 1 51  ? 15.20200  -12.28700 -10.63400 1.000 135.62775 ? 87  GLU   A CB  1 
ATOM   387  C  CG  . GLU   A 1 51  ? 16.16100  -13.43300 -10.34900 1.000 132.21422 ? 87  GLU   A CG  1 
ATOM   388  C  CD  . GLU   A 1 51  ? 16.63400  -14.13200 -11.61000 1.000 133.76614 ? 87  GLU   A CD  1 
ATOM   389  O  OE1 . GLU   A 1 51  ? 17.32200  -13.48900 -12.43100 1.000 135.44927 ? 87  GLU   A OE1 1 
ATOM   390  O  OE2 . GLU   A 1 51  ? 16.30900  -15.32600 -11.78200 1.000 134.80413 ? 87  GLU   A OE2 1 
ATOM   391  N  N   . TYR   A 1 52  ? 15.71300  -9.77800  -8.65100  1.000 126.66086 ? 88  TYR   A N   1 
ATOM   392  C  CA  . TYR   A 1 52  ? 16.54700  -9.01400  -7.73200  1.000 118.94220 ? 88  TYR   A CA  1 
ATOM   393  C  C   . TYR   A 1 52  ? 15.96200  -9.02000  -6.32700  1.000 124.22649 ? 88  TYR   A C   1 
ATOM   394  O  O   . TYR   A 1 52  ? 16.69100  -9.19000  -5.34200  1.000 113.64916 ? 88  TYR   A O   1 
ATOM   395  C  CB  . TYR   A 1 52  ? 16.70000  -7.58800  -8.26000  1.000 124.23170 ? 88  TYR   A CB  1 
ATOM   396  C  CG  . TYR   A 1 52  ? 17.34200  -6.60100  -7.31300  1.000 123.89946 ? 88  TYR   A CG  1 
ATOM   397  C  CD1 . TYR   A 1 52  ? 18.67500  -6.71400  -6.94900  1.000 116.49259 ? 88  TYR   A CD1 1 
ATOM   398  C  CD2 . TYR   A 1 52  ? 16.61300  -5.52900  -6.81300  1.000 125.75781 ? 88  TYR   A CD2 1 
ATOM   399  C  CE1 . TYR   A 1 52  ? 19.26200  -5.79200  -6.09800  1.000 121.11208 ? 88  TYR   A CE1 1 
ATOM   400  C  CE2 . TYR   A 1 52  ? 17.18600  -4.60600  -5.96600  1.000 122.22916 ? 88  TYR   A CE2 1 
ATOM   401  C  CZ  . TYR   A 1 52  ? 18.51700  -4.74700  -5.61300  1.000 128.81766 ? 88  TYR   A CZ  1 
ATOM   402  O  OH  . TYR   A 1 52  ? 19.09700  -3.82900  -4.76300  1.000 136.20570 ? 88  TYR   A OH  1 
ATOM   403  N  N   . ARG   A 1 53  ? 14.64300  -8.85500  -6.21500  1.000 120.01540 ? 89  ARG   A N   1 
ATOM   404  C  CA  . ARG   A 1 53  ? 14.00400  -8.88800  -4.90600  1.000 120.82518 ? 89  ARG   A CA  1 
ATOM   405  C  C   . ARG   A 1 53  ? 14.00600  -10.29200 -4.31900  1.000 114.73352 ? 89  ARG   A C   1 
ATOM   406  O  O   . ARG   A 1 53  ? 13.95600  -10.44900 -3.09400  1.000 115.57751 ? 89  ARG   A O   1 
ATOM   407  C  CB  . ARG   A 1 53  ? 12.57600  -8.35300  -5.00900  1.000 131.08151 ? 89  ARG   A CB  1 
ATOM   408  C  CG  . ARG   A 1 53  ? 12.36600  -7.39600  -6.17000  1.000 129.35143 ? 89  ARG   A CG  1 
ATOM   409  C  CD  . ARG   A 1 53  ? 11.11600  -6.55900  -5.98700  1.000 137.49751 ? 89  ARG   A CD  1 
ATOM   410  N  NE  . ARG   A 1 53  ? 10.96900  -5.55000  -7.03000  1.000 141.43796 ? 89  ARG   A NE  1 
ATOM   411  C  CZ  . ARG   A 1 53  ? 10.50700  -4.32500  -6.82000  1.000 150.78012 ? 89  ARG   A CZ  1 
ATOM   412  N  NH1 . ARG   A 1 53  ? 10.18200  -3.90800  -5.61200  1.000 145.92441 ? 89  ARG   A NH1 1 
ATOM   413  N  NH2 . ARG   A 1 53  ? 10.37000  -3.49600  -7.84800  1.000 150.11919 ? 89  ARG   A NH2 1 
ATOM   414  N  N   . THR   A 1 54  ? 14.07500  -11.32000 -5.16900  1.000 118.29388 ? 90  THR   A N   1 
ATOM   415  C  CA  . THR   A 1 54  ? 14.06900  -12.69200 -4.67300  1.000 119.82842 ? 90  THR   A CA  1 
ATOM   416  C  C   . THR   A 1 54  ? 15.36900  -13.02600 -3.95100  1.000 112.75888 ? 90  THR   A C   1 
ATOM   417  O  O   . THR   A 1 54  ? 15.34700  -13.65400 -2.88600  1.000 107.97238 ? 90  THR   A O   1 
ATOM   418  C  CB  . THR   A 1 54  ? 13.83300  -13.66800 -5.82500  1.000 117.47412 ? 90  THR   A CB  1 
ATOM   419  O  OG1 . THR   A 1 54  ? 12.82900  -13.14000 -6.69900  1.000 121.53886 ? 90  THR   A OG1 1 
ATOM   420  C  CG2 . THR   A 1 54  ? 13.36500  -15.01500 -5.29100  1.000 103.71954 ? 90  THR   A CG2 1 
ATOM   421  N  N   . TYR   A 1 55  ? 16.51000  -12.62200 -4.51500  1.000 115.63005 ? 91  TYR   A N   1 
ATOM   422  C  CA  . TYR   A 1 55  ? 17.79000  -12.87700 -3.86000  1.000 114.13632 ? 91  TYR   A CA  1 
ATOM   423  C  C   . TYR   A 1 55  ? 17.88600  -12.13000 -2.53800  1.000 114.62283 ? 91  TYR   A C   1 
ATOM   424  O  O   . TYR   A 1 55  ? 18.43500  -12.65100 -1.55900  1.000 112.67100 ? 91  TYR   A O   1 
ATOM   425  C  CB  . TYR   A 1 55  ? 18.94500  -12.48200 -4.78200  1.000 108.22440 ? 91  TYR   A CB  1 
ATOM   426  C  CG  . TYR   A 1 55  ? 19.16800  -13.42000 -5.94900  1.000 105.53398 ? 91  TYR   A CG  1 
ATOM   427  C  CD1 . TYR   A 1 55  ? 19.74200  -14.67000 -5.76100  1.000 109.71504 ? 91  TYR   A CD1 1 
ATOM   428  C  CD2 . TYR   A 1 55  ? 18.82200  -13.04600 -7.24100  1.000 109.58084 ? 91  TYR   A CD2 1 
ATOM   429  C  CE1 . TYR   A 1 55  ? 19.95300  -15.52800 -6.82500  1.000 100.09335 ? 91  TYR   A CE1 1 
ATOM   430  C  CE2 . TYR   A 1 55  ? 19.03100  -13.89700 -8.31100  1.000 113.79630 ? 91  TYR   A CE2 1 
ATOM   431  C  CZ  . TYR   A 1 55  ? 19.59600  -15.13600 -8.09800  1.000 101.06473 ? 91  TYR   A CZ  1 
ATOM   432  O  OH  . TYR   A 1 55  ? 19.80700  -15.98700 -9.15900  1.000 104.92012 ? 91  TYR   A OH  1 
ATOM   433  N  N   . LYS   A 1 56  ? 17.36100  -10.90200 -2.49200  1.000 120.51540 ? 92  LYS   A N   1 
ATOM   434  C  CA  . LYS   A 1 56  ? 17.35000  -10.14700 -1.24300  1.000 124.68442 ? 92  LYS   A CA  1 
ATOM   435  C  C   . LYS   A 1 56  ? 16.51100  -10.84600 -0.18000  1.000 126.55823 ? 92  LYS   A C   1 
ATOM   436  O  O   . LYS   A 1 56  ? 16.86700  -10.83600 1.00400   1.000 129.02173 ? 92  LYS   A O   1 
ATOM   437  C  CB  . LYS   A 1 56  ? 16.82700  -8.73200  -1.48600  1.000 125.00975 ? 92  LYS   A CB  1 
ATOM   438  C  CG  . LYS   A 1 56  ? 17.81100  -7.80100  -2.17700  1.000 127.46749 ? 92  LYS   A CG  1 
ATOM   439  C  CD  . LYS   A 1 56  ? 19.09800  -7.61300  -1.38600  1.000 127.34450 ? 92  LYS   A CD  1 
ATOM   440  C  CE  . LYS   A 1 56  ? 19.63500  -6.21400  -1.59600  1.000 130.83165 ? 92  LYS   A CE  1 
ATOM   441  N  NZ  . LYS   A 1 56  ? 19.31600  -5.67800  -2.93300  1.000 129.78582 ? 92  LYS   A NZ  1 
ATOM   442  N  N   . HIS   A 1 57  ? 15.39000  -11.45300 -0.58200  1.000 118.63389 ? 93  HIS   A N   1 
ATOM   443  C  CA  . HIS   A 1 57  ? 14.54700  -12.16600 0.37500   1.000 114.12021 ? 93  HIS   A CA  1 
ATOM   444  C  C   . HIS   A 1 57  ? 15.27700  -13.36900 0.95900   1.000 112.61400 ? 93  HIS   A C   1 
ATOM   445  O  O   . HIS   A 1 57  ? 15.16100  -13.65500 2.15600   1.000 112.02908 ? 93  HIS   A O   1 
ATOM   446  C  CB  . HIS   A 1 57  ? 13.24300  -12.59800 -0.30000  1.000 111.68817 ? 93  HIS   A CB  1 
ATOM   447  C  CG  . HIS   A 1 57  ? 12.16000  -12.99800 0.65700   1.000 114.06297 ? 93  HIS   A CG  1 
ATOM   448  N  ND1 . HIS   A 1 57  ? 12.41600  -13.48100 1.92300   1.000 112.25964 ? 93  HIS   A ND1 1 
ATOM   449  C  CD2 . HIS   A 1 57  ? 10.81200  -12.98500 0.52800   1.000 113.42991 ? 93  HIS   A CD2 1 
ATOM   450  C  CE1 . HIS   A 1 57  ? 11.27400  -13.74800 2.53100   1.000 114.28971 ? 93  HIS   A CE1 1 
ATOM   451  N  NE2 . HIS   A 1 57  ? 10.28500  -13.45600 1.70600   1.000 118.18714 ? 93  HIS   A NE2 1 
ATOM   452  N  N   . LEU   A 1 58  ? 16.03000  -14.08700 0.12800   1.000 114.39557 ? 94  LEU   A N   1 
ATOM   453  C  CA  . LEU   A 1 58  ? 16.81100  -15.23600 0.56300   1.000 117.19974 ? 94  LEU   A CA  1 
ATOM   454  C  C   . LEU   A 1 58  ? 18.24400  -14.86300 0.92400   1.000 119.91270 ? 94  LEU   A C   1 
ATOM   455  O  O   . LEU   A 1 58  ? 19.10200  -15.74900 1.01100   1.000 122.03349 ? 94  LEU   A O   1 
ATOM   456  C  CB  . LEU   A 1 58  ? 16.80500  -16.31300 -0.52400  1.000 111.04126 ? 94  LEU   A CB  1 
ATOM   457  C  CG  . LEU   A 1 58  ? 15.42000  -16.74100 -1.01400  1.000 106.50376 ? 94  LEU   A CG  1 
ATOM   458  C  CD1 . LEU   A 1 58  ? 15.43700  -16.99600 -2.51200  1.000 99.30755  ? 94  LEU   A CD1 1 
ATOM   459  C  CD2 . LEU   A 1 58  ? 14.94400  -17.97600 -0.26500  1.000 93.15341  ? 94  LEU   A CD2 1 
ATOM   460  N  N   . GLN   A 1 59  ? 18.51800  -13.57500 1.12900   1.000 121.38413 ? 95  GLN   A N   1 
ATOM   461  C  CA  . GLN   A 1 59  ? 19.86500  -13.12800 1.45700   1.000 128.83747 ? 95  GLN   A CA  1 
ATOM   462  C  C   . GLN   A 1 59  ? 20.34500  -13.76200 2.75700   1.000 130.20576 ? 95  GLN   A C   1 
ATOM   463  O  O   . GLN   A 1 59  ? 19.57800  -13.92600 3.70900   1.000 129.86384 ? 95  GLN   A O   1 
ATOM   464  C  CB  . GLN   A 1 59  ? 19.89900  -11.59800 1.55900   1.000 133.24892 ? 95  GLN   A CB  1 
ATOM   465  C  CG  . GLN   A 1 59  ? 20.93200  -11.02900 2.52700   1.000 135.33018 ? 95  GLN   A CG  1 
ATOM   466  C  CD  . GLN   A 1 59  ? 20.38300  -10.84500 3.93300   1.000 142.58119 ? 95  GLN   A CD  1 
ATOM   467  O  OE1 . GLN   A 1 59  ? 19.17700  -10.68600 4.12500   1.000 144.16059 ? 95  GLN   A OE1 1 
ATOM   468  N  NE2 . GLN   A 1 59  ? 21.26800  -10.87300 4.92200   1.000 139.44875 ? 95  GLN   A NE2 1 
ATOM   469  N  N   . GLY   A 1 60  ? 21.62600  -14.12700 2.78600   1.000 124.88039 ? 96  GLY   A N   1 
ATOM   470  C  CA  . GLY   A 1 60  ? 22.23900  -14.69000 3.96700   1.000 124.11704 ? 96  GLY   A CA  1 
ATOM   471  C  C   . GLY   A 1 60  ? 22.14800  -16.19400 4.08700   1.000 120.58677 ? 96  GLY   A C   1 
ATOM   472  O  O   . GLY   A 1 60  ? 22.86600  -16.77700 4.91000   1.000 124.61911 ? 96  GLY   A O   1 
ATOM   473  N  N   . CYS   A 1 61  ? 21.29500  -16.84300 3.30100   1.000 116.53168 ? 97  CYS   A N   1 
ATOM   474  C  CA  . CYS   A 1 61  ? 21.16400  -18.28900 3.36300   1.000 113.44295 ? 97  CYS   A CA  1 
ATOM   475  C  C   . CYS   A 1 61  ? 22.27700  -18.96400 2.57000   1.000 111.54506 ? 97  CYS   A C   1 
ATOM   476  O  O   . CYS   A 1 61  ? 22.74500  -18.44800 1.55000   1.000 103.76145 ? 97  CYS   A O   1 
ATOM   477  C  CB  . CYS   A 1 61  ? 19.80000  -18.72700 2.83000   1.000 109.46949 ? 97  CYS   A CB  1 
ATOM   478  S  SG  . CYS   A 1 61  ? 18.40300  -18.08800 3.77800   1.000 115.31071 ? 97  CYS   A SG  1 
ATOM   479  N  N   . ASP   A 1 62  ? 22.70200  -20.12900 3.05400   1.000 113.82977 ? 98  ASP   A N   1 
ATOM   480  C  CA  . ASP   A 1 62  ? 23.75700  -20.87500 2.38400   1.000 102.51897 ? 98  ASP   A CA  1 
ATOM   481  C  C   . ASP   A 1 62  ? 23.26600  -21.39700 1.03900   1.000 95.56368  ? 98  ASP   A C   1 
ATOM   482  O  O   . ASP   A 1 62  ? 22.18300  -21.98300 0.94300   1.000 98.59956  ? 98  ASP   A O   1 
ATOM   483  C  CB  . ASP   A 1 62  ? 24.24000  -22.02900 3.26300   1.000 103.19393 ? 98  ASP   A CB  1 
ATOM   484  C  CG  . ASP   A 1 62  ? 23.11900  -22.67400 4.06100   1.000 114.20350 ? 98  ASP   A CG  1 
ATOM   485  O  OD1 . ASP   A 1 62  ? 22.03600  -22.92400 3.49100   1.000 111.71607 ? 98  ASP   A OD1 1 
ATOM   486  O  OD2 . ASP   A 1 62  ? 23.32700  -22.94700 5.26300   1.000 118.23444 ? 98  ASP   A OD2 1 
ATOM   487  N  N   . GLY   A 1 63  ? 24.06000  -21.17100 -0.00400  1.000 93.62877  ? 99  GLY   A N   1 
ATOM   488  C  CA  . GLY   A 1 63  ? 23.71500  -21.61400 -1.33600  1.000 92.96780  ? 99  GLY   A CA  1 
ATOM   489  C  C   . GLY   A 1 63  ? 22.96900  -20.60400 -2.18200  1.000 88.58863  ? 99  GLY   A C   1 
ATOM   490  O  O   . GLY   A 1 63  ? 22.60000  -20.92900 -3.31900  1.000 90.36540  ? 99  GLY   A O   1 
ATOM   491  N  N   . ILE   A 1 64  ? 22.73400  -19.40200 -1.67300  1.000 89.51558  ? 100 ILE   A N   1 
ATOM   492  C  CA  . ILE   A 1 64  ? 22.06200  -18.34100 -2.41800  1.000 90.03892  ? 100 ILE   A CA  1 
ATOM   493  C  C   . ILE   A 1 64  ? 23.04600  -17.19900 -2.60200  1.000 85.77881  ? 100 ILE   A C   1 
ATOM   494  O  O   . ILE   A 1 64  ? 23.54000  -16.64000 -1.61800  1.000 88.41037  ? 100 ILE   A O   1 
ATOM   495  C  CB  . ILE   A 1 64  ? 20.78600  -17.85200 -1.70900  1.000 96.44895  ? 100 ILE   A CB  1 
ATOM   496  C  CG1 . ILE   A 1 64  ? 19.74100  -18.96700 -1.66200  1.000 96.95300  ? 100 ILE   A CG1 1 
ATOM   497  C  CG2 . ILE   A 1 64  ? 20.23400  -16.62000 -2.41000  1.000 95.95554  ? 100 ILE   A CG2 1 
ATOM   498  C  CD1 . ILE   A 1 64  ? 19.40800  -19.54700 -3.01900  1.000 92.83028  ? 100 ILE   A CD1 1 
ATOM   499  N  N   . PRO   A 1 65  ? 23.37000  -16.80600 -3.83400  1.000 86.62189  ? 101 PRO   A N   1 
ATOM   500  C  CA  . PRO   A 1 65  ? 24.31400  -15.70400 -4.02900  1.000 97.84601  ? 101 PRO   A CA  1 
ATOM   501  C  C   . PRO   A 1 65  ? 23.74400  -14.38300 -3.53900  1.000 101.05387 ? 101 PRO   A C   1 
ATOM   502  O  O   . PRO   A 1 65  ? 22.53400  -14.14600 -3.57600  1.000 96.85675  ? 101 PRO   A O   1 
ATOM   503  C  CB  . PRO   A 1 65  ? 24.53300  -15.68800 -5.54600  1.000 97.73574  ? 101 PRO   A CB  1 
ATOM   504  C  CG  . PRO   A 1 65  ? 23.30800  -16.32200 -6.11000  1.000 94.22119  ? 101 PRO   A CG  1 
ATOM   505  C  CD  . PRO   A 1 65  ? 22.88200  -17.35600 -5.11000  1.000 92.20183  ? 101 PRO   A CD  1 
ATOM   506  N  N   . ASN   A 1 66  ? 24.64100  -13.51800 -3.07200  1.000 98.01047  ? 102 ASN   A N   1 
ATOM   507  C  CA  . ASN   A 1 66  ? 24.24200  -12.22800 -2.52900  1.000 100.76854 ? 102 ASN   A CA  1 
ATOM   508  C  C   . ASN   A 1 66  ? 23.92300  -11.25200 -3.65300  1.000 103.75779 ? 102 ASN   A C   1 
ATOM   509  O  O   . ASN   A 1 66  ? 24.69300  -11.11600 -4.60800  1.000 103.71126 ? 102 ASN   A O   1 
ATOM   510  C  CB  . ASN   A 1 66  ? 25.34400  -11.65700 -1.63700  1.000 100.52115 ? 102 ASN   A CB  1 
ATOM   511  C  CG  . ASN   A 1 66  ? 25.37400  -12.29800 -0.26600  1.000 102.27518 ? 102 ASN   A CG  1 
ATOM   512  O  OD1 . ASN   A 1 66  ? 24.37700  -12.85400 0.19100   1.000 110.15788 ? 102 ASN   A OD1 1 
ATOM   513  N  ND2 . ASN   A 1 66  ? 26.52000  -12.21700 0.40200   1.000 103.28488 ? 102 ASN   A ND2 1 
ATOM   514  N  N   . ALA   A 1 67  ? 22.78300  -10.57400 -3.53600  1.000 104.33328 ? 103 ALA   A N   1 
ATOM   515  C  CA  . ALA   A 1 67  ? 22.40500  -9.53600  -4.48600  1.000 105.76896 ? 103 ALA   A CA  1 
ATOM   516  C  C   . ALA   A 1 67  ? 23.17000  -8.26000  -4.16200  1.000 105.14926 ? 103 ALA   A C   1 
ATOM   517  O  O   . ALA   A 1 67  ? 23.10700  -7.76000  -3.03300  1.000 112.10574 ? 103 ALA   A O   1 
ATOM   518  C  CB  . ALA   A 1 67  ? 20.89800  -9.29200  -4.44400  1.000 114.54894 ? 103 ALA   A CB  1 
ATOM   519  N  N   . TYR   A 1 68  ? 23.89500  -7.73600  -5.14700  1.000 104.67175 ? 104 TYR   A N   1 
ATOM   520  C  CA  . TYR   A 1 68  ? 24.74600  -6.57200  -4.94200  1.000 110.56642 ? 104 TYR   A CA  1 
ATOM   521  C  C   . TYR   A 1 68  ? 24.23200  -5.30300  -5.60100  1.000 105.31620 ? 104 TYR   A C   1 
ATOM   522  O  O   . TYR   A 1 68  ? 24.43700  -4.21900  -5.05200  1.000 110.58227 ? 104 TYR   A O   1 
ATOM   523  C  CB  . TYR   A 1 68  ? 26.16200  -6.85400  -5.45700  1.000 102.88754 ? 104 TYR   A CB  1 
ATOM   524  C  CG  . TYR   A 1 68  ? 26.88800  -7.92500  -4.67900  1.000 112.33518 ? 104 TYR   A CG  1 
ATOM   525  C  CD1 . TYR   A 1 68  ? 26.88100  -7.92800  -3.29000  1.000 112.95978 ? 104 TYR   A CD1 1 
ATOM   526  C  CD2 . TYR   A 1 68  ? 27.57100  -8.94200  -5.33200  1.000 109.51602 ? 104 TYR   A CD2 1 
ATOM   527  C  CE1 . TYR   A 1 68  ? 27.54100  -8.90900  -2.57300  1.000 112.67478 ? 104 TYR   A CE1 1 
ATOM   528  C  CE2 . TYR   A 1 68  ? 28.23200  -9.92700  -4.62500  1.000 106.46304 ? 104 TYR   A CE2 1 
ATOM   529  C  CZ  . TYR   A 1 68  ? 28.21400  -9.90600  -3.24600  1.000 110.79435 ? 104 TYR   A CZ  1 
ATOM   530  O  OH  . TYR   A 1 68  ? 28.87100  -10.88500 -2.53800  1.000 119.67352 ? 104 TYR   A OH  1 
ATOM   531  N  N   . TYR   A 1 69  ? 23.57500  -5.40000  -6.75500  1.000 106.31615 ? 105 TYR   A N   1 
ATOM   532  C  CA  . TYR   A 1 69  ? 23.17300  -4.19800  -7.47000  1.000 113.33708 ? 105 TYR   A CA  1 
ATOM   533  C  C   . TYR   A 1 69  ? 22.08700  -4.51800  -8.48600  1.000 122.32463 ? 105 TYR   A C   1 
ATOM   534  O  O   . TYR   A 1 69  ? 22.12400  -5.56200  -9.14200  1.000 113.63339 ? 105 TYR   A O   1 
ATOM   535  C  CB  . TYR   A 1 69  ? 24.37300  -3.55400  -8.17300  1.000 108.80535 ? 105 TYR   A CB  1 
ATOM   536  C  CG  . TYR   A 1 69  ? 24.01400  -2.38200  -9.05500  1.000 117.42105 ? 105 TYR   A CG  1 
ATOM   537  C  CD1 . TYR   A 1 69  ? 23.88800  -1.10400  -8.52700  1.000 124.60869 ? 105 TYR   A CD1 1 
ATOM   538  C  CD2 . TYR   A 1 69  ? 23.80500  -2.55200  -10.41700 1.000 119.32222 ? 105 TYR   A CD2 1 
ATOM   539  C  CE1 . TYR   A 1 69  ? 23.56200  -0.03100  -9.32900  1.000 120.49281 ? 105 TYR   A CE1 1 
ATOM   540  C  CE2 . TYR   A 1 69  ? 23.47400  -1.48800  -11.22500 1.000 126.66813 ? 105 TYR   A CE2 1 
ATOM   541  C  CZ  . TYR   A 1 69  ? 23.35800  -0.22800  -10.67700 1.000 124.05347 ? 105 TYR   A CZ  1 
ATOM   542  O  OH  . TYR   A 1 69  ? 23.03400  0.83900   -11.48100 1.000 142.40216 ? 105 TYR   A OH  1 
ATOM   543  N  N   . PHE   A 1 70  ? 21.12800  -3.60100  -8.60700  1.000 122.94476 ? 106 PHE   A N   1 
ATOM   544  C  CA  . PHE   A 1 70  ? 20.13100  -3.60700  -9.67300  1.000 127.69676 ? 106 PHE   A CA  1 
ATOM   545  C  C   . PHE   A 1 70  ? 19.99200  -2.17600  -10.16000 1.000 126.80800 ? 106 PHE   A C   1 
ATOM   546  O  O   . PHE   A 1 70  ? 19.60900  -1.29200  -9.38700  1.000 126.30162 ? 106 PHE   A O   1 
ATOM   547  C  CB  . PHE   A 1 70  ? 18.78300  -4.14900  -9.18100  1.000 134.57156 ? 106 PHE   A CB  1 
ATOM   548  C  CG  . PHE   A 1 70  ? 17.66900  -4.08400  -10.20300 1.000 132.38550 ? 106 PHE   A CG  1 
ATOM   549  C  CD1 . PHE   A 1 70  ? 17.93100  -4.10900  -11.56600 1.000 134.00222 ? 106 PHE   A CD1 1 
ATOM   550  C  CD2 . PHE   A 1 70  ? 16.35000  -4.00000  -9.78800  1.000 130.70678 ? 106 PHE   A CD2 1 
ATOM   551  C  CE1 . PHE   A 1 70  ? 16.90000  -4.04700  -12.48700 1.000 135.76633 ? 106 PHE   A CE1 1 
ATOM   552  C  CE2 . PHE   A 1 70  ? 15.31800  -3.94000  -10.70400 1.000 137.38231 ? 106 PHE   A CE2 1 
ATOM   553  C  CZ  . PHE   A 1 70  ? 15.59300  -3.96300  -12.05400 1.000 137.08809 ? 106 PHE   A CZ  1 
ATOM   554  N  N   . GLY   A 1 71  ? 20.30500  -1.94500  -11.43100 1.000 139.25034 ? 107 GLY   A N   1 
ATOM   555  C  CA  . GLY   A 1 71  ? 20.27700  -0.59600  -11.95400 1.000 144.08750 ? 107 GLY   A CA  1 
ATOM   556  C  C   . GLY   A 1 71  ? 19.64300  -0.45500  -13.31900 1.000 147.08876 ? 107 GLY   A C   1 
ATOM   557  O  O   . GLY   A 1 71  ? 19.07900  -1.40800  -13.86400 1.000 142.00599 ? 107 GLY   A O   1 
ATOM   558  N  N   . GLN   A 1 72  ? 19.74400  0.74900   -13.88000 1.000 153.75286 ? 108 GLN   A N   1 
ATOM   559  C  CA  . GLN   A 1 72  ? 19.07900  1.11400   -15.12500 1.000 157.31709 ? 108 GLN   A CA  1 
ATOM   560  C  C   . GLN   A 1 72  ? 20.11800  1.76900   -16.03900 1.000 163.81509 ? 108 GLN   A C   1 
ATOM   561  O  O   . GLN   A 1 72  ? 20.06300  2.96900   -16.31500 1.000 168.86666 ? 108 GLN   A O   1 
ATOM   562  C  CB  . GLN   A 1 72  ? 17.88900  2.04700   -14.86200 1.000 162.12351 ? 108 GLN   A CB  1 
ATOM   563  C  CG  . GLN   A 1 72  ? 17.12800  1.77700   -13.56200 1.000 160.13285 ? 108 GLN   A CG  1 
ATOM   564  C  CD  . GLN   A 1 72  ? 17.83100  2.34000   -12.33500 1.000 159.16546 ? 108 GLN   A CD  1 
ATOM   565  O  OE1 . GLN   A 1 72  ? 18.80600  3.08200   -12.45000 1.000 164.22249 ? 108 GLN   A OE1 1 
ATOM   566  N  NE2 . GLN   A 1 72  ? 17.34300  1.97700   -11.15400 1.000 153.92810 ? 108 GLN   A NE2 1 
ATOM   567  N  N   . GLU   A 1 73  ? 21.07600  0.97200   -16.50100 1.000 169.88196 ? 109 GLU   A N   1 
ATOM   568  C  CA  . GLU   A 1 73  ? 22.15300  1.46500   -17.35000 1.000 183.08556 ? 109 GLU   A CA  1 
ATOM   569  C  C   . GLU   A 1 73  ? 21.75000  1.33600   -18.81300 1.000 188.43818 ? 109 GLU   A C   1 
ATOM   570  O  O   . GLU   A 1 73  ? 21.47000  0.23000   -19.29000 1.000 191.36309 ? 109 GLU   A O   1 
ATOM   571  C  CB  . GLU   A 1 73  ? 23.45000  0.70400   -17.08000 1.000 183.25109 ? 109 GLU   A CB  1 
ATOM   572  C  CG  . GLU   A 1 73  ? 24.26300  1.24400   -15.91300 1.000 173.90181 ? 109 GLU   A CG  1 
ATOM   573  C  CD  . GLU   A 1 73  ? 23.53900  1.13100   -14.58600 1.000 172.64992 ? 109 GLU   A CD  1 
ATOM   574  O  OE1 . GLU   A 1 73  ? 22.74200  0.18400   -14.41900 1.000 175.57446 ? 109 GLU   A OE1 1 
ATOM   575  O  OE2 . GLU   A 1 73  ? 23.76300  1.99300   -13.71000 1.000 168.56198 ? 109 GLU   A OE2 1 
ATOM   576  N  N   . GLY   A 1 74  ? 21.72600  2.46300   -19.51800 1.000 189.52037 ? 110 GLY   A N   1 
ATOM   577  C  CA  . GLY   A 1 74  ? 21.37300  2.44100   -20.92700 1.000 195.94461 ? 110 GLY   A CA  1 
ATOM   578  C  C   . GLY   A 1 74  ? 19.95200  1.95700   -21.12300 1.000 194.38511 ? 110 GLY   A C   1 
ATOM   579  O  O   . GLY   A 1 74  ? 19.01600  2.40900   -20.45500 1.000 185.94434 ? 110 GLY   A O   1 
ATOM   580  N  N   . LEU   A 1 75  ? 19.78200  1.02400   -22.05500 1.000 208.41553 ? 111 LEU   A N   1 
ATOM   581  C  CA  . LEU   A 1 75  ? 18.49800  0.38400   -22.31300 1.000 204.18869 ? 111 LEU   A CA  1 
ATOM   582  C  C   . LEU   A 1 75  ? 18.51100  -1.07800  -21.87100 1.000 204.56318 ? 111 LEU   A C   1 
ATOM   583  O  O   . LEU   A 1 75  ? 17.96600  -1.95400  -22.54500 1.000 207.69895 ? 111 LEU   A O   1 
ATOM   584  C  CB  . LEU   A 1 75  ? 18.11700  0.49800   -23.78800 1.000 207.06600 ? 111 LEU   A CB  1 
ATOM   585  C  CG  . LEU   A 1 75  ? 19.06500  -0.08400  -24.84200 1.000 212.52916 ? 111 LEU   A CG  1 
ATOM   586  C  CD1 . LEU   A 1 75  ? 18.27800  -0.58700  -26.03900 1.000 214.46669 ? 111 LEU   A CD1 1 
ATOM   587  C  CD2 . LEU   A 1 75  ? 20.09700  0.94300   -25.28200 1.000 216.59629 ? 111 LEU   A CD2 1 
ATOM   588  N  N   . HIS   A 1 76  ? 19.11900  -1.35300  -20.71800 1.000 182.71714 ? 112 HIS   A N   1 
ATOM   589  C  CA  . HIS   A 1 76  ? 19.22400  -2.71200  -20.21100 1.000 169.06943 ? 112 HIS   A CA  1 
ATOM   590  C  C   . HIS   A 1 76  ? 19.00600  -2.72700  -18.70600 1.000 156.06245 ? 112 HIS   A C   1 
ATOM   591  O  O   . HIS   A 1 76  ? 19.45000  -1.82000  -17.99600 1.000 155.90501 ? 112 HIS   A O   1 
ATOM   592  C  CB  . HIS   A 1 76  ? 20.59100  -3.33000  -20.53600 1.000 163.63794 ? 112 HIS   A CB  1 
ATOM   593  C  CG  . HIS   A 1 76  ? 21.09300  -3.00200  -21.90800 1.000 175.75875 ? 112 HIS   A CG  1 
ATOM   594  N  ND1 . HIS   A 1 76  ? 22.04000  -2.02700  -22.13900 1.000 184.01076 ? 112 HIS   A ND1 1 
ATOM   595  C  CD2 . HIS   A 1 76  ? 20.77500  -3.51300  -23.12000 1.000 181.37482 ? 112 HIS   A CD2 1 
ATOM   596  C  CE1 . HIS   A 1 76  ? 22.28600  -1.95500  -23.43500 1.000 181.59740 ? 112 HIS   A CE1 1 
ATOM   597  N  NE2 . HIS   A 1 76  ? 21.53100  -2.84500  -24.05300 1.000 184.91409 ? 112 HIS   A NE2 1 
ATOM   598  N  N   . ASN   A 1 77  ? 18.31800  -3.76100  -18.22900 1.000 155.94039 ? 113 ASN   A N   1 
ATOM   599  C  CA  . ASN   A 1 77  ? 18.20600  -4.03400  -16.80200 1.000 152.16906 ? 113 ASN   A CA  1 
ATOM   600  C  C   . ASN   A 1 77  ? 19.37300  -4.91600  -16.37900 1.000 145.67077 ? 113 ASN   A C   1 
ATOM   601  O  O   . ASN   A 1 77  ? 19.66300  -5.92500  -17.03000 1.000 142.85565 ? 113 ASN   A O   1 
ATOM   602  C  CB  . ASN   A 1 77  ? 16.87600  -4.71600  -16.47800 1.000 154.47875 ? 113 ASN   A CB  1 
ATOM   603  C  CG  . ASN   A 1 77  ? 15.70700  -3.75200  -16.48900 1.000 154.88187 ? 113 ASN   A CG  1 
ATOM   604  O  OD1 . ASN   A 1 77  ? 15.78900  -2.65300  -15.94000 1.000 149.95469 ? 113 ASN   A OD1 1 
ATOM   605  N  ND2 . ASN   A 1 77  ? 14.60900  -4.15900  -17.11500 1.000 159.27807 ? 113 ASN   A ND2 1 
ATOM   606  N  N   . ILE   A 1 78  ? 20.04000  -4.53500  -15.29200 1.000 126.16849 ? 114 ILE   A N   1 
ATOM   607  C  CA  . ILE   A 1 78  ? 21.28900  -5.16300  -14.88000 1.000 125.80510 ? 114 ILE   A CA  1 
ATOM   608  C  C   . ILE   A 1 78  ? 21.15200  -5.65800  -13.44800 1.000 122.52402 ? 114 ILE   A C   1 
ATOM   609  O  O   . ILE   A 1 78  ? 20.73500  -4.90400  -12.56300 1.000 120.28860 ? 114 ILE   A O   1 
ATOM   610  C  CB  . ILE   A 1 78  ? 22.47700  -4.18900  -15.00500 1.000 124.49761 ? 114 ILE   A CB  1 
ATOM   611  C  CG1 . ILE   A 1 78  ? 22.50000  -3.56600  -16.40300 1.000 133.47607 ? 114 ILE   A CG1 1 
ATOM   612  C  CG2 . ILE   A 1 78  ? 23.78300  -4.90100  -14.70700 1.000 118.85989 ? 114 ILE   A CG2 1 
ATOM   613  C  CD1 . ILE   A 1 78  ? 23.80500  -2.89700  -16.75700 1.000 141.88839 ? 114 ILE   A CD1 1 
ATOM   614  N  N   . LEU   A 1 79  ? 21.50700  -6.92200  -13.22100 1.000 116.76455 ? 115 LEU   A N   1 
ATOM   615  C  CA  . LEU   A 1 79  ? 21.52300  -7.51600  -11.89100 1.000 118.97532 ? 115 LEU   A CA  1 
ATOM   616  C  C   . LEU   A 1 79  ? 22.88900  -8.13600  -11.64100 1.000 120.07613 ? 115 LEU   A C   1 
ATOM   617  O  O   . LEU   A 1 79  ? 23.36700  -8.94100  -12.44700 1.000 103.50457 ? 115 LEU   A O   1 
ATOM   618  C  CB  . LEU   A 1 79  ? 20.42700  -8.57500  -11.72900 1.000 110.41822 ? 115 LEU   A CB  1 
ATOM   619  C  CG  . LEU   A 1 79  ? 20.51600  -9.43100  -10.46200 1.000 108.50929 ? 115 LEU   A CG  1 
ATOM   620  C  CD1 . LEU   A 1 79  ? 20.51900  -8.56500  -9.21300  1.000 110.92703 ? 115 LEU   A CD1 1 
ATOM   621  C  CD2 . LEU   A 1 79  ? 19.38400  -10.44400 -10.40700 1.000 112.34865 ? 115 LEU   A CD2 1 
ATOM   622  N  N   . VAL   A 1 80  ? 23.50600  -7.76500  -10.52400 1.000 115.84773 ? 116 VAL   A N   1 
ATOM   623  C  CA  . VAL   A 1 80  ? 24.83000  -8.24400  -10.14900 1.000 108.29064 ? 116 VAL   A CA  1 
ATOM   624  C  C   . VAL   A 1 80  ? 24.69100  -9.12000  -8.91100  1.000 110.13313 ? 116 VAL   A C   1 
ATOM   625  O  O   . VAL   A 1 80  ? 24.21400  -8.66100  -7.86500  1.000 108.26515 ? 116 VAL   A O   1 
ATOM   626  C  CB  . VAL   A 1 80  ? 25.80100  -7.08000  -9.89500  1.000 107.02275 ? 116 VAL   A CB  1 
ATOM   627  C  CG1 . VAL   A 1 80  ? 27.03900  -7.57000  -9.15400  1.000 110.68005 ? 116 VAL   A CG1 1 
ATOM   628  C  CG2 . VAL   A 1 80  ? 26.19000  -6.42300  -11.21100 1.000 111.49757 ? 116 VAL   A CG2 1 
ATOM   629  N  N   . ILE   A 1 81  ? 25.09700  -10.38400 -9.03600  1.000 105.57636 ? 117 ILE   A N   1 
ATOM   630  C  CA  . ILE   A 1 81  ? 25.20700  -11.28100 -7.89000  1.000 104.43550 ? 117 ILE   A CA  1 
ATOM   631  C  C   . ILE   A 1 81  ? 26.55900  -11.97900 -7.93300  1.000 102.69418 ? 117 ILE   A C   1 
ATOM   632  O  O   . ILE   A 1 81  ? 27.44000  -11.60900 -8.71800  1.000 97.97682  ? 117 ILE   A O   1 
ATOM   633  C  CB  . ILE   A 1 81  ? 24.06300  -12.31400 -7.84300  1.000 103.97383 ? 117 ILE   A CB  1 
ATOM   634  C  CG1 . ILE   A 1 81  ? 23.80800  -12.92300 -9.22500  1.000 104.89845 ? 117 ILE   A CG1 1 
ATOM   635  C  CG2 . ILE   A 1 81  ? 22.80000  -11.69600 -7.26200  1.000 106.05922 ? 117 ILE   A CG2 1 
ATOM   636  C  CD1 . ILE   A 1 81  ? 22.79700  -14.05600 -9.19500  1.000 104.54233 ? 117 ILE   A CD1 1 
ATOM   637  N  N   . ASP   A 1 82  ? 26.72600  -12.99600 -7.09300  1.000 102.96720 ? 118 ASP   A N   1 
ATOM   638  C  CA  . ASP   A 1 82  ? 27.98600  -13.72100 -7.03000  1.000 93.16619  ? 118 ASP   A CA  1 
ATOM   639  C  C   . ASP   A 1 82  ? 28.14800  -14.62700 -8.24300  1.000 93.43521  ? 118 ASP   A C   1 
ATOM   640  O  O   . ASP   A 1 82  ? 27.22700  -15.36200 -8.61400  1.000 86.89371  ? 118 ASP   A O   1 
ATOM   641  C  CB  . ASP   A 1 82  ? 28.06000  -14.54600 -5.74600  1.000 95.95797  ? 118 ASP   A CB  1 
ATOM   642  C  CG  . ASP   A 1 82  ? 28.48600  -13.72500 -4.54900  1.000 95.51198  ? 118 ASP   A CG  1 
ATOM   643  O  OD1 . ASP   A 1 82  ? 29.34300  -12.83400 -4.71800  1.000 103.76909 ? 118 ASP   A OD1 1 
ATOM   644  O  OD2 . ASP   A 1 82  ? 27.96400  -13.97200 -3.44100  1.000 102.42600 ? 118 ASP   A OD2 1 
ATOM   645  N  N   . LEU   A 1 83  ? 29.32000  -14.55700 -8.86800  1.000 86.71844  ? 119 LEU   A N   1 
ATOM   646  C  CA  . LEU   A 1 83  ? 29.71800  -15.55700 -9.84600  1.000 92.16862  ? 119 LEU   A CA  1 
ATOM   647  C  C   . LEU   A 1 83  ? 29.97300  -16.88900 -9.14700  1.000 81.33172  ? 119 LEU   A C   1 
ATOM   648  O  O   . LEU   A 1 83  ? 30.44700  -16.93700 -8.01000  1.000 80.61694  ? 119 LEU   A O   1 
ATOM   649  C  CB  . LEU   A 1 83  ? 30.97100  -15.09200 -10.59100 1.000 89.82563  ? 119 LEU   A CB  1 
ATOM   650  C  CG  . LEU   A 1 83  ? 31.55400  -15.93800 -11.72300 1.000 91.18033  ? 119 LEU   A CG  1 
ATOM   651  C  CD1 . LEU   A 1 83  ? 30.79300  -15.71500 -13.02000 1.000 87.23008  ? 119 LEU   A CD1 1 
ATOM   652  C  CD2 . LEU   A 1 83  ? 33.02900  -15.61400 -11.89700 1.000 101.31382 ? 119 LEU   A CD2 1 
ATOM   653  N  N   . LEU   A 1 84  ? 29.64200  -17.98100 -9.83200  1.000 85.90663  ? 120 LEU   A N   1 
ATOM   654  C  CA  . LEU   A 1 84  ? 29.78000  -19.31000 -9.25300  1.000 79.71841  ? 120 LEU   A CA  1 
ATOM   655  C  C   . LEU   A 1 84  ? 30.37400  -20.25400 -10.29000 1.000 85.03537  ? 120 LEU   A C   1 
ATOM   656  O  O   . LEU   A 1 84  ? 30.57400  -19.89200 -11.45300 1.000 88.22346  ? 120 LEU   A O   1 
ATOM   657  C  CB  . LEU   A 1 84  ? 28.43400  -19.82400 -8.73000  1.000 86.10950  ? 120 LEU   A CB  1 
ATOM   658  C  CG  . LEU   A 1 84  ? 27.99500  -19.24900 -7.38100  1.000 82.90551  ? 120 LEU   A CG  1 
ATOM   659  C  CD1 . LEU   A 1 84  ? 26.56100  -19.62500 -7.08100  1.000 70.57975  ? 120 LEU   A CD1 1 
ATOM   660  C  CD2 . LEU   A 1 84  ? 28.92000  -19.73100 -6.27100  1.000 79.16322  ? 120 LEU   A CD2 1 
ATOM   661  N  N   . GLY   A 1 85  ? 30.65800  -21.48000 -9.85500  1.000 85.39042  ? 121 GLY   A N   1 
ATOM   662  C  CA  . GLY   A 1 85  ? 31.25600  -22.47600 -10.71000 1.000 84.16021  ? 121 GLY   A CA  1 
ATOM   663  C  C   . GLY   A 1 85  ? 30.25200  -23.12200 -11.64200 1.000 83.47384  ? 121 GLY   A C   1 
ATOM   664  O  O   . GLY   A 1 85  ? 29.11600  -22.65900 -11.78900 1.000 81.02844  ? 121 GLY   A O   1 
ATOM   665  N  N   . PRO   A 1 86  ? 30.65600  -24.21600 -12.28500 1.000 92.06194  ? 122 PRO   A N   1 
ATOM   666  C  CA  . PRO   A 1 86  ? 29.78500  -24.86500 -13.27300 1.000 86.47474  ? 122 PRO   A CA  1 
ATOM   667  C  C   . PRO   A 1 86  ? 28.52900  -25.43500 -12.63200 1.000 77.37578  ? 122 PRO   A C   1 
ATOM   668  O  O   . PRO   A 1 86  ? 28.41900  -25.58900 -11.41500 1.000 74.77169  ? 122 PRO   A O   1 
ATOM   669  C  CB  . PRO   A 1 86  ? 30.66400  -25.98000 -13.85200 1.000 93.58870  ? 122 PRO   A CB  1 
ATOM   670  C  CG  . PRO   A 1 86  ? 32.06500  -25.59500 -13.50000 1.000 111.33712 ? 122 PRO   A CG  1 
ATOM   671  C  CD  . PRO   A 1 86  ? 31.96900  -24.87300 -12.19400 1.000 96.57722  ? 122 PRO   A CD  1 
ATOM   672  N  N   . SER   A 1 87  ? 27.56700  -25.75400 -13.49200 1.000 75.39438  ? 123 SER   A N   1 
ATOM   673  C  CA  . SER   A 1 87  ? 26.32800  -26.36500 -13.04400 1.000 84.58412  ? 123 SER   A CA  1 
ATOM   674  C  C   . SER   A 1 87  ? 26.51000  -27.86800 -12.85800 1.000 79.60249  ? 123 SER   A C   1 
ATOM   675  O  O   . SER   A 1 87  ? 27.47800  -28.46900 -13.33300 1.000 72.51644  ? 123 SER   A O   1 
ATOM   676  C  CB  . SER   A 1 87  ? 25.19900  -26.10300 -14.04200 1.000 73.64091  ? 123 SER   A CB  1 
ATOM   677  O  OG  . SER   A 1 87  ? 25.42100  -26.80100 -15.25700 1.000 69.65482  ? 123 SER   A OG  1 
ATOM   678  N  N   . LEU   A 1 88  ? 25.55200  -28.47500 -12.15300 1.000 77.10795  ? 124 LEU   A N   1 
ATOM   679  C  CA  . LEU   A 1 88  ? 25.54800  -29.92700 -12.03200 1.000 73.17622  ? 124 LEU   A CA  1 
ATOM   680  C  C   . LEU   A 1 88  ? 25.39800  -30.59200 -13.39200 1.000 74.30855  ? 124 LEU   A C   1 
ATOM   681  O  O   . LEU   A 1 88  ? 25.89000  -31.70700 -13.59400 1.000 79.20873  ? 124 LEU   A O   1 
ATOM   682  C  CB  . LEU   A 1 88  ? 24.43400  -30.37600 -11.08900 1.000 66.11890  ? 124 LEU   A CB  1 
ATOM   683  C  CG  . LEU   A 1 88  ? 24.57300  -29.93800 -9.63000  1.000 69.87053  ? 124 LEU   A CG  1 
ATOM   684  C  CD1 . LEU   A 1 88  ? 23.42100  -30.48000 -8.79800  1.000 78.07722  ? 124 LEU   A CD1 1 
ATOM   685  C  CD2 . LEU   A 1 88  ? 25.90700  -30.39400 -9.06200  1.000 70.84250  ? 124 LEU   A CD2 1 
ATOM   686  N  N   . GLU   A 1 89  ? 24.73300  -29.92200 -14.33700 1.000 68.56752  ? 125 GLU   A N   1 
ATOM   687  C  CA  . GLU   A 1 89  ? 24.65400  -30.43700 -15.70000 1.000 75.79909  ? 125 GLU   A CA  1 
ATOM   688  C  C   . GLU   A 1 89  ? 26.00800  -30.36300 -16.39600 1.000 81.09263  ? 125 GLU   A C   1 
ATOM   689  O  O   . GLU   A 1 89  ? 26.36000  -31.25700 -17.17500 1.000 83.64472  ? 125 GLU   A O   1 
ATOM   690  C  CB  . GLU   A 1 89  ? 23.59300  -29.66700 -16.48900 1.000 75.66173  ? 125 GLU   A CB  1 
ATOM   691  C  CG  . GLU   A 1 89  ? 23.49400  -30.04500 -17.96400 1.000 78.13990  ? 125 GLU   A CG  1 
ATOM   692  C  CD  . GLU   A 1 89  ? 22.96400  -31.45200 -18.18700 1.000 84.09420  ? 125 GLU   A CD  1 
ATOM   693  O  OE1 . GLU   A 1 89  ? 22.39900  -32.04100 -17.24200 1.000 85.53103  ? 125 GLU   A OE1 1 
ATOM   694  O  OE2 . GLU   A 1 89  ? 23.11100  -31.96800 -19.31600 1.000 81.03562  ? 125 GLU   A OE2 1 
ATOM   695  N  N   . ASP   A 1 90  ? 26.78200  -29.30700 -16.12900 1.000 77.95656  ? 126 ASP   A N   1 
ATOM   696  C  CA  . ASP   A 1 90  ? 28.12600  -29.21100 -16.69100 1.000 80.92621  ? 126 ASP   A CA  1 
ATOM   697  C  C   . ASP   A 1 90  ? 29.01100  -30.34300 -16.18600 1.000 84.63118  ? 126 ASP   A C   1 
ATOM   698  O  O   . ASP   A 1 90  ? 29.66200  -31.03700 -16.97500 1.000 85.46303  ? 126 ASP   A O   1 
ATOM   699  C  CB  . ASP   A 1 90  ? 28.74500  -27.85500 -16.35100 1.000 87.00940  ? 126 ASP   A CB  1 
ATOM   700  C  CG  . ASP   A 1 90  ? 28.14700  -26.72200 -17.15700 1.000 86.10856  ? 126 ASP   A CG  1 
ATOM   701  O  OD1 . ASP   A 1 90  ? 27.91400  -26.91100 -18.36900 1.000 97.53665  ? 126 ASP   A OD1 1 
ATOM   702  O  OD2 . ASP   A 1 90  ? 27.90700  -25.64200 -16.57700 1.000 78.21633  ? 126 ASP   A OD2 1 
ATOM   703  N  N   . LEU   A 1 91  ? 29.04900  -30.54200 -14.86500 1.000 82.77761  ? 127 LEU   A N   1 
ATOM   704  C  CA  . LEU   A 1 91  ? 29.82900  -31.63600 -14.29500 1.000 84.26689  ? 127 LEU   A CA  1 
ATOM   705  C  C   . LEU   A 1 91  ? 29.26700  -32.98700 -14.70400 1.000 88.28730  ? 127 LEU   A C   1 
ATOM   706  O  O   . LEU   A 1 91  ? 30.01300  -33.97200 -14.78500 1.000 89.97961  ? 127 LEU   A O   1 
ATOM   707  C  CB  . LEU   A 1 91  ? 29.85500  -31.52600 -12.77100 1.000 80.19410  ? 127 LEU   A CB  1 
ATOM   708  C  CG  . LEU   A 1 91  ? 30.22700  -30.15500 -12.20800 1.000 83.57831  ? 127 LEU   A CG  1 
ATOM   709  C  CD1 . LEU   A 1 91  ? 29.88400  -30.06900 -10.72800 1.000 88.21162  ? 127 LEU   A CD1 1 
ATOM   710  C  CD2 . LEU   A 1 91  ? 31.70000  -29.88300 -12.43000 1.000 92.45321  ? 127 LEU   A CD2 1 
ATOM   711  N  N   . PHE   A 1 92  ? 27.95600  -33.05200 -14.95300 1.000 82.90854  ? 128 PHE   A N   1 
ATOM   712  C  CA  . PHE   A 1 92  ? 27.33200  -34.30300 -15.37200 1.000 85.44354  ? 128 PHE   A CA  1 
ATOM   713  C  C   . PHE   A 1 92  ? 27.94100  -34.80100 -16.67600 1.000 88.93905  ? 128 PHE   A C   1 
ATOM   714  O  O   . PHE   A 1 92  ? 28.43100  -35.93300 -16.75300 1.000 87.86919  ? 128 PHE   A O   1 
ATOM   715  C  CB  . PHE   A 1 92  ? 25.82100  -34.10600 -15.51000 1.000 85.81107  ? 128 PHE   A CB  1 
ATOM   716  C  CG  . PHE   A 1 92  ? 25.06000  -35.35400 -15.85700 1.000 83.60758  ? 128 PHE   A CG  1 
ATOM   717  C  CD1 . PHE   A 1 92  ? 25.00500  -36.41800 -14.97400 1.000 80.41166  ? 128 PHE   A CD1 1 
ATOM   718  C  CD2 . PHE   A 1 92  ? 24.36600  -35.44400 -17.05500 1.000 86.35292  ? 128 PHE   A CD2 1 
ATOM   719  C  CE1 . PHE   A 1 92  ? 24.29000  -37.55800 -15.28700 1.000 88.37339  ? 128 PHE   A CE1 1 
ATOM   720  C  CE2 . PHE   A 1 92  ? 23.64700  -36.58300 -17.37200 1.000 88.91232  ? 128 PHE   A CE2 1 
ATOM   721  C  CZ  . PHE   A 1 92  ? 23.61100  -37.64000 -16.48900 1.000 86.82135  ? 128 PHE   A CZ  1 
ATOM   722  N  N   . ASP   A 1 93  ? 27.94600  -33.95000 -17.70600 1.000 92.62408  ? 129 ASP   A N   1 
ATOM   723  C  CA  . ASP   A 1 93  ? 28.54400  -34.32500 -18.98500 1.000 99.74621  ? 129 ASP   A CA  1 
ATOM   724  C  C   . ASP   A 1 93  ? 30.01500  -34.69000 -18.82300 1.000 100.68721 ? 129 ASP   A C   1 
ATOM   725  O  O   . ASP   A 1 93  ? 30.48900  -35.66900 -19.41200 1.000 102.00980 ? 129 ASP   A O   1 
ATOM   726  C  CB  . ASP   A 1 93  ? 28.37500  -33.17900 -19.98600 1.000 105.09354 ? 129 ASP   A CB  1 
ATOM   727  C  CG  . ASP   A 1 93  ? 28.80100  -33.55500 -21.39800 1.000 124.56746 ? 129 ASP   A CG  1 
ATOM   728  O  OD1 . ASP   A 1 93  ? 29.97000  -33.94700 -21.59900 1.000 127.69468 ? 129 ASP   A OD1 1 
ATOM   729  O  OD2 . ASP   A 1 93  ? 27.95900  -33.45000 -22.31300 1.000 125.69650 ? 129 ASP   A OD2 1 
ATOM   730  N  N   . TRP   A 1 94  ? 30.75100  -33.91900 -18.02100 1.000 103.10516 ? 130 TRP   A N   1 
ATOM   731  C  CA  . TRP   A 1 94  ? 32.18800  -34.13700 -17.90000 1.000 111.35784 ? 130 TRP   A CA  1 
ATOM   732  C  C   . TRP   A 1 94  ? 32.50300  -35.44500 -17.18300 1.000 102.18055 ? 130 TRP   A C   1 
ATOM   733  O  O   . TRP   A 1 94  ? 33.53600  -36.06700 -17.45700 1.000 90.51480  ? 130 TRP   A O   1 
ATOM   734  C  CB  . TRP   A 1 94  ? 32.83200  -32.95100 -17.18200 1.000 111.59831 ? 130 TRP   A CB  1 
ATOM   735  C  CG  . TRP   A 1 94  ? 32.59700  -31.63900 -17.88100 1.000 125.27465 ? 130 TRP   A CG  1 
ATOM   736  C  CD1 . TRP   A 1 94  ? 32.09200  -31.45800 -19.13800 1.000 135.69068 ? 130 TRP   A CD1 1 
ATOM   737  C  CD2 . TRP   A 1 94  ? 32.84700  -30.32800 -17.36000 1.000 130.74177 ? 130 TRP   A CD2 1 
ATOM   738  N  NE1 . TRP   A 1 94  ? 32.01700  -30.11900 -19.43100 1.000 141.93466 ? 130 TRP   A NE1 1 
ATOM   739  C  CE2 . TRP   A 1 94  ? 32.47500  -29.40400 -18.35700 1.000 136.46580 ? 130 TRP   A CE2 1 
ATOM   740  C  CE3 . TRP   A 1 94  ? 33.35300  -29.84600 -16.15000 1.000 135.47843 ? 130 TRP   A CE3 1 
ATOM   741  C  CZ2 . TRP   A 1 94  ? 32.59100  -28.02800 -18.17900 1.000 134.44879 ? 130 TRP   A CZ2 1 
ATOM   742  C  CZ3 . TRP   A 1 94  ? 33.46600  -28.48000 -15.97700 1.000 138.70355 ? 130 TRP   A CZ3 1 
ATOM   743  C  CH2 . TRP   A 1 94  ? 33.08900  -27.58700 -16.98600 1.000 138.07983 ? 130 TRP   A CH2 1 
ATOM   744  N  N   . CYS   A 1 95  ? 31.62700  -35.88400 -16.28000 1.000 90.58013  ? 131 CYS   A N   1 
ATOM   745  C  CA  . CYS   A 1 95  ? 31.78300  -37.16100 -15.59700 1.000 86.72886  ? 131 CYS   A CA  1 
ATOM   746  C  C   . CYS   A 1 95  ? 31.27200  -38.34000 -16.41900 1.000 92.00885  ? 131 CYS   A C   1 
ATOM   747  O  O   . CYS   A 1 95  ? 31.02100  -39.41100 -15.85200 1.000 98.84925  ? 131 CYS   A O   1 
ATOM   748  C  CB  . CYS   A 1 95  ? 31.07300  -37.12300 -14.24100 1.000 84.24389  ? 131 CYS   A CB  1 
ATOM   749  S  SG  . CYS   A 1 95  ? 31.86600  -36.07700 -13.00100 1.000 81.95379  ? 131 CYS   A SG  1 
ATOM   750  N  N   . GLY   A 1 96  ? 31.11100  -38.16800 -17.72900 1.000 87.46677  ? 132 GLY   A N   1 
ATOM   751  C  CA  . GLY   A 1 96  ? 30.59900  -39.23300 -18.56700 1.000 97.44247  ? 132 GLY   A CA  1 
ATOM   752  C  C   . GLY   A 1 96  ? 29.09400  -39.33000 -18.61800 1.000 94.54165  ? 132 GLY   A C   1 
ATOM   753  O  O   . GLY   A 1 96  ? 28.56500  -40.39500 -18.95500 1.000 94.13276  ? 132 GLY   A O   1 
ATOM   754  N  N   . ARG   A 1 97  ? 28.38600  -38.24800 -18.29100 1.000 96.41342  ? 133 ARG   A N   1 
ATOM   755  C  CA  . ARG   A 1 97  ? 26.92400  -38.22400 -18.25500 1.000 90.87102  ? 133 ARG   A CA  1 
ATOM   756  C  C   . ARG   A 1 97  ? 26.36100  -39.31600 -17.35000 1.000 94.57823  ? 133 ARG   A C   1 
ATOM   757  O  O   . ARG   A 1 97  ? 25.29900  -39.87900 -17.62600 1.000 90.79972  ? 133 ARG   A O   1 
ATOM   758  C  CB  . ARG   A 1 97  ? 26.33000  -38.32400 -19.66300 1.000 95.98515  ? 133 ARG   A CB  1 
ATOM   759  C  CG  . ARG   A 1 97  ? 26.75700  -37.19000 -20.58300 1.000 95.65052  ? 133 ARG   A CG  1 
ATOM   760  C  CD  . ARG   A 1 97  ? 25.78600  -37.01500 -21.73500 1.000 98.68339  ? 133 ARG   A CD  1 
ATOM   761  N  NE  . ARG   A 1 97  ? 24.41800  -36.84000 -21.26100 1.000 95.93512  ? 133 ARG   A NE  1 
ATOM   762  C  CZ  . ARG   A 1 97  ? 23.91500  -35.69200 -20.82900 1.000 93.38674  ? 133 ARG   A CZ  1 
ATOM   763  N  NH1 . ARG   A 1 97  ? 24.64300  -34.58800 -20.79100 1.000 96.16309  ? 133 ARG   A NH1 1 
ATOM   764  N  NH2 . ARG   A 1 97  ? 22.64900  -35.65100 -20.42200 1.000 86.50725  ? 133 ARG   A NH2 1 
ATOM   765  N  N   . ARG   A 1 98  ? 27.07700  -39.61400 -16.26600 1.000 98.69228  ? 134 ARG   A N   1 
ATOM   766  C  CA  . ARG   A 1 98  ? 26.62700  -40.53800 -15.23500 1.000 98.21404  ? 134 ARG   A CA  1 
ATOM   767  C  C   . ARG   A 1 98  ? 27.31600  -40.17000 -13.93000 1.000 99.41128  ? 134 ARG   A C   1 
ATOM   768  O  O   . ARG   A 1 98  ? 28.50000  -39.82400 -13.92300 1.000 101.00676 ? 134 ARG   A O   1 
ATOM   769  C  CB  . ARG   A 1 98  ? 26.92900  -42.00100 -15.58800 1.000 98.12856  ? 134 ARG   A CB  1 
ATOM   770  C  CG  . ARG   A 1 98  ? 25.96400  -42.62900 -16.58000 1.000 104.85338 ? 134 ARG   A CG  1 
ATOM   771  C  CD  . ARG   A 1 98  ? 25.89700  -44.13400 -16.41700 1.000 112.10989 ? 134 ARG   A CD  1 
ATOM   772  N  NE  . ARG   A 1 98  ? 25.58600  -44.50300 -15.04200 1.000 114.83540 ? 134 ARG   A NE  1 
ATOM   773  C  CZ  . ARG   A 1 98  ? 25.14700  -45.69600 -14.66700 1.000 115.40933 ? 134 ARG   A CZ  1 
ATOM   774  N  NH1 . ARG   A 1 98  ? 24.93000  -46.66000 -15.54700 1.000 117.99034 ? 134 ARG   A NH1 1 
ATOM   775  N  NH2 . ARG   A 1 98  ? 24.91400  -45.92600 -13.37800 1.000 123.34261 ? 134 ARG   A NH2 1 
ATOM   776  N  N   . PHE   A 1 99  ? 26.56900  -40.24400 -12.83300 1.000 83.95219  ? 135 PHE   A N   1 
ATOM   777  C  CA  . PHE   A 1 99  ? 27.09000  -39.95900 -11.50400 1.000 83.05200  ? 135 PHE   A CA  1 
ATOM   778  C  C   . PHE   A 1 99  ? 27.05100  -41.21900 -10.65300 1.000 82.93330  ? 135 PHE   A C   1 
ATOM   779  O  O   . PHE   A 1 99  ? 26.11000  -42.01400 -10.74600 1.000 96.01529  ? 135 PHE   A O   1 
ATOM   780  C  CB  . PHE   A 1 99  ? 26.29100  -38.85400 -10.81300 1.000 71.83771  ? 135 PHE   A CB  1 
ATOM   781  C  CG  . PHE   A 1 99  ? 26.75100  -37.46400 -11.14100 1.000 86.48384  ? 135 PHE   A CG  1 
ATOM   782  C  CD1 . PHE   A 1 99  ? 27.97300  -37.24500 -11.75200 1.000 84.25290  ? 135 PHE   A CD1 1 
ATOM   783  C  CD2 . PHE   A 1 99  ? 25.96100  -36.37100 -10.82400 1.000 81.59736  ? 135 PHE   A CD2 1 
ATOM   784  C  CE1 . PHE   A 1 99  ? 28.39400  -35.96300 -12.05000 1.000 84.03682  ? 135 PHE   A CE1 1 
ATOM   785  C  CE2 . PHE   A 1 99  ? 26.37700  -35.08600 -11.11800 1.000 84.38454  ? 135 PHE   A CE2 1 
ATOM   786  C  CZ  . PHE   A 1 99  ? 27.59600  -34.88200 -11.73200 1.000 78.26218  ? 135 PHE   A CZ  1 
ATOM   787  N  N   . SER   A 1 100 ? 28.07300  -41.39300 -9.82000  1.000 88.93478  ? 136 SER   A N   1 
ATOM   788  C  CA  . SER   A 1 100 ? 28.09500  -42.51000 -8.89300  1.000 90.93466  ? 136 SER   A CA  1 
ATOM   789  C  C   . SER   A 1 100 ? 26.99300  -42.35400 -7.84900  1.000 89.62024  ? 136 SER   A C   1 
ATOM   790  O  O   . SER   A 1 100 ? 26.40100  -41.28200 -7.68400  1.000 84.01430  ? 136 SER   A O   1 
ATOM   791  C  CB  . SER   A 1 100 ? 29.45700  -42.61400 -8.20500  1.000 86.54697  ? 136 SER   A CB  1 
ATOM   792  O  OG  . SER   A 1 100 ? 29.61600  -41.59000 -7.24100  1.000 86.61278  ? 136 SER   A OG  1 
ATOM   793  N  N   . VAL   A 1 101 ? 26.72500  -43.44700 -7.13100  1.000 85.80684  ? 137 VAL   A N   1 
ATOM   794  C  CA  . VAL   A 1 101 ? 25.66300  -43.43300 -6.13000  1.000 86.19427  ? 137 VAL   A CA  1 
ATOM   795  C  C   . VAL   A 1 101 ? 26.03000  -42.51600 -4.96800  1.000 88.25474  ? 137 VAL   A C   1 
ATOM   796  O  O   . VAL   A 1 101 ? 25.16600  -41.84500 -4.39500  1.000 79.04988  ? 137 VAL   A O   1 
ATOM   797  C  CB  . VAL   A 1 101 ? 25.35800  -44.86700 -5.65700  1.000 100.36895 ? 137 VAL   A CB  1 
ATOM   798  C  CG1 . VAL   A 1 101 ? 24.43700  -44.85400 -4.44500  1.000 78.89172  ? 137 VAL   A CG1 1 
ATOM   799  C  CG2 . VAL   A 1 101 ? 24.72900  -45.67100 -6.78800  1.000 96.99929  ? 137 VAL   A CG2 1 
ATOM   800  N  N   . LYS   A 1 102 ? 27.31300  -42.45100 -4.61400  1.000 90.23996  ? 138 LYS   A N   1 
ATOM   801  C  CA  . LYS   A 1 102 ? 27.72000  -41.60000 -3.49900  1.000 87.16146  ? 138 LYS   A CA  1 
ATOM   802  C  C   . LYS   A 1 102 ? 27.48500  -40.12800 -3.80700  1.000 86.75884  ? 138 LYS   A C   1 
ATOM   803  O  O   . LYS   A 1 102 ? 26.97300  -39.38500 -2.96200  1.000 85.61783  ? 138 LYS   A O   1 
ATOM   804  C  CB  . LYS   A 1 102 ? 29.18700  -41.84400 -3.16300  1.000 94.60430  ? 138 LYS   A CB  1 
ATOM   805  C  CG  . LYS   A 1 102 ? 29.74200  -40.96800 -2.06000  1.000 99.72550  ? 138 LYS   A CG  1 
ATOM   806  C  CD  . LYS   A 1 102 ? 31.20800  -41.27800 -1.82400  1.000 103.96115 ? 138 LYS   A CD  1 
ATOM   807  C  CE  . LYS   A 1 102 ? 31.76000  -40.47200 -0.66900  1.000 104.95720 ? 138 LYS   A CE  1 
ATOM   808  N  NZ  . LYS   A 1 102 ? 33.18400  -40.79800 -0.39600  1.000 104.48654 ? 138 LYS   A NZ  1 
ATOM   809  N  N   . THR   A 1 103 ? 27.84600  -39.68900 -5.01400  1.000 80.62558  ? 139 THR   A N   1 
ATOM   810  C  CA  . THR   A 1 103 ? 27.72300  -38.27600 -5.35800  1.000 90.51398  ? 139 THR   A CA  1 
ATOM   811  C  C   . THR   A 1 103 ? 26.26100  -37.83400 -5.38500  1.000 77.95978  ? 139 THR   A C   1 
ATOM   812  O  O   . THR   A 1 103 ? 25.91100  -36.79200 -4.81800  1.000 74.63264  ? 139 THR   A O   1 
ATOM   813  C  CB  . THR   A 1 103 ? 28.39900  -38.00100 -6.70400  1.000 85.02616  ? 139 THR   A CB  1 
ATOM   814  O  OG1 . THR   A 1 103 ? 29.80200  -38.27900 -6.60500  1.000 92.14683  ? 139 THR   A OG1 1 
ATOM   815  C  CG2 . THR   A 1 103 ? 28.20700  -36.54700 -7.10800  1.000 89.37514  ? 139 THR   A CG2 1 
ATOM   816  N  N   . VAL   A 1 104 ? 25.39300  -38.62200 -6.03200  1.000 83.14970  ? 140 VAL   A N   1 
ATOM   817  C  CA  . VAL   A 1 104 ? 23.99100  -38.23000 -6.19800  1.000 80.41869  ? 140 VAL   A CA  1 
ATOM   818  C  C   . VAL   A 1 104 ? 23.30300  -38.11500 -4.84400  1.000 73.84141  ? 140 VAL   A C   1 
ATOM   819  O  O   . VAL   A 1 104 ? 22.42000  -37.27200 -4.65100  1.000 77.69795  ? 140 VAL   A O   1 
ATOM   820  C  CB  . VAL   A 1 104 ? 23.25300  -39.21700 -7.12900  1.000 76.86504  ? 140 VAL   A CB  1 
ATOM   821  C  CG1 . VAL   A 1 104 ? 23.78400  -39.12100 -8.53500  1.000 77.34833  ? 140 VAL   A CG1 1 
ATOM   822  C  CG2 . VAL   A 1 104 ? 23.37100  -40.64500 -6.61400  1.000 88.90839  ? 140 VAL   A CG2 1 
ATOM   823  N  N   . VAL   A 1 105 ? 23.69900  -38.95100 -3.88600  1.000 78.14692  ? 141 VAL   A N   1 
ATOM   824  C  CA  . VAL   A 1 105 ? 23.21100  -38.86500 -2.51300  1.000 79.43539  ? 141 VAL   A CA  1 
ATOM   825  C  C   . VAL   A 1 105 ? 23.56000  -37.57100 -1.79600  1.000 84.37002  ? 141 VAL   A C   1 
ATOM   826  O  O   . VAL   A 1 105 ? 22.65800  -36.83500 -1.36900  1.000 80.27076  ? 141 VAL   A O   1 
ATOM   827  C  CB  . VAL   A 1 105 ? 23.77200  -40.00300 -1.64600  1.000 86.79391  ? 141 VAL   A CB  1 
ATOM   828  C  CG1 . VAL   A 1 105 ? 23.37000  -39.79700 -0.19600  1.000 78.57855  ? 141 VAL   A CG1 1 
ATOM   829  C  CG2 . VAL   A 1 105 ? 23.23900  -41.34000 -2.13300  1.000 83.43009  ? 141 VAL   A CG2 1 
ATOM   830  N  N   . GLN   A 1 106 ? 24.86800  -37.27800 -1.71000  1.000 86.78290  ? 142 GLN   A N   1 
ATOM   831  C  CA  . GLN   A 1 106 ? 25.34400  -36.08300 -1.02000  1.000 85.22337  ? 142 GLN   A CA  1 
ATOM   832  C  C   . GLN   A 1 106 ? 24.81700  -34.85700 -1.75700  1.000 79.68958  ? 142 GLN   A C   1 
ATOM   833  O  O   . GLN   A 1 106 ? 24.51200  -33.83200 -1.13400  1.000 78.88756  ? 142 GLN   A O   1 
ATOM   834  C  CB  . GLN   A 1 106 ? 26.86900  -36.07600 -0.99500  1.000 85.06050  ? 142 GLN   A CB  1 
ATOM   835  C  CG  . GLN   A 1 106 ? 27.47800  -37.39100 -0.52000  1.000 95.11598  ? 142 GLN   A CG  1 
ATOM   836  C  CD  . GLN   A 1 106 ? 28.97700  -37.32700 -0.42000  1.000 100.96297 ? 142 GLN   A CD  1 
ATOM   837  O  OE1 . GLN   A 1 106 ? 29.52200  -37.05000 0.64600   1.000 109.29583 ? 142 GLN   A OE1 1 
ATOM   838  N  NE2 . GLN   A 1 106 ? 29.65700  -37.57100 -1.53200  1.000 98.42391  ? 142 GLN   A NE2 1 
ATOM   839  N  N   . VAL   A 1 107 ? 24.67800  -34.95100 -3.08300  1.000 69.07947  ? 143 VAL   A N   1 
ATOM   840  C  CA  . VAL   A 1 107 ? 24.07100  -33.86100 -3.84100  1.000 74.48362  ? 143 VAL   A CA  1 
ATOM   841  C  C   . VAL   A 1 107 ? 22.60200  -33.69800 -3.45800  1.000 83.62998  ? 143 VAL   A C   1 
ATOM   842  O  O   . VAL   A 1 107 ? 22.12500  -32.57800 -3.24400  1.000 76.07087  ? 143 VAL   A O   1 
ATOM   843  C  CB  . VAL   A 1 107 ? 24.25000  -34.09200 -5.35500  1.000 68.37541  ? 143 VAL   A CB  1 
ATOM   844  C  CG1 . VAL   A 1 107 ? 23.24900  -33.26700 -6.14100  1.000 84.49236  ? 143 VAL   A CG1 1 
ATOM   845  C  CG2 . VAL   A 1 107 ? 25.66500  -33.72000 -5.77900  1.000 76.04702  ? 143 VAL   A CG2 1 
ATOM   846  N  N   . ALA   A 1 108 ? 21.87800  -34.81200 -3.32200  1.000 76.54344  ? 144 ALA   A N   1 
ATOM   847  C  CA  . ALA   A 1 108 ? 20.44100  -34.74300 -3.06500  1.000 81.32900  ? 144 ALA   A CA  1 
ATOM   848  C  C   . ALA   A 1 108 ? 20.13600  -34.09600 -1.71900  1.000 81.67865  ? 144 ALA   A C   1 
ATOM   849  O  O   . ALA   A 1 108 ? 19.15700  -33.34600 -1.58900  1.000 83.31236  ? 144 ALA   A O   1 
ATOM   850  C  CB  . ALA   A 1 108 ? 19.84000  -36.14400 -3.14100  1.000 79.11373  ? 144 ALA   A CB  1 
ATOM   851  N  N   . ILE   A 1 109 ? 20.96300  -34.36600 -0.70500  1.000 77.01291  ? 145 ILE   A N   1 
ATOM   852  C  CA  . ILE   A 1 109 ? 20.70900  -33.75300 0.59400   1.000 84.67268  ? 145 ILE   A CA  1 
ATOM   853  C  C   . ILE   A 1 109 ? 20.95400  -32.24200 0.54200   1.000 82.22524  ? 145 ILE   A C   1 
ATOM   854  O  O   . ILE   A 1 109 ? 20.25600  -31.46700 1.21100   1.000 83.45336  ? 145 ILE   A O   1 
ATOM   855  C  CB  . ILE   A 1 109 ? 21.55000  -34.43700 1.69000   1.000 88.49792  ? 145 ILE   A CB  1 
ATOM   856  C  CG1 . ILE   A 1 109 ? 21.23100  -35.95800 1.74800   1.000 89.20678  ? 145 ILE   A CG1 1 
ATOM   857  C  CG2 . ILE   A 1 109 ? 21.43100  -33.62000 3.04000   1.000 95.71225  ? 145 ILE   A CG2 1 
ATOM   858  C  CD1 . ILE   A 1 109 ? 22.38600  -36.87700 1.39700   1.000 80.55453  ? 145 ILE   A CD1 1 
ATOM   859  N  N   . GLN   A 1 110 ? 21.91400  -31.79000 -0.26800  1.000 80.46516  ? 146 GLN   A N   1 
ATOM   860  C  CA  . GLN   A 1 110 ? 22.14900  -30.35300 -0.38500  1.000 80.86514  ? 146 GLN   A CA  1 
ATOM   861  C  C   . GLN   A 1 110 ? 21.03100  -29.67400 -1.16300  1.000 77.66434  ? 146 GLN   A C   1 
ATOM   862  O  O   . GLN   A 1 110 ? 20.56000  -28.60200 -0.76800  1.000 80.17173  ? 146 GLN   A O   1 
ATOM   863  C  CB  . GLN   A 1 110 ? 23.50200  -30.08100 -1.04400  1.000 72.60715  ? 146 GLN   A CB  1 
ATOM   864  C  CG  . GLN   A 1 110 ? 24.69300  -30.62000 -0.26000  1.000 83.03520  ? 146 GLN   A CG  1 
ATOM   865  C  CD  . GLN   A 1 110 ? 25.98600  -29.88900 -0.57400  1.000 91.98717  ? 146 GLN   A CD  1 
ATOM   866  O  OE1 . GLN   A 1 110 ? 25.97100  -28.77300 -1.09600  1.000 97.99323  ? 146 GLN   A OE1 1 
ATOM   867  N  NE2 . GLN   A 1 110 ? 27.11200  -30.51400 -0.25100  1.000 85.34315  ? 146 GLN   A NE2 1 
ATOM   868  N  N   . MET   A 1 111 ? 20.58700  -30.28300 -2.26500  1.000 71.38474  ? 147 MET   A N   1 
ATOM   869  C  CA  . MET   A 1 111 ? 19.46600  -29.72400 -3.01300  1.000 79.81789  ? 147 MET   A CA  1 
ATOM   870  C  C   . MET   A 1 111 ? 18.20900  -29.67000 -2.15600  1.000 77.38795  ? 147 MET   A C   1 
ATOM   871  O  O   . MET   A 1 111 ? 17.50300  -28.65600 -2.14400  1.000 78.52908  ? 147 MET   A O   1 
ATOM   872  C  CB  . MET   A 1 111 ? 19.22100  -30.54300 -4.27900  1.000 80.20986  ? 147 MET   A CB  1 
ATOM   873  C  CG  . MET   A 1 111 ? 20.45000  -30.71600 -5.15200  1.000 70.56620  ? 147 MET   A CG  1 
ATOM   874  S  SD  . MET   A 1 111 ? 20.12400  -31.79700 -6.55700  1.000 80.62065  ? 147 MET   A SD  1 
ATOM   875  C  CE  . MET   A 1 111 ? 19.80700  -30.61100 -7.86000  1.000 80.34213  ? 147 MET   A CE  1 
ATOM   876  N  N   . LEU   A 1 112 ? 17.92100  -30.74900 -1.41900  1.000 77.02652  ? 148 LEU   A N   1 
ATOM   877  C  CA  . LEU   A 1 112 ? 16.75700  -30.76300 -0.53900  1.000 82.17513  ? 148 LEU   A CA  1 
ATOM   878  C  C   . LEU   A 1 112 ? 16.85100  -29.69300 0.54000   1.000 81.54218  ? 148 LEU   A C   1 
ATOM   879  O  O   . LEU   A 1 112 ? 15.82900  -29.11700 0.92600   1.000 84.02324  ? 148 LEU   A O   1 
ATOM   880  C  CB  . LEU   A 1 112 ? 16.59200  -32.14500 0.09400   1.000 86.65069  ? 148 LEU   A CB  1 
ATOM   881  C  CG  . LEU   A 1 112 ? 15.92900  -33.22200 -0.76900  1.000 83.03501  ? 148 LEU   A CG  1 
ATOM   882  C  CD1 . LEU   A 1 112 ? 16.10700  -34.59100 -0.14100  1.000 87.04819  ? 148 LEU   A CD1 1 
ATOM   883  C  CD2 . LEU   A 1 112 ? 14.45500  -32.90800 -0.95600  1.000 87.37420  ? 148 LEU   A CD2 1 
ATOM   884  N  N   . THR   A 1 113 ? 18.05800  -29.41200 1.03700   1.000 79.62134  ? 149 THR   A N   1 
ATOM   885  C  CA  . THR   A 1 113 ? 18.21400  -28.35400 2.03000   1.000 84.84322  ? 149 THR   A CA  1 
ATOM   886  C  C   . THR   A 1 113 ? 18.01000  -26.98000 1.40400   1.000 79.95776  ? 149 THR   A C   1 
ATOM   887  O  O   . THR   A 1 113 ? 17.37800  -26.10400 2.00700   1.000 80.90535  ? 149 THR   A O   1 
ATOM   888  C  CB  . THR   A 1 113 ? 19.59000  -28.45100 2.68800   1.000 85.74223  ? 149 THR   A CB  1 
ATOM   889  O  OG1 . THR   A 1 113 ? 19.72500  -29.72600 3.32800   1.000 90.61643  ? 149 THR   A OG1 1 
ATOM   890  C  CG2 . THR   A 1 113 ? 19.76200  -27.35200 3.72800   1.000 78.87945  ? 149 THR   A CG2 1 
ATOM   891  N  N   . LEU   A 1 114 ? 18.53400  -26.77400 0.19300   1.000 79.69063  ? 150 LEU   A N   1 
ATOM   892  C  CA  . LEU   A 1 114 ? 18.30900  -25.51700 -0.51400  1.000 75.41365  ? 150 LEU   A CA  1 
ATOM   893  C  C   . LEU   A 1 114 ? 16.82300  -25.29300 -0.76700  1.000 86.02003  ? 150 LEU   A C   1 
ATOM   894  O  O   . LEU   A 1 114 ? 16.28400  -24.22100 -0.47000  1.000 83.37461  ? 150 LEU   A O   1 
ATOM   895  C  CB  . LEU   A 1 114 ? 19.08400  -25.51100 -1.83200  1.000 73.79902  ? 150 LEU   A CB  1 
ATOM   896  C  CG  . LEU   A 1 114 ? 20.61100  -25.56800 -1.76600  1.000 87.92406  ? 150 LEU   A CG  1 
ATOM   897  C  CD1 . LEU   A 1 114 ? 21.18100  -26.03900 -3.09600  1.000 82.34669  ? 150 LEU   A CD1 1 
ATOM   898  C  CD2 . LEU   A 1 114 ? 21.18900  -24.21400 -1.38500  1.000 87.65637  ? 150 LEU   A CD2 1 
ATOM   899  N  N   . VAL   A 1 115 ? 16.14300  -26.30500 -1.31400  1.000 84.47162  ? 151 VAL   A N   1 
ATOM   900  C  CA  . VAL   A 1 115 ? 14.71800  -26.17900 -1.60700  1.000 87.10072  ? 151 VAL   A CA  1 
ATOM   901  C  C   . VAL   A 1 115 ? 13.91400  -26.00700 -0.32500  1.000 87.82232  ? 151 VAL   A C   1 
ATOM   902  O  O   . VAL   A 1 115 ? 12.89100  -25.30900 -0.31200  1.000 83.80929  ? 151 VAL   A O   1 
ATOM   903  C  CB  . VAL   A 1 115 ? 14.23900  -27.39600 -2.42600  1.000 83.77969  ? 151 VAL   A CB  1 
ATOM   904  C  CG1 . VAL   A 1 115 ? 12.74200  -27.32400 -2.67400  1.000 85.13536  ? 151 VAL   A CG1 1 
ATOM   905  C  CG2 . VAL   A 1 115 ? 14.99000  -27.47100 -3.74700  1.000 66.95319  ? 151 VAL   A CG2 1 
ATOM   906  N  N   . GLU   A 1 116 ? 14.36000  -26.62500 0.77100   1.000 85.25934  ? 152 GLU   A N   1 
ATOM   907  C  CA  . GLU   A 1 116 ? 13.70100  -26.40400 2.05400   1.000 86.62452  ? 152 GLU   A CA  1 
ATOM   908  C  C   . GLU   A 1 116 ? 13.82100  -24.94900 2.48800   1.000 91.14434  ? 152 GLU   A C   1 
ATOM   909  O  O   . GLU   A 1 116 ? 12.85200  -24.35700 2.97700   1.000 98.27815  ? 152 GLU   A O   1 
ATOM   910  C  CB  . GLU   A 1 116 ? 14.29300  -27.32200 3.12200   1.000 85.94041  ? 152 GLU   A CB  1 
ATOM   911  C  CG  . GLU   A 1 116 ? 13.72400  -27.08300 4.51200   1.000 86.80698  ? 152 GLU   A CG  1 
ATOM   912  C  CD  . GLU   A 1 116 ? 14.46100  -27.85300 5.58900   1.000 91.55383  ? 152 GLU   A CD  1 
ATOM   913  O  OE1 . GLU   A 1 116 ? 15.57000  -28.35200 5.31100   1.000 91.67643  ? 152 GLU   A OE1 1 
ATOM   914  O  OE2 . GLU   A 1 116 ? 13.92900  -27.95800 6.71500   1.000 92.71745  ? 152 GLU   A OE2 1 
ATOM   915  N  N   . GLU   A 1 117 ? 15.00300  -24.35500 2.31200   1.000 85.38395  ? 153 GLU   A N   1 
ATOM   916  C  CA  . GLU   A 1 117 ? 15.19800  -22.96700 2.71300   1.000 92.64689  ? 153 GLU   A CA  1 
ATOM   917  C  C   . GLU   A 1 117 ? 14.43400  -22.01000 1.80800   1.000 90.54340  ? 153 GLU   A C   1 
ATOM   918  O  O   . GLU   A 1 117 ? 14.06500  -20.91200 2.24100   1.000 94.72151  ? 153 GLU   A O   1 
ATOM   919  C  CB  . GLU   A 1 117 ? 16.69000  -22.62800 2.72000   1.000 93.10314  ? 153 GLU   A CB  1 
ATOM   920  C  CG  . GLU   A 1 117 ? 17.05400  -21.41500 3.56500   1.000 96.16756  ? 153 GLU   A CG  1 
ATOM   921  C  CD  . GLU   A 1 117 ? 17.12200  -21.72600 5.05300   1.000 106.05698 ? 153 GLU   A CD  1 
ATOM   922  O  OE1 . GLU   A 1 117 ? 16.74300  -22.84700 5.45400   1.000 107.13668 ? 153 GLU   A OE1 1 
ATOM   923  O  OE2 . GLU   A 1 117 ? 17.56200  -20.84700 5.82400   1.000 107.85081 ? 153 GLU   A OE2 1 
ATOM   924  N  N   . VAL   A 1 118 ? 14.18700  -22.40200 0.55700   1.000 89.94677  ? 154 VAL   A N   1 
ATOM   925  C  CA  . VAL   A 1 118 ? 13.36600  -21.58300 -0.32900  1.000 93.33504  ? 154 VAL   A CA  1 
ATOM   926  C  C   . VAL   A 1 118 ? 11.91600  -21.59200 0.13700   1.000 101.15373 ? 154 VAL   A C   1 
ATOM   927  O  O   . VAL   A 1 118 ? 11.28200  -20.53900 0.27300   1.000 92.99074  ? 154 VAL   A O   1 
ATOM   928  C  CB  . VAL   A 1 118 ? 13.49400  -22.06900 -1.78400  1.000 82.66154  ? 154 VAL   A CB  1 
ATOM   929  C  CG1 . VAL   A 1 118 ? 12.46900  -21.37600 -2.66700  1.000 86.16284  ? 154 VAL   A CG1 1 
ATOM   930  C  CG2 . VAL   A 1 118 ? 14.89800  -21.82000 -2.30300  1.000 88.74540  ? 154 VAL   A CG2 1 
ATOM   931  N  N   . HIS   A 1 119 ? 11.37100  -22.78500 0.39100   1.000 90.66789  ? 155 HIS   A N   1 
ATOM   932  C  CA  . HIS   A 1 119 ? 10.00400  -22.88500 0.88900   1.000 96.44545  ? 155 HIS   A CA  1 
ATOM   933  C  C   . HIS   A 1 119 ? 9.86600   -22.26300 2.26900   1.000 104.81160 ? 155 HIS   A C   1 
ATOM   934  O  O   . HIS   A 1 119 ? 8.77700   -21.80800 2.64000   1.000 107.42514 ? 155 HIS   A O   1 
ATOM   935  C  CB  . HIS   A 1 119 ? 9.56200   -24.34700 0.92200   1.000 94.23593  ? 155 HIS   A CB  1 
ATOM   936  C  CG  . HIS   A 1 119 ? 9.55800   -25.00500 -0.42100  1.000 91.96920  ? 155 HIS   A CG  1 
ATOM   937  N  ND1 . HIS   A 1 119 ? 9.48200   -26.37300 -0.58000  1.000 82.35580  ? 155 HIS   A ND1 1 
ATOM   938  C  CD2 . HIS   A 1 119 ? 9.62000   -24.48500 -1.66900  1.000 86.15466  ? 155 HIS   A CD2 1 
ATOM   939  C  CE1 . HIS   A 1 119 ? 9.49600   -26.66500 -1.86800  1.000 84.79291  ? 155 HIS   A CE1 1 
ATOM   940  N  NE2 . HIS   A 1 119 ? 9.58100   -25.53700 -2.55000  1.000 85.11085  ? 155 HIS   A NE2 1 
ATOM   941  N  N   . ARG   A 1 120 ? 10.95100  -22.23600 3.04400   1.000 106.21249 ? 156 ARG   A N   1 
ATOM   942  C  CA  . ARG   A 1 120 ? 10.92300  -21.56900 4.33800   1.000 110.10429 ? 156 ARG   A CA  1 
ATOM   943  C  C   . ARG   A 1 120 ? 10.66900  -20.07300 4.20700   1.000 114.33402 ? 156 ARG   A C   1 
ATOM   944  O  O   . ARG   A 1 120 ? 10.17000  -19.45400 5.15500   1.000 117.26406 ? 156 ARG   A O   1 
ATOM   945  C  CB  . ARG   A 1 120 ? 12.23700  -21.81500 5.07800   1.000 110.97154 ? 156 ARG   A CB  1 
ATOM   946  C  CG  . ARG   A 1 120 ? 12.13800  -22.80600 6.22300   1.000 114.09954 ? 156 ARG   A CG  1 
ATOM   947  C  CD  . ARG   A 1 120 ? 12.94000  -22.29700 7.40100   1.000 123.80157 ? 156 ARG   A CD  1 
ATOM   948  N  NE  . ARG   A 1 120 ? 12.54400  -20.93300 7.73200   1.000 135.76646 ? 156 ARG   A NE  1 
ATOM   949  C  CZ  . ARG   A 1 120 ? 13.25300  -20.10100 8.48100   1.000 138.89207 ? 156 ARG   A CZ  1 
ATOM   950  N  NH1 . ARG   A 1 120 ? 14.41700  -20.45700 8.99900   1.000 139.48748 ? 156 ARG   A NH1 1 
ATOM   951  N  NH2 . ARG   A 1 120 ? 12.78600  -18.87600 8.70900   1.000 139.41702 ? 156 ARG   A NH2 1 
ATOM   952  N  N   . HIS   A 1 121 ? 10.99700  -19.48200 3.05700   1.000 106.43094 ? 157 HIS   A N   1 
ATOM   953  C  CA  . HIS   A 1 121 ? 10.76900  -18.06500 2.81200   1.000 112.97783 ? 157 HIS   A CA  1 
ATOM   954  C  C   . HIS   A 1 121 ? 9.50600   -17.81400 1.99600   1.000 112.66004 ? 157 HIS   A C   1 
ATOM   955  O  O   . HIS   A 1 121 ? 9.37200   -16.74700 1.38600   1.000 108.91465 ? 157 HIS   A O   1 
ATOM   956  C  CB  . HIS   A 1 121 ? 11.98200  -17.44400 2.11900   1.000 111.05103 ? 157 HIS   A CB  1 
ATOM   957  C  CG  . HIS   A 1 121 ? 13.19000  -17.33900 2.99700   1.000 110.12219 ? 157 HIS   A CG  1 
ATOM   958  N  ND1 . HIS   A 1 121 ? 13.95400  -18.43200 3.34400   1.000 103.45105 ? 157 HIS   A ND1 1 
ATOM   959  C  CD2 . HIS   A 1 121 ? 13.76000  -16.27200 3.60500   1.000 111.85265 ? 157 HIS   A CD2 1 
ATOM   960  C  CE1 . HIS   A 1 121 ? 14.94600  -18.04200 4.12500   1.000 103.61932 ? 157 HIS   A CE1 1 
ATOM   961  N  NE2 . HIS   A 1 121 ? 14.85100  -16.73600 4.29900   1.000 107.51856 ? 157 HIS   A NE2 1 
ATOM   962  N  N   . ASP   A 1 122 ? 8.57900   -18.77700 1.97900   1.000 118.03272 ? 158 ASP   A N   1 
ATOM   963  C  CA  . ASP   A 1 122 ? 7.26600   -18.64000 1.34300   1.000 117.79578 ? 158 ASP   A CA  1 
ATOM   964  C  C   . ASP   A 1 122 ? 7.35600   -18.57800 -0.18000  1.000 118.91702 ? 158 ASP   A C   1 
ATOM   965  O  O   . ASP   A 1 122 ? 6.51400   -17.95200 -0.82700  1.000 120.72241 ? 158 ASP   A O   1 
ATOM   966  C  CB  . ASP   A 1 122 ? 6.50000   -17.41800 1.87300   1.000 117.70821 ? 158 ASP   A CB  1 
ATOM   967  C  CG  . ASP   A 1 122 ? 6.61800   -17.26200 3.38000   1.000 121.42996 ? 158 ASP   A CG  1 
ATOM   968  O  OD1 . ASP   A 1 122 ? 6.49500   -18.28200 4.09800   1.000 121.95716 ? 158 ASP   A OD1 1 
ATOM   969  O  OD2 . ASP   A 1 122 ? 6.83100   -16.12200 3.84200   1.000 127.99394 ? 158 ASP   A OD2 1 
ATOM   970  N  N   . LEU   A 1 123 ? 8.35500   -19.23400 -0.77000  1.000 104.34356 ? 159 LEU   A N   1 
ATOM   971  C  CA  . LEU   A 1 123 ? 8.53200   -19.25400 -2.21600  1.000 103.52045 ? 159 LEU   A CA  1 
ATOM   972  C  C   . LEU   A 1 123 ? 8.69700   -20.68500 -2.70600  1.000 96.93956  ? 159 LEU   A C   1 
ATOM   973  O  O   . LEU   A 1 123 ? 9.28400   -21.52300 -2.01600  1.000 96.58071  ? 159 LEU   A O   1 
ATOM   974  C  CB  . LEU   A 1 123 ? 9.75800   -18.43300 -2.64700  1.000 102.38053 ? 159 LEU   A CB  1 
ATOM   975  C  CG  . LEU   A 1 123 ? 9.61200   -16.93700 -2.94500  1.000 103.45257 ? 159 LEU   A CG  1 
ATOM   976  C  CD1 . LEU   A 1 123 ? 8.55500   -16.68700 -4.01500  1.000 104.56320 ? 159 LEU   A CD1 1 
ATOM   977  C  CD2 . LEU   A 1 123 ? 9.31000   -16.13900 -1.68300  1.000 110.94297 ? 159 LEU   A CD2 1 
ATOM   978  N  N   . ILE   A 1 124 ? 8.17200   -20.96000 -3.89800  1.000 92.06702  ? 160 ILE   A N   1 
ATOM   979  C  CA  . ILE   A 1 124 ? 8.44100   -22.20500 -4.60800  1.000 90.29262  ? 160 ILE   A CA  1 
ATOM   980  C  C   . ILE   A 1 124 ? 9.28600   -21.86900 -5.82600  1.000 96.63888  ? 160 ILE   A C   1 
ATOM   981  O  O   . ILE   A 1 124 ? 9.24000   -20.75100 -6.35200  1.000 94.47922  ? 160 ILE   A O   1 
ATOM   982  C  CB  . ILE   A 1 124 ? 7.15800   -22.96100 -5.01900  1.000 95.82226  ? 160 ILE   A CB  1 
ATOM   983  C  CG1 . ILE   A 1 124 ? 6.46900   -22.27500 -6.20100  1.000 103.68323 ? 160 ILE   A CG1 1 
ATOM   984  C  CG2 . ILE   A 1 124 ? 6.20700   -23.07800 -3.84000  1.000 102.70923 ? 160 ILE   A CG2 1 
ATOM   985  C  CD1 . ILE   A 1 124 ? 5.15200   -22.91800 -6.58500  1.000 99.68162  ? 160 ILE   A CD1 1 
ATOM   986  N  N   . TYR   A 1 125 ? 10.07100  -22.84700 -6.27400  1.000 88.90001  ? 161 TYR   A N   1 
ATOM   987  C  CA  . TYR   A 1 125 ? 11.04700  -22.59400 -7.32600  1.000 86.02176  ? 161 TYR   A CA  1 
ATOM   988  C  C   . TYR   A 1 125 ? 10.45900  -22.77900 -8.72300  1.000 91.80356  ? 161 TYR   A C   1 
ATOM   989  O  O   . TYR   A 1 125 ? 10.62700  -21.91100 -9.58500  1.000 94.98850  ? 161 TYR   A O   1 
ATOM   990  C  CB  . TYR   A 1 125 ? 12.26500  -23.50000 -7.12700  1.000 95.19932  ? 161 TYR   A CB  1 
ATOM   991  C  CG  . TYR   A 1 125 ? 13.45500  -23.10000 -7.96200  1.000 90.04524  ? 161 TYR   A CG  1 
ATOM   992  C  CD1 . TYR   A 1 125 ? 14.22300  -21.99300 -7.62400  1.000 84.19172  ? 161 TYR   A CD1 1 
ATOM   993  C  CD2 . TYR   A 1 125 ? 13.81000  -23.82800 -9.08600  1.000 88.90632  ? 161 TYR   A CD2 1 
ATOM   994  C  CE1 . TYR   A 1 125 ? 15.31100  -21.62400 -8.38700  1.000 88.99454  ? 161 TYR   A CE1 1 
ATOM   995  C  CE2 . TYR   A 1 125 ? 14.89300  -23.46700 -9.85200  1.000 89.51217  ? 161 TYR   A CE2 1 
ATOM   996  C  CZ  . TYR   A 1 125 ? 15.64100  -22.36700 -9.50100  1.000 92.51923  ? 161 TYR   A CZ  1 
ATOM   997  O  OH  . TYR   A 1 125 ? 16.72000  -22.01500 -10.27200 1.000 93.72658  ? 161 TYR   A OH  1 
ATOM   998  N  N   . ARG   A 1 126 ? 9.78300   -23.90400 -8.96300  1.000 92.13231  ? 162 ARG   A N   1 
ATOM   999  C  CA  . ARG   A 1 126 ? 9.07400   -24.23600 -10.19900 1.000 95.61819  ? 162 ARG   A CA  1 
ATOM   1000 C  C   . ARG   A 1 126 ? 9.98700   -24.42700 -11.40600 1.000 97.51800  ? 162 ARG   A C   1 
ATOM   1001 O  O   . ARG   A 1 126 ? 9.48200   -24.71500 -12.49800 1.000 98.67536  ? 162 ARG   A O   1 
ATOM   1002 C  CB  . ARG   A 1 126 ? 8.01200   -23.18900 -10.57200 1.000 96.92360  ? 162 ARG   A CB  1 
ATOM   1003 C  CG  . ARG   A 1 126 ? 6.71900   -23.28100 -9.78000  1.000 100.57521 ? 162 ARG   A CG  1 
ATOM   1004 C  CD  . ARG   A 1 126 ? 5.57300   -22.60800 -10.52600 1.000 104.65806 ? 162 ARG   A CD  1 
ATOM   1005 N  NE  . ARG   A 1 126 ? 5.70400   -21.15600 -10.56400 1.000 109.53134 ? 162 ARG   A NE  1 
ATOM   1006 C  CZ  . ARG   A 1 126 ? 5.07600   -20.37100 -11.43000 1.000 117.05797 ? 162 ARG   A CZ  1 
ATOM   1007 N  NH1 . ARG   A 1 126 ? 4.29100   -20.86700 -12.37100 1.000 115.77650 ? 162 ARG   A NH1 1 
ATOM   1008 N  NH2 . ARG   A 1 126 ? 5.24700   -19.05400 -11.35400 1.000 121.29723 ? 162 ARG   A NH2 1 
ATOM   1009 N  N   . ASP   A 1 127 ? 11.30200  -24.28300 -11.26000 1.000 103.93663 ? 163 ASP   A N   1 
ATOM   1010 C  CA  . ASP   A 1 127 ? 12.22600  -24.39600 -12.38400 1.000 102.47198 ? 163 ASP   A CA  1 
ATOM   1011 C  C   . ASP   A 1 127 ? 13.37200  -25.34000 -12.04600 1.000 94.02761  ? 163 ASP   A C   1 
ATOM   1012 O  O   . ASP   A 1 127 ? 14.53700  -25.06900 -12.34800 1.000 92.18676  ? 163 ASP   A O   1 
ATOM   1013 C  CB  . ASP   A 1 127 ? 12.75700  -23.02300 -12.79200 1.000 102.70691 ? 163 ASP   A CB  1 
ATOM   1014 C  CG  . ASP   A 1 127 ? 13.29900  -23.00100 -14.20900 1.000 102.12884 ? 163 ASP   A CG  1 
ATOM   1015 O  OD1 . ASP   A 1 127 ? 13.00200  -23.93900 -14.97900 1.000 96.02760  ? 163 ASP   A OD1 1 
ATOM   1016 O  OD2 . ASP   A 1 127 ? 14.02700  -22.04500 -14.55100 1.000 105.54300 ? 163 ASP   A OD2 1 
ATOM   1017 N  N   . ILE   A 1 128 ? 13.05200  -26.47100 -11.42000 1.000 81.08274  ? 164 ILE   A N   1 
ATOM   1018 C  CA  . ILE   A 1 128 ? 14.07400  -27.40900 -10.96500 1.000 84.10822  ? 164 ILE   A CA  1 
ATOM   1019 C  C   . ILE   A 1 128 ? 14.75200  -28.04600 -12.17200 1.000 84.21018  ? 164 ILE   A C   1 
ATOM   1020 O  O   . ILE   A 1 128 ? 14.10400  -28.71200 -12.98800 1.000 82.96542  ? 164 ILE   A O   1 
ATOM   1021 C  CB  . ILE   A 1 128 ? 13.46300  -28.47400 -10.04600 1.000 77.59147  ? 164 ILE   A CB  1 
ATOM   1022 C  CG1 . ILE   A 1 128 ? 13.00900  -27.84700 -8.72500  1.000 85.33545  ? 164 ILE   A CG1 1 
ATOM   1023 C  CG2 . ILE   A 1 128 ? 14.45700  -29.59600 -9.79400  1.000 77.48631  ? 164 ILE   A CG2 1 
ATOM   1024 C  CD1 . ILE   A 1 128 ? 14.14400  -27.33700 -7.87000  1.000 86.07140  ? 164 ILE   A CD1 1 
ATOM   1025 N  N   . LYS   A 1 129 ? 16.06700  -27.84000 -12.29000 1.000 70.23831  ? 165 LYS   A N   1 
ATOM   1026 C  CA  . LYS   A 1 129 ? 16.88300  -28.45700 -13.33100 1.000 83.12345  ? 165 LYS   A CA  1 
ATOM   1027 C  C   . LYS   A 1 129 ? 18.35600  -28.40000 -12.93100 1.000 87.09326  ? 165 LYS   A C   1 
ATOM   1028 O  O   . LYS   A 1 129 ? 18.77300  -27.46700 -12.23400 1.000 79.23459  ? 165 LYS   A O   1 
ATOM   1029 C  CB  . LYS   A 1 129 ? 16.66000  -27.77200 -14.68500 1.000 80.27680  ? 165 LYS   A CB  1 
ATOM   1030 C  CG  . LYS   A 1 129 ? 17.54100  -26.56200 -14.94500 1.000 86.31431  ? 165 LYS   A CG  1 
ATOM   1031 C  CD  . LYS   A 1 129 ? 17.27800  -25.95800 -16.31700 1.000 92.12950  ? 165 LYS   A CD  1 
ATOM   1032 C  CE  . LYS   A 1 129 ? 15.96000  -25.20400 -16.35000 1.000 92.69134  ? 165 LYS   A CE  1 
ATOM   1033 N  NZ  . LYS   A 1 129 ? 15.77200  -24.48900 -17.64200 1.000 91.83315  ? 165 LYS   A NZ  1 
ATOM   1034 N  N   . PRO   A 1 130 ? 19.17500  -29.37300 -13.34000 1.000 85.29870  ? 166 PRO   A N   1 
ATOM   1035 C  CA  . PRO   A 1 130 ? 20.59600  -29.36000 -12.96000 1.000 84.46569  ? 166 PRO   A CA  1 
ATOM   1036 C  C   . PRO   A 1 130 ? 21.39700  -28.23400 -13.58900 1.000 82.40953  ? 166 PRO   A C   1 
ATOM   1037 O  O   . PRO   A 1 130 ? 22.57000  -28.06600 -13.23600 1.000 83.82365  ? 166 PRO   A O   1 
ATOM   1038 C  CB  . PRO   A 1 130 ? 21.10100  -30.72700 -13.44800 1.000 81.71931  ? 166 PRO   A CB  1 
ATOM   1039 C  CG  . PRO   A 1 130 ? 19.87300  -31.55900 -13.62900 1.000 84.51555  ? 166 PRO   A CG  1 
ATOM   1040 C  CD  . PRO   A 1 130 ? 18.81100  -30.59900 -14.06200 1.000 86.28907  ? 166 PRO   A CD  1 
ATOM   1041 N  N   . ASP   A 1 131 ? 20.81900  -27.47100 -14.51500 1.000 85.99976  ? 167 ASP   A N   1 
ATOM   1042 C  CA  . ASP   A 1 131 ? 21.49600  -26.30200 -15.05700 1.000 88.60233  ? 167 ASP   A CA  1 
ATOM   1043 C  C   . ASP   A 1 131 ? 21.44600  -25.10900 -14.11200 1.000 86.70846  ? 167 ASP   A C   1 
ATOM   1044 O  O   . ASP   A 1 131 ? 22.21600  -24.16000 -14.29900 1.000 89.30817  ? 167 ASP   A O   1 
ATOM   1045 C  CB  . ASP   A 1 131 ? 20.88000  -25.92100 -16.40300 1.000 94.17695  ? 167 ASP   A CB  1 
ATOM   1046 C  CG  . ASP   A 1 131 ? 20.70500  -27.11400 -17.32200 1.000 96.82706  ? 167 ASP   A CG  1 
ATOM   1047 O  OD1 . ASP   A 1 131 ? 20.24200  -28.17100 -16.84400 1.000 89.56307  ? 167 ASP   A OD1 1 
ATOM   1048 O  OD2 . ASP   A 1 131 ? 21.02100  -26.99200 -18.52500 1.000 106.77538 ? 167 ASP   A OD2 1 
ATOM   1049 N  N   . ASN   A 1 132 ? 20.57300  -25.13900 -13.10500 1.000 84.91533  ? 168 ASN   A N   1 
ATOM   1050 C  CA  . ASN   A 1 132 ? 20.41300  -24.03700 -12.16700 1.000 85.09279  ? 168 ASN   A CA  1 
ATOM   1051 C  C   . ASN   A 1 132 ? 21.05700  -24.29700 -10.81200 1.000 82.61446  ? 168 ASN   A C   1 
ATOM   1052 O  O   . ASN   A 1 132 ? 21.00500  -23.42200 -9.94200  1.000 80.04494  ? 168 ASN   A O   1 
ATOM   1053 C  CB  . ASN   A 1 132 ? 18.92500  -23.71900 -11.97800 1.000 81.22989  ? 168 ASN   A CB  1 
ATOM   1054 C  CG  . ASN   A 1 132 ? 18.31100  -23.05700 -13.19600 1.000 89.92518  ? 168 ASN   A CG  1 
ATOM   1055 O  OD1 . ASN   A 1 132 ? 18.95100  -22.94100 -14.24100 1.000 91.84315  ? 168 ASN   A OD1 1 
ATOM   1056 N  ND2 . ASN   A 1 132 ? 17.06400  -22.62200 -13.06800 1.000 97.31308  ? 168 ASN   A ND2 1 
ATOM   1057 N  N   . PHE   A 1 133 ? 21.65000  -25.46900 -10.60200 1.000 77.69858  ? 169 PHE   A N   1 
ATOM   1058 C  CA  . PHE   A 1 133 ? 22.38900  -25.77100 -9.38200  1.000 78.40731  ? 169 PHE   A CA  1 
ATOM   1059 C  C   . PHE   A 1 133 ? 23.88000  -25.70700 -9.69000  1.000 73.69933  ? 169 PHE   A C   1 
ATOM   1060 O  O   . PHE   A 1 133 ? 24.38900  -26.51700 -10.47100 1.000 73.02303  ? 169 PHE   A O   1 
ATOM   1061 C  CB  . PHE   A 1 133 ? 22.01800  -27.14900 -8.83400  1.000 80.59150  ? 169 PHE   A CB  1 
ATOM   1062 C  CG  . PHE   A 1 133 ? 20.61000  -27.24500 -8.31000  1.000 80.68781  ? 169 PHE   A CG  1 
ATOM   1063 C  CD1 . PHE   A 1 133 ? 19.54300  -27.37900 -9.18100  1.000 77.96141  ? 169 PHE   A CD1 1 
ATOM   1064 C  CD2 . PHE   A 1 133 ? 20.35800  -27.22700 -6.94600  1.000 79.67313  ? 169 PHE   A CD2 1 
ATOM   1065 C  CE1 . PHE   A 1 133 ? 18.24900  -27.48100 -8.70700  1.000 75.74087  ? 169 PHE   A CE1 1 
ATOM   1066 C  CE2 . PHE   A 1 133 ? 19.06300  -27.32500 -6.46400  1.000 79.39800  ? 169 PHE   A CE2 1 
ATOM   1067 C  CZ  . PHE   A 1 133 ? 18.00800  -27.45400 -7.34800  1.000 72.10933  ? 169 PHE   A CZ  1 
ATOM   1068 N  N   . LEU   A 1 134 ? 24.57400  -24.75100 -9.08300  1.000 79.73297  ? 170 LEU   A N   1 
ATOM   1069 C  CA  . LEU   A 1 134 ? 25.98800  -24.53700 -9.34100  1.000 78.20502  ? 170 LEU   A CA  1 
ATOM   1070 C  C   . LEU   A 1 134 ? 26.81500  -24.86700 -8.10500  1.000 76.73569  ? 170 LEU   A C   1 
ATOM   1071 O  O   . LEU   A 1 134 ? 26.34900  -24.73200 -6.96900  1.000 76.24453  ? 170 LEU   A O   1 
ATOM   1072 C  CB  . LEU   A 1 134 ? 26.26700  -23.08800 -9.75700  1.000 78.14250  ? 170 LEU   A CB  1 
ATOM   1073 C  CG  . LEU   A 1 134 ? 25.31000  -22.36800 -10.70900 1.000 83.57273  ? 170 LEU   A CG  1 
ATOM   1074 C  CD1 . LEU   A 1 134 ? 25.87300  -20.99900 -11.08200 1.000 86.17427  ? 170 LEU   A CD1 1 
ATOM   1075 C  CD2 . LEU   A 1 134 ? 25.03500  -23.19000 -11.95400 1.000 78.00372  ? 170 LEU   A CD2 1 
ATOM   1076 N  N   . ILE   A 1 135 ? 28.05200  -25.30100 -8.34200  1.000 79.94409  ? 171 ILE   A N   1 
ATOM   1077 C  CA  . ILE   A 1 135 ? 29.04300  -25.39800 -7.27800  1.000 84.49782  ? 171 ILE   A CA  1 
ATOM   1078 C  C   . ILE   A 1 135 ? 29.73800  -24.05100 -7.16400  1.000 82.98520  ? 171 ILE   A C   1 
ATOM   1079 O  O   . ILE   A 1 135 ? 29.57000  -23.18300 -8.03000  1.000 72.56885  ? 171 ILE   A O   1 
ATOM   1080 C  CB  . ILE   A 1 135 ? 30.05600  -26.52600 -7.54000  1.000 89.25588  ? 171 ILE   A CB  1 
ATOM   1081 C  CG1 . ILE   A 1 135 ? 30.44400  -26.54900 -9.02000  1.000 85.46150  ? 171 ILE   A CG1 1 
ATOM   1082 C  CG2 . ILE   A 1 135 ? 29.49700  -27.86500 -7.05900  1.000 86.43583  ? 171 ILE   A CG2 1 
ATOM   1083 C  CD1 . ILE   A 1 135 ? 31.74600  -27.26500 -9.31100  1.000 82.52344  ? 171 ILE   A CD1 1 
ATOM   1084 N  N   . GLY   A 1 136 ? 30.51400  -23.86400 -6.10200  1.000 90.91460  ? 172 GLY   A N   1 
ATOM   1085 C  CA  . GLY   A 1 136 ? 31.30600  -22.66500 -5.97800  1.000 96.20459  ? 172 GLY   A CA  1 
ATOM   1086 C  C   . GLY   A 1 136 ? 32.46100  -22.64700 -6.95500  1.000 89.90696  ? 172 GLY   A C   1 
ATOM   1087 O  O   . GLY   A 1 136 ? 32.55200  -23.43700 -7.88700  1.000 82.53908  ? 172 GLY   A O   1 
ATOM   1088 N  N   . ARG   A 1 137 ? 33.36300  -21.70900 -6.71100  1.000 99.38722  ? 173 ARG   A N   1 
ATOM   1089 C  CA  . ARG   A 1 137 ? 34.53600  -21.54700 -7.55500  1.000 104.66453 ? 173 ARG   A CA  1 
ATOM   1090 C  C   . ARG   A 1 137 ? 35.78700  -22.05800 -6.85100  1.000 111.70614 ? 173 ARG   A C   1 
ATOM   1091 O  O   . ARG   A 1 137 ? 35.82600  -22.21700 -5.62900  1.000 120.45557 ? 173 ARG   A O   1 
ATOM   1092 C  CB  . ARG   A 1 137 ? 34.72100  -20.08400 -7.96800  1.000 95.23990  ? 173 ARG   A CB  1 
ATOM   1093 C  CG  . ARG   A 1 137 ? 33.93200  -19.72300 -9.21400  1.000 98.28456  ? 173 ARG   A CG  1 
ATOM   1094 C  CD  . ARG   A 1 137 ? 34.07100  -18.25500 -9.58000  1.000 107.22364 ? 173 ARG   A CD  1 
ATOM   1095 N  NE  . ARG   A 1 137 ? 35.22100  -17.98500 -10.43700 1.000 113.37032 ? 173 ARG   A NE  1 
ATOM   1096 C  CZ  . ARG   A 1 137 ? 35.23700  -18.16900 -11.75000 1.000 116.63541 ? 173 ARG   A CZ  1 
ATOM   1097 N  NH1 . ARG   A 1 137 ? 34.21300  -18.71600 -12.38500 1.000 115.69439 ? 173 ARG   A NH1 1 
ATOM   1098 N  NH2 . ARG   A 1 137 ? 36.30000  -17.77900 -12.44600 1.000 123.74376 ? 173 ARG   A NH2 1 
ATOM   1099 N  N   . ARG   A 1 138 ? 36.82200  -22.29600 -7.65400  1.000 121.94481 ? 174 ARG   A N   1 
ATOM   1100 C  CA  . ARG   A 1 138 ? 38.05300  -22.90000 -7.16500  1.000 133.95863 ? 174 ARG   A CA  1 
ATOM   1101 C  C   . ARG   A 1 138 ? 38.67400  -22.05300 -6.06100  1.000 131.41128 ? 174 ARG   A C   1 
ATOM   1102 O  O   . ARG   A 1 138 ? 38.69200  -20.82100 -6.13500  1.000 131.67041 ? 174 ARG   A O   1 
ATOM   1103 C  CB  . ARG   A 1 138 ? 39.04000  -23.06700 -8.32400  1.000 132.32214 ? 174 ARG   A CB  1 
ATOM   1104 C  CG  . ARG   A 1 138 ? 40.05200  -24.18800 -8.13700  1.000 132.73565 ? 174 ARG   A CG  1 
ATOM   1105 C  CD  . ARG   A 1 138 ? 39.59600  -25.46400 -8.83300  1.000 140.32905 ? 174 ARG   A CD  1 
ATOM   1106 N  NE  . ARG   A 1 138 ? 39.42000  -25.27500 -10.27000 1.000 156.88208 ? 174 ARG   A NE  1 
ATOM   1107 C  CZ  . ARG   A 1 138 ? 39.23600  -26.26100 -11.13700 1.000 170.28500 ? 174 ARG   A CZ  1 
ATOM   1108 N  NH1 . ARG   A 1 138 ? 39.21100  -27.52600 -10.74900 1.000 174.36069 ? 174 ARG   A NH1 1 
ATOM   1109 N  NH2 . ARG   A 1 138 ? 39.07600  -25.97300 -12.42500 1.000 178.18538 ? 174 ARG   A NH2 1 
ATOM   1110 N  N   . GLY   A 1 139 ? 39.18800  -22.72400 -5.03000  1.000 131.02656 ? 175 GLY   A N   1 
ATOM   1111 C  CA  . GLY   A 1 139 ? 39.83300  -22.06000 -3.91900  1.000 142.55922 ? 175 GLY   A CA  1 
ATOM   1112 C  C   . GLY   A 1 139 ? 38.90800  -21.52100 -2.84900  1.000 151.59345 ? 175 GLY   A C   1 
ATOM   1113 O  O   . GLY   A 1 139 ? 39.35700  -21.30100 -1.71600  1.000 153.81131 ? 175 GLY   A O   1 
ATOM   1114 N  N   . ALA   A 1 140 ? 37.63500  -21.30000 -3.16100  1.000 170.32150 ? 176 ALA   A N   1 
ATOM   1115 C  CA  . ALA   A 1 140 ? 36.70100  -20.77100 -2.18300  1.000 172.73011 ? 176 ALA   A CA  1 
ATOM   1116 C  C   . ALA   A 1 140 ? 36.30100  -21.84900 -1.18000  1.000 177.08716 ? 176 ALA   A C   1 
ATOM   1117 O  O   . ALA   A 1 140 ? 36.43000  -23.05100 -1.43000  1.000 172.61809 ? 176 ALA   A O   1 
ATOM   1118 C  CB  . ALA   A 1 140 ? 35.46000  -20.20700 -2.87500  1.000 167.79505 ? 176 ALA   A CB  1 
ATOM   1119 N  N   . THR   A 1 141 ? 35.80600  -21.39700 -0.02400  1.000 182.23556 ? 177 THR   A N   1 
ATOM   1120 C  CA  . THR   A 1 141 ? 35.38800  -22.32100 1.02400   1.000 178.69206 ? 177 THR   A CA  1 
ATOM   1121 C  C   . THR   A 1 141 ? 34.16200  -23.13000 0.62700   1.000 165.38306 ? 177 THR   A C   1 
ATOM   1122 O  O   . THR   A 1 141 ? 33.88000  -24.15700 1.25200   1.000 164.29838 ? 177 THR   A O   1 
ATOM   1123 C  CB  . THR   A 1 141 ? 35.09000  -21.55800 2.31500   1.000 186.55830 ? 177 THR   A CB  1 
ATOM   1124 O  OG1 . THR   A 1 141 ? 33.76100  -21.02200 2.26000   1.000 188.24093 ? 177 THR   A OG1 1 
ATOM   1125 C  CG2 . THR   A 1 141 ? 36.07800  -20.41500 2.49600   1.000 179.74273 ? 177 THR   A CG2 1 
ATOM   1126 N  N   . ASP   A 1 142 ? 33.43000  -22.69100 -0.39100  1.000 151.68979 ? 178 ASP   A N   1 
ATOM   1127 C  CA  . ASP   A 1 142 ? 32.22800  -23.35800 -0.87100  1.000 135.34319 ? 178 ASP   A CA  1 
ATOM   1128 C  C   . ASP   A 1 142 ? 32.40500  -23.81300 -2.31400  1.000 121.99277 ? 178 ASP   A C   1 
ATOM   1129 O  O   . ASP   A 1 142 ? 31.46500  -23.79000 -3.11200  1.000 116.02890 ? 178 ASP   A O   1 
ATOM   1130 C  CB  . ASP   A 1 142 ? 31.01500  -22.44200 -0.73200  1.000 135.10440 ? 178 ASP   A CB  1 
ATOM   1131 C  CG  . ASP   A 1 142 ? 31.27300  -21.04600 -1.27000  1.000 139.19162 ? 178 ASP   A CG  1 
ATOM   1132 O  OD1 . ASP   A 1 142 ? 32.34000  -20.82800 -1.88400  1.000 136.88092 ? 178 ASP   A OD1 1 
ATOM   1133 O  OD2 . ASP   A 1 142 ? 30.41100  -20.16500 -1.07400  1.000 133.93292 ? 178 ASP   A OD2 1 
ATOM   1134 N  N   . GLU   A 1 143 ? 33.62400  -24.23700 -2.65800  1.000 117.72429 ? 179 GLU   A N   1 
ATOM   1135 C  CA  . GLU   A 1 143 ? 33.92600  -24.61600 -4.03600  1.000 110.49438 ? 179 GLU   A CA  1 
ATOM   1136 C  C   . GLU   A 1 143 ? 33.04200  -25.76400 -4.51000  1.000 107.53354 ? 179 GLU   A C   1 
ATOM   1137 O  O   . GLU   A 1 143 ? 32.57700  -25.76600 -5.65700  1.000 102.36034 ? 179 GLU   A O   1 
ATOM   1138 C  CB  . GLU   A 1 143 ? 35.39900  -24.99800 -4.16100  1.000 125.46898 ? 179 GLU   A CB  1 
ATOM   1139 C  CG  . GLU   A 1 143 ? 35.78900  -25.53600 -5.52600  1.000 118.97914 ? 179 GLU   A CG  1 
ATOM   1140 C  CD  . GLU   A 1 143 ? 37.26100  -25.88600 -5.62200  1.000 120.43667 ? 179 GLU   A CD  1 
ATOM   1141 O  OE1 . GLU   A 1 143 ? 38.04800  -25.40800 -4.77800  1.000 120.61498 ? 179 GLU   A OE1 1 
ATOM   1142 O  OE2 . GLU   A 1 143 ? 37.63000  -26.64200 -6.54600  1.000 125.84315 ? 179 GLU   A OE2 1 
ATOM   1143 N  N   . ASN   A 1 144 ? 32.80100  -26.74900 -3.64700  1.000 104.25579 ? 180 ASN   A N   1 
ATOM   1144 C  CA  . ASN   A 1 144 ? 31.97500  -27.89700 -3.99300  1.000 98.77379  ? 180 ASN   A CA  1 
ATOM   1145 C  C   . ASN   A 1 144 ? 30.59600  -27.86300 -3.34800  1.000 101.15382 ? 180 ASN   A C   1 
ATOM   1146 O  O   . ASN   A 1 144 ? 29.80000  -28.78000 -3.57800  1.000 90.59220  ? 180 ASN   A O   1 
ATOM   1147 C  CB  . ASN   A 1 144 ? 32.69200  -29.19800 -3.62100  1.000 99.26701  ? 180 ASN   A CB  1 
ATOM   1148 C  CG  . ASN   A 1 144 ? 33.43500  -29.80400 -4.79500  1.000 106.02480 ? 180 ASN   A CG  1 
ATOM   1149 O  OD1 . ASN   A 1 144 ? 32.94500  -30.73100 -5.44100  1.000 105.89689 ? 180 ASN   A OD1 1 
ATOM   1150 N  ND2 . ASN   A 1 144 ? 34.62000  -29.27700 -5.08400  1.000 104.69145 ? 180 ASN   A ND2 1 
ATOM   1151 N  N   . ASN   A 1 145 ? 30.29100  -26.84500 -2.54600  1.000 107.18157 ? 181 ASN   A N   1 
ATOM   1152 C  CA  . ASN   A 1 145 ? 28.92500  -26.66400 -2.07600  1.000 102.87318 ? 181 ASN   A CA  1 
ATOM   1153 C  C   . ASN   A 1 145 ? 28.01300  -26.33900 -3.25300  1.000 92.67499  ? 181 ASN   A C   1 
ATOM   1154 O  O   . ASN   A 1 145 ? 28.36100  -25.53900 -4.12500  1.000 87.25573  ? 181 ASN   A O   1 
ATOM   1155 C  CB  . ASN   A 1 145 ? 28.85000  -25.54900 -1.03200  1.000 102.29979 ? 181 ASN   A CB  1 
ATOM   1156 C  CG  . ASN   A 1 145 ? 29.17900  -26.03300 0.36700   1.000 106.45512 ? 181 ASN   A CG  1 
ATOM   1157 O  OD1 . ASN   A 1 145 ? 29.48100  -27.20900 0.57300   1.000 104.22485 ? 181 ASN   A OD1 1 
ATOM   1158 N  ND2 . ASN   A 1 145 ? 29.12000  -25.12800 1.33600   1.000 113.18206 ? 181 ASN   A ND2 1 
ATOM   1159 N  N   . VAL   A 1 146 ? 26.84400  -26.97400 -3.28000  1.000 94.01862  ? 182 VAL   A N   1 
ATOM   1160 C  CA  . VAL   A 1 146 ? 25.87200  -26.76700 -4.34600  1.000 87.18535  ? 182 VAL   A CA  1 
ATOM   1161 C  C   . VAL   A 1 146 ? 25.02400  -25.54700 -4.01300  1.000 87.27823  ? 182 VAL   A C   1 
ATOM   1162 O  O   . VAL   A 1 146 ? 24.44800  -25.45700 -2.92300  1.000 87.46855  ? 182 VAL   A O   1 
ATOM   1163 C  CB  . VAL   A 1 146 ? 24.99600  -28.01400 -4.53700  1.000 82.25839  ? 182 VAL   A CB  1 
ATOM   1164 C  CG1 . VAL   A 1 146 ? 23.74600  -27.67000 -5.33900  1.000 73.91383  ? 182 VAL   A CG1 1 
ATOM   1165 C  CG2 . VAL   A 1 146 ? 25.79000  -29.10900 -5.23200  1.000 80.61138  ? 182 VAL   A CG2 1 
ATOM   1166 N  N   . HIS   A 1 147 ? 24.95700  -24.60500 -4.94900  1.000 82.33035  ? 183 HIS   A N   1 
ATOM   1167 C  CA  . HIS   A 1 147 ? 24.18300  -23.38300 -4.79500  1.000 87.04387  ? 183 HIS   A CA  1 
ATOM   1168 C  C   . HIS   A 1 147 ? 22.98200  -23.40200 -5.73400  1.000 83.65991  ? 183 HIS   A C   1 
ATOM   1169 O  O   . HIS   A 1 147 ? 22.93900  -24.15700 -6.70900  1.000 79.42045  ? 183 HIS   A O   1 
ATOM   1170 C  CB  . HIS   A 1 147 ? 25.04500  -22.14600 -5.07800  1.000 87.87924  ? 183 HIS   A CB  1 
ATOM   1171 C  CG  . HIS   A 1 147 ? 26.27300  -22.04900 -4.22500  1.000 89.89460  ? 183 HIS   A CG  1 
ATOM   1172 N  ND1 . HIS   A 1 147 ? 27.31600  -22.94700 -4.31200  1.000 84.11602  ? 183 HIS   A ND1 1 
ATOM   1173 C  CD2 . HIS   A 1 147 ? 26.63000  -21.15000 -3.27700  1.000 92.34151  ? 183 HIS   A CD2 1 
ATOM   1174 C  CE1 . HIS   A 1 147 ? 28.25800  -22.61000 -3.44900  1.000 91.98917  ? 183 HIS   A CE1 1 
ATOM   1175 N  NE2 . HIS   A 1 147 ? 27.86600  -21.52400 -2.80800  1.000 102.86020 ? 183 HIS   A NE2 1 
ATOM   1176 N  N   . LEU   A 1 148 ? 22.00100  -22.55600 -5.42500  1.000 84.57889  ? 184 LEU   A N   1 
ATOM   1177 C  CA  . LEU   A 1 148 ? 20.80700  -22.39600 -6.24400  1.000 82.29899  ? 184 LEU   A CA  1 
ATOM   1178 C  C   . LEU   A 1 148 ? 20.73300  -20.96900 -6.76900  1.000 84.09365  ? 184 LEU   A C   1 
ATOM   1179 O  O   . LEU   A 1 148 ? 20.99100  -20.01200 -6.03300  1.000 84.26182  ? 184 LEU   A O   1 
ATOM   1180 C  CB  . LEU   A 1 148 ? 19.53900  -22.72500 -5.45100  1.000 85.93966  ? 184 LEU   A CB  1 
ATOM   1181 C  CG  . LEU   A 1 148 ? 18.24800  -22.75700 -6.27500  1.000 85.26093  ? 184 LEU   A CG  1 
ATOM   1182 C  CD1 . LEU   A 1 148 ? 18.30400  -23.86400 -7.33800  1.000 82.48369  ? 184 LEU   A CD1 1 
ATOM   1183 C  CD2 . LEU   A 1 148 ? 17.02800  -22.92100 -5.37300  1.000 92.83762  ? 184 LEU   A CD2 1 
ATOM   1184 N  N   . ILE   A 1 149 ? 20.37700  -20.83200 -8.04500  1.000 81.00269  ? 185 ILE   A N   1 
ATOM   1185 C  CA  . ILE   A 1 149 ? 20.30800  -19.54700 -8.72700  1.000 88.83178  ? 185 ILE   A CA  1 
ATOM   1186 C  C   . ILE   A 1 149 ? 19.08100  -19.54300 -9.63300  1.000 92.15692  ? 185 ILE   A C   1 
ATOM   1187 O  O   . ILE   A 1 149 ? 18.31800  -20.51000 -9.68200  1.000 93.03860  ? 185 ILE   A O   1 
ATOM   1188 C  CB  . ILE   A 1 149 ? 21.58200  -19.25400 -9.54400  1.000 84.91656  ? 185 ILE   A CB  1 
ATOM   1189 C  CG1 . ILE   A 1 149 ? 21.87700  -20.42400 -10.48000 1.000 89.08480  ? 185 ILE   A CG1 1 
ATOM   1190 C  CG2 . ILE   A 1 149 ? 22.76600  -18.99500 -8.62500  1.000 90.36526  ? 185 ILE   A CG2 1 
ATOM   1191 C  CD1 . ILE   A 1 149 ? 22.22100  -20.01300 -11.87600 1.000 91.41937  ? 185 ILE   A CD1 1 
ATOM   1192 N  N   . ASP   A 1 150 ? 18.90000  -18.43400 -10.35700 1.000 95.10099  ? 186 ASP   A N   1 
ATOM   1193 C  CA  . ASP   A 1 150 ? 17.83400  -18.27300 -11.34400 1.000 97.69841  ? 186 ASP   A CA  1 
ATOM   1194 C  C   . ASP   A 1 150 ? 16.45400  -18.44100 -10.71900 1.000 95.94747  ? 186 ASP   A C   1 
ATOM   1195 O  O   . ASP   A 1 150 ? 15.90500  -19.54800 -10.69400 1.000 93.10057  ? 186 ASP   A O   1 
ATOM   1196 C  CB  . ASP   A 1 150 ? 18.02000  -19.26300 -12.50000 1.000 97.02789  ? 186 ASP   A CB  1 
ATOM   1197 C  CG  . ASP   A 1 150 ? 17.21100  -18.88900 -13.73500 1.000 99.73913  ? 186 ASP   A CG  1 
ATOM   1198 O  OD1 . ASP   A 1 150 ? 16.14500  -18.25300 -13.59500 1.000 102.29181 ? 186 ASP   A OD1 1 
ATOM   1199 O  OD2 . ASP   A 1 150 ? 17.64600  -19.23600 -14.85300 1.000 102.80844 ? 186 ASP   A OD2 1 
ATOM   1200 N  N   . PHE   A 1 151 ? 15.87400  -17.34500 -10.23100 1.000 102.83735 ? 187 PHE   A N   1 
ATOM   1201 C  CA  . PHE   A 1 151 ? 14.54800  -17.35900 -9.62800  1.000 102.00009 ? 187 PHE   A CA  1 
ATOM   1202 C  C   . PHE   A 1 151 ? 13.52100  -16.63100 -10.49100 1.000 103.05073 ? 187 PHE   A C   1 
ATOM   1203 O  O   . PHE   A 1 151 ? 12.53500  -16.09800 -9.97600  1.000 98.46763  ? 187 PHE   A O   1 
ATOM   1204 C  CB  . PHE   A 1 151 ? 14.59200  -16.75600 -8.22600  1.000 95.96231  ? 187 PHE   A CB  1 
ATOM   1205 C  CG  . PHE   A 1 151 ? 15.37600  -17.57500 -7.24300  1.000 95.30903  ? 187 PHE   A CG  1 
ATOM   1206 C  CD1 . PHE   A 1 151 ? 16.75500  -17.46200 -7.17100  1.000 97.41029  ? 187 PHE   A CD1 1 
ATOM   1207 C  CD2 . PHE   A 1 151 ? 14.73500  -18.46000 -6.39300  1.000 82.96162  ? 187 PHE   A CD2 1 
ATOM   1208 C  CE1 . PHE   A 1 151 ? 17.48000  -18.21600 -6.27000  1.000 93.02615  ? 187 PHE   A CE1 1 
ATOM   1209 C  CE2 . PHE   A 1 151 ? 15.45400  -19.21600 -5.48900  1.000 82.85672  ? 187 PHE   A CE2 1 
ATOM   1210 C  CZ  . PHE   A 1 151 ? 16.83000  -19.09400 -5.42800  1.000 87.91134  ? 187 PHE   A CZ  1 
ATOM   1211 N  N   . GLY   A 1 152 ? 13.73900  -16.60400 -11.80600 1.000 103.66374 ? 188 GLY   A N   1 
ATOM   1212 C  CA  . GLY   A 1 152 ? 12.77500  -16.01400 -12.71900 1.000 106.72612 ? 188 GLY   A CA  1 
ATOM   1213 C  C   . GLY   A 1 152 ? 11.46800  -16.77000 -12.82100 1.000 104.94514 ? 188 GLY   A C   1 
ATOM   1214 O  O   . GLY   A 1 152 ? 10.52600  -16.26400 -13.44000 1.000 107.68756 ? 188 GLY   A O   1 
ATOM   1215 N  N   . MET   A 1 153 ? 11.39200  -17.96600 -12.23500 1.000 103.62344 ? 189 MET   A N   1 
ATOM   1216 C  CA  . MET   A 1 153 ? 10.16400  -18.75100 -12.18700 1.000 98.97348  ? 189 MET   A CA  1 
ATOM   1217 C  C   . MET   A 1 153 ? 9.67200   -18.94200 -10.75600 1.000 99.84052  ? 189 MET   A C   1 
ATOM   1218 O  O   . MET   A 1 153 ? 8.84200   -19.82100 -10.50100 1.000 99.28053  ? 189 MET   A O   1 
ATOM   1219 C  CB  . MET   A 1 153 ? 10.37200  -20.10900 -12.86100 1.000 103.21776 ? 189 MET   A CB  1 
ATOM   1220 C  CG  . MET   A 1 153 ? 9.36400   -20.43700 -13.95300 1.000 108.62936 ? 189 MET   A CG  1 
ATOM   1221 S  SD  . MET   A 1 153 ? 9.51400   -19.35000 -15.38400 1.000 121.74296 ? 189 MET   A SD  1 
ATOM   1222 C  CE  . MET   A 1 153 ? 11.27000  -19.47900 -15.71400 1.000 109.51731 ? 189 MET   A CE  1 
ATOM   1223 N  N   . ALA   A 1 154 ? 10.16600  -18.13800 -9.81700  1.000 94.92410  ? 190 ALA   A N   1 
ATOM   1224 C  CA  . ALA   A 1 154 ? 9.80600   -18.29000 -8.41500  1.000 99.19424  ? 190 ALA   A CA  1 
ATOM   1225 C  C   . ALA   A 1 154 ? 8.47200   -17.61200 -8.13200  1.000 102.66968 ? 190 ALA   A C   1 
ATOM   1226 O  O   . ALA   A 1 154 ? 8.29600   -16.42200 -8.41200  1.000 100.85012 ? 190 ALA   A O   1 
ATOM   1227 C  CB  . ALA   A 1 154 ? 10.89700  -17.70700 -7.51900  1.000 80.28124  ? 190 ALA   A CB  1 
ATOM   1228 N  N   . LYS   A 1 155 ? 7.53600   -18.37100 -7.56800  1.000 98.33443  ? 191 LYS   A N   1 
ATOM   1229 C  CA  . LYS   A 1 155 ? 6.19900   -17.88700 -7.26000  1.000 106.41937 ? 191 LYS   A CA  1 
ATOM   1230 C  C   . LYS   A 1 155 ? 5.89900   -18.09100 -5.78200  1.000 105.10442 ? 191 LYS   A C   1 
ATOM   1231 O  O   . LYS   A 1 155 ? 6.26600   -19.11600 -5.19800  1.000 102.49767 ? 191 LYS   A O   1 
ATOM   1232 C  CB  . LYS   A 1 155 ? 5.14500   -18.60100 -8.11700  1.000 110.44284 ? 191 LYS   A CB  1 
ATOM   1233 C  CG  . LYS   A 1 155 ? 3.71700   -18.48200 -7.60300  1.000 108.23318 ? 191 LYS   A CG  1 
ATOM   1234 C  CD  . LYS   A 1 155 ? 2.70900   -18.89000 -8.66400  1.000 114.56810 ? 191 LYS   A CD  1 
ATOM   1235 C  CE  . LYS   A 1 155 ? 2.60000   -17.82500 -9.74400  1.000 117.80703 ? 191 LYS   A CE  1 
ATOM   1236 N  NZ  . LYS   A 1 155 ? 1.76700   -18.27300 -10.89300 1.000 117.48046 ? 191 LYS   A NZ  1 
ATOM   1237 N  N   . GLN   A 1 156 ? 5.23800   -17.10600 -5.18300  1.000 108.68270 ? 192 GLN   A N   1 
ATOM   1238 C  CA  . GLN   A 1 156 ? 4.82600   -17.21000 -3.79200  1.000 115.27406 ? 192 GLN   A CA  1 
ATOM   1239 C  C   . GLN   A 1 156 ? 3.67900   -18.20400 -3.65000  1.000 110.67257 ? 192 GLN   A C   1 
ATOM   1240 O  O   . GLN   A 1 156 ? 2.72800   -18.19400 -4.43600  1.000 113.69743 ? 192 GLN   A O   1 
ATOM   1241 C  CB  . GLN   A 1 156 ? 4.40800   -15.83600 -3.27700  1.000 120.65549 ? 192 GLN   A CB  1 
ATOM   1242 C  CG  . GLN   A 1 156 ? 3.96500   -15.80600 -1.83300  1.000 127.56228 ? 192 GLN   A CG  1 
ATOM   1243 C  CD  . GLN   A 1 156 ? 3.61700   -14.40700 -1.37600  1.000 130.37441 ? 192 GLN   A CD  1 
ATOM   1244 O  OE1 . GLN   A 1 156 ? 3.18700   -14.20400 -0.24100  1.000 135.21525 ? 192 GLN   A OE1 1 
ATOM   1245 N  NE2 . GLN   A 1 156 ? 3.80100   -13.43400 -2.25500  1.000 130.42896 ? 192 GLN   A NE2 1 
ATOM   1246 N  N   . TYR   A 1 157 ? 3.77400   -19.07500 -2.64200  1.000 111.22449 ? 193 TYR   A N   1 
ATOM   1247 C  CA  . TYR   A 1 157 ? 2.73100   -20.05800 -2.38300  1.000 115.02873 ? 193 TYR   A CA  1 
ATOM   1248 C  C   . TYR   A 1 157 ? 1.99000   -19.83300 -1.07400  1.000 128.04113 ? 193 TYR   A C   1 
ATOM   1249 O  O   . TYR   A 1 157 ? 0.91400   -20.41000 -0.88900  1.000 131.27525 ? 193 TYR   A O   1 
ATOM   1250 C  CB  . TYR   A 1 157 ? 3.31600   -21.47900 -2.38400  1.000 110.57236 ? 193 TYR   A CB  1 
ATOM   1251 C  CG  . TYR   A 1 157 ? 4.05400   -21.86200 -1.11900  1.000 117.50969 ? 193 TYR   A CG  1 
ATOM   1252 C  CD1 . TYR   A 1 157 ? 5.35600   -21.43300 -0.89300  1.000 114.20204 ? 193 TYR   A CD1 1 
ATOM   1253 C  CD2 . TYR   A 1 157 ? 3.45400   -22.66700 -0.15900  1.000 111.53445 ? 193 TYR   A CD2 1 
ATOM   1254 C  CE1 . TYR   A 1 157 ? 6.03600   -21.78700 0.25800   1.000 111.86632 ? 193 TYR   A CE1 1 
ATOM   1255 C  CE2 . TYR   A 1 157 ? 4.12500   -23.02400 0.99600   1.000 114.18562 ? 193 TYR   A CE2 1 
ATOM   1256 C  CZ  . TYR   A 1 157 ? 5.41600   -22.58200 1.19900   1.000 117.69163 ? 193 TYR   A CZ  1 
ATOM   1257 O  OH  . TYR   A 1 157 ? 6.09100   -22.93500 2.34600   1.000 112.72968 ? 193 TYR   A OH  1 
ATOM   1258 N  N   . ARG   A 1 158 ? 2.53400   -19.02100 -0.17200  1.000 130.69569 ? 194 ARG   A N   1 
ATOM   1259 C  CA  . ARG   A 1 158 ? 1.85400   -18.68500 1.06900   1.000 130.55145 ? 194 ARG   A CA  1 
ATOM   1260 C  C   . ARG   A 1 158 ? 2.23300   -17.26300 1.45200   1.000 133.99604 ? 194 ARG   A C   1 
ATOM   1261 O  O   . ARG   A 1 158 ? 3.35100   -16.81300 1.19100   1.000 132.61188 ? 194 ARG   A O   1 
ATOM   1262 C  CB  . ARG   A 1 158 ? 2.21200   -19.66200 2.19700   1.000 131.38486 ? 194 ARG   A CB  1 
ATOM   1263 C  CG  . ARG   A 1 158 ? 3.64600   -19.54800 2.68800   1.000 128.32927 ? 194 ARG   A CG  1 
ATOM   1264 C  CD  . ARG   A 1 158 ? 3.97500   -20.60700 3.72500   1.000 127.42913 ? 194 ARG   A CD  1 
ATOM   1265 N  NE  . ARG   A 1 158 ? 5.30100   -20.40200 4.29400   1.000 124.90899 ? 194 ARG   A NE  1 
ATOM   1266 C  CZ  . ARG   A 1 158 ? 5.92400   -21.27100 5.07900   1.000 124.82627 ? 194 ARG   A CZ  1 
ATOM   1267 N  NH1 . ARG   A 1 158 ? 5.37400   -22.43100 5.39800   1.000 126.51485 ? 194 ARG   A NH1 1 
ATOM   1268 N  NH2 . ARG   A 1 158 ? 7.13000   -20.96900 5.55200   1.000 119.26536 ? 194 ARG   A NH2 1 
ATOM   1269 N  N   . ASP   A 1 159 ? 1.28800   -16.55400 2.06100   1.000 139.22972 ? 195 ASP   A N   1 
ATOM   1270 C  CA  . ASP   A 1 159 ? 1.56200   -15.18900 2.46800   1.000 141.20254 ? 195 ASP   A CA  1 
ATOM   1271 C  C   . ASP   A 1 159 ? 2.47100   -15.18900 3.69600   1.000 143.52012 ? 195 ASP   A C   1 
ATOM   1272 O  O   . ASP   A 1 159 ? 2.41600   -16.10400 4.52100   1.000 143.84927 ? 195 ASP   A O   1 
ATOM   1273 C  CB  . ASP   A 1 159 ? 0.26400   -14.44600 2.76300   1.000 149.68007 ? 195 ASP   A CB  1 
ATOM   1274 C  CG  . ASP   A 1 159 ? -0.20300  -14.63800 4.18200   1.000 158.48797 ? 195 ASP   A CG  1 
ATOM   1275 O  OD1 . ASP   A 1 159 ? -0.57900  -15.77600 4.53200   1.000 159.88726 ? 195 ASP   A OD1 1 
ATOM   1276 O  OD2 . ASP   A 1 159 ? -0.17600  -13.65700 4.95600   1.000 153.92544 ? 195 ASP   A OD2 1 
ATOM   1277 N  N   . PRO   A 1 160 ? 3.34200   -14.18700 3.82600   1.000 145.28201 ? 196 PRO   A N   1 
ATOM   1278 C  CA  . PRO   A 1 160 ? 4.30700   -14.20400 4.93500   1.000 147.98549 ? 196 PRO   A CA  1 
ATOM   1279 C  C   . PRO   A 1 160 ? 3.70200   -13.89100 6.29300   1.000 157.33283 ? 196 PRO   A C   1 
ATOM   1280 O  O   . PRO   A 1 160 ? 4.34800   -14.18300 7.30700   1.000 159.03551 ? 196 PRO   A O   1 
ATOM   1281 C  CB  . PRO   A 1 160 ? 5.33300   -13.13600 4.52900   1.000 142.60237 ? 196 PRO   A CB  1 
ATOM   1282 C  CG  . PRO   A 1 160 ? 5.07700   -12.86500 3.06600   1.000 139.26202 ? 196 PRO   A CG  1 
ATOM   1283 C  CD  . PRO   A 1 160 ? 3.61500   -13.09600 2.87700   1.000 141.60404 ? 196 PRO   A CD  1 
ATOM   1284 N  N   . ARG   A 1 161 ? 2.50100   -13.30700 6.36200   1.000 156.70254 ? 197 ARG   A N   1 
ATOM   1285 C  CA  . ARG   A 1 161 ? 1.95300   -12.87500 7.64300   1.000 159.68241 ? 197 ARG   A CA  1 
ATOM   1286 C  C   . ARG   A 1 161 ? 0.79200   -13.71200 8.15400   1.000 160.95032 ? 197 ARG   A C   1 
ATOM   1287 O  O   . ARG   A 1 161 ? 0.51100   -13.66300 9.35500   1.000 167.91596 ? 197 ARG   A O   1 
ATOM   1288 C  CB  . ARG   A 1 161 ? 1.51000   -11.40700 7.57800   1.000 158.08703 ? 197 ARG   A CB  1 
ATOM   1289 C  CG  . ARG   A 1 161 ? 2.62500   -10.43500 7.93600   1.000 162.40942 ? 197 ARG   A CG  1 
ATOM   1290 C  CD  . ARG   A 1 161 ? 3.11900   -10.63000 9.36500   1.000 163.40468 ? 197 ARG   A CD  1 
ATOM   1291 N  NE  . ARG   A 1 161 ? 2.61400   -9.59900  10.26200  1.000 165.51572 ? 197 ARG   A NE  1 
ATOM   1292 C  CZ  . ARG   A 1 161 ? 2.91000   -9.52400  11.55200  1.000 166.50692 ? 197 ARG   A CZ  1 
ATOM   1293 N  NH1 . ARG   A 1 161 ? 3.69200   -10.41900 12.13200  1.000 168.01674 ? 197 ARG   A NH1 1 
ATOM   1294 N  NH2 . ARG   A 1 161 ? 2.41500   -8.52500  12.27600  1.000 168.53654 ? 197 ARG   A NH2 1 
ATOM   1295 N  N   . THR   A 1 162 ? 0.10200   -14.45700 7.29000   1.000 159.88410 ? 198 THR   A N   1 
ATOM   1296 C  CA  . THR   A 1 162 ? -0.88300  -15.43100 7.74500   1.000 162.66724 ? 198 THR   A CA  1 
ATOM   1297 C  C   . THR   A 1 162 ? -0.50500  -16.85600 7.36200   1.000 163.20732 ? 198 THR   A C   1 
ATOM   1298 O  O   . THR   A 1 162 ? -1.20900  -17.79800 7.74400   1.000 163.41796 ? 198 THR   A O   1 
ATOM   1299 C  CB  . THR   A 1 162 ? -2.28500  -15.09600 7.20900   1.000 164.03410 ? 198 THR   A CB  1 
ATOM   1300 O  OG1 . THR   A 1 162 ? -2.42200  -15.54500 5.85400   1.000 165.29858 ? 198 THR   A OG1 1 
ATOM   1301 C  CG2 . THR   A 1 162 ? -2.55200  -13.59000 7.27200   1.000 162.18671 ? 198 THR   A CG2 1 
ATOM   1302 N  N   . LYS   A 1 163 ? 0.61600   -17.03300 6.65400   1.000 162.44409 ? 199 LYS   A N   1 
ATOM   1303 C  CA  . LYS   A 1 163 ? 1.18600   -18.34100 6.29600   1.000 159.37955 ? 199 LYS   A CA  1 
ATOM   1304 C  C   . LYS   A 1 163 ? 0.15000   -19.28000 5.67400   1.000 165.87200 ? 199 LYS   A C   1 
ATOM   1305 O  O   . LYS   A 1 163 ? 0.23900   -20.50100 5.81000   1.000 166.84267 ? 199 LYS   A O   1 
ATOM   1306 C  CB  . LYS   A 1 163 ? 1.87700   -19.01100 7.49800   1.000 164.39951 ? 199 LYS   A CB  1 
ATOM   1307 C  CG  . LYS   A 1 163 ? 2.04800   -18.15700 8.77900   1.000 173.21620 ? 199 LYS   A CG  1 
ATOM   1308 C  CD  . LYS   A 1 163 ? 2.83000   -16.86200 8.55300   1.000 166.03974 ? 199 LYS   A CD  1 
ATOM   1309 C  CE  . LYS   A 1 163 ? 2.79200   -15.98000 9.80800   1.000 164.36848 ? 199 LYS   A CE  1 
ATOM   1310 N  NZ  . LYS   A 1 163 ? 3.66300   -14.76700 9.75500   1.000 161.91510 ? 199 LYS   A NZ  1 
ATOM   1311 N  N   . GLN   A 1 164 ? -0.83500  -18.71900 4.97600   1.000 152.88380 ? 200 GLN   A N   1 
ATOM   1312 C  CA  . GLN   A 1 164 ? -1.88300  -19.50800 4.34300   1.000 145.91410 ? 200 GLN   A CA  1 
ATOM   1313 C  C   . GLN   A 1 164 ? -1.51900  -19.82200 2.89600   1.000 135.13328 ? 200 GLN   A C   1 
ATOM   1314 O  O   . GLN   A 1 164 ? -1.18800  -18.92100 2.12100   1.000 136.82323 ? 200 GLN   A O   1 
ATOM   1315 C  CB  . GLN   A 1 164 ? -3.22400  -18.77100 4.41000   1.000 150.47865 ? 200 GLN   A CB  1 
ATOM   1316 C  CG  . GLN   A 1 164 ? -4.18400  -19.04500 3.25100   1.000 141.71459 ? 200 GLN   A CG  1 
ATOM   1317 C  CD  . GLN   A 1 164 ? -4.70200  -20.47300 3.21600   1.000 146.29863 ? 200 GLN   A CD  1 
ATOM   1318 O  OE1 . GLN   A 1 164 ? -4.27600  -21.32400 3.99500   1.000 148.53143 ? 200 GLN   A OE1 1 
ATOM   1319 N  NE2 . GLN   A 1 164 ? -5.62900  -20.74100 2.30300   1.000 146.70457 ? 200 GLN   A NE2 1 
ATOM   1320 N  N   . HIS   A 1 165 ? -1.59700  -21.10100 2.53900   1.000 133.38296 ? 201 HIS   A N   1 
ATOM   1321 C  CA  . HIS   A 1 165 ? -1.30500  -21.53900 1.17900   1.000 132.91434 ? 201 HIS   A CA  1 
ATOM   1322 C  C   . HIS   A 1 165 ? -2.34900  -20.99600 0.20900   1.000 126.41008 ? 201 HIS   A C   1 
ATOM   1323 O  O   . HIS   A 1 165 ? -3.54000  -20.92700 0.52600   1.000 135.72187 ? 201 HIS   A O   1 
ATOM   1324 C  CB  . HIS   A 1 165 ? -1.27200  -23.07100 1.12600   1.000 135.54510 ? 201 HIS   A CB  1 
ATOM   1325 C  CG  . HIS   A 1 165 ? -0.64500  -23.64400 -0.11100  1.000 130.23286 ? 201 HIS   A CG  1 
ATOM   1326 N  ND1 . HIS   A 1 165 ? -0.67900  -22.98500 -1.32100  1.000 129.06049 ? 201 HIS   A ND1 1 
ATOM   1327 C  CD2 . HIS   A 1 165 ? 0.05300   -24.78400 -0.33000  1.000 126.14241 ? 201 HIS   A CD2 1 
ATOM   1328 C  CE1 . HIS   A 1 165 ? -0.04300  -23.69800 -2.23100  1.000 125.43040 ? 201 HIS   A CE1 1 
ATOM   1329 N  NE2 . HIS   A 1 165 ? 0.41600   -24.79400 -1.65500  1.000 123.87146 ? 201 HIS   A NE2 1 
ATOM   1330 N  N   . ILE   A 1 166 ? -1.89200  -20.60300 -0.97700  1.000 125.51753 ? 202 ILE   A N   1 
ATOM   1331 C  CA  . ILE   A 1 166 ? -2.77600  -20.17700 -2.06300  1.000 136.41106 ? 202 ILE   A CA  1 
ATOM   1332 C  C   . ILE   A 1 166 ? -3.79200  -21.28200 -2.35000  1.000 130.53853 ? 202 ILE   A C   1 
ATOM   1333 O  O   . ILE   A 1 166 ? -3.52400  -22.46100 -2.07200  1.000 126.35953 ? 202 ILE   A O   1 
ATOM   1334 C  CB  . ILE   A 1 166 ? -1.97100  -19.80300 -3.32200  1.000 131.93192 ? 202 ILE   A CB  1 
ATOM   1335 C  CG1 . ILE   A 1 166 ? -0.97000  -20.90100 -3.67300  1.000 119.63051 ? 202 ILE   A CG1 1 
ATOM   1336 C  CG2 . ILE   A 1 166 ? -1.26500  -18.47000 -3.14400  1.000 131.23049 ? 202 ILE   A CG2 1 
ATOM   1337 C  CD1 . ILE   A 1 166 ? -1.44400  -21.81500 -4.77500  1.000 127.54569 ? 202 ILE   A CD1 1 
ATOM   1338 N  N   . PRO   A 1 167 ? -4.97200  -20.96600 -2.87500  1.000 133.41595 ? 203 PRO   A N   1 
ATOM   1339 C  CA  . PRO   A 1 167 ? -5.93900  -22.02800 -3.16700  1.000 132.58876 ? 203 PRO   A CA  1 
ATOM   1340 C  C   . PRO   A 1 167 ? -5.54900  -22.82300 -4.40400  1.000 140.21410 ? 203 PRO   A C   1 
ATOM   1341 O  O   . PRO   A 1 167 ? -4.91800  -22.31200 -5.33400  1.000 142.46417 ? 203 PRO   A O   1 
ATOM   1342 C  CB  . PRO   A 1 167 ? -7.25000  -21.26600 -3.38200  1.000 126.11574 ? 203 PRO   A CB  1 
ATOM   1343 C  CG  . PRO   A 1 167 ? -6.80600  -19.92100 -3.84800  1.000 133.14416 ? 203 PRO   A CG  1 
ATOM   1344 C  CD  . PRO   A 1 167 ? -5.52700  -19.62600 -3.13600  1.000 133.87072 ? 203 PRO   A CD  1 
ATOM   1345 N  N   . TYR   A 1 168 ? -5.93400  -24.09700 -4.39500  1.000 128.13080 ? 204 TYR   A N   1 
ATOM   1346 C  CA  . TYR   A 1 168 ? -5.70400  -24.97100 -5.53800  1.000 122.22546 ? 204 TYR   A CA  1 
ATOM   1347 C  C   . TYR   A 1 168 ? -6.48400  -24.46600 -6.75300  1.000 136.75869 ? 204 TYR   A C   1 
ATOM   1348 O  O   . TYR   A 1 168 ? -7.56800  -23.89500 -6.61700  1.000 134.20681 ? 204 TYR   A O   1 
ATOM   1349 C  CB  . TYR   A 1 168 ? -6.12100  -26.40200 -5.17700  1.000 122.40141 ? 204 TYR   A CB  1 
ATOM   1350 C  CG  . TYR   A 1 168 ? -5.99100  -27.41200 -6.29500  1.000 121.41224 ? 204 TYR   A CG  1 
ATOM   1351 C  CD1 . TYR   A 1 168 ? -7.04100  -27.64400 -7.17400  1.000 121.79053 ? 204 TYR   A CD1 1 
ATOM   1352 C  CD2 . TYR   A 1 168 ? -4.83200  -28.15700 -6.45100  1.000 124.04721 ? 204 TYR   A CD2 1 
ATOM   1353 C  CE1 . TYR   A 1 168 ? -6.93300  -28.57200 -8.18900  1.000 119.64193 ? 204 TYR   A CE1 1 
ATOM   1354 C  CE2 . TYR   A 1 168 ? -4.71200  -29.08900 -7.46100  1.000 123.01915 ? 204 TYR   A CE2 1 
ATOM   1355 C  CZ  . TYR   A 1 168 ? -5.76500  -29.29400 -8.32900  1.000 121.06636 ? 204 TYR   A CZ  1 
ATOM   1356 O  OH  . TYR   A 1 168 ? -5.65100  -30.22300 -9.33900  1.000 123.76411 ? 204 TYR   A OH  1 
ATOM   1357 N  N   . ARG   A 1 169 ? -5.92900  -24.66700 -7.94200  1.000 124.66494 ? 205 ARG   A N   1 
ATOM   1358 C  CA  . ARG   A 1 169 ? -6.57600  -24.23000 -9.18200  1.000 135.84766 ? 205 ARG   A CA  1 
ATOM   1359 C  C   . ARG   A 1 169 ? -6.13600  -25.15700 -10.31400 1.000 126.17647 ? 205 ARG   A C   1 
ATOM   1360 O  O   . ARG   A 1 169 ? -5.53000  -26.21100 -10.08000 1.000 124.41304 ? 205 ARG   A O   1 
ATOM   1361 C  CB  . ARG   A 1 169 ? -6.26300  -22.74600 -9.47300  1.000 137.84799 ? 205 ARG   A CB  1 
ATOM   1362 C  CG  . ARG   A 1 169 ? -4.82400  -22.46800 -9.89400  1.000 131.15988 ? 205 ARG   A CG  1 
ATOM   1363 C  CD  . ARG   A 1 169 ? -4.72400  -21.16900 -10.69700 1.000 138.93563 ? 205 ARG   A CD  1 
ATOM   1364 N  NE  . ARG   A 1 169 ? -5.27300  -21.31200 -12.04100 1.000 143.41607 ? 205 ARG   A NE  1 
ATOM   1365 C  CZ  . ARG   A 1 169 ? -5.15900  -20.40300 -13.00000 1.000 146.08379 ? 205 ARG   A CZ  1 
ATOM   1366 N  NH1 . ARG   A 1 169 ? -4.51800  -19.26300 -12.80000 1.000 147.31907 ? 205 ARG   A NH1 1 
ATOM   1367 N  NH2 . ARG   A 1 169 ? -5.69900  -20.64500 -14.19200 1.000 147.66353 ? 205 ARG   A NH2 1 
ATOM   1368 N  N   . GLU   A 1 170 ? -6.45600  -24.76800 -11.54400 1.000 132.85152 ? 206 GLU   A N   1 
ATOM   1369 C  CA  . GLU   A 1 170 ? -6.11600  -25.53600 -12.73500 1.000 130.70449 ? 206 GLU   A CA  1 
ATOM   1370 C  C   . GLU   A 1 170 ? -6.19100  -24.59100 -13.93900 1.000 138.94859 ? 206 GLU   A C   1 
ATOM   1371 O  O   . GLU   A 1 170 ? -6.41100  -23.38100 -13.78600 1.000 136.15657 ? 206 GLU   A O   1 
ATOM   1372 C  CB  . GLU   A 1 170 ? -7.02400  -26.77000 -12.85300 1.000 127.93885 ? 206 GLU   A CB  1 
ATOM   1373 C  CG  . GLU   A 1 170 ? -6.49700  -27.89800 -13.70300 1.000 131.45232 ? 206 GLU   A CG  1 
ATOM   1374 C  CD  . GLU   A 1 170 ? -7.09400  -27.87900 -15.08000 1.000 143.97765 ? 206 GLU   A CD  1 
ATOM   1375 O  OE1 . GLU   A 1 170 ? -8.07600  -27.11700 -15.32300 1.000 146.01559 ? 206 GLU   A OE1 1 
ATOM   1376 O  OE2 . GLU   A 1 170 ? -6.58000  -28.60800 -15.95300 1.000 150.83939 ? 206 GLU   A OE2 1 
ATOM   1377 N  N   . LYS   A 1 171 ? -5.95300  -25.15400 -15.13800 1.000 141.55896 ? 207 LYS   A N   1 
ATOM   1378 C  CA  . LYS   A 1 171 ? -5.77900  -24.40400 -16.38100 1.000 147.45752 ? 207 LYS   A CA  1 
ATOM   1379 C  C   . LYS   A 1 171 ? -4.58700  -23.45600 -16.31800 1.000 151.54566 ? 207 LYS   A C   1 
ATOM   1380 O  O   . LYS   A 1 171 ? -4.76900  -22.23500 -16.36700 1.000 155.89885 ? 207 LYS   A O   1 
ATOM   1381 C  CB  . LYS   A 1 171 ? -7.04100  -23.60000 -16.72200 1.000 145.88379 ? 207 LYS   A CB  1 
ATOM   1382 C  CG  . LYS   A 1 171 ? -8.29500  -24.41400 -16.95300 1.000 150.06215 ? 207 LYS   A CG  1 
ATOM   1383 C  CD  . LYS   A 1 171 ? -8.77600  -24.31900 -18.42400 1.000 153.64142 ? 207 LYS   A CD  1 
ATOM   1384 C  CE  . LYS   A 1 171 ? -10.17400 -24.93500 -18.61400 1.000 150.12257 ? 207 LYS   A CE  1 
ATOM   1385 N  NZ  . LYS   A 1 171 ? -10.50500 -25.26200 -20.04800 1.000 150.07919 ? 207 LYS   A NZ  1 
ATOM   1386 N  N   . LYS   A 1 172 ? -3.37400  -23.99700 -16.24600 1.000 150.63261 ? 208 LYS   A N   1 
ATOM   1387 C  CA  . LYS   A 1 172 ? -2.15500  -23.21600 -16.38700 1.000 161.93506 ? 208 LYS   A CA  1 
ATOM   1388 C  C   . LYS   A 1 172 ? -1.31400  -23.84800 -17.48300 1.000 169.07582 ? 208 LYS   A C   1 
ATOM   1389 O  O   . LYS   A 1 172 ? -1.08000  -25.06100 -17.46100 1.000 166.72584 ? 208 LYS   A O   1 
ATOM   1390 C  CB  . LYS   A 1 172 ? -1.37300  -23.15700 -15.07800 1.000 160.52190 ? 208 LYS   A CB  1 
ATOM   1391 C  CG  . LYS   A 1 172 ? -0.11700  -22.33500 -15.18400 1.000 171.41771 ? 208 LYS   A CG  1 
ATOM   1392 C  CD  . LYS   A 1 172 ? -0.39800  -20.92800 -15.71000 1.000 169.63254 ? 208 LYS   A CD  1 
ATOM   1393 C  CE  . LYS   A 1 172 ? 0.86900   -20.31700 -16.31400 1.000 174.25798 ? 208 LYS   A CE  1 
ATOM   1394 N  NZ  . LYS   A 1 172 ? 1.37600   -21.16400 -17.43300 1.000 173.90580 ? 208 LYS   A NZ  1 
ATOM   1395 N  N   . SER   A 1 173 ? -0.89000  -23.03800 -18.45100 1.000 183.53783 ? 209 SER   A N   1 
ATOM   1396 C  CA  . SER   A 1 173 ? -0.11600  -23.55800 -19.56800 1.000 181.34205 ? 209 SER   A CA  1 
ATOM   1397 C  C   . SER   A 1 173 ? 1.20000   -24.15000 -19.07700 1.000 182.34360 ? 209 SER   A C   1 
ATOM   1398 O  O   . SER   A 1 173 ? 1.79100   -23.69100 -18.09600 1.000 180.94802 ? 209 SER   A O   1 
ATOM   1399 C  CB  . SER   A 1 173 ? 0.14900   -22.45700 -20.59500 1.000 183.98700 ? 209 SER   A CB  1 
ATOM   1400 O  OG  . SER   A 1 173 ? 0.85600   -21.37600 -20.00600 1.000 185.88819 ? 209 SER   A OG  1 
ATOM   1401 N  N   . LEU   A 1 174 ? 1.65100   -25.18800 -19.77100 1.000 181.54986 ? 210 LEU   A N   1 
ATOM   1402 C  CA  . LEU   A 1 174 ? 2.84400   -25.93100 -19.37800 1.000 170.73685 ? 210 LEU   A CA  1 
ATOM   1403 C  C   . LEU   A 1 174 ? 4.07200   -25.11700 -19.76300 1.000 165.43431 ? 210 LEU   A C   1 
ATOM   1404 O  O   . LEU   A 1 174 ? 4.46700   -25.07600 -20.93000 1.000 162.20961 ? 210 LEU   A O   1 
ATOM   1405 C  CB  . LEU   A 1 174 ? 2.85600   -27.30400 -20.04000 1.000 171.80654 ? 210 LEU   A CB  1 
ATOM   1406 C  CG  . LEU   A 1 174 ? 1.55000   -28.10500 -20.07200 1.000 166.95307 ? 210 LEU   A CG  1 
ATOM   1407 C  CD1 . LEU   A 1 174 ? 0.76000   -27.84200 -21.35300 1.000 164.01771 ? 210 LEU   A CD1 1 
ATOM   1408 C  CD2 . LEU   A 1 174 ? 1.83500   -29.59000 -19.91500 1.000 153.57497 ? 210 LEU   A CD2 1 
ATOM   1409 N  N   . SER   A 1 175 ? 4.68700   -24.47000 -18.77600 1.000 162.61917 ? 211 SER   A N   1 
ATOM   1410 C  CA  . SER   A 1 175 ? 5.86400   -23.64000 -18.98500 1.000 161.74268 ? 211 SER   A CA  1 
ATOM   1411 C  C   . SER   A 1 175 ? 7.03000   -24.20800 -18.19000 1.000 157.31742 ? 211 SER   A C   1 
ATOM   1412 O  O   . SER   A 1 175 ? 6.90300   -24.45800 -16.98700 1.000 158.96641 ? 211 SER   A O   1 
ATOM   1413 C  CB  . SER   A 1 175 ? 5.59200   -22.19100 -18.57100 1.000 161.64990 ? 211 SER   A CB  1 
ATOM   1414 O  OG  . SER   A 1 175 ? 6.77000   -21.40900 -18.64900 1.000 158.61626 ? 211 SER   A OG  1 
ATOM   1415 N  N   . GLY   A 1 176 ? 8.16000   -24.41000 -18.86400 1.000 144.92691 ? 212 GLY   A N   1 
ATOM   1416 C  CA  . GLY   A 1 176 ? 9.36700   -24.92900 -18.26400 1.000 129.71369 ? 212 GLY   A CA  1 
ATOM   1417 C  C   . GLY   A 1 176 ? 9.93800   -26.06200 -19.08400 1.000 125.09986 ? 212 GLY   A C   1 
ATOM   1418 O  O   . GLY   A 1 176 ? 9.54100   -26.30100 -20.22900 1.000 119.35327 ? 212 GLY   A O   1 
ATOM   1419 N  N   . THR   A 1 177 ? 10.89600  -26.77100 -18.49100 1.000 118.48821 ? 213 THR   A N   1 
ATOM   1420 C  CA  . THR   A 1 177 ? 11.52400  -27.92400 -19.12900 1.000 109.39451 ? 213 THR   A CA  1 
ATOM   1421 C  C   . THR   A 1 177 ? 10.71900  -29.17000 -18.77800 1.000 104.72100 ? 213 THR   A C   1 
ATOM   1422 O  O   . THR   A 1 177 ? 10.68200  -29.59000 -17.61600 1.000 96.04583  ? 213 THR   A O   1 
ATOM   1423 C  CB  . THR   A 1 177 ? 12.98000  -28.05900 -18.69100 1.000 112.36483 ? 213 THR   A CB  1 
ATOM   1424 O  OG1 . THR   A 1 177 ? 13.09900  -27.71800 -17.30400 1.000 109.82741 ? 213 THR   A OG1 1 
ATOM   1425 C  CG2 . THR   A 1 177 ? 13.87100  -27.14200 -19.51700 1.000 111.70088 ? 213 THR   A CG2 1 
ATOM   1426 N  N   . ALA   A 1 178 ? 10.07900  -29.76300 -19.78700 1.000 115.40813 ? 214 ALA   A N   1 
ATOM   1427 C  CA  . ALA   A 1 178 ? 9.17700   -30.88800 -19.57400 1.000 114.02520 ? 214 ALA   A CA  1 
ATOM   1428 C  C   . ALA   A 1 178 ? 9.88800   -32.15100 -19.10700 1.000 103.15489 ? 214 ALA   A C   1 
ATOM   1429 O  O   . ALA   A 1 178 ? 9.21400   -33.08800 -18.66500 1.000 101.62684 ? 214 ALA   A O   1 
ATOM   1430 C  CB  . ALA   A 1 178 ? 8.39800   -31.18000 -20.85800 1.000 122.60547 ? 214 ALA   A CB  1 
ATOM   1431 N  N   . ARG   A 1 179 ? 11.21900  -32.20200 -19.18300 1.000 98.08896  ? 215 ARG   A N   1 
ATOM   1432 C  CA  . ARG   A 1 179 ? 11.91800  -33.43400 -18.83900 1.000 97.10017  ? 215 ARG   A CA  1 
ATOM   1433 C  C   . ARG   A 1 179 ? 11.91000  -33.69200 -17.33600 1.000 91.08203  ? 215 ARG   A C   1 
ATOM   1434 O  O   . ARG   A 1 179 ? 11.96700  -34.85100 -16.91000 1.000 87.45191  ? 215 ARG   A O   1 
ATOM   1435 C  CB  . ARG   A 1 179 ? 13.35200  -33.39500 -19.37600 1.000 97.00804  ? 215 ARG   A CB  1 
ATOM   1436 C  CG  . ARG   A 1 179 ? 14.08700  -34.72300 -19.24500 1.000 97.93174  ? 215 ARG   A CG  1 
ATOM   1437 C  CD  . ARG   A 1 179 ? 15.33800  -34.80000 -20.11200 1.000 106.38482 ? 215 ARG   A CD  1 
ATOM   1438 N  NE  . ARG   A 1 179 ? 16.20800  -33.63700 -19.98800 1.000 106.54228 ? 215 ARG   A NE  1 
ATOM   1439 C  CZ  . ARG   A 1 179 ? 16.72000  -32.98000 -21.02000 1.000 112.02986 ? 215 ARG   A CZ  1 
ATOM   1440 N  NH1 . ARG   A 1 179 ? 16.46800  -33.34800 -22.26600 1.000 114.43289 ? 215 ARG   A NH1 1 
ATOM   1441 N  NH2 . ARG   A 1 179 ? 17.51300  -31.93500 -20.79700 1.000 110.27751 ? 215 ARG   A NH2 1 
ATOM   1442 N  N   . TYR   A 1 180 ? 11.81800  -32.64100 -16.51700 1.000 89.71265  ? 216 TYR   A N   1 
ATOM   1443 C  CA  . TYR   A 1 180 ? 11.89400  -32.79200 -15.07100 1.000 88.56947  ? 216 TYR   A CA  1 
ATOM   1444 C  C   . TYR   A 1 180 ? 10.66900  -32.28800 -14.32000 1.000 91.88545  ? 216 TYR   A C   1 
ATOM   1445 O  O   . TYR   A 1 180 ? 10.56900  -32.53800 -13.11400 1.000 84.93862  ? 216 TYR   A O   1 
ATOM   1446 C  CB  . TYR   A 1 180 ? 13.13400  -32.07200 -14.51600 1.000 89.08724  ? 216 TYR   A CB  1 
ATOM   1447 C  CG  . TYR   A 1 180 ? 14.41200  -32.34700 -15.27600 1.000 85.28011  ? 216 TYR   A CG  1 
ATOM   1448 C  CD1 . TYR   A 1 180 ? 14.75700  -33.63500 -15.67400 1.000 86.70579  ? 216 TYR   A CD1 1 
ATOM   1449 C  CD2 . TYR   A 1 180 ? 15.26900  -31.31000 -15.61300 1.000 91.49903  ? 216 TYR   A CD2 1 
ATOM   1450 C  CE1 . TYR   A 1 180 ? 15.92800  -33.87600 -16.37700 1.000 93.95836  ? 216 TYR   A CE1 1 
ATOM   1451 C  CE2 . TYR   A 1 180 ? 16.43400  -31.54500 -16.31100 1.000 93.27126  ? 216 TYR   A CE2 1 
ATOM   1452 C  CZ  . TYR   A 1 180 ? 16.76000  -32.82700 -16.69100 1.000 96.13455  ? 216 TYR   A CZ  1 
ATOM   1453 O  OH  . TYR   A 1 180 ? 17.92700  -33.04400 -17.38900 1.000 86.52655  ? 216 TYR   A OH  1 
ATOM   1454 N  N   . MET   A 1 181 ? 9.74300   -31.59200 -14.97800 1.000 97.72244  ? 217 MET   A N   1 
ATOM   1455 C  CA  . MET   A 1 181 ? 8.58000   -31.06300 -14.27800 1.000 98.27277  ? 217 MET   A CA  1 
ATOM   1456 C  C   . MET   A 1 181 ? 7.70600   -32.19900 -13.74600 1.000 97.57035  ? 217 MET   A C   1 
ATOM   1457 O  O   . MET   A 1 181 ? 7.71600   -33.32300 -14.25600 1.000 93.35899  ? 217 MET   A O   1 
ATOM   1458 C  CB  . MET   A 1 181 ? 7.76500   -30.15400 -15.19800 1.000 99.77501  ? 217 MET   A CB  1 
ATOM   1459 C  CG  . MET   A 1 181 ? 7.34000   -30.81200 -16.49700 1.000 103.74626 ? 217 MET   A CG  1 
ATOM   1460 S  SD  . MET   A 1 181 ? 6.23800   -29.77900 -17.48700 1.000 121.83657 ? 217 MET   A SD  1 
ATOM   1461 C  CE  . MET   A 1 181 ? 7.23200   -28.29900 -17.67300 1.000 119.87856 ? 217 MET   A CE  1 
ATOM   1462 N  N   . SER   A 1 182 ? 6.94300   -31.89000 -12.70100 1.000 99.52260  ? 218 SER   A N   1 
ATOM   1463 C  CA  . SER   A 1 182 ? 6.15800   -32.90200 -12.01400 1.000 104.91599 ? 218 SER   A CA  1 
ATOM   1464 C  C   . SER   A 1 182 ? 4.96700   -33.34300 -12.86600 1.000 107.75775 ? 218 SER   A C   1 
ATOM   1465 O  O   . SER   A 1 182 ? 4.61000   -32.71800 -13.87000 1.000 105.49161 ? 218 SER   A O   1 
ATOM   1466 C  CB  . SER   A 1 182 ? 5.67200   -32.37600 -10.66300 1.000 106.48236 ? 218 SER   A CB  1 
ATOM   1467 O  OG  . SER   A 1 182 ? 4.80400   -31.26900 -10.82900 1.000 107.62894 ? 218 SER   A OG  1 
ATOM   1468 N  N   . ILE   A 1 183 ? 4.35000   -34.44900 -12.44400 1.000 101.84657 ? 219 ILE   A N   1 
ATOM   1469 C  CA  . ILE   A 1 183 ? 3.15200   -34.94100 -13.11900 1.000 113.65563 ? 219 ILE   A CA  1 
ATOM   1470 C  C   . ILE   A 1 183 ? 2.01300   -33.94000 -12.97400 1.000 113.69430 ? 219 ILE   A C   1 
ATOM   1471 O  O   . ILE   A 1 183 ? 1.24700   -33.70600 -13.91700 1.000 114.04889 ? 219 ILE   A O   1 
ATOM   1472 C  CB  . ILE   A 1 183 ? 2.77300   -36.33200 -12.57400 1.000 109.37517 ? 219 ILE   A CB  1 
ATOM   1473 C  CG1 . ILE   A 1 183 ? 3.52000   -37.42300 -13.34400 1.000 105.26325 ? 219 ILE   A CG1 1 
ATOM   1474 C  CG2 . ILE   A 1 183 ? 1.26400   -36.55200 -12.62200 1.000 109.44953 ? 219 ILE   A CG2 1 
ATOM   1475 C  CD1 . ILE   A 1 183 ? 3.37600   -38.80400 -12.74400 1.000 107.21213 ? 219 ILE   A CD1 1 
ATOM   1476 N  N   . ASN   A 1 184 ? 1.89200   -33.32200 -11.79600 1.000 109.08904 ? 220 ASN   A N   1 
ATOM   1477 C  CA  . ASN   A 1 184 ? 0.85600   -32.31400 -11.59600 1.000 114.15473 ? 220 ASN   A CA  1 
ATOM   1478 C  C   . ASN   A 1 184 ? 1.08400   -31.09300 -12.47700 1.000 113.25989 ? 220 ASN   A C   1 
ATOM   1479 O  O   . ASN   A 1 184 ? 0.12400   -30.41300 -12.85500 1.000 118.95682 ? 220 ASN   A O   1 
ATOM   1480 C  CB  . ASN   A 1 184 ? 0.79900   -31.90500 -10.12600 1.000 115.54394 ? 220 ASN   A CB  1 
ATOM   1481 C  CG  . ASN   A 1 184 ? 0.49300   -33.07000 -9.21200  1.000 119.36999 ? 220 ASN   A CG  1 
ATOM   1482 O  OD1 . ASN   A 1 184 ? 0.89900   -33.08600 -8.04900  1.000 118.84065 ? 220 ASN   A OD1 1 
ATOM   1483 N  ND2 . ASN   A 1 184 ? -0.23100  -34.05100 -9.73100  1.000 116.07569 ? 220 ASN   A ND2 1 
ATOM   1484 N  N   . THR   A 1 185 ? 2.34200   -30.79600 -12.81200 1.000 114.69705 ? 221 THR   A N   1 
ATOM   1485 C  CA  . THR   A 1 185 ? 2.62100   -29.68900 -13.72000 1.000 109.92253 ? 221 THR   A CA  1 
ATOM   1486 C  C   . THR   A 1 185 ? 2.15000   -30.00700 -15.13400 1.000 110.78204 ? 221 THR   A C   1 
ATOM   1487 O  O   . THR   A 1 185 ? 1.60600   -29.13600 -15.82400 1.000 114.56601 ? 221 THR   A O   1 
ATOM   1488 C  CB  . THR   A 1 185 ? 4.11500   -29.36100 -13.70600 1.000 111.59609 ? 221 THR   A CB  1 
ATOM   1489 O  OG1 . THR   A 1 185 ? 4.50400   -28.96400 -12.38500 1.000 109.25241 ? 221 THR   A OG1 1 
ATOM   1490 C  CG2 . THR   A 1 185 ? 4.42900   -28.23500 -14.67900 1.000 105.83061 ? 221 THR   A CG2 1 
ATOM   1491 N  N   . HIS   A 1 186 ? 2.34300   -31.25200 -15.58000 1.000 113.49463 ? 222 HIS   A N   1 
ATOM   1492 C  CA  . HIS   A 1 186 ? 1.82700   -31.65800 -16.88300 1.000 117.60028 ? 222 HIS   A CA  1 
ATOM   1493 C  C   . HIS   A 1 186 ? 0.30500   -31.61000 -16.92300 1.000 122.64786 ? 222 HIS   A C   1 
ATOM   1494 O  O   . HIS   A 1 186 ? -0.27900  -31.31000 -17.97100 1.000 112.03787 ? 222 HIS   A O   1 
ATOM   1495 C  CB  . HIS   A 1 186 ? 2.31500   -33.06400 -17.23400 1.000 107.15124 ? 222 HIS   A CB  1 
ATOM   1496 C  CG  . HIS   A 1 186 ? 3.73700   -33.11800 -17.69700 1.000 121.80202 ? 222 HIS   A CG  1 
ATOM   1497 N  ND1 . HIS   A 1 186 ? 4.11900   -32.75800 -18.97200 1.000 128.11258 ? 222 HIS   A ND1 1 
ATOM   1498 C  CD2 . HIS   A 1 186 ? 4.86900   -33.50100 -17.06000 1.000 110.25036 ? 222 HIS   A CD2 1 
ATOM   1499 C  CE1 . HIS   A 1 186 ? 5.42500   -32.91100 -19.09800 1.000 114.83763 ? 222 HIS   A CE1 1 
ATOM   1500 N  NE2 . HIS   A 1 186 ? 5.90400   -33.36200 -17.95300 1.000 106.47077 ? 222 HIS   A NE2 1 
ATOM   1501 N  N   . LEU   A 1 187 ? -0.35200  -31.90000 -15.80100 1.000 125.65922 ? 223 LEU   A N   1 
ATOM   1502 C  CA  . LEU   A 1 187 ? -1.80700  -31.90200 -15.74100 1.000 125.25042 ? 223 LEU   A CA  1 
ATOM   1503 C  C   . LEU   A 1 187 ? -2.39900  -30.51200 -15.54900 1.000 125.58422 ? 223 LEU   A C   1 
ATOM   1504 O  O   . LEU   A 1 187 ? -3.62000  -30.39400 -15.39900 1.000 135.13474 ? 223 LEU   A O   1 
ATOM   1505 C  CB  . LEU   A 1 187 ? -2.28300  -32.82800 -14.61800 1.000 126.48950 ? 223 LEU   A CB  1 
ATOM   1506 C  CG  . LEU   A 1 187 ? -1.86300  -34.29400 -14.74500 1.000 121.01994 ? 223 LEU   A CG  1 
ATOM   1507 C  CD1 . LEU   A 1 187 ? -2.32300  -35.09700 -13.53800 1.000 120.54852 ? 223 LEU   A CD1 1 
ATOM   1508 C  CD2 . LEU   A 1 187 ? -2.40100  -34.89900 -16.03400 1.000 122.93813 ? 223 LEU   A CD2 1 
ATOM   1509 N  N   . GLY   A 1 188 ? -1.57500  -29.46600 -15.55000 1.000 125.75723 ? 224 GLY   A N   1 
ATOM   1510 C  CA  . GLY   A 1 188 ? -2.06800  -28.11000 -15.42200 1.000 127.16939 ? 224 GLY   A CA  1 
ATOM   1511 C  C   . GLY   A 1 188 ? -2.40600  -27.67100 -14.01700 1.000 131.47061 ? 224 GLY   A C   1 
ATOM   1512 O  O   . GLY   A 1 188 ? -3.02800  -26.61600 -13.84900 1.000 137.07707 ? 224 GLY   A O   1 
ATOM   1513 N  N   . ARG   A 1 189 ? -2.01500  -28.43600 -13.00300 1.000 123.93231 ? 225 ARG   A N   1 
ATOM   1514 C  CA  . ARG   A 1 189 ? -2.32800  -28.08500 -11.62600 1.000 125.63320 ? 225 ARG   A CA  1 
ATOM   1515 C  C   . ARG   A 1 189 ? -1.41700  -26.96800 -11.13100 1.000 123.55405 ? 225 ARG   A C   1 
ATOM   1516 O  O   . ARG   A 1 189 ? -0.27700  -26.81900 -11.58100 1.000 129.34025 ? 225 ARG   A O   1 
ATOM   1517 C  CB  . ARG   A 1 189 ? -2.18900  -29.30600 -10.71600 1.000 126.42286 ? 225 ARG   A CB  1 
ATOM   1518 C  CG  . ARG   A 1 189 ? -2.91900  -30.54100 -11.21800 1.000 130.24104 ? 225 ARG   A CG  1 
ATOM   1519 C  CD  . ARG   A 1 189 ? -2.81600  -31.68800 -10.22400 1.000 134.38917 ? 225 ARG   A CD  1 
ATOM   1520 N  NE  . ARG   A 1 189 ? -3.43800  -32.90800 -10.72400 1.000 133.05538 ? 225 ARG   A NE  1 
ATOM   1521 C  CZ  . ARG   A 1 189 ? -3.56800  -34.02500 -10.02000 1.000 131.82197 ? 225 ARG   A CZ  1 
ATOM   1522 N  NH1 . ARG   A 1 189 ? -3.13400  -34.11000 -8.77300  1.000 133.81504 ? 225 ARG   A NH1 1 
ATOM   1523 N  NH2 . ARG   A 1 189 ? -4.15000  -35.08100 -10.58000 1.000 132.77657 ? 225 ARG   A NH2 1 
ATOM   1524 N  N   . GLU   A 1 190 ? -1.93600  -26.17800 -10.19500 1.000 123.17138 ? 226 GLU   A N   1 
ATOM   1525 C  CA  . GLU   A 1 190 ? -1.13500  -25.14000 -9.56000  1.000 120.60487 ? 226 GLU   A CA  1 
ATOM   1526 C  C   . GLU   A 1 190 ? -0.03900  -25.78700 -8.72400  1.000 112.82187 ? 226 GLU   A C   1 
ATOM   1527 O  O   . GLU   A 1 190 ? -0.32200  -26.59400 -7.83200  1.000 111.49339 ? 226 GLU   A O   1 
ATOM   1528 C  CB  . GLU   A 1 190 ? -2.01300  -24.24400 -8.69300  1.000 120.13776 ? 226 GLU   A CB  1 
ATOM   1529 C  CG  . GLU   A 1 190 ? -1.25000  -23.14000 -7.97800  1.000 115.49968 ? 226 GLU   A CG  1 
ATOM   1530 C  CD  . GLU   A 1 190 ? -0.90400  -21.97100 -8.88200  1.000 119.50266 ? 226 GLU   A CD  1 
ATOM   1531 O  OE1 . GLU   A 1 190 ? -1.82600  -21.22400 -9.27500  1.000 130.14550 ? 226 GLU   A OE1 1 
ATOM   1532 O  OE2 . GLU   A 1 190 ? 0.29200   -21.79700 -9.20100  1.000 119.29772 ? 226 GLU   A OE2 1 
ATOM   1533 N  N   . GLN   A 1 191 ? 1.21000   -25.43400 -9.00800  1.000 109.94542 ? 227 GLN   A N   1 
ATOM   1534 C  CA  . GLN   A 1 191 ? 2.33100   -26.06300 -8.33200  1.000 108.28013 ? 227 GLN   A CA  1 
ATOM   1535 C  C   . GLN   A 1 191 ? 2.42600   -25.58900 -6.88300  1.000 112.02383 ? 227 GLN   A C   1 
ATOM   1536 O  O   . GLN   A 1 191 ? 1.90700   -24.53400 -6.50600  1.000 110.89247 ? 227 GLN   A O   1 
ATOM   1537 C  CB  . GLN   A 1 191 ? 3.63000   -25.77800 -9.08600  1.000 108.76802 ? 227 GLN   A CB  1 
ATOM   1538 C  CG  . GLN   A 1 191 ? 3.67100   -26.43600 -10.46000 1.000 108.80739 ? 227 GLN   A CG  1 
ATOM   1539 C  CD  . GLN   A 1 191 ? 4.77600   -25.89900 -11.34700 1.000 106.14018 ? 227 GLN   A CD  1 
ATOM   1540 O  OE1 . GLN   A 1 191 ? 4.51800   -25.15300 -12.29300 1.000 108.46568 ? 227 GLN   A OE1 1 
ATOM   1541 N  NE2 . GLN   A 1 191 ? 6.01300   -26.28500 -11.05600 1.000 93.18239  ? 227 GLN   A NE2 1 
ATOM   1542 N  N   . SER   A 1 192 ? 3.08800   -26.39900 -6.06400  1.000 102.66194 ? 228 SER   A N   1 
ATOM   1543 C  CA  . SER   A 1 192 ? 3.26800   -26.09400 -4.64900  1.000 108.79272 ? 228 SER   A CA  1 
ATOM   1544 C  C   . SER   A 1 192 ? 4.61000   -26.67100 -4.20800  1.000 102.09387 ? 228 SER   A C   1 
ATOM   1545 O  O   . SER   A 1 192 ? 5.51100   -26.87500 -5.02800  1.000 100.12162 ? 228 SER   A O   1 
ATOM   1546 C  CB  . SER   A 1 192 ? 2.08600   -26.63400 -3.82500  1.000 112.47962 ? 228 SER   A CB  1 
ATOM   1547 O  OG  . SER   A 1 192 ? 2.18600   -28.03600 -3.63800  1.000 111.92175 ? 228 SER   A OG  1 
ATOM   1548 N  N   . ARG   A 1 193 ? 4.74000   -26.94300 -2.90700  1.000 98.00327  ? 229 ARG   A N   1 
ATOM   1549 C  CA  . ARG   A 1 193 ? 5.99700   -27.46200 -2.37700  1.000 95.11829  ? 229 ARG   A CA  1 
ATOM   1550 C  C   . ARG   A 1 193 ? 6.28500   -28.87100 -2.87900  1.000 97.17258  ? 229 ARG   A C   1 
ATOM   1551 O  O   . ARG   A 1 193 ? 7.45200   -29.22400 -3.09200  1.000 97.50338  ? 229 ARG   A O   1 
ATOM   1552 C  CB  . ARG   A 1 193 ? 5.97000   -27.43800 -0.84800  1.000 89.65048  ? 229 ARG   A CB  1 
ATOM   1553 C  CG  . ARG   A 1 193 ? 6.23400   -26.07100 -0.24500  1.000 93.40710  ? 229 ARG   A CG  1 
ATOM   1554 C  CD  . ARG   A 1 193 ? 6.18000   -26.10300 1.27400   1.000 97.69461  ? 229 ARG   A CD  1 
ATOM   1555 N  NE  . ARG   A 1 193 ? 4.81300   -26.01400 1.77300   1.000 104.67971 ? 229 ARG   A NE  1 
ATOM   1556 C  CZ  . ARG   A 1 193 ? 4.49100   -25.82000 3.04400   1.000 110.24403 ? 229 ARG   A CZ  1 
ATOM   1557 N  NH1 . ARG   A 1 193 ? 5.41700   -25.71000 3.98200   1.000 118.72633 ? 229 ARG   A NH1 1 
ATOM   1558 N  NH2 . ARG   A 1 193 ? 3.20800   -25.72800 3.38200   1.000 113.76832 ? 229 ARG   A NH2 1 
ATOM   1559 N  N   . ARG   A 1 194 ? 5.24400   -29.68300 -3.07400  1.000 91.57843  ? 230 ARG   A N   1 
ATOM   1560 C  CA  . ARG   A 1 194 ? 5.42900   -31.06800 -3.48800  1.000 87.55512  ? 230 ARG   A CA  1 
ATOM   1561 C  C   . ARG   A 1 194 ? 5.93700   -31.18700 -4.92000  1.000 91.16940  ? 230 ARG   A C   1 
ATOM   1562 O  O   . ARG   A 1 194 ? 6.55200   -32.20200 -5.26100  1.000 88.67575  ? 230 ARG   A O   1 
ATOM   1563 C  CB  . ARG   A 1 194 ? 4.11100   -31.83400 -3.33700  1.000 102.70528 ? 230 ARG   A CB  1 
ATOM   1564 C  CG  . ARG   A 1 194 ? 3.00400   -31.36400 -4.27400  1.000 92.29055  ? 230 ARG   A CG  1 
ATOM   1565 C  CD  . ARG   A 1 194 ? 1.63900   -31.87900 -3.84100  1.000 111.05589 ? 230 ARG   A CD  1 
ATOM   1566 N  NE  . ARG   A 1 194 ? 0.84000   -32.33200 -4.97700  1.000 116.54456 ? 230 ARG   A NE  1 
ATOM   1567 C  CZ  . ARG   A 1 194 ? -0.40100  -32.79600 -4.88400  1.000 104.74024 ? 230 ARG   A CZ  1 
ATOM   1568 N  NH1 . ARG   A 1 194 ? -1.03700  -32.84800 -3.72800  1.000 111.71569 ? 230 ARG   A NH1 1 
ATOM   1569 N  NH2 . ARG   A 1 194 ? -1.02400  -33.22000 -5.97800  1.000 118.35264 ? 230 ARG   A NH2 1 
ATOM   1570 N  N   . ASP   A 1 195 ? 5.69400   -30.18200 -5.76800  1.000 90.11203  ? 231 ASP   A N   1 
ATOM   1571 C  CA  . ASP   A 1 195 ? 6.16200   -30.25500 -7.14700  1.000 93.21032  ? 231 ASP   A CA  1 
ATOM   1572 C  C   . ASP   A 1 195 ? 7.63700   -29.89400 -7.27300  1.000 93.78689  ? 231 ASP   A C   1 
ATOM   1573 O  O   . ASP   A 1 195 ? 8.30100   -30.34400 -8.21300  1.000 94.20270  ? 231 ASP   A O   1 
ATOM   1574 C  CB  . ASP   A 1 195 ? 5.30800   -29.35100 -8.03600  1.000 97.91005  ? 231 ASP   A CB  1 
ATOM   1575 C  CG  . ASP   A 1 195 ? 3.89100   -29.86500 -8.19400  1.000 101.15063 ? 231 ASP   A CG  1 
ATOM   1576 O  OD1 . ASP   A 1 195 ? 3.58900   -30.95800 -7.67200  1.000 103.12723 ? 231 ASP   A OD1 1 
ATOM   1577 O  OD2 . ASP   A 1 195 ? 3.07700   -29.17500 -8.84200  1.000 109.63764 ? 231 ASP   A OD2 1 
ATOM   1578 N  N   . ASP   A 1 196 ? 8.16700   -29.09200 -6.34500  1.000 89.09220  ? 232 ASP   A N   1 
ATOM   1579 C  CA  . ASP   A 1 196 ? 9.60300   -28.84900 -6.31900  1.000 88.77534  ? 232 ASP   A CA  1 
ATOM   1580 C  C   . ASP   A 1 196 ? 10.37100  -30.05700 -5.80200  1.000 91.11718  ? 232 ASP   A C   1 
ATOM   1581 O  O   . ASP   A 1 196 ? 11.58700  -30.13400 -6.00300  1.000 82.47311  ? 232 ASP   A O   1 
ATOM   1582 C  CB  . ASP   A 1 196 ? 9.92400   -27.62300 -5.46100  1.000 82.56639  ? 232 ASP   A CB  1 
ATOM   1583 C  CG  . ASP   A 1 196 ? 9.58900   -26.31800 -6.15600  1.000 82.02204  ? 232 ASP   A CG  1 
ATOM   1584 O  OD1 . ASP   A 1 196 ? 9.47200   -26.31600 -7.40000  1.000 86.08968  ? 232 ASP   A OD1 1 
ATOM   1585 O  OD2 . ASP   A 1 196 ? 9.45100   -25.28900 -5.46100  1.000 82.55897  ? 232 ASP   A OD2 1 
ATOM   1586 N  N   . LEU   A 1 197 ? 9.69100   -30.99400 -5.14100  1.000 85.04952  ? 233 LEU   A N   1 
ATOM   1587 C  CA  . LEU   A 1 197 ? 10.32900  -32.20500 -4.64500  1.000 87.44087  ? 233 LEU   A CA  1 
ATOM   1588 C  C   . LEU   A 1 197 ? 10.22500  -33.37600 -5.60800  1.000 80.36063  ? 233 LEU   A C   1 
ATOM   1589 O  O   . LEU   A 1 197 ? 11.15100  -34.19100 -5.66700  1.000 76.84245  ? 233 LEU   A O   1 
ATOM   1590 C  CB  . LEU   A 1 197 ? 9.73100   -32.61200 -3.29400  1.000 93.60551  ? 233 LEU   A CB  1 
ATOM   1591 C  CG  . LEU   A 1 197 ? 9.98400   -31.65600 -2.12600  1.000 99.97759  ? 233 LEU   A CG  1 
ATOM   1592 C  CD1 . LEU   A 1 197 ? 9.73200   -32.36200 -0.80800  1.000 98.94327  ? 233 LEU   A CD1 1 
ATOM   1593 C  CD2 . LEU   A 1 197 ? 11.39500  -31.09000 -2.17800  1.000 81.30844  ? 233 LEU   A CD2 1 
ATOM   1594 N  N   . GLU   A 1 198 ? 9.12200   -33.49000 -6.35500  1.000 86.38607  ? 234 GLU   A N   1 
ATOM   1595 C  CA  . GLU   A 1 198 ? 9.04000   -34.52800 -7.37500  1.000 90.65834  ? 234 GLU   A CA  1 
ATOM   1596 C  C   . GLU   A 1 198 ? 10.03300  -34.26200 -8.49600  1.000 83.88628  ? 234 GLU   A C   1 
ATOM   1597 O  O   . GLU   A 1 198 ? 10.68300  -35.19000 -8.99000  1.000 82.04956  ? 234 GLU   A O   1 
ATOM   1598 C  CB  . GLU   A 1 198 ? 7.61600   -34.62500 -7.92200  1.000 83.10079  ? 234 GLU   A CB  1 
ATOM   1599 C  CG  . GLU   A 1 198 ? 7.47100   -35.63900 -9.05200  1.000 89.57133  ? 234 GLU   A CG  1 
ATOM   1600 C  CD  . GLU   A 1 198 ? 6.05200   -35.74700 -9.57200  1.000 100.07161 ? 234 GLU   A CD  1 
ATOM   1601 O  OE1 . GLU   A 1 198 ? 5.14300   -35.15900 -8.95000  1.000 106.25897 ? 234 GLU   A OE1 1 
ATOM   1602 O  OE2 . GLU   A 1 198 ? 5.84500   -36.42000 -10.60300 1.000 96.29044  ? 234 GLU   A OE2 1 
ATOM   1603 N  N   . ALA   A 1 199 ? 10.16400  -32.99800 -8.90600  1.000 85.65864  ? 235 ALA   A N   1 
ATOM   1604 C  CA  . ALA   A 1 199 ? 11.16800  -32.64100 -9.90000  1.000 83.01288  ? 235 ALA   A CA  1 
ATOM   1605 C  C   . ALA   A 1 199 ? 12.56900  -32.97400 -9.40500  1.000 77.58099  ? 235 ALA   A C   1 
ATOM   1606 O  O   . ALA   A 1 199 ? 13.43100  -33.38400 -10.19100 1.000 71.81675  ? 235 ALA   A O   1 
ATOM   1607 C  CB  . ALA   A 1 199 ? 11.05400  -31.15800 -10.25000 1.000 81.83873  ? 235 ALA   A CB  1 
ATOM   1608 N  N   . LEU   A 1 200 ? 12.81400  -32.80400 -8.10200  1.000 75.41679  ? 236 LEU   A N   1 
ATOM   1609 C  CA  . LEU   A 1 200 ? 14.08200  -33.24300 -7.52900  1.000 77.90927  ? 236 LEU   A CA  1 
ATOM   1610 C  C   . LEU   A 1 200 ? 14.26000  -34.74600 -7.68300  1.000 77.40755  ? 236 LEU   A C   1 
ATOM   1611 O  O   . LEU   A 1 200 ? 15.36100  -35.22100 -7.98600  1.000 75.49340  ? 236 LEU   A O   1 
ATOM   1612 C  CB  . LEU   A 1 200 ? 14.17000  -32.84600 -6.05500  1.000 76.64722  ? 236 LEU   A CB  1 
ATOM   1613 C  CG  . LEU   A 1 200 ? 14.64100  -31.42800 -5.73500  1.000 79.31189  ? 236 LEU   A CG  1 
ATOM   1614 C  CD1 . LEU   A 1 200 ? 15.00400  -31.31600 -4.26300  1.000 83.36261  ? 236 LEU   A CD1 1 
ATOM   1615 C  CD2 . LEU   A 1 200 ? 15.81800  -31.04100 -6.61500  1.000 82.72469  ? 236 LEU   A CD2 1 
ATOM   1616 N  N   . GLY   A 1 201 ? 13.18600  -35.51100 -7.47700  1.000 81.85083  ? 237 GLY   A N   1 
ATOM   1617 C  CA  . GLY   A 1 201 ? 13.26500  -36.94700 -7.68800  1.000 81.41262  ? 237 GLY   A CA  1 
ATOM   1618 C  C   . GLY   A 1 201 ? 13.65100  -37.30100 -9.11100  1.000 83.88702  ? 237 GLY   A C   1 
ATOM   1619 O  O   . GLY   A 1 201 ? 14.49900  -38.16700 -9.33600  1.000 88.99554  ? 237 GLY   A O   1 
ATOM   1620 N  N   . HIS   A 1 202 ? 13.04400  -36.62300 -10.08900 1.000 80.93581  ? 238 HIS   A N   1 
ATOM   1621 C  CA  . HIS   A 1 202 ? 13.38600  -36.86900 -11.48600 1.000 81.91366  ? 238 HIS   A CA  1 
ATOM   1622 C  C   . HIS   A 1 202 ? 14.86700  -36.61800 -11.74500 1.000 82.30179  ? 238 HIS   A C   1 
ATOM   1623 O  O   . HIS   A 1 202 ? 15.51100  -37.37300 -12.48400 1.000 79.82031  ? 238 HIS   A O   1 
ATOM   1624 C  CB  . HIS   A 1 202 ? 12.52900  -35.99100 -12.39700 1.000 81.70131  ? 238 HIS   A CB  1 
ATOM   1625 C  CG  . HIS   A 1 202 ? 11.05900  -36.24200 -12.26900 1.000 93.61955  ? 238 HIS   A CG  1 
ATOM   1626 N  ND1 . HIS   A 1 202 ? 10.11000  -35.32000 -12.65200 1.000 93.90924  ? 238 HIS   A ND1 1 
ATOM   1627 C  CD2 . HIS   A 1 202 ? 10.37500  -37.31600 -11.80600 1.000 90.12304  ? 238 HIS   A CD2 1 
ATOM   1628 C  CE1 . HIS   A 1 202 ? 8.90400   -35.81300 -12.42800 1.000 93.59199  ? 238 HIS   A CE1 1 
ATOM   1629 N  NE2 . HIS   A 1 202 ? 9.03700   -37.02200 -11.91400 1.000 90.67325  ? 238 HIS   A NE2 1 
ATOM   1630 N  N   . VAL   A 1 203 ? 15.42400  -35.56700 -11.13800 1.000 78.33305  ? 239 VAL   A N   1 
ATOM   1631 C  CA  . VAL   A 1 203 ? 16.83900  -35.25800 -11.32500 1.000 78.14926  ? 239 VAL   A CA  1 
ATOM   1632 C  C   . VAL   A 1 203 ? 17.71300  -36.34500 -10.70800 1.000 77.91506  ? 239 VAL   A C   1 
ATOM   1633 O  O   . VAL   A 1 203 ? 18.77600  -36.68300 -11.24200 1.000 75.28004  ? 239 VAL   A O   1 
ATOM   1634 C  CB  . VAL   A 1 203 ? 17.15800  -33.86700 -10.74400 1.000 82.81354  ? 239 VAL   A CB  1 
ATOM   1635 C  CG1 . VAL   A 1 203 ? 18.65700  -33.60800 -10.74300 1.000 67.67010  ? 239 VAL   A CG1 1 
ATOM   1636 C  CG2 . VAL   A 1 203 ? 16.43500  -32.78600 -11.53400 1.000 76.62547  ? 239 VAL   A CG2 1 
ATOM   1637 N  N   . PHE   A 1 204 ? 17.27600  -36.91900 -9.58500  1.000 80.26888  ? 240 PHE   A N   1 
ATOM   1638 C  CA  . PHE   A 1 204 ? 18.05800  -37.97000 -8.94000  1.000 75.11588  ? 240 PHE   A CA  1 
ATOM   1639 C  C   . PHE   A 1 204 ? 18.16800  -39.19700 -9.83800  1.000 81.65282  ? 240 PHE   A C   1 
ATOM   1640 O  O   . PHE   A 1 204 ? 19.26700  -39.71300 -10.07200 1.000 82.96190  ? 240 PHE   A O   1 
ATOM   1641 C  CB  . PHE   A 1 204 ? 17.43700  -38.33900 -7.59100  1.000 72.74230  ? 240 PHE   A CB  1 
ATOM   1642 C  CG  . PHE   A 1 204 ? 17.29800  -37.17800 -6.64300  1.000 74.27893  ? 240 PHE   A CG  1 
ATOM   1643 C  CD1 . PHE   A 1 204 ? 18.12100  -36.06800 -6.75200  1.000 80.06634  ? 240 PHE   A CD1 1 
ATOM   1644 C  CD2 . PHE   A 1 204 ? 16.34100  -37.19700 -5.64200  1.000 75.17792  ? 240 PHE   A CD2 1 
ATOM   1645 C  CE1 . PHE   A 1 204 ? 17.98700  -35.00000 -5.88500  1.000 74.99594  ? 240 PHE   A CE1 1 
ATOM   1646 C  CE2 . PHE   A 1 204 ? 16.20300  -36.13300 -4.77000  1.000 80.03454  ? 240 PHE   A CE2 1 
ATOM   1647 C  CZ  . PHE   A 1 204 ? 17.02700  -35.03400 -4.89200  1.000 81.15156  ? 240 PHE   A CZ  1 
ATOM   1648 N  N   . PHE   A 1 205 ? 17.03300  -39.67600 -10.35800 1.000 75.54484  ? 241 PHE   A N   1 
ATOM   1649 C  CA  . PHE   A 1 205 ? 17.07100  -40.79200 -11.29900 1.000 83.33175  ? 241 PHE   A CA  1 
ATOM   1650 C  C   . PHE   A 1 205 ? 17.78100  -40.40800 -12.59000 1.000 82.96038  ? 241 PHE   A C   1 
ATOM   1651 O  O   . PHE   A 1 205 ? 18.41300  -41.25800 -13.22700 1.000 87.46061  ? 241 PHE   A O   1 
ATOM   1652 C  CB  . PHE   A 1 205 ? 15.65400  -41.28100 -11.60100 1.000 88.00538  ? 241 PHE   A CB  1 
ATOM   1653 C  CG  . PHE   A 1 205 ? 14.94300  -41.86000 -10.41100 1.000 92.32598  ? 241 PHE   A CG  1 
ATOM   1654 C  CD1 . PHE   A 1 205 ? 15.17600  -43.16700 -10.01500 1.000 96.07575  ? 241 PHE   A CD1 1 
ATOM   1655 C  CD2 . PHE   A 1 205 ? 14.03300  -41.10100 -9.69600  1.000 88.53445  ? 241 PHE   A CD2 1 
ATOM   1656 C  CE1 . PHE   A 1 205 ? 14.51800  -43.70100 -8.92200  1.000 98.62577  ? 241 PHE   A CE1 1 
ATOM   1657 C  CE2 . PHE   A 1 205 ? 13.37400  -41.62800 -8.60400  1.000 94.66128  ? 241 PHE   A CE2 1 
ATOM   1658 C  CZ  . PHE   A 1 205 ? 13.61500  -42.92900 -8.21800  1.000 102.42808 ? 241 PHE   A CZ  1 
ATOM   1659 N  N   . TYR   A 1 206 ? 17.68400  -39.13900 -12.99200 1.000 86.02621  ? 242 TYR   A N   1 
ATOM   1660 C  CA  . TYR   A 1 206 ? 18.39800  -38.67200 -14.17700 1.000 91.14146  ? 242 TYR   A CA  1 
ATOM   1661 C  C   . TYR   A 1 206 ? 19.90600  -38.79400 -13.99100 1.000 80.76651  ? 242 TYR   A C   1 
ATOM   1662 O  O   . TYR   A 1 206 ? 20.61800  -39.26800 -14.88300 1.000 86.03399  ? 242 TYR   A O   1 
ATOM   1663 C  CB  . TYR   A 1 206 ? 17.99800  -37.22700 -14.48200 1.000 85.18299  ? 242 TYR   A CB  1 
ATOM   1664 C  CG  . TYR   A 1 206 ? 18.86600  -36.51500 -15.49600 1.000 84.73752  ? 242 TYR   A CG  1 
ATOM   1665 C  CD1 . TYR   A 1 206 ? 18.71000  -36.74200 -16.85800 1.000 87.70601  ? 242 TYR   A CD1 1 
ATOM   1666 C  CD2 . TYR   A 1 206 ? 19.82600  -35.59500 -15.09200 1.000 79.88709  ? 242 TYR   A CD2 1 
ATOM   1667 C  CE1 . TYR   A 1 206 ? 19.49700  -36.08400 -17.78700 1.000 84.39044  ? 242 TYR   A CE1 1 
ATOM   1668 C  CE2 . TYR   A 1 206 ? 20.61500  -34.93300 -16.01200 1.000 72.95038  ? 242 TYR   A CE2 1 
ATOM   1669 C  CZ  . TYR   A 1 206 ? 20.44700  -35.18000 -17.35700 1.000 77.98981  ? 242 TYR   A CZ  1 
ATOM   1670 O  OH  . TYR   A 1 206 ? 21.23200  -34.52200 -18.27500 1.000 80.93079  ? 242 TYR   A OH  1 
ATOM   1671 N  N   . PHE   A 1 207 ? 20.41000  -38.37000 -12.83100 1.000 79.41158  ? 243 PHE   A N   1 
ATOM   1672 C  CA  . PHE   A 1 207 ? 21.83300  -38.51300 -12.54200 1.000 78.61500  ? 243 PHE   A CA  1 
ATOM   1673 C  C   . PHE   A 1 207 ? 22.23600  -39.97600 -12.41500 1.000 82.43209  ? 243 PHE   A C   1 
ATOM   1674 O  O   . PHE   A 1 207 ? 23.36500  -40.34000 -12.76300 1.000 81.04245  ? 243 PHE   A O   1 
ATOM   1675 C  CB  . PHE   A 1 207 ? 22.18400  -37.76800 -11.25300 1.000 67.84367  ? 243 PHE   A CB  1 
ATOM   1676 C  CG  . PHE   A 1 207 ? 22.24400  -36.27700 -11.39800 1.000 70.05744  ? 243 PHE   A CG  1 
ATOM   1677 C  CD1 . PHE   A 1 207 ? 22.47900  -35.69200 -12.63000 1.000 70.13160  ? 243 PHE   A CD1 1 
ATOM   1678 C  CD2 . PHE   A 1 207 ? 22.08200  -35.45800 -10.29100 1.000 67.70146  ? 243 PHE   A CD2 1 
ATOM   1679 C  CE1 . PHE   A 1 207 ? 22.54300  -34.31800 -12.75800 1.000 80.54076  ? 243 PHE   A CE1 1 
ATOM   1680 C  CE2 . PHE   A 1 207 ? 22.14700  -34.08300 -10.41200 1.000 67.24920  ? 243 PHE   A CE2 1 
ATOM   1681 C  CZ  . PHE   A 1 207 ? 22.37600  -33.51200 -11.64800 1.000 79.47712  ? 243 PHE   A CZ  1 
ATOM   1682 N  N   . LEU   A 1 208 ? 21.33100  -40.82300 -11.91800 1.000 84.37504  ? 244 LEU   A N   1 
ATOM   1683 C  CA  . LEU   A 1 208 ? 21.65600  -42.22000 -11.65600 1.000 75.26329  ? 244 LEU   A CA  1 
ATOM   1684 C  C   . LEU   A 1 208 ? 21.71500  -43.03700 -12.93900 1.000 82.77245  ? 244 LEU   A C   1 
ATOM   1685 O  O   . LEU   A 1 208 ? 22.65400  -43.81200 -13.14600 1.000 93.78514  ? 244 LEU   A O   1 
ATOM   1686 C  CB  . LEU   A 1 208 ? 20.63000  -42.81900 -10.69600 1.000 83.51406  ? 244 LEU   A CB  1 
ATOM   1687 C  CG  . LEU   A 1 208 ? 20.81200  -42.43500 -9.22900  1.000 79.34271  ? 244 LEU   A CG  1 
ATOM   1688 C  CD1 . LEU   A 1 208 ? 19.59300  -42.83600 -8.41100  1.000 83.04937  ? 244 LEU   A CD1 1 
ATOM   1689 C  CD2 . LEU   A 1 208 ? 22.07200  -43.09300 -8.69200  1.000 77.26356  ? 244 LEU   A CD2 1 
ATOM   1690 N  N   . ARG   A 1 209 ? 20.71600  -42.88600 -13.80300 1.000 93.21421  ? 245 ARG   A N   1 
ATOM   1691 C  CA  . ARG   A 1 209 ? 20.61900  -43.68600 -15.01400 1.000 99.68254  ? 245 ARG   A CA  1 
ATOM   1692 C  C   . ARG   A 1 209 ? 21.30300  -43.04200 -16.21000 1.000 98.55588  ? 245 ARG   A C   1 
ATOM   1693 O  O   . ARG   A 1 209 ? 21.43100  -43.69100 -17.25400 1.000 100.98624 ? 245 ARG   A O   1 
ATOM   1694 C  CB  . ARG   A 1 209 ? 19.14400  -43.94600 -15.34300 1.000 108.31387 ? 245 ARG   A CB  1 
ATOM   1695 C  CG  . ARG   A 1 209 ? 18.85600  -45.34900 -15.84400 1.000 118.97099 ? 245 ARG   A CG  1 
ATOM   1696 C  CD  . ARG   A 1 209 ? 17.36800  -45.66600 -15.77400 1.000 117.53927 ? 245 ARG   A CD  1 
ATOM   1697 N  NE  . ARG   A 1 209 ? 16.71500  -45.56300 -17.07300 1.000 124.53888 ? 245 ARG   A NE  1 
ATOM   1698 C  CZ  . ARG   A 1 209 ? 16.63200  -46.55700 -17.94700 1.000 134.62079 ? 245 ARG   A CZ  1 
ATOM   1699 N  NH1 . ARG   A 1 209 ? 17.16400  -47.74300 -17.69800 1.000 133.03608 ? 245 ARG   A NH1 1 
ATOM   1700 N  NH2 . ARG   A 1 209 ? 16.00300  -46.35500 -19.10100 1.000 133.40442 ? 245 ARG   A NH2 1 
ATOM   1701 N  N   . GLY   A 1 210 ? 21.75300  -41.79400 -16.08400 1.000 92.50471  ? 246 GLY   A N   1 
ATOM   1702 C  CA  . GLY   A 1 210 ? 22.26300  -41.04800 -17.21200 1.000 99.65280  ? 246 GLY   A CA  1 
ATOM   1703 C  C   . GLY   A 1 210 ? 21.21000  -40.56000 -18.17700 1.000 100.84142 ? 246 GLY   A C   1 
ATOM   1704 O  O   . GLY   A 1 210 ? 21.52300  -39.72900 -19.03900 1.000 100.78985 ? 246 GLY   A O   1 
ATOM   1705 N  N   . GLN   A 1 211 ? 19.97800  -41.04400 -18.06600 1.000 109.28475 ? 247 GLN   A N   1 
ATOM   1706 C  CA  . GLN   A 1 211 ? 18.87300  -40.61400 -18.91100 1.000 106.66051 ? 247 GLN   A CA  1 
ATOM   1707 C  C   . GLN   A 1 211 ? 17.57600  -40.94800 -18.18700 1.000 110.80955 ? 247 GLN   A C   1 
ATOM   1708 O  O   . GLN   A 1 211 ? 17.58200  -41.48700 -17.07700 1.000 108.03993 ? 247 GLN   A O   1 
ATOM   1709 C  CB  . GLN   A 1 211 ? 18.92600  -41.28300 -20.28800 1.000 108.89394 ? 247 GLN   A CB  1 
ATOM   1710 C  CG  . GLN   A 1 211 ? 18.57400  -42.76200 -20.26200 1.000 113.12971 ? 247 GLN   A CG  1 
ATOM   1711 C  CD  . GLN   A 1 211 ? 18.10300  -43.27400 -21.60900 1.000 119.91229 ? 247 GLN   A CD  1 
ATOM   1712 O  OE1 . GLN   A 1 211 ? 18.55800  -42.81300 -22.65600 1.000 122.13929 ? 247 GLN   A OE1 1 
ATOM   1713 N  NE2 . GLN   A 1 211 ? 17.17700  -44.22600 -21.58800 1.000 118.16351 ? 247 GLN   A NE2 1 
ATOM   1714 N  N   . LEU   A 1 212 ? 16.46000  -40.62700 -18.83000 1.000 117.08667 ? 248 LEU   A N   1 
ATOM   1715 C  CA  . LEU   A 1 212 ? 15.13600  -40.93100 -18.31900 1.000 110.70498 ? 248 LEU   A CA  1 
ATOM   1716 C  C   . LEU   A 1 212 ? 14.30700  -41.57700 -19.41700 1.000 108.49121 ? 248 LEU   A C   1 
ATOM   1717 O  O   . LEU   A 1 212 ? 14.53100  -41.31500 -20.60300 1.000 108.74821 ? 248 LEU   A O   1 
ATOM   1718 C  CB  . LEU   A 1 212 ? 14.43800  -39.66200 -17.80700 1.000 106.70603 ? 248 LEU   A CB  1 
ATOM   1719 C  CG  . LEU   A 1 212 ? 15.06900  -39.04100 -16.55800 1.000 99.18571  ? 248 LEU   A CG  1 
ATOM   1720 C  CD1 . LEU   A 1 212 ? 14.35500  -37.75800 -16.16200 1.000 94.44613  ? 248 LEU   A CD1 1 
ATOM   1721 C  CD2 . LEU   A 1 212 ? 15.06800  -40.03900 -15.40900 1.000 97.34754  ? 248 LEU   A CD2 1 
ATOM   1722 N  N   . PRO   A 1 213 ? 13.35300  -42.43900 -19.05600 1.000 103.64283 ? 249 PRO   A N   1 
ATOM   1723 C  CA  . PRO   A 1 213 ? 12.56800  -43.12800 -20.09400 1.000 105.65070 ? 249 PRO   A CA  1 
ATOM   1724 C  C   . PRO   A 1 213 ? 11.71400  -42.19300 -20.93200 1.000 113.25595 ? 249 PRO   A C   1 
ATOM   1725 O  O   . PRO   A 1 213 ? 11.39300  -42.52600 -22.07900 1.000 119.76903 ? 249 PRO   A O   1 
ATOM   1726 C  CB  . PRO   A 1 213 ? 11.70800  -44.11000 -19.28600 1.000 106.27964 ? 249 PRO   A CB  1 
ATOM   1727 C  CG  . PRO   A 1 213 ? 11.62800  -43.51100 -17.92600 1.000 104.92567 ? 249 PRO   A CG  1 
ATOM   1728 C  CD  . PRO   A 1 213 ? 12.95500  -42.84900 -17.70000 1.000 107.32095 ? 249 PRO   A CD  1 
ATOM   1729 N  N   . TRP   A 1 214 ? 11.33400  -41.03500 -20.40100 1.000 106.82793 ? 250 TRP   A N   1 
ATOM   1730 C  CA  . TRP   A 1 214 ? 10.55000  -40.05400 -21.15200 1.000 114.22714 ? 250 TRP   A CA  1 
ATOM   1731 C  C   . TRP   A 1 214 ? 11.43000  -39.03100 -21.85500 1.000 111.37795 ? 250 TRP   A C   1 
ATOM   1732 O  O   . TRP   A 1 214 ? 11.08100  -37.85300 -21.96100 1.000 110.98687 ? 250 TRP   A O   1 
ATOM   1733 C  CB  . TRP   A 1 214 ? 9.55400   -39.37100 -20.22200 1.000 112.83949 ? 250 TRP   A CB  1 
ATOM   1734 C  CG  . TRP   A 1 214 ? 10.16400  -38.79900 -18.97400 1.000 109.53723 ? 250 TRP   A CG  1 
ATOM   1735 C  CD1 . TRP   A 1 214 ? 10.83900  -37.61900 -18.85600 1.000 103.85371 ? 250 TRP   A CD1 1 
ATOM   1736 C  CD2 . TRP   A 1 214 ? 10.14200  -39.38100 -17.66400 1.000 106.98924 ? 250 TRP   A CD2 1 
ATOM   1737 N  NE1 . TRP   A 1 214 ? 11.24300  -37.43200 -17.55500 1.000 101.27240 ? 250 TRP   A NE1 1 
ATOM   1738 C  CE2 . TRP   A 1 214 ? 10.82700  -38.50000 -16.80300 1.000 104.07855 ? 250 TRP   A CE2 1 
ATOM   1739 C  CE3 . TRP   A 1 214 ? 9.61200   -40.56300 -17.13700 1.000 108.48375 ? 250 TRP   A CE3 1 
ATOM   1740 C  CZ2 . TRP   A 1 214 ? 10.99500  -38.76400 -15.44400 1.000 104.06703 ? 250 TRP   A CZ2 1 
ATOM   1741 C  CZ3 . TRP   A 1 214 ? 9.77900   -40.82300 -15.78900 1.000 110.75558 ? 250 TRP   A CZ3 1 
ATOM   1742 C  CH2 . TRP   A 1 214 ? 10.46500  -39.92800 -14.95800 1.000 101.91036 ? 250 TRP   A CH2 1 
ATOM   1743 N  N   . GLN   A 1 215 ? 12.58300  -39.46300 -22.35100 1.000 124.87210 ? 251 GLN   A N   1 
ATOM   1744 C  CA  . GLN   A 1 215 ? 13.54300  -38.59400 -23.01100 1.000 124.39265 ? 251 GLN   A CA  1 
ATOM   1745 C  C   . GLN   A 1 215 ? 13.62700  -38.94600 -24.49100 1.000 126.52836 ? 251 GLN   A C   1 
ATOM   1746 O  O   . GLN   A 1 215 ? 13.50300  -40.11100 -24.87900 1.000 127.68039 ? 251 GLN   A O   1 
ATOM   1747 C  CB  . GLN   A 1 215 ? 14.92400  -38.71900 -22.36000 1.000 121.92568 ? 251 GLN   A CB  1 
ATOM   1748 C  CG  . GLN   A 1 215 ? 15.77700  -37.47000 -22.43000 1.000 117.57216 ? 251 GLN   A CG  1 
ATOM   1749 C  CD  . GLN   A 1 215 ? 16.89400  -37.48500 -21.40100 1.000 118.69685 ? 251 GLN   A CD  1 
ATOM   1750 O  OE1 . GLN   A 1 215 ? 16.87900  -38.28200 -20.46300 1.000 116.55881 ? 251 GLN   A OE1 1 
ATOM   1751 N  NE2 . GLN   A 1 215 ? 17.86600  -36.59700 -21.57000 1.000 122.09684 ? 251 GLN   A NE2 1 
ATOM   1752 N  N   . GLY   A 1 216 ? 13.83600  -37.92400 -25.31800 1.000 120.92654 ? 252 GLY   A N   1 
ATOM   1753 C  CA  . GLY   A 1 216 ? 13.92300  -38.13400 -26.75400 1.000 121.71172 ? 252 GLY   A CA  1 
ATOM   1754 C  C   . GLY   A 1 216 ? 12.64700  -38.64500 -27.38500 1.000 120.60262 ? 252 GLY   A C   1 
ATOM   1755 O  O   . GLY   A 1 216 ? 12.70200  -39.33500 -28.40900 1.000 117.84781 ? 252 GLY   A O   1 
ATOM   1756 N  N   . LEU   A 1 217 ? 11.49500  -38.32900 -26.79900 1.000 121.26659 ? 253 LEU   A N   1 
ATOM   1757 C  CA  . LEU   A 1 217 ? 10.22100  -38.75600 -27.35600 1.000 120.83310 ? 253 LEU   A CA  1 
ATOM   1758 C  C   . LEU   A 1 217 ? 9.83600   -37.87300 -28.53600 1.000 121.43955 ? 253 LEU   A C   1 
ATOM   1759 O  O   . LEU   A 1 217 ? 10.04900  -36.65700 -28.51800 1.000 121.76093 ? 253 LEU   A O   1 
ATOM   1760 C  CB  . LEU   A 1 217 ? 9.12600   -38.71500 -26.29000 1.000 120.29798 ? 253 LEU   A CB  1 
ATOM   1761 C  CG  . LEU   A 1 217 ? 9.31200   -39.64000 -25.08600 1.000 116.78615 ? 253 LEU   A CG  1 
ATOM   1762 C  CD1 . LEU   A 1 217 ? 8.03700   -39.70300 -24.25700 1.000 118.20572 ? 253 LEU   A CD1 1 
ATOM   1763 C  CD2 . LEU   A 1 217 ? 9.73600   -41.03100 -25.53400 1.000 119.79880 ? 253 LEU   A CD2 1 
ATOM   1764 N  N   . LYS   A 1 218 ? 9.26700   -38.49500 -29.56300 1.000 120.77674 ? 254 LYS   A N   1 
ATOM   1765 C  CA  . LYS   A 1 218 ? 8.91100   -37.80400 -30.79300 1.000 130.85576 ? 254 LYS   A CA  1 
ATOM   1766 C  C   . LYS   A 1 218 ? 7.42200   -37.48100 -30.81400 1.000 140.34541 ? 254 LYS   A C   1 
ATOM   1767 O  O   . LYS   A 1 218 ? 6.58600   -38.31700 -30.45400 1.000 143.16402 ? 254 LYS   A O   1 
ATOM   1768 C  CB  . LYS   A 1 218 ? 9.28600   -38.64000 -32.02000 1.000 137.93153 ? 254 LYS   A CB  1 
ATOM   1769 C  CG  . LYS   A 1 218 ? 10.49000  -38.09700 -32.78000 1.000 136.16120 ? 254 LYS   A CG  1 
ATOM   1770 C  CD  . LYS   A 1 218 ? 10.97000  -39.07200 -33.84300 1.000 136.10576 ? 254 LYS   A CD  1 
ATOM   1771 C  CE  . LYS   A 1 218 ? 11.60000  -40.30500 -33.21700 1.000 135.49893 ? 254 LYS   A CE  1 
ATOM   1772 N  NZ  . LYS   A 1 218 ? 12.20600  -41.19700 -34.24300 1.000 139.07849 ? 254 LYS   A NZ  1 
ATOM   1773 N  N   . ALA   A 1 219 ? 7.10700   -36.26100 -31.23700 1.000 145.79322 ? 255 ALA   A N   1 
ATOM   1774 C  CA  . ALA   A 1 219 ? 5.73100   -35.79400 -31.35800 1.000 147.56319 ? 255 ALA   A CA  1 
ATOM   1775 C  C   . ALA   A 1 219 ? 5.70600   -34.65900 -32.37100 1.000 150.72781 ? 255 ALA   A C   1 
ATOM   1776 O  O   . ALA   A 1 219 ? 6.73000   -34.00600 -32.60000 1.000 152.90871 ? 255 ALA   A O   1 
ATOM   1777 C  CB  . ALA   A 1 219 ? 5.17800   -35.33400 -29.99800 1.000 146.92303 ? 255 ALA   A CB  1 
ATOM   1778 N  N   . PRO   A 1 220 ? 4.55100   -34.40300 -33.00400 1.000 157.18906 ? 256 PRO   A N   1 
ATOM   1779 C  CA  . PRO   A 1 220 ? 4.48900   -33.34100 -34.02200 1.000 158.25502 ? 256 PRO   A CA  1 
ATOM   1780 C  C   . PRO   A 1 220 ? 4.91500   -31.97500 -33.50600 1.000 158.00043 ? 256 PRO   A C   1 
ATOM   1781 O  O   . PRO   A 1 220 ? 5.88800   -31.40000 -33.99900 1.000 154.54365 ? 256 PRO   A O   1 
ATOM   1782 C  CB  . PRO   A 1 220 ? 3.01500   -33.34800 -34.43600 1.000 159.59096 ? 256 PRO   A CB  1 
ATOM   1783 C  CG  . PRO   A 1 220 ? 2.56600   -34.74700 -34.17800 1.000 159.70208 ? 256 PRO   A CG  1 
ATOM   1784 C  CD  . PRO   A 1 220 ? 3.29400   -35.17100 -32.92800 1.000 153.49597 ? 256 PRO   A CD  1 
ATOM   1785 N  N   . THR   A 1 221 ? 4.19900   -31.44300 -32.52100 1.000 161.34037 ? 257 THR   A N   1 
ATOM   1786 C  CA  . THR   A 1 221 ? 4.51300   -30.16800 -31.90200 1.000 157.94962 ? 257 THR   A CA  1 
ATOM   1787 C  C   . THR   A 1 221 ? 4.94900   -30.41700 -30.45000 1.000 154.76389 ? 257 THR   A C   1 
ATOM   1788 O  O   . THR   A 1 221 ? 5.36700   -31.53400 -30.09500 1.000 152.73235 ? 257 THR   A O   1 
ATOM   1789 C  CB  . THR   A 1 221 ? 3.29800   -29.23500 -32.03100 1.000 159.20476 ? 257 THR   A CB  1 
ATOM   1790 O  OG1 . THR   A 1 221 ? 2.58900   -29.54400 -33.23800 1.000 167.39627 ? 257 THR   A OG1 1 
ATOM   1791 C  CG2 . THR   A 1 221 ? 3.73300   -27.78300 -32.07100 1.000 159.22056 ? 257 THR   A CG2 1 
ATOM   1792 N  N   . ASN   A 1 222 ? 4.85900   -29.38100 -29.61200 1.000 154.72571 ? 258 ASN   A N   1 
ATOM   1793 C  CA  . ASN   A 1 222 ? 5.35100   -29.48500 -28.24200 1.000 153.94130 ? 258 ASN   A CA  1 
ATOM   1794 C  C   . ASN   A 1 222 ? 4.26300   -29.82900 -27.23100 1.000 154.11430 ? 258 ASN   A C   1 
ATOM   1795 O  O   . ASN   A 1 222 ? 4.55700   -30.48700 -26.22700 1.000 149.99394 ? 258 ASN   A O   1 
ATOM   1796 C  CB  . ASN   A 1 222 ? 6.03900   -28.18600 -27.81500 1.000 154.48747 ? 258 ASN   A CB  1 
ATOM   1797 C  CG  . ASN   A 1 222 ? 5.10400   -26.98800 -27.84000 1.000 156.82922 ? 258 ASN   A CG  1 
ATOM   1798 O  OD1 . ASN   A 1 222 ? 4.06400   -26.97600 -27.17800 1.000 162.80535 ? 258 ASN   A OD1 1 
ATOM   1799 N  ND2 . ASN   A 1 222 ? 5.50100   -25.95100 -28.56300 1.000 150.69061 ? 258 ASN   A ND2 1 
ATOM   1800 N  N   . LYS   A 1 223 ? 3.02300   -29.38200 -27.45500 1.000 158.79731 ? 259 LYS   A N   1 
ATOM   1801 C  CA  . LYS   A 1 223 ? 1.91900   -29.76100 -26.57400 1.000 159.74633 ? 259 LYS   A CA  1 
ATOM   1802 C  C   . LYS   A 1 223 ? 1.81200   -31.27700 -26.46100 1.000 157.94049 ? 259 LYS   A C   1 
ATOM   1803 O  O   . LYS   A 1 223 ? 1.86400   -31.84400 -25.36300 1.000 156.63910 ? 259 LYS   A O   1 
ATOM   1804 C  CB  . LYS   A 1 223 ? 0.60100   -29.16600 -27.08300 1.000 158.63937 ? 259 LYS   A CB  1 
ATOM   1805 C  CG  . LYS   A 1 223 ? 0.35800   -27.71700 -26.68800 1.000 159.87777 ? 259 LYS   A CG  1 
ATOM   1806 C  CD  . LYS   A 1 223 ? -1.06100  -27.27400 -27.03300 1.000 159.13485 ? 259 LYS   A CD  1 
ATOM   1807 C  CE  . LYS   A 1 223 ? -2.09400  -27.89900 -26.10200 1.000 162.63010 ? 259 LYS   A CE  1 
ATOM   1808 N  NZ  . LYS   A 1 223 ? -3.45300  -27.31600 -26.29900 1.000 162.09576 ? 259 LYS   A NZ  1 
ATOM   1809 N  N   . GLN   A 1 224 ? 1.66700   -31.94700 -27.60500 1.000 152.55489 ? 260 GLN   A N   1 
ATOM   1810 C  CA  . GLN   A 1 224 ? 1.67200   -33.40400 -27.62900 1.000 149.54781 ? 260 GLN   A CA  1 
ATOM   1811 C  C   . GLN   A 1 224 ? 2.99200   -33.95900 -27.11400 1.000 147.62877 ? 260 GLN   A C   1 
ATOM   1812 O  O   . GLN   A 1 224 ? 3.01100   -35.01700 -26.47600 1.000 141.32351 ? 260 GLN   A O   1 
ATOM   1813 C  CB  . GLN   A 1 224 ? 1.39800   -33.91100 -29.04800 1.000 148.45702 ? 260 GLN   A CB  1 
ATOM   1814 C  CG  . GLN   A 1 224 ? 0.35400   -33.11400 -29.83000 1.000 151.94408 ? 260 GLN   A CG  1 
ATOM   1815 C  CD  . GLN   A 1 224 ? 0.89300   -31.79000 -30.33900 1.000 153.67215 ? 260 GLN   A CD  1 
ATOM   1816 O  OE1 . GLN   A 1 224 ? 2.08100   -31.50200 -30.19800 1.000 156.71251 ? 260 GLN   A OE1 1 
ATOM   1817 N  NE2 . GLN   A 1 224 ? 0.02100   -30.97100 -30.91400 1.000 150.57233 ? 260 GLN   A NE2 1 
ATOM   1818 N  N   . LYS   A 1 225 ? 4.10200   -33.26500 -27.38400 1.000 146.93558 ? 261 LYS   A N   1 
ATOM   1819 C  CA  . LYS   A 1 225 ? 5.37800   -33.63800 -26.78300 1.000 144.76227 ? 261 LYS   A CA  1 
ATOM   1820 C  C   . LYS   A 1 225 ? 5.31300   -33.53000 -25.26600 1.000 138.67303 ? 261 LYS   A C   1 
ATOM   1821 O  O   . LYS   A 1 225 ? 5.62300   -34.49100 -24.55100 1.000 131.19903 ? 261 LYS   A O   1 
ATOM   1822 C  CB  . LYS   A 1 225 ? 6.50200   -32.76300 -27.34500 1.000 146.19066 ? 261 LYS   A CB  1 
ATOM   1823 C  CG  . LYS   A 1 225 ? 7.58700   -32.39000 -26.33800 1.000 140.07046 ? 261 LYS   A CG  1 
ATOM   1824 C  CD  . LYS   A 1 225 ? 8.66700   -31.53900 -26.97500 1.000 140.49200 ? 261 LYS   A CD  1 
ATOM   1825 C  CE  . LYS   A 1 225 ? 9.58800   -32.38800 -27.83400 1.000 136.72831 ? 261 LYS   A CE  1 
ATOM   1826 N  NZ  . LYS   A 1 225 ? 10.18800  -33.49700 -27.04000 1.000 125.48404 ? 261 LYS   A NZ  1 
ATOM   1827 N  N   . TYR   A 1 226 ? 4.89500   -32.36600 -24.75500 1.000 143.84859 ? 262 TYR   A N   1 
ATOM   1828 C  CA  . TYR   A 1 226 ? 4.72900   -32.20900 -23.31400 1.000 136.19926 ? 262 TYR   A CA  1 
ATOM   1829 C  C   . TYR   A 1 226 ? 3.73700   -33.22800 -22.76600 1.000 135.34383 ? 262 TYR   A C   1 
ATOM   1830 O  O   . TYR   A 1 226 ? 3.92000   -33.75500 -21.66300 1.000 126.70147 ? 262 TYR   A O   1 
ATOM   1831 C  CB  . TYR   A 1 226 ? 4.27800   -30.78500 -22.98700 1.000 139.45592 ? 262 TYR   A CB  1 
ATOM   1832 C  CG  . TYR   A 1 226 ? 5.39300   -29.75400 -22.97900 1.000 138.15365 ? 262 TYR   A CG  1 
ATOM   1833 C  CD1 . TYR   A 1 226 ? 6.41200   -29.79200 -23.92200 1.000 140.18124 ? 262 TYR   A CD1 1 
ATOM   1834 C  CD2 . TYR   A 1 226 ? 5.41700   -28.73500 -22.03400 1.000 137.06273 ? 262 TYR   A CD2 1 
ATOM   1835 C  CE1 . TYR   A 1 226 ? 7.42500   -28.85400 -23.92000 1.000 138.72893 ? 262 TYR   A CE1 1 
ATOM   1836 C  CE2 . TYR   A 1 226 ? 6.42600   -27.79100 -22.02400 1.000 132.38915 ? 262 TYR   A CE2 1 
ATOM   1837 C  CZ  . TYR   A 1 226 ? 7.42800   -27.85600 -22.97000 1.000 133.27924 ? 262 TYR   A CZ  1 
ATOM   1838 O  OH  . TYR   A 1 226 ? 8.43800   -26.92100 -22.96800 1.000 132.24013 ? 262 TYR   A OH  1 
ATOM   1839 N  N   . GLU   A 1 227 ? 2.68900   -33.53000 -23.53500 1.000 139.24991 ? 263 GLU   A N   1 
ATOM   1840 C  CA  . GLU   A 1 227 ? 1.74900   -34.57600 -23.14800 1.000 136.98463 ? 263 GLU   A CA  1 
ATOM   1841 C  C   . GLU   A 1 227 ? 2.41900   -35.94600 -23.16900 1.000 133.55198 ? 263 GLU   A C   1 
ATOM   1842 O  O   . GLU   A 1 227 ? 2.34000   -36.71000 -22.20000 1.000 131.80899 ? 263 GLU   A O   1 
ATOM   1843 C  CB  . GLU   A 1 227 ? 0.53500   -34.55500 -24.08100 1.000 148.20453 ? 263 GLU   A CB  1 
ATOM   1844 C  CG  . GLU   A 1 227 ? -0.45000  -33.42500 -23.82600 1.000 146.34001 ? 263 GLU   A CG  1 
ATOM   1845 C  CD  . GLU   A 1 227 ? -1.44800  -33.26300 -24.95700 1.000 151.67424 ? 263 GLU   A CD  1 
ATOM   1846 O  OE1 . GLU   A 1 227 ? -1.07100  -32.70400 -26.00900 1.000 153.48025 ? 263 GLU   A OE1 1 
ATOM   1847 O  OE2 . GLU   A 1 227 ? -2.60500  -33.71000 -24.80100 1.000 161.16074 ? 263 GLU   A OE2 1 
ATOM   1848 N  N   . LYS   A 1 228 ? 3.08200   -36.27500 -24.28300 1.000 134.02295 ? 264 LYS   A N   1 
ATOM   1849 C  CA  . LYS   A 1 228 ? 3.69500   -37.59200 -24.42400 1.000 130.27547 ? 264 LYS   A CA  1 
ATOM   1850 C  C   . LYS   A 1 228 ? 4.72900   -37.86000 -23.33900 1.000 127.96677 ? 264 LYS   A C   1 
ATOM   1851 O  O   . LYS   A 1 228 ? 4.97100   -39.02000 -22.98800 1.000 126.72971 ? 264 LYS   A O   1 
ATOM   1852 C  CB  . LYS   A 1 228 ? 4.34000   -37.73700 -25.80100 1.000 131.12468 ? 264 LYS   A CB  1 
ATOM   1853 C  CG  . LYS   A 1 228 ? 3.49000   -38.48400 -26.81300 1.000 138.34511 ? 264 LYS   A CG  1 
ATOM   1854 C  CD  . LYS   A 1 228 ? 4.34500   -39.04300 -27.94200 1.000 143.07994 ? 264 LYS   A CD  1 
ATOM   1855 C  CE  . LYS   A 1 228 ? 3.64400   -40.19800 -28.64400 1.000 142.05422 ? 264 LYS   A CE  1 
ATOM   1856 N  NZ  . LYS   A 1 228 ? 4.52900   -40.85700 -29.64300 1.000 144.94834 ? 264 LYS   A NZ  1 
ATOM   1857 N  N   . ILE   A 1 229 ? 5.36200   -36.81300 -22.81100 1.000 129.78489 ? 265 ILE   A N   1 
ATOM   1858 C  CA  . ILE   A 1 229 ? 6.27000   -37.01900 -21.69000 1.000 127.37910 ? 265 ILE   A CA  1 
ATOM   1859 C  C   . ILE   A 1 229 ? 5.48100   -37.30300 -20.41800 1.000 124.90547 ? 265 ILE   A C   1 
ATOM   1860 O  O   . ILE   A 1 229 ? 5.93200   -38.06500 -19.55600 1.000 119.09357 ? 265 ILE   A O   1 
ATOM   1861 C  CB  . ILE   A 1 229 ? 7.20300   -35.80500 -21.52300 1.000 121.85038 ? 265 ILE   A CB  1 
ATOM   1862 C  CG1 . ILE   A 1 229 ? 8.02700   -35.56000 -22.79300 1.000 118.24317 ? 265 ILE   A CG1 1 
ATOM   1863 C  CG2 . ILE   A 1 229 ? 8.13300   -35.99800 -20.32700 1.000 120.35696 ? 265 ILE   A CG2 1 
ATOM   1864 C  CD1 . ILE   A 1 229 ? 8.88700   -34.31600 -22.71200 1.000 110.92998 ? 265 ILE   A CD1 1 
ATOM   1865 N  N   . GLY   A 1 230 ? 4.28700   -36.72300 -20.28700 1.000 123.50132 ? 266 GLY   A N   1 
ATOM   1866 C  CA  . GLY   A 1 230 ? 3.49700   -36.94100 -19.08600 1.000 121.33074 ? 266 GLY   A CA  1 
ATOM   1867 C  C   . GLY   A 1 230 ? 2.96400   -38.35700 -18.97200 1.000 128.98034 ? 266 GLY   A C   1 
ATOM   1868 O  O   . GLY   A 1 230 ? 2.84300   -38.89500 -17.86600 1.000 126.92097 ? 266 GLY   A O   1 
ATOM   1869 N  N   . ASP   A 1 231 ? 2.62800   -38.97400 -20.10800 1.000 135.97040 ? 267 ASP   A N   1 
ATOM   1870 C  CA  . ASP   A 1 231 ? 2.10800   -40.33900 -20.09600 1.000 130.12982 ? 267 ASP   A CA  1 
ATOM   1871 C  C   . ASP   A 1 231 ? 3.13100   -41.31200 -19.51800 1.000 129.26432 ? 267 ASP   A C   1 
ATOM   1872 O  O   . ASP   A 1 231 ? 2.82100   -42.09200 -18.61000 1.000 130.40910 ? 267 ASP   A O   1 
ATOM   1873 C  CB  . ASP   A 1 231 ? 1.71300   -40.75800 -21.51300 1.000 135.53997 ? 267 ASP   A CB  1 
ATOM   1874 C  CG  . ASP   A 1 231 ? 0.76900   -39.77300 -22.16800 1.000 141.73487 ? 267 ASP   A CG  1 
ATOM   1875 O  OD1 . ASP   A 1 231 ? -0.40100  -39.69400 -21.73300 1.000 137.50175 ? 267 ASP   A OD1 1 
ATOM   1876 O  OD2 . ASP   A 1 231 ? 1.18900   -39.06800 -23.11000 1.000 145.54172 ? 267 ASP   A OD2 1 
ATOM   1877 N  N   . LYS   A 1 232 ? 4.36500   -41.26800 -20.02700 1.000 131.33964 ? 268 LYS   A N   1 
ATOM   1878 C  CA  . LYS   A 1 232 ? 5.40200   -42.17500 -19.54600 1.000 122.26281 ? 268 LYS   A CA  1 
ATOM   1879 C  C   . LYS   A 1 232 ? 5.74300   -41.91500 -18.08400 1.000 121.80541 ? 268 LYS   A C   1 
ATOM   1880 O  O   . LYS   A 1 232 ? 6.13300   -42.84100 -17.36400 1.000 124.35409 ? 268 LYS   A O   1 
ATOM   1881 C  CB  . LYS   A 1 232 ? 6.64800   -42.04800 -20.42200 1.000 115.47085 ? 268 LYS   A CB  1 
ATOM   1882 C  CG  . LYS   A 1 232 ? 7.25600   -43.37700 -20.82500 1.000 120.34452 ? 268 LYS   A CG  1 
ATOM   1883 C  CD  . LYS   A 1 232 ? 7.60100   -43.39200 -22.30600 1.000 119.80592 ? 268 LYS   A CD  1 
ATOM   1884 C  CE  . LYS   A 1 232 ? 8.18800   -44.73100 -22.72800 1.000 116.94988 ? 268 LYS   A CE  1 
ATOM   1885 N  NZ  . LYS   A 1 232 ? 8.15400   -44.92000 -24.20700 1.000 116.83365 ? 268 LYS   A NZ  1 
ATOM   1886 N  N   . LYS   A 1 233 ? 5.60200   -40.66900 -17.62700 1.000 119.21696 ? 269 LYS   A N   1 
ATOM   1887 C  CA  . LYS   A 1 233 ? 5.81600   -40.38100 -16.21400 1.000 120.07880 ? 269 LYS   A CA  1 
ATOM   1888 C  C   . LYS   A 1 233 ? 4.77900   -41.07200 -15.34100 1.000 124.42297 ? 269 LYS   A C   1 
ATOM   1889 O  O   . LYS   A 1 233 ? 5.07200   -41.42700 -14.19400 1.000 125.97733 ? 269 LYS   A O   1 
ATOM   1890 C  CB  . LYS   A 1 233 ? 5.79000   -38.87300 -15.97100 1.000 117.09491 ? 269 LYS   A CB  1 
ATOM   1891 C  CG  . LYS   A 1 233 ? 7.01300   -38.13900 -16.49000 1.000 114.11688 ? 269 LYS   A CG  1 
ATOM   1892 C  CD  . LYS   A 1 233 ? 6.98700   -36.66900 -16.11100 1.000 108.23664 ? 269 LYS   A CD  1 
ATOM   1893 C  CE  . LYS   A 1 233 ? 8.25700   -35.96800 -16.56700 1.000 102.34420 ? 269 LYS   A CE  1 
ATOM   1894 N  NZ  . LYS   A 1 233 ? 8.26000   -34.52500 -16.20400 1.000 101.76954 ? 269 LYS   A NZ  1 
ATOM   1895 N  N   . ARG   A 1 234 ? 3.57200   -41.27100 -15.86300 1.000 140.76987 ? 270 ARG   A N   1 
ATOM   1896 C  CA  . ARG   A 1 234 ? 2.52000   -41.94200 -15.11700 1.000 146.28061 ? 270 ARG   A CA  1 
ATOM   1897 C  C   . ARG   A 1 234 ? 2.40300   -43.41900 -15.46700 1.000 145.36165 ? 270 ARG   A C   1 
ATOM   1898 O  O   . ARG   A 1 234 ? 1.79000   -44.17700 -14.70600 1.000 146.38006 ? 270 ARG   A O   1 
ATOM   1899 C  CB  . ARG   A 1 234 ? 1.18300   -41.23200 -15.35700 1.000 142.37919 ? 270 ARG   A CB  1 
ATOM   1900 C  CG  . ARG   A 1 234 ? 0.08400   -41.59800 -14.37900 1.000 149.73893 ? 270 ARG   A CG  1 
ATOM   1901 C  CD  . ARG   A 1 234 ? -0.87300  -40.43600 -14.17000 1.000 142.11475 ? 270 ARG   A CD  1 
ATOM   1902 N  NE  . ARG   A 1 234 ? -0.94300  -39.54300 -15.32100 1.000 143.62311 ? 270 ARG   A NE  1 
ATOM   1903 C  CZ  . ARG   A 1 234 ? -1.65500  -39.78000 -16.41400 1.000 146.48623 ? 270 ARG   A CZ  1 
ATOM   1904 N  NH1 . ARG   A 1 234 ? -2.33500  -40.90400 -16.56600 1.000 155.59752 ? 270 ARG   A NH1 1 
ATOM   1905 N  NH2 . ARG   A 1 234 ? -1.68400  -38.86500 -17.37900 1.000 146.04209 ? 270 ARG   A NH2 1 
ATOM   1906 N  N   . THR   A 1 235 ? 2.99100   -43.84500 -16.58600 1.000 135.04645 ? 271 THR   A N   1 
ATOM   1907 C  CA  . THR   A 1 235 ? 2.97200   -45.25600 -16.95500 1.000 134.62322 ? 271 THR   A CA  1 
ATOM   1908 C  C   . THR   A 1 235 ? 3.97500   -46.05700 -16.13300 1.000 140.41303 ? 271 THR   A C   1 
ATOM   1909 O  O   . THR   A 1 235 ? 3.64300   -47.12200 -15.60100 1.000 142.02959 ? 271 THR   A O   1 
ATOM   1910 C  CB  . THR   A 1 235 ? 3.26600   -45.41400 -18.44800 1.000 134.25276 ? 271 THR   A CB  1 
ATOM   1911 O  OG1 . THR   A 1 235 ? 2.65600   -44.34000 -19.17400 1.000 130.75375 ? 271 THR   A OG1 1 
ATOM   1912 C  CG2 . THR   A 1 235 ? 2.71300   -46.73600 -18.96100 1.000 139.27624 ? 271 THR   A CG2 1 
ATOM   1913 N  N   . THR   A 1 236 ? 5.20300   -45.56200 -16.02100 1.000 141.56704 ? 272 THR   A N   1 
ATOM   1914 C  CA  . THR   A 1 236 ? 6.24500   -46.28400 -15.30100 1.000 140.26354 ? 272 THR   A CA  1 
ATOM   1915 C  C   . THR   A 1 236 ? 6.15800   -45.97300 -13.81200 1.000 140.50185 ? 272 THR   A C   1 
ATOM   1916 O  O   . THR   A 1 236 ? 6.23700   -44.79900 -13.43100 1.000 132.79492 ? 272 THR   A O   1 
ATOM   1917 C  CB  . THR   A 1 236 ? 7.62800   -45.90900 -15.82200 1.000 135.30722 ? 272 THR   A CB  1 
ATOM   1918 O  OG1 . THR   A 1 236 ? 8.06900   -44.70100 -15.18800 1.000 128.32936 ? 272 THR   A OG1 1 
ATOM   1919 C  CG2 . THR   A 1 236 ? 7.59800   -45.70600 -17.33100 1.000 129.48956 ? 272 THR   A CG2 1 
ATOM   1920 N  N   . PRO   A 1 237 ? 5.99600   -46.97600 -12.94400 1.000 152.76754 ? 273 PRO   A N   1 
ATOM   1921 C  CA  . PRO   A 1 237 ? 6.04100   -46.71500 -11.49800 1.000 141.79184 ? 273 PRO   A CA  1 
ATOM   1922 C  C   . PRO   A 1 237 ? 7.41800   -46.25900 -11.04100 1.000 137.40705 ? 273 PRO   A C   1 
ATOM   1923 O  O   . PRO   A 1 237 ? 8.34900   -46.16800 -11.84800 1.000 137.00900 ? 273 PRO   A O   1 
ATOM   1924 C  CB  . PRO   A 1 237 ? 5.66000   -48.07000 -10.88500 1.000 145.53189 ? 273 PRO   A CB  1 
ATOM   1925 C  CG  . PRO   A 1 237 ? 5.97500   -49.07600 -11.94900 1.000 149.74683 ? 273 PRO   A CG  1 
ATOM   1926 C  CD  . PRO   A 1 237 ? 5.69500   -48.38500 -13.24800 1.000 148.66038 ? 273 PRO   A CD  1 
ATOM   1927 N  N   . ALA   A 1 238 ? 7.56500   -45.96100 -9.75100  1.000 132.75636 ? 274 ALA   A N   1 
ATOM   1928 C  CA  . ALA   A 1 238 ? 8.86400   -45.54400 -9.23900  1.000 118.07807 ? 274 ALA   A CA  1 
ATOM   1929 C  C   . ALA   A 1 238 ? 9.81300   -46.71500 -9.03600  1.000 121.23571 ? 274 ALA   A C   1 
ATOM   1930 O  O   . ALA   A 1 238 ? 11.02200  -46.49900 -8.90000  1.000 114.39982 ? 274 ALA   A O   1 
ATOM   1931 C  CB  . ALA   A 1 238 ? 8.69700   -44.78100 -7.92400  1.000 112.48192 ? 274 ALA   A CB  1 
ATOM   1932 N  N   . VAL   A 1 239 ? 9.29700   -47.94400 -9.01500  1.000 113.27365 ? 275 VAL   A N   1 
ATOM   1933 C  CA  . VAL   A 1 239 ? 10.14900  -49.11200 -8.82200  1.000 114.51910 ? 275 VAL   A CA  1 
ATOM   1934 C  C   . VAL   A 1 239 ? 10.94500  -49.42200 -10.08400 1.000 116.07104 ? 275 VAL   A C   1 
ATOM   1935 O  O   . VAL   A 1 239 ? 12.13000  -49.76900 -10.01100 1.000 122.39868 ? 275 VAL   A O   1 
ATOM   1936 C  CB  . VAL   A 1 239 ? 9.29700   -50.31300 -8.37200  1.000 118.02744 ? 275 VAL   A CB  1 
ATOM   1937 C  CG1 . VAL   A 1 239 ? 10.02300  -51.62700 -8.63800  1.000 120.15647 ? 275 VAL   A CG1 1 
ATOM   1938 C  CG2 . VAL   A 1 239 ? 8.96000   -50.19000 -6.89400  1.000 116.12229 ? 275 VAL   A CG2 1 
ATOM   1939 N  N   . THR   A 1 240 ? 10.32200  -49.29000 -11.25900 1.000 112.05833 ? 276 THR   A N   1 
ATOM   1940 C  CA  . THR   A 1 240 ? 11.03700  -49.58800 -12.49600 1.000 116.99023 ? 276 THR   A CA  1 
ATOM   1941 C  C   . THR   A 1 240 ? 12.11200  -48.54700 -12.79000 1.000 125.14299 ? 276 THR   A C   1 
ATOM   1942 O  O   . THR   A 1 240 ? 13.10200  -48.85700 -13.46200 1.000 128.36432 ? 276 THR   A O   1 
ATOM   1943 C  CB  . THR   A 1 240 ? 10.05700  -49.70400 -13.66500 1.000 121.44075 ? 276 THR   A CB  1 
ATOM   1944 O  OG1 . THR   A 1 240 ? 10.78500  -49.94900 -14.87400 1.000 117.68050 ? 276 THR   A OG1 1 
ATOM   1945 C  CG2 . THR   A 1 240 ? 9.24800   -48.43400 -13.82100 1.000 130.53905 ? 276 THR   A CG2 1 
ATOM   1946 N  N   . LEU   A 1 241 ? 11.94200  -47.31700 -12.29900 1.000 119.33826 ? 277 LEU   A N   1 
ATOM   1947 C  CA  . LEU   A 1 241 ? 13.01700  -46.33600 -12.38800 1.000 117.89610 ? 277 LEU   A CA  1 
ATOM   1948 C  C   . LEU   A 1 241 ? 14.15700  -46.65300 -11.43100 1.000 114.40932 ? 277 LEU   A C   1 
ATOM   1949 O  O   . LEU   A 1 241 ? 15.29400  -46.23100 -11.67500 1.000 113.51117 ? 277 LEU   A O   1 
ATOM   1950 C  CB  . LEU   A 1 241 ? 12.48600  -44.92900 -12.11100 1.000 114.69618 ? 277 LEU   A CB  1 
ATOM   1951 C  CG  . LEU   A 1 241 ? 11.69100  -44.29000 -13.24900 1.000 114.03885 ? 277 LEU   A CG  1 
ATOM   1952 C  CD1 . LEU   A 1 241 ? 11.43900  -42.81600 -12.97600 1.000 102.96177 ? 277 LEU   A CD1 1 
ATOM   1953 C  CD2 . LEU   A 1 241 ? 12.43300  -44.47800 -14.55700 1.000 116.54701 ? 277 LEU   A CD2 1 
ATOM   1954 N  N   . CYS   A 1 242 ? 13.88100  -47.38900 -10.35900 1.000 115.56684 ? 278 CYS   A N   1 
ATOM   1955 C  CA  . CYS   A 1 242 ? 14.88900  -47.78500 -9.38800  1.000 110.18086 ? 278 CYS   A CA  1 
ATOM   1956 C  C   . CYS   A 1 242 ? 15.54600  -49.11500 -9.73200  1.000 117.58238 ? 278 CYS   A C   1 
ATOM   1957 O  O   . CYS   A 1 242 ? 16.20400  -49.70700 -8.87000  1.000 108.42201 ? 278 CYS   A O   1 
ATOM   1958 C  CB  . CYS   A 1 242 ? 14.26700  -47.86600 -7.99400  1.000 106.54610 ? 278 CYS   A CB  1 
ATOM   1959 S  SG  . CYS   A 1 242 ? 15.08300  -46.85300 -6.75900  1.000 104.71720 ? 278 CYS   A SG  1 
ATOM   1960 N  N   . ASP   A 1 243 ? 15.37800  -49.59500 -10.96400 1.000 121.98053 ? 279 ASP   A N   1 
ATOM   1961 C  CA  . ASP   A 1 243 ? 15.91900  -50.89100 -11.35500 1.000 125.65924 ? 279 ASP   A CA  1 
ATOM   1962 C  C   . ASP   A 1 243 ? 17.43400  -50.90100 -11.20500 1.000 129.29839 ? 279 ASP   A C   1 
ATOM   1963 O  O   . ASP   A 1 243 ? 18.13300  -50.07700 -11.80200 1.000 125.52435 ? 279 ASP   A O   1 
ATOM   1964 C  CB  . ASP   A 1 243 ? 15.52900  -51.20900 -12.79600 1.000 128.71523 ? 279 ASP   A CB  1 
ATOM   1965 C  CG  . ASP   A 1 243 ? 15.73100  -52.67000 -13.14300 1.000 139.28765 ? 279 ASP   A CG  1 
ATOM   1966 O  OD1 . ASP   A 1 243 ? 16.02300  -53.46400 -12.22300 1.000 143.05820 ? 279 ASP   A OD1 1 
ATOM   1967 O  OD2 . ASP   A 1 243 ? 15.57800  -53.02900 -14.32900 1.000 143.87086 ? 279 ASP   A OD2 1 
ATOM   1968 N  N   . GLY   A 1 244 ? 17.93900  -51.83900 -10.40500 1.000 147.20542 ? 280 GLY   A N   1 
ATOM   1969 C  CA  . GLY   A 1 244 ? 19.35900  -51.89900 -10.12900 1.000 148.88403 ? 280 GLY   A CA  1 
ATOM   1970 C  C   . GLY   A 1 244 ? 19.88800  -50.77000 -9.27800  1.000 141.87756 ? 280 GLY   A C   1 
ATOM   1971 O  O   . GLY   A 1 244 ? 21.10500  -50.66300 -9.10200  1.000 147.86271 ? 280 GLY   A O   1 
ATOM   1972 N  N   . LEU   A 1 245 ? 19.01400  -49.92800 -8.74400  1.000 121.76493 ? 281 LEU   A N   1 
ATOM   1973 C  CA  . LEU   A 1 245 ? 19.37900  -48.77400 -7.94400  1.000 110.60347 ? 281 LEU   A CA  1 
ATOM   1974 C  C   . LEU   A 1 245 ? 18.89200  -48.93900 -6.51000  1.000 110.21169 ? 281 LEU   A C   1 
ATOM   1975 O  O   . LEU   A 1 245 ? 18.00000  -49.75100 -6.23600  1.000 118.01842 ? 281 LEU   A O   1 
ATOM   1976 C  CB  . LEU   A 1 245 ? 18.78400  -47.49700 -8.55200  1.000 107.75779 ? 281 LEU   A CB  1 
ATOM   1977 C  CG  . LEU   A 1 245 ? 19.19100  -47.22000 -9.99900  1.000 110.45947 ? 281 LEU   A CG  1 
ATOM   1978 C  CD1 . LEU   A 1 245 ? 18.68600  -45.85700 -10.44600 1.000 109.72465 ? 281 LEU   A CD1 1 
ATOM   1979 C  CD2 . LEU   A 1 245 ? 20.70200  -47.32500 -10.16100 1.000 109.76251 ? 281 LEU   A CD2 1 
ATOM   1980 N  N   . PRO   A 1 246 ? 19.47100  -48.20200 -5.56300  1.000 106.23778 ? 282 PRO   A N   1 
ATOM   1981 C  CA  . PRO   A 1 246 ? 18.99200  -48.27500 -4.17300  1.000 107.26794 ? 282 PRO   A CA  1 
ATOM   1982 C  C   . PRO   A 1 246 ? 17.52700  -47.88100 -4.07400  1.000 115.44827 ? 282 PRO   A C   1 
ATOM   1983 O  O   . PRO   A 1 246 ? 17.13000  -46.78600 -4.48000  1.000 103.39455 ? 282 PRO   A O   1 
ATOM   1984 C  CB  . PRO   A 1 246 ? 19.90000  -47.28400 -3.43800  1.000 108.90860 ? 282 PRO   A CB  1 
ATOM   1985 C  CG  . PRO   A 1 246 ? 21.13900  -47.22800 -4.26600  1.000 97.69499  ? 282 PRO   A CG  1 
ATOM   1986 C  CD  . PRO   A 1 246 ? 20.68900  -47.38100 -5.68500  1.000 97.02581  ? 282 PRO   A CD  1 
ATOM   1987 N  N   . GLN   A 1 247 ? 16.72300  -48.78500 -3.50400  1.000 131.06282 ? 283 GLN   A N   1 
ATOM   1988 C  CA  . GLN   A 1 247 ? 15.27100  -48.63400 -3.51300  1.000 135.68222 ? 283 GLN   A CA  1 
ATOM   1989 C  C   . GLN   A 1 247 ? 14.79700  -47.38600 -2.77900  1.000 134.53107 ? 283 GLN   A C   1 
ATOM   1990 O  O   . GLN   A 1 247 ? 13.63600  -46.99300 -2.94300  1.000 134.09011 ? 283 GLN   A O   1 
ATOM   1991 C  CB  . GLN   A 1 247 ? 14.60700  -49.87000 -2.89900  1.000 138.77815 ? 283 GLN   A CB  1 
ATOM   1992 C  CG  . GLN   A 1 247 ? 15.17700  -51.19600 -3.38000  1.000 145.36079 ? 283 GLN   A CG  1 
ATOM   1993 C  CD  . GLN   A 1 247 ? 16.35400  -51.66400 -2.54300  1.000 153.24974 ? 283 GLN   A CD  1 
ATOM   1994 O  OE1 . GLN   A 1 247 ? 17.43500  -51.93700 -3.06700  1.000 153.93176 ? 283 GLN   A OE1 1 
ATOM   1995 N  NE2 . GLN   A 1 247 ? 16.14700  -51.76500 -1.23500  1.000 159.16641 ? 283 GLN   A NE2 1 
ATOM   1996 N  N   . GLN   A 1 248 ? 15.65900  -46.75700 -1.97400  1.000 113.60343 ? 284 GLN   A N   1 
ATOM   1997 C  CA  . GLN   A 1 248 ? 15.26700  -45.53400 -1.28400  1.000 113.05302 ? 284 GLN   A CA  1 
ATOM   1998 C  C   . GLN   A 1 248 ? 14.89500  -44.41900 -2.25200  1.000 103.26891 ? 284 GLN   A C   1 
ATOM   1999 O  O   . GLN   A 1 248 ? 14.14200  -43.51400 -1.87700  1.000 99.29685  ? 284 GLN   A O   1 
ATOM   2000 C  CB  . GLN   A 1 248 ? 16.38700  -45.05600 -0.35700  1.000 111.51679 ? 284 GLN   A CB  1 
ATOM   2001 C  CG  . GLN   A 1 248 ? 16.65500  -45.95700 0.84200   1.000 108.81826 ? 284 GLN   A CG  1 
ATOM   2002 C  CD  . GLN   A 1 248 ? 17.65600  -47.06000 0.54500   1.000 106.59488 ? 284 GLN   A CD  1 
ATOM   2003 O  OE1 . GLN   A 1 248 ? 17.73900  -47.55700 -0.57800  1.000 106.05532 ? 284 GLN   A OE1 1 
ATOM   2004 N  NE2 . GLN   A 1 248 ? 18.42800  -47.44200 1.55600   1.000 102.08497 ? 284 GLN   A NE2 1 
ATOM   2005 N  N   . PHE   A 1 249 ? 15.40600  -44.45900 -3.48500  1.000 98.19274  ? 285 PHE   A N   1 
ATOM   2006 C  CA  . PHE   A 1 249 ? 14.99500  -43.47500 -4.48000  1.000 99.13975  ? 285 PHE   A CA  1 
ATOM   2007 C  C   . PHE   A 1 249 ? 13.56500  -43.72500 -4.94100  1.000 102.66182 ? 285 PHE   A C   1 
ATOM   2008 O  O   . PHE   A 1 249 ? 12.79800  -42.77600 -5.14500  1.000 93.71582  ? 285 PHE   A O   1 
ATOM   2009 C  CB  . PHE   A 1 249 ? 15.95600  -43.48900 -5.66700  1.000 91.70664  ? 285 PHE   A CB  1 
ATOM   2010 C  CG  . PHE   A 1 249 ? 17.30500  -42.90100 -5.36400  1.000 95.10119  ? 285 PHE   A CG  1 
ATOM   2011 C  CD1 . PHE   A 1 249 ? 17.49100  -41.52800 -5.36100  1.000 94.15317  ? 285 PHE   A CD1 1 
ATOM   2012 C  CD2 . PHE   A 1 249 ? 18.38800  -43.71900 -5.09100  1.000 85.44280  ? 285 PHE   A CD2 1 
ATOM   2013 C  CE1 . PHE   A 1 249 ? 18.72900  -40.98200 -5.08500  1.000 82.80953  ? 285 PHE   A CE1 1 
ATOM   2014 C  CE2 . PHE   A 1 249 ? 19.62900  -43.18000 -4.81500  1.000 83.90471  ? 285 PHE   A CE2 1 
ATOM   2015 C  CZ  . PHE   A 1 249 ? 19.80000  -41.81000 -4.81200  1.000 89.57487  ? 285 PHE   A CZ  1 
ATOM   2016 N  N   . ALA   A 1 250 ? 13.18800  -44.99600 -5.11600  1.000 103.86453 ? 286 ALA   A N   1 
ATOM   2017 C  CA  . ALA   A 1 250 ? 11.80500  -45.31400 -5.45400  1.000 101.15501 ? 286 ALA   A CA  1 
ATOM   2018 C  C   . ALA   A 1 250 ? 10.85800  -44.87400 -4.34700  1.000 99.68825  ? 286 ALA   A C   1 
ATOM   2019 O  O   . ALA   A 1 250 ? 9.76100   -44.37300 -4.62000  1.000 103.04965 ? 286 ALA   A O   1 
ATOM   2020 C  CB  . ALA   A 1 250 ? 11.65500  -46.81100 -5.72100  1.000 102.90906 ? 286 ALA   A CB  1 
ATOM   2021 N  N   . GLU   A 1 251 ? 11.26600  -45.05500 -3.08900  1.000 102.84625 ? 287 GLU   A N   1 
ATOM   2022 C  CA  . GLU   A 1 251 ? 10.45000  -44.58800 -1.97400  1.000 111.24265 ? 287 GLU   A CA  1 
ATOM   2023 C  C   . GLU   A 1 251 ? 10.34300  -43.07000 -1.96500  1.000 104.28794 ? 287 GLU   A C   1 
ATOM   2024 O  O   . GLU   A 1 251 ? 9.27600   -42.52000 -1.66900  1.000 103.08416 ? 287 GLU   A O   1 
ATOM   2025 C  CB  . GLU   A 1 251 ? 11.02600  -45.08200 -0.64900  1.000 115.43166 ? 287 GLU   A CB  1 
ATOM   2026 C  CG  . GLU   A 1 251 ? 10.92200  -46.57800 -0.43200  1.000 127.13522 ? 287 GLU   A CG  1 
ATOM   2027 C  CD  . GLU   A 1 251 ? 11.28600  -46.97600 0.98300   1.000 143.83361 ? 287 GLU   A CD  1 
ATOM   2028 O  OE1 . GLU   A 1 251 ? 10.98800  -46.19800 1.91400   1.000 146.44978 ? 287 GLU   A OE1 1 
ATOM   2029 O  OE2 . GLU   A 1 251 ? 11.87600  -48.06100 1.16500   1.000 153.95856 ? 287 GLU   A OE2 1 
ATOM   2030 N  N   . TYR   A 1 252 ? 11.43900  -42.37500 -2.28400  1.000 98.15466  ? 288 TYR   A N   1 
ATOM   2031 C  CA  . TYR   A 1 252 ? 11.42100  -40.91700 -2.25900  1.000 98.70183  ? 288 TYR   A CA  1 
ATOM   2032 C  C   . TYR   A 1 252 ? 10.42400  -40.36100 -3.26700  1.000 95.55684  ? 288 TYR   A C   1 
ATOM   2033 O  O   . TYR   A 1 252 ? 9.58900   -39.51400 -2.92900  1.000 100.23226 ? 288 TYR   A O   1 
ATOM   2034 C  CB  . TYR   A 1 252 ? 12.81800  -40.35500 -2.52800  1.000 93.63056  ? 288 TYR   A CB  1 
ATOM   2035 C  CG  . TYR   A 1 252 ? 12.80700  -38.85700 -2.74200  1.000 85.65688  ? 288 TYR   A CG  1 
ATOM   2036 C  CD1 . TYR   A 1 252 ? 12.70500  -37.98600 -1.66600  1.000 91.97922  ? 288 TYR   A CD1 1 
ATOM   2037 C  CD2 . TYR   A 1 252 ? 12.87600  -38.31500 -4.01900  1.000 79.28616  ? 288 TYR   A CD2 1 
ATOM   2038 C  CE1 . TYR   A 1 252 ? 12.68100  -36.61800 -1.85300  1.000 88.65921  ? 288 TYR   A CE1 1 
ATOM   2039 C  CE2 . TYR   A 1 252 ? 12.85000  -36.94800 -4.21500  1.000 79.87961  ? 288 TYR   A CE2 1 
ATOM   2040 C  CZ  . TYR   A 1 252 ? 12.75400  -36.10500 -3.13000  1.000 79.57565  ? 288 TYR   A CZ  1 
ATOM   2041 O  OH  . TYR   A 1 252 ? 12.72900  -34.74200 -3.32200  1.000 78.13329  ? 288 TYR   A OH  1 
ATOM   2042 N  N   . LEU   A 1 253 ? 10.49700  -40.82400 -4.51700  1.000 92.76154  ? 289 LEU   A N   1 
ATOM   2043 C  CA  . LEU   A 1 253 ? 9.61200   -40.28800 -5.54500  1.000 94.67604  ? 289 LEU   A CA  1 
ATOM   2044 C  C   . LEU   A 1 253 ? 8.15800   -40.66200 -5.27500  1.000 100.63402 ? 289 LEU   A C   1 
ATOM   2045 O  O   . LEU   A 1 253 ? 7.25400   -39.84900 -5.49800  1.000 93.47916  ? 289 LEU   A O   1 
ATOM   2046 C  CB  . LEU   A 1 253 ? 10.05400  -40.77300 -6.92500  1.000 93.35384  ? 289 LEU   A CB  1 
ATOM   2047 C  CG  . LEU   A 1 253 ? 9.33000   -40.14600 -8.11800  1.000 94.55431  ? 289 LEU   A CG  1 
ATOM   2048 C  CD1 . LEU   A 1 253 ? 9.15800   -38.64900 -7.91500  1.000 94.44367  ? 289 LEU   A CD1 1 
ATOM   2049 C  CD2 . LEU   A 1 253 ? 10.09000  -40.42200 -9.40600  1.000 98.75592  ? 289 LEU   A CD2 1 
ATOM   2050 N  N   . ASP   A 1 254 ? 7.91400   -41.87900 -4.78500  1.000 96.46064  ? 290 ASP   A N   1 
ATOM   2051 C  CA  . ASP   A 1 254 ? 6.54600   -42.28500 -4.47700  1.000 101.28018 ? 290 ASP   A CA  1 
ATOM   2052 C  C   . ASP   A 1 254 ? 5.97400   -41.48200 -3.31500  1.000 104.62911 ? 290 ASP   A C   1 
ATOM   2053 O  O   . ASP   A 1 254 ? 4.78400   -41.14700 -3.31200  1.000 104.40893 ? 290 ASP   A O   1 
ATOM   2054 C  CB  . ASP   A 1 254 ? 6.49600   -43.78000 -4.17000  1.000 106.54174 ? 290 ASP   A CB  1 
ATOM   2055 C  CG  . ASP   A 1 254 ? 6.30700   -44.62100 -5.41400  1.000 112.81125 ? 290 ASP   A CG  1 
ATOM   2056 O  OD1 . ASP   A 1 254 ? 5.94300   -44.05100 -6.46400  1.000 106.68124 ? 290 ASP   A OD1 1 
ATOM   2057 O  OD2 . ASP   A 1 254 ? 6.52200   -45.85000 -5.34500  1.000 121.19914 ? 290 ASP   A OD2 1 
ATOM   2058 N  N   . SER   A 1 255 ? 6.80400   -41.16600 -2.31900  1.000 100.26934 ? 291 SER   A N   1 
ATOM   2059 C  CA  . SER   A 1 255 ? 6.31900   -40.40800 -1.17100  1.000 103.03995 ? 291 SER   A CA  1 
ATOM   2060 C  C   . SER   A 1 255 ? 5.94800   -38.98500 -1.57000  1.000 105.77919 ? 291 SER   A C   1 
ATOM   2061 O  O   . SER   A 1 255 ? 4.84800   -38.51000 -1.26100  1.000 105.09667 ? 291 SER   A O   1 
ATOM   2062 C  CB  . SER   A 1 255 ? 7.37100   -40.40200 -0.06100  1.000 102.28198 ? 291 SER   A CB  1 
ATOM   2063 O  OG  . SER   A 1 255 ? 6.90600   -39.69200 1.07400   1.000 108.30788 ? 291 SER   A OG  1 
ATOM   2064 N  N   . VAL   A 1 256 ? 6.85200   -38.29000 -2.26700  1.000 104.98043 ? 292 VAL   A N   1 
ATOM   2065 C  CA  . VAL   A 1 256 ? 6.58800   -36.91800 -2.68800  1.000 106.86479 ? 292 VAL   A CA  1 
ATOM   2066 C  C   . VAL   A 1 256 ? 5.51100   -36.82600 -3.75600  1.000 104.87674 ? 292 VAL   A C   1 
ATOM   2067 O  O   . VAL   A 1 256 ? 5.00500   -35.73000 -4.01700  1.000 107.89465 ? 292 VAL   A O   1 
ATOM   2068 C  CB  . VAL   A 1 256 ? 7.87300   -36.23600 -3.20400  1.000 100.67135 ? 292 VAL   A CB  1 
ATOM   2069 C  CG1 . VAL   A 1 256 ? 9.01600   -36.43000 -2.21500  1.000 99.53997  ? 292 VAL   A CG1 1 
ATOM   2070 C  CG2 . VAL   A 1 256 ? 8.24200   -36.76000 -4.58500  1.000 96.62846  ? 292 VAL   A CG2 1 
ATOM   2071 N  N   . ARG   A 1 257 ? 5.14900   -37.94500 -4.38400  1.000 102.24051 ? 293 ARG   A N   1 
ATOM   2072 C  CA  . ARG   A 1 257 ? 4.06300   -37.94900 -5.35400  1.000 105.74703 ? 293 ARG   A CA  1 
ATOM   2073 C  C   . ARG   A 1 257 ? 2.69600   -38.12800 -4.71200  1.000 98.69096  ? 293 ARG   A C   1 
ATOM   2074 O  O   . ARG   A 1 257 ? 1.68700   -37.77100 -5.32900  1.000 95.10161  ? 293 ARG   A O   1 
ATOM   2075 C  CB  . ARG   A 1 257 ? 4.28400   -39.05000 -6.39700  1.000 103.19284 ? 293 ARG   A CB  1 
ATOM   2076 C  CG  . ARG   A 1 257 ? 5.17000   -38.62900 -7.56000  1.000 98.41473  ? 293 ARG   A CG  1 
ATOM   2077 C  CD  . ARG   A 1 257 ? 5.38600   -39.77200 -8.54000  1.000 97.32578  ? 293 ARG   A CD  1 
ATOM   2078 N  NE  . ARG   A 1 257 ? 6.06700   -39.33200 -9.75200  1.000 92.57796  ? 293 ARG   A NE  1 
ATOM   2079 C  CZ  . ARG   A 1 257 ? 6.41600   -40.13500 -10.74800 1.000 95.19764  ? 293 ARG   A CZ  1 
ATOM   2080 N  NH1 . ARG   A 1 257 ? 6.17500   -41.43500 -10.70500 1.000 87.33570  ? 293 ARG   A NH1 1 
ATOM   2081 N  NH2 . ARG   A 1 257 ? 7.02400   -39.62100 -11.81400 1.000 93.93745  ? 293 ARG   A NH2 1 
ATOM   2082 N  N   . SER   A 1 258 ? 2.63800   -38.66700 -3.49500  1.000 104.66826 ? 294 SER   A N   1 
ATOM   2083 C  CA  . SER   A 1 258 ? 1.38800   -38.82400 -2.76700  1.000 101.24754 ? 294 SER   A CA  1 
ATOM   2084 C  C   . SER   A 1 258 ? 1.18700   -37.73900 -1.71700  1.000 103.34185 ? 294 SER   A C   1 
ATOM   2085 O  O   . SER   A 1 258 ? 0.33000   -37.88900 -0.84100  1.000 96.93322  ? 294 SER   A O   1 
ATOM   2086 C  CB  . SER   A 1 258 ? 1.32700   -40.20400 -2.10800  1.000 100.68687 ? 294 SER   A CB  1 
ATOM   2087 O  OG  . SER   A 1 258 ? 2.33100   -40.34600 -1.11700  1.000 106.16742 ? 294 SER   A OG  1 
ATOM   2088 N  N   . LEU   A 1 259 ? 1.96300   -36.65600 -1.77900  1.000 105.28885 ? 295 LEU   A N   1 
ATOM   2089 C  CA  . LEU   A 1 259 ? 1.83000   -35.56700 -0.82200  1.000 106.30120 ? 295 LEU   A CA  1 
ATOM   2090 C  C   . LEU   A 1 259 ? 0.61200   -34.71200 -1.16100  1.000 104.73409 ? 295 LEU   A C   1 
ATOM   2091 O  O   . LEU   A 1 259 ? 0.36000   -34.42700 -2.33500  1.000 104.54058 ? 295 LEU   A O   1 
ATOM   2092 C  CB  . LEU   A 1 259 ? 3.08400   -34.69600 -0.82100  1.000 102.49434 ? 295 LEU   A CB  1 
ATOM   2093 C  CG  . LEU   A 1 259 ? 4.19100   -35.07900 0.16100   1.000 99.96704  ? 295 LEU   A CG  1 
ATOM   2094 C  CD1 . LEU   A 1 259 ? 5.46000   -34.30500 -0.14700  1.000 101.67321 ? 295 LEU   A CD1 1 
ATOM   2095 C  CD2 . LEU   A 1 259 ? 3.74200   -34.82300 1.59100   1.000 103.31173 ? 295 LEU   A CD2 1 
ATOM   2096 N  N   . PRO   A 1 260 ? -0.16300  -34.30300 -0.16200  1.000 108.83640 ? 296 PRO   A N   1 
ATOM   2097 C  CA  . PRO   A 1 260 ? -1.28200  -33.39400 -0.42500  1.000 113.05404 ? 296 PRO   A CA  1 
ATOM   2098 C  C   . PRO   A 1 260 ? -0.79100  -32.00200 -0.79900  1.000 115.21085 ? 296 PRO   A C   1 
ATOM   2099 O  O   . PRO   A 1 260 ? 0.38700   -31.65600 -0.67800  1.000 106.82921 ? 296 PRO   A O   1 
ATOM   2100 C  CB  . PRO   A 1 260 ? -2.07300  -33.39000 0.88600   1.000 106.90270 ? 296 PRO   A CB  1 
ATOM   2101 C  CG  . PRO   A 1 260 ? -1.13900  -33.88800 1.91300   1.000 112.79805 ? 296 PRO   A CG  1 
ATOM   2102 C  CD  . PRO   A 1 260 ? -0.14600  -34.78000 1.23100   1.000 112.42620 ? 296 PRO   A CD  1 
ATOM   2103 N  N   . PHE   A 1 261 ? -1.75200  -31.19800 -1.26100  1.000 121.27220 ? 297 PHE   A N   1 
ATOM   2104 C  CA  . PHE   A 1 261 ? -1.44900  -29.95000 -1.95700  1.000 121.70381 ? 297 PHE   A CA  1 
ATOM   2105 C  C   . PHE   A 1 261 ? -0.74500  -28.95100 -1.04600  1.000 125.80312 ? 297 PHE   A C   1 
ATOM   2106 O  O   . PHE   A 1 261 ? 0.27300   -28.36200 -1.42500  1.000 124.51580 ? 297 PHE   A O   1 
ATOM   2107 C  CB  . PHE   A 1 261 ? -2.74500  -29.36300 -2.52800  1.000 125.69366 ? 297 PHE   A CB  1 
ATOM   2108 C  CG  . PHE   A 1 261 ? -2.63100  -27.93600 -2.98900  1.000 128.79530 ? 297 PHE   A CG  1 
ATOM   2109 C  CD1 . PHE   A 1 261 ? -2.11200  -27.62900 -4.24000  1.000 123.84278 ? 297 PHE   A CD1 1 
ATOM   2110 C  CD2 . PHE   A 1 261 ? -3.08600  -26.90200 -2.18600  1.000 129.21632 ? 297 PHE   A CD2 1 
ATOM   2111 C  CE1 . PHE   A 1 261 ? -2.02600  -26.31800 -4.66500  1.000 122.56972 ? 297 PHE   A CE1 1 
ATOM   2112 C  CE2 . PHE   A 1 261 ? -2.99600  -25.59700 -2.60800  1.000 127.80315 ? 297 PHE   A CE2 1 
ATOM   2113 C  CZ  . PHE   A 1 261 ? -2.46200  -25.30000 -3.85100  1.000 123.21369 ? 297 PHE   A CZ  1 
ATOM   2114 N  N   . ASP   A 1 262 ? -1.26500  -28.75400 0.16500   1.000 146.13514 ? 298 ASP   A N   1 
ATOM   2115 C  CA  . ASP   A 1 262 ? -0.78100  -27.71800 1.07000   1.000 143.30640 ? 298 ASP   A CA  1 
ATOM   2116 C  C   . ASP   A 1 262 ? 0.13200   -28.24200 2.17100   1.000 141.54930 ? 298 ASP   A C   1 
ATOM   2117 O  O   . ASP   A 1 262 ? 0.53000   -27.46700 3.04700   1.000 148.03636 ? 298 ASP   A O   1 
ATOM   2118 C  CB  . ASP   A 1 262 ? -1.96700  -26.98700 1.70700   1.000 144.11554 ? 298 ASP   A CB  1 
ATOM   2119 C  CG  . ASP   A 1 262 ? -2.95800  -27.93900 2.34700   1.000 141.65179 ? 298 ASP   A CG  1 
ATOM   2120 O  OD1 . ASP   A 1 262 ? -2.75500  -29.16700 2.24000   1.000 142.81593 ? 298 ASP   A OD1 1 
ATOM   2121 O  OD2 . ASP   A 1 262 ? -3.94000  -27.46400 2.95400   1.000 150.22443 ? 298 ASP   A OD2 1 
ATOM   2122 N  N   . ALA   A 1 263 ? 0.47500   -29.52500 2.15000   1.000 125.57589 ? 299 ALA   A N   1 
ATOM   2123 C  CA  . ALA   A 1 263 ? 1.22200   -30.11200 3.25100   1.000 126.13923 ? 299 ALA   A CA  1 
ATOM   2124 C  C   . ALA   A 1 263 ? 2.66900   -29.63800 3.25300   1.000 127.33504 ? 299 ALA   A C   1 
ATOM   2125 O  O   . ALA   A 1 263 ? 3.27700   -29.40500 2.20500   1.000 119.41924 ? 299 ALA   A O   1 
ATOM   2126 C  CB  . ALA   A 1 263 ? 1.18500   -31.63600 3.16900   1.000 118.88474 ? 299 ALA   A CB  1 
ATOM   2127 N  N   . GLU   A 1 264 ? 3.21600   -29.49300 4.45400   1.000 127.39168 ? 300 GLU   A N   1 
ATOM   2128 C  CA  . GLU   A 1 264 ? 4.64300   -29.26700 4.61100   1.000 130.78334 ? 300 GLU   A CA  1 
ATOM   2129 C  C   . GLU   A 1 264 ? 5.36800   -30.61100 4.48100   1.000 126.83189 ? 300 GLU   A C   1 
ATOM   2130 O  O   . GLU   A 1 264 ? 5.13500   -31.49900 5.30200   1.000 130.34800 ? 300 GLU   A O   1 
ATOM   2131 C  CB  . GLU   A 1 264 ? 4.95100   -28.63800 5.96100   1.000 139.54409 ? 300 GLU   A CB  1 
ATOM   2132 C  CG  . GLU   A 1 264 ? 6.39600   -28.18800 6.11900   1.000 139.11056 ? 300 GLU   A CG  1 
ATOM   2133 C  CD  . GLU   A 1 264 ? 6.86300   -28.21100 7.56100   1.000 159.40116 ? 300 GLU   A CD  1 
ATOM   2134 O  OE1 . GLU   A 1 264 ? 6.71600   -29.26400 8.21700   1.000 163.24851 ? 300 GLU   A OE1 1 
ATOM   2135 O  OE2 . GLU   A 1 264 ? 7.37300   -27.17700 8.04100   1.000 165.93321 ? 300 GLU   A OE2 1 
ATOM   2136 N  N   . PRO   A 1 265 ? 6.22800   -30.77900 3.48700   1.000 113.62212 ? 301 PRO   A N   1 
ATOM   2137 C  CA  . PRO   A 1 265 ? 6.84700   -32.09100 3.27400   1.000 110.45189 ? 301 PRO   A CA  1 
ATOM   2138 C  C   . PRO   A 1 265 ? 7.93900   -32.35000 4.29100   1.000 109.39644 ? 301 PRO   A C   1 
ATOM   2139 O  O   . PRO   A 1 265 ? 8.68300   -31.43200 4.67000   1.000 109.41064 ? 301 PRO   A O   1 
ATOM   2140 C  CB  . PRO   A 1 265 ? 7.41600   -31.98400 1.84900   1.000 109.49125 ? 301 PRO   A CB  1 
ATOM   2141 C  CG  . PRO   A 1 265 ? 7.46900   -30.50800 1.53000   1.000 104.24842 ? 301 PRO   A CG  1 
ATOM   2142 C  CD  . PRO   A 1 265 ? 6.81700   -29.73500 2.63900   1.000 104.09951 ? 301 PRO   A CD  1 
ATOM   2143 N  N   . PRO   A 1 266 ? 8.06700   -33.59100 4.76700   1.000 104.16153 ? 302 PRO   A N   1 
ATOM   2144 C  CA  . PRO   A 1 266 ? 9.10400   -33.89500 5.76200   1.000 106.19289 ? 302 PRO   A CA  1 
ATOM   2145 C  C   . PRO   A 1 266 ? 10.50000  -33.85100 5.16200   1.000 102.76897 ? 302 PRO   A C   1 
ATOM   2146 O  O   . PRO   A 1 266 ? 11.05300  -34.89100 4.79100   1.000 100.84356 ? 302 PRO   A O   1 
ATOM   2147 C  CB  . PRO   A 1 266 ? 8.73500   -35.30800 6.22900   1.000 105.92774 ? 302 PRO   A CB  1 
ATOM   2148 C  CG  . PRO   A 1 266 ? 8.01300   -35.90600 5.06800   1.000 105.96537 ? 302 PRO   A CG  1 
ATOM   2149 C  CD  . PRO   A 1 266 ? 7.25800   -34.77400 4.42500   1.000 103.00133 ? 302 PRO   A CD  1 
ATOM   2150 N  N   . TYR   A 1 267 ? 11.07600  -32.64800 5.07100   1.000 98.22427  ? 303 TYR   A N   1 
ATOM   2151 C  CA  . TYR   A 1 267 ? 12.36000  -32.47300 4.39700   1.000 97.37080  ? 303 TYR   A CA  1 
ATOM   2152 C  C   . TYR   A 1 267 ? 13.43800  -33.36000 5.00600   1.000 100.03524 ? 303 TYR   A C   1 
ATOM   2153 O  O   . TYR   A 1 267 ? 14.16600  -34.05700 4.29000   1.000 100.33890 ? 303 TYR   A O   1 
ATOM   2154 C  CB  . TYR   A 1 267 ? 12.78500  -31.00500 4.45300   1.000 92.18704  ? 303 TYR   A CB  1 
ATOM   2155 C  CG  . TYR   A 1 267 ? 11.87000  -30.06900 3.69600   1.000 96.78985  ? 303 TYR   A CG  1 
ATOM   2156 C  CD1 . TYR   A 1 267 ? 11.96700  -29.93700 2.31700   1.000 93.36671  ? 303 TYR   A CD1 1 
ATOM   2157 C  CD2 . TYR   A 1 267 ? 10.91600  -29.31100 4.36200   1.000 95.29882  ? 303 TYR   A CD2 1 
ATOM   2158 C  CE1 . TYR   A 1 267 ? 11.13500  -29.08000 1.62100   1.000 95.33734  ? 303 TYR   A CE1 1 
ATOM   2159 C  CE2 . TYR   A 1 267 ? 10.08000  -28.45200 3.67500   1.000 93.07404  ? 303 TYR   A CE2 1 
ATOM   2160 C  CZ  . TYR   A 1 267 ? 10.19400  -28.34000 2.30500   1.000 92.03366  ? 303 TYR   A CZ  1 
ATOM   2161 O  OH  . TYR   A 1 267 ? 9.36400   -27.48500 1.61800   1.000 93.02496  ? 303 TYR   A OH  1 
ATOM   2162 N  N   . GLU   A 1 268 ? 13.55000  -33.35300 6.33400   1.000 98.04567  ? 304 GLU   A N   1 
ATOM   2163 C  CA  . GLU   A 1 268 ? 14.61800  -34.09800 6.98100   1.000 99.06107  ? 304 GLU   A CA  1 
ATOM   2164 C  C   . GLU   A 1 268 ? 14.36700  -35.60000 6.98700   1.000 100.06248 ? 304 GLU   A C   1 
ATOM   2165 O  O   . GLU   A 1 268 ? 15.30900  -36.36800 7.19900   1.000 98.95388  ? 304 GLU   A O   1 
ATOM   2166 C  CB  . GLU   A 1 268 ? 14.82300  -33.58100 8.40900   1.000 102.90420 ? 304 GLU   A CB  1 
ATOM   2167 C  CG  . GLU   A 1 268 ? 16.13800  -33.99400 9.06500   1.000 107.95596 ? 304 GLU   A CG  1 
ATOM   2168 C  CD  . GLU   A 1 268 ? 17.36300  -33.35800 8.41800   1.000 109.69074 ? 304 GLU   A CD  1 
ATOM   2169 O  OE1 . GLU   A 1 268 ? 17.23700  -32.72400 7.34800   1.000 103.50988 ? 304 GLU   A OE1 1 
ATOM   2170 O  OE2 . GLU   A 1 268 ? 18.46400  -33.49300 8.98800   1.000 123.53927 ? 304 GLU   A OE2 1 
ATOM   2171 N  N   . GLU   A 1 269 ? 13.12600  -36.03700 6.76400   1.000 102.17156 ? 305 GLU   A N   1 
ATOM   2172 C  CA  . GLU   A 1 269 ? 12.87700  -37.46500 6.61600   1.000 104.18274 ? 305 GLU   A CA  1 
ATOM   2173 C  C   . GLU   A 1 269 ? 13.40900  -37.97100 5.28100   1.000 101.29708 ? 305 GLU   A C   1 
ATOM   2174 O  O   . GLU   A 1 269 ? 13.99600  -39.05700 5.21400   1.000 104.84826 ? 305 GLU   A O   1 
ATOM   2175 C  CB  . GLU   A 1 269 ? 11.38300  -37.75200 6.76100   1.000 108.11953 ? 305 GLU   A CB  1 
ATOM   2176 C  CG  . GLU   A 1 269 ? 11.06300  -39.21400 7.02700   1.000 105.68682 ? 305 GLU   A CG  1 
ATOM   2177 C  CD  . GLU   A 1 269 ? 9.89700   -39.38400 7.97900   1.000 119.71479 ? 305 GLU   A CD  1 
ATOM   2178 O  OE1 . GLU   A 1 269 ? 9.40500   -38.36000 8.49800   1.000 119.10006 ? 305 GLU   A OE1 1 
ATOM   2179 O  OE2 . GLU   A 1 269 ? 9.47200   -40.53400 8.21300   1.000 131.73665 ? 305 GLU   A OE2 1 
ATOM   2180 N  N   . TYR   A 1 270 ? 13.22700  -37.19000 4.21300   1.000 99.09940  ? 306 TYR   A N   1 
ATOM   2181 C  CA  . TYR   A 1 270 ? 13.73400  -37.58600 2.90400   1.000 99.24853  ? 306 TYR   A CA  1 
ATOM   2182 C  C   . TYR   A 1 270 ? 15.25800  -37.58100 2.88000   1.000 100.86795 ? 306 TYR   A C   1 
ATOM   2183 O  O   . TYR   A 1 270 ? 15.88300  -38.49400 2.32900   1.000 100.73633 ? 306 TYR   A O   1 
ATOM   2184 C  CB  . TYR   A 1 270 ? 13.17700  -36.66000 1.82200   1.000 99.90642  ? 306 TYR   A CB  1 
ATOM   2185 C  CG  . TYR   A 1 270 ? 11.67500  -36.72200 1.67100   1.000 103.74900 ? 306 TYR   A CG  1 
ATOM   2186 C  CD1 . TYR   A 1 270 ? 11.04100  -37.91300 1.34200   1.000 105.11736 ? 306 TYR   A CD1 1 
ATOM   2187 C  CD2 . TYR   A 1 270 ? 10.89200  -35.58800 1.83800   1.000 105.98846 ? 306 TYR   A CD2 1 
ATOM   2188 C  CE1 . TYR   A 1 270 ? 9.66800   -37.97600 1.19700   1.000 109.25267 ? 306 TYR   A CE1 1 
ATOM   2189 C  CE2 . TYR   A 1 270 ? 9.51600   -35.64100 1.69500   1.000 104.91989 ? 306 TYR   A CE2 1 
ATOM   2190 C  CZ  . TYR   A 1 270 ? 8.91100   -36.83700 1.37400   1.000 109.08588 ? 306 TYR   A CZ  1 
ATOM   2191 O  OH  . TYR   A 1 270 ? 7.54500   -36.89500 1.22900   1.000 108.18468 ? 306 TYR   A OH  1 
ATOM   2192 N  N   . ARG   A 1 271 ? 15.87300  -36.55300 3.47200   1.000 102.07522 ? 307 ARG   A N   1 
ATOM   2193 C  CA  . ARG   A 1 271 ? 17.33100  -36.48900 3.49800   1.000 98.47296  ? 307 ARG   A CA  1 
ATOM   2194 C  C   . ARG   A 1 271 ? 17.92000  -37.64500 4.29700   1.000 100.95587 ? 307 ARG   A C   1 
ATOM   2195 O  O   . ARG   A 1 271 ? 18.91400  -38.25300 3.88200   1.000 100.16165 ? 307 ARG   A O   1 
ATOM   2196 C  CB  . ARG   A 1 271 ? 17.79100  -35.14600 4.06600   1.000 95.93752  ? 307 ARG   A CB  1 
ATOM   2197 C  CG  . ARG   A 1 271 ? 17.43200  -33.95900 3.18200   1.000 95.06834  ? 307 ARG   A CG  1 
ATOM   2198 C  CD  . ARG   A 1 271 ? 18.05900  -32.66400 3.67700   1.000 89.72292  ? 307 ARG   A CD  1 
ATOM   2199 N  NE  . ARG   A 1 271 ? 17.40400  -32.14300 4.86900   1.000 95.84002  ? 307 ARG   A NE  1 
ATOM   2200 C  CZ  . ARG   A 1 271 ? 16.49600  -31.17800 4.85300   1.000 92.44735  ? 307 ARG   A CZ  1 
ATOM   2201 N  NH1 . ARG   A 1 271 ? 16.11400  -30.60700 3.72200   1.000 85.26449  ? 307 ARG   A NH1 1 
ATOM   2202 N  NH2 . ARG   A 1 271 ? 15.96200  -30.77100 6.00100   1.000 90.45245  ? 307 ARG   A NH2 1 
ATOM   2203 N  N   . MET   A 1 272 ? 17.31700  -37.96600 5.44400   1.000 100.77497 ? 308 MET   A N   1 
ATOM   2204 C  CA  . MET   A 1 272 ? 17.75800  -39.12900 6.20400   1.000 102.57785 ? 308 MET   A CA  1 
ATOM   2205 C  C   . MET   A 1 272 ? 17.48900  -40.41800 5.43900   1.000 101.78345 ? 308 MET   A C   1 
ATOM   2206 O  O   . MET   A 1 272 ? 18.27900  -41.36700 5.50800   1.000 99.53009  ? 308 MET   A O   1 
ATOM   2207 C  CB  . MET   A 1 272 ? 17.07500  -39.15500 7.57100   1.000 108.97316 ? 308 MET   A CB  1 
ATOM   2208 C  CG  . MET   A 1 272 ? 17.97500  -38.67000 8.68500   1.000 120.61199 ? 308 MET   A CG  1 
ATOM   2209 S  SD  . MET   A 1 272 ? 19.41400  -39.74800 8.81500   1.000 146.63737 ? 308 MET   A SD  1 
ATOM   2210 C  CE  . MET   A 1 272 ? 20.62000  -38.63600 9.53400   1.000 136.67749 ? 308 MET   A CE  1 
ATOM   2211 N  N   . LEU   A 1 273 ? 16.37700  -40.46800 4.69900   1.000 101.03933 ? 309 LEU   A N   1 
ATOM   2212 C  CA  . LEU   A 1 273 ? 16.10300  -41.62700 3.85600   1.000 102.05993 ? 309 LEU   A CA  1 
ATOM   2213 C  C   . LEU   A 1 273 ? 17.19600  -41.81200 2.81300   1.000 100.81965 ? 309 LEU   A C   1 
ATOM   2214 O  O   . LEU   A 1 273 ? 17.58600  -42.94400 2.50100   1.000 102.18114 ? 309 LEU   A O   1 
ATOM   2215 C  CB  . LEU   A 1 273 ? 14.73900  -41.47600 3.18200   1.000 97.72889  ? 309 LEU   A CB  1 
ATOM   2216 C  CG  . LEU   A 1 273 ? 14.29100  -42.63500 2.28900   1.000 100.07356 ? 309 LEU   A CG  1 
ATOM   2217 C  CD1 . LEU   A 1 273 ? 13.33900  -43.55800 3.03700   1.000 108.14766 ? 309 LEU   A CD1 1 
ATOM   2218 C  CD2 . LEU   A 1 273 ? 13.65400  -42.10900 1.01500   1.000 102.23746 ? 309 LEU   A CD2 1 
ATOM   2219 N  N   . LEU   A 1 274 ? 17.70900  -40.70800 2.26800   1.000 94.39964  ? 310 LEU   A N   1 
ATOM   2220 C  CA  . LEU   A 1 274 ? 18.81100  -40.78300 1.31800   1.000 97.12920  ? 310 LEU   A CA  1 
ATOM   2221 C  C   . LEU   A 1 274 ? 20.14900  -40.98400 2.01500   1.000 94.09476  ? 310 LEU   A C   1 
ATOM   2222 O  O   . LEU   A 1 274 ? 21.09400  -41.49000 1.40000   1.000 94.22613  ? 310 LEU   A O   1 
ATOM   2223 C  CB  . LEU   A 1 274 ? 18.84400  -39.51700 0.46400   1.000 104.57360 ? 310 LEU   A CB  1 
ATOM   2224 C  CG  . LEU   A 1 274 ? 17.58400  -39.27100 -0.36600  1.000 99.21702  ? 310 LEU   A CG  1 
ATOM   2225 C  CD1 . LEU   A 1 274 ? 17.59200  -37.87100 -0.95200  1.000 99.23996  ? 310 LEU   A CD1 1 
ATOM   2226 C  CD2 . LEU   A 1 274 ? 17.45800  -40.31500 -1.46600  1.000 96.57456  ? 310 LEU   A CD2 1 
ATOM   2227 N  N   . LEU   A 1 275 ? 20.25400  -40.59000 3.28600   1.000 101.92727 ? 311 LEU   A N   1 
ATOM   2228 C  CA  . LEU   A 1 275 ? 21.47500  -40.86000 4.03700   1.000 100.91706 ? 311 LEU   A CA  1 
ATOM   2229 C  C   . LEU   A 1 275 ? 21.63500  -42.35200 4.29100   1.000 105.94174 ? 311 LEU   A C   1 
ATOM   2230 O  O   . LEU   A 1 275 ? 22.74000  -42.89300 4.17700   1.000 108.41901 ? 311 LEU   A O   1 
ATOM   2231 C  CB  . LEU   A 1 275 ? 21.46600  -40.08500 5.35600   1.000 105.57723 ? 311 LEU   A CB  1 
ATOM   2232 C  CG  . LEU   A 1 275 ? 22.80100  -39.82600 6.06600   1.000 108.26650 ? 311 LEU   A CG  1 
ATOM   2233 C  CD1 . LEU   A 1 275 ? 23.31000  -41.04900 6.82600   1.000 113.08275 ? 311 LEU   A CD1 1 
ATOM   2234 C  CD2 . LEU   A 1 275 ? 23.84600  -39.34200 5.07200   1.000 103.46201 ? 311 LEU   A CD2 1 
ATOM   2235 N  N   . SER   A 1 276 ? 20.53700  -43.03500 4.62900   1.000 102.24684 ? 312 SER   A N   1 
ATOM   2236 C  CA  . SER   A 1 276 ? 20.58700  -44.47000 4.88700   1.000 102.55225 ? 312 SER   A CA  1 
ATOM   2237 C  C   . SER   A 1 276 ? 21.07000  -45.26100 3.68000   1.000 108.35208 ? 312 SER   A C   1 
ATOM   2238 O  O   . SER   A 1 276 ? 21.48300  -46.41500 3.83500   1.000 115.95216 ? 312 SER   A O   1 
ATOM   2239 C  CB  . SER   A 1 276 ? 19.20800  -44.97400 5.31500   1.000 106.44224 ? 312 SER   A CB  1 
ATOM   2240 O  OG  . SER   A 1 276 ? 18.26600  -44.82100 4.26800   1.000 108.67145 ? 312 SER   A OG  1 
ATOM   2241 N  N   . VAL   A 1 277 ? 21.01700  -44.67400 2.48300   1.000 103.34561 ? 313 VAL   A N   1 
ATOM   2242 C  CA  . VAL   A 1 277 ? 21.56000  -45.34000 1.30300   1.000 107.96519 ? 313 VAL   A CA  1 
ATOM   2243 C  C   . VAL   A 1 277 ? 23.05000  -45.59500 1.47900   1.000 114.02098 ? 313 VAL   A C   1 
ATOM   2244 O  O   . VAL   A 1 277 ? 23.55600  -46.67500 1.14800   1.000 116.51135 ? 313 VAL   A O   1 
ATOM   2245 C  CB  . VAL   A 1 277 ? 21.27400  -44.50300 0.04300   1.000 104.91001 ? 313 VAL   A CB  1 
ATOM   2246 C  CG1 . VAL   A 1 277 ? 21.76800  -45.22600 -1.20400  1.000 100.50541 ? 313 VAL   A CG1 1 
ATOM   2247 C  CG2 . VAL   A 1 277 ? 19.79000  -44.18100 -0.05000  1.000 104.30205 ? 313 VAL   A CG2 1 
ATOM   2248 N  N   . LEU   A 1 278 ? 23.77600  -44.61000 2.01300   1.000 116.34883 ? 314 LEU   A N   1 
ATOM   2249 C  CA  . LEU   A 1 278 ? 25.20000  -44.78900 2.26900   1.000 119.18434 ? 314 LEU   A CA  1 
ATOM   2250 C  C   . LEU   A 1 278 ? 25.46400  -45.78900 3.38600   1.000 127.32174 ? 314 LEU   A C   1 
ATOM   2251 O  O   . LEU   A 1 278 ? 26.59800  -46.26100 3.52200   1.000 123.27379 ? 314 LEU   A O   1 
ATOM   2252 C  CB  . LEU   A 1 278 ? 25.84500  -43.44300 2.60200   1.000 115.72592 ? 314 LEU   A CB  1 
ATOM   2253 C  CG  . LEU   A 1 278 ? 25.90300  -42.44600 1.44300   1.000 107.13207 ? 314 LEU   A CG  1 
ATOM   2254 C  CD1 . LEU   A 1 278 ? 26.43600  -41.10200 1.90500   1.000 103.67385 ? 314 LEU   A CD1 1 
ATOM   2255 C  CD2 . LEU   A 1 278 ? 26.75300  -42.99900 0.30900   1.000 113.80829 ? 314 LEU   A CD2 1 
ATOM   2256 N  N   . ASP   A 1 279 ? 24.45000  -46.12300 4.18700   1.000 147.86507 ? 315 ASP   A N   1 
ATOM   2257 C  CA  . ASP   A 1 279 ? 24.61400  -47.15800 5.20200   1.000 148.79677 ? 315 ASP   A CA  1 
ATOM   2258 C  C   . ASP   A 1 279 ? 24.58700  -48.55000 4.58300   1.000 154.43534 ? 315 ASP   A C   1 
ATOM   2259 O  O   . ASP   A 1 279 ? 25.37900  -49.41800 4.96500   1.000 160.14960 ? 315 ASP   A O   1 
ATOM   2260 C  CB  . ASP   A 1 279 ? 23.52200  -47.03300 6.26600   1.000 153.24205 ? 315 ASP   A CB  1 
ATOM   2261 C  CG  . ASP   A 1 279 ? 24.03400  -47.31200 7.66600   1.000 172.26129 ? 315 ASP   A CG  1 
ATOM   2262 O  OD1 . ASP   A 1 279 ? 25.00000  -48.09000 7.80700   1.000 182.89797 ? 315 ASP   A OD1 1 
ATOM   2263 O  OD2 . ASP   A 1 279 ? 23.48200  -46.73400 8.62700   1.000 183.73991 ? 315 ASP   A OD2 1 
ATOM   2264 N  N   . ASP   A 1 280 ? 23.68600  -48.77700 3.62200   1.000 134.51241 ? 316 ASP   A N   1 
ATOM   2265 C  CA  . ASP   A 1 280 ? 23.55800  -50.08900 2.99900   1.000 131.91016 ? 316 ASP   A CA  1 
ATOM   2266 C  C   . ASP   A 1 280 ? 24.73000  -50.41900 2.08400   1.000 130.41820 ? 316 ASP   A C   1 
ATOM   2267 O  O   . ASP   A 1 280 ? 24.91800  -51.59100 1.73900   1.000 135.17926 ? 316 ASP   A O   1 
ATOM   2268 C  CB  . ASP   A 1 280 ? 22.25300  -50.17000 2.20400   1.000 130.63108 ? 316 ASP   A CB  1 
ATOM   2269 C  CG  . ASP   A 1 280 ? 21.02500  -49.98900 3.07400   1.000 130.31502 ? 316 ASP   A CG  1 
ATOM   2270 O  OD1 . ASP   A 1 280 ? 21.17900  -49.86100 4.30600   1.000 131.30494 ? 316 ASP   A OD1 1 
ATOM   2271 O  OD2 . ASP   A 1 280 ? 19.90400  -49.97500 2.52200   1.000 128.59406 ? 316 ASP   A OD2 1 
ATOM   2272 N  N   . LEU   A 1 281 ? 25.51500  -49.42200 1.68300   1.000 132.17686 ? 317 LEU   A N   1 
ATOM   2273 C  CA  . LEU   A 1 281 ? 26.62200  -49.62100 0.75900   1.000 127.78264 ? 317 LEU   A CA  1 
ATOM   2274 C  C   . LEU   A 1 281 ? 27.98500  -49.49700 1.42500   1.000 128.72249 ? 317 LEU   A C   1 
ATOM   2275 O  O   . LEU   A 1 281 ? 29.00400  -49.73700 0.76800   1.000 125.99621 ? 317 LEU   A O   1 
ATOM   2276 C  CB  . LEU   A 1 281 ? 26.51600  -48.62400 -0.39900  1.000 124.05526 ? 317 LEU   A CB  1 
ATOM   2277 C  CG  . LEU   A 1 281 ? 25.20000  -48.66800 -1.17900  1.000 118.28442 ? 317 LEU   A CG  1 
ATOM   2278 C  CD1 . LEU   A 1 281 ? 24.88900  -47.30800 -1.77600  1.000 110.01648 ? 317 LEU   A CD1 1 
ATOM   2279 C  CD2 . LEU   A 1 281 ? 25.25400  -49.73200 -2.26600  1.000 115.14019 ? 317 LEU   A CD2 1 
ATOM   2280 N  N   . GLY   A 1 282 ? 28.03300  -49.13100 2.70100   1.000 133.91572 ? 318 GLY   A N   1 
ATOM   2281 C  CA  . GLY   A 1 282 ? 29.29800  -49.01900 3.40800   1.000 140.23972 ? 318 GLY   A CA  1 
ATOM   2282 C  C   . GLY   A 1 282 ? 30.15800  -47.85200 2.97200   1.000 140.28809 ? 318 GLY   A C   1 
ATOM   2283 O  O   . GLY   A 1 282 ? 31.37600  -48.00900 2.82000   1.000 141.88735 ? 318 GLY   A O   1 
ATOM   2284 N  N   . GLN   A 1 283 ? 29.55600  -46.68300 2.77100   1.000 122.86655 ? 319 GLN   A N   1 
ATOM   2285 C  CA  . GLN   A 1 283 ? 30.27300  -45.49400 2.33800   1.000 124.94710 ? 319 GLN   A CA  1 
ATOM   2286 C  C   . GLN   A 1 283 ? 30.07100  -44.36900 3.34400   1.000 127.99162 ? 319 GLN   A C   1 
ATOM   2287 O  O   . GLN   A 1 283 ? 29.03700  -44.29100 4.01600   1.000 121.65604 ? 319 GLN   A O   1 
ATOM   2288 C  CB  . GLN   A 1 283 ? 29.81000  -45.04100 0.94900   1.000 121.62020 ? 319 GLN   A CB  1 
ATOM   2289 C  CG  . GLN   A 1 283 ? 29.86400  -46.13400 -0.10300  1.000 117.31798 ? 319 GLN   A CG  1 
ATOM   2290 C  CD  . GLN   A 1 283 ? 31.26300  -46.68000 -0.30600  1.000 119.49205 ? 319 GLN   A CD  1 
ATOM   2291 O  OE1 . GLN   A 1 283 ? 32.24600  -45.94300 -0.23500  1.000 121.19483 ? 319 GLN   A OE1 1 
ATOM   2292 N  NE2 . GLN   A 1 283 ? 31.36000  -47.98000 -0.55600  1.000 117.77787 ? 319 GLN   A NE2 1 
ATOM   2293 N  N   . ALA   A 1 284 ? 31.06900  -43.49500 3.43800   1.000 124.60479 ? 320 ALA   A N   1 
ATOM   2294 C  CA  . ALA   A 1 284 ? 31.05200  -42.37900 4.37400   1.000 117.95496 ? 320 ALA   A CA  1 
ATOM   2295 C  C   . ALA   A 1 284 ? 30.60900  -41.11100 3.65700   1.000 116.82416 ? 320 ALA   A C   1 
ATOM   2296 O  O   . ALA   A 1 284 ? 31.11000  -40.79800 2.57100   1.000 119.69006 ? 320 ALA   A O   1 
ATOM   2297 C  CB  . ALA   A 1 284 ? 32.43000  -42.17600 5.00400   1.000 122.15314 ? 320 ALA   A CB  1 
ATOM   2298 N  N   . CYS   A 1 285 ? 29.67300  -40.38400 4.26800   1.000 116.30361 ? 321 CYS   A N   1 
ATOM   2299 C  CA  . CYS   A 1 285 ? 29.19200  -39.11500 3.72000   1.000 116.97956 ? 321 CYS   A CA  1 
ATOM   2300 C  C   . CYS   A 1 285 ? 30.21000  -38.02000 4.04200   1.000 116.81622 ? 321 CYS   A C   1 
ATOM   2301 O  O   . CYS   A 1 285 ? 29.96100  -37.08100 4.80100   1.000 120.57292 ? 321 CYS   A O   1 
ATOM   2302 C  CB  . CYS   A 1 285 ? 27.81100  -38.78200 4.26900   1.000 113.55160 ? 321 CYS   A CB  1 
ATOM   2303 S  SG  . CYS   A 1 285 ? 26.95400  -37.45600 3.38400   1.000 112.39544 ? 321 CYS   A SG  1 
ATOM   2304 N  N   . ASP   A 1 286 ? 31.38900  -38.15900 3.43500   1.000 120.83400 ? 322 ASP   A N   1 
ATOM   2305 C  CA  . ASP   A 1 286 ? 32.49500  -37.24200 3.68200   1.000 130.86348 ? 322 ASP   A CA  1 
ATOM   2306 C  C   . ASP   A 1 286 ? 32.46700  -36.01400 2.77800   1.000 128.11200 ? 322 ASP   A C   1 
ATOM   2307 O  O   . ASP   A 1 286 ? 32.86500  -34.92800 3.21500   1.000 130.33174 ? 322 ASP   A O   1 
ATOM   2308 C  CB  . ASP   A 1 286 ? 33.83200  -37.97900 3.52500   1.000 126.01296 ? 322 ASP   A CB  1 
ATOM   2309 C  CG  . ASP   A 1 286 ? 33.94500  -38.71500 2.20100   1.000 119.81925 ? 322 ASP   A CG  1 
ATOM   2310 O  OD1 . ASP   A 1 286 ? 33.13700  -38.43500 1.29100   1.000 125.54895 ? 322 ASP   A OD1 1 
ATOM   2311 O  OD2 . ASP   A 1 286 ? 34.84000  -39.57500 2.07200   1.000 112.96071 ? 322 ASP   A OD2 1 
ATOM   2312 N  N   . GLY   A 1 287 ? 32.01100  -36.16100 1.53400   1.000 129.13690 ? 323 GLY   A N   1 
ATOM   2313 C  CA  . GLY   A 1 287 ? 31.94600  -35.05400 0.59700   1.000 122.98142 ? 323 GLY   A CA  1 
ATOM   2314 C  C   . GLY   A 1 287 ? 32.46200  -35.39300 -0.78900  1.000 118.80284 ? 323 GLY   A C   1 
ATOM   2315 O  O   . GLY   A 1 287 ? 32.16400  -34.68200 -1.75500  1.000 113.40458 ? 323 GLY   A O   1 
ATOM   2316 N  N   . ASP   A 1 288 ? 33.23000  -36.48000 -0.89600  1.000 109.09343 ? 324 ASP   A N   1 
ATOM   2317 C  CA  . ASP   A 1 288 ? 33.91000  -36.82500 -2.14200  1.000 109.28249 ? 324 ASP   A CA  1 
ATOM   2318 C  C   . ASP   A 1 288 ? 32.91100  -36.99600 -3.28200  1.000 100.55312 ? 324 ASP   A C   1 
ATOM   2319 O  O   . ASP   A 1 288 ? 32.02900  -37.85800 -3.22500  1.000 103.42530 ? 324 ASP   A O   1 
ATOM   2320 C  CB  . ASP   A 1 288 ? 34.72800  -38.10200 -1.94100  1.000 113.73543 ? 324 ASP   A CB  1 
ATOM   2321 C  CG  . ASP   A 1 288 ? 35.73900  -38.33400 -3.04800  1.000 103.66230 ? 324 ASP   A CG  1 
ATOM   2322 O  OD1 . ASP   A 1 288 ? 35.34800  -38.32000 -4.23300  1.000 110.47483 ? 324 ASP   A OD1 1 
ATOM   2323 O  OD2 . ASP   A 1 288 ? 36.92900  -38.53300 -2.72700  1.000 112.91615 ? 324 ASP   A OD2 1 
ATOM   2324 N  N   . MET   A 1 289 ? 33.05200  -36.16700 -4.31400  1.000 83.41949  ? 325 MET   A N   1 
ATOM   2325 C  CA  . MET   A 1 289 ? 32.17300  -36.16500 -5.47400  1.000 99.51930  ? 325 MET   A CA  1 
ATOM   2326 C  C   . MET   A 1 289 ? 32.89400  -36.74200 -6.68500  1.000 97.28187  ? 325 MET   A C   1 
ATOM   2327 O  O   . MET   A 1 289 ? 34.12400  -36.85000 -6.71200  1.000 94.06827  ? 325 MET   A O   1 
ATOM   2328 C  CB  . MET   A 1 289 ? 31.68400  -34.74700 -5.79500  1.000 95.31501  ? 325 MET   A CB  1 
ATOM   2329 C  CG  . MET   A 1 289 ? 31.03700  -34.01700 -4.62600  1.000 91.37229  ? 325 MET   A CG  1 
ATOM   2330 S  SD  . MET   A 1 289 ? 29.35600  -34.56000 -4.27300  1.000 96.57686  ? 325 MET   A SD  1 
ATOM   2331 C  CE  . MET   A 1 289 ? 28.97800  -33.56300 -2.83200  1.000 101.89888 ? 325 MET   A CE  1 
ATOM   2332 N  N   . ASP   A 1 290 ? 32.10100  -37.10700 -7.69800  1.000 92.44274  ? 326 ASP   A N   1 
ATOM   2333 C  CA  . ASP   A 1 290 ? 32.66400  -37.64600 -8.93300  1.000 89.87934  ? 326 ASP   A CA  1 
ATOM   2334 C  C   . ASP   A 1 290 ? 33.60600  -36.65100 -9.59700  1.000 96.23405  ? 326 ASP   A C   1 
ATOM   2335 O  O   . ASP   A 1 290 ? 34.69000  -37.02500 -10.06100 1.000 91.05286  ? 326 ASP   A O   1 
ATOM   2336 C  CB  . ASP   A 1 290 ? 31.54400  -38.03000 -9.90200  1.000 96.61331  ? 326 ASP   A CB  1 
ATOM   2337 C  CG  . ASP   A 1 290 ? 30.90300  -39.36200 -9.56400  1.000 103.00451 ? 326 ASP   A CG  1 
ATOM   2338 O  OD1 . ASP   A 1 290 ? 30.53400  -39.57200 -8.39000  1.000 91.82776  ? 326 ASP   A OD1 1 
ATOM   2339 O  OD2 . ASP   A 1 290 ? 30.75400  -40.20100 -10.47700 1.000 100.92757 ? 326 ASP   A OD2 1 
ATOM   2340 N  N   . TRP   A 1 291 ? 33.21400  -35.37800 -9.65400  1.000 99.61091  ? 327 TRP   A N   1 
ATOM   2341 C  CA  . TRP   A 1 291 ? 34.01300  -34.39600 -10.37600 1.000 85.67407  ? 327 TRP   A CA  1 
ATOM   2342 C  C   . TRP   A 1 291 ? 35.29700  -34.01100 -9.65300  1.000 102.99455 ? 327 TRP   A C   1 
ATOM   2343 O  O   . TRP   A 1 291 ? 36.02300  -33.14400 -10.14900 1.000 102.23644 ? 327 TRP   A O   1 
ATOM   2344 C  CB  . TRP   A 1 291 ? 33.18700  -33.14200 -10.66200 1.000 91.67765  ? 327 TRP   A CB  1 
ATOM   2345 C  CG  . TRP   A 1 291 ? 32.62200  -32.48300 -9.44800  1.000 94.14412  ? 327 TRP   A CG  1 
ATOM   2346 C  CD1 . TRP   A 1 291 ? 33.25800  -31.61000 -8.61400  1.000 95.78221  ? 327 TRP   A CD1 1 
ATOM   2347 C  CD2 . TRP   A 1 291 ? 31.29300  -32.63100 -8.93800  1.000 89.82750  ? 327 TRP   A CD2 1 
ATOM   2348 N  NE1 . TRP   A 1 291 ? 32.40700  -31.21000 -7.61200  1.000 94.08795  ? 327 TRP   A NE1 1 
ATOM   2349 C  CE2 . TRP   A 1 291 ? 31.19500  -31.82300 -7.78800  1.000 85.58642  ? 327 TRP   A CE2 1 
ATOM   2350 C  CE3 . TRP   A 1 291 ? 30.17800  -33.37100 -9.34000  1.000 81.02773  ? 327 TRP   A CE3 1 
ATOM   2351 C  CZ2 . TRP   A 1 291 ? 30.02400  -31.73400 -7.03800  1.000 77.89033  ? 327 TRP   A CZ2 1 
ATOM   2352 C  CZ3 . TRP   A 1 291 ? 29.02000  -33.28300 -8.59400  1.000 84.34974  ? 327 TRP   A CZ3 1 
ATOM   2353 C  CH2 . TRP   A 1 291 ? 28.95100  -32.47100 -7.45500  1.000 82.88871  ? 327 TRP   A CH2 1 
ATOM   2354 N  N   . MET   A 1 292 ? 35.61000  -34.62300 -8.51300  1.000 102.62023 ? 328 MET   A N   1 
ATOM   2355 C  CA  . MET   A 1 292 ? 36.87900  -34.34800 -7.85400  1.000 97.01262  ? 328 MET   A CA  1 
ATOM   2356 C  C   . MET   A 1 292 ? 37.94800  -35.31600 -8.33300  1.000 104.17954 ? 328 MET   A C   1 
ATOM   2357 O  O   . MET   A 1 292 ? 38.89500  -35.61500 -7.59900  1.000 110.52050 ? 328 MET   A O   1 
ATOM   2358 C  CB  . MET   A 1 292 ? 36.73500  -34.44300 -6.33700  1.000 103.49522 ? 328 MET   A CB  1 
ATOM   2359 C  CG  . MET   A 1 292 ? 35.61200  -33.62100 -5.75600  1.000 95.52050  ? 328 MET   A CG  1 
ATOM   2360 S  SD  . MET   A 1 292 ? 35.91900  -33.34500 -4.00300  1.000 116.38892 ? 328 MET   A SD  1 
ATOM   2361 C  CE  . MET   A 1 292 ? 34.29600  -32.86700 -3.41600  1.000 98.26126  ? 328 MET   A CE  1 
ATOM   2362 N  N   . HIS   A 1 293 ? 37.80200  -35.81500 -9.55200  1.000 105.22825 ? 329 HIS   A N   1 
ATOM   2363 C  CA  . HIS   A 1 293 ? 38.73800  -36.81900 -10.03800 1.000 108.93644 ? 329 HIS   A CA  1 
ATOM   2364 C  C   . HIS   A 1 293 ? 39.06100  -36.71000 -11.52300 1.000 116.14204 ? 329 HIS   A C   1 
ATOM   2365 O  O   . HIS   A 1 293 ? 39.84600  -37.52700 -12.01500 1.000 127.79801 ? 329 HIS   A O   1 
ATOM   2366 C  CB  . HIS   A 1 293 ? 38.20200  -38.23200 -9.72000  1.000 108.76897 ? 329 HIS   A CB  1 
ATOM   2367 C  CG  . HIS   A 1 293 ? 38.16300  -38.55200 -8.25600  1.000 98.56693  ? 329 HIS   A CG  1 
ATOM   2368 N  ND1 . HIS   A 1 293 ? 39.28900  -38.89300 -7.54100  1.000 106.33899 ? 329 HIS   A ND1 1 
ATOM   2369 C  CD2 . HIS   A 1 293 ? 37.13300  -38.58700 -7.37600  1.000 103.43024 ? 329 HIS   A CD2 1 
ATOM   2370 C  CE1 . HIS   A 1 293 ? 38.95700  -39.12400 -6.28300  1.000 100.24160 ? 329 HIS   A CE1 1 
ATOM   2371 N  NE2 . HIS   A 1 293 ? 37.65600  -38.94500 -6.15600  1.000 98.69784  ? 329 HIS   A NE2 1 
ATOM   2372 N  N   . LEU   A 1 294 ? 38.50700  -35.74800 -12.25600 1.000 121.73746 ? 330 LEU   A N   1 
ATOM   2373 C  CA  . LEU   A 1 294 ? 38.88100  -35.62900 -13.65800 1.000 136.84326 ? 330 LEU   A CA  1 
ATOM   2374 C  C   . LEU   A 1 294 ? 40.26100  -34.99300 -13.79000 1.000 136.00440 ? 330 LEU   A C   1 
ATOM   2375 O  O   . LEU   A 1 294 ? 40.79300  -34.39700 -12.85000 1.000 136.21317 ? 330 LEU   A O   1 
ATOM   2376 C  CB  . LEU   A 1 294 ? 37.87600  -34.78900 -14.45300 1.000 131.77865 ? 330 LEU   A CB  1 
ATOM   2377 C  CG  . LEU   A 1 294 ? 36.36400  -34.87800 -14.27000 1.000 125.25191 ? 330 LEU   A CG  1 
ATOM   2378 C  CD1 . LEU   A 1 294 ? 35.92200  -33.85500 -13.24800 1.000 123.52244 ? 330 LEU   A CD1 1 
ATOM   2379 C  CD2 . LEU   A 1 294 ? 35.66300  -34.63800 -15.59800 1.000 125.61552 ? 330 LEU   A CD2 1 
ATOM   2380 N  N   . ASN   A 1 295 ? 40.83500  -35.13000 -14.98800 1.000 137.99589 ? 331 ASN   A N   1 
ATOM   2381 C  CA  . ASN   A 1 295 ? 42.07400  -34.44900 -15.36600 1.000 147.15868 ? 331 ASN   A CA  1 
ATOM   2382 C  C   . ASN   A 1 295 ? 43.21500  -34.78100 -14.40500 1.000 147.90523 ? 331 ASN   A C   1 
ATOM   2383 O  O   . ASN   A 1 295 ? 43.95500  -33.90500 -13.95600 1.000 153.73544 ? 331 ASN   A O   1 
ATOM   2384 C  CB  . ASN   A 1 295 ? 41.85700  -32.93700 -15.45400 1.000 143.76229 ? 331 ASN   A CB  1 
ATOM   2385 C  CG  . ASN   A 1 295 ? 40.67000  -32.56700 -16.31900 1.000 157.46098 ? 331 ASN   A CG  1 
ATOM   2386 O  OD1 . ASN   A 1 295 ? 40.43500  -33.16800 -17.36800 1.000 157.31396 ? 331 ASN   A OD1 1 
ATOM   2387 N  ND2 . ASN   A 1 295 ? 39.91000  -31.57300 -15.87900 1.000 165.72504 ? 331 ASN   A ND2 1 
ATOM   2388 N  N   . GLY   A 1 296 ? 43.35700  -36.06700 -14.09100 1.000 151.47065 ? 332 GLY   A N   1 
ATOM   2389 C  CA  . GLY   A 1 296 ? 44.42600  -36.49900 -13.21300 1.000 151.65196 ? 332 GLY   A CA  1 
ATOM   2390 C  C   . GLY   A 1 296 ? 44.30200  -36.04400 -11.77800 1.000 156.11240 ? 332 GLY   A C   1 
ATOM   2391 O  O   . GLY   A 1 296 ? 45.27000  -36.14900 -11.02000 1.000 158.85054 ? 332 GLY   A O   1 
ATOM   2392 N  N   . GLY   A 1 297 ? 43.13500  -35.54500 -11.37600 1.000 148.40018 ? 333 GLY   A N   1 
ATOM   2393 C  CA  . GLY   A 1 297 ? 42.93000  -35.04400 -10.03400 1.000 147.35485 ? 333 GLY   A CA  1 
ATOM   2394 C  C   . GLY   A 1 297 ? 42.99600  -33.53900 -9.89400  1.000 146.25883 ? 333 GLY   A C   1 
ATOM   2395 O  O   . GLY   A 1 297 ? 42.82200  -33.03000 -8.77900  1.000 134.24438 ? 333 GLY   A O   1 
ATOM   2396 N  N   . ARG   A 1 298 ? 43.24600  -32.81100 -10.98600 1.000 148.04936 ? 334 ARG   A N   1 
ATOM   2397 C  CA  . ARG   A 1 298 ? 43.27000  -31.35400 -10.91800 1.000 157.16196 ? 334 ARG   A CA  1 
ATOM   2398 C  C   . ARG   A 1 298 ? 41.87700  -30.78000 -10.70000 1.000 161.17266 ? 334 ARG   A C   1 
ATOM   2399 O  O   . ARG   A 1 298 ? 41.73400  -29.72400 -10.07400 1.000 167.27986 ? 334 ARG   A O   1 
ATOM   2400 C  CB  . ARG   A 1 298 ? 43.88000  -30.77700 -12.19600 1.000 159.95142 ? 334 ARG   A CB  1 
ATOM   2401 C  CG  . ARG   A 1 298 ? 45.24400  -31.34300 -12.55300 1.000 161.77996 ? 334 ARG   A CG  1 
ATOM   2402 C  CD  . ARG   A 1 298 ? 45.70100  -30.85100 -13.91900 1.000 172.49210 ? 334 ARG   A CD  1 
ATOM   2403 N  NE  . ARG   A 1 298 ? 46.94900  -31.47700 -14.33800 1.000 182.87758 ? 334 ARG   A NE  1 
ATOM   2404 C  CZ  . ARG   A 1 298 ? 47.02500  -32.58700 -15.06100 1.000 184.85175 ? 334 ARG   A CZ  1 
ATOM   2405 N  NH1 . ARG   A 1 298 ? 45.93800  -33.21900 -15.47400 1.000 179.54784 ? 334 ARG   A NH1 1 
ATOM   2406 N  NH2 . ARG   A 1 298 ? 48.22100  -33.07600 -15.37500 1.000 180.36716 ? 334 ARG   A NH2 1 
ATOM   2407 N  N   . GLY   A 1 299 ? 40.84600  -31.45700 -11.20000 1.000 162.41926 ? 335 GLY   A N   1 
ATOM   2408 C  CA  . GLY   A 1 299 ? 39.49000  -30.95400 -11.12500 1.000 158.56157 ? 335 GLY   A CA  1 
ATOM   2409 C  C   . GLY   A 1 299 ? 38.80900  -30.98400 -12.47700 1.000 165.68219 ? 335 GLY   A C   1 
ATOM   2410 O  O   . GLY   A 1 299 ? 38.73300  -32.03800 -13.11500 1.000 159.49497 ? 335 GLY   A O   1 
ATOM   2411 N  N   . TRP   A 1 300 ? 38.31500  -29.83500 -12.93100 1.000 202.72838 ? 336 TRP   A N   1 
ATOM   2412 C  CA  . TRP   A 1 300 ? 37.69000  -29.71100 -14.24000 1.000 200.16221 ? 336 TRP   A CA  1 
ATOM   2413 C  C   . TRP   A 1 300 ? 38.40300  -28.63400 -15.04500 1.000 208.60490 ? 336 TRP   A C   1 
ATOM   2414 O  O   . TRP   A 1 300 ? 38.80600  -27.60200 -14.49900 1.000 205.57053 ? 336 TRP   A O   1 
ATOM   2415 C  CB  . TRP   A 1 300 ? 36.19800  -29.38200 -14.11600 1.000 192.95774 ? 336 TRP   A CB  1 
ATOM   2416 C  CG  . TRP   A 1 300 ? 35.90700  -28.07300 -13.44300 1.000 196.86254 ? 336 TRP   A CG  1 
ATOM   2417 C  CD1 . TRP   A 1 300 ? 35.64200  -27.87400 -12.12000 1.000 192.20726 ? 336 TRP   A CD1 1 
ATOM   2418 C  CD2 . TRP   A 1 300 ? 35.84900  -26.78000 -14.06200 1.000 206.27011 ? 336 TRP   A CD2 1 
ATOM   2419 N  NE1 . TRP   A 1 300 ? 35.42500  -26.53900 -11.87500 1.000 199.11901 ? 336 TRP   A NE1 1 
ATOM   2420 C  CE2 . TRP   A 1 300 ? 35.54700  -25.84700 -13.05100 1.000 205.10100 ? 336 TRP   A CE2 1 
ATOM   2421 C  CE3 . TRP   A 1 300 ? 36.02500  -26.32200 -15.37200 1.000 208.07129 ? 336 TRP   A CE3 1 
ATOM   2422 C  CZ2 . TRP   A 1 300 ? 35.41700  -24.48300 -13.30800 1.000 200.38584 ? 336 TRP   A CZ2 1 
ATOM   2423 C  CZ3 . TRP   A 1 300 ? 35.89500  -24.96800 -15.62500 1.000 203.94851 ? 336 TRP   A CZ3 1 
ATOM   2424 C  CH2 . TRP   A 1 300 ? 35.59300  -24.06500 -14.59900 1.000 199.53545 ? 336 TRP   A CH2 1 
ATOM   2425 N  N   . ASP   A 1 301 ? 38.56200  -28.88100 -16.34100 1.000 190.43526 ? 337 ASP   A N   1 
ATOM   2426 C  CA  . ASP   A 1 301 ? 39.21800  -27.95000 -17.24500 1.000 184.39082 ? 337 ASP   A CA  1 
ATOM   2427 C  C   . ASP   A 1 301 ? 38.18500  -27.27500 -18.13800 1.000 184.33851 ? 337 ASP   A C   1 
ATOM   2428 O  O   . ASP   A 1 301 ? 37.02400  -27.68700 -18.21500 1.000 183.41179 ? 337 ASP   A O   1 
ATOM   2429 C  CB  . ASP   A 1 301 ? 40.28000  -28.66600 -18.08900 1.000 179.52392 ? 337 ASP   A CB  1 
ATOM   2430 C  CG  . ASP   A 1 301 ? 41.59100  -27.90400 -18.14300 1.000 176.00361 ? 337 ASP   A CG  1 
ATOM   2431 O  OD1 . ASP   A 1 301 ? 41.56000  -26.65800 -18.06200 1.000 177.86012 ? 337 ASP   A OD1 1 
ATOM   2432 O  OD2 . ASP   A 1 301 ? 42.65200  -28.55100 -18.26100 1.000 169.83024 ? 337 ASP   A OD2 1 
ATOM   2433 N  N   . ALA   A 1 302 ? 38.62400  -26.21800 -18.82000 1.000 186.20565 ? 338 ALA   A N   1 
ATOM   2434 C  CA  . ALA   A 1 302 ? 37.74300  -25.40600 -19.65100 1.000 185.20031 ? 338 ALA   A CA  1 
ATOM   2435 C  C   . ALA   A 1 302 ? 37.84000  -25.73300 -21.13400 1.000 193.42970 ? 338 ALA   A C   1 
ATOM   2436 O  O   . ALA   A 1 302 ? 36.80900  -25.83500 -21.80600 1.000 186.52966 ? 338 ALA   A O   1 
ATOM   2437 C  CB  . ALA   A 1 302 ? 38.04200  -23.91800 -19.44000 1.000 179.98964 ? 338 ALA   A CB  1 
ATOM   2438 N  N   . THR   A 1 303 ? 39.05100  -25.90000 -21.66500 1.000 203.33992 ? 339 THR   A N   1 
ATOM   2439 C  CA  . THR   A 1 303 ? 39.23000  -26.13600 -23.09200 1.000 203.50955 ? 339 THR   A CA  1 
ATOM   2440 C  C   . THR   A 1 303 ? 39.11700  -27.60500 -23.48100 1.000 213.24579 ? 339 THR   A C   1 
ATOM   2441 O  O   . THR   A 1 303 ? 38.95600  -27.90300 -24.67000 1.000 217.98532 ? 339 THR   A O   1 
ATOM   2442 C  CB  . THR   A 1 303 ? 40.58800  -25.59700 -23.55600 1.000 203.04872 ? 339 THR   A CB  1 
ATOM   2443 O  OG1 . THR   A 1 303 ? 40.78700  -25.91800 -24.93800 1.000 205.79480 ? 339 THR   A OG1 1 
ATOM   2444 C  CG2 . THR   A 1 303 ? 41.71500  -26.20000 -22.73300 1.000 199.57119 ? 339 THR   A CG2 1 
ATOM   2445 N  N   . ILE   A 1 304 ? 39.19300  -28.52200 -22.52200 1.000 205.03354 ? 340 ILE   A N   1 
ATOM   2446 C  CA  . ILE   A 1 304 ? 39.09300  -29.94800 -22.80200 1.000 199.36919 ? 340 ILE   A CA  1 
ATOM   2447 C  C   . ILE   A 1 304 ? 37.71100  -30.49300 -22.46000 1.000 193.24785 ? 340 ILE   A C   1 
ATOM   2448 O  O   . ILE   A 1 304 ? 37.12800  -31.24400 -23.24300 1.000 192.42075 ? 340 ILE   A O   1 
ATOM   2449 C  CB  . ILE   A 1 304 ? 40.19600  -30.72300 -22.05000 1.000 198.03098 ? 340 ILE   A CB  1 
ATOM   2450 C  CG1 . ILE   A 1 304 ? 41.58000  -30.21700 -22.46100 1.000 198.97660 ? 340 ILE   A CG1 1 
ATOM   2451 C  CG2 . ILE   A 1 304 ? 40.07800  -32.21700 -22.31700 1.000 196.06947 ? 340 ILE   A CG2 1 
ATOM   2452 C  CD1 . ILE   A 1 304 ? 42.32400  -29.50800 -21.35400 1.000 193.85120 ? 340 ILE   A CD1 1 
ATOM   2453 N  N   . ASN   A 1 305 ? 37.17100  -30.12600 -21.29700 1.000 188.31663 ? 341 ASN   A N   1 
ATOM   2454 C  CA  . ASN   A 1 305 ? 35.84900  -30.60500 -20.90500 1.000 183.61743 ? 341 ASN   A CA  1 
ATOM   2455 C  C   . ASN   A 1 305 ? 34.74500  -29.86100 -21.65000 1.000 183.71306 ? 341 ASN   A C   1 
ATOM   2456 O  O   . ASN   A 1 305 ? 33.90800  -30.47800 -22.31800 1.000 182.32130 ? 341 ASN   A O   1 
ATOM   2457 C  CB  . ASN   A 1 305 ? 35.66500  -30.46700 -19.39100 1.000 176.67507 ? 341 ASN   A CB  1 
ATOM   2458 C  CG  . ASN   A 1 305 ? 36.16400  -31.68100 -18.63000 1.000 171.04213 ? 341 ASN   A CG  1 
ATOM   2459 O  OD1 . ASN   A 1 305 ? 37.00200  -31.56900 -17.73500 1.000 171.36064 ? 341 ASN   A OD1 1 
ATOM   2460 N  ND2 . ASN   A 1 305 ? 35.64600  -32.85300 -18.98300 1.000 158.31425 ? 341 ASN   A ND2 1 
ATOM   2461 N  N   . LYS   A 1 306 ? 34.72900  -28.53600 -21.54700 1.000 177.04123 ? 342 LYS   A N   1 
ATOM   2462 C  CA  . LYS   A 1 306 ? 33.69900  -27.73200 -22.19600 1.000 175.98509 ? 342 LYS   A CA  1 
ATOM   2463 C  C   . LYS   A 1 306 ? 34.19000  -27.17400 -23.52900 1.000 180.11754 ? 342 LYS   A C   1 
ATOM   2464 O  O   . LYS   A 1 306 ? 33.58900  -27.42100 -24.57500 1.000 174.22692 ? 342 LYS   A O   1 
ATOM   2465 C  CB  . LYS   A 1 306 ? 33.25400  -26.58900 -21.27900 1.000 169.48916 ? 342 LYS   A CB  1 
ATOM   2466 C  CG  . LYS   A 1 306 ? 32.12000  -25.74600 -21.83900 1.000 168.08721 ? 342 LYS   A CG  1 
ATOM   2467 C  CD  . LYS   A 1 306 ? 30.93500  -26.60900 -22.24100 1.000 163.23850 ? 342 LYS   A CD  1 
ATOM   2468 C  CE  . LYS   A 1 306 ? 29.82200  -25.77000 -22.84600 1.000 160.88774 ? 342 LYS   A CE  1 
ATOM   2469 N  NZ  . LYS   A 1 306 ? 28.78500  -26.61500 -23.49900 1.000 163.38228 ? 342 LYS   A NZ  1 
HETATM 2470 C  C10 . A1BIQ B 2 .   ? 25.02400  -17.71800 -13.14200 1.000 98.59138  ? 401 A1BIQ A C10 1 
HETATM 2471 C  C15 . A1BIQ B 2 .   ? 24.93700  -17.49500 -11.77300 1.000 90.22864  ? 401 A1BIQ A C15 1 
HETATM 2472 C  C17 . A1BIQ B 2 .   ? 24.19800  -20.19200 -14.90600 1.000 97.97411  ? 401 A1BIQ A C17 1 
HETATM 2473 C  C20 . A1BIQ B 2 .   ? 21.87800  -22.12400 -17.22800 1.000 109.20253 ? 401 A1BIQ A C20 1 
HETATM 2474 C  C22 . A1BIQ B 2 .   ? 21.74500  -19.86600 -16.12000 1.000 113.38219 ? 401 A1BIQ A C22 1 
HETATM 2475 C  C02 . A1BIQ B 2 .   ? 22.17900  -13.17500 -12.35700 1.000 106.90022 ? 401 A1BIQ A C02 1 
HETATM 2476 C  C03 . A1BIQ B 2 .   ? 23.40700  -13.52300 -12.89200 1.000 107.86591 ? 401 A1BIQ A C03 1 
HETATM 2477 C  C04 . A1BIQ B 2 .   ? 23.58200  -14.77500 -13.45400 1.000 104.21971 ? 401 A1BIQ A C04 1 
HETATM 2478 C  C05 . A1BIQ B 2 .   ? 21.12900  -14.07700 -12.38200 1.000 108.09245 ? 401 A1BIQ A C05 1 
HETATM 2479 C  C06 . A1BIQ B 2 .   ? 21.30600  -15.32700 -12.94800 1.000 103.99540 ? 401 A1BIQ A C06 1 
HETATM 2480 C  C07 . A1BIQ B 2 .   ? 22.53500  -15.68000 -13.47900 1.000 105.27235 ? 401 A1BIQ A C07 1 
HETATM 2481 C  C08 . A1BIQ B 2 .   ? 22.70600  -17.06200 -14.10800 1.000 104.98304 ? 401 A1BIQ A C08 1 
HETATM 2482 C  C09 . A1BIQ B 2 .   ? 23.75800  -17.93200 -13.97100 1.000 100.24749 ? 401 A1BIQ A C09 1 
HETATM 2483 C  C11 . A1BIQ B 2 .   ? 26.27600  -17.74100 -13.74600 1.000 98.77211  ? 401 A1BIQ A C11 1 
HETATM 2484 C  C12 . A1BIQ B 2 .   ? 27.39500  -17.54300 -12.95300 1.000 90.36121  ? 401 A1BIQ A C12 1 
HETATM 2485 C  C14 . A1BIQ B 2 .   ? 26.11000  -17.30600 -11.06100 1.000 89.15102  ? 401 A1BIQ A C14 1 
HETATM 2486 C  C18 . A1BIQ B 2 .   ? 23.68700  -21.19800 -15.72200 1.000 102.01161 ? 401 A1BIQ A C18 1 
HETATM 2487 C  C19 . A1BIQ B 2 .   ? 22.45300  -21.03000 -16.33000 1.000 112.78963 ? 401 A1BIQ A C19 1 
HETATM 2488 C  C23 . A1BIQ B 2 .   ? 22.28800  -18.85800 -15.28500 1.000 108.75559 ? 401 A1BIQ A C23 1 
HETATM 2489 F  F01 . A1BIQ B 2 .   ? 22.00700  -11.94200 -11.80100 1.000 107.11970 ? 401 A1BIQ A F01 1 
HETATM 2490 N  N13 . A1BIQ B 2 .   ? 27.28800  -17.33300 -11.65500 1.000 86.96746  ? 401 A1BIQ A N13 1 
HETATM 2491 N  N16 . A1BIQ B 2 .   ? 23.47600  -19.03700 -14.71000 1.000 106.01670 ? 401 A1BIQ A N16 1 
HETATM 2492 N  N21 . A1BIQ B 2 .   ? 21.45100  -22.93400 -17.89400 1.000 106.85846 ? 401 A1BIQ A N21 1 
HETATM 2493 N  N24 . A1BIQ B 2 .   ? 21.81400  -17.62300 -14.90500 1.000 108.68078 ? 401 A1BIQ A N24 1 
HETATM 2494 CL CL  . CL    C 3 .   ? 13.98700  -34.38900 -23.68200 1.000 105.97000 ? 402 CL    A CL  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   . SER A 1   ? 2.11050 1.44884 2.25542 0.15669  -0.14942 0.28679  37  SER A N   
2    C CA  . SER A 1   ? 2.05601 1.42012 2.23578 0.16907  -0.13205 0.24532  37  SER A CA  
3    C C   . SER A 1   ? 2.10366 1.49894 2.24963 0.17443  -0.11357 0.22270  37  SER A C   
4    O O   . SER A 1   ? 2.05630 1.46083 2.21361 0.18555  -0.12922 0.20854  37  SER A O   
5    C CB  . SER A 1   ? 2.07760 1.43116 2.32532 0.18674  -0.15569 0.22297  37  SER A CB  
6    O OG  . SER A 1   ? 2.05206 1.42591 2.32759 0.19371  -0.13797 0.18497  37  SER A OG  
7    N N   . SER A 2   ? 2.10650 1.51828 2.21540 0.16636  -0.08059 0.22164  38  SER A N   
8    C CA  . SER A 2   ? 2.04784 1.48101 2.11966 0.16955  -0.06228 0.20312  38  SER A CA  
9    C C   . SER A 2   ? 2.00121 1.46568 2.11362 0.18119  -0.05614 0.16595  38  SER A C   
10   O O   . SER A 2   ? 1.97865 1.45947 2.07727 0.18601  -0.05530 0.14890  38  SER A O   
11   C CB  . SER A 2   ? 2.09462 1.53054 2.11582 0.15995  -0.02678 0.21644  38  SER A CB  
12   O OG  . SER A 2   ? 2.08680 1.53937 2.14225 0.15765  -0.00763 0.21716  38  SER A OG  
13   N N   . VAL A 3   ? 2.04915 1.52157 2.20755 0.18277  -0.05286 0.15411  39  VAL A N   
14   C CA  . VAL A 3   ? 1.94261 1.44541 2.13290 0.19056  -0.04581 0.11939  39  VAL A CA  
15   C C   . VAL A 3   ? 1.92899 1.43605 2.15129 0.20564  -0.06772 0.09957  39  VAL A C   
16   O O   . VAL A 3   ? 2.03152 1.51392 2.27896 0.21215  -0.09123 0.10864  39  VAL A O   
17   C CB  . VAL A 3   ? 1.93592 1.44078 2.15945 0.18396  -0.04013 0.11283  39  VAL A CB  
18   C CG1 . VAL A 3   ? 2.10657 1.57460 2.35997 0.18395  -0.06395 0.12226  39  VAL A CG1 
19   C CG2 . VAL A 3   ? 1.79997 1.33581 2.04832 0.18872  -0.03327 0.07687  39  VAL A CG2 
20   N N   . VAL A 4   ? 1.79923 1.33971 2.02497 0.21158  -0.06002 0.07539  40  VAL A N   
21   C CA  . VAL A 4   ? 1.71040 1.26699 1.97272 0.22658  -0.07592 0.05714  40  VAL A CA  
22   C C   . VAL A 4   ? 1.61228 1.20107 1.90637 0.23220  -0.06185 0.02239  40  VAL A C   
23   O O   . VAL A 4   ? 1.56337 1.16665 1.84298 0.22164  -0.04242 0.01476  40  VAL A O   
24   C CB  . VAL A 4   ? 1.71790 1.28872 1.95368 0.22538  -0.08385 0.06430  40  VAL A CB  
25   C CG1 . VAL A 4   ? 1.82952 1.36692 2.01192 0.21333  -0.09201 0.09693  40  VAL A CG1 
26   C CG2 . VAL A 4   ? 1.68545 1.28983 1.90219 0.21969  -0.06309 0.04687  40  VAL A CG2 
27   N N   . GLY A 5   ? 1.65520 1.25711 1.99408 0.24894  -0.07142 0.00286  41  GLY A N   
28   C CA  . GLY A 5   ? 1.49590 1.12986 1.86002 0.25442  -0.05630 -0.03207 41  GLY A CA  
29   C C   . GLY A 5   ? 1.43088 1.04605 1.80068 0.24851  -0.04767 -0.04813 41  GLY A C   
30   O O   . GLY A 5   ? 1.39677 1.03882 1.76656 0.24348  -0.03202 -0.07350 41  GLY A O   
31   N N   . LEU A 6   ? 1.42842 0.99757 1.80029 0.24551  -0.05965 -0.03175 42  LEU A N   
32   C CA  . LEU A 6   ? 1.47147 1.01420 1.84786 0.23556  -0.05750 -0.04272 42  LEU A CA  
33   C C   . LEU A 6   ? 1.52885 1.08938 1.87322 0.21168  -0.04239 -0.03425 42  LEU A C   
34   O O   . LEU A 6   ? 1.56840 1.10370 1.90775 0.19628  -0.04603 -0.01939 42  LEU A O   
35   C CB  . LEU A 6   ? 1.52276 1.06785 1.92883 0.24826  -0.05249 -0.08541 42  LEU A CB  
36   C CG  . LEU A 6   ? 1.45038 0.98996 1.90115 0.27765  -0.06099 -0.09916 42  LEU A CG  
37   C CD1 . LEU A 6   ? 1.34872 0.89818 1.82018 0.28961  -0.04558 -0.14596 42  LEU A CD1 
38   C CD2 . LEU A 6   ? 1.51424 0.99791 1.98789 0.28592  -0.08449 -0.07738 42  LEU A CD2 
39   N N   . HIS A 7   ? 1.42662 1.03166 1.75399 0.20773  -0.02681 -0.04002 43  HIS A N   
40   C CA  . HIS A 7   ? 1.39672 1.02435 1.70445 0.18756  -0.01249 -0.03395 43  HIS A CA  
41   C C   . HIS A 7   ? 1.41517 1.06620 1.69650 0.18426  -0.00016 -0.01219 43  HIS A C   
42   O O   . HIS A 7   ? 1.42289 1.10369 1.69548 0.17277  0.01329  -0.01144 43  HIS A O   
43   C CB  . HIS A 7   ? 1.37498 1.03266 1.68884 0.18203  -0.00420 -0.06737 43  HIS A CB  
44   C CG  . HIS A 7   ? 1.44897 1.07760 1.77700 0.17974  -0.01205 -0.09226 43  HIS A CG  
45   N ND1 . HIS A 7   ? 1.49207 1.13806 1.82156 0.17873  -0.00472 -0.12980 43  HIS A ND1 
46   C CD2 . HIS A 7   ? 1.49637 1.07588 1.83367 0.17658  -0.02625 -0.08593 43  HIS A CD2 
47   C CE1 . HIS A 7   ? 1.44935 1.05344 1.78504 0.17616  -0.01320 -0.14898 43  HIS A CE1 
48   N NE2 . HIS A 7   ? 1.51525 1.07750 1.85819 0.17448  -0.02791 -0.12201 43  HIS A NE2 
49   N N   . TYR A 8   ? 1.48449 1.11991 1.75078 0.19294  -0.00515 0.00580  44  TYR A N   
50   C CA  . TYR A 8   ? 1.43836 1.08740 1.67258 0.19060  0.00713  0.02002  44  TYR A CA  
51   C C   . TYR A 8   ? 1.52352 1.13903 1.72841 0.19012  0.00545  0.04967  44  TYR A C   
52   O O   . TYR A 8   ? 1.58282 1.17712 1.78367 0.19724  -0.01158 0.05523  44  TYR A O   
53   C CB  . TYR A 8   ? 1.38548 1.05857 1.62036 0.19881  0.00326  0.00307  44  TYR A CB  
54   C CG  . TYR A 8   ? 1.36760 1.07934 1.62618 0.19742  0.00918  -0.02441 44  TYR A CG  
55   C CD1 . TYR A 8   ? 1.28069 1.02063 1.52971 0.18514  0.02434  -0.02477 44  TYR A CD1 
56   C CD2 . TYR A 8   ? 1.34999 1.07012 1.64084 0.20856  0.00084  -0.04877 44  TYR A CD2 
57   C CE1 . TYR A 8   ? 1.27933 1.05602 1.54385 0.18011  0.02892  -0.04745 44  TYR A CE1 
58   C CE2 . TYR A 8   ? 1.35455 1.11076 1.65991 0.20611  0.00995  -0.07522 44  TYR A CE2 
59   C CZ  . TYR A 8   ? 1.35255 1.13740 1.64143 0.18990  0.02292  -0.07381 44  TYR A CZ  
60   O OH  . TYR A 8   ? 1.38825 1.21045 1.68566 0.18388  0.03103  -0.09778 44  TYR A OH  
61   N N   . LYS A 9   ? 1.49692 1.11065 1.68194 0.18145  0.02390  0.07039  45  LYS A N   
62   C CA  . LYS A 9   ? 1.52581 1.11081 1.67731 0.17946  0.02937  0.09888  45  LYS A CA  
63   C C   . LYS A 9   ? 1.55479 1.13474 1.65951 0.18244  0.04017  0.10052  45  LYS A C   
64   O O   . LYS A 9   ? 1.45815 1.05832 1.55740 0.18265  0.05599  0.09127  45  LYS A O   
65   C CB  . LYS A 9   ? 1.52719 1.11659 1.68547 0.16990  0.04779  0.12159  45  LYS A CB  
66   C CG  . LYS A 9   ? 1.57903 1.14776 1.69885 0.16819  0.06427  0.15139  45  LYS A CG  
67   C CD  . LYS A 9   ? 1.52308 1.10580 1.66357 0.15914  0.08285  0.17704  45  LYS A CD  
68   C CE  . LYS A 9   ? 1.37369 0.99402 1.53796 0.15841  0.10110  0.17144  45  LYS A CE  
69   N NZ  . LYS A 9   ? 1.34336 0.98541 1.54243 0.14708  0.11246  0.19879  45  LYS A NZ  
70   N N   . ILE A 10  ? 1.61830 1.16786 1.68692 0.18261  0.02960  0.11323  46  ILE A N   
71   C CA  . ILE A 10  ? 1.64228 1.17686 1.65534 0.18160  0.03657  0.11355  46  ILE A CA  
72   C C   . ILE A 10  ? 1.68268 1.21036 1.66265 0.18022  0.07195  0.12580  46  ILE A C   
73   O O   . ILE A 10  ? 1.72725 1.24783 1.70601 0.17774  0.08594  0.14740  46  ILE A O   
74   C CB  . ILE A 10  ? 1.71804 1.22075 1.69628 0.17779  0.01319  0.12712  46  ILE A CB  
75   C CG1 . ILE A 10  ? 1.72196 1.23736 1.72864 0.18188  -0.01838 0.11264  46  ILE A CG1 
76   C CG2 . ILE A 10  ? 1.69163 1.16405 1.59237 0.17093  0.02803  0.13588  46  ILE A CG2 
77   C CD1 . ILE A 10  ? 1.74830 1.23851 1.73754 0.17783  -0.04833 0.13107  46  ILE A CD1 
78   N N   . GLY A 11  ? 1.75216 1.28269 1.70948 0.18239  0.08742  0.11344  47  GLY A N   
79   C CA  . GLY A 11  ? 1.77938 1.29989 1.70755 0.18563  0.12383  0.12264  47  GLY A CA  
80   C C   . GLY A 11  ? 1.88125 1.35908 1.73252 0.18402  0.13182  0.11911  47  GLY A C   
81   O O   . GLY A 11  ? 1.84911 1.29662 1.65452 0.17758  0.12165  0.12888  47  GLY A O   
82   N N   . LYS A 12  ? 2.07866 1.55056 1.91243 0.18769  0.14779  0.10556  48  LYS A N   
83   C CA  . LYS A 12  ? 2.14781 1.57048 1.90181 0.18482  0.15763  0.09815  48  LYS A CA  
84   C C   . LYS A 12  ? 2.13772 1.54832 1.86762 0.17257  0.11937  0.08388  48  LYS A C   
85   O O   . LYS A 12  ? 2.11135 1.55767 1.89292 0.17103  0.09551  0.07492  48  LYS A O   
86   C CB  . LYS A 12  ? 2.20471 1.61891 1.95249 0.19507  0.19251  0.09087  48  LYS A CB  
87   C CG  . LYS A 12  ? 2.30824 1.66192 1.96842 0.19651  0.21864  0.08520  48  LYS A CG  
88   C CD  . LYS A 12  ? 2.32296 1.66971 1.99246 0.21285  0.25976  0.08211  48  LYS A CD  
89   C CE  . LYS A 12  ? 2.49555 1.78867 2.08931 0.22123  0.30127  0.08186  48  LYS A CE  
90   N NZ  . LYS A 12  ? 2.60413 1.83289 2.09753 0.20607  0.28632  0.06295  48  LYS A NZ  
91   N N   . LYS A 13  ? 2.07514 1.43717 1.72526 0.16223  0.11352  0.08339  49  LYS A N   
92   C CA  . LYS A 13  ? 2.02717 1.37465 1.64779 0.14684  0.07635  0.07380  49  LYS A CA  
93   C C   . LYS A 13  ? 2.12718 1.44943 1.71440 0.14425  0.08810  0.05514  49  LYS A C   
94   O O   . LYS A 13  ? 2.17827 1.45339 1.70296 0.14708  0.11962  0.04978  49  LYS A O   
95   C CB  . LYS A 13  ? 1.97373 1.27966 1.52051 0.13155  0.05846  0.08542  49  LYS A CB  
96   C CG  . LYS A 13  ? 2.06349 1.31738 1.52168 0.11207  0.04378  0.07405  49  LYS A CG  
97   C CD  . LYS A 13  ? 2.11081 1.38986 1.60183 0.09873  -0.00440 0.07142  49  LYS A CD  
98   C CE  . LYS A 13  ? 2.27729 1.50801 1.68907 0.07638  -0.02077 0.05971  49  LYS A CE  
99   N NZ  . LYS A 13  ? 2.34226 1.56133 1.75455 0.08467  0.00853  0.03919  49  LYS A NZ  
100  N N   . ILE A 14  ? 2.10198 1.45423 1.73129 0.13916  0.06417  0.04556  50  ILE A N   
101  C CA  . ILE A 14  ? 2.14650 1.47607 1.75014 0.13251  0.06679  0.03048  50  ILE A CA  
102  C C   . ILE A 14  ? 2.28796 1.61557 1.87568 0.11080  0.02313  0.02667  50  ILE A C   
103  O O   . ILE A 14  ? 2.30096 1.60759 1.86571 0.10013  0.01827  0.01580  50  ILE A O   
104  C CB  . ILE A 14  ? 2.01989 1.39276 1.69467 0.14480  0.08419  0.02673  50  ILE A CB  
105  C CG1 . ILE A 14  ? 1.89869 1.33570 1.64657 0.13997  0.05374  0.02634  50  ILE A CG1 
106  C CG2 . ILE A 14  ? 1.94838 1.33783 1.65628 0.16413  0.12051  0.03704  50  ILE A CG2 
107  C CD1 . ILE A 14  ? 1.65198 1.13031 1.45800 0.14540  0.06633  0.02297  50  ILE A CD1 
108  N N   . GLY A 15  ? 2.63403 1.98235 2.23618 0.10327  -0.01005 0.03816  51  GLY A N   
109  C CA  . GLY A 15  ? 2.62518 1.98756 2.23244 0.08399  -0.05499 0.04158  51  GLY A CA  
110  C C   . GLY A 15  ? 2.83480 2.15019 2.37330 0.06049  -0.06984 0.03302  51  GLY A C   
111  O O   . GLY A 15  ? 2.98893 2.23577 2.43447 0.05011  -0.06101 0.02831  51  GLY A O   
112  N N   . GLU A 16  ? 2.55907 1.91024 2.14142 0.05089  -0.09113 0.03035  52  GLU A N   
113  C CA  . GLU A 16  ? 2.61247 1.92584 2.14058 0.02308  -0.11570 0.02579  52  GLU A CA  
114  C C   . GLU A 16  ? 2.59019 1.95930 2.17233 0.00615  -0.16243 0.03987  52  GLU A C   
115  O O   . GLU A 16  ? 2.64004 2.01521 2.21682 -0.00354 -0.19351 0.05570  52  GLU A O   
116  C CB  . GLU A 16  ? 2.50594 1.80182 2.03191 0.02538  -0.09128 0.01067  52  GLU A CB  
117  C CG  . GLU A 16  ? 2.61175 1.84654 2.08261 0.04168  -0.04488 -0.00224 52  GLU A CG  
118  C CD  . GLU A 16  ? 2.74581 1.88587 2.09958 0.02294  -0.04578 -0.01387 52  GLU A CD  
119  O OE1 . GLU A 16  ? 2.78348 1.89666 2.07945 0.01045  -0.06231 -0.00814 52  GLU A OE1 
120  O OE2 . GLU A 16  ? 2.81043 1.89976 2.12744 0.01977  -0.03042 -0.02876 52  GLU A OE2 
121  N N   . GLY A 17  ? 2.41888 1.83141 2.05573 0.00198  -0.16760 0.03728  53  GLY A N   
122  C CA  . GLY A 17  ? 2.41865 1.89515 2.11819 -0.01191 -0.20664 0.05224  53  GLY A CA  
123  C C   . GLY A 17  ? 2.66387 2.10401 2.30426 -0.04565 -0.25149 0.06515  53  GLY A C   
124  O O   . GLY A 17  ? 2.74230 2.10374 2.28731 -0.06666 -0.25428 0.05641  53  GLY A O   
125  N N   . SER A 18  ? 2.65682 2.15345 2.35422 -0.05150 -0.28757 0.08656  54  SER A N   
126  C CA  . SER A 18  ? 2.71470 2.18532 2.36405 -0.08410 -0.33609 0.10610  54  SER A CA  
127  C C   . SER A 18  ? 2.80846 2.25912 2.43317 -0.07500 -0.34175 0.11786  54  SER A C   
128  O O   . SER A 18  ? 2.79110 2.28540 2.46659 -0.07668 -0.37526 0.14304  54  SER A O   
129  C CB  . SER A 18  ? 2.61772 2.16727 2.35158 -0.09889 -0.37612 0.12911  54  SER A CB  
130  O OG  . SER A 18  ? 2.57130 2.14152 2.32747 -0.10968 -0.37042 0.12109  54  SER A OG  
131  N N   . PHE A 19  ? 3.00584 2.39109 2.55529 -0.06456 -0.30696 0.10139  55  PHE A N   
132  C CA  . PHE A 19  ? 3.03294 2.39876 2.55978 -0.05097 -0.29859 0.10992  55  PHE A CA  
133  C C   . PHE A 19  ? 2.98985 2.42443 2.62465 -0.01567 -0.28381 0.11579  55  PHE A C   
134  O O   . PHE A 19  ? 2.97156 2.40067 2.60738 -0.00523 -0.28509 0.12890  55  PHE A O   
135  C CB  . PHE A 19  ? 3.01654 2.35637 2.48879 -0.08144 -0.34732 0.13548  55  PHE A CB  
136  C CG  . PHE A 19  ? 3.08328 2.33006 2.41878 -0.10038 -0.33751 0.12721  55  PHE A CG  
137  C CD1 . PHE A 19  ? 3.11027 2.28899 2.34924 -0.12648 -0.33588 0.10760  55  PHE A CD1 
138  C CD2 . PHE A 19  ? 3.09636 2.32137 2.39764 -0.09255 -0.32847 0.13862  55  PHE A CD2 
139  C CE1 . PHE A 19  ? 3.14341 2.23284 2.25061 -0.14240 -0.32191 0.09589  55  PHE A CE1 
140  C CE2 . PHE A 19  ? 3.11919 2.26170 2.29052 -0.11026 -0.31513 0.13067  55  PHE A CE2 
141  C CZ  . PHE A 19  ? 3.12152 2.19553 2.19384 -0.13418 -0.31005 0.10744  55  PHE A CZ  
142  N N   . GLY A 20  ? 2.70373 2.19968 2.42548 0.00117  -0.27008 0.10628  56  GLY A N   
143  C CA  . GLY A 20  ? 2.48057 2.03046 2.29177 0.03453  -0.24882 0.10370  56  GLY A CA  
144  C C   . GLY A 20  ? 2.35127 1.86398 2.12938 0.05331  -0.20635 0.09036  56  GLY A C   
145  O O   . GLY A 20  ? 2.41088 1.88644 2.13788 0.05110  -0.17786 0.07417  56  GLY A O   
146  N N   . VAL A 21  ? 2.20448 1.72672 2.01515 0.07166  -0.20241 0.09926  57  VAL A N   
147  C CA  . VAL A 21  ? 2.17872 1.66616 1.95679 0.08524  -0.16693 0.09364  57  VAL A CA  
148  C C   . VAL A 21  ? 2.05531 1.57804 1.89072 0.10648  -0.13176 0.07516  57  VAL A C   
149  O O   . VAL A 21  ? 1.94033 1.51341 1.85623 0.12244  -0.13391 0.07297  57  VAL A O   
150  C CB  . VAL A 21  ? 2.16277 1.64428 1.95289 0.09230  -0.18046 0.11412  57  VAL A CB  
151  C CG1 . VAL A 21  ? 2.12392 1.55647 1.85031 0.09456  -0.15021 0.11562  57  VAL A CG1 
152  C CG2 . VAL A 21  ? 2.25026 1.72335 2.01883 0.07136  -0.22805 0.13802  57  VAL A CG2 
153  N N   . ILE A 22  ? 2.08542 1.58035 1.87873 0.10638  -0.09951 0.06216  58  ILE A N   
154  C CA  . ILE A 22  ? 1.92578 1.45131 1.76560 0.12195  -0.06811 0.04867  58  ILE A CA  
155  C C   . ILE A 22  ? 1.81561 1.31086 1.62877 0.13297  -0.03455 0.05095  58  ILE A C   
156  O O   . ILE A 22  ? 1.92081 1.36304 1.66032 0.12654  -0.02305 0.05461  58  ILE A O   
157  C CB  . ILE A 22  ? 1.94519 1.47318 1.77473 0.11261  -0.06053 0.03665  58  ILE A CB  
158  C CG1 . ILE A 22  ? 2.00960 1.54346 1.83022 0.09198  -0.09707 0.04036  58  ILE A CG1 
159  C CG2 . ILE A 22  ? 1.79415 1.37542 1.69191 0.12467  -0.04208 0.02744  58  ILE A CG2 
160  C CD1 . ILE A 22  ? 1.90827 1.51294 1.81290 0.09601  -0.11931 0.04393  58  ILE A CD1 
161  N N   . PHE A 23  ? 1.68914 1.21846 1.56059 0.14820  -0.01800 0.04895  59  PHE A N   
162  C CA  . PHE A 23  ? 1.75351 1.26496 1.61448 0.15739  0.01061  0.05629  59  PHE A CA  
163  C C   . PHE A 23  ? 1.69575 1.24122 1.60472 0.16646  0.03530  0.04921  59  PHE A C   
164  O O   . PHE A 23  ? 1.59230 1.18127 1.55268 0.16748  0.02698  0.03882  59  PHE A O   
165  C CB  . PHE A 23  ? 1.74215 1.25392 1.62379 0.16208  -0.00254 0.07013  59  PHE A CB  
166  C CG  . PHE A 23  ? 1.77996 1.24490 1.59509 0.15281  -0.01115 0.08650  59  PHE A CG  
167  C CD1 . PHE A 23  ? 1.82065 1.26864 1.59965 0.13903  -0.04189 0.08992  59  PHE A CD1 
168  C CD2 . PHE A 23  ? 1.86360 1.30446 1.65185 0.15514  0.01034  0.10115  59  PHE A CD2 
169  C CE1 . PHE A 23  ? 1.85179 1.25608 1.56200 0.12640  -0.05215 0.10630  59  PHE A CE1 
170  C CE2 . PHE A 23  ? 1.85798 1.25741 1.57887 0.14414  0.00363  0.11734  59  PHE A CE2 
171  C CZ  . PHE A 23  ? 1.84873 1.22811 1.52713 0.12909  -0.02829 0.11925  59  PHE A CZ  
172  N N   . GLU A 24  ? 1.69311 1.22084 1.58470 0.17204  0.06618  0.05694  60  GLU A N   
173  C CA  . GLU A 24  ? 1.61131 1.17313 1.55302 0.17884  0.08631  0.05808  60  GLU A CA  
174  C C   . GLU A 24  ? 1.56600 1.14801 1.55085 0.18204  0.07909  0.06514  60  GLU A C   
175  O O   . GLU A 24  ? 1.58672 1.14508 1.55330 0.18208  0.07256  0.07669  60  GLU A O   
176  C CB  . GLU A 24  ? 1.68104 1.22070 1.59756 0.18489  0.12231  0.06782  60  GLU A CB  
177  C CG  . GLU A 24  ? 1.66981 1.24523 1.64097 0.19036  0.14111  0.07899  60  GLU A CG  
178  C CD  . GLU A 24  ? 1.75214 1.31571 1.71404 0.19902  0.17682  0.08953  60  GLU A CD  
179  O OE1 . GLU A 24  ? 1.76869 1.28904 1.67567 0.20239  0.19022  0.08411  60  GLU A OE1 
180  O OE2 . GLU A 24  ? 1.72719 1.32353 1.73767 0.20220  0.19105  0.10356  60  GLU A OE2 
181  N N   . GLY A 25  ? 1.54385 1.16681 1.58280 0.18240  0.07835  0.05832  61  GLY A N   
182  C CA  . GLY A 25  ? 1.48501 1.12169 1.56324 0.18322  0.07156  0.06167  61  GLY A CA  
183  C C   . GLY A 25  ? 1.30495 0.97413 1.42065 0.17965  0.08509  0.06343  61  GLY A C   
184  O O   . GLY A 25  ? 1.31002 0.99570 1.42725 0.17784  0.09861  0.06354  61  GLY A O   
185  N N   . THR A 26  ? 1.31781 0.99417 1.46435 0.17658  0.07871  0.06676  62  THR A N   
186  C CA  . THR A 26  ? 1.29151 0.99879 1.47282 0.16798  0.08500  0.06960  62  THR A CA  
187  C C   . THR A 26  ? 1.21323 0.92407 1.42264 0.16305  0.06617  0.05634  62  THR A C   
188  O O   . THR A 26  ? 1.23553 0.91823 1.44338 0.16711  0.05421  0.05837  62  THR A O   
189  C CB  . THR A 26  ? 1.25385 0.95903 1.43813 0.16579  0.10599  0.09909  62  THR A CB  
190  O OG1 . THR A 26  ? 1.20817 0.94370 1.43141 0.15311  0.10382  0.10580  62  THR A OG1 
191  C CG2 . THR A 26  ? 1.36805 1.03980 1.53496 0.16868  0.10642  0.11589  62  THR A CG2 
192  N N   . ASN A 27  ? 1.18779 0.92989 1.42005 0.15343  0.06324  0.04276  63  ASN A N   
193  C CA  . ASN A 27  ? 1.25567 0.99643 1.50817 0.14772  0.04794  0.02405  63  ASN A CA  
194  C C   . ASN A 27  ? 1.28736 1.01991 1.55400 0.13374  0.04667  0.04435  63  ASN A C   
195  O O   . ASN A 27  ? 1.25155 1.01089 1.52909 0.11978  0.05367  0.05872  63  ASN A O   
196  C CB  . ASN A 27  ? 1.14384 0.92072 1.40458 0.14068  0.04648  -0.00139 63  ASN A CB  
197  C CG  . ASN A 27  ? 1.20988 0.97967 1.48323 0.13686  0.03444  -0.02831 63  ASN A CG  
198  O OD1 . ASN A 27  ? 1.22923 0.98694 1.50938 0.12302  0.02838  -0.02360 63  ASN A OD1 
199  N ND2 . ASN A 27  ? 1.42085 1.19811 1.69816 0.14853  0.03163  -0.05691 63  ASN A ND2 
200  N N   . ILE A 28  ? 1.22584 0.92297 1.49623 0.13571  0.03525  0.04879  64  ILE A N   
201  C CA  . ILE A 28  ? 1.26861 0.95565 1.55347 0.12013  0.03176  0.07285  64  ILE A CA  
202  C C   . ILE A 28  ? 1.22279 0.92114 1.52400 0.09966  0.01981  0.05897  64  ILE A C   
203  O O   . ILE A 28  ? 1.22083 0.91894 1.53674 0.08075  0.01469  0.08156  64  ILE A O   
204  C CB  . ILE A 28  ? 1.26027 0.90298 1.54313 0.12620  0.01994  0.08284  64  ILE A CB  
205  C CG1 . ILE A 28  ? 1.37124 1.00200 1.62779 0.14325  0.02856  0.09314  64  ILE A CG1 
206  C CG2 . ILE A 28  ? 1.41134 1.04557 1.70818 0.10916  0.01852  0.11664  64  ILE A CG2 
207  C CD1 . ILE A 28  ? 1.42866 1.04096 1.68130 0.15884  0.01315  0.06892  64  ILE A CD1 
208  N N   . ILE A 29  ? 1.23357 0.94307 1.53047 0.10064  0.01521  0.02321  65  ILE A N   
209  C CA  . ILE A 29  ? 1.26303 0.98304 1.56350 0.07757  0.00536  0.00815  65  ILE A CA  
210  C C   . ILE A 29  ? 1.26950 1.03809 1.57368 0.06034  0.01345  0.02771  65  ILE A C   
211  O O   . ILE A 29  ? 1.22115 1.00067 1.53318 0.03405  0.00325  0.03868  65  ILE A O   
212  C CB  . ILE A 29  ? 1.36848 1.08189 1.65947 0.08500  0.00112  -0.03893 65  ILE A CB  
213  C CG1 . ILE A 29  ? 1.42524 1.09004 1.72318 0.10501  -0.00771 -0.05425 65  ILE A CG1 
214  C CG2 . ILE A 29  ? 1.41729 1.13574 1.69903 0.05831  -0.00810 -0.05882 65  ILE A CG2 
215  C CD1 . ILE A 29  ? 1.41042 1.02929 1.71602 0.09128  -0.02462 -0.04585 65  ILE A CD1 
216  N N   . ASN A 30  ? 1.26944 1.06607 1.56970 0.07299  0.02926  0.03480  66  ASN A N   
217  C CA  . ASN A 30  ? 1.23233 1.07335 1.54154 0.05895  0.03608  0.05526  66  ASN A CA  
218  C C   . ASN A 30  ? 1.15481 1.00694 1.47028 0.07399  0.05585  0.08500  66  ASN A C   
219  O O   . ASN A 30  ? 1.17753 1.06452 1.50649 0.06601  0.06245  0.10430  66  ASN A O   
220  C CB  . ASN A 30  ? 1.25972 1.13028 1.55552 0.05167  0.03389  0.02703  66  ASN A CB  
221  C CG  . ASN A 30  ? 1.20060 1.06790 1.48277 0.07487  0.04224  0.00362  66  ASN A CG  
222  O OD1 . ASN A 30  ? 1.18841 1.02568 1.46762 0.09518  0.04516  0.00315  66  ASN A OD1 
223  N ND2 . ASN A 30  ? 1.24326 1.14402 1.51718 0.06921  0.04427  -0.01321 66  ASN A ND2 
224  N N   . GLY A 31  ? 1.19053 1.01197 1.49489 0.09466  0.06532  0.08967  67  GLY A N   
225  C CA  . GLY A 31  ? 1.10790 0.93078 1.41000 0.10845  0.08703  0.11498  67  GLY A CA  
226  C C   . GLY A 31  ? 1.19070 1.02297 1.47626 0.11947  0.09635  0.10346  67  GLY A C   
227  O O   . GLY A 31  ? 1.15911 0.98553 1.43847 0.13129  0.11563  0.12098  67  GLY A O   
228  N N   . VAL A 32  ? 1.22078 1.06584 1.49855 0.11572  0.08464  0.07479  68  VAL A N   
229  C CA  . VAL A 32  ? 1.15103 1.00779 1.41573 0.12204  0.09043  0.06643  68  VAL A CA  
230  C C   . VAL A 32  ? 1.10791 0.92838 1.34414 0.14036  0.09442  0.05935  68  VAL A C   
231  O O   . VAL A 32  ? 1.07757 0.87642 1.30583 0.14638  0.08364  0.04512  68  VAL A O   
232  C CB  . VAL A 32  ? 1.22879 1.11535 1.49463 0.11092  0.07795  0.03988  68  VAL A CB  
233  C CG1 . VAL A 32  ? 1.17251 1.06400 1.42312 0.11893  0.07959  0.02748  68  VAL A CG1 
234  C CG2 . VAL A 32  ? 1.20223 1.12827 1.48598 0.08903  0.07509  0.05236  68  VAL A CG2 
235  N N   . PRO A 33  ? 1.25093 1.06040 1.47016 0.14845  0.10788  0.06934  69  PRO A N   
236  C CA  . PRO A 33  ? 1.24247 1.01410 1.42541 0.16077  0.10834  0.06213  69  PRO A CA  
237  C C   . PRO A 33  ? 1.21786 0.99924 1.39461 0.15936  0.09073  0.03784  69  PRO A C   
238  O O   . PRO A 33  ? 1.22122 1.03888 1.41527 0.15045  0.08535  0.02780  69  PRO A O   
239  C CB  . PRO A 33  ? 1.23065 0.98591 1.39556 0.16708  0.12886  0.07693  69  PRO A CB  
240  C CG  . PRO A 33  ? 1.24702 1.03226 1.44915 0.16218  0.14129  0.09833  69  PRO A CG  
241  C CD  . PRO A 33  ? 1.24934 1.07549 1.48107 0.14624  0.12259  0.08922  69  PRO A CD  
242  N N   . VAL A 34  ? 1.15555 0.90766 1.30877 0.16701  0.08139  0.03131  70  VAL A N   
243  C CA  . VAL A 34  ? 1.25970 1.02302 1.41353 0.16719  0.06367  0.01325  70  VAL A CA  
244  C C   . VAL A 34  ? 1.31419 1.04022 1.42700 0.17038  0.05823  0.01779  70  VAL A C   
245  O O   . VAL A 34  ? 1.32677 1.01425 1.40618 0.17379  0.06898  0.03094  70  VAL A O   
246  C CB  . VAL A 34  ? 1.13503 0.90758 1.31577 0.17190  0.04927  -0.00096 70  VAL A CB  
247  C CG1 . VAL A 34  ? 1.18531 0.99073 1.39645 0.16490  0.05300  -0.01128 70  VAL A CG1 
248  C CG2 . VAL A 34  ? 1.13142 0.86411 1.30103 0.17893  0.04534  0.01057  70  VAL A CG2 
249  N N   . ALA A 35  ? 1.26667 1.00628 1.38084 0.16740  0.04143  0.00734  71  ALA A N   
250  C CA  . ALA A 35  ? 1.32686 1.03423 1.40192 0.16499  0.02852  0.01124  71  ALA A CA  
251  C C   . ALA A 35  ? 1.33626 1.05031 1.43066 0.16993  0.00519  0.00786  71  ALA A C   
252  O O   . ALA A 35  ? 1.38347 1.13891 1.51777 0.17092  -0.00561 -0.00298 71  ALA A O   
253  C CB  . ALA A 35  ? 1.30392 1.02199 1.36827 0.15383  0.02425  0.00793  71  ALA A CB  
254  N N   . ILE A 36  ? 1.42931 1.10466 1.49795 0.17349  -0.00153 0.01906  72  ILE A N   
255  C CA  . ILE A 36  ? 1.51661 1.19333 1.60797 0.17962  -0.02508 0.02168  72  ILE A CA  
256  C C   . ILE A 36  ? 1.54453 1.20530 1.60416 0.17018  -0.04878 0.03044  72  ILE A C   
257  O O   . ILE A 36  ? 1.63650 1.25497 1.63348 0.16025  -0.04623 0.03918  72  ILE A O   
258  C CB  . ILE A 36  ? 1.48729 1.13265 1.57285 0.18583  -0.02251 0.03376  72  ILE A CB  
259  C CG1 . ILE A 36  ? 1.45671 1.11305 1.56468 0.18913  0.00008  0.02910  72  ILE A CG1 
260  C CG2 . ILE A 36  ? 1.53140 1.18072 1.65475 0.19463  -0.04721 0.03644  72  ILE A CG2 
261  C CD1 . ILE A 36  ? 1.44445 1.07081 1.54659 0.19134  0.00336  0.04488  72  ILE A CD1 
262  N N   . LYS A 37  ? 1.55577 1.25020 1.65802 0.17260  -0.07141 0.02839  73  LYS A N   
263  C CA  . LYS A 37  ? 1.65394 1.34277 1.73718 0.16061  -0.10021 0.04037  73  LYS A CA  
264  C C   . LYS A 37  ? 1.79972 1.48632 1.91113 0.16861  -0.12620 0.05508  73  LYS A C   
265  O O   . LYS A 37  ? 1.65362 1.37333 1.83235 0.18595  -0.12755 0.04870  73  LYS A O   
266  C CB  . LYS A 37  ? 1.53167 1.27070 1.64972 0.15420  -0.10768 0.03272  73  LYS A CB  
267  C CG  . LYS A 37  ? 1.61597 1.35409 1.71900 0.13737  -0.14135 0.04820  73  LYS A CG  
268  C CD  . LYS A 37  ? 1.52871 1.31791 1.66450 0.12736  -0.14620 0.04345  73  LYS A CD  
269  C CE  . LYS A 37  ? 1.53178 1.32000 1.65187 0.10544  -0.18317 0.06198  73  LYS A CE  
270  N NZ  . LYS A 37  ? 1.46579 1.30740 1.62146 0.09287  -0.18867 0.06112  73  LYS A NZ  
271  N N   . PHE A 38  ? 1.86032 1.50542 1.91863 0.15573  -0.14658 0.07477  74  PHE A N   
272  C CA  . PHE A 38  ? 1.92484 1.56463 2.00544 0.15953  -0.17660 0.09582  74  PHE A CA  
273  C C   . PHE A 38  ? 2.08852 1.75435 2.18704 0.14767  -0.21277 0.10983  74  PHE A C   
274  O O   . PHE A 38  ? 2.04056 1.71358 2.11208 0.13044  -0.21671 0.10550  74  PHE A O   
275  C CB  . PHE A 38  ? 1.96543 1.54618 1.97497 0.14931  -0.17958 0.11427  74  PHE A CB  
276  C CG  . PHE A 38  ? 1.88224 1.44411 1.89242 0.16176  -0.15136 0.11029  74  PHE A CG  
277  C CD1 . PHE A 38  ? 1.75877 1.34827 1.81629 0.17686  -0.12491 0.08895  74  PHE A CD1 
278  C CD2 . PHE A 38  ? 1.91774 1.43528 1.87820 0.15481  -0.15285 0.13050  74  PHE A CD2 
279  C CE1 . PHE A 38  ? 1.79443 1.36711 1.85308 0.18391  -0.10338 0.08886  74  PHE A CE1 
280  C CE2 . PHE A 38  ? 1.92997 1.43380 1.89472 0.16332  -0.12872 0.13130  74  PHE A CE2 
281  C CZ  . PHE A 38  ? 1.89742 1.42871 1.91308 0.17745  -0.10526 0.11081  74  PHE A CZ  
282  N N   . GLU A 39  ? 2.57591 2.25513 2.72371 0.15601  -0.24143 0.12985  75  GLU A N   
283  C CA  . GLU A 39  ? 2.64845 2.35855 2.82674 0.14549  -0.28055 0.15093  75  GLU A CA  
284  C C   . GLU A 39  ? 2.67588 2.38605 2.90107 0.15630  -0.31095 0.17892  75  GLU A C   
285  O O   . GLU A 39  ? 2.62724 2.34880 2.91684 0.18403  -0.29880 0.17220  75  GLU A O   
286  C CB  . GLU A 39  ? 2.54916 2.32864 2.80364 0.15572  -0.27351 0.13641  75  GLU A CB  
287  C CG  . GLU A 39  ? 2.63533 2.45448 2.92239 0.14056  -0.31254 0.16051  75  GLU A CG  
288  C CD  . GLU A 39  ? 2.59749 2.49654 2.99090 0.16146  -0.30570 0.15348  75  GLU A CD  
289  O OE1 . GLU A 39  ? 2.53339 2.45305 2.99855 0.19293  -0.29456 0.14774  75  GLU A OE1 
290  O OE2 . GLU A 39  ? 2.63929 2.57909 3.04362 0.14620  -0.31000 0.15325  75  GLU A OE2 
291  N N   . PRO A 40  ? 2.33319 2.02780 2.52718 0.13381  -0.35238 0.21138  76  PRO A N   
292  C CA  . PRO A 40  ? 2.18672 1.88515 2.43341 0.14330  -0.38613 0.24416  76  PRO A CA  
293  C C   . PRO A 40  ? 2.11113 1.87887 2.48302 0.17005  -0.39484 0.24696  76  PRO A C   
294  O O   . PRO A 40  ? 2.13456 1.95284 2.54004 0.16577  -0.39729 0.24163  76  PRO A O   
295  C CB  . PRO A 40  ? 2.11707 1.78868 2.29270 0.10576  -0.43069 0.27836  76  PRO A CB  
296  C CG  . PRO A 40  ? 2.02069 1.65075 2.08459 0.07942  -0.41051 0.25715  76  PRO A CG  
297  C CD  . PRO A 40  ? 2.19858 1.86371 2.30048 0.09644  -0.37163 0.22038  76  PRO A CD  
298  N N   . ARG A 41  ? 1.86952 1.63855 2.31235 0.19840  -0.39790 0.25577  77  ARG A N   
299  C CA  . ARG A 41  ? 1.85363 1.68440 2.42033 0.22932  -0.40252 0.25808  77  ARG A CA  
300  C C   . ARG A 41  ? 1.84425 1.71130 2.45232 0.21565  -0.45330 0.30236  77  ARG A C   
301  O O   . ARG A 41  ? 1.79682 1.72869 2.46597 0.21826  -0.45779 0.30383  77  ARG A O   
302  C CB  . ARG A 41  ? 1.81088 1.62180 2.43910 0.26404  -0.39197 0.25396  77  ARG A CB  
303  C CG  . ARG A 41  ? 1.92892 1.67905 2.48859 0.26246  -0.36288 0.23216  77  ARG A CG  
304  C CD  . ARG A 41  ? 1.93428 1.66763 2.56277 0.29648  -0.35120 0.22260  77  ARG A CD  
305  N NE  . ARG A 41  ? 1.78229 1.56498 2.49522 0.32802  -0.32437 0.19000  77  ARG A NE  
306  C CZ  . ARG A 41  ? 1.78233 1.57942 2.47711 0.33137  -0.28360 0.14774  77  ARG A CZ  
307  N NH1 . ARG A 41  ? 1.83050 1.59816 2.43557 0.30797  -0.26509 0.13388  77  ARG A NH1 
308  N NH2 . ARG A 41  ? 1.74497 1.58894 2.51435 0.35889  -0.26011 0.12015  77  ARG A NH2 
309  N N   . LYS A 42  ? 1.81824 1.64747 2.39505 0.19870  -0.49349 0.34217  78  LYS A N   
310  C CA  . LYS A 42  ? 1.87504 1.73385 2.47973 0.17820  -0.54915 0.39073  78  LYS A CA  
311  C C   . LYS A 42  ? 2.06350 1.90595 2.55973 0.12960  -0.56673 0.39481  78  LYS A C   
312  O O   . LYS A 42  ? 2.17868 1.97060 2.58107 0.09486  -0.59644 0.41886  78  LYS A O   
313  C CB  . LYS A 42  ? 1.84887 1.67346 2.46351 0.17772  -0.58747 0.43429  78  LYS A CB  
314  C CG  . LYS A 42  ? 1.69759 1.55172 2.44894 0.22471  -0.58709 0.44368  78  LYS A CG  
315  C CD  . LYS A 42  ? 1.73711 1.67793 2.60781 0.24274  -0.59825 0.45501  78  LYS A CD  
316  C CE  . LYS A 42  ? 1.69623 1.66489 2.56342 0.20549  -0.66026 0.51016  78  LYS A CE  
317  N NZ  . LYS A 42  ? 1.62249 1.68339 2.59971 0.21704  -0.66837 0.52132  78  LYS A NZ  
318  N N   . THR A 43  ? 2.09556 1.97909 2.60257 0.12655  -0.54683 0.36964  79  THR A N   
319  C CA  . THR A 43  ? 2.20341 2.07322 2.61928 0.08279  -0.56123 0.36889  79  THR A CA  
320  C C   . THR A 43  ? 2.24803 2.19373 2.74175 0.07171  -0.59424 0.39403  79  THR A C   
321  O O   . THR A 43  ? 2.17615 2.19063 2.79767 0.10278  -0.59630 0.40679  79  THR A O   
322  C CB  . THR A 43  ? 2.26995 2.11597 2.62149 0.08312  -0.50970 0.31952  79  THR A CB  
323  O OG1 . THR A 43  ? 2.38345 2.20109 2.63820 0.04003  -0.52532 0.31916  79  THR A OG1 
324  C CG2 . THR A 43  ? 2.27642 2.19245 2.72639 0.11404  -0.47570 0.29358  79  THR A CG2 
325  N N   . GLU A 44  ? 2.35385 2.28554 2.76984 0.02659  -0.61945 0.40136  80  GLU A N   
326  C CA  . GLU A 44  ? 2.35209 2.35354 2.83061 0.00704  -0.65383 0.42739  80  GLU A CA  
327  C C   . GLU A 44  ? 2.37149 2.41820 2.87970 0.01405  -0.61616 0.39417  80  GLU A C   
328  O O   . GLU A 44  ? 2.36054 2.47250 2.92680 -0.00197 -0.63957 0.41463  80  GLU A O   
329  C CB  . GLU A 44  ? 2.38300 2.34265 2.76005 -0.05190 -0.70892 0.45674  80  GLU A CB  
330  C CG  . GLU A 44  ? 2.44854 2.32581 2.67550 -0.08286 -0.68866 0.42117  80  GLU A CG  
331  C CD  . GLU A 44  ? 2.45196 2.23825 2.54990 -0.10941 -0.70684 0.42937  80  GLU A CD  
332  O OE1 . GLU A 44  ? 2.39988 2.17399 2.51744 -0.08795 -0.70672 0.44342  80  GLU A OE1 
333  O OE2 . GLU A 44  ? 2.46812 2.19321 2.44313 -0.15256 -0.72074 0.42179  80  GLU A OE2 
334  N N   . ALA A 45  ? 2.56606 2.58351 3.03883 0.03538  -0.56045 0.34734  81  ALA A N   
335  C CA  . ALA A 45  ? 2.58342 2.63995 3.07629 0.03984  -0.52415 0.31677  81  ALA A CA  
336  C C   . ALA A 45  ? 2.65351 2.70889 3.17191 0.08257  -0.46574 0.27620  81  ALA A C   
337  O O   . ALA A 45  ? 2.73581 2.73248 3.17088 0.08053  -0.43451 0.24546  81  ALA A O   
338  C CB  . ALA A 45  ? 2.72605 2.72733 3.10080 -0.00296 -0.52808 0.30346  81  ALA A CB  
339  N N   . PRO A 46  ? 2.20514 2.32414 2.83943 0.12216  -0.44914 0.27506  82  PRO A N   
340  C CA  . PRO A 46  ? 2.08336 2.20328 2.74078 0.15932  -0.39464 0.23397  82  PRO A CA  
341  C C   . PRO A 46  ? 1.94805 2.10731 2.60529 0.15418  -0.36113 0.20633  82  PRO A C   
342  O O   . PRO A 46  ? 1.80570 2.03682 2.52340 0.14664  -0.36988 0.21970  82  PRO A O   
343  C CB  . PRO A 46  ? 1.93203 2.10543 2.71337 0.20069  -0.39267 0.24400  82  PRO A CB  
344  C CG  . PRO A 46  ? 1.92188 2.10846 2.73640 0.18591  -0.44959 0.29538  82  PRO A CG  
345  C CD  . PRO A 46  ? 2.05040 2.23502 2.79759 0.13622  -0.48087 0.31280  82  PRO A CD  
346  N N   . GLN A 47  ? 1.87498 1.99047 2.46752 0.15693  -0.32380 0.17135  83  GLN A N   
347  C CA  . GLN A 47  ? 1.76598 1.91152 2.34853 0.14837  -0.29425 0.14798  83  GLN A CA  
348  C C   . GLN A 47  ? 1.73696 1.86156 2.30129 0.17032  -0.24692 0.10972  83  GLN A C   
349  O O   . GLN A 47  ? 1.60409 1.77500 2.19587 0.17621  -0.21707 0.08941  83  GLN A O   
350  C CB  . GLN A 47  ? 1.75869 1.86301 2.25015 0.10579  -0.31322 0.15543  83  GLN A CB  
351  C CG  . GLN A 47  ? 1.86547 1.87633 2.25047 0.09746  -0.30332 0.14123  83  GLN A CG  
352  C CD  . GLN A 47  ? 1.71380 1.67656 2.00778 0.05862  -0.31874 0.14492  83  GLN A CD  
353  O OE1 . GLN A 47  ? 1.67934 1.67688 1.98693 0.03513  -0.33634 0.15599  83  GLN A OE1 
354  N NE2 . GLN A 47  ? 1.58346 1.46419 1.78431 0.05160  -0.31114 0.13572  83  GLN A NE2 
355  N N   . LEU A 48  ? 1.77253 1.82965 2.28964 0.17948  -0.24139 0.10231  84  LEU A N   
356  C CA  . LEU A 48  ? 1.73360 1.76433 2.22369 0.19320  -0.20187 0.07045  84  LEU A CA  
357  C C   . LEU A 48  ? 1.56175 1.64183 2.12996 0.22506  -0.17324 0.04773  84  LEU A C   
358  O O   . LEU A 48  ? 1.52789 1.60605 2.08021 0.23037  -0.14031 0.02003  84  LEU A O   
359  C CB  . LEU A 48  ? 1.83007 1.78428 2.26275 0.19543  -0.20488 0.07321  84  LEU A CB  
360  C CG  . LEU A 48  ? 1.66735 1.58486 2.05188 0.19811  -0.17025 0.04826  84  LEU A CG  
361  C CD1 . LEU A 48  ? 1.55107 1.48099 1.89886 0.17816  -0.15520 0.03787  84  LEU A CD1 
362  C CD2 . LEU A 48  ? 1.71913 1.56393 2.03677 0.19181  -0.17654 0.05906  84  LEU A CD2 
363  N N   . ARG A 49  ? 1.53316 1.65557 2.18431 0.24608  -0.18508 0.05918  85  ARG A N   
364  C CA  . ARG A 49  ? 1.48266 1.65149 2.20879 0.27857  -0.15462 0.03461  85  ARG A CA  
365  C C   . ARG A 49  ? 1.36562 1.59886 2.10493 0.27054  -0.12813 0.01761  85  ARG A C   
366  O O   . ARG A 49  ? 1.29893 1.53898 2.03291 0.28061  -0.09246 -0.01477 85  ARG A O   
367  C CB  . ARG A 49  ? 1.47573 1.67967 2.29463 0.30353  -0.17388 0.05546  85  ARG A CB  
368  C CG  . ARG A 49  ? 1.39947 1.65045 2.30267 0.34178  -0.14054 0.02962  85  ARG A CG  
369  C CD  . ARG A 49  ? 1.37963 1.67348 2.38335 0.36543  -0.16213 0.05775  85  ARG A CD  
370  N NE  . ARG A 49  ? 1.42674 1.66097 2.42554 0.36938  -0.19733 0.08400  85  ARG A NE  
371  C CZ  . ARG A 49  ? 1.50043 1.68715 2.51854 0.39795  -0.18935 0.07110  85  ARG A CZ  
372  N NH1 . ARG A 49  ? 1.50488 1.69028 2.54409 0.42537  -0.14747 0.02878  85  ARG A NH1 
373  N NH2 . ARG A 49  ? 1.58060 1.71708 2.59290 0.39648  -0.22557 0.10187  85  ARG A NH2 
374  N N   . ASP A 50  ? 1.34699 1.62699 2.09960 0.24851  -0.14743 0.04119  86  ASP A N   
375  C CA  . ASP A 50  ? 1.30628 1.65514 2.07903 0.23860  -0.12526 0.03157  86  ASP A CA  
376  C C   . ASP A 50  ? 1.36768 1.68539 2.05757 0.21179  -0.11168 0.01779  86  ASP A C   
377  O O   . ASP A 50  ? 1.31731 1.68014 2.01429 0.20800  -0.08397 0.00113  86  ASP A O   
378  C CB  . ASP A 50  ? 1.31054 1.72192 2.13165 0.22138  -0.15386 0.06615  86  ASP A CB  
379  C CG  . ASP A 50  ? 1.32387 1.79569 2.25296 0.25248  -0.15700 0.07909  86  ASP A CG  
380  O OD1 . ASP A 50  ? 1.24678 1.71040 2.21211 0.28940  -0.13248 0.05617  86  ASP A OD1 
381  O OD2 . ASP A 50  ? 1.39696 1.92341 2.37726 0.23983  -0.18472 0.11327  86  ASP A OD2 
382  N N   . GLU A 51  ? 1.42059 1.66357 2.03315 0.19327  -0.12959 0.02585  87  GLU A N   
383  C CA  . GLU A 51  ? 1.42551 1.63555 1.96710 0.17325  -0.11400 0.01341  87  GLU A CA  
384  C C   . GLU A 51  ? 1.37212 1.57143 1.90684 0.19121  -0.07862 -0.01740 87  GLU A C   
385  O O   . GLU A 51  ? 1.32456 1.53626 1.83461 0.17907  -0.05812 -0.02974 87  GLU A O   
386  C CB  . GLU A 51  ? 1.51992 1.65043 1.98289 0.15408  -0.13627 0.02729  87  GLU A CB  
387  C CG  . GLU A 51  ? 1.50933 1.60776 1.90645 0.13299  -0.12314 0.02033  87  GLU A CG  
388  C CD  . GLU A 51  ? 1.57906 1.60332 1.90013 0.11332  -0.14381 0.03395  87  GLU A CD  
389  O OE1 . GLU A 51  ? 1.62989 1.59898 1.91758 0.12296  -0.14536 0.03381  87  GLU A OE1 
390  O OE2 . GLU A 51  ? 1.60343 1.62272 1.89579 0.08719  -0.15791 0.04455  87  GLU A OE2 
391  N N   . TYR A 52  ? 1.36055 1.53530 1.91668 0.21760  -0.07410 -0.02787 88  TYR A N   
392  C CA  . TYR A 52  ? 1.26703 1.43149 1.82074 0.23324  -0.04374 -0.05795 88  TYR A CA  
393  C C   . TYR A 52  ? 1.29621 1.53179 1.89204 0.23968  -0.01604 -0.07892 88  TYR A C   
394  O O   . TYR A 52  ? 1.17024 1.40966 1.73825 0.23242  0.00770  -0.09927 88  TYR A O   
395  C CB  . TYR A 52  ? 1.33950 1.46424 1.91649 0.25964  -0.04868 -0.06251 88  TYR A CB  
396  C CG  . TYR A 52  ? 1.33662 1.44992 1.92107 0.27740  -0.02093 -0.09513 88  TYR A CG  
397  C CD1 . TYR A 52  ? 1.27385 1.34930 1.80303 0.26475  -0.00792 -0.10730 88  TYR A CD1 
398  C CD2 . TYR A 52  ? 1.33089 1.46834 1.97899 0.30680  -0.00874 -0.11303 88  TYR A CD2 
399  C CE1 . TYR A 52  ? 1.33626 1.39754 1.86790 0.27613  0.01282  -0.13616 88  TYR A CE1 
400  C CE2 . TYR A 52  ? 1.29315 1.41044 1.94057 0.32107  0.01535  -0.14611 88  TYR A CE2 
401  C CZ  . TYR A 52  ? 1.41011 1.48844 1.99594 0.30311  0.02404  -0.15728 88  TYR A CZ  
402  O OH  . TYR A 52  ? 1.51317 1.56854 2.09348 0.31221  0.04396  -0.18952 88  TYR A OH  
403  N N   . ARG A 53  ? 1.20033 1.49624 1.86347 0.25185  -0.01855 -0.07205 89  ARG A N   
404  C CA  . ARG A 53  ? 1.17233 1.54242 1.87605 0.25826  0.01167  -0.09091 89  ARG A CA  
405  C C   . ARG A 53  ? 1.09230 1.50112 1.76594 0.22513  0.01497  -0.08156 89  ARG A C   
406  O O   . ARG A 53  ? 1.08585 1.54222 1.76335 0.22177  0.04374  -0.10003 89  ARG A O   
407  C CB  . ARG A 53  ? 1.25271 1.68232 2.04547 0.28214  0.00961  -0.08156 89  ARG A CB  
408  C CG  . ARG A 53  ? 1.23458 1.62178 2.05841 0.30414  -0.01609 -0.06685 89  ARG A CG  
409  C CD  . ARG A 53  ? 1.28535 1.73001 2.20891 0.33810  -0.00775 -0.06582 89  ARG A CD  
410  N NE  . ARG A 53  ? 1.33841 1.73975 2.29583 0.36066  -0.03288 -0.05049 89  ARG A NE  
411  C CZ  . ARG A 53  ? 1.43146 1.83863 2.45888 0.40068  -0.01831 -0.06407 89  ARG A CZ  
412  N NH1 . ARG A 53  ? 1.34327 1.79289 2.40830 0.42428  0.02478  -0.09833 89  ARG A NH1 
413  N NH2 . ARG A 53  ? 1.42618 1.79298 2.48469 0.41728  -0.04709 -0.04281 89  ARG A NH2 
414  N N   . THR A 54  ? 1.15648 1.54192 1.79623 0.19914  -0.01426 -0.05329 90  THR A N   
415  C CA  . THR A 54  ? 1.17523 1.58952 1.78819 0.16680  -0.01470 -0.04160 90  THR A CA  
416  C C   . THR A 54  ? 1.11544 1.49898 1.66991 0.15492  0.00438  -0.05810 90  THR A C   
417  O O   . THR A 54  ? 1.04056 1.47028 1.59162 0.13885  0.02097  -0.06164 90  THR A O   
418  C CB  . THR A 54  ? 1.16428 1.54823 1.75097 0.14237  -0.05196 -0.01008 90  THR A CB  
419  O OG1 . THR A 54  ? 1.19539 1.59241 1.83013 0.15395  -0.07593 0.00743  90  THR A OG1 
420  C CG2 . THR A 54  ? 0.97566 1.40554 1.55967 0.11054  -0.05627 0.00645  90  THR A CG2 
421  N N   . TYR A 55  ? 1.19107 1.50070 1.70164 0.16089  0.00122  -0.06460 91  TYR A N   
422  C CA  . TYR A 55  ? 1.19667 1.48008 1.65991 0.15017  0.01728  -0.07596 91  TYR A CA  
423  C C   . TYR A 55  ? 1.18465 1.50633 1.66416 0.15986  0.04681  -0.10450 91  TYR A C   
424  O O   . TYR A 55  ? 1.16189 1.50265 1.61644 0.14184  0.06061  -0.10934 91  TYR A O   
425  C CB  . TYR A 55  ? 1.16226 1.36523 1.58454 0.15653  0.00921  -0.07457 91  TYR A CB  
426  C CG  . TYR A 55  ? 1.15692 1.31245 1.54044 0.14176  -0.01321 -0.05048 91  TYR A CG  
427  C CD1 . TYR A 55  ? 1.22598 1.37009 1.57260 0.11928  -0.01269 -0.03950 91  TYR A CD1 
428  C CD2 . TYR A 55  ? 1.22151 1.33965 1.60241 0.14991  -0.03478 -0.03896 91  TYR A CD2 
429  C CE1 . TYR A 55  ? 1.13487 1.22733 1.44090 0.10736  -0.02987 -0.02217 91  TYR A CE1 
430  C CE2 . TYR A 55  ? 1.30674 1.37596 1.64104 0.13451  -0.05351 -0.02071 91  TYR A CE2 
431  C CZ  . TYR A 55  ? 1.16336 1.21752 1.45912 0.11433  -0.04932 -0.01468 91  TYR A CZ  
432  O OH  . TYR A 55  ? 1.24803 1.24575 1.49271 0.10055  -0.06478 -0.00098 91  TYR A OH  
433  N N   . LYS A 56  ? 1.24321 1.57333 1.76250 0.18760  0.05627  -0.12357 92  LYS A N   
434  C CA  . LYS A 56  ? 1.28193 1.64326 1.81224 0.19794  0.08670  -0.15595 92  LYS A CA  
435  C C   . LYS A 56  ? 1.27152 1.71612 1.82099 0.18444  0.10430  -0.15658 92  LYS A C   
436  O O   . LYS A 56  ? 1.30229 1.77126 1.82869 0.17406  0.12744  -0.17609 92  LYS A O   
437  C CB  . LYS A 56  ? 1.27493 1.62464 1.85023 0.23364  0.09355  -0.17578 92  LYS A CB  
438  C CG  . LYS A 56  ? 1.34065 1.60951 1.89302 0.24556  0.08315  -0.18214 92  LYS A CG  
439  C CD  . LYS A 56  ? 1.36673 1.60471 1.86707 0.23154  0.09636  -0.20161 92  LYS A CD  
440  C CE  . LYS A 56  ? 1.43020 1.60896 1.93185 0.25192  0.09740  -0.22186 92  LYS A CE  
441  N NZ  . LYS A 56  ? 1.41969 1.56106 1.95052 0.27162  0.07501  -0.20352 92  LYS A NZ  
442  N N   . HIS A 57  ? 1.14216 1.63299 1.73239 0.18148  0.09236  -0.13327 93  HIS A N   
443  C CA  . HIS A 57  ? 1.04910 1.62495 1.66200 0.16605  0.10809  -0.12815 93  HIS A CA  
444  C C   . HIS A 57  ? 1.04661 1.62510 1.60711 0.12892  0.10514  -0.11489 93  HIS A C   
445  O O   . HIS A 57  ? 1.02321 1.65639 1.57699 0.11442  0.12749  -0.12298 93  HIS A O   
446  C CB  . HIS A 57  ? 0.98372 1.60572 1.65420 0.16674  0.08955  -0.09938 93  HIS A CB  
447  C CG  . HIS A 57  ? 0.96601 1.68722 1.68064 0.15942  0.11061  -0.09520 93  HIS A CG  
448  N ND1 . HIS A 57  ? 0.93898 1.70169 1.62469 0.13873  0.13548  -0.10508 93  HIS A ND1 
449  C CD2 . HIS A 57  ? 0.91002 1.70178 1.69802 0.16874  0.11050  -0.07895 93  HIS A CD2 
450  C CE1 . HIS A 57  ? 0.91745 1.77160 1.65344 0.13570  0.15221  -0.09648 93  HIS A CE1 
451  N NE2 . HIS A 57  ? 0.93773 1.81298 1.73987 0.15457  0.13809  -0.08024 93  HIS A NE2 
452  N N   . LEU A 58  ? 1.42805 1.49410 1.42436 0.07970  0.12745  -0.13918 94  LEU A N   
453  C CA  . LEU A 58  ? 1.49077 1.55217 1.41012 0.06817  0.11085  -0.13615 94  LEU A CA  
454  C C   . LEU A 58  ? 1.53668 1.57679 1.44266 0.06248  0.08803  -0.14846 94  LEU A C   
455  O O   . LEU A 58  ? 1.57897 1.61616 1.44159 0.05456  0.06676  -0.13846 94  LEU A O   
456  C CB  . LEU A 58  ? 1.40692 1.48986 1.32229 0.06956  0.09767  -0.09970 94  LEU A CB  
457  C CG  . LEU A 58  ? 1.33328 1.44002 1.27335 0.07575  0.11222  -0.08759 94  LEU A CG  
458  C CD1 . LEU A 58  ? 1.22605 1.35188 1.19531 0.08385  0.09488  -0.05503 94  LEU A CD1 
459  C CD2 . LEU A 58  ? 1.17970 1.29128 1.06843 0.06642  0.12293  -0.09189 94  LEU A CD2 
460  N N   . GLN A 59  ? 1.54416 1.56975 1.49813 0.06640  0.09110  -0.17073 95  GLN A N   
461  C CA  . GLN A 59  ? 1.64329 1.64899 1.60296 0.06156  0.06765  -0.18624 95  GLN A CA  
462  C C   . GLN A 59  ? 1.69466 1.68458 1.56798 0.04902  0.05142  -0.21237 95  GLN A C   
463  O O   . GLN A 59  ? 1.71076 1.69556 1.52792 0.04516  0.06860  -0.23471 95  GLN A O   
464  C CB  . GLN A 59  ? 1.67794 1.67113 1.71378 0.06795  0.07760  -0.21153 95  GLN A CB  
465  C CG  . GLN A 59  ? 1.71405 1.68279 1.74509 0.06053  0.05777  -0.25242 95  GLN A CG  
466  C CD  . GLN A 59  ? 1.83066 1.78561 1.80116 0.05402  0.06875  -0.30118 95  GLN A CD  
467  O OE1 . GLN A 59  ? 1.84914 1.81047 1.81783 0.05733  0.10159  -0.30948 95  GLN A OE1 
468  N NE2 . GLN A 59  ? 1.81444 1.74923 1.73475 0.04473  0.04127  -0.33428 95  GLN A NE2 
469  N N   . GLY A 60  ? 1.63348 1.61426 1.49715 0.04291  0.01871  -0.20757 96  GLY A N   
470  C CA  . GLY A 60  ? 1.65533 1.61936 1.44119 0.03195  -0.00713 -0.22793 96  GLY A CA  
471  C C   . GLY A 60  ? 1.63087 1.60351 1.34737 0.02546  -0.01433 -0.20043 96  GLY A C   
472  O O   . GLY A 60  ? 1.70593 1.66459 1.36444 0.01687  -0.04376 -0.20625 96  GLY A O   
473  N N   . CYS A 61  ? 1.56914 1.56402 1.29451 0.02948  0.00869  -0.17074 97  CYS A N   
474  C CA  . CYS A 61  ? 1.54376 1.54821 1.21835 0.02343  0.00476  -0.14518 97  CYS A CA  
475  C C   . CYS A 61  ? 1.50718 1.51741 1.21361 0.02060  -0.02188 -0.11924 97  CYS A C   
476  O O   . CYS A 61  ? 1.38461 1.40005 1.15779 0.02606  -0.02286 -0.11018 97  CYS A O   
477  C CB  . CYS A 61  ? 1.48296 1.50981 1.16658 0.02857  0.03819  -0.12882 97  CYS A CB  
478  S SG  . CYS A 61  ? 1.56783 1.58811 1.22534 0.03097  0.07810  -0.15827 97  CYS A SG  
479  N N   . ASP A 62  ? 1.55238 1.55990 1.21274 0.01202  -0.04061 -0.10594 98  ASP A N   
480  C CA  . ASP A 62  ? 1.39549 1.40777 1.09200 0.00806  -0.06347 -0.08354 98  ASP A CA  
481  C C   . ASP A 62  ? 1.28544 1.32277 1.02278 0.01268  -0.04183 -0.05906 98  ASP A C   
482  O O   . ASP A 62  ? 1.32574 1.37864 1.04195 0.01408  -0.02108 -0.05043 98  ASP A O   
483  C CB  . ASP A 62  ? 1.42450 1.42808 1.06832 -0.00178 -0.08906 -0.07277 98  ASP A CB  
484  C CG  . ASP A 62  ? 1.58813 1.59313 1.15795 -0.00381 -0.06853 -0.06826 98  ASP A CG  
485  O OD1 . ASP A 62  ? 1.54578 1.57015 1.12877 0.00051  -0.03542 -0.05922 98  ASP A OD1 
486  O OD2 . ASP A 62  ? 1.66934 1.65489 1.16814 -0.00962 -0.08594 -0.07279 98  ASP A OD2 
487  N N   . GLY A 63  ? 1.24030 1.28031 1.03685 0.01511  -0.04586 -0.04944 99  GLY A N   
488  C CA  . GLY A 63  ? 1.21554 1.27603 1.04079 0.01953  -0.02809 -0.02910 99  GLY A CA  
489  C C   . GLY A 63  ? 1.14883 1.21724 0.99990 0.03146  -0.00661 -0.02782 99  GLY A C   
490  O O   . GLY A 63  ? 1.16148 1.24632 1.02568 0.03627  0.00481  -0.01122 99  GLY A O   
491  N N   . ILE A 64  ? 1.16160 1.21837 1.02122 0.03652  -0.00251 -0.04513 100 ILE A N   
492  C CA  . ILE A 64  ? 1.15440 1.21647 1.05020 0.04862  0.01573  -0.04117 100 ILE A CA  
493  C C   . ILE A 64  ? 1.08931 1.13262 1.03727 0.05182  0.01224  -0.04566 100 ILE A C   
494  O O   . ILE A 64  ? 1.12703 1.15282 1.07935 0.04771  0.00062  -0.07072 100 ILE A O   
495  C CB  . ILE A 64  ? 1.23917 1.30481 1.12063 0.05271  0.03048  -0.05832 100 ILE A CB  
496  C CG1 . ILE A 64  ? 1.25054 1.33581 1.09742 0.05062  0.03904  -0.05088 100 ILE A CG1 
497  C CG2 . ILE A 64  ? 1.21420 1.28226 1.14941 0.06557  0.04485  -0.05372 100 ILE A CG2 
498  C CD1 . ILE A 64  ? 1.18508 1.29210 1.04994 0.05593  0.04006  -0.02590 100 ILE A CD1 
499  N N   . PRO A 65  ? 1.08594 1.13055 1.07475 0.05919  0.02246  -0.02269 101 PRO A N   
500  C CA  . PRO A 65  ? 1.21401 1.23917 1.26452 0.06252  0.02451  -0.02385 101 PRO A CA  
501  C C   . PRO A 65  ? 1.24593 1.26358 1.33008 0.06984  0.03208  -0.04151 101 PRO A C   
502  O O   . PRO A 65  ? 1.19224 1.22190 1.26598 0.07667  0.04344  -0.04060 101 PRO A O   
503  C CB  . PRO A 65  ? 1.20447 1.23336 1.27568 0.06998  0.04171  0.01117  101 PRO A CB  
504  C CG  . PRO A 65  ? 1.16770 1.21972 1.19256 0.07490  0.04660  0.02512  101 PRO A CG  
505  C CD  . PRO A 65  ? 1.15434 1.21672 1.13219 0.06495  0.03329  0.00518  101 PRO A CD  
506  N N   . ASN A 66  ? 1.19686 1.19445 1.33264 0.06816  0.02541  -0.06015 102 ASN A N   
507  C CA  . ASN A 66  ? 1.22034 1.20847 1.39994 0.07375  0.03244  -0.08397 102 ASN A CA  
508  C C   . ASN A 66  ? 1.23644 1.22521 1.48068 0.08767  0.05573  -0.05425 102 ASN A C   
509  O O   . ASN A 66  ? 1.22575 1.20777 1.50704 0.09118  0.06367  -0.02536 102 ASN A O   
510  C CB  . ASN A 66  ? 1.21127 1.17780 1.43028 0.06682  0.01315  -0.11846 102 ASN A CB  
511  C CG  . ASN A 66  ? 1.25879 1.22125 1.40595 0.05535  -0.01229 -0.15390 102 ASN A CG  
512  O OD1 . ASN A 66  ? 1.37843 1.35144 1.45563 0.05380  -0.00632 -0.15853 102 ASN A OD1 
513  N ND2 . ASN A 66  ? 1.27092 1.21670 1.43674 0.04757  -0.04129 -0.17787 102 ASN A ND2 
514  N N   . ALA A 67  ? 1.23641 1.23175 1.49603 0.09581  0.06846  -0.05948 103 ALA A N   
515  C CA  . ALA A 67  ? 1.23220 1.22655 1.55999 0.11018  0.08689  -0.03005 103 ALA A CA  
516  C C   . ALA A 67  ? 1.20099 1.17357 1.62064 0.11188  0.09211  -0.04780 103 ALA A C   
517  O O   . ALA A 67  ? 1.28573 1.25042 1.72336 0.10680  0.08712  -0.09387 103 ALA A O   
518  C CB  . ALA A 67  ? 1.33853 1.34843 1.66538 0.11821  0.09598  -0.02997 103 ALA A CB  
519  N N   . TYR A 68  ? 1.17917 1.14069 1.65719 0.11885  0.10411  -0.01277 104 TYR A N   
520  C CA  . TYR A 68  ? 1.22675 1.16676 1.80751 0.12034  0.11099  -0.02603 104 TYR A CA  
521  C C   . TYR A 68  ? 1.13297 1.06767 1.80089 0.13555  0.13401  0.00164  104 TYR A C   
522  O O   . TYR A 68  ? 1.17374 1.09528 1.93261 0.13680  0.13913  -0.02575 104 TYR A O   
523  C CB  . TYR A 68  ? 1.12617 1.05211 1.73098 0.11571  0.11214  -0.00862 104 TYR A CB  
524  C CG  . TYR A 68  ? 1.26385 1.19072 1.81366 0.10042  0.08518  -0.03949 104 TYR A CG  
525  C CD1 . TYR A 68  ? 1.27795 1.20266 1.81135 0.09103  0.05956  -0.09374 104 TYR A CD1 
526  C CD2 . TYR A 68  ? 1.23999 1.16865 1.75248 0.09553  0.08532  -0.01397 104 TYR A CD2 
527  C CE1 . TYR A 68  ? 1.29219 1.21627 1.77267 0.07807  0.03036  -0.11636 104 TYR A CE1 
528  C CE2 . TYR A 68  ? 1.21408 1.14356 1.68747 0.08211  0.05862  -0.03862 104 TYR A CE2 
529  C CZ  . TYR A 68  ? 1.27521 1.20237 1.73210 0.07386  0.02895  -0.08708 104 TYR A CZ  
530  O OH  . TYR A 68  ? 1.40168 1.32816 1.81721 0.06149  -0.00196 -0.10617 104 TYR A OH  
531  N N   . TYR A 69  ? 1.15007 1.09400 1.79546 0.14734  0.14560  0.05460  105 TYR A N   
532  C CA  . TYR A 69  ? 1.21312 1.14951 1.94366 0.16306  0.16493  0.09078  105 TYR A CA  
533  C C   . TYR A 69  ? 1.33921 1.29199 2.01657 0.17519  0.16410  0.13938  105 TYR A C   
534  O O   . TYR A 69  ? 1.25628 1.21845 1.84282 0.17336  0.15725  0.16248  105 TYR A O   
535  C CB  . TYR A 69  ? 1.13919 1.05157 1.94335 0.16702  0.18543  0.12235  105 TYR A CB  
536  C CG  . TYR A 69  ? 1.22438 1.12634 2.11074 0.18450  0.20774  0.17278  105 TYR A CG  
537  C CD1 . TYR A 69  ? 1.27788 1.16973 2.28696 0.18922  0.21699  0.15302  105 TYR A CD1 
538  C CD2 . TYR A 69  ? 1.26408 1.16499 2.10464 0.19649  0.21887  0.24040  105 TYR A CD2 
539  C CE1 . TYR A 69  ? 1.20106 1.08253 2.29458 0.20578  0.23718  0.20371  105 TYR A CE1 
540  C CE2 . TYR A 69  ? 1.33786 1.22715 2.24781 0.21346  0.23664  0.29297  105 TYR A CE2 
541  C CZ  . TYR A 69  ? 1.26407 1.14379 2.30560 0.21824  0.24607  0.27673  105 TYR A CZ  
542  O OH  . TYR A 69  ? 1.47435 1.34159 2.59469 0.23573  0.26379  0.33365  105 TYR A OH  
543  N N   . PHE A 70  ? 1.32459 1.28058 2.06616 0.18761  0.16902  0.15246  106 PHE A N   
544  C CA  . PHE A 70  ? 1.38849 1.35640 2.10700 0.20259  0.16420  0.20545  106 PHE A CA  
545  C C   . PHE A 70  ? 1.34414 1.29692 2.17707 0.21818  0.18012  0.24193  106 PHE A C   
546  O O   . PHE A 70  ? 1.30663 1.25726 2.23499 0.21917  0.18636  0.21053  106 PHE A O   
547  C CB  . PHE A 70  ? 1.47913 1.47283 2.16114 0.20156  0.14671  0.18064  106 PHE A CB  
548  C CG  . PHE A 70  ? 1.44893 1.45656 2.12456 0.21766  0.13396  0.23029  106 PHE A CG  
549  C CD1 . PHE A 70  ? 1.48413 1.48505 2.12230 0.22894  0.13111  0.29307  106 PHE A CD1 
550  C CD2 . PHE A 70  ? 1.41093 1.43721 2.11812 0.22158  0.12430  0.21315  106 PHE A CD2 
551  C CE1 . PHE A 70  ? 1.50641 1.51948 2.13261 0.24431  0.11147  0.33789  106 PHE A CE1 
552  C CE2 . PHE A 70  ? 1.48943 1.52941 2.20106 0.23671  0.10560  0.25726  106 PHE A CE2 
553  C CZ  . PHE A 70  ? 1.50239 1.53606 2.17027 0.24835  0.09540  0.31988  106 PHE A CZ  
554  N N   . GLY A 71  ? 1.50885 1.44953 2.33251 0.23027  0.18895  0.30802  107 GLY A N   
555  C CA  . GLY A 71  ? 1.53941 1.46217 2.47309 0.24576  0.20638  0.35183  107 GLY A CA  
556  C C   . GLY A 71  ? 1.58908 1.51181 2.48782 0.26441  0.19913  0.42896  107 GLY A C   
557  O O   . GLY A 71  ? 1.55577 1.49561 2.34420 0.26578  0.17617  0.44371  107 GLY A O   
558  N N   . GLN A 72  ? 1.64821 1.55058 2.64311 0.27920  0.21715  0.47907  108 GLN A N   
559  C CA  . GLN A 72  ? 1.70060 1.59928 2.67746 0.29960  0.20737  0.55810  108 GLN A CA  
560  C C   . GLN A 72  ? 1.78676 1.65096 2.78651 0.30825  0.24253  0.62119  108 GLN A C   
561  O O   . GLN A 72  ? 1.81909 1.66557 2.93151 0.32188  0.25851  0.66336  108 GLN A O   
562  C CB  . GLN A 72  ? 1.72008 1.62880 2.81108 0.31208  0.19276  0.56380  108 GLN A CB  
563  C CG  . GLN A 72  ? 1.67491 1.60881 2.80060 0.30022  0.17896  0.48450  108 GLN A CG  
564  C CD  . GLN A 72  ? 1.63362 1.55695 2.85699 0.28683  0.20530  0.41906  108 GLN A CD  
565  O OE1 . GLN A 72  ? 1.68209 1.58069 2.97693 0.28799  0.23185  0.43360  108 GLN A OE1 
566  N NE2 . GLN A 72  ? 1.56083 1.50168 2.78606 0.27401  0.19830  0.34575  108 GLN A NE2 
567  N N   . GLU A 73  ? 1.90058 1.75408 2.80009 0.30007  0.25837  0.62787  109 GLU A N   
568  C CA  . GLU A 73  ? 2.07473 1.89328 2.98842 0.30610  0.30026  0.68409  109 GLU A CA  
569  C C   . GLU A 73  ? 2.18218 1.99103 2.98658 0.32323  0.29529  0.76685  109 GLU A C   
570  O O   . GLU A 73  ? 2.26270 2.08574 2.92249 0.32014  0.27334  0.76511  109 GLU A O   
571  C CB  . GLU A 73  ? 2.09289 1.90235 2.96747 0.28797  0.32474  0.64656  109 GLU A CB  
572  C CG  . GLU A 73  ? 1.93160 1.73395 2.94192 0.27541  0.34130  0.58818  109 GLU A CG  
573  C CD  . GLU A 73  ? 1.89462 1.72469 2.94061 0.26578  0.30737  0.51282  109 GLU A CD  
574  O OE1 . GLU A 73  ? 1.95697 1.81348 2.90058 0.26145  0.27524  0.49012  109 GLU A OE1 
575  O OE2 . GLU A 73  ? 1.80096 1.62515 2.97847 0.26246  0.31503  0.47503  109 GLU A OE2 
576  N N   . GLY A 74  ? 2.18090 1.97491 3.04510 0.33511  0.31216  0.82502  110 GLY A N   
577  C CA  . GLY A 74  ? 2.30211 2.09260 3.05029 0.34642  0.30340  0.89186  110 GLY A CA  
578  C C   . GLY A 74  ? 2.29787 2.11239 2.97549 0.35691  0.24457  0.90023  110 GLY A C   
579  O O   . GLY A 74  ? 2.15253 1.98639 2.92612 0.36074  0.21626  0.87994  110 GLY A O   
580  N N   . LEU A 75  ? 2.53051 2.34569 3.04264 0.36034  0.22595  0.92492  111 LEU A N   
581  C CA  . LEU A 75  ? 2.49476 2.33609 2.92739 0.36879  0.16571  0.92728  111 LEU A CA  
582  C C   . LEU A 75  ? 2.52417 2.38671 2.86158 0.35660  0.15014  0.87201  111 LEU A C   
583  O O   . LEU A 75  ? 2.60239 2.47909 2.81013 0.35928  0.11490  0.87804  111 LEU A O   
584  C CB  . LEU A 75  ? 2.57403 2.40620 2.88733 0.37841  0.14389  0.98437  111 LEU A CB  
585  C CG  . LEU A 75  ? 2.70219 2.50938 2.86357 0.37326  0.17455  1.00543  111 LEU A CG  
586  C CD1 . LEU A 75  ? 2.77829 2.58703 2.78343 0.38068  0.12598  1.03295  111 LEU A CD1 
587  C CD2 . LEU A 75  ? 2.74647 2.52141 2.96179 0.37307  0.23215  1.04146  111 LEU A CD2 
588  N N   . HIS A 76  ? 2.22391 2.09450 2.62401 0.33711  0.17207  0.80175  112 HIS A N   
589  C CA  . HIS A 76  ? 2.07027 1.96478 2.38881 0.31815  0.15966  0.73485  112 HIS A CA  
590  C C   . HIS A 76  ? 1.86455 1.78078 2.28433 0.30412  0.15340  0.66052  112 HIS A C   
591  O O   . HIS A 76  ? 1.82595 1.72939 2.36834 0.30201  0.17859  0.64750  112 HIS A O   
592  C CB  . HIS A 76  ? 2.03255 1.90585 2.27910 0.30588  0.20213  0.72985  112 HIS A CB  
593  C CG  . HIS A 76  ? 2.22209 2.06185 2.39409 0.31915  0.23002  0.80568  112 HIS A CG  
594  N ND1 . HIS A 76  ? 2.31401 2.11735 2.56021 0.32404  0.28163  0.84697  112 HIS A ND1 
595  C CD2 . HIS A 76  ? 2.34299 2.17822 2.37020 0.32867  0.21512  0.84753  112 HIS A CD2 
596  C CE1 . HIS A 76  ? 2.32445 2.10485 2.47057 0.33304  0.29945  0.90518  112 HIS A CE1 
597  N NE2 . HIS A 76  ? 2.40715 2.20485 2.41389 0.33614  0.25857  0.90636  112 HIS A NE2 
598  N N   . ASN A 77  ? 1.87018 1.81788 2.23696 0.29461  0.12086  0.61137  113 ASN A N   
599  C CA  . ASN A 77  ? 1.79590 1.76205 2.22378 0.27870  0.11895  0.53788  113 ASN A CA  
600  C C   . ASN A 77  ? 1.73236 1.69323 2.10924 0.25938  0.14091  0.49730  113 ASN A C   
601  O O   . ASN A 77  ? 1.73248 1.69606 1.99932 0.25486  0.13789  0.50284  113 ASN A O   
602  C CB  . ASN A 77  ? 1.82149 1.82214 2.22586 0.27823  0.07778  0.50867  113 ASN A CB  
603  C CG  . ASN A 77  ? 1.79247 1.80081 2.29152 0.29431  0.05733  0.53174  113 ASN A CG  
604  O OD1 . ASN A 77  ? 1.69454 1.69098 2.31208 0.29756  0.07670  0.52970  113 ASN A OD1 
605  N ND2 . ASN A 77  ? 1.85563 1.88424 2.31197 0.30442  0.01647  0.55165  113 ASN A ND2 
606  N N   . ILE A 78  ? 1.46005 1.41316 1.92062 0.24808  0.16086  0.45492  114 ILE A N   
607  C CA  . ILE A 78  ? 1.46630 1.40962 1.90410 0.23124  0.18098  0.42220  114 ILE A CA  
608  C C   . ILE A 78  ? 1.41244 1.37342 1.86950 0.21528  0.16667  0.35111  114 ILE A C   
609  O O   . ILE A 78  ? 1.35491 1.31818 1.89733 0.21577  0.16438  0.32380  114 ILE A O   
610  C CB  . ILE A 78  ? 1.43228 1.34287 1.95520 0.23296  0.21919  0.44315  114 ILE A CB  
611  C CG1 . ILE A 78  ? 1.55863 1.44820 2.06466 0.25090  0.23763  0.52130  114 ILE A CG1 
612  C CG2 . ILE A 78  ? 1.37064 1.27121 1.87429 0.21633  0.23711  0.41331  114 ILE A CG2 
613  C CD1 . ILE A 78  ? 1.65630 1.51109 2.22373 0.25140  0.28378  0.54906  114 ILE A CD1 
614  N N   . LEU A 79  ? 1.36262 1.33437 1.73953 0.20121  0.15885  0.32165  115 LEU A N   
615  C CA  . LEU A 79  ? 1.38586 1.37038 1.76428 0.18539  0.14652  0.25991  115 LEU A CA  
616  C C   . LEU A 79  ? 1.40938 1.38137 1.77160 0.17089  0.15764  0.24039  115 LEU A C   
617  O O   . LEU A 79  ? 1.22205 1.19250 1.51815 0.16835  0.16400  0.26004  115 LEU A O   
618  C CB  . LEU A 79  ? 1.29210 1.30585 1.59744 0.18230  0.12059  0.24215  115 LEU A CB  
619  C CG  . LEU A 79  ? 1.27176 1.29648 1.55462 0.16526  0.11101  0.18629  115 LEU A CG  
620  C CD1 . LEU A 79  ? 1.27971 1.29625 1.63876 0.16152  0.11581  0.14770  115 LEU A CD1 
621  C CD2 . LEU A 79  ? 1.33130 1.38365 1.55379 0.16363  0.09083  0.17533  115 LEU A CD2 
622  N N   . VAL A 80  ? 1.33786 1.30069 1.76314 0.16140  0.15852  0.19948  116 VAL A N   
623  C CA  . VAL A 80  ? 1.24415 1.19447 1.67593 0.14782  0.16289  0.17771  116 VAL A CA  
624  C C   . VAL A 80  ? 1.27594 1.24080 1.66781 0.13335  0.13701  0.12572  116 VAL A C   
625  O O   . VAL A 80  ? 1.24182 1.20972 1.66204 0.13133  0.12607  0.09016  116 VAL A O   
626  C CB  . VAL A 80  ? 1.19913 1.12391 1.74334 0.14888  0.18039  0.17387  116 VAL A CB  
627  C CG1 . VAL A 80  ? 1.24155 1.15713 1.80666 0.13333  0.17261  0.13690  116 VAL A CG1 
628  C CG2 . VAL A 80  ? 1.25184 1.15752 1.82705 0.16152  0.21316  0.23280  116 VAL A CG2 
629  N N   . ILE A 81  ? 1.23800 1.21032 1.56310 0.12341  0.12959  0.12211  117 ILE A N   
630  C CA  . ILE A 81  ? 1.23238 1.21370 1.52199 0.10907  0.10618  0.07985  117 ILE A CA  
631  C C   . ILE A 81  ? 1.21215 1.18258 1.50718 0.09790  0.10570  0.07599  117 ILE A C   
632  O O   . ILE A 81  ? 1.14300 1.09672 1.48295 0.10076  0.12755  0.09978  117 ILE A O   
633  C CB  . ILE A 81  ? 1.24553 1.25244 1.45256 0.10767  0.09307  0.07685  117 ILE A CB  
634  C CG1 . ILE A 81  ? 1.27037 1.28687 1.42843 0.11387  0.10202  0.11491  117 ILE A CG1 
635  C CG2 . ILE A 81  ? 1.26513 1.28200 1.48264 0.11417  0.08915  0.06263  117 ILE A CG2 
636  C CD1 . ILE A 81  ? 1.28030 1.32268 1.36915 0.11106  0.08671  0.10772  117 ILE A CD1 
637  N N   . ASP A 82  ? 1.22640 1.20503 1.48086 0.08533  0.08281  0.04824  118 ASP A N   
638  C CA  . ASP A 82  ? 1.10013 1.06970 1.37006 0.07417  0.07724  0.04272  118 ASP A CA  
639  C C   . ASP A 82  ? 1.11419 1.08997 1.34595 0.07414  0.09629  0.07245  118 ASP A C   
640  O O   . ASP A 82  ? 1.04801 1.04324 1.21032 0.07589  0.09433  0.08058  118 ASP A O   
641  C CB  . ASP A 82  ? 1.14495 1.12059 1.38042 0.06170  0.04373  0.00870  118 ASP A CB  
642  C CG  . ASP A 82  ? 1.12902 1.08992 1.41007 0.05831  0.02250  -0.02648 118 ASP A CG  
643  O OD1 . ASP A 82  ? 1.21150 1.15462 1.57664 0.06055  0.02954  -0.02775 118 ASP A OD1 
644  O OD2 . ASP A 82  ? 1.23106 1.19697 1.46369 0.05336  0.00009  -0.05394 118 ASP A OD2 
645  N N   . LEU A 83  ? 1.01809 0.97645 1.30037 0.07200  0.11666  0.08598  119 LEU A N   
646  C CA  . LEU A 83  ? 1.09711 1.05788 1.34700 0.06818  0.13589  0.10379  119 LEU A CA  
647  C C   . LEU A 83  ? 0.96355 0.93641 1.19028 0.05423  0.11011  0.08009  119 LEU A C   
648  O O   . LEU A 83  ? 0.94463 0.91342 1.20503 0.04623  0.08178  0.05494  119 LEU A O   
649  C CB  . LEU A 83  ? 1.05195 0.98739 1.37363 0.06857  0.17053  0.12177  119 LEU A CB  
650  C CG  . LEU A 83  ? 1.07814 1.00881 1.37748 0.06493  0.20342  0.13982  119 LEU A CG  
651  C CD1 . LEU A 83  ? 1.05204 0.98380 1.27851 0.07741  0.23191  0.17449  119 LEU A CD1 
652  C CD2 . LEU A 83  ? 1.18166 1.08603 1.58177 0.05995  0.23029  0.14253  119 LEU A CD2 
653  N N   . LEU A 84  ? 1.03608 1.02335 1.20463 0.05162  0.11801  0.08830  120 LEU A N   
654  C CA  . LEU A 84  ? 0.95948 0.95957 1.10989 0.03918  0.09617  0.07034  120 LEU A CA  
655  C C   . LEU A 84  ? 1.02778 1.02751 1.17567 0.03385  0.12191  0.07936  120 LEU A C   
656  O O   . LEU A 84  ? 1.07324 1.06282 1.21603 0.04014  0.15734  0.09902  120 LEU A O   
657  C CB  . LEU A 84  ? 1.05549 1.07941 1.13686 0.04026  0.07408  0.06161  120 LEU A CB  
658  C CG  . LEU A 84  ? 1.01484 1.03807 1.09712 0.04036  0.04723  0.04281  120 LEU A CG  
659  C CD1 . LEU A 84  ? 0.87234 0.91712 0.89225 0.04347  0.03854  0.03880  120 LEU A CD1 
660  C CD2 . LEU A 84  ? 0.96069 0.97490 1.07225 0.02825  0.01986  0.02394  120 LEU A CD2 
661  N N   . GLY A 85  ? 1.02812 1.03746 1.17887 0.02212  0.10574  0.06517  121 GLY A N   
662  C CA  . GLY A 85  ? 1.00947 1.01903 1.16920 0.01504  0.12966  0.06663  121 GLY A CA  
663  C C   . GLY A 85  ? 1.02080 1.04940 1.10142 0.01896  0.14233  0.07051  121 GLY A C   
664  O O   . GLY A 85  ? 1.00497 1.04494 1.02881 0.02904  0.13505  0.07733  121 GLY A O   
665  N N   . PRO A 86  ? 1.12751 1.16011 1.21032 0.01084  0.15983  0.06345  122 PRO A N   
666  C CA  . PRO A 86  ? 1.07539 1.12509 1.08516 0.01399  0.17120  0.06145  122 PRO A CA  
667  C C   . PRO A 86  ? 0.96417 1.04125 0.93451 0.01444  0.13639  0.05148  122 PRO A C   
668  O O   . PRO A 86  ? 0.92129 1.00356 0.91613 0.00987  0.10810  0.04549  122 PRO A O   
669  C CB  . PRO A 86  ? 1.15591 1.20229 1.19774 0.00222  0.19631  0.04805  122 PRO A CB  
670  C CG  . PRO A 86  ? 1.35870 1.38050 1.49111 -0.00372 0.20971  0.05151  122 PRO A CG  
671  C CD  . PRO A 86  ? 1.16269 1.18317 1.32364 -0.00149 0.17100  0.05471  122 PRO A CD  
672  N N   . SER A 87  ? 0.95469 1.04811 0.86184 0.02027  0.13939  0.04973  123 SER A N   
673  C CA  . SER A 87  ? 1.07117 1.19151 0.95113 0.02086  0.11135  0.03915  123 SER A CA  
674  C C   . SER A 87  ? 0.99437 1.12864 0.90152 0.00765  0.10764  0.01928  123 SER A C   
675  O O   . SER A 87  ? 0.89748 1.02285 0.83496 -0.00088 0.12877  0.01148  123 SER A O   
676  C CB  . SER A 87  ? 0.95040 1.08389 0.76373 0.03290  0.10939  0.04352  123 SER A CB  
677  O OG  . SER A 87  ? 0.91016 1.04515 0.69125 0.03055  0.12861  0.03377  123 SER A OG  
678  N N   . LEU A 88  ? 0.95670 1.11224 0.86080 0.00601  0.08365  0.01156  124 LEU A N   
679  C CA  . LEU A 88  ? 0.89177 1.06276 0.82583 -0.00527 0.08038  -0.00508 124 LEU A CA  
680  C C   . LEU A 88  ? 0.91058 1.09177 0.82104 -0.00580 0.09720  -0.02257 124 LEU A C   
681  O O   . LEU A 88  ? 0.95830 1.14404 0.90724 -0.01672 0.10705  -0.03933 124 LEU A O   
682  C CB  . LEU A 88  ? 0.79581 0.98634 0.73006 -0.00540 0.05696  -0.00680 124 LEU A CB  
683  C CG  . LEU A 88  ? 0.84247 1.02190 0.79040 -0.00699 0.04112  0.00609  124 LEU A CG  
684  C CD1 . LEU A 88  ? 0.94231 1.13922 0.88505 -0.00742 0.02773  0.00493  124 LEU A CD1 
685  C CD2 . LEU A 88  ? 0.84323 1.00639 0.84207 -0.01815 0.03907  0.00947  124 LEU A CD2 
686  N N   . GLU A 89  ? 0.85792 1.04180 0.70553 0.00598  0.09946  -0.01965 125 GLU A N   
687  C CA  . GLU A 89  ? 0.96123 1.15042 0.76837 0.00641  0.11420  -0.03737 125 GLU A CA  
688  C C   . GLU A 89  ? 1.03482 1.19855 0.84777 0.00114  0.15245  -0.03720 125 GLU A C   
689  O O   . GLU A 89  ? 1.06677 1.23244 0.87891 -0.00640 0.17233  -0.06103 125 GLU A O   
690  C CB  . GLU A 89  ? 0.98197 1.17819 0.71464 0.02178  0.10044  -0.02926 125 GLU A CB  
691  C CG  . GLU A 89  ? 1.03430 1.23220 0.70246 0.02424  0.11143  -0.04619 125 GLU A CG  
692  C CD  . GLU A 89  ? 1.09522 1.31921 0.78077 0.01578  0.09909  -0.08387 125 GLU A CD  
693  O OE1 . GLU A 89  ? 1.08756 1.33126 0.83097 0.01098  0.07845  -0.09108 125 GLU A OE1 
694  O OE2 . GLU A 89  ? 1.07143 1.29491 0.71265 0.01389  0.11218  -0.10714 125 GLU A OE2 
695  N N   . ASP A 90  ? 0.99893 1.13797 0.82509 0.00464  0.16603  -0.01307 126 ASP A N   
696  C CA  . ASP A 90  ? 1.03717 1.14999 0.88767 -0.00093 0.20681  -0.01143 126 ASP A CA  
697  C C   . ASP A 90  ? 1.05501 1.16877 0.99182 -0.01711 0.21387  -0.03028 126 ASP A C   
698  O O   . ASP A 90  ? 1.06323 1.17051 1.01347 -0.02498 0.24646  -0.04887 126 ASP A O   
699  C CB  . ASP A 90  ? 1.11634 1.20408 0.98554 0.00579  0.21609  0.01744  126 ASP A CB  
700  C CG  . ASP A 90  ? 1.13350 1.21313 0.92510 0.02168  0.22234  0.04024  126 ASP A CG  
701  O OD1 . ASP A 90  ? 1.30229 1.38042 1.02324 0.02575  0.24077  0.03677  126 ASP A OD1 
702  O OD2 . ASP A 90  ? 1.03239 1.10631 0.83317 0.03029  0.20778  0.06145  126 ASP A OD2 
703  N N   . LEU A 91  ? 1.00965 1.12999 1.00554 -0.02214 0.18402  -0.02528 127 LEU A N   
704  C CA  . LEU A 91  ? 0.99913 1.12097 1.08165 -0.03653 0.18292  -0.03738 127 LEU A CA  
705  C C   . LEU A 91  ? 1.04174 1.18680 1.12598 -0.04340 0.18278  -0.06375 127 LEU A C   
706  O O   . LEU A 91  ? 1.04034 1.18436 1.19412 -0.05540 0.19788  -0.07953 127 LEU A O   
707  C CB  . LEU A 91  ? 0.93289 1.05583 1.05829 -0.03869 0.14528  -0.02252 127 LEU A CB  
708  C CG  . LEU A 91  ? 0.98293 1.08617 1.10650 -0.03144 0.13682  -0.00217 127 LEU A CG  
709  C CD1 . LEU A 91  ? 1.03699 1.14480 1.16985 -0.03200 0.09573  0.00692  127 LEU A CD1 
710  C CD2 . LEU A 91  ? 1.08011 1.15807 1.27462 -0.03685 0.16088  0.00030  127 LEU A CD2 
711  N N   . PHE A 92  ? 0.98777 1.15422 1.00816 -0.03603 0.16501  -0.07027 128 PHE A N   
712  C CA  . PHE A 92  ? 1.00953 1.19971 1.03723 -0.04190 0.16224  -0.09919 128 PHE A CA  
713  C C   . PHE A 92  ? 1.05937 1.24212 1.07779 -0.04732 0.20035  -0.12658 128 PHE A C   
714  O O   . PHE A 92  ? 1.02170 1.20927 1.10766 -0.05970 0.21400  -0.14987 128 PHE A O   
715  C CB  . PHE A 92  ? 1.02788 1.24053 0.99202 -0.03134 0.13556  -0.10179 128 PHE A CB  
716  C CG  . PHE A 92  ? 0.98510 1.22446 0.96715 -0.03664 0.12701  -0.13344 128 PHE A CG  
717  C CD1 . PHE A 92  ? 0.91309 1.16567 0.97652 -0.04673 0.11668  -0.13790 128 PHE A CD1 
718  C CD2 . PHE A 92  ? 1.03738 1.28813 0.95551 -0.03088 0.12662  -0.15783 128 PHE A CD2 
719  C CE1 . PHE A 92  ? 0.99559 1.27295 1.08924 -0.05157 0.11031  -0.16768 128 PHE A CE1 
720  C CE2 . PHE A 92  ? 1.05288 1.32926 0.99612 -0.03583 0.11538  -0.19208 128 PHE A CE2 
721  C CZ  . PHE A 92  ? 0.99050 1.28059 1.02772 -0.04639 0.10915  -0.19770 128 PHE A CZ  
722  N N   . ASP A 93  ? 1.13837 1.30706 1.07386 -0.03813 0.22062  -0.12308 129 ASP A N   
723  C CA  . ASP A 93  ? 1.24181 1.39817 1.14993 -0.04268 0.26329  -0.14848 129 ASP A CA  
724  C C   . ASP A 93  ? 1.22955 1.36510 1.23100 -0.05543 0.30044  -0.15192 129 ASP A C   
725  O O   . ASP A 93  ? 1.23461 1.37023 1.27107 -0.06633 0.32963  -0.18486 129 ASP A O   
726  C CB  . ASP A 93  ? 1.35237 1.49092 1.14978 -0.02912 0.27953  -0.13210 129 ASP A CB  
727  C CG  . ASP A 93  ? 1.62319 1.74788 1.36193 -0.03229 0.32408  -0.15941 129 ASP A CG  
728  O OD1 . ASP A 93  ? 1.64995 1.75589 1.44598 -0.04339 0.36903  -0.17137 129 ASP A OD1 
729  O OD2 . ASP A 93  ? 1.67002 1.80157 1.30431 -0.02351 0.31380  -0.16975 129 ASP A OD2 
730  N N   . TRP A 94  ? 1.24952 1.36731 1.30069 -0.05444 0.29875  -0.12100 130 TRP A N   
731  C CA  . TRP A 94  ? 1.32854 1.42473 1.47781 -0.06531 0.33177  -0.12223 130 TRP A CA  
732  C C   . TRP A 94  ? 1.17084 1.28159 1.42997 -0.07924 0.31729  -0.13891 130 TRP A C   
733  O O   . TRP A 94  ? 0.99913 1.09817 1.34185 -0.09052 0.35093  -0.15518 130 TRP A O   
734  C CB  . TRP A 94  ? 1.32807 1.40329 1.50886 -0.06000 0.32527  -0.08727 130 TRP A CB  
735  C CG  . TRP A 94  ? 1.53748 1.59607 1.62631 -0.04620 0.34325  -0.06656 130 TRP A CG  
736  C CD1 . TRP A 94  ? 1.70553 1.76104 1.68906 -0.03908 0.36908  -0.07343 130 TRP A CD1 
737  C CD2 . TRP A 94  ? 1.61004 1.65199 1.70556 -0.03744 0.33473  -0.03451 130 TRP A CD2 
738  N NE1 . TRP A 94  ? 1.80994 1.84717 1.73576 -0.02595 0.37798  -0.04212 130 TRP A NE1 
739  C CE2 . TRP A 94  ? 1.71888 1.74812 1.71807 -0.02500 0.35906  -0.01943 130 TRP A CE2 
740  C CE3 . TRP A 94  ? 1.64603 1.68189 1.81964 -0.03880 0.30710  -0.01830 130 TRP A CE3 
741  C CZ2 . TRP A 94  ? 1.70195 1.71340 1.69309 -0.01413 0.36000  0.01243  130 TRP A CZ2 
742  C CZ3 . TRP A 94  ? 1.69627 1.71518 1.85865 -0.02856 0.30688  0.00707  130 TRP A CZ3 
743  C CH2 . TRP A 94  ? 1.72041 1.72758 1.79841 -0.01647 0.33498  0.02281  130 TRP A CH2 
744  N N   . CYS A 95  ? 1.01368 1.14852 1.27943 -0.07858 0.27074  -0.13364 131 CYS A N   
745  C CA  . CYS A 95  ? 0.92710 1.07644 1.29177 -0.09050 0.25510  -0.14391 131 CYS A CA  
746  C C   . CYS A 95  ? 0.98712 1.15597 1.35283 -0.09692 0.27068  -0.18412 131 CYS A C   
747  O O   . CYS A 95  ? 1.04397 1.23082 1.48102 -0.10454 0.25210  -0.19154 131 CYS A O   
748  C CB  . CYS A 95  ? 0.88961 1.05283 1.25844 -0.08694 0.20374  -0.11764 131 CYS A CB  
749  S SG  . CYS A 95  ? 0.85800 0.99891 1.25696 -0.08380 0.17781  -0.07862 131 CYS A SG  
750  N N   . GLY A 96  ? 0.95695 1.12155 1.24484 -0.09387 0.30358  -0.21004 132 GLY A N   
751  C CA  . GLY A 96  ? 1.07994 1.26259 1.35984 -0.09965 0.31576  -0.25516 132 GLY A CA  
752  C C   . GLY A 96  ? 1.05770 1.26801 1.26643 -0.09128 0.27780  -0.26333 132 GLY A C   
753  O O   . GLY A 96  ? 1.03676 1.26825 1.27161 -0.09734 0.27424  -0.30005 132 GLY A O   
754  N N   . ARG A 97  ? 1.10718 1.31811 1.23798 -0.07765 0.24962  -0.23204 133 ARG A N   
755  C CA  . ARG A 97  ? 1.04702 1.28364 1.12202 -0.06859 0.21148  -0.23575 133 ARG A CA  
756  C C   . ARG A 97  ? 1.05578 1.31751 1.22026 -0.07579 0.18571  -0.24200 133 ARG A C   
757  O O   . ARG A 97  ? 1.00265 1.28916 1.15816 -0.07410 0.16673  -0.26626 133 ARG A O   
758  C CB  . ARG A 97  ? 1.13983 1.38329 1.12389 -0.06396 0.21898  -0.27214 133 ARG A CB  
759  C CG  . ARG A 97  ? 1.17941 1.39601 1.05886 -0.05476 0.24453  -0.25860 133 ARG A CG  
760  C CD  . ARG A 97  ? 1.25341 1.47930 1.01681 -0.04468 0.23036  -0.28011 133 ARG A CD  
761  N NE  . ARG A 97  ? 1.21382 1.46642 0.96485 -0.03493 0.17755  -0.27092 133 ARG A NE  
762  C CZ  . ARG A 97  ? 1.19582 1.44522 0.90723 -0.02170 0.15426  -0.23035 133 ARG A CZ  
763  N NH1 . ARG A 97  ? 1.25091 1.47231 0.93054 -0.01610 0.17588  -0.19404 133 ARG A NH1 
764  N NH2 . ARG A 97  ? 1.09933 1.37397 0.81358 -0.01412 0.11043  -0.22759 133 ARG A NH2 
765  N N   . ARG A 98  ? 1.08054 1.33483 1.33449 -0.08347 0.18391  -0.21852 134 ARG A N   
766  C CA  . ARG A 98  ? 1.04105 1.31335 1.37728 -0.08927 0.16080  -0.21095 134 ARG A CA  
767  C C   . ARG A 98  ? 1.04770 1.30342 1.42606 -0.09071 0.14774  -0.16736 134 ARG A C   
768  O O   . ARG A 98  ? 1.06688 1.30017 1.47075 -0.09437 0.16351  -0.15770 134 ARG A O   
769  C CB  . ARG A 98  ? 1.00367 1.28759 1.43718 -0.10287 0.17793  -0.24642 134 ARG A CB  
770  C CG  . ARG A 98  ? 1.08892 1.39662 1.49841 -0.10243 0.17785  -0.29365 134 ARG A CG  
771  C CD  . ARG A 98  ? 1.13455 1.46049 1.66462 -0.11484 0.18151  -0.31971 134 ARG A CD  
772  N NE  . ARG A 98  ? 1.14307 1.47592 1.74424 -0.11603 0.15828  -0.28070 134 ARG A NE  
773  C CZ  . ARG A 98  ? 1.11071 1.46255 1.81178 -0.12326 0.15327  -0.29032 134 ARG A CZ  
774  N NH1 . ARG A 98  ? 1.12095 1.48967 1.87248 -0.13039 0.16671  -0.34285 134 ARG A NH1 
775  N NH2 . ARG A 98  ? 1.19443 1.54706 1.94497 -0.12327 0.13555  -0.24664 134 ARG A NH2 
776  N N   . PHE A 99  ? 0.84619 1.11187 1.23175 -0.08780 0.11923  -0.14247 135 PHE A N   
777  C CA  . PHE A 99  ? 0.83108 1.08141 1.24311 -0.08882 0.10067  -0.10240 135 PHE A CA  
778  C C   . PHE A 99  ? 0.79601 1.05551 1.29956 -0.09794 0.09006  -0.09135 135 PHE A C   
779  O O   . PHE A 99  ? 0.94704 1.22837 1.47273 -0.09910 0.08931  -0.10503 135 PHE A O   
780  C CB  . PHE A 99  ? 0.71716 0.96521 1.04714 -0.07709 0.07944  -0.07765 135 PHE A CB  
781  C CG  . PHE A 99  ? 0.93079 1.15965 1.19555 -0.06902 0.08430  -0.07034 135 PHE A CG  
782  C CD1 . PHE A 99  ? 0.90075 1.11129 1.18918 -0.07308 0.10559  -0.07686 135 PHE A CD1 
783  C CD2 . PHE A 99  ? 0.89398 1.12219 1.08416 -0.05744 0.07087  -0.05647 135 PHE A CD2 
784  C CE1 . PHE A 99  ? 0.92109 1.11276 1.15917 -0.06544 0.11356  -0.06748 135 PHE A CE1 
785  C CE2 . PHE A 99  ? 0.95153 1.16180 1.09289 -0.04978 0.07635  -0.04819 135 PHE A CE2 
786  C CZ  . PHE A 99  ? 0.87223 1.06403 1.03734 -0.05364 0.09775  -0.05248 135 PHE A CZ  
787  N N   . SER A 100 ? 0.85831 1.10051 1.42029 -0.10397 0.08004  -0.06495 136 SER A N   
788  C CA  . SER A 100 ? 0.85460 1.10117 1.49933 -0.11137 0.06613  -0.04360 136 SER A CA  
789  C C   . SER A 100 ? 0.85359 1.10563 1.44595 -0.10482 0.04571  -0.01530 136 SER A C   
790  O O   . SER A 100 ? 0.81467 1.06364 1.31385 -0.09511 0.03898  -0.00989 136 SER A O   
791  C CB  . SER A 100 ? 0.78380 1.00833 1.49626 -0.11774 0.05218  -0.01760 136 SER A CB  
792  O OG  . SER A 100 ? 0.81263 1.01913 1.45912 -0.11100 0.02470  0.01405  136 SER A OG  
793  N N   . VAL A 101 ? 0.78084 1.03956 1.43987 -0.11035 0.03942  0.00397  137 VAL A N   
794  C CA  . VAL A 101 ? 0.79890 1.06082 1.41527 -0.10511 0.02869  0.03201  137 VAL A CA  
795  C C   . VAL A 101 ? 0.85729 1.09429 1.40169 -0.10031 0.00445  0.06945  137 VAL A C   
796  O O   . VAL A 101 ? 0.76822 1.00334 1.23197 -0.09266 0.00111  0.08085  137 VAL A O   
797  C CB  . VAL A 101 ? 0.94307 1.21514 1.65535 -0.11237 0.03242  0.04784  137 VAL A CB  
798  C CG1 . VAL A 101 ? 0.68726 0.95497 1.35529 -0.10756 0.02567  0.08639  137 VAL A CG1 
799  C CG2 . VAL A 101 ? 0.87020 1.16986 1.64546 -0.11586 0.05514  0.00301  137 VAL A CG2 
800  N N   . LYS A 102 ? 0.87843 1.09567 1.45460 -0.10476 -0.01323 0.08558  138 LYS A N   
801  C CA  . LYS A 102 ? 0.86959 1.06263 1.37952 -0.10060 -0.04239 0.11639  138 LYS A CA  
802  C C   . LYS A 102 ? 0.89763 1.08567 1.31314 -0.09154 -0.03980 0.09859  138 LYS A C   
803  O O   . LYS A 102 ? 0.91389 1.09213 1.24706 -0.08520 -0.05164 0.11371  138 LYS A O   
804  C CB  . LYS A 102 ? 0.94677 1.12133 1.52643 -0.10717 -0.06677 0.13289  138 LYS A CB  
805  C CG  . LYS A 102 ? 1.04076 1.18972 1.55864 -0.10334 -0.10436 0.15895  138 LYS A CG  
806  C CD  . LYS A 102 ? 1.07007 1.20304 1.67694 -0.10989 -0.13268 0.17249  138 LYS A CD  
807  C CE  . LYS A 102 ? 1.11073 1.21839 1.65878 -0.10620 -0.17850 0.19626  138 LYS A CE  
808  N NZ  . LYS A 102 ? 1.07706 1.16960 1.72335 -0.11217 -0.21353 0.21058  138 LYS A NZ  
809  N N   . THR A 103 ? 0.81465 1.00778 1.24097 -0.09076 -0.02163 0.06692  139 THR A N   
810  C CA  . THR A 103 ? 0.96835 1.15465 1.31612 -0.08181 -0.01845 0.05455  139 THR A CA  
811  C C   . THR A 103 ? 0.82930 1.02988 1.10293 -0.07309 -0.00928 0.04840  139 THR A C   
812  O O   . THR A 103 ? 0.81393 1.00459 1.01718 -0.06572 -0.01819 0.05630  139 THR A O   
813  C CB  . THR A 103 ? 0.88973 1.07652 1.26436 -0.08277 0.00460  0.02648  139 THR A CB  
814  O OG1 . THR A 103 ? 0.95917 1.13002 1.41197 -0.09059 -0.00202 0.03228  139 THR A OG1 
815  C CG2 . THR A 103 ? 0.97316 1.15250 1.27019 -0.07254 0.01029  0.01876  139 THR A CG2 
816  N N   . VAL A 104 ? 0.87917 1.10321 1.17694 -0.07401 0.00786  0.03179  140 VAL A N   
817  C CA  . VAL A 104 ? 0.85684 1.09671 1.10199 -0.06551 0.01552  0.02241  140 VAL A CA  
818  C C   . VAL A 104 ? 0.78795 1.02081 0.99689 -0.06300 0.00714  0.04962  140 VAL A C   
819  O O   . VAL A 104 ? 0.85591 1.09027 1.00599 -0.05456 0.01027  0.04784  140 VAL A O   
820  C CB  . VAL A 104 ? 0.78674 1.05368 1.08011 -0.06793 0.03027  -0.00385 140 VAL A CB  
821  C CG1 . VAL A 104 ? 0.78934 1.06075 1.08879 -0.06861 0.04189  -0.03533 140 VAL A CG1 
822  C CG2 . VAL A 104 ? 0.90911 1.18168 1.28732 -0.07793 0.03160  0.00761  140 VAL A CG2 
823  N N   . VAL A 105 ? 0.83428 1.05760 1.07735 -0.07011 -0.00198 0.07626  141 VAL A N   
824  C CA  . VAL A 105 ? 0.87081 1.08076 1.06661 -0.06843 -0.00816 0.10637  141 VAL A CA  
825  C C   . VAL A 105 ? 0.96873 1.15535 1.08160 -0.06309 -0.02414 0.11372  141 VAL A C   
826  O O   . VAL A 105 ? 0.93855 1.12327 0.98811 -0.05630 -0.01526 0.11222  141 VAL A O   
827  C CB  . VAL A 105 ? 0.95143 1.15096 1.19538 -0.07683 -0.01963 0.13956  141 VAL A CB  
828  C CG1 . VAL A 105 ? 0.87817 1.05759 1.04987 -0.07450 -0.02612 0.17309  141 VAL A CG1 
829  C CG2 . VAL A 105 ? 0.87165 1.09373 1.20459 -0.08211 -0.00063 0.13501  141 VAL A CG2 
830  N N   . GLN A 106 ? 1.00142 1.17084 1.12509 -0.06630 -0.04666 0.11778  142 GLN A N   
831  C CA  . GLN A 106 ? 1.01104 1.15757 1.06948 -0.06216 -0.06674 0.12086  142 GLN A CA  
832  C C   . GLN A 106 ? 0.95190 1.10493 0.97101 -0.05326 -0.05125 0.09489  142 GLN A C   
833  O O   . GLN A 106 ? 0.96737 1.10805 0.92195 -0.04751 -0.05553 0.09324  142 GLN A O   
834  C CB  . GLN A 106 ? 0.99900 1.12956 1.10336 -0.06749 -0.09380 0.12555  142 GLN A CB  
835  C CG  . GLN A 106 ? 1.10596 1.23314 1.27487 -0.07632 -0.11028 0.15147  142 GLN A CG  
836  C CD  . GLN A 106 ? 1.16714 1.27770 1.39130 -0.08110 -0.14104 0.15639  142 GLN A CD  
837  O OE1 . GLN A 106 ? 1.29022 1.37936 1.48316 -0.08128 -0.17768 0.17517  142 GLN A OE1 
838  N NE2 . GLN A 106 ? 1.10435 1.22359 1.41171 -0.08499 -0.12645 0.13771  142 GLN A NE2 
839  N N   . VAL A 107 ? 0.79910 0.97061 0.85499 -0.05180 -0.03315 0.07442  143 VAL A N   
840  C CA  . VAL A 107 ? 0.87768 1.05608 0.89628 -0.04221 -0.01988 0.05551  143 VAL A CA  
841  C C   . VAL A 107 ? 1.00273 1.19237 0.98245 -0.03609 -0.00801 0.05507  143 VAL A C   
842  O O   . VAL A 107 ? 0.92453 1.10827 0.85755 -0.02824 -0.00568 0.05020  143 VAL A O   
843  C CB  . VAL A 107 ? 0.78305 0.97653 0.83838 -0.04197 -0.00489 0.03587  143 VAL A CB  
844  C CG1 . VAL A 107 ? 0.99632 1.20228 1.01173 -0.03120 0.00669  0.02174  143 VAL A CG1 
845  C CG2 . VAL A 107 ? 0.87670 1.05342 0.95932 -0.04506 -0.00810 0.03368  143 VAL A CG2 
846  N N   . ALA A 108 ? 0.89806 1.10301 0.90723 -0.03985 0.00156  0.06006  144 ALA A N   
847  C CA  . ALA A 108 ? 0.96036 1.17777 0.95200 -0.03433 0.01755  0.05776  144 ALA A CA  
848  C C   . ALA A 108 ? 0.99215 1.18912 0.92215 -0.03213 0.01900  0.07210  144 ALA A C   
849  O O   . ALA A 108 ? 1.02124 1.22133 0.92292 -0.02478 0.03260  0.06360  144 ALA A O   
850  C CB  . ALA A 108 ? 0.90626 1.14233 0.95738 -0.03986 0.02887  0.06106  144 ALA A CB  
851  N N   . ILE A 109 ? 0.94759 1.12251 0.85604 -0.03833 0.00426  0.09264  145 ILE A N   
852  C CA  . ILE A 109 ? 1.07657 1.22905 0.91156 -0.03659 0.00490  0.10286  145 ILE A CA  
853  C C   . ILE A 109 ? 1.06374 1.20459 0.85585 -0.02994 -0.00287 0.08376  145 ILE A C   
854  O O   . ILE A 109 ? 1.09955 1.23105 0.84025 -0.02533 0.00995  0.07738  145 ILE A O   
855  C CB  . ILE A 109 ? 1.13932 1.26955 0.95365 -0.04424 -0.01584 0.13120  145 ILE A CB  
856  C CG1 . ILE A 109 ? 1.12643 1.26805 0.99497 -0.05033 -0.00417 0.15413  145 ILE A CG1 
857  C CG2 . ILE A 109 ? 1.27281 1.37473 0.98909 -0.04215 -0.01990 0.13611  145 ILE A CG2 
858  C CD1 . ILE A 109 ? 0.99378 1.13670 0.93023 -0.05787 -0.02735 0.16612  145 ILE A CD1 
859  N N   . GLN A 110 ? 1.03241 1.17307 0.85183 -0.02934 -0.01928 0.07343  146 GLN A N   
860  C CA  . GLN A 110 ? 1.04981 1.17969 0.84301 -0.02266 -0.02408 0.05698  146 GLN A CA  
861  C C   . GLN A 110 ? 1.00211 1.14931 0.79947 -0.01318 -0.00178 0.04224  146 GLN A C   
862  O O   . GLN A 110 ? 1.04728 1.18618 0.81270 -0.00700 0.00499  0.03208  146 GLN A O   
863  C CB  . GLN A 110 ? 0.93504 1.05791 0.76579 -0.02462 -0.04271 0.05340  146 GLN A CB  
864  C CG  . GLN A 110 ? 1.07034 1.17488 0.90973 -0.03322 -0.07181 0.06702  146 GLN A CG  
865  C CD  . GLN A 110 ? 1.17758 1.26795 1.04956 -0.03356 -0.09081 0.05872  146 GLN A CD  
866  O OE1 . GLN A 110 ? 1.25446 1.34295 1.12589 -0.02680 -0.08185 0.04405  146 GLN A OE1 
867  N NE2 . GLN A 110 ? 1.08428 1.16401 0.99436 -0.04121 -0.11679 0.06980  146 GLN A NE2 
868  N N   . MET A 111 ? 0.90058 1.07163 0.74009 -0.01181 0.00764  0.03942  147 MET A N   
869  C CA  . MET A 111 ? 0.99923 1.18791 0.84557 -0.00217 0.02161  0.02774  147 MET A CA  
870  C C   . MET A 111 ? 0.97298 1.16410 0.80331 0.00033  0.03958  0.02734  147 MET A C   
871  O O   . MET A 111 ? 0.99070 1.18169 0.81135 0.00859  0.04872  0.01790  147 MET A O   
872  C CB  . MET A 111 ? 0.98179 1.19509 0.87073 -0.00209 0.02289  0.02224  147 MET A CB  
873  C CG  . MET A 111 ? 0.85546 1.06485 0.76088 -0.00571 0.01390  0.02082  147 MET A CG  
874  S SD  . MET A 111 ? 0.96046 1.19705 0.90571 -0.00712 0.01776  0.00741  147 MET A SD  
875  C CE  . MET A 111 ? 0.96464 1.20577 0.88222 0.00602  0.01734  -0.00098 147 MET A CE  
876  N N   . LEU A 112 ? 0.96721 1.15896 0.80048 -0.00674 0.04815  0.03894  148 LEU A N   
877  C CA  . LEU A 112 ? 1.03764 1.22802 0.85662 -0.00525 0.07329  0.04066  148 LEU A CA  
878  C C   . LEU A 112 ? 1.05976 1.22377 0.81469 -0.00353 0.07853  0.03651  148 LEU A C   
879  O O   . LEU A 112 ? 1.09385 1.25734 0.84131 0.00149  0.10271  0.02700  148 LEU A O   
880  C CB  . LEU A 112 ? 1.08965 1.28068 0.92200 -0.01360 0.08391  0.05984  148 LEU A CB  
881  C CG  . LEU A 112 ? 1.00856 1.22889 0.91750 -0.01452 0.09088  0.05735  148 LEU A CG  
882  C CD1 . LEU A 112 ? 1.05355 1.27043 0.98346 -0.02381 0.09773  0.08037  148 LEU A CD1 
883  C CD2 . LEU A 112 ? 1.04746 1.28442 0.98795 -0.00709 0.11346  0.04426  148 LEU A CD2 
884  N N   . THR A 113 ? 1.05623 1.19811 0.77090 -0.00777 0.05595  0.04030  149 THR A N   
885  C CA  . THR A 113 ? 1.15130 1.26774 0.80461 -0.00638 0.05619  0.02952  149 THR A CA  
886  C C   . THR A 113 ? 1.08217 1.20216 0.75370 0.00282  0.05825  0.00806  149 THR A C   
887  O O   . THR A 113 ? 1.10576 1.21577 0.75250 0.00679  0.07634  -0.00723 149 THR A O   
888  C CB  . THR A 113 ? 1.18314 1.27624 0.79844 -0.01317 0.02367  0.03728  149 THR A CB  
889  O OG1 . THR A 113 ? 1.25182 1.33999 0.85119 -0.02089 0.02090  0.06263  149 THR A OG1 
890  C CG2 . THR A 113 ? 1.12722 1.19361 0.67622 -0.01202 0.01963  0.01979  149 THR A CG2 
891  N N   . LEU A 114 ? 1.05972 1.19231 0.77586 0.00637  0.04282  0.00751  150 LEU A N   
892  C CA  . LEU A 114 ? 0.99675 1.13291 0.73571 0.01624  0.04546  -0.00546 150 LEU A CA  
893  C C   . LEU A 114 ? 1.11693 1.27051 0.88093 0.02390  0.06922  -0.01135 150 LEU A C   
894  O O   . LEU A 114 ? 1.08536 1.23236 0.85013 0.03017  0.08193  -0.02463 150 LEU A O   
895  C CB  . LEU A 114 ? 0.96107 1.10647 0.73648 0.01859  0.02982  0.00078  150 LEU A CB  
896  C CG  . LEU A 114 ? 1.14607 1.27458 0.92006 0.01215  0.00851  0.00477  150 LEU A CG  
897  C CD1 . LEU A 114 ? 1.05895 1.19973 0.87013 0.01218  0.00442  0.01272  150 LEU A CD1 
898  C CD2 . LEU A 114 ? 1.15166 1.25918 0.91970 0.01573  0.00160  -0.00730 150 LEU A CD2 
899  N N   . VAL A 115 ? 1.07936 1.25561 0.87457 0.02337  0.07470  -0.00366 151 VAL A N   
900  C CA  . VAL A 115 ? 1.09321 1.28825 0.92797 0.03071  0.09269  -0.00976 151 VAL A CA  
901  C C   . VAL A 115 ? 1.11312 1.29553 0.92821 0.02886  0.12336  -0.01689 151 VAL A C   
902  O O   . VAL A 115 ? 1.05012 1.23793 0.89632 0.03614  0.14182  -0.02797 151 VAL A O   
903  C CB  . VAL A 115 ? 1.02776 1.24952 0.90596 0.02938  0.08814  -0.00397 151 VAL A CB  
904  C CG1 . VAL A 115 ? 1.02050 1.26243 0.95183 0.03676  0.10256  -0.01172 151 VAL A CG1 
905  C CG2 . VAL A 115 ? 0.80796 1.03981 0.69614 0.03162  0.06261  -0.00148 151 VAL A CG2 
906  N N   . GLU A 116 ? 1.10417 1.26793 0.86737 0.01935  0.13043  -0.00986 152 GLU A N   
907  C CA  . GLU A 116 ? 1.14046 1.28585 0.86502 0.01716  0.16365  -0.01678 152 GLU A CA  
908  C C   . GLU A 116 ? 1.21272 1.33944 0.91092 0.02161  0.16769  -0.03886 152 GLU A C   
909  O O   . GLU A 116 ? 1.30163 1.42405 1.00844 0.02510  0.20036  -0.05431 152 GLU A O   
910  C CB  . GLU A 116 ? 1.16045 1.28552 0.81938 0.00672  0.16465  -0.00029 152 GLU A CB  
911  C CG  . GLU A 116 ? 1.20103 1.30084 0.79640 0.00397  0.20095  -0.00642 152 GLU A CG  
912  C CD  . GLU A 116 ? 1.29728 1.37180 0.80955 -0.00524 0.19380  0.01360  152 GLU A CD  
913  O OE1 . GLU A 116 ? 1.30009 1.37474 0.80846 -0.00922 0.15476  0.02835  152 GLU A OE1 
914  O OE2 . GLU A 116 ? 1.33951 1.39262 0.79071 -0.00828 0.22807  0.01577  152 GLU A OE2 
915  N N   . GLU A 117 ? 1.15079 1.26603 0.82738 0.02133  0.13704  -0.04259 153 GLU A N   
916  C CA  . GLU A 117 ? 1.25355 1.35088 0.91574 0.02517  0.13881  -0.06619 153 GLU A CA  
917  C C   . GLU A 117 ? 1.19710 1.31093 0.93221 0.03660  0.14734  -0.07465 153 GLU A C   
918  O O   . GLU A 117 ? 1.25125 1.35379 0.99394 0.04069  0.16413  -0.09640 153 GLU A O   
919  C CB  . GLU A 117 ? 1.27303 1.35462 0.90984 0.02187  0.10244  -0.06743 153 GLU A CB  
920  C CG  . GLU A 117 ? 1.33095 1.38712 0.93586 0.02209  0.10193  -0.09597 153 GLU A CG  
921  C CD  . GLU A 117 ? 1.49514 1.52567 1.00887 0.01368  0.10915  -0.10620 153 GLU A CD  
922  O OE1 . GLU A 117 ? 1.51987 1.55201 0.99883 0.00856  0.12145  -0.08688 153 GLU A OE1 
923  O OE2 . GLU A 117 ? 1.53831 1.54578 1.01375 0.01230  0.10223  -0.13358 153 GLU A OE2 
924  N N   . VAL A 118 ? 1.16292 1.30247 0.95217 0.04201  0.13465  -0.05840 154 VAL A N   
925  C CA  . VAL A 118 ? 1.17793 1.33376 1.03462 0.05394  0.13784  -0.06079 154 VAL A CA  
926  C C   . VAL A 118 ? 1.26262 1.42620 1.15456 0.05658  0.17163  -0.07115 154 VAL A C   
927  O O   . VAL A 118 ? 1.14757 1.30779 1.07786 0.06349  0.18810  -0.08585 154 VAL A O   
928  C CB  . VAL A 118 ? 1.02366 1.20300 0.91410 0.05893  0.11182  -0.04133 154 VAL A CB  
929  C CG1 . VAL A 118 ? 1.04011 1.23748 0.99620 0.07198  0.11076  -0.03956 154 VAL A CG1 
930  C CG2 . VAL A 118 ? 1.11191 1.28052 0.97949 0.05761  0.08722  -0.03279 154 VAL A CG2 
931  N N   . HIS A 119 ? 1.12703 1.30053 1.01740 0.05099  0.18512  -0.06366 155 HIS A N   
932  C CA  . HIS A 119 ? 1.18434 1.36356 1.11658 0.05251  0.22319  -0.07292 155 HIS A CA  
933  C C   . HIS A 119 ? 1.31562 1.46592 1.20082 0.04811  0.26094  -0.09344 155 HIS A C   
934  O O   . HIS A 119 ? 1.33369 1.48388 1.26409 0.05163  0.29738  -0.10866 155 HIS A O   
935  C CB  . HIS A 119 ? 1.14784 1.34105 1.09165 0.04652  0.23218  -0.05911 155 HIS A CB  
936  C CG  . HIS A 119 ? 1.09274 1.31535 1.08632 0.05042  0.19765  -0.04670 155 HIS A CG  
937  N ND1 . HIS A 119 ? 0.96220 1.19846 0.96848 0.04423  0.19526  -0.03552 155 HIS A ND1 
938  C CD2 . HIS A 119 ? 1.00130 1.24072 1.03146 0.05988  0.16475  -0.04463 155 HIS A CD2 
939  C CE1 . HIS A 119 ? 0.97123 1.23209 1.01843 0.04920  0.16180  -0.03250 155 HIS A CE1 
940  N NE2 . HIS A 119 ? 0.97207 1.23438 1.02738 0.05892  0.14262  -0.03627 155 HIS A NE2 
941  N N   . ARG A 120 ? 1.37142 1.49630 1.16786 0.04035  0.25248  -0.09635 156 ARG A N   
942  C CA  . ARG A 120 ? 1.45061 1.54536 1.18749 0.03617  0.28284  -0.12096 156 ARG A CA  
943  C C   . ARG A 120 ? 1.48998 1.58056 1.27363 0.04408  0.28986  -0.14749 156 ARG A C   
944  O O   . ARG A 120 ? 1.53951 1.61083 1.30516 0.04244  0.32801  -0.17481 156 ARG A O   
945  C CB  . ARG A 120 ? 1.50379 1.57357 1.13905 0.02727  0.25866  -0.11900 156 ARG A CB  
946  C CG  . ARG A 120 ? 1.57725 1.62840 1.12962 0.01776  0.28228  -0.10907 156 ARG A CG  
947  C CD  . ARG A 120 ? 1.74705 1.76276 1.19408 0.01173  0.27616  -0.12865 156 ARG A CD  
948  N NE  . ARG A 120 ? 1.89842 1.90241 1.35767 0.01583  0.29883  -0.16801 156 ARG A NE  
949  C CZ  . ARG A 120 ? 1.96801 1.94566 1.36359 0.01300  0.28650  -0.19754 156 ARG A CZ  
950  N NH1 . ARG A 120 ? 2.00937 1.96902 1.32150 0.00647  0.24726  -0.19146 156 ARG A NH1 
951  N NH2 . ARG A 120 ? 1.96767 1.93718 1.39236 0.01690  0.31177  -0.23585 156 ARG A NH2 
952  N N   . HIS A 121 ? 1.36453 1.47109 1.20828 0.05260  0.25681  -0.13959 157 HIS A N   
953  C CA  . HIS A 121 ? 1.42839 1.53234 1.33191 0.06135  0.26098  -0.15825 157 HIS A CA  
954  C C   . HIS A 121 ? 1.38067 1.50961 1.39029 0.07219  0.27160  -0.15152 157 HIS A C   
955  O O   . HIS A 121 ? 1.30931 1.44286 1.38609 0.08208  0.26225  -0.15359 157 HIS A O   
956  C CB  . HIS A 121 ? 1.40482 1.50555 1.30906 0.06466  0.22014  -0.15060 157 HIS A CB  
957  C CG  . HIS A 121 ? 1.42906 1.50296 1.25212 0.05550  0.20766  -0.16591 157 HIS A CG  
958  N ND1 . HIS A 121 ? 1.37120 1.43934 1.12013 0.04605  0.18981  -0.15233 157 HIS A ND1 
959  C CD2 . HIS A 121 ? 1.46235 1.51377 1.27378 0.05453  0.20695  -0.19501 157 HIS A CD2 
960  C CE1 . HIS A 121 ? 1.40044 1.44375 1.09288 0.04005  0.17500  -0.17086 157 HIS A CE1 
961  N NE2 . HIS A 121 ? 1.44149 1.47443 1.16929 0.04480  0.18489  -0.19914 157 HIS A NE2 
962  N N   . ASP A 122 ? 1.43563 1.58037 1.46871 0.07085  0.28917  -0.14229 158 ASP A N   
963  C CA  . ASP A 122 ? 1.38846 1.55697 1.53027 0.08043  0.29899  -0.13929 158 ASP A CA  
964  C C   . ASP A 122 ? 1.37627 1.57059 1.57145 0.09117  0.25003  -0.11405 158 ASP A C   
965  O O   . ASP A 122 ? 1.36346 1.57301 1.65043 0.10245  0.24439  -0.11156 158 ASP A O   
966  C CB  . ASP A 122 ? 1.37038 1.52794 1.57405 0.08531  0.33550  -0.16683 158 ASP A CB  
967  C CG  . ASP A 122 ? 1.45300 1.57860 1.58219 0.07465  0.38282  -0.19747 158 ASP A CG  
968  O OD1 . ASP A 122 ? 1.48257 1.60065 1.55060 0.06537  0.40720  -0.19476 158 ASP A OD1 
969  O OD2 . ASP A 122 ? 1.54184 1.64876 1.67258 0.07570  0.39575  -0.22420 158 ASP A OD2 
970  N N   . LEU A 123 ? 1.20918 1.40758 1.34782 0.08801  0.21468  -0.09478 159 LEU A N   
971  C CA  . LEU A 123 ? 1.18215 1.40119 1.34997 0.09719  0.17127  -0.07151 159 LEU A CA  
972  C C   . LEU A 123 ? 1.10199 1.33795 1.24332 0.09158  0.15267  -0.05812 159 LEU A C   
973  O O   . LEU A 123 ? 1.12120 1.34679 1.20163 0.07993  0.16295  -0.05977 159 LEU A O   
974  C CB  . LEU A 123 ? 1.18437 1.38870 1.31693 0.09992  0.14820  -0.06271 159 LEU A CB  
975  C CG  . LEU A 123 ? 1.18126 1.37881 1.37065 0.11139  0.14713  -0.06306 159 LEU A CG  
976  C CD1 . LEU A 123 ? 1.15993 1.38147 1.43152 0.12542  0.12839  -0.04584 159 LEU A CD1 
977  C CD2 . LEU A 123 ? 1.27813 1.45561 1.48159 0.10785  0.18589  -0.09424 159 LEU A CD2 
978  N N   . ILE A 124 ? 1.01584 1.27734 1.20495 0.10011  0.12328  -0.04547 160 ILE A N   
979  C CA  . ILE A 124 ? 0.99479 1.27333 1.16259 0.09597  0.09915  -0.03606 160 ILE A CA  
980  C C   . ILE A 124 ? 1.08497 1.36507 1.22179 0.10230  0.06225  -0.01925 160 ILE A C   
981  O O   . ILE A 124 ? 1.05216 1.32858 1.20904 0.11336  0.05050  -0.00997 160 ILE A O   
982  C CB  . ILE A 124 ? 1.03022 1.33713 1.27346 0.09948  0.09362  -0.04034 160 ILE A CB  
983  C CG1 . ILE A 124 ? 1.10376 1.42915 1.40659 0.11498  0.05840  -0.03241 160 ILE A CG1 
984  C CG2 . ILE A 124 ? 1.10374 1.40634 1.39241 0.09509  0.13888  -0.05522 160 ILE A CG2 
985  C CD1 . ILE A 124 ? 1.01401 1.36790 1.40554 0.11940  0.04700  -0.04027 160 ILE A CD1 
986  N N   . TYR A 125 ? 1.00116 1.28505 1.09159 0.09519  0.04741  -0.01416 161 TYR A N   
987  C CA  . TYR A 125 ? 0.97993 1.25945 1.02906 0.09889  0.02254  0.00060  161 TYR A CA  
988  C C   . TYR A 125 ? 1.03916 1.34151 1.10745 0.10925  -0.01063 0.00849  161 TYR A C   
989  O O   . TYR A 125 ? 1.08394 1.38214 1.14306 0.12025  -0.02832 0.02519  161 TYR A O   
990  C CB  . TYR A 125 ? 1.11788 1.38756 1.11169 0.08582  0.02545  0.00014  161 TYR A CB  
991  C CG  . TYR A 125 ? 1.07034 1.32749 1.02347 0.08773  0.01260  0.01358  161 TYR A CG  
992  C CD1 . TYR A 125 ? 1.00835 1.24163 0.94892 0.08963  0.02108  0.01974  161 TYR A CD1 
993  C CD2 . TYR A 125 ? 1.05951 1.32749 0.99103 0.08733  -0.00473 0.01781  161 TYR A CD2 
994  C CE1 . TYR A 125 ? 1.08236 1.30262 0.99641 0.09136  0.01490  0.03364  161 TYR A CE1 
995  C CE2 . TYR A 125 ? 1.08424 1.33801 0.97880 0.08880  -0.00844 0.03054  161 TYR A CE2 
996  C CZ  . TYR A 125 ? 1.13216 1.36192 1.02123 0.09093  0.00257  0.04036  161 TYR A CZ  
997  O OH  . TYR A 125 ? 1.16154 1.37582 1.02382 0.09235  0.00403  0.05459  161 TYR A OH  
998  N N   . ARG A 126 ? 1.02711 1.35240 1.12111 0.10608  -0.02051 -0.00294 162 ARG A N   
999  C CA  . ARG A 126 ? 1.05579 1.40555 1.17171 0.11504  -0.05708 -0.00323 162 ARG A CA  
1000 C C   . ARG A 126 ? 1.10361 1.45064 1.15099 0.11646  -0.08018 0.00578  162 ARG A C   
1001 O O   . ARG A 126 ? 1.11219 1.47722 1.15980 0.12385  -0.11390 0.00374  162 ARG A O   
1002 C CB  . ARG A 126 ? 1.05074 1.40866 1.22325 0.13086  -0.07524 0.00561  162 ARG A CB  
1003 C CG  . ARG A 126 ? 1.06184 1.43312 1.32644 0.13142  -0.06032 -0.00910 162 ARG A CG  
1004 C CD  . ARG A 126 ? 1.08420 1.47262 1.41971 0.14768  -0.09393 -0.00237 162 ARG A CD  
1005 N NE  . ARG A 126 ? 1.15025 1.52179 1.48966 0.15831  -0.09248 0.01772  162 ARG A NE  
1006 C CZ  . ARG A 126 ? 1.22983 1.60966 1.60818 0.17442  -0.12867 0.03546  162 ARG A CZ  
1007 N NH1 . ARG A 126 ? 1.19553 1.60024 1.60322 0.18228  -0.17464 0.03434  162 ARG A NH1 
1008 N NH2 . ARG A 126 ? 1.28508 1.64742 1.67624 0.18315  -0.12129 0.05491  162 ARG A NH2 
1009 N N   . ASP A 127 ? 1.21162 1.53598 1.20153 0.10967  -0.06324 0.01399  163 ASP A N   
1010 C CA  . ASP A 127 ? 1.21635 1.53386 1.14325 0.11064  -0.07542 0.02293  163 ASP A CA  
1011 C C   . ASP A 127 ? 1.12239 1.43058 1.01965 0.09506  -0.05623 0.01305  163 ASP A C   
1012 O O   . ASP A 127 ? 1.11986 1.40832 0.97450 0.09253  -0.04608 0.02338  163 ASP A O   
1013 C CB  . ASP A 127 ? 1.23578 1.53151 1.13511 0.12108  -0.07372 0.04959  163 ASP A CB  
1014 C CG  . ASP A 127 ? 1.25115 1.54209 1.08720 0.12711  -0.08906 0.06369  163 ASP A CG  
1015 O OD1 . ASP A 127 ? 1.17508 1.48345 0.99008 0.12584  -0.10902 0.04944  163 ASP A OD1 
1016 O OD2 . ASP A 127 ? 1.31145 1.57982 1.11888 0.13297  -0.07894 0.08798  163 ASP A OD2 
1017 N N   . ILE A 128 ? 0.94337 1.26513 0.87227 0.08461  -0.05004 -0.00543 164 ILE A N   
1018 C CA  . ILE A 128 ? 0.98912 1.30239 0.90422 0.06978  -0.03333 -0.01214 164 ILE A CA  
1019 C C   . ILE A 128 ? 1.00091 1.31742 0.88127 0.06726  -0.04276 -0.01899 164 ILE A C   
1020 O O   . ILE A 128 ? 0.97541 1.31333 0.86357 0.06948  -0.06196 -0.03475 164 ILE A O   
1021 C CB  . ILE A 128 ? 0.88618 1.21293 0.84901 0.06051  -0.02368 -0.02535 164 ILE A CB  
1022 C CG1 . ILE A 128 ? 0.98173 1.29764 0.96299 0.06088  -0.00421 -0.01891 164 ILE A CG1 
1023 C CG2 . ILE A 128 ? 0.88856 1.21003 0.84554 0.04619  -0.01318 -0.03016 164 ILE A CG2 
1024 C CD1 . ILE A 128 ? 1.01331 1.30069 0.95632 0.05487  0.01152  -0.00868 164 ILE A CD1 
1025 N N   . LYS A 129 ? 0.84303 1.13742 0.68828 0.06235  -0.02835 -0.01007 165 LYS A N   
1026 C CA  . LYS A 129 ? 1.01767 1.30982 0.83082 0.05782  -0.02633 -0.01821 165 LYS A CA  
1027 C C   . LYS A 129 ? 1.07838 1.34536 0.88540 0.04841  -0.00325 -0.01003 165 LYS A C   
1028 O O   . LYS A 129 ? 0.98449 1.23278 0.79329 0.05040  0.00484  0.00614  165 LYS A O   
1029 C CB  . LYS A 129 ? 0.99913 1.29044 0.76059 0.07095  -0.04027 -0.01012 165 LYS A CB  
1030 C CG  . LYS A 129 ? 1.09716 1.36015 0.82224 0.07717  -0.02481 0.01663  165 LYS A CG  
1031 C CD  . LYS A 129 ? 1.19138 1.45167 0.85745 0.09081  -0.03783 0.03031  165 LYS A CD  
1032 C CE  . LYS A 129 ? 1.18898 1.46291 0.86995 0.10548  -0.06683 0.04199  165 LYS A CE  
1033 N NZ  . LYS A 129 ? 1.20104 1.46806 0.82015 0.12033  -0.08300 0.06394  165 LYS A NZ  
1034 N N   . PRO A 130 ? 1.05542 1.32122 0.86432 0.03791  0.00699  -0.02329 166 PRO A N   
1035 C CA  . PRO A 130 ? 1.04915 1.29154 0.86863 0.02875  0.02692  -0.01607 166 PRO A CA  
1036 C C   . PRO A 130 ? 1.04238 1.26065 0.82815 0.03561  0.04093  0.00148  166 PRO A C   
1037 O O   . PRO A 130 ? 1.06032 1.25794 0.86666 0.02908  0.05666  0.00808  166 PRO A O   
1038 C CB  . PRO A 130 ? 1.00502 1.25542 0.84452 0.01695  0.03524  -0.03779 166 PRO A CB  
1039 C CG  . PRO A 130 ? 1.02614 1.30564 0.87942 0.01771  0.01784  -0.05727 166 PRO A CG  
1040 C CD  . PRO A 130 ? 1.05839 1.34532 0.87488 0.03290  0.00011  -0.04928 166 PRO A CD  
1041 N N   . ASP A 131 ? 1.10259 1.32191 0.84311 0.04878  0.03510  0.01110  167 ASP A N   
1042 C CA  . ASP A 131 ? 1.15322 1.34755 0.86571 0.05680  0.05118  0.03456  167 ASP A CA  
1043 C C   . ASP A 131 ? 1.12426 1.30650 0.86377 0.06257  0.04874  0.05290  167 ASP A C   
1044 O O   . ASP A 131 ? 1.16501 1.32373 0.90456 0.06668  0.06551  0.07151  167 ASP A O   
1045 C CB  . ASP A 131 ? 1.24396 1.44172 0.89262 0.06980  0.04359  0.04328  167 ASP A CB  
1046 C CG  . ASP A 131 ? 1.28341 1.49638 0.89920 0.06475  0.03969  0.01701  167 ASP A CG  
1047 O OD1 . ASP A 131 ? 1.17173 1.40683 0.82444 0.05624  0.02654  -0.00832 167 ASP A OD1 
1048 O OD2 . ASP A 131 ? 1.43431 1.63591 0.98676 0.06934  0.05135  0.02111  167 ASP A OD2 
1049 N N   . ASN A 132 ? 1.08793 1.28436 0.85411 0.06259  0.03178  0.04623  168 ASN A N   
1050 C CA  . ASN A 132 ? 1.08579 1.27158 0.87576 0.06756  0.03050  0.05650  168 ASN A CA  
1051 C C   . ASN A 132 ? 1.04702 1.22330 0.86865 0.05577  0.03348  0.04688  168 ASN A C   
1052 O O   . ASN A 132 ? 1.01276 1.17830 0.85028 0.05834  0.03262  0.04919  168 ASN A O   
1053 C CB  . ASN A 132 ? 1.02851 1.23328 0.82458 0.07714  0.01322  0.05566  168 ASN A CB  
1054 C CG  . ASN A 132 ? 1.14621 1.35513 0.91541 0.09213  0.00306  0.07250  168 ASN A CG  
1055 O OD1 . ASN A 132 ? 1.18672 1.38439 0.91851 0.09513  0.01091  0.08477  168 ASN A OD1 
1056 N ND2 . ASN A 132 ? 1.22841 1.45205 1.01699 0.10187  -0.01381 0.07453  168 ASN A ND2 
1057 N N   . PHE A 133 ? 0.98048 1.15973 0.81198 0.04318  0.03514  0.03562  169 PHE A N   
1058 C CA  . PHE A 133 ? 0.98471 1.15246 0.84195 0.03226  0.03269  0.03096  169 PHE A CA  
1059 C C   . PHE A 133 ? 0.92486 1.07202 0.80336 0.02643  0.04362  0.03497  169 PHE A C   
1060 O O   . PHE A 133 ? 0.91361 1.06364 0.79729 0.02094  0.05389  0.03094  169 PHE A O   
1061 C CB  . PHE A 133 ? 1.00352 1.18767 0.87092 0.02241  0.02559  0.02046  169 PHE A CB  
1062 C CG  . PHE A 133 ? 1.00112 1.20266 0.86199 0.02660  0.01949  0.01631  169 PHE A CG  
1063 C CD1 . PHE A 133 ? 0.96141 1.18411 0.81666 0.03428  0.01640  0.01185  169 PHE A CD1 
1064 C CD2 . PHE A 133 ? 0.99016 1.18570 0.85135 0.02271  0.01714  0.01605  169 PHE A CD2 
1065 C CE1 . PHE A 133 ? 0.92431 1.16314 0.79036 0.03795  0.01257  0.00707  169 PHE A CE1 
1066 C CE2 . PHE A 133 ? 0.98207 1.19145 0.84325 0.02612  0.01958  0.01207  169 PHE A CE2 
1067 C CZ  . PHE A 133 ? 0.87877 1.11051 0.75055 0.03365  0.01805  0.00748  169 PHE A CZ  
1068 N N   . LEU A 134 ? 1.00169 1.12791 0.89989 0.02732  0.04284  0.03983  170 LEU A N   
1069 C CA  . LEU A 134 ? 0.97717 1.08230 0.91196 0.02272  0.05389  0.04371  170 LEU A CA  
1070 C C   . LEU A 134 ? 0.95007 1.04435 0.92118 0.01204  0.03537  0.03632  170 LEU A C   
1071 O O   . LEU A 134 ? 0.94835 1.04355 0.90504 0.01126  0.01609  0.03087  170 LEU A O   
1072 C CB  . LEU A 134 ? 0.97927 1.06643 0.92335 0.03301  0.06704  0.05615  170 LEU A CB  
1073 C CG  . LEU A 134 ? 1.05852 1.15237 0.96449 0.04707  0.07681  0.07016  170 LEU A CG  
1074 C CD1 . LEU A 134 ? 1.09060 1.16160 1.02203 0.05572  0.09350  0.08727  170 LEU A CD1 
1075 C CD2 . LEU A 134 ? 0.99696 1.10332 0.86350 0.04788  0.08778  0.07261  170 LEU A CD2 
1076 N N   . ILE A 135 ? 0.97901 1.06159 0.99692 0.00395  0.04149  0.03618  171 ILE A N   
1077 C CA  . ILE A 135 ? 1.02612 1.09403 1.09039 -0.00460 0.01904  0.03186  171 ILE A CA  
1078 C C   . ILE A 135 ? 1.00265 1.04876 1.10164 0.00043  0.02074  0.03246  171 ILE A C   
1079 O O   . ILE A 135 ? 0.87409 0.91556 0.96764 0.00962  0.04547  0.04054  171 ILE A O   
1080 C CB  . ILE A 135 ? 1.06893 1.13505 1.18733 -0.01590 0.02235  0.03074  171 ILE A CB  
1081 C CG1 . ILE A 135 ? 1.01709 1.08070 1.14936 -0.01418 0.06195  0.03280  171 ILE A CG1 
1082 C CG2 . ILE A 135 ? 1.03257 1.11685 1.13475 -0.02303 0.00735  0.02910  171 ILE A CG2 
1083 C CD1 . ILE A 135 ? 0.95765 1.01081 1.16705 -0.02477 0.07395  0.02920  171 ILE A CD1 
1084 N N   . GLY A 136 ? 1.09513 1.12716 1.23205 -0.00514 -0.00733 0.02463  172 GLY A N   
1085 C CA  . GLY A 136 ? 1.15165 1.16281 1.34088 -0.00177 -0.00806 0.02069  172 GLY A CA  
1086 C C   . GLY A 136 ? 1.05158 1.04975 1.31473 -0.00407 0.01978  0.02798  172 GLY A C   
1087 O O   . GLY A 136 ? 0.95652 0.96142 1.21817 -0.00685 0.04605  0.03526  172 GLY A O   
1088 N N   . ARG A 137 ? 1.15501 1.13301 1.48824 -0.00315 0.01575  0.02316  173 ARG A N   
1089 C CA  . ARG A 137 ? 1.19878 1.16019 1.61780 -0.00519 0.04686  0.03003  173 ARG A CA  
1090 C C   . ARG A 137 ? 1.26118 1.21236 1.77078 -0.01625 0.01708  0.01870  173 ARG A C   
1091 O O   . ARG A 137 ? 1.37301 1.32535 1.87840 -0.02043 -0.03316 0.00596  173 ARG A O   
1092 C CB  . ARG A 137 ? 1.07281 1.01706 1.52882 0.00456  0.07128  0.03651  173 ARG A CB  
1093 C CG  . ARG A 137 ? 1.13033 1.07833 1.52570 0.01509  0.11610  0.05861  173 ARG A CG  
1094 C CD  . ARG A 137 ? 1.23623 1.16605 1.67173 0.02568  0.13989  0.07100  173 ARG A CD  
1095 N NE  . ARG A 137 ? 1.29486 1.20210 1.81059 0.02480  0.18305  0.08472  173 ARG A NE  
1096 C CZ  . ARG A 137 ? 1.34868 1.25001 1.83292 0.02842  0.23313  0.10798  173 ARG A CZ  
1097 N NH1 . ARG A 137 ? 1.36693 1.28528 1.74365 0.03255  0.23993  0.11741  173 ARG A NH1 
1098 N NH2 . ARG A 137 ? 1.42094 1.29742 1.98333 0.02805  0.27812  0.12112  173 ARG A NH2 
1099 N N   . ARG A 138 ? 1.36719 1.30658 1.95959 -0.02065 0.04948  0.02410  174 ARG A N   
1100 C CA  . ARG A 138 ? 1.48763 1.41821 2.18398 -0.03139 0.02521  0.01544  174 ARG A CA  
1101 C C   . ARG A 138 ? 1.43853 1.35537 2.19913 -0.03138 -0.02241 0.00032  174 ARG A C   
1102 O O   . ARG A 138 ? 1.43876 1.34400 2.22011 -0.02395 -0.01132 -0.00280 174 ARG A O   
1103 C CB  . ARG A 138 ? 1.44204 1.35877 2.22683 -0.03486 0.08039  0.02236  174 ARG A CB  
1104 C CG  . ARG A 138 ? 1.41609 1.33134 2.29591 -0.04729 0.06760  0.01615  174 ARG A CG  
1105 C CD  . ARG A 138 ? 1.52400 1.45530 2.35256 -0.05230 0.09492  0.01969  174 ARG A CD  
1106 N NE  . ARG A 138 ? 1.74669 1.67271 2.54140 -0.04804 0.16598  0.02700  174 ARG A NE  
1107 C CZ  . ARG A 138 ? 1.92332 1.85786 2.68887 -0.05264 0.20246  0.02461  174 ARG A CZ  
1108 N NH1 . ARG A 138 ? 1.96488 1.91480 2.74523 -0.06189 0.17819  0.01604  174 ARG A NH1 
1109 N NH2 . ARG A 138 ? 2.04134 1.96766 2.76123 -0.04774 0.26456  0.03089  174 ARG A NH2 
1110 N N   . GLY A 139 ? 1.42222 1.33983 2.21636 -0.03957 -0.07802 -0.00927 175 GLY A N   
1111 C CA  . GLY A 139 ? 1.55360 1.45823 2.40477 -0.04057 -0.13361 -0.02773 175 GLY A CA  
1112 C C   . GLY A 139 ? 1.70101 1.61003 2.44883 -0.03577 -0.17448 -0.04087 175 GLY A C   
1113 O O   . GLY A 139 ? 1.72531 1.62565 2.49317 -0.03853 -0.23375 -0.05906 175 GLY A O   
1114 N N   . ALA A 140 ? 1.97032 1.89156 2.60956 -0.02873 -0.14558 -0.03407 176 ALA A N   
1115 C CA  . ALA A 140 ? 2.03111 1.95551 2.57633 -0.02436 -0.17495 -0.04840 176 ALA A CA  
1116 C C   . ALA A 140 ? 2.10973 2.04285 2.57592 -0.03046 -0.21796 -0.04676 176 ALA A C   
1117 O O   . ALA A 140 ? 2.04903 1.99121 2.51847 -0.03644 -0.21567 -0.02975 176 ALA A O   
1118 C CB  . ALA A 140 ? 1.99019 1.92500 2.46025 -0.01462 -0.12908 -0.03992 176 ALA A CB  
1119 N N   . THR A 141 ? 2.20013 2.12878 2.59521 -0.02891 -0.25477 -0.06483 177 THR A N   
1120 C CA  . THR A 141 ? 2.18316 2.11551 2.49081 -0.03383 -0.29339 -0.06051 177 THR A CA  
1121 C C   . THR A 141 ? 2.03672 1.98879 2.25829 -0.03242 -0.25766 -0.04012 177 THR A C   
1122 O O   . THR A 141 ? 2.03947 1.99617 2.20694 -0.03727 -0.27862 -0.02724 177 THR A O   
1123 C CB  . THR A 141 ? 2.30983 2.22961 2.54893 -0.03212 -0.33313 -0.08767 177 THR A CB  
1124 O OG1 . THR A 141 ? 2.35705 2.28498 2.51027 -0.02533 -0.29701 -0.09329 177 THR A OG1 
1125 C CG2 . THR A 141 ? 2.19855 2.10108 2.52978 -0.03099 -0.35745 -0.11602 177 THR A CG2 
1126 N N   . ASP A 142 ? 1.86283 1.82591 2.07479 -0.02552 -0.20636 -0.03568 178 ASP A N   
1127 C CA  . ASP A 142 ? 1.67238 1.65549 1.81456 -0.02320 -0.17376 -0.02033 178 ASP A CA  
1128 C C   . ASP A 142 ? 1.48350 1.47745 1.67422 -0.02282 -0.13266 -0.00475 178 ASP A C   
1129 O O   . ASP A 142 ? 1.41627 1.42450 1.56780 -0.01696 -0.09753 0.00218  178 ASP A O   
1130 C CB  . ASP A 142 ? 1.69038 1.67765 1.76532 -0.01447 -0.15458 -0.03084 178 ASP A CB  
1131 C CG  . ASP A 142 ? 1.72796 1.70573 1.85496 -0.00691 -0.13655 -0.04187 178 ASP A CG  
1132 O OD1 . ASP A 142 ? 1.67321 1.64189 1.88575 -0.00811 -0.13148 -0.03864 178 ASP A OD1 
1133 O OD2 . ASP A 142 ? 1.67342 1.65184 1.76358 0.00024  -0.12478 -0.05294 178 ASP A OD2 
1134 N N   . GLU A 143 ? 1.40301 1.38925 1.68072 -0.02915 -0.13749 -0.00074 179 GLU A N   
1135 C CA  . GLU A 143 ? 1.29390 1.28580 1.61858 -0.02959 -0.09356 0.00973  179 GLU A CA  
1136 C C   . GLU A 143 ? 1.26718 1.28058 1.53802 -0.03141 -0.07475 0.01989  179 GLU A C   
1137 O O   . GLU A 143 ? 1.20433 1.22708 1.45781 -0.02704 -0.03464 0.02413  179 GLU A O   
1138 C CB  . GLU A 143 ? 1.45075 1.42973 1.88677 -0.03769 -0.10222 0.00972  179 GLU A CB  
1139 C CG  . GLU A 143 ? 1.35150 1.33371 1.83546 -0.04011 -0.05262 0.01741  179 GLU A CG  
1140 C CD  . GLU A 143 ? 1.33293 1.30099 1.94212 -0.04852 -0.05651 0.01551  179 GLU A CD  
1141 O OE1 . GLU A 143 ? 1.31967 1.27350 1.98965 -0.05033 -0.09660 0.00799  179 GLU A OE1 
1142 O OE2 . GLU A 143 ? 1.38647 1.35739 2.03761 -0.05347 -0.01971 0.01895  179 GLU A OE2 
1143 N N   . ASN A 144 ? 1.23204 1.25253 1.47667 -0.03757 -0.10425 0.02428  180 ASN A N   
1144 C CA  . ASN A 144 ? 1.16789 1.20890 1.37616 -0.04001 -0.08878 0.03241  180 ASN A CA  
1145 C C   . ASN A 144 ? 1.22496 1.27719 1.34123 -0.03531 -0.09409 0.03354  180 ASN A C   
1146 O O   . ASN A 144 ? 1.09373 1.16381 1.18455 -0.03679 -0.08168 0.03921  180 ASN A O   
1147 C CB  . ASN A 144 ? 1.15557 1.19709 1.41904 -0.05076 -0.10976 0.04133  180 ASN A CB  
1148 C CG  . ASN A 144 ? 1.21376 1.25803 1.55668 -0.05592 -0.07815 0.03924  180 ASN A CG  
1149 O OD1 . ASN A 144 ? 1.20853 1.26938 1.54569 -0.05861 -0.05482 0.03932  180 ASN A OD1 
1150 N ND2 . ASN A 144 ? 1.17621 1.20344 1.59815 -0.05758 -0.07470 0.03456  180 ASN A ND2 
1151 N N   . ASN A 145 ? 1.31903 1.36088 1.39251 -0.03009 -0.10976 0.02582  181 ASN A N   
1152 C CA  . ASN A 145 ? 1.28805 1.33938 1.28129 -0.02480 -0.10341 0.02401  181 ASN A CA  
1153 C C   . ASN A 145 ? 1.15780 1.22570 1.13774 -0.01663 -0.06626 0.02312  181 ASN A C   
1154 O O   . ASN A 145 ? 1.08125 1.14456 1.08952 -0.01125 -0.04908 0.02081  181 ASN A O   
1155 C CB  . ASN A 145 ? 1.29875 1.33338 1.25480 -0.02117 -0.12335 0.01014  181 ASN A CB  
1156 C CG  . ASN A 145 ? 1.36695 1.38832 1.28954 -0.02792 -0.16277 0.01207  181 ASN A CG  
1157 O OD1 . ASN A 145 ? 1.33384 1.35837 1.26786 -0.03493 -0.17631 0.02876  181 ASN A OD1 
1158 N ND2 . ASN A 145 ? 1.47173 1.47705 1.35162 -0.02566 -0.18190 -0.00496 181 ASN A ND2 
1159 N N   . VAL A 146 ? 1.18217 1.26846 1.12165 -0.01537 -0.05494 0.02674  182 VAL A N   
1160 C CA  . VAL A 146 ? 1.09442 1.19840 1.01983 -0.00729 -0.02827 0.02557  182 VAL A CA  
1161 C C   . VAL A 146 ? 1.10805 1.20914 0.99898 0.00235  -0.02370 0.01890  182 VAL A C   
1162 O O   . VAL A 146 ? 1.12343 1.22116 0.97881 0.00171  -0.03142 0.01412  182 VAL A O   
1163 C CB  . VAL A 146 ? 1.02802 1.15426 0.94317 -0.01040 -0.02086 0.02897  182 VAL A CB  
1164 C CG1 . VAL A 146 ? 0.92360 1.06819 0.81660 -0.00068 -0.00337 0.02490  182 VAL A CG1 
1165 C CG2 . VAL A 146 ? 0.98987 1.12126 0.95173 -0.01853 -0.01753 0.03130  182 VAL A CG2 
1166 N N   . HIS A 147 ? 1.04172 1.14228 0.94418 0.01132  -0.00869 0.01953  183 HIS A N   
1167 C CA  . HIS A 147 ? 1.10732 1.20551 0.99444 0.02143  -0.00243 0.01472  183 HIS A CA  
1168 C C   . HIS A 147 ? 1.06215 1.18125 0.93529 0.03036  0.01235  0.02072  183 HIS A C   
1169 O O   . HIS A 147 ? 1.00378 1.13611 0.87772 0.02977  0.01816  0.02696  183 HIS A O   
1170 C CB  . HIS A 147 ? 1.11255 1.19133 1.03513 0.02619  0.00044  0.01461  183 HIS A CB  
1171 C CG  . HIS A 147 ? 1.13585 1.19430 1.08544 0.01809  -0.01947 0.00555  183 HIS A CG  
1172 N ND1 . HIS A 147 ? 1.05441 1.10894 1.03267 0.00873  -0.02893 0.01004  183 HIS A ND1 
1173 C CD2 . HIS A 147 ? 1.16970 1.21061 1.12825 0.01807  -0.03470 -0.01010 183 HIS A CD2 
1174 C CE1 . HIS A 147 ? 1.15134 1.18724 1.15659 0.00376  -0.05280 0.00001  183 HIS A CE1 
1175 N NE2 . HIS A 147 ? 1.29703 1.32433 1.28686 0.00917  -0.05771 -0.01392 183 HIS A NE2 
1176 N N   . LEU A 148 ? 1.07602 1.19766 0.93993 0.03866  0.01673  0.01629  184 LEU A N   
1177 C CA  . LEU A 148 ? 1.04181 1.18238 0.90280 0.04879  0.02455  0.02223  184 LEU A CA  
1178 C C   . LEU A 148 ? 1.06115 1.19260 0.94143 0.06085  0.03082  0.03006  184 LEU A C   
1179 O O   . LEU A 148 ? 1.06344 1.17849 0.95964 0.06200  0.03206  0.02174  184 LEU A O   
1180 C CB  . LEU A 148 ? 1.08714 1.24093 0.93724 0.04870  0.02693  0.01249  184 LEU A CB  
1181 C CG  . LEU A 148 ? 1.06730 1.24409 0.92814 0.05835  0.02926  0.01674  184 LEU A CG  
1182 C CD1 . LEU A 148 ? 1.02797 1.22208 0.88396 0.05610  0.02267  0.02199  184 LEU A CD1 
1183 C CD2 . LEU A 148 ? 1.15826 1.34441 1.02474 0.05826  0.03781  0.00564  184 LEU A CD2 
1184 N N   . ILE A 149 ? 1.01928 1.16051 0.89794 0.07004  0.03364  0.04603  185 ILE A N   
1185 C CA  . ILE A 149 ? 1.11538 1.24750 1.01233 0.08286  0.03964  0.06245  185 ILE A CA  
1186 C C   . ILE A 149 ? 1.15407 1.30631 1.04116 0.09431  0.03279  0.07451  185 ILE A C   
1187 O O   . ILE A 149 ? 1.16302 1.33628 1.03575 0.09161  0.02380  0.06567  185 ILE A O   
1188 C CB  . ILE A 149 ? 1.07027 1.18381 0.97235 0.08298  0.05045  0.07855  185 ILE A CB  
1189 C CG1 . ILE A 149 ? 1.13110 1.25412 0.99959 0.07812  0.05221  0.08279  185 ILE A CG1 
1190 C CG2 . ILE A 149 ? 1.13618 1.22869 1.06860 0.07378  0.05237  0.06606  185 ILE A CG2 
1191 C CD1 . ILE A 149 ? 1.16967 1.28383 1.02002 0.08680  0.06577  0.10707  185 ILE A CD1 
1192 N N   . ASP A 150 ? 1.18897 1.33412 1.09032 0.10760  0.03499  0.09603  186 ASP A N   
1193 C CA  . ASP A 150 ? 1.21941 1.38045 1.11223 0.12072  0.02184  0.11339  186 ASP A CA  
1194 C C   . ASP A 150 ? 1.18135 1.36346 1.10076 0.12284  0.01077  0.09764  186 ASP A C   
1195 O O   . ASP A 150 ? 1.14333 1.34531 1.04875 0.11738  0.00135  0.08366  186 ASP A O   
1196 C CB  . ASP A 150 ? 1.22548 1.39586 1.06528 0.11947  0.01465  0.12017  186 ASP A CB  
1197 C CG  . ASP A 150 ? 1.26423 1.44338 1.08202 0.13497  -0.00280 0.14420  186 ASP A CG  
1198 O OD1 . ASP A 150 ? 1.28148 1.47048 1.13466 0.14532  -0.01704 0.15007  186 ASP A OD1 
1199 O OD2 . ASP A 150 ? 1.32227 1.49737 1.08661 0.13690  -0.00266 0.15700  186 ASP A OD2 
1200 N N   . PHE A 151 ? 1.25413 1.43168 1.22154 0.13073  0.01475  0.09891  187 PHE A N   
1201 C CA  . PHE A 151 ? 1.22489 1.41959 1.23106 0.13340  0.01115  0.08383  187 PHE A CA  
1202 C C   . PHE A 151 ? 1.22228 1.42788 1.26529 0.15035  -0.00616 0.10597  187 PHE A C   
1203 O O   . PHE A 151 ? 1.14229 1.35466 1.24437 0.15566  -0.00365 0.09785  187 PHE A O   
1204 C CB  . PHE A 151 ? 1.14238 1.32335 1.18040 0.12760  0.03212  0.06042  187 PHE A CB  
1205 C CG  . PHE A 151 ? 1.14980 1.32228 1.14923 0.11146  0.04181  0.03835  187 PHE A CG  
1206 C CD1 . PHE A 151 ? 1.19028 1.34285 1.16802 0.10509  0.04422  0.04025  187 PHE A CD1 
1207 C CD2 . PHE A 151 ? 0.99283 1.17616 0.98317 0.10308  0.04816  0.01830  187 PHE A CD2 
1208 C CE1 . PHE A 151 ? 1.14772 1.29235 1.09450 0.09105  0.04638  0.02268  187 PHE A CE1 
1209 C CE2 . PHE A 151 ? 1.00777 1.18146 0.95895 0.08921  0.05403  0.00400  187 PHE A CE2 
1210 C CZ  . PHE A 151 ? 1.08554 1.24033 1.01437 0.08338  0.04989  0.00627  187 PHE A CZ  
1211 N N   . GLY A 152 ? 1.24142 1.44747 1.24986 0.15913  -0.02361 0.13449  188 GLY A N   
1212 C CA  . GLY A 152 ? 1.26852 1.48491 1.30167 0.17612  -0.04878 0.16021  188 GLY A CA  
1213 C C   . GLY A 152 ? 1.22850 1.47451 1.28443 0.17834  -0.07387 0.14602  188 GLY A C   
1214 O O   . GLY A 152 ? 1.24736 1.50414 1.34014 0.19277  -0.10015 0.16432  188 GLY A O   
1215 N N   . MET A 153 ? 1.21176 1.47073 1.25473 0.16479  -0.06767 0.11554  189 MET A N   
1216 C CA  . MET A 153 ? 1.13096 1.41780 1.21178 0.16509  -0.08575 0.09778  189 MET A CA  
1217 C C   . MET A 153 ? 1.12356 1.41283 1.25710 0.15553  -0.05679 0.06962  189 MET A C   
1218 O O   . MET A 153 ? 1.09942 1.40893 1.26386 0.15141  -0.06019 0.05099  189 MET A O   
1219 C CB  . MET A 153 ? 1.19807 1.49952 1.22421 0.15814  -0.10290 0.08718  189 MET A CB  
1220 C CG  . MET A 153 ? 1.25531 1.58088 1.29123 0.16927  -0.14700 0.09117  189 MET A CG  
1221 S SD  . MET A 153 ? 1.44033 1.75408 1.43127 0.18842  -0.17809 0.13451  189 MET A SD  
1222 C CE  . MET A 153 ? 1.32787 1.61334 1.21995 0.17921  -0.14833 0.14457  189 MET A CE  
1223 N N   . ALA A 154 ? 1.06501 1.33269 1.20898 0.15189  -0.02691 0.06510  190 ALA A N   
1224 C CA  . ALA A 154 ? 1.11036 1.37478 1.28379 0.14215  0.00477  0.03754  190 ALA A CA  
1225 C C   . ALA A 154 ? 1.12097 1.39508 1.38493 0.15141  0.00982  0.03187  190 ALA A C   
1226 O O   . ALA A 154 ? 1.08576 1.35278 1.39330 0.16290  0.00551  0.04599  190 ALA A O   
1227 C CB  . ALA A 154 ? 0.89052 1.12685 1.03295 0.13421  0.03081  0.02957  190 ALA A CB  
1228 N N   . LYS A 155 ? 1.04832 1.33776 1.35018 0.14637  0.02174  0.01207  191 LYS A N   
1229 C CA  . LYS A 155 ? 1.11404 1.41411 1.51531 0.15377  0.03126  0.00306  191 LYS A CA  
1230 C C   . LYS A 155 ? 1.09678 1.38610 1.51060 0.14211  0.08164  -0.02593 191 LYS A C   
1231 O O   . LYS A 155 ? 1.08273 1.36931 1.44240 0.12929  0.09779  -0.03647 191 LYS A O   
1232 C CB  . LYS A 155 ? 1.13713 1.46780 1.59139 0.16080  -0.00293 0.00714  191 LYS A CB  
1233 C CG  . LYS A 155 ? 1.06641 1.41043 1.63553 0.16445  0.01366  -0.00885 191 LYS A CG  
1234 C CD  . LYS A 155 ? 1.11399 1.48827 1.75080 0.17535  -0.03424 -0.00127 191 LYS A CD  
1235 C CE  . LYS A 155 ? 1.14700 1.52310 1.80603 0.19300  -0.07880 0.02808  191 LYS A CE  
1236 N NZ  . LYS A 155 ? 1.11936 1.52360 1.82076 0.20407  -0.13757 0.03699  191 LYS A NZ  
1237 N N   . GLN A 156 ? 1.12118 1.40267 1.60560 0.14673  0.10793  -0.03783 192 GLN A N   
1238 C CA  . GLN A 156 ? 1.20526 1.47412 1.70051 0.13663  0.16124  -0.06728 192 GLN A CA  
1239 C C   . GLN A 156 ? 1.12058 1.40997 1.67450 0.13430  0.17331  -0.07573 192 GLN A C   
1240 O O   . GLN A 156 ? 1.12093 1.43389 1.76516 0.14487  0.14756  -0.06776 192 GLN A O   
1241 C CB  . GLN A 156 ? 1.25523 1.50999 1.81914 0.14255  0.18835  -0.08151 192 GLN A CB  
1242 C CG  . GLN A 156 ? 1.34671 1.58432 1.91575 0.13247  0.24925  -0.11597 192 GLN A CG  
1243 C CD  . GLN A 156 ? 1.36356 1.58647 2.00360 0.13794  0.27680  -0.13512 192 GLN A CD  
1244 O OE1 . GLN A 156 ? 1.42674 1.63363 2.07719 0.13087  0.33017  -0.16721 192 GLN A OE1 
1245 N NE2 . GLN A 156 ? 1.34657 1.57320 2.03594 0.15051  0.24329  -0.11547 192 GLN A NE2 
1246 N N   . TYR A 157 ? 1.14689 1.42651 1.65263 0.12072  0.21113  -0.09044 193 TYR A N   
1247 C CA  . TYR A 157 ? 1.16983 1.46539 1.73534 0.11717  0.23206  -0.09799 193 TYR A CA  
1248 C C   . TYR A 157 ? 1.32883 1.60735 1.92880 0.11132  0.29923  -0.12184 193 TYR A C   
1249 O O   . TYR A 157 ? 1.33812 1.62952 2.02022 0.11078  0.32347  -0.12851 193 TYR A O   
1250 C CB  . TYR A 157 ? 1.13594 1.43609 1.62922 0.10648  0.22385  -0.08995 193 TYR A CB  
1251 C CG  . TYR A 157 ? 1.26607 1.53790 1.66086 0.09239  0.26476  -0.09658 193 TYR A CG  
1252 C CD1 . TYR A 157 ? 1.26467 1.51466 1.55983 0.08825  0.25370  -0.09354 193 TYR A CD1 
1253 C CD2 . TYR A 157 ? 1.18965 1.45552 1.59263 0.08360  0.31289  -0.10396 193 TYR A CD2 
1254 C CE1 . TYR A 157 ? 1.27447 1.49838 1.47756 0.07610  0.28244  -0.09899 193 TYR A CE1 
1255 C CE2 . TYR A 157 ? 1.26631 1.50399 1.56823 0.07162  0.34645  -0.10557 193 TYR A CE2 
1256 C CZ  . TYR A 157 ? 1.35138 1.56867 1.55170 0.06808  0.32737  -0.10366 193 TYR A CZ  
1257 O OH  . TYR A 157 ? 1.33212 1.52113 1.42997 0.05685  0.35248  -0.10484 193 TYR A OH  
1258 N N   . ARG A 158 ? 1.39174 1.64086 1.93324 0.10675  0.33120  -0.13693 194 ARG A N   
1259 C CA  . ARG A 158 ? 1.38924 1.61824 1.95289 0.10133  0.39892  -0.16392 194 ARG A CA  
1260 C C   . ARG A 158 ? 1.44304 1.65023 1.99797 0.10419  0.41081  -0.18284 194 ARG A C   
1261 O O   . ARG A 158 ? 1.45182 1.64972 1.93711 0.10461  0.37794  -0.17607 194 ARG A O   
1262 C CB  . ARG A 158 ? 1.44133 1.64941 1.90128 0.08655  0.44001  -0.16835 194 ARG A CB  
1263 C CG  . ARG A 158 ? 1.45830 1.64104 1.77659 0.07872  0.42694  -0.16814 194 ARG A CG  
1264 C CD  . ARG A 158 ? 1.48723 1.65050 1.70399 0.06542  0.45876  -0.16497 194 ARG A CD  
1265 N NE  . ARG A 158 ? 1.50673 1.64390 1.59534 0.05840  0.44378  -0.16795 194 ARG A NE  
1266 C CZ  . ARG A 158 ? 1.54731 1.66603 1.52949 0.04771  0.45237  -0.15853 194 ARG A CZ  
1267 N NH1 . ARG A 158 ? 1.56672 1.68895 1.55133 0.04246  0.48008  -0.14285 194 ARG A NH1 
1268 N NH2 . ARG A 158 ? 1.51923 1.61513 1.39718 0.04255  0.43087  -0.16350 194 ARG A NH2 
1269 N N   . ASP A 159 ? 1.48466 1.68364 2.12180 0.10604  0.46017  -0.20843 195 ASP A N   
1270 C CA  . ASP A 159 ? 1.51412 1.69243 2.15851 0.10836  0.47623  -0.23224 195 ASP A CA  
1271 C C   . ASP A 159 ? 1.60213 1.74542 2.10556 0.09500  0.50828  -0.25610 195 ASP A C   
1272 O O   . ASP A 159 ? 1.63562 1.76660 2.06339 0.08434  0.54287  -0.26034 195 ASP A O   
1273 C CB  . ASP A 159 ? 1.57469 1.75416 2.35832 0.11378  0.52268  -0.25614 195 ASP A CB  
1274 C CG  . ASP A 159 ? 1.70657 1.85957 2.45569 0.10187  0.60393  -0.29116 195 ASP A CG  
1275 O OD1 . ASP A 159 ? 1.73276 1.88788 2.45434 0.09492  0.62907  -0.28354 195 ASP A OD1 
1276 O OD2 . ASP A 159 ? 1.65781 1.78617 2.40448 0.09926  0.64474  -0.32675 195 ASP A OD2 
1277 N N   . PRO A 160 ? 1.64266 1.76878 2.10862 0.09566  0.49424  -0.27034 196 PRO A N   
1278 C CA  . PRO A 160 ? 1.73401 1.82768 2.06108 0.08339  0.51150  -0.29390 196 PRO A CA  
1279 C C   . PRO A 160 ? 1.86894 1.93477 2.17423 0.07536  0.58461  -0.33774 196 PRO A C   
1280 O O   . PRO A 160 ? 1.94392 1.98211 2.11659 0.06424  0.60150  -0.35473 196 PRO A O   
1281 C CB  . PRO A 160 ? 1.66905 1.75603 1.99317 0.08813  0.47144  -0.29780 196 PRO A CB  
1282 C CG  . PRO A 160 ? 1.58064 1.69771 2.01297 0.10240  0.42633  -0.26219 196 PRO A CG  
1283 C CD  . PRO A 160 ? 1.56735 1.70339 2.10957 0.10787  0.45314  -0.25983 196 PRO A CD  
1284 N N   . ARG A 161 ? 1.81840 1.88880 2.24678 0.08053  0.62871  -0.35718 197 ARG A N   
1285 C CA  . ARG A 161 ? 1.87205 1.91272 2.28244 0.07275  0.70503  -0.40468 197 ARG A CA  
1286 C C   . ARG A 161 ? 1.87889 1.91919 2.31730 0.06835  0.76777  -0.40481 197 ARG A C   
1287 O O   . ARG A 161 ? 2.00288 2.01014 2.36701 0.05582  0.81068  -0.42583 197 ARG A O   
1288 C CB  . ARG A 161 ? 1.81169 1.84940 2.34550 0.07998  0.72390  -0.43849 197 ARG A CB  
1289 C CG  . ARG A 161 ? 1.89607 1.91146 2.36329 0.07734  0.70442  -0.46784 197 ARG A CG  
1290 C CD  . ARG A 161 ? 1.97534 1.95231 2.28098 0.06269  0.74473  -0.50799 197 ARG A CD  
1291 N NE  . ARG A 161 ? 2.00236 1.95461 2.33187 0.05553  0.78131  -0.54957 197 ARG A NE  
1292 C CZ  . ARG A 161 ? 2.07020 1.98822 2.26808 0.04279  0.80506  -0.58188 197 ARG A CZ  
1293 N NH1 . ARG A 161 ? 2.14981 2.05248 2.18159 0.03599  0.79310  -0.57398 197 ARG A NH1 
1294 N NH2 . ARG A 161 ? 2.09006 1.98907 2.32449 0.03698  0.83886  -0.62170 197 ARG A NH2 
1295 N N   . THR A 162 ? 1.82320 1.89540 2.35627 0.07478  0.74872  -0.36942 198 THR A N   
1296 C CA  . THR A 162 ? 1.85384 1.92358 2.40319 0.06768  0.79053  -0.35811 198 THR A CA  
1297 C C   . THR A 162 ? 1.87321 1.96088 2.36704 0.06662  0.76823  -0.32206 198 THR A C   
1298 O O   . THR A 162 ? 1.87472 1.95929 2.37513 0.06022  0.79953  -0.30815 198 THR A O   
1299 C CB  . THR A 162 ? 1.80367 1.89126 2.53762 0.07357  0.79661  -0.35482 198 THR A CB  
1300 O OG1 . THR A 162 ? 1.77042 1.90297 2.60720 0.08770  0.74537  -0.32480 198 THR A OG1 
1301 C CG2 . THR A 162 ? 1.75760 1.83395 2.57081 0.07617  0.80197  -0.38366 198 THR A CG2 
1302 N N   . LYS A 163 ? 1.88229 1.98114 2.30870 0.06862  0.69408  -0.29726 199 LYS A N   
1303 C CA  . LYS A 163 ? 1.86301 1.97386 2.21883 0.06463  0.65597  -0.26043 199 LYS A CA  
1304 C C   . LYS A 163 ? 1.89705 2.03786 2.36747 0.06842  0.65878  -0.23897 199 LYS A C   
1305 O O   . LYS A 163 ? 1.92328 2.06664 2.34934 0.06208  0.66190  -0.21727 199 LYS A O   
1306 C CB  . LYS A 163 ? 1.99278 2.06994 2.18372 0.05123  0.68602  -0.26145 199 LYS A CB  
1307 C CG  . LYS A 163 ? 2.14738 2.18382 2.25023 0.04452  0.73778  -0.30217 199 LYS A CG  
1308 C CD  . LYS A 163 ? 2.06094 2.09189 2.15592 0.04881  0.69990  -0.32624 199 LYS A CD  
1309 C CE  . LYS A 163 ? 2.07413 2.06664 2.10448 0.04236  0.75666  -0.37599 199 LYS A CE  
1310 N NZ  . LYS A 163 ? 2.05197 2.03476 2.06530 0.04467  0.72182  -0.40410 199 LYS A NZ  
1311 N N   . GLN A 164 ? 1.67263 1.83667 2.29958 0.07909  0.65447  -0.24485 200 GLN A N   
1312 C CA  . GLN A 164 ? 1.53147 1.72582 2.28678 0.08378  0.65094  -0.22987 200 GLN A CA  
1313 C C   . GLN A 164 ? 1.37302 1.60219 2.15924 0.09270  0.56323  -0.20213 200 GLN A C   
1314 O O   . GLN A 164 ? 1.38383 1.62218 2.19264 0.10226  0.51496  -0.19894 200 GLN A O   
1315 C CB  . GLN A 164 ? 1.53258 1.73280 2.45212 0.09063  0.69324  -0.25248 200 GLN A CB  
1316 C CG  . GLN A 164 ? 1.35178 1.59267 2.44006 0.10212  0.65089  -0.23806 200 GLN A CG  
1317 C CD  . GLN A 164 ? 1.39623 1.64970 2.51275 0.09629  0.65851  -0.22256 200 GLN A CD  
1318 O OE1 . GLN A 164 ? 1.46711 1.70101 2.47540 0.08463  0.69424  -0.21635 200 GLN A OE1 
1319 N NE2 . GLN A 164 ? 1.34405 1.62656 2.60350 0.10354  0.61826  -0.21436 200 GLN A NE2 
1320 N N   . HIS A 165 ? 1.34428 1.59126 2.13240 0.08954  0.54582  -0.18249 201 HIS A N   
1321 C CA  . HIS A 165 ? 1.31979 1.59905 2.13130 0.09682  0.46690  -0.16076 201 HIS A CA  
1322 C C   . HIS A 165 ? 1.17463 1.48316 2.14522 0.11103  0.43463  -0.16289 201 HIS A C   
1323 O O   . HIS A 165 ? 1.24918 1.56283 2.34480 0.11313  0.47490  -0.17691 201 HIS A O   
1324 C CB  . HIS A 165 ? 1.35524 1.64601 2.14885 0.08916  0.46422  -0.14595 201 HIS A CB  
1325 C CG  . HIS A 165 ? 1.28647 1.60284 2.05895 0.09290  0.38817  -0.12788 201 HIS A CG  
1326 N ND1 . HIS A 165 ? 1.24878 1.58662 2.06831 0.10559  0.32606  -0.12349 201 HIS A ND1 
1327 C CD2 . HIS A 165 ? 1.25482 1.57667 1.96135 0.08567  0.36610  -0.11349 201 HIS A CD2 
1328 C CE1 . HIS A 165 ? 1.21184 1.56633 1.98762 0.10568  0.27188  -0.10967 201 HIS A CE1 
1329 N NE2 . HIS A 165 ? 1.21592 1.56196 1.92867 0.09341  0.29526  -0.10527 201 HIS A NE2 
1330 N N   . ILE A 166 ? 1.15877 1.48503 2.12530 0.12110  0.36188  -0.14741 202 ILE A N   
1331 C CA  . ILE A 166 ? 1.24181 1.59730 2.34389 0.13602  0.31400  -0.14220 202 ILE A CA  
1332 C C   . ILE A 166 ? 1.12290 1.50520 2.33177 0.13591  0.30976  -0.14517 202 ILE A C   
1333 O O   . ILE A 166 ? 1.08711 1.46979 2.24418 0.12552  0.32349  -0.14331 202 ILE A O   
1334 C CB  . ILE A 166 ? 1.19961 1.56660 2.24660 0.14566  0.23557  -0.11914 202 ILE A CB  
1335 C CG1 . ILE A 166 ? 1.08254 1.45274 2.01014 0.13755  0.20750  -0.10708 202 ILE A CG1 
1336 C CG2 . ILE A 166 ? 1.21489 1.55878 2.21250 0.14937  0.23982  -0.11680 202 ILE A CG2 
1337 C CD1 . ILE A 166 ? 1.15372 1.55733 2.13511 0.14271  0.15280  -0.10051 202 ILE A CD1 
1338 N N   . PRO A 167 ? 1.09872 1.50361 2.46687 0.14709  0.29103  -0.15004 203 PRO A N   
1339 C CA  . PRO A 167 ? 1.04094 1.47259 2.52423 0.14703  0.28311  -0.15618 203 PRO A CA  
1340 C C   . PRO A 167 ? 1.14048 1.59915 2.58786 0.15089  0.20140  -0.14337 203 PRO A C   
1341 O O   . PRO A 167 ? 1.18883 1.65260 2.57155 0.15941  0.13886  -0.12775 203 PRO A O   
1342 C CB  . PRO A 167 ? 0.89188 1.33815 2.56180 0.15912  0.28080  -0.16599 203 PRO A CB  
1343 C CG  . PRO A 167 ? 0.99348 1.43238 2.63301 0.17003  0.24502  -0.15375 203 PRO A CG  
1344 C CD  . PRO A 167 ? 1.07139 1.47736 2.53773 0.15998  0.28012  -0.15154 203 PRO A CD  
1345 N N   . TYR A 168 ? 0.96757 1.44197 2.45884 0.14419  0.20660  -0.15108 204 TYR A N   
1346 C CA  . TYR A 168 ? 0.88903 1.39080 2.36418 0.14676  0.13343  -0.14761 204 TYR A CA  
1347 C C   . TYR A 168 ? 1.02745 1.55847 2.61029 0.16379  0.05559  -0.14765 204 TYR A C   
1348 O O   . TYR A 168 ? 0.94401 1.48242 2.67282 0.17163  0.06519  -0.15514 204 TYR A O   
1349 C CB  . TYR A 168 ? 0.86845 1.38114 2.40110 0.13612  0.16235  -0.15980 204 TYR A CB  
1350 C CG  . TYR A 168 ? 0.84518 1.38743 2.38050 0.13735  0.09212  -0.16496 204 TYR A CG  
1351 C CD1 . TYR A 168 ? 0.79026 1.36645 2.47077 0.14733  0.03657  -0.18008 204 TYR A CD1 
1352 C CD2 . TYR A 168 ? 0.92599 1.46193 2.32531 0.12817  0.08147  -0.15804 204 TYR A CD2 
1353 C CE1 . TYR A 168 ? 0.75465 1.35718 2.43401 0.14800  -0.02847 -0.19121 204 TYR A CE1 
1354 C CE2 . TYR A 168 ? 0.90301 1.46478 2.30638 0.12842  0.02207  -0.16828 204 TYR A CE2 
1355 C CZ  . TYR A 168 ? 0.82214 1.41695 2.36088 0.13820  -0.03280 -0.18653 204 TYR A CZ  
1356 O OH  . TYR A 168 ? 0.84797 1.46797 2.38653 0.13811  -0.09357 -0.20283 204 TYR A OH  
1357 N N   . ARG A 169 ? 0.89347 1.43966 2.40358 0.16974  -0.02158 -0.13884 205 ARG A N   
1358 C CA  . ARG A 169 ? 1.00108 1.57320 2.58731 0.18672  -0.10564 -0.13508 205 ARG A CA  
1359 C C   . ARG A 169 ? 0.89503 1.48746 2.41163 0.18709  -0.17550 -0.13907 205 ARG A C   
1360 O O   . ARG A 169 ? 0.89606 1.48630 2.34477 0.17387  -0.15369 -0.14870 205 ARG A O   
1361 C CB  . ARG A 169 ? 1.04495 1.60198 2.59066 0.19896  -0.12524 -0.11050 205 ARG A CB  
1362 C CG  . ARG A 169 ? 1.02868 1.56707 2.38772 0.19749  -0.14310 -0.08917 205 ARG A CG  
1363 C CD  . ARG A 169 ? 1.13304 1.66720 2.47868 0.21428  -0.19232 -0.06122 205 ARG A CD  
1364 N NE  . ARG A 169 ? 1.16825 1.72938 2.55153 0.22852  -0.28177 -0.05415 205 ARG A NE  
1365 C CZ  . ARG A 169 ? 1.21229 1.77221 2.56602 0.24445  -0.34031 -0.02427 205 ARG A CZ  
1366 N NH1 . ARG A 169 ? 1.25469 1.78899 2.55378 0.24840  -0.31782 0.00168  205 ARG A NH1 
1367 N NH2 . ARG A 169 ? 1.21569 1.79970 2.59515 0.25698  -0.42462 -0.01989 205 ARG A NH2 
1368 N N   . GLU A 170 ? 0.96729 1.57856 2.50190 0.20243  -0.25984 -0.13201 206 GLU A N   
1369 C CA  . GLU A 170 ? 0.95709 1.58706 2.42202 0.20460  -0.33222 -0.13935 206 GLU A CA  
1370 C C   . GLU A 170 ? 1.07022 1.70548 2.50371 0.22353  -0.41368 -0.11633 206 GLU A C   
1371 O O   . GLU A 170 ? 1.02780 1.65129 2.49424 0.23376  -0.40907 -0.09243 206 GLU A O   
1372 C CB  . GLU A 170 ? 0.87111 1.52937 2.46062 0.19976  -0.34851 -0.17385 206 GLU A CB  
1373 C CG  . GLU A 170 ? 0.93519 1.61020 2.44919 0.19495  -0.39503 -0.19346 206 GLU A CG  
1374 C CD  . GLU A 170 ? 1.09510 1.77558 2.59981 0.20410  -0.48460 -0.19903 206 GLU A CD  
1375 O OE1 . GLU A 170 ? 1.10000 1.77098 2.67695 0.21253  -0.50950 -0.18831 206 GLU A OE1 
1376 O OE2 . GLU A 170 ? 1.20680 1.89840 2.62601 0.20246  -0.53012 -0.21460 206 GLU A OE2 
1377 N N   . LYS A 171 ? 1.12216 1.77283 2.48361 0.22787  -0.48627 -0.12291 207 LYS A N   
1378 C CA  . LYS A 171 ? 1.22319 1.87367 2.50585 0.24467  -0.56396 -0.09690 207 LYS A CA  
1379 C C   . LYS A 171 ? 1.33549 1.95225 2.47030 0.24546  -0.53381 -0.05933 207 LYS A C   
1380 O O   . LYS A 171 ? 1.38639 1.99194 2.54512 0.25810  -0.54177 -0.02778 207 LYS A O   
1381 C CB  . LYS A 171 ? 1.16711 1.81558 2.56023 0.25578  -0.60055 -0.08397 207 LYS A CB  
1382 C CG  . LYS A 171 ? 1.18273 1.83784 2.68110 0.24859  -0.62216 -0.11588 207 LYS A CG  
1383 C CD  . LYS A 171 ? 1.24231 1.89993 2.69543 0.25901  -0.71445 -0.10948 207 LYS A CD  
1384 C CE  . LYS A 171 ? 1.15337 1.81342 2.73718 0.25426  -0.73909 -0.14017 207 LYS A CE  
1385 N NZ  . LYS A 171 ? 1.17028 1.83761 2.69444 0.26127  -0.82782 -0.14726 207 LYS A NZ  
1386 N N   . LYS A 172 ? 1.37637 1.97718 2.36981 0.23255  -0.50140 -0.06230 208 LYS A N   
1387 C CA  . LYS A 172 ? 1.57779 2.14813 2.42688 0.23343  -0.48202 -0.02921 208 LYS A CA  
1388 C C   . LYS A 172 ? 1.71672 2.28633 2.42106 0.23196  -0.52042 -0.03196 208 LYS A C   
1389 O O   . LYS A 172 ? 1.68987 2.27016 2.37479 0.21910  -0.51235 -0.06452 208 LYS A O   
1390 C CB  . LYS A 172 ? 1.57738 2.12354 2.39818 0.21792  -0.39443 -0.02996 208 LYS A CB  
1391 C CG  . LYS A 172 ? 1.76909 2.28436 2.45964 0.21856  -0.37476 0.00114  208 LYS A CG  
1392 C CD  . LYS A 172 ? 1.74322 2.24999 2.45206 0.23721  -0.40632 0.03833  208 LYS A CD  
1393 C CE  . LYS A 172 ? 1.85863 2.33865 2.42373 0.24033  -0.40667 0.07119  208 LYS A CE  
1394 N NZ  . LYS A 172 ? 1.88973 2.37581 2.34208 0.23939  -0.44748 0.06595  208 LYS A NZ  
1395 N N   . SER A 173 ? 1.93650 2.49269 2.54441 0.24525  -0.55995 0.00212  209 SER A N   
1396 C CA  . SER A 173 ? 1.95856 2.51074 2.42087 0.24495  -0.59384 0.00025  209 SER A CA  
1397 C C   . SER A 173 ? 2.00978 2.54290 2.37554 0.22652  -0.53002 -0.01018 209 SER A C   
1398 O O   . SER A 173 ? 1.99854 2.51133 2.36533 0.21899  -0.46811 0.00297  209 SER A O   
1399 C CB  . SER A 173 ? 2.02825 2.56289 2.39953 0.26297  -0.63603 0.04719  209 SER A CB  
1400 O OG  . SER A 173 ? 2.06970 2.57503 2.41817 0.26358  -0.58334 0.08390  209 SER A OG  
1401 N N   . LEU A 174 ? 1.98704 2.78014 2.13088 0.28798  -0.45250 -0.00243 210 LEU A N   
1402 C CA  . LEU A 174 ? 1.88005 2.63330 1.97387 0.24805  -0.40156 -0.00112 210 LEU A CA  
1403 C C   . LEU A 174 ? 1.87807 2.54204 1.86564 0.25473  -0.38782 0.03894  210 LEU A C   
1404 O O   . LEU A 174 ? 1.87828 2.50829 1.77665 0.25917  -0.41063 0.05592  210 LEU A O   
1405 C CB  . LEU A 174 ? 1.89080 2.67030 1.96677 0.21726  -0.41159 -0.02613 210 LEU A CB  
1406 C CG  . LEU A 174 ? 1.76746 2.63495 1.94104 0.21002  -0.44214 -0.06449 210 LEU A CG  
1407 C CD1 . LEU A 174 ? 1.72926 2.61995 1.88272 0.23702  -0.51352 -0.06694 210 LEU A CD1 
1408 C CD2 . LEU A 174 ? 1.59041 2.47133 1.77341 0.16460  -0.41792 -0.09205 210 LEU A CD2 
1409 N N   . SER A 175 ? 1.85294 2.47769 1.84815 0.25354  -0.34932 0.05368  211 SER A N   
1410 C CA  . SER A 175 ? 1.89683 2.43905 1.80960 0.25542  -0.33276 0.09158  211 SER A CA  
1411 C C   . SER A 175 ? 1.85236 2.36971 1.75527 0.21865  -0.28096 0.09073  211 SER A C   
1412 O O   . SER A 175 ? 1.84597 2.38422 1.80980 0.20662  -0.25472 0.07259  211 SER A O   
1413 C CB  . SER A 175 ? 1.90145 2.40879 1.83171 0.28959  -0.34202 0.11147  211 SER A CB  
1414 O OG  . SER A 175 ? 1.91342 2.33893 1.77434 0.28464  -0.32239 0.14738  211 SER A OG  
1415 N N   . GLY A 176 ? 1.73569 2.20934 1.56153 0.20201  -0.26623 0.11088  212 GLY A N   
1416 C CA  . GLY A 176 ? 1.55377 2.00381 1.37094 0.17010  -0.22215 0.11344  212 GLY A CA  
1417 C C   . GLY A 176 ? 1.50799 1.96436 1.28087 0.14909  -0.21265 0.10513  212 GLY A C   
1418 O O   . GLY A 176 ? 1.44709 1.91294 1.17485 0.15888  -0.23949 0.10162  212 GLY A O   
1419 N N   . THR A 177 ? 1.42348 1.87170 1.20684 0.12148  -0.17561 0.10066  213 THR A N   
1420 C CA  . THR A 177 ? 1.31784 1.76952 1.06914 0.10232  -0.16011 0.08863  213 THR A CA  
1421 C C   . THR A 177 ? 1.22405 1.72567 1.02920 0.08902  -0.16722 0.04951  213 THR A C   
1422 O O   . THR A 177 ? 1.08961 1.60561 0.95409 0.07378  -0.14949 0.03856  213 THR A O   
1423 C CB  . THR A 177 ? 1.36821 1.78724 1.11391 0.08215  -0.11914 0.10464  213 THR A CB  
1424 O OG1 . THR A 177 ? 1.31866 1.73403 1.12025 0.07491  -0.10764 0.10735  213 THR A OG1 
1425 C CG2 . THR A 177 ? 1.39686 1.77024 1.07702 0.08893  -0.10883 0.14106  213 THR A CG2 
1426 N N   . ALA A 178 ? 1.36005 1.88437 1.14057 0.09305  -0.19411 0.02908  214 ALA A N   
1427 C CA  . ALA A 178 ? 1.30786 1.88010 1.14448 0.07897  -0.20729 -0.00888 214 ALA A CA  
1428 C C   . ALA A 178 ? 1.16647 1.73175 1.02119 0.04986  -0.17430 -0.02535 214 ALA A C   
1429 O O   . ALA A 178 ? 1.11715 1.71520 1.02901 0.03282  -0.17807 -0.05285 214 ALA A O   
1430 C CB  . ALA A 178 ? 1.42241 2.01460 1.22144 0.08940  -0.25032 -0.02803 214 ALA A CB  
1431 N N   . ARG A 179 ? 1.12959 1.65362 0.94373 0.04374  -0.14223 -0.00822 215 ARG A N   
1432 C CA  . ARG A 179 ? 1.11397 1.62909 0.94630 0.02104  -0.11478 -0.02392 215 ARG A CA  
1433 C C   . ARG A 179 ? 1.01187 1.53445 0.91438 0.00497  -0.09727 -0.02192 215 ARG A C   
1434 O O   . ARG A 179 ? 0.95427 1.47932 0.88919 -0.01473 -0.08596 -0.04009 215 ARG A O   
1435 C CB  . ARG A 179 ? 1.14359 1.61959 0.92268 0.02209  -0.08480 -0.00654 215 ARG A CB  
1436 C CG  . ARG A 179 ? 1.15334 1.61877 0.94885 0.00506  -0.05953 -0.02588 215 ARG A CG  
1437 C CD  . ARG A 179 ? 1.28791 1.72498 1.02924 0.01050  -0.03076 -0.01758 215 ARG A CD  
1438 N NE  . ARG A 179 ? 1.30015 1.72017 1.02780 0.01727  -0.01237 0.02169  215 ARG A NE  
1439 C CZ  . ARG A 179 ? 1.39790 1.80023 1.05850 0.02858  -0.00115 0.03989  215 ARG A CZ  
1440 N NH1 . ARG A 179 ? 1.45346 1.85125 1.04321 0.03711  -0.00688 0.02197  215 ARG A NH1 
1441 N NH2 . ARG A 179 ? 1.38116 1.76677 1.04211 0.02963  0.01647  0.07702  215 ARG A NH2 
1442 N N   . TYR A 180 ? 0.98882 1.50976 0.91009 0.01323  -0.09543 -0.00057 216 TYR A N   
1443 C CA  . TYR A 180 ? 0.95829 1.47882 0.92812 -0.00080 -0.07741 0.00304  216 TYR A CA  
1444 C C   . TYR A 180 ? 0.97448 1.52783 0.98892 0.00519  -0.08809 -0.00368 216 TYR A C   
1445 O O   . TYR A 180 ? 0.87428 1.42984 0.92316 -0.00810 -0.07101 -0.00457 216 TYR A O   
1446 C CB  . TYR A 180 ? 0.98370 1.46494 0.93628 -0.00009 -0.05834 0.03191  216 TYR A CB  
1447 C CG  . TYR A 180 ? 0.95591 1.41078 0.87357 -0.00258 -0.04315 0.04239  216 TYR A CG  
1448 C CD1 . TYR A 180 ? 0.97307 1.42883 0.89252 -0.01387 -0.03304 0.02423  216 TYR A CD1 
1449 C CD2 . TYR A 180 ? 1.05384 1.48226 0.94045 0.00641  -0.03637 0.06973  216 TYR A CD2 
1450 C CE1 . TYR A 180 ? 1.08075 1.51619 0.97306 -0.01283 -0.01382 0.03122  216 TYR A CE1 
1451 C CE2 . TYR A 180 ? 1.09011 1.50135 0.95243 0.00351  -0.01611 0.07968  216 TYR A CE2 
1452 C CZ  . TYR A 180 ? 1.12327 1.54044 0.98897 -0.00443 -0.00356 0.05940  216 TYR A CZ  
1453 O OH  . TYR A 180 ? 1.01265 1.41621 0.85875 -0.00420 0.02176  0.06707  216 TYR A OH  
1454 N N   . MET A 181 ? 1.04003 1.61863 1.05434 0.02613  -0.11491 -0.00801 217 MET A N   
1455 C CA  . MET A 181 ? 1.01714 1.63231 1.08447 0.03626  -0.12225 -0.01593 217 MET A CA  
1456 C C   . MET A 181 ? 0.97225 1.63220 1.10277 0.01372  -0.11568 -0.04206 217 MET A C   
1457 O O   . MET A 181 ? 0.91568 1.58286 1.04867 -0.00493 -0.11970 -0.05833 217 MET A O   
1458 C CB  . MET A 181 ? 1.03153 1.66681 1.09266 0.06649  -0.15791 -0.01509 217 MET A CB  
1459 C CG  . MET A 181 ? 1.08002 1.73803 1.12383 0.06647  -0.18841 -0.03185 217 MET A CG  
1460 S SD  . MET A 181 ? 1.30068 1.98651 1.34205 0.10412  -0.23973 -0.02996 217 MET A SD  
1461 C CE  . MET A 181 ? 1.32340 1.94018 1.29126 0.12819  -0.23317 0.01262  217 MET A CE  
1462 N N   . SER A 182 ? 0.97076 1.65810 1.15254 0.01479  -0.10286 -0.04663 218 SER A N   
1463 C CA  . SER A 182 ? 1.00500 1.73214 1.24919 -0.01060 -0.08710 -0.06590 218 SER A CA  
1464 C C   . SER A 182 ? 1.00286 1.79096 1.30048 -0.01084 -0.11693 -0.09125 218 SER A C   
1465 O O   . SER A 182 ? 0.97258 1.77601 1.25961 0.01410  -0.15256 -0.09361 218 SER A O   
1466 C CB  . SER A 182 ? 1.00923 1.74943 1.28719 -0.00801 -0.05923 -0.06359 218 SER A CB  
1467 O OG  . SER A 182 ? 1.00229 1.77640 1.31072 0.02392  -0.07491 -0.06853 218 SER A OG  
1468 N N   . ILE A 183 ? 0.89768 1.71859 1.25344 -0.04113 -0.10421 -0.10915 219 ILE A N   
1469 C CA  . ILE A 183 ? 1.00330 1.88853 1.42657 -0.04760 -0.13311 -0.13631 219 ILE A CA  
1470 C C   . ILE A 183 ? 0.96194 1.90879 1.44914 -0.02035 -0.14541 -0.14163 219 ILE A C   
1471 O O   . ILE A 183 ? 0.94171 1.93245 1.45918 -0.00382 -0.18864 -0.15594 219 ILE A O   
1472 C CB  . ILE A 183 ? 0.92502 1.82701 1.40373 -0.09085 -0.11154 -0.15154 219 ILE A CB  
1473 C CG1 . ILE A 183 ? 0.90305 1.76032 1.33615 -0.11101 -0.12365 -0.16037 219 ILE A CG1 
1474 C CG2 . ILE A 183 ? 0.86180 1.84927 1.44752 -0.09998 -0.12514 -0.17613 219 ILE A CG2 
1475 C CD1 . ILE A 183 ? 0.91570 1.76683 1.39105 -0.15397 -0.10000 -0.16974 219 ILE A CD1 
1476 N N   . ASN A 184 ? 0.89630 1.84561 1.40298 -0.01284 -0.10938 -0.13134 220 ASN A N   
1477 C CA  . ASN A 184 ? 0.92093 1.92540 1.49102 0.01827  -0.11583 -0.13802 220 ASN A CA  
1478 C C   . ASN A 184 ? 0.93301 1.91441 1.45594 0.06171  -0.15498 -0.12590 220 ASN A C   
1479 O O   . ASN A 184 ? 0.96940 2.00176 1.54865 0.09139  -0.18315 -0.13478 220 ASN A O   
1480 C CB  . ASN A 184 ? 0.93580 1.93517 1.51918 0.01830  -0.06407 -0.13174 220 ASN A CB  
1481 C CG  . ASN A 184 ? 0.96306 1.98352 1.58894 -0.02475 -0.02235 -0.13888 220 ASN A CG  
1482 O OD1 . ASN A 184 ? 0.97812 1.96471 1.57258 -0.03616 0.02135  -0.12751 220 ASN A OD1 
1483 N ND2 . ASN A 184 ? 0.88110 1.95382 1.57543 -0.05019 -0.03736 -0.15710 220 ASN A ND2 
1484 N N   . THR A 185 ? 1.00943 1.91479 1.43374 0.06613  -0.15711 -0.10385 221 THR A N   
1485 C CA  . THR A 185 ? 0.97667 1.85182 1.34806 0.10269  -0.19221 -0.08743 221 THR A CA  
1486 C C   . THR A 185 ? 0.97914 1.88242 1.34765 0.10916  -0.24370 -0.09788 221 THR A C   
1487 O O   . THR A 185 ? 1.02098 1.93886 1.39315 0.14395  -0.28284 -0.09327 221 THR A O   
1488 C CB  . THR A 185 ? 1.05829 1.84914 1.33271 0.09975  -0.17622 -0.06050 221 THR A CB  
1489 O OG1 . THR A 185 ? 1.03763 1.80129 1.31217 0.09607  -0.13692 -0.05266 221 THR A OG1 
1490 C CG2 . THR A 185 ? 1.01691 1.77109 1.23308 0.13313  -0.20858 -0.03908 221 THR A CG2 
1491 N N   . HIS A 186 ? 1.01568 1.92245 1.37415 0.07712  -0.24709 -0.11277 222 HIS A N   
1492 C CA  . HIS A 186 ? 1.06041 1.99427 1.41359 0.07996  -0.29823 -0.12953 222 HIS A CA  
1493 C C   . HIS A 186 ? 1.05840 2.08061 1.52106 0.08939  -0.32955 -0.15270 222 HIS A C   
1494 O O   . HIS A 186 ? 0.91633 1.96361 1.37699 0.11126  -0.38478 -0.15895 222 HIS A O   
1495 C CB  . HIS A 186 ? 0.94292 1.85893 1.26940 0.04206  -0.29173 -0.14686 222 HIS A CB  
1496 C CG  . HIS A 186 ? 1.19082 2.02933 1.40777 0.04053  -0.27697 -0.12840 222 HIS A CG  
1497 N ND1 . HIS A 186 ? 1.30962 2.11763 1.44044 0.05978  -0.30861 -0.12109 222 HIS A ND1 
1498 C CD2 . HIS A 186 ? 1.07264 1.86092 1.25546 0.02231  -0.23317 -0.11540 222 HIS A CD2 
1499 C CE1 . HIS A 186 ? 1.18767 1.93391 1.24172 0.05266  -0.27941 -0.10531 222 HIS A CE1 
1500 N NE2 . HIS A 186 ? 1.07372 1.80894 1.16275 0.03083  -0.23621 -0.10215 222 HIS A NE2 
1501 N N   . LEU A 187 ? 1.04789 2.11955 1.60703 0.07341  -0.29537 -0.16485 223 LEU A N   
1502 C CA  . LEU A 187 ? 0.96985 2.13633 1.65276 0.07941  -0.31711 -0.18801 223 LEU A CA  
1503 C C   . LEU A 187 ? 0.95256 2.14485 1.67422 0.12811  -0.32833 -0.17800 223 LEU A C   
1504 O O   . LEU A 187 ? 1.00627 2.28389 1.84435 0.13892  -0.34193 -0.19662 223 LEU A O   
1505 C CB  . LEU A 187 ? 0.94097 2.15140 1.71366 0.03939  -0.26845 -0.20398 223 LEU A CB  
1506 C CG  . LEU A 187 ? 0.88557 2.07316 1.63947 -0.01022 -0.25875 -0.21617 223 LEU A CG  
1507 C CD1 . LEU A 187 ? 0.84035 2.06243 1.67752 -0.04903 -0.20606 -0.22400 223 LEU A CD1 
1508 C CD2 . LEU A 187 ? 0.89336 2.11327 1.66446 -0.01798 -0.32069 -0.24189 223 LEU A CD2 
1509 N N   . GLY A 188 ? 1.00734 2.12882 1.64204 0.15751  -0.32283 -0.14999 224 GLY A N   
1510 C CA  . GLY A 188 ? 1.01245 2.14349 1.67592 0.20632  -0.33607 -0.13988 224 GLY A CA  
1511 C C   . GLY A 188 ? 1.03844 2.18973 1.76712 0.21278  -0.28220 -0.14515 224 GLY A C   
1512 O O   . GLY A 188 ? 1.08666 2.25873 1.86291 0.25529  -0.29157 -0.14481 224 GLY A O   
1513 N N   . ARG A 189 ? 0.94660 2.08820 1.67407 0.17402  -0.22630 -0.15003 225 ARG A N   
1514 C CA  . ARG A 189 ? 0.94715 2.10424 1.72210 0.17750  -0.17095 -0.15635 225 ARG A CA  
1515 C C   . ARG A 189 ? 0.97835 2.04933 1.66681 0.20237  -0.15286 -0.13516 225 ARG A C   
1516 O O   . ARG A 189 ? 1.11132 2.10467 1.69835 0.19810  -0.16507 -0.11279 225 ARG A O   
1517 C CB  . ARG A 189 ? 0.94916 2.11620 1.73813 0.12606  -0.11962 -0.16447 225 ARG A CB  
1518 C CG  . ARG A 189 ? 0.94873 2.18537 1.81446 0.09177  -0.13664 -0.18425 225 ARG A CG  
1519 C CD  . ARG A 189 ? 0.99554 2.23409 1.87655 0.04139  -0.08178 -0.18793 225 ARG A CD  
1520 N NE  . ARG A 189 ? 0.93662 2.23028 1.88859 0.00387  -0.09894 -0.20648 225 ARG A NE  
1521 C CZ  . ARG A 189 ? 0.90613 2.21101 1.89150 -0.04347 -0.05826 -0.21082 225 ARG A CZ  
1522 N NH1 . ARG A 189 ? 0.95631 2.22308 1.90497 -0.05848 0.00188  -0.19648 225 ARG A NH1 
1523 N NH2 . ARG A 189 ? 0.88018 2.23104 1.93369 -0.07741 -0.08057 -0.22948 225 ARG A NH2 
1524 N N   . GLU A 190 ? 0.95355 2.03963 1.68678 0.22791  -0.12214 -0.14438 226 GLU A N   
1525 C CA  . GLU A 190 ? 0.97413 1.97695 1.63135 0.24810  -0.10194 -0.13033 226 GLU A CA  
1526 C C   . GLU A 190 ? 0.92158 1.86527 1.49987 0.20627  -0.06060 -0.12080 226 GLU A C   
1527 O O   . GLU A 190 ? 0.88410 1.85961 1.49253 0.17672  -0.01804 -0.13321 226 GLU A O   
1528 C CB  . GLU A 190 ? 0.93518 1.96913 1.66039 0.28463  -0.07473 -0.14949 226 GLU A CB  
1529 C CG  . GLU A 190 ? 0.93231 1.87577 1.58037 0.30565  -0.05516 -0.14106 226 GLU A CG  
1530 C CD  . GLU A 190 ? 1.01599 1.90097 1.62359 0.34550  -0.10447 -0.12106 226 GLU A CD  
1531 O OE1 . GLU A 190 ? 1.11561 2.03712 1.79221 0.39065  -0.13042 -0.12910 226 GLU A OE1 
1532 O OE2 . GLU A 190 ? 1.07340 1.87581 1.58355 0.33177  -0.11697 -0.09561 226 GLU A OE2 
1533 N N   . GLN A 191 ? 0.94640 1.80464 1.42639 0.20345  -0.07343 -0.09692 227 GLN A N   
1534 C CA  . GLN A 191 ? 0.96716 1.77058 1.37641 0.16580  -0.04396 -0.08581 227 GLN A CA  
1535 C C   . GLN A 191 ? 1.03019 1.80450 1.42171 0.16787  -0.00001 -0.09358 227 GLN A C   
1536 O O   . GLN A 191 ? 1.00925 1.78229 1.42187 0.20310  0.00538  -0.10460 227 GLN A O   
1537 C CB  . GLN A 191 ? 1.02702 1.75605 1.34962 0.16321  -0.06995 -0.05886 227 GLN A CB  
1538 C CG  . GLN A 191 ? 1.02162 1.77164 1.34092 0.15514  -0.10592 -0.05274 227 GLN A CG  
1539 C CD  . GLN A 191 ? 1.03679 1.72000 1.27606 0.16203  -0.12989 -0.02555 227 GLN A CD  
1540 O OE1 . GLN A 191 ? 1.07075 1.74924 1.30121 0.19097  -0.16469 -0.01575 227 GLN A OE1 
1541 N NE2 . GLN A 191 ? 0.90860 1.54078 1.09112 0.13539  -0.11123 -0.01144 227 GLN A NE2 
1542 N N   . SER A 192 ? 0.93472 1.68231 1.28365 0.13097  0.03040  -0.08879 228 SER A N   
1543 C CA  . SER A 192 ? 1.03582 1.74903 1.34878 0.12753  0.07091  -0.09548 228 SER A CA  
1544 C C   . SER A 192 ? 1.00052 1.64756 1.23103 0.09369  0.07575  -0.07578 228 SER A C   
1545 O O   . SER A 192 ? 0.99599 1.61282 1.19536 0.08445  0.04683  -0.05696 228 SER A O   
1546 C CB  . SER A 192 ? 1.03748 1.82006 1.41617 0.11939  0.11469  -0.11736 228 SER A CB  
1547 O OG  . SER A 192 ? 1.02298 1.82442 1.40512 0.07520  0.13177  -0.11069 228 SER A OG  
1548 N N   . ARG A 193 ? 0.96774 1.59333 1.16261 0.07627  0.11280  -0.07993 229 ARG A N   
1549 C CA  . ARG A 193 ? 0.97750 1.54013 1.09643 0.04700  0.11320  -0.06086 229 ARG A CA  
1550 C C   . ARG A 193 ? 0.99232 1.57399 1.12581 0.01362  0.10788  -0.04733 229 ARG A C   
1551 O O   . ARG A 193 ? 1.02621 1.56247 1.11601 -0.00170 0.08989  -0.02838 229 ARG A O   
1552 C CB  . ARG A 193 ? 0.93439 1.46839 1.00353 0.03767  0.15141  -0.06847 229 ARG A CB  
1553 C CG  . ARG A 193 ? 1.01619 1.49621 1.03664 0.06490  0.14965  -0.07984 229 ARG A CG  
1554 C CD  . ARG A 193 ? 1.10166 1.55086 1.05943 0.05521  0.18790  -0.09060 229 ARG A CD  
1555 N NE  . ARG A 193 ? 1.15572 1.66197 1.15966 0.06963  0.23286  -0.11557 229 ARG A NE  
1556 C CZ  . ARG A 193 ? 1.24904 1.73671 1.20301 0.07063  0.27503  -0.13196 229 ARG A CZ  
1557 N NH1 . ARG A 193 ? 1.41745 1.82734 1.26627 0.05737  0.27298  -0.12646 229 ARG A NH1 
1558 N NH2 . ARG A 193 ? 1.25392 1.80398 1.26478 0.08574  0.32019  -0.15540 229 ARG A NH2 
1559 N N   . ARG A 194 ? 0.87701 1.52522 1.07734 0.00212  0.12317  -0.05825 230 ARG A N   
1560 C CA  . ARG A 194 ? 0.81634 1.47740 1.03296 -0.03106 0.11980  -0.04941 230 ARG A CA  
1561 C C   . ARG A 194 ? 0.86052 1.52007 1.08343 -0.02559 0.07835  -0.04352 230 ARG A C   
1562 O O   . ARG A 194 ? 0.83847 1.48142 1.04938 -0.04954 0.07138  -0.03403 230 ARG A O   
1563 C CB  . ARG A 194 ? 0.95786 1.69154 1.25293 -0.04701 0.14610  -0.06490 230 ARG A CB  
1564 C CG  . ARG A 194 ? 0.77342 1.57997 1.15324 -0.02245 0.12708  -0.08494 230 ARG A CG  
1565 C CD  . ARG A 194 ? 0.95557 1.84021 1.42384 -0.03588 0.16064  -0.10250 230 ARG A CD  
1566 N NE  . ARG A 194 ? 0.97314 1.92635 1.52867 -0.03823 0.13090  -0.11640 230 ARG A NE  
1567 C CZ  . ARG A 194 ? 0.76302 1.79776 1.41886 -0.05085 0.14918  -0.13373 230 ARG A CZ  
1568 N NH1 . ARG A 194 ? 0.83298 1.89491 1.51680 -0.06094 0.20379  -0.13849 230 ARG A NH1 
1569 N NH2 . ARG A 194 ? 0.89174 1.98331 1.62181 -0.05457 0.11227  -0.14732 230 ARG A NH2 
1570 N N   . ASP A 195 ? 0.83798 1.51061 1.07526 0.00656  0.05179  -0.04860 231 ASP A N   
1571 C CA  . ASP A 195 ? 0.88149 1.54912 1.11096 0.01231  0.01524  -0.04152 231 ASP A CA  
1572 C C   . ASP A 195 ? 0.93550 1.53340 1.09458 0.01210  0.00460  -0.01945 231 ASP A C   
1573 O O   . ASP A 195 ? 0.95058 1.53629 1.09240 0.00541  -0.01281 -0.01093 231 ASP A O   
1574 C CB  . ASP A 195 ? 0.91577 1.62148 1.18288 0.04658  -0.01169 -0.05112 231 ASP A CB  
1575 C CG  . ASP A 195 ? 0.90086 1.68799 1.25441 0.04458  -0.01046 -0.07376 231 ASP A CG  
1576 O OD1 . ASP A 195 ? 0.90788 1.71944 1.29104 0.01284  0.01375  -0.08110 231 ASP A OD1 
1577 O OD2 . ASP A 195 ? 0.98106 1.80758 1.37709 0.07424  -0.03529 -0.08292 231 ASP A OD2 
1578 N N   . ASP A 196 ? 0.90399 1.45690 1.02421 0.01867  0.01540  -0.01197 232 ASP A N   
1579 C CA  . ASP A 196 ? 0.93858 1.43021 1.00427 0.01216  0.00616  0.00858  232 ASP A CA  
1580 C C   . ASP A 196 ? 0.97995 1.45325 1.02884 -0.01907 0.01770  0.01758  232 ASP A C   
1581 O O   . ASP A 196 ? 0.89234 1.32815 0.91312 -0.02646 0.00748  0.03418  232 ASP A O   
1582 C CB  . ASP A 196 ? 0.88650 1.33274 0.91791 0.02651  0.00863  0.01057  232 ASP A CB  
1583 C CG  . ASP A 196 ? 0.87923 1.32001 0.91723 0.05907  -0.01030 0.00994  232 ASP A CG  
1584 O OD1 . ASP A 196 ? 0.91956 1.37959 0.97187 0.06859  -0.03013 0.01638  232 ASP A OD1 
1585 O OD2 . ASP A 196 ? 0.90058 1.31220 0.92409 0.07597  -0.00647 0.00304  232 ASP A OD2 
1586 N N   . LEU A 197 ? 0.88761 1.38633 0.95755 -0.03726 0.03928  0.00857  233 LEU A N   
1587 C CA  . LEU A 197 ? 0.93026 1.40680 0.98529 -0.06579 0.04866  0.01947  233 LEU A CA  
1588 C C   . LEU A 197 ? 0.82109 1.32220 0.91005 -0.07968 0.04221  0.01541  233 LEU A C   
1589 O O   . LEU A 197 ? 0.79143 1.26258 0.86565 -0.09430 0.03879  0.02707  233 LEU A O   
1590 C CB  . LEU A 197 ? 1.01085 1.48787 1.05787 -0.08157 0.07877  0.01674  233 LEU A CB  
1591 C CG  . LEU A 197 ? 1.12184 1.56054 1.11632 -0.07236 0.08757  0.01879  233 LEU A CG  
1592 C CD1 . LEU A 197 ? 1.12370 1.54782 1.08788 -0.09447 0.11720  0.02334  233 LEU A CD1 
1593 C CD2 . LEU A 197 ? 0.91792 1.30233 0.86910 -0.06741 0.06101  0.03442  233 LEU A CD2 
1594 N N   . GLU A 198 ? 0.86398 1.41793 1.00037 -0.07457 0.03823  -0.00285 234 GLU A N   
1595 C CA  . GLU A 198 ? 0.90345 1.47549 1.06567 -0.08681 0.02633  -0.01161 234 GLU A CA  
1596 C C   . GLU A 198 ? 0.83624 1.38403 0.96702 -0.07321 0.00405  -0.00450 234 GLU A C   
1597 O O   . GLU A 198 ? 0.82100 1.35118 0.94533 -0.08537 0.00132  -0.00398 234 GLU A O   
1598 C CB  . GLU A 198 ? 0.76613 1.40292 0.98840 -0.08443 0.02038  -0.03465 234 GLU A CB  
1599 C CG  . GLU A 198 ? 0.83522 1.48839 1.07969 -0.09694 0.00168  -0.04928 234 GLU A CG  
1600 C CD  . GLU A 198 ? 0.92335 1.64444 1.23447 -0.09698 -0.01117 -0.07358 234 GLU A CD  
1601 O OE1 . GLU A 198 ? 0.97506 1.73595 1.32635 -0.08916 0.00117  -0.07822 234 GLU A OE1 
1602 O OE2 . GLU A 198 ? 0.86572 1.60157 1.19131 -0.10418 -0.03435 -0.09009 234 GLU A OE2 
1603 N N   . ALA A 199 ? 0.86667 1.41051 0.97746 -0.04769 -0.00919 0.00136  235 ALA A N   
1604 C CA  . ALA A 199 ? 0.85371 1.37107 0.92933 -0.03667 -0.02359 0.01324  235 ALA A CA  
1605 C C   . ALA A 199 ? 0.80823 1.28028 0.85922 -0.04921 -0.01349 0.03121  235 ALA A C   
1606 O O   . ALA A 199 ? 0.74415 1.20217 0.78238 -0.05070 -0.01585 0.03608  235 ALA A O   
1607 C CB  . ALA A 199 ? 0.84652 1.35859 0.90438 -0.00963 -0.03715 0.02165  235 ALA A CB  
1608 N N   . LEU A 200 ? 0.79053 1.24038 0.83459 -0.05711 -0.00268 0.04017  236 LEU A N   
1609 C CA  . LEU A 200 ? 0.84032 1.25123 0.86864 -0.06988 0.00080  0.05677  236 LEU A CA  
1610 C C   . LEU A 200 ? 0.82803 1.23907 0.87403 -0.08725 0.00696  0.05241  236 LEU A C   
1611 O O   . LEU A 200 ? 0.81132 1.20110 0.85598 -0.08970 0.00513  0.06163  236 LEU A O   
1612 C CB  . LEU A 200 ? 0.83952 1.22492 0.84781 -0.07570 0.00654  0.06467  236 LEU A CB  
1613 C CG  . LEU A 200 ? 0.89033 1.24989 0.87328 -0.06220 -0.00316 0.07302  236 LEU A CG  
1614 C CD1 . LEU A 200 ? 0.96350 1.28787 0.91603 -0.07229 -0.00133 0.07942  236 LEU A CD1 
1615 C CD2 . LEU A 200 ? 0.93885 1.28291 0.92140 -0.05741 -0.01523 0.08759  236 LEU A CD2 
1616 N N   . GLY A 201 ? 0.86883 1.30343 0.93771 -0.09953 0.01533  0.03786  237 GLY A N   
1617 C CA  . GLY A 201 ? 0.85888 1.28745 0.94698 -0.11717 0.01972  0.03172  237 GLY A CA  
1618 C C   . GLY A 201 ? 0.88734 1.32137 0.97861 -0.10903 0.01012  0.01980  237 GLY A C   
1619 O O   . GLY A 201 ? 0.95988 1.36851 1.05303 -0.11400 0.01247  0.02182  237 GLY A O   
1620 N N   . HIS A 202 ? 0.84075 1.30548 0.92896 -0.09420 -0.00101 0.00710  238 HIS A N   
1621 C CA  . HIS A 202 ? 0.85719 1.32382 0.93134 -0.08505 -0.00961 -0.00457 238 HIS A CA  
1622 C C   . HIS A 202 ? 0.88045 1.31595 0.93070 -0.07602 -0.00277 0.01340  238 HIS A C   
1623 O O   . HIS A 202 ? 0.85454 1.27792 0.90035 -0.07568 0.00249  0.00517  238 HIS A O   
1624 C CB  . HIS A 202 ? 0.84718 1.34656 0.91053 -0.06784 -0.02716 -0.01453 238 HIS A CB  
1625 C CG  . HIS A 202 ? 0.97117 1.51253 1.07341 -0.07519 -0.03648 -0.03481 238 HIS A CG  
1626 N ND1 . HIS A 202 ? 0.96055 1.53750 1.07008 -0.05794 -0.05414 -0.04030 238 HIS A ND1 
1627 C CD2 . HIS A 202 ? 0.90847 1.46369 1.05211 -0.09859 -0.03043 -0.04998 238 HIS A CD2 
1628 C CE1 . HIS A 202 ? 0.92559 1.54408 1.08641 -0.06987 -0.05843 -0.05982 238 HIS A CE1 
1629 N NE2 . HIS A 202 ? 0.88603 1.49160 1.06754 -0.09680 -0.04261 -0.06553 238 HIS A NE2 
1630 N N   . VAL A 203 ? 0.83805 1.26097 0.87728 -0.06908 -0.00176 0.03595  239 VAL A N   
1631 C CA  . VAL A 203 ? 0.84634 1.24631 0.87667 -0.06368 0.00455  0.05447  239 VAL A CA  
1632 C C   . VAL A 203 ? 0.84263 1.22091 0.89687 -0.07506 0.01215  0.05914  239 VAL A C   
1633 O O   . VAL A 203 ? 0.80952 1.17890 0.87188 -0.07038 0.02067  0.06294  239 VAL A O   
1634 C CB  . VAL A 203 ? 0.91296 1.30182 0.93176 -0.05745 -0.00065 0.07537  239 VAL A CB  
1635 C CG1 . VAL A 203 ? 0.72558 1.09439 0.75119 -0.05798 0.00491  0.09556  239 VAL A CG1 
1636 C CG2 . VAL A 203 ? 0.83781 1.24050 0.83312 -0.04159 -0.00929 0.07383  239 VAL A CG2 
1637 N N   . PHE A 204 ? 0.87152 1.24044 0.93789 -0.08895 0.01054  0.05999  240 PHE A N   
1638 C CA  . PHE A 204 ? 0.80896 1.15045 0.89466 -0.09824 0.01301  0.06837  240 PHE A CA  
1639 C C   . PHE A 204 ? 0.88733 1.22547 0.98963 -0.09836 0.02019  0.04939  240 PHE A C   
1640 O O   . PHE A 204 ? 0.90335 1.22556 1.02326 -0.09193 0.02507  0.05368  240 PHE A O   
1641 C CB  . PHE A 204 ? 0.78484 1.11183 0.86720 -0.11443 0.01157  0.07553  240 PHE A CB  
1642 C CG  . PHE A 204 ? 0.81337 1.13783 0.87106 -0.11327 0.00629  0.08879  240 PHE A CG  
1643 C CD1 . PHE A 204 ? 0.89073 1.21157 0.93985 -0.10181 -0.00215 0.10029  240 PHE A CD1 
1644 C CD2 . PHE A 204 ? 0.82991 1.15347 0.87304 -0.12466 0.01223  0.08831  240 PHE A CD2 
1645 C CE1 . PHE A 204 ? 0.83814 1.14913 0.86223 -0.10081 -0.00897 0.10802  240 PHE A CE1 
1646 C CE2 . PHE A 204 ? 0.90335 1.22015 0.91745 -0.12133 0.00972  0.09546  240 PHE A CE2 
1647 C CZ  . PHE A 204 ? 0.92411 1.23184 0.92744 -0.10891 -0.00311 0.10382  240 PHE A CZ  
1648 N N   . PHE A 205 ? 0.80513 1.15884 0.90640 -0.10504 0.02005  0.02573  241 PHE A N   
1649 C CA  . PHE A 205 ? 0.90333 1.24919 1.01371 -0.10540 0.02413  0.00137  241 PHE A CA  
1650 C C   . PHE A 205 ? 0.90276 1.25664 0.99271 -0.08604 0.03049  -0.00696 241 PHE A C   
1651 O O   . PHE A 205 ? 0.96325 1.30046 1.05940 -0.08028 0.04032  -0.02134 241 PHE A O   
1652 C CB  . PHE A 205 ? 0.95441 1.31866 1.07073 -0.11942 0.01734  -0.02421 241 PHE A CB  
1653 C CG  . PHE A 205 ? 1.00403 1.35963 1.14431 -0.14249 0.01935  -0.01684 241 PHE A CG  
1654 C CD1 . PHE A 205 ? 1.05732 1.37475 1.21837 -0.15723 0.02414  -0.01736 241 PHE A CD1 
1655 C CD2 . PHE A 205 ? 0.94676 1.32954 1.08760 -0.14880 0.01917  -0.00884 241 PHE A CD2 
1656 C CE1 . PHE A 205 ? 1.08870 1.39351 1.26513 -0.18104 0.02949  -0.00591 241 PHE A CE1 
1657 C CE2 . PHE A 205 ? 1.02093 1.39682 1.17895 -0.17124 0.02818  -0.00089 241 PHE A CE2 
1658 C CZ  . PHE A 205 ? 1.12753 1.46364 1.30063 -0.18902 0.03373  0.00252  241 PHE A CZ  
1659 N N   . TYR A 206 ? 0.94330 1.31889 1.00641 -0.07528 0.02740  0.00215  242 TYR A N   
1660 C CA  . TYR A 206 ? 1.01585 1.39575 1.05136 -0.05881 0.03790  0.00108  242 TYR A CA  
1661 C C   . TYR A 206 ? 0.88113 1.24620 0.94143 -0.05288 0.05518  0.01812  242 TYR A C   
1662 O O   . TYR A 206 ? 0.95024 1.31135 1.00731 -0.04278 0.07333  0.00658  242 TYR A O   
1663 C CB  . TYR A 206 ? 0.94518 1.34291 0.94848 -0.05011 0.02954  0.01488  242 TYR A CB  
1664 C CG  . TYR A 206 ? 0.95051 1.34694 0.92219 -0.03620 0.04412  0.02634  242 TYR A CG  
1665 C CD1 . TYR A 206 ? 1.00217 1.40156 0.92870 -0.02658 0.04949  0.00760  242 TYR A CD1 
1666 C CD2 . TYR A 206 ? 0.88704 1.27760 0.87070 -0.03467 0.05266  0.05616  242 TYR A CD2 
1667 C CE1 . TYR A 206 ? 0.97373 1.36962 0.86310 -0.01535 0.06863  0.02133  242 TYR A CE1 
1668 C CE2 . TYR A 206 ? 0.80755 1.19747 0.76676 -0.02589 0.07080  0.06997  242 TYR A CE2 
1669 C CZ  . TYR A 206 ? 0.88711 1.27947 0.79668 -0.01602 0.08147  0.05407  242 TYR A CZ  
1670 O OH  . TYR A 206 ? 0.93608 1.32548 0.81344 -0.00867 0.10519  0.07085  242 TYR A OH  
1671 N N   . PHE A 207 ? 0.85738 1.21569 0.94421 -0.05836 0.04935  0.04392  243 PHE A N   
1672 C CA  . PHE A 207 ? 0.83745 1.18736 0.96221 -0.05373 0.05897  0.06059  243 PHE A CA  
1673 C C   . PHE A 207 ? 0.88099 1.21144 1.03961 -0.05272 0.06408  0.04771  243 PHE A C   
1674 O O   . PHE A 207 ? 0.85249 1.18263 1.04412 -0.04128 0.07932  0.04899  243 PHE A O   
1675 C CB  . PHE A 207 ? 0.69773 1.04129 0.83873 -0.06159 0.04260  0.08816  243 PHE A CB  
1676 C CG  . PHE A 207 ? 0.72890 1.08332 0.84964 -0.05996 0.04023  0.10374  243 PHE A CG  
1677 C CD1 . PHE A 207 ? 0.73173 1.09982 0.83313 -0.05069 0.05707  0.10314  243 PHE A CD1 
1678 C CD2 . PHE A 207 ? 0.70404 1.04855 0.81976 -0.06781 0.02175  0.11934  243 PHE A CD2 
1679 C CE1 . PHE A 207 ? 0.86925 1.23884 0.95209 -0.05030 0.05440  0.12112  243 PHE A CE1 
1680 C CE2 . PHE A 207 ? 0.70333 1.04930 0.80254 -0.06621 0.01823  0.13225  243 PHE A CE2 
1681 C CZ  . PHE A 207 ? 0.85891 1.21637 0.94449 -0.05795 0.03402  0.13483  243 PHE A CZ  
1682 N N   . LEU A 208 ? 0.91206 1.22561 1.06820 -0.06440 0.05311  0.03581  244 LEU A N   
1683 C CA  . LEU A 208 ? 0.79593 1.07952 0.98421 -0.06515 0.05452  0.02729  244 LEU A CA  
1684 C C   . LEU A 208 ? 0.89422 1.17287 1.07789 -0.05441 0.07147  -0.00644 244 LEU A C   
1685 O O   . LEU A 208 ? 1.02812 1.29003 1.24526 -0.04138 0.08348  -0.01225 244 LEU A O   
1686 C CB  . LEU A 208 ? 0.90858 1.17145 1.09312 -0.08544 0.04028  0.02879  244 LEU A CB  
1687 C CG  . LEU A 208 ? 0.85889 1.10944 1.04633 -0.09462 0.02576  0.06154  244 LEU A CG  
1688 C CD1 . LEU A 208 ? 0.91556 1.15308 1.08686 -0.11658 0.02060  0.06224  244 LEU A CD1 
1689 C CD2 . LEU A 208 ? 0.82909 1.05190 1.05467 -0.08570 0.01979  0.07923  244 LEU A CD2 
1690 N N   . ARG A 209 ? 1.03578 1.32775 1.17818 -0.05810 0.07082  -0.03086 245 ARG A N   
1691 C CA  . ARG A 209 ? 1.12734 1.40898 1.25117 -0.05016 0.08213  -0.06842 245 ARG A CA  
1692 C C   . ARG A 209 ? 1.11776 1.41834 1.20858 -0.03073 0.10413  -0.07426 245 ARG A C   
1693 O O   . ARG A 209 ? 1.16034 1.44900 1.22768 -0.02033 0.11877  -0.10648 245 ARG A O   
1694 C CB  . ARG A 209 ? 1.24453 1.53011 1.34080 -0.06619 0.06411  -0.09437 245 ARG A CB  
1695 C CG  . ARG A 209 ? 1.38861 1.64091 1.49084 -0.07121 0.06372  -0.13253 245 ARG A CG  
1696 C CD  . ARG A 209 ? 1.36916 1.62774 1.46905 -0.09543 0.04069  -0.15146 245 ARG A CD  
1697 N NE  . ARG A 209 ? 1.46833 1.74222 1.52137 -0.09184 0.03067  -0.18714 245 ARG A NE  
1698 C CZ  . ARG A 209 ? 1.61078 1.85620 1.64800 -0.09155 0.02952  -0.22914 245 ARG A CZ  
1699 N NH1 . ARG A 209 ? 1.59557 1.79377 1.66542 -0.09308 0.04026  -0.24145 245 ARG A NH1 
1700 N NH2 . ARG A 209 ? 1.60809 1.86834 1.59233 -0.08840 0.01464  -0.26031 245 ARG A NH2 
1701 N N   . GLY A 210 ? 1.03480 1.36015 1.11981 -0.02663 0.10853  -0.04434 246 GLY A N   
1702 C CA  . GLY A 210 ? 1.13274 1.47506 1.17855 -0.01275 0.13097  -0.04381 246 GLY A CA  
1703 C C   . GLY A 210 ? 1.16924 1.52019 1.14208 -0.01284 0.12045  -0.05971 246 GLY A C   
1704 O O   . GLY A 210 ? 1.18012 1.54181 1.10763 -0.00312 0.13573  -0.05068 246 GLY A O   
1705 N N   . GLN A 211 ? 1.28109 1.62804 1.24319 -0.02413 0.09388  -0.08125 247 GLN A N   
1706 C CA  . GLN A 211 ? 1.26346 1.62317 1.16598 -0.02400 0.07410  -0.09724 247 GLN A CA  
1707 C C   . GLN A 211 ? 1.30397 1.67173 1.23455 -0.04209 0.04289  -0.10713 247 GLN A C   
1708 O O   . GLN A 211 ? 1.25403 1.61256 1.23844 -0.05514 0.04154  -0.09938 247 GLN A O   
1709 C CB  . GLN A 211 ? 1.31559 1.66062 1.16126 -0.01364 0.08417  -0.13483 247 GLN A CB  
1710 C CG  . GLN A 211 ? 1.36974 1.68988 1.23880 -0.02266 0.07696  -0.17453 247 GLN A CG  
1711 C CD  . GLN A 211 ? 1.48335 1.79024 1.28253 -0.01708 0.06986  -0.21900 247 GLN A CD  
1712 O OE1 . GLN A 211 ? 1.53484 1.84097 1.26493 -0.00040 0.08752  -0.22199 247 GLN A OE1 
1713 N NE2 . GLN A 211 ? 1.46067 1.75491 1.27410 -0.03289 0.04352  -0.25374 247 GLN A NE2 
1714 N N   . LEU A 212 ? 1.38945 1.77553 1.28378 -0.04286 0.01789  -0.12304 248 LEU A N   
1715 C CA  . LEU A 212 ? 1.29155 1.69562 1.21911 -0.06026 -0.01022 -0.13645 248 LEU A CA  
1716 C C   . LEU A 212 ? 1.27361 1.67971 1.16886 -0.06314 -0.03297 -0.17865 248 LEU A C   
1717 O O   . LEU A 212 ? 1.30147 1.70200 1.12847 -0.04735 -0.03396 -0.19032 248 LEU A O   
1718 C CB  . LEU A 212 ? 1.22782 1.66430 1.16223 -0.05763 -0.02610 -0.11075 248 LEU A CB  
1719 C CG  . LEU A 212 ? 1.12317 1.55510 1.09033 -0.05897 -0.01023 -0.07410 248 LEU A CG  
1720 C CD1 . LEU A 212 ? 1.05448 1.51229 1.02176 -0.05280 -0.02506 -0.05493 248 LEU A CD1 
1721 C CD2 . LEU A 212 ? 1.08674 1.50446 1.10756 -0.07872 -0.00325 -0.07500 248 LEU A CD2 
1722 N N   . PRO A 213 ? 1.19526 1.60710 1.13560 -0.08493 -0.05166 -0.20232 249 PRO A N   
1723 C CA  . PRO A 213 ? 1.22907 1.64093 1.14425 -0.09121 -0.07889 -0.24718 249 PRO A CA  
1724 C C   . PRO A 213 ? 1.32787 1.77600 1.19934 -0.07939 -0.11270 -0.25111 249 PRO A C   
1725 O O   . PRO A 213 ? 1.43041 1.87184 1.24843 -0.07552 -0.13533 -0.28500 249 PRO A O   
1726 C CB  . PRO A 213 ? 1.21034 1.62563 1.20217 -0.12227 -0.08995 -0.26270 249 PRO A CB  
1727 C CG  . PRO A 213 ? 1.16911 1.60500 1.21259 -0.12853 -0.07655 -0.22250 249 PRO A CG  
1728 C CD  . PRO A 213 ? 1.21612 1.63205 1.22954 -0.10712 -0.04829 -0.18943 249 PRO A CD  
1729 N N   . TRP A 214 ? 1.22912 1.71151 1.11834 -0.07189 -0.11934 -0.21853 250 TRP A N   
1730 C CA  . TRP A 214 ? 1.32484 1.83890 1.17637 -0.05579 -0.15393 -0.21660 250 TRP A CA  
1731 C C   . TRP A 214 ? 1.32298 1.81717 1.09170 -0.02916 -0.14034 -0.18965 250 TRP A C   
1732 O O   . TRP A 214 ? 1.31775 1.83042 1.06882 -0.01304 -0.15630 -0.16485 250 TRP A O   
1733 C CB  . TRP A 214 ? 1.26803 1.82911 1.19025 -0.05994 -0.16905 -0.19942 250 TRP A CB  
1734 C CG  . TRP A 214 ? 1.21722 1.77178 1.17291 -0.05928 -0.13564 -0.16186 250 TRP A CG  
1735 C CD1 . TRP A 214 ? 1.15996 1.70365 1.08236 -0.03923 -0.12226 -0.12679 250 TRP A CD1 
1736 C CD2 . TRP A 214 ? 1.16241 1.71648 1.18621 -0.08117 -0.11408 -0.15596 250 TRP A CD2 
1737 N NE1 . TRP A 214 ? 1.11481 1.65241 1.08067 -0.04697 -0.09699 -0.10333 250 TRP A NE1 
1738 C CE2 . TRP A 214 ? 1.12937 1.67270 1.15244 -0.07155 -0.09123 -0.11945 250 TRP A CE2 
1739 C CE3 . TRP A 214 ? 1.16111 1.71827 1.24251 -0.10950 -0.11241 -0.17675 250 TRP A CE3 
1740 C CZ2 . TRP A 214 ? 1.11657 1.65235 1.18515 -0.08718 -0.06911 -0.10421 250 TRP A CZ2 
1741 C CZ3 . TRP A 214 ? 1.17750 1.72584 1.30487 -0.12557 -0.08650 -0.15724 250 TRP A CZ3 
1742 C CH2 . TRP A 214 ? 1.07267 1.61056 1.18890 -0.11331 -0.06617 -0.12180 250 TRP A CH2 
1743 N N   . GLN A 215 ? 1.52307 1.97826 1.24324 -0.02399 -0.10866 -0.19346 251 GLN A N   
1744 C CA  . GLN A 215 ? 1.54827 1.98354 1.19455 -0.00319 -0.08558 -0.16654 251 GLN A CA  
1745 C C   . GLN A 215 ? 1.61556 2.02894 1.16300 0.00750  -0.09217 -0.19508 251 GLN A C   
1746 O O   . GLN A 215 ? 1.63729 2.03571 1.17828 -0.00146 -0.09651 -0.23796 251 GLN A O   
1747 C CB  . GLN A 215 ? 1.51457 1.92819 1.18986 -0.00447 -0.03668 -0.14477 251 GLN A CB  
1748 C CG  . GLN A 215 ? 1.47138 1.87934 1.11648 0.00942  -0.01347 -0.10104 251 GLN A CG  
1749 C CD  . GLN A 215 ? 1.46724 1.86795 1.17475 0.00328  0.02151  -0.07687 251 GLN A CD  
1750 O OE1 . GLN A 215 ? 1.41796 1.81915 1.19160 -0.00998 0.02275  -0.08647 251 GLN A OE1 
1751 N NE2 . GLN A 215 ? 1.51974 1.91251 1.20687 0.01169  0.04798  -0.04373 251 GLN A NE2 
1752 N N   . GLY A 216 ? 1.57482 1.98070 1.03913 0.02643  -0.09291 -0.17099 252 GLY A N   
1753 C CA  . GLY A 216 ? 1.63103 2.01206 0.98141 0.03830  -0.09794 -0.19382 252 GLY A CA  
1754 C C   . GLY A 216 ? 1.62134 2.01444 0.94657 0.03462  -0.15623 -0.23540 252 GLY A C   
1755 O O   . GLY A 216 ? 1.62192 1.98902 0.86674 0.03735  -0.16139 -0.27306 252 GLY A O   
1756 N N   . LEU A 217 ? 1.59314 2.02656 0.98788 0.02845  -0.20047 -0.23195 253 LEU A N   
1757 C CA  . LEU A 217 ? 1.58213 2.03756 0.97141 0.02333  -0.26149 -0.27028 253 LEU A CA  
1758 C C   . LEU A 217 ? 1.62851 2.07829 0.90735 0.04699  -0.30012 -0.25887 253 LEU A C   
1759 O O   . LEU A 217 ? 1.64207 2.09027 0.89402 0.06524  -0.29426 -0.21171 253 LEU A O   
1760 C CB  . LEU A 217 ? 1.51577 2.02433 1.03068 0.00879  -0.29046 -0.26945 253 LEU A CB  
1761 C CG  . LEU A 217 ? 1.43466 1.94750 1.05519 -0.01758 -0.25905 -0.27960 253 LEU A CG  
1762 C CD1 . LEU A 217 ? 1.39727 1.96534 1.12867 -0.03419 -0.29056 -0.28620 253 LEU A CD1 
1763 C CD2 . LEU A 217 ? 1.49332 1.96795 1.09055 -0.03244 -0.24642 -0.32436 253 LEU A CD2 
1764 N N   . LYS A 218 ? 1.64542 2.08683 0.85671 0.04618  -0.34242 -0.30214 254 LYS A N   
1765 C CA  . LYS A 218 ? 1.81898 2.24688 0.90606 0.06872  -0.38458 -0.29524 254 LYS A CA  
1766 C C   . LYS A 218 ? 1.90490 2.38423 1.04336 0.07128  -0.46351 -0.30337 254 LYS A C   
1767 O O   . LYS A 218 ? 1.89829 2.41359 1.12770 0.04982  -0.49540 -0.34355 254 LYS A O   
1768 C CB  . LYS A 218 ? 1.96727 2.34761 0.92589 0.06955  -0.38374 -0.33926 254 LYS A CB  
1769 C CG  . LYS A 218 ? 2.00645 2.33538 0.83168 0.08883  -0.33046 -0.30952 254 LYS A CG  
1770 C CD  . LYS A 218 ? 2.06101 2.34172 0.76867 0.08884  -0.31469 -0.35963 254 LYS A CD  
1771 C CE  . LYS A 218 ? 2.02946 2.30054 0.81834 0.07023  -0.26703 -0.39702 254 LYS A CE  
1772 N NZ  . LYS A 218 ? 2.13119 2.34918 0.80398 0.07498  -0.24118 -0.44590 254 LYS A NZ  
1773 N N   . ALA A 219 ? 1.99056 2.47301 1.07591 0.09757  -0.49414 -0.26365 255 ALA A N   
1774 C CA  . ALA A 219 ? 1.98171 2.50467 1.12035 0.10459  -0.56627 -0.26160 255 ALA A CA  
1775 C C   . ALA A 219 ? 2.07397 2.55059 1.10241 0.12889  -0.58643 -0.21621 255 ALA A C   
1776 O O   . ALA A 219 ? 2.14642 2.57711 1.08631 0.14203  -0.54101 -0.17789 255 ALA A O   
1777 C CB  . ALA A 219 ? 1.90014 2.48997 1.19230 0.10423  -0.56718 -0.24498 255 ALA A CB  
1778 N N   . PRO A 220 ? 2.14962 2.63836 1.18449 0.13271  -0.65341 -0.21761 256 PRO A N   
1779 C CA  . PRO A 220 ? 2.21397 2.65840 1.14060 0.15318  -0.67669 -0.17348 256 PRO A CA  
1780 C C   . PRO A 220 ? 2.21188 2.64558 1.14584 0.17711  -0.65092 -0.11251 256 PRO A C   
1781 O O   . PRO A 220 ? 2.22469 2.59940 1.04786 0.18490  -0.61139 -0.07623 256 PRO A O   
1782 C CB  . PRO A 220 ? 2.19863 2.68416 1.18094 0.15217  -0.75666 -0.18812 256 PRO A CB  
1783 C CG  . PRO A 220 ? 2.16347 2.68472 1.21976 0.12321  -0.76962 -0.25066 256 PRO A CG  
1784 C CD  . PRO A 220 ? 2.05195 2.59344 1.18676 0.11441  -0.70958 -0.26113 256 PRO A CD  
1785 N N   . THR A 221 ? 2.19199 2.68058 1.25763 0.18745  -0.67018 -0.10115 257 THR A N   
1786 C CA  . THR A 221 ? 2.14456 2.62390 1.23291 0.21011  -0.64879 -0.04859 257 THR A CA  
1787 C C   . THR A 221 ? 2.05435 2.57646 1.24951 0.20306  -0.60222 -0.05764 257 THR A C   
1788 O O   . THR A 221 ? 2.01562 2.55660 1.23091 0.18024  -0.57347 -0.09599 257 THR A O   
1789 C CB  . THR A 221 ? 2.13340 2.63732 1.27833 0.23212  -0.71040 -0.02648 257 THR A CB  
1790 O OG1 . THR A 221 ? 2.25964 2.75678 1.34388 0.22801  -0.76562 -0.04113 257 THR A OG1 
1791 C CG2 . THR A 221 ? 2.16562 2.62076 1.26328 0.25761  -0.69717 0.03555  257 THR A CG2 
1792 N N   . ASN A 222 ? 2.02721 2.56296 1.28869 0.22196  -0.59506 -0.02271 258 ASN A N   
1793 C CA  . ASN A 222 ? 1.97652 2.54120 1.33135 0.21132  -0.54438 -0.02343 258 ASN A CA  
1794 C C   . ASN A 222 ? 1.90046 2.54236 1.41282 0.20407  -0.56353 -0.05335 258 ASN A C   
1795 O O   . ASN A 222 ? 1.81567 2.47568 1.40774 0.17736  -0.51786 -0.07040 258 ASN A O   
1796 C CB  . ASN A 222 ? 2.00372 2.52319 1.34291 0.22775  -0.51040 0.03151  258 ASN A CB  
1797 C CG  . ASN A 222 ? 2.02046 2.55056 1.38778 0.26433  -0.56245 0.05803  258 ASN A CG  
1798 O OD1 . ASN A 222 ? 2.03620 2.62801 1.52164 0.27197  -0.59085 0.03812  258 ASN A OD1 
1799 N ND2 . ASN A 222 ? 1.99762 2.45814 1.26979 0.28151  -0.56485 0.10517  258 ASN A ND2 
1800 N N   . LYS A 223 ? 1.92900 2.61188 1.49270 0.22541  -0.62495 -0.05685 259 LYS A N   
1801 C CA  . LYS A 223 ? 1.86151 2.62764 1.58048 0.21781  -0.64168 -0.08797 259 LYS A CA  
1802 C C   . LYS A 223 ? 1.81341 2.61557 1.57204 0.17926  -0.63548 -0.13895 259 LYS A C   
1803 O O   . LYS A 223 ? 1.75644 2.58475 1.61038 0.15325  -0.59151 -0.15333 259 LYS A O   
1804 C CB  . LYS A 223 ? 1.82328 2.61342 1.59087 0.23885  -0.70269 -0.08318 259 LYS A CB  
1805 C CG  . LYS A 223 ? 1.83158 2.61312 1.62993 0.27662  -0.70735 -0.04256 259 LYS A CG  
1806 C CD  . LYS A 223 ? 1.78167 2.60594 1.65879 0.29597  -0.76581 -0.04427 259 LYS A CD  
1807 C CE  . LYS A 223 ? 1.73818 2.65818 1.78284 0.28187  -0.76542 -0.08303 259 LYS A CE  
1808 N NZ  . LYS A 223 ? 1.68436 2.65301 1.82153 0.30544  -0.81478 -0.08007 259 LYS A NZ  
1809 N N   . GLN A 224 ? 1.77837 2.55461 1.46341 0.16766  -0.66714 -0.16051 260 GLN A N   
1810 C CA  . GLN A 224 ? 1.72797 2.52081 1.43336 0.13108  -0.66202 -0.21002 260 GLN A CA  
1811 C C   . GLN A 224 ? 1.72967 2.48184 1.39771 0.11108  -0.59109 -0.20951 260 GLN A C   
1812 O O   . GLN A 224 ? 1.62053 2.38905 1.36007 0.07825  -0.56423 -0.23925 260 GLN A O   
1813 C CB  . GLN A 224 ? 1.75837 2.51331 1.36901 0.12505  -0.70638 -0.23002 260 GLN A CB  
1814 C CG  . GLN A 224 ? 1.80127 2.56312 1.40879 0.14665  -0.76888 -0.21096 260 GLN A CG  
1815 C CD  . GLN A 224 ? 1.87731 2.58246 1.37908 0.18063  -0.76569 -0.15677 260 GLN A CD  
1816 O OE1 . GLN A 224 ? 1.95804 2.61507 1.38125 0.18606  -0.71557 -0.13380 260 GLN A OE1 
1817 N NE2 . GLN A 224 ? 1.83460 2.54653 1.33994 0.20223  -0.81794 -0.13412 260 GLN A NE2 
1818 N N   . LYS A 225 ? 1.77680 2.46523 1.34085 0.12686  -0.55447 -0.17091 261 LYS A N   
1819 C CA  . LYS A 225 ? 1.76767 2.41389 1.31875 0.10825  -0.48014 -0.16105 261 LYS A CA  
1820 C C   . LYS A 225 ? 1.63834 2.31524 1.31536 0.09623  -0.44305 -0.15083 261 LYS A C   
1821 O O   . LYS A 225 ? 1.52449 2.20470 1.25578 0.06773  -0.40739 -0.17075 261 LYS A O   
1822 C CB  . LYS A 225 ? 1.84731 2.42881 1.27846 0.12749  -0.45006 -0.11772 261 LYS A CB  
1823 C CG  . LYS A 225 ? 1.76764 2.32388 1.23052 0.12019  -0.38277 -0.08585 261 LYS A CG  
1824 C CD  . LYS A 225 ? 1.82988 2.32623 1.18194 0.13512  -0.35411 -0.04351 261 LYS A CD  
1825 C CE  . LYS A 225 ? 1.82639 2.28515 1.08352 0.12404  -0.32366 -0.06142 261 LYS A CE  
1826 N NZ  . LYS A 225 ? 1.65845 2.12410 0.98527 0.09750  -0.27899 -0.08807 261 LYS A NZ  
1827 N N   . TYR A 226 ? 1.68338 2.37853 1.40368 0.11896  -0.45179 -0.12017 262 TYR A N   
1828 C CA  . TYR A 226 ? 1.53961 2.26395 1.37140 0.10995  -0.41868 -0.11377 262 TYR A CA  
1829 C C   . TYR A 226 ? 1.47052 2.25840 1.41353 0.08464  -0.43043 -0.15386 262 TYR A C   
1830 O O   . TYR A 226 ? 1.33561 2.13217 1.34630 0.06078  -0.38833 -0.15887 262 TYR A O   
1831 C CB  . TYR A 226 ? 1.56899 2.30268 1.42702 0.14291  -0.43360 -0.08180 262 TYR A CB  
1832 C CG  . TYR A 226 ? 1.60022 2.26727 1.38172 0.15808  -0.40217 -0.03713 262 TYR A CG  
1833 C CD1 . TYR A 226 ? 1.68399 2.29374 1.34851 0.15705  -0.38973 -0.02171 262 TYR A CD1 
1834 C CD2 . TYR A 226 ? 1.57298 2.23392 1.40086 0.17236  -0.38350 -0.01192 262 TYR A CD2 
1835 C CE1 . TYR A 226 ? 1.70445 2.25714 1.30948 0.16656  -0.35904 0.02039  262 TYR A CE1 
1836 C CE2 . TYR A 226 ? 1.55573 2.15383 1.32062 0.18225  -0.35772 0.02758  262 TYR A CE2 
1837 C CZ  . TYR A 226 ? 1.61995 2.16622 1.27783 0.17776  -0.34545 0.04512  262 TYR A CZ  
1838 O OH  . TYR A 226 ? 1.64434 2.13138 1.24881 0.18337  -0.31748 0.08591  262 TYR A OH  
1839 N N   . GLU A 227 ? 1.49931 2.33049 1.46106 0.08770  -0.48882 -0.18164 263 GLU A N   
1840 C CA  . GLU A 227 ? 1.41442 2.30625 1.48412 0.05820  -0.50228 -0.22176 263 GLU A CA  
1841 C C   . GLU A 227 ? 1.39071 2.24770 1.43595 0.02133  -0.47315 -0.24807 263 GLU A C   
1842 O O   . GLU A 227 ? 1.33602 2.20904 1.46308 -0.00874 -0.43933 -0.25966 263 GLU A O   
1843 C CB  . GLU A 227 ? 1.53114 2.47604 1.62392 0.06998  -0.57922 -0.24635 263 GLU A CB  
1844 C CG  . GLU A 227 ? 1.46286 2.46500 1.63239 0.10319  -0.61116 -0.22938 263 GLU A CG  
1845 C CD  . GLU A 227 ? 1.52879 2.54343 1.69071 0.11714  -0.68122 -0.23749 263 GLU A CD  
1846 O OE1 . GLU A 227 ? 1.61183 2.56852 1.65120 0.14009  -0.70759 -0.21645 263 GLU A OE1 
1847 O OE2 . GLU A 227 ? 1.59090 2.66532 1.86715 0.10120  -0.70451 -0.26037 263 GLU A OE2 
1848 N N   . LYS A 228 ? 1.45277 2.25791 1.38158 0.02450  -0.48481 -0.25752 264 LYS A N   
1849 C CA  . LYS A 228 ? 1.42628 2.19420 1.32940 -0.00563 -0.46088 -0.28767 264 LYS A CA  
1850 C C   . LYS A 228 ? 1.40156 2.13514 1.32545 -0.02006 -0.39117 -0.26758 264 LYS A C   
1851 O O   . LYS A 228 ? 1.38088 2.09885 1.33542 -0.04925 -0.36869 -0.29092 264 LYS A O   
1852 C CB  . LYS A 228 ? 1.50254 2.21564 1.26396 0.00687  -0.47670 -0.29871 264 LYS A CB  
1853 C CG  . LYS A 228 ? 1.59465 2.32420 1.33763 -0.00296 -0.53928 -0.34724 264 LYS A CG  
1854 C CD  . LYS A 228 ? 1.72383 2.38554 1.32702 -0.00062 -0.53393 -0.36875 264 LYS A CD  
1855 C CE  . LYS A 228 ? 1.70901 2.37623 1.31217 -0.02350 -0.58319 -0.42945 264 LYS A CE  
1856 N NZ  . LYS A 228 ? 1.81473 2.40999 1.28265 -0.02197 -0.56876 -0.45701 264 LYS A NZ  
1857 N N   . ILE A 229 ? 1.43589 2.15299 1.34236 -0.00010 -0.35986 -0.22461 265 ILE A N   
1858 C CA  . ILE A 229 ? 1.40502 2.09536 1.33944 -0.01381 -0.30156 -0.20543 265 ILE A CA  
1859 C C   . ILE A 229 ? 1.31907 2.05516 1.37161 -0.03427 -0.29066 -0.20954 265 ILE A C   
1860 O O   . ILE A 229 ? 1.23989 1.95814 1.32698 -0.05815 -0.25336 -0.21006 265 ILE A O   
1861 C CB  . ILE A 229 ? 1.36401 2.02099 1.24476 0.01064  -0.27489 -0.16068 265 ILE A CB  
1862 C CG1 . ILE A 229 ? 1.37339 1.98431 1.13500 0.02744  -0.27701 -0.15347 265 ILE A CG1 
1863 C CG2 . ILE A 229 ? 1.34263 1.97482 1.25556 -0.00371 -0.22217 -0.14196 265 ILE A CG2 
1864 C CD1 . ILE A 229 ? 1.30739 1.88626 1.02119 0.04812  -0.25288 -0.10746 265 ILE A CD1 
1865 N N   . GLY A 230 ? 1.26019 2.05573 1.37657 -0.02470 -0.32196 -0.21208 266 GLY A N   
1866 C CA  . GLY A 230 ? 1.17898 2.02305 1.40798 -0.04347 -0.30488 -0.21570 266 GLY A CA  
1867 C C   . GLY A 230 ? 1.24845 2.11169 1.54052 -0.08295 -0.30767 -0.25056 266 GLY A C   
1868 O O   . GLY A 230 ? 1.19740 2.06909 1.55593 -0.10886 -0.27206 -0.24796 266 GLY A O   
1869 N N   . ASP A 231 ? 1.34414 2.21000 1.61212 -0.08925 -0.35083 -0.28333 267 ASP A N   
1870 C CA  . ASP A 231 ? 1.24623 2.12380 1.57431 -0.12923 -0.35880 -0.32019 267 ASP A CA  
1871 C C   . ASP A 231 ? 1.26389 2.07690 1.57066 -0.15335 -0.31012 -0.31689 267 ASP A C   
1872 O O   . ASP A 231 ? 1.24985 2.07131 1.63379 -0.18620 -0.28539 -0.32047 267 ASP A O   
1873 C CB  . ASP A 231 ? 1.32888 2.20765 1.61337 -0.12847 -0.41795 -0.35843 267 ASP A CB  
1874 C CG  . ASP A 231 ? 1.38406 2.32135 1.67987 -0.09995 -0.47423 -0.35857 267 ASP A CG  
1875 O OD1 . ASP A 231 ? 1.26620 2.27946 1.67879 -0.10923 -0.49338 -0.36736 267 ASP A OD1 
1876 O OD2 . ASP A 231 ? 1.47699 2.38515 1.66779 -0.06753 -0.49851 -0.34813 267 ASP A OD2 
1877 N N   . LYS A 232 ? 1.34593 2.09398 1.55040 -0.13660 -0.29465 -0.30787 268 LYS A N   
1878 C CA  . LYS A 232 ? 1.25712 1.94396 1.44435 -0.15358 -0.25226 -0.30485 268 LYS A CA  
1879 C C   . LYS A 232 ? 1.23730 1.92179 1.46896 -0.15965 -0.20662 -0.26803 268 LYS A C   
1880 O O   . LYS A 232 ? 1.27207 1.92315 1.52967 -0.18374 -0.17780 -0.26637 268 LYS A O   
1881 C CB  . LYS A 232 ? 1.22730 1.85597 1.30409 -0.12986 -0.24270 -0.30195 268 LYS A CB  
1882 C CG  . LYS A 232 ? 1.31590 1.88937 1.36727 -0.14642 -0.23227 -0.33288 268 LYS A CG  
1883 C CD  . LYS A 232 ? 1.35214 1.89834 1.30160 -0.12713 -0.25468 -0.35932 268 LYS A CD  
1884 C CE  . LYS A 232 ? 1.34392 1.83168 1.26796 -0.14058 -0.24253 -0.39642 268 LYS A CE  
1885 N NZ  . LYS A 232 ? 1.38101 1.84790 1.21024 -0.12828 -0.27339 -0.43588 268 LYS A NZ  
1886 N N   . LYS A 233 ? 1.19321 1.90722 1.42927 -0.13735 -0.20148 -0.23871 269 LYS A N   
1887 C CA  . LYS A 233 ? 1.19246 1.90500 1.46498 -0.14330 -0.16177 -0.20814 269 LYS A CA  
1888 C C   . LYS A 233 ? 1.20284 1.95397 1.57071 -0.17643 -0.15229 -0.21823 269 LYS A C   
1889 O O   . LYS A 233 ? 1.22273 1.95283 1.61100 -0.19390 -0.11522 -0.19936 269 LYS A O   
1890 C CB  . LYS A 233 ? 1.15300 1.88625 1.40983 -0.11161 -0.16152 -0.18094 269 LYS A CB  
1891 C CG  . LYS A 233 ? 1.16075 1.84664 1.32853 -0.08484 -0.15608 -0.15919 269 LYS A CG  
1892 C CD  . LYS A 233 ? 1.08553 1.78261 1.24436 -0.05763 -0.15420 -0.13118 269 LYS A CD  
1893 C CE  . LYS A 233 ? 1.05441 1.70185 1.13235 -0.03733 -0.14474 -0.10650 269 LYS A CE  
1894 N NZ  . LYS A 233 ? 1.04976 1.69822 1.11880 -0.01287 -0.14454 -0.07950 269 LYS A NZ  
1895 N N   . ARG A 234 ? 1.37135 2.17906 1.79821 -0.18648 -0.18566 -0.24646 270 ARG A N   
1896 C CA  . ARG A 234 ? 1.39216 2.24451 1.92132 -0.22176 -0.17512 -0.25718 270 ARG A CA  
1897 C C   . ARG A 234 ? 1.38102 2.20781 1.93425 -0.26002 -0.18411 -0.28647 270 ARG A C   
1898 O O   . ARG A 234 ? 1.36275 2.20555 1.99347 -0.29703 -0.16412 -0.28881 270 ARG A O   
1899 C CB  . ARG A 234 ? 1.28821 2.22935 1.89220 -0.21139 -0.20538 -0.27015 270 ARG A CB  
1900 C CG  . ARG A 234 ? 1.32226 2.32411 2.04302 -0.24255 -0.18171 -0.27315 270 ARG A CG  
1901 C CD  . ARG A 234 ? 1.17795 2.26038 1.96138 -0.21596 -0.18948 -0.26934 270 ARG A CD  
1902 N NE  . ARG A 234 ? 1.20541 2.30312 1.94849 -0.17559 -0.24229 -0.27689 270 ARG A NE  
1903 C CZ  . ARG A 234 ? 1.21857 2.35608 1.99116 -0.17652 -0.29938 -0.30726 270 ARG A CZ  
1904 N NH1 . ARG A 234 ? 1.29951 2.46565 2.14684 -0.21770 -0.31334 -0.33699 270 ARG A NH1 
1905 N NH2 . ARG A 234 ? 1.22689 2.37186 1.95019 -0.13624 -0.34603 -0.30706 270 ARG A NH2 
1906 N N   . THR A 235 ? 1.28755 2.07033 1.77327 -0.25253 -0.21071 -0.30876 271 THR A N   
1907 C CA  . THR A 235 ? 1.28982 2.03527 1.78998 -0.28626 -0.21976 -0.34066 271 THR A CA  
1908 C C   . THR A 235 ? 1.39446 2.06573 1.87487 -0.30118 -0.17505 -0.32069 271 THR A C   
1909 O O   . THR A 235 ? 1.40161 2.05558 1.93929 -0.33965 -0.16206 -0.32741 271 THR A O   
1910 C CB  . THR A 235 ? 1.31893 2.03861 1.74345 -0.26970 -0.26186 -0.37522 271 THR A CB  
1911 O OG1 . THR A 235 ? 1.26022 2.03673 1.67110 -0.24167 -0.30177 -0.37887 271 THR A OG1 
1912 C CG2 . THR A 235 ? 1.37416 2.07987 1.83783 -0.30703 -0.28858 -0.42116 271 THR A CG2 
1913 N N   . THR A 236 ? 1.44959 2.07592 1.85339 -0.27178 -0.15300 -0.29459 272 THR A N   
1914 C CA  . THR A 236 ? 1.46284 2.01921 1.84732 -0.28010 -0.11726 -0.27486 272 THR A CA  
1915 C C   . THR A 236 ? 1.45059 2.01724 1.87060 -0.29036 -0.08157 -0.23455 272 THR A C   
1916 O O   . THR A 236 ? 1.34890 1.94519 1.75150 -0.26672 -0.07347 -0.21036 272 THR A O   
1917 C CB  . THR A 236 ? 1.44449 1.95440 1.74217 -0.24511 -0.10948 -0.26527 272 THR A CB  
1918 O OG1 . THR A 236 ? 1.35791 1.88444 1.63358 -0.22132 -0.09167 -0.22648 272 THR A OG1 
1919 C CG2 . THR A 236 ? 1.38685 1.90320 1.62997 -0.22547 -0.14298 -0.29901 272 THR A CG2 
1920 N N   . PRO A 237 ? 1.60115 2.13886 2.06446 -0.32503 -0.05955 -0.22607 273 PRO A N   
1921 C CA  . PRO A 237 ? 1.45866 1.99433 1.93445 -0.33358 -0.02278 -0.18522 273 PRO A CA  
1922 C C   . PRO A 237 ? 1.44282 1.92897 1.84905 -0.30549 -0.00640 -0.15322 273 PRO A C   
1923 O O   . PRO A 237 ? 1.46369 1.92091 1.82112 -0.28035 -0.01887 -0.16162 273 PRO A O   
1924 C CB  . PRO A 237 ? 1.50115 2.00164 2.02676 -0.37860 -0.00664 -0.18430 273 PRO A CB  
1925 C CG  . PRO A 237 ? 1.57227 2.02700 2.09042 -0.38451 -0.03187 -0.21982 273 PRO A CG  
1926 C CD  . PRO A 237 ? 1.54868 2.05096 2.04878 -0.35973 -0.06836 -0.25376 273 PRO A CD  
1927 N N   . ALA A 238 ? 1.38859 1.86603 1.78952 -0.30995 0.02179  -0.11725 274 ALA A N   
1928 C CA  . ALA A 238 ? 1.23760 1.66964 1.57919 -0.28626 0.03189  -0.08712 274 ALA A CA  
1929 C C   . ALA A 238 ? 1.30740 1.66333 1.63568 -0.29492 0.03676  -0.07760 274 ALA A C   
1930 O O   . ALA A 238 ? 1.24633 1.56598 1.53436 -0.27208 0.03735  -0.05947 274 ALA A O   
1931 C CB  . ALA A 238 ? 1.16614 1.61109 1.49657 -0.28658 0.05550  -0.05497 274 ALA A CB  
1932 N N   . VAL A 239 ? 1.20188 1.53261 1.56940 -0.32714 0.03897  -0.08936 275 VAL A N   
1933 C CA  . VAL A 239 ? 1.24682 1.49802 1.60636 -0.33377 0.04197  -0.08052 275 VAL A CA  
1934 C C   . VAL A 239 ? 1.28045 1.50743 1.62229 -0.30960 0.02337  -0.11145 275 VAL A C   
1935 O O   . VAL A 239 ? 1.38567 1.56032 1.70461 -0.29084 0.02590  -0.09931 275 VAL A O   
1936 C CB  . VAL A 239 ? 1.28374 1.50884 1.69193 -0.37868 0.05179  -0.08158 275 VAL A CB  
1937 C CG1 . VAL A 239 ? 1.33821 1.47947 1.74771 -0.38332 0.04542  -0.08847 275 VAL A CG1 
1938 C CG2 . VAL A 239 ? 1.26198 1.48327 1.66687 -0.39928 0.08018  -0.03847 275 VAL A CG2 
1939 N N   . THR A 240 ? 1.21371 1.47936 1.56463 -0.30799 0.00443  -0.15220 276 THR A N   
1940 C CA  . THR A 240 ? 1.29430 1.53478 1.61602 -0.28512 -0.00934 -0.18463 276 THR A CA  
1941 C C   . THR A 240 ? 1.41054 1.66253 1.68179 -0.24481 -0.00509 -0.16996 276 THR A C   
1942 O O   . THR A 240 ? 1.47121 1.68908 1.71697 -0.22279 -0.00298 -0.18266 276 THR A O   
1943 C CB  . THR A 240 ? 1.33515 1.61092 1.66813 -0.29494 -0.03500 -0.23209 276 THR A CB  
1944 O OG1 . THR A 240 ? 1.31190 1.55925 1.60017 -0.27065 -0.04499 -0.26463 276 THR A OG1 
1945 C CG2 . THR A 240 ? 1.42375 1.77948 1.75665 -0.28700 -0.04635 -0.22941 276 THR A CG2 
1946 N N   . LEU A 241 ? 1.32533 1.62381 1.58517 -0.23517 -0.00153 -0.14436 277 LEU A N   
1947 C CA  . LEU A 241 ? 1.31920 1.62174 1.53857 -0.20253 0.00429  -0.12416 277 LEU A CA  
1948 C C   . LEU A 241 ? 1.29070 1.54605 1.51028 -0.19704 0.01860  -0.09116 277 LEU A C   
1949 O O   . LEU A 241 ? 1.28896 1.53602 1.48793 -0.17146 0.02303  -0.08112 277 LEU A O   
1950 C CB  . LEU A 241 ? 1.26393 1.62138 1.47262 -0.19434 0.00146  -0.10798 277 LEU A CB  
1951 C CG  . LEU A 241 ? 1.24355 1.64917 1.44024 -0.18505 -0.01843 -0.13502 277 LEU A CG  
1952 C CD1 . LEU A 241 ? 1.09391 1.54145 1.27672 -0.16860 -0.02037 -0.11445 277 LEU A CD1 
1953 C CD2 . LEU A 241 ? 1.29583 1.68175 1.45067 -0.16512 -0.02433 -0.15783 277 LEU A CD2 
1954 N N   . CYS A 242 ? 1.30748 1.53234 1.55120 -0.22103 0.02503  -0.07272 278 CYS A N   
1955 C CA  . CYS A 242 ? 1.25667 1.43150 1.49820 -0.21670 0.03176  -0.03914 278 CYS A CA  
1956 C C   . CYS A 242 ? 1.36448 1.47854 1.62457 -0.21443 0.03095  -0.05174 278 CYS A C   
1957 O O   . CYS A 242 ? 1.26267 1.32706 1.52982 -0.21484 0.03237  -0.02371 278 CYS A O   
1958 C CB  . CYS A 242 ? 1.21273 1.37835 1.45718 -0.24269 0.04003  -0.00782 278 CYS A CB  
1959 S SG  . CYS A 242 ? 1.20284 1.36568 1.41026 -0.22789 0.04140  0.03686  278 CYS A SG  
1960 N N   . ASP A 243 ? 1.41895 1.53206 1.68369 -0.21044 0.02675  -0.09400 279 ASP A N   
1961 C CA  . ASP A 243 ? 1.48033 1.53100 1.76316 -0.20706 0.02720  -0.11348 279 ASP A CA  
1962 C C   . ASP A 243 ? 1.53509 1.55903 1.81863 -0.17420 0.03348  -0.09460 279 ASP A C   
1963 O O   . ASP A 243 ? 1.48165 1.54002 1.74768 -0.14740 0.03885  -0.09822 279 ASP A O   
1964 C CB  . ASP A 243 ? 1.51964 1.57779 1.79316 -0.20407 0.02098  -0.16741 279 ASP A CB  
1965 C CG  . ASP A 243 ? 1.66995 1.65715 1.96520 -0.20914 0.02005  -0.19554 279 ASP A CG  
1966 O OD1 . ASP A 243 ? 1.72678 1.65900 2.04979 -0.21861 0.02305  -0.16975 279 ASP A OD1 
1967 O OD2 . ASP A 243 ? 1.73506 1.71631 2.01507 -0.20354 0.01477  -0.24370 279 ASP A OD2 
1968 N N   . GLY A 244 ? 1.77415 1.73687 2.08211 -0.17673 0.03229  -0.07264 280 GLY A N   
1969 C CA  . GLY A 244 ? 1.79800 1.73837 2.12055 -0.14543 0.03329  -0.05144 280 GLY A CA  
1970 C C   . GLY A 244 ? 1.70171 1.67770 2.01129 -0.13662 0.02901  -0.01002 280 GLY A C   
1971 O O   . GLY A 244 ? 1.77284 1.74345 2.10182 -0.11036 0.02654  0.00675  280 GLY A O   
1972 N N   . LEU A 245 ? 1.44395 1.45657 1.72600 -0.15733 0.02734  0.00470  281 LEU A N   
1973 C CA  . LEU A 245 ? 1.29903 1.34251 1.56088 -0.15149 0.02218  0.03831  281 LEU A CA  
1974 C C   . LEU A 245 ? 1.30954 1.32466 1.55334 -0.17551 0.01657  0.07451  281 LEU A C   
1975 O O   . LEU A 245 ? 1.41696 1.40384 1.66337 -0.20200 0.02185  0.07246  281 LEU A O   
1976 C CB  . LEU A 245 ? 1.24953 1.35832 1.48645 -0.15066 0.02730  0.02320  281 LEU A CB  
1977 C CG  . LEU A 245 ? 1.27436 1.41071 1.51188 -0.12863 0.03495  -0.00919 281 LEU A CG  
1978 C CD1 . LEU A 245 ? 1.25625 1.44918 1.46360 -0.12607 0.03572  -0.01337 281 LEU A CD1 
1979 C CD2 . LEU A 245 ? 1.26153 1.38538 1.52357 -0.10073 0.03865  -0.00038 281 LEU A CD2 
1980 N N   . PRO A 246 ? 1.26497 1.28381 1.48777 -0.16861 0.00640  0.10813  282 PRO A N   
1981 C CA  . PRO A 246 ? 1.29918 1.28934 1.48717 -0.19087 0.00334  0.14242  282 PRO A CA  
1982 C C   . PRO A 246 ? 1.39814 1.42183 1.56654 -0.21751 0.02144  0.13124  282 PRO A C   
1983 O O   . PRO A 246 ? 1.22976 1.30946 1.38931 -0.21209 0.02627  0.11568  282 PRO A O   
1984 C CB  . PRO A 246 ? 1.32443 1.32493 1.48867 -0.17470 -0.01381 0.16915  282 PRO A CB  
1985 C CG  . PRO A 246 ? 1.16372 1.17679 1.37145 -0.14465 -0.02271 0.15843  282 PRO A CG  
1986 C CD  . PRO A 246 ? 1.13771 1.18001 1.36882 -0.14106 -0.00373 0.11709  282 PRO A CD  
1987 N N   . GLN A 247 ? 1.60837 1.59674 1.77469 -0.24648 0.03200  0.14126  283 GLN A N   
1988 C CA  . GLN A 247 ? 1.65380 1.67846 1.82304 -0.27448 0.05254  0.12681  283 GLN A CA  
1989 C C   . GLN A 247 ? 1.63797 1.70487 1.76872 -0.27583 0.06185  0.13853  283 GLN A C   
1990 O O   . GLN A 247 ? 1.61207 1.72727 1.75548 -0.29053 0.07859  0.12104  283 GLN A O   
1991 C CB  . GLN A 247 ? 1.70745 1.68077 1.88472 -0.30898 0.06539  0.14231  283 GLN A CB  
1992 C CG  . GLN A 247 ? 1.80106 1.71137 2.01062 -0.30704 0.05430  0.13666  283 GLN A CG  
1993 C CD  . GLN A 247 ? 1.93192 1.77338 2.11750 -0.29153 0.03753  0.17654  283 GLN A CD  
1994 O OE1 . GLN A 247 ? 1.93979 1.76134 2.14758 -0.26214 0.01997  0.16943  283 GLN A OE1 
1995 N NE2 . GLN A 247 ? 2.03407 1.83959 2.17394 -0.31024 0.04294  0.21889  283 GLN A NE2 
1996 N N   . GLN A 248 ? 1.39293 1.44278 1.48071 -0.26009 0.04970  0.16537  284 GLN A N   
1997 C CA  . GLN A 248 ? 1.38908 1.47142 1.43500 -0.25889 0.05746  0.17179  284 GLN A CA  
1998 C C   . GLN A 248 ? 1.23568 1.38554 1.30253 -0.24301 0.05864  0.14003  284 GLN A C   
1999 O O   . GLN A 248 ? 1.17992 1.36465 1.22826 -0.24520 0.07167  0.13562  284 GLN A O   
2000 C CB  . GLN A 248 ? 1.39759 1.44529 1.39426 -0.24379 0.03595  0.20138  284 GLN A CB  
2001 C CG  . GLN A 248 ? 1.40054 1.37856 1.35549 -0.25866 0.03157  0.23969  284 GLN A CG  
2002 C CD  . GLN A 248 ? 1.37770 1.30697 1.36545 -0.24872 0.00902  0.25149  284 GLN A CD  
2003 O OE1 . GLN A 248 ? 1.34712 1.28942 1.39308 -0.24172 0.01013  0.22643  284 GLN A OE1 
2004 N NE2 . GLN A 248 ? 1.35336 1.22408 1.30132 -0.24589 -0.01313 0.28870  284 GLN A NE2 
2005 N N   . PHE A 249 ? 1.15451 1.32038 1.25599 -0.22549 0.04642  0.11841  285 PHE A N   
2006 C CA  . PHE A 249 ? 1.14288 1.36651 1.25747 -0.21138 0.04629  0.09129  285 PHE A CA  
2007 C C   . PHE A 249 ? 1.16462 1.42686 1.30920 -0.22919 0.05967  0.06662  285 PHE A C   
2008 O O   . PHE A 249 ? 1.03412 1.34560 1.18106 -0.22370 0.06352  0.05368  285 PHE A O   
2009 C CB  . PHE A 249 ? 1.04174 1.26794 1.17476 -0.18897 0.03342  0.07719  285 PHE A CB  
2010 C CG  . PHE A 249 ? 1.09478 1.30516 1.21347 -0.16945 0.02035  0.09774  285 PHE A CG  
2011 C CD1 . PHE A 249 ? 1.08014 1.31780 1.17945 -0.15641 0.01569  0.10079  285 PHE A CD1 
2012 C CD2 . PHE A 249 ? 0.98217 1.15030 1.11397 -0.16413 0.01066  0.11363  285 PHE A CD2 
2013 C CE1 . PHE A 249 ? 0.94196 1.16725 1.03717 -0.14276 0.00179  0.11864  285 PHE A CE1 
2014 C CE2 . PHE A 249 ? 0.96473 1.12642 1.09684 -0.14735 -0.00446 0.13164  285 PHE A CE2 
2015 C CZ  . PHE A 249 ? 1.03237 1.22384 1.14723 -0.13878 -0.00883 0.13377  285 PHE A CZ  
2016 N N   . ALA A 250 ? 1.17748 1.41763 1.35127 -0.25044 0.06450  0.05923  286 ALA A N   
2017 C CA  . ALA A 250 ? 1.11740 1.39567 1.33036 -0.27314 0.07495  0.03644  286 ALA A CA  
2018 C C   . ALA A 250 ? 1.09297 1.39493 1.29980 -0.29038 0.09822  0.05114  286 ALA A C   
2019 O O   . ALA A 250 ? 1.10506 1.46680 1.34356 -0.29470 0.10560  0.03172  286 ALA A O   
2020 C CB  . ALA A 250 ? 1.14187 1.38055 1.38766 -0.29705 0.07532  0.02790  286 ALA A CB  
2021 N N   . GLU A 251 ? 1.16214 1.41820 1.32735 -0.29885 0.10999  0.08503  287 GLU A N   
2022 C CA  . GLU A 251 ? 1.26947 1.54309 1.41415 -0.31291 0.13767  0.09906  287 GLU A CA  
2023 C C   . GLU A 251 ? 1.17295 1.49177 1.29774 -0.28642 0.13594  0.08936  287 GLU A C   
2024 O O   . GLU A 251 ? 1.13635 1.50297 1.27740 -0.29141 0.15803  0.07942  287 GLU A O   
2025 C CB  . GLU A 251 ? 1.36513 1.57024 1.45051 -0.32501 0.14650  0.13889  287 GLU A CB  
2026 C CG  . GLU A 251 ? 1.52503 1.67843 1.62710 -0.35545 0.15434  0.15484  287 GLU A CG  
2027 C CD  . GLU A 251 ? 1.78160 1.86844 1.81498 -0.36888 0.16548  0.19886  287 GLU A CD  
2028 O OE1 . GLU A 251 ? 1.82839 1.92624 1.80980 -0.36861 0.18427  0.21086  287 GLU A OE1 
2029 O OE2 . GLU A 251 ? 1.93450 1.95402 1.96120 -0.37798 0.15433  0.22113  287 GLU A OE2 
2030 N N   . TYR A 252 ? 1.11000 1.41407 1.20536 -0.25808 0.11113  0.09195  288 TYR A N   
2031 C CA  . TYR A 252 ? 1.11372 1.44856 1.18794 -0.23376 0.10731  0.08478  288 TYR A CA  
2032 C C   . TYR A 252 ? 1.03496 1.43675 1.15902 -0.22456 0.10689  0.05439  288 TYR A C   
2033 O O   . TYR A 252 ? 1.07988 1.51978 1.20871 -0.21816 0.12103  0.04599  288 TYR A O   
2034 C CB  . TYR A 252 ? 1.06861 1.37516 1.11377 -0.20986 0.08014  0.09390  288 TYR A CB  
2035 C CG  . TYR A 252 ? 0.96280 1.29726 0.99450 -0.18584 0.07307  0.08429  288 TYR A CG  
2036 C CD1 . TYR A 252 ? 1.06136 1.38495 1.04849 -0.18171 0.08109  0.09221  288 TYR A CD1 
2037 C CD2 . TYR A 252 ? 0.86303 1.22868 0.92080 -0.16729 0.05869  0.06713  288 TYR A CD2 
2038 C CE1 . TYR A 252 ? 1.01700 1.35782 0.99383 -0.15953 0.07386  0.08214  288 TYR A CE1 
2039 C CE2 . TYR A 252 ? 0.86906 1.25209 0.91391 -0.14587 0.05164  0.06198  288 TYR A CE2 
2040 C CZ  . TYR A 252 ? 0.88181 1.25137 0.89032 -0.14197 0.05873  0.06891  288 TYR A CZ  
2041 O OH  . TYR A 252 ? 0.86415 1.24288 0.86168 -0.12021 0.05070  0.06254  288 TYR A OH  
2042 N N   . LEU A 253 ? 0.98310 1.39857 1.14284 -0.22163 0.08924  0.03646  289 LEU A N   
2043 C CA  . LEU A 253 ? 0.97396 1.44963 1.17366 -0.21059 0.07999  0.00886  289 LEU A CA  
2044 C C   . LEU A 253 ? 1.01555 1.53861 1.26948 -0.23293 0.09916  -0.00454 289 LEU A C   
2045 O O   . LEU A 253 ? 0.89601 1.47543 1.18034 -0.22078 0.09944  -0.01999 289 LEU A O   
2046 C CB  . LEU A 253 ? 0.95429 1.42684 1.16589 -0.20374 0.05630  -0.00825 289 LEU A CB  
2047 C CG  . LEU A 253 ? 0.94378 1.46988 1.17897 -0.18758 0.03728  -0.03416 289 LEU A CG  
2048 C CD1 . LEU A 253 ? 0.93994 1.49046 1.15803 -0.16190 0.03566  -0.02794 289 LEU A CD1 
2049 C CD2 . LEU A 253 ? 1.00901 1.51768 1.22559 -0.17509 0.01640  -0.04622 289 LEU A CD2 
2050 N N   . ASP A 254 ? 0.96377 1.46510 1.23619 -0.26563 0.11570  0.00240  290 ASP A N   
2051 C CA  . ASP A 254 ? 0.98878 1.53740 1.32201 -0.29253 0.13878  -0.00796 290 ASP A CA  
2052 C C   . ASP A 254 ? 1.02784 1.59960 1.34799 -0.29000 0.17198  0.00339  290 ASP A C   
2053 O O   . ASP A 254 ? 0.98316 1.62186 1.36205 -0.29340 0.18741  -0.01322 290 ASP A O   
2054 C CB  . ASP A 254 ? 1.06263 1.57124 1.41424 -0.33125 0.15124  0.00149  290 ASP A CB  
2055 C CG  . ASP A 254 ? 1.12312 1.63917 1.52402 -0.34188 0.12500  -0.02646 290 ASP A CG  
2056 O OD1 . ASP A 254 ? 1.02030 1.58615 1.44696 -0.32319 0.10006  -0.05421 290 ASP A OD1 
2057 O OD2 . ASP A 254 ? 1.24287 1.70998 1.65216 -0.36821 0.12744  -0.02107 290 ASP A OD2 
2058 N N   . SER A 255 ? 1.01557 1.53372 1.26049 -0.28299 0.18259  0.02950  291 SER A N   
2059 C CA  . SER A 255 ? 1.05589 1.58636 1.27280 -0.27946 0.21576  0.03726  291 SER A CA  
2060 C C   . SER A 255 ? 1.06958 1.64952 1.30003 -0.24396 0.20665  0.01615  291 SER A C   
2061 O O   . SER A 255 ? 1.02866 1.66449 1.30005 -0.24159 0.23274  0.00233  291 SER A O   
2062 C CB  . SER A 255 ? 1.10300 1.55740 1.22585 -0.27943 0.22023  0.06801  291 SER A CB  
2063 O OG  . SER A 255 ? 1.19119 1.65061 1.27341 -0.27628 0.25360  0.07235  291 SER A OG  
2064 N N   . VAL A 256 ? 1.07603 1.63585 1.27690 -0.21559 0.17123  0.01425  292 VAL A N   
2065 C CA  . VAL A 256 ? 1.08610 1.68003 1.29425 -0.18101 0.15890  -0.00157 292 VAL A CA  
2066 C C   . VAL A 256 ? 1.00921 1.67625 1.29937 -0.17389 0.14649  -0.02737 292 VAL A C   
2067 O O   . VAL A 256 ? 1.02898 1.73234 1.33818 -0.14527 0.13977  -0.04056 292 VAL A O   
2068 C CB  . VAL A 256 ? 1.03938 1.58924 1.19643 -0.15704 0.12556  0.00708  292 VAL A CB  
2069 C CG1 . VAL A 256 ? 1.07184 1.55245 1.15778 -0.16557 0.12860  0.03209  292 VAL A CG1 
2070 C CG2 . VAL A 256 ? 0.97779 1.53352 1.16013 -0.15597 0.09577  0.00018  292 VAL A CG2 
2071 N N   . ARG A 257 ? 0.95292 1.63929 1.29246 -0.19842 0.13945  -0.03565 293 ARG A N   
2072 C CA  . ARG A 257 ? 0.94625 1.70467 1.36698 -0.19555 0.12256  -0.06203 293 ARG A CA  
2073 C C   . ARG A 257 ? 0.80987 1.63305 1.30688 -0.21331 0.15663  -0.07259 293 ARG A C   
2074 O O   . ARG A 257 ? 0.71502 1.61054 1.28787 -0.20231 0.14332  -0.09500 293 ARG A O   
2075 C CB  . ARG A 257 ? 0.91097 1.65961 1.35028 -0.21429 0.09513  -0.07196 293 ARG A CB  
2076 C CG  . ARG A 257 ? 0.87397 1.59681 1.26854 -0.18756 0.05602  -0.07518 293 ARG A CG  
2077 C CD  . ARG A 257 ? 0.86167 1.56974 1.26653 -0.20548 0.03386  -0.08958 293 ARG A CD  
2078 N NE  . ARG A 257 ? 0.82065 1.51375 1.18315 -0.17908 0.00080  -0.09608 293 ARG A NE  
2079 C CZ  . ARG A 257 ? 0.86374 1.53734 1.21600 -0.18585 -0.01973 -0.11168 293 ARG A CZ  
2080 N NH1 . ARG A 257 ? 0.75698 1.41917 1.14221 -0.21802 -0.01506 -0.12382 293 ARG A NH1 
2081 N NH2 . ARG A 257 ? 0.86795 1.52885 1.17240 -0.16014 -0.04358 -0.11544 293 ARG A NH2 
2082 N N   . SER A 258 ? 0.89889 1.69929 1.37873 -0.24018 0.20028  -0.05581 294 SER A N   
2083 C CA  . SER A 258 ? 0.81261 1.67341 1.36093 -0.25939 0.24397  -0.06249 294 SER A CA  
2084 C C   . SER A 258 ? 0.84884 1.71495 1.36274 -0.23594 0.27995  -0.05927 294 SER A C   
2085 O O   . SER A 258 ? 0.74425 1.64633 1.29245 -0.25296 0.32957  -0.05962 294 SER A O   
2086 C CB  . SER A 258 ? 0.81418 1.64564 1.36582 -0.30888 0.27535  -0.04479 294 SER A CB  
2087 O OG  . SER A 258 ? 0.94639 1.69360 1.39389 -0.31357 0.29292  -0.01437 294 SER A OG  
2088 N N   . LEU A 259 ? 0.90861 1.73717 1.35472 -0.19852 0.25844  -0.05712 295 LEU A N   
2089 C CA  . LEU A 259 ? 0.93634 1.75985 1.34277 -0.17364 0.28798  -0.05901 295 LEU A CA  
2090 C C   . LEU A 259 ? 0.85741 1.76727 1.35473 -0.14559 0.29332  -0.08674 295 LEU A C   
2091 O O   . LEU A 259 ? 0.82353 1.77207 1.37647 -0.12667 0.25094  -0.10072 295 LEU A O   
2092 C CB  . LEU A 259 ? 0.94391 1.69503 1.25538 -0.14578 0.25856  -0.04883 295 LEU A CB  
2093 C CG  . LEU A 259 ? 0.97477 1.64071 1.18281 -0.16315 0.26841  -0.02258 295 LEU A CG  
2094 C CD1 . LEU A 259 ? 1.03841 1.64518 1.17954 -0.13893 0.22827  -0.01472 295 LEU A CD1 
2095 C CD2 . LEU A 259 ? 1.03428 1.69163 1.19947 -0.16785 0.32012  -0.02119 295 LEU A CD2 
2096 N N   . PRO A 260 ? 0.89358 1.83485 1.40686 -0.14080 0.34465  -0.09525 296 PRO A N   
2097 C CA  . PRO A 260 ? 0.88915 1.91240 1.49400 -0.10698 0.35051  -0.12283 296 PRO A CA  
2098 C C   . PRO A 260 ? 0.94153 1.93248 1.50348 -0.05639 0.31530  -0.13032 296 PRO A C   
2099 O O   . PRO A 260 ? 0.89741 1.80450 1.35712 -0.04947 0.29499  -0.11526 296 PRO A O   
2100 C CB  . PRO A 260 ? 0.79753 1.85010 1.41418 -0.11690 0.42437  -0.12827 296 PRO A CB  
2101 C CG  . PRO A 260 ? 0.94393 1.90620 1.43568 -0.14360 0.44937  -0.10199 296 PRO A CG  
2102 C CD  . PRO A 260 ? 0.96932 1.87786 1.42451 -0.16836 0.40274  -0.08001 296 PRO A CD  
2103 N N   . PHE A 261 ? 0.96516 2.02654 1.61609 -0.02106 0.30742  -0.15358 297 PHE A N   
2104 C CA  . PHE A 261 ? 0.98349 2.02293 1.61777 0.02719  0.26250  -0.15950 297 PHE A CA  
2105 C C   . PHE A 261 ? 1.09514 2.05631 1.62850 0.05031  0.28032  -0.15770 297 PHE A C   
2106 O O   . PHE A 261 ? 1.12694 2.01743 1.58666 0.06506  0.24236  -0.14573 297 PHE A O   
2107 C CB  . PHE A 261 ? 0.96047 2.09513 1.72019 0.06117  0.25237  -0.18413 297 PHE A CB  
2108 C CG  . PHE A 261 ? 1.01216 2.12279 1.75869 0.11643  0.21755  -0.19055 297 PHE A CG  
2109 C CD1 . PHE A 261 ? 0.96491 2.04912 1.69143 0.13240  0.15269  -0.17890 297 PHE A CD1 
2110 C CD2 . PHE A 261 ? 1.01424 2.12681 1.76858 0.15308  0.25164  -0.20866 297 PHE A CD2 
2111 C CE1 . PHE A 261 ? 0.96266 2.01855 1.67588 0.18152  0.12138  -0.18030 297 PHE A CE1 
2112 C CE2 . PHE A 261 ? 1.00935 2.09214 1.75445 0.20400  0.21854  -0.21395 297 PHE A CE2 
2113 C CZ  . PHE A 261 ? 0.96795 2.02083 1.69278 0.21737  0.15239  -0.19742 297 PHE A CZ  
2114 N N   . ASP A 262 ? 1.35139 2.32262 1.87846 0.05196  0.33915  -0.17049 298 ASP A N   
2115 C CA  . ASP A 262 ? 1.36895 2.27060 1.80543 0.07771  0.35711  -0.17763 298 ASP A CA  
2116 C C   . ASP A 262 ? 1.41334 2.23651 1.72838 0.04429  0.38330  -0.16018 298 ASP A C   
2117 O O   . ASP A 262 ? 1.54410 2.30618 1.77442 0.06074  0.39945  -0.16853 298 ASP A O   
2118 C CB  . ASP A 262 ? 1.33914 2.29789 1.83870 0.11028  0.40572  -0.20907 298 ASP A CB  
2119 C CG  . ASP A 262 ? 1.26034 2.29598 1.82581 0.07919  0.46826  -0.21452 298 ASP A CG  
2120 O OD1 . ASP A 262 ? 1.27348 2.31468 1.83820 0.03192  0.46887  -0.19303 298 ASP A OD1 
2121 O OD2 . ASP A 262 ? 1.33238 2.42188 1.95359 0.10174  0.51899  -0.24024 298 ASP A OD2 
2122 N N   . ALA A 263 ? 1.21664 2.03555 1.51913 -0.00085 0.38442  -0.13700 299 ALA A N   
2123 C CA  . ALA A 263 ? 1.28348 2.03265 1.47658 -0.03224 0.40977  -0.11772 299 ALA A CA  
2124 C C   . ALA A 263 ? 1.36548 2.01887 1.45380 -0.02550 0.36486  -0.10327 299 ALA A C   
2125 O O   . ALA A 263 ? 1.26401 1.90533 1.36804 -0.01501 0.31285  -0.09629 299 ALA A O   
2126 C CB  . ALA A 263 ? 1.17816 1.94455 1.39436 -0.08071 0.41958  -0.09489 299 ALA A CB  
2127 N N   . GLU A 264 ? 1.42482 2.01070 1.40479 -0.03266 0.38597  -0.09885 300 GLU A N   
2128 C CA  . GLU A 264 ? 1.52981 2.02660 1.41275 -0.03601 0.34392  -0.08202 300 GLU A CA  
2129 C C   . GLU A 264 ? 1.49301 1.96866 1.35736 -0.07549 0.32782  -0.04880 300 GLU A C   
2130 O O   . GLU A 264 ? 1.55018 2.02020 1.38225 -0.10404 0.36382  -0.03571 300 GLU A O   
2131 C CB  . GLU A 264 ? 1.70033 2.13090 1.47081 -0.02948 0.36602  -0.09187 300 GLU A CB  
2132 C CG  . GLU A 264 ? 1.75382 2.09636 1.43539 -0.02922 0.31584  -0.08014 300 GLU A CG  
2133 C CD  . GLU A 264 ? 2.07713 2.34861 1.63078 -0.04208 0.33242  -0.07799 300 GLU A CD  
2134 O OE1 . GLU A 264 ? 2.13842 2.40849 1.65579 -0.07155 0.36173  -0.05870 300 GLU A OE1 
2135 O OE2 . GLU A 264 ? 2.20224 2.41487 1.68760 -0.02357 0.31448  -0.09526 300 GLU A OE2 
2136 N N   . PRO A 265 ? 1.32446 1.78564 1.20702 -0.07685 0.27775  -0.03454 301 PRO A N   
2137 C CA  . PRO A 265 ? 1.29085 1.73616 1.16966 -0.10998 0.26400  -0.00688 301 PRO A CA  
2138 C C   . PRO A 265 ? 1.33945 1.70445 1.11266 -0.12550 0.25502  0.01484  301 PRO A C   
2139 O O   . PRO A 265 ? 1.37689 1.69208 1.08814 -0.10935 0.23269  0.01077  301 PRO A O   
2140 C CB  . PRO A 265 ? 1.25808 1.71457 1.18752 -0.09898 0.21617  -0.00425 301 PRO A CB  
2141 C CG  . PRO A 265 ? 1.19400 1.64508 1.12189 -0.06270 0.19778  -0.02164 301 PRO A CG  
2142 C CD  . PRO A 265 ? 1.20612 1.65092 1.09826 -0.04831 0.23347  -0.04103 301 PRO A CD  
2143 N N   . PRO A 266 ? 1.28670 1.63380 1.03716 -0.15732 0.26854  0.03882  302 PRO A N   
2144 C CA  . PRO A 266 ? 1.37285 1.64165 1.02035 -0.17082 0.25428  0.06287  302 PRO A CA  
2145 C C   . PRO A 266 ? 1.34329 1.57474 0.98672 -0.16543 0.19678  0.07667  302 PRO A C   
2146 O O   . PRO A 266 ? 1.31579 1.53634 0.97946 -0.18219 0.17940  0.09862  302 PRO A O   
2147 C CB  . PRO A 266 ? 1.37235 1.63758 1.01484 -0.20542 0.28411  0.08747  302 PRO A CB  
2148 C CG  . PRO A 266 ? 1.31177 1.64489 1.06953 -0.21257 0.28997  0.07955  302 PRO A CG  
2149 C CD  . PRO A 266 ? 1.23347 1.62750 1.05262 -0.18309 0.29448  0.04570  302 PRO A CD  
2150 N N   . TYR A 267 ? 1.29976 1.51077 0.92155 -0.14227 0.16907  0.06327  303 TYR A N   
2151 C CA  . TYR A 267 ? 1.29280 1.47961 0.92723 -0.13693 0.11890  0.07447  303 TYR A CA  
2152 C C   . TYR A 267 ? 1.36034 1.49475 0.94580 -0.15622 0.09466  0.10417  303 TYR A C   
2153 O O   . TYR A 267 ? 1.34886 1.48553 0.97803 -0.16189 0.07055  0.12027  303 TYR A O   
2154 C CB  . TYR A 267 ? 1.24360 1.40640 0.85268 -0.11438 0.09670  0.05719  303 TYR A CB  
2155 C CG  . TYR A 267 ? 1.26820 1.47654 0.93283 -0.08996 0.11085  0.03137  303 TYR A CG  
2156 C CD1 . TYR A 267 ? 1.18849 1.43223 0.92679 -0.07976 0.09237  0.03197  303 TYR A CD1 
2157 C CD2 . TYR A 267 ? 1.25562 1.46931 0.89599 -0.07484 0.14236  0.00654  303 TYR A CD2 
2158 C CE1 . TYR A 267 ? 1.18542 1.46653 0.97043 -0.05533 0.09932  0.01194  303 TYR A CE1 
2159 C CE2 . TYR A 267 ? 1.19457 1.44930 0.89252 -0.04837 0.15150  -0.01606 303 TYR A CE2 
2160 C CZ  . TYR A 267 ? 1.14674 1.43389 0.91622 -0.03876 0.12700  -0.01154 303 TYR A CZ  
2161 O OH  . TYR A 267 ? 1.12930 1.45321 0.95202 -0.01047 0.13043  -0.03059 303 TYR A OH  
2162 N N   . GLU A 268 ? 1.38274 1.46786 0.87468 -0.16455 0.10023  0.11132  304 GLU A N   
2163 C CA  . GLU A 268 ? 1.43162 1.46164 0.87060 -0.17927 0.06870  0.14129  304 GLU A CA  
2164 C C   . GLU A 268 ? 1.43823 1.46962 0.89406 -0.20097 0.08616  0.16730  304 GLU A C   
2165 O O   . GLU A 268 ? 1.44251 1.43491 0.88238 -0.20958 0.05476  0.19471  304 GLU A O   
2166 C CB  . GLU A 268 ? 1.54001 1.51018 0.85970 -0.18072 0.06376  0.14057  304 GLU A CB  
2167 C CG  . GLU A 268 ? 1.64351 1.55274 0.90558 -0.18934 0.01252  0.16810  304 GLU A CG  
2168 C CD  . GLU A 268 ? 1.64907 1.55752 0.96116 -0.17805 -0.04197 0.16507  304 GLU A CD  
2169 O OE1 . GLU A 268 ? 1.52984 1.48204 0.92103 -0.16532 -0.03844 0.14675  304 GLU A OE1 
2170 O OE2 . GLU A 268 ? 1.85223 1.71639 1.12531 -0.18258 -0.08920 0.18273  304 GLU A OE2 
2171 N N   . GLU A 269 ? 1.43799 1.51245 0.93161 -0.21007 0.13366  0.15939  305 GLU A N   
2172 C CA  . GLU A 269 ? 1.45305 1.52818 0.97724 -0.23328 0.14857  0.18219  305 GLU A CA  
2173 C C   . GLU A 269 ? 1.37745 1.47752 0.99386 -0.22884 0.12097  0.18212  305 GLU A C   
2174 O O   . GLU A 269 ? 1.42943 1.49943 1.05490 -0.24058 0.10498  0.20594  305 GLU A O   
2175 C CB  . GLU A 269 ? 1.48047 1.59904 1.02855 -0.24781 0.20734  0.17188  305 GLU A CB  
2176 C CG  . GLU A 269 ? 1.45416 1.55459 1.00687 -0.27934 0.22937  0.20020  305 GLU A CG  
2177 C CD  . GLU A 269 ? 1.64236 1.75052 1.15574 -0.29931 0.29004  0.20340  305 GLU A CD  
2178 O OE1 . GLU A 269 ? 1.64182 1.76647 1.11698 -0.28522 0.31429  0.18195  305 GLU A OE1 
2179 O OE2 . GLU A 269 ? 1.79587 1.89189 1.31764 -0.32922 0.31610  0.22699  305 GLU A OE2 
2180 N N   . TYR A 270 ? 1.31153 1.46187 0.99193 -0.21023 0.11522  0.15571  306 TYR A N   
2181 C CA  . TYR A 270 ? 1.28073 1.45363 1.03663 -0.20426 0.09220  0.15292  306 TYR A CA  
2182 C C   . TYR A 270 ? 1.31921 1.45191 1.06141 -0.19595 0.04883  0.16990  306 TYR A C   
2183 O O   . TYR A 270 ? 1.30759 1.43183 1.08811 -0.19919 0.03382  0.18142  306 TYR A O   
2184 C CB  . TYR A 270 ? 1.25125 1.48159 1.06315 -0.18531 0.09514  0.12396  306 TYR A CB  
2185 C CG  . TYR A 270 ? 1.26978 1.55259 1.11962 -0.19111 0.13232  0.10524  306 TYR A CG  
2186 C CD1 . TYR A 270 ? 1.26487 1.56787 1.16124 -0.21272 0.14958  0.10722  306 TYR A CD1 
2187 C CD2 . TYR A 270 ? 1.28871 1.60190 1.13647 -0.17461 0.14876  0.08413  306 TYR A CD2 
2188 C CE1 . TYR A 270 ? 1.28254 1.64109 1.22747 -0.22056 0.18140  0.08948  306 TYR A CE1 
2189 C CE2 . TYR A 270 ? 1.23974 1.60985 1.13689 -0.17790 0.18196  0.06631  306 TYR A CE2 
2190 C CZ  . TYR A 270 ? 1.26674 1.66279 1.21524 -0.20222 0.19763  0.06942  306 TYR A CZ  
2191 O OH  . TYR A 270 ? 1.21345 1.67313 1.22395 -0.20802 0.22852  0.05117  306 TYR A OH  
2192 N N   . ARG A 271 ? 1.35884 1.46735 1.05220 -0.18489 0.02794  0.16947  307 ARG A N   
2193 C CA  . ARG A 271 ? 1.32422 1.40156 1.01574 -0.17878 -0.01561 0.18504  307 ARG A CA  
2194 C C   . ARG A 271 ? 1.38297 1.41175 1.04115 -0.19196 -0.03096 0.21553  307 ARG A C   
2195 O O   . ARG A 271 ? 1.36206 1.38184 1.06178 -0.18821 -0.05789 0.22970  307 ARG A O   
2196 C CB  . ARG A 271 ? 1.31415 1.37181 0.95923 -0.16868 -0.03707 0.17640  307 ARG A CB  
2197 C CG  . ARG A 271 ? 1.27752 1.37333 0.96131 -0.15266 -0.02991 0.15097  307 ARG A CG  
2198 C CD  . ARG A 271 ? 1.23212 1.29893 0.87801 -0.14452 -0.05662 0.14326  307 ARG A CD  
2199 N NE  . ARG A 271 ? 1.34727 1.38414 0.91008 -0.14552 -0.04272 0.13152  307 ARG A NE  
2200 C CZ  . ARG A 271 ? 1.30301 1.35355 0.85602 -0.13287 -0.01898 0.10587  307 ARG A CZ  
2201 N NH1 . ARG A 271 ? 1.17661 1.26806 0.79500 -0.11847 -0.01110 0.09240  307 ARG A NH1 
2202 N NH2 . ARG A 271 ? 1.31479 1.33474 0.78726 -0.13272 -0.00290 0.09342  307 ARG A NH2 
2203 N N   . MET A 272 ? 1.41685 1.41254 0.99960 -0.20614 -0.01261 0.22706  308 MET A N   
2204 C CA  . MET A 272 ? 1.47025 1.41313 1.01411 -0.21939 -0.02562 0.26088  308 MET A CA  
2205 C C   . MET A 272 ? 1.43376 1.38794 1.04561 -0.22867 -0.00986 0.26883  308 MET A C   
2206 O O   . MET A 272 ? 1.41354 1.33142 1.03673 -0.22969 -0.03479 0.29337  308 MET A O   
2207 C CB  . MET A 272 ? 1.60003 1.50299 1.03746 -0.23429 -0.00225 0.27267  308 MET A CB  
2208 C CG  . MET A 272 ? 1.79696 1.64386 1.14188 -0.22991 -0.04345 0.28660  308 MET A CG  
2209 S SD  . MET A 272 ? 2.13740 1.93687 1.49728 -0.22812 -0.10143 0.32586  308 MET A SD  
2210 C CE  . MET A 272 ? 2.03911 1.80955 1.34447 -0.21542 -0.16359 0.32306  308 MET A CE  
2211 N N   . LEU A 273 ? 1.39177 1.39470 1.05256 -0.23450 0.02850  0.24662  309 LEU A N   
2212 C CA  . LEU A 273 ? 1.37795 1.39230 1.10756 -0.24409 0.04001  0.24684  309 LEU A CA  
2213 C C   . LEU A 273 ? 1.33807 1.36024 1.13237 -0.22594 0.00798  0.24215  309 LEU A C   
2214 O O   . LEU A 273 ? 1.35216 1.34997 1.18029 -0.22941 0.00024  0.25376  309 LEU A O   
2215 C CB  . LEU A 273 ? 1.28782 1.36132 1.06411 -0.25207 0.07890  0.21874  309 LEU A CB  
2216 C CG  . LEU A 273 ? 1.28949 1.37653 1.13633 -0.26579 0.09037  0.21223  309 LEU A CG  
2217 C CD1 . LEU A 273 ? 1.40424 1.47081 1.23407 -0.29755 0.12476  0.22853  309 LEU A CD1 
2218 C CD2 . LEU A 273 ? 1.27172 1.42736 1.18547 -0.25582 0.09733  0.17583  309 LEU A CD2 
2219 N N   . LEU A 274 ? 1.24021 1.29363 1.05291 -0.20634 -0.00830 0.22528  310 LEU A N   
2220 C CA  . LEU A 274 ? 1.25149 1.31566 1.12331 -0.18932 -0.03307 0.22209  310 LEU A CA  
2221 C C   . LEU A 274 ? 1.23227 1.25392 1.08899 -0.18245 -0.07177 0.24861  310 LEU A C   
2222 O O   . LEU A 274 ? 1.21500 1.23717 1.12799 -0.17057 -0.08915 0.25248  310 LEU A O   
2223 C CB  . LEU A 274 ? 1.32165 1.43300 1.21867 -0.17396 -0.03302 0.19835  310 LEU A CB  
2224 C CG  . LEU A 274 ? 1.23050 1.38849 1.15081 -0.17558 -0.00317 0.17181  310 LEU A CG  
2225 C CD1 . LEU A 274 ? 1.21765 1.40894 1.14407 -0.15937 -0.00680 0.15524  310 LEU A CD1 
2226 C CD2 . LEU A 274 ? 1.17359 1.34610 1.14970 -0.17732 0.00495  0.16106  310 LEU A CD2 
2227 N N   . LEU A 275 ? 1.36820 1.35415 1.15043 -0.18833 -0.08664 0.26540  311 LEU A N   
2228 C CA  . LEU A 275 ? 1.37561 1.31874 1.14003 -0.18280 -0.13079 0.29250  311 LEU A CA  
2229 C C   . LEU A 275 ? 1.45183 1.35142 1.22205 -0.18827 -0.13541 0.31871  311 LEU A C   
2230 O O   . LEU A 275 ? 1.47397 1.35800 1.28746 -0.17510 -0.16828 0.33390  311 LEU A O   
2231 C CB  . LEU A 275 ? 1.47797 1.38730 1.14618 -0.18879 -0.14789 0.30151  311 LEU A CB  
2232 C CG  . LEU A 275 ? 1.52835 1.40657 1.17872 -0.18072 -0.20515 0.32024  311 LEU A CG  
2233 C CD1 . LEU A 275 ? 1.61708 1.43912 1.24043 -0.18305 -0.23250 0.35730  311 LEU A CD1 
2234 C CD2 . LEU A 275 ? 1.42039 1.34230 1.16840 -0.16495 -0.22710 0.30849  311 LEU A CD2 
2235 N N   . SER A 276 ? 1.42400 1.30344 1.15748 -0.20761 -0.10181 0.32470  312 SER A N   
2236 C CA  . SER A 276 ? 1.44411 1.27264 1.17976 -0.21622 -0.10337 0.35163  312 SER A CA  
2237 C C   . SER A 276 ? 1.47977 1.32340 1.31372 -0.20323 -0.10601 0.33993  312 SER A C   
2238 O O   . SER A 276 ? 1.58707 1.38239 1.43619 -0.20200 -0.11948 0.36227  312 SER A O   
2239 C CB  . SER A 276 ? 1.51299 1.32660 1.20473 -0.24409 -0.05856 0.35636  312 SER A CB  
2240 O OG  . SER A 276 ? 1.50212 1.37397 1.25293 -0.24971 -0.02200 0.32172  312 SER A OG  
2241 N N   . VAL A 277 ? 1.37552 1.28005 1.27110 -0.19243 -0.09272 0.30542  313 VAL A N   
2242 C CA  . VAL A 277 ? 1.40120 1.32005 1.38093 -0.17724 -0.09349 0.29030  313 VAL A CA  
2243 C C   . VAL A 277 ? 1.47326 1.37155 1.48746 -0.15487 -0.13369 0.30960  313 VAL A C   
2244 O O   . VAL A 277 ? 1.49779 1.36908 1.56003 -0.14439 -0.14072 0.31532  313 VAL A O   
2245 C CB  . VAL A 277 ? 1.32618 1.31225 1.34768 -0.16908 -0.07340 0.25264  313 VAL A CB  
2246 C CG1 . VAL A 277 ? 1.24202 1.23967 1.33706 -0.15386 -0.06848 0.23362  313 VAL A CG1 
2247 C CG2 . VAL A 277 ? 1.31926 1.33070 1.31304 -0.18854 -0.04016 0.23464  313 VAL A CG2 
2248 N N   . LEU A 278 ? 1.50479 1.41529 1.50064 -0.14677 -0.16231 0.31848  314 LEU A N   
2249 C CA  . LEU A 278 ? 1.53089 1.42934 1.56823 -0.12674 -0.20573 0.33772  314 LEU A CA  
2250 C C   . LEU A 278 ? 1.67132 1.49808 1.66824 -0.12874 -0.23569 0.37632  314 LEU A C   
2251 O O   . LEU A 278 ? 1.60892 1.42055 1.65437 -0.10883 -0.27312 0.39394  314 LEU A O   
2252 C CB  . LEU A 278 ? 1.48004 1.40859 1.50843 -0.12275 -0.23219 0.33619  314 LEU A CB  
2253 C CG  . LEU A 278 ? 1.33190 1.32631 1.41232 -0.11674 -0.20963 0.30495  314 LEU A CG  
2254 C CD1 . LEU A 278 ? 1.28764 1.29973 1.35177 -0.11831 -0.23624 0.30541  314 LEU A CD1 
2255 C CD2 . LEU A 278 ? 1.37294 1.39698 1.55428 -0.09635 -0.20315 0.29495  314 LEU A CD2 
2256 N N   . ASP A 279 ? 1.97474 1.75741 1.88605 -0.15172 -0.21952 0.39162  315 ASP A N   
2257 C CA  . ASP A 279 ? 2.02830 1.73361 1.89168 -0.15582 -0.24351 0.43284  315 ASP A CA  
2258 C C   . ASP A 279 ? 2.08991 1.76402 2.01391 -0.15092 -0.23090 0.43584  315 ASP A C   
2259 O O   . ASP A 279 ? 2.17342 1.79653 2.11500 -0.13585 -0.26562 0.46490  315 ASP A O   
2260 C CB  . ASP A 279 ? 2.13609 1.80367 1.88274 -0.18452 -0.22282 0.44974  315 ASP A CB  
2261 C CG  . ASP A 279 ? 2.43018 2.02640 2.08857 -0.18535 -0.26625 0.49501  315 ASP A CG  
2262 O OD1 . ASP A 279 ? 2.56584 2.12449 2.25896 -0.16704 -0.30821 0.52076  315 ASP A OD1 
2263 O OD2 . ASP A 279 ? 2.61746 2.19444 2.16939 -0.20227 -0.25961 0.50405  315 ASP A OD2 
2264 N N   . ASP A 280 ? 1.81725 1.51872 1.77489 -0.16236 -0.18488 0.40474  316 ASP A N   
2265 C CA  . ASP A 280 ? 1.77809 1.44487 1.78903 -0.16094 -0.17133 0.40106  316 ASP A CA  
2266 C C   . ASP A 280 ? 1.72009 1.40529 1.82992 -0.12615 -0.18920 0.38515  316 ASP A C   
2267 O O   . ASP A 280 ? 1.78026 1.42155 1.93439 -0.11719 -0.18902 0.38667  316 ASP A O   
2268 C CB  . ASP A 280 ? 1.74932 1.44485 1.76922 -0.18447 -0.12204 0.36750  316 ASP A CB  
2269 C CG  . ASP A 280 ? 1.77739 1.45844 1.71555 -0.21939 -0.09648 0.38232  316 ASP A CG  
2270 O OD1 . ASP A 280 ? 1.82904 1.46903 1.69091 -0.22567 -0.11404 0.41934  316 ASP A OD1 
2271 O OD2 . ASP A 280 ? 1.74101 1.45343 1.69155 -0.24019 -0.05871 0.35611  316 ASP A OD2 
2272 N N   . LEU A 281 ? 1.70902 1.45630 1.85680 -0.10684 -0.20174 0.36937  317 LEU A N   
2273 C CA  . LEU A 281 ? 1.61017 1.38768 1.85731 -0.07441 -0.20965 0.35174  317 LEU A CA  
2274 C C   . LEU A 281 ? 1.61244 1.38576 1.89267 -0.05025 -0.26069 0.38003  317 LEU A C   
2275 O O   . LEU A 281 ? 1.53798 1.33730 1.91201 -0.02095 -0.26829 0.36933  317 LEU A O   
2276 C CB  . LEU A 281 ? 1.52522 1.38266 1.80565 -0.07145 -0.17936 0.31099  317 LEU A CB  
2277 C CG  . LEU A 281 ? 1.45557 1.32702 1.71169 -0.09209 -0.13524 0.27933  317 LEU A CG  
2278 C CD1 . LEU A 281 ? 1.33109 1.27215 1.57688 -0.09630 -0.11711 0.25504  317 LEU A CD1 
2279 C CD2 . LEU A 281 ? 1.40038 1.25892 1.71550 -0.07930 -0.11502 0.25209  317 LEU A CD2 
2280 N N   . GLY A 282 ? 1.71259 1.45584 1.91976 -0.06121 -0.29594 0.41417  318 GLY A N   
2281 C CA  . GLY A 282 ? 1.78521 1.52284 2.02042 -0.04002 -0.35372 0.44185  318 GLY A CA  
2282 C C   . GLY A 282 ? 1.73846 1.55504 2.03681 -0.02842 -0.36531 0.42291  318 GLY A C   
2283 O O   . GLY A 282 ? 1.72021 1.55966 2.11120 -0.00156 -0.39611 0.42839  318 GLY A O   
2284 N N   . GLN A 283 ? 1.51778 1.37643 1.77415 -0.04808 -0.34098 0.40161  319 GLN A N   
2285 C CA  . GLN A 283 ? 1.50307 1.43104 1.81331 -0.04265 -0.34770 0.38467  319 GLN A CA  
2286 C C   . GLN A 283 ? 1.57225 1.49415 1.79671 -0.06245 -0.37462 0.39407  319 GLN A C   
2287 O O   . GLN A 283 ? 1.54055 1.42286 1.65897 -0.08296 -0.36336 0.39984  319 GLN A O   
2288 C CB  . GLN A 283 ? 1.42989 1.41389 1.77724 -0.04439 -0.29147 0.34612  319 GLN A CB  
2289 C CG  . GLN A 283 ? 1.35278 1.33743 1.76734 -0.02659 -0.25965 0.32909  319 GLN A CG  
2290 C CD  . GLN A 283 ? 1.33901 1.33863 1.86251 0.00465  -0.28365 0.33673  319 GLN A CD  
2291 O OE1 . GLN A 283 ? 1.32625 1.37158 1.90702 0.01274  -0.30724 0.34140  319 GLN A OE1 
2292 N NE2 . GLN A 283 ? 1.31809 1.27935 1.87758 0.02242  -0.27786 0.33713  319 GLN A NE2 
2293 N N   . ALA A 284 ? 1.49954 1.46123 1.77365 -0.05681 -0.40843 0.39360  320 ALA A N   
2294 C CA  . ALA A 284 ? 1.44239 1.39598 1.64338 -0.07387 -0.44113 0.39815  320 ALA A CA  
2295 C C   . ALA A 284 ? 1.41182 1.41368 1.61328 -0.08649 -0.40466 0.36750  320 ALA A C   
2296 O O   . ALA A 284 ? 1.39792 1.45647 1.69329 -0.07789 -0.38291 0.35087  320 ALA A O   
2297 C CB  . ALA A 284 ? 1.47425 1.43657 1.73044 -0.06316 -0.50967 0.41671  320 ALA A CB  
2298 N N   . CYS A 285 ? 1.44919 1.42592 1.54390 -0.10559 -0.39641 0.36101  321 CYS A N   
2299 C CA  . CYS A 285 ? 1.44907 1.46101 1.53461 -0.11593 -0.36735 0.33412  321 CYS A CA  
2300 C C   . CYS A 285 ? 1.43000 1.46067 1.54781 -0.11950 -0.41154 0.33336  321 CYS A C   
2301 O O   . CYS A 285 ? 1.51008 1.51738 1.55375 -0.13285 -0.43068 0.32733  321 CYS A O   
2302 C CB  . CYS A 285 ? 1.45537 1.43442 1.42465 -0.13134 -0.34079 0.32545  321 CYS A CB  
2303 S SG  . CYS A 285 ? 1.42838 1.44850 1.39363 -0.13754 -0.29551 0.29169  321 CYS A SG  
2304 N N   . ASP A 286 ? 1.42687 1.50119 1.66308 -0.10764 -0.42647 0.33765  322 ASP A N   
2305 C CA  . ASP A 286 ? 1.52646 1.62613 1.81963 -0.11304 -0.47101 0.33894  322 ASP A CA  
2306 C C   . ASP A 286 ? 1.46453 1.60707 1.79607 -0.12311 -0.43931 0.31790  322 ASP A C   
2307 O O   . ASP A 286 ? 1.49458 1.63580 1.82163 -0.13765 -0.47088 0.31337  322 ASP A O   
2308 C CB  . ASP A 286 ? 1.41334 1.54538 1.82920 -0.09554 -0.50318 0.35564  322 ASP A CB  
2309 C CG  . ASP A 286 ? 1.28969 1.46523 1.79766 -0.07744 -0.45017 0.34823  322 ASP A CG  
2310 O OD1 . ASP A 286 ? 1.36474 1.55437 1.85118 -0.08157 -0.39314 0.32906  322 ASP A OD1 
2311 O OD2 . ASP A 286 ? 1.16596 1.35996 1.76607 -0.05734 -0.46707 0.36029  322 ASP A OD2 
2312 N N   . GLY A 287 ? 1.45563 1.63064 1.82034 -0.11632 -0.38023 0.30544  323 GLY A N   
2313 C CA  . GLY A 287 ? 1.35637 1.56644 1.74992 -0.12436 -0.34761 0.29024  323 GLY A CA  
2314 C C   . GLY A 287 ? 1.25163 1.51691 1.74542 -0.11213 -0.30556 0.28708  323 GLY A C   
2315 O O   . GLY A 287 ? 1.17371 1.46219 1.67296 -0.11622 -0.26602 0.27604  323 GLY A O   
2316 N N   . ASP A 288 ? 1.09770 1.38073 1.66662 -0.09532 -0.31313 0.29679  324 ASP A N   
2317 C CA  . ASP A 288 ? 1.04757 1.38502 1.71965 -0.08119 -0.27376 0.29207  324 ASP A CA  
2318 C C   . ASP A 288 ? 0.95098 1.29090 1.57868 -0.07617 -0.21259 0.27359  324 ASP A C   
2319 O O   . ASP A 288 ? 1.01762 1.32542 1.58664 -0.06929 -0.20067 0.26712  324 ASP A O   
2320 C CB  . ASP A 288 ? 1.07598 1.42074 1.82470 -0.05888 -0.29307 0.30268  324 ASP A CB  
2321 C CG  . ASP A 288 ? 0.88479 1.29329 1.76061 -0.04303 -0.25915 0.29790  324 ASP A CG  
2322 O OD1 . ASP A 288 ? 0.96630 1.39416 1.83708 -0.03876 -0.20055 0.28143  324 ASP A OD1 
2323 O OD2 . ASP A 288 ? 0.95635 1.39683 1.93713 -0.03410 -0.29141 0.31023  324 ASP A OD2 
2324 N N   . MET A 289 ? 0.71279 1.08904 1.36774 -0.08127 -0.17597 0.26633  325 MET A N   
2325 C CA  . MET A 289 ? 0.93015 1.31100 1.54013 -0.07687 -0.12302 0.24951  325 MET A CA  
2326 C C   . MET A 289 ? 0.86126 1.28547 1.54954 -0.05992 -0.08035 0.24261  325 MET A C   
2327 O O   . MET A 289 ? 0.77464 1.23558 1.56395 -0.05414 -0.08569 0.25183  325 MET A O   
2328 C CB  . MET A 289 ? 0.89277 1.27278 1.45598 -0.09357 -0.11153 0.24803  325 MET A CB  
2329 C CG  . MET A 289 ? 0.88159 1.21949 1.37065 -0.10864 -0.14969 0.25058  325 MET A CG  
2330 S SD  . MET A 289 ? 0.99853 1.29471 1.37624 -0.10511 -0.14159 0.23635  325 MET A SD  
2331 C CE  . MET A 289 ? 1.10349 1.35683 1.41137 -0.12140 -0.18400 0.23977  325 MET A CE  
2332 N N   . ASP A 290 ? 0.81677 1.23789 1.45774 -0.05151 -0.03761 0.22426  326 ASP A N   
2333 C CA  . ASP A 290 ? 0.75506 1.21076 1.44919 -0.03427 0.00923  0.21228  326 ASP A CA  
2334 C C   . ASP A 290 ? 0.79955 1.30194 1.55497 -0.04165 0.03400  0.22309  326 ASP A C   
2335 O O   . ASP A 290 ? 0.68898 1.23253 1.53808 -0.02944 0.05646  0.22374  326 ASP A O   
2336 C CB  . ASP A 290 ? 0.87260 1.31148 1.48678 -0.02791 0.04482  0.18873  326 ASP A CB  
2337 C CG  . ASP A 290 ? 0.97437 1.37692 1.56241 -0.01748 0.03435  0.17424  326 ASP A CG  
2338 O OD1 . ASP A 290 ? 0.85109 1.22148 1.41646 -0.02555 -0.00477 0.18514  326 ASP A OD1 
2339 O OD2 . ASP A 290 ? 0.94921 1.35106 1.53452 -0.00243 0.06622  0.15161  326 ASP A OD2 
2340 N N   . TRP A 291 ? 0.86010 1.35621 1.56845 -0.06153 0.03256  0.23219  327 TRP A N   
2341 C CA  . TRP A 291 ? 0.65461 1.18787 1.41274 -0.07251 0.06142  0.24520  327 TRP A CA  
2342 C C   . TRP A 291 ? 0.82656 1.39140 1.69536 -0.08411 0.03253  0.26391  327 TRP A C   
2343 O O   . TRP A 291 ? 0.78807 1.38535 1.71109 -0.09866 0.05443  0.27750  327 TRP A O   
2344 C CB  . TRP A 291 ? 0.76703 1.27514 1.44116 -0.08944 0.06591  0.25118  327 TRP A CB  
2345 C CG  . TRP A 291 ? 0.82603 1.29522 1.45580 -0.10433 0.01440  0.25656  327 TRP A CG  
2346 C CD1 . TRP A 291 ? 0.83358 1.30068 1.50502 -0.12385 -0.02126 0.27166  327 TRP A CD1 
2347 C CD2 . TRP A 291 ? 0.81739 1.24401 1.35164 -0.10125 -0.00511 0.24417  327 TRP A CD2 
2348 N NE1 . TRP A 291 ? 0.85205 1.27297 1.44988 -0.13093 -0.06068 0.26748  327 TRP A NE1 
2349 C CE2 . TRP A 291 ? 0.77896 1.17761 1.29533 -0.11698 -0.04867 0.25178  327 TRP A CE2 
2350 C CE3 . TRP A 291 ? 0.73382 1.14493 1.19994 -0.08785 0.01042  0.22579  327 TRP A CE3 
2351 C CZ2 . TRP A 291 ? 0.72325 1.08138 1.15486 -0.11744 -0.07053 0.24209  327 TRP A CZ2 
2352 C CZ3 . TRP A 291 ? 0.81192 1.18785 1.20514 -0.09094 -0.01358 0.21827  327 TRP A CZ3 
2353 C CH2 . TRP A 291 ? 0.80755 1.15843 1.18341 -0.10452 -0.05059 0.22668  327 TRP A CH2 
2354 N N   . MET A 292 ? 0.81265 1.36874 1.71772 -0.07943 -0.01710 0.26649  328 MET A N   
2355 C CA  . MET A 292 ? 0.69181 1.28315 1.71107 -0.08842 -0.05096 0.28254  328 MET A CA  
2356 C C   . MET A 292 ? 0.72508 1.36987 1.86339 -0.06546 -0.02673 0.28000  328 MET A C   
2357 O O   . MET A 292 ? 0.76388 1.43434 2.00105 -0.06155 -0.06655 0.28962  328 MET A O   
2358 C CB  . MET A 292 ? 0.79541 1.34808 1.78886 -0.09443 -0.12350 0.28864  328 MET A CB  
2359 C CG  . MET A 292 ? 0.75376 1.25012 1.62547 -0.11207 -0.14563 0.28628  328 MET A CG  
2360 S SD  . MET A 292 ? 1.03169 1.49484 1.89572 -0.12615 -0.22996 0.29626  328 MET A SD  
2361 C CE  . MET A 292 ? 0.88030 1.27195 1.58123 -0.13432 -0.23786 0.28509  328 MET A CE  
2362 N N   . HIS A 293 ? 0.73610 1.39695 1.86514 -0.04828 0.03638  0.26549  329 HIS A N   
2363 C CA  . HIS A 293 ? 0.73214 1.43888 1.96807 -0.02113 0.06530  0.25729  329 HIS A CA  
2364 C C   . HIS A 293 ? 0.80300 1.55063 2.05924 -0.01433 0.14565  0.24788  329 HIS A C   
2365 O O   . HIS A 293 ? 0.90737 1.69545 2.25292 0.01080  0.17887  0.23706  329 HIS A O   
2366 C CB  . HIS A 293 ? 0.75623 1.42174 1.95475 0.00670  0.04961  0.24064  329 HIS A CB  
2367 C CG  . HIS A 293 ? 0.63860 1.26979 1.83670 0.00492  -0.02541 0.25400  329 HIS A CG  
2368 N ND1 . HIS A 293 ? 0.68696 1.34924 2.00420 0.01507  -0.06589 0.26753  329 HIS A ND1 
2369 C CD2 . HIS A 293 ? 0.75720 1.32561 1.84707 -0.00532 -0.06656 0.25674  329 HIS A CD2 
2370 C CE1 . HIS A 293 ? 0.64100 1.25528 1.91244 0.01107  -0.13155 0.27935  329 HIS A CE1 
2371 N NE2 . HIS A 293 ? 0.68674 1.24379 1.81954 -0.00195 -0.12950 0.27298  329 HIS A NE2 
2372 N N   . LEU A 294 ? 0.90443 1.64108 2.07996 -0.03362 0.17896  0.25187  330 LEU A N   
2373 C CA  . LEU A 294 ? 1.07994 1.85286 2.26662 -0.02801 0.25642  0.24659  330 LEU A CA  
2374 C C   . LEU A 294 ? 0.99890 1.84215 2.32650 -0.04231 0.27828  0.26727  330 LEU A C   
2375 O O   . LEU A 294 ? 0.97198 1.83015 2.37335 -0.06304 0.22888  0.28659  330 LEU A O   
2376 C CB  . LEU A 294 ? 1.07292 1.80900 2.12507 -0.04311 0.28381  0.24873  330 LEU A CB  
2377 C CG  . LEU A 294 ? 1.05992 1.72970 1.96938 -0.04187 0.25531  0.23596  330 LEU A CG  
2378 C CD1 . LEU A 294 ? 1.05814 1.69749 1.93766 -0.06770 0.19973  0.25504  330 LEU A CD1 
2379 C CD2 . LEU A 294 ? 1.10534 1.75910 1.90838 -0.03842 0.30638  0.22696  330 LEU A CD2 
2380 N N   . ASN A 295 ? 0.99752 1.88448 2.36122 -0.03208 0.35468  0.26163  331 ASN A N   
2381 C CA  . ASN A 295 ? 1.06779 2.00327 2.52029 -0.04842 0.38426  0.27419  331 ASN A CA  
2382 C C   . ASN A 295 ? 1.02130 1.99062 2.60781 -0.04365 0.33501  0.27441  331 ASN A C   
2383 O O   . ASN A 295 ? 1.06924 2.05570 2.71631 -0.07061 0.30890  0.29151  331 ASN A O   
2384 C CB  . ASN A 295 ? 1.04732 1.96390 2.45109 -0.08924 0.38225  0.30192  331 ASN A CB  
2385 C CG  . ASN A 295 ? 1.28075 2.15755 2.54449 -0.09255 0.42103  0.30624  331 ASN A CG  
2386 O OD1 . ASN A 295 ? 1.29789 2.17515 2.50418 -0.07042 0.47876  0.28868  331 ASN A OD1 
2387 N ND2 . ASN A 295 ? 1.42623 2.25574 2.61483 -0.11782 0.38237  0.32406  331 ASN A ND2 
2388 N N   . GLY A 296 ? 1.04947 2.02457 2.68115 -0.00822 0.32050  0.25510  332 GLY A N   
2389 C CA  . GLY A 296 ? 1.00201 2.00538 2.75469 0.00199  0.27206  0.25589  332 GLY A CA  
2390 C C   . GLY A 296 ? 1.06329 2.04195 2.82632 -0.01845 0.18221  0.27469  332 GLY A C   
2391 O O   . GLY A 296 ? 1.05913 2.06000 2.91647 -0.01683 0.13680  0.27930  332 GLY A O   
2392 N N   . GLY A 297 ? 1.01400 1.94627 2.67826 -0.03706 0.15419  0.28468  333 GLY A N   
2393 C CA  . GLY A 297 ? 1.01451 1.91638 2.66792 -0.05806 0.07086  0.29994  333 GLY A CA  
2394 C C   . GLY A 297 ? 1.00975 1.90369 2.64373 -0.10006 0.05894  0.31666  333 GLY A C   
2395 O O   . GLY A 297 ? 0.87389 1.73718 2.48961 -0.11911 -0.01026 0.32576  333 GLY A O   
2396 N N   . ARG A 298 ? 1.02626 1.94104 2.65790 -0.11495 0.12377  0.32061  334 ARG A N   
2397 C CA  . ARG A 298 ? 1.15357 2.05258 2.76529 -0.15524 0.11527  0.33819  334 ARG A CA  
2398 C C   . ARG A 298 ? 1.26306 2.10581 2.75496 -0.17045 0.09742  0.34630  334 ARG A C   
2399 O O   . ARG A 298 ? 1.35726 2.16950 2.82911 -0.20067 0.05621  0.35793  334 ARG A O   
2400 C CB  . ARG A 298 ? 1.17111 2.10194 2.80438 -0.16656 0.19236  0.34369  334 ARG A CB  
2401 C CG  . ARG A 298 ? 1.13337 2.12727 2.88626 -0.15126 0.22087  0.33453  334 ARG A CG  
2402 C CD  . ARG A 298 ? 1.25947 2.28178 3.01267 -0.16155 0.30544  0.33945  334 ARG A CD  
2403 N NE  . ARG A 298 ? 1.33205 2.41924 3.19722 -0.14402 0.34008  0.32826  334 ARG A NE  
2404 C CZ  . ARG A 298 ? 1.34888 2.45896 3.21569 -0.10759 0.38892  0.30768  334 ARG A CZ  
2405 N NH1 . ARG A 298 ? 1.32869 2.40217 3.09114 -0.08548 0.40951  0.29500  334 ARG A NH1 
2406 N NH2 . ARG A 298 ? 1.23481 2.40581 3.21251 -0.09262 0.41748  0.29800  334 ARG A NH2 
2407 N N   . GLY A 299 ? 1.31672 2.13703 2.71745 -0.14833 0.12588  0.33584  335 GLY A N   
2408 C CA  . GLY A 299 ? 1.34519 2.09110 2.58833 -0.15442 0.11219  0.33190  335 GLY A CA  
2409 C C   . GLY A 299 ? 1.47064 2.20388 2.62065 -0.14348 0.18048  0.32631  335 GLY A C   
2410 O O   . GLY A 299 ? 1.39040 2.13833 2.53135 -0.11526 0.21710  0.30849  335 GLY A O   
2411 N N   . TRP A 300 ? 1.97462 2.67614 3.05200 -0.16467 0.19557  0.34083  336 TRP A N   
2412 C CA  . TRP A 300 ? 1.97937 2.66525 2.96063 -0.15650 0.25512  0.34036  336 TRP A CA  
2413 C C   . TRP A 300 ? 2.06590 2.77354 3.08659 -0.18293 0.30249  0.36940  336 TRP A C   
2414 O O   . TRP A 300 ? 2.01339 2.71490 3.08245 -0.21364 0.27510  0.39005  336 TRP A O   
2415 C CB  . TRP A 300 ? 1.95985 2.57670 2.79497 -0.15251 0.22818  0.33256  336 TRP A CB  
2416 C CG  . TRP A 300 ? 2.03107 2.60674 2.84207 -0.17904 0.18742  0.34973  336 TRP A CG  
2417 C CD1 . TRP A 300 ? 1.98173 2.52867 2.79260 -0.18650 0.12276  0.34379  336 TRP A CD1 
2418 C CD2 . TRP A 300 ? 2.16929 2.72095 2.94708 -0.20067 0.20926  0.37479  336 TRP A CD2 
2419 N NE1 . TRP A 300 ? 2.09204 2.59900 2.87458 -0.21022 0.10318  0.35917  336 TRP A NE1 
2420 C CE2 . TRP A 300 ? 2.17330 2.68093 2.93868 -0.21944 0.15426  0.37979  336 TRP A CE2 
2421 C CE3 . TRP A 300 ? 2.19889 2.75666 2.95021 -0.20574 0.27062  0.39442  336 TRP A CE3 
2422 C CZ2 . TRP A 300 ? 2.13685 2.60441 2.87249 -0.24218 0.15692  0.40282  336 TRP A CZ2 
2423 C CZ3 . TRP A 300 ? 2.17106 2.68907 2.88898 -0.22974 0.27312  0.42214  336 TRP A CZ3 
2424 C CH2 . TRP A 300 ? 2.13158 2.60400 2.84586 -0.24730 0.21576  0.42574  336 TRP A CH2 
2425 N N   . ASP A 301 ? 1.83668 2.56587 2.83312 -0.17233 0.37434  0.37066  337 ASP A N   
2426 C CA  . ASP A 301 ? 1.74527 2.49360 2.76714 -0.19681 0.43176  0.40121  337 ASP A CA  
2427 C C   . ASP A 301 ? 1.81669 2.50434 2.68300 -0.19765 0.45396  0.41287  337 ASP A C   
2428 O O   . ASP A 301 ? 1.85822 2.50268 2.60792 -0.17515 0.43316  0.39247  337 ASP A O   
2429 C CB  . ASP A 301 ? 1.64716 2.44715 2.72678 -0.18141 0.49095  0.38476  337 ASP A CB  
2430 C CG  . ASP A 301 ? 1.55980 2.39003 2.73751 -0.20912 0.50359  0.39900  337 ASP A CG  
2431 O OD1 . ASP A 301 ? 1.59959 2.39781 2.76048 -0.24168 0.49183  0.42557  337 ASP A OD1 
2432 O OD2 . ASP A 301 ? 1.43087 2.31645 2.70546 -0.19802 0.52481  0.38355  337 ASP A OD2 
2433 N N   . ALA A 302 ? 1.84437 2.52407 2.70653 -0.22371 0.49161  0.44408  338 ALA A N   
2434 C CA  . ALA A 302 ? 1.89609 2.51792 2.62276 -0.22824 0.51182  0.46759  338 ALA A CA  
2435 C C   . ALA A 302 ? 2.02736 2.65138 2.67071 -0.21319 0.58227  0.46307  338 ALA A C   
2436 O O   . ALA A 302 ? 1.99654 2.58320 2.50754 -0.19501 0.59261  0.46359  338 ALA A O   
2437 C CB  . ALA A 302 ? 1.83724 2.42066 2.58088 -0.26601 0.49519  0.50070  338 ALA A CB  
2438 N N   . THR A 303 ? 2.11487 2.78246 2.82866 -0.22012 0.62856  0.45743  339 THR A N   
2439 C CA  . THR A 303 ? 2.14394 2.81293 2.77557 -0.21007 0.69723  0.45322  339 THR A CA  
2440 C C   . THR A 303 ? 2.26241 2.96325 2.87671 -0.17172 0.72260  0.41216  339 THR A C   
2441 O O   . THR A 303 ? 2.35988 3.04967 2.87289 -0.15801 0.77187  0.40260  339 THR A O   
2442 C CB  . THR A 303 ? 2.09969 2.80378 2.81146 -0.23703 0.74103  0.46744  339 THR A CB  
2443 O OG1 . THR A 303 ? 2.15974 2.86989 2.78963 -0.22657 0.80946  0.46102  339 THR A OG1 
2444 C CG2 . THR A 303 ? 1.97484 2.75042 2.85754 -0.23640 0.72784  0.44776  339 THR A CG2 
2445 N N   . ILE A 304 ? 2.11681 2.85147 2.82206 -0.15436 0.68830  0.38718  340 ILE A N   
2446 C CA  . ILE A 304 ? 2.03934 2.79788 2.73790 -0.11718 0.70871  0.34674  340 ILE A CA  
2447 C C   . ILE A 304 ? 2.00251 2.72539 2.61464 -0.09524 0.67307  0.33345  340 ILE A C   
2448 O O   . ILE A 304 ? 2.03126 2.73597 2.54388 -0.06937 0.69700  0.30606  340 ILE A O   
2449 C CB  . ILE A 304 ? 1.94728 2.76748 2.80952 -0.10871 0.69781  0.32715  340 ILE A CB  
2450 C CG1 . ILE A 304 ? 1.91538 2.77945 2.86537 -0.12894 0.73659  0.33916  340 ILE A CG1 
2451 C CG2 . ILE A 304 ? 1.91850 2.75472 2.77653 -0.06802 0.71745  0.28467  340 ILE A CG2 
2452 C CD1 . ILE A 304 ? 1.79931 2.68619 2.87996 -0.15736 0.68892  0.35983  340 ILE A CD1 
2453 N N   . ASN A 305 ? 1.94306 2.64039 2.57172 -0.10618 0.59866  0.33945  341 ASN A N   
2454 C CA  . ASN A 305 ? 1.93253 2.58045 2.46365 -0.08853 0.54254  0.31306  341 ASN A CA  
2455 C C   . ASN A 305 ? 2.00359 2.59496 2.38172 -0.09076 0.54023  0.32510  341 ASN A C   
2456 O O   . ASN A 305 ? 2.02937 2.59654 2.30147 -0.06897 0.54453  0.29954  341 ASN A O   
2457 C CB  . ASN A 305 ? 1.82632 2.46519 2.42134 -0.09871 0.46733  0.31378  341 ASN A CB  
2458 C CG  . ASN A 305 ? 1.71106 2.38355 2.40421 -0.08134 0.44838  0.28751  341 ASN A CG  
2459 O OD1 . ASN A 305 ? 1.66493 2.36868 2.47732 -0.09310 0.42390  0.29836  341 ASN A OD1 
2460 N ND2 . ASN A 305 ? 1.57001 2.23241 2.21280 -0.05322 0.45592  0.25290  341 ASN A ND2 
2461 N N   . LYS A 306 ? 1.93071 2.49811 2.29794 -0.11653 0.52991  0.36342  342 LYS A N   
2462 C CA  . LYS A 306 ? 1.98239 2.49248 2.21176 -0.11691 0.52138  0.37992  342 LYS A CA  
2463 C C   . LYS A 306 ? 2.05432 2.56175 2.22758 -0.12525 0.59128  0.40989  342 LYS A C   
2464 O O   . LYS A 306 ? 2.02922 2.51247 2.07814 -0.10767 0.61390  0.40175  342 LYS A O   
2465 C CB  . LYS A 306 ? 1.91027 2.38167 2.14788 -0.13653 0.46459  0.40318  342 LYS A CB  
2466 C CG  . LYS A 306 ? 1.95709 2.36706 2.06239 -0.13217 0.44679  0.41978  342 LYS A CG  
2467 C CD  . LYS A 306 ? 1.93428 2.33023 1.93782 -0.10159 0.42775  0.38456  342 LYS A CD  
2468 C CE  . LYS A 306 ? 1.96443 2.30493 1.84364 -0.09434 0.40629  0.40200  342 LYS A CE  
2469 N NZ  . LYS A 306 ? 2.03152 2.36514 1.81112 -0.06681 0.39486  0.36904  342 LYS A NZ  
# 
