data_9EDW
# 
_entry.id   9EDW 
# 
_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   9EDW         pdb_00009edw 10.2210/pdb9edw/pdb 
WWPDB D_1000290107 ?            ?                   
# 
_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             ? 
# 
_database_PDB_caveat.id     1 
_database_PDB_caveat.text   ? 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9EDW 
_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 1f: 7-fluoro-2-(4-fluorophenyl)-3-(pyridin-4-yl)imidazo[1,2-a]pyridine
;
_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 '7-fluoro-2-(4-fluorophenyl)-3-(pyridin-4-yl)imidazo[1,2-a]pyridine' 307.297   1 ?        ? ? ? 
3 non-polymer syn 'CHLORIDE ION'                                                       35.453    1 ?        ? ? ? 
4 water       nat water                                                                18.015    7 ?        ? ? ? 
# 
_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 '7-fluoro-2-(4-fluorophenyl)-3-(pyridin-4-yl)imidazo[1,2-a]pyridine' A1BIP 
3 'CHLORIDE ION'                                                       CL    
4 water                                                                HOH   
# 
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                 'YCK2, CAALFM_C305650WA, orf19.7001' 
_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 
A1BIP non-polymer         . '7-fluoro-2-(4-fluorophenyl)-3-(pyridin-4-yl)imidazo[1,2-a]pyridine' ? 'C18 H11 F2 N3'  307.297 
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 
HOH   non-polymer         . WATER                                                                ? 'H2 O'           18.015  
ILE   'L-peptide linking' y ISOLEUCINE                                                           ? 'C6 H13 N O2'    131.173 
LEU   'L-peptide linking' y LEUCINE                                                              ? 'C6 H13 N O2'    131.173 
LYS   'L-peptide linking' y LYSINE                                                               ? 'C6 H15 N2 O2 1' 147.195 
MET   'L-peptide linking' y METHIONINE                                                           ? 'C5 H11 N O2 S'  149.211 
PHE   'L-peptide linking' y PHENYLALANINE                                                        ? 'C9 H11 N O2'    165.189 
PRO   'L-peptide linking' y PROLINE                                                              ? 'C5 H9 N O2'     115.130 
SER   'L-peptide linking' y SERINE                                                               ? 'C3 H7 N O3'     105.093 
THR   'L-peptide linking' y THREONINE                                                            ? 'C4 H9 N O3'     119.119 
TRP   'L-peptide linking' y TRYPTOPHAN                                                           ? 'C11 H12 N2 O2'  204.225 
TYR   'L-peptide linking' y TYROSINE                                                             ? 'C9 H11 N O3'    181.189 
VAL   'L-peptide linking' y VALINE                                                               ? 'C5 H11 N O2'    117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   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 
# 
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 A1BIP 1 401 401 A1BIP UNL A . 
C 3 CL    1 402 3   CL    CL  A . 
D 4 HOH   1 501 3   HOH   HOH A . 
D 4 HOH   2 502 6   HOH   HOH A . 
D 4 HOH   3 503 7   HOH   HOH A . 
D 4 HOH   4 504 4   HOH   HOH A . 
D 4 HOH   5 505 1   HOH   HOH A . 
D 4 HOH   6 506 5   HOH   HOH A . 
D 4 HOH   7 507 2   HOH   HOH A . 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX ? ? ? 1.21.2_5419 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? xia2   ? ? ? .           2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? xia2   ? ? ? .           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                     9EDW 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     92.175 
_cell.length_a_esd                 ? 
_cell.length_b                     92.175 
_cell.length_b_esd                 ? 
_cell.length_c                     118.199 
_cell.length_c_esd                 ? 
_cell.volume                       869694.968 
_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                         9EDW 
_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                   9EDW 
_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             2.73 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          54.94 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              8 
_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         2024-05-19 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   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 08B1-1' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        1.18077 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   08B1-1 
_diffrn_source.pdbx_synchrotron_site       CLSI 
# 
_reflns.B_iso_Wilson_estimate                          45.67 
_reflns.entry_id                                       9EDW 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.33 
_reflns.d_resolution_low                               66.14 
_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                                     15999 
_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                                8.9 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          8.0 
_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                                0.050 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.980 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.094 
_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                                    2.33 
_reflns_shell.d_res_low                                     2.39 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           0.9 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             1164 
_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                               7.4 
_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                               1.277 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.265 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          100 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  2.113 
_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                               98.91 
_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                                 9EDW 
_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                            2.33 
_refine.ls_d_res_low                             66.14 
_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                     15954 
_refine.ls_number_reflns_R_free                  822 
_refine.ls_number_reflns_R_work                  15132 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.66 
_refine.ls_percent_reflns_R_free                 5.15 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2703 
_refine.ls_R_factor_R_free                       0.2904 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2690 
_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                 48.8243 
_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                            0.4703 
_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                       2.33 
_refine_hist.d_res_low                        66.14 
_refine_hist.number_atoms_solvent             7 
_refine_hist.number_atoms_total               2500 
_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         24 
_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' ? 0.0026  ? 2554 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.5533  ? 3452 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 0.0413  ? 358  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.0043  ? 451  ? f_plane_restr      ? ? 
'X-RAY DIFFRACTION' ? 15.1127 ? 978  ? 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' 2.33 2.48  . . 151 2497 99.44 . . . . 0.4322 . . . . . . . . . . . 0.4488 
'X-RAY DIFFRACTION' 2.48 2.67  . . 137 2516 99.36 . . . . 0.3939 . . . . . . . . . . . 0.4077 
'X-RAY DIFFRACTION' 2.67 2.94  . . 102 2543 99.59 . . . . 0.3554 . . . . . . . . . . . 0.3806 
'X-RAY DIFFRACTION' 2.94 3.36  . . 127 2544 99.78 . . . . 0.3533 . . . . . . . . . . . 0.3323 
'X-RAY DIFFRACTION' 3.36 4.23  . . 142 2520 99.92 . . . . 0.2569 . . . . . . . . . . . 0.2998 
'X-RAY DIFFRACTION' 4.24 66.14 . . 163 2512 99.89 . . . . 0.2166 . . . . . . . . . . . 0.2496 
# 
_struct.entry_id                     9EDW 
_struct.title                        
;Crystal structure of Yck2 from Candida albicans in complex with inhibitor 1f: 7-fluoro-2-(4-fluorophenyl)-3-(pyridin-4-yl)imidazo[1,2-a]pyridine
;
_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        9EDW 
_struct_keywords.text            
;YCK2, KINASE, KINASE INHIBITOR, STRUCTURAL GENOMICS, CENTER FOR STRUCTURAL BIOLOY OF INFECTIOUS DISEASES, NIAID, NATIONAL INSTITUTE OF ALLERGY AND INFECTIOUS DISEASES, TRANSFERASE, TRANSFERASE-INHIBITOR complex, Center for Structural Biology of Infectious Diseases, CSBID
;
_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 ? 
D N N 4 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    A0A1D8PKB4_CANAL 
_struct_ref.pdbx_db_accession          A0A1D8PKB4 
_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              9EDW 
_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             A0A1D8PKB4 
_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_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_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,D 
# 
_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 LYS A 129 ? ASP A 131 ? LYS A 165 ASP A 167 5 ? 3  
HELX_P HELX_P5  AA5 SER A 182 ? LEU A 187 ? SER A 218 LEU A 223 1 ? 6  
HELX_P HELX_P6  AA6 SER A 192 ? GLY A 210 ? SER A 228 GLY A 246 1 ? 19 
HELX_P HELX_P7  AA7 ASN A 222 ? THR A 236 ? ASN A 258 THR A 272 1 ? 15 
HELX_P HELX_P8  AA8 PRO A 237 ? CYS A 242 ? PRO A 273 CYS A 278 1 ? 6  
HELX_P HELX_P9  AA9 GLN A 247 ? ARG A 257 ? GLN A 283 ARG A 293 1 ? 11 
HELX_P HELX_P10 AB1 PRO A 266 ? LEU A 281 ? PRO A 302 LEU A 317 1 ? 16 
HELX_P HELX_P11 AB2 MET A 289 ? ARG A 298 ? MET A 325 ARG A 334 5 ? 10 
# 
_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 ? 6 ? 
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 
AA1 5 6 ? 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 VAL A 3   ? VAL A 4   ? VAL A 39  VAL A 40  
AA1 2 TYR A 8   ? LYS A 13  ? TYR A 44  LYS A 49  
AA1 3 ILE A 22  ? ASN A 27  ? ILE A 58  ASN A 63  
AA1 4 PRO A 33  ? PRO A 40  ? PRO A 69  PRO A 76  
AA1 5 HIS A 76  ? ASP A 82  ? HIS A 112 ASP A 118 
AA1 6 ALA A 67  ? GLU A 73  ? ALA A 103 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 ? LEU A 134 ? PHE A 169 LEU A 170 
AA3 2 HIS A 147 ? LEU A 148 ? HIS A 183 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 VAL A 4   ? N VAL A 40  O TYR A 8   ? O TYR A 44  
AA1 2 3 N LYS A 12  ? N LYS A 48  O GLU A 24  ? O GLU A 60  
AA1 3 4 N GLY A 25  ? N GLY A 61  O VAL A 34  ? O VAL A 70  
AA1 4 5 N ALA A 35  ? N ALA A 71  O ILE A 81  ? O ILE A 117 
AA1 5 6 O VAL A 80  ? O VAL A 116 N TYR A 68  ? N TYR A 104 
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                   9EDW 
_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  ? ? 73.19   -48.16  
2 1 SER A 54  ? ? 58.20   -133.75 
3 1 ASP A 163 ? ? -163.20 40.90   
4 1 ASP A 186 ? ? 57.69   93.84   
5 1 GLN A 192 ? ? -33.82  129.35  
6 1 SER A 228 ? ? -141.12 -157.36 
7 1 TRP A 250 ? ? -94.91  47.99   
8 1 CYS A 321 ? ? -103.43 66.04   
9 1 ALA A 338 ? ? -100.03 -65.90  
# 
_pdbx_SG_project.full_name_of_center   'Center for Structural Biology of Infectious Diseases' 
_pdbx_SG_project.id                    1 
_pdbx_SG_project.initial_of_center     CSBID 
_pdbx_SG_project.project_name          'NIAID, National Institute of Allergy and Infectious Diseases' 
# 
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 -19.931578614  18.5956809731  16.5309904006 0.482609399806 ? -0.00625538909544 ? -0.0616885434723 
? 0.878897786393 ? -0.127726779714   ? 1.19711418296  ? 6.30739217088 ? -3.04453190488 ? 3.59748884728   ? 4.04027964729 ? 
1.0494570517    ? 6.10141359096 ? 0.498035712066   ? -0.56369653287   ? -0.276355570459  ? 0.279594132348  ? 0.222614803051   ? 
0.247517133281  ? 1.0732636934   ? 0.349355569076 ? -0.586320531429 ? 
2 'X-RAY DIFFRACTION' ? refined -27.2033292916 4.69450527452  7.29416882239 0.477641161506 ? 0.102901016081    ? -0.0130007615445 
? 0.427005298484 ? -0.00991605886121 ? 0.569275410678 ? 5.2707255118  ? 1.31542881587  ? -0.701753351771 ? 5.88479047251 ? 
-0.260645233589 ? 1.31361650504 ? -0.0216884892419 ? 0.00217547836465 ? 0.00185781116466 ? -0.419689632895 ? -0.0091347416468 ? 
-0.945549314539 ? 0.284993553127 ? 0.351952597832 ? 0.0576118697893 ? 
3 'X-RAY DIFFRACTION' ? refined -39.4676635938 -5.58665526709 10.1411397301 0.593675488319 ? 0.149615172527    ? -0.0357872451427 
? 0.289125000133 ? 0.00554374721484  ? 0.346240857949 ? 6.59201821589 ? 0.671751397956 ? -0.431165229303 ? 5.14535493768 ? 
-0.11349539331  ? 3.29166532978 ? -0.497526914139  ? -0.360267154005  ? -0.346658663915  ? -0.242633945008 ? 0.234423803054   ? 
0.299875790634  ? 0.478252727774 ? 0.344235212364 ? 0.0665159779642 ? 
# 
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 47  A 83  ? ? 
;chain 'A' and (resid 37 through 83 )
;
2 'X-RAY DIFFRACTION' 2 A 48  A 84  ? A 177 A 213 ? ? 
;chain 'A' and (resid 84 through 213 )
;
3 'X-RAY DIFFRACTION' 3 A 178 A 214 ? A 306 A 342 ? ? 
;chain 'A' and (resid 214 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 
A1BIP C1   C  Y N 1   
A1BIP C10  C  Y N 2   
A1BIP C11  C  Y N 3   
A1BIP C12  C  Y N 4   
A1BIP C13  C  Y N 5   
A1BIP C14  C  Y N 6   
A1BIP C15  C  Y N 7   
A1BIP C16  C  Y N 8   
A1BIP C17  C  Y N 9   
A1BIP C18  C  Y N 10  
A1BIP C2   C  Y N 11  
A1BIP C3   C  Y N 12  
A1BIP C4   C  Y N 13  
A1BIP C5   C  Y N 14  
A1BIP C6   C  Y N 15  
A1BIP C7   C  Y N 16  
A1BIP C8   C  Y N 17  
A1BIP C9   C  Y N 18  
A1BIP F1   F  N N 19  
A1BIP F2   F  N N 20  
A1BIP N1   N  Y N 21  
A1BIP N2   N  Y N 22  
A1BIP N3   N  Y N 23  
A1BIP H5   H  N N 24  
A1BIP H6   H  N N 25  
A1BIP H7   H  N N 26  
A1BIP H8   H  N N 27  
A1BIP H9   H  N N 28  
A1BIP H10  H  N N 29  
A1BIP H11  H  N N 30  
A1BIP H1   H  N N 31  
A1BIP H2   H  N N 32  
A1BIP H3   H  N N 33  
A1BIP H4   H  N N 34  
ALA   N    N  N N 35  
ALA   CA   C  N S 36  
ALA   C    C  N N 37  
ALA   O    O  N N 38  
ALA   CB   C  N N 39  
ALA   OXT  O  N N 40  
ALA   H    H  N N 41  
ALA   H2   H  N N 42  
ALA   HA   H  N N 43  
ALA   HB1  H  N N 44  
ALA   HB2  H  N N 45  
ALA   HB3  H  N N 46  
ALA   HXT  H  N N 47  
ARG   N    N  N N 48  
ARG   CA   C  N S 49  
ARG   C    C  N N 50  
ARG   O    O  N N 51  
ARG   CB   C  N N 52  
ARG   CG   C  N N 53  
ARG   CD   C  N N 54  
ARG   NE   N  N N 55  
ARG   CZ   C  N N 56  
ARG   NH1  N  N N 57  
ARG   NH2  N  N N 58  
ARG   OXT  O  N N 59  
ARG   H    H  N N 60  
ARG   H2   H  N N 61  
ARG   HA   H  N N 62  
ARG   HB2  H  N N 63  
ARG   HB3  H  N N 64  
ARG   HG2  H  N N 65  
ARG   HG3  H  N N 66  
ARG   HD2  H  N N 67  
ARG   HD3  H  N N 68  
ARG   HE   H  N N 69  
ARG   HH11 H  N N 70  
ARG   HH12 H  N N 71  
ARG   HH21 H  N N 72  
ARG   HH22 H  N N 73  
ARG   HXT  H  N N 74  
ASN   N    N  N N 75  
ASN   CA   C  N S 76  
ASN   C    C  N N 77  
ASN   O    O  N N 78  
ASN   CB   C  N N 79  
ASN   CG   C  N N 80  
ASN   OD1  O  N N 81  
ASN   ND2  N  N N 82  
ASN   OXT  O  N N 83  
ASN   H    H  N N 84  
ASN   H2   H  N N 85  
ASN   HA   H  N N 86  
ASN   HB2  H  N N 87  
ASN   HB3  H  N N 88  
ASN   HD21 H  N N 89  
ASN   HD22 H  N N 90  
ASN   HXT  H  N N 91  
ASP   N    N  N N 92  
ASP   CA   C  N S 93  
ASP   C    C  N N 94  
ASP   O    O  N N 95  
ASP   CB   C  N N 96  
ASP   CG   C  N N 97  
ASP   OD1  O  N N 98  
ASP   OD2  O  N N 99  
ASP   OXT  O  N N 100 
ASP   H    H  N N 101 
ASP   H2   H  N N 102 
ASP   HA   H  N N 103 
ASP   HB2  H  N N 104 
ASP   HB3  H  N N 105 
ASP   HD2  H  N N 106 
ASP   HXT  H  N N 107 
CL    CL   CL N N 108 
CYS   N    N  N N 109 
CYS   CA   C  N R 110 
CYS   C    C  N N 111 
CYS   O    O  N N 112 
CYS   CB   C  N N 113 
CYS   SG   S  N N 114 
CYS   OXT  O  N N 115 
CYS   H    H  N N 116 
CYS   H2   H  N N 117 
CYS   HA   H  N N 118 
CYS   HB2  H  N N 119 
CYS   HB3  H  N N 120 
CYS   HG   H  N N 121 
CYS   HXT  H  N N 122 
GLN   N    N  N N 123 
GLN   CA   C  N S 124 
GLN   C    C  N N 125 
GLN   O    O  N N 126 
GLN   CB   C  N N 127 
GLN   CG   C  N N 128 
GLN   CD   C  N N 129 
GLN   OE1  O  N N 130 
GLN   NE2  N  N N 131 
GLN   OXT  O  N N 132 
GLN   H    H  N N 133 
GLN   H2   H  N N 134 
GLN   HA   H  N N 135 
GLN   HB2  H  N N 136 
GLN   HB3  H  N N 137 
GLN   HG2  H  N N 138 
GLN   HG3  H  N N 139 
GLN   HE21 H  N N 140 
GLN   HE22 H  N N 141 
GLN   HXT  H  N N 142 
GLU   N    N  N N 143 
GLU   CA   C  N S 144 
GLU   C    C  N N 145 
GLU   O    O  N N 146 
GLU   CB   C  N N 147 
GLU   CG   C  N N 148 
GLU   CD   C  N N 149 
GLU   OE1  O  N N 150 
GLU   OE2  O  N N 151 
GLU   OXT  O  N N 152 
GLU   H    H  N N 153 
GLU   H2   H  N N 154 
GLU   HA   H  N N 155 
GLU   HB2  H  N N 156 
GLU   HB3  H  N N 157 
GLU   HG2  H  N N 158 
GLU   HG3  H  N N 159 
GLU   HE2  H  N N 160 
GLU   HXT  H  N N 161 
GLY   N    N  N N 162 
GLY   CA   C  N N 163 
GLY   C    C  N N 164 
GLY   O    O  N N 165 
GLY   OXT  O  N N 166 
GLY   H    H  N N 167 
GLY   H2   H  N N 168 
GLY   HA2  H  N N 169 
GLY   HA3  H  N N 170 
GLY   HXT  H  N N 171 
HIS   N    N  N N 172 
HIS   CA   C  N S 173 
HIS   C    C  N N 174 
HIS   O    O  N N 175 
HIS   CB   C  N N 176 
HIS   CG   C  Y N 177 
HIS   ND1  N  Y N 178 
HIS   CD2  C  Y N 179 
HIS   CE1  C  Y N 180 
HIS   NE2  N  Y N 181 
HIS   OXT  O  N N 182 
HIS   H    H  N N 183 
HIS   H2   H  N N 184 
HIS   HA   H  N N 185 
HIS   HB2  H  N N 186 
HIS   HB3  H  N N 187 
HIS   HD1  H  N N 188 
HIS   HD2  H  N N 189 
HIS   HE1  H  N N 190 
HIS   HE2  H  N N 191 
HIS   HXT  H  N N 192 
HOH   O    O  N N 193 
HOH   H1   H  N N 194 
HOH   H2   H  N N 195 
ILE   N    N  N N 196 
ILE   CA   C  N S 197 
ILE   C    C  N N 198 
ILE   O    O  N N 199 
ILE   CB   C  N S 200 
ILE   CG1  C  N N 201 
ILE   CG2  C  N N 202 
ILE   CD1  C  N N 203 
ILE   OXT  O  N N 204 
ILE   H    H  N N 205 
ILE   H2   H  N N 206 
ILE   HA   H  N N 207 
ILE   HB   H  N N 208 
ILE   HG12 H  N N 209 
ILE   HG13 H  N N 210 
ILE   HG21 H  N N 211 
ILE   HG22 H  N N 212 
ILE   HG23 H  N N 213 
ILE   HD11 H  N N 214 
ILE   HD12 H  N N 215 
ILE   HD13 H  N N 216 
ILE   HXT  H  N N 217 
LEU   N    N  N N 218 
LEU   CA   C  N S 219 
LEU   C    C  N N 220 
LEU   O    O  N N 221 
LEU   CB   C  N N 222 
LEU   CG   C  N N 223 
LEU   CD1  C  N N 224 
LEU   CD2  C  N N 225 
LEU   OXT  O  N N 226 
LEU   H    H  N N 227 
LEU   H2   H  N N 228 
LEU   HA   H  N N 229 
LEU   HB2  H  N N 230 
LEU   HB3  H  N N 231 
LEU   HG   H  N N 232 
LEU   HD11 H  N N 233 
LEU   HD12 H  N N 234 
LEU   HD13 H  N N 235 
LEU   HD21 H  N N 236 
LEU   HD22 H  N N 237 
LEU   HD23 H  N N 238 
LEU   HXT  H  N N 239 
LYS   N    N  N N 240 
LYS   CA   C  N S 241 
LYS   C    C  N N 242 
LYS   O    O  N N 243 
LYS   CB   C  N N 244 
LYS   CG   C  N N 245 
LYS   CD   C  N N 246 
LYS   CE   C  N N 247 
LYS   NZ   N  N N 248 
LYS   OXT  O  N N 249 
LYS   H    H  N N 250 
LYS   H2   H  N N 251 
LYS   HA   H  N N 252 
LYS   HB2  H  N N 253 
LYS   HB3  H  N N 254 
LYS   HG2  H  N N 255 
LYS   HG3  H  N N 256 
LYS   HD2  H  N N 257 
LYS   HD3  H  N N 258 
LYS   HE2  H  N N 259 
LYS   HE3  H  N N 260 
LYS   HZ1  H  N N 261 
LYS   HZ2  H  N N 262 
LYS   HZ3  H  N N 263 
LYS   HXT  H  N N 264 
MET   N    N  N N 265 
MET   CA   C  N S 266 
MET   C    C  N N 267 
MET   O    O  N N 268 
MET   CB   C  N N 269 
MET   CG   C  N N 270 
MET   SD   S  N N 271 
MET   CE   C  N N 272 
MET   OXT  O  N N 273 
MET   H    H  N N 274 
MET   H2   H  N N 275 
MET   HA   H  N N 276 
MET   HB2  H  N N 277 
MET   HB3  H  N N 278 
MET   HG2  H  N N 279 
MET   HG3  H  N N 280 
MET   HE1  H  N N 281 
MET   HE2  H  N N 282 
MET   HE3  H  N N 283 
MET   HXT  H  N N 284 
PHE   N    N  N N 285 
PHE   CA   C  N S 286 
PHE   C    C  N N 287 
PHE   O    O  N N 288 
PHE   CB   C  N N 289 
PHE   CG   C  Y N 290 
PHE   CD1  C  Y N 291 
PHE   CD2  C  Y N 292 
PHE   CE1  C  Y N 293 
PHE   CE2  C  Y N 294 
PHE   CZ   C  Y N 295 
PHE   OXT  O  N N 296 
PHE   H    H  N N 297 
PHE   H2   H  N N 298 
PHE   HA   H  N N 299 
PHE   HB2  H  N N 300 
PHE   HB3  H  N N 301 
PHE   HD1  H  N N 302 
PHE   HD2  H  N N 303 
PHE   HE1  H  N N 304 
PHE   HE2  H  N N 305 
PHE   HZ   H  N N 306 
PHE   HXT  H  N N 307 
PRO   N    N  N N 308 
PRO   CA   C  N S 309 
PRO   C    C  N N 310 
PRO   O    O  N N 311 
PRO   CB   C  N N 312 
PRO   CG   C  N N 313 
PRO   CD   C  N N 314 
PRO   OXT  O  N N 315 
PRO   H    H  N N 316 
PRO   HA   H  N N 317 
PRO   HB2  H  N N 318 
PRO   HB3  H  N N 319 
PRO   HG2  H  N N 320 
PRO   HG3  H  N N 321 
PRO   HD2  H  N N 322 
PRO   HD3  H  N N 323 
PRO   HXT  H  N N 324 
SER   N    N  N N 325 
SER   CA   C  N S 326 
SER   C    C  N N 327 
SER   O    O  N N 328 
SER   CB   C  N N 329 
SER   OG   O  N N 330 
SER   OXT  O  N N 331 
SER   H    H  N N 332 
SER   H2   H  N N 333 
SER   HA   H  N N 334 
SER   HB2  H  N N 335 
SER   HB3  H  N N 336 
SER   HG   H  N N 337 
SER   HXT  H  N N 338 
THR   N    N  N N 339 
THR   CA   C  N S 340 
THR   C    C  N N 341 
THR   O    O  N N 342 
THR   CB   C  N R 343 
THR   OG1  O  N N 344 
THR   CG2  C  N N 345 
THR   OXT  O  N N 346 
THR   H    H  N N 347 
THR   H2   H  N N 348 
THR   HA   H  N N 349 
THR   HB   H  N N 350 
THR   HG1  H  N N 351 
THR   HG21 H  N N 352 
THR   HG22 H  N N 353 
THR   HG23 H  N N 354 
THR   HXT  H  N N 355 
TRP   N    N  N N 356 
TRP   CA   C  N S 357 
TRP   C    C  N N 358 
TRP   O    O  N N 359 
TRP   CB   C  N N 360 
TRP   CG   C  Y N 361 
TRP   CD1  C  Y N 362 
TRP   CD2  C  Y N 363 
TRP   NE1  N  Y N 364 
TRP   CE2  C  Y N 365 
TRP   CE3  C  Y N 366 
TRP   CZ2  C  Y N 367 
TRP   CZ3  C  Y N 368 
TRP   CH2  C  Y N 369 
TRP   OXT  O  N N 370 
TRP   H    H  N N 371 
TRP   H2   H  N N 372 
TRP   HA   H  N N 373 
TRP   HB2  H  N N 374 
TRP   HB3  H  N N 375 
TRP   HD1  H  N N 376 
TRP   HE1  H  N N 377 
TRP   HE3  H  N N 378 
TRP   HZ2  H  N N 379 
TRP   HZ3  H  N N 380 
TRP   HH2  H  N N 381 
TRP   HXT  H  N N 382 
TYR   N    N  N N 383 
TYR   CA   C  N S 384 
TYR   C    C  N N 385 
TYR   O    O  N N 386 
TYR   CB   C  N N 387 
TYR   CG   C  Y N 388 
TYR   CD1  C  Y N 389 
TYR   CD2  C  Y N 390 
TYR   CE1  C  Y N 391 
TYR   CE2  C  Y N 392 
TYR   CZ   C  Y N 393 
TYR   OH   O  N N 394 
TYR   OXT  O  N N 395 
TYR   H    H  N N 396 
TYR   H2   H  N N 397 
TYR   HA   H  N N 398 
TYR   HB2  H  N N 399 
TYR   HB3  H  N N 400 
TYR   HD1  H  N N 401 
TYR   HD2  H  N N 402 
TYR   HE1  H  N N 403 
TYR   HE2  H  N N 404 
TYR   HH   H  N N 405 
TYR   HXT  H  N N 406 
VAL   N    N  N N 407 
VAL   CA   C  N S 408 
VAL   C    C  N N 409 
VAL   O    O  N N 410 
VAL   CB   C  N N 411 
VAL   CG1  C  N N 412 
VAL   CG2  C  N N 413 
VAL   OXT  O  N N 414 
VAL   H    H  N N 415 
VAL   H2   H  N N 416 
VAL   HA   H  N N 417 
VAL   HB   H  N N 418 
VAL   HG11 H  N N 419 
VAL   HG12 H  N N 420 
VAL   HG13 H  N N 421 
VAL   HG21 H  N N 422 
VAL   HG22 H  N N 423 
VAL   HG23 H  N N 424 
VAL   HXT  H  N N 425 
# 
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 
A1BIP F1  C1   sing N N 1   
A1BIP C1  C2   doub Y N 2   
A1BIP C2  C3   sing Y N 3   
A1BIP C3  N1   doub Y N 4   
A1BIP N1  C4   sing Y N 5   
A1BIP C4  C5   sing N N 6   
A1BIP C5  C6   doub Y N 7   
A1BIP C6  C7   sing Y N 8   
A1BIP C7  C8   doub Y N 9   
A1BIP C8  F2   sing N N 10  
A1BIP C8  C9   sing Y N 11  
A1BIP C9  C10  doub Y N 12  
A1BIP C4  C11  doub Y N 13  
A1BIP C11 C12  sing N N 14  
A1BIP C12 C13  doub Y N 15  
A1BIP C13 C14  sing Y N 16  
A1BIP C14 N2   doub Y N 17  
A1BIP N2  C15  sing Y N 18  
A1BIP C15 C16  doub Y N 19  
A1BIP C11 N3   sing Y N 20  
A1BIP N3  C17  sing Y N 21  
A1BIP C17 C18  doub Y N 22  
A1BIP C1  C18  sing Y N 23  
A1BIP C3  N3   sing Y N 24  
A1BIP C5  C10  sing Y N 25  
A1BIP C12 C16  sing Y N 26  
A1BIP C10 H5   sing N N 27  
A1BIP C13 H6   sing N N 28  
A1BIP C14 H7   sing N N 29  
A1BIP C15 H8   sing N N 30  
A1BIP C16 H9   sing N N 31  
A1BIP C17 H10  sing N N 32  
A1BIP C18 H11  sing N N 33  
A1BIP C2  H1   sing N N 34  
A1BIP C6  H2   sing N N 35  
A1BIP C7  H3   sing N N 36  
A1BIP C9  H4   sing N N 37  
ALA   N   CA   sing N N 38  
ALA   N   H    sing N N 39  
ALA   N   H2   sing N N 40  
ALA   CA  C    sing N N 41  
ALA   CA  CB   sing N N 42  
ALA   CA  HA   sing N N 43  
ALA   C   O    doub N N 44  
ALA   C   OXT  sing N N 45  
ALA   CB  HB1  sing N N 46  
ALA   CB  HB2  sing N N 47  
ALA   CB  HB3  sing N N 48  
ALA   OXT HXT  sing N N 49  
ARG   N   CA   sing N N 50  
ARG   N   H    sing N N 51  
ARG   N   H2   sing N N 52  
ARG   CA  C    sing N N 53  
ARG   CA  CB   sing N N 54  
ARG   CA  HA   sing N N 55  
ARG   C   O    doub N N 56  
ARG   C   OXT  sing N N 57  
ARG   CB  CG   sing N N 58  
ARG   CB  HB2  sing N N 59  
ARG   CB  HB3  sing N N 60  
ARG   CG  CD   sing N N 61  
ARG   CG  HG2  sing N N 62  
ARG   CG  HG3  sing N N 63  
ARG   CD  NE   sing N N 64  
ARG   CD  HD2  sing N N 65  
ARG   CD  HD3  sing N N 66  
ARG   NE  CZ   sing N N 67  
ARG   NE  HE   sing N N 68  
ARG   CZ  NH1  sing N N 69  
ARG   CZ  NH2  doub N N 70  
ARG   NH1 HH11 sing N N 71  
ARG   NH1 HH12 sing N N 72  
ARG   NH2 HH21 sing N N 73  
ARG   NH2 HH22 sing N N 74  
ARG   OXT HXT  sing N N 75  
ASN   N   CA   sing N N 76  
ASN   N   H    sing N N 77  
ASN   N   H2   sing N N 78  
ASN   CA  C    sing N N 79  
ASN   CA  CB   sing N N 80  
ASN   CA  HA   sing N N 81  
ASN   C   O    doub N N 82  
ASN   C   OXT  sing N N 83  
ASN   CB  CG   sing N N 84  
ASN   CB  HB2  sing N N 85  
ASN   CB  HB3  sing N N 86  
ASN   CG  OD1  doub N N 87  
ASN   CG  ND2  sing N N 88  
ASN   ND2 HD21 sing N N 89  
ASN   ND2 HD22 sing N N 90  
ASN   OXT HXT  sing N N 91  
ASP   N   CA   sing N N 92  
ASP   N   H    sing N N 93  
ASP   N   H2   sing N N 94  
ASP   CA  C    sing N N 95  
ASP   CA  CB   sing N N 96  
ASP   CA  HA   sing N N 97  
ASP   C   O    doub N N 98  
ASP   C   OXT  sing N N 99  
ASP   CB  CG   sing N N 100 
ASP   CB  HB2  sing N N 101 
ASP   CB  HB3  sing N N 102 
ASP   CG  OD1  doub N N 103 
ASP   CG  OD2  sing N N 104 
ASP   OD2 HD2  sing N N 105 
ASP   OXT HXT  sing N N 106 
CYS   N   CA   sing N N 107 
CYS   N   H    sing N N 108 
CYS   N   H2   sing N N 109 
CYS   CA  C    sing N N 110 
CYS   CA  CB   sing N N 111 
CYS   CA  HA   sing N N 112 
CYS   C   O    doub N N 113 
CYS   C   OXT  sing N N 114 
CYS   CB  SG   sing N N 115 
CYS   CB  HB2  sing N N 116 
CYS   CB  HB3  sing N N 117 
CYS   SG  HG   sing N N 118 
CYS   OXT HXT  sing N N 119 
GLN   N   CA   sing N N 120 
GLN   N   H    sing N N 121 
GLN   N   H2   sing N N 122 
GLN   CA  C    sing N N 123 
GLN   CA  CB   sing N N 124 
GLN   CA  HA   sing N N 125 
GLN   C   O    doub N N 126 
GLN   C   OXT  sing N N 127 
GLN   CB  CG   sing N N 128 
GLN   CB  HB2  sing N N 129 
GLN   CB  HB3  sing N N 130 
GLN   CG  CD   sing N N 131 
GLN   CG  HG2  sing N N 132 
GLN   CG  HG3  sing N N 133 
GLN   CD  OE1  doub N N 134 
GLN   CD  NE2  sing N N 135 
GLN   NE2 HE21 sing N N 136 
GLN   NE2 HE22 sing N N 137 
GLN   OXT HXT  sing N N 138 
GLU   N   CA   sing N N 139 
GLU   N   H    sing N N 140 
GLU   N   H2   sing N N 141 
GLU   CA  C    sing N N 142 
GLU   CA  CB   sing N N 143 
GLU   CA  HA   sing N N 144 
GLU   C   O    doub N N 145 
GLU   C   OXT  sing N N 146 
GLU   CB  CG   sing N N 147 
GLU   CB  HB2  sing N N 148 
GLU   CB  HB3  sing N N 149 
GLU   CG  CD   sing N N 150 
GLU   CG  HG2  sing N N 151 
GLU   CG  HG3  sing N N 152 
GLU   CD  OE1  doub N N 153 
GLU   CD  OE2  sing N N 154 
GLU   OE2 HE2  sing N N 155 
GLU   OXT HXT  sing N N 156 
GLY   N   CA   sing N N 157 
GLY   N   H    sing N N 158 
GLY   N   H2   sing N N 159 
GLY   CA  C    sing N N 160 
GLY   CA  HA2  sing N N 161 
GLY   CA  HA3  sing N N 162 
GLY   C   O    doub N N 163 
GLY   C   OXT  sing N N 164 
GLY   OXT HXT  sing N N 165 
HIS   N   CA   sing N N 166 
HIS   N   H    sing N N 167 
HIS   N   H2   sing N N 168 
HIS   CA  C    sing N N 169 
HIS   CA  CB   sing N N 170 
HIS   CA  HA   sing N N 171 
HIS   C   O    doub N N 172 
HIS   C   OXT  sing N N 173 
HIS   CB  CG   sing N N 174 
HIS   CB  HB2  sing N N 175 
HIS   CB  HB3  sing N N 176 
HIS   CG  ND1  sing Y N 177 
HIS   CG  CD2  doub Y N 178 
HIS   ND1 CE1  doub Y N 179 
HIS   ND1 HD1  sing N N 180 
HIS   CD2 NE2  sing Y N 181 
HIS   CD2 HD2  sing N N 182 
HIS   CE1 NE2  sing Y N 183 
HIS   CE1 HE1  sing N N 184 
HIS   NE2 HE2  sing N N 185 
HIS   OXT HXT  sing N N 186 
HOH   O   H1   sing N N 187 
HOH   O   H2   sing N N 188 
ILE   N   CA   sing N N 189 
ILE   N   H    sing N N 190 
ILE   N   H2   sing N N 191 
ILE   CA  C    sing N N 192 
ILE   CA  CB   sing N N 193 
ILE   CA  HA   sing N N 194 
ILE   C   O    doub N N 195 
ILE   C   OXT  sing N N 196 
ILE   CB  CG1  sing N N 197 
ILE   CB  CG2  sing N N 198 
ILE   CB  HB   sing N N 199 
ILE   CG1 CD1  sing N N 200 
ILE   CG1 HG12 sing N N 201 
ILE   CG1 HG13 sing N N 202 
ILE   CG2 HG21 sing N N 203 
ILE   CG2 HG22 sing N N 204 
ILE   CG2 HG23 sing N N 205 
ILE   CD1 HD11 sing N N 206 
ILE   CD1 HD12 sing N N 207 
ILE   CD1 HD13 sing N N 208 
ILE   OXT HXT  sing N N 209 
LEU   N   CA   sing N N 210 
LEU   N   H    sing N N 211 
LEU   N   H2   sing N N 212 
LEU   CA  C    sing N N 213 
LEU   CA  CB   sing N N 214 
LEU   CA  HA   sing N N 215 
LEU   C   O    doub N N 216 
LEU   C   OXT  sing N N 217 
LEU   CB  CG   sing N N 218 
LEU   CB  HB2  sing N N 219 
LEU   CB  HB3  sing N N 220 
LEU   CG  CD1  sing N N 221 
LEU   CG  CD2  sing N N 222 
LEU   CG  HG   sing N N 223 
LEU   CD1 HD11 sing N N 224 
LEU   CD1 HD12 sing N N 225 
LEU   CD1 HD13 sing N N 226 
LEU   CD2 HD21 sing N N 227 
LEU   CD2 HD22 sing N N 228 
LEU   CD2 HD23 sing N N 229 
LEU   OXT HXT  sing N N 230 
LYS   N   CA   sing N N 231 
LYS   N   H    sing N N 232 
LYS   N   H2   sing N N 233 
LYS   CA  C    sing N N 234 
LYS   CA  CB   sing N N 235 
LYS   CA  HA   sing N N 236 
LYS   C   O    doub N N 237 
LYS   C   OXT  sing N N 238 
LYS   CB  CG   sing N N 239 
LYS   CB  HB2  sing N N 240 
LYS   CB  HB3  sing N N 241 
LYS   CG  CD   sing N N 242 
LYS   CG  HG2  sing N N 243 
LYS   CG  HG3  sing N N 244 
LYS   CD  CE   sing N N 245 
LYS   CD  HD2  sing N N 246 
LYS   CD  HD3  sing N N 247 
LYS   CE  NZ   sing N N 248 
LYS   CE  HE2  sing N N 249 
LYS   CE  HE3  sing N N 250 
LYS   NZ  HZ1  sing N N 251 
LYS   NZ  HZ2  sing N N 252 
LYS   NZ  HZ3  sing N N 253 
LYS   OXT HXT  sing N N 254 
MET   N   CA   sing N N 255 
MET   N   H    sing N N 256 
MET   N   H2   sing N N 257 
MET   CA  C    sing N N 258 
MET   CA  CB   sing N N 259 
MET   CA  HA   sing N N 260 
MET   C   O    doub N N 261 
MET   C   OXT  sing N N 262 
MET   CB  CG   sing N N 263 
MET   CB  HB2  sing N N 264 
MET   CB  HB3  sing N N 265 
MET   CG  SD   sing N N 266 
MET   CG  HG2  sing N N 267 
MET   CG  HG3  sing N N 268 
MET   SD  CE   sing N N 269 
MET   CE  HE1  sing N N 270 
MET   CE  HE2  sing N N 271 
MET   CE  HE3  sing N N 272 
MET   OXT HXT  sing N N 273 
PHE   N   CA   sing N N 274 
PHE   N   H    sing N N 275 
PHE   N   H2   sing N N 276 
PHE   CA  C    sing N N 277 
PHE   CA  CB   sing N N 278 
PHE   CA  HA   sing N N 279 
PHE   C   O    doub N N 280 
PHE   C   OXT  sing N N 281 
PHE   CB  CG   sing N N 282 
PHE   CB  HB2  sing N N 283 
PHE   CB  HB3  sing N N 284 
PHE   CG  CD1  doub Y N 285 
PHE   CG  CD2  sing Y N 286 
PHE   CD1 CE1  sing Y N 287 
PHE   CD1 HD1  sing N N 288 
PHE   CD2 CE2  doub Y N 289 
PHE   CD2 HD2  sing N N 290 
PHE   CE1 CZ   doub Y N 291 
PHE   CE1 HE1  sing N N 292 
PHE   CE2 CZ   sing Y N 293 
PHE   CE2 HE2  sing N N 294 
PHE   CZ  HZ   sing N N 295 
PHE   OXT HXT  sing N N 296 
PRO   N   CA   sing N N 297 
PRO   N   CD   sing N N 298 
PRO   N   H    sing N N 299 
PRO   CA  C    sing N N 300 
PRO   CA  CB   sing N N 301 
PRO   CA  HA   sing N N 302 
PRO   C   O    doub N N 303 
PRO   C   OXT  sing N N 304 
PRO   CB  CG   sing N N 305 
PRO   CB  HB2  sing N N 306 
PRO   CB  HB3  sing N N 307 
PRO   CG  CD   sing N N 308 
PRO   CG  HG2  sing N N 309 
PRO   CG  HG3  sing N N 310 
PRO   CD  HD2  sing N N 311 
PRO   CD  HD3  sing N N 312 
PRO   OXT HXT  sing N N 313 
SER   N   CA   sing N N 314 
SER   N   H    sing N N 315 
SER   N   H2   sing N N 316 
SER   CA  C    sing N N 317 
SER   CA  CB   sing N N 318 
SER   CA  HA   sing N N 319 
SER   C   O    doub N N 320 
SER   C   OXT  sing N N 321 
SER   CB  OG   sing N N 322 
SER   CB  HB2  sing N N 323 
SER   CB  HB3  sing N N 324 
SER   OG  HG   sing N N 325 
SER   OXT HXT  sing N N 326 
THR   N   CA   sing N N 327 
THR   N   H    sing N N 328 
THR   N   H2   sing N N 329 
THR   CA  C    sing N N 330 
THR   CA  CB   sing N N 331 
THR   CA  HA   sing N N 332 
THR   C   O    doub N N 333 
THR   C   OXT  sing N N 334 
THR   CB  OG1  sing N N 335 
THR   CB  CG2  sing N N 336 
THR   CB  HB   sing N N 337 
THR   OG1 HG1  sing N N 338 
THR   CG2 HG21 sing N N 339 
THR   CG2 HG22 sing N N 340 
THR   CG2 HG23 sing N N 341 
THR   OXT HXT  sing N N 342 
TRP   N   CA   sing N N 343 
TRP   N   H    sing N N 344 
TRP   N   H2   sing N N 345 
TRP   CA  C    sing N N 346 
TRP   CA  CB   sing N N 347 
TRP   CA  HA   sing N N 348 
TRP   C   O    doub N N 349 
TRP   C   OXT  sing N N 350 
TRP   CB  CG   sing N N 351 
TRP   CB  HB2  sing N N 352 
TRP   CB  HB3  sing N N 353 
TRP   CG  CD1  doub Y N 354 
TRP   CG  CD2  sing Y N 355 
TRP   CD1 NE1  sing Y N 356 
TRP   CD1 HD1  sing N N 357 
TRP   CD2 CE2  doub Y N 358 
TRP   CD2 CE3  sing Y N 359 
TRP   NE1 CE2  sing Y N 360 
TRP   NE1 HE1  sing N N 361 
TRP   CE2 CZ2  sing Y N 362 
TRP   CE3 CZ3  doub Y N 363 
TRP   CE3 HE3  sing N N 364 
TRP   CZ2 CH2  doub Y N 365 
TRP   CZ2 HZ2  sing N N 366 
TRP   CZ3 CH2  sing Y N 367 
TRP   CZ3 HZ3  sing N N 368 
TRP   CH2 HH2  sing N N 369 
TRP   OXT HXT  sing N N 370 
TYR   N   CA   sing N N 371 
TYR   N   H    sing N N 372 
TYR   N   H2   sing N N 373 
TYR   CA  C    sing N N 374 
TYR   CA  CB   sing N N 375 
TYR   CA  HA   sing N N 376 
TYR   C   O    doub N N 377 
TYR   C   OXT  sing N N 378 
TYR   CB  CG   sing N N 379 
TYR   CB  HB2  sing N N 380 
TYR   CB  HB3  sing N N 381 
TYR   CG  CD1  doub Y N 382 
TYR   CG  CD2  sing Y N 383 
TYR   CD1 CE1  sing Y N 384 
TYR   CD1 HD1  sing N N 385 
TYR   CD2 CE2  doub Y N 386 
TYR   CD2 HD2  sing N N 387 
TYR   CE1 CZ   doub Y N 388 
TYR   CE1 HE1  sing N N 389 
TYR   CE2 CZ   sing Y N 390 
TYR   CE2 HE2  sing N N 391 
TYR   CZ  OH   sing N N 392 
TYR   OH  HH   sing N N 393 
TYR   OXT HXT  sing N N 394 
VAL   N   CA   sing N N 395 
VAL   N   H    sing N N 396 
VAL   N   H2   sing N N 397 
VAL   CA  C    sing N N 398 
VAL   CA  CB   sing N N 399 
VAL   CA  HA   sing N N 400 
VAL   C   O    doub N N 401 
VAL   C   OXT  sing N N 402 
VAL   CB  CG1  sing N N 403 
VAL   CB  CG2  sing N N 404 
VAL   CB  HB   sing N N 405 
VAL   CG1 HG11 sing N N 406 
VAL   CG1 HG12 sing N N 407 
VAL   CG1 HG13 sing N N 408 
VAL   CG2 HG21 sing N N 409 
VAL   CG2 HG22 sing N N 410 
VAL   CG2 HG23 sing N N 411 
VAL   OXT HXT  sing N N 412 
# 
_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                    9EDW 
_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]   0.010849 
_atom_sites.fract_transf_matrix[1][2]   0.006264 
_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]   0.012527 
_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]   0.008460 
_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  ? ? 4.90428 4.07044 ? ? 12.99538 1.63651  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
N  ? ? 4.01032 2.96436 ? ? 19.97189 1.75589  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
O  ? ? 4.49882 3.47563 ? ? 15.80542 1.70748  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
S  ? ? 9.55732 6.39887 ? ? 1.23737  29.19336 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
# 
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   ? -12.66100 28.59700  22.12800  1.000 125.23735 ? 37  SER   A N   1 
ATOM   2    C  CA  . SER   A 1 1   ? -13.39900 29.23300  21.04400  1.000 131.94960 ? 37  SER   A CA  1 
ATOM   3    C  C   . SER   A 1 1   ? -14.62600 28.40900  20.66600  1.000 149.67408 ? 37  SER   A C   1 
ATOM   4    O  O   . SER   A 1 1   ? -14.64200 27.18900  20.83400  1.000 152.64010 ? 37  SER   A O   1 
ATOM   5    C  CB  . SER   A 1 1   ? -12.49500 29.43100  19.82500  1.000 135.86122 ? 37  SER   A CB  1 
ATOM   6    O  OG  . SER   A 1 1   ? -13.17000 30.13100  18.79500  1.000 136.78420 ? 37  SER   A OG  1 
ATOM   7    N  N   . SER   A 1 2   ? -15.65300 29.08300  20.15200  1.000 148.49311 ? 38  SER   A N   1 
ATOM   8    C  CA  . SER   A 1 2   ? -16.90900 28.43600  19.79900  1.000 149.11666 ? 38  SER   A CA  1 
ATOM   9    C  C   . SER   A 1 2   ? -16.93200 27.89700  18.37500  1.000 149.48934 ? 38  SER   A C   1 
ATOM   10   O  O   . SER   A 1 2   ? -17.90200 27.22800  18.00000  1.000 135.74395 ? 38  SER   A O   1 
ATOM   11   C  CB  . SER   A 1 2   ? -18.07500 29.41300  19.99000  1.000 140.42691 ? 38  SER   A CB  1 
ATOM   12   O  OG  . SER   A 1 2   ? -17.86600 30.60700  19.25600  1.000 146.26547 ? 38  SER   A OG  1 
ATOM   13   N  N   . VAL   A 1 3   ? -15.90100 28.16300  17.57800  1.000 180.61428 ? 39  VAL   A N   1 
ATOM   14   C  CA  . VAL   A 1 3   ? -15.85500 27.74900  16.18100  1.000 164.42032 ? 39  VAL   A CA  1 
ATOM   15   C  C   . VAL   A 1 3   ? -14.92600 26.55200  16.04800  1.000 164.60890 ? 39  VAL   A C   1 
ATOM   16   O  O   . VAL   A 1 3   ? -13.75500 26.61400  16.44500  1.000 170.19483 ? 39  VAL   A O   1 
ATOM   17   C  CB  . VAL   A 1 3   ? -15.39400 28.90100  15.27200  1.000 181.92191 ? 39  VAL   A CB  1 
ATOM   18   C  CG1 . VAL   A 1 3   ? -15.25500 28.41900  13.83500  1.000 167.26882 ? 39  VAL   A CG1 1 
ATOM   19   C  CG2 . VAL   A 1 3   ? -16.36800 30.06600  15.35600  1.000 181.76483 ? 39  VAL   A CG2 1 
ATOM   20   N  N   . VAL   A 1 4   ? -15.44700 25.46000  15.49100  1.000 126.70328 ? 40  VAL   A N   1 
ATOM   21   C  CA  . VAL   A 1 4   ? -14.65400 24.28300  15.17200  1.000 125.98131 ? 40  VAL   A CA  1 
ATOM   22   C  C   . VAL   A 1 4   ? -14.77500 24.02000  13.67700  1.000 113.96269 ? 40  VAL   A C   1 
ATOM   23   O  O   . VAL   A 1 4   ? -15.70200 24.48700  13.01100  1.000 101.77020 ? 40  VAL   A O   1 
ATOM   24   C  CB  . VAL   A 1 4   ? -15.08300 23.04200  15.98000  1.000 113.86932 ? 40  VAL   A CB  1 
ATOM   25   C  CG1 . VAL   A 1 4   ? -15.11100 23.35900  17.46800  1.000 121.55305 ? 40  VAL   A CG1 1 
ATOM   26   C  CG2 . VAL   A 1 4   ? -16.43700 22.53700  15.50600  1.000 112.03862 ? 40  VAL   A CG2 1 
ATOM   27   N  N   . GLY   A 1 5   ? -13.81500 23.26400  13.15100  1.000 103.56974 ? 41  GLY   A N   1 
ATOM   28   C  CA  . GLY   A 1 5   ? -13.80800 22.96800  11.73200  1.000 92.29150  ? 41  GLY   A CA  1 
ATOM   29   C  C   . GLY   A 1 5   ? -13.67800 24.17700  10.83900  1.000 91.71464  ? 41  GLY   A C   1 
ATOM   30   O  O   . GLY   A 1 5   ? -14.08800 24.12000  9.67600   1.000 90.39011  ? 41  GLY   A O   1 
ATOM   31   N  N   . LEU   A 1 6   ? -13.12600 25.27700  11.36400  1.000 83.50663  ? 42  LEU   A N   1 
ATOM   32   C  CA  . LEU   A 1 6   ? -12.89200 26.53100  10.65100  1.000 83.88145  ? 42  LEU   A CA  1 
ATOM   33   C  C   . LEU   A 1 6   ? -14.18300 27.30300  10.39900  1.000 94.15660  ? 42  LEU   A C   1 
ATOM   34   O  O   . LEU   A 1 6   ? -14.24700 28.51000  10.65800  1.000 97.04855  ? 42  LEU   A O   1 
ATOM   35   C  CB  . LEU   A 1 6   ? -12.16700 26.29300  9.31800   1.000 84.48461  ? 42  LEU   A CB  1 
ATOM   36   C  CG  . LEU   A 1 6   ? -10.68900 25.89700  9.26700   1.000 89.11784  ? 42  LEU   A CG  1 
ATOM   37   C  CD1 . LEU   A 1 6   ? -10.44700 24.49500  9.81300   1.000 95.12238  ? 42  LEU   A CD1 1 
ATOM   38   C  CD2 . LEU   A 1 6   ? -10.19000 26.01100  7.83500   1.000 84.32534  ? 42  LEU   A CD2 1 
ATOM   39   N  N   . HIS   A 1 7   ? -15.21500 26.62500  9.89000   1.000 69.11511  ? 43  HIS   A N   1 
ATOM   40   C  CA  . HIS   A 1 7   ? -16.39200 27.29400  9.34600   1.000 80.06184  ? 43  HIS   A CA  1 
ATOM   41   C  C   . HIS   A 1 7   ? -17.68600 26.90400  10.05200  1.000 94.07154  ? 43  HIS   A C   1 
ATOM   42   O  O   . HIS   A 1 7   ? -18.76600 27.11600  9.49400   1.000 82.12669  ? 43  HIS   A O   1 
ATOM   43   C  CB  . HIS   A 1 7   ? -16.54000 27.00000  7.84900   1.000 81.82706  ? 43  HIS   A CB  1 
ATOM   44   C  CG  . HIS   A 1 7   ? -15.38500 27.45000  7.00900   1.000 72.29339  ? 43  HIS   A CG  1 
ATOM   45   N  ND1 . HIS   A 1 7   ? -14.25300 28.03300  7.53600   1.000 92.46124  ? 43  HIS   A ND1 1 
ATOM   46   C  CD2 . HIS   A 1 7   ? -15.19100 27.39700  5.67000   1.000 75.67185  ? 43  HIS   A CD2 1 
ATOM   47   C  CE1 . HIS   A 1 7   ? -13.41000 28.31600  6.56000   1.000 102.04822 ? 43  HIS   A CE1 1 
ATOM   48   N  NE2 . HIS   A 1 7   ? -13.95600 27.94200  5.41700   1.000 104.27110 ? 43  HIS   A NE2 1 
ATOM   49   N  N   . TYR   A 1 8   ? -17.62400 26.34100  11.25700  1.000 92.71556  ? 44  TYR   A N   1 
ATOM   50   C  CA  . TYR   A 1 8   ? -18.81800 25.78500  11.88700  1.000 86.72158  ? 44  TYR   A CA  1 
ATOM   51   C  C   . TYR   A 1 8   ? -18.90800 26.22000  13.34200  1.000 105.79943 ? 44  TYR   A C   1 
ATOM   52   O  O   . TYR   A 1 8   ? -18.04400 25.87200  14.15300  1.000 120.10125 ? 44  TYR   A O   1 
ATOM   53   C  CB  . TYR   A 1 8   ? -18.83100 24.25800  11.77000  1.000 78.37438  ? 44  TYR   A CB  1 
ATOM   54   C  CG  . TYR   A 1 8   ? -18.89200 23.79500  10.33300  1.000 70.52387  ? 44  TYR   A CG  1 
ATOM   55   C  CD1 . TYR   A 1 8   ? -20.04200 23.97600  9.57700   1.000 79.29189  ? 44  TYR   A CD1 1 
ATOM   56   C  CD2 . TYR   A 1 8   ? -17.79600 23.19800  9.72500   1.000 77.32624  ? 44  TYR   A CD2 1 
ATOM   57   C  CE1 . TYR   A 1 8   ? -20.10400 23.57000  8.26100   1.000 80.28820  ? 44  TYR   A CE1 1 
ATOM   58   C  CE2 . TYR   A 1 8   ? -17.84800 22.78600  8.40800   1.000 76.20320  ? 44  TYR   A CE2 1 
ATOM   59   C  CZ  . TYR   A 1 8   ? -19.00400 22.97500  7.68200   1.000 73.92551  ? 44  TYR   A CZ  1 
ATOM   60   O  OH  . TYR   A 1 8   ? -19.06000 22.56900  6.37200   1.000 78.93067  ? 44  TYR   A OH  1 
ATOM   61   N  N   . LYS   A 1 9   ? -19.96800 26.95800  13.66400  1.000 102.42773 ? 45  LYS   A N   1 
ATOM   62   C  CA  . LYS   A 1 9   ? -20.23400 27.38700  15.02900  1.000 108.99020 ? 45  LYS   A CA  1 
ATOM   63   C  C   . LYS   A 1 9   ? -21.03100 26.32500  15.77700  1.000 103.40845 ? 45  LYS   A C   1 
ATOM   64   O  O   . LYS   A 1 9   ? -21.96600 25.73000  15.23400  1.000 93.59906  ? 45  LYS   A O   1 
ATOM   65   C  CB  . LYS   A 1 9   ? -21.00000 28.71300  15.03000  1.000 97.89293  ? 45  LYS   A CB  1 
ATOM   66   C  CG  . LYS   A 1 9   ? -21.97400 28.86600  16.18900  1.000 104.59979 ? 45  LYS   A CG  1 
ATOM   67   C  CD  . LYS   A 1 9   ? -22.96400 29.98600  15.94400  1.000 90.63858  ? 45  LYS   A CD  1 
ATOM   68   C  CE  . LYS   A 1 9   ? -24.26000 29.73900  16.69700  1.000 104.66608 ? 45  LYS   A CE  1 
ATOM   69   N  NZ  . LYS   A 1 9   ? -24.07000 29.63500  18.16600  1.000 99.22174  ? 45  LYS   A NZ  1 
ATOM   70   N  N   . ILE   A 1 10  ? -20.65100 26.08800  17.02800  1.000 114.12545 ? 46  ILE   A N   1 
ATOM   71   C  CA  . ILE   A 1 10  ? -21.35000 25.13000  17.87700  1.000 114.12142 ? 46  ILE   A CA  1 
ATOM   72   C  C   . ILE   A 1 10  ? -22.58000 25.79500  18.48000  1.000 118.89127 ? 46  ILE   A C   1 
ATOM   73   O  O   . ILE   A 1 10  ? -22.49600 26.89200  19.04500  1.000 127.28731 ? 46  ILE   A O   1 
ATOM   74   C  CB  . ILE   A 1 10  ? -20.41500 24.59700  18.97200  1.000 109.11926 ? 46  ILE   A CB  1 
ATOM   75   C  CG1 . ILE   A 1 10  ? -19.37100 23.65700  18.37000  1.000 107.42514 ? 46  ILE   A CG1 1 
ATOM   76   C  CG2 . ILE   A 1 10  ? -21.20900 23.90200  20.06300  1.000 126.86010 ? 46  ILE   A CG2 1 
ATOM   77   C  CD1 . ILE   A 1 10  ? -18.33100 23.20700  19.36300  1.000 113.45799 ? 46  ILE   A CD1 1 
ATOM   78   N  N   . GLY   A 1 11  ? -23.72600 25.13000  18.36500  1.000 141.43062 ? 47  GLY   A N   1 
ATOM   79   C  CA  . GLY   A 1 11  ? -24.95900 25.63400  18.93800  1.000 150.51909 ? 47  GLY   A CA  1 
ATOM   80   C  C   . GLY   A 1 11  ? -25.44000 24.80500  20.11200  1.000 169.09544 ? 47  GLY   A C   1 
ATOM   81   O  O   . GLY   A 1 11  ? -24.67600 24.53900  21.04500  1.000 171.59847 ? 47  GLY   A O   1 
ATOM   82   N  N   . LYS   A 1 12  ? -26.70400 24.39200  20.08200  1.000 147.06448 ? 48  LYS   A N   1 
ATOM   83   C  CA  . LYS   A 1 12  ? -27.25700 23.58700  21.15800  1.000 137.23607 ? 48  LYS   A CA  1 
ATOM   84   C  C   . LYS   A 1 12  ? -26.87000 22.12200  20.98400  1.000 127.24504 ? 48  LYS   A C   1 
ATOM   85   O  O   . LYS   A 1 12  ? -26.51900 21.66900  19.89100  1.000 131.78825 ? 48  LYS   A O   1 
ATOM   86   C  CB  . LYS   A 1 12  ? -28.77900 23.71400  21.20600  1.000 137.80847 ? 48  LYS   A CB  1 
ATOM   87   C  CG  . LYS   A 1 12  ? -29.49500 22.95100  20.10100  1.000 132.97366 ? 48  LYS   A CG  1 
ATOM   88   C  CD  . LYS   A 1 12  ? -31.00200 22.96700  20.29500  1.000 124.59771 ? 48  LYS   A CD  1 
ATOM   89   C  CE  . LYS   A 1 12  ? -31.69700 22.13000  19.23400  1.000 122.24482 ? 48  LYS   A CE  1 
ATOM   90   N  NZ  . LYS   A 1 12  ? -33.17700 22.14800  19.38400  1.000 122.19803 ? 48  LYS   A NZ  1 
ATOM   91   N  N   . LYS   A 1 13  ? -26.95200 21.37900  22.08400  1.000 120.72109 ? 49  LYS   A N   1 
ATOM   92   C  CA  . LYS   A 1 13  ? -26.63700 19.95900  22.07000  1.000 118.67842 ? 49  LYS   A CA  1 
ATOM   93   C  C   . LYS   A 1 13  ? -27.85300 19.15300  21.63100  1.000 125.98686 ? 49  LYS   A C   1 
ATOM   94   O  O   . LYS   A 1 13  ? -28.94800 19.31700  22.17700  1.000 117.24539 ? 49  LYS   A O   1 
ATOM   95   C  CB  . LYS   A 1 13  ? -26.17500 19.50100  23.45400  1.000 110.65374 ? 49  LYS   A CB  1 
ATOM   96   C  CG  . LYS   A 1 13  ? -25.99500 18.00200  23.57900  1.000 106.82006 ? 49  LYS   A CG  1 
ATOM   97   C  CD  . LYS   A 1 13  ? -27.19600 17.30700  24.21300  1.000 113.27426 ? 49  LYS   A CD  1 
ATOM   98   C  CE  . LYS   A 1 13  ? -26.89700 15.83000  24.42300  1.000 127.44718 ? 49  LYS   A CE  1 
ATOM   99   N  NZ  . LYS   A 1 13  ? -28.11100 15.03500  24.77300  1.000 125.04695 ? 49  LYS   A NZ  1 
ATOM   100  N  N   . ILE   A 1 14  ? -27.65800 18.27900  20.64900  1.000 126.88982 ? 50  ILE   A N   1 
ATOM   101  C  CA  . ILE   A 1 14  ? -28.59100 17.19500  20.36900  1.000 126.38917 ? 50  ILE   A CA  1 
ATOM   102  C  C   . ILE   A 1 14  ? -27.85500 15.89300  20.64100  1.000 136.98018 ? 50  ILE   A C   1 
ATOM   103  O  O   . ILE   A 1 14  ? -26.65400 15.78300  20.37700  1.000 136.07805 ? 50  ILE   A O   1 
ATOM   104  C  CB  . ILE   A 1 14  ? -29.14800 17.24000  18.92700  1.000 121.87371 ? 50  ILE   A CB  1 
ATOM   105  C  CG1 . ILE   A 1 14  ? -28.09600 16.81100  17.89600  1.000 124.31955 ? 50  ILE   A CG1 1 
ATOM   106  C  CG2 . ILE   A 1 14  ? -29.68300 18.63000  18.59900  1.000 122.19725 ? 50  ILE   A CG2 1 
ATOM   107  C  CD1 . ILE   A 1 14  ? -28.36500 15.44400  17.28900  1.000 125.82488 ? 50  ILE   A CD1 1 
ATOM   108  N  N   . GLY   A 1 15  ? -28.55800 14.92000  21.20100  1.000 150.43999 ? 51  GLY   A N   1 
ATOM   109  C  CA  . GLY   A 1 15  ? -27.88100 13.70900  21.61600  1.000 166.75052 ? 51  GLY   A CA  1 
ATOM   110  C  C   . GLY   A 1 15  ? -28.17000 12.51300  20.73500  1.000 190.93804 ? 51  GLY   A C   1 
ATOM   111  O  O   . GLY   A 1 15  ? -27.80500 12.48800  19.55400  1.000 175.42197 ? 51  GLY   A O   1 
ATOM   112  N  N   . GLU   A 1 16  ? -28.81400 11.50500  21.32200  1.000 242.43849 ? 52  GLU   A N   1 
ATOM   113  C  CA  . GLU   A 1 16  ? -29.32100 10.30800  20.65500  1.000 243.71776 ? 52  GLU   A CA  1 
ATOM   114  C  C   . GLU   A 1 16  ? -28.22600 9.41400   20.08700  1.000 248.00564 ? 52  GLU   A C   1 
ATOM   115  O  O   . GLU   A 1 16  ? -28.53300 8.47200   19.34900  1.000 247.63194 ? 52  GLU   A O   1 
ATOM   116  C  CB  . GLU   A 1 16  ? -30.31800 10.66000  19.54500  1.000 234.47531 ? 52  GLU   A CB  1 
ATOM   117  C  CG  . GLU   A 1 16  ? -31.34300 11.71200  19.94600  1.000 234.03835 ? 52  GLU   A CG  1 
ATOM   118  C  CD  . GLU   A 1 16  ? -32.01100 11.40700  21.27400  1.000 245.79352 ? 52  GLU   A CD  1 
ATOM   119  O  OE1 . GLU   A 1 16  ? -32.40200 10.24200  21.49500  1.000 258.09344 ? 52  GLU   A OE1 1 
ATOM   120  O  OE2 . GLU   A 1 16  ? -32.14200 12.33500  22.10000  1.000 243.73319 ? 52  GLU   A OE2 1 
ATOM   121  N  N   . GLY   A 1 17  ? -26.96200 9.66500   20.41400  1.000 209.04679 ? 53  GLY   A N   1 
ATOM   122  C  CA  . GLY   A 1 17  ? -25.89900 8.75800   20.02800  1.000 210.62914 ? 53  GLY   A CA  1 
ATOM   123  C  C   . GLY   A 1 17  ? -25.09000 8.33100   21.23300  1.000 225.95116 ? 53  GLY   A C   1 
ATOM   124  O  O   . GLY   A 1 17  ? -23.92600 8.71800   21.36700  1.000 222.14485 ? 53  GLY   A O   1 
ATOM   125  N  N   . SER   A 1 18  ? -25.69600 7.52500   22.10400  1.000 239.09669 ? 54  SER   A N   1 
ATOM   126  C  CA  . SER   A 1 18  ? -25.18100 7.26600   23.45700  1.000 245.03339 ? 54  SER   A CA  1 
ATOM   127  C  C   . SER   A 1 18  ? -25.10000 8.63600   24.12700  1.000 252.59175 ? 54  SER   A C   1 
ATOM   128  O  O   . SER   A 1 18  ? -26.06400 9.41300   24.02700  1.000 249.08306 ? 54  SER   A O   1 
ATOM   129  C  CB  . SER   A 1 18  ? -23.87600 6.47600   23.39700  1.000 243.72087 ? 54  SER   A CB  1 
ATOM   130  O  OG  . SER   A 1 18  ? -24.02800 5.28800   22.64000  1.000 238.82377 ? 54  SER   A OG  1 
ATOM   131  N  N   . PHE   A 1 19  ? -24.00600 8.98000   24.80400  1.000 279.68226 ? 55  PHE   A N   1 
ATOM   132  C  CA  . PHE   A 1 19  ? -23.73900 10.36300  25.17500  1.000 279.23429 ? 55  PHE   A CA  1 
ATOM   133  C  C   . PHE   A 1 19  ? -22.63100 10.95200  24.30900  1.000 280.51840 ? 55  PHE   A C   1 
ATOM   134  O  O   . PHE   A 1 19  ? -21.87700 11.82400  24.75000  1.000 294.28987 ? 55  PHE   A O   1 
ATOM   135  C  CB  . PHE   A 1 19  ? -23.39700 10.48900  26.66000  1.000 285.52872 ? 55  PHE   A CB  1 
ATOM   136  C  CG  . PHE   A 1 19  ? -23.41200 11.91000  27.16300  1.000 284.31341 ? 55  PHE   A CG  1 
ATOM   137  C  CD1 . PHE   A 1 19  ? -24.46900 12.75300  26.85700  1.000 273.72181 ? 55  PHE   A CD1 1 
ATOM   138  C  CD2 . PHE   A 1 19  ? -22.36800 12.40400  27.92800  1.000 286.47403 ? 55  PHE   A CD2 1 
ATOM   139  C  CE1 . PHE   A 1 19  ? -24.48700 14.06000  27.30800  1.000 270.73377 ? 55  PHE   A CE1 1 
ATOM   140  C  CE2 . PHE   A 1 19  ? -22.38100 13.71100  28.38400  1.000 283.00775 ? 55  PHE   A CE2 1 
ATOM   141  C  CZ  . PHE   A 1 19  ? -23.44200 14.53900  28.07300  1.000 280.37488 ? 55  PHE   A CZ  1 
ATOM   142  N  N   . GLY   A 1 20  ? -22.51300 10.46300  23.07600  1.000 250.16055 ? 56  GLY   A N   1 
ATOM   143  C  CA  . GLY   A 1 20  ? -21.62500 11.05800  22.10100  1.000 231.70768 ? 56  GLY   A CA  1 
ATOM   144  C  C   . GLY   A 1 20  ? -21.93600 12.52900  21.94500  1.000 228.59031 ? 56  GLY   A C   1 
ATOM   145  O  O   . GLY   A 1 20  ? -23.09900 12.90800  21.77800  1.000 212.77717 ? 56  GLY   A O   1 
ATOM   146  N  N   . VAL   A 1 21  ? -20.90600 13.36700  22.02100  1.000 283.95239 ? 57  VAL   A N   1 
ATOM   147  C  CA  . VAL   A 1 21  ? -21.08200 14.81300  22.06900  1.000 280.09266 ? 57  VAL   A CA  1 
ATOM   148  C  C   . VAL   A 1 21  ? -21.49900 15.32700  20.69800  1.000 269.86602 ? 57  VAL   A C   1 
ATOM   149  O  O   . VAL   A 1 21  ? -20.66100 15.76000  19.90000  1.000 264.35831 ? 57  VAL   A O   1 
ATOM   150  C  CB  . VAL   A 1 21  ? -19.79600 15.49900  22.56400  1.000 274.18405 ? 57  VAL   A CB  1 
ATOM   151  C  CG1 . VAL   A 1 21  ? -20.03800 16.96900  22.82700  1.000 270.42711 ? 57  VAL   A CG1 1 
ATOM   152  C  CG2 . VAL   A 1 21  ? -19.27600 14.80700  23.81500  1.000 279.70499 ? 57  VAL   A CG2 1 
ATOM   153  N  N   . ILE   A 1 22  ? -22.79700 15.27800  20.41600  1.000 187.22717 ? 58  ILE   A N   1 
ATOM   154  C  CA  . ILE   A 1 22  ? -23.35600 15.77700  19.16800  1.000 154.30290 ? 58  ILE   A CA  1 
ATOM   155  C  C   . ILE   A 1 22  ? -23.96400 17.14500  19.43600  1.000 140.69720 ? 58  ILE   A C   1 
ATOM   156  O  O   . ILE   A 1 22  ? -24.43900 17.43500  20.54100  1.000 139.83953 ? 58  ILE   A O   1 
ATOM   157  C  CB  . ILE   A 1 22  ? -24.40000 14.80200  18.58000  1.000 139.32495 ? 58  ILE   A CB  1 
ATOM   158  C  CG1 . ILE   A 1 22  ? -23.92300 13.35400  18.70500  1.000 146.21989 ? 58  ILE   A CG1 1 
ATOM   159  C  CG2 . ILE   A 1 22  ? -24.70100 15.13600  17.12500  1.000 127.12460 ? 58  ILE   A CG2 1 
ATOM   160  C  CD1 . ILE   A 1 22  ? -22.71200 13.03500  17.87000  1.000 136.62346 ? 58  ILE   A CD1 1 
ATOM   161  N  N   . PHE   A 1 23  ? -23.93900 18.00200  18.41900  1.000 131.58015 ? 59  PHE   A N   1 
ATOM   162  C  CA  . PHE   A 1 23  ? -24.46500 19.35300  18.52900  1.000 127.50397 ? 59  PHE   A CA  1 
ATOM   163  C  C   . PHE   A 1 23  ? -25.14800 19.73900  17.22700  1.000 118.29366 ? 59  PHE   A C   1 
ATOM   164  O  O   . PHE   A 1 23  ? -24.91000 19.14400  16.17300  1.000 108.69417 ? 59  PHE   A O   1 
ATOM   165  C  CB  . PHE   A 1 23  ? -23.36000 20.37500  18.84200  1.000 133.31242 ? 59  PHE   A CB  1 
ATOM   166  C  CG  . PHE   A 1 23  ? -23.03800 20.50800  20.30400  1.000 136.94208 ? 59  PHE   A CG  1 
ATOM   167  C  CD1 . PHE   A 1 23  ? -22.13900 19.65000  20.91200  1.000 138.89049 ? 59  PHE   A CD1 1 
ATOM   168  C  CD2 . PHE   A 1 23  ? -23.61800 21.50900  21.06400  1.000 137.89696 ? 59  PHE   A CD2 1 
ATOM   169  C  CE1 . PHE   A 1 23  ? -21.83900 19.78200  22.25400  1.000 145.52533 ? 59  PHE   A CE1 1 
ATOM   170  C  CE2 . PHE   A 1 23  ? -23.32100 21.64300  22.40600  1.000 142.08435 ? 59  PHE   A CE2 1 
ATOM   171  C  CZ  . PHE   A 1 23  ? -22.43000 20.77800  23.00100  1.000 142.55917 ? 59  PHE   A CZ  1 
ATOM   172  N  N   . GLU   A 1 24  ? -26.01300 20.74300  17.31900  1.000 118.45049 ? 60  GLU   A N   1 
ATOM   173  C  CA  . GLU   A 1 24  ? -26.44600 21.47400  16.14100  1.000 115.97379 ? 60  GLU   A CA  1 
ATOM   174  C  C   . GLU   A 1 24  ? -25.41100 22.54200  15.81600  1.000 102.61816 ? 60  GLU   A C   1 
ATOM   175  O  O   . GLU   A 1 24  ? -24.86800 23.19200  16.71300  1.000 114.26458 ? 60  GLU   A O   1 
ATOM   176  C  CB  . GLU   A 1 24  ? -27.82000 22.10900  16.36600  1.000 114.48487 ? 60  GLU   A CB  1 
ATOM   177  C  CG  . GLU   A 1 24  ? -28.07600 23.34700  15.51500  1.000 116.64739 ? 60  GLU   A CG  1 
ATOM   178  C  CD  . GLU   A 1 24  ? -29.54300 23.55200  15.19200  1.000 123.11465 ? 60  GLU   A CD  1 
ATOM   179  O  OE1 . GLU   A 1 24  ? -30.39700 22.94700  15.87200  1.000 118.23713 ? 60  GLU   A OE1 1 
ATOM   180  O  OE2 . GLU   A 1 24  ? -29.83900 24.31400  14.24700  1.000 131.46894 ? 60  GLU   A OE2 1 
ATOM   181  N  N   . GLY   A 1 25  ? -25.11500 22.70300  14.52500  1.000 88.11244  ? 61  GLY   A N   1 
ATOM   182  C  CA  . GLY   A 1 25  ? -24.14100 23.67500  14.08900  1.000 91.21544  ? 61  GLY   A CA  1 
ATOM   183  C  C   . GLY   A 1 25  ? -24.73000 24.61600  13.05700  1.000 77.47341  ? 61  GLY   A C   1 
ATOM   184  O  O   . GLY   A 1 25  ? -25.86700 24.45500  12.60800  1.000 84.54748  ? 61  GLY   A O   1 
ATOM   185  N  N   . THR   A 1 26  ? -23.93100 25.61800  12.69500  1.000 61.39166  ? 62  THR   A N   1 
ATOM   186  C  CA  . THR   A 1 26  ? -24.28900 26.56700  11.64800  1.000 73.16875  ? 62  THR   A CA  1 
ATOM   187  C  C   . THR   A 1 26  ? -23.01900 26.96800  10.91700  1.000 74.66233  ? 62  THR   A C   1 
ATOM   188  O  O   . THR   A 1 26  ? -22.08600 27.49100  11.53300  1.000 78.85200  ? 62  THR   A O   1 
ATOM   189  C  CB  . THR   A 1 26  ? -24.98800 27.80700  12.21600  1.000 77.12448  ? 62  THR   A CB  1 
ATOM   190  O  OG1 . THR   A 1 26  ? -26.11000 27.40600  13.01200  1.000 78.15934  ? 62  THR   A OG1 1 
ATOM   191  C  CG2 . THR   A 1 26  ? -25.47900 28.70500  11.08400  1.000 82.31121  ? 62  THR   A CG2 1 
ATOM   192  N  N   . ASN   A 1 27  ? -22.98000 26.71100  9.61100   1.000 61.83218  ? 63  ASN   A N   1 
ATOM   193  C  CA  . ASN   A 1 27  ? -21.86400 27.15100  8.78700   1.000 78.35640  ? 63  ASN   A CA  1 
ATOM   194  C  C   . ASN   A 1 27  ? -21.83800 28.67400  8.77000   1.000 78.76813  ? 63  ASN   A C   1 
ATOM   195  O  O   . ASN   A 1 27  ? -22.78000 29.31100  8.29000   1.000 69.68390  ? 63  ASN   A O   1 
ATOM   196  C  CB  . ASN   A 1 27  ? -21.98700 26.57500  7.37400   1.000 74.15287  ? 63  ASN   A CB  1 
ATOM   197  C  CG  . ASN   A 1 27  ? -20.71100 26.72100  6.56200   1.000 81.03207  ? 63  ASN   A CG  1 
ATOM   198  O  OD1 . ASN   A 1 27  ? -19.96500 27.68600  6.71600   1.000 79.71738  ? 63  ASN   A OD1 1 
ATOM   199  N  ND2 . ASN   A 1 27  ? -20.45600 25.75400  5.68800   1.000 81.12801  ? 63  ASN   A ND2 1 
ATOM   200  N  N   . ILE   A 1 28  ? -20.77500 29.27200  9.30800   1.000 70.56107  ? 64  ILE   A N   1 
ATOM   201  C  CA  . ILE   A 1 28  ? -20.71300 30.72200  9.46200   1.000 70.66580  ? 64  ILE   A CA  1 
ATOM   202  C  C   . ILE   A 1 28  ? -20.44100 31.39000  8.12100   1.000 72.11938  ? 64  ILE   A C   1 
ATOM   203  O  O   . ILE   A 1 28  ? -20.35300 32.62000  8.03500   1.000 92.47261  ? 64  ILE   A O   1 
ATOM   204  C  CB  . ILE   A 1 28  ? -19.65200 31.12400  10.50400  1.000 88.70221  ? 64  ILE   A CB  1 
ATOM   205  C  CG1 . ILE   A 1 28  ? -18.40600 30.24800  10.36700  1.000 89.10540  ? 64  ILE   A CG1 1 
ATOM   206  C  CG2 . ILE   A 1 28  ? -20.22900 31.04600  11.91200  1.000 94.09632  ? 64  ILE   A CG2 1 
ATOM   207  C  CD1 . ILE   A 1 28  ? -17.33500 30.53800  11.39700  1.000 100.55968 ? 64  ILE   A CD1 1 
ATOM   208  N  N   . ILE   A 1 29  ? -20.30700 30.58900  7.06800   1.000 73.50222  ? 65  ILE   A N   1 
ATOM   209  C  CA  . ILE   A 1 29  ? -20.10800 31.12000  5.72300   1.000 75.17947  ? 65  ILE   A CA  1 
ATOM   210  C  C   . ILE   A 1 29  ? -21.43700 31.36100  5.01900   1.000 81.59349  ? 65  ILE   A C   1 
ATOM   211  O  O   . ILE   A 1 29  ? -21.68100 32.45000  4.49300   1.000 72.44678  ? 65  ILE   A O   1 
ATOM   212  C  CB  . ILE   A 1 29  ? -19.20000 30.17200  4.90900   1.000 80.42364  ? 65  ILE   A CB  1 
ATOM   213  C  CG1 . ILE   A 1 29  ? -17.73200 30.34700  5.30700   1.000 81.42652  ? 65  ILE   A CG1 1 
ATOM   214  C  CG2 . ILE   A 1 29  ? -19.37300 30.41400  3.42100   1.000 74.11309  ? 65  ILE   A CG2 1 
ATOM   215  C  CD1 . ILE   A 1 29  ? -17.02500 31.47900  4.58300   1.000 77.84524  ? 65  ILE   A CD1 1 
ATOM   216  N  N   . ASN   A 1 30  ? -22.32400 30.36100  4.99700   1.000 77.07029  ? 66  ASN   A N   1 
ATOM   217  C  CA  . ASN   A 1 30  ? -23.59200 30.47800  4.28900   1.000 79.45725  ? 66  ASN   A CA  1 
ATOM   218  C  C   . ASN   A 1 30  ? -24.82400 30.40300  5.18200   1.000 74.20988  ? 66  ASN   A C   1 
ATOM   219  O  O   . ASN   A 1 30  ? -25.91300 30.77200  4.72800   1.000 75.83782  ? 66  ASN   A O   1 
ATOM   220  C  CB  . ASN   A 1 30  ? -23.70500 29.40200  3.19500   1.000 83.21102  ? 66  ASN   A CB  1 
ATOM   221  C  CG  . ASN   A 1 30  ? -23.56800 27.99200  3.73600   1.000 80.71947  ? 66  ASN   A CG  1 
ATOM   222  O  OD1 . ASN   A 1 30  ? -23.51100 27.77800  4.94400   1.000 75.21939  ? 66  ASN   A OD1 1 
ATOM   223  N  ND2 . ASN   A 1 30  ? -23.52200 27.01800  2.83500   1.000 85.87427  ? 66  ASN   A ND2 1 
ATOM   224  N  N   . GLY   A 1 31  ? -24.69500 29.94000  6.42200   1.000 82.67181  ? 67  GLY   A N   1 
ATOM   225  C  CA  . GLY   A 1 31  ? -25.81500 29.87600  7.33600   1.000 63.55204  ? 67  GLY   A CA  1 
ATOM   226  C  C   . GLY   A 1 31  ? -26.53900 28.54900  7.39400   1.000 76.81671  ? 67  GLY   A C   1 
ATOM   227  O  O   . GLY   A 1 31  ? -27.50500 28.42600  8.16100   1.000 71.29800  ? 67  GLY   A O   1 
ATOM   228  N  N   . VAL   A 1 32  ? -26.11600 27.55800  6.61700   1.000 76.18523  ? 68  VAL   A N   1 
ATOM   229  C  CA  . VAL   A 1 32  ? -26.81100 26.26500  6.62500   1.000 79.12267  ? 68  VAL   A CA  1 
ATOM   230  C  C   . VAL   A 1 32  ? -26.50400 25.53900  7.92800   1.000 61.41543  ? 68  VAL   A C   1 
ATOM   231  O  O   . VAL   A 1 32  ? -25.37300 25.64000  8.44000   1.000 72.51867  ? 68  VAL   A O   1 
ATOM   232  C  CB  . VAL   A 1 32  ? -26.40400 25.42300  5.41000   1.000 77.44029  ? 68  VAL   A CB  1 
ATOM   233  C  CG1 . VAL   A 1 32  ? -26.67400 26.18400  4.12000   1.000 90.78183  ? 68  VAL   A CG1 1 
ATOM   234  C  CG2 . VAL   A 1 32  ? -24.94000 25.00200  5.49300   1.000 83.65842  ? 68  VAL   A CG2 1 
ATOM   235  N  N   . PRO   A 1 33  ? -27.46600 24.83500  8.51500   1.000 72.51363  ? 69  PRO   A N   1 
ATOM   236  C  CA  . PRO   A 1 33  ? -27.21000 24.08900  9.74900   1.000 64.16804  ? 69  PRO   A CA  1 
ATOM   237  C  C   . PRO   A 1 33  ? -26.61800 22.71400  9.48600   1.000 64.71830  ? 69  PRO   A C   1 
ATOM   238  O  O   . PRO   A 1 33  ? -26.86300 22.07700  8.46000   1.000 76.35555  ? 69  PRO   A O   1 
ATOM   239  C  CB  . PRO   A 1 33  ? -28.60900 23.97500  10.36700  1.000 71.74725  ? 69  PRO   A CB  1 
ATOM   240  C  CG  . PRO   A 1 33  ? -29.51100 23.91300  9.18100   1.000 65.11969  ? 69  PRO   A CG  1 
ATOM   241  C  CD  . PRO   A 1 33  ? -28.88800 24.80100  8.13100   1.000 62.33147  ? 69  PRO   A CD  1 
ATOM   242  N  N   . VAL   A 1 34  ? -25.81600 22.25800  10.44700  1.000 62.01362  ? 70  VAL   A N   1 
ATOM   243  C  CA  . VAL   A 1 34  ? -25.11200 20.99000  10.35800  1.000 75.82787  ? 70  VAL   A CA  1 
ATOM   244  C  C   . VAL   A 1 34  ? -25.32000 20.21600  11.65600  1.000 74.71490  ? 70  VAL   A C   1 
ATOM   245  O  O   . VAL   A 1 34  ? -25.93700 20.70200  12.60300  1.000 74.87103  ? 70  VAL   A O   1 
ATOM   246  C  CB  . VAL   A 1 34  ? -23.60700 21.17700  10.06600  1.000 62.46284  ? 70  VAL   A CB  1 
ATOM   247  C  CG1 . VAL   A 1 34  ? -23.40400 21.91300  8.74800   1.000 76.86551  ? 70  VAL   A CG1 1 
ATOM   248  C  CG2 . VAL   A 1 34  ? -22.93300 21.92200  11.20600  1.000 62.41511  ? 70  VAL   A CG2 1 
ATOM   249  N  N   . ALA   A 1 35  ? -24.79900 18.99200  11.68400  1.000 69.80231  ? 71  ALA   A N   1 
ATOM   250  C  CA  . ALA   A 1 35  ? -24.81700 18.13500  12.86800  1.000 66.74061  ? 71  ALA   A CA  1 
ATOM   251  C  C   . ALA   A 1 35  ? -23.37100 17.78100  13.19900  1.000 93.13589  ? 71  ALA   A C   1 
ATOM   252  O  O   . ALA   A 1 35  ? -22.76100 16.94000  12.53100  1.000 88.70665  ? 71  ALA   A O   1 
ATOM   253  C  CB  . ALA   A 1 35  ? -25.66300 16.88600  12.63900  1.000 72.81323  ? 71  ALA   A CB  1 
ATOM   254  N  N   . ILE   A 1 36  ? -22.82500 18.42800  14.22300  1.000 108.46189 ? 72  ILE   A N   1 
ATOM   255  C  CA  . ILE   A 1 36  ? -21.43100 18.24800  14.61000  1.000 94.75544  ? 72  ILE   A CA  1 
ATOM   256  C  C   . ILE   A 1 36  ? -21.32800 17.04600  15.53800  1.000 101.04732 ? 72  ILE   A C   1 
ATOM   257  O  O   . ILE   A 1 36  ? -22.13400 16.89400  16.46200  1.000 113.16836 ? 72  ILE   A O   1 
ATOM   258  C  CB  . ILE   A 1 36  ? -20.88700 19.51600  15.28900  1.000 103.55898 ? 72  ILE   A CB  1 
ATOM   259  C  CG1 . ILE   A 1 36  ? -21.23900 20.75400  14.46300  1.000 100.34710 ? 72  ILE   A CG1 1 
ATOM   260  C  CG2 . ILE   A 1 36  ? -19.38300 19.41200  15.48800  1.000 102.39610 ? 72  ILE   A CG2 1 
ATOM   261  C  CD1 . ILE   A 1 36  ? -21.02000 22.06100  15.19800  1.000 87.71049  ? 72  ILE   A CD1 1 
ATOM   262  N  N   . LYS   A 1 37  ? -20.33300 16.19400  15.30100  1.000 111.93758 ? 73  LYS   A N   1 
ATOM   263  C  CA  . LYS   A 1 37  ? -20.11600 14.99200  16.09700  1.000 115.81084 ? 73  LYS   A CA  1 
ATOM   264  C  C   . LYS   A 1 37  ? -18.72200 15.03300  16.70400  1.000 127.44493 ? 73  LYS   A C   1 
ATOM   265  O  O   . LYS   A 1 37  ? -17.72600 15.12500  15.97800  1.000 122.84197 ? 73  LYS   A O   1 
ATOM   266  C  CB  . LYS   A 1 37  ? -20.29300 13.72700  15.25400  1.000 93.99115  ? 73  LYS   A CB  1 
ATOM   267  C  CG  . LYS   A 1 37  ? -19.71500 12.47500  15.90000  1.000 90.34903  ? 73  LYS   A CG  1 
ATOM   268  C  CD  . LYS   A 1 37  ? -20.10400 11.21800  15.14100  1.000 95.37985  ? 73  LYS   A CD  1 
ATOM   269  C  CE  . LYS   A 1 37  ? -21.03100 10.33900  15.96600  1.000 94.06819  ? 73  LYS   A CE  1 
ATOM   270  N  NZ  . LYS   A 1 37  ? -21.33700 9.05100   15.28300  1.000 94.32209  ? 73  LYS   A NZ  1 
ATOM   271  N  N   . PHE   A 1 38  ? -18.65500 14.96400  18.02800  1.000 143.77926 ? 74  PHE   A N   1 
ATOM   272  C  CA  . PHE   A 1 38  ? -17.40000 14.87300  18.75600  1.000 147.17230 ? 74  PHE   A CA  1 
ATOM   273  C  C   . PHE   A 1 38  ? -17.12100 13.42400  19.14200  1.000 153.03707 ? 74  PHE   A C   1 
ATOM   274  O  O   . PHE   A 1 38  ? -18.01700 12.57500  19.16100  1.000 154.40841 ? 74  PHE   A O   1 
ATOM   275  C  CB  . PHE   A 1 38  ? -17.43000 15.74600  20.01400  1.000 154.03679 ? 74  PHE   A CB  1 
ATOM   276  C  CG  . PHE   A 1 38  ? -17.36700 17.22200  19.74000  1.000 138.41012 ? 74  PHE   A CG  1 
ATOM   277  C  CD1 . PHE   A 1 38  ? -18.48600 17.91200  19.30100  1.000 129.92292 ? 74  PHE   A CD1 1 
ATOM   278  C  CD2 . PHE   A 1 38  ? -16.19000 17.92400  19.94200  1.000 134.11407 ? 74  PHE   A CD2 1 
ATOM   279  C  CE1 . PHE   A 1 38  ? -18.42600 19.27000  19.05400  1.000 119.84980 ? 74  PHE   A CE1 1 
ATOM   280  C  CE2 . PHE   A 1 38  ? -16.12600 19.28200  19.69700  1.000 125.09385 ? 74  PHE   A CE2 1 
ATOM   281  C  CZ  . PHE   A 1 38  ? -17.24400 19.95300  19.25200  1.000 107.60742 ? 74  PHE   A CZ  1 
ATOM   282  N  N   . GLU   A 1 39  ? -15.85400 13.15100  19.46100  1.000 179.56997 ? 75  GLU   A N   1 
ATOM   283  C  CA  . GLU   A 1 39  ? -15.44300 11.83100  19.89700  1.000 186.45856 ? 75  GLU   A CA  1 
ATOM   284  C  C   . GLU   A 1 39  ? -14.21500 12.00600  20.77600  1.000 183.71691 ? 75  GLU   A C   1 
ATOM   285  O  O   . GLU   A 1 39  ? -13.23200 12.61400  20.32200  1.000 178.51573 ? 75  GLU   A O   1 
ATOM   286  C  CB  . GLU   A 1 39  ? -15.11400 10.89500  18.73400  1.000 184.81022 ? 75  GLU   A CB  1 
ATOM   287  C  CG  . GLU   A 1 39  ? -14.89400 9.45600   19.16300  1.000 184.93325 ? 75  GLU   A CG  1 
ATOM   288  C  CD  . GLU   A 1 39  ? -14.09800 8.65100   18.15200  1.000 180.45293 ? 75  GLU   A CD  1 
ATOM   289  O  OE1 . GLU   A 1 39  ? -13.17500 9.21400   17.52700  1.000 175.09000 ? 75  GLU   A OE1 1 
ATOM   290  O  OE2 . GLU   A 1 39  ? -14.39500 7.45000   17.98400  1.000 182.87867 ? 75  GLU   A OE2 1 
ATOM   291  N  N   . PRO   A 1 40  ? -14.23400 11.49400  22.00800  1.000 172.02676 ? 76  PRO   A N   1 
ATOM   292  C  CA  . PRO   A 1 40  ? -13.08000 11.66500  22.89700  1.000 166.06349 ? 76  PRO   A CA  1 
ATOM   293  C  C   . PRO   A 1 40  ? -11.84400 10.97800  22.33800  1.000 155.65331 ? 76  PRO   A C   1 
ATOM   294  O  O   . PRO   A 1 40  ? -11.90300 9.84800   21.85000  1.000 154.25771 ? 76  PRO   A O   1 
ATOM   295  C  CB  . PRO   A 1 40  ? -13.54100 11.01900  24.20900  1.000 168.14045 ? 76  PRO   A CB  1 
ATOM   296  C  CG  . PRO   A 1 40  ? -15.03500 11.00500  24.13500  1.000 176.00236 ? 76  PRO   A CG  1 
ATOM   297  C  CD  . PRO   A 1 40  ? -15.35500 10.82000  22.67900  1.000 173.89053 ? 76  PRO   A CD  1 
ATOM   298  N  N   . ARG   A 1 41  ? -10.71900 11.68400  22.40300  1.000 147.89306 ? 77  ARG   A N   1 
ATOM   299  C  CA  . ARG   A 1 41  ? -9.45700  11.16100  21.90400  1.000 141.57044 ? 77  ARG   A CA  1 
ATOM   300  C  C   . ARG   A 1 41  ? -8.88600  10.12200  22.86100  1.000 144.91032 ? 77  ARG   A C   1 
ATOM   301  O  O   . ARG   A 1 41  ? -9.13000  10.15900  24.07100  1.000 146.49838 ? 77  ARG   A O   1 
ATOM   302  C  CB  . ARG   A 1 41  ? -8.45100  12.29400  21.70800  1.000 135.71742 ? 77  ARG   A CB  1 
ATOM   303  C  CG  . ARG   A 1 41  ? -7.29300  11.93400  20.79800  1.000 132.43194 ? 77  ARG   A CG  1 
ATOM   304  C  CD  . ARG   A 1 41  ? -7.81700  11.42600  19.46900  1.000 127.31667 ? 77  ARG   A CD  1 
ATOM   305  N  NE  . ARG   A 1 41  ? -6.84100  11.57700  18.39900  1.000 132.05654 ? 77  ARG   A NE  1 
ATOM   306  C  CZ  . ARG   A 1 41  ? -6.56400  12.72600  17.79900  1.000 150.30901 ? 77  ARG   A CZ  1 
ATOM   307  N  NH1 . ARG   A 1 41  ? -7.13900  13.85800  18.17100  1.000 148.18444 ? 77  ARG   A NH1 1 
ATOM   308  N  NH2 . ARG   A 1 41  ? -5.68500  12.74200  16.80400  1.000 168.52606 ? 77  ARG   A NH2 1 
ATOM   309  N  N   . LYS   A 1 42  ? -8.10700  9.19300   22.30100  1.000 135.49935 ? 78  LYS   A N   1 
ATOM   310  C  CA  . LYS   A 1 42  ? -7.47100  8.11700   23.06400  1.000 147.96044 ? 78  LYS   A CA  1 
ATOM   311  C  C   . LYS   A 1 42  ? -8.50700  7.31600   23.85200  1.000 160.73777 ? 78  LYS   A C   1 
ATOM   312  O  O   . LYS   A 1 42  ? -8.34300  7.03500   25.04100  1.000 167.11577 ? 78  LYS   A O   1 
ATOM   313  C  CB  . LYS   A 1 42  ? -6.37600  8.66400   23.98400  1.000 143.08088 ? 78  LYS   A CB  1 
ATOM   314  C  CG  . LYS   A 1 42  ? -4.95900  8.40100   23.48700  1.000 137.25701 ? 78  LYS   A CG  1 
ATOM   315  C  CD  . LYS   A 1 42  ? -4.77700  8.86100   22.04600  1.000 135.77642 ? 78  LYS   A CD  1 
ATOM   316  C  CE  . LYS   A 1 42  ? -3.39200  8.51000   21.52500  1.000 130.74766 ? 78  LYS   A CE  1 
ATOM   317  N  NZ  . LYS   A 1 42  ? -3.22500  8.87800   20.09200  1.000 127.10344 ? 78  LYS   A NZ  1 
ATOM   318  N  N   . THR   A 1 43  ? -9.58700  6.95300   23.17100  1.000 162.74919 ? 79  THR   A N   1 
ATOM   319  C  CA  . THR   A 1 43  ? -10.65900 6.16500   23.75600  1.000 174.77896 ? 79  THR   A CA  1 
ATOM   320  C  C   . THR   A 1 43  ? -10.49100 4.69400   23.38700  1.000 184.81382 ? 79  THR   A C   1 
ATOM   321  O  O   . THR   A 1 43  ? -9.65200  4.32200   22.56300  1.000 179.74587 ? 79  THR   A O   1 
ATOM   322  C  CB  . THR   A 1 43  ? -12.02600 6.68700   23.29600  1.000 173.77586 ? 79  THR   A CB  1 
ATOM   323  O  OG1 . THR   A 1 43  ? -13.06700 6.05000   24.04800  1.000 176.03655 ? 79  THR   A OG1 1 
ATOM   324  C  CG2 . THR   A 1 43  ? -12.23300 6.40800   21.81500  1.000 180.43670 ? 79  THR   A CG2 1 
ATOM   325  N  N   . GLU   A 1 44  ? -11.31000 3.85000   24.01600  1.000 189.36830 ? 80  GLU   A N   1 
ATOM   326  C  CA  . GLU   A 1 44  ? -11.21100 2.41200   23.80800  1.000 187.47765 ? 80  GLU   A CA  1 
ATOM   327  C  C   . GLU   A 1 44  ? -11.84300 1.95700   22.49900  1.000 197.11675 ? 80  GLU   A C   1 
ATOM   328  O  O   . GLU   A 1 44  ? -11.56500 0.84000   22.04900  1.000 194.03529 ? 80  GLU   A O   1 
ATOM   329  C  CB  . GLU   A 1 44  ? -11.85900 1.66900   24.98000  1.000 179.66864 ? 80  GLU   A CB  1 
ATOM   330  C  CG  . GLU   A 1 44  ? -11.28500 0.28300   25.25200  1.000 175.30433 ? 80  GLU   A CG  1 
ATOM   331  C  CD  . GLU   A 1 44  ? -9.98100  0.32400   26.03400  1.000 175.31197 ? 80  GLU   A CD  1 
ATOM   332  O  OE1 . GLU   A 1 44  ? -9.05200  1.05300   25.62600  1.000 175.41282 ? 80  GLU   A OE1 1 
ATOM   333  O  OE2 . GLU   A 1 44  ? -9.88800  -0.37400  27.06600  1.000 173.43472 ? 80  GLU   A OE2 1 
ATOM   334  N  N   . ALA   A 1 45  ? -12.67800 2.78800   21.87500  1.000 230.69504 ? 81  ALA   A N   1 
ATOM   335  C  CA  . ALA   A 1 45  ? -13.37200 2.43600   20.63600  1.000 229.51418 ? 81  ALA   A CA  1 
ATOM   336  C  C   . ALA   A 1 45  ? -13.29500 3.60300   19.66100  1.000 226.85141 ? 81  ALA   A C   1 
ATOM   337  O  O   . ALA   A 1 45  ? -14.22900 4.41300   19.56500  1.000 225.20346 ? 81  ALA   A O   1 
ATOM   338  C  CB  . ALA   A 1 45  ? -14.82400 2.04200   20.91000  1.000 230.76718 ? 81  ALA   A CB  1 
ATOM   339  N  N   . PRO   A 1 46  ? -12.19200 3.72300   18.91900  1.000 192.53663 ? 82  PRO   A N   1 
ATOM   340  C  CA  . PRO   A 1 46  ? -12.08400 4.76700   17.88700  1.000 176.29600 ? 82  PRO   A CA  1 
ATOM   341  C  C   . PRO   A 1 46  ? -12.75300 4.31600   16.59600  1.000 161.24652 ? 82  PRO   A C   1 
ATOM   342  O  O   . PRO   A 1 46  ? -12.32500 3.34500   15.96600  1.000 153.51366 ? 82  PRO   A O   1 
ATOM   343  C  CB  . PRO   A 1 46  ? -10.56700 4.93500   17.70900  1.000 172.95133 ? 82  PRO   A CB  1 
ATOM   344  C  CG  . PRO   A 1 46  ? -9.92700  4.11500   18.81000  1.000 176.10870 ? 82  PRO   A CG  1 
ATOM   345  C  CD  . PRO   A 1 46  ? -10.90800 3.04000   19.13200  1.000 184.50371 ? 82  PRO   A CD  1 
ATOM   346  N  N   . GLN   A 1 47  ? -13.81000 5.02700   16.20000  1.000 154.37687 ? 83  GLN   A N   1 
ATOM   347  C  CA  . GLN   A 1 47  ? -14.52800 4.70700   14.97400  1.000 140.22289 ? 83  GLN   A CA  1 
ATOM   348  C  C   . GLN   A 1 47  ? -14.95100 5.93400   14.18200  1.000 114.75565 ? 83  GLN   A C   1 
ATOM   349  O  O   . GLN   A 1 47  ? -15.62000 5.78000   13.15500  1.000 105.13218 ? 83  GLN   A O   1 
ATOM   350  C  CB  . GLN   A 1 47  ? -15.76800 3.85200   15.28700  1.000 137.85797 ? 83  GLN   A CB  1 
ATOM   351  C  CG  . GLN   A 1 47  ? -15.45300 2.38600   15.53500  1.000 146.17896 ? 83  GLN   A CG  1 
ATOM   352  C  CD  . GLN   A 1 47  ? -16.48400 1.70400   16.41200  1.000 146.78522 ? 83  GLN   A CD  1 
ATOM   353  O  OE1 . GLN   A 1 47  ? -17.48900 2.30600   16.79200  1.000 150.92522 ? 83  GLN   A OE1 1 
ATOM   354  N  NE2 . GLN   A 1 47  ? -16.23500 0.44400   16.74600  1.000 142.91558 ? 83  GLN   A NE2 1 
ATOM   355  N  N   . LEU   A 1 48  ? -14.58100 7.14100   14.61300  1.000 121.36882 ? 84  LEU   A N   1 
ATOM   356  C  CA  . LEU   A 1 48  ? -14.99500 8.33900   13.89500  1.000 110.91624 ? 84  LEU   A CA  1 
ATOM   357  C  C   . LEU   A 1 48  ? -14.16600 8.55500   12.63500  1.000 110.08715 ? 84  LEU   A C   1 
ATOM   358  O  O   . LEU   A 1 48  ? -14.68700 9.04200   11.62500  1.000 102.08358 ? 84  LEU   A O   1 
ATOM   359  C  CB  . LEU   A 1 48  ? -14.90000 9.55900   14.80900  1.000 101.97022 ? 84  LEU   A CB  1 
ATOM   360  C  CG  . LEU   A 1 48  ? -15.44800 10.84600  14.19600  1.000 107.63359 ? 84  LEU   A CG  1 
ATOM   361  C  CD1 . LEU   A 1 48  ? -16.85600 10.61000  13.69200  1.000 84.61148  ? 84  LEU   A CD1 1 
ATOM   362  C  CD2 . LEU   A 1 48  ? -15.43000 11.96900  15.20600  1.000 100.56395 ? 84  LEU   A CD2 1 
ATOM   363  N  N   . ARG   A 1 49  ? -12.87800 8.20200   12.67300  1.000 111.79532 ? 85  ARG   A N   1 
ATOM   364  C  CA  . ARG   A 1 49  ? -12.03200 8.38300   11.49800  1.000 113.04968 ? 85  ARG   A CA  1 
ATOM   365  C  C   . ARG   A 1 49  ? -12.51000 7.53900   10.32400  1.000 109.75823 ? 85  ARG   A C   1 
ATOM   366  O  O   . ARG   A 1 49  ? -12.30700 7.91700   9.16500   1.000 105.61661 ? 85  ARG   A O   1 
ATOM   367  C  CB  . ARG   A 1 49  ? -10.58000 8.04900   11.83500  1.000 104.81072 ? 85  ARG   A CB  1 
ATOM   368  C  CG  . ARG   A 1 49  ? -10.39300 6.72200   12.55200  1.000 116.60535 ? 85  ARG   A CG  1 
ATOM   369  C  CD  . ARG   A 1 49  ? -8.92000  6.37300   12.66400  1.000 112.78881 ? 85  ARG   A CD  1 
ATOM   370  N  NE  . ARG   A 1 49  ? -8.64500  5.50700   13.80400  1.000 127.89152 ? 85  ARG   A NE  1 
ATOM   371  C  CZ  . ARG   A 1 49  ? -7.43200  5.12100   14.17300  1.000 129.43678 ? 85  ARG   A CZ  1 
ATOM   372  N  NH1 . ARG   A 1 49  ? -6.35400  5.48800   13.49900  1.000 114.55843 ? 85  ARG   A NH1 1 
ATOM   373  N  NH2 . ARG   A 1 49  ? -7.29500  4.34800   15.24700  1.000 143.11593 ? 85  ARG   A NH2 1 
ATOM   374  N  N   . ASP   A 1 50  ? -13.14700 6.40200   10.60000  1.000 109.52286 ? 86  ASP   A N   1 
ATOM   375  C  CA  . ASP   A 1 50  ? -13.64300 5.53800   9.53800   1.000 101.16506 ? 86  ASP   A CA  1 
ATOM   376  C  C   . ASP   A 1 50  ? -15.06700 5.87200   9.12000   1.000 98.78425  ? 86  ASP   A C   1 
ATOM   377  O  O   . ASP   A 1 50  ? -15.43200 5.63800   7.96200   1.000 98.87048  ? 86  ASP   A O   1 
ATOM   378  C  CB  . ASP   A 1 50  ? -13.55700 4.07200   9.97100   1.000 108.52022 ? 86  ASP   A CB  1 
ATOM   379  C  CG  . ASP   A 1 50  ? -12.12800 3.57000   10.03700  1.000 119.68450 ? 86  ASP   A CG  1 
ATOM   380  O  OD1 . ASP   A 1 50  ? -11.37300 4.03200   10.91800  1.000 121.94787 ? 86  ASP   A OD1 1 
ATOM   381  O  OD2 . ASP   A 1 50  ? -11.75600 2.71800   9.20300   1.000 117.55626 ? 86  ASP   A OD2 1 
ATOM   382  N  N   . GLU   A 1 51  ? -15.88100 6.41300   10.03100  1.000 104.76974 ? 87  GLU   A N   1 
ATOM   383  C  CA  . GLU   A 1 51  ? -17.22700 6.82600   9.64800   1.000 96.00509  ? 87  GLU   A CA  1 
ATOM   384  C  C   . GLU   A 1 51  ? -17.19100 7.96500   8.63900   1.000 88.67526  ? 87  GLU   A C   1 
ATOM   385  O  O   . GLU   A 1 51  ? -18.05600 8.03700   7.75900   1.000 83.57193  ? 87  GLU   A O   1 
ATOM   386  C  CB  . GLU   A 1 51  ? -18.03800 7.23100   10.88000  1.000 93.27924  ? 87  GLU   A CB  1 
ATOM   387  C  CG  . GLU   A 1 51  ? -19.49900 7.52300   10.57300  1.000 83.00625  ? 87  GLU   A CG  1 
ATOM   388  C  CD  . GLU   A 1 51  ? -20.32300 7.80700   11.81300  1.000 86.92676  ? 87  GLU   A CD  1 
ATOM   389  O  OE1 . GLU   A 1 51  ? -19.79700 8.43900   12.75400  1.000 96.00637  ? 87  GLU   A OE1 1 
ATOM   390  O  OE2 . GLU   A 1 51  ? -21.50100 7.39400   11.84700  1.000 82.27083  ? 87  GLU   A OE2 1 
ATOM   391  N  N   . TYR   A 1 52  ? -16.20400 8.85800   8.75400   1.000 85.53083  ? 88  TYR   A N   1 
ATOM   392  C  CA  . TYR   A 1 52  ? -16.01200 9.88900   7.73900   1.000 92.57274  ? 88  TYR   A CA  1 
ATOM   393  C  C   . TYR   A 1 52  ? -15.79800 9.26000   6.36800   1.000 92.45947  ? 88  TYR   A C   1 
ATOM   394  O  O   . TYR   A 1 52  ? -16.50100 9.58800   5.40500   1.000 79.91258  ? 88  TYR   A O   1 
ATOM   395  C  CB  . TYR   A 1 52  ? -14.83300 10.78800  8.12300   1.000 99.12761  ? 88  TYR   A CB  1 
ATOM   396  C  CG  . TYR   A 1 52  ? -14.32000 11.72000  7.03300   1.000 104.26226 ? 88  TYR   A CG  1 
ATOM   397  C  CD1 . TYR   A 1 52  ? -15.17900 12.34400  6.13700   1.000 90.78608  ? 88  TYR   A CD1 1 
ATOM   398  C  CD2 . TYR   A 1 52  ? -12.96500 12.00900  6.93900   1.000 100.29921 ? 88  TYR   A CD2 1 
ATOM   399  C  CE1 . TYR   A 1 52  ? -14.69100 13.20300  5.14900   1.000 95.43560  ? 88  TYR   A CE1 1 
ATOM   400  C  CE2 . TYR   A 1 52  ? -12.47500 12.85900  5.96800   1.000 103.91070 ? 88  TYR   A CE2 1 
ATOM   401  C  CZ  . TYR   A 1 52  ? -13.33200 13.45400  5.07500   1.000 111.13727 ? 88  TYR   A CZ  1 
ATOM   402  O  OH  . TYR   A 1 52  ? -12.82400 14.30300  4.11200   1.000 125.06555 ? 88  TYR   A OH  1 
ATOM   403  N  N   . ARG   A 1 53  ? -14.83100 8.34400   6.26300   1.000 96.26029  ? 89  ARG   A N   1 
ATOM   404  C  CA  . ARG   A 1 53  ? -14.50000 7.76700   4.96400   1.000 92.94346  ? 89  ARG   A CA  1 
ATOM   405  C  C   . ARG   A 1 53  ? -15.67900 7.01000   4.36300   1.000 84.35622  ? 89  ARG   A C   1 
ATOM   406  O  O   . ARG   A 1 53  ? -15.75300 6.84900   3.13900   1.000 97.82477  ? 89  ARG   A O   1 
ATOM   407  C  CB  . ARG   A 1 53  ? -13.28000 6.85300   5.08800   1.000 93.18314  ? 89  ARG   A CB  1 
ATOM   408  C  CG  . ARG   A 1 53  ? -12.68800 6.45900   3.74800   1.000 114.65419 ? 89  ARG   A CG  1 
ATOM   409  C  CD  . ARG   A 1 53  ? -11.31500 5.82400   3.88300   1.000 120.40982 ? 89  ARG   A CD  1 
ATOM   410  N  NE  . ARG   A 1 53  ? -10.73600 5.53400   2.57600   1.000 127.55652 ? 89  ARG   A NE  1 
ATOM   411  C  CZ  . ARG   A 1 53  ? -9.57800  4.91700   2.38700   1.000 120.00471 ? 89  ARG   A CZ  1 
ATOM   412  N  NH1 . ARG   A 1 53  ? -8.83800  4.51000   3.40400   1.000 119.85756 ? 89  ARG   A NH1 1 
ATOM   413  N  NH2 . ARG   A 1 53  ? -9.15300  4.70100   1.14500   1.000 120.97911 ? 89  ARG   A NH2 1 
ATOM   414  N  N   . THR   A 1 54  ? -16.61500 6.55000   5.19700   1.000 76.89567  ? 90  THR   A N   1 
ATOM   415  C  CA  . THR   A 1 54  ? -17.80600 5.89200   4.66800   1.000 89.05130  ? 90  THR   A CA  1 
ATOM   416  C  C   . THR   A 1 54  ? -18.75000 6.90000   4.02200   1.000 92.11570  ? 90  THR   A C   1 
ATOM   417  O  O   . THR   A 1 54  ? -19.39600 6.59500   3.01200   1.000 86.62635  ? 90  THR   A O   1 
ATOM   418  C  CB  . THR   A 1 54  ? -18.52500 5.12200   5.77600   1.000 93.65900  ? 90  THR   A CB  1 
ATOM   419  O  OG1 . THR   A 1 54  ? -17.56300 4.43600   6.58600   1.000 84.49951  ? 90  THR   A OG1 1 
ATOM   420  C  CG2 . THR   A 1 54  ? -19.48600 4.10300   5.17600   1.000 83.90304  ? 90  THR   A CG2 1 
ATOM   421  N  N   . TYR   A 1 55  ? -18.84500 8.10700   4.58700   1.000 79.96642  ? 91  TYR   A N   1 
ATOM   422  C  CA  . TYR   A 1 55  ? -19.71700 9.12500   4.00800   1.000 87.90733  ? 91  TYR   A CA  1 
ATOM   423  C  C   . TYR   A 1 55  ? -19.16500 9.66700   2.69400   1.000 91.02289  ? 91  TYR   A C   1 
ATOM   424  O  O   . TYR   A 1 55  ? -19.94200 10.01200  1.79600   1.000 90.00870  ? 91  TYR   A O   1 
ATOM   425  C  CB  . TYR   A 1 55  ? -19.93900 10.26700  5.00200   1.000 86.84678  ? 91  TYR   A CB  1 
ATOM   426  C  CG  . TYR   A 1 55  ? -20.94200 9.95300   6.09300   1.000 80.40162  ? 91  TYR   A CG  1 
ATOM   427  C  CD1 . TYR   A 1 55  ? -22.28500 9.75900   5.79400   1.000 82.29559  ? 91  TYR   A CD1 1 
ATOM   428  C  CD2 . TYR   A 1 55  ? -20.55000 9.86600   7.42200   1.000 79.11314  ? 91  TYR   A CD2 1 
ATOM   429  C  CE1 . TYR   A 1 55  ? -23.20600 9.47600   6.78600   1.000 73.38478  ? 91  TYR   A CE1 1 
ATOM   430  C  CE2 . TYR   A 1 55  ? -21.46400 9.58400   8.42100   1.000 85.05173  ? 91  TYR   A CE2 1 
ATOM   431  C  CZ  . TYR   A 1 55  ? -22.78900 9.39000   8.09800   1.000 76.70059  ? 91  TYR   A CZ  1 
ATOM   432  O  OH  . TYR   A 1 55  ? -23.70100 9.11000   9.09000   1.000 64.94380  ? 91  TYR   A OH  1 
ATOM   433  N  N   . LYS   A 1 56  ? -17.83800 9.76000   2.56300   1.000 97.96638  ? 92  LYS   A N   1 
ATOM   434  C  CA  . LYS   A 1 56  ? -17.25200 10.16400  1.28700   1.000 108.55485 ? 92  LYS   A CA  1 
ATOM   435  C  C   . LYS   A 1 56  ? -17.45600 9.09300   0.22500   1.000 110.76684 ? 92  LYS   A C   1 
ATOM   436  O  O   . LYS   A 1 56  ? -17.66700 9.40900   -0.95300  1.000 118.69845 ? 92  LYS   A O   1 
ATOM   437  C  CB  . LYS   A 1 56  ? -15.76200 10.46600  1.45500   1.000 124.56019 ? 92  LYS   A CB  1 
ATOM   438  C  CG  . LYS   A 1 56  ? -15.45100 11.80800  2.08800   1.000 117.49410 ? 92  LYS   A CG  1 
ATOM   439  C  CD  . LYS   A 1 56  ? -15.87300 12.96200  1.19100   1.000 111.19289 ? 92  LYS   A CD  1 
ATOM   440  C  CE  . LYS   A 1 56  ? -15.48200 14.29200  1.82100   1.000 114.30021 ? 92  LYS   A CE  1 
ATOM   441  N  NZ  . LYS   A 1 56  ? -15.82100 15.45900  0.95700   1.000 116.72203 ? 92  LYS   A NZ  1 
ATOM   442  N  N   . HIS   A 1 57  ? -17.38900 7.81900   0.61900   1.000 108.42386 ? 93  HIS   A N   1 
ATOM   443  C  CA  . HIS   A 1 57  ? -17.62700 6.73300   -0.32700  1.000 104.54801 ? 93  HIS   A CA  1 
ATOM   444  C  C   . HIS   A 1 57  ? -19.04600 6.80000   -0.88000  1.000 96.57468  ? 93  HIS   A C   1 
ATOM   445  O  O   . HIS   A 1 57  ? -19.26200 6.68300   -2.09200  1.000 103.93669 ? 93  HIS   A O   1 
ATOM   446  C  CB  . HIS   A 1 57  ? -17.36100 5.38600   0.35100   1.000 96.61003  ? 93  HIS   A CB  1 
ATOM   447  C  CG  . HIS   A 1 57  ? -17.35100 4.21800   -0.58800  1.000 108.06140 ? 93  HIS   A CG  1 
ATOM   448  N  ND1 . HIS   A 1 57  ? -17.45800 4.35600   -1.95500  1.000 110.10555 ? 93  HIS   A ND1 1 
ATOM   449  C  CD2 . HIS   A 1 57  ? -17.24300 2.88900   -0.35200  1.000 110.68410 ? 93  HIS   A CD2 1 
ATOM   450  C  CE1 . HIS   A 1 57  ? -17.41900 3.16200   -2.52000  1.000 115.26315 ? 93  HIS   A CE1 1 
ATOM   451  N  NE2 . HIS   A 1 57  ? -17.28900 2.25500   -1.56900  1.000 121.02021 ? 93  HIS   A NE2 1 
ATOM   452  N  N   . LEU   A 1 58  ? -20.02500 7.00600   -0.00400  1.000 93.06293  ? 94  LEU   A N   1 
ATOM   453  C  CA  . LEU   A 1 58  ? -21.42000 7.12700   -0.40200  1.000 92.43286  ? 94  LEU   A CA  1 
ATOM   454  C  C   . LEU   A 1 58  ? -21.81700 8.55900   -0.74000  1.000 89.31131  ? 94  LEU   A C   1 
ATOM   455  O  O   . LEU   A 1 58  ? -23.01400 8.84900   -0.83700  1.000 94.95842  ? 94  LEU   A O   1 
ATOM   456  C  CB  . LEU   A 1 58  ? -22.32600 6.58400   0.70500   1.000 88.68907  ? 94  LEU   A CB  1 
ATOM   457  C  CG  . LEU   A 1 58  ? -22.22900 5.07900   0.96300   1.000 84.06162  ? 94  LEU   A CG  1 
ATOM   458  C  CD1 . LEU   A 1 58  ? -22.60400 4.75900   2.40000   1.000 72.70789  ? 94  LEU   A CD1 1 
ATOM   459  C  CD2 . LEU   A 1 58  ? -23.12000 4.31400   -0.00500  1.000 84.77010  ? 94  LEU   A CD2 1 
ATOM   460  N  N   . GLN   A 1 59  ? -20.85000 9.45700   -0.92000  1.000 91.48561  ? 95  GLN   A N   1 
ATOM   461  C  CA  . GLN   A 1 59  ? -21.17100 10.83800  -1.25500  1.000 96.08392  ? 95  GLN   A CA  1 
ATOM   462  C  C   . GLN   A 1 59  ? -21.76400 10.91000  -2.65600  1.000 95.58263  ? 95  GLN   A C   1 
ATOM   463  O  O   . GLN   A 1 59  ? -21.23800 10.31000  -3.59900  1.000 86.95620  ? 95  GLN   A O   1 
ATOM   464  C  CB  . GLN   A 1 59  ? -19.92600 11.71900  -1.15000  1.000 86.22373  ? 95  GLN   A CB  1 
ATOM   465  C  CG  . GLN   A 1 59  ? -20.18500 13.19100  -1.43900  1.000 90.01771  ? 95  GLN   A CG  1 
ATOM   466  C  CD  . GLN   A 1 59  ? -19.18600 14.10600  -0.75700  1.000 91.99956  ? 95  GLN   A CD  1 
ATOM   467  O  OE1 . GLN   A 1 59  ? -19.41600 14.57100  0.36000   1.000 90.13062  ? 95  GLN   A OE1 1 
ATOM   468  N  NE2 . GLN   A 1 59  ? -18.07000 14.37200  -1.42600  1.000 82.94081  ? 95  GLN   A NE2 1 
ATOM   469  N  N   . GLY   A 1 60  ? -22.86800 11.64100  -2.78800  1.000 86.22937  ? 96  GLY   A N   1 
ATOM   470  C  CA  . GLY   A 1 60  ? -23.62400 11.69100  -4.01800  1.000 94.25688  ? 96  GLY   A CA  1 
ATOM   471  C  C   . GLY   A 1 60  ? -24.82700 10.77300  -4.05300  1.000 97.76476  ? 96  GLY   A C   1 
ATOM   472  O  O   . GLY   A 1 60  ? -25.66000 10.90600  -4.95800  1.000 93.53929  ? 96  GLY   A O   1 
ATOM   473  N  N   . CYS   A 1 61  ? -24.94100 9.84900   -3.10100  1.000 86.62987  ? 97  CYS   A N   1 
ATOM   474  C  CA  . CYS   A 1 61  ? -26.08000 8.94300   -3.05000  1.000 97.38129  ? 97  CYS   A CA  1 
ATOM   475  C  C   . CYS   A 1 61  ? -27.26400 9.62000   -2.37100  1.000 93.23720  ? 97  CYS   A C   1 
ATOM   476  O  O   . CYS   A 1 61  ? -27.09900 10.37800  -1.41000  1.000 84.12605  ? 97  CYS   A O   1 
ATOM   477  C  CB  . CYS   A 1 61  ? -25.71000 7.65800   -2.30500  1.000 98.73836  ? 97  CYS   A CB  1 
ATOM   478  S  SG  . CYS   A 1 61  ? -24.38600 6.70500   -3.08500  1.000 105.58116 ? 97  CYS   A SG  1 
ATOM   479  N  N   . ASP   A 1 62  ? -28.46500 9.34800   -2.87900  1.000 94.27370  ? 98  ASP   A N   1 
ATOM   480  C  CA  . ASP   A 1 62  ? -29.65900 9.93900   -2.29000  1.000 93.16541  ? 98  ASP   A CA  1 
ATOM   481  C  C   . ASP   A 1 62  ? -29.95100 9.32300   -0.92300  1.000 86.08350  ? 98  ASP   A C   1 
ATOM   482  O  O   . ASP   A 1 62  ? -29.85800 8.10500   -0.73400  1.000 87.86258  ? 98  ASP   A O   1 
ATOM   483  C  CB  . ASP   A 1 62  ? -30.86800 9.80800   -3.23000  1.000 99.77609  ? 98  ASP   A CB  1 
ATOM   484  C  CG  . ASP   A 1 62  ? -31.03900 8.41200   -3.82000  1.000 122.23713 ? 98  ASP   A CG  1 
ATOM   485  O  OD1 . ASP   A 1 62  ? -30.36100 7.46600   -3.38500  1.000 114.77302 ? 98  ASP   A OD1 1 
ATOM   486  O  OD2 . ASP   A 1 62  ? -31.87200 8.25700   -4.73400  1.000 120.83643 ? 98  ASP   A OD2 1 
ATOM   487  N  N   . GLY   A 1 63  ? -30.26800 10.18600  0.04100   1.000 73.17042  ? 99  GLY   A N   1 
ATOM   488  C  CA  . GLY   A 1 63  ? -30.58100 9.77800   1.39200   1.000 73.16974  ? 99  GLY   A CA  1 
ATOM   489  C  C   . GLY   A 1 63  ? -29.40000 9.70400   2.33700   1.000 69.52871  ? 99  GLY   A C   1 
ATOM   490  O  O   . GLY   A 1 63  ? -29.61000 9.56200   3.54700   1.000 62.86488  ? 99  GLY   A O   1 
ATOM   491  N  N   . ILE   A 1 64  ? -28.17500 9.77600   1.83100   1.000 70.55160  ? 100 ILE   A N   1 
ATOM   492  C  CA  . ILE   A 1 64  ? -26.97400 9.78000   2.66300   1.000 65.10260  ? 100 ILE   A CA  1 
ATOM   493  C  C   . ILE   A 1 64  ? -26.47900 11.22100  2.75100   1.000 74.91607  ? 100 ILE   A C   1 
ATOM   494  O  O   . ILE   A 1 64  ? -26.24000 11.84300  1.70500   1.000 63.72925  ? 100 ILE   A O   1 
ATOM   495  C  CB  . ILE   A 1 64  ? -25.88200 8.86100   2.09500   1.000 76.23648  ? 100 ILE   A CB  1 
ATOM   496  C  CG1 . ILE   A 1 64  ? -26.46100 7.49300   1.73200   1.000 69.56640  ? 100 ILE   A CG1 1 
ATOM   497  C  CG2 . ILE   A 1 64  ? -24.74800 8.70500   3.10000   1.000 68.84103  ? 100 ILE   A CG2 1 
ATOM   498  C  CD1 . ILE   A 1 64  ? -27.06200 6.75200   2.90500   1.000 73.02711  ? 100 ILE   A CD1 1 
ATOM   499  N  N   . PRO   A 1 65  ? -26.32500 11.78400  3.94600   1.000 63.82016  ? 101 PRO   A N   1 
ATOM   500  C  CA  . PRO   A 1 65  ? -25.86400 13.17100  4.04800   1.000 78.33598  ? 101 PRO   A CA  1 
ATOM   501  C  C   . PRO   A 1 65  ? -24.40300 13.30900  3.64900   1.000 83.01153  ? 101 PRO   A C   1 
ATOM   502  O  O   . PRO   A 1 65  ? -23.64600 12.33800  3.58400   1.000 73.73975  ? 101 PRO   A O   1 
ATOM   503  C  CB  . PRO   A 1 65  ? -26.06700 13.50400  5.53000   1.000 75.79358  ? 101 PRO   A CB  1 
ATOM   504  C  CG  . PRO   A 1 65  ? -25.97500 12.18800  6.21800   1.000 65.37694  ? 101 PRO   A CG  1 
ATOM   505  C  CD  . PRO   A 1 65  ? -26.57600 11.18500  5.26800   1.000 52.44830  ? 101 PRO   A CD  1 
ATOM   506  N  N   . ASN   A 1 66  ? -24.01400 14.55100  3.38200   1.000 81.08941  ? 102 ASN   A N   1 
ATOM   507  C  CA  . ASN   A 1 66  ? -22.64900 14.87400  3.00100   1.000 66.42808  ? 102 ASN   A CA  1 
ATOM   508  C  C   . ASN   A 1 66  ? -21.77900 15.06800  4.23600   1.000 77.93991  ? 102 ASN   A C   1 
ATOM   509  O  O   . ASN   A 1 66  ? -22.24500 15.51900  5.28500   1.000 68.41887  ? 102 ASN   A O   1 
ATOM   510  C  CB  . ASN   A 1 66  ? -22.60900 16.13900  2.14200   1.000 75.62313  ? 102 ASN   A CB  1 
ATOM   511  C  CG  . ASN   A 1 66  ? -23.29300 15.95700  0.80300   1.000 82.19352  ? 102 ASN   A CG  1 
ATOM   512  O  OD1 . ASN   A 1 66  ? -23.30600 14.86200  0.24300   1.000 80.98207  ? 102 ASN   A OD1 1 
ATOM   513  N  ND2 . ASN   A 1 66  ? -23.86600 17.03600  0.28100   1.000 75.83962  ? 102 ASN   A ND2 1 
ATOM   514  N  N   . ALA   A 1 67  ? -20.50300 14.71600  4.10000   1.000 90.82513  ? 103 ALA   A N   1 
ATOM   515  C  CA  . ALA   A 1 67  ? -19.50100 14.96700  5.12700   1.000 85.01651  ? 103 ALA   A CA  1 
ATOM   516  C  C   . ALA   A 1 67  ? -18.66800 16.17200  4.71200   1.000 92.88072  ? 103 ALA   A C   1 
ATOM   517  O  O   . ALA   A 1 67  ? -18.20500 16.24800  3.56900   1.000 100.30494 ? 103 ALA   A O   1 
ATOM   518  C  CB  . ALA   A 1 67  ? -18.60700 13.74400  5.33600   1.000 92.25038  ? 103 ALA   A CB  1 
ATOM   519  N  N   . TYR   A 1 68  ? -18.48000 17.11100  5.63800   1.000 83.70300  ? 104 TYR   A N   1 
ATOM   520  C  CA  . TYR   A 1 68  ? -17.86900 18.39200  5.30900   1.000 85.02831  ? 104 TYR   A CA  1 
ATOM   521  C  C   . TYR   A 1 68  ? -16.51800 18.63400  5.96500   1.000 89.76138  ? 104 TYR   A C   1 
ATOM   522  O  O   . TYR   A 1 68  ? -15.72100 19.40100  5.42200   1.000 99.76753  ? 104 TYR   A O   1 
ATOM   523  C  CB  . TYR   A 1 68  ? -18.81100 19.54100  5.68900   1.000 81.06134  ? 104 TYR   A CB  1 
ATOM   524  C  CG  . TYR   A 1 68  ? -20.11400 19.55300  4.91900   1.000 87.98098  ? 104 TYR   A CG  1 
ATOM   525  C  CD1 . TYR   A 1 68  ? -20.13600 19.82700  3.55800   1.000 87.48871  ? 104 TYR   A CD1 1 
ATOM   526  C  CD2 . TYR   A 1 68  ? -21.32300 19.30400  5.55700   1.000 82.94206  ? 104 TYR   A CD2 1 
ATOM   527  C  CE1 . TYR   A 1 68  ? -21.32500 19.84300  2.85000   1.000 84.26458  ? 104 TYR   A CE1 1 
ATOM   528  C  CE2 . TYR   A 1 68  ? -22.51700 19.31800  4.85800   1.000 81.47878  ? 104 TYR   A CE2 1 
ATOM   529  C  CZ  . TYR   A 1 68  ? -22.51200 19.58800  3.50600   1.000 83.24775  ? 104 TYR   A CZ  1 
ATOM   530  O  OH  . TYR   A 1 68  ? -23.69700 19.60400  2.80600   1.000 80.06651  ? 104 TYR   A OH  1 
ATOM   531  N  N   . TYR   A 1 69  ? -16.23400 18.01300  7.10900   1.000 80.98967  ? 105 TYR   A N   1 
ATOM   532  C  CA  . TYR   A 1 69  ? -14.98100 18.28800  7.79900   1.000 103.85602 ? 105 TYR   A CA  1 
ATOM   533  C  C   . TYR   A 1 69  ? -14.63700 17.14200  8.73900   1.000 103.60357 ? 105 TYR   A C   1 
ATOM   534  O  O   . TYR   A 1 69  ? -15.52200 16.48300  9.29200   1.000 100.19506 ? 105 TYR   A O   1 
ATOM   535  C  CB  . TYR   A 1 69  ? -15.05200 19.60700  8.58200   1.000 97.26004  ? 105 TYR   A CB  1 
ATOM   536  C  CG  . TYR   A 1 69  ? -14.02200 19.71700  9.68500   1.000 101.70890 ? 105 TYR   A CG  1 
ATOM   537  C  CD1 . TYR   A 1 69  ? -12.70400 20.05200  9.40200   1.000 108.17312 ? 105 TYR   A CD1 1 
ATOM   538  C  CD2 . TYR   A 1 69  ? -14.36600 19.47700  11.01000  1.000 98.69915  ? 105 TYR   A CD2 1 
ATOM   539  C  CE1 . TYR   A 1 69  ? -11.75900 20.14800  10.40800  1.000 112.26064 ? 105 TYR   A CE1 1 
ATOM   540  C  CE2 . TYR   A 1 69  ? -13.42700 19.56800  12.01900  1.000 107.15531 ? 105 TYR   A CE2 1 
ATOM   541  C  CZ  . TYR   A 1 69  ? -12.12800 19.90500  11.71400  1.000 114.50309 ? 105 TYR   A CZ  1 
ATOM   542  O  OH  . TYR   A 1 69  ? -11.19400 20.00000  12.72100  1.000 132.07910 ? 105 TYR   A OH  1 
ATOM   543  N  N   . PHE   A 1 70  ? -13.33300 16.91800  8.90600   1.000 101.87178 ? 106 PHE   A N   1 
ATOM   544  C  CA  . PHE   A 1 70  ? -12.81500 16.03700  9.94500   1.000 107.21043 ? 106 PHE   A CA  1 
ATOM   545  C  C   . PHE   A 1 70  ? -11.37700 16.43800  10.23600  1.000 110.43655 ? 106 PHE   A C   1 
ATOM   546  O  O   . PHE   A 1 70  ? -10.56700 16.55800  9.31300   1.000 119.79335 ? 106 PHE   A O   1 
ATOM   547  C  CB  . PHE   A 1 70  ? -12.89300 14.56300  9.53200   1.000 110.20756 ? 106 PHE   A CB  1 
ATOM   548  C  CG  . PHE   A 1 70  ? -12.20700 13.62600  10.49100  1.000 115.29878 ? 106 PHE   A CG  1 
ATOM   549  C  CD1 . PHE   A 1 70  ? -12.37500 13.76700  11.85900  1.000 117.11052 ? 106 PHE   A CD1 1 
ATOM   550  C  CD2 . PHE   A 1 70  ? -11.40800 12.59700  10.02300  1.000 113.87349 ? 106 PHE   A CD2 1 
ATOM   551  C  CE1 . PHE   A 1 70  ? -11.74700 12.91100  12.74300  1.000 122.30186 ? 106 PHE   A CE1 1 
ATOM   552  C  CE2 . PHE   A 1 70  ? -10.78000 11.73300  10.90300  1.000 106.28221 ? 106 PHE   A CE2 1 
ATOM   553  C  CZ  . PHE   A 1 70  ? -10.95100 11.89100  12.26400  1.000 105.87805 ? 106 PHE   A CZ  1 
ATOM   554  N  N   . GLY   A 1 71  ? -11.07100 16.65000  11.51200  1.000 126.70416 ? 107 GLY   A N   1 
ATOM   555  C  CA  . GLY   A 1 71  ? -9.72400  17.02000  11.90700  1.000 150.17354 ? 107 GLY   A CA  1 
ATOM   556  C  C   . GLY   A 1 71  ? -9.57700  16.96700  13.41100  1.000 174.29345 ? 107 GLY   A C   1 
ATOM   557  O  O   . GLY   A 1 71  ? -10.54100 16.73600  14.14700  1.000 156.48111 ? 107 GLY   A O   1 
ATOM   558  N  N   . GLN   A 1 72  ? -8.34200  17.18100  13.85800  1.000 247.62835 ? 108 GLN   A N   1 
ATOM   559  C  CA  . GLN   A 1 72  ? -8.04900  17.21900  15.28200  1.000 246.72921 ? 108 GLN   A CA  1 
ATOM   560  C  C   . GLN   A 1 72  ? -8.34500  18.60300  15.84100  1.000 244.89178 ? 108 GLN   A C   1 
ATOM   561  O  O   . GLN   A 1 72  ? -8.11700  19.61900  15.17800  1.000 244.50810 ? 108 GLN   A O   1 
ATOM   562  C  CB  . GLN   A 1 72  ? -6.58600  16.85700  15.54400  1.000 244.71880 ? 108 GLN   A CB  1 
ATOM   563  C  CG  . GLN   A 1 72  ? -6.11500  15.57300  14.87800  1.000 251.06979 ? 108 GLN   A CG  1 
ATOM   564  C  CD  . GLN   A 1 72  ? -4.67200  15.24300  15.21500  1.000 271.54724 ? 108 GLN   A CD  1 
ATOM   565  O  OE1 . GLN   A 1 72  ? -4.18400  15.58200  16.29300  1.000 268.61522 ? 108 GLN   A OE1 1 
ATOM   566  N  NE2 . GLN   A 1 72  ? -3.98100  14.58200  14.29100  1.000 276.01347 ? 108 GLN   A NE2 1 
ATOM   567  N  N   . GLU   A 1 73  ? -8.85800  18.64000  17.07100  1.000 195.54452 ? 109 GLU   A N   1 
ATOM   568  C  CA  . GLU   A 1 73  ? -9.15400  19.90900  17.73300  1.000 187.61612 ? 109 GLU   A CA  1 
ATOM   569  C  C   . GLU   A 1 73  ? -9.08300  19.65500  19.23600  1.000 186.34821 ? 109 GLU   A C   1 
ATOM   570  O  O   . GLU   A 1 73  ? -10.03300 19.13100  19.82700  1.000 178.34294 ? 109 GLU   A O   1 
ATOM   571  C  CB  . GLU   A 1 73  ? -10.51400 20.45100  17.31200  1.000 176.75546 ? 109 GLU   A CB  1 
ATOM   572  C  CG  . GLU   A 1 73  ? -10.73100 21.91500  17.65200  1.000 169.24835 ? 109 GLU   A CG  1 
ATOM   573  C  CD  . GLU   A 1 73  ? -11.53600 22.64100  16.59100  1.000 146.98558 ? 109 GLU   A CD  1 
ATOM   574  O  OE1 . GLU   A 1 73  ? -11.91100 22.00400  15.58300  1.000 134.88600 ? 109 GLU   A OE1 1 
ATOM   575  O  OE2 . GLU   A 1 73  ? -11.78800 23.85100  16.76300  1.000 145.05852 ? 109 GLU   A OE2 1 
ATOM   576  N  N   . GLY   A 1 74  ? -7.95500  20.02600  19.83900  1.000 213.72593 ? 110 GLY   A N   1 
ATOM   577  C  CA  . GLY   A 1 74  ? -7.69900  19.72900  21.23300  1.000 219.34941 ? 110 GLY   A CA  1 
ATOM   578  C  C   . GLY   A 1 74  ? -7.54600  18.24300  21.48100  1.000 218.43934 ? 110 GLY   A C   1 
ATOM   579  O  O   . GLY   A 1 74  ? -6.62000  17.60900  20.96700  1.000 225.59264 ? 110 GLY   A O   1 
ATOM   580  N  N   . LEU   A 1 75  ? -8.44800  17.67600  22.27600  1.000 171.93305 ? 111 LEU   A N   1 
ATOM   581  C  CA  . LEU   A 1 75  ? -8.46200  16.25200  22.59500  1.000 159.83082 ? 111 LEU   A CA  1 
ATOM   582  C  C   . LEU   A 1 75  ? -9.75100  15.61300  22.08800  1.000 159.05105 ? 111 LEU   A C   1 
ATOM   583  O  O   . LEU   A 1 75  ? -10.38600 14.80900  22.77500  1.000 156.19635 ? 111 LEU   A O   1 
ATOM   584  C  CB  . LEU   A 1 75  ? -8.29300  16.02400  24.09800  1.000 158.54767 ? 111 LEU   A CB  1 
ATOM   585  C  CG  . LEU   A 1 75  ? -6.99000  16.53800  24.71600  1.000 164.64429 ? 111 LEU   A CG  1 
ATOM   586  C  CD1 . LEU   A 1 75  ? -6.99400  16.35000  26.22600  1.000 152.82616 ? 111 LEU   A CD1 1 
ATOM   587  C  CD2 . LEU   A 1 75  ? -5.78600  15.84600  24.09200  1.000 145.19932 ? 111 LEU   A CD2 1 
ATOM   588  N  N   . HIS   A 1 76  ? -10.17100 15.98900  20.88100  1.000 160.19521 ? 112 HIS   A N   1 
ATOM   589  C  CA  . HIS   A 1 76  ? -11.42600 15.51500  20.31500  1.000 148.46661 ? 112 HIS   A CA  1 
ATOM   590  C  C   . HIS   A 1 76  ? -11.27900 15.32100  18.81200  1.000 143.97558 ? 112 HIS   A C   1 
ATOM   591  O  O   . HIS   A 1 76  ? -10.45700 15.97200  18.16300  1.000 152.65115 ? 112 HIS   A O   1 
ATOM   592  C  CB  . HIS   A 1 76  ? -12.58400 16.49100  20.58900  1.000 137.57260 ? 112 HIS   A CB  1 
ATOM   593  C  CG  . HIS   A 1 76  ? -13.41000 16.13600  21.78600  1.000 136.55135 ? 112 HIS   A CG  1 
ATOM   594  N  ND1 . HIS   A 1 76  ? -14.01400 14.90600  21.93700  1.000 144.69822 ? 112 HIS   A ND1 1 
ATOM   595  C  CD2 . HIS   A 1 76  ? -13.74300 16.85400  22.88500  1.000 129.74830 ? 112 HIS   A CD2 1 
ATOM   596  C  CE1 . HIS   A 1 76  ? -14.67400 14.87800  23.08100  1.000 148.66060 ? 112 HIS   A CE1 1 
ATOM   597  N  NE2 . HIS   A 1 76  ? -14.52600 16.04700  23.67600  1.000 142.36957 ? 112 HIS   A NE2 1 
ATOM   598  N  N   . ASN   A 1 77  ? -12.12800 14.41900  18.30200  1.000 141.59285 ? 113 ASN   A N   1 
ATOM   599  C  CA  . ASN   A 1 77  ? -12.23200 14.20900  16.83900  1.000 137.51387 ? 113 ASN   A CA  1 
ATOM   600  C  C   . ASN   A 1 77  ? -13.60200 14.78100  16.47600  1.000 133.55413 ? 113 ASN   A C   1 
ATOM   601  O  O   . ASN   A 1 77  ? -14.55100 14.54800  17.25100  1.000 133.93373 ? 113 ASN   A O   1 
ATOM   602  C  CB  . ASN   A 1 77  ? -12.06100 12.73900  16.45400  1.000 135.81427 ? 113 ASN   A CB  1 
ATOM   603  C  CG  . ASN   A 1 77  ? -10.62100 12.28300  16.53200  1.000 137.75453 ? 113 ASN   A CG  1 
ATOM   604  O  OD1 . ASN   A 1 77  ? -9.83100  12.83500  17.29500  1.000 137.56689 ? 113 ASN   A OD1 1 
ATOM   605  N  ND2 . ASN   A 1 77  ? -10.26800 11.28000  15.74500  1.000 137.03510 ? 113 ASN   A ND2 1 
ATOM   606  N  N   . ILE   A 1 78  ? -13.71200 15.49600  15.36200  1.000 125.39246 ? 114 ILE   A N   1 
ATOM   607  C  CA  . ILE   A 1 78  ? -14.93400 16.20300  14.99700  1.000 112.91013 ? 114 ILE   A CA  1 
ATOM   608  C  C   . ILE   A 1 78  ? -15.32300 15.83600  13.57200  1.000 103.83709 ? 114 ILE   A C   1 
ATOM   609  O  O   . ILE   A 1 78  ? -14.48000 15.86200  12.66800  1.000 99.05881  ? 114 ILE   A O   1 
ATOM   610  C  CB  . ILE   A 1 78  ? -14.76600 17.72500  15.14900  1.000 114.29152 ? 114 ILE   A CB  1 
ATOM   611  C  CG1 . ILE   A 1 78  ? -14.90300 18.10900  16.62100  1.000 121.80231 ? 114 ILE   A CG1 1 
ATOM   612  C  CG2 . ILE   A 1 78  ? -15.76800 18.46500  14.28300  1.000 108.30887 ? 114 ILE   A CG2 1 
ATOM   613  C  CD1 . ILE   A 1 78  ? -13.61000 17.98300  17.39700  1.000 117.38581 ? 114 ILE   A CD1 1 
ATOM   614  N  N   . LEU   A 1 79  ? -16.59700 15.48700  13.37800  1.000 106.28169 ? 115 LEU   A N   1 
ATOM   615  C  CA  . LEU   A 1 79  ? -17.15300 15.16900  12.06500  1.000 96.80037  ? 115 LEU   A CA  1 
ATOM   616  C  C   . LEU   A 1 79  ? -18.39500 16.01600  11.82900  1.000 90.49711  ? 115 LEU   A C   1 
ATOM   617  O  O   . LEU   A 1 79  ? -19.36700 15.92100  12.58500  1.000 91.97867  ? 115 LEU   A O   1 
ATOM   618  C  CB  . LEU   A 1 79  ? -17.50200 13.68100  11.95100  1.000 77.74077  ? 115 LEU   A CB  1 
ATOM   619  C  CG  . LEU   A 1 79  ? -18.33800 13.27600  10.73400  1.000 79.88242  ? 115 LEU   A CG  1 
ATOM   620  C  CD1 . LEU   A 1 79  ? -17.55100 13.47500  9.44800   1.000 75.40035  ? 115 LEU   A CD1 1 
ATOM   621  C  CD2 . LEU   A 1 79  ? -18.81600 11.83600  10.86400  1.000 77.22996  ? 115 LEU   A CD2 1 
ATOM   622  N  N   . VAL   A 1 80  ? -18.37000 16.82800  10.77600  1.000 90.90874  ? 116 VAL   A N   1 
ATOM   623  C  CA  . VAL   A 1 80  ? -19.48700 17.69600  10.42500  1.000 79.71668  ? 116 VAL   A CA  1 
ATOM   624  C  C   . VAL   A 1 80  ? -20.22100 17.07000  9.24800   1.000 84.79401  ? 116 VAL   A C   1 
ATOM   625  O  O   . VAL   A 1 80  ? -19.61600 16.78200  8.21000   1.000 78.93922  ? 116 VAL   A O   1 
ATOM   626  C  CB  . VAL   A 1 80  ? -19.01200 19.11900  10.08900  1.000 73.31281  ? 116 VAL   A CB  1 
ATOM   627  C  CG1 . VAL   A 1 80  ? -20.18200 19.97100  9.62300   1.000 77.10098  ? 116 VAL   A CG1 1 
ATOM   628  C  CG2 . VAL   A 1 80  ? -18.33400 19.75300  11.29500  1.000 73.19140  ? 116 VAL   A CG2 1 
ATOM   629  N  N   . ILE   A 1 81  ? -21.52100 16.83700  9.41500   1.000 78.24285  ? 117 ILE   A N   1 
ATOM   630  C  CA  . ILE   A 1 81  ? -22.38300 16.34800  8.35300   1.000 67.09136  ? 117 ILE   A CA  1 
ATOM   631  C  C   . ILE   A 1 81  ? -23.65700 17.18400  8.34000   1.000 71.11966  ? 117 ILE   A C   1 
ATOM   632  O  O   . ILE   A 1 81  ? -23.81100 18.13100  9.10900   1.000 65.07182  ? 117 ILE   A O   1 
ATOM   633  C  CB  . ILE   A 1 81  ? -22.71400 14.84800  8.50000   1.000 56.50443  ? 117 ILE   A CB  1 
ATOM   634  C  CG1 . ILE   A 1 81  ? -23.43700 14.58700  9.82200   1.000 71.24427  ? 117 ILE   A CG1 1 
ATOM   635  C  CG2 . ILE   A 1 81  ? -21.45600 13.99800  8.37400   1.000 78.16692  ? 117 ILE   A CG2 1 
ATOM   636  C  CD1 . ILE   A 1 81  ? -24.38600 13.40900  9.76800   1.000 72.79598  ? 117 ILE   A CD1 1 
ATOM   637  N  N   . ASP   A 1 82  ? -24.57600 16.81500  7.45200   1.000 61.56624  ? 118 ASP   A N   1 
ATOM   638  C  CA  . ASP   A 1 82  ? -25.83600 17.53000  7.32400   1.000 74.36030  ? 118 ASP   A CA  1 
ATOM   639  C  C   . ASP   A 1 82  ? -26.71700 17.31000  8.54800   1.000 67.38502  ? 118 ASP   A C   1 
ATOM   640  O  O   . ASP   A 1 82  ? -26.65800 16.27100  9.21000   1.000 67.54347  ? 118 ASP   A O   1 
ATOM   641  C  CB  . ASP   A 1 82  ? -26.57600 17.07800  6.06500   1.000 52.30698  ? 118 ASP   A CB  1 
ATOM   642  C  CG  . ASP   A 1 82  ? -26.00800 17.69200  4.80300   1.000 74.64827  ? 118 ASP   A CG  1 
ATOM   643  O  OD1 . ASP   A 1 82  ? -25.84500 18.93000  4.76500   1.000 80.83020  ? 118 ASP   A OD1 1 
ATOM   644  O  OD2 . ASP   A 1 82  ? -25.72300 16.93900  3.84900   1.000 77.69046  ? 118 ASP   A OD2 1 
ATOM   645  N  N   . LEU   A 1 83  ? -27.54200 18.30900  8.84400   1.000 68.71931  ? 119 LEU   A N   1 
ATOM   646  C  CA  . LEU   A 1 83  ? -28.51800 18.22000  9.92100   1.000 68.42634  ? 119 LEU   A CA  1 
ATOM   647  C  C   . LEU   A 1 83  ? -29.85700 17.77300  9.35000   1.000 65.91290  ? 119 LEU   A C   1 
ATOM   648  O  O   . LEU   A 1 83  ? -30.34700 18.35000  8.37400   1.000 67.30234  ? 119 LEU   A O   1 
ATOM   649  C  CB  . LEU   A 1 83  ? -28.66300 19.56700  10.63000  1.000 64.68221  ? 119 LEU   A CB  1 
ATOM   650  C  CG  . LEU   A 1 83  ? -29.74000 19.67700  11.71000  1.000 67.95744  ? 119 LEU   A CG  1 
ATOM   651  C  CD1 . LEU   A 1 83  ? -29.37200 18.86300  12.94300  1.000 58.87614  ? 119 LEU   A CD1 1 
ATOM   652  C  CD2 . LEU   A 1 83  ? -29.96700 21.13300  12.07200  1.000 83.04324  ? 119 LEU   A CD2 1 
ATOM   653  N  N   . LEU   A 1 84  ? -30.44400 16.75000  9.95900   1.000 68.95351  ? 120 LEU   A N   1 
ATOM   654  C  CA  . LEU   A 1 84  ? -31.68300 16.15000  9.48800   1.000 51.63276  ? 120 LEU   A CA  1 
ATOM   655  C  C   . LEU   A 1 84  ? -32.75300 16.23800  10.57300  1.000 67.74178  ? 120 LEU   A C   1 
ATOM   656  O  O   . LEU   A 1 84  ? -32.50500 16.69800  11.69100  1.000 62.47694  ? 120 LEU   A O   1 
ATOM   657  C  CB  . LEU   A 1 84  ? -31.45000 14.69900  9.05900   1.000 61.92754  ? 120 LEU   A CB  1 
ATOM   658  C  CG  . LEU   A 1 84  ? -30.52500 14.52000  7.85400   1.000 69.12418  ? 120 LEU   A CG  1 
ATOM   659  C  CD1 . LEU   A 1 84  ? -30.10500 13.07000  7.71400   1.000 50.94771  ? 120 LEU   A CD1 1 
ATOM   660  C  CD2 . LEU   A 1 84  ? -31.20400 15.00600  6.58200   1.000 62.57523  ? 120 LEU   A CD2 1 
ATOM   661  N  N   . GLY   A 1 85  ? -33.95400 15.78200  10.22600  1.000 58.42180  ? 121 GLY   A N   1 
ATOM   662  C  CA  . GLY   A 1 85  ? -35.09800 15.88400  11.10000  1.000 64.11890  ? 121 GLY   A CA  1 
ATOM   663  C  C   . GLY   A 1 85  ? -35.24300 14.70300  12.03800  1.000 58.48403  ? 121 GLY   A C   1 
ATOM   664  O  O   . GLY   A 1 85  ? -34.29400 13.95200  12.28400  1.000 56.37528  ? 121 GLY   A O   1 
ATOM   665  N  N   . PRO   A 1 86  ? -36.44400 14.52000  12.58100  1.000 59.11263  ? 122 PRO   A N   1 
ATOM   666  C  CA  . PRO   A 1 86  ? -36.65700 13.45800  13.57000  1.000 58.77366  ? 122 PRO   A CA  1 
ATOM   667  C  C   . PRO   A 1 86  ? -36.50200 12.07200  12.96200  1.000 59.52228  ? 122 PRO   A C   1 
ATOM   668  O  O   . PRO   A 1 86  ? -36.54600 11.87900  11.74500  1.000 44.82878  ? 122 PRO   A O   1 
ATOM   669  C  CB  . PRO   A 1 86  ? -38.09700 13.69100  14.04400  1.000 65.28327  ? 122 PRO   A CB  1 
ATOM   670  C  CG  . PRO   A 1 86  ? -38.41800 15.10000  13.64500  1.000 73.64032  ? 122 PRO   A CG  1 
ATOM   671  C  CD  . PRO   A 1 86  ? -37.64900 15.34200  12.38600  1.000 61.49881  ? 122 PRO   A CD  1 
ATOM   672  N  N   . SER   A 1 87  ? -36.31900 11.09700  13.84700  1.000 38.01173  ? 123 SER   A N   1 
ATOM   673  C  CA  . SER   A 1 87  ? -36.18200 9.70800   13.44400  1.000 57.25620  ? 123 SER   A CA  1 
ATOM   674  C  C   . SER   A 1 87  ? -37.55400 9.07300   13.23900  1.000 63.86561  ? 123 SER   A C   1 
ATOM   675  O  O   . SER   A 1 87  ? -38.58300 9.59900   13.67000  1.000 55.73143  ? 123 SER   A O   1 
ATOM   676  C  CB  . SER   A 1 87  ? -35.39700 8.91700   14.49200  1.000 34.77952  ? 123 SER   A CB  1 
ATOM   677  O  OG  . SER   A 1 87  ? -36.11500 8.83000   15.71000  1.000 66.29520  ? 123 SER   A OG  1 
ATOM   678  N  N   . LEU   A 1 88  ? -37.55600 7.92200   12.56200  1.000 55.17108  ? 124 LEU   A N   1 
ATOM   679  C  CA  . LEU   A 1 88  ? -38.79400 7.16500   12.41100  1.000 49.60353  ? 124 LEU   A CA  1 
ATOM   680  C  C   . LEU   A 1 88  ? -39.29500 6.65900   13.75500  1.000 59.06717  ? 124 LEU   A C   1 
ATOM   681  O  O   . LEU   A 1 88  ? -40.49800 6.44100   13.92600  1.000 56.91893  ? 124 LEU   A O   1 
ATOM   682  C  CB  . LEU   A 1 88  ? -38.59000 6.00000   11.44400  1.000 32.18832  ? 124 LEU   A CB  1 
ATOM   683  C  CG  . LEU   A 1 88  ? -38.29200 6.38000   9.99300   1.000 32.06376  ? 124 LEU   A CG  1 
ATOM   684  C  CD1 . LEU   A 1 88  ? -38.21200 5.13700   9.12400   1.000 52.74528  ? 124 LEU   A CD1 1 
ATOM   685  C  CD2 . LEU   A 1 88  ? -39.34300 7.34500   9.46400   1.000 32.49421  ? 124 LEU   A CD2 1 
ATOM   686  N  N   . GLU   A 1 89  ? -38.38800 6.46500   14.71600  1.000 53.45725  ? 125 GLU   A N   1 
ATOM   687  C  CA  . GLU   A 1 89  ? -38.80600 6.13800   16.07400  1.000 57.98821  ? 125 GLU   A CA  1 
ATOM   688  C  C   . GLU   A 1 89  ? -39.47400 7.33500   16.74200  1.000 72.17759  ? 125 GLU   A C   1 
ATOM   689  O  O   . GLU   A 1 89  ? -40.42900 7.17200   17.51000  1.000 71.86834  ? 125 GLU   A O   1 
ATOM   690  C  CB  . GLU   A 1 89  ? -37.60200 5.66300   16.88800  1.000 65.04842  ? 125 GLU   A CB  1 
ATOM   691  C  CG  . GLU   A 1 89  ? -37.91600 5.25900   18.32200  1.000 76.16962  ? 125 GLU   A CG  1 
ATOM   692  C  CD  . GLU   A 1 89  ? -38.57000 3.89300   18.42500  1.000 70.90675  ? 125 GLU   A CD  1 
ATOM   693  O  OE1 . GLU   A 1 89  ? -38.68500 3.20000   17.39200  1.000 68.93410  ? 125 GLU   A OE1 1 
ATOM   694  O  OE2 . GLU   A 1 89  ? -38.96500 3.50900   19.54600  1.000 69.37723  ? 125 GLU   A OE2 1 
ATOM   695  N  N   . ASP   A 1 90  ? -38.98800 8.54600   16.45500  1.000 68.90911  ? 126 ASP   A N   1 
ATOM   696  C  CA  . ASP   A 1 90  ? -39.60300 9.74700   17.01400  1.000 67.28947  ? 126 ASP   A CA  1 
ATOM   697  C  C   . ASP   A 1 90  ? -41.00400 9.95500   16.45400  1.000 69.74107  ? 126 ASP   A C   1 
ATOM   698  O  O   . ASP   A 1 90  ? -41.96200 10.16500  17.20800  1.000 79.72637  ? 126 ASP   A O   1 
ATOM   699  C  CB  . ASP   A 1 90  ? -38.72500 10.96700  16.73500  1.000 59.17493  ? 126 ASP   A CB  1 
ATOM   700  C  CG  . ASP   A 1 90  ? -37.42200 10.93900  17.51100  1.000 67.40322  ? 126 ASP   A CG  1 
ATOM   701  O  OD1 . ASP   A 1 90  ? -37.41800 10.43100  18.65100  1.000 75.08671  ? 126 ASP   A OD1 1 
ATOM   702  O  OD2 . ASP   A 1 90  ? -36.40200 11.42600  16.98000  1.000 61.26620  ? 126 ASP   A OD2 1 
ATOM   703  N  N   . LEU   A 1 91  ? -41.14300 9.90000   15.12700  1.000 59.75128  ? 127 LEU   A N   1 
ATOM   704  C  CA  . LEU   A 1 91  ? -42.45800 10.03000  14.50900  1.000 65.83765  ? 127 LEU   A CA  1 
ATOM   705  C  C   . LEU   A 1 91  ? -43.37800 8.88100   14.89900  1.000 71.27116  ? 127 LEU   A C   1 
ATOM   706  O  O   . LEU   A 1 91  ? -44.60500 9.03900   14.88400  1.000 74.53796  ? 127 LEU   A O   1 
ATOM   707  C  CB  . LEU   A 1 91  ? -42.31400 10.10200  12.99000  1.000 69.70351  ? 127 LEU   A CB  1 
ATOM   708  C  CG  . LEU   A 1 91  ? -41.41900 11.22600  12.46300  1.000 69.48990  ? 127 LEU   A CG  1 
ATOM   709  C  CD1 . LEU   A 1 91  ? -41.04400 10.98000  11.01200  1.000 63.49322  ? 127 LEU   A CD1 1 
ATOM   710  C  CD2 . LEU   A 1 91  ? -42.10600 12.57300  12.62000  1.000 61.36885  ? 127 LEU   A CD2 1 
ATOM   711  N  N   . PHE   A 1 92  ? -42.81000 7.72400   15.24400  1.000 63.34124  ? 128 PHE   A N   1 
ATOM   712  C  CA  . PHE   A 1 92  ? -43.62400 6.58900   15.66700  1.000 66.04058  ? 128 PHE   A CA  1 
ATOM   713  C  C   . PHE   A 1 92  ? -44.31200 6.88100   16.99400  1.000 68.34009  ? 128 PHE   A C   1 
ATOM   714  O  O   . PHE   A 1 92  ? -45.51700 6.65200   17.14600  1.000 71.65698  ? 128 PHE   A O   1 
ATOM   715  C  CB  . PHE   A 1 92  ? -42.75200 5.33700   15.76900  1.000 57.93910  ? 128 PHE   A CB  1 
ATOM   716  C  CG  . PHE   A 1 92  ? -43.52800 4.05400   15.88700  1.000 68.60017  ? 128 PHE   A CG  1 
ATOM   717  C  CD1 . PHE   A 1 92  ? -44.36900 3.64100   14.86800  1.000 67.65673  ? 128 PHE   A CD1 1 
ATOM   718  C  CD2 . PHE   A 1 92  ? -43.40400 3.25400   17.01300  1.000 78.60939  ? 128 PHE   A CD2 1 
ATOM   719  C  CE1 . PHE   A 1 92  ? -45.07600 2.45800   14.97000  1.000 70.04866  ? 128 PHE   A CE1 1 
ATOM   720  C  CE2 . PHE   A 1 92  ? -44.10700 2.06900   17.12000  1.000 71.60793  ? 128 PHE   A CE2 1 
ATOM   721  C  CZ  . PHE   A 1 92  ? -44.94400 1.67000   16.09700  1.000 60.66024  ? 128 PHE   A CZ  1 
ATOM   722  N  N   . ASP   A 1 93  ? -43.55700 7.40100   17.96400  1.000 61.34817  ? 129 ASP   A N   1 
ATOM   723  C  CA  . ASP   A 1 93  ? -44.12500 7.72700   19.26700  1.000 77.04327  ? 129 ASP   A CA  1 
ATOM   724  C  C   . ASP   A 1 93  ? -45.19300 8.80800   19.15900  1.000 80.49297  ? 129 ASP   A C   1 
ATOM   725  O  O   . ASP   A 1 93  ? -46.18900 8.78500   19.89300  1.000 84.93127  ? 129 ASP   A O   1 
ATOM   726  C  CB  . ASP   A 1 93  ? -43.01100 8.16900   20.21500  1.000 82.94829  ? 129 ASP   A CB  1 
ATOM   727  C  CG  . ASP   A 1 93  ? -42.41100 7.01400   20.98600  1.000 99.08916  ? 129 ASP   A CG  1 
ATOM   728  O  OD1 . ASP   A 1 93  ? -43.11600 6.44100   21.84300  1.000 106.50454 ? 129 ASP   A OD1 1 
ATOM   729  O  OD2 . ASP   A 1 93  ? -41.23900 6.67000   20.72800  1.000 104.04944 ? 129 ASP   A OD2 1 
ATOM   730  N  N   . TRP   A 1 94  ? -45.00800 9.75900   18.24400  1.000 74.51169  ? 130 TRP   A N   1 
ATOM   731  C  CA  . TRP   A 1 94  ? -45.90800 10.89900  18.14100  1.000 80.93345  ? 130 TRP   A CA  1 
ATOM   732  C  C   . TRP   A 1 94  ? -47.21600 10.55700  17.44100  1.000 78.82241  ? 130 TRP   A C   1 
ATOM   733  O  O   . TRP   A 1 94  ? -48.18500 11.31200  17.56700  1.000 84.14198  ? 130 TRP   A O   1 
ATOM   734  C  CB  . TRP   A 1 94  ? -45.20600 12.04900  17.41100  1.000 77.75995  ? 130 TRP   A CB  1 
ATOM   735  C  CG  . TRP   A 1 94  ? -43.90200 12.45200  18.04900  1.000 102.68472 ? 130 TRP   A CG  1 
ATOM   736  C  CD1 . TRP   A 1 94  ? -43.45200 12.09800  19.29000  1.000 112.27982 ? 130 TRP   A CD1 1 
ATOM   737  C  CD2 . TRP   A 1 94  ? -42.87800 13.27300  17.47300  1.000 106.23463 ? 130 TRP   A CD2 1 
ATOM   738  N  NE1 . TRP   A 1 94  ? -42.21700 12.64900  19.52200  1.000 118.72836 ? 130 TRP   A NE1 1 
ATOM   739  C  CE2 . TRP   A 1 94  ? -41.84200 13.37500  18.42300  1.000 114.31131 ? 130 TRP   A CE2 1 
ATOM   740  C  CE3 . TRP   A 1 94  ? -42.73700 13.93200  16.24900  1.000 99.38465  ? 130 TRP   A CE3 1 
ATOM   741  C  CZ2 . TRP   A 1 94  ? -40.68300 14.10900  18.18600  1.000 110.87804 ? 130 TRP   A CZ2 1 
ATOM   742  C  CZ3 . TRP   A 1 94  ? -41.58200 14.66000  16.01700  1.000 102.43489 ? 130 TRP   A CZ3 1 
ATOM   743  C  CH2 . TRP   A 1 94  ? -40.57300 14.74400  16.98100  1.000 96.62662  ? 130 TRP   A CH2 1 
ATOM   744  N  N   . CYS   A 1 95  ? -47.26900 9.44100   16.71500  1.000 63.57237  ? 131 CYS   A N   1 
ATOM   745  C  CA  . CYS   A 1 95  ? -48.48500 8.99500   16.05000  1.000 71.74921  ? 131 CYS   A CA  1 
ATOM   746  C  C   . CYS   A 1 95  ? -49.24500 7.95100   16.85900  1.000 76.56237  ? 131 CYS   A C   1 
ATOM   747  O  O   . CYS   A 1 95  ? -50.16100 7.31500   16.32700  1.000 87.88365  ? 131 CYS   A O   1 
ATOM   748  C  CB  . CYS   A 1 95  ? -48.15400 8.44000   14.66300  1.000 72.34485  ? 131 CYS   A CB  1 
ATOM   749  S  SG  . CYS   A 1 95  ? -47.46400 9.65500   13.51700  1.000 69.28912  ? 131 CYS   A SG  1 
ATOM   750  N  N   . GLY   A 1 96  ? -48.89100 7.76300   18.12700  1.000 70.91691  ? 132 GLY   A N   1 
ATOM   751  C  CA  . GLY   A 1 96  ? -49.53200 6.75900   18.95100  1.000 75.25362  ? 132 GLY   A CA  1 
ATOM   752  C  C   . GLY   A 1 96  ? -48.87400 5.40000   18.93100  1.000 80.60148  ? 132 GLY   A C   1 
ATOM   753  O  O   . GLY   A 1 96  ? -49.53000 4.40900   19.27300  1.000 77.03324  ? 132 GLY   A O   1 
ATOM   754  N  N   . ARG   A 1 97  ? -47.60100 5.32300   18.53800  1.000 75.85880  ? 133 ARG   A N   1 
ATOM   755  C  CA  . ARG   A 1 97  ? -46.85600 4.06400   18.46600  1.000 69.03259  ? 133 ARG   A CA  1 
ATOM   756  C  C   . ARG   A 1 97  ? -47.53900 3.06000   17.53900  1.000 77.10413  ? 133 ARG   A C   1 
ATOM   757  O  O   . ARG   A 1 97  ? -47.63000 1.86900   17.84300  1.000 72.89659  ? 133 ARG   A O   1 
ATOM   758  C  CB  . ARG   A 1 97  ? -46.63800 3.46600   19.85900  1.000 73.20254  ? 133 ARG   A CB  1 
ATOM   759  C  CG  . ARG   A 1 97  ? -45.84800 4.36500   20.79600  1.000 82.53629  ? 133 ARG   A CG  1 
ATOM   760  C  CD  . ARG   A 1 97  ? -45.33400 3.59300   21.99800  1.000 93.62225  ? 133 ARG   A CD  1 
ATOM   761  N  NE  . ARG   A 1 97  ? -44.57600 2.41400   21.59500  1.000 86.63079  ? 133 ARG   A NE  1 
ATOM   762  C  CZ  . ARG   A 1 97  ? -43.31500 2.43700   21.18800  1.000 88.55771  ? 133 ARG   A CZ  1 
ATOM   763  N  NH1 . ARG   A 1 97  ? -42.63400 3.56800   21.10800  1.000 87.93188  ? 133 ARG   A NH1 1 
ATOM   764  N  NH2 . ARG   A 1 97  ? -42.72200 1.29600   20.84800  1.000 89.13943  ? 133 ARG   A NH2 1 
ATOM   765  N  N   . ARG   A 1 98  ? -48.00800 3.54600   16.39000  1.000 74.68651  ? 134 ARG   A N   1 
ATOM   766  C  CA  . ARG   A 1 98  ? -48.65500 2.70400   15.39000  1.000 73.68220  ? 134 ARG   A CA  1 
ATOM   767  C  C   . ARG   A 1 98  ? -48.72900 3.47400   14.07900  1.000 82.53678  ? 134 ARG   A C   1 
ATOM   768  O  O   . ARG   A 1 98  ? -49.20400 4.61300   14.05700  1.000 83.09760  ? 134 ARG   A O   1 
ATOM   769  C  CB  . ARG   A 1 98  ? -50.05900 2.28200   15.84200  1.000 75.66391  ? 134 ARG   A CB  1 
ATOM   770  C  CG  . ARG   A 1 98  ? -50.17800 0.81800   16.23600  1.000 79.98550  ? 134 ARG   A CG  1 
ATOM   771  C  CD  . ARG   A 1 98  ? -51.53800 0.51700   16.84300  1.000 89.75803  ? 134 ARG   A CD  1 
ATOM   772  N  NE  . ARG   A 1 98  ? -51.79400 -0.91700  16.90000  1.000 98.80789  ? 134 ARG   A NE  1 
ATOM   773  C  CZ  . ARG   A 1 98  ? -52.28800 -1.62400  15.89300  1.000 96.97008  ? 134 ARG   A CZ  1 
ATOM   774  N  NH1 . ARG   A 1 98  ? -52.59900 -1.05800  14.73800  1.000 85.89578  ? 134 ARG   A NH1 1 
ATOM   775  N  NH2 . ARG   A 1 98  ? -52.47100 -2.93300  16.04700  1.000 87.68797  ? 134 ARG   A NH2 1 
ATOM   776  N  N   . PHE   A 1 99  ? -48.26100 2.85500   12.99800  1.000 65.43117  ? 135 PHE   A N   1 
ATOM   777  C  CA  . PHE   A 1 99  ? -48.30300 3.44400   11.66700  1.000 65.10851  ? 135 PHE   A CA  1 
ATOM   778  C  C   . PHE   A 1 99  ? -49.33500 2.71900   10.81200  1.000 73.05910  ? 135 PHE   A C   1 
ATOM   779  O  O   . PHE   A 1 99  ? -49.51200 1.50300   10.93700  1.000 72.41808  ? 135 PHE   A O   1 
ATOM   780  C  CB  . PHE   A 1 99  ? -46.93300 3.37400   10.98600  1.000 64.59753  ? 135 PHE   A CB  1 
ATOM   781  C  CG  . PHE   A 1 99  ? -45.98600 4.46400   11.39700  1.000 78.00845  ? 135 PHE   A CG  1 
ATOM   782  C  CD1 . PHE   A 1 99  ? -46.41100 5.51100   12.19700  1.000 58.43269  ? 135 PHE   A CD1 1 
ATOM   783  C  CD2 . PHE   A 1 99  ? -44.66800 4.44600   10.96900  1.000 63.61206  ? 135 PHE   A CD2 1 
ATOM   784  C  CE1 . PHE   A 1 99  ? -45.53700 6.51400   12.57100  1.000 71.08594  ? 135 PHE   A CE1 1 
ATOM   785  C  CE2 . PHE   A 1 99  ? -43.79000 5.44500   11.33900  1.000 72.34044  ? 135 PHE   A CE2 1 
ATOM   786  C  CZ  . PHE   A 1 99  ? -44.22400 6.48000   12.14000  1.000 68.13723  ? 135 PHE   A CZ  1 
ATOM   787  N  N   . SER   A 1 100 ? -50.01100 3.46400   9.94100   1.000 65.97121  ? 136 SER   A N   1 
ATOM   788  C  CA  . SER   A 1 100 ? -50.97900 2.84900   9.04800   1.000 76.97451  ? 136 SER   A CA  1 
ATOM   789  C  C   . SER   A 1 100 ? -50.26300 2.00900   7.98800   1.000 69.57554  ? 136 SER   A C   1 
ATOM   790  O  O   . SER   A 1 100 ? -49.03400 1.98500   7.89600   1.000 65.45077  ? 136 SER   A O   1 
ATOM   791  C  CB  . SER   A 1 100 ? -51.86400 3.91200   8.39600   1.000 77.16222  ? 136 SER   A CB  1 
ATOM   792  O  OG  . SER   A 1 100 ? -51.14600 4.67900   7.44900   1.000 56.71224  ? 136 SER   A OG  1 
ATOM   793  N  N   . VAL   A 1 101 ? -51.05200 1.30100   7.18100   1.000 49.52093  ? 137 VAL   A N   1 
ATOM   794  C  CA  . VAL   A 1 101 ? -50.46400 0.39800   6.19700   1.000 73.83999  ? 137 VAL   A CA  1 
ATOM   795  C  C   . VAL   A 1 101 ? -49.78100 1.18500   5.08400   1.000 67.81158  ? 137 VAL   A C   1 
ATOM   796  O  O   . VAL   A 1 101 ? -48.70000 0.80900   4.61400   1.000 59.79967  ? 137 VAL   A O   1 
ATOM   797  C  CB  . VAL   A 1 101 ? -51.53700 -0.56000  5.64700   1.000 65.00688  ? 137 VAL   A CB  1 
ATOM   798  C  CG1 . VAL   A 1 101 ? -50.94500 -1.48400  4.59300   1.000 50.81364  ? 137 VAL   A CG1 1 
ATOM   799  C  CG2 . VAL   A 1 101 ? -52.14900 -1.37000  6.78200   1.000 72.00222  ? 137 VAL   A CG2 1 
ATOM   800  N  N   . LYS   A 1 102 ? -50.38700 2.29700   4.66100   1.000 69.54876  ? 138 LYS   A N   1 
ATOM   801  C  CA  . LYS   A 1 102 ? -49.85000 3.05800   3.53600   1.000 67.28737  ? 138 LYS   A CA  1 
ATOM   802  C  C   . LYS   A 1 102 ? -48.50200 3.67800   3.87800   1.000 71.74650  ? 138 LYS   A C   1 
ATOM   803  O  O   . LYS   A 1 102 ? -47.58700 3.68600   3.04500   1.000 78.61042  ? 138 LYS   A O   1 
ATOM   804  C  CB  . LYS   A 1 102 ? -50.84800 4.13500   3.11600   1.000 73.67670  ? 138 LYS   A CB  1 
ATOM   805  C  CG  . LYS   A 1 102 ? -50.34000 5.11600   2.07700   1.000 78.11489  ? 138 LYS   A CG  1 
ATOM   806  C  CD  . LYS   A 1 102 ? -51.41200 6.14000   1.73800   1.000 87.68501  ? 138 LYS   A CD  1 
ATOM   807  C  CE  . LYS   A 1 102 ? -50.85700 7.26500   0.88200   1.000 97.78320  ? 138 LYS   A CE  1 
ATOM   808  N  NZ  . LYS   A 1 102 ? -51.90600 8.26500   0.54000   1.000 86.10884  ? 138 LYS   A NZ  1 
ATOM   809  N  N   . THR   A 1 103 ? -48.36000 4.19900   5.10100   1.000 61.96091  ? 139 THR   A N   1 
ATOM   810  C  CA  . THR   A 1 103 ? -47.09300 4.79600   5.50900   1.000 66.05829  ? 139 THR   A CA  1 
ATOM   811  C  C   . THR   A 1 103 ? -46.01700 3.74800   5.75200   1.000 56.42453  ? 139 THR   A C   1 
ATOM   812  O  O   . THR   A 1 103 ? -44.84500 4.00300   5.46300   1.000 61.34574  ? 139 THR   A O   1 
ATOM   813  C  CB  . THR   A 1 103 ? -47.25800 5.65700   6.76800   1.000 66.56665  ? 139 THR   A CB  1 
ATOM   814  O  OG1 . THR   A 1 103 ? -45.97600 6.16900   7.15600   1.000 64.27915  ? 139 THR   A OG1 1 
ATOM   815  C  CG2 . THR   A 1 103 ? -47.85500 4.86200   7.93300   1.000 78.07308  ? 139 THR   A CG2 1 
ATOM   816  N  N   . VAL   A 1 104 ? -46.38200 2.57900   6.28200   1.000 71.42304  ? 140 VAL   A N   1 
ATOM   817  C  CA  . VAL   A 1 104 ? -45.39700 1.51600   6.44300   1.000 55.09336  ? 140 VAL   A CA  1 
ATOM   818  C  C   . VAL   A 1 104 ? -44.89900 1.05500   5.08300   1.000 44.67354  ? 140 VAL   A C   1 
ATOM   819  O  O   . VAL   A 1 104 ? -43.70000 0.82200   4.89100   1.000 50.82742  ? 140 VAL   A O   1 
ATOM   820  C  CB  . VAL   A 1 104 ? -45.98700 0.35200   7.25900   1.000 49.25683  ? 140 VAL   A CB  1 
ATOM   821  C  CG1 . VAL   A 1 104 ? -45.03100 -0.82100  7.27200   1.000 66.38056  ? 140 VAL   A CG1 1 
ATOM   822  C  CG2 . VAL   A 1 104 ? -46.27500 0.79500   8.67700   1.000 69.61685  ? 140 VAL   A CG2 1 
ATOM   823  N  N   . VAL   A 1 105 ? -45.80800 0.94100   4.11300   1.000 54.93864  ? 141 VAL   A N   1 
ATOM   824  C  CA  . VAL   A 1 105 ? -45.43000 0.53500   2.76200   1.000 41.41394  ? 141 VAL   A CA  1 
ATOM   825  C  C   . VAL   A 1 105 ? -44.51800 1.57800   2.13000   1.000 63.09039  ? 141 VAL   A C   1 
ATOM   826  O  O   . VAL   A 1 105 ? -43.42400 1.26000   1.64800   1.000 50.58423  ? 141 VAL   A O   1 
ATOM   827  C  CB  . VAL   A 1 105 ? -46.68500 0.29800   1.90300   1.000 51.68657  ? 141 VAL   A CB  1 
ATOM   828  C  CG1 . VAL   A 1 105 ? -46.31000 0.25500   0.43300   1.000 49.32172  ? 141 VAL   A CG1 1 
ATOM   829  C  CG2 . VAL   A 1 105 ? -47.38100 -0.98900  2.31900   1.000 61.72843  ? 141 VAL   A CG2 1 
ATOM   830  N  N   . GLN   A 1 106 ? -44.95400 2.84200   2.13300   1.000 62.09977  ? 142 GLN   A N   1 
ATOM   831  C  CA  . GLN   A 1 106 ? -44.19900 3.89800   1.46400   1.000 61.74838  ? 142 GLN   A CA  1 
ATOM   832  C  C   . GLN   A 1 106 ? -42.81900 4.07500   2.08300   1.000 53.10597  ? 142 GLN   A C   1 
ATOM   833  O  O   . GLN   A 1 106 ? -41.83300 4.29600   1.36900   1.000 59.18662  ? 142 GLN   A O   1 
ATOM   834  C  CB  . GLN   A 1 106 ? -44.98000 5.21200   1.51200   1.000 51.74926  ? 142 GLN   A CB  1 
ATOM   835  C  CG  . GLN   A 1 106 ? -46.22200 5.23500   0.63500   1.000 69.65167  ? 142 GLN   A CG  1 
ATOM   836  C  CD  . GLN   A 1 106 ? -47.01300 6.52000   0.77600   1.000 77.17775  ? 142 GLN   A CD  1 
ATOM   837  O  OE1 . GLN   A 1 106 ? -47.63900 6.98800   -0.17600  1.000 87.08633  ? 142 GLN   A OE1 1 
ATOM   838  N  NE2 . GLN   A 1 106 ? -46.99200 7.09700   1.97100   1.000 80.77541  ? 142 GLN   A NE2 1 
ATOM   839  N  N   . VAL   A 1 107 ? -42.72700 3.98800   3.41100   1.000 54.55178  ? 143 VAL   A N   1 
ATOM   840  C  CA  . VAL   A 1 107 ? -41.42300 4.07800   4.05900   1.000 54.13688  ? 143 VAL   A CA  1 
ATOM   841  C  C   . VAL   A 1 107 ? -40.58300 2.84900   3.73400   1.000 58.29745  ? 143 VAL   A C   1 
ATOM   842  O  O   . VAL   A 1 107 ? -39.37700 2.95700   3.47800   1.000 54.22274  ? 143 VAL   A O   1 
ATOM   843  C  CB  . VAL   A 1 107 ? -41.58800 4.27100   5.57700   1.000 50.97482  ? 143 VAL   A CB  1 
ATOM   844  C  CG1 . VAL   A 1 107 ? -40.25200 4.12300   6.27800   1.000 42.52013  ? 143 VAL   A CG1 1 
ATOM   845  C  CG2 . VAL   A 1 107 ? -42.18400 5.63800   5.87500   1.000 62.09707  ? 143 VAL   A CG2 1 
ATOM   846  N  N   . ALA   A 1 108 ? -41.20800 1.66800   3.71500   1.000 53.07742  ? 144 ALA   A N   1 
ATOM   847  C  CA  . ALA   A 1 108 ? -40.47500 0.43300   3.45200   1.000 58.52350  ? 144 ALA   A CA  1 
ATOM   848  C  C   . ALA   A 1 108 ? -39.74500 0.48800   2.11700   1.000 67.21554  ? 144 ALA   A C   1 
ATOM   849  O  O   . ALA   A 1 108 ? -38.58900 0.06000   2.01300   1.000 52.20460  ? 144 ALA   A O   1 
ATOM   850  C  CB  . ALA   A 1 108 ? -41.43000 -0.76100  3.48000   1.000 51.17806  ? 144 ALA   A CB  1 
ATOM   851  N  N   . ILE   A 1 109 ? -40.40300 1.02100   1.08700   1.000 55.88797  ? 145 ILE   A N   1 
ATOM   852  C  CA  . ILE   A 1 109 ? -39.79800 1.07500   -0.23900  1.000 64.68664  ? 145 ILE   A CA  1 
ATOM   853  C  C   . ILE   A 1 109 ? -38.57500 1.98400   -0.23700  1.000 64.93052  ? 145 ILE   A C   1 
ATOM   854  O  O   . ILE   A 1 109 ? -37.56400 1.68400   -0.88300  1.000 58.77797  ? 145 ILE   A O   1 
ATOM   855  C  CB  . ILE   A 1 109 ? -40.84600 1.52300   -1.27100  1.000 66.37925  ? 145 ILE   A CB  1 
ATOM   856  C  CG1 . ILE   A 1 109 ? -42.09600 0.65200   -1.15000  1.000 65.44364  ? 145 ILE   A CG1 1 
ATOM   857  C  CG2 . ILE   A 1 109 ? -40.28300 1.43900   -2.68000  1.000 61.15466  ? 145 ILE   A CG2 1 
ATOM   858  C  CD1 . ILE   A 1 109 ? -43.34900 1.30200   -1.69600  1.000 69.90635  ? 145 ILE   A CD1 1 
ATOM   859  N  N   . GLN   A 1 110 ? -38.63900 3.10200   0.49000   1.000 49.00447  ? 146 GLN   A N   1 
ATOM   860  C  CA  . GLN   A 1 110 ? -37.48500 3.99300   0.55900   1.000 66.15978  ? 146 GLN   A CA  1 
ATOM   861  C  C   . GLN   A 1 110 ? -36.35100 3.37300   1.36800   1.000 60.93359  ? 146 GLN   A C   1 
ATOM   862  O  O   . GLN   A 1 110 ? -35.17600 3.54300   1.02700   1.000 63.46707  ? 146 GLN   A O   1 
ATOM   863  C  CB  . GLN   A 1 110 ? -37.89100 5.34400   1.14700   1.000 52.99545  ? 146 GLN   A CB  1 
ATOM   864  C  CG  . GLN   A 1 110 ? -38.65500 6.23700   0.18400   1.000 63.38643  ? 146 GLN   A CG  1 
ATOM   865  C  CD  . GLN   A 1 110 ? -38.88300 7.62800   0.74200   1.000 63.48117  ? 146 GLN   A CD  1 
ATOM   866  O  OE1 . GLN   A 1 110 ? -37.93500 8.35700   1.03600   1.000 59.85689  ? 146 GLN   A OE1 1 
ATOM   867  N  NE2 . GLN   A 1 110 ? -40.14700 8.00200   0.89700   1.000 57.90980  ? 146 GLN   A NE2 1 
ATOM   868  N  N   . MET   A 1 111 ? -36.68000 2.64800   2.44100   1.000 55.85922  ? 147 MET   A N   1 
ATOM   869  C  CA  . MET   A 1 111 ? -35.63900 2.00300   3.23500   1.000 67.26781  ? 147 MET   A CA  1 
ATOM   870  C  C   . MET   A 1 111 ? -34.93000 0.91900   2.43400   1.000 71.24712  ? 147 MET   A C   1 
ATOM   871  O  O   . MET   A 1 111 ? -33.71600 0.72800   2.57100   1.000 70.20456  ? 147 MET   A O   1 
ATOM   872  C  CB  . MET   A 1 111 ? -36.23700 1.41800   4.51400   1.000 45.13245  ? 147 MET   A CB  1 
ATOM   873  C  CG  . MET   A 1 111 ? -36.97500 2.43000   5.37100   1.000 54.09387  ? 147 MET   A CG  1 
ATOM   874  S  SD  . MET   A 1 111 ? -37.77200 1.66600   6.79700   1.000 69.74100  ? 147 MET   A SD  1 
ATOM   875  C  CE  . MET   A 1 111 ? -36.52800 1.89700   8.06100   1.000 54.61650  ? 147 MET   A CE  1 
ATOM   876  N  N   . LEU   A 1 112 ? -35.67400 0.19900   1.59000   1.000 57.19273  ? 148 LEU   A N   1 
ATOM   877  C  CA  . LEU   A 1 112 ? -35.06400 -0.82500  0.74800   1.000 70.64868  ? 148 LEU   A CA  1 
ATOM   878  C  C   . LEU   A 1 112 ? -34.10500 -0.20900  -0.26300  1.000 74.30511  ? 148 LEU   A C   1 
ATOM   879  O  O   . LEU   A 1 112 ? -33.05400 -0.78800  -0.56200  1.000 60.34576  ? 148 LEU   A O   1 
ATOM   880  C  CB  . LEU   A 1 112 ? -36.14800 -1.63200  0.03300   1.000 53.17858  ? 148 LEU   A CB  1 
ATOM   881  C  CG  . LEU   A 1 112 ? -37.07600 -2.48900  0.89600   1.000 64.13377  ? 148 LEU   A CG  1 
ATOM   882  C  CD1 . LEU   A 1 112 ? -38.20700 -3.06300  0.05800   1.000 66.55776  ? 148 LEU   A CD1 1 
ATOM   883  C  CD2 . LEU   A 1 112 ? -36.30300 -3.60000  1.57600   1.000 61.96482  ? 148 LEU   A CD2 1 
ATOM   884  N  N   . THR   A 1 113 ? -34.45100 0.96300   -0.80100  1.000 62.40106  ? 149 THR   A N   1 
ATOM   885  C  CA  . THR   A 1 113 ? -33.58100 1.61300   -1.77600  1.000 65.40800  ? 149 THR   A CA  1 
ATOM   886  C  C   . THR   A 1 113 ? -32.30600 2.12800   -1.11900  1.000 60.64633  ? 149 THR   A C   1 
ATOM   887  O  O   . THR   A 1 113 ? -31.21800 2.02900   -1.69900  1.000 61.31634  ? 149 THR   A O   1 
ATOM   888  C  CB  . THR   A 1 113 ? -34.32500 2.75500   -2.46800  1.000 69.27185  ? 149 THR   A CB  1 
ATOM   889  O  OG1 . THR   A 1 113 ? -35.59800 2.28700   -2.93200  1.000 77.46510  ? 149 THR   A OG1 1 
ATOM   890  C  CG2 . THR   A 1 113 ? -33.52200 3.27100   -3.65400  1.000 75.93046  ? 149 THR   A CG2 1 
ATOM   891  N  N   . LEU   A 1 114 ? -32.42000 2.68100   0.09100   1.000 62.93213  ? 150 LEU   A N   1 
ATOM   892  C  CA  . LEU   A 1 114 ? -31.23900 3.16700   0.79800   1.000 62.21533  ? 150 LEU   A CA  1 
ATOM   893  C  C   . LEU   A 1 114 ? -30.28400 2.02700   1.12400   1.000 58.35701  ? 150 LEU   A C   1 
ATOM   894  O  O   . LEU   A 1 114 ? -29.06300 2.17200   0.98800   1.000 57.78837  ? 150 LEU   A O   1 
ATOM   895  C  CB  . LEU   A 1 114 ? -31.65600 3.89400   2.07800   1.000 69.83521  ? 150 LEU   A CB  1 
ATOM   896  C  CG  . LEU   A 1 114 ? -32.53100 5.13800   1.92500   1.000 60.70670  ? 150 LEU   A CG  1 
ATOM   897  C  CD1 . LEU   A 1 114 ? -33.00500 5.62700   3.28500   1.000 62.92097  ? 150 LEU   A CD1 1 
ATOM   898  C  CD2 . LEU   A 1 114 ? -31.78100 6.23600   1.18900   1.000 74.58346  ? 150 LEU   A CD2 1 
ATOM   899  N  N   . VAL   A 1 115 ? -30.82200 0.88500   1.55500   1.000 62.00413  ? 151 VAL   A N   1 
ATOM   900  C  CA  . VAL   A 1 115 ? -29.97800 -0.25400  1.90000   1.000 64.04736  ? 151 VAL   A CA  1 
ATOM   901  C  C   . VAL   A 1 115 ? -29.31400 -0.82600  0.65300   1.000 60.88420  ? 151 VAL   A C   1 
ATOM   902  O  O   . VAL   A 1 115 ? -28.15000 -1.24300  0.68900   1.000 66.06975  ? 151 VAL   A O   1 
ATOM   903  C  CB  . VAL   A 1 115 ? -30.80600 -1.31200  2.65200   1.000 67.45946  ? 151 VAL   A CB  1 
ATOM   904  C  CG1 . VAL   A 1 115 ? -30.03600 -2.61400  2.77600   1.000 57.39967  ? 151 VAL   A CG1 1 
ATOM   905  C  CG2 . VAL   A 1 115 ? -31.19400 -0.79200  4.02700   1.000 48.98598  ? 151 VAL   A CG2 1 
ATOM   906  N  N   . GLU   A 1 116 ? -30.03400 -0.84400  -0.47200  1.000 59.79008  ? 152 GLU   A N   1 
ATOM   907  C  CA  . GLU   A 1 116 ? -29.45500 -1.36000  -1.70900  1.000 72.20686  ? 152 GLU   A CA  1 
ATOM   908  C  C   . GLU   A 1 116 ? -28.28500 -0.50200  -2.17500  1.000 76.97743  ? 152 GLU   A C   1 
ATOM   909  O  O   . GLU   A 1 116 ? -27.27300 -1.02900  -2.64900  1.000 87.32248  ? 152 GLU   A O   1 
ATOM   910  C  CB  . GLU   A 1 116 ? -30.52000 -1.44500  -2.80100  1.000 63.00780  ? 152 GLU   A CB  1 
ATOM   911  C  CG  . GLU   A 1 116 ? -29.97300 -1.89400  -4.15000  1.000 84.50269  ? 152 GLU   A CG  1 
ATOM   912  C  CD  . GLU   A 1 116 ? -31.01200 -1.84200  -5.24900  1.000 85.12352  ? 152 GLU   A CD  1 
ATOM   913  O  OE1 . GLU   A 1 116 ? -32.18200 -1.54000  -4.94200  1.000 79.40400  ? 152 GLU   A OE1 1 
ATOM   914  O  OE2 . GLU   A 1 116 ? -30.65800 -2.10100  -6.41900  1.000 89.74074  ? 152 GLU   A OE2 1 
ATOM   915  N  N   . GLU   A 1 117 ? -28.40700 0.82300   -2.05500  1.000 101.28101 ? 153 GLU   A N   1 
ATOM   916  C  CA  . GLU   A 1 117 ? -27.30700 1.69800   -2.45000  1.000 106.97588 ? 153 GLU   A CA  1 
ATOM   917  C  C   . GLU   A 1 117 ? -26.07800 1.46000   -1.58400  1.000 105.70127 ? 153 GLU   A C   1 
ATOM   918  O  O   . GLU   A 1 117 ? -24.94300 1.53100   -2.07000  1.000 109.11474 ? 153 GLU   A O   1 
ATOM   919  C  CB  . GLU   A 1 117 ? -27.74300 3.16200   -2.37800  1.000 113.09944 ? 153 GLU   A CB  1 
ATOM   920  C  CG  . GLU   A 1 117 ? -28.48100 3.65300   -3.61400  1.000 124.20236 ? 153 GLU   A CG  1 
ATOM   921  C  CD  . GLU   A 1 117 ? -27.58100 3.75100   -4.83400  1.000 135.41481 ? 153 GLU   A CD  1 
ATOM   922  O  OE1 . GLU   A 1 117 ? -26.35100 3.88400   -4.66200  1.000 130.77985 ? 153 GLU   A OE1 1 
ATOM   923  O  OE2 . GLU   A 1 117 ? -28.10600 3.69500   -5.96600  1.000 135.48290 ? 153 GLU   A OE2 1 
ATOM   924  N  N   . VAL   A 1 118 ? -26.28300 1.17600   -0.29700  1.000 70.27839  ? 154 VAL   A N   1 
ATOM   925  C  CA  . VAL   A 1 118 ? -25.16600 0.81600   0.57200   1.000 75.54255  ? 154 VAL   A CA  1 
ATOM   926  C  C   . VAL   A 1 118 ? -24.52800 -0.48400  0.10000   1.000 83.29639  ? 154 VAL   A C   1 
ATOM   927  O  O   . VAL   A 1 118 ? -23.30000 -0.63700  0.12200   1.000 79.44222  ? 154 VAL   A O   1 
ATOM   928  C  CB  . VAL   A 1 118 ? -25.64200 0.72400   2.03400   1.000 65.82548  ? 154 VAL   A CB  1 
ATOM   929  C  CG1 . VAL   A 1 118 ? -24.55300 0.14500   2.92300   1.000 72.32090  ? 154 VAL   A CG1 1 
ATOM   930  C  CG2 . VAL   A 1 118 ? -26.06600 2.09600   2.53700   1.000 85.56032  ? 154 VAL   A CG2 1 
ATOM   931  N  N   . HIS   A 1 119 ? -25.35000 -1.43100  -0.35900  1.000 69.16082  ? 155 HIS   A N   1 
ATOM   932  C  CA  . HIS   A 1 119 ? -24.82400 -2.71300  -0.81500  1.000 83.39047  ? 155 HIS   A CA  1 
ATOM   933  C  C   . HIS   A 1 119 ? -24.11800 -2.59400  -2.16100  1.000 79.46542  ? 155 HIS   A C   1 
ATOM   934  O  O   . HIS   A 1 119 ? -23.17100 -3.34300  -2.42700  1.000 90.20439  ? 155 HIS   A O   1 
ATOM   935  C  CB  . HIS   A 1 119 ? -25.95100 -3.74300  -0.88500  1.000 72.86168  ? 155 HIS   A CB  1 
ATOM   936  C  CG  . HIS   A 1 119 ? -26.51500 -4.11000  0.45300   1.000 67.51618  ? 155 HIS   A CG  1 
ATOM   937  N  ND1 . HIS   A 1 119 ? -27.58900 -4.96000  0.60300   1.000 77.34176  ? 155 HIS   A ND1 1 
ATOM   938  C  CD2 . HIS   A 1 119 ? -26.14900 -3.74300  1.70400   1.000 68.76521  ? 155 HIS   A CD2 1 
ATOM   939  C  CE1 . HIS   A 1 119 ? -27.86000 -5.10200  1.88800   1.000 66.30326  ? 155 HIS   A CE1 1 
ATOM   940  N  NE2 . HIS   A 1 119 ? -27.00200 -4.37200  2.57800   1.000 68.13992  ? 155 HIS   A NE2 1 
ATOM   941  N  N   . ARG   A 1 120 ? -24.55600 -1.66800  -3.02000  1.000 74.45407  ? 156 ARG   A N   1 
ATOM   942  C  CA  . ARG   A 1 120 ? -23.86400 -1.45500  -4.28700  1.000 86.01359  ? 156 ARG   A CA  1 
ATOM   943  C  C   . ARG   A 1 120 ? -22.47300 -0.87200  -4.08900  1.000 93.39282  ? 156 ARG   A C   1 
ATOM   944  O  O   . ARG   A 1 120 ? -21.61300 -1.04200  -4.96000  1.000 90.27370  ? 156 ARG   A O   1 
ATOM   945  C  CB  . ARG   A 1 120 ? -24.67900 -0.53800  -5.20300  1.000 94.08026  ? 156 ARG   A CB  1 
ATOM   946  C  CG  . ARG   A 1 120 ? -25.99700 -1.13000  -5.67700  1.000 93.06583  ? 156 ARG   A CG  1 
ATOM   947  C  CD  . ARG   A 1 120 ? -26.42900 -0.55400  -7.02300  1.000 99.18624  ? 156 ARG   A CD  1 
ATOM   948  N  NE  . ARG   A 1 120 ? -26.45700 0.90500   -7.03400  1.000 111.09306 ? 156 ARG   A NE  1 
ATOM   949  C  CZ  . ARG   A 1 120 ? -25.57100 1.66800   -7.66000  1.000 111.31212 ? 156 ARG   A CZ  1 
ATOM   950  N  NH1 . ARG   A 1 120 ? -24.56900 1.14400   -8.34700  1.000 102.18439 ? 156 ARG   A NH1 1 
ATOM   951  N  NH2 . ARG   A 1 120 ? -25.69500 2.99100   -7.59600  1.000 106.21125 ? 156 ARG   A NH2 1 
ATOM   952  N  N   . HIS   A 1 121 ? -22.23300 -0.18900  -2.97000  1.000 90.93508  ? 157 HIS   A N   1 
ATOM   953  C  CA  . HIS   A 1 121 ? -20.91600 0.33000   -2.63500  1.000 97.89958  ? 157 HIS   A CA  1 
ATOM   954  C  C   . HIS   A 1 121 ? -20.11900 -0.62600  -1.75500  1.000 91.47174  ? 157 HIS   A C   1 
ATOM   955  O  O   . HIS   A 1 121 ? -19.23100 -0.18000  -1.01900  1.000 97.44948  ? 157 HIS   A O   1 
ATOM   956  C  CB  . HIS   A 1 121 ? -21.04300 1.69700   -1.95900  1.000 93.55433  ? 157 HIS   A CB  1 
ATOM   957  C  CG  . HIS   A 1 121 ? -21.47100 2.78900   -2.89000  1.000 104.81597 ? 157 HIS   A CG  1 
ATOM   958  N  ND1 . HIS   A 1 121 ? -22.75200 2.88200   -3.38900  1.000 96.29747  ? 157 HIS   A ND1 1 
ATOM   959  C  CD2 . HIS   A 1 121 ? -20.78400 3.82700   -3.42100  1.000 104.66609 ? 157 HIS   A CD2 1 
ATOM   960  C  CE1 . HIS   A 1 121 ? -22.83700 3.93300   -4.18400  1.000 98.49484  ? 157 HIS   A CE1 1 
ATOM   961  N  NE2 . HIS   A 1 121 ? -21.65700 4.52500   -4.22000  1.000 97.05524  ? 157 HIS   A NE2 1 
ATOM   962  N  N   . ASP   A 1 122 ? -20.42800 -1.92300  -1.81100  1.000 93.70823  ? 158 ASP   A N   1 
ATOM   963  C  CA  . ASP   A 1 122 ? -19.66500 -2.97300  -1.13700  1.000 87.66277  ? 158 ASP   A CA  1 
ATOM   964  C  C   . ASP   A 1 122 ? -19.71200 -2.84500  0.38400   1.000 88.25934  ? 158 ASP   A C   1 
ATOM   965  O  O   . ASP   A 1 122 ? -18.73400 -3.15200  1.06800   1.000 101.40639 ? 158 ASP   A O   1 
ATOM   966  C  CB  . ASP   A 1 122 ? -18.20900 -3.00000  -1.61900  1.000 94.51626  ? 158 ASP   A CB  1 
ATOM   967  C  CG  . ASP   A 1 122 ? -18.08700 -2.85500  -3.12600  1.000 104.85857 ? 158 ASP   A CG  1 
ATOM   968  O  OD1 . ASP   A 1 122 ? -18.97800 -3.34500  -3.85100  1.000 99.02050  ? 158 ASP   A OD1 1 
ATOM   969  O  OD2 . ASP   A 1 122 ? -17.09700 -2.24600  -3.58600  1.000 122.05462 ? 158 ASP   A OD2 1 
ATOM   970  N  N   . LEU   A 1 123 ? -20.84500 -2.40500  0.93000   1.000 94.51492  ? 159 LEU   A N   1 
ATOM   971  C  CA  . LEU   A 1 123 ? -21.01500 -2.23500  2.36600   1.000 86.80805  ? 159 LEU   A CA  1 
ATOM   972  C  C   . LEU   A 1 123 ? -22.32900 -2.86100  2.81200   1.000 73.36651  ? 159 LEU   A C   1 
ATOM   973  O  O   . LEU   A 1 123 ? -23.32600 -2.80800  2.08700   1.000 80.78305  ? 159 LEU   A O   1 
ATOM   974  C  CB  . LEU   A 1 123 ? -21.00200 -0.74600  2.75900   1.000 82.25473  ? 159 LEU   A CB  1 
ATOM   975  C  CG  . LEU   A 1 123 ? -19.70000 -0.07200  3.20500   1.000 88.91802  ? 159 LEU   A CG  1 
ATOM   976  C  CD1 . LEU   A 1 123 ? -19.14100 -0.74600  4.44400   1.000 87.76995  ? 159 LEU   A CD1 1 
ATOM   977  C  CD2 . LEU   A 1 123 ? -18.66400 -0.04400  2.09500   1.000 94.94873  ? 159 LEU   A CD2 1 
ATOM   978  N  N   . ILE   A 1 124 ? -22.32700 -3.45900  4.00400   1.000 71.89182  ? 160 ILE   A N   1 
ATOM   979  C  CA  . ILE   A 1 124 ? -23.55800 -3.84800  4.68300   1.000 68.81278  ? 160 ILE   A CA  1 
ATOM   980  C  C   . ILE   A 1 124 ? -23.64600 -3.03600  5.96700   1.000 76.82154  ? 160 ILE   A C   1 
ATOM   981  O  O   . ILE   A 1 124 ? -22.63500 -2.55600  6.48500   1.000 80.65665  ? 160 ILE   A O   1 
ATOM   982  C  CB  . ILE   A 1 124 ? -23.64500 -5.36800  4.96800   1.000 82.71011  ? 160 ILE   A CB  1 
ATOM   983  C  CG1 . ILE   A 1 124 ? -22.77000 -5.77500  6.15700   1.000 82.26617  ? 160 ILE   A CG1 1 
ATOM   984  C  CG2 . ILE   A 1 124 ? -23.26900 -6.16900  3.72900   1.000 75.81938  ? 160 ILE   A CG2 1 
ATOM   985  C  CD1 . ILE   A 1 124 ? -22.79200 -7.28100  6.44300   1.000 72.07138  ? 160 ILE   A CD1 1 
ATOM   986  N  N   . TYR   A 1 125 ? -24.86500 -2.87100  6.47700   1.000 76.72517  ? 161 TYR   A N   1 
ATOM   987  C  CA  . TYR   A 1 125 ? -25.10900 -1.88400  7.52400   1.000 61.29517  ? 161 TYR   A CA  1 
ATOM   988  C  C   . TYR   A 1 125 ? -24.90700 -2.44100  8.93300   1.000 72.81769  ? 161 TYR   A C   1 
ATOM   989  O  O   . TYR   A 1 125 ? -24.22700 -1.81700  9.75400   1.000 67.70979  ? 161 TYR   A O   1 
ATOM   990  C  CB  . TYR   A 1 125 ? -26.52100 -1.31800  7.36600   1.000 63.13392  ? 161 TYR   A CB  1 
ATOM   991  C  CG  . TYR   A 1 125 ? -26.78900 -0.10900  8.22100   1.000 66.85213  ? 161 TYR   A CG  1 
ATOM   992  C  CD1 . TYR   A 1 125 ? -26.24000 1.12800   7.90500   1.000 48.70680  ? 161 TYR   A CD1 1 
ATOM   993  C  CD2 . TYR   A 1 125 ? -27.59400 -0.20100  9.34200   1.000 69.73064  ? 161 TYR   A CD2 1 
ATOM   994  C  CE1 . TYR   A 1 125 ? -26.48900 2.23700   8.69100   1.000 63.84389  ? 161 TYR   A CE1 1 
ATOM   995  C  CE2 . TYR   A 1 125 ? -27.84800 0.89700   10.12600  1.000 77.09325  ? 161 TYR   A CE2 1 
ATOM   996  C  CZ  . TYR   A 1 125 ? -27.29500 2.11100   9.80200   1.000 70.72014  ? 161 TYR   A CZ  1 
ATOM   997  O  OH  . TYR   A 1 125 ? -27.56300 3.19300   10.60400  1.000 71.32697  ? 161 TYR   A OH  1 
ATOM   998  N  N   . ARG   A 1 126 ? -25.51000 -3.59500  9.23000   1.000 60.98427  ? 162 ARG   A N   1 
ATOM   999  C  CA  . ARG   A 1 126 ? -25.35100 -4.31200  10.50100  1.000 70.15377  ? 162 ARG   A CA  1 
ATOM   1000 C  C   . ARG   A 1 126 ? -25.84000 -3.51600  11.71100  1.000 80.49961  ? 162 ARG   A C   1 
ATOM   1001 O  O   . ARG   A 1 126 ? -25.33600 -3.70400  12.82100  1.000 95.27048  ? 162 ARG   A O   1 
ATOM   1002 C  CB  . ARG   A 1 126 ? -23.89800 -4.75200  10.72500  1.000 83.87081  ? 162 ARG   A CB  1 
ATOM   1003 C  CG  . ARG   A 1 126 ? -23.36700 -5.68900  9.65500   1.000 82.89045  ? 162 ARG   A CG  1 
ATOM   1004 C  CD  . ARG   A 1 126 ? -21.92100 -6.08700  9.90600   1.000 82.19040  ? 162 ARG   A CD  1 
ATOM   1005 N  NE  . ARG   A 1 126 ? -21.22000 -5.14000  10.76400  1.000 89.45592  ? 162 ARG   A NE  1 
ATOM   1006 C  CZ  . ARG   A 1 126 ? -20.59800 -5.46700  11.88900  1.000 93.46990  ? 162 ARG   A CZ  1 
ATOM   1007 N  NH1 . ARG   A 1 126 ? -20.54600 -6.72000  12.31100  1.000 97.92906  ? 162 ARG   A NH1 1 
ATOM   1008 N  NH2 . ARG   A 1 126 ? -20.00000 -4.51600  12.60100  1.000 89.22798  ? 162 ARG   A NH2 1 
ATOM   1009 N  N   . ASP   A 1 127 ? -26.83300 -2.64400  11.53500  1.000 79.66553  ? 163 ASP   A N   1 
ATOM   1010 C  CA  . ASP   A 1 127 ? -27.39600 -1.92800  12.67500  1.000 80.37005  ? 163 ASP   A CA  1 
ATOM   1011 C  C   . ASP   A 1 127 ? -28.74600 -1.32700  12.31100  1.000 72.90610  ? 163 ASP   A C   1 
ATOM   1012 O  O   . ASP   A 1 127 ? -29.05100 -0.19200  12.69000  1.000 65.68453  ? 163 ASP   A O   1 
ATOM   1013 C  CB  . ASP   A 1 127 ? -26.43400 -0.83600  13.15500  1.000 83.25297  ? 163 ASP   A CB  1 
ATOM   1014 C  CG  . ASP   A 1 127 ? -26.72100 -0.38600  14.57800  1.000 77.57776  ? 163 ASP   A CG  1 
ATOM   1015 O  OD1 . ASP   A 1 127 ? -27.61600 -0.96800  15.22500  1.000 75.08994  ? 163 ASP   A OD1 1 
ATOM   1016 O  OD2 . ASP   A 1 127 ? -26.04700 0.55300   15.05000  1.000 97.99462  ? 163 ASP   A OD2 1 
ATOM   1017 N  N   . ILE   A 1 128 ? -29.55700 -2.08300  11.57300  1.000 67.12151  ? 164 ILE   A N   1 
ATOM   1018 C  CA  . ILE   A 1 128 ? -30.83200 -1.57600  11.07800  1.000 58.13273  ? 164 ILE   A CA  1 
ATOM   1019 C  C   . ILE   A 1 128 ? -31.75900 -1.30400  12.25600  1.000 64.84920  ? 164 ILE   A C   1 
ATOM   1020 O  O   . ILE   A 1 128 ? -32.06000 -2.20300  13.05000  1.000 49.74715  ? 164 ILE   A O   1 
ATOM   1021 C  CB  . ILE   A 1 128 ? -31.46600 -2.56100  10.08900  1.000 41.11982  ? 164 ILE   A CB  1 
ATOM   1022 C  CG1 . ILE   A 1 128 ? -30.63000 -2.65000  8.80900   1.000 60.16806  ? 164 ILE   A CG1 1 
ATOM   1023 C  CG2 . ILE   A 1 128 ? -32.89600 -2.15100  9.77400   1.000 65.00741  ? 164 ILE   A CG2 1 
ATOM   1024 C  CD1 . ILE   A 1 128 ? -30.62800 -1.37800  7.99000   1.000 49.16813  ? 164 ILE   A CD1 1 
ATOM   1025 N  N   . LYS   A 1 129 ? -32.20900 -0.05600  12.37500  1.000 50.95580  ? 165 LYS   A N   1 
ATOM   1026 C  CA  . LYS   A 1 129 ? -33.18600 0.33400   13.38100  1.000 59.69426  ? 165 LYS   A CA  1 
ATOM   1027 C  C   . LYS   A 1 129 ? -33.81700 1.64600   12.94600  1.000 61.02182  ? 165 LYS   A C   1 
ATOM   1028 O  O   . LYS   A 1 129 ? -33.15000 2.46100   12.29900  1.000 58.07268  ? 165 LYS   A O   1 
ATOM   1029 C  CB  . LYS   A 1 129 ? -32.54100 0.48200   14.76800  1.000 47.20052  ? 165 LYS   A CB  1 
ATOM   1030 C  CG  . LYS   A 1 129 ? -31.42000 1.50400   14.84700  1.000 66.09356  ? 165 LYS   A CG  1 
ATOM   1031 C  CD  . LYS   A 1 129 ? -31.16300 1.89800   16.29200  1.000 70.07562  ? 165 LYS   A CD  1 
ATOM   1032 C  CE  . LYS   A 1 129 ? -29.67900 1.94700   16.61000  1.000 76.23087  ? 165 LYS   A CE  1 
ATOM   1033 N  NZ  . LYS   A 1 129 ? -29.44200 2.37200   18.01800  1.000 73.52518  ? 165 LYS   A NZ  1 
ATOM   1034 N  N   . PRO   A 1 130 ? -35.09000 1.87900   13.27400  1.000 56.95679  ? 166 PRO   A N   1 
ATOM   1035 C  CA  . PRO   A 1 130 ? -35.73100 3.13800   12.86100  1.000 64.55317  ? 166 PRO   A CA  1 
ATOM   1036 C  C   . PRO   A 1 130 ? -35.09900 4.37100   13.47900  1.000 61.28745  ? 166 PRO   A C   1 
ATOM   1037 O  O   . PRO   A 1 130 ? -35.26100 5.47100   12.93500  1.000 55.31779  ? 166 PRO   A O   1 
ATOM   1038 C  CB  . PRO   A 1 130 ? -37.18300 2.96000   13.32500  1.000 48.19792  ? 166 PRO   A CB  1 
ATOM   1039 C  CG  . PRO   A 1 130 ? -37.09900 1.96800   14.44000  1.000 61.56277  ? 166 PRO   A CG  1 
ATOM   1040 C  CD  . PRO   A 1 130 ? -36.00200 1.02300   14.05000  1.000 47.41271  ? 166 PRO   A CD  1 
ATOM   1041 N  N   . ASP   A 1 131 ? -34.38100 4.22300   14.59500  1.000 48.29093  ? 167 ASP   A N   1 
ATOM   1042 C  CA  . ASP   A 1 131 ? -33.72900 5.36300   15.22700  1.000 62.06279  ? 167 ASP   A CA  1 
ATOM   1043 C  C   . ASP   A 1 131 ? -32.67700 5.99400   14.32600  1.000 61.83967  ? 167 ASP   A C   1 
ATOM   1044 O  O   . ASP   A 1 131 ? -32.37000 7.18000   14.48600  1.000 52.52681  ? 167 ASP   A O   1 
ATOM   1045 C  CB  . ASP   A 1 131 ? -33.08500 4.93800   16.55100  1.000 66.92450  ? 167 ASP   A CB  1 
ATOM   1046 C  CG  . ASP   A 1 131 ? -34.03600 4.15800   17.44500  1.000 72.64523  ? 167 ASP   A CG  1 
ATOM   1047 O  OD1 . ASP   A 1 131 ? -34.38600 3.01200   17.09300  1.000 65.19307  ? 167 ASP   A OD1 1 
ATOM   1048 O  OD2 . ASP   A 1 131 ? -34.42300 4.68600   18.50800  1.000 81.29879  ? 167 ASP   A OD2 1 
ATOM   1049 N  N   . ASN   A 1 132 ? -32.12200 5.23300   13.38300  1.000 53.69070  ? 168 ASN   A N   1 
ATOM   1050 C  CA  . ASN   A 1 132 ? -31.09800 5.72700   12.47300  1.000 60.09626  ? 168 ASN   A CA  1 
ATOM   1051 C  C   . ASN   A 1 132 ? -31.66000 6.19800   11.13900  1.000 61.44005  ? 168 ASN   A C   1 
ATOM   1052 O  O   . ASN   A 1 132 ? -30.88700 6.61000   10.26800  1.000 65.06317  ? 168 ASN   A O   1 
ATOM   1053 C  CB  . ASN   A 1 132 ? -30.03900 4.64500   12.23400  1.000 58.59414  ? 168 ASN   A CB  1 
ATOM   1054 C  CG  . ASN   A 1 132 ? -29.27200 4.29400   13.49400  1.000 69.38759  ? 168 ASN   A CG  1 
ATOM   1055 O  OD1 . ASN   A 1 132 ? -29.17800 5.09800   14.42100  1.000 77.64909  ? 168 ASN   A OD1 1 
ATOM   1056 N  ND2 . ASN   A 1 132 ? -28.71400 3.08900   13.53200  1.000 54.13274  ? 168 ASN   A ND2 1 
ATOM   1057 N  N   . PHE   A 1 133 ? -32.97600 6.14500   10.95200  1.000 51.34873  ? 169 PHE   A N   1 
ATOM   1058 C  CA  . PHE   A 1 133 ? -33.63000 6.65200   9.75200   1.000 55.30128  ? 169 PHE   A CA  1 
ATOM   1059 C  C   . PHE   A 1 133 ? -34.34000 7.95200   10.10100  1.000 49.86991  ? 169 PHE   A C   1 
ATOM   1060 O  O   . PHE   A 1 133 ? -35.28300 7.95000   10.89900  1.000 58.42544  ? 169 PHE   A O   1 
ATOM   1061 C  CB  . PHE   A 1 133 ? -34.62100 5.63300   9.18900   1.000 58.00903  ? 169 PHE   A CB  1 
ATOM   1062 C  CG  . PHE   A 1 133 ? -33.97400 4.41100   8.60400   1.000 63.31362  ? 169 PHE   A CG  1 
ATOM   1063 C  CD1 . PHE   A 1 133 ? -33.61500 3.34600   9.41100   1.000 59.05410  ? 169 PHE   A CD1 1 
ATOM   1064 C  CD2 . PHE   A 1 133 ? -33.73300 4.32200   7.24300   1.000 59.56259  ? 169 PHE   A CD2 1 
ATOM   1065 C  CE1 . PHE   A 1 133 ? -33.02300 2.21700   8.87600   1.000 52.27891  ? 169 PHE   A CE1 1 
ATOM   1066 C  CE2 . PHE   A 1 133 ? -33.14100 3.19600   6.70100   1.000 62.39230  ? 169 PHE   A CE2 1 
ATOM   1067 C  CZ  . PHE   A 1 133 ? -32.78600 2.14300   7.51800   1.000 49.08491  ? 169 PHE   A CZ  1 
ATOM   1068 N  N   . LEU   A 1 134 ? -33.89200 9.05400   9.50700   1.000 52.20590  ? 170 LEU   A N   1 
ATOM   1069 C  CA  . LEU   A 1 134 ? -34.43400 10.37200  9.79700   1.000 46.05911  ? 170 LEU   A CA  1 
ATOM   1070 C  C   . LEU   A 1 134 ? -35.02000 10.98800  8.53500   1.000 49.08822  ? 170 LEU   A C   1 
ATOM   1071 O  O   . LEU   A 1 134 ? -34.55900 10.72100  7.42300   1.000 53.62971  ? 170 LEU   A O   1 
ATOM   1072 C  CB  . LEU   A 1 134 ? -33.35800 11.31300  10.36300  1.000 38.28131  ? 170 LEU   A CB  1 
ATOM   1073 C  CG  . LEU   A 1 134 ? -32.20700 10.73500  11.19000  1.000 56.66069  ? 170 LEU   A CG  1 
ATOM   1074 C  CD1 . LEU   A 1 134 ? -31.24900 11.84600  11.59500  1.000 71.63223  ? 170 LEU   A CD1 1 
ATOM   1075 C  CD2 . LEU   A 1 134 ? -32.71300 9.99700   12.41600  1.000 67.10030  ? 170 LEU   A CD2 1 
ATOM   1076 N  N   . ILE   A 1 135 ? -36.04200 11.82500  8.71700   1.000 51.80546  ? 171 ILE   A N   1 
ATOM   1077 C  CA  . ILE   A 1 135 ? -36.57200 12.62700  7.62100   1.000 57.30532  ? 171 ILE   A CA  1 
ATOM   1078 C  C   . ILE   A 1 135 ? -35.71200 13.87500  7.48400   1.000 66.43213  ? 171 ILE   A C   1 
ATOM   1079 O  O   . ILE   A 1 135 ? -34.67500 14.00300  8.14400   1.000 51.51346  ? 171 ILE   A O   1 
ATOM   1080 C  CB  . ILE   A 1 135 ? -38.05000 12.99800  7.84200   1.000 72.86257  ? 171 ILE   A CB  1 
ATOM   1081 C  CG1 . ILE   A 1 135 ? -38.25800 13.55400  9.25200   1.000 70.17217  ? 171 ILE   A CG1 1 
ATOM   1082 C  CG2 . ILE   A 1 135 ? -38.95100 11.79900  7.58000   1.000 57.14467  ? 171 ILE   A CG2 1 
ATOM   1083 C  CD1 . ILE   A 1 135 ? -39.66400 14.04200  9.51300   1.000 65.10517  ? 171 ILE   A CD1 1 
ATOM   1084 N  N   . GLY   A 1 136 ? -36.13300 14.79900  6.63100   1.000 80.36033  ? 172 GLY   A N   1 
ATOM   1085 C  CA  . GLY   A 1 136 ? -35.43700 16.05300  6.44400   1.000 79.20456  ? 172 GLY   A CA  1 
ATOM   1086 C  C   . GLY   A 1 136 ? -35.93400 17.13000  7.38200   1.000 88.86007  ? 172 GLY   A C   1 
ATOM   1087 O  O   . GLY   A 1 136 ? -36.62500 16.86700  8.37000   1.000 90.71430  ? 172 GLY   A O   1 
ATOM   1088 N  N   . ARG   A 1 137 ? -35.57100 18.36500  7.06300   1.000 93.98738  ? 173 ARG   A N   1 
ATOM   1089 C  CA  . ARG   A 1 137 ? -35.97700 19.51700  7.84800   1.000 99.55296  ? 173 ARG   A CA  1 
ATOM   1090 C  C   . ARG   A 1 137 ? -37.19800 20.18600  7.23400   1.000 105.00859 ? 173 ARG   A C   1 
ATOM   1091 O  O   . ARG   A 1 137 ? -37.49100 20.04400  6.04500   1.000 107.66624 ? 173 ARG   A O   1 
ATOM   1092 C  CB  . ARG   A 1 137 ? -34.83800 20.53000  7.97100   1.000 101.23117 ? 173 ARG   A CB  1 
ATOM   1093 C  CG  . ARG   A 1 137 ? -33.89700 20.24800  9.12400   1.000 89.77634  ? 173 ARG   A CG  1 
ATOM   1094 C  CD  . ARG   A 1 137 ? -33.43400 21.54200  9.76500   1.000 91.50592  ? 173 ARG   A CD  1 
ATOM   1095 N  NE  . ARG   A 1 137 ? -33.29400 21.41100  11.20900  1.000 94.22745  ? 173 ARG   A NE  1 
ATOM   1096 C  CZ  . ARG   A 1 137 ? -33.10100 22.42900  12.03700  1.000 106.86590 ? 173 ARG   A CZ  1 
ATOM   1097 N  NH1 . ARG   A 1 137 ? -33.02100 23.67300  11.59400  1.000 94.38977  ? 173 ARG   A NH1 1 
ATOM   1098 N  NH2 . ARG   A 1 137 ? -32.99200 22.19300  13.34100  1.000 105.46533 ? 173 ARG   A NH2 1 
ATOM   1099 N  N   . ARG   A 1 138 ? -37.90300 20.93200  8.07700   1.000 111.65860 ? 174 ARG   A N   1 
ATOM   1100 C  CA  . ARG   A 1 138 ? -39.10400 21.62700  7.64600   1.000 112.17450 ? 174 ARG   A CA  1 
ATOM   1101 C  C   . ARG   A 1 138 ? -38.78900 22.64300  6.55400   1.000 111.00318 ? 174 ARG   A C   1 
ATOM   1102 O  O   . ARG   A 1 138 ? -37.76600 23.33200  6.59600   1.000 117.31397 ? 174 ARG   A O   1 
ATOM   1103 C  CB  . ARG   A 1 138 ? -39.75500 22.30800  8.84800   1.000 124.07708 ? 174 ARG   A CB  1 
ATOM   1104 C  CG  . ARG   A 1 138 ? -40.83700 21.46900  9.48800   1.000 119.45412 ? 174 ARG   A CG  1 
ATOM   1105 C  CD  . ARG   A 1 138 ? -42.11900 21.58800  8.66300   1.000 114.02049 ? 174 ARG   A CD  1 
ATOM   1106 N  NE  . ARG   A 1 138 ? -43.12300 20.61100  9.06300   1.000 119.04369 ? 174 ARG   A NE  1 
ATOM   1107 C  CZ  . ARG   A 1 138 ? -44.29200 20.44900  8.45800   1.000 126.87461 ? 174 ARG   A CZ  1 
ATOM   1108 N  NH1 . ARG   A 1 138 ? -44.66700 21.22900  7.45600   1.000 123.92132 ? 174 ARG   A NH1 1 
ATOM   1109 N  NH2 . ARG   A 1 138 ? -45.10200 19.47300  8.86300   1.000 117.51284 ? 174 ARG   A NH2 1 
ATOM   1110 N  N   . GLY   A 1 139 ? -39.67500 22.72000  5.56100   1.000 111.69503 ? 175 GLY   A N   1 
ATOM   1111 C  CA  . GLY   A 1 139 ? -39.51900 23.64300  4.45700   1.000 125.88245 ? 175 GLY   A CA  1 
ATOM   1112 C  C   . GLY   A 1 139 ? -38.52800 23.22900  3.39100   1.000 123.19691 ? 175 GLY   A C   1 
ATOM   1113 O  O   . GLY   A 1 139 ? -38.41800 23.92400  2.37200   1.000 127.13303 ? 175 GLY   A O   1 
ATOM   1114 N  N   . ALA   A 1 140 ? -37.80400 22.13200  3.58200   1.000 119.26593 ? 176 ALA   A N   1 
ATOM   1115 C  CA  . ALA   A 1 140 ? -36.83000 21.66800  2.60600   1.000 119.98756 ? 176 ALA   A CA  1 
ATOM   1116 C  C   . ALA   A 1 140 ? -37.49100 20.75900  1.57400   1.000 125.20852 ? 176 ALA   A C   1 
ATOM   1117 O  O   . ALA   A 1 140 ? -38.60000 20.25600  1.76900   1.000 121.67252 ? 176 ALA   A O   1 
ATOM   1118 C  CB  . ALA   A 1 140 ? -35.68400 20.93000  3.29800   1.000 110.13100 ? 176 ALA   A CB  1 
ATOM   1119 N  N   . THR   A 1 141 ? -36.78600 20.55200  0.45900   1.000 126.64867 ? 177 THR   A N   1 
ATOM   1120 C  CA  . THR   A 1 141 ? -37.31900 19.70900  -0.60700  1.000 138.61176 ? 177 THR   A CA  1 
ATOM   1121 C  C   . THR   A 1 141 ? -37.33900 18.23900  -0.20500  1.000 134.78968 ? 177 THR   A C   1 
ATOM   1122 O  O   . THR   A 1 141 ? -38.19100 17.47900  -0.68000  1.000 148.02931 ? 177 THR   A O   1 
ATOM   1123 C  CB  . THR   A 1 141 ? -36.50400 19.90200  -1.88600  1.000 146.35403 ? 177 THR   A CB  1 
ATOM   1124 O  OG1 . THR   A 1 141 ? -36.22600 21.29700  -2.07100  1.000 136.62378 ? 177 THR   A OG1 1 
ATOM   1125 C  CG2 . THR   A 1 141 ? -37.27400 19.39100  -3.09500  1.000 142.40519 ? 177 THR   A CG2 1 
ATOM   1126 N  N   . ASP   A 1 142 ? -36.41800 17.82100  0.66000   1.000 114.18782 ? 178 ASP   A N   1 
ATOM   1127 C  CA  . ASP   A 1 142 ? -36.38800 16.46700  1.21000   1.000 97.66595  ? 178 ASP   A CA  1 
ATOM   1128 C  C   . ASP   A 1 142 ? -36.93400 16.43000  2.63000   1.000 93.64789  ? 178 ASP   A C   1 
ATOM   1129 O  O   . ASP   A 1 142 ? -36.41800 15.70700  3.48900   1.000 95.10457  ? 178 ASP   A O   1 
ATOM   1130 C  CB  . ASP   A 1 142 ? -34.96900 15.91400  1.16500   1.000 104.63394 ? 178 ASP   A CB  1 
ATOM   1131 C  CG  . ASP   A 1 142 ? -33.93200 16.94800  1.55700   1.000 110.48630 ? 178 ASP   A CG  1 
ATOM   1132 O  OD1 . ASP   A 1 142 ? -33.95600 17.41100  2.71600   1.000 97.28051  ? 178 ASP   A OD1 1 
ATOM   1133 O  OD2 . ASP   A 1 142 ? -33.09300 17.29800  0.70000   1.000 105.97888 ? 178 ASP   A OD2 1 
ATOM   1134 N  N   . GLU   A 1 143 ? -37.98800 17.20900  2.88900   1.000 96.07320  ? 179 GLU   A N   1 
ATOM   1135 C  CA  . GLU   A 1 143 ? -38.50400 17.34900  4.24700   1.000 97.23023  ? 179 GLU   A CA  1 
ATOM   1136 C  C   . GLU   A 1 143 ? -39.05300 16.03100  4.77500   1.000 96.25459  ? 179 GLU   A C   1 
ATOM   1137 O  O   . GLU   A 1 143 ? -38.87400 15.70700  5.95400   1.000 99.70772  ? 179 GLU   A O   1 
ATOM   1138 C  CB  . GLU   A 1 143 ? -39.58200 18.43300  4.28100   1.000 109.79624 ? 179 GLU   A CB  1 
ATOM   1139 C  CG  . GLU   A 1 143 ? -40.33700 18.56000  5.59600   1.000 111.03460 ? 179 GLU   A CG  1 
ATOM   1140 C  CD  . GLU   A 1 143 ? -41.54300 19.46800  5.46200   1.000 116.36530 ? 179 GLU   A CD  1 
ATOM   1141 O  OE1 . GLU   A 1 143 ? -41.45700 20.47700  4.72900   1.000 110.03992 ? 179 GLU   A OE1 1 
ATOM   1142 O  OE2 . GLU   A 1 143 ? -42.59100 19.16300  6.06700   1.000 130.75441 ? 179 GLU   A OE2 1 
ATOM   1143 N  N   . ASN   A 1 144 ? -39.71500 15.25100  3.92000   1.000 85.08390  ? 180 ASN   A N   1 
ATOM   1144 C  CA  . ASN   A 1 144 ? -40.35500 14.01200  4.34600   1.000 89.10443  ? 180 ASN   A CA  1 
ATOM   1145 C  C   . ASN   A 1 144 ? -39.78600 12.78700  3.63800   1.000 86.53603  ? 180 ASN   A C   1 
ATOM   1146 O  O   . ASN   A 1 144 ? -40.41100 11.72200  3.65100   1.000 72.09258  ? 180 ASN   A O   1 
ATOM   1147 C  CB  . ASN   A 1 144 ? -41.86800 14.09700  4.14100   1.000 74.02760  ? 180 ASN   A CB  1 
ATOM   1148 C  CG  . ASN   A 1 144 ? -42.54400 14.97300  5.17800   1.000 91.38141  ? 180 ASN   A CG  1 
ATOM   1149 O  OD1 . ASN   A 1 144 ? -42.35700 14.78500  6.38100   1.000 80.38980  ? 180 ASN   A OD1 1 
ATOM   1150 N  ND2 . ASN   A 1 144 ? -43.32200 15.94500  4.71700   1.000 98.27759  ? 180 ASN   A ND2 1 
ATOM   1151 N  N   . ASN   A 1 145 ? -38.61600 12.91300  3.02200   1.000 87.71140  ? 181 ASN   A N   1 
ATOM   1152 C  CA  . ASN   A 1 145 ? -37.92400 11.75100  2.48900   1.000 78.81663  ? 181 ASN   A CA  1 
ATOM   1153 C  C   . ASN   A 1 145 ? -37.12400 11.07000  3.59200   1.000 74.82593  ? 181 ASN   A C   1 
ATOM   1154 O  O   . ASN   A 1 145 ? -36.70600 11.70200  4.56600   1.000 71.22785  ? 181 ASN   A O   1 
ATOM   1155 C  CB  . ASN   A 1 145 ? -37.00200 12.14900  1.33700   1.000 78.39866  ? 181 ASN   A CB  1 
ATOM   1156 C  CG  . ASN   A 1 145 ? -37.76400 12.49900  0.07400   1.000 89.48791  ? 181 ASN   A CG  1 
ATOM   1157 O  OD1 . ASN   A 1 145 ? -38.89400 12.05100  -0.12600  1.000 91.25380  ? 181 ASN   A OD1 1 
ATOM   1158 N  ND2 . ASN   A 1 145 ? -37.14600 13.29600  -0.78900  1.000 88.93521  ? 181 ASN   A ND2 1 
ATOM   1159 N  N   . VAL   A 1 146 ? -36.91700 9.76800   3.43400   1.000 72.41980  ? 182 VAL   A N   1 
ATOM   1160 C  CA  . VAL   A 1 146 ? -36.22200 8.96400   4.43200   1.000 61.64320  ? 182 VAL   A CA  1 
ATOM   1161 C  C   . VAL   A 1 146 ? -34.72900 8.98100   4.13500   1.000 71.59129  ? 182 VAL   A C   1 
ATOM   1162 O  O   . VAL   A 1 146 ? -34.30900 8.78000   2.98900   1.000 70.46015  ? 182 VAL   A O   1 
ATOM   1163 C  CB  . VAL   A 1 146 ? -36.76600 7.52600   4.45600   1.000 74.46171  ? 182 VAL   A CB  1 
ATOM   1164 C  CG1 . VAL   A 1 146 ? -36.00500 6.68400   5.46800   1.000 70.10766  ? 182 VAL   A CG1 1 
ATOM   1165 C  CG2 . VAL   A 1 146 ? -38.25400 7.52900   4.77400   1.000 62.07594  ? 182 VAL   A CG2 1 
ATOM   1166 N  N   . HIS   A 1 147 ? -33.92700 9.22100   5.17000   1.000 69.18532  ? 183 HIS   A N   1 
ATOM   1167 C  CA  . HIS   A 1 147 ? -32.47700 9.26300   5.07600   1.000 66.96844  ? 183 HIS   A CA  1 
ATOM   1168 C  C   . HIS   A 1 147 ? -31.87600 8.18800   5.97500   1.000 62.13615  ? 183 HIS   A C   1 
ATOM   1169 O  O   . HIS   A 1 147 ? -32.52300 7.69000   6.90000   1.000 55.75501  ? 183 HIS   A O   1 
ATOM   1170 C  CB  . HIS   A 1 147 ? -31.93200 10.64400  5.47400   1.000 64.00290  ? 183 HIS   A CB  1 
ATOM   1171 C  CG  . HIS   A 1 147 ? -32.52400 11.78000  4.69600   1.000 70.19451  ? 183 HIS   A CG  1 
ATOM   1172 N  ND1 . HIS   A 1 147 ? -33.82300 12.20500  4.86900   1.000 73.14341  ? 183 HIS   A ND1 1 
ATOM   1173 C  CD2 . HIS   A 1 147 ? -31.98900 12.58400  3.74700   1.000 73.82778  ? 183 HIS   A CD2 1 
ATOM   1174 C  CE1 . HIS   A 1 147 ? -34.06500 13.21900  4.05700   1.000 73.43913  ? 183 HIS   A CE1 1 
ATOM   1175 N  NE2 . HIS   A 1 147 ? -32.96800 13.46900  3.36600   1.000 82.87587  ? 183 HIS   A NE2 1 
ATOM   1176 N  N   . LEU   A 1 148 ? -30.62300 7.83300   5.69500   1.000 61.22181  ? 184 LEU   A N   1 
ATOM   1177 C  CA  . LEU   A 1 148 ? -29.89700 6.83300   6.46900   1.000 56.70898  ? 184 LEU   A CA  1 
ATOM   1178 C  C   . LEU   A 1 148 ? -28.59500 7.44200   6.96800   1.000 68.86768  ? 184 LEU   A C   1 
ATOM   1179 O  O   . LEU   A 1 148 ? -27.83800 8.02200   6.18300   1.000 68.46994  ? 184 LEU   A O   1 
ATOM   1180 C  CB  . LEU   A 1 148 ? -29.61200 5.57800   5.63500   1.000 49.29722  ? 184 LEU   A CB  1 
ATOM   1181 C  CG  . LEU   A 1 148 ? -28.85400 4.45800   6.35200   1.000 57.67320  ? 184 LEU   A CG  1 
ATOM   1182 C  CD1 . LEU   A 1 148 ? -29.65800 3.94600   7.53700   1.000 67.21585  ? 184 LEU   A CD1 1 
ATOM   1183 C  CD2 . LEU   A 1 148 ? -28.52100 3.32500   5.39300   1.000 44.88970  ? 184 LEU   A CD2 1 
ATOM   1184 N  N   . ILE   A 1 149 ? -28.33600 7.30900   8.26800   1.000 67.06501  ? 185 ILE   A N   1 
ATOM   1185 C  CA  . ILE   A 1 149 ? -27.16600 7.89000   8.91100   1.000 71.00196  ? 185 ILE   A CA  1 
ATOM   1186 C  C   . ILE   A 1 149 ? -26.52100 6.83500   9.80400   1.000 74.12528  ? 185 ILE   A C   1 
ATOM   1187 O  O   . ILE   A 1 149 ? -26.97900 5.69300   9.87800   1.000 74.76409  ? 185 ILE   A O   1 
ATOM   1188 C  CB  . ILE   A 1 149 ? -27.51700 9.15000   9.72900   1.000 79.93433  ? 185 ILE   A CB  1 
ATOM   1189 C  CG1 . ILE   A 1 149 ? -28.52800 8.80600   10.82100  1.000 75.24784  ? 185 ILE   A CG1 1 
ATOM   1190 C  CG2 . ILE   A 1 149 ? -28.06600 10.24500  8.83100   1.000 98.67235  ? 185 ILE   A CG2 1 
ATOM   1191 C  CD1 . ILE   A 1 149 ? -27.94600 8.89500   12.22300  1.000 81.11480  ? 185 ILE   A CD1 1 
ATOM   1192 N  N   . ASP   A 1 150 ? -25.43900 7.23100   10.48300  1.000 64.68280  ? 186 ASP   A N   1 
ATOM   1193 C  CA  . ASP   A 1 150 ? -24.71800 6.39100   11.43900  1.000 64.89942  ? 186 ASP   A CA  1 
ATOM   1194 C  C   . ASP   A 1 150 ? -24.22300 5.09800   10.80300  1.000 67.56422  ? 186 ASP   A C   1 
ATOM   1195 O  O   . ASP   A 1 150 ? -24.95200 4.10200   10.75900  1.000 64.04514  ? 186 ASP   A O   1 
ATOM   1196 C  CB  . ASP   A 1 150 ? -25.60100 6.07500   12.65100  1.000 71.19239  ? 186 ASP   A CB  1 
ATOM   1197 C  CG  . ASP   A 1 150 ? -24.80300 5.57900   13.84900  1.000 70.00895  ? 186 ASP   A CG  1 
ATOM   1198 O  OD1 . ASP   A 1 150 ? -23.63700 5.16700   13.67700  1.000 66.47454  ? 186 ASP   A OD1 1 
ATOM   1199 O  OD2 . ASP   A 1 150 ? -25.35000 5.59800   14.97200  1.000 79.62697  ? 186 ASP   A OD2 1 
ATOM   1200 N  N   . PHE   A 1 151 ? -22.98000 5.09400   10.32300  1.000 63.26133  ? 187 PHE   A N   1 
ATOM   1201 C  CA  . PHE   A 1 151 ? -22.38700 3.91600   9.70200   1.000 71.25827  ? 187 PHE   A CA  1 
ATOM   1202 C  C   . PHE   A 1 151 ? -21.21700 3.38000   10.52000  1.000 72.41690  ? 187 PHE   A C   1 
ATOM   1203 O  O   . PHE   A 1 151 ? -20.30100 2.76300   9.97400   1.000 80.57780  ? 187 PHE   A O   1 
ATOM   1204 C  CB  . PHE   A 1 151 ? -21.95200 4.22200   8.27000   1.000 65.41033  ? 187 PHE   A CB  1 
ATOM   1205 C  CG  . PHE   A 1 151 ? -23.09600 4.50400   7.34300   1.000 70.63848  ? 187 PHE   A CG  1 
ATOM   1206 C  CD1 . PHE   A 1 151 ? -23.64900 5.77100   7.27100   1.000 68.75448  ? 187 PHE   A CD1 1 
ATOM   1207 C  CD2 . PHE   A 1 151 ? -23.62500 3.50000   6.55000   1.000 68.99705  ? 187 PHE   A CD2 1 
ATOM   1208 C  CE1 . PHE   A 1 151 ? -24.70600 6.03300   6.42300   1.000 72.56580  ? 187 PHE   A CE1 1 
ATOM   1209 C  CE2 . PHE   A 1 151 ? -24.68000 3.75500   5.70000   1.000 67.19288  ? 187 PHE   A CE2 1 
ATOM   1210 C  CZ  . PHE   A 1 151 ? -25.22200 5.02300   5.63600   1.000 74.20634  ? 187 PHE   A CZ  1 
ATOM   1211 N  N   . GLY   A 1 152 ? -21.24400 3.60100   11.83700  1.000 89.03176  ? 188 GLY   A N   1 
ATOM   1212 C  CA  . GLY   A 1 152 ? -20.22800 3.04200   12.71200  1.000 94.65963  ? 188 GLY   A CA  1 
ATOM   1213 C  C   . GLY   A 1 152 ? -20.23600 1.52900   12.77900  1.000 97.02217  ? 188 GLY   A C   1 
ATOM   1214 O  O   . GLY   A 1 152 ? -19.26100 0.93400   13.25100  1.000 111.89428 ? 188 GLY   A O   1 
ATOM   1215 N  N   . MET   A 1 153 ? -21.31500 0.89600   12.32400  1.000 85.25396  ? 189 MET   A N   1 
ATOM   1216 C  CA  . MET   A 1 153 ? -21.42500 -0.55500  12.29000  1.000 80.35628  ? 189 MET   A CA  1 
ATOM   1217 C  C   . MET   A 1 153 ? -21.37700 -1.11500  10.87600  1.000 79.67199  ? 189 MET   A C   1 
ATOM   1218 O  O   . MET   A 1 153 ? -21.59800 -2.31500  10.69300  1.000 85.59688  ? 189 MET   A O   1 
ATOM   1219 C  CB  . MET   A 1 153 ? -22.72200 -0.99700  12.98000  1.000 88.95377  ? 189 MET   A CB  1 
ATOM   1220 C  CG  . MET   A 1 153 ? -22.73200 -0.77200  14.48700  1.000 97.20254  ? 189 MET   A CG  1 
ATOM   1221 S  SD  . MET   A 1 153 ? -21.75500 -2.00000  15.37300  1.000 110.59991 ? 189 MET   A SD  1 
ATOM   1222 C  CE  . MET   A 1 153 ? -21.35800 -1.09500  16.86700  1.000 115.99603 ? 189 MET   A CE  1 
ATOM   1223 N  N   . ALA   A 1 154 ? -21.09800 -0.28000  9.87700   1.000 66.92072  ? 190 ALA   A N   1 
ATOM   1224 C  CA  . ALA   A 1 154 ? -21.11900 -0.73000  8.49400   1.000 76.67811  ? 190 ALA   A CA  1 
ATOM   1225 C  C   . ALA   A 1 154 ? -19.93600 -1.64400  8.23700   1.000 79.35898  ? 190 ALA   A C   1 
ATOM   1226 O  O   . ALA   A 1 154 ? -18.83200 -1.41200  8.73000   1.000 79.81681  ? 190 ALA   A O   1 
ATOM   1227 C  CB  . ALA   A 1 154 ? -21.07700 0.45400   7.53400   1.000 64.16207  ? 190 ALA   A CB  1 
ATOM   1228 N  N   . LYS   A 1 155 ? -20.16100 -2.70300  7.47400   1.000 95.52717  ? 191 LYS   A N   1 
ATOM   1229 C  CA  . LYS   A 1 155 ? -19.07600 -3.62700  7.19600   1.000 89.29498  ? 191 LYS   A CA  1 
ATOM   1230 C  C   . LYS   A 1 155 ? -19.02500 -4.02000  5.73300   1.000 93.37088  ? 191 LYS   A C   1 
ATOM   1231 O  O   . LYS   A 1 155 ? -19.97400 -4.61000  5.19800   1.000 109.84154 ? 191 LYS   A O   1 
ATOM   1232 C  CB  . LYS   A 1 155 ? -19.16500 -4.86500  8.06900   1.000 89.88769  ? 191 LYS   A CB  1 
ATOM   1233 C  CG  . LYS   A 1 155 ? -17.82600 -5.50200  8.24200   1.000 91.68839  ? 191 LYS   A CG  1 
ATOM   1234 C  CD  . LYS   A 1 155 ? -18.01900 -6.84000  8.90700   1.000 95.25454  ? 191 LYS   A CD  1 
ATOM   1235 C  CE  . LYS   A 1 155 ? -16.74800 -7.39800  9.53400   1.000 106.97248 ? 191 LYS   A CE  1 
ATOM   1236 N  NZ  . LYS   A 1 155 ? -16.32000 -6.54700  10.67500  1.000 103.65188 ? 191 LYS   A NZ  1 
ATOM   1237 N  N   . GLN   A 1 156 ? -17.91000 -3.63500  5.11300   1.000 92.40073  ? 192 GLN   A N   1 
ATOM   1238 C  CA  . GLN   A 1 156 ? -17.39000 -4.25300  3.90500   1.000 88.70861  ? 192 GLN   A CA  1 
ATOM   1239 C  C   . GLN   A 1 156 ? -17.66900 -5.76100  3.85500   1.000 96.69734  ? 192 GLN   A C   1 
ATOM   1240 O  O   . GLN   A 1 156 ? -17.36100 -6.50100  4.79700   1.000 103.28799 ? 192 GLN   A O   1 
ATOM   1241 C  CB  . GLN   A 1 156 ? -15.88900 -3.98000  3.86900   1.000 107.27030 ? 192 GLN   A CB  1 
ATOM   1242 C  CG  . GLN   A 1 156 ? -15.12000 -4.51500  5.12000   1.000 118.16272 ? 192 GLN   A CG  1 
ATOM   1243 C  CD  . GLN   A 1 156 ? -14.81600 -3.49000  6.19200   1.000 117.79275 ? 192 GLN   A CD  1 
ATOM   1244 O  OE1 . GLN   A 1 156 ? -15.69300 -2.72000  6.62900   1.000 108.11991 ? 192 GLN   A OE1 1 
ATOM   1245 N  NE2 . GLN   A 1 156 ? -13.54200 -3.48000  6.63300   1.000 105.61110 ? 192 GLN   A NE2 1 
ATOM   1246 N  N   . TYR   A 1 157 ? -18.23400 -6.22500  2.72600   1.000 95.06251  ? 193 TYR   A N   1 
ATOM   1247 C  CA  . TYR   A 1 157 ? -18.55900 -7.64000  2.53900   1.000 86.57205  ? 193 TYR   A CA  1 
ATOM   1248 C  C   . TYR   A 1 157 ? -18.01300 -8.25900  1.25600   1.000 95.71014  ? 193 TYR   A C   1 
ATOM   1249 O  O   . TYR   A 1 157 ? -18.12700 -9.47800  1.09100   1.000 101.82839 ? 193 TYR   A O   1 
ATOM   1250 C  CB  . TYR   A 1 157 ? -20.08400 -7.85600  2.58100   1.000 77.48600  ? 193 TYR   A CB  1 
ATOM   1251 C  CG  . TYR   A 1 157 ? -20.81100 -7.43800  1.32100   1.000 92.34901  ? 193 TYR   A CG  1 
ATOM   1252 C  CD1 . TYR   A 1 157 ? -21.01600 -6.09800  1.03100   1.000 92.44718  ? 193 TYR   A CD1 1 
ATOM   1253 C  CD2 . TYR   A 1 157 ? -21.29700 -8.38400  0.42500   1.000 90.93916  ? 193 TYR   A CD2 1 
ATOM   1254 C  CE1 . TYR   A 1 157 ? -21.67900 -5.70800  -0.12100  1.000 84.95615  ? 193 TYR   A CE1 1 
ATOM   1255 C  CE2 . TYR   A 1 157 ? -21.95800 -8.00500  -0.72500  1.000 96.36359  ? 193 TYR   A CE2 1 
ATOM   1256 C  CZ  . TYR   A 1 157 ? -22.14700 -6.67200  -0.99600  1.000 94.03004  ? 193 TYR   A CZ  1 
ATOM   1257 O  OH  . TYR   A 1 157 ? -22.81000 -6.32900  -2.15300  1.000 88.14387  ? 193 TYR   A OH  1 
ATOM   1258 N  N   . ARG   A 1 158 ? -17.42800 -7.47400  0.35100   1.000 107.44087 ? 194 ARG   A N   1 
ATOM   1259 C  CA  . ARG   A 1 158 ? -16.86300 -8.01100  -0.88000  1.000 90.19651  ? 194 ARG   A CA  1 
ATOM   1260 C  C   . ARG   A 1 158 ? -15.75600 -7.08300  -1.35500  1.000 109.69151 ? 194 ARG   A C   1 
ATOM   1261 O  O   . ARG   A 1 158 ? -15.73800 -5.89600  -1.02100  1.000 111.06862 ? 194 ARG   A O   1 
ATOM   1262 C  CB  . ARG   A 1 158 ? -17.92100 -8.18800  -1.98200  1.000 98.94570  ? 194 ARG   A CB  1 
ATOM   1263 C  CG  . ARG   A 1 158 ? -18.51800 -6.89500  -2.50300  1.000 107.52964 ? 194 ARG   A CG  1 
ATOM   1264 C  CD  . ARG   A 1 158 ? -19.60200 -7.18100  -3.52700  1.000 97.52265  ? 194 ARG   A CD  1 
ATOM   1265 N  NE  . ARG   A 1 158 ? -20.12900 -5.95300  -4.10900  1.000 106.68478 ? 194 ARG   A NE  1 
ATOM   1266 C  CZ  . ARG   A 1 158 ? -21.13300 -5.89600  -4.97300  1.000 104.98856 ? 194 ARG   A CZ  1 
ATOM   1267 N  NH1 . ARG   A 1 158 ? -21.76000 -6.98700  -5.38100  1.000 103.48596 ? 194 ARG   A NH1 1 
ATOM   1268 N  NH2 . ARG   A 1 158 ? -21.52000 -4.71100  -5.43700  1.000 108.85404 ? 194 ARG   A NH2 1 
ATOM   1269 N  N   . ASP   A 1 159 ? -14.82300 -7.64600  -2.11600  1.000 121.97995 ? 195 ASP   A N   1 
ATOM   1270 C  CA  . ASP   A 1 159 ? -13.70700 -6.86700  -2.62500  1.000 129.91805 ? 195 ASP   A CA  1 
ATOM   1271 C  C   . ASP   A 1 159 ? -14.20900 -5.81600  -3.61000  1.000 135.67375 ? 195 ASP   A C   1 
ATOM   1272 O  O   . ASP   A 1 159 ? -15.08700 -6.09700  -4.42900  1.000 134.33318 ? 195 ASP   A O   1 
ATOM   1273 C  CB  . ASP   A 1 159 ? -12.68800 -7.77300  -3.31300  1.000 134.60887 ? 195 ASP   A CB  1 
ATOM   1274 C  CG  . ASP   A 1 159 ? -11.38900 -7.05900  -3.62100  1.000 139.87339 ? 195 ASP   A CG  1 
ATOM   1275 O  OD1 . ASP   A 1 159 ? -10.59900 -6.83900  -2.68100  1.000 139.40182 ? 195 ASP   A OD1 1 
ATOM   1276 O  OD2 . ASP   A 1 159 ? -11.15700 -6.71000  -4.79600  1.000 145.95437 ? 195 ASP   A OD2 1 
ATOM   1277 N  N   . PRO   A 1 160 ? -13.67500 -4.59700  -3.55000  1.000 149.49994 ? 196 PRO   A N   1 
ATOM   1278 C  CA  . PRO   A 1 160 ? -14.12700 -3.55500  -4.48100  1.000 148.84375 ? 196 PRO   A CA  1 
ATOM   1279 C  C   . PRO   A 1 160 ? -13.71800 -3.79900  -5.92500  1.000 171.83089 ? 196 PRO   A C   1 
ATOM   1280 O  O   . PRO   A 1 160 ? -14.27300 -3.14700  -6.81700  1.000 175.69009 ? 196 PRO   A O   1 
ATOM   1281 C  CB  . PRO   A 1 160 ? -13.47400 -2.28100  -3.92500  1.000 150.62414 ? 196 PRO   A CB  1 
ATOM   1282 C  CG  . PRO   A 1 160 ? -13.12200 -2.61000  -2.50000  1.000 147.08058 ? 196 PRO   A CG  1 
ATOM   1283 C  CD  . PRO   A 1 160 ? -12.78800 -4.06600  -2.50600  1.000 146.51797 ? 196 PRO   A CD  1 
ATOM   1284 N  N   . ARG   A 1 161 ? -12.77200 -4.70100  -6.19100  1.000 164.52546 ? 197 ARG   A N   1 
ATOM   1285 C  CA  . ARG   A 1 161 ? -12.30500 -4.92100  -7.55500  1.000 159.99127 ? 197 ARG   A CA  1 
ATOM   1286 C  C   . ARG   A 1 161 ? -12.59200 -6.31100  -8.09500  1.000 159.63594 ? 197 ARG   A C   1 
ATOM   1287 O  O   . ARG   A 1 161 ? -12.80700 -6.45200  -9.30000  1.000 167.27468 ? 197 ARG   A O   1 
ATOM   1288 C  CB  . ARG   A 1 161 ? -10.80000 -4.63400  -7.66200  1.000 162.06961 ? 197 ARG   A CB  1 
ATOM   1289 C  CG  . ARG   A 1 161 ? -10.42300 -3.15400  -7.50100  1.000 165.98378 ? 197 ARG   A CG  1 
ATOM   1290 C  CD  . ARG   A 1 161 ? -10.81100 -2.27900  -8.70900  1.000 173.23555 ? 197 ARG   A CD  1 
ATOM   1291 N  NE  . ARG   A 1 161 ? -12.24100 -2.29700  -8.99700  1.000 177.24993 ? 197 ARG   A NE  1 
ATOM   1292 C  CZ  . ARG   A 1 161 ? -12.87200 -1.41700  -9.76100  1.000 173.41523 ? 197 ARG   A CZ  1 
ATOM   1293 N  NH1 . ARG   A 1 161 ? -12.23900 -0.38600  -10.29900 1.000 167.80217 ? 197 ARG   A NH1 1 
ATOM   1294 N  NH2 . ARG   A 1 161 ? -14.17400 -1.57200  -9.99000  1.000 166.54643 ? 197 ARG   A NH2 1 
ATOM   1295 N  N   . THR   A 1 162 ? -12.60700 -7.33700  -7.24700  1.000 152.62475 ? 198 THR   A N   1 
ATOM   1296 C  CA  . THR   A 1 162 ? -12.99500 -8.67300  -7.67600  1.000 150.94677 ? 198 THR   A CA  1 
ATOM   1297 C  C   . THR   A 1 162 ? -14.44500 -8.99700  -7.34800  1.000 141.79891 ? 198 THR   A C   1 
ATOM   1298 O  O   . THR   A 1 162 ? -14.98100 -9.97500  -7.88200  1.000 140.37218 ? 198 THR   A O   1 
ATOM   1299 C  CB  . THR   A 1 162 ? -12.08600 -9.72900  -7.03700  1.000 155.04069 ? 198 THR   A CB  1 
ATOM   1300 O  OG1 . THR   A 1 162 ? -12.58300 -10.06500 -5.73700  1.000 148.48269 ? 198 THR   A OG1 1 
ATOM   1301 C  CG2 . THR   A 1 162 ? -10.66600 -9.19400  -6.90700  1.000 153.70599 ? 198 THR   A CG2 1 
ATOM   1302 N  N   . LYS   A 1 163 ? -15.08600 -8.19800  -6.49100  1.000 142.37717 ? 199 LYS   A N   1 
ATOM   1303 C  CA  . LYS   A 1 163 ? -16.47100 -8.41500  -6.07100  1.000 133.41572 ? 199 LYS   A CA  1 
ATOM   1304 C  C   . LYS   A 1 163 ? -16.67300 -9.80600  -5.47800  1.000 134.92863 ? 199 LYS   A C   1 
ATOM   1305 O  O   . LYS   A 1 163 ? -17.74200 -10.40400 -5.62000  1.000 142.59826 ? 199 LYS   A O   1 
ATOM   1306 C  CB  . LYS   A 1 163 ? -17.45100 -8.17500  -7.22300  1.000 130.24649 ? 199 LYS   A CB  1 
ATOM   1307 C  CG  . LYS   A 1 163 ? -18.09300 -6.79300  -7.22100  1.000 129.95286 ? 199 LYS   A CG  1 
ATOM   1308 C  CD  . LYS   A 1 163 ? -17.06900 -5.68900  -7.43100  1.000 144.58557 ? 199 LYS   A CD  1 
ATOM   1309 C  CE  . LYS   A 1 163 ? -16.40000 -5.80500  -8.79100  1.000 155.95544 ? 199 LYS   A CE  1 
ATOM   1310 N  NZ  . LYS   A 1 163 ? -15.45300 -4.68300  -9.03900  1.000 161.09032 ? 199 LYS   A NZ  1 
ATOM   1311 N  N   . GLN   A 1 164 ? -15.65200 -10.33100 -4.80700  1.000 131.76784 ? 200 GLN   A N   1 
ATOM   1312 C  CA  . GLN   A 1 164 ? -15.73600 -11.64200 -4.17800  1.000 126.37084 ? 200 GLN   A CA  1 
ATOM   1313 C  C   . GLN   A 1 164 ? -16.21900 -11.49900 -2.74100  1.000 115.08864 ? 200 GLN   A C   1 
ATOM   1314 O  O   . GLN   A 1 164 ? -15.63900 -10.74200 -1.95600  1.000 105.87179 ? 200 GLN   A O   1 
ATOM   1315 C  CB  . GLN   A 1 164 ? -14.38300 -12.35400 -4.21600  1.000 132.94684 ? 200 GLN   A CB  1 
ATOM   1316 C  CG  . GLN   A 1 164 ? -14.21000 -13.43400 -3.15200  1.000 140.26849 ? 200 GLN   A CG  1 
ATOM   1317 C  CD  . GLN   A 1 164 ? -15.20200 -14.57900 -3.28300  1.000 146.30686 ? 200 GLN   A CD  1 
ATOM   1318 O  OE1 . GLN   A 1 164 ? -15.91400 -14.69900 -4.28200  1.000 154.34623 ? 200 GLN   A OE1 1 
ATOM   1319 N  NE2 . GLN   A 1 164 ? -15.24800 -15.43300 -2.26800  1.000 147.63992 ? 200 GLN   A NE2 1 
ATOM   1320 N  N   . HIS   A 1 165 ? -17.27400 -12.23700 -2.40500  1.000 121.70690 ? 201 HIS   A N   1 
ATOM   1321 C  CA  . HIS   A 1 165 ? -17.86900 -12.17100 -1.07800  1.000 112.58702 ? 201 HIS   A CA  1 
ATOM   1322 C  C   . HIS   A 1 165 ? -16.87400 -12.63300 -0.01500  1.000 110.62870 ? 201 HIS   A C   1 
ATOM   1323 O  O   . HIS   A 1 165 ? -15.92600 -13.37600 -0.28800  1.000 112.47145 ? 201 HIS   A O   1 
ATOM   1324 C  CB  . HIS   A 1 165 ? -19.13000 -13.03500 -1.02600  1.000 109.47753 ? 201 HIS   A CB  1 
ATOM   1325 C  CG  . HIS   A 1 165 ? -20.18200 -12.52400 -0.09100  1.000 102.22379 ? 201 HIS   A CG  1 
ATOM   1326 N  ND1 . HIS   A 1 165 ? -20.04800 -12.56800 1.28000   1.000 103.59082 ? 201 HIS   A ND1 1 
ATOM   1327 C  CD2 . HIS   A 1 165 ? -21.39500 -11.97300 -0.33300  1.000 92.39708  ? 201 HIS   A CD2 1 
ATOM   1328 C  CE1 . HIS   A 1 165 ? -21.12900 -12.05700 1.84200   1.000 95.09526  ? 201 HIS   A CE1 1 
ATOM   1329 N  NE2 . HIS   A 1 165 ? -21.96200 -11.69000 0.88600   1.000 88.06519  ? 201 HIS   A NE2 1 
ATOM   1330 N  N   . ILE   A 1 166 ? -17.09900 -12.17600 1.21300   1.000 100.93855 ? 202 ILE   A N   1 
ATOM   1331 C  CA  . ILE   A 1 166 ? -16.29900 -12.60300 2.35700   1.000 107.55690 ? 202 ILE   A CA  1 
ATOM   1332 C  C   . ILE   A 1 166 ? -16.65900 -14.04900 2.67700   1.000 104.00901 ? 202 ILE   A C   1 
ATOM   1333 O  O   . ILE   A 1 166 ? -17.81300 -14.45700 2.47700   1.000 112.44223 ? 202 ILE   A O   1 
ATOM   1334 C  CB  . ILE   A 1 166 ? -16.52100 -11.69200 3.57500   1.000 82.72648  ? 202 ILE   A CB  1 
ATOM   1335 C  CG1 . ILE   A 1 166 ? -18.01300 -11.58400 3.89900   1.000 86.54413  ? 202 ILE   A CG1 1 
ATOM   1336 C  CG2 . ILE   A 1 166 ? -15.91500 -10.31600 3.33500   1.000 82.52296  ? 202 ILE   A CG2 1 
ATOM   1337 C  CD1 . ILE   A 1 166 ? -18.30900 -10.83100 5.17700   1.000 83.10332  ? 202 ILE   A CD1 1 
ATOM   1338 N  N   . PRO   A 1 167 ? -15.71700 -14.85800 3.15300   1.000 100.29492 ? 203 PRO   A N   1 
ATOM   1339 C  CA  . PRO   A 1 167 ? -16.04400 -16.24800 3.48200   1.000 105.55388 ? 203 PRO   A CA  1 
ATOM   1340 C  C   . PRO   A 1 167 ? -16.99700 -16.33700 4.66300   1.000 105.86389 ? 203 PRO   A C   1 
ATOM   1341 O  O   . PRO   A 1 167 ? -16.99500 -15.49400 5.56400   1.000 108.73983 ? 203 PRO   A O   1 
ATOM   1342 C  CB  . PRO   A 1 167 ? -14.68200 -16.86600 3.82000   1.000 105.42695 ? 203 PRO   A CB  1 
ATOM   1343 C  CG  . PRO   A 1 167 ? -13.68200 -15.97000 3.16000   1.000 107.29233 ? 203 PRO   A CG  1 
ATOM   1344 C  CD  . PRO   A 1 167 ? -14.27200 -14.59600 3.24400   1.000 101.12413 ? 203 PRO   A CD  1 
ATOM   1345 N  N   . TYR   A 1 168 ? -17.82400 -17.37600 4.64000   1.000 97.50808  ? 204 TYR   A N   1 
ATOM   1346 C  CA  . TYR   A 1 168 ? -18.74400 -17.63400 5.73700   1.000 89.93327  ? 204 TYR   A CA  1 
ATOM   1347 C  C   . TYR   A 1 168 ? -17.97500 -18.09400 6.97100   1.000 116.22638 ? 204 TYR   A C   1 
ATOM   1348 O  O   . TYR   A 1 168 ? -16.99800 -18.84100 6.87100   1.000 97.56914  ? 204 TYR   A O   1 
ATOM   1349 C  CB  . TYR   A 1 168 ? -19.76500 -18.69100 5.31200   1.000 90.62010  ? 204 TYR   A CB  1 
ATOM   1350 C  CG  . TYR   A 1 168 ? -20.75800 -19.11700 6.37300   1.000 88.69139  ? 204 TYR   A CG  1 
ATOM   1351 C  CD1 . TYR   A 1 168 ? -20.46300 -20.14600 7.25700   1.000 92.03015  ? 204 TYR   A CD1 1 
ATOM   1352 C  CD2 . TYR   A 1 168 ? -22.00600 -18.51600 6.46400   1.000 103.28373 ? 204 TYR   A CD2 1 
ATOM   1353 C  CE1 . TYR   A 1 168 ? -21.36900 -20.54900 8.21600   1.000 90.70432  ? 204 TYR   A CE1 1 
ATOM   1354 C  CE2 . TYR   A 1 168 ? -22.92300 -18.91500 7.42000   1.000 86.50500  ? 204 TYR   A CE2 1 
ATOM   1355 C  CZ  . TYR   A 1 168 ? -22.59600 -19.93300 8.29300   1.000 112.01862 ? 204 TYR   A CZ  1 
ATOM   1356 O  OH  . TYR   A 1 168 ? -23.49300 -20.34300 9.24900   1.000 108.17316 ? 204 TYR   A OH  1 
ATOM   1357 N  N   . ARG   A 1 169 ? -18.41400 -17.63300 8.14000   1.000 92.87377  ? 205 ARG   A N   1 
ATOM   1358 C  CA  . ARG   A 1 169 ? -17.82500 -18.06500 9.40100   1.000 115.22340 ? 205 ARG   A CA  1 
ATOM   1359 C  C   . ARG   A 1 169 ? -18.85900 -17.89900 10.50500  1.000 95.60224  ? 205 ARG   A C   1 
ATOM   1360 O  O   . ARG   A 1 169 ? -19.93400 -17.33100 10.29800  1.000 94.01480  ? 205 ARG   A O   1 
ATOM   1361 C  CB  . ARG   A 1 169 ? -16.54700 -17.28800 9.73200   1.000 122.40360 ? 205 ARG   A CB  1 
ATOM   1362 C  CG  . ARG   A 1 169 ? -16.74700 -15.79200 9.87000   1.000 112.37757 ? 205 ARG   A CG  1 
ATOM   1363 C  CD  . ARG   A 1 169 ? -15.66600 -15.16600 10.73700  1.000 109.46898 ? 205 ARG   A CD  1 
ATOM   1364 N  NE  . ARG   A 1 169 ? -15.81600 -15.53900 12.13900  1.000 123.65428 ? 205 ARG   A NE  1 
ATOM   1365 C  CZ  . ARG   A 1 169 ? -15.10400 -15.02600 13.13300  1.000 132.40269 ? 205 ARG   A CZ  1 
ATOM   1366 N  NH1 . ARG   A 1 169 ? -14.16900 -14.11500 12.91600  1.000 145.94526 ? 205 ARG   A NH1 1 
ATOM   1367 N  NH2 . ARG   A 1 169 ? -15.33900 -15.43300 14.37700  1.000 131.00592 ? 205 ARG   A NH2 1 
ATOM   1368 N  N   . GLU   A 1 170 ? -18.52000 -18.41300 11.68600  1.000 100.70837 ? 206 GLU   A N   1 
ATOM   1369 C  CA  . GLU   A 1 170 ? -19.41700 -18.37800 12.83500  1.000 90.09571  ? 206 GLU   A CA  1 
ATOM   1370 C  C   . GLU   A 1 170 ? -18.61700 -17.96100 14.06500  1.000 104.95699 ? 206 GLU   A C   1 
ATOM   1371 O  O   . GLU   A 1 170 ? -17.49000 -17.46700 13.96100  1.000 116.27869 ? 206 GLU   A O   1 
ATOM   1372 C  CB  . GLU   A 1 170 ? -20.10400 -19.73600 13.04000  1.000 105.37394 ? 206 GLU   A CB  1 
ATOM   1373 C  CG  . GLU   A 1 170 ? -20.72300 -20.30700 11.77900  1.000 105.80345 ? 206 GLU   A CG  1 
ATOM   1374 C  CD  . GLU   A 1 170 ? -21.74100 -21.38700 12.06100  1.000 124.75460 ? 206 GLU   A CD  1 
ATOM   1375 O  OE1 . GLU   A 1 170 ? -22.21000 -21.47100 13.21500  1.000 134.58725 ? 206 GLU   A OE1 1 
ATOM   1376 O  OE2 . GLU   A 1 170 ? -22.07100 -22.14400 11.12300  1.000 119.60700 ? 206 GLU   A OE2 1 
ATOM   1377 N  N   . LYS   A 1 171 ? -19.22200 -18.16200 15.23900  1.000 103.21326 ? 207 LYS   A N   1 
ATOM   1378 C  CA  . LYS   A 1 171 ? -18.59700 -17.87000 16.53100  1.000 113.64786 ? 207 LYS   A CA  1 
ATOM   1379 C  C   . LYS   A 1 171 ? -18.15500 -16.41000 16.62500  1.000 126.69434 ? 207 LYS   A C   1 
ATOM   1380 O  O   . LYS   A 1 171 ? -16.99700 -16.10200 16.91700  1.000 138.27984 ? 207 LYS   A O   1 
ATOM   1381 C  CB  . LYS   A 1 171 ? -17.42700 -18.81800 16.80400  1.000 130.65503 ? 207 LYS   A CB  1 
ATOM   1382 C  CG  . LYS   A 1 171 ? -17.69600 -19.80400 17.92700  1.000 131.72077 ? 207 LYS   A CG  1 
ATOM   1383 C  CD  . LYS   A 1 171 ? -18.07800 -19.07000 19.20200  1.000 137.26878 ? 207 LYS   A CD  1 
ATOM   1384 C  CE  . LYS   A 1 171 ? -18.63300 -20.02000 20.24800  1.000 142.82568 ? 207 LYS   A CE  1 
ATOM   1385 N  NZ  . LYS   A 1 171 ? -19.07000 -19.28800 21.46900  1.000 140.30723 ? 207 LYS   A NZ  1 
ATOM   1386 N  N   . LYS   A 1 172 ? -19.09700 -15.50400 16.38600  1.000 118.04664 ? 208 LYS   A N   1 
ATOM   1387 C  CA  . LYS   A 1 172 ? -18.84600 -14.07400 16.44700  1.000 128.85606 ? 208 LYS   A CA  1 
ATOM   1388 C  C   . LYS   A 1 172 ? -19.60200 -13.46000 17.61800  1.000 128.35592 ? 208 LYS   A C   1 
ATOM   1389 O  O   . LYS   A 1 172 ? -20.55900 -14.03700 18.14200  1.000 127.29692 ? 208 LYS   A O   1 
ATOM   1390 C  CB  . LYS   A 1 172 ? -19.25800 -13.38900 15.14100  1.000 122.35280 ? 208 LYS   A CB  1 
ATOM   1391 C  CG  . LYS   A 1 172 ? -18.96100 -14.20200 13.89600  1.000 125.21781 ? 208 LYS   A CG  1 
ATOM   1392 C  CD  . LYS   A 1 172 ? -19.40900 -13.46500 12.65000  1.000 114.92892 ? 208 LYS   A CD  1 
ATOM   1393 C  CE  . LYS   A 1 172 ? -18.56400 -12.23000 12.40800  1.000 114.53016 ? 208 LYS   A CE  1 
ATOM   1394 N  NZ  . LYS   A 1 172 ? -17.13200 -12.58100 12.21900  1.000 102.28965 ? 208 LYS   A NZ  1 
ATOM   1395 N  N   . SER   A 1 173 ? -19.15800 -12.27600 18.02700  1.000 130.11441 ? 209 SER   A N   1 
ATOM   1396 C  CA  . SER   A 1 173 ? -19.82800 -11.57300 19.11000  1.000 134.11736 ? 209 SER   A CA  1 
ATOM   1397 C  C   . SER   A 1 173 ? -21.13700 -10.96600 18.62000  1.000 135.12574 ? 209 SER   A C   1 
ATOM   1398 O  O   . SER   A 1 173 ? -21.23100 -10.47900 17.49000  1.000 135.21853 ? 209 SER   A O   1 
ATOM   1399 C  CB  . SER   A 1 173 ? -18.91900 -10.48500 19.68500  1.000 136.46586 ? 209 SER   A CB  1 
ATOM   1400 O  OG  . SER   A 1 173 ? -18.50700 -9.57000  18.68400  1.000 138.18926 ? 209 SER   A OG  1 
ATOM   1401 N  N   . LEU   A 1 174 ? -22.15500 -11.01100 19.47700  1.000 132.34023 ? 210 LEU   A N   1 
ATOM   1402 C  CA  . LEU   A 1 174 ? -23.45400 -10.44800 19.13300  1.000 124.63999 ? 210 LEU   A CA  1 
ATOM   1403 C  C   . LEU   A 1 174 ? -23.33000 -8.94800  18.90000  1.000 132.86220 ? 210 LEU   A C   1 
ATOM   1404 O  O   . LEU   A 1 174 ? -22.85600 -8.20900  19.76800  1.000 125.17978 ? 210 LEU   A O   1 
ATOM   1405 C  CB  . LEU   A 1 174 ? -24.46800 -10.73200 20.24400  1.000 113.06473 ? 210 LEU   A CB  1 
ATOM   1406 C  CG  . LEU   A 1 174 ? -24.96500 -12.16800 20.46700  1.000 109.43449 ? 210 LEU   A CG  1 
ATOM   1407 C  CD1 . LEU   A 1 174 ? -25.42400 -12.79500 19.16000  1.000 106.76022 ? 210 LEU   A CD1 1 
ATOM   1408 C  CD2 . LEU   A 1 174 ? -23.92600 -13.04700 21.15800  1.000 110.53720 ? 210 LEU   A CD2 1 
ATOM   1409 N  N   . SER   A 1 175 ? -23.75600 -8.49900  17.72100  1.000 151.25965 ? 211 SER   A N   1 
ATOM   1410 C  CA  . SER   A 1 175 ? -23.59200 -7.11100  17.30400  1.000 153.25561 ? 211 SER   A CA  1 
ATOM   1411 C  C   . SER   A 1 175 ? -24.90500 -6.58500  16.74700  1.000 153.43358 ? 211 SER   A C   1 
ATOM   1412 O  O   . SER   A 1 175 ? -25.39900 -7.09100  15.73400  1.000 150.53852 ? 211 SER   A O   1 
ATOM   1413 C  CB  . SER   A 1 175 ? -22.48100 -6.98100  16.25800  1.000 155.18788 ? 211 SER   A CB  1 
ATOM   1414 O  OG  . SER   A 1 175 ? -22.41500 -5.66300  15.73900  1.000 153.78186 ? 211 SER   A OG  1 
ATOM   1415 N  N   . GLY   A 1 176 ? -25.45800 -5.56400  17.39900  1.000 158.21960 ? 212 GLY   A N   1 
ATOM   1416 C  CA  . GLY   A 1 176 ? -26.67200 -4.90200  16.97900  1.000 147.03914 ? 212 GLY   A CA  1 
ATOM   1417 C  C   . GLY   A 1 176 ? -27.65500 -4.78300  18.12100  1.000 138.38512 ? 212 GLY   A C   1 
ATOM   1418 O  O   . GLY   A 1 176 ? -27.31800 -4.98200  19.29400  1.000 125.57429 ? 212 GLY   A O   1 
ATOM   1419 N  N   . THR   A 1 177 ? -28.89400 -4.44000  17.77700  1.000 117.76686 ? 213 THR   A N   1 
ATOM   1420 C  CA  . THR   A 1 177 ? -29.98000 -4.34500  18.74400  1.000 112.47135 ? 213 THR   A CA  1 
ATOM   1421 C  C   . THR   A 1 177 ? -30.80900 -5.62100  18.68500  1.000 105.31857 ? 213 THR   A C   1 
ATOM   1422 O  O   . THR   A 1 177 ? -31.24800 -6.03100  17.60600  1.000 95.41707  ? 213 THR   A O   1 
ATOM   1423 C  CB  . THR   A 1 177 ? -30.86200 -3.12700  18.46900  1.000 97.75667  ? 213 THR   A CB  1 
ATOM   1424 O  OG1 . THR   A 1 177 ? -30.03600 -2.00000  18.15800  1.000 91.50669  ? 213 THR   A OG1 1 
ATOM   1425 C  CG2 . THR   A 1 177 ? -31.70300 -2.79300  19.69600  1.000 99.76120  ? 213 THR   A CG2 1 
ATOM   1426 N  N   . ALA   A 1 178 ? -31.02900 -6.23800  19.85000  1.000 117.84970 ? 214 ALA   A N   1 
ATOM   1427 C  CA  . ALA   A 1 178 ? -31.66200 -7.55300  19.90500  1.000 123.04587 ? 214 ALA   A CA  1 
ATOM   1428 C  C   . ALA   A 1 178 ? -33.08900 -7.55200  19.37200  1.000 112.64726 ? 214 ALA   A C   1 
ATOM   1429 O  O   . ALA   A 1 178 ? -33.58800 -8.60900  18.97200  1.000 112.56358 ? 214 ALA   A O   1 
ATOM   1430 C  CB  . ALA   A 1 178 ? -31.65000 -8.08200  21.34100  1.000 141.87935 ? 214 ALA   A CB  1 
ATOM   1431 N  N   . ARG   A 1 179 ? -33.75800 -6.39900  19.35300  1.000 82.48115  ? 215 ARG   A N   1 
ATOM   1432 C  CA  . ARG   A 1 179 ? -35.15800 -6.37400  18.94900  1.000 75.60565  ? 215 ARG   A CA  1 
ATOM   1433 C  C   . ARG   A 1 179 ? -35.33000 -6.52900  17.44300  1.000 81.45338  ? 215 ARG   A C   1 
ATOM   1434 O  O   . ARG   A 1 179 ? -36.38600 -6.99200  16.99800  1.000 56.56919  ? 215 ARG   A O   1 
ATOM   1435 C  CB  . ARG   A 1 179 ? -35.81800 -5.07900  19.42300  1.000 84.41864  ? 215 ARG   A CB  1 
ATOM   1436 C  CG  . ARG   A 1 179 ? -37.33900 -5.13100  19.47100  1.000 82.41083  ? 215 ARG   A CG  1 
ATOM   1437 C  CD  . ARG   A 1 179 ? -37.93700 -3.75500  19.72400  1.000 77.89303  ? 215 ARG   A CD  1 
ATOM   1438 N  NE  . ARG   A 1 179 ? -37.44600 -3.15200  20.95700  1.000 87.74846  ? 215 ARG   A NE  1 
ATOM   1439 C  CZ  . ARG   A 1 179 ? -37.74800 -1.92400  21.35800  1.000 77.52699  ? 215 ARG   A CZ  1 
ATOM   1440 N  NH1 . ARG   A 1 179 ? -38.53500 -1.13700  20.64200  1.000 71.64866  ? 215 ARG   A NH1 1 
ATOM   1441 N  NH2 . ARG   A 1 179 ? -37.24600 -1.47400  22.50500  1.000 73.77999  ? 215 ARG   A NH2 1 
ATOM   1442 N  N   . TYR   A 1 180 ? -34.31900 -6.16800  16.64800  1.000 70.90103  ? 216 TYR   A N   1 
ATOM   1443 C  CA  . TYR   A 1 180 ? -34.44700 -6.15100  15.19600  1.000 57.42798  ? 216 TYR   A CA  1 
ATOM   1444 C  C   . TYR   A 1 180 ? -33.43800 -7.02200  14.46100  1.000 70.44547  ? 216 TYR   A C   1 
ATOM   1445 O  O   . TYR   A 1 180 ? -33.60700 -7.23800  13.25600  1.000 58.82762  ? 216 TYR   A O   1 
ATOM   1446 C  CB  . TYR   A 1 180 ? -34.32300 -4.71300  14.66400  1.000 48.26452  ? 216 TYR   A CB  1 
ATOM   1447 C  CG  . TYR   A 1 180 ? -35.21300 -3.71500  15.37000  1.000 76.46836  ? 216 TYR   A CG  1 
ATOM   1448 C  CD1 . TYR   A 1 180 ? -36.52800 -4.02800  15.69100  1.000 58.49175  ? 216 TYR   A CD1 1 
ATOM   1449 C  CD2 . TYR   A 1 180 ? -34.73600 -2.46100  15.72000  1.000 67.80403  ? 216 TYR   A CD2 1 
ATOM   1450 C  CE1 . TYR   A 1 180 ? -37.34200 -3.11900  16.33900  1.000 74.24225  ? 216 TYR   A CE1 1 
ATOM   1451 C  CE2 . TYR   A 1 180 ? -35.54200 -1.54500  16.37000  1.000 62.18728  ? 216 TYR   A CE2 1 
ATOM   1452 C  CZ  . TYR   A 1 180 ? -36.84400 -1.87900  16.67600  1.000 69.56659  ? 216 TYR   A CZ  1 
ATOM   1453 O  OH  . TYR   A 1 180 ? -37.65300 -0.97200  17.32200  1.000 58.92793  ? 216 TYR   A OH  1 
ATOM   1454 N  N   . MET   A 1 181 ? -32.40300 -7.52300  15.13300  1.000 57.05088  ? 217 MET   A N   1 
ATOM   1455 C  CA  . MET   A 1 181 ? -31.36600 -8.27800  14.44400  1.000 83.54029  ? 217 MET   A CA  1 
ATOM   1456 C  C   . MET   A 1 181 ? -31.92400 -9.58300  13.88800  1.000 71.40991  ? 217 MET   A C   1 
ATOM   1457 O  O   . MET   A 1 181 ? -32.93000 -10.11300 14.36700  1.000 66.62681  ? 217 MET   A O   1 
ATOM   1458 C  CB  . MET   A 1 181 ? -30.19900 -8.56400  15.38900  1.000 73.00626  ? 217 MET   A CB  1 
ATOM   1459 C  CG  . MET   A 1 181 ? -30.62300 -9.09400  16.74600  1.000 78.88014  ? 217 MET   A CG  1 
ATOM   1460 S  SD  . MET   A 1 181 ? -29.21700 -9.58400  17.76700  1.000 107.74166 ? 217 MET   A SD  1 
ATOM   1461 C  CE  . MET   A 1 181 ? -27.98600 -8.37500  17.26800  1.000 114.27440 ? 217 MET   A CE  1 
ATOM   1462 N  N   . SER   A 1 182 ? -31.25300 -10.10300 12.86500  1.000 56.26424  ? 218 SER   A N   1 
ATOM   1463 C  CA  . SER   A 1 182 ? -31.72400 -11.30100 12.19000  1.000 79.18096  ? 218 SER   A CA  1 
ATOM   1464 C  C   . SER   A 1 182 ? -31.52000 -12.53300 13.07100  1.000 67.03128  ? 218 SER   A C   1 
ATOM   1465 O  O   . SER   A 1 182 ? -30.86900 -12.48900 14.11900  1.000 68.81791  ? 218 SER   A O   1 
ATOM   1466 C  CB  . SER   A 1 182 ? -31.00000 -11.48400 10.85700  1.000 65.48461  ? 218 SER   A CB  1 
ATOM   1467 O  OG  . SER   A 1 182 ? -29.62500 -11.76300 11.06000  1.000 82.61149  ? 218 SER   A OG  1 
ATOM   1468 N  N   . ILE   A 1 183 ? -32.09800 -13.65000 12.62500  1.000 79.55205  ? 219 ILE   A N   1 
ATOM   1469 C  CA  . ILE   A 1 183 ? -31.88100 -14.92100 13.31000  1.000 74.77434  ? 219 ILE   A CA  1 
ATOM   1470 C  C   . ILE   A 1 183 ? -30.42800 -15.35700 13.17200  1.000 70.04723  ? 219 ILE   A C   1 
ATOM   1471 O  O   . ILE   A 1 183 ? -29.83300 -15.89300 14.11500  1.000 81.77659  ? 219 ILE   A O   1 
ATOM   1472 C  CB  . ILE   A 1 183 ? -32.85400 -15.98700 12.76900  1.000 70.91925  ? 219 ILE   A CB  1 
ATOM   1473 C  CG1 . ILE   A 1 183 ? -34.18200 -15.93300 13.52900  1.000 78.27277  ? 219 ILE   A CG1 1 
ATOM   1474 C  CG2 . ILE   A 1 183 ? -32.24100 -17.38000 12.84000  1.000 84.99054  ? 219 ILE   A CG2 1 
ATOM   1475 C  CD1 . ILE   A 1 183 ? -35.20100 -16.94100 13.04500  1.000 89.63351  ? 219 ILE   A CD1 1 
ATOM   1476 N  N   . ASN   A 1 184 ? -29.82800 -15.11400 12.00400  1.000 68.06852  ? 220 ASN   A N   1 
ATOM   1477 C  CA  . ASN   A 1 184 ? -28.43800 -15.50100 11.78700  1.000 89.75998  ? 220 ASN   A CA  1 
ATOM   1478 C  C   . ASN   A 1 184 ? -27.49000 -14.74900 12.71100  1.000 86.25857  ? 220 ASN   A C   1 
ATOM   1479 O  O   . ASN   A 1 184 ? -26.44600 -15.28700 13.09600  1.000 92.49010  ? 220 ASN   A O   1 
ATOM   1480 C  CB  . ASN   A 1 184 ? -28.05100 -15.26800 10.32700  1.000 86.05584  ? 220 ASN   A CB  1 
ATOM   1481 C  CG  . ASN   A 1 184 ? -28.86200 -16.11400 9.36900   1.000 88.35300  ? 220 ASN   A CG  1 
ATOM   1482 O  OD1 . ASN   A 1 184 ? -29.20500 -17.25700 9.67100   1.000 90.65921  ? 220 ASN   A OD1 1 
ATOM   1483 N  ND2 . ASN   A 1 184 ? -29.17900 -15.55300 8.20900   1.000 85.62022  ? 220 ASN   A ND2 1 
ATOM   1484 N  N   . THR   A 1 185 ? -27.82600 -13.51000 13.07800  1.000 76.50369  ? 221 THR   A N   1 
ATOM   1485 C  CA  . THR   A 1 185 ? -26.96400 -12.76800 13.99100  1.000 82.90264  ? 221 THR   A CA  1 
ATOM   1486 C  C   . THR   A 1 185 ? -27.05600 -13.32700 15.40500  1.000 80.13001  ? 221 THR   A C   1 
ATOM   1487 O  O   . THR   A 1 185 ? -26.05100 -13.38100 16.12300  1.000 85.73060  ? 221 THR   A O   1 
ATOM   1488 C  CB  . THR   A 1 185 ? -27.32200 -11.28200 13.97500  1.000 87.10470  ? 221 THR   A CB  1 
ATOM   1489 O  OG1 . THR   A 1 185 ? -27.43200 -10.83300 12.61800  1.000 85.54762  ? 221 THR   A OG1 1 
ATOM   1490 C  CG2 . THR   A 1 185 ? -26.24400 -10.46500 14.68600  1.000 85.81670  ? 221 THR   A CG2 1 
ATOM   1491 N  N   . HIS   A 1 186 ? -28.25300 -13.75300 15.82000  1.000 72.41766  ? 222 HIS   A N   1 
ATOM   1492 C  CA  . HIS   A 1 186 ? -28.40700 -14.37400 17.13200  1.000 83.42148  ? 222 HIS   A CA  1 
ATOM   1493 C  C   . HIS   A 1 186 ? -27.56400 -15.63400 17.26000  1.000 88.21365  ? 222 HIS   A C   1 
ATOM   1494 O  O   . HIS   A 1 186 ? -27.06100 -15.93800 18.34800  1.000 102.10010 ? 222 HIS   A O   1 
ATOM   1495 C  CB  . HIS   A 1 186 ? -29.87800 -14.70300 17.39400  1.000 77.32018  ? 222 HIS   A CB  1 
ATOM   1496 C  CG  . HIS   A 1 186 ? -30.68400 -13.53800 17.87400  1.000 88.72374  ? 222 HIS   A CG  1 
ATOM   1497 N  ND1 . HIS   A 1 186 ? -30.77200 -13.19400 19.20600  1.000 90.38369  ? 222 HIS   A ND1 1 
ATOM   1498 C  CD2 . HIS   A 1 186 ? -31.44500 -12.64100 17.20400  1.000 87.32043  ? 222 HIS   A CD2 1 
ATOM   1499 C  CE1 . HIS   A 1 186 ? -31.54900 -12.13400 19.33500  1.000 94.66265  ? 222 HIS   A CE1 1 
ATOM   1500 N  NE2 . HIS   A 1 186 ? -31.97100 -11.77900 18.13500  1.000 90.35216  ? 222 HIS   A NE2 1 
ATOM   1501 N  N   . LEU   A 1 187 ? -27.39600 -16.37300 16.16600  1.000 83.62667  ? 223 LEU   A N   1 
ATOM   1502 C  CA  . LEU   A 1 187 ? -26.62500 -17.60900 16.14900  1.000 98.62671  ? 223 LEU   A CA  1 
ATOM   1503 C  C   . LEU   A 1 187 ? -25.12900 -17.37600 15.99800  1.000 100.66294 ? 223 LEU   A C   1 
ATOM   1504 O  O   . LEU   A 1 187 ? -24.37900 -18.34700 15.84700  1.000 97.46296  ? 223 LEU   A O   1 
ATOM   1505 C  CB  . LEU   A 1 187 ? -27.12500 -18.51400 15.02200  1.000 93.17542  ? 223 LEU   A CB  1 
ATOM   1506 C  CG  . LEU   A 1 187 ? -28.60900 -18.85400 15.13600  1.000 95.57430  ? 223 LEU   A CG  1 
ATOM   1507 C  CD1 . LEU   A 1 187 ? -29.04500 -19.78300 14.01700  1.000 89.32912  ? 223 LEU   A CD1 1 
ATOM   1508 C  CD2 . LEU   A 1 187 ? -28.89600 -19.46700 16.49500  1.000 100.48124 ? 223 LEU   A CD2 1 
ATOM   1509 N  N   . GLY   A 1 188 ? -24.68100 -16.12400 16.03200  1.000 98.24243  ? 224 GLY   A N   1 
ATOM   1510 C  CA  . GLY   A 1 188 ? -23.26600 -15.83500 15.90800  1.000 95.87494  ? 224 GLY   A CA  1 
ATOM   1511 C  C   . GLY   A 1 188 ? -22.68900 -16.08900 14.53400  1.000 95.18509  ? 224 GLY   A C   1 
ATOM   1512 O  O   . GLY   A 1 188 ? -21.49000 -16.36000 14.41600  1.000 115.54486 ? 224 GLY   A O   1 
ATOM   1513 N  N   . ARG   A 1 189 ? -23.50600 -16.00700 13.49000  1.000 90.19995  ? 225 ARG   A N   1 
ATOM   1514 C  CA  . ARG   A 1 189 ? -23.03400 -16.23600 12.13400  1.000 99.41185  ? 225 ARG   A CA  1 
ATOM   1515 C  C   . ARG   A 1 189 ? -22.60200 -14.92400 11.48800  1.000 100.60169 ? 225 ARG   A C   1 
ATOM   1516 O  O   . ARG   A 1 189 ? -23.00000 -13.83400 11.90700  1.000 105.35930 ? 225 ARG   A O   1 
ATOM   1517 C  CB  . ARG   A 1 189 ? -24.12100 -16.89800 11.28500  1.000 90.43795  ? 225 ARG   A CB  1 
ATOM   1518 C  CG  . ARG   A 1 189 ? -24.94500 -17.94800 12.01500  1.000 95.60825  ? 225 ARG   A CG  1 
ATOM   1519 C  CD  . ARG   A 1 189 ? -25.54300 -18.93300 11.02600  1.000 104.48675 ? 225 ARG   A CD  1 
ATOM   1520 N  NE  . ARG   A 1 189 ? -26.96900 -19.15900 11.22100  1.000 108.08979 ? 225 ARG   A NE  1 
ATOM   1521 C  CZ  . ARG   A 1 189 ? -27.69800 -19.98200 10.48000  1.000 103.62299 ? 225 ARG   A CZ  1 
ATOM   1522 N  NH1 . ARG   A 1 189 ? -27.16100 -20.68400 9.49500   1.000 96.85799  ? 225 ARG   A NH1 1 
ATOM   1523 N  NH2 . ARG   A 1 189 ? -28.99900 -20.10200 10.73000  1.000 91.59562  ? 225 ARG   A NH2 1 
ATOM   1524 N  N   . GLU   A 1 190 ? -21.77100 -15.04300 10.45300  1.000 120.59155 ? 226 GLU   A N   1 
ATOM   1525 C  CA  . GLU   A 1 190 ? -21.35000 -13.87000 9.70000   1.000 112.07346 ? 226 GLU   A CA  1 
ATOM   1526 C  C   . GLU   A 1 190 ? -22.54900 -13.23600 9.00600   1.000 109.21164 ? 226 GLU   A C   1 
ATOM   1527 O  O   . GLU   A 1 190 ? -23.38700 -13.92700 8.42200   1.000 105.40089 ? 226 GLU   A O   1 
ATOM   1528 C  CB  . GLU   A 1 190 ? -20.28100 -14.24800 8.67300   1.000 110.14332 ? 226 GLU   A CB  1 
ATOM   1529 C  CG  . GLU   A 1 190 ? -19.74700 -13.07200 7.86000   1.000 114.59974 ? 226 GLU   A CG  1 
ATOM   1530 C  CD  . GLU   A 1 190 ? -18.66700 -12.28900 8.58700   1.000 120.90483 ? 226 GLU   A CD  1 
ATOM   1531 O  OE1 . GLU   A 1 190 ? -17.58400 -12.85900 8.83700   1.000 127.02807 ? 226 GLU   A OE1 1 
ATOM   1532 O  OE2 . GLU   A 1 190 ? -18.90100 -11.10600 8.90900   1.000 116.76343 ? 226 GLU   A OE2 1 
ATOM   1533 N  N   . GLN   A 1 191 ? -22.63500 -11.91400 9.08700   1.000 83.26339  ? 227 GLN   A N   1 
ATOM   1534 C  CA  . GLN   A 1 191 ? -23.72500 -11.18100 8.46700   1.000 78.16569  ? 227 GLN   A CA  1 
ATOM   1535 C  C   . GLN   A 1 191 ? -23.38100 -10.84700 7.02200   1.000 67.68592  ? 227 GLN   A C   1 
ATOM   1536 O  O   . GLN   A 1 191 ? -22.21300 -10.68600 6.66000   1.000 64.81123  ? 227 GLN   A O   1 
ATOM   1537 C  CB  . GLN   A 1 191 ? -24.02600 -9.89900  9.24400   1.000 74.03845  ? 227 GLN   A CB  1 
ATOM   1538 C  CG  . GLN   A 1 191 ? -24.31000 -10.12800 10.71900  1.000 79.69157  ? 227 GLN   A CG  1 
ATOM   1539 C  CD  . GLN   A 1 191 ? -24.62700 -8.84300  11.45600  1.000 83.94438  ? 227 GLN   A CD  1 
ATOM   1540 O  OE1 . GLN   A 1 191 ? -25.31000 -7.96400  10.93100  1.000 81.53744  ? 227 GLN   A OE1 1 
ATOM   1541 N  NE2 . GLN   A 1 191 ? -24.12600 -8.72500  12.68000  1.000 76.45564  ? 227 GLN   A NE2 1 
ATOM   1542 N  N   . SER   A 1 192 ? -24.41500 -10.75300 6.19600   1.000 55.81969  ? 228 SER   A N   1 
ATOM   1543 C  CA  . SER   A 1 192 ? -24.25300 -10.40200 4.79000   1.000 77.68216  ? 228 SER   A CA  1 
ATOM   1544 C  C   . SER   A 1 192 ? -25.40800 -9.48400  4.40800   1.000 57.93968  ? 228 SER   A C   1 
ATOM   1545 O  O   . SER   A 1 192 ? -26.02300 -8.83400  5.26000   1.000 64.50329  ? 228 SER   A O   1 
ATOM   1546 C  CB  . SER   A 1 192 ? -24.17400 -11.66600 3.92000   1.000 61.02284  ? 228 SER   A CB  1 
ATOM   1547 O  OG  . SER   A 1 192 ? -25.40400 -12.37000 3.92800   1.000 61.19210  ? 228 SER   A OG  1 
ATOM   1548 N  N   . ARG   A 1 193 ? -25.71200 -9.42800  3.10900   1.000 58.88629  ? 229 ARG   A N   1 
ATOM   1549 C  CA  . ARG   A 1 193 ? -26.79300 -8.56800  2.64100   1.000 60.60170  ? 229 ARG   A CA  1 
ATOM   1550 C  C   . ARG   A 1 193 ? -28.14700 -9.05000  3.14600   1.000 61.37497  ? 229 ARG   A C   1 
ATOM   1551 O  O   . ARG   A 1 193 ? -29.00100 -8.23500  3.51000   1.000 65.15387  ? 229 ARG   A O   1 
ATOM   1552 C  CB  . ARG   A 1 193 ? -26.78000 -8.49200  1.11400   1.000 69.42282  ? 229 ARG   A CB  1 
ATOM   1553 C  CG  . ARG   A 1 193 ? -25.64600 -7.64900  0.55400   1.000 76.04243  ? 229 ARG   A CG  1 
ATOM   1554 C  CD  . ARG   A 1 193 ? -25.54900 -7.75600  -0.96000  1.000 75.29395  ? 229 ARG   A CD  1 
ATOM   1555 N  NE  . ARG   A 1 193 ? -25.10000 -9.07600  -1.38600  1.000 71.70279  ? 229 ARG   A NE  1 
ATOM   1556 C  CZ  . ARG   A 1 193 ? -24.65800 -9.36100  -2.60400  1.000 91.20643  ? 229 ARG   A CZ  1 
ATOM   1557 N  NH1 . ARG   A 1 193 ? -24.58500 -8.43500  -3.54700  1.000 83.84609  ? 229 ARG   A NH1 1 
ATOM   1558 N  NH2 . ARG   A 1 193 ? -24.27400 -10.60400 -2.88100  1.000 89.59035  ? 229 ARG   A NH2 1 
ATOM   1559 N  N   . ARG   A 1 194 ? -28.35700 -10.36900 3.19500   1.000 53.51383  ? 230 ARG   A N   1 
ATOM   1560 C  CA  . ARG   A 1 194 ? -29.65800 -10.90400 3.58400   1.000 55.01604  ? 230 ARG   A CA  1 
ATOM   1561 C  C   . ARG   A 1 194 ? -30.05800 -10.51000 5.00000   1.000 69.10429  ? 230 ARG   A C   1 
ATOM   1562 O  O   . ARG   A 1 194 ? -31.25400 -10.49000 5.31100   1.000 67.78348  ? 230 ARG   A O   1 
ATOM   1563 C  CB  . ARG   A 1 194 ? -29.66400 -12.42900 3.46300   1.000 75.10519  ? 230 ARG   A CB  1 
ATOM   1564 C  CG  . ARG   A 1 194 ? -28.79400 -13.12300 4.49900   1.000 72.76004  ? 230 ARG   A CG  1 
ATOM   1565 C  CD  . ARG   A 1 194 ? -28.90400 -14.63500 4.42700   1.000 78.47869  ? 230 ARG   A CD  1 
ATOM   1566 N  NE  . ARG   A 1 194 ? -27.98500 -15.26700 5.36700   1.000 85.17140  ? 230 ARG   A NE  1 
ATOM   1567 C  CZ  . ARG   A 1 194 ? -27.84900 -16.57700 5.52500   1.000 88.31688  ? 230 ARG   A CZ  1 
ATOM   1568 N  NH1 . ARG   A 1 194 ? -28.56600 -17.43700 4.82100   1.000 84.81754  ? 230 ARG   A NH1 1 
ATOM   1569 N  NH2 . ARG   A 1 194 ? -26.97200 -17.03400 6.41300   1.000 88.48774  ? 230 ARG   A NH2 1 
ATOM   1570 N  N   . ASP   A 1 195 ? -29.09100 -10.19800 5.86700   1.000 62.65711  ? 231 ASP   A N   1 
ATOM   1571 C  CA  . ASP   A 1 195 ? -29.42500 -9.89700  7.25500   1.000 56.92754  ? 231 ASP   A CA  1 
ATOM   1572 C  C   . ASP   A 1 195 ? -29.89900 -8.46200  7.44100   1.000 69.26561  ? 231 ASP   A C   1 
ATOM   1573 O  O   . ASP   A 1 195 ? -30.72000 -8.20200  8.32700   1.000 59.37604  ? 231 ASP   A O   1 
ATOM   1574 C  CB  . ASP   A 1 195 ? -28.23100 -10.18400 8.16800   1.000 61.74988  ? 231 ASP   A CB  1 
ATOM   1575 C  CG  . ASP   A 1 195 ? -28.10600 -11.65700 8.51400   1.000 85.86571  ? 231 ASP   A CG  1 
ATOM   1576 O  OD1 . ASP   A 1 195 ? -29.01800 -12.43000 8.15000   1.000 71.67448  ? 231 ASP   A OD1 1 
ATOM   1577 O  OD2 . ASP   A 1 195 ? -27.09700 -12.04600 9.14300   1.000 70.43093  ? 231 ASP   A OD2 1 
ATOM   1578 N  N   . ASP   A 1 196 ? -29.39600 -7.52100  6.63600   1.000 59.92121  ? 232 ASP   A N   1 
ATOM   1579 C  CA  . ASP   A 1 196 ? -29.95600 -6.17200  6.64900   1.000 60.72442  ? 232 ASP   A CA  1 
ATOM   1580 C  C   . ASP   A 1 196 ? -31.41100 -6.18400  6.20500   1.000 57.49911  ? 232 ASP   A C   1 
ATOM   1581 O  O   . ASP   A 1 196 ? -32.23400 -5.41800  6.71800   1.000 69.99863  ? 232 ASP   A O   1 
ATOM   1582 C  CB  . ASP   A 1 196 ? -29.14300 -5.24600  5.74400   1.000 54.82226  ? 232 ASP   A CB  1 
ATOM   1583 C  CG  . ASP   A 1 196 ? -27.78500 -4.91300  6.31600   1.000 58.10024  ? 232 ASP   A CG  1 
ATOM   1584 O  OD1 . ASP   A 1 196 ? -27.61400 -5.00100  7.55000   1.000 52.15094  ? 232 ASP   A OD1 1 
ATOM   1585 O  OD2 . ASP   A 1 196 ? -26.88800 -4.55700  5.52500   1.000 54.64093  ? 232 ASP   A OD2 1 
ATOM   1586 N  N   . LEU   A 1 197 ? -31.74300 -7.05000  5.24700   1.000 61.43811  ? 233 LEU   A N   1 
ATOM   1587 C  CA  . LEU   A 1 197 ? -33.09700 -7.10900  4.71500   1.000 63.20619  ? 233 LEU   A CA  1 
ATOM   1588 C  C   . LEU   A 1 197 ? -34.05500 -7.80600  5.67300   1.000 62.36239  ? 233 LEU   A C   1 
ATOM   1589 O  O   . LEU   A 1 197 ? -35.23100 -7.43300  5.74200   1.000 73.30447  ? 233 LEU   A O   1 
ATOM   1590 C  CB  . LEU   A 1 197 ? -33.09500 -7.81100  3.35400   1.000 60.52857  ? 233 LEU   A CB  1 
ATOM   1591 C  CG  . LEU   A 1 197 ? -32.63700 -7.05300  2.09700   1.000 68.82985  ? 233 LEU   A CG  1 
ATOM   1592 C  CD1 . LEU   A 1 197 ? -33.63000 -5.96100  1.72900   1.000 72.73191  ? 233 LEU   A CD1 1 
ATOM   1593 C  CD2 . LEU   A 1 197 ? -31.22600 -6.47600  2.22000   1.000 58.25267  ? 233 LEU   A CD2 1 
ATOM   1594 N  N   . GLU   A 1 198 ? -33.58400 -8.81200  6.41400   1.000 60.60197  ? 234 GLU   A N   1 
ATOM   1595 C  CA  . GLU   A 1 198 ? -34.43300 -9.42600  7.43000   1.000 66.46730  ? 234 GLU   A CA  1 
ATOM   1596 C  C   . GLU   A 1 198 ? -34.66500 -8.47400  8.59600   1.000 63.47576  ? 234 GLU   A C   1 
ATOM   1597 O  O   . GLU   A 1 198 ? -35.76200 -8.43800  9.16800   1.000 47.85168  ? 234 GLU   A O   1 
ATOM   1598 C  CB  . GLU   A 1 198 ? -33.81600 -10.73500 7.92300   1.000 50.64149  ? 234 GLU   A CB  1 
ATOM   1599 C  CG  . GLU   A 1 198 ? -34.64000 -11.42600 8.99900   1.000 71.51837  ? 234 GLU   A CG  1 
ATOM   1600 C  CD  . GLU   A 1 198 ? -33.95800 -12.65100 9.57100   1.000 80.32422  ? 234 GLU   A CD  1 
ATOM   1601 O  OE1 . GLU   A 1 198 ? -33.03500 -13.18300 8.91900   1.000 69.37829  ? 234 GLU   A OE1 1 
ATOM   1602 O  OE2 . GLU   A 1 198 ? -34.34500 -13.07800 10.67900  1.000 75.36253  ? 234 GLU   A OE2 1 
ATOM   1603 N  N   . ALA   A 1 199 ? -33.64400 -7.69700  8.96500   1.000 58.07942  ? 235 ALA   A N   1 
ATOM   1604 C  CA  . ALA   A 1 199 ? -33.82500 -6.68800  10.00200  1.000 69.99880  ? 235 ALA   A CA  1 
ATOM   1605 C  C   . ALA   A 1 199 ? -34.85200 -5.64600  9.57700   1.000 53.67508  ? 235 ALA   A C   1 
ATOM   1606 O  O   . ALA   A 1 199 ? -35.66000 -5.19100  10.39400  1.000 49.25859  ? 235 ALA   A O   1 
ATOM   1607 C  CB  . ALA   A 1 199 ? -32.48800 -6.02800  10.33400  1.000 60.75943  ? 235 ALA   A CB  1 
ATOM   1608 N  N   . LEU   A 1 200 ? -34.83800 -5.26000  8.29700   1.000 63.65806  ? 236 LEU   A N   1 
ATOM   1609 C  CA  . LEU   A 1 200 ? -35.87600 -4.37300  7.78300   1.000 59.86063  ? 236 LEU   A CA  1 
ATOM   1610 C  C   . LEU   A 1 200 ? -37.25300 -5.01600  7.87400   1.000 68.26433  ? 236 LEU   A C   1 
ATOM   1611 O  O   . LEU   A 1 200 ? -38.25400 -4.31600  8.06700   1.000 46.00456  ? 236 LEU   A O   1 
ATOM   1612 C  CB  . LEU   A 1 200 ? -35.57200 -3.98400  6.33600   1.000 61.76973  ? 236 LEU   A CB  1 
ATOM   1613 C  CG  . LEU   A 1 200 ? -34.42000 -3.01100  6.08500   1.000 55.15808  ? 236 LEU   A CG  1 
ATOM   1614 C  CD1 . LEU   A 1 200 ? -34.12000 -2.92200  4.59900   1.000 63.21280  ? 236 LEU   A CD1 1 
ATOM   1615 C  CD2 . LEU   A 1 200 ? -34.74900 -1.63700  6.64600   1.000 58.26016  ? 236 LEU   A CD2 1 
ATOM   1616 N  N   . GLY   A 1 201 ? -37.32400 -6.34100  7.73700   1.000 57.64839  ? 237 GLY   A N   1 
ATOM   1617 C  CA  . GLY   A 1 201 ? -38.60300 -7.01800  7.86100   1.000 47.78090  ? 237 GLY   A CA  1 
ATOM   1618 C  C   . GLY   A 1 201 ? -39.16700 -6.95000  9.26700   1.000 57.04503  ? 237 GLY   A C   1 
ATOM   1619 O  O   . GLY   A 1 201 ? -40.38000 -6.82400  9.45200   1.000 46.61370  ? 237 GLY   A O   1 
ATOM   1620 N  N   . HIS   A 1 202 ? -38.29700 -7.03000  10.27700  1.000 53.91803  ? 238 HIS   A N   1 
ATOM   1621 C  CA  . HIS   A 1 202 ? -38.75900 -6.92700  11.65700  1.000 35.76290  ? 238 HIS   A CA  1 
ATOM   1622 C  C   . HIS   A 1 202 ? -39.24000 -5.52000  11.98200  1.000 63.87598  ? 238 HIS   A C   1 
ATOM   1623 O  O   . HIS   A 1 202 ? -40.14900 -5.35000  12.80300  1.000 60.33980  ? 238 HIS   A O   1 
ATOM   1624 C  CB  . HIS   A 1 202 ? -37.64400 -7.34100  12.61800  1.000 55.61879  ? 238 HIS   A CB  1 
ATOM   1625 C  CG  . HIS   A 1 202 ? -37.15900 -8.74300  12.41400  1.000 62.85033  ? 238 HIS   A CG  1 
ATOM   1626 N  ND1 . HIS   A 1 202 ? -35.84400 -9.11100  12.60300  1.000 74.28318  ? 238 HIS   A ND1 1 
ATOM   1627 C  CD2 . HIS   A 1 202 ? -37.81400 -9.86900  12.04200  1.000 68.63071  ? 238 HIS   A CD2 1 
ATOM   1628 C  CE1 . HIS   A 1 202 ? -35.70900 -10.40100 12.35300  1.000 64.65474  ? 238 HIS   A CE1 1 
ATOM   1629 N  NE2 . HIS   A 1 202 ? -36.89000 -10.88500 12.01100  1.000 76.12923  ? 238 HIS   A NE2 1 
ATOM   1630 N  N   . VAL   A 1 203 ? -38.64600 -4.50400  11.35200  1.000 57.74788  ? 239 VAL   A N   1 
ATOM   1631 C  CA  . VAL   A 1 203 ? -39.06800 -3.13000  11.60000  1.000 61.96904  ? 239 VAL   A CA  1 
ATOM   1632 C  C   . VAL   A 1 203 ? -40.45600 -2.88100  11.02500  1.000 63.20114  ? 239 VAL   A C   1 
ATOM   1633 O  O   . VAL   A 1 203 ? -41.24800 -2.12500  11.60300  1.000 66.89941  ? 239 VAL   A O   1 
ATOM   1634 C  CB  . VAL   A 1 203 ? -38.03200 -2.14400  11.03000  1.000 58.56519  ? 239 VAL   A CB  1 
ATOM   1635 C  CG1 . VAL   A 1 203 ? -38.44800 -0.70800  11.30800  1.000 55.82631  ? 239 VAL   A CG1 1 
ATOM   1636 C  CG2 . VAL   A 1 203 ? -36.65900 -2.41900  11.61800  1.000 62.62534  ? 239 VAL   A CG2 1 
ATOM   1637 N  N   . PHE   A 1 204 ? -40.78300 -3.50800  9.89400   1.000 57.70074  ? 240 PHE   A N   1 
ATOM   1638 C  CA  . PHE   A 1 204 ? -42.09600 -3.29800  9.29300   1.000 61.41924  ? 240 PHE   A CA  1 
ATOM   1639 C  C   . PHE   A 1 204 ? -43.20200 -3.81600  10.20500  1.000 65.86857  ? 240 PHE   A C   1 
ATOM   1640 O  O   . PHE   A 1 204 ? -44.16900 -3.10100  10.48800  1.000 73.73279  ? 240 PHE   A O   1 
ATOM   1641 C  CB  . PHE   A 1 204 ? -42.15700 -3.96100  7.91500   1.000 58.32479  ? 240 PHE   A CB  1 
ATOM   1642 C  CG  . PHE   A 1 204 ? -41.08100 -3.49600  6.97000   1.000 58.77896  ? 240 PHE   A CG  1 
ATOM   1643 C  CD1 . PHE   A 1 204 ? -40.52400 -2.23300  7.09800   1.000 60.36940  ? 240 PHE   A CD1 1 
ATOM   1644 C  CD2 . PHE   A 1 204 ? -40.62100 -4.32500  5.96100   1.000 60.11318  ? 240 PHE   A CD2 1 
ATOM   1645 C  CE1 . PHE   A 1 204 ? -39.52900 -1.80700  6.23800   1.000 59.17706  ? 240 PHE   A CE1 1 
ATOM   1646 C  CE2 . PHE   A 1 204 ? -39.62700 -3.90300  5.09600   1.000 66.18672  ? 240 PHE   A CE2 1 
ATOM   1647 C  CZ  . PHE   A 1 204 ? -39.08000 -2.64300  5.23500   1.000 52.99528  ? 240 PHE   A CZ  1 
ATOM   1648 N  N   . PHE   A 1 205 ? -43.06300 -5.05100  10.70000  1.000 55.40677  ? 241 PHE   A N   1 
ATOM   1649 C  CA  . PHE   A 1 205 ? -44.04100 -5.57400  11.65000  1.000 66.84690  ? 241 PHE   A CA  1 
ATOM   1650 C  C   . PHE   A 1 205 ? -44.06100 -4.76300  12.93900  1.000 70.92346  ? 241 PHE   A C   1 
ATOM   1651 O  O   . PHE   A 1 205 ? -45.10100 -4.67800  13.60200  1.000 73.94539  ? 241 PHE   A O   1 
ATOM   1652 C  CB  . PHE   A 1 205 ? -43.75200 -7.04400  11.95600  1.000 73.04866  ? 241 PHE   A CB  1 
ATOM   1653 C  CG  . PHE   A 1 205 ? -43.99100 -7.96500  10.79600  1.000 70.11593  ? 241 PHE   A CG  1 
ATOM   1654 C  CD1 . PHE   A 1 205 ? -45.27600 -8.35500  10.45700  1.000 78.23021  ? 241 PHE   A CD1 1 
ATOM   1655 C  CD2 . PHE   A 1 205 ? -42.93100 -8.44800  10.04800  1.000 64.13243  ? 241 PHE   A CD2 1 
ATOM   1656 C  CE1 . PHE   A 1 205 ? -45.49900 -9.20500  9.38900   1.000 84.39956  ? 241 PHE   A CE1 1 
ATOM   1657 C  CE2 . PHE   A 1 205 ? -43.14700 -9.29800  8.98000   1.000 75.20129  ? 241 PHE   A CE2 1 
ATOM   1658 C  CZ  . PHE   A 1 205 ? -44.43300 -9.67700  8.65100   1.000 80.81755  ? 241 PHE   A CZ  1 
ATOM   1659 N  N   . TYR   A 1 206 ? -42.92600 -4.16600  13.30900  1.000 69.13585  ? 242 TYR   A N   1 
ATOM   1660 C  CA  . TYR   A 1 206 ? -42.88700 -3.30300  14.48500  1.000 65.59676  ? 242 TYR   A CA  1 
ATOM   1661 C  C   . TYR   A 1 206 ? -43.74100 -2.05900  14.28000  1.000 70.54672  ? 242 TYR   A C   1 
ATOM   1662 O  O   . TYR   A 1 206 ? -44.38600 -1.57500  15.21800  1.000 58.35062  ? 242 TYR   A O   1 
ATOM   1663 C  CB  . TYR   A 1 206 ? -41.43800 -2.92700  14.79800  1.000 58.50656  ? 242 TYR   A CB  1 
ATOM   1664 C  CG  . TYR   A 1 206 ? -41.26200 -1.85300  15.85000  1.000 61.84079  ? 242 TYR   A CG  1 
ATOM   1665 C  CD1 . TYR   A 1 206 ? -41.31300 -2.16200  17.20300  1.000 71.16923  ? 242 TYR   A CD1 1 
ATOM   1666 C  CD2 . TYR   A 1 206 ? -41.01900 -0.53400  15.48800  1.000 60.51034  ? 242 TYR   A CD2 1 
ATOM   1667 C  CE1 . TYR   A 1 206 ? -41.14200 -1.18300  18.16600  1.000 67.28480  ? 242 TYR   A CE1 1 
ATOM   1668 C  CE2 . TYR   A 1 206 ? -40.84800 0.45000   16.44200  1.000 66.45065  ? 242 TYR   A CE2 1 
ATOM   1669 C  CZ  . TYR   A 1 206 ? -40.91000 0.12100   17.77900  1.000 73.27639  ? 242 TYR   A CZ  1 
ATOM   1670 O  OH  . TYR   A 1 206 ? -40.73800 1.10000   18.73000  1.000 84.73801  ? 242 TYR   A OH  1 
ATOM   1671 N  N   . PHE   A 1 207 ? -43.76500 -1.53200  13.05400  1.000 65.47867  ? 243 PHE   A N   1 
ATOM   1672 C  CA  . PHE   A 1 207 ? -44.58400 -0.35800  12.76900  1.000 66.79400  ? 243 PHE   A CA  1 
ATOM   1673 C  C   . PHE   A 1 207 ? -46.06500 -0.71600  12.68800  1.000 70.34032  ? 243 PHE   A C   1 
ATOM   1674 O  O   . PHE   A 1 207 ? -46.91600 0.03400   13.18100  1.000 71.13163  ? 243 PHE   A O   1 
ATOM   1675 C  CB  . PHE   A 1 207 ? -44.12600 0.30100   11.46700  1.000 54.73119  ? 243 PHE   A CB  1 
ATOM   1676 C  CG  . PHE   A 1 207 ? -42.79900 1.00000   11.56600  1.000 55.25921  ? 243 PHE   A CG  1 
ATOM   1677 C  CD1 . PHE   A 1 207 ? -42.28000 1.37000   12.79600  1.000 69.19981  ? 243 PHE   A CD1 1 
ATOM   1678 C  CD2 . PHE   A 1 207 ? -42.07400 1.29500   10.42300  1.000 51.34056  ? 243 PHE   A CD2 1 
ATOM   1679 C  CE1 . PHE   A 1 207 ? -41.06000 2.01600   12.88300  1.000 61.76359  ? 243 PHE   A CE1 1 
ATOM   1680 C  CE2 . PHE   A 1 207 ? -40.85500 1.94000   10.50400  1.000 52.45006  ? 243 PHE   A CE2 1 
ATOM   1681 C  CZ  . PHE   A 1 207 ? -40.34700 2.30100   11.73500  1.000 54.00756  ? 243 PHE   A CZ  1 
ATOM   1682 N  N   . LEU   A 1 208 ? -46.39400 -1.85100  12.06500  1.000 66.76715  ? 244 LEU   A N   1 
ATOM   1683 C  CA  . LEU   A 1 208 ? -47.79600 -2.21200  11.86600  1.000 68.88726  ? 244 LEU   A CA  1 
ATOM   1684 C  C   . LEU   A 1 208 ? -48.45800 -2.60100  13.17900  1.000 72.83184  ? 244 LEU   A C   1 
ATOM   1685 O  O   . LEU   A 1 208 ? -49.54100 -2.10600  13.51200  1.000 70.91720  ? 244 LEU   A O   1 
ATOM   1686 C  CB  . LEU   A 1 208 ? -47.90800 -3.36200  10.86800  1.000 66.42927  ? 244 LEU   A CB  1 
ATOM   1687 C  CG  . LEU   A 1 208 ? -47.17600 -3.20100  9.54300   1.000 72.53689  ? 244 LEU   A CG  1 
ATOM   1688 C  CD1 . LEU   A 1 208 ? -46.67300 -4.54800  9.06800   1.000 69.55768  ? 244 LEU   A CD1 1 
ATOM   1689 C  CD2 . LEU   A 1 208 ? -48.11400 -2.60600  8.52400   1.000 67.41055  ? 244 LEU   A CD2 1 
ATOM   1690 N  N   . ARG   A 1 209 ? -47.82500 -3.50100  13.93000  1.000 63.70301  ? 245 ARG   A N   1 
ATOM   1691 C  CA  . ARG   A 1 209 ? -48.41900 -4.02300  15.15000  1.000 70.66496  ? 245 ARG   A CA  1 
ATOM   1692 C  C   . ARG   A 1 209 ? -48.23700 -3.08500  16.33200  1.000 71.35023  ? 245 ARG   A C   1 
ATOM   1693 O  O   . ARG   A 1 209 ? -48.96200 -3.20900  17.32200  1.000 70.20432  ? 245 ARG   A O   1 
ATOM   1694 C  CB  . ARG   A 1 209 ? -47.81300 -5.38800  15.48600  1.000 76.21278  ? 245 ARG   A CB  1 
ATOM   1695 C  CG  . ARG   A 1 209 ? -47.85100 -6.38100  14.33900  1.000 75.72627  ? 245 ARG   A CG  1 
ATOM   1696 C  CD  . ARG   A 1 209 ? -47.04800 -7.63200  14.66800  1.000 79.73897  ? 245 ARG   A CD  1 
ATOM   1697 N  NE  . ARG   A 1 209 ? -47.43000 -8.20600  15.95400  1.000 80.23425  ? 245 ARG   A NE  1 
ATOM   1698 C  CZ  . ARG   A 1 209 ? -48.40000 -9.09400  16.12200  1.000 94.45811  ? 245 ARG   A CZ  1 
ATOM   1699 N  NH1 . ARG   A 1 209 ? -49.10600 -9.54900  15.09900  1.000 101.15066 ? 245 ARG   A NH1 1 
ATOM   1700 N  NH2 . ARG   A 1 209 ? -48.67300 -9.53300  17.34800  1.000 82.05930  ? 245 ARG   A NH2 1 
ATOM   1701 N  N   . GLY   A 1 210 ? -47.29700 -2.14900  16.25300  1.000 69.98679  ? 246 GLY   A N   1 
ATOM   1702 C  CA  . GLY   A 1 210 ? -46.94600 -1.33200  17.38100  1.000 75.35167  ? 246 GLY   A CA  1 
ATOM   1703 C  C   . GLY   A 1 210 ? -45.98000 -1.99900  18.34100  1.000 74.17932  ? 246 GLY   A C   1 
ATOM   1704 O  O   . GLY   A 1 210 ? -45.25000 -1.30600  19.05700  1.000 73.83712  ? 246 GLY   A O   1 
ATOM   1705 N  N   . GLN   A 1 211 ? -45.95000 -3.33100  18.36000  1.000 70.28471  ? 247 GLN   A N   1 
ATOM   1706 C  CA  . GLN   A 1 211 ? -45.01900 -4.07500  19.19500  1.000 79.93569  ? 247 GLN   A CA  1 
ATOM   1707 C  C   . GLN   A 1 211 ? -44.66300 -5.38300  18.49700  1.000 75.95322  ? 247 GLN   A C   1 
ATOM   1708 O  O   . GLN   A 1 211 ? -45.30200 -5.79100  17.52500  1.000 83.13130  ? 247 GLN   A O   1 
ATOM   1709 C  CB  . GLN   A 1 211 ? -45.60900 -4.33900  20.58800  1.000 84.78992  ? 247 GLN   A CB  1 
ATOM   1710 C  CG  . GLN   A 1 211 ? -44.70800 -3.97100  21.76300  1.000 96.31171  ? 247 GLN   A CG  1 
ATOM   1711 C  CD  . GLN   A 1 211 ? -45.29600 -4.40000  23.10200  1.000 102.16382 ? 247 GLN   A CD  1 
ATOM   1712 O  OE1 . GLN   A 1 211 ? -45.83700 -5.50000  23.23000  1.000 99.84026  ? 247 GLN   A OE1 1 
ATOM   1713 N  NE2 . GLN   A 1 211 ? -45.19300 -3.53100  24.10500  1.000 103.29089 ? 247 GLN   A NE2 1 
ATOM   1714 N  N   . LEU   A 1 212 ? -43.62000 -6.03500  19.00100  1.000 83.24553  ? 248 LEU   A N   1 
ATOM   1715 C  CA  . LEU   A 1 212 ? -43.23800 -7.36000  18.55100  1.000 80.44307  ? 248 LEU   A CA  1 
ATOM   1716 C  C   . LEU   A 1 212 ? -43.37300 -8.35900  19.69400  1.000 72.64716  ? 248 LEU   A C   1 
ATOM   1717 O  O   . LEU   A 1 212 ? -43.15600 -8.00500  20.85700  1.000 89.22973  ? 248 LEU   A O   1 
ATOM   1718 C  CB  . LEU   A 1 212 ? -41.79800 -7.36300  18.02300  1.000 69.97490  ? 248 LEU   A CB  1 
ATOM   1719 C  CG  . LEU   A 1 212 ? -41.64200 -6.93300  16.56300  1.000 73.66169  ? 248 LEU   A CG  1 
ATOM   1720 C  CD1 . LEU   A 1 212 ? -40.20500 -6.53300  16.26400  1.000 78.11681  ? 248 LEU   A CD1 1 
ATOM   1721 C  CD2 . LEU   A 1 212 ? -42.09300 -8.04800  15.62700  1.000 81.08156  ? 248 LEU   A CD2 1 
ATOM   1722 N  N   . PRO   A 1 213 ? -43.72800 -9.61300  19.39900  1.000 77.19135  ? 249 PRO   A N   1 
ATOM   1723 C  CA  . PRO   A 1 213 ? -43.96500 -10.57700 20.48400  1.000 78.91126  ? 249 PRO   A CA  1 
ATOM   1724 C  C   . PRO   A 1 213 ? -42.74400 -10.83900 21.34300  1.000 84.52057  ? 249 PRO   A C   1 
ATOM   1725 O  O   . PRO   A 1 213 ? -42.89900 -11.25500 22.49800  1.000 83.18059  ? 249 PRO   A O   1 
ATOM   1726 C  CB  . PRO   A 1 213 ? -44.40900 -11.84300 19.73700  1.000 79.63143  ? 249 PRO   A CB  1 
ATOM   1727 C  CG  . PRO   A 1 213 ? -43.83400 -11.70100 18.37700  1.000 80.49960  ? 249 PRO   A CG  1 
ATOM   1728 C  CD  . PRO   A 1 213 ? -43.89500 -10.22900 18.07300  1.000 75.02672  ? 249 PRO   A CD  1 
ATOM   1729 N  N   . TRP   A 1 214 ? -41.54000 -10.61000 20.82800  1.000 89.29412  ? 250 TRP   A N   1 
ATOM   1730 C  CA  . TRP   A 1 214 ? -40.32200 -10.80100 21.61400  1.000 83.55521  ? 250 TRP   A CA  1 
ATOM   1731 C  C   . TRP   A 1 214 ? -39.85700 -9.49600  22.25500  1.000 98.90358  ? 250 TRP   A C   1 
ATOM   1732 O  O   . TRP   A 1 214 ? -38.68500 -9.12500  22.19800  1.000 100.00248 ? 250 TRP   A O   1 
ATOM   1733 C  CB  . TRP   A 1 214 ? -39.22800 -11.41400 20.74600  1.000 79.06264  ? 250 TRP   A CB  1 
ATOM   1734 C  CG  . TRP   A 1 214 ? -38.97100 -10.68500 19.46200  1.000 84.20536  ? 250 TRP   A CG  1 
ATOM   1735 C  CD1 . TRP   A 1 214 ? -38.23000 -9.55100  19.29700  1.000 77.34851  ? 250 TRP   A CD1 1 
ATOM   1736 C  CD2 . TRP   A 1 214 ? -39.43700 -11.05200 18.15700  1.000 80.81162  ? 250 TRP   A CD2 1 
ATOM   1737 N  NE1 . TRP   A 1 214 ? -38.21500 -9.18400  17.97400  1.000 80.78029  ? 250 TRP   A NE1 1 
ATOM   1738 C  CE2 . TRP   A 1 214 ? -38.94800 -10.08900 17.25300  1.000 72.05280  ? 250 TRP   A CE2 1 
ATOM   1739 C  CE3 . TRP   A 1 214 ? -40.22500 -12.09900 17.66700  1.000 85.80549  ? 250 TRP   A CE3 1 
ATOM   1740 C  CZ2 . TRP   A 1 214 ? -39.21700 -10.14100 15.88800  1.000 74.32276  ? 250 TRP   A CZ2 1 
ATOM   1741 C  CZ3 . TRP   A 1 214 ? -40.49300 -12.14800 16.31000  1.000 79.27369  ? 250 TRP   A CZ3 1 
ATOM   1742 C  CH2 . TRP   A 1 214 ? -39.99100 -11.17500 15.43700  1.000 64.57147  ? 250 TRP   A CH2 1 
ATOM   1743 N  N   . GLN   A 1 215 ? -40.79200 -8.79200  22.88900  1.000 101.96156 ? 251 GLN   A N   1 
ATOM   1744 C  CA  . GLN   A 1 215 ? -40.49600 -7.59600  23.66500  1.000 95.68868  ? 251 GLN   A CA  1 
ATOM   1745 C  C   . GLN   A 1 215 ? -40.94800 -7.81300  25.10200  1.000 102.03028 ? 251 GLN   A C   1 
ATOM   1746 O  O   . GLN   A 1 215 ? -42.07100 -8.26800  25.34300  1.000 102.91296 ? 251 GLN   A O   1 
ATOM   1747 C  CB  . GLN   A 1 215 ? -41.18500 -6.35900  23.07800  1.000 104.25774 ? 251 GLN   A CB  1 
ATOM   1748 C  CG  . GLN   A 1 215 ? -40.68800 -5.95700  21.70100  1.000 111.23086 ? 251 GLN   A CG  1 
ATOM   1749 C  CD  . GLN   A 1 215 ? -41.18600 -4.58700  21.28300  1.000 101.69332 ? 251 GLN   A CD  1 
ATOM   1750 O  OE1 . GLN   A 1 215 ? -41.48500 -4.35100  20.11300  1.000 90.21198  ? 251 GLN   A OE1 1 
ATOM   1751 N  NE2 . GLN   A 1 215 ? -41.27000 -3.67100  22.24200  1.000 97.85503  ? 251 GLN   A NE2 1 
ATOM   1752 N  N   . GLY   A 1 216 ? -40.07000 -7.49500  26.05000  1.000 98.40839  ? 252 GLY   A N   1 
ATOM   1753 C  CA  . GLY   A 1 216 ? -40.40900 -7.59600  27.45300  1.000 97.91031  ? 252 GLY   A CA  1 
ATOM   1754 C  C   . GLY   A 1 216 ? -40.17700 -8.94700  28.08800  1.000 108.51593 ? 252 GLY   A C   1 
ATOM   1755 O  O   . GLY   A 1 216 ? -40.89200 -9.30300  29.03300  1.000 113.96557 ? 252 GLY   A O   1 
ATOM   1756 N  N   . LEU   A 1 217 ? -39.20000 -9.71200  27.60900  1.000 104.34983 ? 253 LEU   A N   1 
ATOM   1757 C  CA  . LEU   A 1 217 ? -38.90700 -11.01000 28.19600  1.000 111.27617 ? 253 LEU   A CA  1 
ATOM   1758 C  C   . LEU   A 1 217 ? -38.03300 -10.85100 29.43500  1.000 116.67340 ? 253 LEU   A C   1 
ATOM   1759 O  O   . LEU   A 1 217 ? -37.28600 -9.87900  29.57600  1.000 120.44236 ? 253 LEU   A O   1 
ATOM   1760 C  CB  . LEU   A 1 217 ? -38.20700 -11.92600 27.19000  1.000 102.64066 ? 253 LEU   A CB  1 
ATOM   1761 C  CG  . LEU   A 1 217 ? -38.91000 -12.26800 25.87300  1.000 96.53659  ? 253 LEU   A CG  1 
ATOM   1762 C  CD1 . LEU   A 1 217 ? -40.41300 -12.43800 26.06600  1.000 96.82504  ? 253 LEU   A CD1 1 
ATOM   1763 C  CD2 . LEU   A 1 217 ? -38.60500 -11.22400 24.81700  1.000 94.32559  ? 253 LEU   A CD2 1 
ATOM   1764 N  N   . LYS   A 1 218 ? -38.13100 -11.82500 30.33400  1.000 120.73015 ? 254 LYS   A N   1 
ATOM   1765 C  CA  . LYS   A 1 218 ? -37.37300 -11.82400 31.57600  1.000 131.99746 ? 254 LYS   A CA  1 
ATOM   1766 C  C   . LYS   A 1 218 ? -36.21100 -12.80300 31.48700  1.000 144.90080 ? 254 LYS   A C   1 
ATOM   1767 O  O   . LYS   A 1 218 ? -36.39000 -13.96100 31.10000  1.000 153.58914 ? 254 LYS   A O   1 
ATOM   1768 C  CB  . LYS   A 1 218 ? -38.26800 -12.19100 32.76300  1.000 140.49724 ? 254 LYS   A CB  1 
ATOM   1769 C  CG  . LYS   A 1 218 ? -39.47500 -11.28700 32.93300  1.000 128.48733 ? 254 LYS   A CG  1 
ATOM   1770 C  CD  . LYS   A 1 218 ? -39.06600 -9.82600  32.89000  1.000 126.98094 ? 254 LYS   A CD  1 
ATOM   1771 C  CE  . LYS   A 1 218 ? -40.26500 -8.92400  32.66500  1.000 124.03066 ? 254 LYS   A CE  1 
ATOM   1772 N  NZ  . LYS   A 1 218 ? -39.85000 -7.58200  32.17500  1.000 121.80632 ? 254 LYS   A NZ  1 
ATOM   1773 N  N   . ALA   A 1 219 ? -35.01700 -12.33200 31.85500  1.000 146.47244 ? 255 ALA   A N   1 
ATOM   1774 C  CA  . ALA   A 1 219 ? -33.84500 -13.19400 31.89200  1.000 140.63039 ? 255 ALA   A CA  1 
ATOM   1775 C  C   . ALA   A 1 219 ? -32.88000 -12.64900 32.92700  1.000 138.30243 ? 255 ALA   A C   1 
ATOM   1776 O  O   . ALA   A 1 219 ? -32.72500 -11.42400 33.02000  1.000 136.74414 ? 255 ALA   A O   1 
ATOM   1777 C  CB  . ALA   A 1 219 ? -33.16400 -13.27900 30.52300  1.000 136.02809 ? 255 ALA   A CB  1 
ATOM   1778 N  N   . PRO   A 1 220 ? -32.22700 -13.50500 33.71800  1.000 139.45974 ? 256 PRO   A N   1 
ATOM   1779 C  CA  . PRO   A 1 220 ? -31.33400 -12.97700 34.76700  1.000 141.82418 ? 256 PRO   A CA  1 
ATOM   1780 C  C   . PRO   A 1 220 ? -30.14300 -12.21900 34.20700  1.000 137.75795 ? 256 PRO   A C   1 
ATOM   1781 O  O   . PRO   A 1 220 ? -29.80000 -11.14200 34.71300  1.000 137.90737 ? 256 PRO   A O   1 
ATOM   1782 C  CB  . PRO   A 1 220 ? -30.91800 -14.23900 35.53900  1.000 146.22002 ? 256 PRO   A CB  1 
ATOM   1783 C  CG  . PRO   A 1 220 ? -31.14900 -15.37100 34.59700  1.000 143.88179 ? 256 PRO   A CG  1 
ATOM   1784 C  CD  . PRO   A 1 220 ? -32.30500 -14.97600 33.73300  1.000 138.78110 ? 256 PRO   A CD  1 
ATOM   1785 N  N   . THR   A 1 221 ? -29.51100 -12.73800 33.16200  1.000 129.19003 ? 257 THR   A N   1 
ATOM   1786 C  CA  . THR   A 1 221 ? -28.36000 -12.09100 32.55600  1.000 112.92578 ? 257 THR   A CA  1 
ATOM   1787 C  C   . THR   A 1 221 ? -28.74300 -11.47200 31.21700  1.000 121.63887 ? 257 THR   A C   1 
ATOM   1788 O  O   . THR   A 1 221 ? -29.87900 -11.58300 30.74400  1.000 125.96784 ? 257 THR   A O   1 
ATOM   1789 C  CB  . THR   A 1 221 ? -27.20700 -13.07900 32.37100  1.000 117.91805 ? 257 THR   A CB  1 
ATOM   1790 O  OG1 . THR   A 1 221 ? -27.33400 -13.73300 31.10200  1.000 108.51005 ? 257 THR   A OG1 1 
ATOM   1791 C  CG2 . THR   A 1 221 ? -27.21600 -14.11700 33.47200  1.000 119.40034 ? 257 THR   A CG2 1 
ATOM   1792 N  N   . ASN   A 1 222 ? -27.75900 -10.81100 30.60800  1.000 115.24282 ? 258 ASN   A N   1 
ATOM   1793 C  CA  . ASN   A 1 222 ? -27.94500 -10.19500 29.30100  1.000 115.49513 ? 258 ASN   A CA  1 
ATOM   1794 C  C   . ASN   A 1 222 ? -27.83600 -11.22900 28.18700  1.000 115.35433 ? 258 ASN   A C   1 
ATOM   1795 O  O   . ASN   A 1 222 ? -28.61700 -11.19700 27.23000  1.000 110.84305 ? 258 ASN   A O   1 
ATOM   1796 C  CB  . ASN   A 1 222 ? -26.91100 -9.08100  29.10800  1.000 111.58438 ? 258 ASN   A CB  1 
ATOM   1797 C  CG  . ASN   A 1 222 ? -27.13500 -8.27100  27.84800  1.000 112.62405 ? 258 ASN   A CG  1 
ATOM   1798 O  OD1 . ASN   A 1 222 ? -27.67600 -7.16300  27.88200  1.000 100.48286 ? 258 ASN   A OD1 1 
ATOM   1799 N  ND2 . ASN   A 1 222 ? -26.69800 -8.81400  26.72800  1.000 114.60764 ? 258 ASN   A ND2 1 
ATOM   1800 N  N   . LYS   A 1 223 ? -26.87700 -12.15400 28.30200  1.000 117.32974 ? 259 LYS   A N   1 
ATOM   1801 C  CA  . LYS   A 1 223 ? -26.67600 -13.16600 27.26900  1.000 122.54353 ? 259 LYS   A CA  1 
ATOM   1802 C  C   . LYS   A 1 223 ? -27.88900 -14.08100 27.13800  1.000 130.49845 ? 259 LYS   A C   1 
ATOM   1803 O  O   . LYS   A 1 223 ? -28.27200 -14.46100 26.02500  1.000 125.93953 ? 259 LYS   A O   1 
ATOM   1804 C  CB  . LYS   A 1 223 ? -25.42100 -13.98100 27.58500  1.000 128.22385 ? 259 LYS   A CB  1 
ATOM   1805 C  CG  . LYS   A 1 223 ? -25.02100 -14.98000 26.51800  1.000 127.31897 ? 259 LYS   A CG  1 
ATOM   1806 C  CD  . LYS   A 1 223 ? -23.75000 -15.71000 26.92300  1.000 120.52615 ? 259 LYS   A CD  1 
ATOM   1807 C  CE  . LYS   A 1 223 ? -23.27400 -16.66500 25.84300  1.000 121.21115 ? 259 LYS   A CE  1 
ATOM   1808 N  NZ  . LYS   A 1 223 ? -22.02400 -17.36800 26.24800  1.000 129.58173 ? 259 LYS   A NZ  1 
ATOM   1809 N  N   . GLN   A 1 224 ? -28.50300 -14.45200 28.26400  1.000 141.99983 ? 260 GLN   A N   1 
ATOM   1810 C  CA  . GLN   A 1 224 ? -29.66100 -15.33800 28.22800  1.000 140.97754 ? 260 GLN   A CA  1 
ATOM   1811 C  C   . GLN   A 1 224 ? -30.90700 -14.64000 27.69900  1.000 138.80518 ? 260 GLN   A C   1 
ATOM   1812 O  O   . GLN   A 1 224 ? -31.83900 -15.31800 27.25300  1.000 141.62701 ? 260 GLN   A O   1 
ATOM   1813 C  CB  . GLN   A 1 224 ? -29.92800 -15.90300 29.62300  1.000 144.45645 ? 260 GLN   A CB  1 
ATOM   1814 C  CG  . GLN   A 1 224 ? -28.70600 -16.54600 30.26100  1.000 150.28066 ? 260 GLN   A CG  1 
ATOM   1815 C  CD  . GLN   A 1 224 ? -28.98700 -17.05300 31.65700  1.000 157.57379 ? 260 GLN   A CD  1 
ATOM   1816 O  OE1 . GLN   A 1 224 ? -30.13600 -17.08600 32.09300  1.000 157.17195 ? 260 GLN   A OE1 1 
ATOM   1817 N  NE2 . GLN   A 1 224 ? -27.93800 -17.45400 32.36800  1.000 163.53909 ? 260 GLN   A NE2 1 
ATOM   1818 N  N   . LYS   A 1 225 ? -30.94600 -13.30700 27.74700  1.000 131.58357 ? 261 LYS   A N   1 
ATOM   1819 C  CA  . LYS   A 1 225 ? -32.06500 -12.57100 27.17100  1.000 135.26873 ? 261 LYS   A CA  1 
ATOM   1820 C  C   . LYS   A 1 225 ? -32.00100 -12.56200 25.64900  1.000 127.21914 ? 261 LYS   A C   1 
ATOM   1821 O  O   . LYS   A 1 225 ? -33.03800 -12.65400 24.98200  1.000 121.48683 ? 261 LYS   A O   1 
ATOM   1822 C  CB  . LYS   A 1 225 ? -32.08900 -11.14200 27.71500  1.000 131.37193 ? 261 LYS   A CB  1 
ATOM   1823 C  CG  . LYS   A 1 225 ? -33.25300 -10.30800 27.21100  1.000 125.97658 ? 261 LYS   A CG  1 
ATOM   1824 C  CD  . LYS   A 1 225 ? -33.25900 -8.92800  27.84300  1.000 119.81966 ? 261 LYS   A CD  1 
ATOM   1825 C  CE  . LYS   A 1 225 ? -34.44200 -8.11100  27.35400  1.000 108.96749 ? 261 LYS   A CE  1 
ATOM   1826 N  NZ  . LYS   A 1 225 ? -34.49400 -6.77200  27.99900  1.000 110.35930 ? 261 LYS   A NZ  1 
ATOM   1827 N  N   . TYR   A 1 226 ? -30.79800 -12.44400 25.08500  1.000 125.22324 ? 262 TYR   A N   1 
ATOM   1828 C  CA  . TYR   A 1 226 ? -30.65600 -12.48500 23.63300  1.000 114.52354 ? 262 TYR   A CA  1 
ATOM   1829 C  C   . TYR   A 1 226 ? -30.95900 -13.87700 23.09700  1.000 115.95153 ? 262 TYR   A C   1 
ATOM   1830 O  O   . TYR   A 1 226 ? -31.50300 -14.02200 21.99600  1.000 109.00902 ? 262 TYR   A O   1 
ATOM   1831 C  CB  . TYR   A 1 226 ? -29.24900 -12.04500 23.22700  1.000 112.44052 ? 262 TYR   A CB  1 
ATOM   1832 C  CG  . TYR   A 1 226 ? -28.98100 -10.56200 23.37700  1.000 111.33374 ? 262 TYR   A CG  1 
ATOM   1833 C  CD1 . TYR   A 1 226 ? -29.41100 -9.86500  24.49600  1.000 116.18373 ? 262 TYR   A CD1 1 
ATOM   1834 C  CD2 . TYR   A 1 226 ? -28.27900 -9.86100  22.40400  1.000 109.22025 ? 262 TYR   A CD2 1 
ATOM   1835 C  CE1 . TYR   A 1 226 ? -29.16100 -8.51600  24.63800  1.000 116.02122 ? 262 TYR   A CE1 1 
ATOM   1836 C  CE2 . TYR   A 1 226 ? -28.02300 -8.50500  22.54200  1.000 112.66128 ? 262 TYR   A CE2 1 
ATOM   1837 C  CZ  . TYR   A 1 226 ? -28.46600 -7.84000  23.66200  1.000 118.95980 ? 262 TYR   A CZ  1 
ATOM   1838 O  OH  . TYR   A 1 226 ? -28.22300 -6.49200  23.81000  1.000 123.37368 ? 262 TYR   A OH  1 
ATOM   1839 N  N   . GLU   A 1 227 ? -30.61300 -14.91300 23.86300  1.000 125.04402 ? 263 GLU   A N   1 
ATOM   1840 C  CA  . GLU   A 1 227 ? -30.97800 -16.27000 23.47400  1.000 128.65137 ? 263 GLU   A CA  1 
ATOM   1841 C  C   . GLU   A 1 227 ? -32.48600 -16.45500 23.51100  1.000 127.61050 ? 263 GLU   A C   1 
ATOM   1842 O  O   . GLU   A 1 227 ? -33.07900 -16.99900 22.57300  1.000 132.39286 ? 263 GLU   A O   1 
ATOM   1843 C  CB  . GLU   A 1 227 ? -30.29500 -17.28600 24.38600  1.000 151.99553 ? 263 GLU   A CB  1 
ATOM   1844 C  CG  . GLU   A 1 227 ? -28.78500 -17.30100 24.30100  1.000 143.24193 ? 263 GLU   A CG  1 
ATOM   1845 C  CD  . GLU   A 1 227 ? -28.18900 -18.46900 25.05600  1.000 152.63643 ? 263 GLU   A CD  1 
ATOM   1846 O  OE1 . GLU   A 1 227 ? -28.93800 -19.42400 25.35000  1.000 157.61228 ? 263 GLU   A OE1 1 
ATOM   1847 O  OE2 . GLU   A 1 227 ? -26.97800 -18.43100 25.35700  1.000 160.16987 ? 263 GLU   A OE2 1 
ATOM   1848 N  N   . LYS   A 1 228 ? -33.12900 -16.00700 24.59300  1.000 123.48173 ? 264 LYS   A N   1 
ATOM   1849 C  CA  . LYS   A 1 228 ? -34.57600 -16.15300 24.67800  1.000 114.19890 ? 264 LYS   A CA  1 
ATOM   1850 C  C   . LYS   A 1 228 ? -35.28800 -15.32100 23.62000  1.000 106.53247 ? 264 LYS   A C   1 
ATOM   1851 O  O   . LYS   A 1 228 ? -36.36500 -15.70800 23.15900  1.000 97.94128  ? 264 LYS   A O   1 
ATOM   1852 C  CB  . LYS   A 1 228 ? -35.07600 -15.78300 26.07400  1.000 109.94955 ? 264 LYS   A CB  1 
ATOM   1853 C  CG  . LYS   A 1 228 ? -36.55300 -16.09900 26.26500  1.000 109.25855 ? 264 LYS   A CG  1 
ATOM   1854 C  CD  . LYS   A 1 228 ? -36.87100 -16.54600 27.67900  1.000 108.53092 ? 264 LYS   A CD  1 
ATOM   1855 C  CE  . LYS   A 1 228 ? -37.50200 -15.42900 28.49300  1.000 106.81625 ? 264 LYS   A CE  1 
ATOM   1856 N  NZ  . LYS   A 1 228 ? -38.06200 -15.93900 29.78000  1.000 113.17897 ? 264 LYS   A NZ  1 
ATOM   1857 N  N   . ILE   A 1 229 ? -34.70800 -14.18900 23.21800  1.000 103.99326 ? 265 ILE   A N   1 
ATOM   1858 C  CA  . ILE   A 1 229 ? -35.31700 -13.38400 22.16300  1.000 104.17302 ? 265 ILE   A CA  1 
ATOM   1859 C  C   . ILE   A 1 229 ? -35.18900 -14.08800 20.81700  1.000 100.68024 ? 265 ILE   A C   1 
ATOM   1860 O  O   . ILE   A 1 229 ? -36.15700 -14.17900 20.05400  1.000 95.45830  ? 265 ILE   A O   1 
ATOM   1861 C  CB  . ILE   A 1 229 ? -34.69600 -11.97600 22.13600  1.000 100.78617 ? 265 ILE   A CB  1 
ATOM   1862 C  CG1 . ILE   A 1 229 ? -35.38600 -11.08000 23.16800  1.000 89.31222  ? 265 ILE   A CG1 1 
ATOM   1863 C  CG2 . ILE   A 1 229 ? -34.79300 -11.37100 20.73900  1.000 83.11162  ? 265 ILE   A CG2 1 
ATOM   1864 C  CD1 . ILE   A 1 229 ? -34.55500 -9.89700  23.61000  1.000 96.70432  ? 265 ILE   A CD1 1 
ATOM   1865 N  N   . GLY   A 1 230 ? -33.99600 -14.60100 20.50800  1.000 99.78256  ? 266 GLY   A N   1 
ATOM   1866 C  CA  . GLY   A 1 230 ? -33.81400 -15.32200 19.26000  1.000 101.53305 ? 266 GLY   A CA  1 
ATOM   1867 C  C   . GLY   A 1 230 ? -34.61400 -16.60600 19.19600  1.000 104.16376 ? 266 GLY   A C   1 
ATOM   1868 O  O   . GLY   A 1 230 ? -34.98600 -17.05700 18.11000  1.000 99.81497  ? 266 GLY   A O   1 
ATOM   1869 N  N   . ASP   A 1 231 ? -34.89100 -17.21100 20.35400  1.000 119.37257 ? 267 ASP   A N   1 
ATOM   1870 C  CA  . ASP   A 1 231 ? -35.72200 -18.40900 20.38200  1.000 116.08322 ? 267 ASP   A CA  1 
ATOM   1871 C  C   . ASP   A 1 231 ? -37.15400 -18.09800 19.96400  1.000 112.29115 ? 267 ASP   A C   1 
ATOM   1872 O  O   . ASP   A 1 231 ? -37.76700 -18.87000 19.21900  1.000 121.28498 ? 267 ASP   A O   1 
ATOM   1873 C  CB  . ASP   A 1 231 ? -35.69200 -19.04000 21.77600  1.000 114.68482 ? 267 ASP   A CB  1 
ATOM   1874 C  CG  . ASP   A 1 231 ? -34.35800 -19.69200 22.09600  1.000 119.80433 ? 267 ASP   A CG  1 
ATOM   1875 O  OD1 . ASP   A 1 231 ? -33.46200 -19.68000 21.22600  1.000 117.91494 ? 267 ASP   A OD1 1 
ATOM   1876 O  OD2 . ASP   A 1 231 ? -34.20500 -20.21600 23.22000  1.000 122.02182 ? 267 ASP   A OD2 1 
ATOM   1877 N  N   . LYS   A 1 232 ? -37.70500 -16.97100 20.42600  1.000 99.67384  ? 268 LYS   A N   1 
ATOM   1878 C  CA  . LYS   A 1 232 ? -39.06800 -16.61800 20.04200  1.000 98.97446  ? 268 LYS   A CA  1 
ATOM   1879 C  C   . LYS   A 1 232 ? -39.17600 -16.36300 18.54600  1.000 90.51552  ? 268 LYS   A C   1 
ATOM   1880 O  O   . LYS   A 1 232 ? -40.25200 -16.53200 17.96300  1.000 84.60206  ? 268 LYS   A O   1 
ATOM   1881 C  CB  . LYS   A 1 232 ? -39.54800 -15.38800 20.81500  1.000 91.86360  ? 268 LYS   A CB  1 
ATOM   1882 C  CG  . LYS   A 1 232 ? -39.29700 -15.44100 22.30900  1.000 100.94344 ? 268 LYS   A CG  1 
ATOM   1883 C  CD  . LYS   A 1 232 ? -40.52100 -15.01700 23.10000  1.000 105.23422 ? 268 LYS   A CD  1 
ATOM   1884 C  CE  . LYS   A 1 232 ? -41.20900 -16.22400 23.71700  1.000 106.96498 ? 268 LYS   A CE  1 
ATOM   1885 N  NZ  . LYS   A 1 232 ? -42.38500 -15.83800 24.54300  1.000 98.27270  ? 268 LYS   A NZ  1 
ATOM   1886 N  N   . LYS   A 1 233 ? -38.07400 -15.96400 17.90800  1.000 86.32360  ? 269 LYS   A N   1 
ATOM   1887 C  CA  . LYS   A 1 233 ? -38.11300 -15.68800 16.47700  1.000 85.96147  ? 269 LYS   A CA  1 
ATOM   1888 C  C   . LYS   A 1 233 ? -38.16400 -16.97000 15.65700  1.000 99.15518  ? 269 LYS   A C   1 
ATOM   1889 O  O   . LYS   A 1 233 ? -38.71600 -16.97300 14.55100  1.000 100.32966 ? 269 LYS   A O   1 
ATOM   1890 C  CB  . LYS   A 1 233 ? -36.91200 -14.83200 16.08200  1.000 85.14191  ? 269 LYS   A CB  1 
ATOM   1891 C  CG  . LYS   A 1 233 ? -36.85200 -13.51500 16.84200  1.000 92.80043  ? 269 LYS   A CG  1 
ATOM   1892 C  CD  . LYS   A 1 233 ? -35.73200 -12.61800 16.34500  1.000 86.10629  ? 269 LYS   A CD  1 
ATOM   1893 C  CE  . LYS   A 1 233 ? -35.68400 -11.32800 17.14800  1.000 84.58668  ? 269 LYS   A CE  1 
ATOM   1894 N  NZ  . LYS   A 1 233 ? -34.54400 -10.45500 16.76000  1.000 76.61491  ? 269 LYS   A NZ  1 
ATOM   1895 N  N   . ARG   A 1 234 ? -37.60800 -18.06700 16.17600  1.000 93.52874  ? 270 ARG   A N   1 
ATOM   1896 C  CA  . ARG   A 1 234 ? -37.68700 -19.34100 15.47300  1.000 99.52950  ? 270 ARG   A CA  1 
ATOM   1897 C  C   . ARG   A 1 234 ? -38.99800 -20.07300 15.72500  1.000 102.31934 ? 270 ARG   A C   1 
ATOM   1898 O  O   . ARG   A 1 234 ? -39.37000 -20.93800 14.92400  1.000 104.49021 ? 270 ARG   A O   1 
ATOM   1899 C  CB  . ARG   A 1 234 ? -36.51700 -20.24600 15.86800  1.000 97.08959  ? 270 ARG   A CB  1 
ATOM   1900 C  CG  . ARG   A 1 234 ? -35.18300 -19.83900 15.26900  1.000 95.23866  ? 270 ARG   A CG  1 
ATOM   1901 C  CD  . ARG   A 1 234 ? -34.28700 -21.05100 15.07500  1.000 79.78194  ? 270 ARG   A CD  1 
ATOM   1902 N  NE  . ARG   A 1 234 ? -33.00200 -20.90500 15.74700  1.000 99.96508  ? 270 ARG   A NE  1 
ATOM   1903 C  CZ  . ARG   A 1 234 ? -32.76200 -21.28800 16.99400  1.000 109.84511 ? 270 ARG   A CZ  1 
ATOM   1904 N  NH1 . ARG   A 1 234 ? -33.70500 -21.83500 17.74300  1.000 93.81900  ? 270 ARG   A NH1 1 
ATOM   1905 N  NH2 . ARG   A 1 234 ? -31.54600 -21.11800 17.50200  1.000 110.24111 ? 270 ARG   A NH2 1 
ATOM   1906 N  N   . THR   A 1 235 ? -39.70300 -19.75300 16.81000  1.000 92.43107  ? 271 THR   A N   1 
ATOM   1907 C  CA  . THR   A 1 235 ? -40.97300 -20.40000 17.10800  1.000 101.19958 ? 271 THR   A CA  1 
ATOM   1908 C  C   . THR   A 1 235 ? -42.16300 -19.70800 16.46000  1.000 101.84626 ? 271 THR   A C   1 
ATOM   1909 O  O   . THR   A 1 235 ? -43.22300 -20.32800 16.32300  1.000 99.51027  ? 271 THR   A O   1 
ATOM   1910 C  CB  . THR   A 1 235 ? -41.20400 -20.46200 18.62200  1.000 93.85247  ? 271 THR   A CB  1 
ATOM   1911 O  OG1 . THR   A 1 235 ? -41.38100 -19.13600 19.13600  1.000 109.55454 ? 271 THR   A OG1 1 
ATOM   1912 C  CG2 . THR   A 1 235 ? -40.02300 -21.12000 19.31800  1.000 100.35212 ? 271 THR   A CG2 1 
ATOM   1913 N  N   . THR   A 1 236 ? -42.01600 -18.44400 16.06300  1.000 102.63569 ? 272 THR   A N   1 
ATOM   1914 C  CA  . THR   A 1 236 ? -43.11600 -17.69800 15.47300  1.000 100.50628 ? 272 THR   A CA  1 
ATOM   1915 C  C   . THR   A 1 236 ? -42.98000 -17.70100 13.95900  1.000 104.10474 ? 272 THR   A C   1 
ATOM   1916 O  O   . THR   A 1 236 ? -42.04600 -17.07800 13.43000  1.000 92.22166  ? 272 THR   A O   1 
ATOM   1917 C  CB  . THR   A 1 236 ? -43.14300 -16.26400 16.00000  1.000 96.53470  ? 272 THR   A CB  1 
ATOM   1918 O  OG1 . THR   A 1 236 ? -41.87000 -15.64300 15.78100  1.000 95.25577  ? 272 THR   A OG1 1 
ATOM   1919 C  CG2 . THR   A 1 236 ? -43.46200 -16.24800 17.48800  1.000 86.37257  ? 272 THR   A CG2 1 
ATOM   1920 N  N   . PRO   A 1 237 ? -43.86000 -18.37900 13.22500  1.000 114.06177 ? 273 PRO   A N   1 
ATOM   1921 C  CA  . PRO   A 1 237 ? -43.84000 -18.27000 11.76200  1.000 106.53900 ? 273 PRO   A CA  1 
ATOM   1922 C  C   . PRO   A 1 237 ? -44.15200 -16.84900 11.31900  1.000 106.00695 ? 273 PRO   A C   1 
ATOM   1923 O  O   . PRO   A 1 237 ? -44.56100 -15.98900 12.10200  1.000 100.58681 ? 273 PRO   A O   1 
ATOM   1924 C  CB  . PRO   A 1 237 ? -44.92900 -19.25100 11.31200  1.000 113.83932 ? 273 PRO   A CB  1 
ATOM   1925 C  CG  . PRO   A 1 237 ? -45.08900 -20.19800 12.46300  1.000 120.95877 ? 273 PRO   A CG  1 
ATOM   1926 C  CD  . PRO   A 1 237 ? -44.84100 -19.37400 13.69100  1.000 117.59439 ? 273 PRO   A CD  1 
ATOM   1927 N  N   . ALA   A 1 238 ? -43.94700 -16.60200 10.02500  1.000 105.26819 ? 274 ALA   A N   1 
ATOM   1928 C  CA  . ALA   A 1 238 ? -44.26000 -15.29500 9.46500   1.000 95.68687  ? 274 ALA   A CA  1 
ATOM   1929 C  C   . ALA   A 1 238 ? -45.75600 -15.07200 9.30300   1.000 92.53881  ? 274 ALA   A C   1 
ATOM   1930 O  O   . ALA   A 1 238 ? -46.18700 -13.92300 9.16300   1.000 91.76417  ? 274 ALA   A O   1 
ATOM   1931 C  CB  . ALA   A 1 238 ? -43.56400 -15.11800 8.11400   1.000 83.71672  ? 274 ALA   A CB  1 
ATOM   1932 N  N   . VAL   A 1 239 ? -46.55500 -16.14000 9.32200   1.000 92.21603  ? 275 VAL   A N   1 
ATOM   1933 C  CA  . VAL   A 1 239 ? -47.99500 -15.99200 9.14500   1.000 95.11693  ? 275 VAL   A CA  1 
ATOM   1934 C  C   . VAL   A 1 239 ? -48.63400 -15.44300 10.41300  1.000 102.25970 ? 275 VAL   A C   1 
ATOM   1935 O  O   . VAL   A 1 239 ? -49.51500 -14.57500 10.35800  1.000 102.74419 ? 275 VAL   A O   1 
ATOM   1936 C  CB  . VAL   A 1 239 ? -48.61600 -17.33700 8.72700   1.000 105.69476 ? 275 VAL   A CB  1 
ATOM   1937 C  CG1 . VAL   A 1 239 ? -50.12000 -17.20200 8.54000   1.000 106.96939 ? 275 VAL   A CG1 1 
ATOM   1938 C  CG2 . VAL   A 1 239 ? -47.95800 -17.84600 7.45500   1.000 107.49344 ? 275 VAL   A CG2 1 
ATOM   1939 N  N   . THR   A 1 240 ? -48.19200 -15.92600 11.57500  1.000 101.99902 ? 276 THR   A N   1 
ATOM   1940 C  CA  . THR   A 1 240 ? -48.74800 -15.45100 12.83600  1.000 107.02051 ? 276 THR   A CA  1 
ATOM   1941 C  C   . THR   A 1 240 ? -48.36100 -14.00100 13.11300  1.000 104.26292 ? 276 THR   A C   1 
ATOM   1942 O  O   . THR   A 1 240 ? -49.18500 -13.23000 13.61800  1.000 114.91015 ? 276 THR   A O   1 
ATOM   1943 C  CB  . THR   A 1 240 ? -48.31000 -16.38600 13.96600  1.000 110.09301 ? 276 THR   A CB  1 
ATOM   1944 O  OG1 . THR   A 1 240 ? -49.10200 -17.58200 13.92400  1.000 126.00394 ? 276 THR   A OG1 1 
ATOM   1945 C  CG2 . THR   A 1 240 ? -48.46300 -15.72900 15.32200  1.000 107.64050 ? 276 THR   A CG2 1 
ATOM   1946 N  N   . LEU   A 1 241 ? -47.13000 -13.60100 12.77400  1.000 95.80469  ? 277 LEU   A N   1 
ATOM   1947 C  CA  . LEU   A 1 241 ? -46.77200 -12.18800 12.86200  1.000 93.87849  ? 277 LEU   A CA  1 
ATOM   1948 C  C   . LEU   A 1 241 ? -47.62700 -11.33100 11.93700  1.000 93.84172  ? 277 LEU   A C   1 
ATOM   1949 O  O   . LEU   A 1 241 ? -47.85100 -10.14900 12.22100  1.000 92.04122  ? 277 LEU   A O   1 
ATOM   1950 C  CB  . LEU   A 1 241 ? -45.29300 -11.98300 12.53400  1.000 88.75771  ? 277 LEU   A CB  1 
ATOM   1951 C  CG  . LEU   A 1 241 ? -44.29500 -12.29700 13.64600  1.000 82.67169  ? 277 LEU   A CG  1 
ATOM   1952 C  CD1 . LEU   A 1 241 ? -42.98900 -11.55000 13.41800  1.000 87.93600  ? 277 LEU   A CD1 1 
ATOM   1953 C  CD2 . LEU   A 1 241 ? -44.88800 -11.95000 14.99800  1.000 76.11089  ? 277 LEU   A CD2 1 
ATOM   1954 N  N   . CYS   A 1 242 ? -48.10800 -11.90300 10.83300  1.000 91.29436  ? 278 CYS   A N   1 
ATOM   1955 C  CA  . CYS   A 1 242 ? -48.93300 -11.18300 9.87100   1.000 85.97348  ? 278 CYS   A CA  1 
ATOM   1956 C  C   . CYS   A 1 242 ? -50.42400 -11.32000 10.16100  1.000 97.17880  ? 278 CYS   A C   1 
ATOM   1957 O  O   . CYS   A 1 242 ? -51.24600 -11.20700 9.24000   1.000 101.99372 ? 278 CYS   A O   1 
ATOM   1958 C  CB  . CYS   A 1 242 ? -48.61600 -11.66200 8.45400   1.000 86.75223  ? 278 CYS   A CB  1 
ATOM   1959 S  SG  . CYS   A 1 242 ? -48.84200 -10.40600 7.18600   1.000 97.51419  ? 278 CYS   A SG  1 
ATOM   1960 N  N   . ASP   A 1 243 ? -50.79300 -11.56200 11.41700  1.000 98.67818  ? 279 ASP   A N   1 
ATOM   1961 C  CA  . ASP   A 1 243 ? -52.19500 -11.71600 11.78600  1.000 104.09385 ? 279 ASP   A CA  1 
ATOM   1962 C  C   . ASP   A 1 243 ? -52.95700 -10.42000 11.54000  1.000 108.96032 ? 279 ASP   A C   1 
ATOM   1963 O  O   . ASP   A 1 243 ? -52.65200 -9.38500  12.14200  1.000 108.40611 ? 279 ASP   A O   1 
ATOM   1964 C  CB  . ASP   A 1 243 ? -52.30200 -12.13700 13.25300  1.000 103.52866 ? 279 ASP   A CB  1 
ATOM   1965 C  CG  . ASP   A 1 243 ? -53.72300 -12.06000 13.78800  1.000 109.81504 ? 279 ASP   A CG  1 
ATOM   1966 O  OD1 . ASP   A 1 243 ? -54.17600 -10.95000 14.14000  1.000 98.04962  ? 279 ASP   A OD1 1 
ATOM   1967 O  OD2 . ASP   A 1 243 ? -54.38900 -13.11400 13.85300  1.000 95.66896  ? 279 ASP   A OD2 1 
ATOM   1968 N  N   . GLY   A 1 244 ? -53.95400 -10.48100 10.65900  1.000 167.83517 ? 280 GLY   A N   1 
ATOM   1969 C  CA  . GLY   A 1 244 ? -54.73500 -9.30700  10.32700  1.000 171.19167 ? 280 GLY   A CA  1 
ATOM   1970 C  C   . GLY   A 1 244 ? -54.00700 -8.26200  9.51700   1.000 170.48826 ? 280 GLY   A C   1 
ATOM   1971 O  O   . GLY   A 1 244 ? -54.49000 -7.13100  9.41400   1.000 178.21746 ? 280 GLY   A O   1 
ATOM   1972 N  N   . LEU   A 1 245 ? -52.86300 -8.60200  8.93900   1.000 116.19306 ? 281 LEU   A N   1 
ATOM   1973 C  CA  . LEU   A 1 245 ? -52.04900 -7.69100  8.15700   1.000 102.34716 ? 281 LEU   A CA  1 
ATOM   1974 C  C   . LEU   A 1 245 ? -51.90900 -8.20900  6.73200   1.000 96.68010  ? 281 LEU   A C   1 
ATOM   1975 O  O   . LEU   A 1 245 ? -52.09800 -9.40400  6.47600   1.000 98.37049  ? 281 LEU   A O   1 
ATOM   1976 C  CB  . LEU   A 1 245 ? -50.66100 -7.52300  8.79300   1.000 96.28267  ? 281 LEU   A CB  1 
ATOM   1977 C  CG  . LEU   A 1 245 ? -50.65300 -6.96700  10.21800  1.000 97.26112  ? 281 LEU   A CG  1 
ATOM   1978 C  CD1 . LEU   A 1 245 ? -49.23000 -6.84700  10.73500  1.000 91.04476  ? 281 LEU   A CD1 1 
ATOM   1979 C  CD2 . LEU   A 1 245 ? -51.36600 -5.62300  10.27900  1.000 98.80429  ? 281 LEU   A CD2 1 
ATOM   1980 N  N   . PRO   A 1 246 ? -51.59900 -7.33200  5.77500   1.000 84.94494  ? 282 PRO   A N   1 
ATOM   1981 C  CA  . PRO   A 1 246 ? -51.41500 -7.78500  4.38900   1.000 84.71945  ? 282 PRO   A CA  1 
ATOM   1982 C  C   . PRO   A 1 246 ? -50.33500 -8.85400  4.29100   1.000 95.15710  ? 282 PRO   A C   1 
ATOM   1983 O  O   . PRO   A 1 246 ? -49.19700 -8.65200  4.71900   1.000 87.83028  ? 282 PRO   A O   1 
ATOM   1984 C  CB  . PRO   A 1 246 ? -51.01700 -6.50300  3.65100   1.000 86.83566  ? 282 PRO   A CB  1 
ATOM   1985 C  CG  . PRO   A 1 246 ? -51.62800 -5.40800  4.46000   1.000 82.11330  ? 282 PRO   A CG  1 
ATOM   1986 C  CD  . PRO   A 1 246 ? -51.54300 -5.86400  5.88800   1.000 80.62120  ? 282 PRO   A CD  1 
ATOM   1987 N  N   . GLN   A 1 247 ? -50.70600 -9.99500  3.70100   1.000 95.33707  ? 283 GLN   A N   1 
ATOM   1988 C  CA  . GLN   A 1 247 ? -49.84700 -11.17600 3.69700   1.000 97.37384  ? 283 GLN   A CA  1 
ATOM   1989 C  C   . GLN   A 1 247 ? -48.53500 -10.95400 2.95600   1.000 97.70374  ? 283 GLN   A C   1 
ATOM   1990 O  O   . GLN   A 1 247 ? -47.60600 -11.75300 3.11800   1.000 96.00922  ? 283 GLN   A O   1 
ATOM   1991 C  CB  . GLN   A 1 247 ? -50.59400 -12.35800 3.07700   1.000 101.87091 ? 283 GLN   A CB  1 
ATOM   1992 C  CG  . GLN   A 1 247 ? -50.12900 -13.72300 3.56300   1.000 111.59470 ? 283 GLN   A CG  1 
ATOM   1993 C  CD  . GLN   A 1 247 ? -50.62600 -14.04500 4.96000   1.000 120.88585 ? 283 GLN   A CD  1 
ATOM   1994 O  OE1 . GLN   A 1 247 ? -51.49100 -13.35300 5.49900   1.000 120.33767 ? 283 GLN   A OE1 1 
ATOM   1995 N  NE2 . GLN   A 1 247 ? -50.08200 -15.10100 5.55300   1.000 115.49796 ? 283 GLN   A NE2 1 
ATOM   1996 N  N   . GLN   A 1 248 ? -48.43500 -9.90000  2.14200   1.000 96.36646  ? 284 GLN   A N   1 
ATOM   1997 C  CA  . GLN   A 1 248 ? -47.17500 -9.61300  1.46500   1.000 92.42513  ? 284 GLN   A CA  1 
ATOM   1998 C  C   . GLN   A 1 248 ? -46.05500 -9.28900  2.44400   1.000 78.61467  ? 284 GLN   A C   1 
ATOM   1999 O  O   . GLN   A 1 248 ? -44.88000 -9.43500  2.09100   1.000 67.64455  ? 284 GLN   A O   1 
ATOM   2000 C  CB  . GLN   A 1 248 ? -47.35000 -8.45800  0.47900   1.000 81.93658  ? 284 GLN   A CB  1 
ATOM   2001 C  CG  . GLN   A 1 248 ? -48.14100 -8.81700  -0.76600  1.000 88.42198  ? 284 GLN   A CG  1 
ATOM   2002 C  CD  . GLN   A 1 248 ? -49.48100 -8.11600  -0.83000  1.000 81.55194  ? 284 GLN   A CD  1 
ATOM   2003 O  OE1 . GLN   A 1 248 ? -50.19200 -8.01700  0.17100   1.000 75.78758  ? 284 GLN   A OE1 1 
ATOM   2004 N  NE2 . GLN   A 1 248 ? -49.83200 -7.61900  -2.01000  1.000 76.89811  ? 284 GLN   A NE2 1 
ATOM   2005 N  N   . PHE   A 1 249 ? -46.38700 -8.84500  3.65900   1.000 77.72199  ? 285 PHE   A N   1 
ATOM   2006 C  CA  . PHE   A 1 249 ? -45.35900 -8.63900  4.67400   1.000 73.09700  ? 285 PHE   A CA  1 
ATOM   2007 C  C   . PHE   A 1 249 ? -44.81300 -9.96100  5.19300   1.000 75.06350  ? 285 PHE   A C   1 
ATOM   2008 O  O   . PHE   A 1 249 ? -43.62900 -10.04600 5.53900   1.000 72.08336  ? 285 PHE   A O   1 
ATOM   2009 C  CB  . PHE   A 1 249 ? -45.91400 -7.80000  5.82500   1.000 71.00470  ? 285 PHE   A CB  1 
ATOM   2010 C  CG  . PHE   A 1 249 ? -46.04800 -6.34100  5.49700   1.000 75.84686  ? 285 PHE   A CG  1 
ATOM   2011 C  CD1 . PHE   A 1 249 ? -45.00700 -5.65600  4.89800   1.000 78.05692  ? 285 PHE   A CD1 1 
ATOM   2012 C  CD2 . PHE   A 1 249 ? -47.21400 -5.65200  5.78300   1.000 66.64173  ? 285 PHE   A CD2 1 
ATOM   2013 C  CE1 . PHE   A 1 249 ? -45.12600 -4.31100  4.59100   1.000 65.91668  ? 285 PHE   A CE1 1 
ATOM   2014 C  CE2 . PHE   A 1 249 ? -47.33600 -4.30600  5.47400   1.000 75.78501  ? 285 PHE   A CE2 1 
ATOM   2015 C  CZ  . PHE   A 1 249 ? -46.29100 -3.63800  4.88000   1.000 67.67792  ? 285 PHE   A CZ  1 
ATOM   2016 N  N   . ALA   A 1 250 ? -45.65000 -10.99900 5.25300   1.000 75.36408  ? 286 ALA   A N   1 
ATOM   2017 C  CA  . ALA   A 1 250 ? -45.15700 -12.31500 5.64300   1.000 74.99310  ? 286 ALA   A CA  1 
ATOM   2018 C  C   . ALA   A 1 250 ? -44.32100 -12.93800 4.53200   1.000 63.67859  ? 286 ALA   A C   1 
ATOM   2019 O  O   . ALA   A 1 250 ? -43.32300 -13.61500 4.80400   1.000 83.01333  ? 286 ALA   A O   1 
ATOM   2020 C  CB  . ALA   A 1 250 ? -46.32500 -13.22800 6.01400   1.000 81.81008  ? 286 ALA   A CB  1 
ATOM   2021 N  N   . GLU   A 1 251 ? -44.71700 -12.72100 3.27500   1.000 60.44078  ? 287 GLU   A N   1 
ATOM   2022 C  CA  . GLU   A 1 251 ? -43.94100 -13.24000 2.15300   1.000 73.67230  ? 287 GLU   A CA  1 
ATOM   2023 C  C   . GLU   A 1 251 ? -42.55200 -12.61900 2.10500   1.000 71.15859  ? 287 GLU   A C   1 
ATOM   2024 O  O   . GLU   A 1 251 ? -41.57500 -13.29200 1.75900   1.000 73.50990  ? 287 GLU   A O   1 
ATOM   2025 C  CB  . GLU   A 1 251 ? -44.67800 -12.98500 0.83900   1.000 63.30544  ? 287 GLU   A CB  1 
ATOM   2026 C  CG  . GLU   A 1 251 ? -45.81000 -13.94900 0.55200   1.000 87.63919  ? 287 GLU   A CG  1 
ATOM   2027 C  CD  . GLU   A 1 251 ? -45.69300 -14.57000 -0.82500  1.000 103.16564 ? 287 GLU   A CD  1 
ATOM   2028 O  OE1 . GLU   A 1 251 ? -45.68800 -13.81200 -1.81800  1.000 100.19603 ? 287 GLU   A OE1 1 
ATOM   2029 O  OE2 . GLU   A 1 251 ? -45.58900 -15.81100 -0.91400  1.000 98.61722  ? 287 GLU   A OE2 1 
ATOM   2030 N  N   . TYR   A 1 252 ? -42.44600 -11.33100 2.44100   1.000 63.73188  ? 288 TYR   A N   1 
ATOM   2031 C  CA  . TYR   A 1 252 ? -41.15000 -10.66000 2.40200   1.000 63.95333  ? 288 TYR   A CA  1 
ATOM   2032 C  C   . TYR   A 1 252 ? -40.18600 -11.26800 3.41200   1.000 63.07219  ? 288 TYR   A C   1 
ATOM   2033 O  O   . TYR   A 1 252 ? -39.05900 -11.64200 3.06500   1.000 58.72384  ? 288 TYR   A O   1 
ATOM   2034 C  CB  . TYR   A 1 252 ? -41.32600 -9.16200  2.65700   1.000 65.90591  ? 288 TYR   A CB  1 
ATOM   2035 C  CG  . TYR   A 1 252 ? -40.02300 -8.42200  2.87300   1.000 46.85732  ? 288 TYR   A CG  1 
ATOM   2036 C  CD1 . TYR   A 1 252 ? -39.24800 -8.01100  1.79600   1.000 65.10952  ? 288 TYR   A CD1 1 
ATOM   2037 C  CD2 . TYR   A 1 252 ? -39.56800 -8.13500  4.15400   1.000 51.61427  ? 288 TYR   A CD2 1 
ATOM   2038 C  CE1 . TYR   A 1 252 ? -38.05700 -7.33600  1.98900   1.000 59.33764  ? 288 TYR   A CE1 1 
ATOM   2039 C  CE2 . TYR   A 1 252 ? -38.37800 -7.46300  4.35600   1.000 56.17040  ? 288 TYR   A CE2 1 
ATOM   2040 C  CZ  . TYR   A 1 252 ? -37.62700 -7.06500  3.27000   1.000 62.31712  ? 288 TYR   A CZ  1 
ATOM   2041 O  OH  . TYR   A 1 252 ? -36.44300 -6.39400  3.46600   1.000 62.82644  ? 288 TYR   A OH  1 
ATOM   2042 N  N   . LEU   A 1 253 ? -40.61400 -11.37600 4.67200   1.000 60.86686  ? 289 LEU   A N   1 
ATOM   2043 C  CA  . LEU   A 1 253 ? -39.72800 -11.88600 5.71400   1.000 49.95379  ? 289 LEU   A CA  1 
ATOM   2044 C  C   . LEU   A 1 253 ? -39.32700 -13.33100 5.44300   1.000 75.76809  ? 289 LEU   A C   1 
ATOM   2045 O  O   . LEU   A 1 253 ? -38.17500 -13.71600 5.67500   1.000 75.13922  ? 289 LEU   A O   1 
ATOM   2046 C  CB  . LEU   A 1 253 ? -40.40200 -11.76200 7.07900   1.000 54.99388  ? 289 LEU   A CB  1 
ATOM   2047 C  CG  . LEU   A 1 253 ? -39.56400 -12.17500 8.28900   1.000 68.72101  ? 289 LEU   A CG  1 
ATOM   2048 C  CD1 . LEU   A 1 253 ? -38.31900 -11.30800 8.40200   1.000 59.91633  ? 289 LEU   A CD1 1 
ATOM   2049 C  CD2 . LEU   A 1 253 ? -40.39200 -12.09900 9.56100   1.000 50.73870  ? 289 LEU   A CD2 1 
ATOM   2050 N  N   . ASP   A 1 254 ? -40.26200 -14.14600 4.94800   1.000 56.79553  ? 290 ASP   A N   1 
ATOM   2051 C  CA  . ASP   A 1 254 ? -39.93800 -15.53400 4.63400   1.000 76.14078  ? 290 ASP   A CA  1 
ATOM   2052 C  C   . ASP   A 1 254 ? -38.94700 -15.62700 3.48100   1.000 71.99147  ? 290 ASP   A C   1 
ATOM   2053 O  O   . ASP   A 1 254 ? -38.07800 -16.50600 3.47200   1.000 74.64401  ? 290 ASP   A O   1 
ATOM   2054 C  CB  . ASP   A 1 254 ? -41.21100 -16.31200 4.30400   1.000 74.71403  ? 290 ASP   A CB  1 
ATOM   2055 C  CG  . ASP   A 1 254 ? -41.93100 -16.80400 5.54100   1.000 94.13531  ? 290 ASP   A CG  1 
ATOM   2056 O  OD1 . ASP   A 1 254 ? -41.26200 -17.00900 6.57600   1.000 87.60019  ? 290 ASP   A OD1 1 
ATOM   2057 O  OD2 . ASP   A 1 254 ? -43.16400 -16.99300 5.47800   1.000 109.72170 ? 290 ASP   A OD2 1 
ATOM   2058 N  N   . SER   A 1 255 ? -39.06100 -14.72900 2.50000   1.000 70.24017  ? 291 SER   A N   1 
ATOM   2059 C  CA  . SER   A 1 255 ? -38.18300 -14.79600 1.33700   1.000 82.48623  ? 291 SER   A CA  1 
ATOM   2060 C  C   . SER   A 1 255 ? -36.75900 -14.38200 1.69000   1.000 81.68349  ? 291 SER   A C   1 
ATOM   2061 O  O   . SER   A 1 255 ? -35.79600 -15.03400 1.26700   1.000 63.05533  ? 291 SER   A O   1 
ATOM   2062 C  CB  . SER   A 1 255 ? -38.73400 -13.91900 0.21300   1.000 75.70247  ? 291 SER   A CB  1 
ATOM   2063 O  OG  . SER   A 1 255 ? -37.94100 -14.03300 -0.95600  1.000 61.84217  ? 291 SER   A OG  1 
ATOM   2064 N  N   . VAL   A 1 256 ? -36.60300 -13.30400 2.46300   1.000 49.65674  ? 292 VAL   A N   1 
ATOM   2065 C  CA  . VAL   A 1 256 ? -35.26800 -12.84200 2.82600   1.000 68.37449  ? 292 VAL   A CA  1 
ATOM   2066 C  C   . VAL   A 1 256 ? -34.59300 -13.79100 3.80600   1.000 76.08314  ? 292 VAL   A C   1 
ATOM   2067 O  O   . VAL   A 1 256 ? -33.36300 -13.77600 3.92900   1.000 82.06371  ? 292 VAL   A O   1 
ATOM   2068 C  CB  . VAL   A 1 256 ? -35.32600 -11.41500 3.40200   1.000 71.20399  ? 292 VAL   A CB  1 
ATOM   2069 C  CG1 . VAL   A 1 256 ? -36.06900 -10.48900 2.44900   1.000 72.68156  ? 292 VAL   A CG1 1 
ATOM   2070 C  CG2 . VAL   A 1 256 ? -35.97700 -11.41800 4.77700   1.000 62.23336  ? 292 VAL   A CG2 1 
ATOM   2071 N  N   . ARG   A 1 257 ? -35.36600 -14.61800 4.51000   1.000 68.14466  ? 293 ARG   A N   1 
ATOM   2072 C  CA  . ARG   A 1 257 ? -34.79800 -15.63500 5.38500   1.000 79.19657  ? 293 ARG   A CA  1 
ATOM   2073 C  C   . ARG   A 1 257 ? -34.37000 -16.88600 4.63100   1.000 74.66805  ? 293 ARG   A C   1 
ATOM   2074 O  O   . ARG   A 1 257 ? -33.68800 -17.73600 5.21200   1.000 83.43084  ? 293 ARG   A O   1 
ATOM   2075 C  CB  . ARG   A 1 257 ? -35.80400 -16.01100 6.47600   1.000 79.03021  ? 293 ARG   A CB  1 
ATOM   2076 C  CG  . ARG   A 1 257 ? -35.92000 -14.98700 7.59400   1.000 85.55088  ? 293 ARG   A CG  1 
ATOM   2077 C  CD  . ARG   A 1 257 ? -37.04700 -15.34700 8.54800   1.000 89.52755  ? 293 ARG   A CD  1 
ATOM   2078 N  NE  . ARG   A 1 257 ? -36.99500 -14.56500 9.77800   1.000 75.23245  ? 293 ARG   A NE  1 
ATOM   2079 C  CZ  . ARG   A 1 257 ? -37.90300 -14.62700 10.74200  1.000 77.63163  ? 293 ARG   A CZ  1 
ATOM   2080 N  NH1 . ARG   A 1 257 ? -38.96300 -15.41200 10.64400  1.000 74.66617  ? 293 ARG   A NH1 1 
ATOM   2081 N  NH2 . ARG   A 1 257 ? -37.74400 -13.88100 11.83200  1.000 74.09372  ? 293 ARG   A NH2 1 
ATOM   2082 N  N   . SER   A 1 258 ? -34.75000 -17.01700 3.36200   1.000 74.79924  ? 294 SER   A N   1 
ATOM   2083 C  CA  . SER   A 1 258 ? -34.37400 -18.15600 2.53900   1.000 81.69549  ? 294 SER   A CA  1 
ATOM   2084 C  C   . SER   A 1 258 ? -33.26500 -17.82000 1.55100   1.000 79.73391  ? 294 SER   A C   1 
ATOM   2085 O  O   . SER   A 1 258 ? -32.94600 -18.64400 0.68800   1.000 71.85541  ? 294 SER   A O   1 
ATOM   2086 C  CB  . SER   A 1 258 ? -35.59700 -18.69200 1.79300   1.000 78.58357  ? 294 SER   A CB  1 
ATOM   2087 O  OG  . SER   A 1 258 ? -36.65800 -18.96700 2.69000   1.000 76.12524  ? 294 SER   A OG  1 
ATOM   2088 N  N   . LEU   A 1 259 ? -32.67400 -16.63200 1.65500   1.000 80.75099  ? 295 LEU   A N   1 
ATOM   2089 C  CA  . LEU   A 1 259 ? -31.61100 -16.23300 0.74400   1.000 83.26190  ? 295 LEU   A CA  1 
ATOM   2090 C  C   . LEU   A 1 259 ? -30.29000 -16.88400 1.15000   1.000 68.04387  ? 295 LEU   A C   1 
ATOM   2091 O  O   . LEU   A 1 259 ? -29.96700 -16.94500 2.33900   1.000 63.36680  ? 295 LEU   A O   1 
ATOM   2092 C  CB  . LEU   A 1 259 ? -31.44900 -14.71400 0.73600   1.000 79.68678  ? 295 LEU   A CB  1 
ATOM   2093 C  CG  . LEU   A 1 259 ? -32.49400 -13.89100 -0.01800  1.000 73.67063  ? 295 LEU   A CG  1 
ATOM   2094 C  CD1 . LEU   A 1 259 ? -32.24700 -12.40600 0.19100   1.000 69.50742  ? 295 LEU   A CD1 1 
ATOM   2095 C  CD2 . LEU   A 1 259 ? -32.47200 -14.23600 -1.49800  1.000 77.65633  ? 295 LEU   A CD2 1 
ATOM   2096 N  N   . PRO   A 1 260 ? -29.51700 -17.38200 0.18600   1.000 74.57584  ? 296 PRO   A N   1 
ATOM   2097 C  CA  . PRO   A 1 260 ? -28.15900 -17.84700 0.49200   1.000 85.94453  ? 296 PRO   A CA  1 
ATOM   2098 C  C   . PRO   A 1 260 ? -27.30100 -16.71900 1.04500   1.000 83.30651  ? 296 PRO   A C   1 
ATOM   2099 O  O   . PRO   A 1 260 ? -27.64400 -15.53600 0.97800   1.000 78.02925  ? 296 PRO   A O   1 
ATOM   2100 C  CB  . PRO   A 1 260 ? -27.63800 -18.34100 -0.86200  1.000 87.85635  ? 296 PRO   A CB  1 
ATOM   2101 C  CG  . PRO   A 1 260 ? -28.87100 -18.69400 -1.62900  1.000 90.61343  ? 296 PRO   A CG  1 
ATOM   2102 C  CD  . PRO   A 1 260 ? -29.92100 -17.71100 -1.19100  1.000 74.55214  ? 296 PRO   A CD  1 
ATOM   2103 N  N   . PHE   A 1 261 ? -26.15200 -17.10800 1.60000   1.000 92.46709  ? 297 PHE   A N   1 
ATOM   2104 C  CA  . PHE   A 1 261 ? -25.28200 -16.14300 2.26800   1.000 96.20527  ? 297 PHE   A CA  1 
ATOM   2105 C  C   . PHE   A 1 261 ? -24.72500 -15.12200 1.28400   1.000 100.57337 ? 297 PHE   A C   1 
ATOM   2106 O  O   . PHE   A 1 261 ? -24.74900 -13.91300 1.54500   1.000 94.99941  ? 297 PHE   A O   1 
ATOM   2107 C  CB  . PHE   A 1 261 ? -24.14800 -16.87500 2.98500   1.000 102.46828 ? 297 PHE   A CB  1 
ATOM   2108 C  CG  . PHE   A 1 261 ? -23.17400 -15.96100 3.67000   1.000 96.27121  ? 297 PHE   A CG  1 
ATOM   2109 C  CD1 . PHE   A 1 261 ? -23.47900 -15.39900 4.89700   1.000 90.29174  ? 297 PHE   A CD1 1 
ATOM   2110 C  CD2 . PHE   A 1 261 ? -21.95100 -15.66700 3.09000   1.000 97.12950  ? 297 PHE   A CD2 1 
ATOM   2111 C  CE1 . PHE   A 1 261 ? -22.58500 -14.55800 5.53000   1.000 93.33658  ? 297 PHE   A CE1 1 
ATOM   2112 C  CE2 . PHE   A 1 261 ? -21.05300 -14.82800 3.72000   1.000 97.55435  ? 297 PHE   A CE2 1 
ATOM   2113 C  CZ  . PHE   A 1 261 ? -21.37100 -14.27300 4.94100   1.000 103.20321 ? 297 PHE   A CZ  1 
ATOM   2114 N  N   . ASP   A 1 262 ? -24.21400 -15.58800 0.14600   1.000 96.96071  ? 298 ASP   A N   1 
ATOM   2115 C  CA  . ASP   A 1 262 ? -23.58100 -14.71900 -0.83600  1.000 98.81838  ? 298 ASP   A CA  1 
ATOM   2116 C  C   . ASP   A 1 262 ? -24.51200 -14.33700 -1.98100  1.000 97.13145  ? 298 ASP   A C   1 
ATOM   2117 O  O   . ASP   A 1 262 ? -24.05000 -13.78300 -2.98300  1.000 97.91257  ? 298 ASP   A O   1 
ATOM   2118 C  CB  . ASP   A 1 262 ? -22.31200 -15.37800 -1.38700  1.000 97.15602  ? 298 ASP   A CB  1 
ATOM   2119 C  CG  . ASP   A 1 262 ? -22.58200 -16.70900 -2.07800  1.000 97.82913  ? 298 ASP   A CG  1 
ATOM   2120 O  OD1 . ASP   A 1 262 ? -23.74900 -17.15300 -2.12800  1.000 97.29393  ? 298 ASP   A OD1 1 
ATOM   2121 O  OD2 . ASP   A 1 262 ? -21.61200 -17.31700 -2.57700  1.000 102.47276 ? 298 ASP   A OD2 1 
ATOM   2122 N  N   . ALA   A 1 263 ? -25.80600 -14.61400 -1.85500  1.000 94.93054  ? 299 ALA   A N   1 
ATOM   2123 C  CA  . ALA   A 1 263 ? -26.74800 -14.31500 -2.92100  1.000 88.50665  ? 299 ALA   A CA  1 
ATOM   2124 C  C   . ALA   A 1 263 ? -27.09900 -12.83300 -2.93800  1.000 95.65426  ? 299 ALA   A C   1 
ATOM   2125 O  O   . ALA   A 1 263 ? -27.03600 -12.14300 -1.91600  1.000 75.81227  ? 299 ALA   A O   1 
ATOM   2126 C  CB  . ALA   A 1 263 ? -28.02100 -15.14600 -2.76400  1.000 86.38222  ? 299 ALA   A CB  1 
ATOM   2127 N  N   . GLU   A 1 264 ? -27.47500 -12.34700 -4.11900  1.000 97.24672  ? 300 GLU   A N   1 
ATOM   2128 C  CA  . GLU   A 1 264 ? -27.86200 -10.95300 -4.28200  1.000 92.33558  ? 300 GLU   A CA  1 
ATOM   2129 C  C   . GLU   A 1 264 ? -29.37700 -10.83700 -4.18500  1.000 87.07102  ? 300 GLU   A C   1 
ATOM   2130 O  O   . GLU   A 1 264 ? -30.08700 -11.48800 -4.96400  1.000 85.56259  ? 300 GLU   A O   1 
ATOM   2131 C  CB  . GLU   A 1 264 ? -27.37500 -10.41400 -5.61700  1.000 100.14797 ? 300 GLU   A CB  1 
ATOM   2132 C  CG  . GLU   A 1 264 ? -27.10300 -8.91800  -5.61700  1.000 110.05648 ? 300 GLU   A CG  1 
ATOM   2133 C  CD  . GLU   A 1 264 ? -26.14400 -8.50000  -6.71600  1.000 118.11296 ? 300 GLU   A CD  1 
ATOM   2134 O  OE1 . GLU   A 1 264 ? -24.92200 -8.69800  -6.54400  1.000 110.31319 ? 300 GLU   A OE1 1 
ATOM   2135 O  OE2 . GLU   A 1 264 ? -26.60800 -7.97900  -7.75200  1.000 126.04987 ? 300 GLU   A OE2 1 
ATOM   2136 N  N   . PRO   A 1 265 ? -29.90800 -10.04500 -3.25900  1.000 86.05645  ? 301 PRO   A N   1 
ATOM   2137 C  CA  . PRO   A 1 265 ? -31.36100 -9.99400  -3.06100  1.000 84.88423  ? 301 PRO   A CA  1 
ATOM   2138 C  C   . PRO   A 1 265 ? -32.05400 -9.33900  -4.24000  1.000 78.46050  ? 301 PRO   A C   1 
ATOM   2139 O  O   . PRO   A 1 265 ? -31.52100 -8.39400  -4.84200  1.000 76.54144  ? 301 PRO   A O   1 
ATOM   2140 C  CB  . PRO   A 1 265 ? -31.51700 -9.14900  -1.78600  1.000 74.12085  ? 301 PRO   A CB  1 
ATOM   2141 C  CG  . PRO   A 1 265 ? -30.16100 -9.14500  -1.14200  1.000 84.04907  ? 301 PRO   A CG  1 
ATOM   2142 C  CD  . PRO   A 1 265 ? -29.18700 -9.22800  -2.27100  1.000 78.97716  ? 301 PRO   A CD  1 
ATOM   2143 N  N   . PRO   A 1 266 ? -33.24300 -9.81800  -4.61000  1.000 74.20565  ? 302 PRO   A N   1 
ATOM   2144 C  CA  . PRO   A 1 266 ? -34.02700 -9.13000  -5.64300  1.000 81.52858  ? 302 PRO   A CA  1 
ATOM   2145 C  C   . PRO   A 1 266 ? -34.71800 -7.89300  -5.09000  1.000 76.46089  ? 302 PRO   A C   1 
ATOM   2146 O  O   . PRO   A 1 266 ? -35.88500 -7.95200  -4.69100  1.000 77.50324  ? 302 PRO   A O   1 
ATOM   2147 C  CB  . PRO   A 1 266 ? -35.03600 -10.19700 -6.08400  1.000 80.38761  ? 302 PRO   A CB  1 
ATOM   2148 C  CG  . PRO   A 1 266 ? -35.20700 -11.06200 -4.87500  1.000 81.75428  ? 302 PRO   A CG  1 
ATOM   2149 C  CD  . PRO   A 1 266 ? -33.87500 -11.07600 -4.17200  1.000 82.67398  ? 302 PRO   A CD  1 
ATOM   2150 N  N   . TYR   A 1 267 ? -34.00200 -6.76500  -5.06600  1.000 82.47913  ? 303 TYR   A N   1 
ATOM   2151 C  CA  . TYR   A 1 267 ? -34.51600 -5.56600  -4.41000  1.000 75.78687  ? 303 TYR   A CA  1 
ATOM   2152 C  C   . TYR   A 1 267 ? -35.77200 -5.04800  -5.10000  1.000 81.72871  ? 303 TYR   A C   1 
ATOM   2153 O  O   . TYR   A 1 267 ? -36.78700 -4.78400  -4.44600  1.000 78.64304  ? 303 TYR   A O   1 
ATOM   2154 C  CB  . TYR   A 1 267 ? -33.43800 -4.48200  -4.38000  1.000 74.65921  ? 303 TYR   A CB  1 
ATOM   2155 C  CG  . TYR   A 1 267 ? -32.17400 -4.90300  -3.67300  1.000 78.93736  ? 303 TYR   A CG  1 
ATOM   2156 C  CD1 . TYR   A 1 267 ? -32.07800 -4.84700  -2.29000  1.000 65.54250  ? 303 TYR   A CD1 1 
ATOM   2157 C  CD2 . TYR   A 1 267 ? -31.07600 -5.35700  -4.38900  1.000 70.54599  ? 303 TYR   A CD2 1 
ATOM   2158 C  CE1 . TYR   A 1 267 ? -30.92400 -5.23300  -1.63900  1.000 68.92948  ? 303 TYR   A CE1 1 
ATOM   2159 C  CE2 . TYR   A 1 267 ? -29.91800 -5.74600  -3.74800  1.000 76.67792  ? 303 TYR   A CE2 1 
ATOM   2160 C  CZ  . TYR   A 1 267 ? -29.84700 -5.68100  -2.37400  1.000 77.71165  ? 303 TYR   A CZ  1 
ATOM   2161 O  OH  . TYR   A 1 267 ? -28.69200 -6.06800  -1.73700  1.000 80.19555  ? 303 TYR   A OH  1 
ATOM   2162 N  N   . GLU   A 1 268 ? -35.71700 -4.89000  -6.42500  1.000 77.76332  ? 304 GLU   A N   1 
ATOM   2163 C  CA  . GLU   A 1 268 ? -36.86300 -4.36500  -7.16000  1.000 75.25631  ? 304 GLU   A CA  1 
ATOM   2164 C  C   . GLU   A 1 268 ? -38.08700 -5.25600  -7.00400  1.000 84.30487  ? 304 GLU   A C   1 
ATOM   2165 O  O   . GLU   A 1 268 ? -39.21900 -4.75800  -6.97500  1.000 82.75621  ? 304 GLU   A O   1 
ATOM   2166 C  CB  . GLU   A 1 268 ? -36.50800 -4.21600  -8.63700  1.000 88.22722  ? 304 GLU   A CB  1 
ATOM   2167 C  CG  . GLU   A 1 268 ? -35.14400 -3.60400  -8.88000  1.000 101.86893 ? 304 GLU   A CG  1 
ATOM   2168 C  CD  . GLU   A 1 268 ? -34.60900 -3.91900  -10.26100 1.000 114.84740 ? 304 GLU   A CD  1 
ATOM   2169 O  OE1 . GLU   A 1 268 ? -35.41400 -4.28800  -11.14200 1.000 106.03094 ? 304 GLU   A OE1 1 
ATOM   2170 O  OE2 . GLU   A 1 268 ? -33.38100 -3.81000  -10.46200 1.000 120.29199 ? 304 GLU   A OE2 1 
ATOM   2171 N  N   . GLU   A 1 269 ? -37.88300 -6.57000  -6.90100  1.000 77.06846  ? 305 GLU   A N   1 
ATOM   2172 C  CA  . GLU   A 1 269 ? -39.01000 -7.48300  -6.75300  1.000 77.40243  ? 305 GLU   A CA  1 
ATOM   2173 C  C   . GLU   A 1 269 ? -39.65100 -7.34800  -5.37700  1.000 79.69173  ? 305 GLU   A C   1 
ATOM   2174 O  O   . GLU   A 1 269 ? -40.87400 -7.46700  -5.24200  1.000 76.30559  ? 305 GLU   A O   1 
ATOM   2175 C  CB  . GLU   A 1 269 ? -38.55300 -8.92000  -7.00500  1.000 82.49843  ? 305 GLU   A CB  1 
ATOM   2176 C  CG  . GLU   A 1 269 ? -39.69000 -9.91600  -7.13800  1.000 65.51137  ? 305 GLU   A CG  1 
ATOM   2177 C  CD  . GLU   A 1 269 ? -39.42300 -10.96500 -8.19900  1.000 101.93324 ? 305 GLU   A CD  1 
ATOM   2178 O  OE1 . GLU   A 1 269 ? -38.26500 -11.42200 -8.31300  1.000 106.37473 ? 305 GLU   A OE1 1 
ATOM   2179 O  OE2 . GLU   A 1 269 ? -40.37000 -11.32400 -8.93000  1.000 93.69334  ? 305 GLU   A OE2 1 
ATOM   2180 N  N   . TYR   A 1 270 ? -38.84200 -7.09600  -4.34500  1.000 74.26431  ? 306 TYR   A N   1 
ATOM   2181 C  CA  . TYR   A 1 270 ? -39.39200 -6.88000  -3.01100  1.000 70.19862  ? 306 TYR   A CA  1 
ATOM   2182 C  C   . TYR   A 1 270 ? -40.20600 -5.59300  -2.95200  1.000 79.97359  ? 306 TYR   A C   1 
ATOM   2183 O  O   . TYR   A 1 270 ? -41.25800 -5.54800  -2.30300  1.000 72.14599  ? 306 TYR   A O   1 
ATOM   2184 C  CB  . TYR   A 1 270 ? -38.26600 -6.84900  -1.97600  1.000 70.35415  ? 306 TYR   A CB  1 
ATOM   2185 C  CG  . TYR   A 1 270 ? -37.61700 -8.19100  -1.72300  1.000 80.48557  ? 306 TYR   A CG  1 
ATOM   2186 C  CD1 . TYR   A 1 270 ? -38.38100 -9.34500  -1.60100  1.000 82.44929  ? 306 TYR   A CD1 1 
ATOM   2187 C  CD2 . TYR   A 1 270 ? -36.23800 -8.30500  -1.60900  1.000 81.95763  ? 306 TYR   A CD2 1 
ATOM   2188 C  CE1 . TYR   A 1 270 ? -37.79000 -10.57300 -1.37000  1.000 73.15163  ? 306 TYR   A CE1 1 
ATOM   2189 C  CE2 . TYR   A 1 270 ? -35.63700 -9.52900  -1.37900  1.000 82.62376  ? 306 TYR   A CE2 1 
ATOM   2190 C  CZ  . TYR   A 1 270 ? -36.41800 -10.65900 -1.26000  1.000 82.14346  ? 306 TYR   A CZ  1 
ATOM   2191 O  OH  . TYR   A 1 270 ? -35.82400 -11.87900 -1.03100  1.000 80.27668  ? 306 TYR   A OH  1 
ATOM   2192 N  N   . ARG   A 1 271 ? -39.73700 -4.53800  -3.62300  1.000 80.18392  ? 307 ARG   A N   1 
ATOM   2193 C  CA  . ARG   A 1 271 ? -40.46400 -3.27200  -3.60700  1.000 81.05904  ? 307 ARG   A CA  1 
ATOM   2194 C  C   . ARG   A 1 271 ? -41.77200 -3.37700  -4.38200  1.000 77.27515  ? 307 ARG   A C   1 
ATOM   2195 O  O   . ARG   A 1 271 ? -42.77300 -2.75700  -4.00600  1.000 74.03148  ? 307 ARG   A O   1 
ATOM   2196 C  CB  . ARG   A 1 271 ? -39.58900 -2.15300  -4.17100  1.000 72.65495  ? 307 ARG   A CB  1 
ATOM   2197 C  CG  . ARG   A 1 271 ? -38.22200 -2.04900  -3.51400  1.000 76.84483  ? 307 ARG   A CG  1 
ATOM   2198 C  CD  . ARG   A 1 271 ? -37.56800 -0.71100  -3.81100  1.000 73.02926  ? 307 ARG   A CD  1 
ATOM   2199 N  NE  . ARG   A 1 271 ? -36.23200 -0.85600  -4.37600  1.000 75.17647  ? 307 ARG   A NE  1 
ATOM   2200 C  CZ  . ARG   A 1 271 ? -35.96900 -0.87700  -5.67600  1.000 85.82104  ? 307 ARG   A CZ  1 
ATOM   2201 N  NH1 . ARG   A 1 271 ? -36.93300 -0.77700  -6.57700  1.000 87.40583  ? 307 ARG   A NH1 1 
ATOM   2202 N  NH2 . ARG   A 1 271 ? -34.70900 -0.99800  -6.08100  1.000 67.25477  ? 307 ARG   A NH2 1 
ATOM   2203 N  N   . MET   A 1 272 ? -41.78400 -4.15500  -5.46800  1.000 74.05116  ? 308 MET   A N   1 
ATOM   2204 C  CA  . MET   A 1 272 ? -43.03200 -4.37800  -6.18900  1.000 83.28422  ? 308 MET   A CA  1 
ATOM   2205 C  C   . MET   A 1 272 ? -43.98700 -5.25700  -5.39300  1.000 84.48012  ? 308 MET   A C   1 
ATOM   2206 O  O   . MET   A 1 272 ? -45.20900 -5.13600  -5.54400  1.000 89.15193  ? 308 MET   A O   1 
ATOM   2207 C  CB  . MET   A 1 272 ? -42.74700 -4.99700  -7.55700  1.000 67.69312  ? 308 MET   A CB  1 
ATOM   2208 C  CG  . MET   A 1 272 ? -42.49500 -3.97500  -8.65200  1.000 92.13086  ? 308 MET   A CG  1 
ATOM   2209 S  SD  . MET   A 1 272 ? -41.64900 -4.68600  -10.07400 1.000 125.06947 ? 308 MET   A SD  1 
ATOM   2210 C  CE  . MET   A 1 272 ? -42.66500 -6.12800  -10.38600 1.000 91.40348  ? 308 MET   A CE  1 
ATOM   2211 N  N   . LEU   A 1 273 ? -43.45400 -6.14000  -4.54600  1.000 85.66304  ? 309 LEU   A N   1 
ATOM   2212 C  CA  . LEU   A 1 273 ? -44.31100 -6.94500  -3.68200  1.000 91.16842  ? 309 LEU   A CA  1 
ATOM   2213 C  C   . LEU   A 1 273 ? -45.00800 -6.07900  -2.64200  1.000 82.20189  ? 309 LEU   A C   1 
ATOM   2214 O  O   . LEU   A 1 273 ? -46.19500 -6.27200  -2.35600  1.000 86.64647  ? 309 LEU   A O   1 
ATOM   2215 C  CB  . LEU   A 1 273 ? -43.48900 -8.04200  -3.00300  1.000 80.56176  ? 309 LEU   A CB  1 
ATOM   2216 C  CG  . LEU   A 1 273 ? -44.23000 -8.94500  -2.01400  1.000 83.59260  ? 309 LEU   A CG  1 
ATOM   2217 C  CD1 . LEU   A 1 273 ? -45.21300 -9.85100  -2.74000  1.000 91.83185  ? 309 LEU   A CD1 1 
ATOM   2218 C  CD2 . LEU   A 1 273 ? -43.24800 -9.76100  -1.18700  1.000 80.51843  ? 309 LEU   A CD2 1 
ATOM   2219 N  N   . LEU   A 1 274 ? -44.28700 -5.11300  -2.07100  1.000 81.42642  ? 310 LEU   A N   1 
ATOM   2220 C  CA  . LEU   A 1 274 ? -44.86800 -4.21600  -1.08200  1.000 85.37348  ? 310 LEU   A CA  1 
ATOM   2221 C  C   . LEU   A 1 274 ? -45.76500 -3.15100  -1.70600  1.000 79.01279  ? 310 LEU   A C   1 
ATOM   2222 O  O   . LEU   A 1 274 ? -46.64200 -2.62300  -1.01500  1.000 80.66121  ? 310 LEU   A O   1 
ATOM   2223 C  CB  . LEU   A 1 274 ? -43.75500 -3.55800  -0.26300  1.000 78.06261  ? 310 LEU   A CB  1 
ATOM   2224 C  CG  . LEU   A 1 274 ? -42.84000 -4.53000  0.49000   1.000 66.29455  ? 310 LEU   A CG  1 
ATOM   2225 C  CD1 . LEU   A 1 274 ? -41.67500 -3.79600  1.15100   1.000 70.12993  ? 310 LEU   A CD1 1 
ATOM   2226 C  CD2 . LEU   A 1 274 ? -43.63500 -5.33700  1.51300   1.000 67.07519  ? 310 LEU   A CD2 1 
ATOM   2227 N  N   . LEU   A 1 275 ? -45.57500 -2.83100  -2.99100  1.000 78.51640  ? 311 LEU   A N   1 
ATOM   2228 C  CA  . LEU   A 1 275 ? -46.44600 -1.86900  -3.66400  1.000 80.53310  ? 311 LEU   A CA  1 
ATOM   2229 C  C   . LEU   A 1 275 ? -47.83500 -2.44800  -3.90700  1.000 88.73117  ? 311 LEU   A C   1 
ATOM   2230 O  O   . LEU   A 1 275 ? -48.83900 -1.75300  -3.71700  1.000 96.17536  ? 311 LEU   A O   1 
ATOM   2231 C  CB  . LEU   A 1 275 ? -45.82000 -1.42400  -4.99100  1.000 80.37086  ? 311 LEU   A CB  1 
ATOM   2232 C  CG  . LEU   A 1 275 ? -46.01500 0.00600   -5.53000  1.000 90.87898  ? 311 LEU   A CG  1 
ATOM   2233 C  CD1 . LEU   A 1 275 ? -45.26300 0.18300   -6.85200  1.000 99.52886  ? 311 LEU   A CD1 1 
ATOM   2234 C  CD2 . LEU   A 1 275 ? -47.48300 0.40700   -5.69100  1.000 92.32796  ? 311 LEU   A CD2 1 
ATOM   2235 N  N   . SER   A 1 276 ? -47.91400 -3.71600  -4.32600  1.000 83.04134  ? 312 SER   A N   1 
ATOM   2236 C  CA  . SER   A 1 276 ? -49.20400 -4.33400  -4.61700  1.000 90.95287  ? 312 SER   A CA  1 
ATOM   2237 C  C   . SER   A 1 276 ? -50.12800 -4.37100  -3.40700  1.000 90.69438  ? 312 SER   A C   1 
ATOM   2238 O  O   . SER   A 1 276 ? -51.32500 -4.63600  -3.57200  1.000 101.36189 ? 312 SER   A O   1 
ATOM   2239 C  CB  . SER   A 1 276 ? -49.00400 -5.75100  -5.16400  1.000 88.14458  ? 312 SER   A CB  1 
ATOM   2240 O  OG  . SER   A 1 276 ? -48.23700 -6.54900  -4.28100  1.000 83.59399  ? 312 SER   A OG  1 
ATOM   2241 N  N   . VAL   A 1 277 ? -49.60700 -4.12200  -2.20400  1.000 81.82020  ? 313 VAL   A N   1 
ATOM   2242 C  CA  . VAL   A 1 277 ? -50.47000 -3.94000  -1.04100  1.000 94.05056  ? 313 VAL   A CA  1 
ATOM   2243 C  C   . VAL   A 1 277 ? -51.42100 -2.77300  -1.26900  1.000 92.24795  ? 313 VAL   A C   1 
ATOM   2244 O  O   . VAL   A 1 277 ? -52.61800 -2.85700  -0.96700  1.000 95.44583  ? 313 VAL   A O   1 
ATOM   2245 C  CB  . VAL   A 1 277 ? -49.62100 -3.73600  0.22700   1.000 70.20393  ? 313 VAL   A CB  1 
ATOM   2246 C  CG1 . VAL   A 1 277 ? -50.51400 -3.51200  1.43700   1.000 65.33579  ? 313 VAL   A CG1 1 
ATOM   2247 C  CG2 . VAL   A 1 277 ? -48.69900 -4.92400  0.44700   1.000 84.90688  ? 313 VAL   A CG2 1 
ATOM   2248 N  N   . LEU   A 1 278 ? -50.90700 -1.67000  -1.81700  1.000 89.99232  ? 314 LEU   A N   1 
ATOM   2249 C  CA  . LEU   A 1 278 ? -51.74500 -0.50400  -2.07300  1.000 90.35182  ? 314 LEU   A CA  1 
ATOM   2250 C  C   . LEU   A 1 278 ? -52.75300 -0.76300  -3.18600  1.000 99.76972  ? 314 LEU   A C   1 
ATOM   2251 O  O   . LEU   A 1 278 ? -53.82000 -0.14100  -3.20700  1.000 97.67123  ? 314 LEU   A O   1 
ATOM   2252 C  CB  . LEU   A 1 278 ? -50.86900 0.70100   -2.41800  1.000 88.84112  ? 314 LEU   A CB  1 
ATOM   2253 C  CG  . LEU   A 1 278 ? -49.74400 1.00000   -1.42500  1.000 83.09840  ? 314 LEU   A CG  1 
ATOM   2254 C  CD1 . LEU   A 1 278 ? -48.93300 2.20700   -1.86900  1.000 71.68796  ? 314 LEU   A CD1 1 
ATOM   2255 C  CD2 . LEU   A 1 278 ? -50.30300 1.20800   -0.02600  1.000 77.68193  ? 314 LEU   A CD2 1 
ATOM   2256 N  N   . ASP   A 1 279 ? -52.44000 -1.67000  -4.11400  1.000 116.60629 ? 315 ASP   A N   1 
ATOM   2257 C  CA  . ASP   A 1 279 ? -53.38200 -1.97500  -5.18700  1.000 117.04429 ? 315 ASP   A CA  1 
ATOM   2258 C  C   . ASP   A 1 279 ? -54.54300 -2.82300  -4.68200  1.000 124.57506 ? 315 ASP   A C   1 
ATOM   2259 O  O   . ASP   A 1 279 ? -55.68700 -2.64100  -5.11600  1.000 144.64247 ? 315 ASP   A O   1 
ATOM   2260 C  CB  . ASP   A 1 279 ? -52.66500 -2.68100  -6.33800  1.000 121.44074 ? 315 ASP   A CB  1 
ATOM   2261 C  CG  . ASP   A 1 279 ? -51.77500 -1.74400  -7.13400  1.000 135.14546 ? 315 ASP   A CG  1 
ATOM   2262 O  OD1 . ASP   A 1 279 ? -51.60500 -0.58100  -6.71300  1.000 146.25420 ? 315 ASP   A OD1 1 
ATOM   2263 O  OD2 . ASP   A 1 279 ? -51.25200 -2.16900  -8.18500  1.000 137.86673 ? 315 ASP   A OD2 1 
ATOM   2264 N  N   . ASP   A 1 280 ? -54.27000 -3.75200  -3.76300  1.000 104.29590 ? 316 ASP   A N   1 
ATOM   2265 C  CA  . ASP   A 1 280 ? -55.32900 -4.61200  -3.24400  1.000 113.79271 ? 316 ASP   A CA  1 
ATOM   2266 C  C   . ASP   A 1 280 ? -56.33300 -3.83100  -2.40700  1.000 111.61008 ? 316 ASP   A C   1 
ATOM   2267 O  O   . ASP   A 1 280 ? -57.49800 -4.23100  -2.30700  1.000 116.76816 ? 316 ASP   A O   1 
ATOM   2268 C  CB  . ASP   A 1 280 ? -54.72800 -5.74800  -2.41500  1.000 108.25682 ? 316 ASP   A CB  1 
ATOM   2269 C  CG  . ASP   A 1 280 ? -53.89600 -6.70600  -3.24900  1.000 104.84873 ? 316 ASP   A CG  1 
ATOM   2270 O  OD1 . ASP   A 1 280 ? -53.92300 -6.59400  -4.49200  1.000 112.65586 ? 316 ASP   A OD1 1 
ATOM   2271 O  OD2 . ASP   A 1 280 ? -53.21400 -7.57100  -2.65800  1.000 96.77835  ? 316 ASP   A OD2 1 
ATOM   2272 N  N   . LEU   A 1 281 ? -55.90800 -2.72000  -1.80700  1.000 99.06872  ? 317 LEU   A N   1 
ATOM   2273 C  CA  . LEU   A 1 281 ? -56.73200 -1.96600  -0.87300  1.000 99.57273  ? 317 LEU   A CA  1 
ATOM   2274 C  C   . LEU   A 1 281 ? -57.18500 -0.62300  -1.43100  1.000 96.73820  ? 317 LEU   A C   1 
ATOM   2275 O  O   . LEU   A 1 281 ? -57.72900 0.19500   -0.68200  1.000 93.52969  ? 317 LEU   A O   1 
ATOM   2276 C  CB  . LEU   A 1 281 ? -55.97000 -1.76100  0.43700   1.000 93.25471  ? 317 LEU   A CB  1 
ATOM   2277 C  CG  . LEU   A 1 281 ? -55.13400 -2.95600  0.89800   1.000 83.14734  ? 317 LEU   A CG  1 
ATOM   2278 C  CD1 . LEU   A 1 281 ? -54.16200 -2.53500  1.99400   1.000 79.95323  ? 317 LEU   A CD1 1 
ATOM   2279 C  CD2 . LEU   A 1 281 ? -56.02200 -4.10700  1.35600   1.000 94.01432  ? 317 LEU   A CD2 1 
ATOM   2280 N  N   . GLY   A 1 282 ? -56.96100 -0.36800  -2.71700  1.000 96.44274  ? 318 GLY   A N   1 
ATOM   2281 C  CA  . GLY   A 1 282 ? -57.44000 0.85100   -3.34900  1.000 101.23244 ? 318 GLY   A CA  1 
ATOM   2282 C  C   . GLY   A 1 282 ? -56.78400 2.12900   -2.87300  1.000 90.65651  ? 318 GLY   A C   1 
ATOM   2283 O  O   . GLY   A 1 282 ? -57.47100 3.14200   -2.68800  1.000 96.24193  ? 318 GLY   A O   1 
ATOM   2284 N  N   . GLN   A 1 283 ? -55.46800 2.11300   -2.67900  1.000 80.02090  ? 319 GLN   A N   1 
ATOM   2285 C  CA  . GLN   A 1 283 ? -54.73200 3.27500   -2.20900  1.000 88.42234  ? 319 GLN   A CA  1 
ATOM   2286 C  C   . GLN   A 1 283 ? -53.69100 3.69200   -3.23700  1.000 90.89661  ? 319 GLN   A C   1 
ATOM   2287 O  O   . GLN   A 1 283 ? -53.20200 2.87300   -4.02100  1.000 99.09780  ? 319 GLN   A O   1 
ATOM   2288 C  CB  . GLN   A 1 283 ? -54.05100 2.99000   -0.86700  1.000 76.53393  ? 319 GLN   A CB  1 
ATOM   2289 C  CG  . GLN   A 1 283 ? -54.99800 2.47700   0.19800   1.000 70.64898  ? 319 GLN   A CG  1 
ATOM   2290 C  CD  . GLN   A 1 283 ? -56.16800 3.41100   0.43000   1.000 86.89823  ? 319 GLN   A CD  1 
ATOM   2291 O  OE1 . GLN   A 1 283 ? -56.01300 4.63200   0.43100   1.000 95.87907  ? 319 GLN   A OE1 1 
ATOM   2292 N  NE2 . GLN   A 1 283 ? -57.35100 2.83900   0.62100   1.000 82.00538  ? 319 GLN   A NE2 1 
ATOM   2293 N  N   . ALA   A 1 284 ? -53.35700 4.97900   -3.22500  1.000 80.26420  ? 320 ALA   A N   1 
ATOM   2294 C  CA  . ALA   A 1 284 ? -52.34600 5.54500   -4.10300  1.000 89.45613  ? 320 ALA   A CA  1 
ATOM   2295 C  C   . ALA   A 1 284 ? -51.08300 5.84900   -3.30900  1.000 97.36879  ? 320 ALA   A C   1 
ATOM   2296 O  O   . ALA   A 1 284 ? -51.13300 6.08800   -2.10000  1.000 93.42495  ? 320 ALA   A O   1 
ATOM   2297 C  CB  . ALA   A 1 284 ? -52.85600 6.82000   -4.78200  1.000 89.78553  ? 320 ALA   A CB  1 
ATOM   2298 N  N   . CYS   A 1 285 ? -49.94500 5.83400   -3.99900  1.000 98.36449  ? 321 CYS   A N   1 
ATOM   2299 C  CA  . CYS   A 1 285 ? -48.65700 6.10200   -3.36200  1.000 88.47197  ? 321 CYS   A CA  1 
ATOM   2300 C  C   . CYS   A 1 285 ? -48.20000 7.51900   -3.70700  1.000 103.77177 ? 321 CYS   A C   1 
ATOM   2301 O  O   . CYS   A 1 285 ? -47.20200 7.74600   -4.39200  1.000 114.93752 ? 321 CYS   A O   1 
ATOM   2302 C  CB  . CYS   A 1 285 ? -47.62800 5.05900   -3.78300  1.000 103.43298 ? 321 CYS   A CB  1 
ATOM   2303 S  SG  . CYS   A 1 285 ? -46.08400 5.13700   -2.84800  1.000 112.72140 ? 321 CYS   A SG  1 
ATOM   2304 N  N   . ASP   A 1 286 ? -48.96500 8.48700   -3.20400  1.000 101.27615 ? 322 ASP   A N   1 
ATOM   2305 C  CA  . ASP   A 1 286 ? -48.68700 9.88900   -3.48400  1.000 99.48302  ? 322 ASP   A CA  1 
ATOM   2306 C  C   . ASP   A 1 286 ? -47.64600 10.49400  -2.55000  1.000 87.73194  ? 322 ASP   A C   1 
ATOM   2307 O  O   . ASP   A 1 286 ? -47.13100 11.57700  -2.84700  1.000 87.85944  ? 322 ASP   A O   1 
ATOM   2308 C  CB  . ASP   A 1 286 ? -49.98100 10.70400  -3.40800  1.000 98.69849  ? 322 ASP   A CB  1 
ATOM   2309 C  CG  . ASP   A 1 286 ? -50.80100 10.38200  -2.17400  1.000 89.00364  ? 322 ASP   A CG  1 
ATOM   2310 O  OD1 . ASP   A 1 286 ? -50.23200 10.37800  -1.06400  1.000 79.15667  ? 322 ASP   A OD1 1 
ATOM   2311 O  OD2 . ASP   A 1 286 ? -52.01900 10.14200  -2.31100  1.000 107.53382 ? 322 ASP   A OD2 1 
ATOM   2312 N  N   . GLY   A 1 287 ? -47.32800 9.83300   -1.43800  1.000 89.75648  ? 323 GLY   A N   1 
ATOM   2313 C  CA  . GLY   A 1 287 ? -46.37200 10.34700  -0.47500  1.000 86.18885  ? 323 GLY   A CA  1 
ATOM   2314 C  C   . GLY   A 1 287 ? -46.97900 10.83700  0.82100   1.000 77.94156  ? 323 GLY   A C   1 
ATOM   2315 O  O   . GLY   A 1 287 ? -46.24000 11.33900  1.67700   1.000 66.27165  ? 323 GLY   A O   1 
ATOM   2316 N  N   . ASP   A 1 288 ? -48.29300 10.71400  0.99500   1.000 76.19993  ? 324 ASP   A N   1 
ATOM   2317 C  CA  . ASP   A 1 288 ? -48.94700 11.13100  2.22900   1.000 79.83627  ? 324 ASP   A CA  1 
ATOM   2318 C  C   . ASP   A 1 288 ? -48.53200 10.20500  3.36700   1.000 68.61060  ? 324 ASP   A C   1 
ATOM   2319 O  O   . ASP   A 1 288 ? -48.77000 8.99400   3.31000   1.000 76.25808  ? 324 ASP   A O   1 
ATOM   2320 C  CB  . ASP   A 1 288 ? -50.46500 11.11900  2.04800   1.000 79.01316  ? 324 ASP   A CB  1 
ATOM   2321 C  CG  . ASP   A 1 288 ? -51.20200 11.84500  3.16700   1.000 81.54147  ? 324 ASP   A CG  1 
ATOM   2322 O  OD1 . ASP   A 1 288 ? -50.63200 12.02000  4.26500   1.000 86.23102  ? 324 ASP   A OD1 1 
ATOM   2323 O  OD2 . ASP   A 1 288 ? -52.36500 12.24300  2.94400   1.000 87.76423  ? 324 ASP   A OD2 1 
ATOM   2324 N  N   . MET   A 1 289 ? -47.90400 10.76800  4.39400   1.000 67.98578  ? 325 MET   A N   1 
ATOM   2325 C  CA  . MET   A 1 289 ? -47.51500 10.01500  5.57500   1.000 75.42462  ? 325 MET   A CA  1 
ATOM   2326 C  C   . MET   A 1 289 ? -48.33000 10.47000  6.77900   1.000 63.15580  ? 325 MET   A C   1 
ATOM   2327 O  O   . MET   A 1 289 ? -48.92900 11.54900  6.78100   1.000 50.85814  ? 325 MET   A O   1 
ATOM   2328 C  CB  . MET   A 1 289 ? -46.01600 10.16100  5.85900   1.000 57.16726  ? 325 MET   A CB  1 
ATOM   2329 C  CG  . MET   A 1 289 ? -45.23400 8.87100   5.66500   1.000 77.52723  ? 325 MET   A CG  1 
ATOM   2330 S  SD  . MET   A 1 289 ? -44.76600 8.55100   3.95600   1.000 70.53172  ? 325 MET   A SD  1 
ATOM   2331 C  CE  . MET   A 1 289 ? -43.37900 9.67000   3.77900   1.000 84.11119  ? 325 MET   A CE  1 
ATOM   2332 N  N   . ASP   A 1 290 ? -48.33900 9.62000   7.81200   1.000 66.88143  ? 326 ASP   A N   1 
ATOM   2333 C  CA  . ASP   A 1 290 ? -49.20500 9.84600   8.96800   1.000 53.76334  ? 326 ASP   A CA  1 
ATOM   2334 C  C   . ASP   A 1 290 ? -48.80100 11.09400  9.74200   1.000 48.92804  ? 326 ASP   A C   1 
ATOM   2335 O  O   . ASP   A 1 290 ? -49.66400 11.86700  10.17500  1.000 74.73688  ? 326 ASP   A O   1 
ATOM   2336 C  CB  . ASP   A 1 290 ? -49.18600 8.62400   9.88900   1.000 77.97745  ? 326 ASP   A CB  1 
ATOM   2337 C  CG  . ASP   A 1 290 ? -49.83500 7.40600   9.26100   1.000 84.34942  ? 326 ASP   A CG  1 
ATOM   2338 O  OD1 . ASP   A 1 290 ? -50.20500 7.47600   8.07000   1.000 88.00020  ? 326 ASP   A OD1 1 
ATOM   2339 O  OD2 . ASP   A 1 290 ? -49.97500 6.38100   9.96100   1.000 76.32549  ? 326 ASP   A OD2 1 
ATOM   2340 N  N   . TRP   A 1 291 ? -47.49900 11.31000  9.92900   1.000 62.49942  ? 327 TRP   A N   1 
ATOM   2341 C  CA  . TRP   A 1 291 ? -47.04600 12.45200  10.71200  1.000 73.85245  ? 327 TRP   A CA  1 
ATOM   2342 C  C   . TRP   A 1 291 ? -47.33500 13.78400  10.03400  1.000 52.89862  ? 327 TRP   A C   1 
ATOM   2343 O  O   . TRP   A 1 291 ? -47.17400 14.83000  10.67000  1.000 66.28610  ? 327 TRP   A O   1 
ATOM   2344 C  CB  . TRP   A 1 291 ? -45.55000 12.33000  11.00600  1.000 76.00815  ? 327 TRP   A CB  1 
ATOM   2345 C  CG  . TRP   A 1 291 ? -44.69500 12.19800  9.78500   1.000 67.78981  ? 327 TRP   A CG  1 
ATOM   2346 C  CD1 . TRP   A 1 291 ? -44.34100 13.19200  8.92200   1.000 67.10479  ? 327 TRP   A CD1 1 
ATOM   2347 C  CD2 . TRP   A 1 291 ? -44.06900 11.00400  9.30000   1.000 49.37292  ? 327 TRP   A CD2 1 
ATOM   2348 N  NE1 . TRP   A 1 291 ? -43.54100 12.69100  7.92400   1.000 74.39364  ? 327 TRP   A NE1 1 
ATOM   2349 C  CE2 . TRP   A 1 291 ? -43.35700 11.35000  8.13400   1.000 61.53977  ? 327 TRP   A CE2 1 
ATOM   2350 C  CE3 . TRP   A 1 291 ? -44.04300 9.67500   9.73700   1.000 70.36614  ? 327 TRP   A CE3 1 
ATOM   2351 C  CZ2 . TRP   A 1 291 ? -42.62700 10.41700  7.40100   1.000 57.77373  ? 327 TRP   A CZ2 1 
ATOM   2352 C  CZ3 . TRP   A 1 291 ? -43.31800 8.75100   9.00600   1.000 61.57206  ? 327 TRP   A CZ3 1 
ATOM   2353 C  CH2 . TRP   A 1 291 ? -42.61900 9.12700   7.85300   1.000 67.30639  ? 327 TRP   A CH2 1 
ATOM   2354 N  N   . MET   A 1 292 ? -47.75800 13.77100  8.77200   1.000 64.89901  ? 328 MET   A N   1 
ATOM   2355 C  CA  . MET   A 1 292 ? -48.16200 14.98200  8.07000   1.000 71.89434  ? 328 MET   A CA  1 
ATOM   2356 C  C   . MET   A 1 292 ? -49.53200 15.48500  8.50300   1.000 82.34454  ? 328 MET   A C   1 
ATOM   2357 O  O   . MET   A 1 292 ? -49.97400 16.52800  8.01100   1.000 97.97451  ? 328 MET   A O   1 
ATOM   2358 C  CB  . MET   A 1 292 ? -48.15700 14.73500  6.55900   1.000 61.16221  ? 328 MET   A CB  1 
ATOM   2359 C  CG  . MET   A 1 292 ? -46.80200 14.32700  6.00700   1.000 54.81251  ? 328 MET   A CG  1 
ATOM   2360 S  SD  . MET   A 1 292 ? -46.84800 13.98700  4.23700   1.000 80.85662  ? 328 MET   A SD  1 
ATOM   2361 C  CE  . MET   A 1 292 ? -47.45100 15.55200  3.60900   1.000 88.48589  ? 328 MET   A CE  1 
ATOM   2362 N  N   . HIS   A 1 293 ? -50.21000 14.76900  9.40100   1.000 70.93253  ? 329 HIS   A N   1 
ATOM   2363 C  CA  . HIS   A 1 293 ? -51.50500 15.17400  9.93000   1.000 82.19770  ? 329 HIS   A CA  1 
ATOM   2364 C  C   . HIS   A 1 293 ? -51.44600 15.50800  11.41500  1.000 85.72437  ? 329 HIS   A C   1 
ATOM   2365 O  O   . HIS   A 1 293 ? -52.49400 15.66200  12.05000  1.000 91.07655  ? 329 HIS   A O   1 
ATOM   2366 C  CB  . HIS   A 1 293 ? -52.54400 14.07800  9.68100   1.000 85.16763  ? 329 HIS   A CB  1 
ATOM   2367 C  CG  . HIS   A 1 293 ? -52.78500 13.79000  8.23300   1.000 61.89124  ? 329 HIS   A CG  1 
ATOM   2368 N  ND1 . HIS   A 1 293 ? -53.56100 14.60100  7.43300   1.000 88.69272  ? 329 HIS   A ND1 1 
ATOM   2369 C  CD2 . HIS   A 1 293 ? -52.35800 12.77900  7.44000   1.000 61.67245  ? 329 HIS   A CD2 1 
ATOM   2370 C  CE1 . HIS   A 1 293 ? -53.60000 14.10300  6.21000   1.000 65.34853  ? 329 HIS   A CE1 1 
ATOM   2371 N  NE2 . HIS   A 1 293 ? -52.87800 12.99700  6.18700   1.000 74.63039  ? 329 HIS   A NE2 1 
ATOM   2372 N  N   . LEU   A 1 294 ? -50.24800 15.62000  11.98200  1.000 87.05588  ? 330 LEU   A N   1 
ATOM   2373 C  CA  . LEU   A 1 294 ? -50.10800 15.93600  13.39400  1.000 103.78328 ? 330 LEU   A CA  1 
ATOM   2374 C  C   . LEU   A 1 294 ? -50.47400 17.39000  13.66500  1.000 97.63580  ? 330 LEU   A C   1 
ATOM   2375 O  O   . LEU   A 1 294 ? -50.23700 18.27800  12.84200  1.000 107.76211 ? 330 LEU   A O   1 
ATOM   2376 C  CB  . LEU   A 1 294 ? -48.67500 15.67600  13.86000  1.000 88.13594  ? 330 LEU   A CB  1 
ATOM   2377 C  CG  . LEU   A 1 294 ? -48.21000 14.22700  14.00600  1.000 95.29243  ? 330 LEU   A CG  1 
ATOM   2378 C  CD1 . LEU   A 1 294 ? -46.69200 14.17000  14.03300  1.000 81.04655  ? 330 LEU   A CD1 1 
ATOM   2379 C  CD2 . LEU   A 1 294 ? -48.78900 13.61000  15.26800  1.000 84.24170  ? 330 LEU   A CD2 1 
ATOM   2380 N  N   . ASN   A 1 295 ? -51.06200 17.62000  14.84100  1.000 109.32687 ? 331 ASN   A N   1 
ATOM   2381 C  CA  . ASN   A 1 295 ? -51.30800 18.96600  15.36100  1.000 125.74795 ? 331 ASN   A CA  1 
ATOM   2382 C  C   . ASN   A 1 295 ? -52.16300 19.79600  14.40300  1.000 118.70434 ? 331 ASN   A C   1 
ATOM   2383 O  O   . ASN   A 1 295 ? -51.80700 20.91300  14.02200  1.000 129.40303 ? 331 ASN   A O   1 
ATOM   2384 C  CB  . ASN   A 1 295 ? -49.98700 19.67100  15.67800  1.000 122.29446 ? 331 ASN   A CB  1 
ATOM   2385 C  CG  . ASN   A 1 295 ? -49.19000 18.95300  16.74800  1.000 130.04654 ? 331 ASN   A CG  1 
ATOM   2386 O  OD1 . ASN   A 1 295 ? -49.75700 18.36800  17.67100  1.000 132.22252 ? 331 ASN   A OD1 1 
ATOM   2387 N  ND2 . ASN   A 1 295 ? -47.86900 18.98500  16.62600  1.000 136.08378 ? 331 ASN   A ND2 1 
ATOM   2388 N  N   . GLY   A 1 296 ? -53.30400 19.23500  14.01000  1.000 129.22457 ? 332 GLY   A N   1 
ATOM   2389 C  CA  . GLY   A 1 296 ? -54.23500 19.94900  13.16000  1.000 127.10793 ? 332 GLY   A CA  1 
ATOM   2390 C  C   . GLY   A 1 296 ? -53.78200 20.16400  11.73400  1.000 131.36526 ? 332 GLY   A C   1 
ATOM   2391 O  O   . GLY   A 1 296 ? -54.46900 20.86200  10.98300  1.000 125.05710 ? 332 GLY   A O   1 
ATOM   2392 N  N   . GLY   A 1 297 ? -52.64800 19.59000  11.33600  1.000 134.81851 ? 333 GLY   A N   1 
ATOM   2393 C  CA  . GLY   A 1 297 ? -52.09400 19.76500  10.00600  1.000 126.71191 ? 333 GLY   A CA  1 
ATOM   2394 C  C   . GLY   A 1 297 ? -50.78600 20.52700  9.96900   1.000 130.91928 ? 333 GLY   A C   1 
ATOM   2395 O  O   . GLY   A 1 297 ? -50.10700 20.52000  8.93200   1.000 128.99702 ? 333 GLY   A O   1 
ATOM   2396 N  N   . ARG   A 1 298 ? -50.41000 21.19100  11.06700  1.000 130.82453 ? 334 ARG   A N   1 
ATOM   2397 C  CA  . ARG   A 1 298 ? -49.15700 21.94100  11.09400  1.000 133.98605 ? 334 ARG   A CA  1 
ATOM   2398 C  C   . ARG   A 1 298 ? -47.95500 21.01500  10.95300  1.000 135.45055 ? 334 ARG   A C   1 
ATOM   2399 O  O   . ARG   A 1 298 ? -46.94000 21.38500  10.35200  1.000 135.12022 ? 334 ARG   A O   1 
ATOM   2400 C  CB  . ARG   A 1 298 ? -49.05600 22.74100  12.39300  1.000 129.46850 ? 334 ARG   A CB  1 
ATOM   2401 C  CG  . ARG   A 1 298 ? -50.32900 23.47500  12.78100  1.000 130.05858 ? 334 ARG   A CG  1 
ATOM   2402 C  CD  . ARG   A 1 298 ? -50.52100 24.74800  11.97500  1.000 138.57135 ? 334 ARG   A CD  1 
ATOM   2403 N  NE  . ARG   A 1 298 ? -49.31300 25.56300  11.95700  1.000 142.14730 ? 334 ARG   A NE  1 
ATOM   2404 C  CZ  . ARG   A 1 298 ? -48.86800 26.26900  12.98700  1.000 151.02386 ? 334 ARG   A CZ  1 
ATOM   2405 N  NH1 . ARG   A 1 298 ? -49.49100 26.25800  14.15400  1.000 152.66301 ? 334 ARG   A NH1 1 
ATOM   2406 N  NH2 . ARG   A 1 298 ? -47.77000 27.00500  12.84300  1.000 147.19626 ? 334 ARG   A NH2 1 
ATOM   2407 N  N   . GLY   A 1 299 ? -48.05400 19.81000  11.49000  1.000 121.34777 ? 335 GLY   A N   1 
ATOM   2408 C  CA  . GLY   A 1 299 ? -46.93700 18.89200  11.54500  1.000 109.02085 ? 335 GLY   A CA  1 
ATOM   2409 C  C   . GLY   A 1 299 ? -46.41400 18.76200  12.96400  1.000 119.72663 ? 335 GLY   A C   1 
ATOM   2410 O  O   . GLY   A 1 299 ? -46.99900 19.26400  13.92900  1.000 119.05822 ? 335 GLY   A O   1 
ATOM   2411 N  N   . TRP   A 1 300 ? -45.27800 18.07900  13.07900  1.000 117.44885 ? 336 TRP   A N   1 
ATOM   2412 C  CA  . TRP   A 1 300 ? -44.69900 17.80300  14.38600  1.000 121.13934 ? 336 TRP   A CA  1 
ATOM   2413 C  C   . TRP   A 1 300 ? -44.15700 19.07700  15.02200  1.000 136.26150 ? 336 TRP   A C   1 
ATOM   2414 O  O   . TRP   A 1 300 ? -43.54300 19.91300  14.35300  1.000 123.24091 ? 336 TRP   A O   1 
ATOM   2415 C  CB  . TRP   A 1 300 ? -43.59100 16.75900  14.26100  1.000 109.65014 ? 336 TRP   A CB  1 
ATOM   2416 C  CG  . TRP   A 1 300 ? -42.39600 17.21600  13.47500  1.000 108.93548 ? 336 TRP   A CG  1 
ATOM   2417 C  CD1 . TRP   A 1 300 ? -41.24100 17.74700  13.97200  1.000 108.35399 ? 336 TRP   A CD1 1 
ATOM   2418 C  CD2 . TRP   A 1 300 ? -42.23800 17.17100  12.05200  1.000 104.46922 ? 336 TRP   A CD2 1 
ATOM   2419 N  NE1 . TRP   A 1 300 ? -40.37500 18.04000  12.94500  1.000 105.01414 ? 336 TRP   A NE1 1 
ATOM   2420 C  CE2 . TRP   A 1 300 ? -40.96400 17.69600  11.75700  1.000 112.40150 ? 336 TRP   A CE2 1 
ATOM   2421 C  CE3 . TRP   A 1 300 ? -43.05200 16.74100  11.00000  1.000 93.93590  ? 336 TRP   A CE3 1 
ATOM   2422 C  CZ2 . TRP   A 1 300 ? -40.48500 17.80100  10.45300  1.000 104.31381 ? 336 TRP   A CZ2 1 
ATOM   2423 C  CZ3 . TRP   A 1 300 ? -42.57500 16.84700  9.70700   1.000 96.97917  ? 336 TRP   A CZ3 1 
ATOM   2424 C  CH2 . TRP   A 1 300 ? -41.30300 17.37200  9.44400   1.000 108.90423 ? 336 TRP   A CH2 1 
ATOM   2425 N  N   . ASP   A 1 301 ? -44.38700 19.21900  16.32400  1.000 166.46637 ? 337 ASP   A N   1 
ATOM   2426 C  CA  . ASP   A 1 301 ? -43.98200 20.39200  17.07800  1.000 160.94404 ? 337 ASP   A CA  1 
ATOM   2427 C  C   . ASP   A 1 301 ? -42.73000 20.08200  17.90000  1.000 169.08331 ? 337 ASP   A C   1 
ATOM   2428 O  O   . ASP   A 1 301 ? -42.14000 19.00200  17.79900  1.000 158.70513 ? 337 ASP   A O   1 
ATOM   2429 C  CB  . ASP   A 1 301 ? -45.13900 20.86900  17.95900  1.000 165.79777 ? 337 ASP   A CB  1 
ATOM   2430 C  CG  . ASP   A 1 301 ? -45.72200 22.18700  17.49000  1.000 170.67662 ? 337 ASP   A CG  1 
ATOM   2431 O  OD1 . ASP   A 1 301 ? -45.22100 22.73100  16.48700  1.000 176.35369 ? 337 ASP   A OD1 1 
ATOM   2432 O  OD2 . ASP   A 1 301 ? -46.67700 22.68400  18.12400  1.000 179.92772 ? 337 ASP   A OD2 1 
ATOM   2433 N  N   . ALA   A 1 302 ? -42.31700 21.04000  18.73000  1.000 171.02382 ? 338 ALA   A N   1 
ATOM   2434 C  CA  . ALA   A 1 302 ? -41.11000 20.87900  19.53000  1.000 174.66600 ? 338 ALA   A CA  1 
ATOM   2435 C  C   . ALA   A 1 302 ? -41.43500 20.47700  20.96300  1.000 176.34847 ? 338 ALA   A C   1 
ATOM   2436 O  O   . ALA   A 1 302 ? -41.10300 19.36800  21.39100  1.000 171.85615 ? 338 ALA   A O   1 
ATOM   2437 C  CB  . ALA   A 1 302 ? -40.28700 22.16900  19.51900  1.000 169.22461 ? 338 ALA   A CB  1 
ATOM   2438 N  N   . THR   A 1 303 ? -42.08600 21.36800  21.71400  1.000 175.49994 ? 339 THR   A N   1 
ATOM   2439 C  CA  . THR   A 1 303 ? -42.33100 21.12100  23.13000  1.000 178.40519 ? 339 THR   A CA  1 
ATOM   2440 C  C   . THR   A 1 303 ? -43.54300 20.23200  23.38400  1.000 181.76845 ? 339 THR   A C   1 
ATOM   2441 O  O   . THR   A 1 303 ? -43.64600 19.64800  24.46800  1.000 183.91045 ? 339 THR   A O   1 
ATOM   2442 C  CB  . THR   A 1 303 ? -42.50500 22.45000  23.87400  1.000 171.96380 ? 339 THR   A CB  1 
ATOM   2443 O  OG1 . THR   A 1 303 ? -42.83500 22.19800  25.24700  1.000 171.45845 ? 339 THR   A OG1 1 
ATOM   2444 C  CG2 . THR   A 1 303 ? -43.60500 23.28100  23.23500  1.000 166.65618 ? 339 THR   A CG2 1 
ATOM   2445 N  N   . ILE   A 1 304 ? -44.45200 20.10400  22.41700  1.000 174.91012 ? 340 ILE   A N   1 
ATOM   2446 C  CA  . ILE   A 1 304 ? -45.65900 19.31500  22.64000  1.000 164.97814 ? 340 ILE   A CA  1 
ATOM   2447 C  C   . ILE   A 1 304 ? -45.39000 17.83000  22.42300  1.000 163.76391 ? 340 ILE   A C   1 
ATOM   2448 O  O   . ILE   A 1 304 ? -45.92100 16.98000  23.14700  1.000 162.24901 ? 340 ILE   A O   1 
ATOM   2449 C  CB  . ILE   A 1 304 ? -46.80300 19.82600  21.74200  1.000 158.22364 ? 340 ILE   A CB  1 
ATOM   2450 C  CG1 . ILE   A 1 304 ? -47.23000 21.23600  22.15900  1.000 160.22293 ? 340 ILE   A CG1 1 
ATOM   2451 C  CG2 . ILE   A 1 304 ? -47.99600 18.88300  21.79300  1.000 154.07615 ? 340 ILE   A CG2 1 
ATOM   2452 C  CD1 . ILE   A 1 304 ? -46.57400 22.34200  21.36700  1.000 162.31806 ? 340 ILE   A CD1 1 
ATOM   2453 N  N   . ASN   A 1 305 ? -44.55100 17.49000  21.44400  1.000 166.79303 ? 341 ASN   A N   1 
ATOM   2454 C  CA  . ASN   A 1 305 ? -44.30700 16.10100  21.07100  1.000 159.29338 ? 341 ASN   A CA  1 
ATOM   2455 C  C   . ASN   A 1 305 ? -43.04100 15.52200  21.69300  1.000 163.43783 ? 341 ASN   A C   1 
ATOM   2456 O  O   . ASN   A 1 305 ? -43.06900 14.39900  22.20700  1.000 165.76170 ? 341 ASN   A O   1 
ATOM   2457 C  CB  . ASN   A 1 305 ? -44.24200 15.97300  19.54300  1.000 143.19441 ? 341 ASN   A CB  1 
ATOM   2458 C  CG  . ASN   A 1 305 ? -45.61000 16.08300  18.89200  1.000 138.61162 ? 341 ASN   A CG  1 
ATOM   2459 O  OD1 . ASN   A 1 305 ? -45.84700 16.95500  18.05500  1.000 129.80135 ? 341 ASN   A OD1 1 
ATOM   2460 N  ND2 . ASN   A 1 305 ? -46.52000 15.19600  19.27800  1.000 135.89209 ? 341 ASN   A ND2 1 
ATOM   2461 N  N   . LYS   A 1 306 ? -41.93200 16.25700  21.65500  1.000 176.36917 ? 342 LYS   A N   1 
ATOM   2462 C  CA  . LYS   A 1 306 ? -40.65100 15.74300  22.14300  1.000 176.78568 ? 342 LYS   A CA  1 
ATOM   2463 C  C   . LYS   A 1 306 ? -40.70900 15.40300  23.62900  1.000 181.13915 ? 342 LYS   A C   1 
ATOM   2464 O  O   . LYS   A 1 306 ? -40.33000 14.30500  24.03800  1.000 184.54586 ? 342 LYS   A O   1 
ATOM   2465 C  CB  . LYS   A 1 306 ? -39.53200 16.75600  21.88900  1.000 167.36360 ? 342 LYS   A CB  1 
ATOM   2466 C  CG  . LYS   A 1 306 ? -38.21100 16.14500  21.44800  1.000 158.48919 ? 342 LYS   A CG  1 
ATOM   2467 C  CD  . LYS   A 1 306 ? -38.25400 15.75300  19.98000  1.000 144.49585 ? 342 LYS   A CD  1 
ATOM   2468 C  CE  . LYS   A 1 306 ? -36.91700 15.21100  19.50200  1.000 127.50409 ? 342 LYS   A CE  1 
ATOM   2469 N  NZ  . LYS   A 1 306 ? -36.94700 14.86300  18.05300  1.000 115.77726 ? 342 LYS   A NZ  1 
HETATM 2470 C  C1  . A1BIP B 2 .   ? -29.68900 9.10400   16.48300  1.000 122.80221 ? 401 A1BIP A C1  1 
HETATM 2471 C  C10 . A1BIP B 2 .   ? -24.15800 10.85400  13.37400  1.000 84.00589  ? 401 A1BIP A C10 1 
HETATM 2472 C  C11 . A1BIP B 2 .   ? -27.67100 11.84400  14.21400  1.000 85.75490  ? 401 A1BIP A C11 1 
HETATM 2473 C  C12 . A1BIP B 2 .   ? -28.13200 13.01900  13.44500  1.000 82.69352  ? 401 A1BIP A C12 1 
HETATM 2474 C  C13 . A1BIP B 2 .   ? -29.05500 13.91300  13.98100  1.000 78.73074  ? 401 A1BIP A C13 1 
HETATM 2475 C  C14 . A1BIP B 2 .   ? -29.45600 14.98800  13.21600  1.000 67.80124  ? 401 A1BIP A C14 1 
HETATM 2476 C  C15 . A1BIP B 2 .   ? -28.15300 14.35000  11.46800  1.000 61.58394  ? 401 A1BIP A C15 1 
HETATM 2477 C  C16 . A1BIP B 2 .   ? -27.68600 13.24400  12.14500  1.000 70.34285  ? 401 A1BIP A C16 1 
HETATM 2478 C  C17 . A1BIP B 2 .   ? -29.88000 11.03500  15.15300  1.000 94.77835  ? 401 A1BIP A C17 1 
HETATM 2479 C  C18 . A1BIP B 2 .   ? -30.46000 10.09200  15.92100  1.000 109.27323 ? 401 A1BIP A C18 1 
HETATM 2480 C  C2  . A1BIP B 2 .   ? -28.33100 9.02600   16.29800  1.000 116.33137 ? 401 A1BIP A C2  1 
HETATM 2481 C  C3  . A1BIP B 2 .   ? -27.72100 10.01100  15.49900  1.000 104.01716 ? 401 A1BIP A C3  1 
HETATM 2482 C  C4  . A1BIP B 2 .   ? -26.41100 11.31100  14.35400  1.000 91.11388  ? 401 A1BIP A C4  1 
HETATM 2483 C  C5  . A1BIP B 2 .   ? -25.11800 11.77000  13.80800  1.000 85.49290  ? 401 A1BIP A C5  1 
HETATM 2484 C  C6  . A1BIP B 2 .   ? -24.82600 13.13300  13.70300  1.000 85.28464  ? 401 A1BIP A C6  1 
HETATM 2485 C  C7  . A1BIP B 2 .   ? -23.61500 13.56600  13.19400  1.000 83.83152  ? 401 A1BIP A C7  1 
HETATM 2486 C  C8  . A1BIP B 2 .   ? -22.71000 12.62600  12.78400  1.000 86.05885  ? 401 A1BIP A C8  1 
HETATM 2487 C  C9  . A1BIP B 2 .   ? -22.94700 11.28100  12.86000  1.000 83.90260  ? 401 A1BIP A C9  1 
HETATM 2488 F  F1  . A1BIP B 2 .   ? -30.29200 8.15600   17.25600  1.000 130.66941 ? 401 A1BIP A F1  1 
HETATM 2489 F  F2  . A1BIP B 2 .   ? -21.51900 13.04800  12.27800  1.000 86.28113  ? 401 A1BIP A F2  1 
HETATM 2490 N  N1  . A1BIP B 2 .   ? -26.44900 10.18900  15.14000  1.000 90.50519  ? 401 A1BIP A N1  1 
HETATM 2491 N  N2  . A1BIP B 2 .   ? -29.02400 15.22100  11.97700  1.000 62.38458  ? 401 A1BIP A N2  1 
HETATM 2492 N  N3  . A1BIP B 2 .   ? -28.52000 11.00100  14.94100  1.000 91.27155  ? 401 A1BIP A N3  1 
HETATM 2493 CL CL  . CL    C 3 .   ? -37.25700 -4.43100  24.13900  1.000 93.91364  ? 402 CL    A CL  1 
HETATM 2494 O  O   . HOH   D 4 .   ? -16.75000 -19.45700 2.59800   1.000 72.15440  ? 501 HOH   A O   1 
HETATM 2495 O  O   . HOH   D 4 .   ? -28.77600 -5.09500  11.22500  1.000 63.68265  ? 502 HOH   A O   1 
HETATM 2496 O  O   . HOH   D 4 .   ? -35.03500 -16.38500 -1.70200  1.000 80.44628  ? 503 HOH   A O   1 
HETATM 2497 O  O   . HOH   D 4 .   ? -45.57100 18.49400  4.03600   1.000 69.77244  ? 504 HOH   A O   1 
HETATM 2498 O  O   . HOH   D 4 .   ? -26.21000 -20.55900 6.08000   1.000 72.07830  ? 505 HOH   A O   1 
HETATM 2499 O  O   . HOH   D 4 .   ? -52.99400 4.47900   12.97000  1.000 65.25355  ? 506 HOH   A O   1 
HETATM 2500 O  O   . HOH   D 4 .   ? -22.90200 -20.89300 3.21800   1.000 80.94621  ? 507 HOH   A O   1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1    N N   . SER A 1   ? 1.02505 1.73579 1.99760 0.00983  -0.04373 -0.37119 37  SER A N   
2    C CA  . SER A 1   ? 1.11824 1.79441 2.10083 -0.01591 -0.02667 -0.34247 37  SER A CA  
3    C C   . SER A 1   ? 1.35932 2.01997 2.30765 -0.01424 -0.01299 -0.31648 37  SER A C   
4    O O   . SER A 1   ? 1.40044 2.07523 2.32396 0.00031  -0.01380 -0.31154 37  SER A O   
5    C CB  . SER A 1   ? 1.16082 1.83705 2.16423 -0.03531 -0.01634 -0.32226 37  SER A CB  
6    O OG  . SER A 1   ? 1.17944 1.82509 2.19265 -0.05720 -0.00234 -0.29561 37  SER A OG  
7    N N   . SER A 2   ? 1.35256 1.98443 2.30507 -0.02857 -0.00360 -0.30172 38  SER A N   
8    C CA  . SER A 2   ? 1.37354 1.99138 2.30083 -0.02944 0.00790  -0.27895 38  SER A CA  
9    C C   . SER A 2   ? 1.38860 1.98520 2.30612 -0.03979 0.01924  -0.24939 38  SER A C   
10   O O   . SER A 2   ? 1.22428 1.80813 2.12524 -0.04040 0.02505  -0.23207 38  SER A O   
11   C CB  . SER A 2   ? 1.26511 1.86884 2.20164 -0.03372 0.00929  -0.28345 38  SER A CB  
12   O OG  . SER A 2   ? 1.33842 1.91525 2.30375 -0.04887 0.00776  -0.28306 38  SER A OG  
13   N N   . VAL A 3   ? 1.77707 2.37680 2.70866 -0.04681 0.02193  -0.24440 39  VAL A N   
14   C CA  . VAL A 3   ? 1.57638 2.16891 2.50193 -0.05128 0.03286  -0.22025 39  VAL A CA  
15   C C   . VAL A 3   ? 1.57202 2.19431 2.48806 -0.03418 0.02828  -0.22487 39  VAL A C   
16   O O   . VAL A 3   ? 1.62869 2.28105 2.55689 -0.02888 0.02264  -0.24019 39  VAL A O   
17   C CB  . VAL A 3   ? 1.78965 2.37918 2.74338 -0.06986 0.04201  -0.20812 39  VAL A CB  
18   C CG1 . VAL A 3   ? 1.60269 2.20125 2.55151 -0.06885 0.05497  -0.18512 39  VAL A CG1 
19   C CG2 . VAL A 3   ? 1.79424 2.34990 2.76209 -0.08238 0.04097  -0.20779 39  VAL A CG2 
20   N N   . VAL A 4   ? 1.09991 1.71501 1.99922 -0.02317 0.02683  -0.21548 40  VAL A N   
21   C CA  . VAL A 4   ? 1.08413 1.72518 1.97741 -0.00036 0.01719  -0.22368 40  VAL A CA  
22   C C   . VAL A 4   ? 0.93166 1.57318 1.82523 0.00478  0.02477  -0.20892 40  VAL A C   
23   O O   . VAL A 4   ? 0.78539 1.40055 1.68087 -0.00812 0.03439  -0.19197 40  VAL A O   
24   C CB  . VAL A 4   ? 0.94288 1.57086 1.81278 0.01678  -0.00237 -0.23066 40  VAL A CB  
25   C CG1 . VAL A 4   ? 1.03682 1.67422 1.90742 0.01497  -0.00707 -0.24446 40  VAL A CG1 
26   C CG2 . VAL A 4   ? 0.94637 1.52259 1.78800 0.00990  -0.00380 -0.20670 40  VAL A CG2 
27   N N   . GLY A 5   ? 0.78936 1.46607 1.67975 0.02940  0.01828  -0.21911 41  GLY A N   
28   C CA  . GLY A 5   ? 0.64437 1.33261 1.52968 0.04407  0.02393  -0.20978 41  GLY A CA  
29   C C   . GLY A 5   ? 0.62350 1.33022 1.53102 0.02284  0.05122  -0.18853 41  GLY A C   
30   O O   . GLY A 5   ? 0.60625 1.31556 1.51261 0.03175  0.05898  -0.17697 41  GLY A O   
31   N N   . LEU A 6   ? 0.51001 1.22610 1.43676 -0.00308 0.06219  -0.18295 42  LEU A N   
32   C CA  . LEU A 6   ? 0.50052 1.23161 1.45498 -0.02821 0.08386  -0.15980 42  LEU A CA  
33   C C   . LEU A 6   ? 0.64789 1.32608 1.60355 -0.04678 0.08826  -0.14452 42  LEU A C   
34   O O   . LEU A 6   ? 0.68325 1.34403 1.66012 -0.07275 0.09242  -0.13662 42  LEU A O   
35   C CB  . LEU A 6   ? 0.48478 1.27695 1.44829 -0.01327 0.10152  -0.14707 42  LEU A CB  
36   C CG  . LEU A 6   ? 0.51670 1.38031 1.48905 0.00216  0.10465  -0.15576 42  LEU A CG  
37   C CD1 . LEU A 6   ? 0.60407 1.46708 1.54306 0.04011  0.07890  -0.18806 42  LEU A CD1 
38   C CD2 . LEU A 6   ? 0.42998 1.35932 1.41468 0.01173  0.13062  -0.13435 42  LEU A CD2 
39   N N   . HIS A 7   ? 0.34554 0.99749 1.28303 -0.03157 0.08345  -0.14330 43  HIS A N   
40   C CA  . HIS A 7   ? 0.49578 1.10799 1.43821 -0.04319 0.08859  -0.12839 43  HIS A CA  
41   C C   . HIS A 7   ? 0.69564 1.25939 1.61926 -0.04198 0.07227  -0.13793 43  HIS A C   
42   O O   . HIS A 7   ? 0.55302 1.08880 1.47863 -0.04295 0.07200  -0.12999 43  HIS A O   
43   C CB  . HIS A 7   ? 0.51562 1.14207 1.45137 -0.02468 0.09863  -0.11306 43  HIS A CB  
44   C CG  . HIS A 7   ? 0.36917 1.05449 1.32316 -0.02627 0.12175  -0.09597 43  HIS A CG  
45   N ND1 . HIS A 7   ? 0.59963 1.32643 1.58704 -0.04720 0.13100  -0.09557 43  HIS A ND1 
46   C CD2 . HIS A 7   ? 0.41336 1.12047 1.34135 -0.00827 0.13593  -0.07480 43  HIS A CD2 
47   C CE1 . HIS A 7   ? 0.69331 1.48209 1.70197 -0.04762 0.15543  -0.07513 43  HIS A CE1 
48   N NE2 . HIS A 7   ? 0.73945 1.51700 1.70537 -0.02219 0.16014  -0.06070 43  HIS A NE2 
49   N N   . TYR A 8   ? 0.68454 1.24406 1.59417 -0.03948 0.05954  -0.15354 44  TYR A N   
50   C CA  . TYR A 8   ? 0.62303 1.15229 1.51971 -0.03893 0.04764  -0.15749 44  TYR A CA  
51   C C   . TYR A 8   ? 0.86718 1.39345 1.75927 -0.04835 0.04468  -0.16824 44  TYR A C   
52   O O   . TYR A 8   ? 1.04109 1.59022 1.93199 -0.04221 0.03943  -0.18102 44  TYR A O   
53   C CB  . TYR A 8   ? 0.52393 1.05112 1.40283 -0.01906 0.03112  -0.16142 44  TYR A CB  
54   C CG  . TYR A 8   ? 0.43656 0.95066 1.29237 -0.00048 0.02697  -0.15242 44  TYR A CG  
55   C CD1 . TYR A 8   ? 0.56030 1.04185 1.41058 -0.00251 0.02509  -0.14186 44  TYR A CD1 
56   C CD2 . TYR A 8   ? 0.51974 1.05993 1.35838 0.02412  0.02325  -0.15802 44  TYR A CD2 
57   C CE1 . TYR A 8   ? 0.58519 1.05560 1.40980 0.02034  0.01824  -0.13695 44  TYR A CE1 
58   C CE2 . TYR A 8   ? 0.51630 1.05076 1.32831 0.04853  0.01813  -0.15316 44  TYR A CE2 
59   C CZ  . TYR A 8   ? 0.50279 0.99994 1.30611 0.04693  0.01503  -0.14252 44  TYR A CZ  
60   O OH  . TYR A 8   ? 0.57829 1.07026 1.35046 0.07689  0.00682  -0.14085 44  TYR A OH  
61   N N   . LYS A 9   ? 0.83170 1.33614 1.72395 -0.05805 0.04623  -0.16681 45  LYS A N   
62   C CA  . LYS A 9   ? 0.91274 1.42398 1.80441 -0.06040 0.04301  -0.18074 45  LYS A CA  
63   C C   . LYS A 9   ? 0.84259 1.36279 1.72368 -0.05681 0.03886  -0.17893 45  LYS A C   
64   O O   . LYS A 9   ? 0.72359 1.22985 1.60289 -0.05978 0.03774  -0.16588 45  LYS A O   
65   C CB  . LYS A 9   ? 0.77345 1.26752 1.67851 -0.06747 0.04455  -0.18509 45  LYS A CB  
66   C CG  . LYS A 9   ? 0.85488 1.36149 1.75795 -0.06334 0.04154  -0.19793 45  LYS A CG  
67   C CD  . LYS A 9   ? 0.67770 1.16895 1.59720 -0.06454 0.03993  -0.20452 45  LYS A CD  
68   C CE  . LYS A 9   ? 0.84989 1.36378 1.76317 -0.05840 0.04110  -0.20932 45  LYS A CE  
69   N NZ  . LYS A 9   ? 0.76739 1.32309 1.67949 -0.04930 0.04039  -0.22648 45  LYS A NZ  
70   N N   . ILE A 10  ? 0.96916 1.51699 1.85010 -0.05124 0.03552  -0.19186 46  ILE A N   
71   C CA  . ILE A 10  ? 0.96220 1.53092 1.84297 -0.05086 0.03424  -0.18683 46  ILE A CA  
72   C C   . ILE A 10  ? 1.01778 1.59933 1.90022 -0.05538 0.04241  -0.18718 46  ILE A C   
73   O O   . ILE A 10  ? 1.11914 1.71209 2.00511 -0.04880 0.04281  -0.20641 46  ILE A O   
74   C CB  . ILE A 10  ? 0.89868 1.48768 1.75968 -0.03704 0.02633  -0.19734 46  ILE A CB  
75   C CG1 . ILE A 10  ? 0.89005 1.46002 1.73160 -0.02706 0.01411  -0.19371 46  ILE A CG1 
76   C CG2 . ILE A 10  ? 1.13263 1.72835 1.95913 -0.03625 0.02782  -0.18164 46  ILE A CG2 
77   C CD1 . ILE A 10  ? 0.96903 1.55487 1.78699 -0.00852 0.00219  -0.20781 46  ILE A CD1 
78   N N   . GLY A 11  ? 1.30118 1.88506 2.18748 -0.06568 0.04632  -0.16847 47  GLY A N   
79   C CA  . GLY A 11  ? 1.40589 2.01685 2.29630 -0.06819 0.05574  -0.16819 47  GLY A CA  
80   C C   . GLY A 11  ? 1.63398 2.28227 2.50861 -0.07099 0.06320  -0.15247 47  GLY A C   
81   O O   . GLY A 11  ? 1.67110 2.33130 2.51756 -0.05921 0.06113  -0.15610 47  GLY A O   
82   N N   . LYS A 12  ? 1.34712 2.01056 2.23010 -0.08601 0.07113  -0.13105 48  LYS A N   
83   C CA  . LYS A 12  ? 1.21918 1.91629 2.07887 -0.09387 0.08152  -0.10408 48  LYS A CA  
84   C C   . LYS A 12  ? 1.11987 1.76563 1.94924 -0.10794 0.06843  -0.07043 48  LYS A C   
85   O O   . LYS A 12  ? 1.19455 1.78498 2.02783 -0.11220 0.05118  -0.06868 48  LYS A O   
86   C CB  . LYS A 12  ? 1.20055 1.94490 2.09064 -0.10823 0.09608  -0.09214 48  LYS A CB  
87   C CG  . LYS A 12  ? 1.14389 1.85042 2.05808 -0.13376 0.08654  -0.06901 48  LYS A CG  
88   C CD  . LYS A 12  ? 1.00583 1.77211 1.95620 -0.15058 0.10119  -0.05550 48  LYS A CD  
89   C CE  . LYS A 12  ? 0.97953 1.70647 1.95875 -0.17682 0.08588  -0.03445 48  LYS A CE  
90   N NZ  . LYS A 12  ? 0.94926 1.73496 1.95875 -0.19362 0.09726  -0.02148 48  LYS A NZ  
91   N N   . LYS A 13  ? 1.04259 1.70644 1.83782 -0.11204 0.07467  -0.04346 49  LYS A N   
92   C CA  . LYS A 13  ? 1.04644 1.65449 1.80831 -0.12495 0.05771  -0.00849 49  LYS A CA  
93   C C   . LYS A 13  ? 1.13462 1.73014 1.92216 -0.16003 0.05619  0.02891  49  LYS A C   
94   O O   . LYS A 13  ? 0.99679 1.65246 1.80555 -0.17685 0.07827  0.04712  49  LYS A O   
95   C CB  . LYS A 13  ? 0.95674 1.58223 1.66537 -0.11400 0.06262  0.00893  49  LYS A CB  
96   C CG  . LYS A 13  ? 0.94199 1.50496 1.61172 -0.12896 0.04296  0.05180  49  LYS A CG  
97   C CD  . LYS A 13  ? 1.01556 1.60289 1.68546 -0.16276 0.05857  0.10576  49  LYS A CD  
98   C CE  . LYS A 13  ? 1.23496 1.74645 1.86100 -0.17734 0.03324  0.15074  49  LYS A CE  
99   N NZ  . LYS A 13  ? 1.19639 1.71796 1.83687 -0.22222 0.04370  0.21115  49  LYS A NZ  
100  N N   . ILE A 14  ? 1.17008 1.69250 1.95865 -0.16927 0.02811  0.03806  50  ILE A N   
101  C CA  . ILE A 14  ? 1.16813 1.65971 1.97437 -0.20377 0.01497  0.07760  50  ILE A CA  
102  C C   . ILE A 14  ? 1.34306 1.76128 2.10028 -0.20467 -0.01353 0.10407  50  ILE A C   
103  O O   . ILE A 14  ? 1.35705 1.73338 2.07992 -0.17506 -0.03287 0.08020  50  ILE A O   
104  C CB  . ILE A 14  ? 1.10577 1.56738 1.95750 -0.21067 -0.00303 0.06216  50  ILE A CB  
105  C CG1 . ILE A 14  ? 1.17019 1.55571 1.99768 -0.18646 -0.03677 0.04050  50  ILE A CG1 
106  C CG2 . ILE A 14  ? 1.07637 1.59947 1.96710 -0.20085 0.02021  0.03025  50  ILE A CG2 
107  C CD1 . ILE A 14  ? 1.21459 1.52408 2.04211 -0.20219 -0.07660 0.06269  50  ILE A CD1 
108  N N   . GLY A 15  ? 1.51871 1.92398 2.27335 -0.23828 -0.01677 0.15428  51  GLY A N   
109  C CA  . GLY A 15  ? 1.76806 2.09840 2.46930 -0.23818 -0.04582 0.18335  51  GLY A CA  
110  C C   . GLY A 15  ? 2.09995 2.33873 2.81610 -0.25954 -0.09089 0.20249  51  GLY A C   
111  O O   . GLY A 15  ? 1.91445 2.10844 2.64235 -0.23977 -0.11921 0.16699  51  GLY A O   
112  N N   . GLU A 16  ? 2.76226 2.97269 3.47661 -0.29904 -0.09955 0.25991  52  GLU A N   
113  C CA  . GLU A 16  ? 2.79927 2.92242 3.53847 -0.33012 -0.14537 0.28695  52  GLU A CA  
114  C C   . GLU A 16  ? 2.90738 2.91749 3.59822 -0.29776 -0.20260 0.26786  52  GLU A C   
115  O O   . GLU A 16  ? 2.92358 2.85104 3.63427 -0.31269 -0.25106 0.27614  52  GLU A O   
116  C CB  . GLU A 16  ? 2.64884 2.79410 3.46605 -0.34790 -0.14873 0.26670  52  GLU A CB  
117  C CG  . GLU A 16  ? 2.58635 2.85185 3.45419 -0.36786 -0.09472 0.27010  52  GLU A CG  
118  C CD  . GLU A 16  ? 2.71696 3.03811 3.58397 -0.40770 -0.06189 0.33190  52  GLU A CD  
119  O OE1 . GLU A 16  ? 2.88893 3.15493 3.76252 -0.44877 -0.08560 0.38523  52  GLU A OE1 
120  O OE2 . GLU A 16  ? 2.66050 3.08098 3.51928 -0.39684 -0.01370 0.32791  52  GLU A OE2 
121  N N   . GLY A 17  ? 2.43538 2.44157 3.06587 -0.25160 -0.20213 0.23956  53  GLY A N   
122  C CA  . GLY A 17  ? 2.50493 2.41307 3.08495 -0.21700 -0.25641 0.22257  53  GLY A CA  
123  C C   . GLY A 17  ? 2.73044 2.61709 3.23759 -0.20145 -0.25846 0.24561  53  GLY A C   
124  O O   . GLY A 17  ? 2.69070 2.59244 3.15736 -0.15426 -0.25764 0.20637  53  GLY A O   
125  N N   . SER A 18  ? 2.91348 2.76637 3.40473 -0.24121 -0.26211 0.31062  54  SER A N   
126  C CA  . SER A 18  ? 3.01273 2.86452 3.43291 -0.23246 -0.25127 0.34442  54  SER A CA  
127  C C   . SER A 18  ? 3.06530 3.04357 3.48847 -0.21647 -0.18926 0.32162  54  SER A C   
128  O O   . SER A 18  ? 2.97391 3.03445 3.45566 -0.24385 -0.14869 0.32430  54  SER A O   
129  C CB  . SER A 18  ? 3.05106 2.80791 3.40131 -0.18423 -0.30575 0.32198  54  SER A CB  
130  O OG  . SER A 18  ? 3.02670 2.66575 3.38176 -0.19501 -0.36881 0.33389  54  SER A OG  
131  N N   . PHE A 19  ? 3.42122 3.41892 3.78651 -0.17101 -0.18413 0.29559  55  PHE A N   
132  C CA  . PHE A 19  ? 3.37549 3.48185 3.75229 -0.14640 -0.13863 0.25461  55  PHE A CA  
133  C C   . PHE A 19  ? 3.38727 3.49615 3.77500 -0.10171 -0.15395 0.18341  55  PHE A C   
134  O O   . PHE A 19  ? 3.54580 3.71410 3.92178 -0.06885 -0.13547 0.14556  55  PHE A O   
135  C CB  . PHE A 19  ? 3.46341 3.60964 3.77574 -0.12870 -0.11713 0.27520  55  PHE A CB  
136  C CG  . PHE A 19  ? 3.40317 3.66514 3.73431 -0.10993 -0.07106 0.23915  55  PHE A CG  
137  C CD1 . PHE A 19  ? 3.22196 3.55900 3.61922 -0.13674 -0.03453 0.23610  55  PHE A CD1 
138  C CD2 . PHE A 19  ? 3.43568 3.72854 3.72048 -0.06271 -0.06983 0.20424  55  PHE A CD2 
139  C CE1 . PHE A 19  ? 3.14620 3.58078 3.55967 -0.11569 0.00044  0.19933  55  PHE A CE1 
140  C CE2 . PHE A 19  ? 3.35211 3.74352 3.65737 -0.04400 -0.03532 0.16719  55  PHE A CE2 
141  C CZ  . PHE A 19  ? 3.27525 3.73440 3.64332 -0.06994 -0.00117 0.16485  55  PHE A CZ  
142  N N   . GLY A 20  ? 3.01555 3.06262 3.42679 -0.09951 -0.18941 0.16517  56  GLY A N   
143  C CA  . GLY A 20  ? 2.76984 2.83331 3.20068 -0.06277 -0.19733 0.10366  56  GLY A CA  
144  C C   . GLY A 20  ? 2.68070 2.84104 3.16366 -0.06772 -0.15019 0.07628  56  GLY A C   
145  O O   . GLY A 20  ? 2.45527 2.64676 2.98254 -0.10210 -0.12610 0.09497  56  GLY A O   
146  N N   . VAL A 21  ? 3.36667 3.57477 3.84745 -0.03370 -0.13956 0.03163  57  VAL A N   
147  C CA  . VAL A 21  ? 3.27484 3.56793 3.79947 -0.03600 -0.09963 0.00564  57  VAL A CA  
148  C C   . VAL A 21  ? 3.12525 3.42360 3.70482 -0.04615 -0.09496 -0.01261 57  VAL A C   
149  O O   . VAL A 21  ? 3.04757 3.35530 3.64154 -0.02340 -0.10016 -0.04884 57  VAL A O   
150  C CB  . VAL A 21  ? 3.19032 3.52569 3.70174 0.00049  -0.09648 -0.03572 57  VAL A CB  
151  C CG1 . VAL A 21  ? 3.10241 3.51629 3.65630 -0.00359 -0.06109 -0.05912 57  VAL A CG1 
152  C CG2 . VAL A 21  ? 3.28802 3.60525 3.73425 0.01922  -0.11081 -0.02038 57  VAL A CG2 
153  N N   . ILE A 22  ? 2.06872 2.36568 2.67938 -0.07973 -0.08486 0.01371  58  ILE A N   
154  C CA  . ILE A 22  ? 1.63380 1.93575 2.29327 -0.08841 -0.08115 -0.00142 58  ILE A CA  
155  C C   . ILE A 22  ? 1.42354 1.80023 2.12209 -0.09832 -0.04243 -0.01288 58  ILE A C   
156  O O   . ILE A 22  ? 1.39954 1.82014 2.09359 -0.10858 -0.02030 0.00218  58  ILE A O   
157  C CB  . ILE A 22  ? 1.45700 1.70535 2.13137 -0.11573 -0.10360 0.02866  58  ILE A CB  
158  C CG1 . ILE A 22  ? 1.58678 1.75312 2.21578 -0.10928 -0.14648 0.04782  58  ILE A CG1 
159  C CG2 . ILE A 22  ? 1.29310 1.53267 2.00438 -0.11086 -0.11189 0.00508  58  ILE A CG2 
160  C CD1 . ILE A 22  ? 1.48609 1.61496 2.09003 -0.06729 -0.17807 0.01144  58  ILE A CD1 
161  N N   . PHE A 23  ? 1.29158 1.68300 2.02486 -0.09154 -0.03588 -0.04016 59  PHE A N   
162  C CA  . PHE A 23  ? 1.20814 1.65804 1.97839 -0.09655 -0.00681 -0.05575 59  PHE A CA  
163  C C   . PHE A 23  ? 1.08275 1.52211 1.88976 -0.10304 -0.00852 -0.06314 59  PHE A C   
164  O O   . PHE A 23  ? 0.97810 1.37224 1.77954 -0.09559 -0.03049 -0.06508 59  PHE A O   
165  C CB  . PHE A 23  ? 1.27036 1.75407 2.04084 -0.07417 0.00339  -0.08864 59  PHE A CB  
166  C CG  . PHE A 23  ? 1.31285 1.83158 2.05874 -0.06584 0.01227  -0.08979 59  PHE A CG  
167  C CD1 . PHE A 23  ? 1.35976 1.85646 2.06099 -0.05100 -0.00391 -0.08464 59  PHE A CD1 
168  C CD2 . PHE A 23  ? 1.30055 1.87472 2.06419 -0.06672 0.03343  -0.09982 59  PHE A CD2 
169  C CE1 . PHE A 23  ? 1.44250 1.97176 2.11503 -0.03820 0.00245  -0.08696 59  PHE A CE1 
170  C CE2 . PHE A 23  ? 1.35080 1.96120 2.08655 -0.05211 0.03947  -0.10449 59  PHE A CE2 
171  C CZ  . PHE A 23  ? 1.37990 1.96776 2.06893 -0.03820 0.02471  -0.09697 59  PHE A CZ  
172  N N   . GLU A 24  ? 1.05901 1.54158 1.90000 -0.11188 0.01217  -0.06987 60  GLU A N   
173  C CA  . GLU A 24  ? 1.01888 1.49699 1.89061 -0.10939 0.01248  -0.08499 60  GLU A CA  
174  C C   . GLU A 24  ? 0.84600 1.33304 1.71999 -0.09070 0.01972  -0.11130 60  GLU A C   
175  O O   . GLU A 24  ? 0.98331 1.50195 1.85627 -0.08479 0.03088  -0.12423 60  GLU A O   
176  C CB  . GLU A 24  ? 0.97425 1.49384 1.88181 -0.12333 0.02737  -0.08358 60  GLU A CB  
177  C CG  . GLU A 24  ? 0.99730 1.51638 1.91839 -0.11124 0.03144  -0.10567 60  GLU A CG  
178  C CD  . GLU A 24  ? 1.07245 1.60020 2.00515 -0.11885 0.03167  -0.10116 60  GLU A CD  
179  O OE1 . GLU A 24  ? 0.99399 1.55491 1.94357 -0.13762 0.03655  -0.08365 60  GLU A OE1 
180  O OE2 . GLU A 24  ? 1.18647 1.69241 2.11634 -0.10668 0.02707  -0.11417 60  GLU A OE2 
181  N N   . GLY A 25  ? 0.66999 1.13035 1.54753 -0.08116 0.01185  -0.11821 61  GLY A N   
182  C CA  . GLY A 25  ? 0.70387 1.17354 1.58837 -0.06938 0.02009  -0.13497 61  GLY A CA  
183  C C   . GLY A 25  ? 0.53118 0.98727 1.42518 -0.06787 0.02439  -0.13729 61  GLY A C   
184  O O   . GLY A 25  ? 0.62168 1.06644 1.52429 -0.07212 0.01866  -0.13181 61  GLY A O   
185  N N   . THR A 26  ? 0.32938 0.78410 1.21912 -0.06225 0.03275  -0.14382 62  THR A N   
186  C CA  . THR A 26  ? 0.48120 0.91925 1.37963 -0.05984 0.03601  -0.14262 62  THR A CA  
187  C C   . THR A 26  ? 0.49603 0.94060 1.40019 -0.05523 0.04328  -0.14020 62  THR A C   
188  O O   . THR A 26  ? 0.54526 1.00235 1.44841 -0.06028 0.04936  -0.14488 62  THR A O   
189  C CB  . THR A 26  ? 0.53045 0.96629 1.43364 -0.06467 0.04012  -0.15103 62  THR A CB  
190  O OG1 . THR A 26  ? 0.54041 0.98911 1.44018 -0.06789 0.03771  -0.15264 62  THR A OG1 
191  C CG2 . THR A 26  ? 0.59617 1.01260 1.51868 -0.06120 0.03918  -0.14990 62  THR A CG2 
192  N N   . ASN A 27  ? 0.33335 0.77367 1.24232 -0.04398 0.04195  -0.13251 63  ASN A N   
193  C CA  . ASN A 27  ? 0.53882 0.99242 1.44594 -0.03887 0.05379  -0.12333 63  ASN A CA  
194  C C   . ASN A 27  ? 0.53464 0.98542 1.47278 -0.05553 0.06533  -0.11859 63  ASN A C   
195  O O   . ASN A 27  ? 0.42919 0.85113 1.36734 -0.05489 0.06195  -0.11415 63  ASN A O   
196  C CB  . ASN A 27  ? 0.50207 0.94088 1.37453 -0.01520 0.04809  -0.11295 63  ASN A CB  
197  C CG  . ASN A 27  ? 0.58156 1.05213 1.44516 -0.00482 0.06306  -0.10163 63  ASN A CG  
198  O OD1 . ASN A 27  ? 0.54738 1.04167 1.43985 -0.02289 0.08112  -0.09316 63  ASN A OD1 
199  N ND2 . ASN A 27  ? 0.59377 1.06870 1.42003 0.02517  0.05392  -0.10216 63  ASN A ND2 
200  N N   . ILE A 28  ? 0.42088 0.88909 1.37103 -0.06858 0.07326  -0.11935 64  ILE A N   
201  C CA  . ILE A 28  ? 0.41822 0.87109 1.39567 -0.08653 0.07606  -0.11648 64  ILE A CA  
202  C C   . ILE A 28  ? 0.42925 0.88215 1.42880 -0.09222 0.08965  -0.09024 64  ILE A C   
203  O O   . ILE A 28  ? 0.68429 1.11719 1.71205 -0.11032 0.09064  -0.08067 64  ILE A O   
204  C CB  . ILE A 28  ? 0.64035 1.10721 1.62272 -0.09804 0.07417  -0.12711 64  ILE A CB  
205  C CG1 . ILE A 28  ? 0.63502 1.14353 1.60705 -0.09234 0.08170  -0.12362 64  ILE A CG1 
206  C CG2 . ILE A 28  ? 0.71716 1.17399 1.68409 -0.09274 0.06042  -0.15135 64  ILE A CG2 
207  C CD1 . ILE A 28  ? 0.77060 1.29854 1.75166 -0.10047 0.07683  -0.13734 64  ILE A CD1 
208  N N   . ILE A 29  ? 0.45645 0.91805 1.41825 -0.07275 0.09618  -0.07540 65  ILE A N   
209  C CA  . ILE A 29  ? 0.48549 0.94012 1.43087 -0.06926 0.10947  -0.04429 65  ILE A CA  
210  C C   . ILE A 29  ? 0.59399 0.99693 1.50926 -0.05383 0.09769  -0.03957 65  ILE A C   
211  O O   . ILE A 29  ? 0.48781 0.85866 1.40618 -0.06223 0.10019  -0.01992 65  ILE A O   
212  C CB  . ILE A 29  ? 0.54604 1.04750 1.46219 -0.04790 0.12185  -0.03423 65  ILE A CB  
213  C CG1 . ILE A 29  ? 0.52585 1.08702 1.48097 -0.06639 0.13868  -0.03060 65  ILE A CG1 
214  C CG2 . ILE A 29  ? 0.48209 0.97460 1.35927 -0.02984 0.13208  -0.00481 65  ILE A CG2 
215  C CD1 . ILE A 29  ? 0.46594 1.04534 1.44648 -0.08992 0.16212  0.00634  65  ILE A CD1 
216  N N   . ASN A 30  ? 0.54959 0.94109 1.43764 -0.03156 0.08161  -0.05726 66  ASN A N   
217  C CA  . ASN A 30  ? 0.60182 0.95200 1.46519 -0.01368 0.06715  -0.05744 66  ASN A CA  
218  C C   . ASN A 30  ? 0.53447 0.86785 1.41732 -0.01762 0.04900  -0.08307 66  ASN A C   
219  O O   . ASN A 30  ? 0.56784 0.87083 1.44283 -0.00617 0.03614  -0.08657 66  ASN A O   
220  C CB  . ASN A 30  ? 0.66430 1.01698 1.48036 0.02016  0.05968  -0.05526 66  ASN A CB  
221  C CG  . ASN A 30  ? 0.62765 0.99942 1.43991 0.02830  0.04720  -0.07585 66  ASN A CG  
222  O OD1 . ASN A 30  ? 0.54486 0.92749 1.38564 0.00867  0.04576  -0.08918 66  ASN A OD1 
223  N ND2 . ASN A 30  ? 0.70580 1.07814 1.47889 0.06045  0.03487  -0.07877 66  ASN A ND2 
224  N N   . GLY A 31  ? 0.62565 0.98329 1.53221 -0.03113 0.04797  -0.10047 67  GLY A N   
225  C CA  . GLY A 31  ? 0.37714 0.73444 1.30312 -0.03565 0.03619  -0.12088 67  GLY A CA  
226  C C   . GLY A 31  ? 0.54726 0.90946 1.46197 -0.02750 0.02324  -0.12823 67  GLY A C   
227  O O   . GLY A 31  ? 0.46704 0.84009 1.40186 -0.03438 0.01680  -0.14075 67  GLY A O   
228  N N   . VAL A 32  ? 0.55079 0.90759 1.43632 -0.01269 0.01749  -0.12102 68  VAL A N   
229  C CA  . VAL A 32  ? 0.59255 0.94251 1.47124 -0.00667 -0.00252 -0.12788 68  VAL A CA  
230  C C   . VAL A 32  ? 0.35741 0.72803 1.24807 -0.02428 -0.00071 -0.13082 68  VAL A C   
231  O O   . VAL A 32  ? 0.49294 0.88162 1.38082 -0.02867 0.01179  -0.12927 68  VAL A O   
232  C CB  . VAL A 32  ? 0.58952 0.92270 1.43016 0.02097  -0.01631 -0.12467 68  VAL A CB  
233  C CG1 . VAL A 32  ? 0.77132 1.08682 1.59116 0.04233  -0.01610 -0.11850 68  VAL A CG1 
234  C CG2 . VAL A 32  ? 0.66743 1.02129 1.48991 0.02673  -0.00636 -0.12013 68  VAL A CG2 
235  N N   . PRO A 33  ? 0.49263 0.86448 1.39808 -0.03544 -0.01248 -0.13332 69  PRO A N   
236  C CA  . PRO A 33  ? 0.38033 0.76854 1.28922 -0.05157 -0.01068 -0.12961 69  PRO A CA  
237  C C   . PRO A 33  ? 0.40493 0.76816 1.28591 -0.04228 -0.03035 -0.12456 69  PRO A C   
238  O O   . PRO A 33  ? 0.56695 0.90027 1.43395 -0.02617 -0.05247 -0.12649 69  PRO A O   
239  C CB  . PRO A 33  ? 0.46067 0.86551 1.39989 -0.06921 -0.01327 -0.12865 69  PRO A CB  
240  C CG  . PRO A 33  ? 0.38226 0.76406 1.32794 -0.05834 -0.03127 -0.13315 69  PRO A CG  
241  C CD  . PRO A 33  ? 0.35989 0.72416 1.28426 -0.03582 -0.02650 -0.13802 69  PRO A CD  
242  N N   . VAL A 34  ? 0.37076 0.74444 1.24104 -0.04816 -0.02634 -0.12131 70  VAL A N   
243  C CA  . VAL A 34  ? 0.56446 0.91205 1.40460 -0.03580 -0.04805 -0.11920 70  VAL A CA  
244  C C   . VAL A 34  ? 0.55130 0.89711 1.39042 -0.05563 -0.05266 -0.10651 70  VAL A C   
245  O O   . VAL A 34  ? 0.53635 0.91181 1.39659 -0.07642 -0.03482 -0.09990 70  VAL A O   
246  C CB  . VAL A 34  ? 0.39730 0.76020 1.21580 -0.01406 -0.04088 -0.12849 70  VAL A CB  
247  C CG1 . VAL A 34  ? 0.57853 0.94762 1.39438 0.00382  -0.03287 -0.13267 70  VAL A CG1 
248  C CG2 . VAL A 34  ? 0.37954 0.78044 1.21151 -0.02661 -0.01785 -0.13133 70  VAL A CG2 
249  N N   . ALA A 35  ? 0.51036 0.82111 1.32070 -0.04574 -0.07849 -0.10275 71  ALA A N   
250  C CA  . ALA A 35  ? 0.47995 0.77816 1.27773 -0.06152 -0.08657 -0.08544 71  ALA A CA  
251  C C   . ALA A 35  ? 0.82699 1.12281 1.58894 -0.03797 -0.09308 -0.09571 71  ALA A C   
252  O O   . ALA A 35  ? 0.79164 1.05199 1.52683 -0.01293 -0.12196 -0.10480 71  ALA A O   
253  C CB  . ALA A 35  ? 0.57418 0.81937 1.37303 -0.07422 -0.12059 -0.06856 71  ALA A CB  
254  N N   . ILE A 36  ? 1.00739 1.34402 1.76965 -0.04174 -0.06956 -0.09866 72  ILE A N   
255  C CA  . ILE A 36  ? 0.83919 1.18573 1.57535 -0.01888 -0.07420 -0.11299 72  ILE A CA  
256  C C   . ILE A 36  ? 0.94357 1.25271 1.64306 -0.01917 -0.09720 -0.09678 72  ILE A C   
257  O O   . ILE A 36  ? 1.09716 1.40553 1.79720 -0.04359 -0.08971 -0.07287 72  ILE A O   
258  C CB  . ILE A 36  ? 0.92424 1.32889 1.68164 -0.02160 -0.04443 -0.12720 72  ILE A CB  
259  C CG1 . ILE A 36  ? 0.86276 1.29215 1.65783 -0.02878 -0.02353 -0.13498 72  ILE A CG1 
260  C CG2 . ILE A 36  ? 0.90819 1.33219 1.65020 0.00312  -0.05060 -0.14726 72  ILE A CG2 
261  C CD1 . ILE A 36  ? 0.67820 1.15280 1.50159 -0.03731 -0.00030 -0.14731 72  ILE A CD1 
262  N N   . LYS A 37  ? 1.10231 1.38296 1.76785 0.00979  -0.12549 -0.10855 73  LYS A N   
263  C CA  . LYS A 37  ? 1.18191 1.41352 1.80486 0.01503  -0.15488 -0.09369 73  LYS A CA  
264  C C   . LYS A 37  ? 1.32910 1.58668 1.92654 0.04472  -0.15760 -0.11595 73  LYS A C   
265  O O   . LYS A 37  ? 1.26377 1.54221 1.86146 0.07510  -0.16459 -0.14506 73  LYS A O   
266  C CB  . LYS A 37  ? 0.93754 1.09463 1.53907 0.02800  -0.20075 -0.09052 73  LYS A CB  
267  C CG  . LYS A 37  ? 0.92851 1.02538 1.47897 0.04518  -0.24055 -0.08288 73  LYS A CG  
268  C CD  . LYS A 37  ? 1.02647 1.03673 1.56079 0.05292  -0.29282 -0.07755 73  LYS A CD  
269  C CE  . LYS A 37  ? 1.03460 0.97993 1.55963 0.01495  -0.31128 -0.03110 73  LYS A CE  
270  N NZ  . LYS A 37  ? 1.07446 0.92285 1.58650 0.02174  -0.37199 -0.02715 73  LYS A NZ  
271  N N   . PHE A 38  ? 1.54136 1.80440 2.11720 0.03795  -0.15194 -0.10272 74  PHE A N   
272  C CA  . PHE A 38  ? 1.58765 1.86934 2.13489 0.06800  -0.16106 -0.12373 74  PHE A CA  
273  C C   . PHE A 38  ? 1.70625 1.91392 2.19454 0.08626  -0.20459 -0.10984 74  PHE A C   
274  O O   . PHE A 38  ? 1.75067 1.89389 2.22226 0.06577  -0.22265 -0.07538 74  PHE A O   
275  C CB  . PHE A 38  ? 1.65510 1.98915 2.20844 0.05765  -0.13216 -0.12290 74  PHE A CB  
276  C CG  . PHE A 38  ? 1.41569 1.81858 2.02469 0.04863  -0.09879 -0.14608 74  PHE A CG  
277  C CD1 . PHE A 38  ? 1.29210 1.70620 1.93818 0.01983  -0.07532 -0.13326 74  PHE A CD1 
278  C CD2 . PHE A 38  ? 1.33812 1.79248 1.96513 0.06856  -0.09438 -0.18093 74  PHE A CD2 
279  C CE1 . PHE A 38  ? 1.13157 1.59703 1.82515 0.01280  -0.05022 -0.15338 74  PHE A CE1 
280  C CE2 . PHE A 38  ? 1.18789 1.69564 1.86946 0.05630  -0.06851 -0.19898 74  PHE A CE2 
281  C CZ  . PHE A 38  ? 0.95625 1.46459 1.66775 0.02920  -0.04746 -0.18439 74  PHE A CZ  
282  N N   . GLU A 39  ? 2.04893 2.26537 2.50853 0.12480  -0.22423 -0.13723 75  GLU A N   
283  C CA  . GLU A 39  ? 2.18117 2.32469 2.57871 0.14971  -0.27027 -0.12881 75  GLU A CA  
284  C C   . GLU A 39  ? 2.14146 2.32409 2.51485 0.18443  -0.27496 -0.15702 75  GLU A C   
285  O O   . GLU A 39  ? 2.04347 2.29164 2.44767 0.20857  -0.26748 -0.19914 75  GLU A O   
286  C CB  . GLU A 39  ? 2.18252 2.27308 2.56635 0.17861  -0.31365 -0.14597 75  GLU A CB  
287  C CG  . GLU A 39  ? 2.23824 2.23191 2.55646 0.20106  -0.36957 -0.13269 75  GLU A CG  
288  C CD  . GLU A 39  ? 2.19888 2.16004 2.49747 0.25148  -0.41829 -0.17036 75  GLU A CD  
289  O OE1 . GLU A 39  ? 2.09731 2.13562 2.41969 0.28337  -0.40624 -0.21420 75  GLU A OE1 
290  O OE2 . GLU A 39  ? 2.27593 2.13614 2.53648 0.25991  -0.47024 -0.15598 75  GLU A OE2 
291  N N   . PRO A 40  ? 2.02253 2.17061 2.34309 0.18782  -0.28742 -0.13417 76  PRO A N   
292  C CA  . PRO A 40  ? 1.94306 2.12853 2.23806 0.22518  -0.29562 -0.16436 76  PRO A CA  
293  C C   . PRO A 40  ? 1.82169 1.99460 2.09783 0.27609  -0.33816 -0.20491 76  PRO A C   
294  O O   . PRO A 40  ? 1.84297 1.93596 2.08216 0.29134  -0.37967 -0.19596 76  PRO A O   
295  C CB  . PRO A 40  ? 2.00966 2.14136 2.23756 0.21934  -0.30569 -0.12121 76  PRO A CB  
296  C CG  . PRO A 40  ? 2.11280 2.21873 2.35575 0.16655  -0.28151 -0.06901 76  PRO A CG  
297  C CD  . PRO A 40  ? 2.07991 2.16209 2.36505 0.15513  -0.29078 -0.07686 76  PRO A CD  
298  N N   . ARG A 41  ? 1.68559 1.94178 1.99189 0.30337  -0.32993 -0.25217 77  ARG A N   
299  C CA  . ARG A 41  ? 1.60343 1.87444 1.90117 0.35519  -0.36541 -0.29697 77  ARG A CA  
300  C C   . ARG A 41  ? 1.69239 1.90213 1.91141 0.39658  -0.41339 -0.29903 77  ARG A C   
301  O O   . ARG A 41  ? 1.73120 1.92257 1.91250 0.38970  -0.40965 -0.27666 77  ARG A O   
302  C CB  . ARG A 41  ? 1.46680 1.85689 1.83296 0.36491  -0.33892 -0.34362 77  ARG A CB  
303  C CG  . ARG A 41  ? 1.40569 1.83945 1.78667 0.41006  -0.36218 -0.38840 77  ARG A CG  
304  C CD  . ARG A 41  ? 1.35360 1.74987 1.73398 0.40800  -0.36898 -0.37710 77  ARG A CD  
305  N NE  . ARG A 41  ? 1.37328 1.85215 1.79211 0.44022  -0.36808 -0.41813 77  ARG A NE  
306  C CZ  . ARG A 41  ? 1.54621 2.12547 2.03938 0.41843  -0.32309 -0.42846 77  ARG A CZ  
307  N NH1 . ARG A 41  ? 1.49587 2.10028 2.03418 0.36771  -0.28039 -0.40707 77  ARG A NH1 
308  N NH2 . ARG A 41  ? 1.74123 2.39870 2.26329 0.44955  -0.32205 -0.46017 77  ARG A NH2 
309  N N   . LYS A 42  ? 1.59279 1.77256 1.78300 0.44472  -0.46054 -0.32763 78  LYS A N   
310  C CA  . LYS A 42  ? 1.79949 1.91174 1.91059 0.49291  -0.51592 -0.33495 78  LYS A CA  
311  C C   . LYS A 42  ? 2.02442 2.01706 2.06582 0.46679  -0.53271 -0.27138 78  LYS A C   
312  O O   . LYS A 42  ? 2.13523 2.09629 2.11811 0.48028  -0.54680 -0.25591 78  LYS A O   
313  C CB  . LYS A 42  ? 1.70996 1.90119 1.82527 0.52532  -0.51371 -0.37499 78  LYS A CB  
314  C CG  . LYS A 42  ? 1.61261 1.86184 1.74069 0.58709  -0.54665 -0.43965 78  LYS A CG  
315  C CD  . LYS A 42  ? 1.54381 1.86912 1.74596 0.58075  -0.52295 -0.46429 78  LYS A CD  
316  C CE  . LYS A 42  ? 1.45429 1.84670 1.66682 0.64485  -0.55458 -0.52660 78  LYS A CE  
317  N NZ  . LYS A 42  ? 1.37044 1.82630 1.63261 0.63019  -0.52033 -0.54113 78  LYS A NZ  
318  N N   . THR A 43  ? 2.06821 1.99774 2.11778 0.42857  -0.53101 -0.23282 79  THR A N   
319  C CA  . THR A 43  ? 2.27432 2.09403 2.27245 0.39414  -0.54547 -0.16661 79  THR A CA  
320  C C   . THR A 43  ? 2.46282 2.15754 2.40173 0.42615  -0.61883 -0.16252 79  THR A C   
321  O O   . THR A 43  ? 2.39676 2.09539 2.33738 0.47626  -0.65603 -0.21409 79  THR A O   
322  C CB  . THR A 43  ? 2.24044 2.06954 2.29271 0.32816  -0.50095 -0.12605 79  THR A CB  
323  O OG1 . THR A 43  ? 2.31074 2.05596 2.32188 0.28831  -0.50562 -0.05716 79  THR A OG1 
324  C CG2 . THR A 43  ? 2.31890 2.12790 2.40898 0.32958  -0.51878 -0.14484 79  THR A CG2 
325  N N   . GLU A 44  ? 2.57487 2.15881 2.46145 0.39710  -0.64105 -0.09936 80  GLU A N   
326  C CA  . GLU A 44  ? 2.61744 2.06268 2.44318 0.42344  -0.71805 -0.08852 80  GLU A CA  
327  C C   . GLU A 44  ? 2.74398 2.13711 2.60845 0.40781  -0.74301 -0.09079 80  GLU A C   
328  O O   . GLU A 44  ? 2.75285 2.04204 2.57757 0.44394  -0.81527 -0.10391 80  GLU A O   
329  C CB  . GLU A 44  ? 2.57612 1.91748 2.33300 0.39280  -0.73358 -0.01239 80  GLU A CB  
330  C CG  . GLU A 44  ? 2.59630 1.79926 2.26521 0.43937  -0.81853 -0.00835 80  GLU A CG  
331  C CD  . GLU A 44  ? 2.60505 1.84002 2.21598 0.50749  -0.83716 -0.05092 80  GLU A CD  
332  O OE1 . GLU A 44  ? 2.55526 1.90346 2.20617 0.54901  -0.82069 -0.12259 80  GLU A OE1 
333  O OE2 . GLU A 44  ? 2.63844 1.78665 2.16464 0.51876  -0.86881 -0.01082 80  GLU A OE2 
334  N N   . ALA A 45  ? 3.12239 2.58203 3.06094 0.35973  -0.69008 -0.08196 81  ALA A N   
335  C CA  . ALA A 45  ? 3.10875 2.52517 3.08657 0.34397  -0.71136 -0.08437 81  ALA A CA  
336  C C   . ALA A 45  ? 3.00872 2.55062 3.05998 0.34366  -0.65963 -0.12660 81  ALA A C   
337  O O   . ALA A 45  ? 2.95324 2.54533 3.05813 0.28969  -0.60575 -0.09984 81  ALA A O   
338  C CB  . ALA A 45  ? 3.14651 2.48540 3.13619 0.27194  -0.70741 -0.01029 81  ALA A CB  
339  N N   . PRO A 46  ? 2.55414 2.15225 2.60912 0.40414  -0.67449 -0.19150 82  PRO A N   
340  C CA  . PRO A 46  ? 2.28835 2.00070 2.40939 0.40480  -0.62822 -0.22678 82  PRO A CA  
341  C C   . PRO A 46  ? 2.10728 1.77196 2.24739 0.40463  -0.65611 -0.23256 82  PRO A C   
342  O O   . PRO A 46  ? 2.04150 1.64400 2.14731 0.45591  -0.72030 -0.26383 82  PRO A O   
343  C CB  . PRO A 46  ? 2.22196 2.01499 2.33441 0.47174  -0.63691 -0.28935 82  PRO A CB  
344  C CG  . PRO A 46  ? 2.30699 2.03420 2.35014 0.50369  -0.68223 -0.28747 82  PRO A CG  
345  C CD  . PRO A 46  ? 2.47757 2.05588 2.47685 0.47545  -0.72677 -0.23458 82  PRO A CD  
346  N N   . GLN A 47  ? 1.99257 1.68674 2.18631 0.35149  -0.61158 -0.20636 83  GLN A N   
347  C CA  . GLN A 47  ? 1.81846 1.47457 2.03480 0.34987  -0.63527 -0.21288 83  GLN A CA  
348  C C   . GLN A 47  ? 1.44206 1.19804 1.72009 0.32671  -0.57449 -0.21981 83  GLN A C   
349  O O   . GLN A 47  ? 1.32151 1.05350 1.61954 0.32491  -0.58976 -0.22503 83  GLN A O   
350  C CB  . GLN A 47  ? 1.83059 1.36531 2.04207 0.30159  -0.66945 -0.16047 83  GLN A CB  
351  C CG  . GLN A 47  ? 2.00015 1.40360 2.15039 0.33338  -0.75326 -0.15964 83  GLN A CG  
352  C CD  . GLN A 47  ? 2.04570 1.34399 2.18748 0.27221  -0.77097 -0.08997 83  GLN A CD  
353  O OE1 . GLN A 47  ? 2.07238 1.40460 2.25749 0.20713  -0.71931 -0.04435 83  GLN A OE1 
354  N NE2 . GLN A 47  ? 2.05728 1.22956 2.14330 0.29336  -0.84476 -0.08010 83  GLN A NE2 
355  N N   . LEU A 48  ? 1.15962 1.48305 1.96879 0.10728  -0.20317 0.01306  84  LEU A N   
356  C CA  . LEU A 48  ? 1.03744 1.34605 1.83082 0.09588  -0.17136 -0.00549 84  LEU A CA  
357  C C   . LEU A 48  ? 1.00236 1.31134 1.86911 0.10370  -0.12655 -0.00332 84  LEU A C   
358  O O   . LEU A 48  ? 0.92077 1.20207 1.75588 0.10178  -0.08668 -0.00887 84  LEU A O   
359  C CB  . LEU A 48  ? 0.91344 1.24613 1.71483 0.07413  -0.20214 -0.02381 84  LEU A CB  
360  C CG  . LEU A 48  ? 0.99642 1.31117 1.78200 0.06156  -0.17251 -0.04185 84  LEU A CG  
361  C CD1 . LEU A 48  ? 0.75034 1.02239 1.44212 0.06519  -0.14910 -0.04150 84  LEU A CD1 
362  C CD2 . LEU A 48  ? 0.89826 1.23321 1.68951 0.03946  -0.20340 -0.06407 84  LEU A CD2 
363  N N   . ARG A 49  ? 0.98046 1.32084 1.94641 0.11194  -0.13198 0.00617  85  ARG A N   
364  C CA  . ARG A 49  ? 0.97086 1.31273 2.01178 0.11878  -0.08428 0.00764  85  ARG A CA  
365  C C   . ARG A 49  ? 0.95799 1.25942 1.95290 0.13340  -0.03592 0.01255  85  ARG A C   
366  O O   . ARG A 49  ? 0.90625 1.19288 1.91382 0.13350  0.01315  0.00938  85  ARG A O   
367  C CB  . ARG A 49  ? 0.82755 1.19732 1.95746 0.12111  -0.09742 0.01687  85  ARG A CB  
368  C CG  . ARG A 49  ? 0.97691 1.35039 2.10317 0.13351  -0.12868 0.03359  85  ARG A CG  
369  C CD  . ARG A 49  ? 0.89379 1.28597 2.10571 0.13572  -0.13203 0.04382  85  ARG A CD  
370  N NE  . ARG A 49  ? 1.07929 1.48693 2.29308 0.13968  -0.18206 0.06073  85  ARG A NE  
371  C CZ  . ARG A 49  ? 1.06817 1.49541 2.35442 0.14149  -0.19846 0.07309  85  ARG A CZ  
372  N NH1 . ARG A 49  ? 0.85079 1.28438 2.21752 0.14001  -0.16833 0.06921  85  ARG A NH1 
373  N NH2 . ARG A 49  ? 1.23995 1.67982 2.51799 0.14431  -0.24602 0.09137  85  ARG A NH2 
374  N N   . ASP A 50  ? 0.98008 1.26212 1.91916 0.14417  -0.04848 0.01996  86  ASP A N   
375  C CA  . ASP A 50  ? 0.90306 1.14517 1.79558 0.15625  -0.00602 0.02081  86  ASP A CA  
376  C C   . ASP A 50  ? 0.92366 1.12734 1.70234 0.14716  0.00499  0.01260  86  ASP A C   
377  O O   . ASP A 50  ? 0.94874 1.12010 1.68779 0.15042  0.04681  0.00907  86  ASP A O   
378  C CB  . ASP A 50  ? 0.99366 1.23240 1.89721 0.17317  -0.02204 0.03340  86  ASP A CB  
379  C CG  . ASP A 50  ? 1.08777 1.35486 2.10484 0.18414  -0.02031 0.04324  86  ASP A CG  
380  O OD1 . ASP A 50  ? 1.08964 1.39077 2.15306 0.17471  -0.05730 0.04856  86  ASP A OD1 
381  O OD2 . ASP A 50  ? 1.06276 1.30809 2.09575 0.19484  0.01893  0.04307  86  ASP A OD2 
382  N N   . GLU A 51  ? 1.01596 1.22262 1.74219 0.13501  -0.03138 0.00884  87  GLU A N   
383  C CA  . GLU A 51  ? 0.94708 1.12073 1.57994 0.12628  -0.02153 0.00176  87  GLU A CA  
384  C C   . GLU A 51  ? 0.85574 1.02080 1.49271 0.11707  0.01246  -0.00356 87  GLU A C   
385  O O   . GLU A 51  ? 0.82363 0.95594 1.39578 0.11498  0.03623  -0.00411 87  GLU A O   
386  C CB  . GLU A 51  ? 0.92540 1.10610 1.51269 0.11469  -0.06311 -0.00328 87  GLU A CB  
387  C CG  . GLU A 51  ? 0.83531 0.98312 1.33543 0.10755  -0.05486 -0.00926 87  GLU A CG  
388  C CD  . GLU A 51  ? 0.89772 1.05074 1.35435 0.09677  -0.08976 -0.01609 87  GLU A CD  
389  O OE1 . GLU A 51  ? 0.99198 1.17396 1.48187 0.08731  -0.11579 -0.02298 87  GLU A OE1 
390  O OE2 . GLU A 51  ? 0.86957 0.99757 1.25878 0.09653  -0.09012 -0.01602 87  GLU A OE2 
391  N N   . TYR A 52  ? 0.78052 0.97469 1.49457 0.11060  0.01338  -0.00564 88  TYR A N   
392  C CA  . TYR A 52  ? 0.86734 1.05339 1.59661 0.10253  0.05003  -0.00613 88  TYR A CA  
393  C C   . TYR A 52  ? 0.87866 1.03977 1.59460 0.11195  0.09921  -0.00001 88  TYR A C   
394  O O   . TYR A 52  ? 0.75081 0.88121 1.40429 0.10686  0.12559  0.00243  88  TYR A O   
395  C CB  . TYR A 52  ? 0.90427 1.12814 1.73399 0.09485  0.04395  -0.00905 88  TYR A CB  
396  C CG  . TYR A 52  ? 0.95807 1.17730 1.82612 0.08818  0.08790  -0.00523 88  TYR A CG  
397  C CD1 . TYR A 52  ? 0.82011 1.00608 1.62327 0.08112  0.11376  -0.00075 88  TYR A CD1 
398  C CD2 . TYR A 52  ? 0.86228 1.11210 1.83653 0.08795  0.10164  -0.00372 88  TYR A CD2 
399  C CE1 . TYR A 52  ? 0.86993 1.05063 1.70556 0.07399  0.15408  0.00742  88  TYR A CE1 
400  C CE2 . TYR A 52  ? 0.89709 1.14246 1.90858 0.08076  0.14466  0.00178  88  TYR A CE2 
401  C CZ  . TYR A 52  ? 1.02462 1.23450 1.96359 0.07361  0.17135  0.00834  88  TYR A CZ  
402  O OH  . TYR A 52  ? 1.19125 1.39568 2.16499 0.06553  0.21458  0.01822  88  TYR A OH  
403  N N   . ARG A 53  ? 0.90318 1.07669 1.67758 0.12512  0.11192  0.00232  89  ARG A N   
404  C CA  . ARG A 53  ? 0.87093 1.02123 1.63926 0.13279  0.16480  0.00324  89  ARG A CA  
405  C C   . ARG A 53  ? 0.81226 0.91955 1.47334 0.13537  0.17453  0.00051  89  ARG A C   
406  O O   . ARG A 53  ? 1.00531 1.08468 1.62690 0.13461  0.21821  -0.00127 89  ARG A O   
407  C CB  . ARG A 53  ? 0.83561 1.00777 1.69716 0.14789  0.17518  0.00425  89  ARG A CB  
408  C CG  . ARG A 53  ? 1.10909 1.26235 1.98490 0.15362  0.23863  0.00106  89  ARG A CG  
409  C CD  . ARG A 53  ? 1.13456 1.31466 2.12580 0.16613  0.25171  0.00213  89  ARG A CD  
410  N NE  . ARG A 53  ? 1.23403 1.38982 2.22272 0.16540  0.31448  -0.00358 89  ARG A NE  
411  C CZ  . ARG A 53  ? 1.11551 1.27571 2.16842 0.16826  0.33209  -0.00408 89  ARG A CZ  
412  N NH1 . ARG A 53  ? 1.07930 1.26788 2.20685 0.17276  0.29133  0.00326  89  ARG A NH1 
413  N NH2 . ARG A 53  ? 1.14072 1.27509 2.18085 0.16572  0.39235  -0.01172 89  ARG A NH2 
414  N N   . THR A 54  ? 0.73649 0.83762 1.34757 0.13668  0.13489  -0.00034 90  THR A N   
415  C CA  . THR A 54  ? 0.93573 0.99761 1.45020 0.13708  0.14047  -0.00347 90  THR A CA  
416  C C   . THR A 54  ? 1.00426 1.04569 1.45002 0.12267  0.14715  -0.00164 90  THR A C   
417  O O   . THR A 54  ? 0.96911 0.97741 1.34488 0.12023  0.16938  -0.00292 90  THR A O   
418  C CB  . THR A 54  ? 1.00269 1.06490 1.49103 0.14189  0.09833  -0.00285 90  THR A CB  
419  O OG1 . THR A 54  ? 0.85232 0.94135 1.41693 0.15358  0.08206  0.00170  90  THR A OG1 
420  C CG2 . THR A 54  ? 0.91762 0.94070 1.32962 0.14552  0.10927  -0.00735 90  THR A CG2 
421  N N   . TYR A 55  ? 0.83711 0.89737 1.30387 0.11234  0.12686  0.00135  91  TYR A N   
422  C CA  . TYR A 55  ? 0.96092 1.00279 1.37637 0.09967  0.13184  0.00646  91  TYR A CA  
423  C C   . TYR A 55  ? 1.00315 1.03352 1.42179 0.09468  0.17647  0.01452  91  TYR A C   
424  O O   . TYR A 55  ? 1.02159 1.02463 1.37370 0.08701  0.18888  0.02240  91  TYR A O   
425  C CB  . TYR A 55  ? 0.93024 0.99349 1.37605 0.09005  0.10109  0.00481  91  TYR A CB  
426  C CG  . TYR A 55  ? 0.86089 0.92412 1.26988 0.08967  0.06211  -0.00211 91  TYR A CG  
427  C CD1 . TYR A 55  ? 0.91910 0.95446 1.25330 0.08727  0.05683  -0.00041 91  TYR A CD1 
428  C CD2 . TYR A 55  ? 0.82183 0.91351 1.27060 0.09027  0.03061  -0.00964 91  TYR A CD2 
429  C CE1 . TYR A 55  ? 0.81604 0.85139 1.12085 0.08623  0.02632  -0.00666 91  TYR A CE1 
430  C CE2 . TYR A 55  ? 0.91087 1.00108 1.31963 0.08823  -0.00054 -0.01540 91  TYR A CE2 
431  C CZ  . TYR A 55  ? 0.83774 0.89953 1.17700 0.08655  -0.00002 -0.01421 91  TYR A CZ  
432  O OH  . TYR A 55  ? 0.70111 0.76154 1.00492 0.08392  -0.02619 -0.01991 91  TYR A OH  
433  N N   . LYS A 56  ? 1.05831 1.10968 1.55429 0.09802  0.20058  0.01451  92  LYS A N   
434  C CA  . LYS A 56  ? 1.19607 1.23512 1.69341 0.09302  0.25008  0.02245  92  LYS A CA  
435  C C   . LYS A 56  ? 1.25797 1.26422 1.68644 0.09775  0.28282  0.01797  92  LYS A C   
436  O O   . LYS A 56  ? 1.38621 1.36677 1.75702 0.08888  0.31522  0.02570  92  LYS A O   
437  C CB  . LYS A 56  ? 1.35113 1.42283 1.95876 0.09550  0.27001  0.02209  92  LYS A CB  
438  C CG  . LYS A 56  ? 1.23085 1.32916 1.90422 0.08498  0.25150  0.02676  92  LYS A CG  
439  C CD  . LYS A 56  ? 1.16993 1.24729 1.80760 0.07100  0.27405  0.04197  92  LYS A CD  
440  C CE  . LYS A 56  ? 1.17472 1.27722 1.89095 0.06035  0.25910  0.04429  92  LYS A CE  
441  N NZ  . LYS A 56  ? 1.21939 1.30128 1.91423 0.04719  0.28210  0.06335  92  LYS A NZ  
442  N N   . HIS A 57  ? 1.22731 1.23265 1.65966 0.11060  0.27492  0.00559  93  HIS A N   
443  C CA  . HIS A 57  ? 1.21071 1.18236 1.57928 0.11437  0.30499  -0.00411 93  HIS A CA  
444  C C   . HIS A 57  ? 1.15847 1.09644 1.41449 0.10408  0.29194  -0.00136 93  HIS A C   
445  O O   . HIS A 57  ? 1.28486 1.19305 1.47121 0.09642  0.32398  -0.00227 93  HIS A O   
446  C CB  . HIS A 57  ? 1.09628 1.07336 1.50110 0.13050  0.29318  -0.01624 93  HIS A CB  
447  C CG  . HIS A 57  ? 1.26636 1.21048 1.62900 0.13545  0.33082  -0.03125 93  HIS A CG  
448  N ND1 . HIS A 57  ? 1.32536 1.23921 1.61894 0.12496  0.37445  -0.03573 93  HIS A ND1 
449  C CD2 . HIS A 57  ? 1.29699 1.23203 1.67647 0.14872  0.33198  -0.04375 93  HIS A CD2 
450  C CE1 . HIS A 57  ? 1.40847 1.29567 1.67533 0.13065  0.40189  -0.05465 93  HIS A CE1 
451  N NE2 . HIS A 57  ? 1.45871 1.35769 1.78181 0.14581  0.37750  -0.05976 93  HIS A NE2 
452  N N   . LEU A 58  ? 1.11849 1.06148 1.35600 0.10259  0.24488  0.00205  94  LEU A N   
453  C CA  . LEU A 58  ? 1.14965 1.06598 1.29639 0.09321  0.22658  0.00633  94  LEU A CA  
454  C C   . LEU A 58  ? 1.11453 1.03141 1.24749 0.08007  0.22217  0.02461  94  LEU A C   
455  O O   . LEU A 58  ? 1.20941 1.11162 1.28696 0.07291  0.19790  0.03169  94  LEU A O   
456  C CB  . LEU A 58  ? 1.10360 1.02386 1.24232 0.09824  0.18239  0.00080  94  LEU A CB  
457  C CG  . LEU A 58  ? 1.04807 0.95937 1.18652 0.11009  0.18293  -0.01338 94  LEU A CG  
458  C CD1 . LEU A 58  ? 0.88860 0.81819 1.05578 0.11645  0.14160  -0.01344 94  LEU A CD1 
459  C CD2 . LEU A 58  ? 1.09901 0.97184 1.15003 0.10500  0.19241  -0.02159 94  LEU A CD2 
460  N N   . GLN A 59  ? 1.11774 1.05117 1.30713 0.07681  0.24505  0.03360  95  GLN A N   
461  C CA  . GLN A 59  ? 1.17777 1.10985 1.36313 0.06450  0.24317  0.05343  95  GLN A CA  
462  C C   . GLN A 59  ? 1.21389 1.11144 1.30637 0.05391  0.26317  0.06717  95  GLN A C   
463  O O   . GLN A 59  ? 1.12190 1.00301 1.17902 0.05298  0.30137  0.06265  95  GLN A O   
464  C CB  . GLN A 59  ? 1.01525 0.97210 1.28876 0.06263  0.26610  0.05959  95  GLN A CB  
465  C CG  . GLN A 59  ? 1.06076 1.01573 1.34377 0.05001  0.26558  0.08132  95  GLN A CG  
466  C CD  . GLN A 59  ? 1.03964 1.02638 1.42954 0.04836  0.26826  0.08106  95  GLN A CD  
467  O OE1 . GLN A 59  ? 0.99433 1.00059 1.42963 0.04833  0.23353  0.07281  95  GLN A OE1 
468  N NE2 . GLN A 59  ? 0.90956 0.90134 1.34047 0.04550  0.31090  0.08841  95  GLN A NE2 
469  N N   . GLY A 60  ? 1.11223 0.99866 1.16543 0.04525  0.23699  0.08368  96  GLY A N   
470  C CA  . GLY A 60  ? 1.25574 1.11067 1.21492 0.03409  0.24283  0.09972  96  GLY A CA  
471  C C   . GLY A 60  ? 1.33008 1.16654 1.21800 0.03441  0.21355  0.08964  96  GLY A C   
472  O O   . GLY A 60  ? 1.30991 1.12290 1.12126 0.02352  0.20570  0.10455  96  GLY A O   
473  N N   . CYS A 61  ? 1.17755 1.02415 1.08984 0.04557  0.19584  0.06671  97  CYS A N   
474  C CA  . CYS A 61  ? 1.33834 1.16829 1.19341 0.04566  0.16874  0.05635  97  CYS A CA  
475  C C   . CYS A 61  ? 1.27942 1.11681 1.14637 0.04304  0.12663  0.06727  97  CYS A C   
476  O O   . CYS A 61  ? 1.13357 0.99427 1.06856 0.04665  0.11486  0.06959  97  CYS A O   
477  C CB  . CYS A 61  ? 1.34515 1.18097 1.22549 0.05855  0.16946  0.03071  97  CYS A CB  
478  S SG  . CYS A 61  ? 1.43640 1.26133 1.31387 0.06364  0.22155  0.01367  97  CYS A SG  
479  N N   . ASP A 62  ? 1.32042 1.13793 1.12362 0.03579  0.10450  0.07224  98  ASP A N   
480  C CA  . ASP A 62  ? 1.29854 1.12249 1.11883 0.03359  0.06694  0.08225  98  ASP A CA  
481  C C   . ASP A 62  ? 1.18997 1.02938 1.05143 0.04337  0.04811  0.06204  98  ASP A C   
482  O O   . ASP A 62  ? 1.22062 1.05387 1.06389 0.04895  0.05095  0.04362  98  ASP A O   
483  C CB  . ASP A 62  ? 1.41389 1.21495 1.16220 0.02252  0.04553  0.09499  98  ASP A CB  
484  C CG  . ASP A 62  ? 1.72872 1.50800 1.40774 0.02021  0.05002  0.07555  98  ASP A CG  
485  O OD1 . ASP A 62  ? 1.62884 1.41005 1.32196 0.02928  0.06760  0.05203  98  ASP A OD1 
486  O OD2 . ASP A 62  ? 1.73985 1.49939 1.35200 0.00854  0.03423  0.08394  98  ASP A OD2 
487  N N   . GLY A 63  ? 1.00131 0.85962 0.91921 0.04474  0.03119  0.06559  99  GLY A N   
488  C CA  . GLY A 63  ? 0.98481 0.85823 0.93708 0.05132  0.01413  0.04885  99  GLY A CA  
489  C C   . GLY A 63  ? 0.91388 0.80974 0.91816 0.05912  0.02489  0.03587  99  GLY A C   
490  O O   . GLY A 63  ? 0.81530 0.72587 0.84740 0.06245  0.00927  0.02457  99  GLY A O   
491  N N   . ILE A 64  ? 0.92102 0.82052 0.93911 0.06119  0.05065  0.03761  100 ILE A N   
492  C CA  . ILE A 64  ? 0.82382 0.74805 0.90173 0.06785  0.05835  0.02773  100 ILE A CA  
493  C C   . ILE A 64  ? 0.92545 0.86503 1.05599 0.06186  0.06405  0.03630  100 ILE A C   
494  O O   . ILE A 64  ? 0.79041 0.71939 0.91162 0.05625  0.08376  0.05180  100 ILE A O   
495  C CB  . ILE A 64  ? 0.96691 0.88739 1.04234 0.07488  0.08557  0.02232  100 ILE A CB  
496  C CG1 . ILE A 64  ? 0.90916 0.80643 0.92761 0.07861  0.08434  0.01383  100 ILE A CG1 
497  C CG2 . ILE A 64  ? 0.84052 0.78978 0.98535 0.08298  0.08490  0.01334  100 ILE A CG2 
498  C CD1 . ILE A 64  ? 0.94894 0.85242 0.97334 0.08415  0.05696  0.00459  100 ILE A CD1 
499  N N   . PRO A 65  ? 0.75972 0.72222 0.94293 0.06131  0.04820  0.02674  101 PRO A N   
500  C CA  . PRO A 65  ? 0.92057 0.89591 1.15993 0.05424  0.05384  0.03160  101 PRO A CA  
501  C C   . PRO A 65  ? 0.96129 0.94921 1.24355 0.05566  0.07944  0.03427  101 PRO A C   
502  O O   . PRO A 65  ? 0.84213 0.83514 1.12450 0.06354  0.08991  0.02841  101 PRO A O   
503  C CB  . PRO A 65  ? 0.86928 0.86502 1.14551 0.05228  0.02952  0.01338  101 PRO A CB  
504  C CG  . PRO A 65  ? 0.74280 0.74475 0.99647 0.06043  0.01730  0.00183  101 PRO A CG  
505  C CD  . PRO A 65  ? 0.60867 0.58486 0.79927 0.06535  0.02477  0.01060  101 PRO A CD  
506  N N   . ASN A 66  ? 0.92040 0.91311 1.24752 0.04788  0.09108  0.04381  102 ASN A N   
507  C CA  . ASN A 66  ? 0.71272 0.71870 1.09254 0.04704  0.11789  0.04785  102 ASN A CA  
508  C C   . ASN A 66  ? 0.82215 0.86169 1.27752 0.04733  0.10325  0.02895  102 ASN A C   
509  O O   . ASN A 66  ? 0.69226 0.74233 1.16501 0.04298  0.07648  0.01542  102 ASN A O   
510  C CB  . ASN A 66  ? 0.82690 0.82179 1.22465 0.03713  0.13782  0.06951  102 ASN A CB  
511  C CG  . ASN A 66  ? 0.94681 0.90989 1.26628 0.03488  0.15227  0.09245  102 ASN A CG  
512  O OD1 . ASN A 66  ? 0.95505 0.90573 1.21617 0.04001  0.16208  0.09025  102 ASN A OD1 
513  N ND2 . ASN A 66  ? 0.87128 0.82025 1.19003 0.02632  0.15244  0.11477  102 ASN A ND2 
514  N N   . ALA A 67  ? 0.96449 1.02111 1.46534 0.05155  0.12128  0.02727  103 ALA A N   
515  C CA  . ALA A 67  ? 0.85213 0.94376 1.43435 0.05018  0.10705  0.01277  103 ALA A CA  
516  C C   . ALA A 67  ? 0.92457 1.02582 1.57865 0.04050  0.12963  0.02015  103 ALA A C   
517  O O   . ALA A 67  ? 1.02241 1.11187 1.67685 0.04057  0.16692  0.03679  103 ALA A O   
518  C CB  . ALA A 67  ? 0.93162 1.03978 1.53369 0.06210  0.10839  0.00743  103 ALA A CB  
519  N N   . TYR A 68  ? 0.78189 0.90314 1.49530 0.03076  0.10886  0.00681  104 TYR A N   
520  C CA  . TYR A 68  ? 0.77298 0.89980 1.55791 0.01930  0.12786  0.01300  104 TYR A CA  
521  C C   . TYR A 68  ? 0.78746 0.95188 1.67118 0.01491  0.12217  -0.00061 104 TYR A C   
522  O O   . TYR A 68  ? 0.89009 1.06027 1.84035 0.00788  0.14885  0.00867  104 TYR A O   
523  C CB  . TYR A 68  ? 0.72688 0.84117 1.51191 0.00837  0.11318  0.00837  104 TYR A CB  
524  C CG  . TYR A 68  ? 0.85240 0.93118 1.55930 0.01084  0.11938  0.02706  104 TYR A CG  
525  C CD1 . TYR A 68  ? 0.86099 0.91670 1.54648 0.01008  0.15169  0.05701  104 TYR A CD1 
526  C CD2 . TYR A 68  ? 0.80889 0.87805 1.46448 0.01268  0.09230  0.01583  104 TYR A CD2 
527  C CE1 . TYR A 68  ? 0.85387 0.87922 1.46858 0.01103  0.15135  0.07623  104 TYR A CE1 
528  C CE2 . TYR A 68  ? 0.82058 0.86037 1.41487 0.01457  0.09459  0.03370  104 TYR A CE2 
529  C CZ  . TYR A 68  ? 0.85673 0.87540 1.43091 0.01368  0.12135  0.06432  104 TYR A CZ  
530  O OH  . TYR A 68  ? 0.84573 0.83718 1.35925 0.01434  0.11785  0.08417  104 TYR A OH  
531  N N   . TYR A 69  ? 0.66318 0.85379 1.56027 0.01783  0.08717  -0.02029 105 TYR A N   
532  C CA  . TYR A 69  ? 0.90741 1.13685 1.90179 0.01176  0.07374  -0.03309 105 TYR A CA  
533  C C   . TYR A 69  ? 0.89735 1.15168 1.88743 0.02055  0.03916  -0.04323 105 TYR A C   
534  O O   . TYR A 69  ? 0.88261 1.12636 1.79798 0.02544  0.01517  -0.04845 105 TYR A O   
535  C CB  . TYR A 69  ? 0.80462 1.04381 1.84701 -0.00650 0.05388  -0.05249 105 TYR A CB  
536  C CG  . TYR A 69  ? 0.82066 1.10217 1.94165 -0.01500 0.02075  -0.07380 105 TYR A CG  
537  C CD1 . TYR A 69  ? 0.86610 1.16708 2.07691 -0.01869 0.03489  -0.06941 105 TYR A CD1 
538  C CD2 . TYR A 69  ? 0.78772 1.08360 1.87879 -0.02023 -0.02569 -0.09708 105 TYR A CD2 
539  C CE1 . TYR A 69  ? 0.89592 1.22093 2.14855 -0.02605 -0.00015 -0.08649 105 TYR A CE1 
540  C CE2 . TYR A 69  ? 0.86057 1.19538 2.01546 -0.02997 -0.06114 -0.11530 105 TYR A CE2 
541  C CZ  . TYR A 69  ? 0.92855 1.27099 2.15105 -0.03174 -0.04896 -0.10863 105 TYR A CZ  
542  O OH  . TYR A 69  ? 1.13104 1.49848 2.38888 -0.04018 -0.08580 -0.12356 105 TYR A OH  
543  N N   . PHE A 70  ? 0.83530 1.12330 1.91206 0.02229  0.03709  -0.04347 106 PHE A N   
544  C CA  . PHE A 70  ? 0.88579 1.20497 1.98276 0.02780  -0.00353 -0.05098 106 PHE A CA  
545  C C   . PHE A 70  ? 0.88098 1.23292 2.08218 0.02066  -0.01112 -0.05458 106 PHE A C   
546  O O   . PHE A 70  ? 0.98785 1.33233 2.23142 0.02337  0.02752  -0.04213 106 PHE A O   
547  C CB  . PHE A 70  ? 0.94160 1.24979 1.99599 0.04817  0.00689  -0.03619 106 PHE A CB  
548  C CG  . PHE A 70  ? 0.98257 1.32373 2.07453 0.05573  -0.03218 -0.03663 106 PHE A CG  
549  C CD1 . PHE A 70  ? 1.00248 1.36431 2.08288 0.04552  -0.08586 -0.05005 106 PHE A CD1 
550  C CD2 . PHE A 70  ? 0.94621 1.29647 2.08400 0.07256  -0.01476 -0.02291 106 PHE A CD2 
551  C CE1 . PHE A 70  ? 1.04773 1.44005 2.15913 0.05153  -0.12592 -0.04532 106 PHE A CE1 
552  C CE2 . PHE A 70  ? 0.83546 1.20686 1.99593 0.07858  -0.05249 -0.01844 106 PHE A CE2 
553  C CZ  . PHE A 70  ? 0.82807 1.22097 1.97384 0.06829  -0.10941 -0.02726 106 PHE A CZ  
554  N N   . GLY A 71  ? 1.07506 1.44973 2.28939 0.00977  -0.06017 -0.07112 107 GLY A N   
555  C CA  . GLY A 71  ? 1.34190 1.73609 2.62792 0.00191  -0.07391 -0.07466 107 GLY A CA  
556  C C   . GLY A 71  ? 1.64171 2.06193 2.91872 -0.00815 -0.13420 -0.09113 107 GLY A C   
557  O O   . GLY A 71  ? 1.43773 1.85832 2.64952 -0.01114 -0.16281 -0.10138 107 GLY A O   
558  N N   . GLN A 72  ? 2.54193 2.98361 3.88320 -0.01428 -0.15289 -0.09310 108 GLN A N   
559  C CA  . GLN A 72  ? 2.52405 2.99247 3.85806 -0.02651 -0.21073 -0.10757 108 GLN A CA  
560  C C   . GLN A 72  ? 2.50412 2.96873 3.83192 -0.04925 -0.22193 -0.13680 108 GLN A C   
561  O O   . GLN A 72  ? 2.48957 2.93923 3.86139 -0.05550 -0.18933 -0.14201 108 GLN A O   
562  C CB  . GLN A 72  ? 2.46475 2.95949 3.87396 -0.02376 -0.22847 -0.09659 108 GLN A CB  
563  C CG  . GLN A 72  ? 2.53735 3.03171 3.97045 -0.00130 -0.20890 -0.06908 108 GLN A CG  
564  C CD  . GLN A 72  ? 2.76091 3.28143 4.27521 0.00053  -0.22892 -0.05898 108 GLN A CD  
565  O OE1 . GLN A 72  ? 2.71025 3.25660 4.23931 -0.01293 -0.27621 -0.06867 108 GLN A OE1 
566  N NE2 . GLN A 72  ? 2.80223 3.31578 4.36924 0.01616  -0.19223 -0.04033 108 GLN A NE2 
567  N N   . GLU A 73  ? 1.89487 2.37028 3.16464 -0.06217 -0.26633 -0.15586 109 GLU A N   
568  C CA  . GLU A 73  ? 1.80018 2.27059 3.05779 -0.08513 -0.27773 -0.18843 109 GLU A CA  
569  C C   . GLU A 73  ? 1.79215 2.28722 3.00101 -0.09977 -0.33512 -0.20349 109 GLU A C   
570  O O   . GLU A 73  ? 1.72052 2.21064 2.84506 -0.10113 -0.35341 -0.20812 109 GLU A O   
571  C CB  . GLU A 73  ? 1.69038 2.12778 2.89774 -0.08738 -0.24857 -0.20065 109 GLU A CB  
572  C CG  . GLU A 73  ? 1.59675 2.02011 2.81380 -0.10767 -0.24332 -0.23191 109 GLU A CG  
573  C CD  . GLU A 73  ? 1.32471 1.71235 2.54772 -0.10372 -0.19454 -0.22910 109 GLU A CD  
574  O OE1 . GLU A 73  ? 1.17794 1.55384 2.39328 -0.08703 -0.16580 -0.20299 109 GLU A OE1 
575  O OE2 . GLU A 73  ? 1.30176 1.67261 2.53720 -0.11733 -0.18484 -0.25176 109 GLU A OE2 
576  N N   . GLY A 74  ? 2.11330 2.63432 3.37300 -0.11167 -0.36272 -0.21000 110 GLY A N   
577  C CA  . GLY A 74  ? 2.18958 2.73845 3.40624 -0.12685 -0.41906 -0.21889 110 GLY A CA  
578  C C   . GLY A 74  ? 2.18111 2.74721 3.37138 -0.11046 -0.44448 -0.18751 110 GLY A C   
579  O O   . GLY A 74  ? 2.24448 2.82388 3.50313 -0.09397 -0.43962 -0.16105 110 GLY A O   
580  N N   . LEU A 75  ? 1.62585 2.18914 2.71769 -0.11481 -0.46950 -0.18991 111 LEU A N   
581  C CA  . LEU A 75  ? 1.48108 2.05579 2.53597 -0.09935 -0.49402 -0.15886 111 LEU A CA  
582  C C   . LEU A 75  ? 1.50309 2.04772 2.49240 -0.08420 -0.46887 -0.15083 111 LEU A C   
583  O O   . LEU A 75  ? 1.49454 2.03769 2.40252 -0.08321 -0.49292 -0.14184 111 LEU A O   
584  C CB  . LEU A 75  ? 1.47726 2.07803 2.46881 -0.11875 -0.55087 -0.16314 111 LEU A CB  
585  C CG  . LEU A 75  ? 1.52221 2.15843 2.57510 -0.13493 -0.58430 -0.16940 111 LEU A CG  
586  C CD1 . LEU A 75  ? 1.39116 2.05244 2.36309 -0.15759 -0.63921 -0.17576 111 LEU A CD1 
587  C CD2 . LEU A 75  ? 1.23590 1.89017 2.39084 -0.11286 -0.58211 -0.13647 111 LEU A CD2 
588  N N   . HIS A 76  ? 1.51503 2.03477 2.53689 -0.07332 -0.41967 -0.15342 112 HIS A N   
589  C CA  . HIS A 76  ? 1.39448 1.88615 2.36042 -0.06056 -0.39410 -0.14879 112 HIS A CA  
590  C C   . HIS A 76  ? 1.32153 1.79900 2.34989 -0.03936 -0.34442 -0.13036 112 HIS A C   
591  O O   . HIS A 76  ? 1.40468 1.88512 2.51025 -0.04013 -0.32040 -0.13090 112 HIS A O   
592  C CB  . HIS A 76  ? 1.28374 1.75276 2.19063 -0.07843 -0.38405 -0.18315 112 HIS A CB  
593  C CG  . HIS A 76  ? 1.30652 1.77286 2.10894 -0.09059 -0.41706 -0.19475 112 HIS A CG  
594  N ND1 . HIS A 76  ? 1.43213 1.89252 2.17322 -0.07641 -0.42836 -0.17252 112 HIS A ND1 
595  C CD2 . HIS A 76  ? 1.23995 1.70559 1.98430 -0.11642 -0.43727 -0.22622 112 HIS A CD2 
596  C CE1 . HIS A 76  ? 1.51475 1.97119 2.16248 -0.09314 -0.45391 -0.18792 112 HIS A CE1 
597  N NE2 . HIS A 76  ? 1.43452 1.89434 2.08054 -0.11812 -0.45871 -0.22165 112 HIS A NE2 
598  N N   . ASN A 77  ? 1.31105 1.77123 2.29760 -0.02181 -0.32880 -0.11465 113 ASN A N   
599  C CA  . ASN A 77  ? 1.25277 1.69495 2.27719 -0.00309 -0.27711 -0.09929 113 ASN A CA  
600  C C   . ASN A 77  ? 1.23768 1.64454 2.19223 -0.00778 -0.25005 -0.11364 113 ASN A C   
601  O O   . ASN A 77  ? 1.27714 1.67002 2.14170 -0.01310 -0.26933 -0.12202 113 ASN A O   
602  C CB  . ASN A 77  ? 1.23193 1.67266 2.25574 0.02146  -0.27247 -0.06923 113 ASN A CB  
603  C CG  . ASN A 77  ? 1.22587 1.68769 2.32049 0.02772  -0.28151 -0.05244 113 ASN A CG  
604  O OD1 . ASN A 77  ? 1.20584 1.69011 2.33097 0.01285  -0.31112 -0.06117 113 ASN A OD1 
605  N ND2 . ASN A 77  ? 1.21020 1.66385 2.33266 0.04912  -0.25512 -0.03004 113 ASN A ND2 
606  N N   . ILE A 78  ? 1.13154 1.51836 2.11444 -0.00624 -0.20405 -0.11336 114 ILE A N   
607  C CA  . ILE A 78  ? 1.00672 1.35604 1.92730 -0.01181 -0.17759 -0.12386 114 ILE A CA  
608  C C   . ILE A 78  ? 0.90846 1.22632 1.81055 0.00530  -0.12944 -0.10091 114 ILE A C   
609  O O   . ILE A 78  ? 0.82401 1.14828 1.79149 0.01208  -0.10186 -0.08727 114 ILE A O   
610  C CB  . ILE A 78  ? 1.00515 1.35934 1.97806 -0.03277 -0.17415 -0.14855 114 ILE A CB  
611  C CG1 . ILE A 78  ? 1.10266 1.47396 2.05132 -0.05301 -0.21927 -0.17930 114 ILE A CG1 
612  C CG2 . ILE A 78  ? 0.95235 1.26725 1.89564 -0.03278 -0.13386 -0.14742 114 ILE A CG2 
613  C CD1 . ILE A 78  ? 1.01622 1.42608 2.01783 -0.06036 -0.25742 -0.18230 114 ILE A CD1 
614  N N   . LEU A 79  ? 0.98048 1.26482 1.79292 0.01090  -0.11915 -0.09741 115 LEU A N   
615  C CA  . LEU A 79  ? 0.88274 1.13414 1.66109 0.02386  -0.07855 -0.07817 115 LEU A CA  
616  C C   . LEU A 79  ? 0.82885 1.04998 1.55965 0.01587  -0.06524 -0.08507 115 LEU A C   
617  O O   . LEU A 79  ? 0.87035 1.08198 1.54244 0.01167  -0.08377 -0.09688 115 LEU A O   
618  C CB  . LEU A 79  ? 0.66444 0.90421 1.38515 0.04087  -0.08090 -0.06321 115 LEU A CB  
619  C CG  . LEU A 79  ? 0.72331 0.92521 1.38666 0.05112  -0.04583 -0.04872 115 LEU A CG  
620  C CD1 . LEU A 79  ? 0.65211 0.85025 1.36251 0.05598  -0.00583 -0.03567 115 LEU A CD1 
621  C CD2 . LEU A 79  ? 0.71328 0.90287 1.31824 0.06463  -0.05433 -0.04006 115 LEU A CD2 
622  N N   . VAL A 80  ? 0.82987 1.03569 1.58856 0.01385  -0.03212 -0.07563 116 VAL A N   
623  C CA  . VAL A 80  ? 0.70770 0.88505 1.43613 0.00741  -0.01889 -0.07654 116 VAL A CA  
624  C C   . VAL A 80  ? 0.80295 0.94918 1.46965 0.01968  0.00567  -0.05260 116 VAL A C   
625  O O   . VAL A 80  ? 0.72616 0.86796 1.40522 0.02664  0.03231  -0.03422 116 VAL A O   
626  C CB  . VAL A 80  ? 0.60082 0.78056 1.40418 -0.00519 -0.00213 -0.07923 116 VAL A CB  
627  C CG1 . VAL A 80  ? 0.66749 0.81570 1.44630 -0.00950 0.01231  -0.07410 116 VAL A CG1 
628  C CG2 . VAL A 80  ? 0.56944 0.77923 1.43227 -0.02016 -0.02946 -0.10810 116 VAL A CG2 
629  N N   . ILE A 81  ? 0.74928 0.87431 1.34928 0.02117  -0.00275 -0.05426 117 ILE A N   
630  C CA  . ILE A 81  ? 0.63832 0.73323 1.17761 0.02956  0.01452  -0.03408 117 ILE A CA  
631  C C   . ILE A 81  ? 0.70259 0.77693 1.22270 0.02280  0.01268  -0.03496 117 ILE A C   
632  O O   . ILE A 81  ? 0.61136 0.69303 1.16804 0.01238  0.00329  -0.05261 117 ILE A O   
633  C CB  . ILE A 81  ? 0.52615 0.61616 1.00461 0.04126  0.00430  -0.03207 117 ILE A CB  
634  C CG1 . ILE A 81  ? 0.72017 0.81648 1.17031 0.03785  -0.02528 -0.05017 117 ILE A CG1 
635  C CG2 . ILE A 81  ? 0.78500 0.89268 1.29231 0.05007  0.00991  -0.02804 117 ILE A CG2 
636  C CD1 . ILE A 81  ? 0.76939 0.84731 1.14921 0.04649  -0.03075 -0.04414 117 ILE A CD1 
637  N N   . ASP A 82  ? 0.60842 0.65678 1.07403 0.02836  0.02143  -0.01679 118 ASP A N   
638  C CA  . ASP A 82  ? 0.78092 0.80998 1.23445 0.02376  0.01866  -0.01268 118 ASP A CA  
639  C C   . ASP A 82  ? 0.69765 0.73063 1.13204 0.02159  -0.00291 -0.03558 118 ASP A C   
640  O O   . ASP A 82  ? 0.70798 0.74986 1.10851 0.02610  -0.01607 -0.04567 118 ASP A O   
641  C CB  . ASP A 82  ? 0.52904 0.53199 0.92640 0.02928  0.02798  0.01353  118 ASP A CB  
642  C CG  . ASP A 82  ? 0.81036 0.80308 1.22286 0.02692  0.05220  0.03908  118 ASP A CG  
643  O OD1 . ASP A 82  ? 0.86979 0.86330 1.33808 0.01933  0.05916  0.04410  118 ASP A OD1 
644  O OD2 . ASP A 82  ? 0.86713 0.84946 1.23530 0.03171  0.06633  0.05368  118 ASP A OD2 
645  N N   . LEU A 83  ? 0.70893 0.73401 1.16808 0.01434  -0.00415 -0.04278 119 LEU A N   
646  C CA  . LEU A 83  ? 0.71092 0.73605 1.15293 0.01088  -0.01743 -0.06489 119 LEU A CA  
647  C C   . LEU A 83  ? 0.70023 0.70404 1.10012 0.01669  -0.01848 -0.04871 119 LEU A C   
648  O O   . LEU A 83  ? 0.71888 0.70653 1.13177 0.01745  -0.01110 -0.02670 119 LEU A O   
649  C CB  . LEU A 83  ? 0.64269 0.67099 1.14395 -0.00098 -0.01476 -0.08727 119 LEU A CB  
650  C CG  . LEU A 83  ? 0.68897 0.71439 1.17871 -0.00664 -0.02059 -0.11334 119 LEU A CG  
651  C CD1 . LEU A 83  ? 0.58119 0.62483 1.03100 -0.01031 -0.03571 -0.13754 119 LEU A CD1 
652  C CD2 . LEU A 83  ? 0.85890 0.88002 1.41635 -0.01749 -0.01065 -0.13245 119 LEU A CD2 
653  N N   . LEU A 84  ? 0.75459 0.75883 1.10650 0.01992  -0.02924 -0.05766 120 LEU A N   
654  C CA  . LEU A 84  ? 0.55394 0.54063 0.86723 0.02475  -0.03270 -0.04440 120 LEU A CA  
655  C C   . LEU A 84  ? 0.75763 0.74464 1.07161 0.01979  -0.03699 -0.06537 120 LEU A C   
656  O O   . LEU A 84  ? 0.68040 0.67975 1.01368 0.01205  -0.03661 -0.09154 120 LEU A O   
657  C CB  . LEU A 84  ? 0.70460 0.68762 0.96074 0.03328  -0.03712 -0.03339 120 LEU A CB  
658  C CG  . LEU A 84  ? 0.79948 0.77800 1.04893 0.03805  -0.02681 -0.01360 120 LEU A CG  
659  C CD1 . LEU A 84  ? 0.58477 0.56211 0.78890 0.04611  -0.02834 -0.01191 120 LEU A CD1 
660  C CD2 . LEU A 84  ? 0.72548 0.68404 0.96806 0.03715  -0.02205 0.01073  120 LEU A CD2 
661  N N   . GLY A 85  ? 0.65147 0.62474 0.94355 0.02299  -0.04027 -0.05480 121 GLY A N   
662  C CA  . GLY A 85  ? 0.72166 0.69334 1.02123 0.01856  -0.03919 -0.07170 121 GLY A CA  
663  C C   . GLY A 85  ? 0.66530 0.64232 0.91451 0.01853  -0.04416 -0.08448 121 GLY A C   
664  O O   . GLY A 85  ? 0.64625 0.63203 0.86372 0.02108  -0.05030 -0.08499 121 GLY A O   
665  N N   . PRO A 86  ? 0.67596 0.64777 0.92228 0.01565  -0.04071 -0.09295 122 PRO A N   
666  C CA  . PRO A 86  ? 0.68619 0.66162 0.88532 0.01374  -0.04246 -0.10365 122 PRO A CA  
667  C C   . PRO A 86  ? 0.71328 0.68204 0.86626 0.02240  -0.05310 -0.08303 122 PRO A C   
668  O O   . PRO A 86  ? 0.53078 0.48942 0.68309 0.02866  -0.05775 -0.06303 122 PRO A O   
669  C CB  . PRO A 86  ? 0.76433 0.73323 0.98290 0.00875  -0.03121 -0.11398 122 PRO A CB  
670  C CG  . PRO A 86  ? 0.84881 0.81498 1.13421 0.00665  -0.02293 -0.11726 122 PRO A CG  
671  C CD  . PRO A 86  ? 0.69301 0.65628 0.98738 0.01340  -0.03317 -0.09288 122 PRO A CD  
672  N N   . SER A 87  ? 0.45290 0.42609 0.56528 0.02159  -0.05650 -0.08846 123 SER A N   
673  C CA  . SER A 87  ? 0.71217 0.67736 0.78595 0.02944  -0.06457 -0.07179 123 SER A CA  
674  C C   . SER A 87  ? 0.80371 0.75426 0.86864 0.02912  -0.06251 -0.06541 123 SER A C   
675  O O   . SER A 87  ? 0.69370 0.64357 0.78027 0.02269  -0.05391 -0.07494 123 SER A O   
676  C CB  . SER A 87  ? 0.43502 0.41063 0.47581 0.02905  -0.07122 -0.07541 123 SER A CB  
677  O OG  . SER A 87  ? 0.83964 0.81741 0.86186 0.01990  -0.06598 -0.08799 123 SER A OG  
678  N N   . LEU A 88  ? 0.70641 0.64498 0.74485 0.03568  -0.06927 -0.05068 124 LEU A N   
679  C CA  . LEU A 88  ? 0.64286 0.56803 0.67382 0.03417  -0.06965 -0.04534 124 LEU A CA  
680  C C   . LEU A 88  ? 0.76674 0.69500 0.78254 0.02837  -0.06216 -0.05348 124 LEU A C   
681  O O   . LEU A 88  ? 0.73831 0.66012 0.76423 0.02369  -0.05624 -0.05427 124 LEU A O   
682  C CB  . LEU A 88  ? 0.43627 0.34613 0.44061 0.04079  -0.07767 -0.03210 124 LEU A CB  
683  C CG  . LEU A 88  ? 0.43625 0.33867 0.44335 0.04395  -0.08275 -0.02321 124 LEU A CG  
684  C CD1 . LEU A 88  ? 0.71502 0.59926 0.68980 0.04786  -0.08738 -0.01634 124 LEU A CD1 
685  C CD2 . LEU A 88  ? 0.43165 0.33297 0.47001 0.03856  -0.08658 -0.01956 124 LEU A CD2 
686  N N   . GLU A 89  ? 0.70016 0.63882 0.69216 0.02765  -0.06272 -0.05808 125 GLU A N   
687  C CA  . GLU A 89  ? 0.76409 0.70628 0.73291 0.01944  -0.05474 -0.06514 125 GLU A CA  
688  C C   . GLU A 89  ? 0.93361 0.88342 0.92540 0.00879  -0.03934 -0.08631 125 GLU A C   
689  O O   . GLU A 89  ? 0.93278 0.87942 0.91847 0.00075  -0.02448 -0.09326 125 GLU A O   
690  C CB  . GLU A 89  ? 0.86123 0.81385 0.79647 0.02041  -0.06483 -0.06160 125 GLU A CB  
691  C CG  . GLU A 89  ? 1.01375 0.96938 0.91097 0.01030  -0.05916 -0.06465 125 GLU A CG  
692  C CD  . GLU A 89  ? 0.95956 0.89911 0.83546 0.01239  -0.05658 -0.04630 125 GLU A CD  
693  O OE1 . GLU A 89  ? 0.93415 0.86037 0.82466 0.02189  -0.06147 -0.03374 125 GLU A OE1 
694  O OE2 . GLU A 89  ? 0.95140 0.89044 0.79417 0.00318  -0.04857 -0.04498 125 GLU A OE2 
695  N N   . ASP A 90  ? 0.87901 0.83760 0.90162 0.00820  -0.03960 -0.09746 126 ASP A N   
696  C CA  . ASP A 90  ? 0.84621 0.80947 0.90101 -0.00140 -0.02270 -0.12023 126 ASP A CA  
697  C C   . ASP A 90  ? 0.86619 0.81958 0.96408 -0.00088 -0.01248 -0.11701 126 ASP A C   
698  O O   . ASP A 90  ? 0.98856 0.94115 1.09953 -0.00899 0.00710  -0.13147 126 ASP A O   
699  C CB  . ASP A 90  ? 0.72973 0.70233 0.81632 -0.00169 -0.02608 -0.13069 126 ASP A CB  
700  C CG  . ASP A 90  ? 0.83988 0.82661 0.89452 -0.00569 -0.03606 -0.13947 126 ASP A CG  
701  O OD1 . ASP A 90  ? 0.95052 0.94149 0.96094 -0.01361 -0.03476 -0.14746 126 ASP A OD1 
702  O OD2 . ASP A 90  ? 0.75297 0.74718 0.82769 -0.00176 -0.04595 -0.13682 126 ASP A OD2 
703  N N   . LEU A 91  ? 0.73428 0.68061 0.85539 0.00771  -0.02552 -0.09797 127 LEU A N   
704  C CA  . LEU A 91  ? 0.79933 0.73834 0.96386 0.00805  -0.02343 -0.09062 127 LEU A CA  
705  C C   . LEU A 91  ? 0.87629 0.80864 1.02305 0.00528  -0.01844 -0.08644 127 LEU A C   
706  O O   . LEU A 91  ? 0.90397 0.83452 1.09361 0.00193  -0.00969 -0.08779 127 LEU A O   
707  C CB  . LEU A 91  ? 0.84617 0.77861 1.02364 0.01572  -0.04327 -0.06878 127 LEU A CB  
708  C CG  . LEU A 91  ? 0.83495 0.77200 1.03335 0.01827  -0.04668 -0.06750 127 LEU A CG  
709  C CD1 . LEU A 91  ? 0.76647 0.69505 0.95093 0.02462  -0.06454 -0.04378 127 LEU A CD1 
710  C CD2 . LEU A 91  ? 0.70838 0.64878 0.97457 0.01449  -0.03559 -0.07662 127 LEU A CD2 
711  N N   . PHE A 92  ? 0.79539 0.72412 0.88717 0.00670  -0.02352 -0.07988 128 PHE A N   
712  C CA  . PHE A 92  ? 0.83766 0.75821 0.91337 0.00330  -0.01714 -0.07407 128 PHE A CA  
713  C C   . PHE A 92  ? 0.86389 0.78948 0.94325 -0.00759 0.00958  -0.09139 128 PHE A C   
714  O O   . PHE A 92  ? 0.89742 0.81917 1.00605 -0.01240 0.02330  -0.09190 128 PHE A O   
715  C CB  . PHE A 92  ? 0.75531 0.66950 0.77661 0.00799  -0.02806 -0.06122 128 PHE A CB  
716  C CG  . PHE A 92  ? 0.89821 0.79944 0.90885 0.00606  -0.02529 -0.05005 128 PHE A CG  
717  C CD1 . PHE A 92  ? 0.88030 0.77109 0.91926 0.00745  -0.03410 -0.04193 128 PHE A CD1 
718  C CD2 . PHE A 92  ? 1.03855 0.93763 1.01062 0.00160  -0.01551 -0.04635 128 PHE A CD2 
719  C CE1 . PHE A 92  ? 0.91591 0.79419 0.95142 0.00438  -0.03160 -0.03331 128 PHE A CE1 
720  C CE2 . PHE A 92  ? 0.95601 0.84140 0.92336 -0.00064 -0.01122 -0.03406 128 PHE A CE2 
721  C CZ  . PHE A 92  ? 0.80922 0.68408 0.81152 0.00073  -0.01848 -0.02900 128 PHE A CZ  
722  N N   . ASP A 93  ? 0.78204 0.71653 0.83238 -0.01296 0.01809  -0.10715 129 ASP A N   
723  C CA  . ASP A 93  ? 0.98260 0.92043 1.02426 -0.02586 0.04645  -0.12776 129 ASP A CA  
724  C C   . ASP A 93  ? 1.00206 0.94164 1.11467 -0.02953 0.06732  -0.14506 129 ASP A C   
725  O O   . ASP A 93  ? 1.05427 0.99210 1.18063 -0.03845 0.09544  -0.15678 129 ASP A O   
726  C CB  . ASP A 93  ? 1.07002 1.01754 1.06410 -0.03254 0.04586  -0.14357 129 ASP A CB  
727  C CG  . ASP A 93  ? 1.29893 1.24534 1.22067 -0.03525 0.03746  -0.12940 129 ASP A CG  
728  O OD1 . ASP A 93  ? 1.40416 1.34493 1.29760 -0.04454 0.05679  -0.12894 129 ASP A OD1 
729  O OD2 . ASP A 93  ? 1.36835 1.31940 1.26566 -0.02803 0.01235  -0.11666 129 ASP A OD2 
730  N N   . TRP A 94  ? 0.90857 0.85116 1.07138 -0.02271 0.05558  -0.14521 130 TRP A N   
731  C CA  . TRP A 94  ? 0.96343 0.90796 1.20371 -0.02486 0.07340  -0.15984 130 TRP A CA  
732  C C   . TRP A 94  ? 0.91879 0.85947 1.21663 -0.02133 0.07210  -0.14398 130 TRP A C   
733  O O   . TRP A 94  ? 0.96160 0.90469 1.33072 -0.02401 0.09172  -0.15551 130 TRP A O   
734  C CB  . TRP A 94  ? 0.91007 0.85809 1.18636 -0.01908 0.05981  -0.16092 130 TRP A CB  
735  C CG  . TRP A 94  ? 1.23875 1.19271 1.47009 -0.02354 0.05860  -0.17770 130 TRP A CG  
736  C CD1 . TRP A 94  ? 1.37988 1.33746 1.54878 -0.03380 0.06949  -0.19537 130 TRP A CD1 
737  C CD2 . TRP A 94  ? 1.27731 1.23520 1.52391 -0.01924 0.04375  -0.17673 130 TRP A CD2 
738  N NE1 . TRP A 94  ? 1.46615 1.43138 1.61361 -0.03630 0.05902  -0.20678 130 TRP A NE1 
739  C CE2 . TRP A 94  ? 1.39331 1.35882 1.59118 -0.02729 0.04510  -0.19636 130 TRP A CE2 
740  C CE3 . TRP A 94  ? 1.17477 1.13050 1.47090 -0.01050 0.02910  -0.15941 130 TRP A CE3 
741  C CZ2 . TRP A 94  ? 1.34494 1.31710 1.55082 -0.02661 0.03318  -0.20122 130 TRP A CZ2 
742  C CZ3 . TRP A 94  ? 1.21072 1.17103 1.51031 -0.00970 0.02086  -0.16263 130 TRP A CZ3 
743  C CH2 . TRP A 94  ? 1.14777 1.11677 1.40683 -0.01757 0.02342  -0.18445 130 TRP A CH2 
744  N N   . CYS A 95  ? 0.73553 0.67047 1.00946 -0.01600 0.04936  -0.11925 131 CYS A N   
745  C CA  . CYS A 95  ? 0.82311 0.75525 1.14778 -0.01481 0.04301  -0.10448 131 CYS A CA  
746  C C   . CYS A 95  ? 0.89052 0.81885 1.19965 -0.02250 0.06309  -0.10604 131 CYS A C   
747  O O   . CYS A 95  ? 1.02331 0.94882 1.36705 -0.02263 0.05483  -0.09251 131 CYS A O   
748  C CB  . CYS A 95  ? 0.83739 0.76350 1.14789 -0.00670 0.00553  -0.07917 131 CYS A CB  
749  S SG  . CYS A 95  ? 0.78944 0.71830 1.12493 0.00113  -0.01703 -0.07006 131 CYS A SG  
750  N N   . GLY A 96  ? 0.83633 0.76442 1.09377 -0.03030 0.08832  -0.12122 132 GLY A N   
751  C CA  . GLY A 96  ? 0.90068 0.82343 1.13519 -0.03877 0.10998  -0.11928 132 GLY A CA  
752  C C   . GLY A 96  ? 0.99497 0.90799 1.15953 -0.03655 0.09224  -0.09905 132 GLY A C   
753  O O   . GLY A 96  ? 0.95402 0.85963 1.11326 -0.04186 0.10360  -0.08935 132 GLY A O   
754  N N   . ARG A 97  ? 0.95055 0.86294 1.06880 -0.02879 0.06652  -0.09195 133 ARG A N   
755  C CA  . ARG A 97  ? 0.88651 0.78928 0.94713 -0.02456 0.04911  -0.07266 133 ARG A CA  
756  C C   . ARG A 97  ? 0.98403 0.87498 1.07060 -0.02120 0.03516  -0.05536 133 ARG A C   
757  O O   . ARG A 97  ? 0.94329 0.82289 1.00356 -0.02324 0.03733  -0.04231 133 ARG A O   
758  C CB  . ARG A 97  ? 0.95988 0.86044 0.96104 -0.03360 0.06840  -0.07210 133 ARG A CB  
759  C CG  . ARG A 97  ? 1.08704 0.99889 1.05007 -0.03942 0.07693  -0.09081 133 ARG A CG  
760  C CD  . ARG A 97  ? 1.25358 1.16274 1.14090 -0.04729 0.08262  -0.08207 133 ARG A CD  
761  N NE  . ARG A 97  ? 1.17717 1.07823 1.03618 -0.03748 0.05609  -0.05428 133 ARG A NE  
762  C CZ  . ARG A 97  ? 1.20542 1.11188 1.04749 -0.02776 0.02868  -0.04819 133 ARG A CZ  
763  N NH1 . ARG A 97  ? 1.19081 1.11113 1.03907 -0.02707 0.02180  -0.06641 133 ARG A NH1 
764  N NH2 . ARG A 97  ? 1.22145 1.11866 1.04678 -0.01861 0.00964  -0.02379 133 ARG A NH2 
765  N N   . ARG A 98  ? 0.93550 0.82835 1.07390 -0.01699 0.01898  -0.05456 134 ARG A N   
766  C CA  . ARG A 98  ? 0.91806 0.80067 1.08087 -0.01592 0.00041  -0.04152 134 ARG A CA  
767  C C   . ARG A 98  ? 1.01694 0.90367 1.21542 -0.01078 -0.02481 -0.03925 134 ARG A C   
768  O O   . ARG A 98  ? 1.00360 0.90203 1.25169 -0.01166 -0.01933 -0.04617 134 ARG A O   
769  C CB  . ARG A 98  ? 0.92769 0.80962 1.13757 -0.02551 0.01955  -0.04171 134 ARG A CB  
770  C CG  . ARG A 98  ? 0.99722 0.86401 1.17786 -0.02956 0.02521  -0.03017 134 ARG A CG  
771  C CD  . ARG A 98  ? 1.10399 0.97191 1.33449 -0.04063 0.05121  -0.03113 134 ARG A CD  
772  N NE  . ARG A 98  ? 1.22803 1.07914 1.44708 -0.04475 0.05111  -0.01718 134 ARG A NE  
773  C CZ  . ARG A 98  ? 1.19694 1.03898 1.44850 -0.04549 0.02798  -0.01105 134 ARG A CZ  
774  N NH1 . ARG A 98  ? 1.04110 0.89017 1.33238 -0.04295 0.00060  -0.01511 134 ARG A NH1 
775  N NH2 . ARG A 98  ? 1.08809 0.91262 1.33103 -0.05000 0.03130  -0.00005 134 ARG A NH2 
776  N N   . PHE A 99  ? 0.81242 0.68822 0.98544 -0.00605 -0.05094 -0.02921 135 PHE A N   
777  C CA  . PHE A 99  ? 0.80162 0.67842 0.99378 -0.00314 -0.07713 -0.02330 135 PHE A CA  
778  C C   . PHE A 99  ? 0.89578 0.76481 1.11532 -0.00906 -0.09722 -0.01604 135 PHE A C   
779  O O   . PHE A 99  ? 0.89770 0.75402 1.09984 -0.01253 -0.09606 -0.01532 135 PHE A O   
780  C CB  . PHE A 99  ? 0.81599 0.68578 0.95264 0.00462  -0.09031 -0.01987 135 PHE A CB  
781  C CG  . PHE A 99  ? 0.98473 0.86604 1.11320 0.00963  -0.08065 -0.02543 135 PHE A CG  
782  C CD1 . PHE A 99  ? 0.71886 0.61379 0.88753 0.00668  -0.06355 -0.03496 135 PHE A CD1 
783  C CD2 . PHE A 99  ? 0.81767 0.69577 0.90352 0.01651  -0.08699 -0.02319 135 PHE A CD2 
784  C CE1 . PHE A 99  ? 0.87762 0.78184 1.04148 0.00951  -0.05542 -0.04317 135 PHE A CE1 
785  C CE2 . PHE A 99  ? 0.92466 0.81431 1.00964 0.01978  -0.07935 -0.02884 135 PHE A CE2 
786  C CZ  . PHE A 99  ? 0.85462 0.75689 0.97740 0.01578  -0.06487 -0.03932 135 PHE A CZ  
787  N N   . SER A 100 ? 0.78836 0.66480 1.05345 -0.01096 -0.11761 -0.00961 136 SER A N   
788  C CA  . SER A 100 ? 0.92063 0.79204 1.21201 -0.01843 -0.14371 -0.00263 136 SER A CA  
789  C C   . SER A 100 ? 0.85510 0.70783 1.08062 -0.01846 -0.16634 -0.00056 136 SER A C   
790  O O   . SER A 100 ? 0.82445 0.66977 0.99261 -0.01133 -0.16059 -0.00272 136 SER A O   
791  C CB  . SER A 100 ? 0.89545 0.78152 1.25485 -0.02058 -0.16414 0.00748  136 SER A CB  
792  O OG  . SER A 100 ? 0.64631 0.53142 0.97708 -0.01593 -0.18431 0.01733  136 SER A OG  
793  N N   . VAL A 101 ? 0.59973 0.44476 0.83708 -0.02759 -0.19136 0.00165  137 VAL A N   
794  C CA  . VAL A 101 ? 0.93590 0.75982 1.10986 -0.03015 -0.20919 -0.00201 137 VAL A CA  
795  C C   . VAL A 101 ? 0.87312 0.69622 1.00718 -0.02761 -0.22869 0.00535  137 VAL A C   
796  O O   . VAL A 101 ? 0.79833 0.60639 0.86739 -0.02385 -0.22518 0.00023  137 VAL A O   
797  C CB  . VAL A 101 ? 0.81897 0.63426 1.01674 -0.04350 -0.23188 -0.00519 137 VAL A CB  
798  C CG1 . VAL A 101 ? 0.67014 0.46067 0.79988 -0.04811 -0.24843 -0.01432 137 VAL A CG1 
799  C CG2 . VAL A 101 ? 0.89458 0.70889 1.13228 -0.04636 -0.20752 -0.01033 137 VAL A CG2 
800  N N   . LYS A 102 ? 0.87578 0.71467 1.05208 -0.02948 -0.24726 0.01903  138 LYS A N   
801  C CA  . LYS A 102 ? 0.86009 0.69710 0.99942 -0.02908 -0.26784 0.03138  138 LYS A CA  
802  C C   . LYS A 102 ? 0.92824 0.76552 1.03228 -0.01740 -0.24224 0.03027  138 LYS A C   
803  O O   . LYS A 102 ? 1.03933 0.86514 1.08236 -0.01648 -0.24622 0.03239  138 LYS A O   
804  C CB  . LYS A 102 ? 0.91335 0.76796 1.11807 -0.03282 -0.29387 0.05110  138 LYS A CB  
805  C CG  . LYS A 102 ? 0.97959 0.83387 1.15455 -0.03203 -0.31321 0.07062  138 LYS A CG  
806  C CD  . LYS A 102 ? 1.06895 0.94098 1.32170 -0.03494 -0.34107 0.09424  138 LYS A CD  
807  C CE  . LYS A 102 ? 1.20404 1.07594 1.43533 -0.03261 -0.35505 0.11855  138 LYS A CE  
808  N NZ  . LYS A 102 ? 1.02266 0.91133 1.33776 -0.03446 -0.38478 0.14609  138 LYS A NZ  
809  N N   . THR A 103 ? 0.78739 0.63772 0.92912 -0.00981 -0.21485 0.02553  139 THR A N   
810  C CA  . THR A 103 ? 0.84729 0.70020 0.96242 -0.00030 -0.19288 0.02263  139 THR A CA  
811  C C   . THR A 103 ? 0.74970 0.58905 0.80512 0.00410  -0.17714 0.01056  139 THR A C   
812  O O   . THR A 103 ? 0.82545 0.66185 0.84356 0.00994  -0.16964 0.01083  139 THR A O   
813  C CB  . THR A 103 ? 0.83015 0.70015 0.99893 0.00400  -0.16949 0.01725  139 THR A CB  
814  O OG1 . THR A 103 ? 0.80944 0.68212 0.95075 0.01134  -0.15165 0.01232  139 THR A OG1 
815  C CG2 . THR A 103 ? 0.96908 0.84062 1.15672 0.00153  -0.15100 0.00481  139 THR A CG2 
816  N N   . VAL A 104 ? 0.94332 0.77443 0.99600 0.00163  -0.17105 0.00153  140 VAL A N   
817  C CA  . VAL A 104 ? 0.75756 0.57385 0.76188 0.00650  -0.15842 -0.00692 140 VAL A CA  
818  C C   . VAL A 104 ? 0.64831 0.44638 0.60269 0.00420  -0.17199 -0.00847 140 VAL A C   
819  O O   . VAL A 104 ? 0.74157 0.53201 0.65763 0.01109  -0.15983 -0.01260 140 VAL A O   
820  C CB  . VAL A 104 ? 0.68176 0.49054 0.69924 0.00341  -0.14960 -0.01258 140 VAL A CB  
821  C CG1 . VAL A 104 ? 0.91887 0.70917 0.89412 0.00870  -0.14013 -0.01838 140 VAL A CG1 
822  C CG2 . VAL A 104 ? 0.92282 0.74793 0.97437 0.00501  -0.12949 -0.01234 140 VAL A CG2 
823  N N   . VAL A 105 ? 0.78036 0.57184 0.73521 -0.00653 -0.19718 -0.00583 141 VAL A N   
824  C CA  . VAL A 105 ? 0.63441 0.40691 0.53222 -0.01236 -0.21075 -0.00963 141 VAL A CA  
825  C C   . VAL A 105 ? 0.91707 0.69421 0.78587 -0.00803 -0.20780 0.00031  141 VAL A C   
826  O O   . VAL A 105 ? 0.77917 0.54348 0.59932 -0.00441 -0.19380 -0.00663 141 VAL A O   
827  C CB  . VAL A 105 ? 0.76384 0.53140 0.66862 -0.02750 -0.24415 -0.00764 141 VAL A CB  
828  C CG1 . VAL A 105 ? 0.76198 0.51304 0.59898 -0.03610 -0.26097 -0.00871 141 VAL A CG1 
829  C CG2 . VAL A 105 ? 0.88844 0.64465 0.81231 -0.03346 -0.24431 -0.02141 141 VAL A CG2 
830  N N   . GLN A 106 ? 0.88652 0.68153 0.79146 -0.00829 -0.21843 0.01715  142 GLN A N   
831  C CA  . GLN A 106 ? 0.88818 0.68645 0.77152 -0.00592 -0.21725 0.03068  142 GLN A CA  
832  C C   . GLN A 106 ? 0.78048 0.58251 0.65480 0.00599  -0.18609 0.02406  142 GLN A C   
833  O O   . GLN A 106 ? 0.87332 0.66833 0.70717 0.00749  -0.17689 0.02675  142 GLN A O   
834  C CB  . GLN A 106 ? 0.73659 0.55295 0.67669 -0.00720 -0.23294 0.05094  142 GLN A CB  
835  C CG  . GLN A 106 ? 0.96051 0.77559 0.91035 -0.01942 -0.27051 0.06450  142 GLN A CG  
836  C CD  . GLN A 106 ? 1.02521 0.85921 1.04798 -0.01854 -0.28486 0.08628  142 GLN A CD  
837  O OE1 . GLN A 106 ? 1.14940 0.98420 1.17528 -0.02654 -0.31719 0.10802  142 GLN A OE1 
838  N NE2 . GLN A 106 ? 1.04585 0.89457 1.12868 -0.00941 -0.26125 0.08054  142 GLN A NE2 
839  N N   . VAL A 107 ? 0.78244 0.59621 0.69407 0.01337  -0.16971 0.01590  143 VAL A N   
840  C CA  . VAL A 107 ? 0.77729 0.59683 0.68284 0.02347  -0.14549 0.00966  143 VAL A CA  
841  C C   . VAL A 107 ? 0.85074 0.65271 0.71159 0.02676  -0.13455 -0.00173 143 VAL A C   
842  O O   . VAL A 107 ? 0.80581 0.60689 0.64752 0.03278  -0.11926 -0.00313 143 VAL A O   
843  C CB  . VAL A 107 ? 0.71749 0.55351 0.66581 0.02784  -0.13407 0.00395  143 VAL A CB  
844  C CG1 . VAL A 107 ? 0.61186 0.45381 0.54990 0.03671  -0.11535 -0.00270 143 VAL A CG1 
845  C CG2 . VAL A 107 ? 0.83662 0.68902 0.83376 0.02573  -0.13751 0.01123  143 VAL A CG2 
846  N N   . ALA A 108 ? 0.79297 0.58014 0.64360 0.02266  -0.14067 -0.01048 144 ALA A N   
847  C CA  . ALA A 108 ? 0.87939 0.64697 0.69727 0.02613  -0.12836 -0.02317 144 ALA A CA  
848  C C   . ALA A 108 ? 1.01051 0.76364 0.77974 0.02356  -0.12365 -0.02639 144 ALA A C   
849  O O   . ALA A 108 ? 0.82769 0.57399 0.58186 0.03128  -0.10258 -0.03405 144 ALA A O   
850  C CB  . ALA A 108 ? 0.79163 0.54260 0.61031 0.01917  -0.13800 -0.03211 144 ALA A CB  
851  N N   . ILE A 109 ? 0.87649 0.62520 0.62179 0.01223  -0.14259 -0.01937 145 ILE A N   
852  C CA  . ILE A 109 ? 1.01274 0.74543 0.69963 0.00649  -0.13759 -0.02150 145 ILE A CA  
853  C C   . ILE A 109 ? 1.01089 0.75540 0.70077 0.01511  -0.11575 -0.01248 145 ILE A C   
854  O O   . ILE A 109 ? 0.94897 0.68105 0.60328 0.01680  -0.09373 -0.02071 145 ILE A O   
855  C CB  . ILE A 109 ? 1.04499 0.77274 0.70437 -0.00915 -0.16855 -0.01054 145 ILE A CB  
856  C CG1 . ILE A 109 ? 1.03151 0.75185 0.70321 -0.01814 -0.19207 -0.01986 145 ILE A CG1 
857  C CG2 . ILE A 109 ? 1.01113 0.71829 0.59418 -0.01855 -0.16319 -0.01422 145 ILE A CG2 
858  C CD1 . ILE A 109 ? 1.08249 0.81053 0.76310 -0.03089 -0.22966 -0.00283 145 ILE A CD1 
859  N N   . GLN A 110 ? 0.78571 0.55378 0.52245 0.01998  -0.11906 0.00254  146 GLN A N   
860  C CA  . GLN A 110 ? 0.99485 0.77524 0.74368 0.02702  -0.09923 0.01012  146 GLN A CA  
861  C C   . GLN A 110 ? 0.92057 0.70618 0.68845 0.03933  -0.07562 -0.00295 146 GLN A C   
862  O O   . GLN A 110 ? 0.95443 0.74083 0.71620 0.04402  -0.05404 -0.00380 146 GLN A O   
863  C CB  . GLN A 110 ? 0.80413 0.60626 0.60319 0.02768  -0.10917 0.02614  146 GLN A CB  
864  C CG  . GLN A 110 ? 0.94040 0.73942 0.72857 0.01760  -0.12940 0.04681  146 GLN A CG  
865  C CD  . GLN A 110 ? 0.91519 0.73364 0.76317 0.01989  -0.13344 0.06194  146 GLN A CD  
866  O OE1 . GLN A 110 ? 0.85861 0.68710 0.72858 0.02525  -0.11528 0.06420  146 GLN A OE1 
867  N NE2 . GLN A 110 ? 0.83163 0.65541 0.71327 0.01548  -0.15645 0.07099  146 GLN A NE2 
868  N N   . MET A 111 ? 0.84622 0.63601 0.64017 0.04430  -0.07956 -0.01098 147 MET A N   
869  C CA  . MET A 111 ? 0.98235 0.77755 0.79597 0.05584  -0.06260 -0.01879 147 MET A CA  
870  C C   . MET A 111 ? 1.05031 0.82327 0.83348 0.05855  -0.04517 -0.03120 147 MET A C   
871  O O   . MET A 111 ? 1.03021 0.80794 0.82930 0.06811  -0.02545 -0.03436 147 MET A O   
872  C CB  . MET A 111 ? 0.69107 0.49254 0.53121 0.05860  -0.07171 -0.02066 147 MET A CB  
873  C CG  . MET A 111 ? 0.78773 0.60930 0.65829 0.05503  -0.08337 -0.01337 147 MET A CG  
874  S SD  . MET A 111 ? 0.97818 0.80332 0.86833 0.05518  -0.08883 -0.01567 147 MET A SD  
875  C CE  . MET A 111 ? 0.77247 0.61946 0.68324 0.06422  -0.07983 -0.01464 147 MET A CE  
876  N N   . LEU A 112 ? 0.89365 0.64222 0.63719 0.04954  -0.05184 -0.04006 148 LEU A N   
877  C CA  . LEU A 112 ? 1.08330 0.80656 0.79448 0.04993  -0.03219 -0.05716 148 LEU A CA  
878  C C   . LEU A 112 ? 1.13980 0.86063 0.82282 0.04855  -0.01054 -0.05672 148 LEU A C   
879  O O   . LEU A 112 ? 0.96618 0.67756 0.64912 0.05533  0.01756  -0.06882 148 LEU A O   
880  C CB  . LEU A 112 ? 0.88401 0.58133 0.55520 0.03693  -0.04685 -0.06963 148 LEU A CB  
881  C CG  . LEU A 112 ? 1.01450 0.70827 0.71403 0.03690  -0.06256 -0.07277 148 LEU A CG  
882  C CD1 . LEU A 112 ? 1.06483 0.73608 0.72799 0.02077  -0.08123 -0.08451 148 LEU A CD1 
883  C CD2 . LEU A 112 ? 0.97975 0.66567 0.70895 0.04976  -0.04324 -0.08125 148 LEU A CD2 
884  N N   . THR A 113 ? 0.99293 0.72163 0.65640 0.03980  -0.02132 -0.04145 149 THR A N   
885  C CA  . THR A 113 ? 1.04185 0.76740 0.67595 0.03672  0.00076  -0.03685 149 THR A CA  
886  C C   . THR A 113 ? 0.95607 0.70407 0.64414 0.04982  0.02288  -0.03150 149 THR A C   
887  O O   . THR A 113 ? 0.96880 0.71136 0.64958 0.05265  0.05400  -0.03755 149 THR A O   
888  C CB  . THR A 113 ? 1.09978 0.82777 0.70447 0.02397  -0.01962 -0.01611 149 THR A CB  
889  O OG1 . THR A 113 ? 1.22153 0.93388 0.78791 0.01162  -0.04791 -0.01939 149 THR A OG1 
890  C CG2 . THR A 113 ? 1.20308 0.92094 0.76098 0.01736  0.00465  -0.01008 149 THR A CG2 
891  N N   . LEU A 114 ? 0.95795 0.73154 0.70165 0.05667  0.00799  -0.02171 150 LEU A N   
892  C CA  . LEU A 114 ? 0.92295 0.72019 0.72076 0.06721  0.02303  -0.01803 150 LEU A CA  
893  C C   . LEU A 114 ? 0.86730 0.66170 0.68830 0.07904  0.04209  -0.03178 150 LEU A C   
894  O O   . LEU A 114 ? 0.84779 0.65120 0.69670 0.08562  0.06610  -0.03267 150 LEU A O   
895  C CB  . LEU A 114 ? 0.99554 0.81808 0.83980 0.06946  0.00109  -0.00947 150 LEU A CB  
896  C CG  . LEU A 114 ? 0.87824 0.70681 0.72153 0.06013  -0.01583 0.00460  150 LEU A CG  
897  C CD1 . LEU A 114 ? 0.88429 0.73388 0.77254 0.06211  -0.03277 0.00535  150 LEU A CD1 
898  C CD2 . LEU A 114 ? 1.05105 0.88444 0.89835 0.05701  0.00001  0.01663  150 LEU A CD2 
899  N N   . VAL A 115 ? 0.91882 0.70086 0.73619 0.08201  0.03224  -0.04109 151 VAL A N   
900  C CA  . VAL A 115 ? 0.93623 0.71366 0.78362 0.09427  0.04824  -0.05105 151 VAL A CA  
901  C C   . VAL A 115 ? 0.91340 0.66663 0.73330 0.09357  0.08135  -0.06677 151 VAL A C   
902  O O   . VAL A 115 ? 0.96469 0.72163 0.82402 0.10461  0.10611  -0.07218 151 VAL A O   
903  C CB  . VAL A 115 ? 0.98169 0.74884 0.83262 0.09628  0.02991  -0.05417 151 VAL A CB  
904  C CG1 . VAL A 115 ? 0.84919 0.60344 0.72830 0.10818  0.04757  -0.06370 151 VAL A CG1 
905  C CG2 . VAL A 115 ? 0.72854 0.52174 0.61096 0.09813  0.00522  -0.03977 151 VAL A CG2 
906  N N   . GLU A 116 ? 0.93014 0.65867 0.68294 0.07976  0.08265  -0.07481 152 GLU A N   
907  C CA  . GLU A 116 ? 1.10929 0.81176 0.82248 0.07572  0.11689  -0.09333 152 GLU A CA  
908  C C   . GLU A 116 ? 1.16073 0.87656 0.88750 0.07786  0.14679  -0.08657 152 GLU A C   
909  O O   . GLU A 116 ? 1.29076 0.99707 1.03003 0.08354  0.18436  -0.10104 152 GLU A O   
910  C CB  . GLU A 116 ? 1.02992 0.70506 0.65902 0.05701  0.10619  -0.10171 152 GLU A CB  
911  C CG  . GLU A 116 ? 1.33121 0.97700 0.90251 0.04867  0.14284  -0.12338 152 GLU A CG  
912  C CD  . GLU A 116 ? 1.37789 0.99931 0.85711 0.02704  0.12646  -0.12908 152 GLU A CD  
913  O OE1 . GLU A 116 ? 1.30578 0.93391 0.77730 0.02019  0.08538  -0.11597 152 GLU A OE1 
914  O OE2 . GLU A 116 ? 1.46623 1.06227 0.88124 0.01603  0.15465  -0.14684 152 GLU A OE2 
915  N N   . GLU A 117 ? 1.46015 1.19725 1.19082 0.07313  0.13318  -0.06508 153 GLU A N   
916  C CA  . GLU A 117 ? 1.52089 1.27161 1.27210 0.07416  0.16158  -0.05633 153 GLU A CA  
917  C C   . GLU A 117 ? 1.46784 1.24221 1.30611 0.09095  0.17666  -0.05820 153 GLU A C   
918  O O   . GLU A 117 ? 1.50212 1.27919 1.36455 0.09460  0.21351  -0.06227 153 GLU A O   
919  C CB  . GLU A 117 ? 1.59325 1.36134 1.34267 0.06611  0.14109  -0.03190 153 GLU A CB  
920  C CG  . GLU A 117 ? 1.76846 1.51491 1.43576 0.04881  0.13831  -0.02330 153 GLU A CG  
921  C CD  . GLU A 117 ? 1.92888 1.65979 1.55647 0.04227  0.18178  -0.02642 153 GLU A CD  
922  O OE1 . GLU A 117 ? 1.84759 1.59251 1.52894 0.05123  0.21364  -0.02840 153 GLU A OE1 
923  O OE2 . GLU A 117 ? 1.96680 1.67192 1.50901 0.02704  0.18413  -0.02676 153 GLU A OE2 
924  N N   . VAL A 118 ? 0.99693 0.78934 0.88399 0.10048  0.14837  -0.05409 154 VAL A N   
925  C CA  . VAL A 118 ? 1.02897 0.84401 0.99730 0.11596  0.15525  -0.05375 154 VAL A CA  
926  C C   . VAL A 118 ? 1.13015 0.92433 1.11041 0.12481  0.18633  -0.07201 154 VAL A C   
927  O O   . VAL A 118 ? 1.05655 0.86336 1.09853 0.13526  0.21207  -0.07412 154 VAL A O   
928  C CB  . VAL A 118 ? 0.88808 0.72313 0.88986 0.12149  0.11584  -0.04411 154 VAL A CB  
929  C CG1 . VAL A 118 ? 0.93758 0.79339 1.01690 0.13691  0.11684  -0.04153 154 VAL A CG1 
930  C CG2 . VAL A 118 ? 1.12989 0.98736 1.13365 0.11338  0.09255  -0.03035 154 VAL A CG2 
931  N N   . HIS A 119 ? 0.97961 0.74117 0.90701 0.12025  0.18562  -0.08686 155 HIS A N   
932  C CA  . HIS A 119 ? 1.16377 0.90072 1.10397 0.12786  0.21683  -0.10823 155 HIS A CA  
933  C C   . HIS A 119 ? 1.13002 0.84940 1.03991 0.12171  0.26537  -0.12451 155 HIS A C   
934  O O   . HIS A 119 ? 1.25442 0.96550 1.20743 0.13171  0.30229  -0.14003 155 HIS A O   
935  C CB  . HIS A 119 ? 1.05588 0.76178 0.95075 0.12265  0.20096  -0.12162 155 HIS A CB  
936  C CG  . HIS A 119 ? 0.97143 0.69079 0.90309 0.13008  0.16264  -0.10681 155 HIS A CG  
937  N ND1 . HIS A 119 ? 1.11300 0.80930 1.01633 0.12538  0.14434  -0.11380 155 HIS A ND1 
938  C CD2 . HIS A 119 ? 0.95609 0.70910 0.94757 0.14017  0.14010  -0.08542 155 HIS A CD2 
939  C CE1 . HIS A 119 ? 0.95386 0.66832 0.89703 0.13274  0.11525  -0.09552 155 HIS A CE1 
940  N NE2 . HIS A 119 ? 0.94932 0.69800 0.94169 0.14132  0.11117  -0.07861 155 HIS A NE2 
941  N N   . ARG A 120 ? 1.09270 0.80558 0.93064 0.10514  0.26767  -0.12012 156 ARG A N   
942  C CA  . ARG A 120 ? 1.25680 0.95363 1.05770 0.09707  0.31580  -0.13201 156 ARG A CA  
943  C C   . ARG A 120 ? 1.31386 1.03930 1.19534 0.10747  0.34524  -0.12237 156 ARG A C   
944  O O   . ARG A 120 ? 1.27886 0.99204 1.15909 0.10633  0.39599  -0.13682 156 ARG A O   
945  C CB  . ARG A 120 ? 1.39526 1.07996 1.09940 0.07609  0.30618  -0.12225 156 ARG A CB  
946  C CG  . ARG A 120 ? 1.42113 1.07518 1.03976 0.06232  0.28137  -0.13483 156 ARG A CG  
947  C CD  . ARG A 120 ? 1.54112 1.17333 1.05417 0.04016  0.28995  -0.13328 156 ARG A CD  
948  N NE  . ARG A 120 ? 1.68459 1.33949 1.19695 0.03486  0.27662  -0.09989 156 ARG A NE  
949  C CZ  . ARG A 120 ? 1.68740 1.34671 1.19524 0.03097  0.31276  -0.08959 156 ARG A CZ  
950  N NH1 . ARG A 120 ? 1.57897 1.22296 1.08062 0.03150  0.36723  -0.11083 156 ARG A NH1 
951  N NH2 . ARG A 120 ? 1.61419 1.29278 1.12857 0.02615  0.29659  -0.05744 156 ARG A NH2 
952  N N   . HIS A 121 ? 1.24664 1.00976 1.19872 0.11621  0.31583  -0.10007 157 HIS A N   
953  C CA  . HIS A 121 ? 1.29429 1.08896 1.33649 0.12598  0.33644  -0.09096 157 HIS A CA  
954  C C   . HIS A 121 ? 1.17535 0.98533 1.31483 0.14591  0.33636  -0.09583 157 HIS A C   
955  O O   . HIS A 121 ? 1.20973 1.05561 1.43730 0.15514  0.33026  -0.08254 157 HIS A O   
956  C CB  . HIS A 121 ? 1.22077 1.04794 1.28593 0.12161  0.30426  -0.06585 157 HIS A CB  
957  C CG  . HIS A 121 ? 1.39009 1.20676 1.38568 0.10419  0.31287  -0.05527 157 HIS A CG  
958  N ND1 . HIS A 121 ? 1.32150 1.11368 1.22368 0.09097  0.29192  -0.05338 157 HIS A ND1 
959  C CD2 . HIS A 121 ? 1.37993 1.20719 1.38972 0.09751  0.33928  -0.04315 157 HIS A CD2 
960  C CE1 . HIS A 121 ? 1.36477 1.15286 1.22472 0.07743  0.30284  -0.03842 157 HIS A CE1 
961  N NE2 . HIS A 121 ? 1.31916 1.12706 1.24144 0.08091  0.33314  -0.03176 157 HIS A NE2 
962  N N   . ASP A 122 ? 1.21619 0.99966 1.34463 0.15200  0.34061  -0.11338 158 ASP A N   
963  C CA  . ASP A 122 ? 1.10599 0.89729 1.32751 0.17152  0.34538  -0.11707 158 ASP A CA  
964  C C   . ASP A 122 ? 1.08157 0.90763 1.36425 0.18140  0.29313  -0.09262 158 ASP A C   
965  O O   . ASP A 122 ? 1.20722 1.05835 1.58742 0.19666  0.29152  -0.08377 158 ASP A O   
966  C CB  . ASP A 122 ? 1.16323 0.96530 1.46265 0.18052  0.39637  -0.12467 158 ASP A CB  
967  C CG  . ASP A 122 ? 1.32758 1.09901 1.55756 0.16710  0.45212  -0.14657 158 ASP A CG  
968  O OD1 . ASP A 122 ? 1.29838 1.03094 1.43301 0.15557  0.45785  -0.16521 158 ASP A OD1 
969  O OD2 . ASP A 122 ? 1.52722 1.31359 1.79671 0.16664  0.49018  -0.14498 158 ASP A OD2 
970  N N   . LEU A 123 ? 1.17876 1.00682 1.40556 0.17213  0.25011  -0.08144 159 LEU A N   
971  C CA  . LEU A 123 ? 1.05811 0.91585 1.32435 0.17772  0.20203  -0.06055 159 LEU A CA  
972  C C   . LEU A 123 ? 0.91331 0.75026 1.12403 0.17376  0.17146  -0.06003 159 LEU A C   
973  O O   . LEU A 123 ? 1.04261 0.85267 1.17411 0.16116  0.17440  -0.07073 159 LEU A O   
974  C CB  . LEU A 123 ? 0.98998 0.87907 1.25625 0.16839  0.18156  -0.04627 159 LEU A CB  
975  C CG  . LEU A 123 ? 1.03143 0.96006 1.38699 0.17449  0.18432  -0.03620 159 LEU A CG  
976  C CD1 . LEU A 123 ? 0.98330 0.93642 1.41514 0.18861  0.15529  -0.02397 159 LEU A CD1 
977  C CD2 . LEU A 123 ? 1.09877 1.02237 1.48648 0.17696  0.23717  -0.04688 159 LEU A CD2 
978  N N   . ILE A 124 ? 0.87596 0.72594 1.12966 0.18363  0.14137  -0.04583 160 ILE A N   
979  C CA  . ILE A 124 ? 0.85570 0.69404 1.06484 0.17865  0.10870  -0.03953 160 ILE A CA  
980  C C   . ILE A 124 ? 0.94023 0.81423 1.16441 0.17627  0.06958  -0.01917 160 ILE A C   
981  O O   . ILE A 124 ? 0.95839 0.86463 1.24157 0.18202  0.06331  -0.00914 160 ILE A O   
982  C CB  . ILE A 124 ? 1.03099 0.84635 1.26527 0.18972  0.10938  -0.03998 160 ILE A CB  
983  C CG1 . ILE A 124 ? 0.98870 0.83152 1.30552 0.20492  0.08876  -0.01684 160 ILE A CG1 
984  C CG2 . ILE A 124 ? 0.95429 0.73640 1.19010 0.19327  0.15389  -0.06491 160 ILE A CG2 
985  C CD1 . ILE A 124 ? 0.85577 0.67483 1.20779 0.21719  0.09000  -0.01230 160 ILE A CD1 
986  N N   . TYR A 125 ? 0.95835 0.82663 1.13023 0.16647  0.04409  -0.01502 161 TYR A N   
987  C CA  . TYR A 125 ? 0.75386 0.65174 0.92334 0.15956  0.01345  -0.00280 161 TYR A CA  
988  C C   . TYR A 125 ? 0.88353 0.79870 1.08451 0.16620  -0.01593 0.01557  161 TYR A C   
989  O O   . TYR A 125 ? 0.79654 0.74466 1.03146 0.16642  -0.03477 0.02533  161 TYR A O   
990  C CB  . TYR A 125 ? 0.80375 0.68854 0.90651 0.14497  0.00411  -0.00804 161 TYR A CB  
991  C CG  . TYR A 125 ? 0.84289 0.75462 0.94257 0.13605  -0.01824 -0.00210 161 TYR A CG  
992  C CD1 . TYR A 125 ? 0.60137 0.53180 0.71746 0.13138  -0.01169 -0.00486 161 TYR A CD1 
993  C CD2 . TYR A 125 ? 0.88379 0.80044 0.96522 0.13124  -0.04278 0.00494  161 TYR A CD2 
994  C CE1 . TYR A 125 ? 0.78521 0.73765 0.90292 0.12243  -0.03030 -0.00323 161 TYR A CE1 
995  C CE2 . TYR A 125 ? 0.97104 0.90980 1.04836 0.12189  -0.05912 0.00544  161 TYR A CE2 
996  C CZ  . TYR A 125 ? 0.87792 0.83409 0.97503 0.11765  -0.05347 0.00010  161 TYR A CZ  
997  O OH  . TYR A 125 ? 0.87920 0.85482 0.97608 0.10761  -0.06830 -0.00293 161 TYR A OH  
998  N N   . ARG A 126 ? 0.74546 0.63827 0.93339 0.16995  -0.02145 0.02119  162 ARG A N   
999  C CA  . ARG A 126 ? 0.84971 0.75308 1.06273 0.17640  -0.04766 0.04352  162 ARG A CA  
1000 C C   . ARG A 126 ? 0.98263 0.90989 1.16610 0.16502  -0.07841 0.05376  162 ARG A C   
1001 O O   . ARG A 126 ? 1.15490 1.10344 1.36150 0.16813  -0.10361 0.07318  162 ARG A O   
1002 C CB  . ARG A 126 ? 0.99054 0.91300 1.28317 0.19193  -0.04851 0.05604  162 ARG A CB  
1003 C CG  . ARG A 126 ? 0.97378 0.87085 1.30482 0.20451  -0.01419 0.04496  162 ARG A CG  
1004 C CD  . ARG A 126 ? 0.92658 0.84539 1.35089 0.22096  -0.01417 0.05840  162 ARG A CD  
1005 N NE  . ARG A 126 ? 0.99414 0.95741 1.44737 0.21820  -0.04297 0.07230  162 ARG A NE  
1006 C CZ  . ARG A 126 ? 1.02040 1.00937 1.52165 0.22515  -0.07685 0.09909  162 ARG A CZ  
1007 N NH1 . ARG A 126 ? 1.07131 1.04629 1.60326 0.23714  -0.08550 0.11922  162 ARG A NH1 
1008 N NH2 . ARG A 126 ? 0.94680 0.97603 1.46743 0.21915  -0.10408 0.10668  162 ARG A NH2 
1009 N N   . ASP A 127 ? 0.99030 0.91377 1.12285 0.15116  -0.07711 0.04111  163 ASP A N   
1010 C CA  . ASP A 127 ? 1.00281 0.94461 1.10627 0.13939  -0.10029 0.04605  163 ASP A CA  
1011 C C   . ASP A 127 ? 0.92971 0.85656 0.98384 0.12659  -0.09279 0.03222  163 ASP A C   
1012 O O   . ASP A 127 ? 0.83743 0.78041 0.87787 0.11606  -0.09941 0.02511  163 ASP A O   
1013 C CB  . ASP A 127 ? 1.01765 0.99551 1.15007 0.13649  -0.11321 0.04503  163 ASP A CB  
1014 C CG  . ASP A 127 ? 0.94727 0.94540 1.05493 0.12546  -0.14043 0.05136  163 ASP A CG  
1015 O OD1 . ASP A 127 ? 0.93312 0.91787 1.00208 0.12109  -0.14718 0.05963  163 ASP A OD1 
1016 O OD2 . ASP A 127 ? 1.19015 1.21691 1.31629 0.11976  -0.15363 0.04678  163 ASP A OD2 
1017 N N   . ILE A 128 ? 0.87371 0.76981 0.90679 0.12704  -0.07966 0.02760  164 ILE A N   
1018 C CA  . ILE A 128 ? 0.77703 0.65934 0.77241 0.11552  -0.07457 0.01597  164 ILE A CA  
1019 C C   . ILE A 128 ? 0.86680 0.75720 0.83997 0.10553  -0.08864 0.02105  164 ILE A C   
1020 O O   . ILE A 128 ? 0.68012 0.56364 0.64641 0.10640  -0.09553 0.03350  164 ILE A O   
1021 C CB  . ILE A 128 ? 0.57808 0.42650 0.55778 0.11665  -0.06167 0.00936  164 ILE A CB  
1022 C CG1 . ILE A 128 ? 0.81895 0.65746 0.80969 0.12310  -0.04199 -0.00130 164 ILE A CG1 
1023 C CG2 . ILE A 128 ? 0.89541 0.73261 0.84196 0.10387  -0.06392 0.00161  164 ILE A CG2 
1024 C CD1 . ILE A 128 ? 0.68168 0.52820 0.65828 0.11590  -0.03519 -0.01024 164 ILE A CD1 
1025 N N   . LYS A 129 ? 0.68947 0.59325 0.65337 0.09562  -0.09031 0.01172  165 LYS A N   
1026 C CA  . LYS A 129 ? 0.80494 0.71457 0.74860 0.08454  -0.09664 0.01084  165 LYS A CA  
1027 C C   . LYS A 129 ? 0.81976 0.73448 0.76431 0.07575  -0.09144 -0.00298 165 LYS A C   
1028 O O   . LYS A 129 ? 0.77367 0.69721 0.73562 0.07754  -0.08822 -0.00832 165 LYS A O   
1029 C CB  . LYS A 129 ? 0.63957 0.57217 0.58166 0.08238  -0.11067 0.01798  165 LYS A CB  
1030 C CG  . LYS A 129 ? 0.86223 0.82071 0.82832 0.08262  -0.11706 0.01124  165 LYS A CG  
1031 C CD  . LYS A 129 ? 0.90983 0.89062 0.86211 0.07369  -0.13336 0.01193  165 LYS A CD  
1032 C CE  . LYS A 129 ? 0.96987 0.97466 0.95189 0.07931  -0.15020 0.01884  165 LYS A CE  
1033 N NZ  . LYS A 129 ? 0.93528 0.96235 0.89599 0.06745  -0.17045 0.01774  165 LYS A NZ  
1034 N N   . PRO A 130 ? 0.77412 0.68328 0.70670 0.06641  -0.08915 -0.00739 166 PRO A N   
1035 C CA  . PRO A 130 ? 0.86482 0.77848 0.80943 0.05916  -0.08482 -0.01828 166 PRO A CA  
1036 C C   . PRO A 130 ? 0.81073 0.74720 0.77071 0.05492  -0.08605 -0.02759 166 PRO A C   
1037 O O   . PRO A 130 ? 0.72712 0.66709 0.70761 0.05171  -0.08197 -0.03444 166 PRO A O   
1038 C CB  . PRO A 130 ? 0.66272 0.56789 0.60070 0.05075  -0.08107 -0.02025 166 PRO A CB  
1039 C CG  . PRO A 130 ? 0.83931 0.74364 0.75615 0.05051  -0.08251 -0.01220 166 PRO A CG  
1040 C CD  . PRO A 130 ? 0.66267 0.56144 0.57736 0.06198  -0.08864 -0.00116 166 PRO A CD  
1041 N N   . ASP A 131 ? 0.64379 0.59538 0.59566 0.05388  -0.09329 -0.02728 167 ASP A N   
1042 C CA  . ASP A 131 ? 0.80622 0.77979 0.77210 0.04758  -0.09696 -0.03964 167 ASP A CA  
1043 C C   . ASP A 131 ? 0.78986 0.77155 0.78822 0.05337  -0.09675 -0.04011 167 ASP A C   
1044 O O   . ASP A 131 ? 0.65972 0.65496 0.68110 0.04705  -0.09570 -0.05238 167 ASP A O   
1045 C CB  . ASP A 131 ? 0.86980 0.85840 0.81463 0.04426  -0.11044 -0.03669 167 ASP A CB  
1046 C CG  . ASP A 131 ? 0.95832 0.93685 0.86502 0.03835  -0.10816 -0.03116 167 ASP A CG  
1047 O OD1 . ASP A 131 ? 0.87260 0.83387 0.77057 0.04546  -0.10657 -0.01553 167 ASP A OD1 
1048 O OD2 . ASP A 131 ? 1.07224 1.05899 0.95776 0.02553  -0.10585 -0.04348 167 ASP A OD2 
1049 N N   . ASN A 132 ? 0.68831 0.66064 0.69105 0.06434  -0.09473 -0.02830 168 ASN A N   
1050 C CA  . ASN A 132 ? 0.75763 0.73605 0.78970 0.06964  -0.08909 -0.02736 168 ASN A CA  
1051 C C   . ASN A 132 ? 0.78020 0.74184 0.81240 0.06922  -0.07643 -0.02623 168 ASN A C   
1052 O O   . ASN A 132 ? 0.81948 0.78270 0.86992 0.07240  -0.06755 -0.02346 168 ASN A O   
1053 C CB  . ASN A 132 ? 0.73569 0.71442 0.77620 0.08151  -0.09025 -0.01667 168 ASN A CB  
1054 C CG  . ASN A 132 ? 0.86262 0.86231 0.91148 0.08225  -0.10814 -0.01256 168 ASN A CG  
1055 O OD1 . ASN A 132 ? 0.96019 0.97870 1.01142 0.07263  -0.11897 -0.02129 168 ASN A OD1 
1056 N ND2 . ASN A 132 ? 0.66891 0.66481 0.72308 0.09294  -0.11230 0.00073  168 ASN A ND2 
1057 N N   . PHE A 133 ? 0.66378 0.61009 0.67715 0.06461  -0.07589 -0.02655 169 PHE A N   
1058 C CA  . PHE A 133 ? 0.71896 0.65101 0.73123 0.06229  -0.07037 -0.02249 169 PHE A CA  
1059 C C   . PHE A 133 ? 0.63941 0.57905 0.67637 0.05379  -0.07090 -0.02855 169 PHE A C   
1060 O O   . PHE A 133 ? 0.74789 0.68804 0.78397 0.04863  -0.07339 -0.03525 169 PHE A O   
1061 C CB  . PHE A 133 ? 0.77056 0.68045 0.75308 0.06274  -0.07282 -0.01775 169 PHE A CB  
1062 C CG  . PHE A 133 ? 0.84890 0.74561 0.81113 0.07058  -0.06834 -0.01442 169 PHE A CG  
1063 C CD1 . PHE A 133 ? 0.79578 0.69334 0.75467 0.07619  -0.07078 -0.01395 169 PHE A CD1 
1064 C CD2 . PHE A 133 ? 0.81166 0.69350 0.75794 0.07169  -0.06040 -0.01151 169 PHE A CD2 
1065 C CE1 . PHE A 133 ? 0.71739 0.60098 0.66800 0.08432  -0.06436 -0.01191 169 PHE A CE1 
1066 C CE2 . PHE A 133 ? 0.85776 0.72513 0.78773 0.07827  -0.05152 -0.01321 169 PHE A CE2 
1067 C CZ  . PHE A 133 ? 0.68651 0.55458 0.62391 0.08536  -0.05298 -0.01407 169 PHE A CZ  
1068 N N   . LEU A 134 ? 0.65872 0.60305 0.72182 0.05216  -0.06573 -0.02612 170 LEU A N   
1069 C CA  . LEU A 134 ? 0.56707 0.51741 0.66555 0.04492  -0.06419 -0.03196 170 LEU A CA  
1070 C C   . LEU A 134 ? 0.60688 0.54383 0.71441 0.04380  -0.06361 -0.01623 170 LEU A C   
1071 O O   . LEU A 134 ? 0.67435 0.60176 0.76157 0.04696  -0.06124 -0.00268 170 LEU A O   
1072 C CB  . LEU A 134 ? 0.45089 0.41977 0.58385 0.04199  -0.06020 -0.04252 170 LEU A CB  
1073 C CG  . LEU A 134 ? 0.68047 0.66573 0.80665 0.04429  -0.06491 -0.05045 170 LEU A CG  
1074 C CD1 . LEU A 134 ? 0.84969 0.85347 1.01854 0.03876  -0.06342 -0.06148 170 LEU A CD1 
1075 C CD2 . LEU A 134 ? 0.82084 0.80953 0.91914 0.04166  -0.07294 -0.05998 170 LEU A CD2 
1076 N N   . ILE A 135 ? 0.63121 0.56721 0.76996 0.03869  -0.06528 -0.01751 171 ILE A N   
1077 C CA  . ILE A 135 ? 0.69747 0.62362 0.85625 0.03703  -0.06841 0.00131  171 ILE A CA  
1078 C C   . ILE A 135 ? 0.79726 0.73046 0.99640 0.03523  -0.05906 0.00349  171 ILE A C   
1079 O O   . ILE A 135 ? 0.60092 0.54704 0.80931 0.03510  -0.05169 -0.01075 171 ILE A O   
1080 C CB  . ILE A 135 ? 0.88528 0.80815 1.07501 0.03348  -0.07474 0.00173  171 ILE A CB  
1081 C CG1 . ILE A 135 ? 0.83484 0.76983 1.06154 0.02959  -0.06410 -0.02324 171 ILE A CG1 
1082 C CG2 . ILE A 135 ? 0.70141 0.61455 0.85528 0.03409  -0.08603 0.00634  171 ILE A CG2 
1083 C CD1 . ILE A 135 ? 0.75654 0.68928 1.02788 0.02638  -0.06366 -0.02548 171 ILE A CD1 
1084 N N   . GLY A 136 ? 0.96709 0.89217 1.19406 0.03316  -0.06104 0.02301  172 GLY A N   
1085 C CA  . GLY A 136 ? 0.93577 0.86448 1.20916 0.03063  -0.05111 0.02848  172 GLY A CA  
1086 C C   . GLY A 136 ? 1.03397 0.96919 1.37312 0.02637  -0.04631 0.01166  172 GLY A C   
1087 O O   . GLY A 136 ? 1.05432 0.99430 1.39811 0.02493  -0.04673 -0.00958 172 GLY A O   
1088 N N   . ARG A 137 ? 1.08185 1.01559 1.47366 0.02353  -0.03871 0.02064  173 ARG A N   
1089 C CA  . ARG A 137 ? 1.12741 1.06396 1.59119 0.01888  -0.03070 0.00329  173 ARG A CA  
1090 C C   . ARG A 137 ? 1.18571 1.10987 1.69427 0.02012  -0.03727 0.02647  173 ARG A C   
1091 O O   . ARG A 137 ? 1.22968 1.14347 1.71768 0.02281  -0.04963 0.06163  173 ARG A O   
1092 C CB  . ARG A 137 ? 1.13171 1.07366 1.64095 0.01411  -0.01785 -0.00347 173 ARG A CB  
1093 C CG  . ARG A 137 ? 0.98458 0.94385 1.48266 0.00967  -0.01315 -0.03884 173 ARG A CG  
1094 C CD  . ARG A 137 ? 0.98119 0.94524 1.55037 0.00084  -0.00157 -0.06118 173 ARG A CD  
1095 N NE  . ARG A 137 ? 1.01345 0.99091 1.57586 -0.00672 -0.00076 -0.10357 173 ARG A NE  
1096 C CZ  . ARG A 137 ? 1.15459 1.13559 1.77023 -0.01725 0.00866  -0.13464 173 ARG A CZ  
1097 N NH1 . ARG A 137 ? 0.97495 0.94661 1.66481 -0.02036 0.01933  -0.12815 173 ARG A NH1 
1098 N NH2 . ARG A 137 ? 1.14070 1.13343 1.73307 -0.02601 0.00741  -0.17308 173 ARG A NH2 
1099 N N   . ARG A 138 ? 1.24846 1.17391 1.82015 0.01733  -0.02891 0.00568  174 ARG A N   
1100 C CA  . ARG A 138 ? 1.23762 1.15354 1.87096 0.01941  -0.03432 0.02549  174 ARG A CA  
1101 C C   . ARG A 138 ? 1.21251 1.11778 1.88733 0.02001  -0.03742 0.06258  174 ARG A C   
1102 O O   . ARG A 138 ? 1.28491 1.19052 1.98197 0.01650  -0.02448 0.05824  174 ARG A O   
1103 C CB  . ARG A 138 ? 1.36474 1.28353 2.06609 0.01581  -0.01693 -0.01004 174 ARG A CB  
1104 C CG  . ARG A 138 ? 1.31094 1.23390 1.99387 0.01662  -0.01777 -0.02628 174 ARG A CG  
1105 C CD  . ARG A 138 ? 1.22993 1.14613 1.95620 0.02199  -0.03345 0.00650  174 ARG A CD  
1106 N NE  . ARG A 138 ? 1.29938 1.22022 2.00352 0.02269  -0.03736 -0.00267 174 ARG A NE  
1107 C CZ  . ARG A 138 ? 1.38873 1.30771 2.12422 0.02623  -0.05439 0.02206  174 ARG A CZ  
1108 N NH1 . ARG A 138 ? 1.33514 1.24781 2.12550 0.02969  -0.07124 0.05904  174 ARG A NH1 
1109 N NH2 . ARG A 138 ? 1.27589 1.19990 1.98916 0.02557  -0.05623 0.01162  174 ARG A NH2 
1110 N N   . GLY A 139 ? 1.22084 1.11691 1.90616 0.02348  -0.05623 0.10135  175 GLY A N   
1111 C CA  . GLY A 139 ? 1.39321 1.27741 2.11234 0.02350  -0.06266 0.14455  175 GLY A CA  
1112 C C   . GLY A 139 ? 1.38639 1.26551 2.02902 0.02170  -0.06665 0.17193  175 GLY A C   
1113 O O   . GLY A 139 ? 1.43511 1.30272 2.09264 0.02035  -0.07225 0.21332  175 GLY A O   
1114 N N   . ALA A 140 ? 1.36053 1.24685 1.92418 0.02140  -0.06217 0.15161  176 ALA A N   
1115 C CA  . ALA A 140 ? 1.39499 1.27624 1.88775 0.01973  -0.05993 0.17230  176 ALA A CA  
1116 C C   . ALA A 140 ? 1.48897 1.36110 1.90728 0.01979  -0.08270 0.19855  176 ALA A C   
1117 O O   . ALA A 140 ? 1.44443 1.31800 1.86057 0.02153  -0.10105 0.19441  176 ALA A O   
1118 C CB  . ALA A 140 ? 1.27883 1.17239 1.73326 0.01999  -0.04352 0.13781  176 ALA A CB  
1119 N N   . THR A 141 ? 1.53091 1.39329 1.88787 0.01638  -0.07995 0.22427  177 THR A N   
1120 C CA  . THR A 141 ? 1.71303 1.56440 1.98919 0.01340  -0.10103 0.24694  177 THR A CA  
1121 C C   . THR A 141 ? 1.68394 1.54003 1.89742 0.01572  -0.10274 0.21481  177 THR A C   
1122 O O   . THR A 141 ? 1.86869 1.71869 2.03706 0.01353  -0.12543 0.22157  177 THR A O   
1123 C CB  . THR A 141 ? 1.83416 1.67174 2.05489 0.00710  -0.09190 0.27994  177 THR A CB  
1124 O OG1 . THR A 141 ? 1.68954 1.52342 1.97812 0.00531  -0.08271 0.30671  177 THR A OG1 
1125 C CG2 . THR A 141 ? 1.81388 1.63726 1.95961 0.00056  -0.11960 0.31071  177 THR A CG2 
1126 N N   . ASP A 142 ? 1.41943 1.28624 1.63294 0.01951  -0.08109 0.18128  178 ASP A N   
1127 C CA  . ASP A 142 ? 1.22402 1.09563 1.39120 0.02288  -0.08132 0.15153  178 ASP A CA  
1128 C C   . ASP A 142 ? 1.15207 1.03746 1.36867 0.02647  -0.08285 0.12189  178 ASP A C   
1129 O O   . ASP A 142 ? 1.17215 1.06679 1.37459 0.02956  -0.07346 0.09396  178 ASP A O   
1130 C CB  . ASP A 142 ? 1.32342 1.19767 1.45453 0.02474  -0.05807 0.13819  178 ASP A CB  
1131 C CG  . ASP A 142 ? 1.37496 1.25949 1.56353 0.02467  -0.03757 0.13560  178 ASP A CG  
1132 O OD1 . ASP A 142 ? 1.18393 1.08219 1.43010 0.02615  -0.03593 0.11384  178 ASP A OD1 
1133 O OD2 . ASP A 142 ? 1.32440 1.20267 1.49964 0.02170  -0.02194 0.15429  178 ASP A OD2 
1134 N N   . GLU A 143 ? 1.16267 1.04914 1.43853 0.02566  -0.09383 0.12881  179 GLU A N   
1135 C CA  . GLU A 143 ? 1.15647 1.05461 1.48322 0.02730  -0.08868 0.09920  179 GLU A CA  
1136 C C   . GLU A 143 ? 1.15732 1.05804 1.44188 0.02872  -0.09543 0.08001  179 GLU A C   
1137 O O   . GLU A 143 ? 1.19608 1.10675 1.48561 0.02953  -0.08429 0.05066  179 GLU A O   
1138 C CB  . GLU A 143 ? 1.28994 1.18660 1.69522 0.02658  -0.09614 0.11200  179 GLU A CB  
1139 C CG  . GLU A 143 ? 1.28507 1.19110 1.74264 0.02701  -0.08775 0.08087  179 GLU A CG  
1140 C CD  . GLU A 143 ? 1.32629 1.22960 1.86546 0.02755  -0.09581 0.09630  179 GLU A CD  
1141 O OE1 . GLU A 143 ? 1.23456 1.13089 1.81556 0.02762  -0.10020 0.12470  179 GLU A OE1 
1142 O OE2 . GLU A 143 ? 1.49804 1.40601 2.06402 0.02800  -0.09726 0.08241  179 GLU A OE2 
1143 N N   . ASN A 144 ? 1.03356 0.92468 1.27455 0.02763  -0.11428 0.09664  180 ASN A N   
1144 C CA  . ASN A 144 ? 1.09497 0.98627 1.30432 0.02795  -0.12145 0.08093  180 ASN A CA  
1145 C C   . ASN A 144 ? 1.09269 0.97370 1.22158 0.02786  -0.12449 0.08201  180 ASN A C   
1146 O O   . ASN A 144 ? 0.92116 0.79727 1.02075 0.02671  -0.13465 0.07534  180 ASN A O   
1147 C CB  . ASN A 144 ? 0.89254 0.78262 1.13756 0.02537  -0.14192 0.09300  180 ASN A CB  
1148 C CG  . ASN A 144 ? 1.08105 0.98175 1.40928 0.02637  -0.13167 0.08017  180 ASN A CG  
1149 O OD1 . ASN A 144 ? 0.93660 0.84523 1.27261 0.02707  -0.11277 0.05119  180 ASN A OD1 
1150 N ND2 . ASN A 144 ? 1.14770 1.04784 1.53856 0.02586  -0.14348 0.10194  180 ASN A ND2 
1151 N N   . ASN A 145 ? 1.11943 0.99618 1.21702 0.02857  -0.11321 0.08888  181 ASN A N   
1152 C CA  . ASN A 145 ? 1.03299 0.89997 1.06171 0.02935  -0.10798 0.08341  181 ASN A CA  
1153 C C   . ASN A 145 ? 0.97900 0.85596 1.00809 0.03553  -0.09200 0.05748  181 ASN A C   
1154 O O   . ASN A 145 ? 0.91408 0.80586 0.98639 0.03768  -0.08236 0.04630  181 ASN A O   
1155 C CB  . ASN A 145 ? 1.04142 0.89929 1.03808 0.02693  -0.09805 0.10165  181 ASN A CB  
1156 C CG  . ASN A 145 ? 1.19524 1.03932 1.16557 0.01893  -0.11806 0.13075  181 ASN A CG  
1157 O OD1 . ASN A 145 ? 1.22270 1.06197 1.18256 0.01507  -0.14190 0.13409  181 ASN A OD1 
1158 N ND2 . ASN A 145 ? 1.19367 1.03178 1.15369 0.01536  -0.10964 0.15370  181 ASN A ND2 
1159 N N   . VAL A 146 ? 0.96741 0.83546 0.94875 0.03753  -0.09075 0.04812  182 VAL A N   
1160 C CA  . VAL A 146 ? 0.82849 0.70451 0.80916 0.04388  -0.07996 0.02870  182 VAL A CA  
1161 C C   . VAL A 146 ? 0.95574 0.83500 0.92940 0.04836  -0.06148 0.02776  182 VAL A C   
1162 O O   . VAL A 146 ? 0.95762 0.82352 0.89603 0.04704  -0.05376 0.03614  182 VAL A O   
1163 C CB  . VAL A 146 ? 1.00695 0.87040 0.95186 0.04449  -0.08681 0.02044  182 VAL A CB  
1164 C CG1 . VAL A 146 ? 0.94885 0.81950 0.89542 0.05167  -0.07719 0.00625  182 VAL A CG1 
1165 C CG2 . VAL A 146 ? 0.84474 0.70732 0.80655 0.03928  -0.10354 0.02159  182 VAL A CG2 
1166 N N   . HIS A 147 ? 0.90791 0.80542 0.91539 0.05248  -0.05400 0.01689  183 HIS A N   
1167 C CA  . HIS A 147 ? 0.87347 0.77963 0.89140 0.05703  -0.03787 0.01497  183 HIS A CA  
1168 C C   . HIS A 147 ? 0.80963 0.72401 0.82724 0.06424  -0.03765 0.00209  183 HIS A C   
1169 O O   . HIS A 147 ? 0.72903 0.64588 0.74353 0.06435  -0.04926 -0.00511 183 HIS A O   
1170 C CB  . HIS A 147 ? 0.81293 0.73642 0.88247 0.05400  -0.03302 0.01570  183 HIS A CB  
1171 C CG  . HIS A 147 ? 0.89015 0.80557 0.97135 0.04756  -0.03402 0.03213  183 HIS A CG  
1172 N ND1 . HIS A 147 ? 0.92551 0.83654 1.01707 0.04346  -0.04842 0.03561  183 HIS A ND1 
1173 C CD2 . HIS A 147 ? 0.93507 0.84604 1.02401 0.04456  -0.02209 0.04878  183 HIS A CD2 
1174 C CE1 . HIS A 147 ? 0.92614 0.83051 1.03370 0.03904  -0.04835 0.05518  183 HIS A CE1 
1175 N NE2 . HIS A 147 ? 1.04772 0.95106 1.15012 0.03909  -0.03237 0.06439  183 HIS A NE2 
1176 N N   . LEU A 148 ? 0.79436 0.71302 0.81877 0.07017  -0.02339 0.00134  184 LEU A N   
1177 C CA  . LEU A 148 ? 0.73091 0.65861 0.76516 0.07842  -0.02433 -0.00616 184 LEU A CA  
1178 C C   . LEU A 148 ? 0.85991 0.81282 0.94393 0.08067  -0.01959 -0.00818 184 LEU A C   
1179 O O   . LEU A 148 ? 0.84827 0.80314 0.95013 0.08015  -0.00257 -0.00349 184 LEU A O   
1180 C CB  . LEU A 148 ? 0.65341 0.56123 0.65843 0.08487  -0.01149 -0.00664 184 LEU A CB  
1181 C CG  . LEU A 148 ? 0.75093 0.66546 0.77492 0.09525  -0.01204 -0.01065 184 LEU A CG  
1182 C CD1 . LEU A 148 ? 0.87335 0.79060 0.88995 0.09467  -0.03333 -0.01153 184 LEU A CD1 
1183 C CD2 . LEU A 148 ? 0.60341 0.49518 0.60702 0.10142  0.00679  -0.01425 184 LEU A CD2 
1184 N N   . ILE A 149 ? 0.82343 0.79580 0.92893 0.08177  -0.03507 -0.01443 185 ILE A N   
1185 C CA  . ILE A 149 ? 0.84756 0.84737 1.00282 0.08161  -0.03820 -0.01812 185 ILE A CA  
1186 C C   . ILE A 149 ? 0.87945 0.89212 1.04485 0.08930  -0.05144 -0.01765 185 ILE A C   
1187 O O   . ILE A 149 ? 0.90238 0.90030 1.03801 0.09509  -0.05472 -0.01376 185 ILE A O   
1188 C CB  . ILE A 149 ? 0.94948 0.96374 1.12392 0.07043  -0.04949 -0.02746 185 ILE A CB  
1189 C CG1 . ILE A 149 ? 0.90078 0.91348 1.04481 0.06630  -0.06644 -0.03465 185 ILE A CG1 
1190 C CG2 . ILE A 149 ? 1.18971 1.19170 1.36769 0.06410  -0.03701 -0.02350 185 ILE A CG2 
1191 C CD1 . ILE A 149 ? 0.96169 0.99931 1.12100 0.06186  -0.08475 -0.04443 185 ILE A CD1 
1192 N N   . ASP A 150 ? 0.73493 0.77557 0.94715 0.08875  -0.06085 -0.02013 186 ASP A N   
1193 C CA  . ASP A 150 ? 0.72556 0.78414 0.95618 0.09486  -0.08012 -0.01583 186 ASP A CA  
1194 C C   . ASP A 150 ? 0.76075 0.80732 0.99906 0.10947  -0.06769 -0.00557 186 ASP A C   
1195 O O   . ASP A 150 ? 0.73611 0.76104 0.93627 0.11404  -0.06777 -0.00137 186 ASP A O   
1196 C CB  . ASP A 150 ? 0.81914 0.87738 1.00847 0.08892  -0.10312 -0.01762 186 ASP A CB  
1197 C CG  . ASP A 150 ? 0.78990 0.87285 0.99727 0.09029  -0.13029 -0.01142 186 ASP A CG  
1198 O OD1 . ASP A 150 ? 0.72413 0.82167 0.97993 0.09969  -0.13233 -0.00269 186 ASP A OD1 
1199 O OD2 . ASP A 150 ? 0.92136 1.00938 1.09472 0.08135  -0.14965 -0.01436 186 ASP A OD2 
1200 N N   . PHE A 151 ? 0.68335 0.74335 0.97693 0.11649  -0.05496 -0.00282 187 PHE A N   
1201 C CA  . PHE A 151 ? 0.78170 0.83079 1.09500 0.13082  -0.03786 0.00364  187 PHE A CA  
1202 C C   . PHE A 151 ? 0.76536 0.84283 1.14332 0.13981  -0.05650 0.01318  187 PHE A C   
1203 O O   . PHE A 151 ? 0.85157 0.93054 1.27948 0.15178  -0.03827 0.01709  187 PHE A O   
1204 C CB  . PHE A 151 ? 0.70809 0.74453 1.03268 0.13244  0.00067  -0.00079 187 PHE A CB  
1205 C CG  . PHE A 151 ? 0.80719 0.81265 1.06410 0.12481  0.01616  -0.00546 187 PHE A CG  
1206 C CD1 . PHE A 151 ? 0.78801 0.79597 1.02838 0.11244  0.01251  -0.00720 187 PHE A CD1 
1207 C CD2 . PHE A 151 ? 0.81132 0.78509 1.02516 0.12938  0.03236  -0.00801 187 PHE A CD2 
1208 C CE1 . PHE A 151 ? 0.86381 0.84537 1.04800 0.10569  0.02199  -0.00731 187 PHE A CE1 
1209 C CE2 . PHE A 151 ? 0.81791 0.76546 0.96965 0.12080  0.04084  -0.01114 187 PHE A CE2 
1210 C CZ  . PHE A 151 ? 0.90972 0.86223 1.04755 0.10939  0.03422  -0.00874 187 PHE A CZ  
1211 N N   . GLY A 152 ? 0.96820 1.06834 1.34625 0.13351  -0.09306 0.01709  188 GLY A N   
1212 C CA  . GLY A 152 ? 1.01178 1.13983 1.44502 0.14070  -0.11964 0.03055  188 GLY A CA  
1213 C C   . GLY A 152 ? 1.04609 1.15837 1.48194 0.15565  -0.12115 0.04640  188 GLY A C   
1214 O O   . GLY A 152 ? 1.20700 1.34007 1.70440 0.16558  -0.13807 0.06160  188 GLY A O   
1215 N N   . MET A 153 ? 0.92873 1.00501 1.30552 0.15717  -0.10528 0.04396  189 MET A N   
1216 C CA  . MET A 153 ? 0.87276 0.92787 1.25254 0.17043  -0.10227 0.05656  189 MET A CA  
1217 C C   . MET A 153 ? 0.87157 0.89683 1.25878 0.17955  -0.05996 0.04551  189 MET A C   
1218 O O   . MET A 153 ? 0.95507 0.95578 1.34143 0.18926  -0.05168 0.05040  189 MET A O   
1219 C CB  . MET A 153 ? 1.01186 1.04759 1.32039 0.16355  -0.11849 0.06202  189 MET A CB  
1220 C CG  . MET A 153 ? 1.11245 1.17355 1.40725 0.15520  -0.15902 0.07559  189 MET A CG  
1221 S SD  . MET A 153 ? 1.25829 1.33488 1.60913 0.16940  -0.18838 0.10799  189 MET A SD  
1222 C CE  . MET A 153 ? 1.31608 1.43502 1.65622 0.15386  -0.23552 0.11498  189 MET A CE  
1223 N N   . ALA A 154 ? 0.70845 0.73353 1.10070 0.17537  -0.03206 0.03047  190 ALA A N   
1224 C CA  . ALA A 154 ? 0.84547 0.84003 1.22792 0.18019  0.00995  0.01745  190 ALA A CA  
1225 C C   . ALA A 154 ? 0.85199 0.85009 1.31321 0.19700  0.02805  0.02126  190 ALA A C   
1226 O O   . ALA A 154 ? 0.82132 0.85297 1.35838 0.20292  0.01719  0.03103  190 ALA A O   
1227 C CB  . ALA A 154 ? 0.69287 0.68741 1.05759 0.16995  0.03467  0.00494  190 ALA A CB  
1228 N N   . LYS A 155 ? 1.07220 1.03580 1.52160 0.20443  0.05543  0.01243  191 LYS A N   
1229 C CA  . LYS A 155 ? 0.96617 0.92941 1.49722 0.22137  0.07771  0.01351  191 LYS A CA  
1230 C C   . LYS A 155 ? 1.03517 0.96386 1.54863 0.22242  0.13089  -0.01091 191 LYS A C   
1231 O O   . LYS A 155 ? 1.27840 1.16934 1.72574 0.21775  0.14190  -0.02402 191 LYS A O   
1232 C CB  . LYS A 155 ? 0.96592 0.92324 1.52616 0.23337  0.05336  0.03125  191 LYS A CB  
1233 C CG  . LYS A 155 ? 0.94520 0.92090 1.61764 0.25165  0.05940  0.04271  191 LYS A CG  
1234 C CD  . LYS A 155 ? 0.98710 0.94737 1.68477 0.26394  0.04107  0.06115  191 LYS A CD  
1235 C CE  . LYS A 155 ? 1.09601 1.08519 1.88327 0.27170  0.02522  0.08229  191 LYS A CE  
1236 N NZ  . LYS A 155 ? 1.03219 1.06783 1.83828 0.26641  -0.02239 0.10457  191 LYS A NZ  
1237 N N   . GLN A 156 ? 0.99849 0.94173 1.57058 0.22661  0.16330  -0.01757 192 GLN A N   
1238 C CA  . GLN A 156 ? 0.95443 0.87127 1.54482 0.23262  0.21887  -0.03890 192 GLN A CA  
1239 C C   . GLN A 156 ? 1.06402 0.94707 1.66297 0.24386  0.22765  -0.04590 192 GLN A C   
1240 O O   . GLN A 156 ? 1.12157 1.01668 1.78622 0.25741  0.20119  -0.02686 192 GLN A O   
1241 C CB  . GLN A 156 ? 1.14162 1.09141 1.84275 0.24301  0.23961  -0.03433 192 GLN A CB  
1242 C CG  . GLN A 156 ? 1.23911 1.22306 2.02748 0.25231  0.19711  -0.00859 192 GLN A CG  
1243 C CD  . GLN A 156 ? 1.20753 1.23805 2.03001 0.24914  0.15147  0.01228  192 GLN A CD  
1244 O OE1 . GLN A 156 ? 1.10524 1.13944 1.86338 0.23908  0.12331  0.01563  192 GLN A OE1 
1245 N NE2 . GLN A 156 ? 1.01298 1.07815 1.92161 0.24989  0.14020  0.02500  192 GLN A NE2 
1246 N N   . TYR A 157 ? 1.07998 0.91947 1.61250 0.23701  0.26480  -0.07311 193 TYR A N   
1247 C CA  . TYR A 157 ? 0.98372 0.78518 1.52044 0.24495  0.27827  -0.08612 193 TYR A CA  
1248 C C   . TYR A 157 ? 1.10953 0.88568 1.64134 0.23949  0.33181  -0.11556 193 TYR A C   
1249 O O   . TYR A 157 ? 1.19290 0.94349 1.73262 0.24125  0.34007  -0.12621 193 TYR A O   
1250 C CB  . TYR A 157 ? 0.91215 0.68479 1.34717 0.23125  0.25305  -0.09057 193 TYR A CB  
1251 C CG  . TYR A 157 ? 1.14492 0.88801 1.47592 0.21219  0.27863  -0.11756 193 TYR A CG  
1252 C CD1 . TYR A 157 ? 1.15808 0.91889 1.43561 0.19823  0.27233  -0.11255 193 TYR A CD1 
1253 C CD2 . TYR A 157 ? 1.15724 0.85403 1.44400 0.20713  0.30704  -0.14729 193 TYR A CD2 
1254 C CE1 . TYR A 157 ? 1.10395 0.83849 1.28551 0.18038  0.29141  -0.13177 193 TYR A CE1 
1255 C CE2 . TYR A 157 ? 1.26824 0.93912 1.45402 0.18770  0.32537  -0.17042 193 TYR A CE2 
1256 C CZ  . TYR A 157 ? 1.24987 0.94025 1.38259 0.17470  0.31635  -0.16033 193 TYR A CZ  
1257 O OH  . TYR A 157 ? 1.21791 0.88202 1.24913 0.15505  0.33114  -0.17891 193 TYR A OH  
1258 N N   . ARG A 158 ? 1.26045 1.04259 1.77922 0.23146  0.36869  -0.12828 194 ARG A N   
1259 C CA  . ARG A 158 ? 1.05278 0.81188 1.56239 0.22378  0.42104  -0.15551 194 ARG A CA  
1260 C C   . ARG A 158 ? 1.27869 1.06457 1.82452 0.21984  0.45067  -0.15255 194 ARG A C   
1261 O O   . ARG A 158 ? 1.28748 1.09987 1.83275 0.21871  0.43591  -0.13670 194 ARG A O   
1262 C CB  . ARG A 158 ? 1.21929 0.93041 1.60978 0.20812  0.44433  -0.18673 194 ARG A CB  
1263 C CG  . ARG A 158 ? 1.35909 1.06618 1.66036 0.19546  0.44985  -0.18918 194 ARG A CG  
1264 C CD  . ARG A 158 ? 1.28899 0.94854 1.46789 0.17748  0.46368  -0.21770 194 ARG A CD  
1265 N NE  . ARG A 158 ? 1.43566 1.09639 1.52148 0.15948  0.46024  -0.21221 194 ARG A NE  
1266 C CZ  . ARG A 158 ? 1.46380 1.09286 1.43242 0.13903  0.45824  -0.22744 194 ARG A CZ  
1267 N NH1 . ARG A 158 ? 1.47227 1.06176 1.39796 0.13385  0.46399  -0.25558 194 ARG A NH1 
1268 N NH2 . ARG A 158 ? 1.53409 1.17143 1.43043 0.12275  0.44819  -0.21315 194 ARG A NH2 
1269 N N   . ASP A 159 ? 1.42453 1.20277 2.00738 0.21722  0.49321  -0.16768 195 ASP A N   
1270 C CA  . ASP A 159 ? 1.50442 1.30423 2.12765 0.21224  0.52627  -0.16539 195 ASP A CA  
1271 C C   . ASP A 159 ? 1.61690 1.40073 2.13736 0.19605  0.55303  -0.17702 195 ASP A C   
1272 O O   . ASP A 159 ? 1.64743 1.39184 2.06478 0.18470  0.56884  -0.19955 195 ASP A O   
1273 C CB  . ASP A 159 ? 1.54948 1.33719 2.22785 0.21147  0.57084  -0.18200 195 ASP A CB  
1274 C CG  . ASP A 159 ? 1.58490 1.39865 2.33100 0.20839  0.60050  -0.17474 195 ASP A CG  
1275 O OD1 . ASP A 159 ? 1.53193 1.38537 2.37933 0.21814  0.57309  -0.14970 195 ASP A OD1 
1276 O OD2 . ASP A 159 ? 1.68516 1.47913 2.38131 0.19482  0.64972  -0.19331 195 ASP A OD2 
1277 N N   . PRO A 160 ? 1.77387 1.58745 2.31899 0.19306  0.55647  -0.16075 196 PRO A N   
1278 C CA  . PRO A 160 ? 1.80268 1.60138 2.25133 0.17693  0.58241  -0.16649 196 PRO A CA  
1279 C C   . PRO A 160 ? 2.12181 1.88915 2.51783 0.16178  0.64120  -0.19011 196 PRO A C   
1280 O O   . PRO A 160 ? 2.21283 1.95859 2.50400 0.14554  0.66097  -0.19622 196 PRO A O   
1281 C CB  . PRO A 160 ? 1.78833 1.63126 2.30344 0.17883  0.57027  -0.14043 196 PRO A CB  
1282 C CG  . PRO A 160 ? 1.69674 1.57598 2.31567 0.19543  0.52042  -0.12128 196 PRO A CG  
1283 C CD  . PRO A 160 ? 1.68262 1.54550 2.33890 0.20303  0.52762  -0.13346 196 PRO A CD  
1284 N N   . ARG A 161 ? 2.00843 1.77179 2.47100 0.16536  0.66917  -0.20227 197 ARG A N   
1285 C CA  . ARG A 161 ? 1.97600 1.70977 2.39317 0.15049  0.72757  -0.22586 197 ARG A CA  
1286 C C   . ARG A 161 ? 1.99489 1.69077 2.37979 0.14793  0.74461  -0.25657 197 ARG A C   
1287 O O   . ARG A 161 ? 2.13386 1.79525 2.42657 0.13080  0.78166  -0.28083 197 ARG A O   
1288 C CB  . ARG A 161 ? 1.95929 1.71698 2.48164 0.15267  0.76017  -0.21746 197 ARG A CB  
1289 C CG  . ARG A 161 ? 1.99227 1.78075 2.53362 0.14877  0.75731  -0.19217 197 ARG A CG  
1290 C CD  . ARG A 161 ? 2.13202 1.89576 2.55439 0.12830  0.79263  -0.19730 197 ARG A CD  
1291 N NE  . ARG A 161 ? 2.23583 1.97156 2.52730 0.11977  0.77349  -0.20552 197 ARG A NE  
1292 C CZ  . ARG A 161 ? 2.22987 1.94939 2.40972 0.10255  0.78354  -0.20071 197 ARG A CZ  
1293 N NH1 . ARG A 161 ? 2.15529 1.88409 2.33633 0.09250  0.81315  -0.18583 197 ARG A NH1 
1294 N NH2 . ARG A 161 ? 2.19005 1.88287 2.25509 0.09417  0.76125  -0.20877 197 ARG A NH2 
1295 N N   . THR A 162 ? 1.88046 1.58160 2.33698 0.16319  0.71759  -0.25541 198 THR A N   
1296 C CA  . THR A 162 ? 1.88041 1.54518 2.30970 0.16083  0.72963  -0.28382 198 THR A CA  
1297 C C   . THR A 162 ? 1.79793 1.44291 2.14687 0.15984  0.68873  -0.28859 198 THR A C   
1298 O O   . THR A 162 ? 1.80778 1.41753 2.10819 0.15280  0.69834  -0.31566 198 THR A O   
1299 C CB  . THR A 162 ? 1.88380 1.56165 2.44539 0.17679  0.73002  -0.27952 198 THR A CB  
1300 O OG1 . THR A 162 ? 1.77970 1.47565 2.38631 0.19259  0.67362  -0.25727 198 THR A OG1 
1301 C CG2 . THR A 162 ? 1.82092 1.53170 2.48751 0.18150  0.75116  -0.26273 198 THR A CG2 
1302 N N   . LYS A 163 ? 1.80235 1.46835 2.13898 0.16575  0.64419  -0.26405 199 LYS A N   
1303 C CA  . LYS A 163 ? 1.71759 1.36603 1.98557 0.16512  0.60316  -0.26546 199 LYS A CA  
1304 C C   . LYS A 163 ? 1.72320 1.35997 2.04350 0.17632  0.58444  -0.27104 199 LYS A C   
1305 O O   . LYS A 163 ? 1.85277 1.45886 2.10645 0.16987  0.56929  -0.28687 199 LYS A O   
1306 C CB  . LYS A 163 ? 1.73808 1.34893 1.86176 0.14239  0.61666  -0.28912 199 LYS A CB  
1307 C CG  . LYS A 163 ? 1.75620 1.37567 1.80575 0.13405  0.59917  -0.27186 199 LYS A CG  
1308 C CD  . LYS A 163 ? 1.91973 1.56774 2.00612 0.13351  0.62614  -0.25453 199 LYS A CD  
1309 C CE  . LYS A 163 ? 2.08356 1.71167 2.13037 0.11748  0.68074  -0.27516 199 LYS A CE  
1310 N NZ  . LYS A 163 ? 2.12956 1.78258 2.20856 0.11490  0.70807  -0.25673 199 LYS A NZ  
1311 N N   . GLN A 164 ? 1.63465 1.29573 2.07620 0.19193  0.58383  -0.25634 200 GLN A N   
1312 C CA  . GLN A 164 ? 1.54896 1.20151 2.05105 0.20325  0.56617  -0.25530 200 GLN A CA  
1313 C C   . GLN A 164 ? 1.38601 1.06270 1.92413 0.21743  0.50763  -0.22178 200 GLN A C   
1314 O O   . GLN A 164 ? 1.23634 0.95298 1.83333 0.22638  0.48600  -0.19311 200 GLN A O   
1315 C CB  . GLN A 164 ? 1.59094 1.25500 2.20543 0.21125  0.59542  -0.25489 200 GLN A CB  
1316 C CG  . GLN A 164 ? 1.64897 1.32186 2.35873 0.22752  0.56543  -0.23570 200 GLN A CG  
1317 C CD  . GLN A 164 ? 1.75293 1.38626 2.41981 0.22464  0.55955  -0.25483 200 GLN A CD  
1318 O OE1 . GLN A 164 ? 1.89853 1.49618 2.46974 0.20930  0.58202  -0.28780 200 GLN A OE1 
1319 N NE2 . GLN A 164 ? 1.74419 1.38387 2.48158 0.23798  0.52764  -0.23298 200 GLN A NE2 
1320 N N   . HIS A 165 ? 1.48999 1.14187 1.99244 0.21789  0.48194  -0.22575 201 HIS A N   
1321 C CA  . HIS A 165 ? 1.36196 1.03026 1.88558 0.22902  0.42781  -0.19480 201 HIS A CA  
1322 C C   . HIS A 165 ? 1.28553 0.98767 1.93019 0.24578  0.40741  -0.16332 201 HIS A C   
1323 O O   . HIS A 165 ? 1.28498 0.98784 2.00059 0.24955  0.43394  -0.16882 201 HIS A O   
1324 C CB  . HIS A 165 ? 1.35353 0.98394 1.82217 0.22433  0.41077  -0.20695 201 HIS A CB  
1325 C CG  . HIS A 165 ? 1.27206 0.90728 1.70470 0.22637  0.36361  -0.18521 201 HIS A CG  
1326 N ND1 . HIS A 165 ? 1.25830 0.92184 1.75584 0.24052  0.32214  -0.14735 201 HIS A ND1 
1327 C CD2 . HIS A 165 ? 1.18647 0.80065 1.52355 0.21442  0.35140  -0.19565 201 HIS A CD2 
1328 C CE1 . HIS A 165 ? 1.16969 0.82911 1.61439 0.23769  0.28919  -0.13615 201 HIS A CE1 
1329 N NE2 . HIS A 165 ? 1.12193 0.75106 1.47309 0.22241  0.30665  -0.16518 201 HIS A NE2 
1330 N N   . ILE A 166 ? 1.14621 0.87644 1.81256 0.25443  0.35874  -0.12954 202 ILE A N   
1331 C CA  . ILE A 166 ? 1.18551 0.94827 1.95289 0.26794  0.32840  -0.09523 202 ILE A CA  
1332 C C   . ILE A 166 ? 1.14131 0.87818 1.93238 0.27286  0.32074  -0.09254 202 ILE A C   
1333 O O   . ILE A 166 ? 1.28249 0.98451 2.00530 0.26702  0.31761  -0.10663 202 ILE A O   
1334 C CB  . ILE A 166 ? 0.85855 0.65706 1.62762 0.27247  0.27623  -0.06115 202 ILE A CB  
1335 C CG1 . ILE A 166 ? 0.94313 0.71818 1.62697 0.26832  0.25012  -0.06062 202 ILE A CG1 
1336 C CG2 . ILE A 166 ? 0.84449 0.67456 1.61645 0.26836  0.28426  -0.06105 202 ILE A CG2 
1337 C CD1 . ILE A 166 ? 0.88866 0.69584 1.57305 0.27183  0.19801  -0.02686 202 ILE A CD1 
1338 N N   . PRO A 167 ? 1.05677 0.80845 1.94553 0.28233  0.31795  -0.07469 203 PRO A N   
1339 C CA  . PRO A 167 ? 1.12200 0.84913 2.03944 0.28688  0.31150  -0.06937 203 PRO A CA  
1340 C C   . PRO A 167 ? 1.13504 0.86373 2.02357 0.29004  0.25967  -0.03861 203 PRO A C   
1341 O O   . PRO A 167 ? 1.16232 0.92320 2.04610 0.29264  0.22115  -0.01033 203 PRO A O   
1342 C CB  . PRO A 167 ? 1.07258 0.82326 2.10991 0.29639  0.31670  -0.05101 203 PRO A CB  
1343 C CG  . PRO A 167 ? 1.08078 0.85419 2.14165 0.29323  0.34614  -0.06370 203 PRO A CG  
1344 C CD  . PRO A 167 ? 1.02454 0.81202 2.00569 0.28747  0.32750  -0.06252 203 PRO A CD  
1345 N N   . TYR A 168 ? 1.04796 0.74062 1.91629 0.28817  0.26030  -0.04530 204 TYR A N   
1346 C CA  . TYR A 168 ? 0.96111 0.65036 1.80558 0.28975  0.21613  -0.01531 204 TYR A CA  
1347 C C   . TYR A 168 ? 1.25593 0.97602 2.18412 0.30064  0.18228  0.03029  204 TYR A C   
1348 O O   . TYR A 168 ? 0.98950 0.71510 2.00259 0.30702  0.19827  0.03383  204 TYR A O   
1349 C CB  . TYR A 168 ? 0.99736 0.63886 1.80693 0.28326  0.22971  -0.03596 204 TYR A CB  
1350 C CG  . TYR A 168 ? 0.98299 0.61543 1.77145 0.28304  0.19052  -0.00589 204 TYR A CG  
1351 C CD1 . TYR A 168 ? 1.00158 0.63789 1.85726 0.29079  0.17243  0.02732  204 TYR A CD1 
1352 C CD2 . TYR A 168 ? 1.20120 0.81962 1.90349 0.27375  0.17387  -0.01030 204 TYR A CD2 
1353 C CE1 . TYR A 168 ? 0.99556 0.62262 1.82817 0.28887  0.13994  0.05635  204 TYR A CE1 
1354 C CE2 . TYR A 168 ? 0.99789 0.60723 1.68168 0.27176  0.14191  0.01744  204 TYR A CE2 
1355 C CZ  . TYR A 168 ? 1.29869 0.91234 2.04517 0.27908  0.12593  0.05094  204 TYR A CZ  
1356 O OH  . TYR A 168 ? 1.26017 0.86457 1.98534 0.27565  0.09709  0.08048  204 TYR A OH  
1357 N N   . ARG A 169 ? 0.96196 0.70220 1.86461 0.30138  0.13515  0.06550  205 ARG A N   
1358 C CA  . ARG A 169 ? 1.21537 0.98302 2.17958 0.30874  0.09696  0.11142  205 ARG A CA  
1359 C C   . ARG A 169 ? 0.98733 0.75515 1.88997 0.30459  0.05377  0.14133  205 ARG A C   
1360 O O   . ARG A 169 ? 0.99950 0.75093 1.82171 0.29682  0.05323  0.12677  205 ARG A O   
1361 C CB  . ARG A 169 ? 1.27161 1.08672 2.29244 0.31308  0.08365  0.12667  205 ARG A CB  
1362 C CG  . ARG A 169 ? 1.15526 0.99596 2.11861 0.30751  0.06640  0.12415  205 ARG A CG  
1363 C CD  . ARG A 169 ? 1.08390 0.97474 2.10068 0.30999  0.03247  0.15334  205 ARG A CD  
1364 N NE  . ARG A 169 ? 1.25862 1.16382 2.27586 0.31066  -0.01772 0.19653  205 ARG A NE  
1365 C CZ  . ARG A 169 ? 1.34677 1.29360 2.39033 0.30978  -0.05873 0.22604  205 ARG A CZ  
1366 N NH1 . ARG A 169 ? 1.49491 1.47477 2.57558 0.30870  -0.05716 0.21787  205 ARG A NH1 
1367 N NH2 . ARG A 169 ? 1.33105 1.28587 2.36071 0.30837  -0.10217 0.26428  205 ARG A NH2 
1368 N N   . GLU A 170 ? 1.03306 0.81909 1.97431 0.30870  0.01820  0.18424  206 GLU A N   
1369 C CA  . GLU A 170 ? 0.91737 0.70401 1.80186 0.30340  -0.02153 0.21692  206 GLU A CA  
1370 C C   . GLU A 170 ? 1.08232 0.91417 1.99139 0.30499  -0.06651 0.25788  206 GLU A C   
1371 O O   . GLU A 170 ? 1.19757 1.06130 2.15919 0.30902  -0.06828 0.25679  206 GLU A O   
1372 C CB  . GLU A 170 ? 1.12081 0.87098 2.01194 0.30315  -0.01673 0.22812  206 GLU A CB  
1373 C CG  . GLU A 170 ? 1.14470 0.85041 2.02494 0.30049  0.02807  0.18459  206 GLU A CG  
1374 C CD  . GLU A 170 ? 1.40215 1.07143 2.26652 0.29594  0.02757  0.19389  206 GLU A CD  
1375 O OE1 . GLU A 170 ? 1.53267 1.20923 2.37181 0.29300  -0.00643 0.23267  206 GLU A OE1 
1376 O OE2 . GLU A 170 ? 1.34529 0.97872 2.22051 0.29384  0.06210  0.16146  206 GLU A OE2 
1377 N N   . LYS A 171 ? 1.07340 0.90718 1.94106 0.29997  -0.10262 0.29353  207 LYS A N   
1378 C CA  . LYS A 171 ? 1.19002 1.06281 2.06527 0.29840  -0.14945 0.33430  207 LYS A CA  
1379 C C   . LYS A 171 ? 1.35006 1.26157 2.20218 0.29373  -0.16633 0.32510  207 LYS A C   
1380 O O   . LYS A 171 ? 1.46655 1.41327 2.37418 0.29656  -0.18345 0.33605  207 LYS A O   
1381 C CB  . LYS A 171 ? 1.36829 1.25261 2.34340 0.30779  -0.15540 0.35827  207 LYS A CB  
1382 C CG  . LYS A 171 ? 1.38469 1.26124 2.35886 0.30683  -0.18371 0.40289  207 LYS A CG  
1383 C CD  . LYS A 171 ? 1.47376 1.37406 2.36777 0.29589  -0.22966 0.43233  207 LYS A CD  
1384 C CE  . LYS A 171 ? 1.55743 1.44199 2.42730 0.29235  -0.25111 0.47376  207 LYS A CE  
1385 N NZ  . LYS A 171 ? 1.54883 1.45390 2.32831 0.27925  -0.29118 0.49873  207 LYS A NZ  
1386 N N   . LYS A 172 ? 1.26888 1.17384 2.04251 0.28563  -0.16213 0.30515  208 LYS A N   
1387 C CA  . LYS A 172 ? 1.40343 1.34223 2.15029 0.27960  -0.17643 0.29410  208 LYS A CA  
1388 C C   . LYS A 172 ? 1.42027 1.37279 2.08388 0.26654  -0.21529 0.31564  208 LYS A C   
1389 O O   . LYS A 172 ? 1.43135 1.36016 2.04520 0.26154  -0.22145 0.33198  208 LYS A O   
1390 C CB  . LYS A 172 ? 1.33299 1.25544 2.06042 0.27977  -0.13780 0.25104  208 LYS A CB  
1391 C CG  . LYS A 172 ? 1.36178 1.25446 2.14146 0.28891  -0.09055 0.22417  208 LYS A CG  
1392 C CD  . LYS A 172 ? 1.24844 1.12425 1.99409 0.28657  -0.05401 0.18233  208 LYS A CD  
1393 C CE  . LYS A 172 ? 1.22405 1.13721 1.99037 0.28563  -0.05426 0.17154  208 LYS A CE  
1394 N NZ  . LYS A 172 ? 1.03144 0.96532 1.88978 0.29297  -0.04381 0.17437  208 LYS A NZ  
1395 N N   . SER A 173 ? 1.43453 1.42554 2.08368 0.25938  -0.23960 0.31403  209 SER A N   
1396 C CA  . SER A 173 ? 1.50791 1.51418 2.07376 0.24416  -0.27411 0.32838  209 SER A CA  
1397 C C   . SER A 173 ? 1.55177 1.53544 2.04695 0.23672  -0.25625 0.30552  209 SER A C   
1398 O O   . SER A 173 ? 1.55112 1.52550 2.06107 0.24120  -0.22704 0.27433  209 SER A O   
1399 C CB  . SER A 173 ? 1.51853 1.57290 2.09365 0.23666  -0.30577 0.32936  209 SER A CB  
1400 O OG  . SER A 173 ? 1.52496 1.59140 2.13420 0.23958  -0.28420 0.29708  209 SER A OG  
1401 N N   . LEU A 174 ? 1.54547 1.51929 1.96357 0.22448  -0.27270 0.32187  210 LEU A N   
1402 C CA  . LEU A 174 ? 1.47693 1.42997 1.82885 0.21522  -0.25917 0.30379  210 LEU A CA  
1403 C C   . LEU A 174 ? 1.57897 1.56004 1.90915 0.20596  -0.26370 0.27660  210 LEU A C   
1404 O O   . LEU A 174 ? 1.47489 1.49166 1.78971 0.19672  -0.29684 0.28587  210 LEU A O   
1405 C CB  . LEU A 174 ? 1.35988 1.30212 1.63395 0.20082  -0.27560 0.32803  210 LEU A CB  
1406 C CG  . LEU A 174 ? 1.32410 1.23126 1.60265 0.20515  -0.26454 0.35120  210 LEU A CG  
1407 C CD1 . LEU A 174 ? 1.29113 1.15848 1.60680 0.21580  -0.22576 0.32822  210 LEU A CD1 
1408 C CD2 . LEU A 174 ? 1.31789 1.23795 1.64406 0.21282  -0.28346 0.38158  210 LEU A CD2 
1409 N N   . SER A 175 ? 1.82073 1.78513 2.14132 0.20457  -0.22647 0.23759  211 SER A N   
1410 C CA  . SER A 175 ? 1.84399 1.83108 2.14794 0.19488  -0.21989 0.20619  211 SER A CA  
1411 C C   . SER A 175 ? 1.87751 1.84137 2.11090 0.18133  -0.19424 0.17681  211 SER A C   
1412 O O   . SER A 175 ? 1.85085 1.78284 2.08608 0.18614  -0.16404 0.16123  211 SER A O   
1413 C CB  . SER A 175 ? 1.83918 1.83511 2.22215 0.20895  -0.19994 0.19119  211 SER A CB  
1414 O OG  . SER A 175 ? 1.82160 1.83391 2.18749 0.19895  -0.18846 0.16182  211 SER A OG  
1415 N N   . GLY A 176 ? 1.95232 1.93235 2.12696 0.16382  -0.20681 0.16815  212 GLY A N   
1416 C CA  . GLY A 176 ? 1.83513 1.79938 1.95231 0.15053  -0.18652 0.14217  212 GLY A CA  
1417 C C   . GLY A 176 ? 1.74748 1.71122 1.79930 0.13488  -0.19979 0.15095  212 GLY A C   
1418 O O   . GLY A 176 ? 1.58405 1.56408 1.62312 0.13119  -0.22714 0.17489  212 GLY A O   
1419 N N   . THR A 177 ? 1.50660 1.45193 1.51608 0.12456  -0.18000 0.13178  213 THR A N   
1420 C CA  . THR A 177 ? 1.46055 1.40145 1.41139 0.10920  -0.18302 0.13612  213 THR A CA  
1421 C C   . THR A 177 ? 1.38323 1.29113 1.32727 0.11233  -0.17160 0.15209  213 THR A C   
1422 O O   . THR A 177 ? 1.25994 1.14355 1.22192 0.11791  -0.15138 0.13941  213 THR A O   
1423 C CB  . THR A 177 ? 1.28327 1.22666 1.20437 0.09564  -0.16798 0.10577  213 THR A CB  
1424 O OG1 . THR A 177 ? 1.18850 1.15639 1.13195 0.09542  -0.17280 0.08852  213 THR A OG1 
1425 C CG2 . THR A 177 ? 1.32554 1.27366 1.19127 0.07840  -0.17163 0.10739  213 THR A CG2 
1426 N N   . ALA A 178 ? 1.54719 1.67141 1.25916 0.33058  -0.06929 0.10439  214 ALA A N   
1427 C CA  . ALA A 178 ? 1.62848 1.70970 1.33700 0.33979  -0.04517 0.13480  214 ALA A CA  
1428 C C   . ALA A 178 ? 1.51997 1.54471 1.21540 0.32807  -0.02943 0.12848  214 ALA A C   
1429 O O   . ALA A 178 ? 1.53210 1.50920 1.23560 0.33170  -0.00918 0.14767  214 ALA A O   
1430 C CB  . ALA A 178 ? 1.86280 1.97680 1.55117 0.34841  -0.04542 0.15914  214 ALA A CB  
1431 N N   . ARG A 179 ? 1.13918 1.16729 0.82744 0.30629  -0.03633 0.09677  215 ARG A N   
1432 C CA  . ARG A 179 ? 1.06738 1.04947 0.75582 0.28996  -0.02170 0.08872  215 ARG A CA  
1433 C C   . ARG A 179 ? 1.15019 1.08148 0.86319 0.27595  -0.01605 0.07882  215 ARG A C   
1434 O O   . ARG A 179 ? 0.84801 0.73581 0.56555 0.26663  -0.00287 0.08198  215 ARG A O   
1435 C CB  . ARG A 179 ? 1.17481 1.17757 0.85514 0.27433  -0.03065 0.05802  215 ARG A CB  
1436 C CG  . ARG A 179 ? 1.15902 1.13162 0.84060 0.26380  -0.01426 0.05575  215 ARG A CG  
1437 C CD  . ARG A 179 ? 1.09484 1.08303 0.78171 0.24939  -0.02252 0.02024  215 ARG A CD  
1438 N NE  . ARG A 179 ? 1.21101 1.25265 0.87038 0.25695  -0.03121 0.00778  215 ARG A NE  
1439 C CZ  . ARG A 179 ? 1.07443 1.13493 0.73632 0.24713  -0.03870 -0.02804 215 ARG A CZ  
1440 N NH1 . ARG A 179 ? 0.99858 1.02947 0.69427 0.23161  -0.03928 -0.05077 215 ARG A NH1 
1441 N NH2 . ARG A 179 ? 1.02081 1.13087 0.65162 0.25333  -0.04701 -0.04191 215 ARG A NH2 
1442 N N   . TYR A 180 ? 1.00909 0.94760 0.73722 0.27289  -0.02535 0.06691  216 TYR A N   
1443 C CA  . TYR A 180 ? 0.84827 0.74409 0.58964 0.25660  -0.02080 0.05435  216 TYR A CA  
1444 C C   . TYR A 180 ? 1.01288 0.89762 0.76610 0.26853  -0.01011 0.06390  216 TYR A C   
1445 O O   . TYR A 180 ? 0.87816 0.72315 0.63386 0.25601  -0.00172 0.05423  216 TYR A O   
1446 C CB  . TYR A 180 ? 0.72569 0.63335 0.47480 0.23507  -0.03764 0.02714  216 TYR A CB  
1447 C CG  . TYR A 180 ? 1.07990 0.99962 0.82592 0.22505  -0.04793 0.01202  216 TYR A CG  
1448 C CD1 . TYR A 180 ? 0.86138 0.75846 0.60258 0.22309  -0.03862 0.01646  216 TYR A CD1 
1449 C CD2 . TYR A 180 ? 0.95625 0.91024 0.70976 0.21720  -0.06508 -0.00877 216 TYR A CD2 
1450 C CE1 . TYR A 180 ? 1.05552 0.96590 0.79945 0.21613  -0.04401 0.00004  216 TYR A CE1 
1451 C CE2 . TYR A 180 ? 0.88216 0.84419 0.63648 0.20967  -0.07179 -0.02732 216 TYR A CE2 
1452 C CZ  . TYR A 180 ? 0.98418 0.92535 0.73368 0.21045  -0.06014 -0.02310 216 TYR A CZ  
1453 O OH  . TYR A 180 ? 0.84405 0.79527 0.59967 0.20502  -0.06292 -0.04398 216 TYR A OH  
1454 N N   . MET A 181 ? 0.82873 0.74900 0.58994 0.29266  -0.01032 0.08161  217 MET A N   
1455 C CA  . MET A 181 ? 1.15878 1.07388 0.94149 0.30677  0.00147  0.08808  217 MET A CA  
1456 C C   . MET A 181 ? 1.02524 0.87917 0.80884 0.31280  0.02460  0.09890  217 MET A C   
1457 O O   . MET A 181 ? 0.97774 0.80388 0.74990 0.31294  0.03060  0.11227  217 MET A O   
1458 C CB  . MET A 181 ? 1.00134 0.97214 0.80042 0.33432  -0.00686 0.10858  217 MET A CB  
1459 C CG  . MET A 181 ? 1.07707 1.06167 0.85835 0.35076  -0.01055 0.13657  217 MET A CG  
1460 S SD  . MET A 181 ? 1.41307 1.46197 1.21865 0.37152  -0.02129 0.16003  217 MET A SD  
1461 C CE  . MET A 181 ? 1.46868 1.57428 1.29894 0.37099  -0.04205 0.13565  217 MET A CE  
1462 N N   . SER A 182 ? 0.83497 0.66826 0.63455 0.31664  0.03959  0.09102  218 SER A N   
1463 C CA  . SER A 182 ? 1.14544 0.91587 0.94720 0.31926  0.06214  0.09239  218 SER A CA  
1464 C C   . SER A 182 ? 0.98454 0.75454 0.80780 0.34059  0.07183  0.12239  218 SER A C   
1465 O O   . SER A 182 ? 0.98687 0.80719 0.82070 0.35621  0.06103  0.14312  218 SER A O   
1466 C CB  . SER A 182 ? 0.97500 0.72794 0.78517 0.31518  0.07804  0.06995  218 SER A CB  
1467 O OG  . SER A 182 ? 1.16793 0.95991 1.01102 0.34183  0.08447  0.07945  218 SER A OG  
1468 N N   . ILE A 183 ? 1.15840 0.87416 0.99005 0.33354  0.08990  0.12215  219 ILE A N   
1469 C CA  . ILE A 183 ? 1.09057 0.80068 0.94983 0.34739  0.09982  0.14854  219 ILE A CA  
1470 C C   . ILE A 183 ? 1.01108 0.74570 0.90469 0.37094  0.10554  0.15297  219 ILE A C   
1471 O O   . ILE A 183 ? 1.14281 0.90601 1.05832 0.38946  0.10099  0.18120  219 ILE A O   
1472 C CB  . ILE A 183 ? 1.06143 0.70569 0.92749 0.33231  0.11650  0.14277  219 ILE A CB  
1473 C CG1 . ILE A 183 ? 1.16271 0.79809 1.01321 0.31760  0.11174  0.15724  219 ILE A CG1 
1474 C CG2 . ILE A 183 ? 1.23340 0.85793 1.13792 0.34878  0.13156  0.15687  219 ILE A CG2 
1475 C CD1 . ILE A 183 ? 1.32233 0.89767 1.18567 0.30035  0.12555  0.15187  219 ILE A CD1 
1476 N N   . ASN A 184 ? 0.98698 0.71313 0.88619 0.37075  0.11589  0.12553  220 ASN A N   
1477 C CA  . ASN A 184 ? 1.23942 0.99213 1.17892 0.39334  0.12498  0.12649  220 ASN A CA  
1478 C C   . ASN A 184 ? 1.16507 0.99428 1.11808 0.40978  0.10373  0.14482  220 ASN A C   
1479 O O   . ASN A 184 ? 1.21975 1.08019 1.21427 0.43140  0.10366  0.16084  220 ASN A O   
1480 C CB  . ASN A 184 ? 1.20013 0.93273 1.13688 0.38703  0.14432  0.09011  220 ASN A CB  
1481 C CG  . ASN A 184 ? 1.25758 0.91784 1.18160 0.36965  0.16373  0.06740  220 ASN A CG  
1482 O OD1 . ASN A 184 ? 1.29088 0.91861 1.23514 0.37262  0.17001  0.07897  220 ASN A OD1 
1483 N ND2 . ASN A 184 ? 1.24298 0.87830 1.13190 0.34998  0.17176  0.03438  220 ASN A ND2 
1484 N N   . THR A 185 ? 1.04118 0.90257 0.96305 0.39930  0.08339  0.14104  221 THR A N   
1485 C CA  . THR A 185 ? 1.09293 1.03017 1.02683 0.41090  0.05946  0.15396  221 THR A CA  
1486 C C   . THR A 185 ? 1.05104 1.00918 0.98436 0.41942  0.04595  0.18709  221 THR A C   
1487 O O   . THR A 185 ? 1.09524 1.10741 1.05471 0.43555  0.03161  0.20405  221 THR A O   
1488 C CB  . THR A 185 ? 1.14788 1.11120 1.05049 0.39582  0.04038  0.13614  221 THR A CB  
1489 O OG1 . THR A 185 ? 1.14047 1.07417 1.03577 0.37597  0.05421  0.10504  221 THR A OG1 
1490 C CG2 . THR A 185 ? 1.09692 1.14303 1.02069 0.40474  0.01554  0.14029  221 THR A CG2 
1491 N N   . HIS A 186 ? 0.97633 0.89416 0.88106 0.40824  0.05059  0.19717  222 HIS A N   
1492 C CA  . HIS A 186 ? 1.11212 1.04497 1.01255 0.41646  0.04306  0.23073  222 HIS A CA  
1493 C C   . HIS A 186 ? 1.16017 1.08705 1.10450 0.43826  0.05110  0.25411  222 HIS A C   
1494 O O   . HIS A 186 ? 1.32136 1.28555 1.27244 0.45234  0.03671  0.28328  222 HIS A O   
1495 C CB  . HIS A 186 ? 1.06029 0.94695 0.93057 0.40048  0.05328  0.23677  222 HIS A CB  
1496 C CG  . HIS A 186 ? 1.21128 1.11985 1.03997 0.38504  0.04018  0.22572  222 HIS A CG  
1497 N ND1 . HIS A 186 ? 1.22527 1.17934 1.02956 0.38807  0.02560  0.24289  222 HIS A ND1 
1498 C CD2 . HIS A 186 ? 1.20657 1.09690 1.01431 0.36695  0.03932  0.19807  222 HIS A CD2 
1499 C CE1 . HIS A 186 ? 1.28712 1.25027 1.05935 0.37326  0.01832  0.22371  222 HIS A CE1 
1500 N NE2 . HIS A 186 ? 1.24415 1.16848 1.02035 0.36085  0.02523  0.19802  222 HIS A NE2 
1501 N N   . LEU A 187 ? 1.10785 0.98784 1.08174 0.44138  0.07311  0.24041  223 LEU A N   
1502 C CA  . LEU A 187 ? 1.28636 1.15274 1.30827 0.46293  0.08319  0.25734  223 LEU A CA  
1503 C C   . LEU A 187 ? 1.27981 1.19980 1.34512 0.48336  0.07573  0.25490  223 LEU A C   
1504 O O   . LEU A 187 ? 1.22643 1.13705 1.33967 0.50358  0.08506  0.26425  223 LEU A O   
1505 C CB  . LEU A 187 ? 1.23765 1.02949 1.27310 0.45591  0.11109  0.23719  223 LEU A CB  
1506 C CG  . LEU A 187 ? 1.29616 1.03550 1.29973 0.43451  0.11812  0.23972  223 LEU A CG  
1507 C CD1 . LEU A 187 ? 1.23520 0.90376 1.25514 0.42579  0.14212  0.21637  223 LEU A CD1 
1508 C CD2 . LEU A 187 ? 1.35623 1.10415 1.35744 0.44269  0.10959  0.28230  223 LEU A CD2 
1509 N N   . GLY A 188 ? 1.23374 1.21032 1.28871 0.47862  0.05912  0.24173  224 GLY A N   
1510 C CA  . GLY A 188 ? 1.16821 1.20359 1.27102 0.49561  0.05119  0.23900  224 GLY A CA  
1511 C C   . GLY A 188 ? 1.15381 1.16805 1.29475 0.50100  0.07912  0.21120  224 GLY A C   
1512 O O   . GLY A 188 ? 1.38058 1.43148 1.57812 0.52073  0.08091  0.21353  224 GLY A O   
1513 N N   . ARG A 189 ? 1.11931 1.07726 1.23062 0.48330  0.10133  0.18341  225 ARG A N   
1514 C CA  . ARG A 189 ? 1.23542 1.17037 1.37141 0.48484  0.13138  0.15222  225 ARG A CA  
1515 C C   . ARG A 189 ? 1.23837 1.21652 1.36752 0.47545  0.13190  0.12818  225 ARG A C   
1516 O O   . ARG A 189 ? 1.30058 1.30669 1.39590 0.46296  0.11010  0.12969  225 ARG A O   
1517 C CB  . ARG A 189 ? 1.16040 1.01087 1.26496 0.46809  0.15466  0.13189  225 ARG A CB  
1518 C CG  . ARG A 189 ? 1.24290 1.04838 1.34141 0.46843  0.15062  0.15638  225 ARG A CG  
1519 C CD  . ARG A 189 ? 1.38109 1.11051 1.47842 0.45882  0.17713  0.13228  225 ARG A CD  
1520 N NE  . ARG A 189 ? 1.45613 1.13603 1.51476 0.43702  0.17366  0.13618  225 ARG A NE  
1521 C CZ  . ARG A 189 ? 1.42297 1.03717 1.47706 0.42354  0.19087  0.11602  225 ARG A CZ  
1522 N NH1 . ARG A 189 ? 1.33813 0.92433 1.41771 0.42973  0.21351  0.08844  225 ARG A NH1 
1523 N NH2 . ARG A 189 ? 1.29224 0.87066 1.31732 0.40261  0.18524  0.12138  225 ARG A NH2 
1524 N N   . GLU A 190 ? 1.47799 1.46248 1.64146 0.48124  0.15873  0.10454  226 GLU A N   
1525 C CA  . GLU A 190 ? 1.35894 1.38159 1.51775 0.47053  0.16684  0.08110  226 GLU A CA  
1526 C C   . GLU A 190 ? 1.36377 1.33470 1.45107 0.44395  0.17259  0.05968  226 GLU A C   
1527 O O   . GLU A 190 ? 1.35042 1.24923 1.40510 0.43256  0.18858  0.04624  226 GLU A O   
1528 C CB  . GLU A 190 ? 1.31429 1.34986 1.52080 0.47919  0.20173  0.05849  226 GLU A CB  
1529 C CG  . GLU A 190 ? 1.35565 1.43672 1.56190 0.46608  0.21657  0.03644  226 GLU A CG  
1530 C CD  . GLU A 190 ? 1.38346 1.56270 1.64767 0.47638  0.19391  0.05324  226 GLU A CD  
1531 O OE1 . GLU A 190 ? 1.42401 1.64441 1.75806 0.49648  0.19618  0.06195  226 GLU A OE1 
1532 O OE2 . GLU A 190 ? 1.32871 1.54035 1.56742 0.45220  0.16717  0.05378  226 GLU A OE2 
1533 N N   . GLN A 191 ? 1.03010 1.03933 1.09420 0.42097  0.15209  0.05414  227 GLN A N   
1534 C CA  . GLN A 191 ? 1.00145 0.96823 1.00026 0.38066  0.14677  0.03441  227 GLN A CA  
1535 C C   . GLN A 191 ? 0.87650 0.83349 0.86177 0.35809  0.17441  0.00465  227 GLN A C   
1536 O O   . GLN A 191 ? 0.80991 0.81509 0.83753 0.36530  0.19099  -0.00091 227 GLN A O   
1537 C CB  . GLN A 191 ? 0.94148 0.94850 0.92315 0.35953  0.10941  0.04135  227 GLN A CB  
1538 C CG  . GLN A 191 ? 1.00502 1.03127 0.99162 0.37980  0.08254  0.06923  227 GLN A CG  
1539 C CD  . GLN A 191 ? 1.05313 1.11661 1.01976 0.35784  0.04877  0.06796  227 GLN A CD  
1540 O OE1 . GLN A 191 ? 1.04133 1.08249 0.97424 0.32564  0.04386  0.04977  227 GLN A OE1 
1541 N NE2 . GLN A 191 ? 0.93212 1.05270 0.92014 0.37562  0.02441  0.08675  227 GLN A NE2 
1542 N N   . SER A 192 ? 0.76590 0.66324 0.69175 0.33007  0.17934  -0.01334 228 SER A N   
1543 C CA  . SER A 192 ? 1.05756 0.94113 0.95288 0.30422  0.20302  -0.03972 228 SER A CA  
1544 C C   . SER A 192 ? 0.83821 0.69163 0.67161 0.26522  0.18029  -0.04493 228 SER A C   
1545 O O   . SER A 192 ? 0.91967 0.78257 0.74859 0.25808  0.14771  -0.03011 228 SER A O   
1546 C CB  . SER A 192 ? 0.86483 0.69855 0.75522 0.31795  0.24206  -0.06133 228 SER A CB  
1547 O OG  . SER A 192 ? 0.90260 0.66637 0.75606 0.31363  0.23622  -0.06550 228 SER A OG  
1548 N N   . ARG A 193 ? 0.87811 0.69617 0.66314 0.24034  0.19756  -0.06652 229 ARG A N   
1549 C CA  . ARG A 193 ? 0.92762 0.71820 0.65677 0.20424  0.17426  -0.06858 229 ARG A CA  
1550 C C   . ARG A 193 ? 0.96015 0.70216 0.66966 0.20441  0.15353  -0.06461 229 ARG A C   
1551 O O   . ARG A 193 ? 1.01357 0.75377 0.70821 0.18707  0.12325  -0.05472 229 ARG A O   
1552 C CB  . ARG A 193 ? 1.06502 0.83141 0.74132 0.17846  0.19653  -0.09015 229 ARG A CB  
1553 C CG  . ARG A 193 ? 1.12839 0.94534 0.81554 0.16666  0.21323  -0.08905 229 ARG A CG  
1554 C CD  . ARG A 193 ? 1.14586 0.94031 0.77466 0.14425  0.24262  -0.11033 229 ARG A CD  
1555 N NE  . ARG A 193 ? 1.10544 0.87973 0.73921 0.16677  0.28220  -0.13600 229 ARG A NE  
1556 C CZ  . ARG A 193 ? 1.36788 1.13436 0.96318 0.15611  0.31982  -0.16072 229 ARG A CZ  
1557 N NH1 . ARG A 193 ? 1.28758 1.06655 0.83164 0.12218  0.32322  -0.15867 229 ARG A NH1 
1558 N NH2 . ARG A 193 ? 1.35038 1.09505 0.95859 0.18022  0.35643  -0.18778 229 ARG A NH2 
1559 N N   . ARG A 194 ? 0.87168 0.57415 0.58745 0.22406  0.17100  -0.07210 230 ARG A N   
1560 C CA  . ARG A 194 ? 0.91177 0.56610 0.61249 0.22083  0.15550  -0.06878 230 ARG A CA  
1561 C C   . ARG A 194 ? 1.07300 0.75280 0.79984 0.23145  0.12830  -0.04147 230 ARG A C   
1562 O O   . ARG A 194 ? 1.07057 0.72297 0.78192 0.21980  0.11039  -0.03679 230 ARG A O   
1563 C CB  . ARG A 194 ? 1.17746 0.78467 0.89152 0.24164  0.18205  -0.07995 230 ARG A CB  
1564 C CG  . ARG A 194 ? 1.11955 0.75126 0.89374 0.28255  0.19326  -0.05907 230 ARG A CG  
1565 C CD  . ARG A 194 ? 1.20251 0.78161 0.99771 0.30127  0.21672  -0.06610 230 ARG A CD  
1566 N NE  . ARG A 194 ? 1.25368 0.86887 1.11357 0.33391  0.22034  -0.04034 230 ARG A NE  
1567 C CZ  . ARG A 194 ? 1.28814 0.88034 1.18716 0.34615  0.23156  -0.03693 230 ARG A CZ  
1568 N NH1 . ARG A 194 ? 1.26786 0.80226 1.15257 0.32946  0.24170  -0.05994 230 ARG A NH1 
1569 N NH2 . ARG A 194 ? 1.25954 0.88841 1.21418 0.37536  0.23014  -0.01016 230 ARG A NH2 
1570 N N   . ASP A 195 ? 0.95983 0.69472 0.72613 0.25252  0.12500  -0.02477 231 ASP A N   
1571 C CA  . ASP A 195 ? 0.87270 0.63383 0.65646 0.26354  0.10077  -0.00153 231 ASP A CA  
1572 C C   . ASP A 195 ? 1.02644 0.81145 0.79388 0.23824  0.07289  -0.00202 231 ASP A C   
1573 O O   . ASP A 195 ? 0.90205 0.68760 0.66636 0.23736  0.05402  0.00827  231 ASP A O   
1574 C CB  . ASP A 195 ? 0.90089 0.71376 0.73156 0.29640  0.10367  0.01654  231 ASP A CB  
1575 C CG  . ASP A 195 ? 1.20776 0.99226 1.06249 0.32809  0.12262  0.02946  231 ASP A CG  
1576 O OD1 . ASP A 195 ? 1.05511 0.77785 0.89034 0.32234  0.13292  0.02331  231 ASP A OD1 
1577 O OD2 . ASP A 195 ? 0.98500 0.80861 0.88244 0.35843  0.12604  0.04662  231 ASP A OD2 
1578 N N   . ASP A 196 ? 0.90437 0.70842 0.66394 0.21788  0.07208  -0.01323 232 ASP A N   
1579 C CA  . ASP A 196 ? 0.91600 0.72935 0.66190 0.19188  0.04670  -0.01419 232 ASP A CA  
1580 C C   . ASP A 196 ? 0.90347 0.66599 0.61524 0.17261  0.03606  -0.01882 232 ASP A C   
1581 O O   . ASP A 196 ? 1.06117 0.82545 0.77301 0.16256  0.01334  -0.01487 232 ASP A O   
1582 C CB  . ASP A 196 ? 0.83417 0.67029 0.57854 0.17186  0.05114  -0.02109 232 ASP A CB  
1583 C CG  . ASP A 196 ? 0.84010 0.73796 0.62948 0.18522  0.05403  -0.01627 232 ASP A CG  
1584 O OD1 . ASP A 196 ? 0.74543 0.67410 0.56197 0.20486  0.04071  -0.00717 232 ASP A OD1 
1585 O OD2 . ASP A 196 ? 0.78671 0.70544 0.58396 0.17475  0.06939  -0.02113 232 ASP A OD2 
1586 N N   . LEU A 197 ? 0.97664 0.69529 0.66244 0.16716  0.05213  -0.02957 233 LEU A N   
1587 C CA  . LEU A 197 ? 1.02378 0.69787 0.67990 0.14643  0.03951  -0.03551 233 LEU A CA  
1588 C C   . LEU A 197 ? 1.01407 0.66967 0.68575 0.15854  0.03421  -0.02710 233 LEU A C   
1589 O O   . LEU A 197 ? 1.15943 0.80003 0.82577 0.14333  0.01523  -0.02582 233 LEU A O   
1590 C CB  . LEU A 197 ? 1.01492 0.65063 0.63426 0.13377  0.05723  -0.05424 233 LEU A CB  
1591 C CG  . LEU A 197 ? 1.13007 0.77172 0.71342 0.10983  0.05967  -0.06249 233 LEU A CG  
1592 C CD1 . LEU A 197 ? 1.18909 0.82350 0.75090 0.08212  0.02758  -0.05498 233 LEU A CD1 
1593 C CD2 . LEU A 197 ? 0.97217 0.66244 0.57872 0.11840  0.07358  -0.05686 233 LEU A CD2 
1594 N N   . GLU A 198 ? 0.98348 0.64116 0.67796 0.18586  0.05129  -0.01872 234 GLU A N   
1595 C CA  . GLU A 198 ? 1.05720 0.70157 0.76669 0.19705  0.04844  -0.00448 234 GLU A CA  
1596 C C   . GLU A 198 ? 1.00123 0.68723 0.72333 0.20040  0.02891  0.00890  234 GLU A C   
1597 O O   . GLU A 198 ? 0.80552 0.48232 0.53031 0.19541  0.02032  0.01499  234 GLU A O   
1598 C CB  . GLU A 198 ? 0.85293 0.48720 0.58402 0.22649  0.07136  0.00675  234 GLU A CB  
1599 C CG  . GLU A 198 ? 1.11740 0.73719 0.86278 0.23772  0.07166  0.02775  234 GLU A CG  
1600 C CD  . GLU A 198 ? 1.22343 0.83459 0.99394 0.26930  0.09199  0.04670  234 GLU A CD  
1601 O OE1 . GLU A 198 ? 1.08480 0.68659 0.86467 0.28108  0.10939  0.03673  234 GLU A OE1 
1602 O OE2 . GLU A 198 ? 1.15373 0.77219 0.93751 0.28018  0.09098  0.07236  234 GLU A OE2 
1603 N N   . ALA A 199 ? 0.91362 0.64724 0.64589 0.20783  0.02299  0.01101  235 ALA A N   
1604 C CA  . ALA A 199 ? 1.04877 0.82121 0.78966 0.20779  0.00364  0.01590  235 ALA A CA  
1605 C C   . ALA A 199 ? 0.84945 0.60831 0.58165 0.18159  -0.01431 0.00499  235 ALA A C   
1606 O O   . ALA A 199 ? 0.78833 0.55611 0.52716 0.18068  -0.02511 0.00679  235 ALA A O   
1607 C CB  . ALA A 199 ? 0.90889 0.73393 0.66576 0.21604  -0.00136 0.01551  235 ALA A CB  
1608 N N   . LEU A 200 ? 0.98751 0.72592 0.70529 0.16090  -0.01695 -0.00535 236 LEU A N   
1609 C CA  . LEU A 200 ? 0.94711 0.66824 0.65908 0.13734  -0.03630 -0.01067 236 LEU A CA  
1610 C C   . LEU A 200 ? 1.06397 0.75347 0.77630 0.13373  -0.03825 -0.00908 236 LEU A C   
1611 O O   . LEU A 200 ? 0.77807 0.46694 0.50295 0.12362  -0.05481 -0.00976 236 LEU A O   
1612 C CB  . LEU A 200 ? 0.98467 0.68916 0.67314 0.11598  -0.03837 -0.01669 236 LEU A CB  
1613 C CG  . LEU A 200 ? 0.88903 0.62426 0.58246 0.11013  -0.03946 -0.01670 236 LEU A CG  
1614 C CD1 . LEU A 200 ? 1.00834 0.72422 0.66924 0.08983  -0.03365 -0.01936 236 LEU A CD1 
1615 C CD2 . LEU A 200 ? 0.91464 0.66786 0.63112 0.10182  -0.06210 -0.01541 236 LEU A CD2 
1616 N N   . GLY A 201 ? 0.94057 0.60369 0.64612 0.14171  -0.02070 -0.00751 237 GLY A N   
1617 C CA  . GLY A 201 ? 0.82275 0.45696 0.53575 0.13612  -0.02099 -0.00559 237 GLY A CA  
1618 C C   . GLY A 201 ? 0.92483 0.58115 0.66148 0.14926  -0.02008 0.00659  237 GLY A C   
1619 O O   . GLY A 201 ? 0.79000 0.43894 0.54217 0.13927  -0.02748 0.00699  237 GLY A O   
1620 N N   . HIS A 202 ? 0.87375 0.56138 0.61350 0.17150  -0.01091 0.01672  238 HIS A N   
1621 C CA  . HIS A 202 ? 0.63128 0.34491 0.38263 0.18366  -0.00889 0.02794  238 HIS A CA  
1622 C C   . HIS A 202 ? 0.97549 0.71517 0.73633 0.17389  -0.02671 0.01622  238 HIS A C   
1623 O O   . HIS A 202 ? 0.92312 0.67337 0.69615 0.17520  -0.02490 0.01822  238 HIS A O   
1624 C CB  . HIS A 202 ? 0.87397 0.61862 0.62067 0.20939  0.00073  0.04266  238 HIS A CB  
1625 C CG  . HIS A 202 ? 0.97443 0.69227 0.72133 0.22390  0.01966  0.05692  238 HIS A CG  
1626 N ND1 . HIS A 202 ? 1.11181 0.85011 0.86050 0.24488  0.02555  0.06579  238 HIS A ND1 
1627 C CD2 . HIS A 202 ? 1.06143 0.73260 0.81363 0.22075  0.03408  0.06281  238 HIS A CD2 
1628 C CE1 . HIS A 202 ? 0.99934 0.70214 0.75510 0.25642  0.04408  0.07703  238 HIS A CE1 
1629 N NE2 . HIS A 202 ? 1.15891 0.81824 0.91542 0.24096  0.04983  0.07437  238 HIS A NE2 
1630 N N   . VAL A 203 ? 0.89543 0.64463 0.65410 0.16404  -0.04151 0.00395  239 VAL A N   
1631 C CA  . VAL A 203 ? 0.93776 0.70467 0.71211 0.15492  -0.05849 -0.00808 239 VAL A CA  
1632 C C   . VAL A 203 ? 0.95633 0.69727 0.74775 0.13864  -0.06835 -0.01121 239 VAL A C   
1633 O O   . VAL A 203 ? 0.99096 0.74464 0.80628 0.13780  -0.07473 -0.01804 239 VAL A O   
1634 C CB  . VAL A 203 ? 0.89104 0.67058 0.66359 0.14671  -0.07075 -0.01647 239 VAL A CB  
1635 C CG1 . VAL A 203 ? 0.84486 0.63626 0.64003 0.13767  -0.08787 -0.02937 239 VAL A CG1 
1636 C CG2 . VAL A 203 ? 0.93382 0.74655 0.69911 0.16277  -0.06275 -0.01347 239 VAL A CG2 
1637 N N   . PHE A 204 ? 0.90126 0.60795 0.68316 0.12578  -0.07020 -0.00816 240 PHE A N   
1638 C CA  . PHE A 204 ? 0.94858 0.63552 0.74955 0.10915  -0.08473 -0.00991 240 PHE A CA  
1639 C C   . PHE A 204 ? 0.99414 0.68639 0.82217 0.11524  -0.07374 -0.00600 240 PHE A C   
1640 O O   . PHE A 204 ? 1.07890 0.78219 0.94042 0.11151  -0.08293 -0.01011 240 PHE A O   
1641 C CB  . PHE A 204 ? 0.92882 0.58085 0.70641 0.09260  -0.09003 -0.01018 240 PHE A CB  
1642 C CG  . PHE A 204 ? 0.94596 0.59465 0.69271 0.08509  -0.09566 -0.01270 240 PHE A CG  
1643 C CD1 . PHE A 204 ? 0.95655 0.62672 0.71050 0.08466  -0.10624 -0.01283 240 PHE A CD1 
1644 C CD2 . PHE A 204 ? 0.98266 0.60641 0.69495 0.07742  -0.08767 -0.01644 240 PHE A CD2 
1645 C CE1 . PHE A 204 ? 0.95007 0.61921 0.67918 0.07558  -0.10816 -0.01216 240 PHE A CE1 
1646 C CE2 . PHE A 204 ? 1.06907 0.69373 0.75200 0.06987  -0.08784 -0.01839 240 PHE A CE2 
1647 C CZ  . PHE A 204 ? 0.89093 0.53950 0.58316 0.06838  -0.09778 -0.01399 240 PHE A CZ  
1648 N N   . PHE A 205 ? 0.86726 0.55247 0.68548 0.12542  -0.05188 0.00344  241 PHE A N   
1649 C CA  . PHE A 205 ? 1.00158 0.69420 0.84409 0.13047  -0.03660 0.01158  241 PHE A CA  
1650 C C   . PHE A 205 ? 1.03683 0.77011 0.88783 0.14440  -0.03070 0.00896  241 PHE A C   
1651 O O   . PHE A 205 ? 1.06140 0.80809 0.94009 0.14429  -0.02211 0.00942  241 PHE A O   
1652 C CB  . PHE A 205 ? 1.09079 0.76449 0.92024 0.13948  -0.01338 0.02708  241 PHE A CB  
1653 C CG  . PHE A 205 ? 1.06908 0.69861 0.89640 0.12395  -0.01525 0.02401  241 PHE A CG  
1654 C CD1 . PHE A 205 ? 1.16777 0.77962 1.02500 0.10583  -0.01883 0.02239  241 PHE A CD1 
1655 C CD2 . PHE A 205 ? 1.01031 0.61830 0.80814 0.12672  -0.01267 0.01988  241 PHE A CD2 
1656 C CE1 . PHE A 205 ? 1.26086 0.83220 1.11374 0.08889  -0.02282 0.01458  241 PHE A CE1 
1657 C CE2 . PHE A 205 ? 1.16667 0.73270 0.95794 0.11169  -0.01265 0.01091  241 PHE A CE2 
1658 C CZ  . PHE A 205 ? 1.23591 0.78250 1.05229 0.09183  -0.01917 0.00722  241 PHE A CZ  
1659 N N   . TYR A 206 ? 1.01417 0.76965 0.84303 0.15534  -0.03419 0.00383  242 TYR A N   
1660 C CA  . TYR A 206 ? 0.95537 0.74950 0.78751 0.16603  -0.03158 -0.00577 242 TYR A CA  
1661 C C   . TYR A 206 ? 1.00488 0.80270 0.87288 0.15593  -0.04619 -0.02406 242 TYR A C   
1662 O O   . TYR A 206 ? 0.83652 0.65819 0.72235 0.16201  -0.03720 -0.03400 242 TYR A O   
1663 C CB  . TYR A 206 ? 0.86679 0.68406 0.67213 0.17619  -0.03704 -0.00992 242 TYR A CB  
1664 C CG  . TYR A 206 ? 0.89592 0.75173 0.70202 0.18274  -0.04059 -0.02820 242 TYR A CG  
1665 C CD1 . TYR A 206 ? 1.00973 0.89734 0.79704 0.19726  -0.02497 -0.02447 242 TYR A CD1 
1666 C CD2 . TYR A 206 ? 0.87227 0.73132 0.69553 0.17336  -0.05930 -0.04949 242 TYR A CD2 
1667 C CE1 . TYR A 206 ? 0.95040 0.87390 0.73221 0.20174  -0.02824 -0.04708 242 TYR A CE1 
1668 C CE2 . TYR A 206 ? 0.93611 0.82631 0.76240 0.17785  -0.06231 -0.07198 242 TYR A CE2 
1669 C CZ  . TYR A 206 ? 1.01910 0.94246 0.82260 0.19183  -0.04694 -0.07350 242 TYR A CZ  
1670 O OH  . TYR A 206 ? 1.15465 1.10967 0.95533 0.19482  -0.04996 -0.10156 242 TYR A OH  
1671 N N   . PHE A 207 ? 0.94470 0.71917 0.82403 0.14121  -0.06777 -0.02783 243 PHE A N   
1672 C CA  . PHE A 207 ? 0.94794 0.72190 0.86803 0.13314  -0.08471 -0.03992 243 PHE A CA  
1673 C C   . PHE A 207 ? 0.98144 0.74997 0.94120 0.12766  -0.08196 -0.03560 243 PHE A C   
1674 O O   . PHE A 207 ? 0.97192 0.75657 0.97420 0.13113  -0.08146 -0.04666 243 PHE A O   
1675 C CB  . PHE A 207 ? 0.80395 0.55523 0.72035 0.11863  -0.10996 -0.03837 243 PHE A CB  
1676 C CG  . PHE A 207 ? 0.81390 0.57589 0.70982 0.12096  -0.11406 -0.04547 243 PHE A CG  
1677 C CD1 . PHE A 207 ? 0.98105 0.77399 0.87423 0.13427  -0.10364 -0.05931 243 PHE A CD1 
1678 C CD2 . PHE A 207 ? 0.77585 0.51983 0.65503 0.10785  -0.12832 -0.03878 243 PHE A CD2 
1679 C CE1 . PHE A 207 ? 0.88643 0.69268 0.76762 0.13369  -0.10999 -0.06754 243 PHE A CE1 
1680 C CE2 . PHE A 207 ? 0.78912 0.54605 0.65770 0.10755  -0.13053 -0.04443 243 PHE A CE2 
1681 C CZ  . PHE A 207 ? 0.79680 0.58518 0.67005 0.12008  -0.12270 -0.05944 243 PHE A CZ  
1682 N N   . LEU A 208 ? 0.94600 0.69282 0.89803 0.11864  -0.07956 -0.02187 244 LEU A N   
1683 C CA  . LEU A 208 ? 0.95922 0.70250 0.95568 0.10916  -0.08065 -0.01795 244 LEU A CA  
1684 C C   . LEU A 208 ? 0.99335 0.76292 1.01101 0.12022  -0.05083 -0.01683 244 LEU A C   
1685 O O   . LEU A 208 ? 0.94557 0.73390 1.01507 0.12015  -0.04859 -0.02338 244 LEU A O   
1686 C CB  . LEU A 208 ? 0.94397 0.65541 0.92463 0.09380  -0.08601 -0.00784 244 LEU A CB  
1687 C CG  . LEU A 208 ? 1.04187 0.72727 0.98693 0.08169  -0.10937 -0.00866 244 LEU A CG  
1688 C CD1 . LEU A 208 ? 1.02607 0.68328 0.93353 0.07667  -0.09765 -0.00449 244 LEU A CD1 
1689 C CD2 . LEU A 208 ? 0.96895 0.64744 0.94490 0.06433  -0.14128 -0.00880 244 LEU A CD2 
1690 N N   . ARG A 209 ? 0.88935 0.66207 0.86900 0.13032  -0.02662 -0.00647 245 ARG A N   
1691 C CA  . ARG A 209 ? 0.96638 0.76241 0.95616 0.13891  0.00445  0.00124  245 ARG A CA  
1692 C C   . ARG A 209 ? 0.96451 0.79903 0.94745 0.15447  0.01611  -0.01379 245 ARG A C   
1693 O O   . ARG A 209 ? 0.93634 0.79687 0.93423 0.16001  0.04190  -0.01287 245 ARG A O   
1694 C CB  . ARG A 209 ? 1.05435 0.83591 1.00548 0.14426  0.02440  0.02382  245 ARG A CB  
1695 C CG  . ARG A 209 ? 1.06199 0.80038 1.01489 0.12941  0.01556  0.03279  245 ARG A CG  
1696 C CD  . ARG A 209 ? 1.13095 0.85052 1.04825 0.13912  0.03486  0.05352  245 ARG A CD  
1697 N NE  . ARG A 209 ? 1.13025 0.86910 1.04918 0.14892  0.06530  0.07375  245 ARG A NE  
1698 C CZ  . ARG A 209 ? 1.30403 1.03032 1.25463 0.13840  0.08422  0.08915  245 ARG A CZ  
1699 N NH1 . ARG A 209 ? 1.38752 1.08239 1.37336 0.11721  0.07357  0.08350  245 ARG A NH1 
1700 N NH2 . ARG A 209 ? 1.14149 0.88890 1.08749 0.14753  0.11429  0.11105  245 ARG A NH2 
1701 N N   . GLY A 210 ? 0.95290 0.79234 0.91394 0.15993  -0.00081 -0.02934 246 GLY A N   
1702 C CA  . GLY A 210 ? 1.01436 0.88801 0.96066 0.17312  0.00859  -0.04797 246 GLY A CA  
1703 C C   . GLY A 210 ? 1.01247 0.90532 0.90069 0.18610  0.02414  -0.03613 246 GLY A C   
1704 O O   . GLY A 210 ? 1.00814 0.92721 0.87013 0.19485  0.02144  -0.05310 246 GLY A O   
1705 N N   . GLN A 211 ? 0.97353 0.85324 0.84373 0.18720  0.03831  -0.00691 247 GLN A N   
1706 C CA  . GLN A 211 ? 1.10773 1.00283 0.92663 0.20144  0.05019  0.01244  247 GLN A CA  
1707 C C   . GLN A 211 ? 1.07182 0.93036 0.88370 0.19982  0.05167  0.04099  247 GLN A C   
1708 O O   . GLN A 211 ? 1.16386 0.98809 1.00665 0.18581  0.04804  0.04382  247 GLN A O   
1709 C CB  . GLN A 211 ? 1.16326 1.09220 0.96618 0.21017  0.08001  0.02084  247 GLN A CB  
1710 C CG  . GLN A 211 ? 1.31294 1.28412 1.06234 0.22513  0.08133  0.01497  247 GLN A CG  
1711 C CD  . GLN A 211 ? 1.38536 1.38912 1.10729 0.23256  0.11358  0.02932  247 GLN A CD  
1712 O OE1 . GLN A 211 ? 1.35925 1.34926 1.08496 0.23137  0.13551  0.06314  247 GLN A OE1 
1713 N NE2 . GLN A 211 ? 1.39504 1.44146 1.08809 0.23876  0.11790  0.00292  247 GLN A NE2 
1714 N N   . LEU A 212 ? 1.17447 1.04129 0.94719 0.21470  0.05576  0.06069  248 LEU A N   
1715 C CA  . LEU A 212 ? 1.15199 0.98449 0.91999 0.21811  0.06263  0.08876  248 LEU A CA  
1716 C C   . LEU A 212 ? 1.05651 0.89962 0.80413 0.23095  0.08817  0.12347  248 LEU A C   
1717 O O   . LEU A 212 ? 1.26269 1.14876 0.97888 0.24258  0.09389  0.12699  248 LEU A O   
1718 C CB  . LEU A 212 ? 1.02671 0.85618 0.77585 0.22714  0.04537  0.08723  248 LEU A CB  
1719 C CG  . LEU A 212 ? 1.07709 0.87711 0.84461 0.21184  0.02674  0.06606  248 LEU A CG  
1720 C CD1 . LEU A 212 ? 1.13405 0.94908 0.88495 0.21991  0.01168  0.05881  248 LEU A CD1 
1721 C CD2 . LEU A 212 ? 1.18267 0.93218 0.96588 0.20220  0.03487  0.07645  248 LEU A CD2 
1722 N N   . PRO A 213 ? 1.12202 0.92583 0.88507 0.22803  0.10380  0.14990  249 PRO A N   
1723 C CA  . PRO A 213 ? 1.14698 0.95654 0.89475 0.23818  0.13039  0.18913  249 PRO A CA  
1724 C C   . PRO A 213 ? 1.22397 1.06094 0.92649 0.26299  0.12721  0.21345  249 PRO A C   
1725 O O   . PRO A 213 ? 1.20828 1.06851 0.88370 0.27281  0.14528  0.24406  249 PRO A O   
1726 C CB  . PRO A 213 ? 1.16431 0.91539 0.94593 0.22823  0.14267  0.20810  249 PRO A CB  
1727 C CG  . PRO A 213 ? 1.18173 0.90152 0.97537 0.22232  0.12004  0.18255  249 PRO A CG  
1728 C CD  . PRO A 213 ? 1.10241 0.85318 0.89509 0.21445  0.09823  0.14524  249 PRO A CD  
1729 N N   . TRP A 214 ? 1.28657 1.12539 0.98081 0.27303  0.10474  0.20280  250 TRP A N   
1730 C CA  . TRP A 214 ? 1.21430 1.08691 0.87351 0.29717  0.09640  0.22488  250 TRP A CA  
1731 C C   . TRP A 214 ? 1.39879 1.33077 1.02832 0.29944  0.07752  0.19716  250 TRP A C   
1732 O O   . TRP A 214 ? 1.40751 1.36459 1.02754 0.30974  0.05582  0.18911  250 TRP A O   
1733 C CB  . TRP A 214 ? 1.16112 1.00586 0.83703 0.30852  0.08597  0.23127  250 TRP A CB  
1734 C CG  . TRP A 214 ? 1.22414 1.05358 0.92170 0.29431  0.06930  0.19096  250 TRP A CG  
1735 C CD1 . TRP A 214 ? 1.12786 0.99289 0.81813 0.29287  0.04705  0.16239  250 TRP A CD1 
1736 C CD2 . TRP A 214 ? 1.18943 0.96416 0.91688 0.27787  0.07343  0.17647  250 TRP A CD2 
1737 N NE1 . TRP A 214 ? 1.17382 1.00927 0.88619 0.27707  0.03898  0.13542  250 TRP A NE1 
1738 C CE2 . TRP A 214 ? 1.07489 0.85651 0.80627 0.26793  0.05380  0.14251  250 TRP A CE2 
1739 C CE3 . TRP A 214 ? 1.26295 0.98387 1.01340 0.26866  0.09115  0.18827  250 TRP A CE3 
1740 C CZ2 . TRP A 214 ? 1.11180 0.85118 0.86095 0.25026  0.05096  0.12208  250 TRP A CZ2 
1741 C CZ3 . TRP A 214 ? 1.18736 0.86658 0.95810 0.25029  0.08632  0.16275  250 TRP A CZ3 
1742 C CH2 . TRP A 214 ? 0.99917 0.68913 0.76512 0.24179  0.06619  0.13095  250 TRP A CH2 
1743 N N   . GLN A 215 ? 1.43306 1.38883 1.05219 0.28911  0.08718  0.18026  251 GLN A N   
1744 C CA  . GLN A 215 ? 1.34567 1.35567 0.93440 0.29042  0.07401  0.15097  251 GLN A CA  
1745 C C   . GLN A 215 ? 1.42863 1.47633 0.97173 0.29779  0.09424  0.17131  251 GLN A C   
1746 O O   . GLN A 215 ? 1.44173 1.47491 0.99358 0.29063  0.12274  0.18615  251 GLN A O   
1747 C CB  . GLN A 215 ? 1.44552 1.45067 1.06513 0.27169  0.06771  0.10326  251 GLN A CB  
1748 C CG  . GLN A 215 ? 1.53229 1.50701 1.18697 0.26258  0.04570  0.08290  251 GLN A CG  
1749 C CD  . GLN A 215 ? 1.40218 1.37902 1.08268 0.24712  0.03446  0.03985  251 GLN A CD  
1750 O OE1 . GLN A 215 ? 1.25656 1.19849 0.97260 0.23397  0.02579  0.02871  251 GLN A OE1 
1751 N NE2 . GLN A 215 ? 1.34634 1.36356 1.00814 0.24886  0.03401  0.01536  251 GLN A NE2 
1752 N N   . GLY A 216 ? 1.38202 1.48101 0.87604 0.31066  0.07951  0.17236  252 GLY A N   
1753 C CA  . GLY A 216 ? 1.37846 1.51948 0.82221 0.31452  0.09559  0.18677  252 GLY A CA  
1754 C C   . GLY A 216 ? 1.51572 1.65205 0.95534 0.32099  0.10466  0.24049  252 GLY A C   
1755 O O   . GLY A 216 ? 1.58838 1.73900 1.00279 0.31721  0.12856  0.25998  252 GLY A O   
1756 N N   . LEU A 217 ? 1.46045 1.57753 0.92684 0.33008  0.08802  0.26348  253 LEU A N   
1757 C CA  . LEU A 217 ? 1.54976 1.66023 1.01800 0.33746  0.09502  0.31245  253 LEU A CA  
1758 C C   . LEU A 217 ? 1.61164 1.77972 1.04169 0.34203  0.07471  0.31770  253 LEU A C   
1759 O O   . LEU A 217 ? 1.65045 1.85737 1.06844 0.34077  0.04865  0.28363  253 LEU A O   
1760 C CB  . LEU A 217 ? 1.43878 1.50493 0.95617 0.34558  0.08824  0.33041  253 LEU A CB  
1761 C CG  . LEU A 217 ? 1.36943 1.37068 0.92784 0.33920  0.10442  0.32637  253 LEU A CG  
1762 C CD1 . LEU A 217 ? 1.38248 1.36143 0.93501 0.32801  0.13690  0.33824  253 LEU A CD1 
1763 C CD2 . LEU A 217 ? 1.33911 1.33573 0.90910 0.33599  0.08586  0.28352  253 LEU A CD2 
1764 N N   . LYS A 218 ? 1.66798 1.83944 1.07977 0.34576  0.08598  0.36162  254 LYS A N   
1765 C CA  . LYS A 218 ? 1.80801 2.03010 1.17719 0.34979  0.06715  0.37469  254 LYS A CA  
1766 C C   . LYS A 218 ? 1.96487 2.17979 1.36091 0.36518  0.04831  0.41029  254 LYS A C   
1767 O O   . LYS A 218 ? 2.07905 2.24863 1.50801 0.37139  0.06388  0.44664  254 LYS A O   
1768 C CB  . LYS A 218 ? 1.92728 2.16248 1.24849 0.34288  0.09193  0.40120  254 LYS A CB  
1769 C CG  . LYS A 218 ? 1.77980 2.02487 1.07726 0.32798  0.11642  0.36648  254 LYS A CG  
1770 C CD  . LYS A 218 ? 1.75330 2.03504 1.03636 0.32254  0.09365  0.30665  254 LYS A CD  
1771 C CE  . LYS A 218 ? 1.71741 1.99605 0.99914 0.31037  0.11882  0.26617  254 LYS A CE  
1772 N NZ  . LYS A 218 ? 1.68054 1.97511 0.97244 0.30629  0.09564  0.20714  254 LYS A NZ  
1773 N N   . ALA A 219 ? 1.97333 2.23309 1.35887 0.37059  0.01501  0.39822  255 ALA A N   
1774 C CA  . ALA A 219 ? 1.89017 2.15246 1.30068 0.38671  -0.00463 0.43185  255 ALA A CA  
1775 C C   . ALA A 219 ? 1.85228 2.17869 1.22389 0.38819  -0.03770 0.42663  255 ALA A C   
1776 O O   . ALA A 219 ? 1.82697 2.18858 1.18010 0.37731  -0.05257 0.38065  255 ALA A O   
1777 C CB  . ALA A 219 ? 1.82012 2.05371 1.29462 0.39389  -0.01180 0.41683  255 ALA A CB  
1778 N N   . PRO A 220 ? 1.86604 2.20766 1.22514 0.40049  -0.05114 0.47163  256 PRO A N   
1779 C CA  . PRO A 220 ? 1.88918 2.29373 1.20576 0.40046  -0.08546 0.46727  256 PRO A CA  
1780 C C   . PRO A 220 ? 1.81530 2.25043 1.16844 0.40248  -0.11738 0.43281  256 PRO A C   
1781 O O   . PRO A 220 ? 1.81184 2.29406 1.13395 0.39096  -0.13921 0.39631  256 PRO A O   
1782 C CB  . PRO A 220 ? 1.94888 2.35223 1.25459 0.41622  -0.09207 0.53063  256 PRO A CB  
1783 C CG  . PRO A 220 ? 1.91982 2.26030 1.28673 0.42786  -0.06895 0.56027  256 PRO A CG  
1784 C CD  . PRO A 220 ? 1.86346 2.16443 1.24516 0.41399  -0.03674 0.52827  256 PRO A CD  
1785 N N   . THR A 221 ? 1.69337 2.10209 1.11318 0.41536  -0.11913 0.44123  257 THR A N   
1786 C CA  . THR A 221 ? 1.46411 1.90136 0.92520 0.41732  -0.14604 0.41205  257 THR A CA  
1787 C C   . THR A 221 ? 1.57258 1.97706 1.07208 0.40846  -0.12959 0.37105  257 THR A C   
1788 O O   . THR A 221 ? 1.64369 2.00279 1.13973 0.40209  -0.09965 0.36616  257 THR A O   
1789 C CB  . THR A 221 ? 1.51055 1.94930 1.02050 0.43956  -0.16217 0.45027  257 THR A CB  
1790 O OG1 . THR A 221 ? 1.39042 1.77291 0.95956 0.44802  -0.13854 0.45460  257 THR A OG1 
1791 C CG2 . THR A 221 ? 1.53897 1.98077 1.01693 0.45181  -0.16596 0.50569  257 THR A CG2 
1792 N N   . ASN A 222 ? 1.47069 1.90027 1.00774 0.40765  -0.15088 0.34291  258 ASN A N   
1793 C CA  . ASN A 222 ? 1.47089 1.87291 1.04448 0.39963  -0.13953 0.30603  258 ASN A CA  
1794 C C   . ASN A 222 ? 1.46881 1.81878 1.09535 0.41387  -0.12004 0.32822  258 ASN A C   
1795 O O   . ASN A 222 ? 1.42384 1.72525 1.06245 0.40773  -0.09648 0.31333  258 ASN A O   
1796 C CB  . ASN A 222 ? 1.39834 1.84900 0.99236 0.39127  -0.16898 0.26871  258 ASN A CB  
1797 C CG  . ASN A 222 ? 1.40977 1.83616 1.03327 0.37990  -0.15965 0.22891  258 ASN A CG  
1798 O OD1 . ASN A 222 ? 1.26152 1.69378 0.86259 0.36187  -0.16119 0.18977  258 ASN A OD1 
1799 N ND2 . ASN A 222 ? 1.42731 1.82564 1.10162 0.39050  -0.15021 0.23820  258 ASN A ND2 
1800 N N   . LYS A 223 ? 1.48027 1.83853 1.13920 0.43283  -0.13024 0.36252  259 LYS A N   
1801 C CA  . LYS A 223 ? 1.54485 1.85358 1.25767 0.44707  -0.11140 0.37995  259 LYS A CA  
1802 C C   . LYS A 223 ? 1.67092 1.91516 1.37226 0.44642  -0.07878 0.40166  259 LYS A C   
1803 O O   . LYS A 223 ? 1.62089 1.81129 1.35294 0.44541  -0.05604 0.39301  259 LYS A O   
1804 C CB  . LYS A 223 ? 1.59582 1.92949 1.34661 0.46939  -0.13024 0.41357  259 LYS A CB  
1805 C CG  . LYS A 223 ? 1.57871 1.86642 1.39241 0.48591  -0.11231 0.42600  259 LYS A CG  
1806 C CD  . LYS A 223 ? 1.46866 1.78704 1.32375 0.51011  -0.13368 0.45837  259 LYS A CD  
1807 C CE  . LYS A 223 ? 1.46922 1.74388 1.39237 0.52801  -0.11475 0.46506  259 LYS A CE  
1808 N NZ  . LYS A 223 ? 1.54900 1.85507 1.51945 0.55434  -0.13630 0.49634  259 LYS A NZ  
1809 N N   . GLN A 224 ? 1.82961 2.07881 1.48692 0.44557  -0.07603 0.42968  260 GLN A N   
1810 C CA  . GLN A 224 ? 1.83825 2.03015 1.48810 0.44332  -0.04503 0.45332  260 GLN A CA  
1811 C C   . GLN A 224 ? 1.82617 1.99065 1.45714 0.42391  -0.02407 0.42053  260 GLN A C   
1812 O O   . GLN A 224 ? 1.87678 1.98581 1.51859 0.41982  0.00305  0.43123  260 GLN A O   
1813 C CB  . GLN A 224 ? 1.89077 2.10037 1.49755 0.44746  -0.04769 0.49545  260 GLN A CB  
1814 C CG  . GLN A 224 ? 1.94963 2.19005 1.57029 0.46752  -0.07345 0.53126  260 GLN A CG  
1815 C CD  . GLN A 224 ? 2.05304 2.31120 1.62285 0.47038  -0.07786 0.57444  260 GLN A CD  
1816 O OE1 . GLN A 224 ? 2.06700 2.30820 1.59661 0.45799  -0.05600 0.58104  260 GLN A OE1 
1817 N NE2 . GLN A 224 ? 2.11628 2.40984 1.68762 0.48683  -0.10631 0.60552  260 GLN A NE2 
1818 N N   . LYS A 225 ? 1.73066 1.93202 1.33689 0.41153  -0.03718 0.38074  261 LYS A N   
1819 C CA  . LYS A 225 ? 1.78993 1.96580 1.38386 0.39527  -0.02041 0.34823  261 LYS A CA  
1820 C C   . LYS A 225 ? 1.68783 1.81931 1.32661 0.39338  -0.01196 0.32663  261 LYS A C   
1821 O O   . LYS A 225 ? 1.62999 1.71352 1.27243 0.38418  0.00937  0.31866  261 LYS A O   
1822 C CB  . LYS A 225 ? 1.73604 1.96294 1.29255 0.38299  -0.03814 0.31052  261 LYS A CB  
1823 C CG  . LYS A 225 ? 1.67955 1.88354 1.22344 0.36800  -0.02303 0.27694  261 LYS A CG  
1824 C CD  . LYS A 225 ? 1.59673 1.84961 1.10626 0.35588  -0.03992 0.23737  261 LYS A CD  
1825 C CE  . LYS A 225 ? 1.47021 1.69915 0.97091 0.34311  -0.02477 0.20466  261 LYS A CE  
1826 N NZ  . LYS A 225 ? 1.48324 1.75534 0.95457 0.33043  -0.03868 0.16155  261 LYS A NZ  
1827 N N   . TYR A 226 ? 1.64570 1.79384 1.31837 0.40117  -0.02838 0.31703  262 TYR A N   
1828 C CA  . TYR A 226 ? 1.51071 1.61812 1.22254 0.39952  -0.01891 0.29742  262 TYR A CA  
1829 C C   . TYR A 226 ? 1.53940 1.58568 1.28055 0.40637  0.00507  0.32262  262 TYR A C   
1830 O O   . TYR A 226 ? 1.46310 1.45803 1.22071 0.39787  0.02179  0.30617  262 TYR A O   
1831 C CB  . TYR A 226 ? 1.46104 1.60725 1.20395 0.40699  -0.03976 0.28336  262 TYR A CB  
1832 C CG  . TYR A 226 ? 1.43642 1.63178 1.16198 0.39464  -0.06210 0.24785  262 TYR A CG  
1833 C CD1 . TYR A 226 ? 1.50053 1.73206 1.18186 0.38558  -0.07375 0.24043  262 TYR A CD1 
1834 C CD2 . TYR A 226 ? 1.39643 1.60203 1.15141 0.39116  -0.07069 0.22041  262 TYR A CD2 
1835 C CE1 . TYR A 226 ? 1.48870 1.76116 1.15842 0.37220  -0.09416 0.20345  262 TYR A CE1 
1836 C CE2 . TYR A 226 ? 1.42913 1.67761 1.17387 0.37760  -0.09200 0.18739  262 TYR A CE2 
1837 C CZ  . TYR A 226 ? 1.51218 1.79203 1.21571 0.36756  -0.10413 0.17745  262 TYR A CZ  
1838 O OH  . TYR A 226 ? 1.55759 1.87538 1.25466 0.35170  -0.12484 0.14001  262 TYR A OH  
1839 N N   . GLU A 227 ? 1.65114 1.70065 1.39931 0.42050  0.00553  0.36154  263 GLU A N   
1840 C CA  . GLU A 227 ? 1.70745 1.69633 1.48439 0.42548  0.02829  0.38550  263 GLU A CA  
1841 C C   . GLU A 227 ? 1.71530 1.66211 1.47121 0.40927  0.05072  0.38800  263 GLU A C   
1842 O O   . GLU A 227 ? 1.78728 1.67560 1.56745 0.40094  0.07000  0.37933  263 GLU A O   
1843 C CB  . GLU A 227 ? 1.99470 1.99748 1.78296 0.44480  0.02123  0.42975  263 GLU A CB  
1844 C CG  . GLU A 227 ? 1.86011 1.90058 1.68185 0.46341  0.00002  0.43194  263 GLU A CG  
1845 C CD  . GLU A 227 ? 1.97233 2.01381 1.81335 0.48436  -0.00566 0.47849  263 GLU A CD  
1846 O OE1 . GLU A 227 ? 2.05097 2.04869 1.88889 0.48409  0.01219  0.50672  263 GLU A OE1 
1847 O OE2 . GLU A 227 ? 2.04590 2.13199 1.90784 0.50094  -0.02881 0.48793  263 GLU A OE2 
1848 N N   . LYS A 228 ? 1.66752 1.64504 1.37919 0.40367  0.04877  0.39839  264 LYS A N   
1849 C CA  . LYS A 228 ? 1.56671 1.50992 1.26241 0.38902  0.07200  0.40274  264 LYS A CA  
1850 C C   . LYS A 228 ? 1.47692 1.39538 1.17545 0.37303  0.07777  0.36234  264 LYS A C   
1851 O O   . LYS A 228 ? 1.38055 1.25104 1.08973 0.36059  0.09838  0.36250  264 LYS A O   
1852 C CB  . LYS A 228 ? 1.51523 1.50196 1.16039 0.38706  0.07091  0.42024  264 LYS A CB  
1853 C CG  . LYS A 228 ? 1.52104 1.47485 1.15543 0.37365  0.09936  0.43281  264 LYS A CG  
1854 C CD  . LYS A 228 ? 1.51525 1.49492 1.11351 0.37618  0.10653  0.47223  264 LYS A CD  
1855 C CE  . LYS A 228 ? 1.49573 1.52260 1.04019 0.36702  0.10715  0.45484  264 LYS A CE  
1856 N NZ  . LYS A 228 ? 1.58320 1.62695 1.09014 0.36493  0.12217  0.49297  264 LYS A NZ  
1857 N N   . ILE A 229 ? 1.43666 1.38623 1.12838 0.37208  0.05860  0.32867  265 ILE A N   
1858 C CA  . ILE A 229 ? 1.44653 1.37039 1.14118 0.35779  0.06078  0.29247  265 ILE A CA  
1859 C C   . ILE A 229 ? 1.40775 1.27480 1.14284 0.35399  0.07073  0.28319  265 ILE A C   
1860 O O   . ILE A 229 ? 1.35458 1.17444 1.09796 0.33902  0.08360  0.27056  265 ILE A O   
1861 C CB  . ILE A 229 ? 1.39309 1.36551 1.07082 0.35686  0.03646  0.26017  265 ILE A CB  
1862 C CG1 . ILE A 229 ? 1.24949 1.26046 0.88350 0.35160  0.03259  0.25317  265 ILE A CG1 
1863 C CG2 . ILE A 229 ? 1.17406 1.11474 0.86907 0.34638  0.03396  0.22664  265 ILE A CG2 
1864 C CD1 . ILE A 229 ? 1.32868 1.40006 0.94558 0.35157  0.00571  0.22679  265 ILE A CD1 
1865 N N   . GLY A 230 ? 1.38588 1.25799 1.14742 0.36698  0.06485  0.28783  266 GLY A N   
1866 C CA  . GLY A 230 ? 1.41349 1.23368 1.21062 0.36443  0.07670  0.27623  266 GLY A CA  
1867 C C   . GLY A 230 ? 1.45908 1.22373 1.27494 0.35892  0.09812  0.29528  266 GLY A C   
1868 O O   . GLY A 230 ? 1.41429 1.12725 1.25097 0.34732  0.10959  0.27668  266 GLY A O   
1869 N N   . ASP A 231 ? 1.65090 1.42586 1.45886 0.36562  0.10318  0.33174  267 ASP A N   
1870 C CA  . ASP A 231 ? 1.61997 1.34299 1.44768 0.35857  0.12396  0.35250  267 ASP A CA  
1871 C C   . ASP A 231 ? 1.58479 1.27598 1.40578 0.33461  0.13597  0.33607  267 ASP A C   
1872 O O   . ASP A 231 ? 1.70774 1.34393 1.55660 0.32096  0.14951  0.32884  267 ASP A O   
1873 C CB  . ASP A 231 ? 1.59859 1.34376 1.41515 0.37077  0.12643  0.39878  267 ASP A CB  
1874 C CG  . ASP A 231 ? 1.65114 1.41334 1.48754 0.39434  0.11557  0.42071  267 ASP A CG  
1875 O OD1 . ASP A 231 ? 1.62014 1.37727 1.48282 0.40194  0.10930  0.39931  267 ASP A OD1 
1876 O OD2 . ASP A 231 ? 1.67617 1.45769 1.50240 0.40565  0.11354  0.46056  267 ASP A OD2 
1877 N N   . LYS A 232 ? 1.42493 1.15035 1.21187 0.32906  0.13028  0.32840  268 LYS A N   
1878 C CA  . LYS A 232 ? 1.42562 1.12337 1.21158 0.30819  0.14103  0.31441  268 LYS A CA  
1879 C C   . LYS A 232 ? 1.32484 0.98446 1.12988 0.29324  0.13552  0.27494  268 LYS A C   
1880 O O   . LYS A 232 ? 1.25773 0.87799 1.07877 0.27306  0.14440  0.26379  268 LYS A O   
1881 C CB  . LYS A 232 ? 1.33355 1.07712 1.07973 0.30903  0.13597  0.31185  268 LYS A CB  
1882 C CG  . LYS A 232 ? 1.44243 1.23589 1.15707 0.32302  0.13718  0.34403  268 LYS A CG  
1883 C CD  . LYS A 232 ? 1.50059 1.30880 1.18903 0.31505  0.15408  0.35490  268 LYS A CD  
1884 C CE  . LYS A 232 ? 1.52541 1.31066 1.22811 0.30997  0.17965  0.39464  268 LYS A CE  
1885 N NZ  . LYS A 232 ? 1.41661 1.22237 1.09493 0.30125  0.20160  0.40736  268 LYS A NZ  
1886 N N   . LYS A 233 ? 1.26760 0.94037 1.07194 0.30149  0.12085  0.25388  269 LYS A N   
1887 C CA  . LYS A 233 ? 1.27054 0.91044 1.08516 0.28705  0.11613  0.21698  269 LYS A CA  
1888 C C   . LYS A 233 ? 1.44512 1.03036 1.29196 0.27954  0.12926  0.21237  269 LYS A C   
1889 O O   . LYS A 233 ? 1.47031 1.01758 1.32417 0.25997  0.12938  0.18414  269 LYS A O   
1890 C CB  . LYS A 233 ? 1.25282 0.92641 1.05578 0.29816  0.09999  0.19828  269 LYS A CB  
1891 C CG  . LYS A 233 ? 1.34208 1.06885 1.11506 0.30365  0.08381  0.19673  269 LYS A CG  
1892 C CD  . LYS A 233 ? 1.24885 1.00632 1.01647 0.31040  0.06697  0.17563  269 LYS A CD  
1893 C CE  . LYS A 233 ? 1.22085 1.03121 0.96185 0.31413  0.04857  0.17073  269 LYS A CE  
1894 N NZ  . LYS A 233 ? 1.10803 0.95311 0.84988 0.31957  0.03085  0.15215  269 LYS A NZ  
1895 N N   . ARG A 234 ? 1.36920 0.94904 1.23543 0.29451  0.13874  0.23855  270 ARG A N   
1896 C CA  . ARG A 234 ? 1.45249 0.97730 1.35188 0.28873  0.15177  0.23343  270 ARG A CA  
1897 C C   . ARG A 234 ? 1.49490 0.98270 1.41007 0.27034  0.16458  0.24643  270 ARG A C   
1898 O O   . ARG A 234 ? 1.53086 0.96766 1.47163 0.25676  0.17234  0.23076  270 ARG A O   
1899 C CB  . ARG A 234 ? 1.41287 0.94250 1.33360 0.31402  0.15603  0.25591  270 ARG A CB  
1900 C CG  . ARG A 234 ? 1.38121 0.93364 1.30378 0.33002  0.14841  0.23719  270 ARG A CG  
1901 C CD  . ARG A 234 ? 1.18074 0.70941 1.14120 0.34849  0.15842  0.24553  270 ARG A CD  
1902 N NE  . ARG A 234 ? 1.41745 0.99577 1.38499 0.37602  0.14905  0.26683  270 ARG A NE  
1903 C CZ  . ARG A 234 ? 1.53317 1.13716 1.50328 0.39181  0.14392  0.30825  270 ARG A CZ  
1904 N NH1 . ARG A 234 ? 1.33845 0.92332 1.30292 0.38386  0.15066  0.33510  270 ARG A NH1 
1905 N NH2 . ARG A 234 ? 1.51934 1.17101 1.49832 0.41555  0.13149  0.32391  270 ARG A NH2 
1906 N N   . THR A 235 ? 1.36593 0.87896 1.26707 0.26913  0.16813  0.27339  271 THR A N   
1907 C CA  . THR A 235 ? 1.48080 0.96352 1.40081 0.25096  0.18359  0.28881  271 THR A CA  
1908 C C   . THR A 235 ? 1.49292 0.96259 1.41418 0.22455  0.18071  0.26187  271 THR A C   
1909 O O   . THR A 235 ? 1.46535 0.90138 1.41420 0.20376  0.19182  0.26411  271 THR A O   
1910 C CB  . THR A 235 ? 1.38140 0.89813 1.28644 0.26224  0.19388  0.33411  271 THR A CB  
1911 O OG1 . THR A 235 ? 1.57624 1.14185 1.44448 0.26567  0.18618  0.33104  271 THR A OG1 
1912 C CG2 . THR A 235 ? 1.45860 0.99188 1.36244 0.28839  0.19204  0.36364  271 THR A CG2 
1913 N N   . THR A 236 ? 1.50266 0.99833 1.39870 0.22433  0.16494  0.23725  272 THR A N   
1914 C CA  . THR A 236 ? 1.47797 0.96362 1.37719 0.20132  0.15886  0.21353  272 THR A CA  
1915 C C   . THR A 236 ? 1.53278 0.98492 1.43781 0.18563  0.14512  0.17230  272 THR A C   
1916 O O   . THR A 236 ? 1.38493 0.85195 1.26713 0.19544  0.13256  0.15360  272 THR A O   
1917 C CB  . THR A 236 ? 1.42285 0.95447 1.29056 0.21087  0.14943  0.21282  272 THR A CB  
1918 O OG1 . THR A 236 ? 1.40638 0.96508 1.24783 0.22805  0.13348  0.19975  272 THR A OG1 
1919 C CG2 . THR A 236 ? 1.28732 0.85177 1.14267 0.22388  0.16585  0.25182  272 THR A CG2 
1920 N N   . PRO A 237 ? 1.66398 1.07288 1.59697 0.16055  0.14711  0.15682  273 PRO A N   
1921 C CA  . PRO A 237 ? 1.57971 0.95961 1.50867 0.14314  0.13205  0.11518  273 PRO A CA  
1922 C C   . PRO A 237 ? 1.57380 0.97451 1.47947 0.13488  0.11266  0.09551  273 PRO A C   
1923 O O   . PRO A 237 ? 1.49621 0.92863 1.39700 0.14048  0.11146  0.11061  273 PRO A O   
1924 C CB  . PRO A 237 ? 1.67484 1.01059 1.63994 0.11566  0.13614  0.10634  273 PRO A CB  
1925 C CG  . PRO A 237 ? 1.75741 1.09132 1.74715 0.12478  0.15804  0.14537  273 PRO A CG  
1926 C CD  . PRO A 237 ? 1.70496 1.08926 1.67383 0.14637  0.16367  0.17689  273 PRO A CD  
1927 N N   . ALA A 238 ? 1.57682 0.95741 1.46548 0.12179  0.09791  0.06079  274 ALA A N   
1928 C CA  . ALA A 238 ? 1.45958 0.85267 1.32341 0.11113  0.07581  0.04209  274 ALA A CA  
1929 C C   . ALA A 238 ? 1.40916 0.80364 1.30325 0.08223  0.06224  0.03562  274 ALA A C   
1930 O O   . ALA A 238 ? 1.38751 0.81964 1.27948 0.07346  0.03987  0.02786  274 ALA A O   
1931 C CB  . ALA A 238 ? 1.32545 0.70060 1.15481 0.10359  0.06395  0.00946  274 ALA A CB  
1932 N N   . VAL A 239 ? 1.40574 0.76253 1.33552 0.06693  0.07472  0.03914  275 VAL A N   
1933 C CA  . VAL A 239 ? 1.42652 0.79113 1.39635 0.03740  0.06098  0.03246  275 VAL A CA  
1934 C C   . VAL A 239 ? 1.49151 0.90439 1.48950 0.04563  0.07066  0.06049  275 VAL A C   
1935 O O   . VAL A 239 ? 1.47798 0.92701 1.49882 0.03229  0.05263  0.05344  275 VAL A O   
1936 C CB  . VAL A 239 ? 1.56666 0.87859 1.57067 0.01485  0.07035  0.02420  275 VAL A CB  
1937 C CG1 . VAL A 239 ? 1.56233 0.88499 1.61703 -0.01759 0.05544  0.01738  275 VAL A CG1 
1938 C CG2 . VAL A 239 ? 1.61127 0.88906 1.58393 0.00702  0.05892  -0.01034 275 VAL A CG2 
1939 N N   . THR A 240 ? 1.48778 0.90374 1.48398 0.06874  0.09953  0.09286  276 THR A N   
1940 C CA  . THR A 240 ? 1.53001 0.99324 1.54304 0.07692  0.11335  0.11845  276 THR A CA  
1941 C C   . THR A 240 ? 1.48643 1.00408 1.47101 0.09126  0.09683  0.10969  276 THR A C   
1942 O O   . THR A 240 ? 1.59985 1.15850 1.60770 0.08655  0.09535  0.10974  276 THR A O   
1943 C CB  . THR A 240 ? 1.57440 1.02568 1.58295 0.09740  0.14673  0.15835  276 THR A CB  
1944 O OG1 . THR A 240 ? 1.77495 1.18392 1.82870 0.07781  0.16475  0.17034  276 THR A OG1 
1945 C CG2 . THR A 240 ? 1.52769 1.03598 1.52618 0.11319  0.16053  0.18295  276 THR A CG2 
1946 N N   . LEU A 241 ? 1.39372 0.91239 1.33403 0.10792  0.08555  0.10024  277 LEU A N   
1947 C CA  . LEU A 241 ? 1.36135 0.92517 1.28043 0.11625  0.06669  0.08737  277 LEU A CA  
1948 C C   . LEU A 241 ? 1.35117 0.92243 1.29196 0.09317  0.03889  0.06231  277 LEU A C   
1949 O O   . LEU A 241 ? 1.31365 0.92356 1.25994 0.09623  0.02696  0.05551  277 LEU A O   
1950 C CB  . LEU A 241 ? 1.31162 0.87357 1.18720 0.13395  0.05978  0.08149  277 LEU A CB  
1951 C CG  . LEU A 241 ? 1.23610 0.81609 1.08896 0.16309  0.07770  0.10684  277 LEU A CG  
1952 C CD1 . LEU A 241 ? 1.30596 0.90834 1.12686 0.17762  0.06365  0.09565  277 LEU A CD1 
1953 C CD2 . LEU A 241 ? 1.13736 0.75813 0.99637 0.17021  0.09022  0.12539  277 LEU A CD2 
1954 N N   . CYS A 242 ? 1.32668 0.86122 1.28087 0.07024  0.02693  0.04809  278 CYS A N   
1955 C CA  . CYS A 242 ? 1.25044 0.79207 1.22410 0.04736  -0.00441 0.02799  278 CYS A CA  
1956 C C   . CYS A 242 ? 1.36664 0.92250 1.40322 0.02990  -0.00350 0.03231  278 CYS A C   
1957 O O   . CYS A 242 ? 1.42035 0.97171 1.48324 0.00598  -0.02951 0.01764  278 CYS A O   
1958 C CB  . CYS A 242 ? 1.28320 0.78330 1.22969 0.03001  -0.02187 0.00713  278 CYS A CB  
1959 S SG  . CYS A 242 ? 1.41951 0.93463 1.35096 0.01265  -0.06599 -0.01255 278 CYS A SG  
1960 N N   . ASP A 243 ? 1.37031 0.94702 1.43199 0.04059  0.02569  0.05306  279 ASP A N   
1961 C CA  . ASP A 243 ? 1.41046 1.00641 1.53822 0.02449  0.03328  0.05898  279 ASP A CA  
1962 C C   . ASP A 243 ? 1.44655 1.08407 1.60937 0.01969  0.00758  0.04509  279 ASP A C   
1963 O O   . ASP A 243 ? 1.43241 1.10333 1.58320 0.03882  0.00923  0.04423  279 ASP A O   
1964 C CB  . ASP A 243 ? 1.39420 1.00890 1.53052 0.03937  0.07426  0.08655  279 ASP A CB  
1965 C CG  . ASP A 243 ? 1.43915 1.08757 1.64575 0.02575  0.08783  0.09285  279 ASP A CG  
1966 O OD1 . ASP A 243 ? 1.26769 0.96218 1.49558 0.03263  0.08291  0.08425  279 ASP A OD1 
1967 O OD2 . ASP A 243 ? 1.25352 0.88202 1.49944 0.00785  0.10503  0.10558  279 ASP A OD2 
1968 N N   . GLY A 244 ? 2.17728 1.81257 2.38712 -0.00584 -0.01751 0.03370  280 GLY A N   
1969 C CA  . GLY A 244 ? 2.19289 1.86585 2.44576 -0.00987 -0.04592 0.02383  280 GLY A CA  
1970 C C   . GLY A 244 ? 2.19951 1.86969 2.40858 -0.00326 -0.07939 0.01202  280 GLY A C   
1971 O O   . GLY A 244 ? 2.27614 1.97691 2.51841 0.00032  -0.10009 0.00807  280 GLY A O   
1972 N N   . LEU A 245 ? 1.54682 1.18109 1.68690 -0.00127 -0.08347 0.00744  281 LEU A N   
1973 C CA  . LEU A 245 ? 1.38867 1.01834 1.48172 0.00313  -0.11012 -0.00081 281 LEU A CA  
1974 C C   . LEU A 245 ? 1.33994 0.93432 1.39915 -0.01976 -0.13638 -0.01303 281 LEU A C   
1975 O O   . LEU A 245 ? 1.37107 0.93635 1.43020 -0.03423 -0.12723 -0.01839 281 LEU A O   
1976 C CB  . LEU A 245 ? 1.33131 0.95802 1.36898 0.02763  -0.08791 0.00329  281 LEU A CB  
1977 C CG  . LEU A 245 ? 1.32563 0.98857 1.38128 0.05009  -0.06339 0.01142  281 LEU A CG  
1978 C CD1 . LEU A 245 ? 1.26587 0.92812 1.26530 0.07118  -0.04857 0.01417  281 LEU A CD1 
1979 C CD2 . LEU A 245 ? 1.31934 1.01564 1.41914 0.05190  -0.08241 0.00516  281 LEU A CD2 
1980 N N   . PRO A 246 ? 1.20112 0.79607 1.23033 -0.02490 -0.16863 -0.01813 282 PRO A N   
1981 C CA  . PRO A 246 ? 1.22362 0.78780 1.20753 -0.04753 -0.19270 -0.03126 282 PRO A CA  
1982 C C   . PRO A 246 ? 1.38735 0.91273 1.31546 -0.04352 -0.16461 -0.04070 282 PRO A C   
1983 O O   . PRO A 246 ? 1.30665 0.83107 1.19943 -0.02237 -0.14375 -0.03608 282 PRO A O   
1984 C CB  . PRO A 246 ? 1.25680 0.83233 1.21023 -0.04680 -0.22302 -0.02713 282 PRO A CB  
1985 C CG  . PRO A 246 ? 1.16392 0.77735 1.17866 -0.03222 -0.22780 -0.01447 282 PRO A CG  
1986 C CD  . PRO A 246 ? 1.13301 0.75673 1.17350 -0.01284 -0.18586 -0.01175 282 PRO A CD  
1987 N N   . GLN A 247 ? 1.40098 0.89475 1.32664 -0.06437 -0.16535 -0.05567 283 GLN A N   
1988 C CA  . GLN A 247 ? 1.45266 0.90454 1.34256 -0.05948 -0.13463 -0.06603 283 GLN A CA  
1989 C C   . GLN A 247 ? 1.48652 0.92295 1.30282 -0.05229 -0.13266 -0.07638 283 GLN A C   
1990 O O   . GLN A 247 ? 1.48261 0.89156 1.27375 -0.03907 -0.10261 -0.08182 283 GLN A O   
1991 C CB  . GLN A 247 ? 1.51574 0.93327 1.42161 -0.08757 -0.13997 -0.08577 283 GLN A CB  
1992 C CG  . GLN A 247 ? 1.65229 1.02675 1.56105 -0.07982 -0.10062 -0.08902 283 GLN A CG  
1993 C CD  . GLN A 247 ? 1.74497 1.13319 1.71495 -0.06678 -0.07338 -0.06247 283 GLN A CD  
1994 O OE1 . GLN A 247 ? 1.70878 1.13855 1.72495 -0.06809 -0.08331 -0.04797 283 GLN A OE1 
1995 N NE2 . GLN A 247 ? 1.68776 1.04152 1.65912 -0.05342 -0.03744 -0.05477 283 GLN A NE2 
1996 N N   . GLN A 248 ? 1.47414 0.92811 1.25924 -0.06040 -0.16263 -0.07713 284 GLN A N   
1997 C CA  . GLN A 248 ? 1.44983 0.89449 1.16740 -0.05478 -0.15699 -0.08398 284 GLN A CA  
1998 C C   . GLN A 248 ? 1.27032 0.73005 0.98663 -0.02353 -0.12750 -0.06960 284 GLN A C   
1999 O O   . GLN A 248 ? 1.14971 0.59884 0.82163 -0.01500 -0.11048 -0.07669 284 GLN A O   
2000 C CB  . GLN A 248 ? 1.32076 0.78348 1.00898 -0.07044 -0.19501 -0.07976 284 GLN A CB  
2001 C CG  . GLN A 248 ? 1.41597 0.86353 1.08014 -0.10305 -0.22738 -0.09695 284 GLN A CG  
2002 C CD  . GLN A 248 ? 1.30233 0.77845 1.01782 -0.11639 -0.26858 -0.08305 284 GLN A CD  
2003 O OE1 . GLN A 248 ? 1.19883 0.69464 0.98611 -0.10602 -0.26387 -0.07109 284 GLN A OE1 
2004 N NE2 . GLN A 248 ? 1.25365 0.73491 0.93322 -0.13885 -0.30882 -0.08326 284 GLN A NE2 
2005 N N   . PHE A 249 ? 1.23370 0.72139 0.99799 -0.00690 -0.12112 -0.05119 285 PHE A N   
2006 C CA  . PHE A 249 ? 1.17015 0.67474 0.93247 0.02148  -0.09529 -0.03937 285 PHE A CA  
2007 C C   . PHE A 249 ? 1.20374 0.68350 0.96483 0.03585  -0.06157 -0.03970 285 PHE A C   
2008 O O   . PHE A 249 ? 1.17091 0.65543 0.91250 0.05658  -0.04214 -0.03547 285 PHE A O   
2009 C CB  . PHE A 249 ? 1.11612 0.65794 0.92380 0.03363  -0.09780 -0.02381 285 PHE A CB  
2010 C CG  . PHE A 249 ? 1.16821 0.73440 0.97922 0.02898  -0.12522 -0.02104 285 PHE A CG  
2011 C CD1 . PHE A 249 ? 1.20910 0.77696 0.97975 0.02975  -0.13123 -0.02229 285 PHE A CD1 
2012 C CD2 . PHE A 249 ? 1.02821 0.61516 0.88871 0.02407  -0.14341 -0.01595 285 PHE A CD2 
2013 C CE1 . PHE A 249 ? 1.04739 0.63213 0.82502 0.02460  -0.15594 -0.01619 285 PHE A CE1 
2014 C CE2 . PHE A 249 ? 1.13499 0.73914 1.00535 0.02178  -0.16875 -0.01170 285 PHE A CE2 
2015 C CZ  . PHE A 249 ? 1.04768 0.64816 0.87562 0.02152  -0.17549 -0.01067 285 PHE A CZ  
2016 N N   . ALA A 250 ? 1.20752 0.66105 0.99492 0.02512  -0.05496 -0.04311 286 ALA A N   
2017 C CA  . ALA A 250 ? 1.21293 0.63364 1.00282 0.03770  -0.02340 -0.04166 286 ALA A CA  
2018 C C   . ALA A 250 ? 1.09632 0.48028 0.84290 0.03304  -0.01647 -0.06570 286 ALA A C   
2019 O O   . ALA A 250 ? 1.34914 0.71719 1.08780 0.05428  0.01045  -0.06358 286 ALA A O   
2020 C CB  . ALA A 250 ? 1.29068 0.69067 1.12705 0.02442  -0.01703 -0.03760 286 ALA A CB  
2021 N N   . GLU A 251 ? 1.06864 0.44086 0.78698 0.00607  -0.04032 -0.08872 287 GLU A N   
2022 C CA  . GLU A 251 ? 1.26340 0.60383 0.93198 -0.00044 -0.03193 -0.11616 287 GLU A CA  
2023 C C   . GLU A 251 ? 1.23524 0.59812 0.87035 0.02022  -0.01909 -0.11133 287 GLU A C   
2024 O O   . GLU A 251 ? 1.27941 0.62056 0.89307 0.03149  0.00648  -0.12583 287 GLU A O   
2025 C CB  . GLU A 251 ? 1.14585 0.47786 0.78161 -0.03533 -0.06435 -0.13923 287 GLU A CB  
2026 C CG  . GLU A 251 ? 1.45653 0.75553 1.11783 -0.06021 -0.07338 -0.15722 287 GLU A CG  
2027 C CD  . GLU A 251 ? 1.67451 0.95308 1.29223 -0.08270 -0.07651 -0.19384 287 GLU A CD  
2028 O OE1 . GLU A 251 ? 1.64826 0.94367 1.21506 -0.09948 -0.10230 -0.20187 287 GLU A OE1 
2029 O OE2 . GLU A 251 ? 1.61936 0.87062 1.25702 -0.08253 -0.05243 -0.21290 287 GLU A OE2 
2030 N N   . TYR A 252 ? 1.12623 0.53284 0.76245 0.02501  -0.03559 -0.09248 288 TYR A N   
2031 C CA  . TYR A 252 ? 1.12886 0.56066 0.74041 0.04077  -0.02535 -0.08742 288 TYR A CA  
2032 C C   . TYR A 252 ? 1.10813 0.54522 0.74310 0.07324  0.00572  -0.07610 288 TYR A C   
2033 O O   . TYR A 252 ? 1.06064 0.49273 0.67787 0.08572  0.02750  -0.08529 288 TYR A O   
2034 C CB  . TYR A 252 ? 1.13765 0.61071 0.75576 0.03786  -0.05024 -0.06983 288 TYR A CB  
2035 C CG  . TYR A 252 ? 0.88974 0.39339 0.49724 0.05393  -0.03965 -0.06163 288 TYR A CG  
2036 C CD1 . TYR A 252 ? 1.13494 0.63989 0.69904 0.04310  -0.03855 -0.07052 288 TYR A CD1 
2037 C CD2 . TYR A 252 ? 0.92887 0.46297 0.56927 0.07799  -0.03069 -0.04525 288 TYR A CD2 
2038 C CE1 . TYR A 252 ? 1.05198 0.58782 0.61476 0.05516  -0.02783 -0.06267 288 TYR A CE1 
2039 C CE2 . TYR A 252 ? 0.97739 0.54286 0.61396 0.09007  -0.02391 -0.03989 288 TYR A CE2 
2040 C CZ  . TYR A 252 ? 1.06642 0.63269 0.66865 0.07825  -0.02205 -0.04832 288 TYR A CZ  
2041 O OH  . TYR A 252 ? 1.06012 0.66044 0.66656 0.08776  -0.01428 -0.04257 288 TYR A OH  
2042 N N   . LEU A 253 ? 1.06226 0.51253 0.73787 0.08781  0.00842  -0.05484 289 LEU A N   
2043 C CA  . LEU A 253 ? 0.91373 0.37501 0.60927 0.11937  0.03262  -0.03774 289 LEU A CA  
2044 C C   . LEU A 253 ? 1.25452 0.67042 0.95391 0.12912  0.05943  -0.04717 289 LEU A C   
2045 O O   . LEU A 253 ? 1.24335 0.66480 0.94680 0.15408  0.07975  -0.04236 289 LEU A O   
2046 C CB  . LEU A 253 ? 0.95908 0.44198 0.68846 0.12951  0.03040  -0.01274 289 LEU A CB  
2047 C CG  . LEU A 253 ? 1.12125 0.62378 0.86605 0.16179  0.04947  0.01117  289 LEU A CG  
2048 C CD1 . LEU A 253 ? 0.99967 0.54543 0.73144 0.17609  0.04562  0.01209  289 LEU A CD1 
2049 C CD2 . LEU A 253 ? 0.87931 0.40108 0.64745 0.16700  0.04901  0.03428  289 LEU A CD2 
2050 N N   . ASP A 254 ? 1.02769 0.39848 0.73179 0.10975  0.05932  -0.06174 290 ASP A N   
2051 C CA  . ASP A 254 ? 1.28002 0.61392 0.99906 0.11443  0.08337  -0.07418 290 ASP A CA  
2052 C C   . ASP A 254 ? 1.24300 0.56645 0.92589 0.11403  0.09493  -0.10349 290 ASP A C   
2053 O O   . ASP A 254 ? 1.27182 0.58982 0.97450 0.13214  0.11926  -0.10705 290 ASP A O   
2054 C CB  . ASP A 254 ? 1.26603 0.56649 1.00627 0.08746  0.07634  -0.08667 290 ASP A CB  
2055 C CG  . ASP A 254 ? 1.49326 0.79880 1.28466 0.09396  0.08128  -0.05581 290 ASP A CG  
2056 O OD1 . ASP A 254 ? 1.39661 0.72425 1.20754 0.12151  0.09613  -0.02728 290 ASP A OD1 
2057 O OD2 . ASP A 254 ? 1.68911 0.97911 1.50070 0.07032  0.06980  -0.05930 290 ASP A OD2 
2058 N N   . SER A 255 ? 1.23813 0.56148 0.86920 0.09303  0.07758  -0.12342 291 SER A N   
2059 C CA  . SER A 255 ? 1.40855 0.72664 0.99891 0.08843  0.09115  -0.15185 291 SER A CA  
2060 C C   . SER A 255 ? 1.38534 0.73876 0.97951 0.11741  0.11029  -0.13949 291 SER A C   
2061 O O   . SER A 255 ? 1.14988 0.49871 0.74722 0.13059  0.13787  -0.15479 291 SER A O   
2062 C CB  . SER A 255 ? 1.33931 0.66227 0.87477 0.05432  0.06365  -0.16855 291 SER A CB  
2063 O OG  . SER A 255 ? 1.18132 0.49892 0.66948 0.04706  0.07978  -0.19647 291 SER A OG  
2064 N N   . VAL A 256 ? 0.95843 0.36249 0.56581 0.12489  0.09380  -0.11125 292 VAL A N   
2065 C CA  . VAL A 256 ? 1.17717 0.62476 0.79599 0.14850  0.10701  -0.09924 292 VAL A CA  
2066 C C   . VAL A 256 ? 1.25993 0.70598 0.92491 0.18480  0.12988  -0.08337 292 VAL A C   
2067 O O   . VAL A 256 ? 1.32077 0.79578 1.00150 0.20727  0.14666  -0.07955 292 VAL A O   
2068 C CB  . VAL A 256 ? 1.19462 0.69381 0.81700 0.14383  0.08094  -0.07733 292 VAL A CB  
2069 C CG1 . VAL A 256 ? 1.22729 0.72394 0.81035 0.10972  0.05585  -0.08695 292 VAL A CG1 
2070 C CG2 . VAL A 256 ? 1.06518 0.57606 0.72334 0.15632  0.06925  -0.05205 292 VAL A CG2 
2071 N N   . ARG A 257 ? 1.16116 0.57609 0.85193 0.19095  0.13061  -0.07109 293 ARG A N   
2072 C CA  . ARG A 257 ? 1.28050 0.70574 1.02287 0.21752  0.14684  -0.04958 293 ARG A CA  
2073 C C   . ARG A 257 ? 1.22790 0.62180 0.98734 0.21903  0.17024  -0.07214 293 ARG A C   
2074 O O   . ARG A 257 ? 1.32179 0.72305 1.12515 0.24318  0.18398  -0.05635 293 ARG A O   
2075 C CB  . ARG A 257 ? 1.27007 0.69280 1.03992 0.21575  0.13617  -0.02217 293 ARG A CB  
2076 C CG  . ARG A 257 ? 1.33844 0.80569 1.10642 0.22529  0.11888  0.00581  293 ARG A CG  
2077 C CD  . ARG A 257 ? 1.38298 0.84692 1.17174 0.21857  0.11274  0.02840  293 ARG A CD  
2078 N NE  . ARG A 257 ? 1.18573 0.69776 0.97500 0.23214  0.10164  0.05531  293 ARG A NE  
2079 C CZ  . ARG A 257 ? 1.20982 0.72990 1.00993 0.22863  0.09829  0.07627  293 ARG A CZ  
2080 N NH1 . ARG A 257 ? 1.17859 0.66244 0.99594 0.21178  0.10430  0.07652  293 ARG A NH1 
2081 N NH2 . ARG A 257 ? 1.15171 0.71831 0.94520 0.24192  0.08973  0.09594  293 ARG A NH2 
2082 N N   . SER A 258 ? 1.25194 0.61291 0.97717 0.19357  0.17282  -0.10901 294 SER A N   
2083 C CA  . SER A 258 ? 1.34513 0.67689 1.08204 0.19303  0.19441  -0.13800 294 SER A CA  
2084 C C   . SER A 258 ? 1.32379 0.67237 1.03336 0.19627  0.21308  -0.16403 294 SER A C   
2085 O O   . SER A 258 ? 1.23094 0.55819 0.94105 0.19319  0.23165  -0.19518 294 SER A O   
2086 C CB  . SER A 258 ? 1.32631 0.61338 1.04612 0.16058  0.18425  -0.16490 294 SER A CB  
2087 O OG  . SER A 258 ? 1.28905 0.56464 1.03872 0.15537  0.16915  -0.14052 294 SER A OG  
2088 N N   . LEU A 259 ? 1.33111 0.71897 1.01810 0.20194  0.20941  -0.15301 295 LEU A N   
2089 C CA  . LEU A 259 ? 1.36321 0.77409 1.02627 0.20275  0.22950  -0.17440 295 LEU A CA  
2090 C C   . LEU A 259 ? 1.14185 0.57930 0.86421 0.23802  0.25516  -0.16666 295 LEU A C   
2091 O O   . LEU A 259 ? 1.05900 0.52040 0.82825 0.26405  0.24899  -0.13278 295 LEU A O   
2092 C CB  . LEU A 259 ? 1.32023 0.76442 0.94309 0.19495  0.21605  -0.16363 295 LEU A CB  
2093 C CG  . LEU A 259 ? 1.27155 0.69901 0.82859 0.15625  0.19018  -0.17483 295 LEU A CG  
2094 C CD1 . LEU A 259 ? 1.20205 0.68673 0.75219 0.14643  0.16755  -0.15085 295 LEU A CD1 
2095 C CD2 . LEU A 259 ? 1.34368 0.75317 0.85374 0.13092  0.20312  -0.21171 295 LEU A CD2 
2096 N N   . PRO A 260 ? 1.22469 0.66221 0.94665 0.23919  0.28208  -0.19706 296 PRO A N   
2097 C CA  . PRO A 260 ? 1.33772 0.80865 1.11913 0.27295  0.30573  -0.19066 296 PRO A CA  
2098 C C   . PRO A 260 ? 1.27986 0.81172 1.07370 0.28770  0.30353  -0.16582 296 PRO A C   
2099 O O   . PRO A 260 ? 1.22340 0.76924 0.97211 0.27045  0.28894  -0.16000 296 PRO A O   
2100 C CB  . PRO A 260 ? 1.37145 0.83295 1.13375 0.26405  0.33438  -0.23442 296 PRO A CB  
2101 C CG  . PRO A 260 ? 1.44122 0.85035 1.15133 0.23148  0.32280  -0.26139 296 PRO A CG  
2102 C CD  . PRO A 260 ? 1.25142 0.65760 0.92362 0.21056  0.29028  -0.23942 296 PRO A CD  
2103 N N   . PHE A 261 ? 1.36126 0.93106 1.22101 0.32045  0.31647  -0.15124 297 PHE A N   
2104 C CA  . PHE A 261 ? 1.37789 1.01312 1.26435 0.33753  0.31126  -0.12570 297 PHE A CA  
2105 C C   . PHE A 261 ? 1.43489 1.10160 1.28484 0.31999  0.32880  -0.14623 297 PHE A C   
2106 O O   . PHE A 261 ? 1.36133 1.05888 1.18933 0.31267  0.31547  -0.13194 297 PHE A O   
2107 C CB  . PHE A 261 ? 1.41735 1.08946 1.38652 0.37450  0.31898  -0.10728 297 PHE A CB  
2108 C CG  . PHE A 261 ? 1.30108 1.04909 1.30770 0.39214  0.31107  -0.08262 297 PHE A CG  
2109 C CD1 . PHE A 261 ? 1.21470 0.98856 1.22741 0.40036  0.27814  -0.04680 297 PHE A CD1 
2110 C CD2 . PHE A 261 ? 1.28470 1.08320 1.32258 0.39917  0.33603  -0.09656 297 PHE A CD2 
2111 C CE1 . PHE A 261 ? 1.21614 1.06508 1.26514 0.41520  0.26675  -0.02695 297 PHE A CE1 
2112 C CE2 . PHE A 261 ? 1.25054 1.12479 1.33129 0.41334  0.32699  -0.07459 297 PHE A CE2 
2113 C CZ  . PHE A 261 ? 1.31169 1.21151 1.39805 0.42144  0.29050  -0.04046 297 PHE A CZ  
2114 N N   . ASP A 262 ? 1.39370 1.05468 1.23569 0.31239  0.35924  -0.17957 298 ASP A N   
2115 C CA  . ASP A 262 ? 1.41655 1.11250 1.22560 0.29393  0.38084  -0.19687 298 ASP A CA  
2116 C C   . ASP A 262 ? 1.43960 1.09567 1.15528 0.25224  0.37774  -0.22135 298 ASP A C   
2117 O O   . ASP A 262 ? 1.45439 1.13330 1.13254 0.23204  0.39742  -0.23726 298 ASP A O   
2118 C CB  . ASP A 262 ? 1.36834 1.09608 1.22706 0.31174  0.41716  -0.21659 298 ASP A CB  
2119 C CG  . ASP A 262 ? 1.39626 1.07238 1.24842 0.31257  0.43182  -0.24920 298 ASP A CG  
2120 O OD1 . ASP A 262 ? 1.42179 1.03939 1.23555 0.29769  0.41372  -0.25610 298 ASP A OD1 
2121 O OD2 . ASP A 262 ? 1.43623 1.13220 1.32507 0.32862  0.46190  -0.26909 298 ASP A OD2 
2122 N N   . ALA A 263 ? 1.44189 1.04373 1.12131 0.23754  0.35173  -0.22213 299 ALA A N   
2123 C CA  . ALA A 263 ? 1.39981 0.96749 0.99555 0.19771  0.34147  -0.24348 299 ALA A CA  
2124 C C   . ALA A 263 ? 1.50196 1.08682 1.04565 0.17397  0.32042  -0.22444 299 ALA A C   
2125 O O   . ALA A 263 ? 1.23071 0.84342 0.80639 0.18552  0.30036  -0.19332 299 ALA A O   
2126 C CB  . ALA A 263 ? 1.39571 0.90473 0.98168 0.18943  0.31928  -0.25067 299 ALA A CB  
2127 N N   . GLU A 264 ? 1.54908 1.12637 1.01948 0.13757  0.31721  -0.23953 300 GLU A N   
2128 C CA  . GLU A 264 ? 1.49987 1.09018 0.91829 0.10998  0.29325  -0.21901 300 GLU A CA  
2129 C C   . GLU A 264 ? 1.45848 1.00776 0.84207 0.08862  0.24909  -0.21321 300 GLU A C   
2130 O O   . GLU A 264 ? 1.46325 0.97786 0.80988 0.07101  0.24423  -0.23691 300 GLU A O   
2131 C CB  . GLU A 264 ? 1.60951 1.22312 0.97253 0.08154  0.31114  -0.22931 300 GLU A CB  
2132 C CG  . GLU A 264 ? 1.72630 1.37987 1.07548 0.06186  0.29734  -0.19725 300 GLU A CG  
2133 C CD  . GLU A 264 ? 1.82963 1.51547 1.14266 0.04501  0.33452  -0.20426 300 GLU A CD  
2134 O OE1 . GLU A 264 ? 1.69950 1.42572 1.06618 0.06644  0.37242  -0.20867 300 GLU A OE1 
2135 O OE2 . GLU A 264 ? 1.95465 1.63534 1.19933 0.01085  0.32083  -0.20078 300 GLU A OE2 
2136 N N   . PRO A 265 ? 1.42973 0.99667 0.84335 0.08758  0.21084  -0.18013 301 PRO A N   
2137 C CA  . PRO A 265 ? 1.43236 0.96489 0.82796 0.07132  0.17140  -0.17434 301 PRO A CA  
2138 C C   . PRO A 265 ? 1.38060 0.90023 0.70032 0.03250  0.15111  -0.17878 301 PRO A C   
2139 O O   . PRO A 265 ? 1.35616 0.90507 0.64700 0.01643  0.15375  -0.16719 301 PRO A O   
2140 C CB  . PRO A 265 ? 1.26692 0.83293 0.71640 0.08200  0.14272  -0.13906 301 PRO A CB  
2141 C CG  . PRO A 265 ? 1.36007 0.97038 0.86303 0.11005  0.16742  -0.13046 301 PRO A CG  
2142 C CD  . PRO A 265 ? 1.30235 0.92326 0.77516 0.10323  0.20341  -0.14981 301 PRO A CD  
2143 N N   . PRO A 266 ? 1.35159 0.82911 0.63877 0.01541  0.12949  -0.19331 302 PRO A N   
2144 C CA  . PRO A 266 ? 1.46920 0.93994 0.68857 -0.02132 0.09989  -0.19099 302 PRO A CA  
2145 C C   . PRO A 266 ? 1.39040 0.88196 0.63280 -0.03006 0.05688  -0.15285 302 PRO A C   
2146 O O   . PRO A 266 ? 1.40318 0.87786 0.66373 -0.03504 0.02465  -0.14729 302 PRO A O   
2147 C CB  . PRO A 266 ? 1.46721 0.90536 0.68179 -0.03264 0.08803  -0.21644 302 PRO A CB  
2148 C CG  . PRO A 266 ? 1.47249 0.88566 0.74815 -0.00501 0.09673  -0.21995 302 PRO A CG  
2149 C CD  . PRO A 266 ? 1.46452 0.89927 0.77745 0.02774  0.13242  -0.21278 302 PRO A CD  
2150 N N   . TYR A 267 ? 1.45224 0.98106 0.70053 -0.03230 0.05776  -0.12743 303 TYR A N   
2151 C CA  . TYR A 267 ? 1.34913 0.89717 0.63326 -0.03597 0.02162  -0.09345 303 TYR A CA  
2152 C C   . TYR A 267 ? 1.44368 0.97332 0.68832 -0.06398 -0.02048 -0.08304 303 TYR A C   
2153 O O   . TYR A 267 ? 1.39339 0.91833 0.67636 -0.06199 -0.05253 -0.07094 303 TYR A O   
2154 C CB  . TYR A 267 ? 1.31736 0.90436 0.61499 -0.03689 0.03296  -0.07157 303 TYR A CB  
2155 C CG  . TYR A 267 ? 1.34620 0.96114 0.69192 -0.00941 0.06960  -0.07915 303 TYR A CG  
2156 C CD1 . TYR A 267 ? 1.14696 0.78075 0.56261 0.01533  0.06261  -0.06978 303 TYR A CD1 
2157 C CD2 . TYR A 267 ? 1.24421 0.87033 0.56588 -0.00782 0.11102  -0.09568 303 TYR A CD2 
2158 C CE1 . TYR A 267 ? 1.16459 0.82876 0.62566 0.04092  0.09085  -0.07378 303 TYR A CE1 
2159 C CE2 . TYR A 267 ? 1.29381 0.95048 0.66912 0.01920  0.14247  -0.10094 303 TYR A CE2 
2160 C CZ  . TYR A 267 ? 1.27706 0.95326 0.72236 0.04347  0.12970  -0.08846 303 TYR A CZ  
2161 O OH  . TYR A 267 ? 1.27867 0.98995 0.77845 0.07071  0.15606  -0.09088 303 TYR A OH  
2162 N N   . GLU A 268 ? 1.42126 0.94381 0.58958 -0.09001 -0.02086 -0.08659 304 GLU A N   
2163 C CA  . GLU A 268 ? 1.40008 0.91718 0.54214 -0.11536 -0.06400 -0.07104 304 GLU A CA  
2164 C C   . GLU A 268 ? 1.51764 1.01061 0.67495 -0.11639 -0.08595 -0.09034 304 GLU A C   
2165 O O   . GLU A 268 ? 1.49205 0.98490 0.66740 -0.12681 -0.12759 -0.07264 304 GLU A O   
2166 C CB  . GLU A 268 ? 1.57852 1.11123 0.66248 -0.13748 -0.05457 -0.07069 304 GLU A CB  
2167 C CG  . GLU A 268 ? 1.74868 1.30550 0.81638 -0.13740 -0.02085 -0.05833 304 GLU A CG  
2168 C CD  . GLU A 268 ? 1.92804 1.49866 0.93698 -0.15250 0.00399  -0.07198 304 GLU A CD  
2169 O OE1 . GLU A 268 ? 1.83040 1.39422 0.80407 -0.16753 -0.01584 -0.08215 304 GLU A OE1 
2170 O OE2 . GLU A 268 ? 1.99359 1.58441 0.99255 -0.14904 0.04397  -0.07366 304 GLU A OE2 
2171 N N   . GLU A 269 ? 1.43222 0.90552 0.59051 -0.10554 -0.05768 -0.12566 305 GLU A N   
2172 C CA  . GLU A 269 ? 1.43823 0.88684 0.61588 -0.10908 -0.07531 -0.14475 305 GLU A CA  
2173 C C   . GLU A 269 ? 1.45003 0.88919 0.68870 -0.09287 -0.09287 -0.13171 305 GLU A C   
2174 O O   . GLU A 269 ? 1.40280 0.83263 0.66383 -0.10297 -0.12491 -0.13035 305 GLU A O   
2175 C CB  . GLU A 269 ? 1.51139 0.93974 0.68344 -0.10101 -0.03761 -0.18462 305 GLU A CB  
2176 C CG  . GLU A 269 ? 1.29939 0.70331 0.48643 -0.11177 -0.05435 -0.20743 305 GLU A CG  
2177 C CD  . GLU A 269 ? 1.77483 1.16996 0.92821 -0.12093 -0.03193 -0.24610 305 GLU A CD  
2178 O OE1 . GLU A 269 ? 1.83333 1.22849 0.97993 -0.10518 0.01016  -0.26277 305 GLU A OE1 
2179 O OE2 . GLU A 269 ? 1.67736 1.06837 0.81419 -0.14320 -0.05716 -0.26115 305 GLU A OE2 
2180 N N   . TYR A 270 ? 1.35762 0.81721 0.64688 -0.06571 -0.06991 -0.11792 306 TYR A N   
2181 C CA  . TYR A 270 ? 1.27742 0.74852 0.64129 -0.04750 -0.08187 -0.10021 306 TYR A CA  
2182 C C   . TYR A 270 ? 1.38919 0.87874 0.77071 -0.05920 -0.12249 -0.07217 306 TYR A C   
2183 O O   . TYR A 270 ? 1.27424 0.76428 0.70270 -0.05686 -0.14403 -0.06524 306 TYR A O   
2184 C CB  . TYR A 270 ? 1.25827 0.75174 0.66313 -0.01760 -0.05115 -0.09268 306 TYR A CB  
2185 C CG  . TYR A 270 ? 1.39022 0.86550 0.80237 0.00188  -0.01368 -0.11472 306 TYR A CG  
2186 C CD1 . TYR A 270 ? 1.42321 0.86324 0.84625 0.00179  -0.01172 -0.13198 306 TYR A CD1 
2187 C CD2 . TYR A 270 ? 1.40173 0.89504 0.81725 0.02047  0.01977  -0.11723 306 TYR A CD2 
2188 C CE1 . TYR A 270 ? 1.30876 0.72612 0.74455 0.02093  0.02284  -0.14992 306 TYR A CE1 
2189 C CE2 . TYR A 270 ? 1.41093 0.88703 0.84137 0.04165  0.05350  -0.13519 306 TYR A CE2 
2190 C CZ  . TYR A 270 ? 1.41537 0.85052 0.85519 0.04242  0.05504  -0.15090 306 TYR A CZ  
2191 O OH  . TYR A 270 ? 1.39254 0.80467 0.85294 0.06473  0.08889  -0.16669 306 TYR A OH  
2192 N N   . ARG A 271 ? 1.39771 0.90219 0.74673 -0.07149 -0.13150 -0.05468 307 ARG A N   
2193 C CA  . ARG A 271 ? 1.39712 0.91462 0.76814 -0.08090 -0.16989 -0.02565 307 ARG A CA  
2194 C C   . ARG A 271 ? 1.36064 0.86404 0.71142 -0.10342 -0.20909 -0.02523 307 ARG A C   
2195 O O   . ARG A 271 ? 1.30101 0.81243 0.69943 -0.10364 -0.24150 -0.00794 307 ARG A O   
2196 C CB  . ARG A 271 ? 1.29512 0.82754 0.63790 -0.08997 -0.16801 -0.00361 307 ARG A CB  
2197 C CG  . ARG A 271 ? 1.33439 0.88654 0.69881 -0.07133 -0.13068 -0.00570 307 ARG A CG  
2198 C CD  . ARG A 271 ? 1.28105 0.85040 0.64332 -0.08133 -0.13507 0.02151  307 ARG A CD  
2199 N NE  . ARG A 271 ? 1.31690 0.89802 0.64144 -0.08508 -0.09889 0.01623  307 ARG A NE  
2200 C CZ  . ARG A 271 ? 1.47843 1.05257 0.72981 -0.10756 -0.09244 0.01850  307 ARG A CZ  
2201 N NH1 . ARG A 271 ? 1.52115 1.07636 0.72351 -0.12909 -0.12382 0.02683  307 ARG A NH1 
2202 N NH2 . ARG A 271 ? 1.24609 0.83635 0.47293 -0.10877 -0.05368 0.01252  307 ARG A NH2 
2203 N N   . MET A 272 ? 1.34859 0.83349 0.63153 -0.12253 -0.20708 -0.04613 308 MET A N   
2204 C CA  . MET A 272 ? 1.46469 0.95059 0.74915 -0.14190 -0.24003 -0.04724 308 MET A CA  
2205 C C   . MET A 272 ? 1.46944 0.93915 0.80127 -0.13671 -0.24882 -0.06582 308 MET A C   
2206 O O   . MET A 272 ? 1.51518 0.99335 0.87884 -0.14800 -0.28407 -0.05812 308 MET A O   
2207 C CB  . MET A 272 ? 1.28906 0.77464 0.50833 -0.16042 -0.22741 -0.06631 308 MET A CB  
2208 C CG  . MET A 272 ? 1.60452 1.11226 0.78377 -0.17581 -0.23937 -0.03957 308 MET A CG  
2209 S SD  . MET A 272 ? 2.04898 1.55962 1.14347 -0.19062 -0.20802 -0.06636 308 MET A SD  
2210 C CE  . MET A 272 ? 1.62891 1.12265 0.72136 -0.20071 -0.21853 -0.10767 308 MET A CE  
2211 N N   . LEU A 273 ? 1.48236 0.93708 0.83537 -0.11741 -0.21233 -0.08591 309 LEU A N   
2212 C CA  . LEU A 273 ? 1.53436 0.98018 0.94944 -0.10972 -0.21169 -0.09603 309 LEU A CA  
2213 C C   . LEU A 273 ? 1.38675 0.85909 0.87746 -0.09642 -0.22940 -0.06892 309 LEU A C   
2214 O O   . LEU A 273 ? 1.42622 0.90161 0.96435 -0.10268 -0.25070 -0.06816 309 LEU A O   
2215 C CB  . LEU A 273 ? 1.40237 0.82984 0.82877 -0.08843 -0.16481 -0.11528 309 LEU A CB  
2216 C CG  . LEU A 273 ? 1.42363 0.83890 0.91361 -0.07887 -0.15644 -0.12071 309 LEU A CG  
2217 C CD1 . LEU A 273 ? 1.54043 0.92819 1.02058 -0.10557 -0.17414 -0.14569 309 LEU A CD1 
2218 C CD2 . LEU A 273 ? 1.38331 0.78663 0.88939 -0.05135 -0.11137 -0.12641 309 LEU A CD2 
2219 N N   . LEU A 274 ? 1.36493 0.85801 0.87090 -0.07897 -0.21972 -0.04897 310 LEU A N   
2220 C CA  . LEU A 274 ? 1.38403 0.90113 0.95864 -0.06550 -0.23323 -0.02841 310 LEU A CA  
2221 C C   . LEU A 274 ? 1.29600 0.82438 0.88174 -0.08106 -0.27832 -0.00801 310 LEU A C   
2222 O O   . LEU A 274 ? 1.28922 0.83411 0.94143 -0.07317 -0.29423 0.00316  310 LEU A O   
2223 C CB  . LEU A 274 ? 1.28168 0.81571 0.86863 -0.04347 -0.20872 -0.01902 310 LEU A CB  
2224 C CG  . LEU A 274 ? 1.13425 0.66429 0.72035 -0.02345 -0.16744 -0.03318 310 LEU A CG  
2225 C CD1 . LEU A 274 ? 1.17224 0.72547 0.76691 -0.00556 -0.14980 -0.02414 310 LEU A CD1 
2226 C CD2 . LEU A 274 ? 1.12847 0.65618 0.76390 -0.01204 -0.15866 -0.03789 310 LEU A CD2 
2227 N N   . LEU A 275 ? 1.31303 0.83408 0.83615 -0.10212 -0.29850 -0.00172 311 LEU A N   
2228 C CA  . LEU A 275 ? 1.33250 0.86344 0.86395 -0.11690 -0.34573 0.02301  311 LEU A CA  
2229 C C   . LEU A 275 ? 1.42627 0.95914 0.98597 -0.13087 -0.37747 0.01509  311 LEU A C   
2230 O O   . LEU A 275 ? 1.49342 1.04517 1.11564 -0.12894 -0.40839 0.03408  311 LEU A O   
2231 C CB  . LEU A 275 ? 1.35428 0.88445 0.81499 -0.13441 -0.34839 0.03590  311 LEU A CB  
2232 C CG  . LEU A 275 ? 1.47588 1.02216 0.95495 -0.13919 -0.37159 0.07280  311 LEU A CG  
2233 C CD1 . LEU A 275 ? 1.60991 1.15758 1.01416 -0.15715 -0.36184 0.08064  311 LEU A CD1 
2234 C CD2 . LEU A 275 ? 1.47055 1.03054 1.00696 -0.14364 -0.41196 0.08833  311 LEU A CD2 
2235 N N   . SER A 276 ? 1.37107 0.88776 0.89636 -0.14370 -0.36599 -0.01350 312 SER A N   
2236 C CA  . SER A 276 ? 1.45726 0.98158 1.01695 -0.15855 -0.39021 -0.02250 312 SER A CA  
2237 C C   . SER A 276 ? 1.41922 0.95418 1.07257 -0.14714 -0.39708 -0.02115 312 SER A C   
2238 O O   . SER A 276 ? 1.53394 1.08377 1.23358 -0.15928 -0.42309 -0.02227 312 SER A O   
2239 C CB  . SER A 276 ? 1.44438 0.94688 0.95783 -0.17236 -0.36864 -0.05790 312 SER A CB  
2240 O OG  . SER A 276 ? 1.39620 0.87079 0.90920 -0.15760 -0.32818 -0.07903 312 SER A OG  
2241 N N   . VAL A 277 ? 1.29190 0.83238 0.98452 -0.11977 -0.36188 -0.01601 313 VAL A N   
2242 C CA  . VAL A 277 ? 1.40833 0.97108 1.19408 -0.10422 -0.35838 -0.00926 313 VAL A CA  
2243 C C   . VAL A 277 ? 1.35926 0.94867 1.19707 -0.10624 -0.40162 0.01457  313 VAL A C   
2244 O O   . VAL A 277 ? 1.36863 0.97864 1.27924 -0.10878 -0.41879 0.01606  313 VAL A O   
2245 C CB  . VAL A 277 ? 1.09916 0.66581 0.90246 -0.07525 -0.31567 -0.00769 313 VAL A CB  
2246 C CG1 . VAL A 277 ? 0.99963 0.59173 0.89110 -0.05973 -0.30870 -0.00253 313 VAL A CG1 
2247 C CG2 . VAL A 277 ? 1.30811 0.85006 1.06791 -0.07061 -0.27572 -0.02694 313 VAL A CG2 
2248 N N   . LEU A 278 ? 1.34086 0.93059 1.14785 -0.10508 -0.41924 0.03529  314 LEU A N   
2249 C CA  . LEU A 278 ? 1.32112 0.93151 1.18033 -0.10442 -0.46137 0.06229  314 LEU A CA  
2250 C C   . LEU A 278 ? 1.43766 1.05838 1.29476 -0.12643 -0.49570 0.06807  314 LEU A C   
2251 O O   . LEU A 278 ? 1.37948 1.02401 1.30757 -0.12318 -0.52118 0.08514  314 LEU A O   
2252 C CB  . LEU A 278 ? 1.31503 0.91816 1.14238 -0.09820 -0.46128 0.08550  314 LEU A CB  
2253 C CG  . LEU A 278 ? 1.24539 0.84173 1.07024 -0.07710 -0.42113 0.07884  314 LEU A CG  
2254 C CD1 . LEU A 278 ? 1.11131 0.70083 0.91167 -0.07697 -0.42423 0.10157  314 LEU A CD1 
2255 C CD2 . LEU A 278 ? 1.14058 0.75599 1.05499 -0.05360 -0.40328 0.07087  314 LEU A CD2 
2256 N N   . ASP A 279 ? 1.68146 1.28732 1.46173 -0.14675 -0.49117 0.05226  315 ASP A N   
2257 C CA  . ASP A 279 ? 1.68408 1.30435 1.45872 -0.16741 -0.52045 0.05396  315 ASP A CA  
2258 C C   . ASP A 279 ? 1.75033 1.38647 1.59648 -0.17271 -0.52955 0.03679  315 ASP A C   
2259 O O   . ASP A 279 ? 1.97998 1.64273 1.87304 -0.18064 -0.56129 0.04748  315 ASP A O   
2260 C CB  . ASP A 279 ? 1.77997 1.38290 1.45133 -0.18723 -0.51014 0.03733  315 ASP A CB  
2261 C CG  . ASP A 279 ? 1.97599 1.57440 1.58452 -0.18810 -0.50745 0.06005  315 ASP A CG  
2262 O OD1 . ASP A 279 ? 2.10328 1.70603 1.74769 -0.17320 -0.51016 0.08697  315 ASP A OD1 
2263 O OD2 . ASP A 279 ? 2.03978 1.63150 1.56703 -0.20443 -0.50070 0.04940  315 ASP A OD2 
2264 N N   . ASP A 280 ? 1.49422 1.11486 1.35368 -0.16916 -0.49992 0.01109  316 ASP A N   
2265 C CA  . ASP A 280 ? 1.58558 1.21983 1.51819 -0.17687 -0.50089 -0.00476 316 ASP A CA  
2266 C C   . ASP A 280 ? 1.50867 1.17903 1.55297 -0.16205 -0.51604 0.01424  316 ASP A C   
2267 O O   . ASP A 280 ? 1.54148 1.23791 1.65727 -0.17082 -0.52872 0.01082  316 ASP A O   
2268 C CB  . ASP A 280 ? 1.52939 1.13188 1.45199 -0.17533 -0.45762 -0.03231 316 ASP A CB  
2269 C CG  . ASP A 280 ? 1.52907 1.09751 1.35719 -0.18938 -0.43924 -0.05687 316 ASP A CG  
2270 O OD1 . ASP A 280 ? 1.64431 1.21870 1.41740 -0.20464 -0.46125 -0.05656 316 ASP A OD1 
2271 O OD2 . ASP A 280 ? 1.44317 0.97914 1.25482 -0.18370 -0.40008 -0.07622 316 ASP A OD2 
2272 N N   . LEU A 281 ? 1.34135 1.01608 1.40674 -0.13954 -0.51294 0.03235  317 LEU A N   
2273 C CA  . LEU A 281 ? 1.29987 1.00840 1.47504 -0.12043 -0.51692 0.04500  317 LEU A CA  
2274 C C   . LEU A 281 ? 1.24893 0.97492 1.45176 -0.11044 -0.54749 0.07555  317 LEU A C   
2275 O O   . LEU A 281 ? 1.17113 0.92060 1.46197 -0.08995 -0.54669 0.08565  317 LEU A O   
2276 C CB  . LEU A 281 ? 1.21963 0.92095 1.40268 -0.09171 -0.46174 0.03954  317 LEU A CB  
2277 C CG  . LEU A 281 ? 1.11982 0.79294 1.24646 -0.09301 -0.41504 0.01759  317 LEU A CG  
2278 C CD1 . LEU A 281 ? 1.08489 0.75285 1.20012 -0.06495 -0.37112 0.01748  317 LEU A CD1 
2279 C CD2 . LEU A 281 ? 1.23671 0.91876 1.41664 -0.10424 -0.40098 0.00335  317 LEU A CD2 
2280 N N   . GLY A 282 ? 1.27364 0.98658 1.40417 -0.12439 -0.56769 0.08908  318 GLY A N   
2281 C CA  . GLY A 282 ? 1.32241 1.04661 1.47734 -0.11997 -0.59355 0.11896  318 GLY A CA  
2282 C C   . GLY A 282 ? 1.18764 0.90106 1.35583 -0.09924 -0.57951 0.13460  318 GLY A C   
2283 O O   . GLY A 282 ? 1.22801 0.95763 1.47111 -0.08691 -0.58998 0.15087  318 GLY A O   
2284 N N   . GLN A 283 ? 1.08457 0.77161 1.18425 -0.09596 -0.55417 0.12781  319 GLN A N   
2285 C CA  . GLN A 283 ? 1.19102 0.86840 1.30023 -0.07903 -0.53686 0.13788  319 GLN A CA  
2286 C C   . GLN A 283 ? 1.26008 0.91516 1.27841 -0.09248 -0.53595 0.15237  319 GLN A C   
2287 O O   . GLN A 283 ? 1.39603 1.03869 1.33054 -0.11019 -0.53536 0.14593  319 GLN A O   
2288 C CB  . GLN A 283 ? 1.03741 0.71083 1.15971 -0.05935 -0.50304 0.11693  319 GLN A CB  
2289 C CG  . GLN A 283 ? 0.92471 0.62456 1.13508 -0.04599 -0.49853 0.10216  319 GLN A CG  
2290 C CD  . GLN A 283 ? 1.08778 0.81460 1.39936 -0.03554 -0.50893 0.11212  319 GLN A CD  
2291 O OE1 . GLN A 283 ? 1.19607 0.92032 1.52658 -0.02709 -0.50553 0.12253  319 GLN A OE1 
2292 N NE2 . GLN A 283 ? 0.99322 0.74834 1.37428 -0.03788 -0.52059 0.10728  319 GLN A NE2 
2293 N N   . ALA A 284 ? 1.11934 0.77180 1.15854 -0.08470 -0.53316 0.16985  320 ALA A N   
2294 C CA  . ALA A 284 ? 1.26504 0.90102 1.23287 -0.09637 -0.52988 0.18692  320 ALA A CA  
2295 C C   . ALA A 284 ? 1.37483 0.99793 1.32681 -0.08457 -0.49563 0.17600  320 ALA A C   
2296 O O   . ALA A 284 ? 1.30264 0.93266 1.31442 -0.06472 -0.47899 0.16114  320 ALA A O   
2297 C CB  . ALA A 284 ? 1.25506 0.89787 1.25851 -0.09900 -0.55492 0.21851  320 ALA A CB  
2298 N N   . CYS A 285 ? 1.41935 1.02740 1.29065 -0.09695 -0.48365 0.18244  321 CYS A N   
2299 C CA  . CYS A 285 ? 1.30379 0.90164 1.15610 -0.08817 -0.45238 0.17408  321 CYS A CA  
2300 C C   . CYS A 285 ? 1.49329 1.08833 1.36123 -0.09053 -0.45530 0.19903  321 CYS A C   
2301 O O   . CYS A 285 ? 1.65767 1.24299 1.46644 -0.10296 -0.44600 0.21206  321 CYS A O   
2302 C CB  . CYS A 285 ? 1.52861 1.11366 1.28771 -0.09896 -0.43204 0.16169  321 CYS A CB  
2303 S SG  . CYS A 285 ? 1.65511 1.23164 1.39616 -0.08562 -0.39330 0.14832  321 CYS A SG  
2304 N N   . ASP A 286 ? 1.43015 1.03451 1.38337 -0.07816 -0.46712 0.20530  322 ASP A N   
2305 C CA  . ASP A 286 ? 1.39986 0.99925 1.38079 -0.07914 -0.47299 0.22943  322 ASP A CA  
2306 C C   . ASP A 286 ? 1.24704 0.83962 1.24676 -0.06789 -0.44592 0.21715  322 ASP A C   
2307 O O   . ASP A 286 ? 1.24846 0.83142 1.25838 -0.07222 -0.44719 0.23730  322 ASP A O   
2308 C CB  . ASP A 286 ? 1.35734 0.96836 1.42439 -0.07038 -0.49756 0.24115  322 ASP A CB  
2309 C CG  . ASP A 286 ? 1.20506 0.83249 1.34418 -0.05044 -0.48931 0.21224  322 ASP A CG  
2310 O OD1 . ASP A 286 ? 1.07462 0.70304 1.22993 -0.03627 -0.46168 0.18733  322 ASP A OD1 
2311 O OD2 . ASP A 286 ? 1.42126 1.06283 1.60170 -0.04901 -0.50989 0.21504  322 ASP A OD2 
2312 N N   . GLY A 287 ? 1.26932 0.86633 1.27469 -0.05397 -0.42252 0.18597  323 GLY A N   
2313 C CA  . GLY A 287 ? 1.21930 0.81231 1.24317 -0.04286 -0.39825 0.17103  323 GLY A CA  
2314 C C   . GLY A 287 ? 1.08266 0.68948 1.18928 -0.02080 -0.38972 0.14714  323 GLY A C   
2315 O O   . GLY A 287 ? 0.92943 0.53363 1.05496 -0.01170 -0.37083 0.13123  323 GLY A O   
2316 N N   . ASP A 288 ? 1.03867 0.66111 1.19547 -0.01286 -0.40217 0.14294  324 ASP A N   
2317 C CA  . ASP A 288 ? 1.05343 0.69267 1.28731 0.00817  -0.38964 0.11844  324 ASP A CA  
2318 C C   . ASP A 288 ? 0.91426 0.56259 1.13004 0.02100  -0.36076 0.08696  324 ASP A C   
2319 O O   . ASP A 288 ? 1.02048 0.67321 1.20377 0.01954  -0.35903 0.08254  324 ASP A O   
2320 C CB  . ASP A 288 ? 1.01833 0.67392 1.30990 0.01181  -0.40944 0.12443  324 ASP A CB  
2321 C CG  . ASP A 288 ? 1.01555 0.68794 1.39472 0.03238  -0.39660 0.10334  324 ASP A CG  
2322 O OD1 . ASP A 288 ? 1.07168 0.74662 1.45808 0.04510  -0.36891 0.07648  324 ASP A OD1 
2323 O OD2 . ASP A 288 ? 1.07023 0.75357 1.51084 0.03560  -0.41403 0.11288  324 ASP A OD2 
2324 N N   . MET A 289 ? 0.89922 0.54867 1.13526 0.03300  -0.33893 0.06530  325 MET A N   
2325 C CA  . MET A 289 ? 0.99483 0.65458 1.21638 0.04672  -0.31125 0.03539  325 MET A CA  
2326 C C   . MET A 289 ? 0.80996 0.49006 1.09961 0.06560  -0.29589 0.00909  325 MET A C   
2327 O O   . MET A 289 ? 0.63374 0.31570 0.98293 0.06883  -0.30384 0.01068  325 MET A O   
2328 C CB  . MET A 289 ? 0.78194 0.42785 0.96231 0.04419  -0.29783 0.02733  325 MET A CB  
2329 C CG  . MET A 289 ? 1.06651 0.70543 1.17375 0.04013  -0.28925 0.02855  325 MET A CG  
2330 S SD  . MET A 289 ? 1.00727 0.62390 1.04872 0.01559  -0.30918 0.06438  325 MET A SD  
2331 C CE  . MET A 289 ? 1.18736 0.78614 1.22234 0.00534  -0.30708 0.07328  325 MET A CE  
2332 N N   . ASP A 290 ? 0.85605 0.55050 1.13464 0.07846  -0.27196 -0.01500 326 ASP A N   
2333 C CA  . ASP A 290 ? 0.66367 0.38032 0.99877 0.09605  -0.25305 -0.04075 326 ASP A CA  
2334 C C   . ASP A 290 ? 0.59213 0.30741 0.95951 0.10347  -0.24226 -0.06403 326 ASP A C   
2335 O O   . ASP A 290 ? 0.89452 0.62002 1.32513 0.11252  -0.23801 -0.07589 326 ASP A O   
2336 C CB  . ASP A 290 ? 0.97506 0.70575 1.28197 0.10735  -0.22799 -0.05873 326 ASP A CB  
2337 C CG  . ASP A 290 ? 1.06012 0.79212 1.35265 0.10103  -0.23656 -0.03990 326 ASP A CG  
2338 O OD1 . ASP A 290 ? 1.10861 0.83126 1.40374 0.08648  -0.26443 -0.01502 326 ASP A OD1 
2339 O OD2 . ASP A 290 ? 0.95996 0.70139 1.23868 0.11011  -0.21625 -0.05039 326 ASP A OD2 
2340 N N   . TRP A 291 ? 0.78130 0.48377 1.10963 0.09925  -0.23790 -0.07270 327 TRP A N   
2341 C CA  . TRP A 291 ? 0.91588 0.61638 1.27379 0.10390  -0.22839 -0.09955 327 TRP A CA  
2342 C C   . TRP A 291 ? 0.63853 0.32270 1.04867 0.09686  -0.24631 -0.08376 327 TRP A C   
2343 O O   . TRP A 291 ? 0.79684 0.47733 1.24440 0.10108  -0.23852 -0.10689 327 TRP A O   
2344 C CB  . TRP A 291 ? 0.96252 0.65493 1.27051 0.09842  -0.22343 -0.11225 327 TRP A CB  
2345 C CG  . TRP A 291 ? 0.87890 0.54826 1.14854 0.08052  -0.24226 -0.07947 327 TRP A CG  
2346 C CD1 . TRP A 291 ? 0.87143 0.51932 1.15892 0.06604  -0.25889 -0.05775 327 TRP A CD1 
2347 C CD2 . TRP A 291 ? 0.66886 0.33316 0.87393 0.07521  -0.24365 -0.06460 327 TRP A CD2 
2348 N NE1 . TRP A 291 ? 0.98651 0.61822 1.22189 0.05072  -0.26947 -0.03002 327 TRP A NE1 
2349 C CE2 . TRP A 291 ? 0.83777 0.47837 1.02209 0.05632  -0.26032 -0.03524 327 TRP A CE2 
2350 C CE3 . TRP A 291 ? 0.94501 0.62091 1.10767 0.08512  -0.23077 -0.07239 327 TRP A CE3 
2351 C CZ2 . TRP A 291 ? 0.81510 0.44391 0.93613 0.04671  -0.26312 -0.01643 327 TRP A CZ2 
2352 C CZ3 . TRP A 291 ? 0.85417 0.53040 0.95489 0.07391  -0.22965 -0.05207 327 TRP A CZ3 
2353 C CH2 . TRP A 291 ? 0.94093 0.59540 1.02100 0.05527  -0.24459 -0.02688 327 TRP A CH2 
2354 N N   . MET A 292 ? 0.79318 0.46730 1.20539 0.08611  -0.27035 -0.04595 328 MET A N   
2355 C CA  . MET A 292 ? 0.86960 0.52926 1.33279 0.08106  -0.28936 -0.02590 328 MET A CA  
2356 C C   . MET A 292 ? 0.97205 0.64643 1.51024 0.09531  -0.28694 -0.03662 328 MET A C   
2357 O O   . MET A 292 ? 1.15661 0.81938 1.74659 0.09432  -0.30223 -0.02142 328 MET A O   
2358 C CB  . MET A 292 ? 0.74841 0.39518 1.18030 0.06399  -0.31701 0.01844  328 MET A CB  
2359 C CG  . MET A 292 ? 0.69741 0.32751 1.05771 0.04847  -0.31831 0.03178  328 MET A CG  
2360 S SD  . MET A 292 ? 1.04755 0.66424 1.36039 0.02713  -0.34726 0.08066  328 MET A SD  
2361 C CE  . MET A 292 ? 1.12611 0.72961 1.50634 0.02454  -0.36853 0.10581  328 MET A CE  
2362 N N   . HIS A 293 ? 0.81621 0.51539 1.36351 0.10869  -0.26715 -0.06092 329 HIS A N   
2363 C CA  . HIS A 293 ? 0.92865 0.64516 1.54933 0.12305  -0.25929 -0.07490 329 HIS A CA  
2364 C C   . HIS A 293 ? 0.96358 0.69166 1.60190 0.13816  -0.22607 -0.12149 329 HIS A C   
2365 O O   . HIS A 293 ? 1.00729 0.75409 1.69912 0.15168  -0.21115 -0.13940 329 HIS A O   
2366 C CB  . HIS A 293 ? 0.95692 0.69579 1.58327 0.12484  -0.26314 -0.06257 329 HIS A CB  
2367 C CG  . HIS A 293 ? 0.66947 0.39954 1.28257 0.10917  -0.29805 -0.02089 329 HIS A CG  
2368 N ND1 . HIS A 293 ? 0.99198 0.71743 1.66051 0.10634  -0.32380 0.00281  329 HIS A ND1 
2369 C CD2 . HIS A 293 ? 0.69020 0.41469 1.23838 0.09517  -0.31169 0.00012  329 HIS A CD2 
2370 C CE1 . HIS A 293 ? 0.70999 0.42878 1.34418 0.09027  -0.35274 0.03660  329 HIS A CE1 
2371 N NE2 . HIS A 293 ? 0.85254 0.57005 1.41302 0.08284  -0.34531 0.03410  329 HIS A NE2 
2372 N N   . LEU A 294 ? 0.99813 0.71729 1.59232 0.13533  -0.21415 -0.14274 330 LEU A N   
2373 C CA  . LEU A 294 ? 1.20389 0.93526 1.80414 0.14712  -0.18452 -0.18994 330 LEU A CA  
2374 C C   . LEU A 294 ? 1.10695 0.82662 1.77614 0.15223  -0.18283 -0.20720 330 LEU A C   
2375 O O   . LEU A 294 ? 1.23461 0.92887 1.93099 0.14363  -0.20443 -0.18521 330 LEU A O   
2376 C CB  . LEU A 294 ? 1.02894 0.75591 1.56391 0.14034  -0.17762 -0.20777 330 LEU A CB  
2377 C CG  . LEU A 294 ? 1.13805 0.87928 1.60335 0.14034  -0.17068 -0.20389 330 LEU A CG  
2378 C CD1 . LEU A 294 ? 0.97894 0.70993 1.39053 0.12980  -0.17555 -0.20997 330 LEU A CD1 
2379 C CD2 . LEU A 294 ? 0.99014 0.76223 1.44843 0.15647  -0.13978 -0.23593 330 LEU A CD2 
2380 N N   . ASN A 295 ? 1.23987 0.97774 1.93632 0.16664  -0.15511 -0.24699 331 ASN A N   
2381 C CA  . ASN A 295 ? 1.43168 1.15837 2.18779 0.17304  -0.14673 -0.27506 331 ASN A CA  
2382 C C   . ASN A 295 ? 1.32227 1.03270 2.15525 0.17445  -0.16890 -0.24465 331 ASN A C   
2383 O O   . ASN A 295 ? 1.45590 1.13817 2.32266 0.16948  -0.18226 -0.23946 331 ASN A O   
2384 C CB  . ASN A 295 ? 1.40371 1.11006 2.13286 0.16263  -0.14768 -0.29645 331 ASN A CB  
2385 C CG  . ASN A 295 ? 1.51851 1.24588 2.17678 0.16221  -0.12677 -0.33120 331 ASN A CG  
2386 O OD1 . ASN A 295 ? 1.54143 1.29720 2.18522 0.17418  -0.10145 -0.35600 331 ASN A OD1 
2387 N ND2 . ASN A 295 ? 1.61355 1.32947 2.22755 0.14812  -0.13714 -0.33181 331 ASN A ND2 
2388 N N   . GLY A 296 ? 1.43925 1.16841 2.30229 0.18090  -0.17353 -0.22356 332 GLY A N   
2389 C CA  . GLY A 296 ? 1.39009 1.11029 2.32914 0.18362  -0.19558 -0.19537 332 GLY A CA  
2390 C C   . GLY A 296 ? 1.45623 1.15169 2.38337 0.16792  -0.23336 -0.14646 332 GLY A C   
2391 O O   . GLY A 296 ? 1.35936 1.04484 2.34740 0.16942  -0.25476 -0.12032 332 GLY A O   
2392 N N   . GLY A 297 ? 1.52880 1.21468 2.37900 0.15314  -0.24156 -0.13273 333 GLY A N   
2393 C CA  . GLY A 297 ? 1.44151 1.10414 2.26883 0.13666  -0.27327 -0.08779 333 GLY A CA  
2394 C C   . GLY A 297 ? 1.51216 1.14555 2.31663 0.12610  -0.27410 -0.09138 333 GLY A C   
2395 O O   . GLY A 297 ? 1.50555 1.12083 2.27491 0.11036  -0.29505 -0.05551 333 GLY A O   
2396 N N   . ARG A 298 ? 1.50628 1.13488 2.32957 0.13292  -0.25136 -0.13460 334 ARG A N   
2397 C CA  . ARG A 298 ? 1.56034 1.16177 2.36875 0.12109  -0.25199 -0.14165 334 ARG A CA  
2398 C C   . ARG A 298 ? 1.60580 1.21062 2.33009 0.10705  -0.25197 -0.13627 334 ARG A C   
2399 O O   . ARG A 298 ? 1.61601 1.19784 2.32010 0.09129  -0.26314 -0.11769 334 ARG A O   
2400 C CB  . ARG A 298 ? 1.49244 1.09196 2.33482 0.13024  -0.22727 -0.19574 334 ARG A CB  
2401 C CG  . ARG A 298 ? 1.47181 1.07381 2.39602 0.14783  -0.21943 -0.21127 334 ARG A CG  
2402 C CD  . ARG A 298 ? 1.56837 1.13620 2.56051 0.14591  -0.23946 -0.18434 334 ARG A CD  
2403 N NE  . ARG A 298 ? 1.62684 1.16295 2.61116 0.13209  -0.24155 -0.19072 334 ARG A NE  
2404 C CZ  . ARG A 298 ? 1.73676 1.26341 2.73804 0.13362  -0.22194 -0.23955 334 ARG A CZ  
2405 N NH1 . ARG A 298 ? 1.74465 1.29140 2.76446 0.14885  -0.19683 -0.28785 334 ARG A NH1 
2406 N NH2 . ARG A 298 ? 1.69918 1.19588 2.69773 0.11814  -0.22699 -0.24080 334 ARG A NH2 
2407 N N   . GLY A 299 ? 1.43345 1.06601 2.11120 0.11254  -0.23862 -0.15111 335 GLY A N   
2408 C CA  . GLY A 299 ? 1.30062 0.93842 1.90325 0.10264  -0.23542 -0.15254 335 GLY A CA  
2409 C C   . GLY A 299 ? 1.43755 1.09221 2.01931 0.10884  -0.21029 -0.20418 335 GLY A C   
2410 O O   . GLY A 299 ? 1.41368 1.07827 2.03172 0.12101  -0.19280 -0.23993 335 GLY A O   
2411 N N   . TRP A 300 ? 1.42755 1.08689 1.94808 0.09975  -0.20897 -0.20850 336 TRP A N   
2412 C CA  . TRP A 300 ? 1.47742 1.15907 1.96625 0.10418  -0.18894 -0.25508 336 TRP A CA  
2413 C C   . TRP A 300 ? 1.66150 1.33262 2.18320 0.09843  -0.18440 -0.28920 336 TRP A C   
2414 O O   . TRP A 300 ? 1.49792 1.14163 2.04305 0.08426  -0.19863 -0.27309 336 TRP A O   
2415 C CB  . TRP A 300 ? 1.35191 1.04258 1.77172 0.09587  -0.19258 -0.24842 336 TRP A CB  
2416 C CG  . TRP A 300 ? 1.35266 1.02032 1.76608 0.07567  -0.20913 -0.22957 336 TRP A CG  
2417 C CD1 . TRP A 300 ? 1.34622 1.01566 1.75507 0.06363  -0.20810 -0.25568 336 TRP A CD1 
2418 C CD2 . TRP A 300 ? 1.30572 0.94807 1.71556 0.06305  -0.22813 -0.18025 336 TRP A CD2 
2419 N NE1 . TRP A 300 ? 1.31195 0.95744 1.72066 0.04408  -0.22337 -0.22488 336 TRP A NE1 
2420 C CE2 . TRP A 300 ? 1.41252 1.04017 1.81805 0.04372  -0.23493 -0.17779 336 TRP A CE2 
2421 C CE3 . TRP A 300 ? 1.17585 0.80955 1.58374 0.06438  -0.24020 -0.13854 336 TRP A CE3 
2422 C CZ2 . TRP A 300 ? 1.32132 0.92382 1.71830 0.02634  -0.25019 -0.13327 336 TRP A CZ2 
2423 C CZ3 . TRP A 300 ? 1.22694 0.83740 1.62043 0.04742  -0.25779 -0.09611 336 TRP A CZ3 
2424 C CH2 . TRP A 300 ? 1.38568 0.97962 1.77257 0.02896  -0.26112 -0.09269 336 TRP A CH2 
2425 N N   . ASP A 301 ? 2.03695 1.72978 2.55824 0.10838  -0.16347 -0.33656 337 ASP A N   
2426 C CA  . ASP A 301 ? 1.95986 1.64524 2.51004 0.10353  -0.15700 -0.37653 337 ASP A CA  
2427 C C   . ASP A 301 ? 2.07397 1.78217 2.56825 0.09340  -0.15336 -0.40873 337 ASP A C   
2428 O O   . ASP A 301 ? 1.95491 1.68254 2.39262 0.09085  -0.15713 -0.39657 337 ASP A O   
2429 C CB  . ASP A 301 ? 2.00538 1.69976 2.59441 0.12034  -0.13625 -0.40955 337 ASP A CB  
2430 C CG  . ASP A 301 ? 2.05119 1.71225 2.72150 0.12171  -0.14282 -0.40305 337 ASP A CG  
2431 O OD1 . ASP A 301 ? 2.12565 1.75664 2.81834 0.10909  -0.16352 -0.37075 337 ASP A OD1 
2432 O OD2 . ASP A 301 ? 2.15307 1.81804 2.86533 0.13563  -0.12631 -0.42956 337 ASP A OD2 
2433 N N   . ALA A 302 ? 2.09313 1.80061 2.60439 0.08743  -0.14724 -0.45100 338 ALA A N   
2434 C CA  . ALA A 302 ? 2.14665 1.88010 2.60977 0.07537  -0.14767 -0.48286 338 ALA A CA  
2435 C C   . ALA A 302 ? 2.16883 1.94233 2.58928 0.08707  -0.12671 -0.52722 338 ALA A C   
2436 O O   . ALA A 302 ? 2.12137 1.93113 2.47725 0.09064  -0.12347 -0.52712 338 ALA A O   
2437 C CB  . ALA A 302 ? 2.07250 1.78161 2.57565 0.05671  -0.15704 -0.50105 338 ALA A CB  
2438 N N   . THR A 303 ? 2.14886 1.91632 2.60301 0.09336  -0.11159 -0.56427 339 THR A N   
2439 C CA  . THR A 303 ? 2.18825 1.99275 2.59758 0.10169  -0.09012 -0.60937 339 THR A CA  
2440 C C   . THR A 303 ? 2.23015 2.05407 2.62215 0.12251  -0.06865 -0.59999 339 THR A C   
2441 O O   . THR A 303 ? 2.26390 2.12538 2.59848 0.12911  -0.05046 -0.62517 339 THR A O   
2442 C CB  . THR A 303 ? 2.09826 1.88746 2.54812 0.09910  -0.08045 -0.65765 339 THR A CB  
2443 O OG1 . THR A 303 ? 2.09623 1.92132 2.49709 0.10746  -0.05744 -0.70087 339 THR A OG1 
2444 C CG2 . THR A 303 ? 2.01611 1.76580 2.55027 0.10960  -0.07580 -0.64528 339 THR A CG2 
2445 N N   . ILE A 304 ? 2.13519 1.93660 2.57400 0.13188  -0.07070 -0.56249 340 ILE A N   
2446 C CA  . ILE A 304 ? 2.00505 1.82512 2.43824 0.15034  -0.04966 -0.55405 340 ILE A CA  
2447 C C   . ILE A 304 ? 2.00267 1.84713 2.37249 0.15260  -0.05198 -0.52451 340 ILE A C   
2448 O O   . ILE A 304 ? 1.98639 1.86226 2.31608 0.16436  -0.02956 -0.53175 340 ILE A O   
2449 C CB  . ILE A 304 ? 1.90190 1.69279 2.41708 0.15909  -0.05280 -0.52746 340 ILE A CB  
2450 C CG1 . ILE A 304 ? 1.91263 1.68366 2.49145 0.16176  -0.04432 -0.56201 340 ILE A CG1 
2451 C CG2 . ILE A 304 ? 1.84253 1.65487 2.35679 0.17559  -0.03476 -0.51139 340 ILE A CG2 
2452 C CD1 . ILE A 304 ? 1.93639 1.66708 2.56387 0.14795  -0.06875 -0.55101 340 ILE A CD1 
2453 N N   . ASN A 305 ? 2.04936 1.87961 2.40841 0.14155  -0.07711 -0.49099 341 ASN A N   
2454 C CA  . ASN A 305 ? 1.96643 1.81289 2.27310 0.14459  -0.08124 -0.46048 341 ASN A CA  
2455 C C   . ASN A 305 ? 2.03265 1.91031 2.26693 0.13746  -0.08585 -0.47411 341 ASN A C   
2456 O O   . ASN A 305 ? 2.07055 1.98052 2.24711 0.14684  -0.07421 -0.47054 341 ASN A O   
2457 C CB  . ASN A 305 ? 1.76412 1.57671 2.09990 0.13797  -0.10536 -0.41218 341 ASN A CB  
2458 C CG  . ASN A 305 ? 1.69289 1.48839 2.08533 0.14744  -0.10305 -0.38755 341 ASN A CG  
2459 O OD1 . ASN A 305 ? 1.57278 1.33815 2.02092 0.14170  -0.11847 -0.36888 341 ASN A OD1 
2460 N ND2 . ASN A 305 ? 1.65520 1.47306 2.03502 0.16164  -0.08406 -0.38566 341 ASN A ND2 
2461 N N   . LYS A 306 ? 2.19714 2.06841 2.43567 0.12100  -0.10293 -0.48715 342 LYS A N   
2462 C CA  . LYS A 306 ? 2.21126 2.11660 2.38919 0.11255  -0.11252 -0.49579 342 LYS A CA  
2463 C C   . LYS A 306 ? 2.27000 2.22172 2.39074 0.11995  -0.09411 -0.52862 342 LYS A C   
2464 O O   . LYS A 306 ? 2.32217 2.31071 2.37902 0.12587  -0.09233 -0.51765 342 LYS A O   
2465 C CB  . LYS A 306 ? 2.08728 1.97853 2.29324 0.09146  -0.13242 -0.50726 342 LYS A CB  
2466 C CG  . LYS A 306 ? 1.98005 1.88841 2.15340 0.07987  -0.15227 -0.48815 342 LYS A CG  
2467 C CD  . LYS A 306 ? 1.80736 1.68120 2.00163 0.07785  -0.16396 -0.44241 342 LYS A CD  
2468 C CE  . LYS A 306 ? 1.59556 1.48597 1.76305 0.06538  -0.18172 -0.42560 342 LYS A CE  
2469 N NZ  . LYS A 306 ? 1.45419 1.30778 1.63705 0.06117  -0.19207 -0.38247 342 LYS A NZ  
# 
