data_9EDY
# 
_entry.id   9EDY 
# 
_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   9EDY         pdb_00009edy 10.2210/pdb9edy/pdb 
WWPDB D_1000290240 ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2025-01-08 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9EDY 
_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 2b: 6-fluoro-2-(4-fluorophenyl)-3-(pyridin-4-yl)pyrazolo[1,5-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'                        35625.461 1  2.7.11.1 ? 'residues 35-345' 
? 
2 non-polymer syn '6-fluoro-2-(4-fluorophenyl)-3-(pyridin-4-yl)pyrazolo[1,5-a]pyridine' 307.297   1  ?        ? ?                 
? 
3 non-polymer syn 'CHLORIDE ION'                                                        35.453    3  ?        ? ?                 
? 
4 water       nat water                                                                 18.015    75 ?        ? ?                 
? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        Yck2 
# 
_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       
;NNSSVVGLHYKIGKKIGEGSFGVIFEGTNIINGVPVAIKFEPRKTEAPQLRDEYRTYKHLQGCDGIPNAYYFGQEGLHNI
LVIDLLGPSLEDLFDWCGRRFSVKTVVQVAIQMLTLVEEVHRHDLIYRDIKPDNFLIGRRGATDENNVHLIDFGMAKQYR
DPRTKQHIPYREKKSLSGTARYMSINTHLGREQSRRDDLEALGHVFFYFLRGQLPWQGLKAPTNKQKYEKIGDKKRTTPA
VTLCDGLPQQFAEYLDSVRSLPFDAEPPYEEYRMLLLSVLDDLGQACDGDMDWMHLNGGRGWDATINKKPN
;
_entity_poly.pdbx_seq_one_letter_code_can   
;NNSSVVGLHYKIGKKIGEGSFGVIFEGTNIINGVPVAIKFEPRKTEAPQLRDEYRTYKHLQGCDGIPNAYYFGQEGLHNI
LVIDLLGPSLEDLFDWCGRRFSVKTVVQVAIQMLTLVEEVHRHDLIYRDIKPDNFLIGRRGATDENNVHLIDFGMAKQYR
DPRTKQHIPYREKKSLSGTARYMSINTHLGREQSRRDDLEALGHVFFYFLRGQLPWQGLKAPTNKQKYEKIGDKKRTTPA
VTLCDGLPQQFAEYLDSVRSLPFDAEPPYEEYRMLLLSVLDDLGQACDGDMDWMHLNGGRGWDATINKKPN
;
_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 '6-fluoro-2-(4-fluorophenyl)-3-(pyridin-4-yl)pyrazolo[1,5-a]pyridine' A1BIN 
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   ASN n 
1 2   ASN n 
1 3   SER n 
1 4   SER n 
1 5   VAL n 
1 6   VAL n 
1 7   GLY n 
1 8   LEU n 
1 9   HIS n 
1 10  TYR n 
1 11  LYS n 
1 12  ILE n 
1 13  GLY n 
1 14  LYS n 
1 15  LYS n 
1 16  ILE n 
1 17  GLY n 
1 18  GLU n 
1 19  GLY n 
1 20  SER n 
1 21  PHE n 
1 22  GLY n 
1 23  VAL n 
1 24  ILE n 
1 25  PHE n 
1 26  GLU n 
1 27  GLY n 
1 28  THR n 
1 29  ASN n 
1 30  ILE n 
1 31  ILE n 
1 32  ASN n 
1 33  GLY n 
1 34  VAL n 
1 35  PRO n 
1 36  VAL n 
1 37  ALA n 
1 38  ILE n 
1 39  LYS n 
1 40  PHE n 
1 41  GLU n 
1 42  PRO n 
1 43  ARG n 
1 44  LYS n 
1 45  THR n 
1 46  GLU n 
1 47  ALA n 
1 48  PRO n 
1 49  GLN n 
1 50  LEU n 
1 51  ARG n 
1 52  ASP n 
1 53  GLU n 
1 54  TYR n 
1 55  ARG n 
1 56  THR n 
1 57  TYR n 
1 58  LYS n 
1 59  HIS n 
1 60  LEU n 
1 61  GLN n 
1 62  GLY n 
1 63  CYS n 
1 64  ASP n 
1 65  GLY n 
1 66  ILE n 
1 67  PRO n 
1 68  ASN n 
1 69  ALA n 
1 70  TYR n 
1 71  TYR n 
1 72  PHE n 
1 73  GLY n 
1 74  GLN n 
1 75  GLU n 
1 76  GLY n 
1 77  LEU n 
1 78  HIS n 
1 79  ASN n 
1 80  ILE n 
1 81  LEU n 
1 82  VAL n 
1 83  ILE n 
1 84  ASP n 
1 85  LEU n 
1 86  LEU n 
1 87  GLY n 
1 88  PRO n 
1 89  SER n 
1 90  LEU n 
1 91  GLU n 
1 92  ASP n 
1 93  LEU n 
1 94  PHE n 
1 95  ASP n 
1 96  TRP n 
1 97  CYS n 
1 98  GLY n 
1 99  ARG n 
1 100 ARG n 
1 101 PHE n 
1 102 SER n 
1 103 VAL n 
1 104 LYS n 
1 105 THR n 
1 106 VAL n 
1 107 VAL n 
1 108 GLN n 
1 109 VAL n 
1 110 ALA n 
1 111 ILE n 
1 112 GLN n 
1 113 MET n 
1 114 LEU n 
1 115 THR n 
1 116 LEU n 
1 117 VAL n 
1 118 GLU n 
1 119 GLU n 
1 120 VAL n 
1 121 HIS n 
1 122 ARG n 
1 123 HIS n 
1 124 ASP n 
1 125 LEU n 
1 126 ILE n 
1 127 TYR n 
1 128 ARG n 
1 129 ASP n 
1 130 ILE n 
1 131 LYS n 
1 132 PRO n 
1 133 ASP n 
1 134 ASN n 
1 135 PHE n 
1 136 LEU n 
1 137 ILE n 
1 138 GLY n 
1 139 ARG n 
1 140 ARG n 
1 141 GLY n 
1 142 ALA n 
1 143 THR n 
1 144 ASP n 
1 145 GLU n 
1 146 ASN n 
1 147 ASN n 
1 148 VAL n 
1 149 HIS n 
1 150 LEU n 
1 151 ILE n 
1 152 ASP n 
1 153 PHE n 
1 154 GLY n 
1 155 MET n 
1 156 ALA n 
1 157 LYS n 
1 158 GLN n 
1 159 TYR n 
1 160 ARG n 
1 161 ASP n 
1 162 PRO n 
1 163 ARG n 
1 164 THR n 
1 165 LYS n 
1 166 GLN n 
1 167 HIS n 
1 168 ILE n 
1 169 PRO n 
1 170 TYR n 
1 171 ARG n 
1 172 GLU n 
1 173 LYS n 
1 174 LYS n 
1 175 SER n 
1 176 LEU n 
1 177 SER n 
1 178 GLY n 
1 179 THR n 
1 180 ALA n 
1 181 ARG n 
1 182 TYR n 
1 183 MET n 
1 184 SER n 
1 185 ILE n 
1 186 ASN n 
1 187 THR n 
1 188 HIS n 
1 189 LEU n 
1 190 GLY n 
1 191 ARG n 
1 192 GLU n 
1 193 GLN n 
1 194 SER n 
1 195 ARG n 
1 196 ARG n 
1 197 ASP n 
1 198 ASP n 
1 199 LEU n 
1 200 GLU n 
1 201 ALA n 
1 202 LEU n 
1 203 GLY n 
1 204 HIS n 
1 205 VAL n 
1 206 PHE n 
1 207 PHE n 
1 208 TYR n 
1 209 PHE n 
1 210 LEU n 
1 211 ARG n 
1 212 GLY n 
1 213 GLN n 
1 214 LEU n 
1 215 PRO n 
1 216 TRP n 
1 217 GLN n 
1 218 GLY n 
1 219 LEU n 
1 220 LYS n 
1 221 ALA n 
1 222 PRO n 
1 223 THR n 
1 224 ASN n 
1 225 LYS n 
1 226 GLN n 
1 227 LYS n 
1 228 TYR n 
1 229 GLU n 
1 230 LYS n 
1 231 ILE n 
1 232 GLY n 
1 233 ASP n 
1 234 LYS n 
1 235 LYS n 
1 236 ARG n 
1 237 THR n 
1 238 THR n 
1 239 PRO n 
1 240 ALA n 
1 241 VAL n 
1 242 THR n 
1 243 LEU n 
1 244 CYS n 
1 245 ASP n 
1 246 GLY n 
1 247 LEU n 
1 248 PRO n 
1 249 GLN n 
1 250 GLN n 
1 251 PHE n 
1 252 ALA n 
1 253 GLU n 
1 254 TYR n 
1 255 LEU n 
1 256 ASP n 
1 257 SER n 
1 258 VAL n 
1 259 ARG n 
1 260 SER n 
1 261 LEU n 
1 262 PRO n 
1 263 PHE n 
1 264 ASP n 
1 265 ALA n 
1 266 GLU n 
1 267 PRO n 
1 268 PRO n 
1 269 TYR n 
1 270 GLU n 
1 271 GLU n 
1 272 TYR n 
1 273 ARG n 
1 274 MET n 
1 275 LEU n 
1 276 LEU n 
1 277 LEU n 
1 278 SER n 
1 279 VAL n 
1 280 LEU n 
1 281 ASP n 
1 282 ASP n 
1 283 LEU n 
1 284 GLY n 
1 285 GLN n 
1 286 ALA n 
1 287 CYS n 
1 288 ASP n 
1 289 GLY n 
1 290 ASP n 
1 291 MET n 
1 292 ASP n 
1 293 TRP n 
1 294 MET n 
1 295 HIS n 
1 296 LEU n 
1 297 ASN n 
1 298 GLY n 
1 299 GLY n 
1 300 ARG n 
1 301 GLY n 
1 302 TRP n 
1 303 ASP n 
1 304 ALA n 
1 305 THR n 
1 306 ILE n 
1 307 ASN n 
1 308 LYS n 
1 309 LYS n 
1 310 PRO n 
1 311 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                   311 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 FOB64_000203 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Candida albicans' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     5476 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     562 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               LOBSTR 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          plasmid 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       pMCSG53 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
A1BIN non-polymer         . '6-fluoro-2-(4-fluorophenyl)-3-(pyridin-4-yl)pyrazolo[1,5-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   ASN 1   35  35  ASN ASN A . n 
A 1 2   ASN 2   36  36  ASN ASN A . n 
A 1 3   SER 3   37  37  SER SER A . n 
A 1 4   SER 4   38  38  SER SER A . n 
A 1 5   VAL 5   39  39  VAL VAL A . n 
A 1 6   VAL 6   40  40  VAL VAL A . n 
A 1 7   GLY 7   41  41  GLY GLY A . n 
A 1 8   LEU 8   42  42  LEU LEU A . n 
A 1 9   HIS 9   43  43  HIS HIS A . n 
A 1 10  TYR 10  44  44  TYR TYR A . n 
A 1 11  LYS 11  45  45  LYS LYS A . n 
A 1 12  ILE 12  46  46  ILE ILE A . n 
A 1 13  GLY 13  47  47  GLY GLY A . n 
A 1 14  LYS 14  48  48  LYS LYS A . n 
A 1 15  LYS 15  49  49  LYS LYS A . n 
A 1 16  ILE 16  50  50  ILE ILE A . n 
A 1 17  GLY 17  51  51  GLY GLY A . n 
A 1 18  GLU 18  52  52  GLU GLU A . n 
A 1 19  GLY 19  53  53  GLY GLY A . n 
A 1 20  SER 20  54  54  SER SER A . n 
A 1 21  PHE 21  55  55  PHE PHE A . n 
A 1 22  GLY 22  56  56  GLY GLY A . n 
A 1 23  VAL 23  57  57  VAL VAL A . n 
A 1 24  ILE 24  58  58  ILE ILE A . n 
A 1 25  PHE 25  59  59  PHE PHE A . n 
A 1 26  GLU 26  60  60  GLU GLU A . n 
A 1 27  GLY 27  61  61  GLY GLY A . n 
A 1 28  THR 28  62  62  THR THR A . n 
A 1 29  ASN 29  63  63  ASN ASN A . n 
A 1 30  ILE 30  64  64  ILE ILE A . n 
A 1 31  ILE 31  65  65  ILE ILE A . n 
A 1 32  ASN 32  66  66  ASN ASN A . n 
A 1 33  GLY 33  67  67  GLY GLY A . n 
A 1 34  VAL 34  68  68  VAL VAL A . n 
A 1 35  PRO 35  69  69  PRO PRO A . n 
A 1 36  VAL 36  70  70  VAL VAL A . n 
A 1 37  ALA 37  71  71  ALA ALA A . n 
A 1 38  ILE 38  72  72  ILE ILE A . n 
A 1 39  LYS 39  73  73  LYS LYS A . n 
A 1 40  PHE 40  74  74  PHE PHE A . n 
A 1 41  GLU 41  75  75  GLU GLU A . n 
A 1 42  PRO 42  76  76  PRO PRO A . n 
A 1 43  ARG 43  77  77  ARG ARG A . n 
A 1 44  LYS 44  78  78  LYS LYS A . n 
A 1 45  THR 45  79  79  THR THR A . n 
A 1 46  GLU 46  80  80  GLU GLU A . n 
A 1 47  ALA 47  81  81  ALA ALA A . n 
A 1 48  PRO 48  82  82  PRO PRO A . n 
A 1 49  GLN 49  83  83  GLN GLN A . n 
A 1 50  LEU 50  84  84  LEU LEU A . n 
A 1 51  ARG 51  85  85  ARG ARG A . n 
A 1 52  ASP 52  86  86  ASP ASP A . n 
A 1 53  GLU 53  87  87  GLU GLU A . n 
A 1 54  TYR 54  88  88  TYR TYR A . n 
A 1 55  ARG 55  89  89  ARG ARG A . n 
A 1 56  THR 56  90  90  THR THR A . n 
A 1 57  TYR 57  91  91  TYR TYR A . n 
A 1 58  LYS 58  92  92  LYS LYS A . n 
A 1 59  HIS 59  93  93  HIS HIS A . n 
A 1 60  LEU 60  94  94  LEU LEU A . n 
A 1 61  GLN 61  95  95  GLN GLN A . n 
A 1 62  GLY 62  96  96  GLY GLY A . n 
A 1 63  CYS 63  97  97  CYS CYS A . n 
A 1 64  ASP 64  98  98  ASP ASP A . n 
A 1 65  GLY 65  99  99  GLY GLY A . n 
A 1 66  ILE 66  100 100 ILE ILE A . n 
A 1 67  PRO 67  101 101 PRO PRO A . n 
A 1 68  ASN 68  102 102 ASN ASN A . n 
A 1 69  ALA 69  103 103 ALA ALA A . n 
A 1 70  TYR 70  104 104 TYR TYR A . n 
A 1 71  TYR 71  105 105 TYR TYR A . n 
A 1 72  PHE 72  106 106 PHE PHE A . n 
A 1 73  GLY 73  107 107 GLY GLY A . n 
A 1 74  GLN 74  108 108 GLN GLN A . n 
A 1 75  GLU 75  109 109 GLU GLU A . n 
A 1 76  GLY 76  110 110 GLY GLY A . n 
A 1 77  LEU 77  111 111 LEU LEU A . n 
A 1 78  HIS 78  112 112 HIS HIS A . n 
A 1 79  ASN 79  113 113 ASN ASN A . n 
A 1 80  ILE 80  114 114 ILE ILE A . n 
A 1 81  LEU 81  115 115 LEU LEU A . n 
A 1 82  VAL 82  116 116 VAL VAL A . n 
A 1 83  ILE 83  117 117 ILE ILE A . n 
A 1 84  ASP 84  118 118 ASP ASP A . n 
A 1 85  LEU 85  119 119 LEU LEU A . n 
A 1 86  LEU 86  120 120 LEU LEU A . n 
A 1 87  GLY 87  121 121 GLY GLY A . n 
A 1 88  PRO 88  122 122 PRO PRO A . n 
A 1 89  SER 89  123 123 SER SER A . n 
A 1 90  LEU 90  124 124 LEU LEU A . n 
A 1 91  GLU 91  125 125 GLU GLU A . n 
A 1 92  ASP 92  126 126 ASP ASP A . n 
A 1 93  LEU 93  127 127 LEU LEU A . n 
A 1 94  PHE 94  128 128 PHE PHE A . n 
A 1 95  ASP 95  129 129 ASP ASP A . n 
A 1 96  TRP 96  130 130 TRP TRP A . n 
A 1 97  CYS 97  131 131 CYS CYS A . n 
A 1 98  GLY 98  132 132 GLY GLY A . n 
A 1 99  ARG 99  133 133 ARG ARG A . n 
A 1 100 ARG 100 134 134 ARG ARG A . n 
A 1 101 PHE 101 135 135 PHE PHE A . n 
A 1 102 SER 102 136 136 SER SER A . n 
A 1 103 VAL 103 137 137 VAL VAL A . n 
A 1 104 LYS 104 138 138 LYS LYS A . n 
A 1 105 THR 105 139 139 THR THR A . n 
A 1 106 VAL 106 140 140 VAL VAL A . n 
A 1 107 VAL 107 141 141 VAL VAL A . n 
A 1 108 GLN 108 142 142 GLN GLN A . n 
A 1 109 VAL 109 143 143 VAL VAL A . n 
A 1 110 ALA 110 144 144 ALA ALA A . n 
A 1 111 ILE 111 145 145 ILE ILE A . n 
A 1 112 GLN 112 146 146 GLN GLN A . n 
A 1 113 MET 113 147 147 MET MET A . n 
A 1 114 LEU 114 148 148 LEU LEU A . n 
A 1 115 THR 115 149 149 THR THR A . n 
A 1 116 LEU 116 150 150 LEU LEU A . n 
A 1 117 VAL 117 151 151 VAL VAL A . n 
A 1 118 GLU 118 152 152 GLU GLU A . n 
A 1 119 GLU 119 153 153 GLU GLU A . n 
A 1 120 VAL 120 154 154 VAL VAL A . n 
A 1 121 HIS 121 155 155 HIS HIS A . n 
A 1 122 ARG 122 156 156 ARG ARG A . n 
A 1 123 HIS 123 157 157 HIS HIS A . n 
A 1 124 ASP 124 158 158 ASP ASP A . n 
A 1 125 LEU 125 159 159 LEU LEU A . n 
A 1 126 ILE 126 160 160 ILE ILE A . n 
A 1 127 TYR 127 161 161 TYR TYR A . n 
A 1 128 ARG 128 162 162 ARG ARG A . n 
A 1 129 ASP 129 163 163 ASP ASP A . n 
A 1 130 ILE 130 164 164 ILE ILE A . n 
A 1 131 LYS 131 165 165 LYS LYS A . n 
A 1 132 PRO 132 166 166 PRO PRO A . n 
A 1 133 ASP 133 167 167 ASP ASP A . n 
A 1 134 ASN 134 168 168 ASN ASN A . n 
A 1 135 PHE 135 169 169 PHE PHE A . n 
A 1 136 LEU 136 170 170 LEU LEU A . n 
A 1 137 ILE 137 171 171 ILE ILE A . n 
A 1 138 GLY 138 172 172 GLY GLY A . n 
A 1 139 ARG 139 173 173 ARG ARG A . n 
A 1 140 ARG 140 174 174 ARG ARG A . n 
A 1 141 GLY 141 175 175 GLY GLY A . n 
A 1 142 ALA 142 176 176 ALA ALA A . n 
A 1 143 THR 143 177 177 THR THR A . n 
A 1 144 ASP 144 178 178 ASP ASP A . n 
A 1 145 GLU 145 179 179 GLU GLU A . n 
A 1 146 ASN 146 180 180 ASN ASN A . n 
A 1 147 ASN 147 181 181 ASN ASN A . n 
A 1 148 VAL 148 182 182 VAL VAL A . n 
A 1 149 HIS 149 183 183 HIS HIS A . n 
A 1 150 LEU 150 184 184 LEU LEU A . n 
A 1 151 ILE 151 185 185 ILE ILE A . n 
A 1 152 ASP 152 186 186 ASP ASP A . n 
A 1 153 PHE 153 187 187 PHE PHE A . n 
A 1 154 GLY 154 188 188 GLY GLY A . n 
A 1 155 MET 155 189 189 MET MET A . n 
A 1 156 ALA 156 190 190 ALA ALA A . n 
A 1 157 LYS 157 191 191 LYS LYS A . n 
A 1 158 GLN 158 192 192 GLN GLN A . n 
A 1 159 TYR 159 193 193 TYR TYR A . n 
A 1 160 ARG 160 194 194 ARG ARG A . n 
A 1 161 ASP 161 195 195 ASP ASP A . n 
A 1 162 PRO 162 196 196 PRO PRO A . n 
A 1 163 ARG 163 197 197 ARG ARG A . n 
A 1 164 THR 164 198 198 THR THR A . n 
A 1 165 LYS 165 199 199 LYS LYS A . n 
A 1 166 GLN 166 200 200 GLN GLN A . n 
A 1 167 HIS 167 201 201 HIS HIS A . n 
A 1 168 ILE 168 202 202 ILE ILE A . n 
A 1 169 PRO 169 203 203 PRO PRO A . n 
A 1 170 TYR 170 204 204 TYR TYR A . n 
A 1 171 ARG 171 205 205 ARG ARG A . n 
A 1 172 GLU 172 206 206 GLU GLU A . n 
A 1 173 LYS 173 207 207 LYS LYS A . n 
A 1 174 LYS 174 208 208 LYS LYS A . n 
A 1 175 SER 175 209 209 SER SER A . n 
A 1 176 LEU 176 210 210 LEU LEU A . n 
A 1 177 SER 177 211 211 SER SER A . n 
A 1 178 GLY 178 212 212 GLY GLY A . n 
A 1 179 THR 179 213 213 THR THR A . n 
A 1 180 ALA 180 214 214 ALA ALA A . n 
A 1 181 ARG 181 215 215 ARG ARG A . n 
A 1 182 TYR 182 216 216 TYR TYR A . n 
A 1 183 MET 183 217 217 MET MET A . n 
A 1 184 SER 184 218 218 SER SER A . n 
A 1 185 ILE 185 219 219 ILE ILE A . n 
A 1 186 ASN 186 220 220 ASN ASN A . n 
A 1 187 THR 187 221 221 THR THR A . n 
A 1 188 HIS 188 222 222 HIS HIS A . n 
A 1 189 LEU 189 223 223 LEU LEU A . n 
A 1 190 GLY 190 224 224 GLY GLY A . n 
A 1 191 ARG 191 225 225 ARG ARG A . n 
A 1 192 GLU 192 226 226 GLU GLU A . n 
A 1 193 GLN 193 227 227 GLN GLN A . n 
A 1 194 SER 194 228 228 SER SER A . n 
A 1 195 ARG 195 229 229 ARG ARG A . n 
A 1 196 ARG 196 230 230 ARG ARG A . n 
A 1 197 ASP 197 231 231 ASP ASP A . n 
A 1 198 ASP 198 232 232 ASP ASP A . n 
A 1 199 LEU 199 233 233 LEU LEU A . n 
A 1 200 GLU 200 234 234 GLU GLU A . n 
A 1 201 ALA 201 235 235 ALA ALA A . n 
A 1 202 LEU 202 236 236 LEU LEU A . n 
A 1 203 GLY 203 237 237 GLY GLY A . n 
A 1 204 HIS 204 238 238 HIS HIS A . n 
A 1 205 VAL 205 239 239 VAL VAL A . n 
A 1 206 PHE 206 240 240 PHE PHE A . n 
A 1 207 PHE 207 241 241 PHE PHE A . n 
A 1 208 TYR 208 242 242 TYR TYR A . n 
A 1 209 PHE 209 243 243 PHE PHE A . n 
A 1 210 LEU 210 244 244 LEU LEU A . n 
A 1 211 ARG 211 245 245 ARG ARG A . n 
A 1 212 GLY 212 246 246 GLY GLY A . n 
A 1 213 GLN 213 247 247 GLN GLN A . n 
A 1 214 LEU 214 248 248 LEU LEU A . n 
A 1 215 PRO 215 249 249 PRO PRO A . n 
A 1 216 TRP 216 250 250 TRP TRP A . n 
A 1 217 GLN 217 251 251 GLN GLN A . n 
A 1 218 GLY 218 252 252 GLY GLY A . n 
A 1 219 LEU 219 253 253 LEU LEU A . n 
A 1 220 LYS 220 254 254 LYS LYS A . n 
A 1 221 ALA 221 255 255 ALA ALA A . n 
A 1 222 PRO 222 256 256 PRO PRO A . n 
A 1 223 THR 223 257 257 THR THR A . n 
A 1 224 ASN 224 258 258 ASN ASN A . n 
A 1 225 LYS 225 259 259 LYS LYS A . n 
A 1 226 GLN 226 260 260 GLN GLN A . n 
A 1 227 LYS 227 261 261 LYS LYS A . n 
A 1 228 TYR 228 262 262 TYR TYR A . n 
A 1 229 GLU 229 263 263 GLU GLU A . n 
A 1 230 LYS 230 264 264 LYS LYS A . n 
A 1 231 ILE 231 265 265 ILE ILE A . n 
A 1 232 GLY 232 266 266 GLY GLY A . n 
A 1 233 ASP 233 267 267 ASP ASP A . n 
A 1 234 LYS 234 268 268 LYS LYS A . n 
A 1 235 LYS 235 269 269 LYS LYS A . n 
A 1 236 ARG 236 270 270 ARG ARG A . n 
A 1 237 THR 237 271 271 THR THR A . n 
A 1 238 THR 238 272 272 THR THR A . n 
A 1 239 PRO 239 273 273 PRO PRO A . n 
A 1 240 ALA 240 274 274 ALA ALA A . n 
A 1 241 VAL 241 275 275 VAL VAL A . n 
A 1 242 THR 242 276 276 THR THR A . n 
A 1 243 LEU 243 277 277 LEU LEU A . n 
A 1 244 CYS 244 278 278 CYS CYS A . n 
A 1 245 ASP 245 279 279 ASP ASP A . n 
A 1 246 GLY 246 280 280 GLY GLY A . n 
A 1 247 LEU 247 281 281 LEU LEU A . n 
A 1 248 PRO 248 282 282 PRO PRO A . n 
A 1 249 GLN 249 283 283 GLN GLN A . n 
A 1 250 GLN 250 284 284 GLN GLN A . n 
A 1 251 PHE 251 285 285 PHE PHE A . n 
A 1 252 ALA 252 286 286 ALA ALA A . n 
A 1 253 GLU 253 287 287 GLU GLU A . n 
A 1 254 TYR 254 288 288 TYR TYR A . n 
A 1 255 LEU 255 289 289 LEU LEU A . n 
A 1 256 ASP 256 290 290 ASP ASP A . n 
A 1 257 SER 257 291 291 SER SER A . n 
A 1 258 VAL 258 292 292 VAL VAL A . n 
A 1 259 ARG 259 293 293 ARG ARG A . n 
A 1 260 SER 260 294 294 SER SER A . n 
A 1 261 LEU 261 295 295 LEU LEU A . n 
A 1 262 PRO 262 296 296 PRO PRO A . n 
A 1 263 PHE 263 297 297 PHE PHE A . n 
A 1 264 ASP 264 298 298 ASP ASP A . n 
A 1 265 ALA 265 299 299 ALA ALA A . n 
A 1 266 GLU 266 300 300 GLU GLU A . n 
A 1 267 PRO 267 301 301 PRO PRO A . n 
A 1 268 PRO 268 302 302 PRO PRO A . n 
A 1 269 TYR 269 303 303 TYR TYR A . n 
A 1 270 GLU 270 304 304 GLU GLU A . n 
A 1 271 GLU 271 305 305 GLU GLU A . n 
A 1 272 TYR 272 306 306 TYR TYR A . n 
A 1 273 ARG 273 307 307 ARG ARG A . n 
A 1 274 MET 274 308 308 MET MET A . n 
A 1 275 LEU 275 309 309 LEU LEU A . n 
A 1 276 LEU 276 310 310 LEU LEU A . n 
A 1 277 LEU 277 311 311 LEU LEU A . n 
A 1 278 SER 278 312 312 SER SER A . n 
A 1 279 VAL 279 313 313 VAL VAL A . n 
A 1 280 LEU 280 314 314 LEU LEU A . n 
A 1 281 ASP 281 315 315 ASP ASP A . n 
A 1 282 ASP 282 316 316 ASP ASP A . n 
A 1 283 LEU 283 317 317 LEU LEU A . n 
A 1 284 GLY 284 318 318 GLY GLY A . n 
A 1 285 GLN 285 319 319 GLN GLN A . n 
A 1 286 ALA 286 320 320 ALA ALA A . n 
A 1 287 CYS 287 321 321 CYS CYS A . n 
A 1 288 ASP 288 322 322 ASP ASP A . n 
A 1 289 GLY 289 323 323 GLY GLY A . n 
A 1 290 ASP 290 324 324 ASP ASP A . n 
A 1 291 MET 291 325 325 MET MET A . n 
A 1 292 ASP 292 326 326 ASP ASP A . n 
A 1 293 TRP 293 327 327 TRP TRP A . n 
A 1 294 MET 294 328 328 MET MET A . n 
A 1 295 HIS 295 329 329 HIS HIS A . n 
A 1 296 LEU 296 330 330 LEU LEU A . n 
A 1 297 ASN 297 331 331 ASN ASN A . n 
A 1 298 GLY 298 332 332 GLY GLY A . n 
A 1 299 GLY 299 333 333 GLY GLY A . n 
A 1 300 ARG 300 334 334 ARG ARG A . n 
A 1 301 GLY 301 335 335 GLY GLY A . n 
A 1 302 TRP 302 336 336 TRP TRP A . n 
A 1 303 ASP 303 337 337 ASP ASP A . n 
A 1 304 ALA 304 338 338 ALA ALA A . n 
A 1 305 THR 305 339 339 THR THR A . n 
A 1 306 ILE 306 340 ?   ?   ?   A . n 
A 1 307 ASN 307 341 ?   ?   ?   A . n 
A 1 308 LYS 308 342 ?   ?   ?   A . n 
A 1 309 LYS 309 343 ?   ?   ?   A . n 
A 1 310 PRO 310 344 ?   ?   ?   A . n 
A 1 311 ASN 311 345 ?   ?   ?   A . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1BIN 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1BIN 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
B 2 A1BIN 1  401 401 A1BIN DRG A . 
C 3 CL    1  402 1   CL    CL  A . 
D 3 CL    1  403 2   CL    CL  A . 
E 3 CL    1  404 3   CL    CL  A . 
F 4 HOH   1  501 14  HOH   HOH A . 
F 4 HOH   2  502 25  HOH   HOH A . 
F 4 HOH   3  503 2   HOH   HOH A . 
F 4 HOH   4  504 76  HOH   HOH A . 
F 4 HOH   5  505 125 HOH   HOH A . 
F 4 HOH   6  506 8   HOH   HOH A . 
F 4 HOH   7  507 1   HOH   HOH A . 
F 4 HOH   8  508 126 HOH   HOH A . 
F 4 HOH   9  509 6   HOH   HOH A . 
F 4 HOH   10 510 90  HOH   HOH A . 
F 4 HOH   11 511 178 HOH   HOH A . 
F 4 HOH   12 512 134 HOH   HOH A . 
F 4 HOH   13 513 44  HOH   HOH A . 
F 4 HOH   14 514 169 HOH   HOH A . 
F 4 HOH   15 515 40  HOH   HOH A . 
F 4 HOH   16 516 181 HOH   HOH A . 
F 4 HOH   17 517 177 HOH   HOH A . 
F 4 HOH   18 518 135 HOH   HOH A . 
F 4 HOH   19 519 164 HOH   HOH A . 
F 4 HOH   20 520 175 HOH   HOH A . 
F 4 HOH   21 521 45  HOH   HOH A . 
F 4 HOH   22 522 170 HOH   HOH A . 
F 4 HOH   23 523 116 HOH   HOH A . 
F 4 HOH   24 524 5   HOH   HOH A . 
F 4 HOH   25 525 13  HOH   HOH A . 
F 4 HOH   26 526 171 HOH   HOH A . 
F 4 HOH   27 527 15  HOH   HOH A . 
F 4 HOH   28 528 161 HOH   HOH A . 
F 4 HOH   29 529 18  HOH   HOH A . 
F 4 HOH   30 530 180 HOH   HOH A . 
F 4 HOH   31 531 19  HOH   HOH A . 
F 4 HOH   32 532 167 HOH   HOH A . 
F 4 HOH   33 533 27  HOH   HOH A . 
F 4 HOH   34 534 188 HOH   HOH A . 
F 4 HOH   35 535 20  HOH   HOH A . 
F 4 HOH   36 536 14  HOH   HOH A . 
F 4 HOH   37 537 192 HOH   HOH A . 
F 4 HOH   38 538 187 HOH   HOH A . 
F 4 HOH   39 539 176 HOH   HOH A . 
F 4 HOH   40 540 190 HOH   HOH A . 
F 4 HOH   41 541 22  HOH   HOH A . 
F 4 HOH   42 542 22  HOH   HOH A . 
F 4 HOH   43 543 23  HOH   HOH A . 
F 4 HOH   44 544 16  HOH   HOH A . 
F 4 HOH   45 545 163 HOH   HOH A . 
F 4 HOH   46 546 184 HOH   HOH A . 
F 4 HOH   47 547 173 HOH   HOH A . 
F 4 HOH   48 548 185 HOH   HOH A . 
F 4 HOH   49 549 165 HOH   HOH A . 
F 4 HOH   50 550 172 HOH   HOH A . 
F 4 HOH   51 551 174 HOH   HOH A . 
F 4 HOH   52 552 189 HOH   HOH A . 
F 4 HOH   53 553 179 HOH   HOH A . 
F 4 HOH   54 554 162 HOH   HOH A . 
F 4 HOH   55 555 182 HOH   HOH A . 
F 4 HOH   56 556 2   HOH   HOH A . 
F 4 HOH   57 557 191 HOH   HOH A . 
F 4 HOH   58 558 10  HOH   HOH A . 
F 4 HOH   59 559 186 HOH   HOH A . 
F 4 HOH   60 560 24  HOH   HOH A . 
F 4 HOH   61 561 168 HOH   HOH A . 
F 4 HOH   62 562 17  HOH   HOH A . 
F 4 HOH   63 563 15  HOH   HOH A . 
F 4 HOH   64 564 183 HOH   HOH A . 
F 4 HOH   65 565 7   HOH   HOH A . 
F 4 HOH   66 566 12  HOH   HOH A . 
F 4 HOH   67 567 21  HOH   HOH A . 
F 4 HOH   68 568 5   HOH   HOH A . 
F 4 HOH   69 569 3   HOH   HOH A . 
F 4 HOH   70 570 11  HOH   HOH A . 
F 4 HOH   71 571 8   HOH   HOH A . 
F 4 HOH   72 572 4   HOH   HOH A . 
F 4 HOH   73 573 9   HOH   HOH A . 
F 4 HOH   74 574 6   HOH   HOH A . 
F 4 HOH   75 575 26  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                     9EDY 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     91.488 
_cell.length_a_esd                 ? 
_cell.length_b                     91.488 
_cell.length_b_esd                 ? 
_cell.length_c                     119.170 
_cell.length_c_esd                 ? 
_cell.volume                       863828.915 
_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                         9EDY 
_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                   9EDY 
_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             2.69 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          54.35 
_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, 0.025 M Magnesium chloride, 20% (w/v) PEG3350' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            298 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS EIGER X 9M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2023-04-13 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   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                          58.56 
_reflns.entry_id                                       9EDY 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.30 
_reflns.d_resolution_low                               47.64 
_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                                     16511 
_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                                4.5 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          5.3 
_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                                0.090 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.988 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.117 
_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                                    2.30 
_reflns_shell.d_res_low                                     2.36 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           0.7 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             1230 
_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                               3.3 
_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                               1.138 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.321 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          99.2 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  1.341 
_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                               69.54 
_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                                 9EDY 
_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                            2.30 
_refine.ls_d_res_low                             47.62 
_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                     16481 
_refine.ls_number_reflns_R_free                  976 
_refine.ls_number_reflns_R_work                  15505 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.61 
_refine.ls_percent_reflns_R_free                 5.92 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2046 
_refine.ls_R_factor_R_free                       0.2376 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2024 
_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                 34.7678 
_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                            0.3475 
_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                       2.30 
_refine_hist.d_res_low                        47.62 
_refine_hist.number_atoms_solvent             75 
_refine_hist.number_atoms_total               2561 
_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        2460 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         26 
_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' ? 0.0021  ? 2545 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.4762  ? 3441 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 0.0379  ? 356  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.0039  ? 451  ? f_plane_restr      ? ? 
'X-RAY DIFFRACTION' ? 14.3578 ? 973  ? 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' 2.30 2.42  . . 115 2195 98.47  . . . . 0.3414 . . . . . . . . . . . 0.3701 
'X-RAY DIFFRACTION' 2.42 2.57  . . 121 2236 99.54  . . . . 0.2988 . . . . . . . . . . . 0.3236 
'X-RAY DIFFRACTION' 2.57 2.77  . . 147 2222 99.71  . . . . 0.2721 . . . . . . . . . . . 0.3061 
'X-RAY DIFFRACTION' 2.77 3.05  . . 132 2217 99.70  . . . . 0.2500 . . . . . . . . . . . 0.3037 
'X-RAY DIFFRACTION' 3.05 3.49  . . 157 2223 99.96  . . . . 0.2180 . . . . . . . . . . . 0.2723 
'X-RAY DIFFRACTION' 3.49 4.40  . . 153 2209 100.00 . . . . 0.1610 . . . . . . . . . . . 0.2073 
'X-RAY DIFFRACTION' 4.40 47.62 . . 151 2203 99.87  . . . . 0.1662 . . . . . . . . . . . 0.1952 
# 
_struct.entry_id                     9EDY 
_struct.title                        
;Crystal structure of Yck2 from Candida albicans in complex with inhibitor 2b: 6-fluoro-2-(4-fluorophenyl)-3-(pyridin-4-yl)pyrazolo[1,5-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        9EDY 
_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 3 ? 
E N N 3 ? 
F N N 4 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    A0A8H6C375_CANAX 
_struct_ref.pdbx_db_accession          A0A8H6C375 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;NNSSVVGLHYKIGKKIGEGSFGVIFEGTNIINGVPVAIKFEPRKTEAPQLRDEYRTYKHLQGCDGIPNAYYFGQEGLHNI
LVIDLLGPSLEDLFDWCGRRFSVKTVVQVAIQMLTLVEEVHRHDLIYRDIKPDNFLIGRRGATDENNVHLIDFGMAKQYR
DPRTKQHIPYREKKSLSGTARYMSINTHLGREQSRRDDLEALGHVFFYFLRGQLPWQGLKAPTNKQKYEKIGDKKRTTPA
VTLCDGLPQQFAEYLDSVRSLPFDAEPPYEEYRMLLLSVLDDLGQACDGDMDWMHLNGGRGWDATINKKPN
;
_struct_ref.pdbx_align_begin           35 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              9EDY 
_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                 311 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             A0A8H6C375 
_struct_ref_seq.db_align_beg                  35 
_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       35 
_struct_ref_seq.pdbx_auth_seq_align_end       345 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F 
# 
_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 49  ? LEU A 60  ? GLN A 83  LEU A 94  1 ? 12 
HELX_P HELX_P2  AA2 SER A 89  ? CYS A 97  ? SER A 123 CYS A 131 1 ? 9  
HELX_P HELX_P3  AA3 SER A 102 ? HIS A 123 ? SER A 136 HIS A 157 1 ? 22 
HELX_P HELX_P4  AA4 SER A 184 ? LEU A 189 ? SER A 218 LEU A 223 1 ? 6  
HELX_P HELX_P5  AA5 SER A 194 ? GLY A 212 ? SER A 228 GLY A 246 1 ? 19 
HELX_P HELX_P6  AA6 THR A 223 ? THR A 238 ? THR A 257 THR A 272 1 ? 16 
HELX_P HELX_P7  AA7 PRO A 239 ? CYS A 244 ? PRO A 273 CYS A 278 1 ? 6  
HELX_P HELX_P8  AA8 GLN A 249 ? SER A 260 ? GLN A 283 SER A 294 1 ? 12 
HELX_P HELX_P9  AA9 PRO A 268 ? LEU A 283 ? PRO A 302 LEU A 317 1 ? 16 
HELX_P HELX_P10 AB1 MET A 291 ? MET A 294 ? MET A 325 MET A 328 5 ? 4  
HELX_P HELX_P11 AB2 HIS A 295 ? ARG A 300 ? HIS A 329 ARG A 334 1 ? 6  
# 
_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 5   ? VAL A 6   ? VAL A 39  VAL A 40  
AA1 2 TYR A 10  ? LYS A 15  ? TYR A 44  LYS A 49  
AA1 3 ILE A 24  ? ASN A 29  ? ILE A 58  ASN A 63  
AA1 4 PRO A 35  ? PRO A 42  ? PRO A 69  PRO A 76  
AA1 5 HIS A 78  ? ASP A 84  ? HIS A 112 ASP A 118 
AA1 6 ALA A 69  ? GLU A 75  ? ALA A 103 GLU A 109 
AA2 1 LEU A 125 ? ILE A 126 ? LEU A 159 ILE A 160 
AA2 2 LYS A 157 ? GLN A 158 ? LYS A 191 GLN A 192 
AA3 1 PHE A 135 ? LEU A 136 ? PHE A 169 LEU A 170 
AA3 2 HIS A 149 ? LEU A 150 ? 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 6   ? N VAL A 40  O TYR A 10  ? O TYR A 44  
AA1 2 3 N LYS A 14  ? N LYS A 48  O GLU A 26  ? O GLU A 60  
AA1 3 4 N PHE A 25  ? N PHE A 59  O ILE A 38  ? O ILE A 72  
AA1 4 5 N GLU A 41  ? N GLU A 75  O ASN A 79  ? O ASN A 113 
AA1 5 6 O VAL A 82  ? O VAL A 116 N TYR A 70  ? N TYR A 104 
AA2 1 2 N ILE A 126 ? N ILE A 160 O LYS A 157 ? O LYS A 191 
AA3 1 2 N LEU A 136 ? N LEU A 170 O HIS A 149 ? O HIS A 183 
# 
_pdbx_entry_details.entry_id                   9EDY 
_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  ? ? 73.09   -41.35 
2 1 PHE A 55  ? ? -97.84  33.86  
3 1 ARG A 77  ? ? -68.42  -71.26 
4 1 GLN A 83  ? ? -143.13 -20.95 
5 1 ASP A 158 ? ? 75.94   33.62  
6 1 ASP A 163 ? ? -141.68 40.11  
7 1 ASP A 178 ? ? -98.82  41.41  
8 1 ASP A 186 ? ? 59.90   91.13  
9 1 ARG A 334 ? ? -137.06 -37.16 
# 
_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 26.2260571676 -7.73660798616 -16.721853526  0.771244399213 ? 0.0017314264824 ? -0.0849943089953  ? 
0.432528594885 ? 0.0775987953646   ? 0.639630675169 ? 8.96361987614 ? -0.347606549304 ? 2.80282248817   ? 5.29217898473 ? 
0.486827566004   ? 7.86619846087 ? -0.235083293685  ? 0.741920417647   ? -0.271085141173 ? -1.5702125011   ? 0.422171819843   ? 
0.0738155425349 ? -0.154949619547 ? -0.507263381795 ? -0.257267750019 ? 
2 'X-RAY DIFFRACTION' ? refined 17.5787321818 -21.1143547966 -7.10190065468 0.279451492151 ? 0.0433366833906 ? -0.00969391604888 ? 
0.398625768114 ? -0.0406657518368  ? 0.55098859447  ? 3.59294919212 ? 0.371304077501  ? 0.0981741715929 ? 4.24355410839 ? 
-0.295724419017  ? 1.93754987248 ? -0.0871969163559 ? -0.0894173615693 ? 0.914220262248  ? 0.0674650995786 ? 0.0400198982698  ? 
0.103868896781  ? -0.328964934313 ? -0.332729107631 ? 0.0540201364605 ? 
3 'X-RAY DIFFRACTION' ? refined 14.3116564613 -36.9295096648 -9.49077620905 0.25550240483  ? -0.093737620092 ? 0.0264232524609   ? 
0.386304736235 ? -0.00403244577833 ? 0.325031279774 ? 4.00640595595 ? -0.840942494952 ? 0.700128158969  ? 3.79169903934 ? 
-0.0869786719163 ? 3.50147651371 ? 0.0502983895506  ? 0.074029277251   ? -0.234056709875 ? -0.14282144767  ? -0.0689965038577 ? 
0.219574715137  ? 0.136740086634  ? -0.331867841131 ? 0.0067533938311 ? 
# 
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 35  ? A 49  A 83  ? ? 
;chain 'A' and (resid 35 through 83 )
;
2 'X-RAY DIFFRACTION' 2 A 50  A 84  ? A 179 A 213 ? ? 
;chain 'A' and (resid 84 through 213 )
;
3 'X-RAY DIFFRACTION' 3 A 180 A 214 ? A 305 A 339 ? ? 
;chain 'A' and (resid 214 through 339 )
;
# 
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 ILE 340 ? A ILE 306 
2 1 Y 1 A ASN 341 ? A ASN 307 
3 1 Y 1 A LYS 342 ? A LYS 308 
4 1 Y 1 A LYS 343 ? A LYS 309 
5 1 Y 1 A PRO 344 ? A PRO 310 
6 1 Y 1 A ASN 345 ? A ASN 311 
# 
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 
A1BIN C4   C  Y N 1   
A1BIN C14  C  Y N 2   
A1BIN C5   C  Y N 3   
A1BIN C6   C  Y N 4   
A1BIN C11  C  Y N 5   
A1BIN C7   C  Y N 6   
A1BIN C8   C  Y N 7   
A1BIN C9   C  Y N 8   
A1BIN C10  C  Y N 9   
A1BIN C12  C  Y N 10  
A1BIN C13  C  Y N 11  
A1BIN N1   N  Y N 12  
A1BIN N2   N  Y N 13  
A1BIN C3   C  Y N 14  
A1BIN N3   N  Y N 15  
A1BIN C1   C  Y N 16  
A1BIN C15  C  Y N 17  
A1BIN C16  C  Y N 18  
A1BIN C17  C  Y N 19  
A1BIN C18  C  Y N 20  
A1BIN C2   C  Y N 21  
A1BIN F1   F  N N 22  
A1BIN F2   F  N N 23  
A1BIN H3   H  N N 24  
A1BIN H8   H  N N 25  
A1BIN H7   H  N N 26  
A1BIN H4   H  N N 27  
A1BIN H5   H  N N 28  
A1BIN H6   H  N N 29  
A1BIN H2   H  N N 30  
A1BIN H9   H  N N 31  
A1BIN H10  H  N N 32  
A1BIN H11  H  N N 33  
A1BIN H1   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 
A1BIN F1  C1   sing N N 1   
A1BIN C1  C2   sing Y N 2   
A1BIN C2  C3   doub Y N 3   
A1BIN C1  C4   doub Y N 4   
A1BIN C4  N1   sing Y N 5   
A1BIN N1  C5   sing Y N 6   
A1BIN C5  C6   doub Y N 7   
A1BIN C6  C7   sing N N 8   
A1BIN C7  C8   doub Y N 9   
A1BIN C8  C9   sing Y N 10  
A1BIN C9  N2   doub Y N 11  
A1BIN N2  C10  sing Y N 12  
A1BIN C10 C11  doub Y N 13  
A1BIN C6  C12  sing Y N 14  
A1BIN C12 C13  sing N N 15  
A1BIN C13 C14  doub Y N 16  
A1BIN C14 C15  sing Y N 17  
A1BIN C15 C16  doub Y N 18  
A1BIN C16 F2   sing N N 19  
A1BIN C16 C17  sing Y N 20  
A1BIN C17 C18  doub Y N 21  
A1BIN C12 N3   doub Y N 22  
A1BIN C3  C5   sing Y N 23  
A1BIN N1  N3   sing Y N 24  
A1BIN C7  C11  sing Y N 25  
A1BIN C13 C18  sing Y N 26  
A1BIN C4  H3   sing N N 27  
A1BIN C14 H8   sing N N 28  
A1BIN C11 H7   sing N N 29  
A1BIN C8  H4   sing N N 30  
A1BIN C9  H5   sing N N 31  
A1BIN C10 H6   sing N N 32  
A1BIN C3  H2   sing N N 33  
A1BIN C15 H9   sing N N 34  
A1BIN C17 H10  sing N N 35  
A1BIN C18 H11  sing N N 36  
A1BIN C2  H1   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                    9EDY 
_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]   0.010930 
_atom_sites.fract_transf_matrix[1][2]   0.006311 
_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]   0.012621 
_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]   0.008391 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
_atom_type.scat_dispersion_real 
_atom_type.scat_dispersion_imag 
_atom_type.scat_Cromer_Mann_a1 
_atom_type.scat_Cromer_Mann_a2 
_atom_type.scat_Cromer_Mann_a3 
_atom_type.scat_Cromer_Mann_a4 
_atom_type.scat_Cromer_Mann_b1 
_atom_type.scat_Cromer_Mann_b2 
_atom_type.scat_Cromer_Mann_b3 
_atom_type.scat_Cromer_Mann_b4 
_atom_type.scat_Cromer_Mann_c 
_atom_type.scat_source 
_atom_type.scat_dispersion_source 
C  ? ? 3.54356 2.42580 ? ? 25.62398 1.50364  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
CL ? ? 9.50761 7.44341 ? ? 1.04373  23.83732 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
F  ? ? 8.95735 ?       ? ? 7.27484  ?        ? ? 0.0 
;1-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
N  ? ? 4.01032 2.96436 ? ? 19.97189 1.75589  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
O  ? ? 4.49882 3.47563 ? ? 15.80542 1.70748  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
S  ? ? 9.55732 6.39887 ? ? 1.23737  29.19336 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N   . ASN   A 1 1   ? 32.80900  3.42200   -25.54500 1.000 168.78974 ? 35  ASN   A N   1 
ATOM   2    C  CA  . ASN   A 1 1   ? 32.76400  3.08400   -24.12900 1.000 163.24362 ? 35  ASN   A CA  1 
ATOM   3    C  C   . ASN   A 1 1   ? 33.81700  2.03800   -23.79000 1.000 161.87147 ? 35  ASN   A C   1 
ATOM   4    O  O   . ASN   A 1 1   ? 33.49100  0.95300   -23.30800 1.000 154.43774 ? 35  ASN   A O   1 
ATOM   5    C  CB  . ASN   A 1 1   ? 31.37300  2.57900   -23.73700 1.000 149.15977 ? 35  ASN   A CB  1 
ATOM   6    C  CG  . ASN   A 1 1   ? 30.29400  3.62500   -23.93500 1.000 153.24782 ? 35  ASN   A CG  1 
ATOM   7    O  OD1 . ASN   A 1 1   ? 30.54600  4.82400   -23.82100 1.000 153.84053 ? 35  ASN   A OD1 1 
ATOM   8    N  ND2 . ASN   A 1 1   ? 29.08100  3.17400   -24.23300 1.000 145.24389 ? 35  ASN   A ND2 1 
ATOM   9    N  N   . ASN   A 1 2   ? 35.08000  2.36400   -24.05200 1.000 163.07144 ? 36  ASN   A N   1 
ATOM   10   C  CA  . ASN   A 1 2   ? 36.16300  1.44700   -23.72600 1.000 161.62111 ? 36  ASN   A CA  1 
ATOM   11   C  C   . ASN   A 1 2   ? 36.25400  1.25800   -22.21800 1.000 159.81791 ? 36  ASN   A C   1 
ATOM   12   O  O   . ASN   A 1 2   ? 36.03200  2.19400   -21.44400 1.000 155.68906 ? 36  ASN   A O   1 
ATOM   13   C  CB  . ASN   A 1 2   ? 37.49000  1.96600   -24.28000 1.000 159.68274 ? 36  ASN   A CB  1 
ATOM   14   C  CG  . ASN   A 1 2   ? 37.57200  1.86200   -25.79000 1.000 168.99722 ? 36  ASN   A CG  1 
ATOM   15   O  OD1 . ASN   A 1 2   ? 36.55200  1.80000   -26.47600 1.000 175.35100 ? 36  ASN   A OD1 1 
ATOM   16   N  ND2 . ASN   A 1 2   ? 38.79100  1.83500   -26.31600 1.000 167.78775 ? 36  ASN   A ND2 1 
ATOM   17   N  N   . SER   A 1 3   ? 36.58000  0.03200   -21.80700 1.000 164.67076 ? 37  SER   A N   1 
ATOM   18   C  CA  . SER   A 1 3   ? 36.57300  -0.37600  -20.40200 1.000 145.84931 ? 37  SER   A CA  1 
ATOM   19   C  C   . SER   A 1 3   ? 35.19200  -0.13100  -19.78500 1.000 130.91005 ? 37  SER   A C   1 
ATOM   20   O  O   . SER   A 1 3   ? 34.99600  0.71600   -18.91100 1.000 121.35836 ? 37  SER   A O   1 
ATOM   21   C  CB  . SER   A 1 3   ? 37.67500  0.34100   -19.61300 1.000 140.93205 ? 37  SER   A CB  1 
ATOM   22   O  OG  . SER   A 1 3   ? 37.71100  -0.11600  -18.27500 1.000 130.56321 ? 37  SER   A OG  1 
ATOM   23   N  N   . SER   A 1 4   ? 34.23300  -0.90800  -20.28400 1.000 117.28733 ? 38  SER   A N   1 
ATOM   24   C  CA  . SER   A 1 4   ? 32.84200  -0.76200  -19.87700 1.000 112.70654 ? 38  SER   A CA  1 
ATOM   25   C  C   . SER   A 1 4   ? 32.66700  -1.20100  -18.42900 1.000 92.28903  ? 38  SER   A C   1 
ATOM   26   O  O   . SER   A 1 4   ? 32.93700  -2.35600  -18.08400 1.000 84.94033  ? 38  SER   A O   1 
ATOM   27   C  CB  . SER   A 1 4   ? 31.93900  -1.58000  -20.79700 1.000 119.99748 ? 38  SER   A CB  1 
ATOM   28   O  OG  . SER   A 1 4   ? 32.11300  -1.20300  -22.15200 1.000 134.37763 ? 38  SER   A OG  1 
ATOM   29   N  N   . VAL   A 1 5   ? 32.21400  -0.27900  -17.58300 1.000 96.31151  ? 39  VAL   A N   1 
ATOM   30   C  CA  . VAL   A 1 5   ? 31.93900  -0.55300  -16.17800 1.000 84.70718  ? 39  VAL   A CA  1 
ATOM   31   C  C   . VAL   A 1 5   ? 30.47400  -0.23200  -15.91700 1.000 74.45616  ? 39  VAL   A C   1 
ATOM   32   O  O   . VAL   A 1 5   ? 30.05600  0.92700   -16.03500 1.000 84.20157  ? 39  VAL   A O   1 
ATOM   33   C  CB  . VAL   A 1 5   ? 32.84900  0.25800   -15.24300 1.000 76.06219  ? 39  VAL   A CB  1 
ATOM   34   C  CG1 . VAL   A 1 5   ? 32.47700  -0.00000  -13.79000 1.000 76.09299  ? 39  VAL   A CG1 1 
ATOM   35   C  CG2 . VAL   A 1 5   ? 34.31200  -0.08500  -15.49200 1.000 79.42140  ? 39  VAL   A CG2 1 
ATOM   36   N  N   . VAL   A 1 6   ? 29.69800  -1.25500  -15.56800 1.000 72.16475  ? 40  VAL   A N   1 
ATOM   37   C  CA  . VAL   A 1 6   ? 28.29100  -1.09400  -15.22600 1.000 66.05953  ? 40  VAL   A CA  1 
ATOM   38   C  C   . VAL   A 1 6   ? 28.14500  -1.14600  -13.71300 1.000 62.33212  ? 40  VAL   A C   1 
ATOM   39   O  O   . VAL   A 1 6   ? 28.97500  -1.72500  -13.00500 1.000 78.36371  ? 40  VAL   A O   1 
ATOM   40   C  CB  . VAL   A 1 6   ? 27.41600  -2.16600  -15.91200 1.000 86.88106  ? 40  VAL   A CB  1 
ATOM   41   C  CG1 . VAL   A 1 6   ? 27.51900  -2.05200  -17.42700 1.000 84.61077  ? 40  VAL   A CG1 1 
ATOM   42   C  CG2 . VAL   A 1 6   ? 27.81700  -3.55800  -15.44700 1.000 80.57282  ? 40  VAL   A CG2 1 
ATOM   43   N  N   . GLY   A 1 7   ? 27.07800  -0.53000  -13.21000 1.000 60.92170  ? 41  GLY   A N   1 
ATOM   44   C  CA  . GLY   A 1 7   ? 26.81300  -0.54500  -11.78800 1.000 63.01171  ? 41  GLY   A CA  1 
ATOM   45   C  C   . GLY   A 1 7   ? 27.83700  0.16600   -10.93900 1.000 66.69440  ? 41  GLY   A C   1 
ATOM   46   O  O   . GLY   A 1 7   ? 27.95300  -0.14400  -9.74900  1.000 71.00496  ? 41  GLY   A O   1 
ATOM   47   N  N   . LEU   A 1 8   ? 28.59300  1.09900   -11.52900 1.000 64.89260  ? 42  LEU   A N   1 
ATOM   48   C  CA  . LEU   A 1 8   ? 29.60300  1.91000   -10.85100 1.000 64.36181  ? 42  LEU   A CA  1 
ATOM   49   C  C   . LEU   A 1 8   ? 30.86100  1.12500   -10.49800 1.000 65.33144  ? 42  LEU   A C   1 
ATOM   50   O  O   . LEU   A 1 8   ? 31.97700  1.63500   -10.64300 1.000 66.32149  ? 42  LEU   A O   1 
ATOM   51   C  CB  . LEU   A 1 8   ? 29.03100  2.55100   -9.58200  1.000 62.88188  ? 42  LEU   A CB  1 
ATOM   52   C  CG  . LEU   A 1 8   ? 28.03800  3.68300   -9.80600  1.000 82.00829  ? 42  LEU   A CG  1 
ATOM   53   C  CD1 . LEU   A 1 8   ? 27.40800  4.10200   -8.49900  1.000 60.11888  ? 42  LEU   A CD1 1 
ATOM   54   C  CD2 . LEU   A 1 8   ? 28.76800  4.83800   -10.45000 1.000 82.04284  ? 42  LEU   A CD2 1 
ATOM   55   N  N   . HIS   A 1 9   ? 30.69800  -0.11000  -10.02500 1.000 46.09945  ? 43  HIS   A N   1 
ATOM   56   C  CA  . HIS   A 1 9   ? 31.79200  -0.85800  -9.42100  1.000 55.46757  ? 43  HIS   A CA  1 
ATOM   57   C  C   . HIS   A 1 9   ? 32.08400  -2.17700  -10.12000 1.000 55.20403  ? 43  HIS   A C   1 
ATOM   58   O  O   . HIS   A 1 9   ? 32.86100  -2.97200  -9.59100  1.000 54.15504  ? 43  HIS   A O   1 
ATOM   59   C  CB  . HIS   A 1 9   ? 31.49100  -1.13700  -7.94300  1.000 44.16199  ? 43  HIS   A CB  1 
ATOM   60   C  CG  . HIS   A 1 9   ? 31.25900  0.09300   -7.12400  1.000 64.70136  ? 43  HIS   A CG  1 
ATOM   61   N  ND1 . HIS   A 1 9   ? 31.61100  1.35500   -7.55100  1.000 48.72515  ? 43  HIS   A ND1 1 
ATOM   62   C  CD2 . HIS   A 1 9   ? 30.71100  0.25100   -5.89600  1.000 73.13090  ? 43  HIS   A CD2 1 
ATOM   63   C  CE1 . HIS   A 1 9   ? 31.28800  2.23800   -6.62200  1.000 67.66185  ? 43  HIS   A CE1 1 
ATOM   64   N  NE2 . HIS   A 1 9   ? 30.74000  1.59300   -5.60700  1.000 56.50510  ? 43  HIS   A NE2 1 
ATOM   65   N  N   . TYR   A 1 10  ? 31.49100  -2.44500  -11.28100 1.000 50.48499  ? 44  TYR   A N   1 
ATOM   66   C  CA  . TYR   A 1 10  ? 31.54500  -3.78200  -11.86200 1.000 51.32465  ? 44  TYR   A CA  1 
ATOM   67   C  C   . TYR   A 1 10  ? 32.05700  -3.71900  -13.29200 1.000 58.76892  ? 44  TYR   A C   1 
ATOM   68   O  O   . TYR   A 1 10  ? 31.40500  -3.14300  -14.16700 1.000 71.01735  ? 44  TYR   A O   1 
ATOM   69   C  CB  . TYR   A 1 10  ? 30.17100  -4.45000  -11.77600 1.000 53.53580  ? 44  TYR   A CB  1 
ATOM   70   C  CG  . TYR   A 1 10  ? 29.67700  -4.45900  -10.35000 1.000 44.75981  ? 44  TYR   A CG  1 
ATOM   71   C  CD1 . TYR   A 1 10  ? 30.23300  -5.31900  -9.41300  1.000 47.31026  ? 44  TYR   A CD1 1 
ATOM   72   C  CD2 . TYR   A 1 10  ? 28.69400  -3.57700  -9.92700  1.000 48.96233  ? 44  TYR   A CD2 1 
ATOM   73   C  CE1 . TYR   A 1 10  ? 29.80600  -5.32000  -8.10200  1.000 54.77157  ? 44  TYR   A CE1 1 
ATOM   74   C  CE2 . TYR   A 1 10  ? 28.25800  -3.57100  -8.61700  1.000 54.99007  ? 44  TYR   A CE2 1 
ATOM   75   C  CZ  . TYR   A 1 10  ? 28.81800  -4.44400  -7.70900  1.000 50.25660  ? 44  TYR   A CZ  1 
ATOM   76   O  OH  . TYR   A 1 10  ? 28.39100  -4.44100  -6.40300  1.000 65.45661  ? 44  TYR   A OH  1 
ATOM   77   N  N   . LYS   A 1 11  ? 33.22200  -4.32200  -13.51600 1.000 58.23451  ? 45  LYS   A N   1 
ATOM   78   C  CA  . LYS   A 1 11  ? 33.89800  -4.30700  -14.80600 1.000 71.35432  ? 45  LYS   A CA  1 
ATOM   79   C  C   . LYS   A 1 11  ? 33.41800  -5.48100  -15.65100 1.000 67.30941  ? 45  LYS   A C   1 
ATOM   80   O  O   . LYS   A 1 11  ? 33.55400  -6.64100  -15.24500 1.000 64.11368  ? 45  LYS   A O   1 
ATOM   81   C  CB  . LYS   A 1 11  ? 35.41000  -4.37100  -14.59700 1.000 66.93248  ? 45  LYS   A CB  1 
ATOM   82   C  CG  . LYS   A 1 11  ? 36.22500  -4.65700  -15.84400 1.000 77.61189  ? 45  LYS   A CG  1 
ATOM   83   C  CD  . LYS   A 1 11  ? 37.69100  -4.85900  -15.48100 1.000 84.59560  ? 45  LYS   A CD  1 
ATOM   84   C  CE  . LYS   A 1 11  ? 38.56500  -5.00400  -16.71600 1.000 85.56622  ? 45  LYS   A CE  1 
ATOM   85   N  NZ  . LYS   A 1 11  ? 38.46200  -3.82000  -17.61400 1.000 91.44642  ? 45  LYS   A NZ  1 
ATOM   86   N  N   . ILE   A 1 12  ? 32.86000  -5.17900  -16.82400 1.000 63.79196  ? 46  ILE   A N   1 
ATOM   87   C  CA  . ILE   A 1 12  ? 32.38800  -6.22200  -17.72700 1.000 74.51894  ? 46  ILE   A CA  1 
ATOM   88   C  C   . ILE   A 1 12  ? 33.57700  -7.01400  -18.25500 1.000 67.12580  ? 46  ILE   A C   1 
ATOM   89   O  O   . ILE   A 1 12  ? 34.59800  -6.44000  -18.65700 1.000 73.93213  ? 46  ILE   A O   1 
ATOM   90   C  CB  . ILE   A 1 12  ? 31.56100  -5.60800  -18.86700 1.000 88.40458  ? 46  ILE   A CB  1 
ATOM   91   C  CG1 . ILE   A 1 12  ? 30.09600  -5.48900  -18.44900 1.000 75.41327  ? 46  ILE   A CG1 1 
ATOM   92   C  CG2 . ILE   A 1 12  ? 31.68500  -6.43000  -20.14200 1.000 81.56294  ? 46  ILE   A CG2 1 
ATOM   93   C  CD1 . ILE   A 1 12  ? 29.44100  -6.82600  -18.17000 1.000 87.26763  ? 46  ILE   A CD1 1 
ATOM   94   N  N   . GLY   A 1 13  ? 33.45100  -8.34100  -18.25300 1.000 77.97331  ? 47  GLY   A N   1 
ATOM   95   C  CA  . GLY   A 1 13  ? 34.55500  -9.19900  -18.63300 1.000 72.15639  ? 47  GLY   A CA  1 
ATOM   96   C  C   . GLY   A 1 13  ? 34.26300  -10.17400 -19.75600 1.000 80.14215  ? 47  GLY   A C   1 
ATOM   97   O  O   . GLY   A 1 13  ? 34.29200  -9.80300  -20.93300 1.000 103.63894 ? 47  GLY   A O   1 
ATOM   98   N  N   . LYS   A 1 14  ? 33.98200  -11.42500 -19.40400 1.000 91.01906  ? 48  LYS   A N   1 
ATOM   99   C  CA  . LYS   A 1 14  ? 33.89200  -12.52100 -20.36100 1.000 88.34422  ? 48  LYS   A CA  1 
ATOM   100  C  C   . LYS   A 1 14  ? 32.45400  -13.01100 -20.46800 1.000 87.40917  ? 48  LYS   A C   1 
ATOM   101  O  O   . LYS   A 1 14  ? 31.80200  -13.25600 -19.45000 1.000 83.59631  ? 48  LYS   A O   1 
ATOM   102  C  CB  . LYS   A 1 14  ? 34.80500  -13.67400 -19.94200 1.000 87.23634  ? 48  LYS   A CB  1 
ATOM   103  C  CG  . LYS   A 1 14  ? 35.57400  -14.31200 -21.08200 1.000 96.64879  ? 48  LYS   A CG  1 
ATOM   104  C  CD  . LYS   A 1 14  ? 35.96600  -15.73900 -20.73700 1.000 119.19928 ? 48  LYS   A CD  1 
ATOM   105  C  CE  . LYS   A 1 14  ? 36.62100  -15.82100 -19.36600 1.000 112.84286 ? 48  LYS   A CE  1 
ATOM   106  N  NZ  . LYS   A 1 14  ? 36.88100  -17.23100 -18.96400 1.000 117.76447 ? 48  LYS   A NZ  1 
ATOM   107  N  N   . LYS   A 1 15  ? 31.97400  -13.17900 -21.69700 1.000 86.93257  ? 49  LYS   A N   1 
ATOM   108  C  CA  . LYS   A 1 15  ? 30.61300  -13.65300 -21.91600 1.000 84.34401  ? 49  LYS   A CA  1 
ATOM   109  C  C   . LYS   A 1 15  ? 30.50500  -15.13800 -21.59300 1.000 94.75713  ? 49  LYS   A C   1 
ATOM   110  O  O   . LYS   A 1 15  ? 31.32600  -15.94400 -22.04200 1.000 88.85372  ? 49  LYS   A O   1 
ATOM   111  C  CB  . LYS   A 1 15  ? 30.19700  -13.39800 -23.36100 1.000 97.22416  ? 49  LYS   A CB  1 
ATOM   112  C  CG  . LYS   A 1 15  ? 28.74700  -13.72400 -23.67800 1.000 97.87395  ? 49  LYS   A CG  1 
ATOM   113  C  CD  . LYS   A 1 15  ? 28.48200  -13.43800 -25.14500 1.000 108.16449 ? 49  LYS   A CD  1 
ATOM   114  C  CE  . LYS   A 1 15  ? 29.11100  -12.10500 -25.53800 1.000 100.81844 ? 49  LYS   A CE  1 
ATOM   115  N  NZ  . LYS   A 1 15  ? 29.28800  -11.96400 -27.00500 1.000 105.68615 ? 49  LYS   A NZ  1 
ATOM   116  N  N   . ILE   A 1 16  ? 29.48500  -15.50100 -20.81400 1.000 84.80127  ? 50  ILE   A N   1 
ATOM   117  C  CA  . ILE   A 1 16  ? 29.27200  -16.88500 -20.40500 1.000 96.09573  ? 50  ILE   A CA  1 
ATOM   118  C  C   . ILE   A 1 16  ? 27.79400  -17.23700 -20.52000 1.000 92.10355  ? 50  ILE   A C   1 
ATOM   119  O  O   . ILE   A 1 16  ? 27.36500  -18.30800 -20.07600 1.000 94.44490  ? 50  ILE   A O   1 
ATOM   120  C  CB  . ILE   A 1 16  ? 29.77100  -17.12700 -18.96800 1.000 88.76919  ? 50  ILE   A CB  1 
ATOM   121  C  CG1 . ILE   A 1 16  ? 28.99000  -16.25500 -17.98200 1.000 81.40863  ? 50  ILE   A CG1 1 
ATOM   122  C  CG2 . ILE   A 1 16  ? 31.26700  -16.86200 -18.85300 1.000 82.00067  ? 50  ILE   A CG2 1 
ATOM   123  C  CD1 . ILE   A 1 16  ? 29.43800  -16.40400 -16.54700 1.000 72.37335  ? 50  ILE   A CD1 1 
ATOM   124  N  N   . GLY   A 1 17  ? 27.00500  -16.34400 -21.12100 1.000 106.40119 ? 51  GLY   A N   1 
ATOM   125  C  CA  . GLY   A 1 17  ? 25.56500  -16.47100 -21.12700 1.000 111.76402 ? 51  GLY   A CA  1 
ATOM   126  C  C   . GLY   A 1 17  ? 25.00100  -17.02100 -22.43100 1.000 130.15860 ? 51  GLY   A C   1 
ATOM   127  O  O   . GLY   A 1 17  ? 25.71600  -17.40700 -23.35300 1.000 128.22712 ? 51  GLY   A O   1 
ATOM   128  N  N   . GLU   A 1 18  ? 23.67300  -17.04800 -22.48300 1.000 141.18992 ? 52  GLU   A N   1 
ATOM   129  C  CA  . GLU   A 1 18  ? 22.90800  -17.53200 -23.62100 1.000 144.10014 ? 52  GLU   A CA  1 
ATOM   130  C  C   . GLU   A 1 18  ? 22.16700  -16.36800 -24.27600 1.000 142.06879 ? 52  GLU   A C   1 
ATOM   131  O  O   . GLU   A 1 18  ? 22.32100  -15.20500 -23.89300 1.000 138.09072 ? 52  GLU   A O   1 
ATOM   132  C  CB  . GLU   A 1 18  ? 21.93500  -18.63400 -23.19000 1.000 143.39991 ? 52  GLU   A CB  1 
ATOM   133  C  CG  . GLU   A 1 18  ? 20.73700  -18.15500 -22.37100 1.000 147.53112 ? 52  GLU   A CG  1 
ATOM   134  C  CD  . GLU   A 1 18  ? 20.97500  -18.20000 -20.87100 1.000 137.76432 ? 52  GLU   A CD  1 
ATOM   135  O  OE1 . GLU   A 1 18  ? 21.94000  -17.57200 -20.39100 1.000 122.64382 ? 52  GLU   A OE1 1 
ATOM   136  O  OE2 . GLU   A 1 18  ? 20.19100  -18.87200 -20.16800 1.000 133.53053 ? 52  GLU   A OE2 1 
ATOM   137  N  N   . GLY   A 1 19  ? 21.35100  -16.69300 -25.27500 1.000 146.98919 ? 53  GLY   A N   1 
ATOM   138  C  CA  . GLY   A 1 19  ? 20.62000  -15.67700 -26.00600 1.000 150.21300 ? 53  GLY   A CA  1 
ATOM   139  C  C   . GLY   A 1 19  ? 19.13600  -15.64300 -25.70500 1.000 162.10452 ? 53  GLY   A C   1 
ATOM   140  O  O   . GLY   A 1 19  ? 18.41700  -14.77500 -26.20700 1.000 166.25545 ? 53  GLY   A O   1 
ATOM   141  N  N   . SER   A 1 20  ? 18.66400  -16.58000 -24.88300 1.000 172.02469 ? 54  SER   A N   1 
ATOM   142  C  CA  . SER   A 1 20  ? 17.24800  -16.68200 -24.54600 1.000 176.61885 ? 54  SER   A CA  1 
ATOM   143  C  C   . SER   A 1 20  ? 16.90700  -16.00400 -23.22500 1.000 169.74145 ? 54  SER   A C   1 
ATOM   144  O  O   . SER   A 1 20  ? 15.95800  -15.21800 -23.15800 1.000 166.72367 ? 54  SER   A O   1 
ATOM   145  C  CB  . SER   A 1 20  ? 16.82400  -18.15500 -24.50200 1.000 168.48741 ? 54  SER   A CB  1 
ATOM   146  O  OG  . SER   A 1 20  ? 17.58200  -18.87900 -23.54800 1.000 155.72132 ? 54  SER   A OG  1 
ATOM   147  N  N   . PHE   A 1 21  ? 17.66600  -16.29200 -22.16700 1.000 160.89561 ? 55  PHE   A N   1 
ATOM   148  C  CA  . PHE   A 1 21  ? 17.41500  -15.74700 -20.83900 1.000 158.90167 ? 55  PHE   A CA  1 
ATOM   149  C  C   . PHE   A 1 21  ? 18.29000  -14.53500 -20.53700 1.000 150.63260 ? 55  PHE   A C   1 
ATOM   150  O  O   . PHE   A 1 21  ? 18.69200  -14.32900 -19.38700 1.000 134.08610 ? 55  PHE   A O   1 
ATOM   151  C  CB  . PHE   A 1 21  ? 17.62400  -16.83300 -19.78200 1.000 153.47903 ? 55  PHE   A CB  1 
ATOM   152  C  CG  . PHE   A 1 21  ? 16.63200  -16.78700 -18.65400 1.000 143.74193 ? 55  PHE   A CG  1 
ATOM   153  C  CD1 . PHE   A 1 21  ? 16.07400  -15.58700 -18.24600 1.000 135.41687 ? 55  PHE   A CD1 1 
ATOM   154  C  CD2 . PHE   A 1 21  ? 16.25500  -17.95100 -18.00500 1.000 133.08079 ? 55  PHE   A CD2 1 
ATOM   155  C  CE1 . PHE   A 1 21  ? 15.16100  -15.54900 -17.20800 1.000 128.84368 ? 55  PHE   A CE1 1 
ATOM   156  C  CE2 . PHE   A 1 21  ? 15.34200  -17.92000 -16.96900 1.000 118.23984 ? 55  PHE   A CE2 1 
ATOM   157  C  CZ  . PHE   A 1 21  ? 14.79500  -16.71700 -16.56900 1.000 125.45433 ? 55  PHE   A CZ  1 
ATOM   158  N  N   . GLY   A 1 22  ? 18.59400  -13.72700 -21.55000 1.000 151.83937 ? 56  GLY   A N   1 
ATOM   159  C  CA  . GLY   A 1 22  ? 19.48700  -12.60000 -21.37000 1.000 143.32173 ? 56  GLY   A CA  1 
ATOM   160  C  C   . GLY   A 1 22  ? 20.94000  -13.02300 -21.31700 1.000 136.27376 ? 56  GLY   A C   1 
ATOM   161  O  O   . GLY   A 1 22  ? 21.26600  -14.07200 -20.75500 1.000 145.19666 ? 56  GLY   A O   1 
ATOM   162  N  N   . VAL   A 1 23  ? 21.82700  -12.21600 -21.90100 1.000 113.43676 ? 57  VAL   A N   1 
ATOM   163  C  CA  . VAL   A 1 23  ? 23.23900  -12.57200 -21.94300 1.000 118.79739 ? 57  VAL   A CA  1 
ATOM   164  C  C   . VAL   A 1 23  ? 23.86100  -12.37000 -20.56800 1.000 105.41915 ? 57  VAL   A C   1 
ATOM   165  O  O   . VAL   A 1 23  ? 23.61000  -11.36400 -19.89000 1.000 100.38727 ? 57  VAL   A O   1 
ATOM   166  C  CB  . VAL   A 1 23  ? 23.97000  -11.74700 -23.01600 1.000 122.90588 ? 57  VAL   A CB  1 
ATOM   167  C  CG1 . VAL   A 1 23  ? 25.36400  -12.30500 -23.25200 1.000 125.96014 ? 57  VAL   A CG1 1 
ATOM   168  C  CG2 . VAL   A 1 23  ? 23.17000  -11.73200 -24.30900 1.000 127.56671 ? 57  VAL   A CG2 1 
ATOM   169  N  N   . ILE   A 1 24  ? 24.67900  -13.33200 -20.14800 1.000 85.79474  ? 58  ILE   A N   1 
ATOM   170  C  CA  . ILE   A 1 24  ? 25.33500  -13.31400 -18.84600 1.000 79.92321  ? 58  ILE   A CA  1 
ATOM   171  C  C   . ILE   A 1 24  ? 26.83100  -13.13500 -19.05900 1.000 85.50870  ? 58  ILE   A C   1 
ATOM   172  O  O   . ILE   A 1 24  ? 27.40700  -13.70400 -19.99400 1.000 83.90423  ? 58  ILE   A O   1 
ATOM   173  C  CB  . ILE   A 1 24  ? 25.03100  -14.60100 -18.05300 1.000 80.29754  ? 58  ILE   A CB  1 
ATOM   174  C  CG1 . ILE   A 1 24  ? 23.53100  -14.70600 -17.77400 1.000 77.24249  ? 58  ILE   A CG1 1 
ATOM   175  C  CG2 . ILE   A 1 24  ? 25.81800  -14.64500 -16.75100 1.000 77.55346  ? 58  ILE   A CG2 1 
ATOM   176  C  CD1 . ILE   A 1 24  ? 23.14200  -15.93900 -17.00200 1.000 71.59539  ? 58  ILE   A CD1 1 
ATOM   177  N  N   . PHE   A 1 25  ? 27.45700  -12.33600 -18.19700 1.000 79.72314  ? 59  PHE   A N   1 
ATOM   178  C  CA  . PHE   A 1 25  ? 28.87300  -12.02500 -18.29800 1.000 74.97567  ? 59  PHE   A CA  1 
ATOM   179  C  C   . PHE   A 1 25  ? 29.56800  -12.28900 -16.97000 1.000 69.94421  ? 59  PHE   A C   1 
ATOM   180  O  O   . PHE   A 1 25  ? 28.95000  -12.28200 -15.90300 1.000 67.03215  ? 59  PHE   A O   1 
ATOM   181  C  CB  . PHE   A 1 25  ? 29.10600  -10.56000 -18.69700 1.000 74.42167  ? 59  PHE   A CB  1 
ATOM   182  C  CG  . PHE   A 1 25  ? 28.78200  -10.25500 -20.12900 1.000 76.08561  ? 59  PHE   A CG  1 
ATOM   183  C  CD1 . PHE   A 1 25  ? 27.48300  -9.97300  -20.51600 1.000 81.50031  ? 59  PHE   A CD1 1 
ATOM   184  C  CD2 . PHE   A 1 25  ? 29.78100  -10.23500 -21.08800 1.000 80.19047  ? 59  PHE   A CD2 1 
ATOM   185  C  CE1 . PHE   A 1 25  ? 27.18500  -9.68500  -21.83400 1.000 88.54758  ? 59  PHE   A CE1 1 
ATOM   186  C  CE2 . PHE   A 1 25  ? 29.48900  -9.94800  -22.40800 1.000 84.28902  ? 59  PHE   A CE2 1 
ATOM   187  C  CZ  . PHE   A 1 25  ? 28.19000  -9.67400  -22.78100 1.000 89.32260  ? 59  PHE   A CZ  1 
ATOM   188  N  N   . GLU   A 1 26  ? 30.87200  -12.52900 -17.05700 1.000 71.38263  ? 60  GLU   A N   1 
ATOM   189  C  CA  . GLU   A 1 26  ? 31.74100  -12.46100 -15.89500 1.000 72.83076  ? 60  GLU   A CA  1 
ATOM   190  C  C   . GLU   A 1 26  ? 32.06300  -11.00600 -15.58800 1.000 68.41282  ? 60  GLU   A C   1 
ATOM   191  O  O   . GLU   A 1 26  ? 32.03600  -10.14200 -16.46900 1.000 69.73359  ? 60  GLU   A O   1 
ATOM   192  C  CB  . GLU   A 1 26  ? 33.03700  -13.23800 -16.13100 1.000 81.50619  ? 60  GLU   A CB  1 
ATOM   193  C  CG  . GLU   A 1 26  ? 33.02300  -14.66700 -15.61600 1.000 84.97452  ? 60  GLU   A CG  1 
ATOM   194  C  CD  . GLU   A 1 26  ? 34.39100  -15.31800 -15.68600 1.000 94.96498  ? 60  GLU   A CD  1 
ATOM   195  O  OE1 . GLU   A 1 26  ? 35.29200  -14.73800 -16.32800 1.000 106.16517 ? 60  GLU   A OE1 1 
ATOM   196  O  OE2 . GLU   A 1 26  ? 34.56700  -16.40500 -15.09700 1.000 97.10424  ? 60  GLU   A OE2 1 
ATOM   197  N  N   . GLY   A 1 27  ? 32.37200  -10.73800 -14.32300 1.000 67.56724  ? 61  GLY   A N   1 
ATOM   198  C  CA  . GLY   A 1 27  ? 32.65700  -9.38300  -13.90300 1.000 70.19906  ? 61  GLY   A CA  1 
ATOM   199  C  C   . GLY   A 1 27  ? 33.62400  -9.36900  -12.74200 1.000 46.81679  ? 61  GLY   A C   1 
ATOM   200  O  O   . GLY   A 1 27  ? 33.89000  -10.39300 -12.10800 1.000 61.86848  ? 61  GLY   A O   1 
ATOM   201  N  N   . THR   A 1 28  ? 34.15400  -8.18000  -12.47400 1.000 63.13137  ? 62  THR   A N   1 
ATOM   202  C  CA  . THR   A 1 28  ? 35.08000  -7.96900  -11.37000 1.000 52.96781  ? 62  THR   A CA  1 
ATOM   203  C  C   . THR   A 1 28  ? 34.71900  -6.66300  -10.68400 1.000 53.13317  ? 62  THR   A C   1 
ATOM   204  O  O   . THR   A 1 28  ? 34.65900  -5.61600  -11.33600 1.000 55.65746  ? 62  THR   A O   1 
ATOM   205  C  CB  . THR   A 1 28  ? 36.53300  -7.93000  -11.85500 1.000 64.90957  ? 62  THR   A CB  1 
ATOM   206  O  OG1 . THR   A 1 28  ? 36.89900  -9.21100  -12.38400 1.000 79.19979  ? 62  THR   A OG1 1 
ATOM   207  C  CG2 . THR   A 1 28  ? 37.46800  -7.57200  -10.70800 1.000 56.23142  ? 62  THR   A CG2 1 
ATOM   208  N  N   . ASN   A 1 29  ? 34.46600  -6.72600  -9.38100  1.000 48.07485  ? 63  ASN   A N   1 
ATOM   209  C  CA  . ASN   A 1 29  ? 34.27500  -5.51100  -8.60500  1.000 50.84558  ? 63  ASN   A CA  1 
ATOM   210  C  C   . ASN   A 1 29  ? 35.57200  -4.71200  -8.59700  1.000 47.23816  ? 63  ASN   A C   1 
ATOM   211  O  O   . ASN   A 1 29  ? 36.61100  -5.20500  -8.15200  1.000 51.50106  ? 63  ASN   A O   1 
ATOM   212  C  CB  . ASN   A 1 29  ? 33.83400  -5.85900  -7.18300  1.000 39.74752  ? 63  ASN   A CB  1 
ATOM   213  C  CG  . ASN   A 1 29  ? 33.33700  -4.64900  -6.40900  1.000 60.08133  ? 63  ASN   A CG  1 
ATOM   214  O  OD1 . ASN   A 1 29  ? 33.98700  -3.60600  -6.37600  1.000 58.56868  ? 63  ASN   A OD1 1 
ATOM   215  N  ND2 . ASN   A 1 29  ? 32.17200  -4.78500  -5.78600  1.000 58.27124  ? 63  ASN   A ND2 1 
ATOM   216  N  N   . ILE   A 1 30  ? 35.51800  -3.47900  -9.11000  1.000 41.89815  ? 64  ILE   A N   1 
ATOM   217  C  CA  . ILE   A 1 30  ? 36.72900  -2.67300  -9.25900  1.000 44.45799  ? 64  ILE   A CA  1 
ATOM   218  C  C   . ILE   A 1 30  ? 37.19000  -2.04600  -7.95500  1.000 51.01580  ? 64  ILE   A C   1 
ATOM   219  O  O   . ILE   A 1 30  ? 38.18300  -1.30900  -7.95400  1.000 53.40792  ? 64  ILE   A O   1 
ATOM   220  C  CB  . ILE   A 1 30  ? 36.52700  -1.56200  -10.30900 1.000 62.46225  ? 64  ILE   A CB  1 
ATOM   221  C  CG1 . ILE   A 1 30  ? 35.42000  -0.60500  -9.87200  1.000 65.07698  ? 64  ILE   A CG1 1 
ATOM   222  C  CG2 . ILE   A 1 30  ? 36.20600  -2.16800  -11.66600 1.000 60.25175  ? 64  ILE   A CG2 1 
ATOM   223  C  CD1 . ILE   A 1 30  ? 35.17300  0.52600   -10.84600 1.000 69.55181  ? 64  ILE   A CD1 1 
ATOM   224  N  N   . ILE   A 1 31  ? 36.50800  -2.31200  -6.84800  1.000 54.33613  ? 65  ILE   A N   1 
ATOM   225  C  CA  . ILE   A 1 31  ? 36.90800  -1.80600  -5.54000  1.000 45.76462  ? 65  ILE   A CA  1 
ATOM   226  C  C   . ILE   A 1 31  ? 37.69000  -2.85300  -4.75600  1.000 51.95863  ? 65  ILE   A C   1 
ATOM   227  O  O   . ILE   A 1 31  ? 38.72000  -2.54600  -4.16000  1.000 53.47925  ? 65  ILE   A O   1 
ATOM   228  C  CB  . ILE   A 1 31  ? 35.67500  -1.31100  -4.74800  1.000 48.73245  ? 65  ILE   A CB  1 
ATOM   229  C  CG1 . ILE   A 1 31  ? 35.40900  0.16900   -5.02900  1.000 54.90435  ? 65  ILE   A CG1 1 
ATOM   230  C  CG2 . ILE   A 1 31  ? 35.86000  -1.53200  -3.25100  1.000 62.93978  ? 65  ILE   A CG2 1 
ATOM   231  C  CD1 . ILE   A 1 31  ? 34.89700  0.46000   -6.41900  1.000 60.06815  ? 65  ILE   A CD1 1 
ATOM   232  N  N   . ASN   A 1 32  ? 37.22200  -4.10300  -4.75500  1.000 59.82439  ? 66  ASN   A N   1 
ATOM   233  C  CA  . ASN   A 1 32  ? 37.84300  -5.15900  -3.97000  1.000 54.25168  ? 66  ASN   A CA  1 
ATOM   234  C  C   . ASN   A 1 32  ? 38.25800  -6.37400  -4.78400  1.000 59.50220  ? 66  ASN   A C   1 
ATOM   235  O  O   . ASN   A 1 32  ? 38.90700  -7.26900  -4.23200  1.000 67.86581  ? 66  ASN   A O   1 
ATOM   236  C  CB  . ASN   A 1 32  ? 36.90000  -5.61100  -2.84600  1.000 59.83688  ? 66  ASN   A CB  1 
ATOM   237  C  CG  . ASN   A 1 32  ? 35.51100  -5.95200  -3.34800  1.000 63.66827  ? 66  ASN   A CG  1 
ATOM   238  O  OD1 . ASN   A 1 32  ? 35.33600  -6.35800  -4.49300  1.000 64.17178  ? 66  ASN   A OD1 1 
ATOM   239  N  ND2 . ASN   A 1 32  ? 34.51300  -5.78200  -2.48800  1.000 66.61776  ? 66  ASN   A ND2 1 
ATOM   240  N  N   . GLY   A 1 33  ? 37.90200  -6.43900  -6.06200  1.000 58.78916  ? 67  GLY   A N   1 
ATOM   241  C  CA  . GLY   A 1 33  ? 38.35400  -7.52000  -6.91100  1.000 43.62136  ? 67  GLY   A CA  1 
ATOM   242  C  C   . GLY   A 1 33  ? 37.59900  -8.82100  -6.77900  1.000 56.77294  ? 67  GLY   A C   1 
ATOM   243  O  O   . GLY   A 1 33  ? 38.09900  -9.85700  -7.22900  1.000 63.46815  ? 67  GLY   A O   1 
ATOM   244  N  N   . VAL   A 1 34  ? 36.41000  -8.80800  -6.18300  1.000 54.88493  ? 68  VAL   A N   1 
ATOM   245  C  CA  . VAL   A 1 34  ? 35.62400  -10.03400 -6.08000  1.000 64.87888  ? 68  VAL   A CA  1 
ATOM   246  C  C   . VAL   A 1 34  ? 34.94000  -10.27300 -7.42200  1.000 58.89307  ? 68  VAL   A C   1 
ATOM   247  O  O   . VAL   A 1 34  ? 34.48300  -9.32000  -8.07100  1.000 46.60346  ? 68  VAL   A O   1 
ATOM   248  C  CB  . VAL   A 1 34  ? 34.61400  -9.98300  -4.91700  1.000 57.49815  ? 68  VAL   A CB  1 
ATOM   249  C  CG1 . VAL   A 1 34  ? 35.29200  -9.51800  -3.63200  1.000 56.11893  ? 68  VAL   A CG1 1 
ATOM   250  C  CG2 . VAL   A 1 34  ? 33.40500  -9.11600  -5.25200  1.000 58.20707  ? 68  VAL   A CG2 1 
ATOM   251  N  N   . PRO   A 1 35  ? 34.88900  -11.51300 -7.89400  1.000 61.96024  ? 69  PRO   A N   1 
ATOM   252  C  CA  . PRO   A 1 35  ? 34.21800  -11.79600 -9.16400  1.000 41.46308  ? 69  PRO   A CA  1 
ATOM   253  C  C   . PRO   A 1 35  ? 32.70900  -11.79400 -9.00200  1.000 42.73946  ? 69  PRO   A C   1 
ATOM   254  O  O   . PRO   A 1 35  ? 32.16900  -12.12200 -7.94300  1.000 46.52733  ? 69  PRO   A O   1 
ATOM   255  C  CB  . PRO   A 1 35  ? 34.73300  -13.19300 -9.52500  1.000 51.97128  ? 69  PRO   A CB  1 
ATOM   256  C  CG  . PRO   A 1 35  ? 35.01700  -13.82300 -8.20200  1.000 50.72792  ? 69  PRO   A CG  1 
ATOM   257  C  CD  . PRO   A 1 35  ? 35.50900  -12.71400 -7.31100  1.000 42.83936  ? 69  PRO   A CD  1 
ATOM   258  N  N   . VAL   A 1 36  ? 32.02400  -11.40500 -10.07700 1.000 40.44672  ? 70  VAL   A N   1 
ATOM   259  C  CA  . VAL   A 1 36  ? 30.57100  -11.32400 -10.08600 1.000 41.73234  ? 70  VAL   A CA  1 
ATOM   260  C  C   . VAL   A 1 36  ? 30.05000  -11.86800 -11.40800 1.000 50.61827  ? 70  VAL   A C   1 
ATOM   261  O  O   . VAL   A 1 36  ? 30.78400  -11.99700 -12.39000 1.000 43.79688  ? 70  VAL   A O   1 
ATOM   262  C  CB  . VAL   A 1 36  ? 30.05700  -9.88200  -9.87000  1.000 47.30241  ? 70  VAL   A CB  1 
ATOM   263  C  CG1 . VAL   A 1 36  ? 30.41200  -9.38200  -8.47600  1.000 41.71497  ? 70  VAL   A CG1 1 
ATOM   264  C  CG2 . VAL   A 1 36  ? 30.61200  -8.95000  -10.93500 1.000 38.95219  ? 70  VAL   A CG2 1 
ATOM   265  N  N   . ALA   A 1 37  ? 28.76400  -12.20000 -11.41300 1.000 46.00086  ? 71  ALA   A N   1 
ATOM   266  C  CA  . ALA   A 1 37  ? 28.03400  -12.55200 -12.62300 1.000 61.64643  ? 71  ALA   A CA  1 
ATOM   267  C  C   . ALA   A 1 37  ? 27.06100  -11.42100 -12.92300 1.000 56.12660  ? 71  ALA   A C   1 
ATOM   268  O  O   . ALA   A 1 37  ? 26.22700  -11.07700 -12.07900 1.000 59.36488  ? 71  ALA   A O   1 
ATOM   269  C  CB  . ALA   A 1 37  ? 27.29300  -13.88000 -12.46100 1.000 57.33240  ? 71  ALA   A CB  1 
ATOM   270  N  N   . ILE   A 1 38  ? 27.17800  -10.83900 -14.11200 1.000 57.10124  ? 72  ILE   A N   1 
ATOM   271  C  CA  . ILE   A 1 38  ? 26.37600  -9.69000  -14.51600 1.000 70.07664  ? 72  ILE   A CA  1 
ATOM   272  C  C   . ILE   A 1 38  ? 25.42300  -10.14500 -15.61100 1.000 69.45601  ? 72  ILE   A C   1 
ATOM   273  O  O   . ILE   A 1 38  ? 25.85900  -10.60500 -16.67300 1.000 72.36961  ? 72  ILE   A O   1 
ATOM   274  C  CB  . ILE   A 1 38  ? 27.25700  -8.52700  -14.99200 1.000 70.64192  ? 72  ILE   A CB  1 
ATOM   275  C  CG1 . ILE   A 1 38  ? 28.32600  -8.21000  -13.94400 1.000 64.63452  ? 72  ILE   A CG1 1 
ATOM   276  C  CG2 . ILE   A 1 38  ? 26.40800  -7.30000  -15.26600 1.000 75.16255  ? 72  ILE   A CG2 1 
ATOM   277  C  CD1 . ILE   A 1 38  ? 29.36100  -7.21300  -14.41400 1.000 55.63676  ? 72  ILE   A CD1 1 
ATOM   278  N  N   . LYS   A 1 39  ? 24.12500  -10.00900 -15.35900 1.000 70.66939  ? 73  LYS   A N   1 
ATOM   279  C  CA  . LYS   A 1 39  ? 23.08800  -10.50500 -16.25400 1.000 65.97111  ? 73  LYS   A CA  1 
ATOM   280  C  C   . LYS   A 1 39  ? 22.37100  -9.32800  -16.90200 1.000 81.23455  ? 73  LYS   A C   1 
ATOM   281  O  O   . LYS   A 1 39  ? 21.86000  -8.44500  -16.20500 1.000 71.52014  ? 73  LYS   A O   1 
ATOM   282  C  CB  . LYS   A 1 39  ? 22.10300  -11.39300 -15.49600 1.000 69.27538  ? 73  LYS   A CB  1 
ATOM   283  C  CG  . LYS   A 1 39  ? 20.93500  -11.88900 -16.32900 1.000 80.90683  ? 73  LYS   A CG  1 
ATOM   284  C  CD  . LYS   A 1 39  ? 20.42100  -13.21200 -15.79400 1.000 72.31289  ? 73  LYS   A CD  1 
ATOM   285  C  CE  . LYS   A 1 39  ? 18.96500  -13.43800 -16.16000 1.000 73.67029  ? 73  LYS   A CE  1 
ATOM   286  N  NZ  . LYS   A 1 39  ? 18.17900  -13.81900 -14.95400 1.000 75.42657  ? 73  LYS   A NZ  1 
ATOM   287  N  N   . PHE   A 1 40  ? 22.33600  -9.32300  -18.22900 1.000 81.78218  ? 74  PHE   A N   1 
ATOM   288  C  CA  . PHE   A 1 40  ? 21.68300  -8.27600  -18.99800 1.000 80.80062  ? 74  PHE   A CA  1 
ATOM   289  C  C   . PHE   A 1 40  ? 20.28100  -8.71200  -19.40500 1.000 95.54808  ? 74  PHE   A C   1 
ATOM   290  O  O   . PHE   A 1 40  ? 19.97700  -9.90300  -19.50200 1.000 99.55113  ? 74  PHE   A O   1 
ATOM   291  C  CB  . PHE   A 1 40  ? 22.49500  -7.92300  -20.24800 1.000 84.12862  ? 74  PHE   A CB  1 
ATOM   292  C  CG  . PHE   A 1 40  ? 23.81400  -7.25800  -19.96000 1.000 95.92192  ? 74  PHE   A CG  1 
ATOM   293  C  CD1 . PHE   A 1 40  ? 24.15700  -6.87600  -18.67300 1.000 88.55125  ? 74  PHE   A CD1 1 
ATOM   294  C  CD2 . PHE   A 1 40  ? 24.70800  -7.00600  -20.98800 1.000 94.13852  ? 74  PHE   A CD2 1 
ATOM   295  C  CE1 . PHE   A 1 40  ? 25.37000  -6.26300  -18.41500 1.000 87.39557  ? 74  PHE   A CE1 1 
ATOM   296  C  CE2 . PHE   A 1 40  ? 25.92200  -6.39100  -20.73700 1.000 98.65359  ? 74  PHE   A CE2 1 
ATOM   297  C  CZ  . PHE   A 1 40  ? 26.25300  -6.02100  -19.44900 1.000 94.40998  ? 74  PHE   A CZ  1 
ATOM   298  N  N   . GLU   A 1 41  ? 19.42400  -7.71900  -19.64400 1.000 90.92660  ? 75  GLU   A N   1 
ATOM   299  C  CA  . GLU   A 1 41  ? 18.06600  -7.95300  -20.09000 1.000 97.66007  ? 75  GLU   A CA  1 
ATOM   300  C  C   . GLU   A 1 41  ? 17.61600  -6.69900  -20.82500 1.000 101.95140 ? 75  GLU   A C   1 
ATOM   301  O  O   . GLU   A 1 41  ? 17.83000  -5.59000  -20.31300 1.000 104.96690 ? 75  GLU   A O   1 
ATOM   302  C  CB  . GLU   A 1 41  ? 17.10700  -8.25300  -18.93700 1.000 96.11630  ? 75  GLU   A CB  1 
ATOM   303  C  CG  . GLU   A 1 41  ? 15.70200  -8.62200  -19.38800 1.000 105.78520 ? 75  GLU   A CG  1 
ATOM   304  C  CD  . GLU   A 1 41  ? 14.66400  -8.40100  -18.30700 1.000 102.95288 ? 75  GLU   A CD  1 
ATOM   305  O  OE1 . GLU   A 1 41  ? 14.77700  -7.40100  -17.56800 1.000 109.13396 ? 75  GLU   A OE1 1 
ATOM   306  O  OE2 . GLU   A 1 41  ? 13.73400  -9.22700  -18.19600 1.000 108.07351 ? 75  GLU   A OE2 1 
ATOM   307  N  N   . PRO   A 1 42  ? 17.01800  -6.83100  -22.00800 1.000 99.75034  ? 76  PRO   A N   1 
ATOM   308  C  CA  . PRO   A 1 42  ? 16.49900  -5.64800  -22.70400 1.000 105.77059 ? 76  PRO   A CA  1 
ATOM   309  C  C   . PRO   A 1 42  ? 15.45900  -4.92500  -21.86000 1.000 112.58997 ? 76  PRO   A C   1 
ATOM   310  O  O   . PRO   A 1 42  ? 14.65200  -5.54800  -21.16700 1.000 112.36512 ? 76  PRO   A O   1 
ATOM   311  C  CB  . PRO   A 1 42  ? 15.88700  -6.22900  -23.98300 1.000 89.45113  ? 76  PRO   A CB  1 
ATOM   312  C  CG  . PRO   A 1 42  ? 16.61800  -7.51700  -24.19500 1.000 106.18922 ? 76  PRO   A CG  1 
ATOM   313  C  CD  . PRO   A 1 42  ? 16.89600  -8.05300  -22.82100 1.000 101.55756 ? 76  PRO   A CD  1 
ATOM   314  N  N   . ARG   A 1 43  ? 15.49300  -3.59400  -21.91700 1.000 133.69903 ? 77  ARG   A N   1 
ATOM   315  C  CA  . ARG   A 1 43  ? 14.59500  -2.77300  -21.11400 1.000 135.38164 ? 77  ARG   A CA  1 
ATOM   316  C  C   . ARG   A 1 43  ? 13.15300  -2.91400  -21.58400 1.000 137.04551 ? 77  ARG   A C   1 
ATOM   317  O  O   . ARG   A 1 43  ? 12.32600  -3.51800  -20.89300 1.000 144.41939 ? 77  ARG   A O   1 
ATOM   318  C  CB  . ARG   A 1 43  ? 15.02900  -1.30500  -21.15500 1.000 131.90647 ? 77  ARG   A CB  1 
ATOM   319  C  CG  . ARG   A 1 43  ? 14.05400  -0.34800  -20.48400 1.000 140.17197 ? 77  ARG   A CG  1 
ATOM   320  C  CD  . ARG   A 1 43  ? 13.79500  -0.73000  -19.03600 1.000 139.80270 ? 77  ARG   A CD  1 
ATOM   321  N  NE  . ARG   A 1 43  ? 12.71500  0.05900   -18.45500 1.000 164.59140 ? 77  ARG   A NE  1 
ATOM   322  C  CZ  . ARG   A 1 43  ? 12.32200  -0.02000  -17.19100 1.000 158.75049 ? 77  ARG   A CZ  1 
ATOM   323  N  NH1 . ARG   A 1 43  ? 12.90900  -0.84100  -16.33500 1.000 140.39489 ? 77  ARG   A NH1 1 
ATOM   324  N  NH2 . ARG   A 1 43  ? 11.31600  0.74400   -16.77500 1.000 159.16298 ? 77  ARG   A NH2 1 
ATOM   325  N  N   . LYS   A 1 44  ? 12.83900  -2.35600  -22.75400 1.000 97.66162  ? 78  LYS   A N   1 
ATOM   326  C  CA  . LYS   A 1 44  ? 11.49100  -2.43400  -23.31300 1.000 115.36875 ? 78  LYS   A CA  1 
ATOM   327  C  C   . LYS   A 1 44  ? 11.33100  -3.80300  -23.97000 1.000 129.19017 ? 78  LYS   A C   1 
ATOM   328  O  O   . LYS   A 1 44  ? 11.44600  -3.97300  -25.18600 1.000 124.70526 ? 78  LYS   A O   1 
ATOM   329  C  CB  . LYS   A 1 44  ? 11.24800  -1.29400  -24.29300 1.000 108.91537 ? 78  LYS   A CB  1 
ATOM   330  C  CG  . LYS   A 1 44  ? 9.78900   -1.09900  -24.66500 1.000 109.04905 ? 78  LYS   A CG  1 
ATOM   331  C  CD  . LYS   A 1 44  ? 9.55200   -1.44100  -26.12300 1.000 114.32663 ? 78  LYS   A CD  1 
ATOM   332  C  CE  . LYS   A 1 44  ? 10.38900  -0.55100  -27.02600 1.000 116.26260 ? 78  LYS   A CE  1 
ATOM   333  N  NZ  . LYS   A 1 44  ? 10.31600  -0.96300  -28.45300 1.000 121.46081 ? 78  LYS   A NZ  1 
ATOM   334  N  N   . THR   A 1 45  ? 11.06200  -4.80100  -23.13100 1.000 117.42966 ? 79  THR   A N   1 
ATOM   335  C  CA  . THR   A 1 45  ? 10.96900  -6.18900  -23.55100 1.000 116.84175 ? 79  THR   A CA  1 
ATOM   336  C  C   . THR   A 1 45  ? 9.55800   -6.71100  -23.31800 1.000 132.33352 ? 79  THR   A C   1 
ATOM   337  O  O   . THR   A 1 45  ? 8.77500   -6.13500  -22.55700 1.000 131.72535 ? 79  THR   A O   1 
ATOM   338  C  CB  . THR   A 1 45  ? 11.98500  -7.06300  -22.79900 1.000 124.10794 ? 79  THR   A CB  1 
ATOM   339  O  OG1 . THR   A 1 45  ? 11.88000  -8.42200  -23.24100 1.000 128.12136 ? 79  THR   A OG1 1 
ATOM   340  C  CG2 . THR   A 1 45  ? 11.73300  -7.00000  -21.29900 1.000 114.24051 ? 79  THR   A CG2 1 
ATOM   341  N  N   . GLU   A 1 46  ? 9.24000   -7.81900  -23.99000 1.000 138.39225 ? 80  GLU   A N   1 
ATOM   342  C  CA  . GLU   A 1 46  ? 7.92700   -8.43300  -23.86000 1.000 143.81151 ? 80  GLU   A CA  1 
ATOM   343  C  C   . GLU   A 1 46  ? 7.76400   -9.20400  -22.55600 1.000 142.50459 ? 80  GLU   A C   1 
ATOM   344  O  O   . GLU   A 1 46  ? 6.63100   -9.39400  -22.10300 1.000 147.28376 ? 80  GLU   A O   1 
ATOM   345  C  CB  . GLU   A 1 46  ? 7.66600   -9.36500  -25.04700 1.000 142.59522 ? 80  GLU   A CB  1 
ATOM   346  C  CG  . GLU   A 1 46  ? 6.19500   -9.63900  -25.33500 1.000 138.42475 ? 80  GLU   A CG  1 
ATOM   347  C  CD  . GLU   A 1 46  ? 5.53400   -8.53300  -26.14100 1.000 145.86585 ? 80  GLU   A CD  1 
ATOM   348  O  OE1 . GLU   A 1 46  ? 5.68400   -7.34700  -25.77900 1.000 153.09869 ? 80  GLU   A OE1 1 
ATOM   349  O  OE2 . GLU   A 1 46  ? 4.86800   -8.85200  -27.14900 1.000 156.46631 ? 80  GLU   A OE2 1 
ATOM   350  N  N   . ALA   A 1 47  ? 8.86200   -9.64600  -21.94300 1.000 141.35919 ? 81  ALA   A N   1 
ATOM   351  C  CA  . ALA   A 1 47  ? 8.82500   -10.42800 -20.70700 1.000 142.55005 ? 81  ALA   A CA  1 
ATOM   352  C  C   . ALA   A 1 47  ? 9.75600   -9.79400  -19.68100 1.000 138.75107 ? 81  ALA   A C   1 
ATOM   353  O  O   . ALA   A 1 47  ? 10.90800  -10.22100 -19.52200 1.000 139.78472 ? 81  ALA   A O   1 
ATOM   354  C  CB  . ALA   A 1 47  ? 9.20400   -11.88700 -20.96500 1.000 130.07021 ? 81  ALA   A CB  1 
ATOM   355  N  N   . PRO   A 1 48  ? 9.29000   -8.76800  -18.96800 1.000 138.04274 ? 82  PRO   A N   1 
ATOM   356  C  CA  . PRO   A 1 48  ? 10.10700  -8.17100  -17.89800 1.000 129.79004 ? 82  PRO   A CA  1 
ATOM   357  C  C   . PRO   A 1 48  ? 10.18100  -9.10500  -16.69800 1.000 127.04158 ? 82  PRO   A C   1 
ATOM   358  O  O   . PRO   A 1 48  ? 9.15500   -9.51800  -16.15400 1.000 129.18250 ? 82  PRO   A O   1 
ATOM   359  C  CB  . PRO   A 1 48  ? 9.36200   -6.87200  -17.56200 1.000 132.27107 ? 82  PRO   A CB  1 
ATOM   360  C  CG  . PRO   A 1 48  ? 8.42500   -6.63900  -18.71800 1.000 141.97703 ? 82  PRO   A CG  1 
ATOM   361  C  CD  . PRO   A 1 48  ? 8.05800   -8.00100  -19.20800 1.000 137.62428 ? 82  PRO   A CD  1 
ATOM   362  N  N   . GLN   A 1 49  ? 11.40500  -9.43400  -16.28300 1.000 121.55930 ? 83  GLN   A N   1 
ATOM   363  C  CA  . GLN   A 1 49  ? 11.61300  -10.36100 -15.17300 1.000 114.07699 ? 83  GLN   A CA  1 
ATOM   364  C  C   . GLN   A 1 49  ? 12.78700  -10.01800 -14.27100 1.000 101.06220 ? 83  GLN   A C   1 
ATOM   365  O  O   . GLN   A 1 49  ? 12.80700  -10.48700 -13.12800 1.000 91.41806  ? 83  GLN   A O   1 
ATOM   366  C  CB  . GLN   A 1 49  ? 11.81500  -11.78900 -15.69600 1.000 119.22441 ? 83  GLN   A CB  1 
ATOM   367  C  CG  . GLN   A 1 49  ? 10.54200  -12.58300 -15.90500 1.000 129.79989 ? 83  GLN   A CG  1 
ATOM   368  C  CD  . GLN   A 1 49  ? 10.82500  -14.03700 -16.23100 1.000 122.56021 ? 83  GLN   A CD  1 
ATOM   369  O  OE1 . GLN   A 1 49  ? 11.96100  -14.40500 -16.53400 1.000 123.82204 ? 83  GLN   A OE1 1 
ATOM   370  N  NE2 . GLN   A 1 49  ? 9.79600   -14.87200 -16.16400 1.000 118.04807 ? 83  GLN   A NE2 1 
ATOM   371  N  N   . LEU   A 1 50  ? 13.76400  -9.23000  -14.72400 1.000 99.38373  ? 84  LEU   A N   1 
ATOM   372  C  CA  . LEU   A 1 50  ? 14.99300  -9.07000  -13.95300 1.000 90.93752  ? 84  LEU   A CA  1 
ATOM   373  C  C   . LEU   A 1 50  ? 14.77200  -8.26800  -12.67700 1.000 82.12132  ? 84  LEU   A C   1 
ATOM   374  O  O   . LEU   A 1 50  ? 15.51000  -8.45000  -11.70200 1.000 86.85645  ? 84  LEU   A O   1 
ATOM   375  C  CB  . LEU   A 1 50  ? 16.07200  -8.41600  -14.81600 1.000 82.15237  ? 84  LEU   A CB  1 
ATOM   376  C  CG  . LEU   A 1 50  ? 17.49600  -8.52300  -14.27200 1.000 84.52488  ? 84  LEU   A CG  1 
ATOM   377  C  CD1 . LEU   A 1 50  ? 17.71900  -9.91700  -13.71500 1.000 74.24285  ? 84  LEU   A CD1 1 
ATOM   378  C  CD2 . LEU   A 1 50  ? 18.51100  -8.21300  -15.35900 1.000 86.26884  ? 84  LEU   A CD2 1 
ATOM   379  N  N   . ARG   A 1 51  ? 13.77300  -7.38300  -12.65700 1.000 84.01370  ? 85  ARG   A N   1 
ATOM   380  C  CA  . ARG   A 1 51  ? 13.51100  -6.60100  -11.45300 1.000 73.72223  ? 85  ARG   A CA  1 
ATOM   381  C  C   . ARG   A 1 51  ? 13.06700  -7.49800  -10.30500 1.000 77.21095  ? 85  ARG   A C   1 
ATOM   382  O  O   . ARG   A 1 51  ? 13.59900  -7.40800  -9.19300  1.000 76.92115  ? 85  ARG   A O   1 
ATOM   383  C  CB  . ARG   A 1 51  ? 12.45800  -5.52900  -11.73600 1.000 85.23384  ? 85  ARG   A CB  1 
ATOM   384  C  CG  . ARG   A 1 51  ? 12.21900  -4.56700  -10.58000 1.000 85.33382  ? 85  ARG   A CG  1 
ATOM   385  C  CD  . ARG   A 1 51  ? 10.79600  -4.69000  -10.05500 1.000 93.96109  ? 85  ARG   A CD  1 
ATOM   386  N  NE  . ARG   A 1 51  ? 10.52000  -3.77100  -8.95800  1.000 113.91509 ? 85  ARG   A NE  1 
ATOM   387  C  CZ  . ARG   A 1 51  ? 9.41200   -3.79600  -8.23200  1.000 108.96364 ? 85  ARG   A CZ  1 
ATOM   388  N  NH1 . ARG   A 1 51  ? 8.45000   -4.67600  -8.46800  1.000 119.00298 ? 85  ARG   A NH1 1 
ATOM   389  N  NH2 . ARG   A 1 51  ? 9.26800   -2.92400  -7.23900  1.000 104.93351 ? 85  ARG   A NH2 1 
ATOM   390  N  N   . ASP   A 1 52  ? 12.09800  -8.38000  -10.56000 1.000 86.53326  ? 86  ASP   A N   1 
ATOM   391  C  CA  . ASP   A 1 52  ? 11.59200  -9.24700  -9.50300  1.000 80.77708  ? 86  ASP   A CA  1 
ATOM   392  C  C   . ASP   A 1 52  ? 12.60300  -10.31600 -9.11100  1.000 73.13770  ? 86  ASP   A C   1 
ATOM   393  O  O   . ASP   A 1 52  ? 12.55700  -10.82200 -7.98400  1.000 71.87611  ? 86  ASP   A O   1 
ATOM   394  C  CB  . ASP   A 1 52  ? 10.27600  -9.89600  -9.93400  1.000 80.02600  ? 86  ASP   A CB  1 
ATOM   395  C  CG  . ASP   A 1 52  ? 9.06400   -9.12700  -9.45500  1.000 96.45804  ? 86  ASP   A CG  1 
ATOM   396  O  OD1 . ASP   A 1 52  ? 9.24400   -8.13600  -8.72000  1.000 97.40301  ? 86  ASP   A OD1 1 
ATOM   397  O  OD2 . ASP   A 1 52  ? 7.93300   -9.51300  -9.81300  1.000 114.71966 ? 86  ASP   A OD2 1 
ATOM   398  N  N   . GLU   A 1 53  ? 13.51100  -10.68100 -10.02100 1.000 75.48733  ? 87  GLU   A N   1 
ATOM   399  C  CA  . GLU   A 1 53  ? 14.56600  -11.62600 -9.66900  1.000 77.55134  ? 87  GLU   A CA  1 
ATOM   400  C  C   . GLU   A 1 53  ? 15.56000  -10.99600 -8.70200  1.000 64.63870  ? 87  GLU   A C   1 
ATOM   401  O  O   . GLU   A 1 53  ? 16.07200  -11.67000 -7.80100  1.000 58.65784  ? 87  GLU   A O   1 
ATOM   402  C  CB  . GLU   A 1 53  ? 15.27000  -12.11900 -10.93400 1.000 69.24900  ? 87  GLU   A CB  1 
ATOM   403  C  CG  . GLU   A 1 53  ? 16.33300  -13.17500 -10.67400 1.000 81.73768  ? 87  GLU   A CG  1 
ATOM   404  C  CD  . GLU   A 1 53  ? 16.83200  -13.83900 -11.94400 1.000 74.02337  ? 87  GLU   A CD  1 
ATOM   405  O  OE1 . GLU   A 1 53  ? 16.17900  -13.68900 -12.99900 1.000 92.30003  ? 87  GLU   A OE1 1 
ATOM   406  O  OE2 . GLU   A 1 53  ? 17.88000  -14.51500 -11.88200 1.000 75.34025  ? 87  GLU   A OE2 1 
ATOM   407  N  N   . TYR   A 1 54  ? 15.84700  -9.70400  -8.87800  1.000 74.69019  ? 88  TYR   A N   1 
ATOM   408  C  CA  . TYR   A 1 54  ? 16.68700  -8.99300  -7.92100  1.000 61.14567  ? 88  TYR   A CA  1 
ATOM   409  C  C   . TYR   A 1 54  ? 16.05500  -8.98300  -6.53500  1.000 64.15845  ? 88  TYR   A C   1 
ATOM   410  O  O   . TYR   A 1 54  ? 16.75100  -9.13900  -5.52600  1.000 65.81156  ? 88  TYR   A O   1 
ATOM   411  C  CB  . TYR   A 1 54  ? 16.93700  -7.56700  -8.40700  1.000 70.94952  ? 88  TYR   A CB  1 
ATOM   412  C  CG  . TYR   A 1 54  ? 17.50700  -6.63900  -7.35800  1.000 68.00611  ? 88  TYR   A CG  1 
ATOM   413  C  CD1 . TYR   A 1 54  ? 18.81600  -6.77700  -6.91600  1.000 68.00690  ? 88  TYR   A CD1 1 
ATOM   414  C  CD2 . TYR   A 1 54  ? 16.74000  -5.61200  -6.82200  1.000 75.44575  ? 88  TYR   A CD2 1 
ATOM   415  C  CE1 . TYR   A 1 54  ? 19.34200  -5.92600  -5.96500  1.000 85.57254  ? 88  TYR   A CE1 1 
ATOM   416  C  CE2 . TYR   A 1 54  ? 17.25800  -4.75600  -5.87000  1.000 74.64364  ? 88  TYR   A CE2 1 
ATOM   417  C  CZ  . TYR   A 1 54  ? 18.56000  -4.91800  -5.44600  1.000 75.32110  ? 88  TYR   A CZ  1 
ATOM   418  O  OH  . TYR   A 1 54  ? 19.08200  -4.06800  -4.49900  1.000 95.98775  ? 88  TYR   A OH  1 
ATOM   419  N  N   . ARG   A 1 55  ? 14.73400  -8.80400  -6.46400  1.000 81.45792  ? 89  ARG   A N   1 
ATOM   420  C  CA  . ARG   A 1 55  ? 14.05900  -8.79900  -5.17200  1.000 67.64401  ? 89  ARG   A CA  1 
ATOM   421  C  C   . ARG   A 1 55  ? 13.95800  -10.18900 -4.56900  1.000 64.60865  ? 89  ARG   A C   1 
ATOM   422  O  O   . ARG   A 1 55  ? 13.80200  -10.30900 -3.34900  1.000 66.59482  ? 89  ARG   A O   1 
ATOM   423  C  CB  . ARG   A 1 55  ? 12.67300  -8.18200  -5.31500  1.000 74.95880  ? 89  ARG   A CB  1 
ATOM   424  C  CG  . ARG   A 1 55  ? 12.71200  -6.95100  -6.18500  1.000 87.34260  ? 89  ARG   A CG  1 
ATOM   425  C  CD  . ARG   A 1 55  ? 11.67600  -5.92500  -5.80600  1.000 91.91813  ? 89  ARG   A CD  1 
ATOM   426  N  NE  . ARG   A 1 55  ? 11.83700  -4.70500  -6.58900  1.000 110.73618 ? 89  ARG   A NE  1 
ATOM   427  C  CZ  . ARG   A 1 55  ? 12.17600  -3.53200  -6.07600  1.000 118.12379 ? 89  ARG   A CZ  1 
ATOM   428  N  NH1 . ARG   A 1 55  ? 12.32700  -3.36900  -4.77300  1.000 115.01904 ? 89  ARG   A NH1 1 
ATOM   429  N  NH2 . ARG   A 1 55  ? 12.36100  -2.49500  -6.88800  1.000 99.12348  ? 89  ARG   A NH2 1 
ATOM   430  N  N   . THR   A 1 56  ? 14.03500  -11.23800 -5.39000  1.000 69.52274  ? 90  THR   A N   1 
ATOM   431  C  CA  . THR   A 1 56  ? 14.04300  -12.59100 -4.84800  1.000 63.08928  ? 90  THR   A CA  1 
ATOM   432  C  C   . THR   A 1 56  ? 15.35800  -12.88500 -4.13700  1.000 64.60627  ? 90  THR   A C   1 
ATOM   433  O  O   . THR   A 1 56  ? 15.36300  -13.47900 -3.05300  1.000 71.43410  ? 90  THR   A O   1 
ATOM   434  C  CB  . THR   A 1 56  ? 13.79400  -13.61300 -5.95800  1.000 62.05531  ? 90  THR   A CB  1 
ATOM   435  O  OG1 . THR   A 1 56  ? 12.55100  -13.32400 -6.61000  1.000 60.91435  ? 90  THR   A OG1 1 
ATOM   436  C  CG2 . THR   A 1 56  ? 13.73600  -15.02000 -5.37700  1.000 52.34484  ? 90  THR   A CG2 1 
ATOM   437  N  N   . TYR   A 1 57  ? 16.48500  -12.47800 -4.73000  1.000 48.98417  ? 91  TYR   A N   1 
ATOM   438  C  CA  . TYR   A 1 57  ? 17.77100  -12.66000 -4.06500  1.000 54.38197  ? 91  TYR   A CA  1 
ATOM   439  C  C   . TYR   A 1 57  ? 17.84000  -11.85200 -2.77600  1.000 55.41466  ? 91  TYR   A C   1 
ATOM   440  O  O   . TYR   A 1 57  ? 18.36000  -12.33000 -1.76100  1.000 61.79845  ? 91  TYR   A O   1 
ATOM   441  C  CB  . TYR   A 1 57  ? 18.91700  -12.26700 -4.99800  1.000 53.70737  ? 91  TYR   A CB  1 
ATOM   442  C  CG  . TYR   A 1 57  ? 19.10600  -13.18400 -6.18600  1.000 47.35351  ? 91  TYR   A CG  1 
ATOM   443  C  CD1 . TYR   A 1 57  ? 19.44900  -14.51900 -6.01200  1.000 61.70767  ? 91  TYR   A CD1 1 
ATOM   444  C  CD2 . TYR   A 1 57  ? 18.96500  -12.70900 -7.48300  1.000 55.46297  ? 91  TYR   A CD2 1 
ATOM   445  C  CE1 . TYR   A 1 57  ? 19.62900  -15.35800 -7.09600  1.000 53.10190  ? 91  TYR   A CE1 1 
ATOM   446  C  CE2 . TYR   A 1 57  ? 19.14300  -13.53900 -8.57300  1.000 50.38453  ? 91  TYR   A CE2 1 
ATOM   447  C  CZ  . TYR   A 1 57  ? 19.47400  -14.86200 -8.37400  1.000 57.75885  ? 91  TYR   A CZ  1 
ATOM   448  O  OH  . TYR   A 1 57  ? 19.65200  -15.69000 -9.45800  1.000 52.49818  ? 91  TYR   A OH  1 
ATOM   449  N  N   . LYS   A 1 58  ? 17.32400  -10.62000 -2.79900  1.000 65.45846  ? 92  LYS   A N   1 
ATOM   450  C  CA  . LYS   A 1 58  ? 17.28200  -9.81100  -1.58500  1.000 63.57092  ? 92  LYS   A CA  1 
ATOM   451  C  C   . LYS   A 1 58  ? 16.38700  -10.45100 -0.53100  1.000 67.26891  ? 92  LYS   A C   1 
ATOM   452  O  O   . LYS   A 1 58  ? 16.68400  -10.38900 0.66800   1.000 73.94199  ? 92  LYS   A O   1 
ATOM   453  C  CB  . LYS   A 1 58  ? 16.79700  -8.39800  -1.91300  1.000 57.20304  ? 92  LYS   A CB  1 
ATOM   454  C  CG  . LYS   A 1 58  ? 17.85200  -7.31600  -1.74500  1.000 75.76254  ? 92  LYS   A CG  1 
ATOM   455  C  CD  . LYS   A 1 58  ? 19.03600  -7.54300  -2.66900  1.000 72.92037  ? 92  LYS   A CD  1 
ATOM   456  C  CE  . LYS   A 1 58  ? 20.07400  -6.44100  -2.51400  1.000 85.50107  ? 92  LYS   A CE  1 
ATOM   457  N  NZ  . LYS   A 1 58  ? 20.61900  -6.37400  -1.13100  1.000 84.95490  ? 92  LYS   A NZ  1 
ATOM   458  N  N   . HIS   A 1 59  ? 15.28600  -11.07000 -0.96100  1.000 68.28283  ? 93  HIS   A N   1 
ATOM   459  C  CA  . HIS   A 1 59  ? 14.40000  -11.75500 -0.02600  1.000 74.48785  ? 93  HIS   A CA  1 
ATOM   460  C  C   . HIS   A 1 59  ? 15.08400  -12.97000 0.58700   1.000 59.78978  ? 93  HIS   A C   1 
ATOM   461  O  O   . HIS   A 1 59  ? 14.94700  -13.22900 1.78800   1.000 68.09173  ? 93  HIS   A O   1 
ATOM   462  C  CB  . HIS   A 1 59  ? 13.10900  -12.16100 -0.74000  1.000 73.23850  ? 93  HIS   A CB  1 
ATOM   463  C  CG  . HIS   A 1 59  ? 12.04700  -12.69000 0.17100   1.000 84.73039  ? 93  HIS   A CG  1 
ATOM   464  N  ND1 . HIS   A 1 59  ? 12.12900  -12.60400 1.54500   1.000 93.72665  ? 93  HIS   A ND1 1 
ATOM   465  C  CD2 . HIS   A 1 59  ? 10.87200  -13.30900 -0.09600  1.000 78.63036  ? 93  HIS   A CD2 1 
ATOM   466  C  CE1 . HIS   A 1 59  ? 11.05300  -13.15000 2.08300   1.000 84.02628  ? 93  HIS   A CE1 1 
ATOM   467  N  NE2 . HIS   A 1 59  ? 10.27500  -13.58500 1.10900   1.000 83.84663  ? 93  HIS   A NE2 1 
ATOM   468  N  N   . LEU   A 1 60  ? 15.83000  -13.72000 -0.22000  1.000 57.37714  ? 94  LEU   A N   1 
ATOM   469  C  CA  . LEU   A 1 60  ? 16.55200  -14.89800 0.23700   1.000 58.74009  ? 94  LEU   A CA  1 
ATOM   470  C  C   . LEU   A 1 60  ? 17.96100  -14.57600 0.71600   1.000 60.75806  ? 94  LEU   A C   1 
ATOM   471  O  O   . LEU   A 1 60  ? 18.77800  -15.49200 0.85600   1.000 70.44720  ? 94  LEU   A O   1 
ATOM   472  C  CB  . LEU   A 1 60  ? 16.61100  -15.94000 -0.88300  1.000 61.95809  ? 94  LEU   A CB  1 
ATOM   473  C  CG  . LEU   A 1 60  ? 15.27400  -16.49800 -1.37200  1.000 57.00048  ? 94  LEU   A CG  1 
ATOM   474  C  CD1 . LEU   A 1 60  ? 15.46000  -17.25800 -2.67500  1.000 60.61053  ? 94  LEU   A CD1 1 
ATOM   475  C  CD2 . LEU   A 1 60  ? 14.65700  -17.39600 -0.31300  1.000 59.47729  ? 94  LEU   A CD2 1 
ATOM   476  N  N   . GLN   A 1 61  ? 18.26300  -13.30500 0.96700   1.000 62.21715  ? 95  GLN   A N   1 
ATOM   477  C  CA  . GLN   A 1 61  ? 19.60700  -12.92400 1.37700   1.000 67.68940  ? 95  GLN   A CA  1 
ATOM   478  C  C   . GLN   A 1 61  ? 19.91600  -13.46900 2.76500   1.000 66.67624  ? 95  GLN   A C   1 
ATOM   479  O  O   . GLN   A 1 61  ? 19.08700  -13.40400 3.67800   1.000 59.06632  ? 95  GLN   A O   1 
ATOM   480  C  CB  . GLN   A 1 61  ? 19.75900  -11.40400 1.35500   1.000 77.11972  ? 95  GLN   A CB  1 
ATOM   481  C  CG  . GLN   A 1 61  ? 21.16800  -10.91600 1.65100   1.000 71.50316  ? 95  GLN   A CG  1 
ATOM   482  C  CD  . GLN   A 1 61  ? 21.37900  -9.46900  1.25600   1.000 80.97190  ? 95  GLN   A CD  1 
ATOM   483  O  OE1 . GLN   A 1 61  ? 21.56600  -9.15500  0.08000   1.000 84.31988  ? 95  GLN   A OE1 1 
ATOM   484  N  NE2 . GLN   A 1 61  ? 21.34800  -8.57700  2.23900   1.000 76.60437  ? 95  GLN   A NE2 1 
ATOM   485  N  N   . GLY   A 1 62  ? 21.12100  -14.01100 2.92000   1.000 70.43101  ? 96  GLY   A N   1 
ATOM   486  C  CA  . GLY   A 1 62  ? 21.52400  -14.66900 4.14100   1.000 68.94572  ? 96  GLY   A CA  1 
ATOM   487  C  C   . GLY   A 1 62  ? 21.38600  -16.17600 4.11500   1.000 71.29696  ? 96  GLY   A C   1 
ATOM   488  O  O   . GLY   A 1 62  ? 21.90800  -16.84400 5.01500   1.000 81.94822  ? 96  GLY   A O   1 
ATOM   489  N  N   . CYS   A 1 63  ? 20.70200  -16.72800 3.11500   1.000 73.23227  ? 97  CYS   A N   1 
ATOM   490  C  CA  . CYS   A 1 63  ? 20.56000  -18.17200 2.99600   1.000 71.13546  ? 97  CYS   A CA  1 
ATOM   491  C  C   . CYS   A 1 63  ? 21.83400  -18.77800 2.42500   1.000 66.33887  ? 97  CYS   A C   1 
ATOM   492  O  O   . CYS   A 1 63  ? 22.39400  -18.26800 1.44900   1.000 54.14305  ? 97  CYS   A O   1 
ATOM   493  C  CB  . CYS   A 1 63  ? 19.36900  -18.52600 2.10700   1.000 74.65615  ? 97  CYS   A CB  1 
ATOM   494  S  SG  . CYS   A 1 63  ? 17.77200  -17.98300 2.73800   1.000 82.06063  ? 97  CYS   A SG  1 
ATOM   495  N  N   . ASP   A 1 64  ? 22.28700  -19.87000 3.03600   1.000 76.24041  ? 98  ASP   A N   1 
ATOM   496  C  CA  . ASP   A 1 64  ? 23.44400  -20.59700 2.53200   1.000 58.81637  ? 98  ASP   A CA  1 
ATOM   497  C  C   . ASP   A 1 64  ? 23.09800  -21.24600 1.19800   1.000 57.26519  ? 98  ASP   A C   1 
ATOM   498  O  O   . ASP   A 1 64  ? 22.19500  -22.08500 1.12400   1.000 62.24875  ? 98  ASP   A O   1 
ATOM   499  C  CB  . ASP   A 1 64  ? 23.88600  -21.64600 3.54800   1.000 65.75304  ? 98  ASP   A CB  1 
ATOM   500  C  CG  . ASP   A 1 64  ? 25.11900  -21.22300 4.32300   1.000 96.77959  ? 98  ASP   A CG  1 
ATOM   501  O  OD1 . ASP   A 1 64  ? 26.09000  -20.76700 3.68200   1.000 93.86717  ? 98  ASP   A OD1 1 
ATOM   502  O  OD2 . ASP   A 1 64  ? 25.11900  -21.34100 5.56700   1.000 105.11795 ? 98  ASP   A OD2 1 
ATOM   503  N  N   . GLY   A 1 65  ? 23.81200  -20.85400 0.14400   1.000 54.43861  ? 99  GLY   A N   1 
ATOM   504  C  CA  . GLY   A 1 65  ? 23.58200  -21.37100 -1.18900  1.000 52.92379  ? 99  GLY   A CA  1 
ATOM   505  C  C   . GLY   A 1 65  ? 22.93000  -20.39500 -2.14000  1.000 50.63509  ? 99  GLY   A C   1 
ATOM   506  O  O   . GLY   A 1 65  ? 22.93100  -20.64600 -3.35000  1.000 58.50258  ? 99  GLY   A O   1 
ATOM   507  N  N   . ILE   A 1 66  ? 22.36500  -19.30100 -1.64600  1.000 58.68437  ? 100 ILE   A N   1 
ATOM   508  C  CA  . ILE   A 1 66  ? 21.78000  -18.26300 -2.49100  1.000 60.58511  ? 100 ILE   A CA  1 
ATOM   509  C  C   . ILE   A 1 66  ? 22.82100  -17.16200 -2.66200  1.000 54.39516  ? 100 ILE   A C   1 
ATOM   510  O  O   . ILE   A 1 66  ? 23.28500  -16.60700 -1.65400  1.000 55.05960  ? 100 ILE   A O   1 
ATOM   511  C  CB  . ILE   A 1 66  ? 20.48200  -17.70400 -1.89100  1.000 65.88699  ? 100 ILE   A CB  1 
ATOM   512  C  CG1 . ILE   A 1 66  ? 19.48500  -18.83400 -1.63100  1.000 54.75228  ? 100 ILE   A CG1 1 
ATOM   513  C  CG2 . ILE   A 1 66  ? 19.87300  -16.66300 -2.82100  1.000 43.96180  ? 100 ILE   A CG2 1 
ATOM   514  C  CD1 . ILE   A 1 66  ? 19.09300  -19.59400 -2.87300  1.000 53.54037  ? 100 ILE   A CD1 1 
ATOM   515  N  N   . PRO   A 1 67  ? 23.21600  -16.82100 -3.88600  1.000 48.20238  ? 101 PRO   A N   1 
ATOM   516  C  CA  . PRO   A 1 67  ? 24.22900  -15.77800 -4.06400  1.000 51.25350  ? 101 PRO   A CA  1 
ATOM   517  C  C   . PRO   A 1 67  ? 23.70000  -14.41600 -3.65000  1.000 57.60641  ? 101 PRO   A C   1 
ATOM   518  O  O   . PRO   A 1 67  ? 22.49800  -14.14300 -3.70700  1.000 69.98939  ? 101 PRO   A O   1 
ATOM   519  C  CB  . PRO   A 1 67  ? 24.52600  -15.82500 -5.56700  1.000 51.18741  ? 101 PRO   A CB  1 
ATOM   520  C  CG  . PRO   A 1 67  ? 23.26600  -16.33400 -6.16600  1.000 48.51796  ? 101 PRO   A CG  1 
ATOM   521  C  CD  . PRO   A 1 67  ? 22.72500  -17.33500 -5.17700  1.000 45.94729  ? 101 PRO   A CD  1 
ATOM   522  N  N   . ASN   A 1 68  ? 24.62100  -13.56000 -3.21800  1.000 54.41361  ? 102 ASN   A N   1 
ATOM   523  C  CA  . ASN   A 1 68  ? 24.25700  -12.20300 -2.84400  1.000 47.11171  ? 102 ASN   A CA  1 
ATOM   524  C  C   . ASN   A 1 68  ? 23.96900  -11.36800 -4.08300  1.000 49.79704  ? 102 ASN   A C   1 
ATOM   525  O  O   . ASN   A 1 68  ? 24.65100  -11.48600 -5.10300  1.000 54.95968  ? 102 ASN   A O   1 
ATOM   526  C  CB  . ASN   A 1 68  ? 25.37500  -11.55200 -2.02900  1.000 49.28027  ? 102 ASN   A CB  1 
ATOM   527  C  CG  . ASN   A 1 68  ? 25.35300  -11.96600 -0.57400  1.000 55.66741  ? 102 ASN   A CG  1 
ATOM   528  O  OD1 . ASN   A 1 68  ? 24.30500  -12.31800 -0.03500  1.000 66.13040  ? 102 ASN   A OD1 1 
ATOM   529  N  ND2 . ASN   A 1 68  ? 26.51200  -11.92100 0.07400   1.000 66.50564  ? 102 ASN   A ND2 1 
ATOM   530  N  N   . ALA   A 1 69  ? 22.94500  -10.52700 -3.99200  1.000 64.29984  ? 103 ALA   A N   1 
ATOM   531  C  CA  . ALA   A 1 69  ? 22.64700  -9.53800  -5.01800  1.000 61.72987  ? 103 ALA   A CA  1 
ATOM   532  C  C   . ALA   A 1 69  ? 23.24500  -8.20400  -4.59400  1.000 58.10509  ? 103 ALA   A C   1 
ATOM   533  O  O   . ALA   A 1 69  ? 22.97800  -7.72300  -3.48800  1.000 75.87911  ? 103 ALA   A O   1 
ATOM   534  C  CB  . ALA   A 1 69  ? 21.14000  -9.40400  -5.23600  1.000 64.70815  ? 103 ALA   A CB  1 
ATOM   535  N  N   . TYR   A 1 70  ? 24.05500  -7.61400  -5.47000  1.000 55.29865  ? 104 TYR   A N   1 
ATOM   536  C  CA  . TYR   A 1 70  ? 24.78100  -6.39500  -5.14100  1.000 63.51127  ? 104 TYR   A CA  1 
ATOM   537  C  C   . TYR   A 1 70  ? 24.24400  -5.14600  -5.82100  1.000 62.76398  ? 104 TYR   A C   1 
ATOM   538  O  O   . TYR   A 1 70  ? 24.30800  -4.06800  -5.22900  1.000 64.18457  ? 104 TYR   A O   1 
ATOM   539  C  CB  . TYR   A 1 70  ? 26.26500  -6.54900  -5.49700  1.000 62.80244  ? 104 TYR   A CB  1 
ATOM   540  C  CG  . TYR   A 1 70  ? 26.97600  -7.61500  -4.69900  1.000 64.57287  ? 104 TYR   A CG  1 
ATOM   541  C  CD1 . TYR   A 1 70  ? 27.21600  -7.44700  -3.34300  1.000 64.49817  ? 104 TYR   A CD1 1 
ATOM   542  C  CD2 . TYR   A 1 70  ? 27.41400  -8.78600  -5.30300  1.000 58.72179  ? 104 TYR   A CD2 1 
ATOM   543  C  CE1 . TYR   A 1 70  ? 27.86700  -8.41700  -2.60600  1.000 63.76780  ? 104 TYR   A CE1 1 
ATOM   544  C  CE2 . TYR   A 1 70  ? 28.06700  -9.76200  -4.57500  1.000 52.85216  ? 104 TYR   A CE2 1 
ATOM   545  C  CZ  . TYR   A 1 70  ? 28.29100  -9.57200  -3.22700  1.000 61.02437  ? 104 TYR   A CZ  1 
ATOM   546  O  OH  . TYR   A 1 70  ? 28.94000  -10.53800 -2.49300  1.000 80.75936  ? 104 TYR   A OH  1 
ATOM   547  N  N   . TYR   A 1 71  ? 23.71900  -5.25400  -7.03800  1.000 62.66118  ? 105 TYR   A N   1 
ATOM   548  C  CA  . TYR   A 1 71  ? 23.29300  -4.07000  -7.76800  1.000 63.32573  ? 105 TYR   A CA  1 
ATOM   549  C  C   . TYR   A 1 71  ? 22.18200  -4.42300  -8.74500  1.000 65.49134  ? 105 TYR   A C   1 
ATOM   550  O  O   . TYR   A 1 71  ? 22.18900  -5.50000  -9.34700  1.000 67.63483  ? 105 TYR   A O   1 
ATOM   551  C  CB  . TYR   A 1 71  ? 24.46800  -3.43000  -8.51700  1.000 65.81896  ? 105 TYR   A CB  1 
ATOM   552  C  CG  . TYR   A 1 71  ? 24.04400  -2.45100  -9.58900  1.000 69.10972  ? 105 TYR   A CG  1 
ATOM   553  C  CD1 . TYR   A 1 71  ? 23.58200  -1.18500  -9.25900  1.000 71.18377  ? 105 TYR   A CD1 1 
ATOM   554  C  CD2 . TYR   A 1 71  ? 24.08700  -2.80400  -10.93200 1.000 76.06537  ? 105 TYR   A CD2 1 
ATOM   555  C  CE1 . TYR   A 1 71  ? 23.18600  -0.29200  -10.23600 1.000 78.84539  ? 105 TYR   A CE1 1 
ATOM   556  C  CE2 . TYR   A 1 71  ? 23.69200  -1.92000  -11.91500 1.000 73.65984  ? 105 TYR   A CE2 1 
ATOM   557  C  CZ  . TYR   A 1 71  ? 23.24800  -0.66300  -11.56300 1.000 73.09394  ? 105 TYR   A CZ  1 
ATOM   558  O  OH  . TYR   A 1 71  ? 22.85700  0.22500   -12.54100 1.000 101.31902 ? 105 TYR   A OH  1 
ATOM   559  N  N   . PHE   A 1 72  ? 21.23500  -3.49900  -8.89800  1.000 75.94801  ? 106 PHE   A N   1 
ATOM   560  C  CA  . PHE   A 1 72  ? 20.23000  -3.57200  -9.95000  1.000 64.91006  ? 106 PHE   A CA  1 
ATOM   561  C  C   . PHE   A 1 72  ? 19.86100  -2.15700  -10.36400 1.000 76.57033  ? 106 PHE   A C   1 
ATOM   562  O  O   . PHE   A 1 72  ? 19.60700  -1.30600  -9.50700  1.000 76.91308  ? 106 PHE   A O   1 
ATOM   563  C  CB  . PHE   A 1 72  ? 18.98300  -4.33600  -9.49500  1.000 83.00379  ? 106 PHE   A CB  1 
ATOM   564  C  CG  . PHE   A 1 72  ? 17.81300  -4.18300  -10.42500 1.000 92.08636  ? 106 PHE   A CG  1 
ATOM   565  C  CD1 . PHE   A 1 72  ? 17.89000  -4.62800  -11.73600 1.000 91.27086  ? 106 PHE   A CD1 1 
ATOM   566  C  CD2 . PHE   A 1 72  ? 16.63800  -3.59200  -9.99200  1.000 85.17704  ? 106 PHE   A CD2 1 
ATOM   567  C  CE1 . PHE   A 1 72  ? 16.81900  -4.48400  -12.59700 1.000 82.15849  ? 106 PHE   A CE1 1 
ATOM   568  C  CE2 . PHE   A 1 72  ? 15.56200  -3.44600  -10.84800 1.000 94.28559  ? 106 PHE   A CE2 1 
ATOM   569  C  CZ  . PHE   A 1 72  ? 15.65400  -3.89200  -12.15200 1.000 88.00684  ? 106 PHE   A CZ  1 
ATOM   570  N  N   . GLY   A 1 73  ? 19.83500  -1.91400  -11.66900 1.000 84.90483  ? 107 GLY   A N   1 
ATOM   571  C  CA  . GLY   A 1 73  ? 19.49400  -0.59700  -12.17500 1.000 86.93568  ? 107 GLY   A CA  1 
ATOM   572  C  C   . GLY   A 1 73  ? 19.41500  -0.60800  -13.68500 1.000 88.15936  ? 107 GLY   A C   1 
ATOM   573  O  O   . GLY   A 1 73  ? 19.58900  -1.64300  -14.33300 1.000 88.94575  ? 107 GLY   A O   1 
ATOM   574  N  N   . GLN   A 1 74  ? 19.14600  0.57100   -14.23900 1.000 100.15778 ? 108 GLN   A N   1 
ATOM   575  C  CA  . GLN   A 1 74  ? 19.04000  0.76500   -15.67900 1.000 109.51069 ? 108 GLN   A CA  1 
ATOM   576  C  C   . GLN   A 1 74  ? 20.27600  1.48800   -16.19200 1.000 107.55016 ? 108 GLN   A C   1 
ATOM   577  O  O   . GLN   A 1 74  ? 20.66200  2.52900   -15.65000 1.000 112.68188 ? 108 GLN   A O   1 
ATOM   578  C  CB  . GLN   A 1 74  ? 17.78800  1.56700   -16.04100 1.000 118.70943 ? 108 GLN   A CB  1 
ATOM   579  C  CG  . GLN   A 1 74  ? 16.47800  0.86400   -15.74800 1.000 119.53400 ? 108 GLN   A CG  1 
ATOM   580  C  CD  . GLN   A 1 74  ? 15.29300  1.59200   -16.34800 1.000 134.97971 ? 108 GLN   A CD  1 
ATOM   581  O  OE1 . GLN   A 1 74  ? 15.20700  1.76400   -17.56400 1.000 125.88153 ? 108 GLN   A OE1 1 
ATOM   582  N  NE2 . GLN   A 1 74  ? 14.37600  2.03400   -15.49600 1.000 148.53561 ? 108 GLN   A NE2 1 
ATOM   583  N  N   . GLU   A 1 75  ? 20.89300  0.93300   -17.23400 1.000 106.15094 ? 109 GLU   A N   1 
ATOM   584  C  CA  . GLU   A 1 75  ? 22.03600  1.56000   -17.89300 1.000 114.62969 ? 109 GLU   A CA  1 
ATOM   585  C  C   . GLU   A 1 75  ? 21.83500  1.42100   -19.39500 1.000 124.31584 ? 109 GLU   A C   1 
ATOM   586  O  O   . GLU   A 1 75  ? 21.96600  0.32100   -19.94200 1.000 121.36944 ? 109 GLU   A O   1 
ATOM   587  C  CB  . GLU   A 1 75  ? 23.35400  0.92700   -17.45100 1.000 111.46386 ? 109 GLU   A CB  1 
ATOM   588  C  CG  . GLU   A 1 75  ? 23.58700  0.99300   -15.95200 1.000 97.85195  ? 109 GLU   A CG  1 
ATOM   589  C  CD  . GLU   A 1 75  ? 25.05300  1.01800   -15.59000 1.000 101.13859 ? 109 GLU   A CD  1 
ATOM   590  O  OE1 . GLU   A 1 75  ? 25.88800  0.70400   -16.46300 1.000 106.88559 ? 109 GLU   A OE1 1 
ATOM   591  O  OE2 . GLU   A 1 75  ? 25.37000  1.36500   -14.43400 1.000 110.98829 ? 109 GLU   A OE2 1 
ATOM   592  N  N   . GLY   A 1 76  ? 21.51700  2.53100   -20.05700 1.000 127.44351 ? 110 GLY   A N   1 
ATOM   593  C  CA  . GLY   A 1 76  ? 21.16900  2.46100   -21.46500 1.000 134.03576 ? 110 GLY   A CA  1 
ATOM   594  C  C   . GLY   A 1 76  ? 19.80800  1.81600   -21.64500 1.000 137.74513 ? 110 GLY   A C   1 
ATOM   595  O  O   . GLY   A 1 76  ? 18.84800  2.11800   -20.92900 1.000 124.13484 ? 110 GLY   A O   1 
ATOM   596  N  N   . LEU   A 1 77  ? 19.72200  0.90600   -22.61600 1.000 141.26995 ? 111 LEU   A N   1 
ATOM   597  C  CA  . LEU   A 1 77  ? 18.50700  0.14300   -22.87100 1.000 138.76681 ? 111 LEU   A CA  1 
ATOM   598  C  C   . LEU   A 1 77  ? 18.57300  -1.25900  -22.27300 1.000 133.72636 ? 111 LEU   A C   1 
ATOM   599  O  O   . LEU   A 1 77  ? 18.01900  -2.20500  -22.84100 1.000 131.61889 ? 111 LEU   A O   1 
ATOM   600  C  CB  . LEU   A 1 77  ? 18.22400  0.07100   -24.37400 1.000 149.82439 ? 111 LEU   A CB  1 
ATOM   601  C  CG  . LEU   A 1 77  ? 19.27100  -0.54400  -25.30900 1.000 142.53172 ? 111 LEU   A CG  1 
ATOM   602  C  CD1 . LEU   A 1 77  ? 18.59100  -1.14700  -26.52800 1.000 138.44660 ? 111 LEU   A CD1 1 
ATOM   603  C  CD2 . LEU   A 1 77  ? 20.30500  0.48600   -25.74100 1.000 146.51318 ? 111 LEU   A CD2 1 
ATOM   604  N  N   . HIS   A 1 78  ? 19.23800  -1.40800  -21.12800 1.000 127.60448 ? 112 HIS   A N   1 
ATOM   605  C  CA  . HIS   A 1 78  ? 19.42600  -2.70900  -20.50400 1.000 109.01318 ? 112 HIS   A CA  1 
ATOM   606  C  C   . HIS   A 1 78  ? 19.22100  -2.61300  -19.00000 1.000 96.15088  ? 112 HIS   A C   1 
ATOM   607  O  O   . HIS   A 1 78  ? 19.69100  -1.67000  -18.35800 1.000 111.83607 ? 112 HIS   A O   1 
ATOM   608  C  CB  . HIS   A 1 78  ? 20.82600  -3.27200  -20.78600 1.000 95.12515  ? 112 HIS   A CB  1 
ATOM   609  C  CG  . HIS   A 1 78  ? 20.93400  -4.00800  -22.08500 1.000 112.15192 ? 112 HIS   A CG  1 
ATOM   610  N  ND1 . HIS   A 1 78  ? 20.29300  -5.20600  -22.31600 1.000 106.80667 ? 112 HIS   A ND1 1 
ATOM   611  C  CD2 . HIS   A 1 78  ? 21.62100  -3.72400  -23.21700 1.000 112.07043 ? 112 HIS   A CD2 1 
ATOM   612  C  CE1 . HIS   A 1 78  ? 20.57300  -5.62400  -23.53700 1.000 108.85491 ? 112 HIS   A CE1 1 
ATOM   613  N  NE2 . HIS   A 1 78  ? 21.37700  -4.74300  -24.10500 1.000 128.77216 ? 112 HIS   A NE2 1 
ATOM   614  N  N   . ASN   A 1 79  ? 18.51400  -3.59700  -18.44900 1.000 103.51082 ? 113 ASN   A N   1 
ATOM   615  C  CA  . ASN   A 1 79  ? 18.47700  -3.81700  -17.01100 1.000 93.00621  ? 113 ASN   A CA  1 
ATOM   616  C  C   . ASN   A 1 79  ? 19.62900  -4.73100  -16.61900 1.000 94.90938  ? 113 ASN   A C   1 
ATOM   617  O  O   . ASN   A 1 79  ? 19.94900  -5.68700  -17.33100 1.000 82.29149  ? 113 ASN   A O   1 
ATOM   618  C  CB  . ASN   A 1 79  ? 17.14300  -4.43000  -16.58300 1.000 96.39057  ? 113 ASN   A CB  1 
ATOM   619  C  CG  . ASN   A 1 79  ? 16.04100  -3.39800  -16.45500 1.000 111.45893 ? 113 ASN   A CG  1 
ATOM   620  O  OD1 . ASN   A 1 79  ? 15.01900  -3.47400  -17.13600 1.000 112.83891 ? 113 ASN   A OD1 1 
ATOM   621  N  ND2 . ASN   A 1 79  ? 16.24400  -2.42500  -15.57400 1.000 120.23713 ? 113 ASN   A ND2 1 
ATOM   622  N  N   . ILE   A 1 80  ? 20.25200  -4.43200  -15.48300 1.000 90.05416  ? 114 ILE   A N   1 
ATOM   623  C  CA  . ILE   A 1 80  ? 21.47700  -5.09800  -15.06100 1.000 77.49674  ? 114 ILE   A CA  1 
ATOM   624  C  C   . ILE   A 1 80  ? 21.28600  -5.63700  -13.65200 1.000 79.18347  ? 114 ILE   A C   1 
ATOM   625  O  O   . ILE   A 1 80  ? 20.84700  -4.90600  -12.75700 1.000 73.64411  ? 114 ILE   A O   1 
ATOM   626  C  CB  . ILE   A 1 80  ? 22.68400  -4.14200  -15.12200 1.000 86.09857  ? 114 ILE   A CB  1 
ATOM   627  C  CG1 . ILE   A 1 80  ? 23.11400  -3.93400  -16.57600 1.000 84.55009  ? 114 ILE   A CG1 1 
ATOM   628  C  CG2 . ILE   A 1 80  ? 23.83400  -4.66500  -14.27200 1.000 70.37157  ? 114 ILE   A CG2 1 
ATOM   629  C  CD1 . ILE   A 1 80  ? 23.88700  -2.65900  -16.80900 1.000 90.70051  ? 114 ILE   A CD1 1 
ATOM   630  N  N   . LEU   A 1 81  ? 21.60800  -6.91400  -13.45900 1.000 62.59594  ? 115 LEU   A N   1 
ATOM   631  C  CA  . LEU   A 1 81  ? 21.63200  -7.53800  -12.14400 1.000 69.39883  ? 115 LEU   A CA  1 
ATOM   632  C  C   . LEU   A 1 81  ? 23.02000  -8.10700  -11.89700 1.000 66.28214  ? 115 LEU   A C   1 
ATOM   633  O  O   . LEU   A 1 81  ? 23.55300  -8.84000  -12.73600 1.000 65.64323  ? 115 LEU   A O   1 
ATOM   634  C  CB  . LEU   A 1 81  ? 20.58200  -8.64300  -12.02400 1.000 62.49940  ? 115 LEU   A CB  1 
ATOM   635  C  CG  . LEU   A 1 81  ? 20.59500  -9.39500  -10.69200 1.000 67.66496  ? 115 LEU   A CG  1 
ATOM   636  C  CD1 . LEU   A 1 81  ? 20.36400  -8.43000  -9.54500  1.000 57.12091  ? 115 LEU   A CD1 1 
ATOM   637  C  CD2 . LEU   A 1 81  ? 19.56300  -10.51100 -10.67100 1.000 70.15257  ? 115 LEU   A CD2 1 
ATOM   638  N  N   . VAL   A 1 82  ? 23.60000  -7.76900  -10.75000 1.000 67.98809  ? 116 VAL   A N   1 
ATOM   639  C  CA  . VAL   A 1 82  ? 24.93400  -8.21800  -10.37500 1.000 60.53028  ? 116 VAL   A CA  1 
ATOM   640  C  C   . VAL   A 1 82  ? 24.80300  -9.10600  -9.14700  1.000 52.34753  ? 116 VAL   A C   1 
ATOM   641  O  O   . VAL   A 1 82  ? 24.27300  -8.67300  -8.11600  1.000 60.21119  ? 116 VAL   A O   1 
ATOM   642  C  CB  . VAL   A 1 82  ? 25.87600  -7.03600  -10.10000 1.000 56.57470  ? 116 VAL   A CB  1 
ATOM   643  C  CG1 . VAL   A 1 82  ? 27.25700  -7.53900  -9.71900  1.000 55.92583  ? 116 VAL   A CG1 1 
ATOM   644  C  CG2 . VAL   A 1 82  ? 25.94800  -6.12300  -11.31500 1.000 59.06565  ? 116 VAL   A CG2 1 
ATOM   645  N  N   . ILE   A 1 83  ? 25.27400  -10.34600 -9.25700  1.000 58.08875  ? 117 ILE   A N   1 
ATOM   646  C  CA  . ILE   A 1 83  ? 25.30000  -11.28400 -8.14800  1.000 62.40136  ? 117 ILE   A CA  1 
ATOM   647  C  C   . ILE   A 1 83  ? 26.68500  -11.91700 -8.07100  1.000 50.07290  ? 117 ILE   A C   1 
ATOM   648  O  O   . ILE   A 1 83  ? 27.55700  -11.65100 -8.89500  1.000 54.53723  ? 117 ILE   A O   1 
ATOM   649  C  CB  . ILE   A 1 83  ? 24.21500  -12.37400 -8.26700  1.000 44.77406  ? 117 ILE   A CB  1 
ATOM   650  C  CG1 . ILE   A 1 83  ? 24.35700  -13.12100 -9.59400  1.000 51.39353  ? 117 ILE   A CG1 1 
ATOM   651  C  CG2 . ILE   A 1 83  ? 22.82200  -11.77800 -8.10100  1.000 53.17496  ? 117 ILE   A CG2 1 
ATOM   652  C  CD1 . ILE   A 1 83  ? 23.77800  -14.51800 -9.56700  1.000 49.77986  ? 117 ILE   A CD1 1 
ATOM   653  N  N   . ASP   A 1 84  ? 26.87300  -12.76600 -7.06400  1.000 50.88935  ? 118 ASP   A N   1 
ATOM   654  C  CA  . ASP   A 1 84  ? 28.12800  -13.48700 -6.91000  1.000 44.47682  ? 118 ASP   A CA  1 
ATOM   655  C  C   . ASP   A 1 84  ? 28.39000  -14.37400 -8.12100  1.000 46.87591  ? 118 ASP   A C   1 
ATOM   656  O  O   . ASP   A 1 84  ? 27.46500  -14.87400 -8.76700  1.000 41.62324  ? 118 ASP   A O   1 
ATOM   657  C  CB  . ASP   A 1 84  ? 28.10000  -14.34300 -5.64300  1.000 51.07361  ? 118 ASP   A CB  1 
ATOM   658  C  CG  . ASP   A 1 84  ? 28.27100  -13.52400 -4.37700  1.000 45.37634  ? 118 ASP   A CG  1 
ATOM   659  O  OD1 . ASP   A 1 84  ? 29.14800  -12.63600 -4.35400  1.000 71.56806  ? 118 ASP   A OD1 1 
ATOM   660  O  OD2 . ASP   A 1 84  ? 27.53100  -13.77200 -3.40100  1.000 57.69204  ? 118 ASP   A OD2 1 
ATOM   661  N  N   . LEU   A 1 85  ? 29.67000  -14.56400 -8.43000  1.000 44.98165  ? 119 LEU   A N   1 
ATOM   662  C  CA  . LEU   A 1 85  ? 30.07700  -15.49000 -9.47500  1.000 47.45415  ? 119 LEU   A CA  1 
ATOM   663  C  C   . LEU   A 1 85  ? 30.29800  -16.86900 -8.86900  1.000 52.32670  ? 119 LEU   A C   1 
ATOM   664  O  O   . LEU   A 1 85  ? 30.90900  -17.00500 -7.80500  1.000 49.57780  ? 119 LEU   A O   1 
ATOM   665  C  CB  . LEU   A 1 85  ? 31.35000  -15.00700 -10.17000 1.000 47.18736  ? 119 LEU   A CB  1 
ATOM   666  C  CG  . LEU   A 1 85  ? 31.81100  -15.84500 -11.36500 1.000 56.94151  ? 119 LEU   A CG  1 
ATOM   667  C  CD1 . LEU   A 1 85  ? 30.75400  -15.84900 -12.46000 1.000 46.99891  ? 119 LEU   A CD1 1 
ATOM   668  C  CD2 . LEU   A 1 85  ? 33.14200  -15.34300 -11.90200 1.000 46.38401  ? 119 LEU   A CD2 1 
ATOM   669  N  N   . LEU   A 1 86  ? 29.79000  -17.89100 -9.55100  1.000 50.55076  ? 120 LEU   A N   1 
ATOM   670  C  CA  . LEU   A 1 86  ? 29.84100  -19.26300 -9.06900  1.000 48.95558  ? 120 LEU   A CA  1 
ATOM   671  C  C   . LEU   A 1 86  ? 30.42600  -20.15700 -10.15600 1.000 53.18542  ? 120 LEU   A C   1 
ATOM   672  O  O   . LEU   A 1 86  ? 30.69100  -19.72000 -11.27900 1.000 52.62422  ? 120 LEU   A O   1 
ATOM   673  C  CB  . LEU   A 1 86  ? 28.45000  -19.74300 -8.63700  1.000 45.91218  ? 120 LEU   A CB  1 
ATOM   674  C  CG  . LEU   A 1 86  ? 27.84900  -18.98500 -7.45100  1.000 47.78857  ? 120 LEU   A CG  1 
ATOM   675  C  CD1 . LEU   A 1 86  ? 26.37900  -19.32300 -7.28500  1.000 44.42830  ? 120 LEU   A CD1 1 
ATOM   676  C  CD2 . LEU   A 1 86  ? 28.61800  -19.29400 -6.17500  1.000 39.02949  ? 120 LEU   A CD2 1 
ATOM   677  N  N   . GLY   A 1 87  ? 30.62700  -21.42600 -9.80900  1.000 57.49434  ? 121 GLY   A N   1 
ATOM   678  C  CA  . GLY   A 1 87  ? 31.25600  -22.37200 -10.69800 1.000 49.55943  ? 121 GLY   A CA  1 
ATOM   679  C  C   . GLY   A 1 87  ? 30.27900  -23.04400 -11.64000 1.000 44.03266  ? 121 GLY   A C   1 
ATOM   680  O  O   . GLY   A 1 87  ? 29.18500  -22.54000 -11.90700 1.000 49.72793  ? 121 GLY   A O   1 
ATOM   681  N  N   . PRO   A 1 88  ? 30.66300  -24.20700 -12.16100 1.000 58.70939  ? 122 PRO   A N   1 
ATOM   682  C  CA  . PRO   A 1 88  ? 29.81600  -24.89600 -13.13900 1.000 62.63302  ? 122 PRO   A CA  1 
ATOM   683  C  C   . PRO   A 1 88  ? 28.54900  -25.44300 -12.50200 1.000 40.25683  ? 122 PRO   A C   1 
ATOM   684  O  O   . PRO   A 1 88  ? 28.44400  -25.60600 -11.28400 1.000 37.95944  ? 122 PRO   A O   1 
ATOM   685  C  CB  . PRO   A 1 88  ? 30.71000  -26.03500 -13.65000 1.000 57.80272  ? 122 PRO   A CB  1 
ATOM   686  C  CG  . PRO   A 1 88  ? 32.09800  -25.70400 -13.17300 1.000 52.75577  ? 122 PRO   A CG  1 
ATOM   687  C  CD  . PRO   A 1 88  ? 31.91800  -24.93000 -11.91300 1.000 47.61486  ? 122 PRO   A CD  1 
ATOM   688  N  N   . SER   A 1 89  ? 27.57300  -25.73000 -13.35800 1.000 36.26357  ? 123 SER   A N   1 
ATOM   689  C  CA  . SER   A 1 89  ? 26.33000  -26.32900 -12.90600 1.000 46.61444  ? 123 SER   A CA  1 
ATOM   690  C  C   . SER   A 1 89  ? 26.50600  -27.83400 -12.72100 1.000 48.59771  ? 123 SER   A C   1 
ATOM   691  O  O   . SER   A 1 89  ? 27.47200  -28.43800 -13.19400 1.000 41.38950  ? 123 SER   A O   1 
ATOM   692  C  CB  . SER   A 1 89  ? 25.19900  -26.04600 -13.89800 1.000 40.37017  ? 123 SER   A CB  1 
ATOM   693  O  OG  . SER   A 1 89  ? 25.46500  -26.61000 -15.17100 1.000 41.34792  ? 123 SER   A OG  1 
ATOM   694  N  N   . LEU   A 1 90  ? 25.55700  -28.43800 -12.00300 1.000 50.71849  ? 124 LEU   A N   1 
ATOM   695  C  CA  . LEU   A 1 90  ? 25.56600  -29.88800 -11.85900 1.000 41.73651  ? 124 LEU   A CA  1 
ATOM   696  C  C   . LEU   A 1 90  ? 25.35600  -30.58300 -13.19400 1.000 40.63347  ? 124 LEU   A C   1 
ATOM   697  O  O   . LEU   A 1 90  ? 25.76700  -31.73600 -13.35200 1.000 48.40493  ? 124 LEU   A O   1 
ATOM   698  C  CB  . LEU   A 1 90  ? 24.49800  -30.33000 -10.86100 1.000 40.32303  ? 124 LEU   A CB  1 
ATOM   699  C  CG  . LEU   A 1 90  ? 24.74200  -29.87100 -9.42400  1.000 35.75806  ? 124 LEU   A CG  1 
ATOM   700  C  CD1 . LEU   A 1 90  ? 23.60400  -30.30600 -8.52800  1.000 35.63041  ? 124 LEU   A CD1 1 
ATOM   701  C  CD2 . LEU   A 1 90  ? 26.06900  -30.41200 -8.91400  1.000 40.18806  ? 124 LEU   A CD2 1 
ATOM   702  N  N   . GLU   A 1 91  ? 24.73100  -29.90400 -14.15900 1.000 48.88486  ? 125 GLU   A N   1 
ATOM   703  C  CA  . GLU   A 1 91  ? 24.65900  -30.44500 -15.51000 1.000 46.20594  ? 125 GLU   A CA  1 
ATOM   704  C  C   . GLU   A 1 91  ? 26.02700  -30.42900 -16.17900 1.000 52.16190  ? 125 GLU   A C   1 
ATOM   705  O  O   . GLU   A 1 91  ? 26.38500  -31.37000 -16.89600 1.000 47.83989  ? 125 GLU   A O   1 
ATOM   706  C  CB  . GLU   A 1 91  ? 23.64400  -29.65700 -16.33700 1.000 47.73925  ? 125 GLU   A CB  1 
ATOM   707  C  CG  . GLU   A 1 91  ? 23.53600  -30.09700 -17.78700 1.000 50.92057  ? 125 GLU   A CG  1 
ATOM   708  C  CD  . GLU   A 1 91  ? 22.89100  -31.46100 -17.94300 1.000 58.81037  ? 125 GLU   A CD  1 
ATOM   709  O  OE1 . GLU   A 1 91  ? 22.13900  -31.87200 -17.03500 1.000 63.13283  ? 125 GLU   A OE1 1 
ATOM   710  O  OE2 . GLU   A 1 91  ? 23.13600  -32.12400 -18.97400 1.000 48.27650  ? 125 GLU   A OE2 1 
ATOM   711  N  N   . ASP   A 1 92  ? 26.81000  -29.37000 -15.94900 1.000 46.32193  ? 126 ASP   A N   1 
ATOM   712  C  CA  . ASP   A 1 92  ? 28.16300  -29.31400 -16.49400 1.000 48.84996  ? 126 ASP   A CA  1 
ATOM   713  C  C   . ASP   A 1 92  ? 29.03300  -30.41900 -15.90800 1.000 43.18495  ? 126 ASP   A C   1 
ATOM   714  O  O   . ASP   A 1 92  ? 29.68500  -31.17000 -16.64300 1.000 48.85277  ? 126 ASP   A O   1 
ATOM   715  C  CB  . ASP   A 1 92  ? 28.78600  -27.94300 -16.22200 1.000 51.84023  ? 126 ASP   A CB  1 
ATOM   716  C  CG  . ASP   A 1 92  ? 28.09800  -26.82900 -16.98000 1.000 55.09900  ? 126 ASP   A CG  1 
ATOM   717  O  OD1 . ASP   A 1 92  ? 27.68200  -27.06100 -18.13400 1.000 57.86031  ? 126 ASP   A OD1 1 
ATOM   718  O  OD2 . ASP   A 1 92  ? 27.97300  -25.71900 -16.42000 1.000 52.68444  ? 126 ASP   A OD2 1 
ATOM   719  N  N   . LEU   A 1 93  ? 29.05700  -30.52800 -14.57800 1.000 42.05466  ? 127 LEU   A N   1 
ATOM   720  C  CA  . LEU   A 1 93  ? 29.82500  -31.58700 -13.93400 1.000 43.52407  ? 127 LEU   A CA  1 
ATOM   721  C  C   . LEU   A 1 93  ? 29.29100  -32.96300 -14.30400 1.000 51.99188  ? 127 LEU   A C   1 
ATOM   722  O  O   . LEU   A 1 93  ? 30.05400  -33.93500 -14.34300 1.000 50.82063  ? 127 LEU   A O   1 
ATOM   723  C  CB  . LEU   A 1 93  ? 29.80400  -31.39200 -12.41800 1.000 41.63756  ? 127 LEU   A CB  1 
ATOM   724  C  CG  . LEU   A 1 93  ? 30.22500  -30.00100 -11.93800 1.000 41.34290  ? 127 LEU   A CG  1 
ATOM   725  C  CD1 . LEU   A 1 93  ? 29.77000  -29.76800 -10.51000 1.000 48.95845  ? 127 LEU   A CD1 1 
ATOM   726  C  CD2 . LEU   A 1 93  ? 31.72900  -29.83000 -12.05400 1.000 41.58114  ? 127 LEU   A CD2 1 
ATOM   727  N  N   . PHE   A 1 94  ? 27.98700  -33.06400 -14.57200 1.000 54.31405  ? 128 PHE   A N   1 
ATOM   728  C  CA  . PHE   A 1 94  ? 27.40900  -34.31600 -15.04900 1.000 41.28006  ? 128 PHE   A CA  1 
ATOM   729  C  C   . PHE   A 1 94  ? 28.05000  -34.74100 -16.36400 1.000 48.80427  ? 128 PHE   A C   1 
ATOM   730  O  O   . PHE   A 1 94  ? 28.53200  -35.87100 -16.49600 1.000 50.96873  ? 128 PHE   A O   1 
ATOM   731  C  CB  . PHE   A 1 94  ? 25.89600  -34.15300 -15.20500 1.000 47.99110  ? 128 PHE   A CB  1 
ATOM   732  C  CG  . PHE   A 1 94  ? 25.14900  -35.44200 -15.38000 1.000 49.33206  ? 128 PHE   A CG  1 
ATOM   733  C  CD1 . PHE   A 1 94  ? 25.17700  -36.41900 -14.39800 1.000 43.75455  ? 128 PHE   A CD1 1 
ATOM   734  C  CD2 . PHE   A 1 94  ? 24.38200  -35.66000 -16.51300 1.000 46.03876  ? 128 PHE   A CD2 1 
ATOM   735  C  CE1 . PHE   A 1 94  ? 24.47400  -37.59800 -14.55600 1.000 45.32049  ? 128 PHE   A CE1 1 
ATOM   736  C  CE2 . PHE   A 1 94  ? 23.67600  -36.83600 -16.67500 1.000 45.53224  ? 128 PHE   A CE2 1 
ATOM   737  C  CZ  . PHE   A 1 94  ? 23.72100  -37.80600 -15.69500 1.000 43.13974  ? 128 PHE   A CZ  1 
ATOM   738  N  N   . ASP   A 1 95  ? 28.07900  -33.83400 -17.34500 1.000 41.05435  ? 129 ASP   A N   1 
ATOM   739  C  CA  . ASP   A 1 95  ? 28.71000  -34.13500 -18.62700 1.000 54.24201  ? 129 ASP   A CA  1 
ATOM   740  C  C   . ASP   A 1 95  ? 30.17400  -34.52300 -18.45400 1.000 52.78257  ? 129 ASP   A C   1 
ATOM   741  O  O   . ASP   A 1 95  ? 30.66700  -35.43400 -19.12900 1.000 62.38341  ? 129 ASP   A O   1 
ATOM   742  C  CB  . ASP   A 1 95  ? 28.59200  -32.93200 -19.56500 1.000 54.04032  ? 129 ASP   A CB  1 
ATOM   743  C  CG  . ASP   A 1 95  ? 27.32000  -32.95200 -20.38400 1.000 64.69898  ? 129 ASP   A CG  1 
ATOM   744  O  OD1 . ASP   A 1 95  ? 26.92900  -34.04400 -20.84500 1.000 77.10089  ? 129 ASP   A OD1 1 
ATOM   745  O  OD2 . ASP   A 1 95  ? 26.71400  -31.87600 -20.57100 1.000 80.31511  ? 129 ASP   A OD2 1 
ATOM   746  N  N   . TRP   A 1 96  ? 30.88300  -33.84400 -17.55000 1.000 46.50587  ? 130 TRP   A N   1 
ATOM   747  C  CA  . TRP   A 1 96  ? 32.31200  -34.08100 -17.38600 1.000 53.85619  ? 130 TRP   A CA  1 
ATOM   748  C  C   . TRP   A 1 96  ? 32.61000  -35.39800 -16.68100 1.000 47.45199  ? 130 TRP   A C   1 
ATOM   749  O  O   . TRP   A 1 96  ? 33.71900  -35.92400 -16.82400 1.000 47.37824  ? 130 TRP   A O   1 
ATOM   750  C  CB  . TRP   A 1 96  ? 32.94200  -32.91400 -16.62400 1.000 50.13149  ? 130 TRP   A CB  1 
ATOM   751  C  CG  . TRP   A 1 96  ? 32.80800  -31.60400 -17.34400 1.000 66.82952  ? 130 TRP   A CG  1 
ATOM   752  C  CD1 . TRP   A 1 96  ? 32.66300  -31.42100 -18.68900 1.000 68.75737  ? 130 TRP   A CD1 1 
ATOM   753  C  CD2 . TRP   A 1 96  ? 32.79200  -30.29600 -16.75900 1.000 70.26707  ? 130 TRP   A CD2 1 
ATOM   754  N  NE1 . TRP   A 1 96  ? 32.56600  -30.08100 -18.97800 1.000 77.21574  ? 130 TRP   A NE1 1 
ATOM   755  C  CE2 . TRP   A 1 96  ? 32.64200  -29.36900 -17.81000 1.000 74.97727  ? 130 TRP   A CE2 1 
ATOM   756  C  CE3 . TRP   A 1 96  ? 32.89300  -29.81900 -15.44900 1.000 52.37966  ? 130 TRP   A CE3 1 
ATOM   757  C  CZ2 . TRP   A 1 96  ? 32.59100  -27.99400 -17.59100 1.000 74.18899  ? 130 TRP   A CZ2 1 
ATOM   758  C  CZ3 . TRP   A 1 96  ? 32.84100  -28.45300 -15.23500 1.000 66.56429  ? 130 TRP   A CZ3 1 
ATOM   759  C  CH2 . TRP   A 1 96  ? 32.69300  -27.55700 -16.30000 1.000 77.62999  ? 130 TRP   A CH2 1 
ATOM   760  N  N   . CYS   A 1 97  ? 31.65300  -35.94400 -15.93100 1.000 57.74507  ? 131 CYS   A N   1 
ATOM   761  C  CA  . CYS   A 1 97  ? 31.82400  -37.21700 -15.24700 1.000 43.71255  ? 131 CYS   A CA  1 
ATOM   762  C  C   . CYS   A 1 97  ? 31.26800  -38.38900 -16.05000 1.000 43.06083  ? 131 CYS   A C   1 
ATOM   763  O  O   . CYS   A 1 97  ? 31.03000  -39.46200 -15.48500 1.000 50.13402  ? 131 CYS   A O   1 
ATOM   764  C  CB  . CYS   A 1 97  ? 31.17200  -37.16500 -13.86500 1.000 57.33342  ? 131 CYS   A CB  1 
ATOM   765  S  SG  . CYS   A 1 97  ? 31.93600  -35.99300 -12.72000 1.000 46.21387  ? 131 CYS   A SG  1 
ATOM   766  N  N   . GLY   A 1 98  ? 31.06000  -38.20800 -17.35300 1.000 45.80290  ? 132 GLY   A N   1 
ATOM   767  C  CA  . GLY   A 1 98  ? 30.52800  -39.27300 -18.18000 1.000 50.52405  ? 132 GLY   A CA  1 
ATOM   768  C  C   . GLY   A 1 98  ? 29.02400  -39.39300 -18.17000 1.000 55.83124  ? 132 GLY   A C   1 
ATOM   769  O  O   . GLY   A 1 98  ? 28.49500  -40.44200 -18.55400 1.000 58.04160  ? 132 GLY   A O   1 
ATOM   770  N  N   . ARG   A 1 99  ? 28.31900  -38.34800 -17.73500 1.000 51.56142  ? 133 ARG   A N   1 
ATOM   771  C  CA  . ARG   A 1 99  ? 26.85800  -38.33000 -17.66200 1.000 51.04104  ? 133 ARG   A CA  1 
ATOM   772  C  C   . ARG   A 1 99  ? 26.33200  -39.46300 -16.78200 1.000 55.17018  ? 133 ARG   A C   1 
ATOM   773  O  O   . ARG   A 1 99  ? 25.39300  -40.17800 -17.13700 1.000 43.42753  ? 133 ARG   A O   1 
ATOM   774  C  CB  . ARG   A 1 99  ? 26.23500  -38.36800 -19.06000 1.000 49.28650  ? 133 ARG   A CB  1 
ATOM   775  C  CG  . ARG   A 1 99  ? 26.55900  -37.13200 -19.88500 1.000 43.03502  ? 133 ARG   A CG  1 
ATOM   776  C  CD  . ARG   A 1 99  ? 25.69700  -37.04100 -21.12900 1.000 60.26501  ? 133 ARG   A CD  1 
ATOM   777  N  NE  . ARG   A 1 99  ? 24.27500  -37.01600 -20.80800 1.000 64.94858  ? 133 ARG   A NE  1 
ATOM   778  C  CZ  . ARG   A 1 99  ? 23.61200  -35.93700 -20.41300 1.000 65.11863  ? 133 ARG   A CZ  1 
ATOM   779  N  NH1 . ARG   A 1 99  ? 24.21900  -34.77300 -20.24800 1.000 61.64977  ? 133 ARG   A NH1 1 
ATOM   780  N  NH2 . ARG   A 1 99  ? 22.30700  -36.02800 -20.17900 1.000 61.77240  ? 133 ARG   A NH2 1 
ATOM   781  N  N   . ARG   A 1 100 ? 26.95100  -39.61100 -15.61000 1.000 50.59723  ? 134 ARG   A N   1 
ATOM   782  C  CA  . ARG   A 1 100 ? 26.48600  -40.53200 -14.57900 1.000 45.63228  ? 134 ARG   A CA  1 
ATOM   783  C  C   . ARG   A 1 100 ? 27.16300  -40.21600 -13.25300 1.000 48.33322  ? 134 ARG   A C   1 
ATOM   784  O  O   . ARG   A 1 100 ? 28.39500  -40.21900 -13.16600 1.000 54.33994  ? 134 ARG   A O   1 
ATOM   785  C  CB  . ARG   A 1 100 ? 26.76100  -41.98500 -14.97200 1.000 55.65030  ? 134 ARG   A CB  1 
ATOM   786  C  CG  . ARG   A 1 100 ? 26.03600  -43.00300 -14.10500 1.000 58.38994  ? 134 ARG   A CG  1 
ATOM   787  C  CD  . ARG   A 1 100 ? 26.88200  -44.24600 -13.89200 1.000 77.32695  ? 134 ARG   A CD  1 
ATOM   788  N  NE  . ARG   A 1 100 ? 26.07300  -45.41900 -13.58500 1.000 74.90448  ? 134 ARG   A NE  1 
ATOM   789  C  CZ  . ARG   A 1 100 ? 25.56500  -46.23300 -14.50100 1.000 83.81661  ? 134 ARG   A CZ  1 
ATOM   790  N  NH1 . ARG   A 1 100 ? 25.75400  -46.02200 -15.79200 1.000 83.64695  ? 134 ARG   A NH1 1 
ATOM   791  N  NH2 . ARG   A 1 100 ? 24.85100  -47.28400 -14.11100 1.000 93.81595  ? 134 ARG   A NH2 1 
ATOM   792  N  N   . PHE   A 1 101 ? 26.37700  -39.94000 -12.21800 1.000 40.28342  ? 135 PHE   A N   1 
ATOM   793  C  CA  . PHE   A 1 101 ? 26.90400  -39.67800 -10.88700 1.000 47.12892  ? 135 PHE   A CA  1 
ATOM   794  C  C   . PHE   A 1 101 ? 26.79800  -40.93200 -10.03000 1.000 44.18707  ? 135 PHE   A C   1 
ATOM   795  O  O   . PHE   A 1 101 ? 25.82600  -41.68700 -10.13200 1.000 49.86289  ? 135 PHE   A O   1 
ATOM   796  C  CB  . PHE   A 1 101 ? 26.15900  -38.52300 -10.21200 1.000 42.28302  ? 135 PHE   A CB  1 
ATOM   797  C  CG  . PHE   A 1 101 ? 26.62400  -37.15900 -10.64200 1.000 45.25636  ? 135 PHE   A CG  1 
ATOM   798  C  CD1 . PHE   A 1 101 ? 27.90400  -36.96800 -11.13400 1.000 47.24384  ? 135 PHE   A CD1 1 
ATOM   799  C  CD2 . PHE   A 1 101 ? 25.77900  -36.06400 -10.54300 1.000 42.26933  ? 135 PHE   A CD2 1 
ATOM   800  C  CE1 . PHE   A 1 101 ? 28.33100  -35.71000 -11.52500 1.000 48.87391  ? 135 PHE   A CE1 1 
ATOM   801  C  CE2 . PHE   A 1 101 ? 26.20100  -34.80600 -10.93200 1.000 46.28498  ? 135 PHE   A CE2 1 
ATOM   802  C  CZ  . PHE   A 1 101 ? 27.47800  -34.62900 -11.42400 1.000 45.03712  ? 135 PHE   A CZ  1 
ATOM   803  N  N   . SER   A 1 102 ? 27.80400  -41.14800 -9.18700  1.000 43.03550  ? 136 SER   A N   1 
ATOM   804  C  CA  . SER   A 1 102 ? 27.77800  -42.26500 -8.25800  1.000 47.73676  ? 136 SER   A CA  1 
ATOM   805  C  C   . SER   A 1 102 ? 26.64900  -42.08800 -7.24700  1.000 48.76603  ? 136 SER   A C   1 
ATOM   806  O  O   . SER   A 1 102 ? 26.09300  -41.00000 -7.07800  1.000 54.08763  ? 136 SER   A O   1 
ATOM   807  C  CB  . SER   A 1 102 ? 29.11500  -42.38700 -7.53100  1.000 42.98990  ? 136 SER   A CB  1 
ATOM   808  O  OG  . SER   A 1 102 ? 29.39200  -41.21300 -6.78800  1.000 41.79493  ? 136 SER   A OG  1 
ATOM   809  N  N   . VAL   A 1 103 ? 26.31300  -43.18500 -6.56600  1.000 46.98960  ? 137 VAL   A N   1 
ATOM   810  C  CA  . VAL   A 1 103 ? 25.25000  -43.14100 -5.56500  1.000 50.92753  ? 137 VAL   A CA  1 
ATOM   811  C  C   . VAL   A 1 103 ? 25.62000  -42.18700 -4.43600  1.000 44.42897  ? 137 VAL   A C   1 
ATOM   812  O  O   . VAL   A 1 103 ? 24.78500  -41.40300 -3.96700  1.000 39.80590  ? 137 VAL   A O   1 
ATOM   813  C  CB  . VAL   A 1 103 ? 24.95400  -44.55800 -5.04000  1.000 41.62977  ? 137 VAL   A CB  1 
ATOM   814  C  CG1 . VAL   A 1 103 ? 23.93600  -44.50600 -3.92000  1.000 30.94086  ? 137 VAL   A CG1 1 
ATOM   815  C  CG2 . VAL   A 1 103 ? 24.45800  -45.44800 -6.16900  1.000 34.73779  ? 137 VAL   A CG2 1 
ATOM   816  N  N   . LYS   A 1 104 ? 26.87700  -42.23000 -3.99100  1.000 43.14195  ? 138 LYS   A N   1 
ATOM   817  C  CA  . LYS   A 1 104 ? 27.31700  -41.35200 -2.91200  1.000 49.72385  ? 138 LYS   A CA  1 
ATOM   818  C  C   . LYS   A 1 104 ? 27.23100  -39.88700 -3.32100  1.000 49.15912  ? 138 LYS   A C   1 
ATOM   819  O  O   . LYS   A 1 104 ? 26.79800  -39.03800 -2.53200  1.000 50.31535  ? 138 LYS   A O   1 
ATOM   820  C  CB  . LYS   A 1 104 ? 28.74300  -41.71400 -2.49900  1.000 41.67763  ? 138 LYS   A CB  1 
ATOM   821  C  CG  . LYS   A 1 104 ? 29.38000  -40.76700 -1.50200  1.000 46.44014  ? 138 LYS   A CG  1 
ATOM   822  C  CD  . LYS   A 1 104 ? 30.81400  -41.18100 -1.21900  1.000 45.86944  ? 138 LYS   A CD  1 
ATOM   823  C  CE  . LYS   A 1 104 ? 31.49500  -40.21700 -0.26700  1.000 51.74949  ? 138 LYS   A CE  1 
ATOM   824  N  NZ  . LYS   A 1 104 ? 32.87400  -40.66300 0.07600   1.000 56.86295  ? 138 LYS   A NZ  1 
ATOM   825  N  N   . THR   A 1 105 ? 27.63700  -39.57000 -4.55300  1.000 46.30855  ? 139 THR   A N   1 
ATOM   826  C  CA  . THR   A 1 105 ? 27.54600  -38.19100 -5.02400  1.000 49.09064  ? 139 THR   A CA  1 
ATOM   827  C  C   . THR   A 1 105 ? 26.09400  -37.74300 -5.14100  1.000 44.06413  ? 139 THR   A C   1 
ATOM   828  O  O   . THR   A 1 105 ? 25.75600  -36.61800 -4.75700  1.000 40.18603  ? 139 THR   A O   1 
ATOM   829  C  CB  . THR   A 1 105 ? 28.26900  -38.04400 -6.36400  1.000 43.35664  ? 139 THR   A CB  1 
ATOM   830  O  OG1 . THR   A 1 105 ? 29.68300  -38.10000 -6.14900  1.000 55.24730  ? 139 THR   A OG1 1 
ATOM   831  C  CG2 . THR   A 1 105 ? 27.92200  -36.71900 -7.02800  1.000 39.56960  ? 139 THR   A CG2 1 
ATOM   832  N  N   . VAL   A 1 106 ? 25.22000  -38.61400 -5.65100  1.000 44.66891  ? 140 VAL   A N   1 
ATOM   833  C  CA  . VAL   A 1 106 ? 23.81200  -38.25200 -5.79700  1.000 37.92328  ? 140 VAL   A CA  1 
ATOM   834  C  C   . VAL   A 1 106 ? 23.18200  -37.98900 -4.43700  1.000 36.76403  ? 140 VAL   A C   1 
ATOM   835  O  O   . VAL   A 1 106 ? 22.40900  -37.03900 -4.27000  1.000 42.71809  ? 140 VAL   A O   1 
ATOM   836  C  CB  . VAL   A 1 106 ? 23.05300  -39.34600 -6.57100  1.000 36.33590  ? 140 VAL   A CB  1 
ATOM   837  C  CG1 . VAL   A 1 106 ? 21.55300  -39.09500 -6.51400  1.000 35.98856  ? 140 VAL   A CG1 1 
ATOM   838  C  CG2 . VAL   A 1 106 ? 23.51900  -39.38600 -8.00700  1.000 26.98284  ? 140 VAL   A CG2 1 
ATOM   839  N  N   . VAL   A 1 107 ? 23.50800  -38.81500 -3.44100  1.000 37.24600  ? 141 VAL   A N   1 
ATOM   840  C  CA  . VAL   A 1 107 ? 22.91400  -38.65700 -2.11400  1.000 36.21405  ? 141 VAL   A CA  1 
ATOM   841  C  C   . VAL   A 1 107 ? 23.34400  -37.33500 -1.49000  1.000 52.13990  ? 141 VAL   A C   1 
ATOM   842  O  O   . VAL   A 1 107 ? 22.51200  -36.55500 -1.00900  1.000 54.26513  ? 141 VAL   A O   1 
ATOM   843  C  CB  . VAL   A 1 107 ? 23.28200  -39.85100 -1.21600  1.000 44.81203  ? 141 VAL   A CB  1 
ATOM   844  C  CG1 . VAL   A 1 107 ? 22.97700  -39.53400 0.23900   1.000 35.93550  ? 141 VAL   A CG1 1 
ATOM   845  C  CG2 . VAL   A 1 107 ? 22.53400  -41.09900 -1.66100  1.000 44.05869  ? 141 VAL   A CG2 1 
ATOM   846  N  N   . GLN   A 1 108 ? 24.65100  -37.06400 -1.48800  1.000 51.47017  ? 142 GLN   A N   1 
ATOM   847  C  CA  . GLN   A 1 108 ? 25.15400  -35.84100 -0.86800  1.000 47.28031  ? 142 GLN   A CA  1 
ATOM   848  C  C   . GLN   A 1 108 ? 24.65900  -34.60300 -1.60500  1.000 49.12694  ? 142 GLN   A C   1 
ATOM   849  O  O   . GLN   A 1 108 ? 24.31200  -33.59400 -0.97900  1.000 45.96099  ? 142 GLN   A O   1 
ATOM   850  C  CB  . GLN   A 1 108 ? 26.68000  -35.86600 -0.82900  1.000 36.51989  ? 142 GLN   A CB  1 
ATOM   851  C  CG  . GLN   A 1 108 ? 27.26200  -37.00000 -0.00700  1.000 54.81779  ? 142 GLN   A CG  1 
ATOM   852  C  CD  . GLN   A 1 108 ? 28.77200  -37.05700 -0.09500  1.000 46.52429  ? 142 GLN   A CD  1 
ATOM   853  O  OE1 . GLN   A 1 108 ? 29.45800  -37.25900 0.90600   1.000 63.94777  ? 142 GLN   A OE1 1 
ATOM   854  N  NE2 . GLN   A 1 108 ? 29.30000  -36.88000 -1.30100  1.000 48.70950  ? 142 GLN   A NE2 1 
ATOM   855  N  N   . VAL   A 1 109 ? 24.62300  -34.66000 -2.93700  1.000 43.47572  ? 143 VAL   A N   1 
ATOM   856  C  CA  . VAL   A 1 109 ? 24.08500  -33.54800 -3.71100  1.000 31.63271  ? 143 VAL   A CA  1 
ATOM   857  C  C   . VAL   A 1 109 ? 22.59100  -33.38900 -3.45300  1.000 49.50412  ? 143 VAL   A C   1 
ATOM   858  O  O   . VAL   A 1 109 ? 22.06900  -32.26700 -3.45000  1.000 48.48776  ? 143 VAL   A O   1 
ATOM   859  C  CB  . VAL   A 1 109 ? 24.39400  -33.75500 -5.20600  1.000 33.63674  ? 143 VAL   A CB  1 
ATOM   860  C  CG1 . VAL   A 1 109 ? 23.55900  -32.84000 -6.06600  1.000 51.37742  ? 143 VAL   A CG1 1 
ATOM   861  C  CG2 . VAL   A 1 109 ? 25.87200  -33.51900 -5.47500  1.000 52.23963  ? 143 VAL   A CG2 1 
ATOM   862  N  N   . ALA   A 1 110 ? 21.88800  -34.49400 -3.19500  1.000 47.78071  ? 144 ALA   A N   1 
ATOM   863  C  CA  . ALA   A 1 110 ? 20.44100  -34.43100 -3.01500  1.000 39.02590  ? 144 ALA   A CA  1 
ATOM   864  C  C   . ALA   A 1 110 ? 20.06500  -33.75100 -1.70500  1.000 46.29414  ? 144 ALA   A C   1 
ATOM   865  O  O   . ALA   A 1 110 ? 19.11900  -32.95700 -1.66400  1.000 43.21594  ? 144 ALA   A O   1 
ATOM   866  C  CB  . ALA   A 1 110 ? 19.84200  -35.83500 -3.06900  1.000 37.54671  ? 144 ALA   A CB  1 
ATOM   867  N  N   . ILE   A 1 111 ? 20.78200  -34.05800 -0.62000  1.000 38.76358  ? 145 ILE   A N   1 
ATOM   868  C  CA  . ILE   A 1 111 ? 20.41900  -33.48400 0.67200   1.000 48.60280  ? 145 ILE   A CA  1 
ATOM   869  C  C   . ILE   A 1 111 ? 20.71700  -31.99100 0.70400   1.000 47.04085  ? 145 ILE   A C   1 
ATOM   870  O  O   . ILE   A 1 111 ? 20.08200  -31.24200 1.45600   1.000 57.14239  ? 145 ILE   A O   1 
ATOM   871  C  CB  . ILE   A 1 111 ? 21.12700  -34.23000 1.81900   1.000 44.04933  ? 145 ILE   A CB  1 
ATOM   872  C  CG1 . ILE   A 1 111 ? 22.64600  -34.11100 1.69500   1.000 55.97708  ? 145 ILE   A CG1 1 
ATOM   873  C  CG2 . ILE   A 1 111 ? 20.70400  -35.69200 1.84100   1.000 48.23630  ? 145 ILE   A CG2 1 
ATOM   874  C  CD1 . ILE   A 1 111 ? 23.40200  -34.84300 2.78600   1.000 61.01129  ? 145 ILE   A CD1 1 
ATOM   875  N  N   . GLN   A 1 112 ? 21.67200  -31.52900 -0.10300  1.000 49.78476  ? 146 GLN   A N   1 
ATOM   876  C  CA  . GLN   A 1 112 ? 21.90900  -30.09600 -0.20900  1.000 46.06428  ? 146 GLN   A CA  1 
ATOM   877  C  C   . GLN   A 1 112 ? 20.85700  -29.41900 -1.07700  1.000 43.47507  ? 146 GLN   A C   1 
ATOM   878  O  O   . GLN   A 1 112 ? 20.48200  -28.27300 -0.80600  1.000 46.56782  ? 146 GLN   A O   1 
ATOM   879  C  CB  . GLN   A 1 112 ? 23.31000  -29.82800 -0.76000  1.000 35.97697  ? 146 GLN   A CB  1 
ATOM   880  C  CG  . GLN   A 1 112 ? 24.43500  -30.33300 0.13500   1.000 53.20927  ? 146 GLN   A CG  1 
ATOM   881  C  CD  . GLN   A 1 112 ? 25.80200  -29.89200 -0.34900  1.000 49.24809  ? 146 GLN   A CD  1 
ATOM   882  O  OE1 . GLN   A 1 112 ? 25.94000  -28.84300 -0.97900  1.000 57.94218  ? 146 GLN   A OE1 1 
ATOM   883  N  NE2 . GLN   A 1 112 ? 26.82000  -30.69200 -0.06000  1.000 53.01507  ? 146 GLN   A NE2 1 
ATOM   884  N  N   . MET   A 1 113 ? 20.36700  -30.10800 -2.11000  1.000 40.48416  ? 147 MET   A N   1 
ATOM   885  C  CA  . MET   A 1 113 ? 19.28400  -29.55700 -2.91900  1.000 45.82392  ? 147 MET   A CA  1 
ATOM   886  C  C   . MET   A 1 113 ? 17.98500  -29.48800 -2.12600  1.000 45.80057  ? 147 MET   A C   1 
ATOM   887  O  O   . MET   A 1 113 ? 17.23300  -28.51400 -2.24200  1.000 37.89519  ? 147 MET   A O   1 
ATOM   888  C  CB  . MET   A 1 113 ? 19.09700  -30.39200 -4.18500  1.000 34.39551  ? 147 MET   A CB  1 
ATOM   889  C  CG  . MET   A 1 113 ? 20.26900  -30.32600 -5.14900  1.000 37.53377  ? 147 MET   A CG  1 
ATOM   890  S  SD  . MET   A 1 113 ? 20.28300  -31.68400 -6.33500  1.000 49.18279  ? 147 MET   A SD  1 
ATOM   891  C  CE  . MET   A 1 113 ? 19.60100  -30.90000 -7.78900  1.000 35.12856  ? 147 MET   A CE  1 
ATOM   892  N  N   . LEU   A 1 114 ? 17.70300  -30.51300 -1.31900  1.000 53.44688  ? 148 LEU   A N   1 
ATOM   893  C  CA  . LEU   A 1 114 ? 16.50900  -30.48500 -0.48000  1.000 50.11398  ? 148 LEU   A CA  1 
ATOM   894  C  C   . LEU   A 1 114 ? 16.58300  -29.35900 0.54100   1.000 49.32877  ? 148 LEU   A C   1 
ATOM   895  O  O   . LEU   A 1 114 ? 15.56400  -28.74100 0.87000   1.000 49.88938  ? 148 LEU   A O   1 
ATOM   896  C  CB  . LEU   A 1 114 ? 16.32300  -31.83200 0.21900   1.000 47.59976  ? 148 LEU   A CB  1 
ATOM   897  C  CG  . LEU   A 1 114 ? 15.88300  -33.00600 -0.65700  1.000 48.31860  ? 148 LEU   A CG  1 
ATOM   898  C  CD1 . LEU   A 1 114 ? 15.98600  -34.31100 0.11300   1.000 44.04340  ? 148 LEU   A CD1 1 
ATOM   899  C  CD2 . LEU   A 1 114 ? 14.46400  -32.79000 -1.15800  1.000 42.90781  ? 148 LEU   A CD2 1 
ATOM   900  N  N   . THR   A 1 115 ? 17.78200  -29.07800 1.05500   1.000 58.73528  ? 149 THR   A N   1 
ATOM   901  C  CA  . THR   A 1 115 ? 17.94300  -27.97100 1.99200   1.000 49.06110  ? 149 THR   A CA  1 
ATOM   902  C  C   . THR   A 1 115 ? 17.77800  -26.62900 1.28900   1.000 47.16669  ? 149 THR   A C   1 
ATOM   903  O  O   . THR   A 1 115 ? 17.17900  -25.70000 1.84300   1.000 52.69994  ? 149 THR   A O   1 
ATOM   904  C  CB  . THR   A 1 115 ? 19.30800  -28.05900 2.67600   1.000 40.93837  ? 149 THR   A CB  1 
ATOM   905  O  OG1 . THR   A 1 115 ? 19.39900  -29.28900 3.40300   1.000 53.61040  ? 149 THR   A OG1 1 
ATOM   906  C  CG2 . THR   A 1 115 ? 19.50500  -26.89600 3.63900   1.000 45.82976  ? 149 THR   A CG2 1 
ATOM   907  N  N   . LEU   A 1 116 ? 18.29900  -26.51000 0.06600   1.000 53.43578  ? 150 LEU   A N   1 
ATOM   908  C  CA  . LEU   A 1 116 ? 18.14100  -25.27400 -0.69200  1.000 40.89991  ? 150 LEU   A CA  1 
ATOM   909  C  C   . LEU   A 1 116 ? 16.67800  -25.02400 -1.03200  1.000 42.73080  ? 150 LEU   A C   1 
ATOM   910  O  O   . LEU   A 1 116 ? 16.16300  -23.91700 -0.83700  1.000 51.65646  ? 150 LEU   A O   1 
ATOM   911  C  CB  . LEU   A 1 116 ? 18.98700  -25.33000 -1.96500  1.000 34.37175  ? 150 LEU   A CB  1 
ATOM   912  C  CG  . LEU   A 1 116 ? 20.49700  -25.18400 -1.78400  1.000 49.10082  ? 150 LEU   A CG  1 
ATOM   913  C  CD1 . LEU   A 1 116 ? 21.22300  -25.54200 -3.06900  1.000 43.02431  ? 150 LEU   A CD1 1 
ATOM   914  C  CD2 . LEU   A 1 116 ? 20.83500  -23.76800 -1.35500  1.000 53.70553  ? 150 LEU   A CD2 1 
ATOM   915  N  N   . VAL   A 1 117 ? 15.99100  -26.04700 -1.54500  1.000 43.56585  ? 151 VAL   A N   1 
ATOM   916  C  CA  . VAL   A 1 117 ? 14.58300  -25.89600 -1.90400  1.000 47.84767  ? 151 VAL   A CA  1 
ATOM   917  C  C   . VAL   A 1 117 ? 13.74300  -25.62800 -0.66300  1.000 46.82126  ? 151 VAL   A C   1 
ATOM   918  O  O   . VAL   A 1 117 ? 12.78700  -24.84200 -0.70100  1.000 53.03787  ? 151 VAL   A O   1 
ATOM   919  C  CB  . VAL   A 1 117 ? 14.09100  -27.13800 -2.67100  1.000 45.67906  ? 151 VAL   A CB  1 
ATOM   920  C  CG1 . VAL   A 1 117 ? 12.59500  -27.05500 -2.92300  1.000 42.32231  ? 151 VAL   A CG1 1 
ATOM   921  C  CG2 . VAL   A 1 117 ? 14.84100  -27.27700 -3.98700  1.000 38.85506  ? 151 VAL   A CG2 1 
ATOM   922  N  N   . GLU   A 1 118 ? 14.08800  -26.26500 0.45900   1.000 46.48904  ? 152 GLU   A N   1 
ATOM   923  C  CA  . GLU   A 1 118 ? 13.37800  -25.99300 1.70500   1.000 48.50758  ? 152 GLU   A CA  1 
ATOM   924  C  C   . GLU   A 1 118 ? 13.52300  -24.53100 2.10300   1.000 56.34333  ? 152 GLU   A C   1 
ATOM   925  O  O   . GLU   A 1 118 ? 12.53800  -23.87200 2.44800   1.000 62.42983  ? 152 GLU   A O   1 
ATOM   926  C  CB  . GLU   A 1 118 ? 13.88600  -26.90300 2.82600   1.000 43.66011  ? 152 GLU   A CB  1 
ATOM   927  C  CG  . GLU   A 1 118 ? 13.19700  -26.65000 4.16300   1.000 54.59895  ? 152 GLU   A CG  1 
ATOM   928  C  CD  . GLU   A 1 118 ? 13.77900  -27.46800 5.30200   1.000 60.57099  ? 152 GLU   A CD  1 
ATOM   929  O  OE1 . GLU   A 1 118 ? 14.73000  -28.24000 5.06100   1.000 63.26980  ? 152 GLU   A OE1 1 
ATOM   930  O  OE2 . GLU   A 1 118 ? 13.28500  -27.33600 6.44200   1.000 59.97137  ? 152 GLU   A OE2 1 
ATOM   931  N  N   . GLU   A 1 119 ? 14.75100  -24.00500 2.05300   1.000 56.19628  ? 153 GLU   A N   1 
ATOM   932  C  CA  . GLU   A 1 119 ? 14.97400  -22.60300 2.39200   1.000 64.22028  ? 153 GLU   A CA  1 
ATOM   933  C  C   . GLU   A 1 119 ? 14.17600  -21.67900 1.48100   1.000 54.10634  ? 153 GLU   A C   1 
ATOM   934  O  O   . GLU   A 1 119 ? 13.67700  -20.63800 1.92400   1.000 60.55603  ? 153 GLU   A O   1 
ATOM   935  C  CB  . GLU   A 1 119 ? 16.46500  -22.27500 2.31900   1.000 70.12683  ? 153 GLU   A CB  1 
ATOM   936  C  CG  . GLU   A 1 119 ? 17.23700  -22.62900 3.58000   1.000 77.70270  ? 153 GLU   A CG  1 
ATOM   937  C  CD  . GLU   A 1 119 ? 16.85500  -21.75200 4.75800   1.000 77.54929  ? 153 GLU   A CD  1 
ATOM   938  O  OE1 . GLU   A 1 119 ? 16.40500  -20.61000 4.53000   1.000 78.87371  ? 153 GLU   A OE1 1 
ATOM   939  O  OE2 . GLU   A 1 119 ? 17.00100  -22.20600 5.91300   1.000 84.30519  ? 153 GLU   A OE2 1 
ATOM   940  N  N   . VAL   A 1 120 ? 14.04200  -22.04300 0.20400   1.000 49.58371  ? 154 VAL   A N   1 
ATOM   941  C  CA  . VAL   A 1 120 ? 13.19400  -21.27200 -0.70100  1.000 50.90727  ? 154 VAL   A CA  1 
ATOM   942  C  C   . VAL   A 1 120 ? 11.75000  -21.29500 -0.21800  1.000 60.82300  ? 154 VAL   A C   1 
ATOM   943  O  O   . VAL   A 1 120 ? 11.06600  -20.26300 -0.20100  1.000 61.75579  ? 154 VAL   A O   1 
ATOM   944  C  CB  . VAL   A 1 120 ? 13.32300  -21.80500 -2.14000  1.000 46.61544  ? 154 VAL   A CB  1 
ATOM   945  C  CG1 . VAL   A 1 120 ? 12.27500  -21.17400 -3.03900  1.000 48.71453  ? 154 VAL   A CG1 1 
ATOM   946  C  CG2 . VAL   A 1 120 ? 14.72100  -21.54000 -2.67800  1.000 48.44003  ? 154 VAL   A CG2 1 
ATOM   947  N  N   . HIS   A 1 121 ? 11.26700  -22.46900 0.19600   1.000 58.30985  ? 155 HIS   A N   1 
ATOM   948  C  CA  . HIS   A 1 121 ? 9.89800   -22.58000 0.69000   1.000 55.25079  ? 155 HIS   A CA  1 
ATOM   949  C  C   . HIS   A 1 121 ? 9.71400   -21.85200 2.01500   1.000 54.05794  ? 155 HIS   A C   1 
ATOM   950  O  O   . HIS   A 1 121 ? 8.60800   -21.38600 2.31500   1.000 61.87188  ? 155 HIS   A O   1 
ATOM   951  C  CB  . HIS   A 1 121 ? 9.51000   -24.05100 0.83800   1.000 48.83091  ? 155 HIS   A CB  1 
ATOM   952  C  CG  . HIS   A 1 121 ? 9.49500   -24.80400 -0.45500  1.000 53.18666  ? 155 HIS   A CG  1 
ATOM   953  N  ND1 . HIS   A 1 121 ? 9.30700   -26.16700 -0.52100  1.000 46.52282  ? 155 HIS   A ND1 1 
ATOM   954  C  CD2 . HIS   A 1 121 ? 9.64300   -24.38300 -1.73300  1.000 51.20385  ? 155 HIS   A CD2 1 
ATOM   955  C  CE1 . HIS   A 1 121 ? 9.33900   -26.55400 -1.78300  1.000 47.44321  ? 155 HIS   A CE1 1 
ATOM   956  N  NE2 . HIS   A 1 121 ? 9.54200   -25.49000 -2.53900  1.000 47.06231  ? 155 HIS   A NE2 1 
ATOM   957  N  N   . ARG   A 1 122 ? 10.77700  -21.74900 2.81600   1.000 58.48537  ? 156 ARG   A N   1 
ATOM   958  C  CA  . ARG   A 1 122 ? 10.68000  -21.05900 4.09800   1.000 56.73915  ? 156 ARG   A CA  1 
ATOM   959  C  C   . ARG   A 1 122 ? 10.30500  -19.59600 3.90700   1.000 62.01913  ? 156 ARG   A C   1 
ATOM   960  O  O   . ARG   A 1 122 ? 9.55100   -19.02900 4.70800   1.000 62.94144  ? 156 ARG   A O   1 
ATOM   961  C  CB  . ARG   A 1 122 ? 12.00100  -21.17800 4.86000   1.000 65.28899  ? 156 ARG   A CB  1 
ATOM   962  C  CG  . ARG   A 1 122 ? 12.38500  -22.60400 5.22000   1.000 77.48364  ? 156 ARG   A CG  1 
ATOM   963  C  CD  . ARG   A 1 122 ? 11.37600  -23.21000 6.17100   1.000 78.15269  ? 156 ARG   A CD  1 
ATOM   964  N  NE  . ARG   A 1 122 ? 11.89500  -23.28800 7.53100   1.000 101.20873 ? 156 ARG   A NE  1 
ATOM   965  C  CZ  . ARG   A 1 122 ? 11.16500  -23.10000 8.62100   1.000 120.65074 ? 156 ARG   A CZ  1 
ATOM   966  N  NH1 . ARG   A 1 122 ? 9.88600   -22.77200 8.54700   1.000 105.08102 ? 156 ARG   A NH1 1 
ATOM   967  N  NH2 . ARG   A 1 122 ? 11.73600  -23.23500 9.81500   1.000 117.93765 ? 156 ARG   A NH2 1 
ATOM   968  N  N   . HIS   A 1 123 ? 10.81200  -18.97200 2.84700   1.000 61.48060  ? 157 HIS   A N   1 
ATOM   969  C  CA  . HIS   A 1 123 ? 10.54500  -17.57100 2.56200   1.000 74.07995  ? 157 HIS   A CA  1 
ATOM   970  C  C   . HIS   A 1 123 ? 9.30000   -17.37400 1.70400   1.000 59.30395  ? 157 HIS   A C   1 
ATOM   971  O  O   . HIS   A 1 123 ? 9.10500   -16.28000 1.16500   1.000 80.87550  ? 157 HIS   A O   1 
ATOM   972  C  CB  . HIS   A 1 123 ? 11.76100  -16.93100 1.89000   1.000 70.89926  ? 157 HIS   A CB  1 
ATOM   973  C  CG  . HIS   A 1 123 ? 12.98500  -16.91500 2.75300   1.000 67.98548  ? 157 HIS   A CG  1 
ATOM   974  N  ND1 . HIS   A 1 123 ? 13.61900  -18.06600 3.16800   1.000 57.68242  ? 157 HIS   A ND1 1 
ATOM   975  C  CD2 . HIS   A 1 123 ? 13.68700  -15.88700 3.28500   1.000 69.48548  ? 157 HIS   A CD2 1 
ATOM   976  C  CE1 . HIS   A 1 123 ? 14.66000  -17.74800 3.91700   1.000 54.41664  ? 157 HIS   A CE1 1 
ATOM   977  N  NE2 . HIS   A 1 123 ? 14.72400  -16.43200 4.00200   1.000 70.64355  ? 157 HIS   A NE2 1 
ATOM   978  N  N   . ASP   A 1 124 ? 8.46200   -18.41000 1.57600   1.000 63.58527  ? 158 ASP   A N   1 
ATOM   979  C  CA  . ASP   A 1 124 ? 7.15800   -18.34500 0.90700   1.000 61.72979  ? 158 ASP   A CA  1 
ATOM   980  C  C   . ASP   A 1 124 ? 7.28800   -18.32000 -0.61100  1.000 68.02178  ? 158 ASP   A C   1 
ATOM   981  O  O   . ASP   A 1 124 ? 6.48100   -17.69400 -1.30200  1.000 82.25199  ? 158 ASP   A O   1 
ATOM   982  C  CB  . ASP   A 1 124 ? 6.33200   -17.14900 1.38800   1.000 65.43487  ? 158 ASP   A CB  1 
ATOM   983  C  CG  . ASP   A 1 124 ? 6.46000   -16.93100 2.87200   1.000 72.86716  ? 158 ASP   A CG  1 
ATOM   984  O  OD1 . ASP   A 1 124 ? 6.57100   -17.93400 3.60500   1.000 82.01070  ? 158 ASP   A OD1 1 
ATOM   985  O  OD2 . ASP   A 1 124 ? 6.48400   -15.76300 3.30200   1.000 85.87359  ? 158 ASP   A OD2 1 
ATOM   986  N  N   . LEU   A 1 125 ? 8.29400   -19.00500 -1.14000  1.000 58.76335  ? 159 LEU   A N   1 
ATOM   987  C  CA  . LEU   A 1 125 ? 8.49900   -19.11300 -2.57400  1.000 59.52237  ? 159 LEU   A CA  1 
ATOM   988  C  C   . LEU   A 1 125 ? 8.53400   -20.57700 -2.98500  1.000 65.79054  ? 159 LEU   A C   1 
ATOM   989  O  O   . LEU   A 1 125 ? 8.97600   -21.44500 -2.22500  1.000 57.89180  ? 159 LEU   A O   1 
ATOM   990  C  CB  . LEU   A 1 125 ? 9.80700   -18.43500 -3.01900  1.000 60.14887  ? 159 LEU   A CB  1 
ATOM   991  C  CG  . LEU   A 1 125 ? 9.94200   -16.91100 -3.11400  1.000 68.10688  ? 159 LEU   A CG  1 
ATOM   992  C  CD1 . LEU   A 1 125 ? 8.77700   -16.28800 -3.87600  1.000 69.07832  ? 159 LEU   A CD1 1 
ATOM   993  C  CD2 . LEU   A 1 125 ? 10.11000  -16.28300 -1.74500  1.000 75.81147  ? 159 LEU   A CD2 1 
ATOM   994  N  N   . ILE   A 1 126 ? 8.05300   -20.84300 -4.19400  1.000 55.82021  ? 160 ILE   A N   1 
ATOM   995  C  CA  . ILE   A 1 126 ? 8.26800   -22.11400 -4.87200  1.000 47.85618  ? 160 ILE   A CA  1 
ATOM   996  C  C   . ILE   A 1 126 ? 9.11400   -21.84200 -6.10500  1.000 53.68010  ? 160 ILE   A C   1 
ATOM   997  O  O   . ILE   A 1 126 ? 8.92800   -20.82800 -6.78900  1.000 59.21155  ? 160 ILE   A O   1 
ATOM   998  C  CB  . ILE   A 1 126 ? 6.94500   -22.81300 -5.24400  1.000 55.93257  ? 160 ILE   A CB  1 
ATOM   999  C  CG1 . ILE   A 1 126 ? 5.98200   -21.83600 -5.92200  1.000 60.54876  ? 160 ILE   A CG1 1 
ATOM   1000 C  CG2 . ILE   A 1 126 ? 6.31000   -23.44300 -4.01200  1.000 62.66373  ? 160 ILE   A CG2 1 
ATOM   1001 C  CD1 . ILE   A 1 126 ? 4.66300   -22.46100 -6.31800  1.000 48.42184  ? 160 ILE   A CD1 1 
ATOM   1002 N  N   . TYR   A 1 127 ? 10.05400  -22.74400 -6.38100  1.000 50.23740  ? 161 TYR   A N   1 
ATOM   1003 C  CA  . TYR   A 1 127 ? 11.02800  -22.50400 -7.43900  1.000 52.38416  ? 161 TYR   A CA  1 
ATOM   1004 C  C   . TYR   A 1 127 ? 10.42100  -22.72100 -8.82200  1.000 55.90683  ? 161 TYR   A C   1 
ATOM   1005 O  O   . TYR   A 1 127 ? 10.56300  -21.87200 -9.71000  1.000 59.44884  ? 161 TYR   A O   1 
ATOM   1006 C  CB  . TYR   A 1 127 ? 12.24700  -23.40100 -7.22600  1.000 48.37103  ? 161 TYR   A CB  1 
ATOM   1007 C  CG  . TYR   A 1 127 ? 13.40600  -23.07400 -8.12600  1.000 43.02825  ? 161 TYR   A CG  1 
ATOM   1008 C  CD1 . TYR   A 1 127 ? 14.17200  -21.93500 -7.92000  1.000 39.00815  ? 161 TYR   A CD1 1 
ATOM   1009 C  CD2 . TYR   A 1 127 ? 13.74000  -23.90700 -9.18100  1.000 49.97332  ? 161 TYR   A CD2 1 
ATOM   1010 C  CE1 . TYR   A 1 127 ? 15.23600  -21.63500 -8.74600  1.000 52.45519  ? 161 TYR   A CE1 1 
ATOM   1011 C  CE2 . TYR   A 1 127 ? 14.79900  -23.61700 -10.00600 1.000 53.28318  ? 161 TYR   A CE2 1 
ATOM   1012 C  CZ  . TYR   A 1 127 ? 15.54200  -22.48300 -9.78800  1.000 49.74345  ? 161 TYR   A CZ  1 
ATOM   1013 O  OH  . TYR   A 1 127 ? 16.59500  -22.20900 -10.62400 1.000 41.65683  ? 161 TYR   A OH  1 
ATOM   1014 N  N   . ARG   A 1 128 ? 9.75200   -23.85700 -9.02200  1.000 45.77632  ? 162 ARG   A N   1 
ATOM   1015 C  CA  . ARG   A 1 128 ? 8.97900   -24.19200 -10.21800 1.000 58.67030  ? 162 ARG   A CA  1 
ATOM   1016 C  C   . ARG   A 1 128 ? 9.82400   -24.35100 -11.47700 1.000 54.39358  ? 162 ARG   A C   1 
ATOM   1017 O  O   . ARG   A 1 128 ? 9.26300   -24.44900 -12.57600 1.000 65.75279  ? 162 ARG   A O   1 
ATOM   1018 C  CB  . ARG   A 1 128 ? 7.87700   -23.16200 -10.49400 1.000 47.26240  ? 162 ARG   A CB  1 
ATOM   1019 C  CG  . ARG   A 1 128 ? 6.86300   -23.00200 -9.37600  1.000 60.80214  ? 162 ARG   A CG  1 
ATOM   1020 C  CD  . ARG   A 1 128 ? 5.65600   -22.22100 -9.86700  1.000 72.70627  ? 162 ARG   A CD  1 
ATOM   1021 N  NE  . ARG   A 1 128 ? 6.03500   -20.91600 -10.39600 1.000 62.94237  ? 162 ARG   A NE  1 
ATOM   1022 C  CZ  . ARG   A 1 128 ? 5.29800   -20.20600 -11.23900 1.000 73.59488  ? 162 ARG   A CZ  1 
ATOM   1023 N  NH1 . ARG   A 1 128 ? 4.14100   -20.65800 -11.69500 1.000 72.75474  ? 162 ARG   A NH1 1 
ATOM   1024 N  NH2 . ARG   A 1 128 ? 5.73600   -19.01600 -11.64100 1.000 68.71621  ? 162 ARG   A NH2 1 
ATOM   1025 N  N   . ASP   A 1 129 ? 11.14900  -24.38200 -11.36200 1.000 65.19170  ? 163 ASP   A N   1 
ATOM   1026 C  CA  . ASP   A 1 129 ? 12.01400  -24.57800 -12.52200 1.000 66.97036  ? 163 ASP   A CA  1 
ATOM   1027 C  C   . ASP   A 1 129 ? 13.19500  -25.46200 -12.15300 1.000 56.77680  ? 163 ASP   A C   1 
ATOM   1028 O  O   . ASP   A 1 129 ? 14.33100  -25.22100 -12.57600 1.000 56.80836  ? 163 ASP   A O   1 
ATOM   1029 C  CB  . ASP   A 1 129 ? 12.49400  -23.24200 -13.09000 1.000 71.65555  ? 163 ASP   A CB  1 
ATOM   1030 C  CG  . ASP   A 1 129 ? 12.89200  -23.33900 -14.55100 1.000 80.23578  ? 163 ASP   A CG  1 
ATOM   1031 O  OD1 . ASP   A 1 129 ? 12.49100  -24.31900 -15.21500 1.000 66.94246  ? 163 ASP   A OD1 1 
ATOM   1032 O  OD2 . ASP   A 1 129 ? 13.61000  -22.43800 -15.03500 1.000 74.15015  ? 163 ASP   A OD2 1 
ATOM   1033 N  N   . ILE   A 1 130 ? 12.93900  -26.49700 -11.35100 1.000 45.95723  ? 164 ILE   A N   1 
ATOM   1034 C  CA  . ILE   A 1 130 ? 14.00600  -27.36600 -10.86500 1.000 42.66669  ? 164 ILE   A CA  1 
ATOM   1035 C  C   . ILE   A 1 130 ? 14.67100  -28.06200 -12.04300 1.000 49.06116  ? 164 ILE   A C   1 
ATOM   1036 O  O   . ILE   A 1 130 ? 14.01000  -28.73300 -12.84400 1.000 38.51128  ? 164 ILE   A O   1 
ATOM   1037 C  CB  . ILE   A 1 130 ? 13.45800  -28.37700 -9.85300  1.000 47.65898  ? 164 ILE   A CB  1 
ATOM   1038 C  CG1 . ILE   A 1 130 ? 13.11200  -27.68200 -8.53400  1.000 43.47190  ? 164 ILE   A CG1 1 
ATOM   1039 C  CG2 . ILE   A 1 130 ? 14.45800  -29.49900 -9.62400  1.000 53.38294  ? 164 ILE   A CG2 1 
ATOM   1040 C  CD1 . ILE   A 1 130 ? 14.31800  -27.14400 -7.79400  1.000 42.68808  ? 164 ILE   A CD1 1 
ATOM   1041 N  N   . LYS   A 1 131 ? 15.98800  -27.89900 -12.15300 1.000 44.91422  ? 165 LYS   A N   1 
ATOM   1042 C  CA  . LYS   A 1 131 ? 16.78200  -28.52300 -13.20200 1.000 48.86119  ? 165 LYS   A CA  1 
ATOM   1043 C  C   . LYS   A 1 131 ? 18.23700  -28.50400 -12.76200 1.000 50.58858  ? 165 LYS   A C   1 
ATOM   1044 O  O   . LYS   A 1 131 ? 18.64000  -27.60100 -12.01900 1.000 47.60373  ? 165 LYS   A O   1 
ATOM   1045 C  CB  . LYS   A 1 131 ? 16.61400  -27.79000 -14.54200 1.000 50.68018  ? 165 LYS   A CB  1 
ATOM   1046 C  CG  . LYS   A 1 131 ? 17.18900  -26.38300 -14.55300 1.000 49.81852  ? 165 LYS   A CG  1 
ATOM   1047 C  CD  . LYS   A 1 131 ? 17.17400  -25.77200 -15.94500 1.000 55.13587  ? 165 LYS   A CD  1 
ATOM   1048 C  CE  . LYS   A 1 131 ? 15.77100  -25.38300 -16.37200 1.000 60.63362  ? 165 LYS   A CE  1 
ATOM   1049 N  NZ  . LYS   A 1 131 ? 15.77700  -24.68000 -17.68400 1.000 68.91836  ? 165 LYS   A NZ  1 
ATOM   1050 N  N   . PRO   A 1 132 ? 19.04400  -29.48000 -13.18500 1.000 43.40133  ? 166 PRO   A N   1 
ATOM   1051 C  CA  . PRO   A 1 132 ? 20.46000  -29.48500 -12.78100 1.000 46.54391  ? 166 PRO   A CA  1 
ATOM   1052 C  C   . PRO   A 1 132 ? 21.24800  -28.30800 -13.32400 1.000 49.32452  ? 166 PRO   A C   1 
ATOM   1053 O  O   . PRO   A 1 132 ? 22.31700  -27.99200 -12.78400 1.000 44.81802  ? 166 PRO   A O   1 
ATOM   1054 C  CB  . PRO   A 1 132 ? 20.98100  -30.81400 -13.34600 1.000 47.14436  ? 166 PRO   A CB  1 
ATOM   1055 C  CG  . PRO   A 1 132 ? 20.05400  -31.12800 -14.47800 1.000 52.22068  ? 166 PRO   A CG  1 
ATOM   1056 C  CD  . PRO   A 1 132 ? 18.70900  -30.63000 -14.04200 1.000 45.02209  ? 166 PRO   A CD  1 
ATOM   1057 N  N   . ASP   A 1 133 ? 20.74800  -27.65300 -14.37500 1.000 45.33385  ? 167 ASP   A N   1 
ATOM   1058 C  CA  . ASP   A 1 133 ? 21.43200  -26.52300 -14.98900 1.000 41.64577  ? 167 ASP   A CA  1 
ATOM   1059 C  C   . ASP   A 1 133 ? 21.47900  -25.30500 -14.07500 1.000 48.32285  ? 167 ASP   A C   1 
ATOM   1060 O  O   . ASP   A 1 133 ? 22.35500  -24.44900 -14.24600 1.000 38.51832  ? 167 ASP   A O   1 
ATOM   1061 C  CB  . ASP   A 1 133 ? 20.73700  -26.15100 -16.30200 1.000 53.88072  ? 167 ASP   A CB  1 
ATOM   1062 C  CG  . ASP   A 1 133 ? 20.49900  -27.35500 -17.20900 1.000 47.48956  ? 167 ASP   A CG  1 
ATOM   1063 O  OD1 . ASP   A 1 133 ? 19.67400  -28.22400 -16.85000 1.000 58.72743  ? 167 ASP   A OD1 1 
ATOM   1064 O  OD2 . ASP   A 1 133 ? 21.14000  -27.43400 -18.28000 1.000 59.21308  ? 167 ASP   A OD2 1 
ATOM   1065 N  N   . ASN   A 1 134 ? 20.55700  -25.20500 -13.11800 1.000 50.02289  ? 168 ASN   A N   1 
ATOM   1066 C  CA  . ASN   A 1 134 ? 20.45300  -24.05200 -12.23300 1.000 43.05630  ? 168 ASN   A CA  1 
ATOM   1067 C  C   . ASN   A 1 134 ? 21.05800  -24.29600 -10.85700 1.000 35.88932  ? 168 ASN   A C   1 
ATOM   1068 O  O   . ASN   A 1 134 ? 21.03300  -23.39200 -10.01500 1.000 51.17617  ? 168 ASN   A O   1 
ATOM   1069 C  CB  . ASN   A 1 134 ? 18.98600  -23.63400 -12.08700 1.000 40.11110  ? 168 ASN   A CB  1 
ATOM   1070 C  CG  . ASN   A 1 134 ? 18.41700  -23.04400 -13.36300 1.000 59.50932  ? 168 ASN   A CG  1 
ATOM   1071 O  OD1 . ASN   A 1 134 ? 19.15900  -22.56900 -14.22300 1.000 63.02035  ? 168 ASN   A OD1 1 
ATOM   1072 N  ND2 . ASN   A 1 134 ? 17.09400  -23.06400 -13.48900 1.000 42.04874  ? 168 ASN   A ND2 1 
ATOM   1073 N  N   . PHE   A 1 135 ? 21.58700  -25.48700 -10.60100 1.000 43.87117  ? 169 PHE   A N   1 
ATOM   1074 C  CA  . PHE   A 1 135 ? 22.30400  -25.77700 -9.36700  1.000 42.12286  ? 169 PHE   A CA  1 
ATOM   1075 C  C   . PHE   A 1 135 ? 23.79900  -25.70900 -9.65000  1.000 44.89132  ? 169 PHE   A C   1 
ATOM   1076 O  O   . PHE   A 1 135 ? 24.32700  -26.52600 -10.40900 1.000 37.47509  ? 169 PHE   A O   1 
ATOM   1077 C  CB  . PHE   A 1 135 ? 21.91400  -27.14600 -8.81200  1.000 51.30174  ? 169 PHE   A CB  1 
ATOM   1078 C  CG  . PHE   A 1 135 ? 20.53700  -27.18800 -8.21200  1.000 41.79424  ? 169 PHE   A CG  1 
ATOM   1079 C  CD1 . PHE   A 1 135 ? 19.43300  -27.47400 -8.99600  1.000 41.45234  ? 169 PHE   A CD1 1 
ATOM   1080 C  CD2 . PHE   A 1 135 ? 20.34900  -26.94100 -6.86200  1.000 37.84652  ? 169 PHE   A CD2 1 
ATOM   1081 C  CE1 . PHE   A 1 135 ? 18.16500  -27.51400 -8.44700  1.000 48.36602  ? 169 PHE   A CE1 1 
ATOM   1082 C  CE2 . PHE   A 1 135 ? 19.08300  -26.98000 -6.30500  1.000 42.30128  ? 169 PHE   A CE2 1 
ATOM   1083 C  CZ  . PHE   A 1 135 ? 17.99000  -27.26700 -7.09900  1.000 42.79753  ? 169 PHE   A CZ  1 
ATOM   1084 N  N   . LEU   A 1 136 ? 24.47100  -24.73400 -9.04600  1.000 47.48402  ? 170 LEU   A N   1 
ATOM   1085 C  CA  . LEU   A 1 136 ? 25.86900  -24.44700 -9.32800  1.000 48.36615  ? 170 LEU   A CA  1 
ATOM   1086 C  C   . LEU   A 1 136 ? 26.72200  -24.72000 -8.09700  1.000 40.87075  ? 170 LEU   A C   1 
ATOM   1087 O  O   . LEU   A 1 136 ? 26.27200  -24.55000 -6.96300  1.000 39.42547  ? 170 LEU   A O   1 
ATOM   1088 C  CB  . LEU   A 1 136 ? 26.05700  -22.98600 -9.76400  1.000 45.76199  ? 170 LEU   A CB  1 
ATOM   1089 C  CG  . LEU   A 1 136 ? 25.82000  -22.56700 -11.21900 1.000 47.43180  ? 170 LEU   A CG  1 
ATOM   1090 C  CD1 . LEU   A 1 136 ? 24.50300  -23.09100 -11.76800 1.000 41.95626  ? 170 LEU   A CD1 1 
ATOM   1091 C  CD2 . LEU   A 1 136 ? 25.86400  -21.05200 -11.31800 1.000 45.39763  ? 170 LEU   A CD2 1 
ATOM   1092 N  N   . ILE   A 1 137 ? 27.96500  -25.13800 -8.32300  1.000 41.77105  ? 171 ILE   A N   1 
ATOM   1093 C  CA  . ILE   A 1 137 ? 28.91600  -25.26200 -7.22400  1.000 43.44607  ? 171 ILE   A CA  1 
ATOM   1094 C  C   . ILE   A 1 137 ? 29.64200  -23.93300 -7.07500  1.000 56.26899  ? 171 ILE   A C   1 
ATOM   1095 O  O   . ILE   A 1 137 ? 29.36800  -22.98000 -7.81400  1.000 50.31189  ? 171 ILE   A O   1 
ATOM   1096 C  CB  . ILE   A 1 137 ? 29.90800  -26.41900 -7.44400  1.000 42.29622  ? 171 ILE   A CB  1 
ATOM   1097 C  CG1 . ILE   A 1 137 ? 30.71300  -26.20700 -8.72700  1.000 49.51797  ? 171 ILE   A CG1 1 
ATOM   1098 C  CG2 . ILE   A 1 137 ? 29.17700  -27.75400 -7.46900  1.000 50.55294  ? 171 ILE   A CG2 1 
ATOM   1099 C  CD1 . ILE   A 1 137 ? 31.88200  -27.16000 -8.87300  1.000 50.93095  ? 171 ILE   A CD1 1 
ATOM   1100 N  N   . GLY   A 1 138 ? 30.56100  -23.85300 -6.11800  1.000 55.10576  ? 172 GLY   A N   1 
ATOM   1101 C  CA  . GLY   A 1 138 ? 31.32900  -22.64800 -5.89900  1.000 52.01489  ? 172 GLY   A CA  1 
ATOM   1102 C  C   . GLY   A 1 138 ? 32.51700  -22.55300 -6.83700  1.000 50.58472  ? 172 GLY   A C   1 
ATOM   1103 O  O   . GLY   A 1 138 ? 32.65800  -23.30400 -7.80300  1.000 50.69167  ? 172 GLY   A O   1 
ATOM   1104 N  N   . ARG   A 1 139 ? 33.38900  -21.59900 -6.53600  1.000 59.54876  ? 173 ARG   A N   1 
ATOM   1105 C  CA  . ARG   A 1 139 ? 34.61200  -21.39800 -7.29700  1.000 57.88573  ? 173 ARG   A CA  1 
ATOM   1106 C  C   . ARG   A 1 139 ? 35.78000  -22.09000 -6.60100  1.000 61.45763  ? 173 ARG   A C   1 
ATOM   1107 O  O   . ARG   A 1 139 ? 35.73300  -22.38900 -5.40500  1.000 73.37143  ? 173 ARG   A O   1 
ATOM   1108 C  CB  . ARG   A 1 139 ? 34.90100  -19.90400 -7.47700  1.000 63.33455  ? 173 ARG   A CB  1 
ATOM   1109 C  CG  . ARG   A 1 139 ? 33.68900  -19.10500 -7.93200  1.000 52.23784  ? 173 ARG   A CG  1 
ATOM   1110 C  CD  . ARG   A 1 139 ? 34.03400  -17.66600 -8.28700  1.000 71.03637  ? 173 ARG   A CD  1 
ATOM   1111 N  NE  . ARG   A 1 139 ? 34.50300  -17.52900 -9.66100  1.000 78.42135  ? 173 ARG   A NE  1 
ATOM   1112 C  CZ  . ARG   A 1 139 ? 35.71900  -17.12500 -10.00400 1.000 72.60207  ? 173 ARG   A CZ  1 
ATOM   1113 N  NH1 . ARG   A 1 139 ? 36.62000  -16.79700 -9.09300  1.000 50.62309  ? 173 ARG   A NH1 1 
ATOM   1114 N  NH2 . ARG   A 1 139 ? 36.03400  -17.03500 -11.29300 1.000 64.87135  ? 173 ARG   A NH2 1 
ATOM   1115 N  N   . ARG   A 1 140 ? 36.83200  -22.35000 -7.37600  1.000 64.91421  ? 174 ARG   A N   1 
ATOM   1116 C  CA  . ARG   A 1 140 ? 37.98500  -23.07400 -6.85900  1.000 76.57873  ? 174 ARG   A CA  1 
ATOM   1117 C  C   . ARG   A 1 140 ? 38.63000  -22.31500 -5.70500  1.000 72.38439  ? 174 ARG   A C   1 
ATOM   1118 O  O   . ARG   A 1 140 ? 38.62100  -21.08200 -5.65800  1.000 77.07708  ? 174 ARG   A O   1 
ATOM   1119 C  CB  . ARG   A 1 140 ? 39.01000  -23.30100 -7.97100  1.000 67.45125  ? 174 ARG   A CB  1 
ATOM   1120 C  CG  . ARG   A 1 140 ? 40.11800  -24.28300 -7.62300  1.000 91.55230  ? 174 ARG   A CG  1 
ATOM   1121 C  CD  . ARG   A 1 140 ? 39.88000  -25.61100 -8.31100  1.000 95.90682  ? 174 ARG   A CD  1 
ATOM   1122 N  NE  . ARG   A 1 140 ? 39.50400  -25.40500 -9.70400  1.000 111.03537 ? 174 ARG   A NE  1 
ATOM   1123 C  CZ  . ARG   A 1 140 ? 39.23200  -26.37600 -10.56400 1.000 106.23132 ? 174 ARG   A CZ  1 
ATOM   1124 N  NH1 . ARG   A 1 140 ? 39.30000  -27.65000 -10.21400 1.000 77.84883  ? 174 ARG   A NH1 1 
ATOM   1125 N  NH2 . ARG   A 1 140 ? 38.88000  -26.05900 -11.80600 1.000 103.57768 ? 174 ARG   A NH2 1 
ATOM   1126 N  N   . GLY   A 1 141 ? 39.18500  -23.07000 -4.75600  1.000 70.84200  ? 175 GLY   A N   1 
ATOM   1127 C  CA  . GLY   A 1 141 ? 39.85700  -22.49900 -3.60900  1.000 88.22077  ? 175 GLY   A CA  1 
ATOM   1128 C  C   . GLY   A 1 141 ? 38.96000  -21.84300 -2.58400  1.000 84.58106  ? 175 GLY   A C   1 
ATOM   1129 O  O   . GLY   A 1 141 ? 39.45700  -21.43400 -1.52700  1.000 84.42780  ? 175 GLY   A O   1 
ATOM   1130 N  N   . ALA   A 1 142 ? 37.66300  -21.72500 -2.85000  1.000 86.12905  ? 176 ALA   A N   1 
ATOM   1131 C  CA  . ALA   A 1 142 ? 36.75100  -21.10200 -1.90600  1.000 74.12891  ? 176 ALA   A CA  1 
ATOM   1132 C  C   . ALA   A 1 142 ? 36.31100  -22.10300 -0.84200  1.000 81.57202  ? 176 ALA   A C   1 
ATOM   1133 O  O   . ALA   A 1 142 ? 36.46700  -23.31800 -0.98900  1.000 79.96506  ? 176 ALA   A O   1 
ATOM   1134 C  CB  . ALA   A 1 142 ? 35.53100  -20.53300 -2.63000  1.000 70.16439  ? 176 ALA   A CB  1 
ATOM   1135 N  N   . THR   A 1 143 ? 35.75400  -21.56800 0.24700   1.000 94.01934  ? 177 THR   A N   1 
ATOM   1136 C  CA  . THR   A 1 143 ? 35.27800  -22.42500 1.32800   1.000 88.49994  ? 177 THR   A CA  1 
ATOM   1137 C  C   . THR   A 1 143 ? 34.07700  -23.25100 0.88400   1.000 83.57452  ? 177 THR   A C   1 
ATOM   1138 O  O   . THR   A 1 143 ? 33.93600  -24.41600 1.27600   1.000 93.85484  ? 177 THR   A O   1 
ATOM   1139 C  CB  . THR   A 1 143 ? 34.92500  -21.58100 2.55200   1.000 99.64473  ? 177 THR   A CB  1 
ATOM   1140 O  OG1 . THR   A 1 143 ? 35.92600  -20.57200 2.74300   1.000 109.02896 ? 177 THR   A OG1 1 
ATOM   1141 C  CG2 . THR   A 1 143 ? 34.85700  -22.45400 3.79600   1.000 99.26086  ? 177 THR   A CG2 1 
ATOM   1142 N  N   . ASP   A 1 144 ? 33.20300  -22.66600 0.06800   1.000 77.15031  ? 178 ASP   A N   1 
ATOM   1143 C  CA  . ASP   A 1 144 ? 32.04300  -23.35400 -0.49500  1.000 75.07741  ? 178 ASP   A CA  1 
ATOM   1144 C  C   . ASP   A 1 144 ? 32.30500  -23.82900 -1.91800  1.000 58.30326  ? 178 ASP   A C   1 
ATOM   1145 O  O   . ASP   A 1 144 ? 31.43700  -23.72300 -2.78900  1.000 69.95219  ? 178 ASP   A O   1 
ATOM   1146 C  CB  . ASP   A 1 144 ? 30.81300  -22.44800 -0.44400  1.000 70.51131  ? 178 ASP   A CB  1 
ATOM   1147 C  CG  . ASP   A 1 144 ? 31.01500  -21.12600 -1.17900  1.000 86.23493  ? 178 ASP   A CG  1 
ATOM   1148 O  OD1 . ASP   A 1 144 ? 32.10100  -20.90200 -1.75700  1.000 76.88779  ? 178 ASP   A OD1 1 
ATOM   1149 O  OD2 . ASP   A 1 144 ? 30.07500  -20.30300 -1.17700  1.000 97.46664  ? 178 ASP   A OD2 1 
ATOM   1150 N  N   . GLU   A 1 145 ? 33.50200  -24.36200 -2.17400  1.000 66.17023  ? 179 GLU   A N   1 
ATOM   1151 C  CA  . GLU   A 1 145 ? 33.88400  -24.72300 -3.53600  1.000 70.40210  ? 179 GLU   A CA  1 
ATOM   1152 C  C   . GLU   A 1 145 ? 33.01100  -25.84500 -4.08400  1.000 66.77923  ? 179 GLU   A C   1 
ATOM   1153 O  O   . GLU   A 1 145 ? 32.60800  -25.81300 -5.25300  1.000 69.72916  ? 179 GLU   A O   1 
ATOM   1154 C  CB  . GLU   A 1 145 ? 35.35900  -25.12400 -3.57300  1.000 69.61827  ? 179 GLU   A CB  1 
ATOM   1155 C  CG  . GLU   A 1 145 ? 35.85000  -25.58900 -4.93400  1.000 59.67828  ? 179 GLU   A CG  1 
ATOM   1156 C  CD  . GLU   A 1 145 ? 37.32000  -25.95900 -4.92500  1.000 68.76937  ? 179 GLU   A CD  1 
ATOM   1157 O  OE1 . GLU   A 1 145 ? 37.98300  -25.74300 -3.88800  1.000 84.59946  ? 179 GLU   A OE1 1 
ATOM   1158 O  OE2 . GLU   A 1 145 ? 37.81300  -26.46700 -5.95400  1.000 78.22187  ? 179 GLU   A OE2 1 
ATOM   1159 N  N   . ASN   A 1 146 ? 32.70400  -26.84200 -3.25700  1.000 70.24222  ? 180 ASN   A N   1 
ATOM   1160 C  CA  . ASN   A 1 146 ? 31.93500  -28.00200 -3.68900  1.000 56.85986  ? 180 ASN   A CA  1 
ATOM   1161 C  C   . ASN   A 1 146 ? 30.52900  -28.03200 -3.10300  1.000 62.17014  ? 180 ASN   A C   1 
ATOM   1162 O  O   . ASN   A 1 146 ? 29.84000  -29.05100 -3.22400  1.000 65.00185  ? 180 ASN   A O   1 
ATOM   1163 C  CB  . ASN   A 1 146 ? 32.68500  -29.28700 -3.33400  1.000 65.67182  ? 180 ASN   A CB  1 
ATOM   1164 C  CG  . ASN   A 1 146 ? 33.99000  -29.42500 -4.09400  1.000 65.06175  ? 180 ASN   A CG  1 
ATOM   1165 O  OD1 . ASN   A 1 146 ? 34.04000  -29.21500 -5.30700  1.000 58.69655  ? 180 ASN   A OD1 1 
ATOM   1166 N  ND2 . ASN   A 1 146 ? 35.05700  -29.76800 -3.38300  1.000 70.53294  ? 180 ASN   A ND2 1 
ATOM   1167 N  N   . ASN   A 1 147 ? 30.08800  -26.94700 -2.47500  1.000 62.46998  ? 181 ASN   A N   1 
ATOM   1168 C  CA  . ASN   A 1 147 ? 28.71800  -26.85900 -1.99500  1.000 56.70989  ? 181 ASN   A CA  1 
ATOM   1169 C  C   . ASN   A 1 147 ? 27.78600  -26.44300 -3.12600  1.000 60.43476  ? 181 ASN   A C   1 
ATOM   1170 O  O   . ASN   A 1 147 ? 28.18600  -25.75500 -4.07000  1.000 52.85291  ? 181 ASN   A O   1 
ATOM   1171 C  CB  . ASN   A 1 147 ? 28.61100  -25.86800 -0.83600  1.000 61.37347  ? 181 ASN   A CB  1 
ATOM   1172 C  CG  . ASN   A 1 147 ? 29.31300  -26.35600 0.41600   1.000 66.36273  ? 181 ASN   A CG  1 
ATOM   1173 O  OD1 . ASN   A 1 147 ? 29.53200  -27.55600 0.59100   1.000 70.99215  ? 181 ASN   A OD1 1 
ATOM   1174 N  ND2 . ASN   A 1 147 ? 29.66200  -25.42800 1.29900   1.000 60.77966  ? 181 ASN   A ND2 1 
ATOM   1175 N  N   . VAL   A 1 148 ? 26.53400  -26.86800 -3.02200  1.000 61.90063  ? 182 VAL   A N   1 
ATOM   1176 C  CA  . VAL   A 1 148 ? 25.54000  -26.62300 -4.05900  1.000 47.92693  ? 182 VAL   A CA  1 
ATOM   1177 C  C   . VAL   A 1 148 ? 24.87200  -25.27900 -3.80700  1.000 56.76359  ? 182 VAL   A C   1 
ATOM   1178 O  O   . VAL   A 1 148 ? 24.58900  -24.90800 -2.66200  1.000 47.45033  ? 182 VAL   A O   1 
ATOM   1179 C  CB  . VAL   A 1 148 ? 24.50700  -27.76600 -4.10800  1.000 51.94528  ? 182 VAL   A CB  1 
ATOM   1180 C  CG1 . VAL   A 1 148 ? 23.52200  -27.55200 -5.24500  1.000 37.64735  ? 182 VAL   A CG1 1 
ATOM   1181 C  CG2 . VAL   A 1 148 ? 25.21100  -29.10600 -4.25800  1.000 53.57786  ? 182 VAL   A CG2 1 
ATOM   1182 N  N   . HIS   A 1 149 ? 24.62800  -24.54300 -4.88700  1.000 54.53133  ? 183 HIS   A N   1 
ATOM   1183 C  CA  . HIS   A 1 149 ? 23.96600  -23.25100 -4.85100  1.000 44.91857  ? 183 HIS   A CA  1 
ATOM   1184 C  C   . HIS   A 1 149 ? 22.76900  -23.28200 -5.79100  1.000 53.74074  ? 183 HIS   A C   1 
ATOM   1185 O  O   . HIS   A 1 149 ? 22.65300  -24.15700 -6.65300  1.000 49.67656  ? 183 HIS   A O   1 
ATOM   1186 C  CB  . HIS   A 1 149 ? 24.91600  -22.11400 -5.26000  1.000 51.07018  ? 183 HIS   A CB  1 
ATOM   1187 C  CG  . HIS   A 1 149 ? 26.13900  -22.00200 -4.40400  1.000 44.38502  ? 183 HIS   A CG  1 
ATOM   1188 N  ND1 . HIS   A 1 149 ? 27.20600  -22.86700 -4.51200  1.000 49.55379  ? 183 HIS   A ND1 1 
ATOM   1189 C  CD2 . HIS   A 1 149 ? 26.46700  -21.12000 -3.43000  1.000 55.95412  ? 183 HIS   A CD2 1 
ATOM   1190 C  CE1 . HIS   A 1 149 ? 28.13800  -22.52500 -3.64100  1.000 46.25396  ? 183 HIS   A CE1 1 
ATOM   1191 N  NE2 . HIS   A 1 149 ? 27.71500  -21.46800 -2.97100  1.000 58.68866  ? 183 HIS   A NE2 1 
ATOM   1192 N  N   . LEU   A 1 150 ? 21.87400  -22.31100 -5.61900  1.000 43.01818  ? 184 LEU   A N   1 
ATOM   1193 C  CA  . LEU   A 1 150 ? 20.68600  -22.19600 -6.45400  1.000 47.34643  ? 184 LEU   A CA  1 
ATOM   1194 C  C   . LEU   A 1 150 ? 20.58500  -20.77500 -6.98600  1.000 49.75174  ? 184 LEU   A C   1 
ATOM   1195 O  O   . LEU   A 1 150 ? 20.66500  -19.81300 -6.21600  1.000 45.98471  ? 184 LEU   A O   1 
ATOM   1196 C  CB  . LEU   A 1 150 ? 19.42000  -22.56900 -5.67500  1.000 55.61634  ? 184 LEU   A CB  1 
ATOM   1197 C  CG  . LEU   A 1 150 ? 18.13300  -22.65000 -6.49900  1.000 61.28992  ? 184 LEU   A CG  1 
ATOM   1198 C  CD1 . LEU   A 1 150 ? 18.28700  -23.64300 -7.64100  1.000 44.56730  ? 184 LEU   A CD1 1 
ATOM   1199 C  CD2 . LEU   A 1 150 ? 16.94900  -23.02100 -5.61800  1.000 53.57695  ? 184 LEU   A CD2 1 
ATOM   1200 N  N   . ILE   A 1 151 ? 20.41300  -20.64900 -8.30000  1.000 44.47673  ? 185 ILE   A N   1 
ATOM   1201 C  CA  . ILE   A 1 151 ? 20.32800  -19.36500 -8.97600  1.000 51.11370  ? 185 ILE   A CA  1 
ATOM   1202 C  C   . ILE   A 1 151 ? 19.12900  -19.38600 -9.91800  1.000 54.85362  ? 185 ILE   A C   1 
ATOM   1203 O  O   . ILE   A 1 151 ? 18.42200  -20.38500 -10.02800 1.000 51.53523  ? 185 ILE   A O   1 
ATOM   1204 C  CB  . ILE   A 1 151 ? 21.62600  -19.02100 -9.73900  1.000 45.98158  ? 185 ILE   A CB  1 
ATOM   1205 C  CG1 . ILE   A 1 151 ? 22.06900  -20.19400 -10.61800 1.000 46.35089  ? 185 ILE   A CG1 1 
ATOM   1206 C  CG2 . ILE   A 1 151 ? 22.72900  -18.65400 -8.77000  1.000 57.87073  ? 185 ILE   A CG2 1 
ATOM   1207 C  CD1 . ILE   A 1 151 ? 21.56200  -20.13400 -12.04200 1.000 53.66322  ? 185 ILE   A CD1 1 
ATOM   1208 N  N   . ASP   A 1 152 ? 18.91500  -18.26000 -10.60300 1.000 47.89918  ? 186 ASP   A N   1 
ATOM   1209 C  CA  . ASP   A 1 152 ? 17.84900  -18.10000 -11.58800 1.000 60.66158  ? 186 ASP   A CA  1 
ATOM   1210 C  C   . ASP   A 1 152 ? 16.47200  -18.31400 -10.96900 1.000 57.10032  ? 186 ASP   A C   1 
ATOM   1211 O  O   . ASP   A 1 152 ? 15.96200  -19.43900 -10.94400 1.000 51.32747  ? 186 ASP   A O   1 
ATOM   1212 C  CB  . ASP   A 1 152 ? 18.05700  -19.05800 -12.76600 1.000 57.53537  ? 186 ASP   A CB  1 
ATOM   1213 C  CG  . ASP   A 1 152 ? 17.09800  -18.79300 -13.91300 1.000 62.61935  ? 186 ASP   A CG  1 
ATOM   1214 O  OD1 . ASP   A 1 152 ? 16.36400  -17.78400 -13.86500 1.000 63.98379  ? 186 ASP   A OD1 1 
ATOM   1215 O  OD2 . ASP   A 1 152 ? 17.08100  -19.59700 -14.86800 1.000 82.54891  ? 186 ASP   A OD2 1 
ATOM   1216 N  N   . PHE   A 1 153 ? 15.85200  -17.23800 -10.48700 1.000 60.94223  ? 187 PHE   A N   1 
ATOM   1217 C  CA  . PHE   A 1 153 ? 14.52100  -17.30200 -9.89600  1.000 54.52508  ? 187 PHE   A CA  1 
ATOM   1218 C  C   . PHE   A 1 153 ? 13.47700  -16.59300 -10.75200 1.000 49.66532  ? 187 PHE   A C   1 
ATOM   1219 O  O   . PHE   A 1 153 ? 12.54600  -15.98100 -10.22600 1.000 63.51915  ? 187 PHE   A O   1 
ATOM   1220 C  CB  . PHE   A 1 153 ? 14.53900  -16.72300 -8.48300  1.000 52.38037  ? 187 PHE   A CB  1 
ATOM   1221 C  CG  . PHE   A 1 153 ? 15.35300  -17.53000 -7.51000  1.000 54.71873  ? 187 PHE   A CG  1 
ATOM   1222 C  CD1 . PHE   A 1 153 ? 16.72300  -17.34900 -7.41800  1.000 52.02756  ? 187 PHE   A CD1 1 
ATOM   1223 C  CD2 . PHE   A 1 153 ? 14.74900  -18.47300 -6.69200  1.000 51.47827  ? 187 PHE   A CD2 1 
ATOM   1224 C  CE1 . PHE   A 1 153 ? 17.47500  -18.09100 -6.52900  1.000 59.34012  ? 187 PHE   A CE1 1 
ATOM   1225 C  CE2 . PHE   A 1 153 ? 15.49700  -19.21600 -5.80000  1.000 59.64752  ? 187 PHE   A CE2 1 
ATOM   1226 C  CZ  . PHE   A 1 153 ? 16.86200  -19.02400 -5.71900  1.000 48.77730  ? 187 PHE   A CZ  1 
ATOM   1227 N  N   . GLY   A 1 154 ? 13.61800  -16.67000 -12.07700 1.000 62.05046  ? 188 GLY   A N   1 
ATOM   1228 C  CA  . GLY   A 1 154 ? 12.63300  -16.08000 -12.96400 1.000 68.81423  ? 188 GLY   A CA  1 
ATOM   1229 C  C   . GLY   A 1 154 ? 11.30000  -16.79300 -12.96100 1.000 65.02268  ? 188 GLY   A C   1 
ATOM   1230 O  O   . GLY   A 1 154 ? 10.30100  -16.22100 -13.40800 1.000 62.06154  ? 188 GLY   A O   1 
ATOM   1231 N  N   . MET   A 1 155 ? 11.26400  -18.03000 -12.47400 1.000 64.25808  ? 189 MET   A N   1 
ATOM   1232 C  CA  . MET   A 1 155 ? 10.03200  -18.79200 -12.34500 1.000 59.76281  ? 189 MET   A CA  1 
ATOM   1233 C  C   . MET   A 1 155 ? 9.53000   -18.85500 -10.91000 1.000 59.79111  ? 189 MET   A C   1 
ATOM   1234 O  O   . MET   A 1 155 ? 8.52200   -19.51800 -10.64900 1.000 63.56772  ? 189 MET   A O   1 
ATOM   1235 C  CB  . MET   A 1 155 ? 10.22900  -20.21300 -12.88500 1.000 70.17422  ? 189 MET   A CB  1 
ATOM   1236 C  CG  . MET   A 1 155 ? 10.56500  -20.27200 -14.36700 1.000 63.94698  ? 189 MET   A CG  1 
ATOM   1237 S  SD  . MET   A 1 155 ? 9.16800   -19.81100 -15.40700 1.000 93.32656  ? 189 MET   A SD  1 
ATOM   1238 C  CE  . MET   A 1 155 ? 8.93800   -21.31900 -16.34500 1.000 89.57234  ? 189 MET   A CE  1 
ATOM   1239 N  N   . ALA   A 1 156 ? 10.20800  -18.19200 -9.97700  1.000 55.56734  ? 190 ALA   A N   1 
ATOM   1240 C  CA  . ALA   A 1 156 ? 9.79900   -18.23300 -8.58000  1.000 57.27205  ? 190 ALA   A CA  1 
ATOM   1241 C  C   . ALA   A 1 156 ? 8.44200   -17.56700 -8.39700  1.000 62.68517  ? 190 ALA   A C   1 
ATOM   1242 O  O   . ALA   A 1 156 ? 8.15000   -16.53200 -9.00400  1.000 66.28424  ? 190 ALA   A O   1 
ATOM   1243 C  CB  . ALA   A 1 156 ? 10.84500  -17.55300 -7.69600  1.000 61.06732  ? 190 ALA   A CB  1 
ATOM   1244 N  N   . LYS   A 1 157 ? 7.61000   -18.16900 -7.55000  1.000 56.42211  ? 191 LYS   A N   1 
ATOM   1245 C  CA  . LYS   A 1 157 ? 6.25500   -17.69500 -7.31900  1.000 60.87482  ? 191 LYS   A CA  1 
ATOM   1246 C  C   . LYS   A 1 157 ? 5.93000   -17.79500 -5.83800  1.000 59.33858  ? 191 LYS   A C   1 
ATOM   1247 O  O   . LYS   A 1 157 ? 6.35600   -18.73500 -5.16200  1.000 72.30476  ? 191 LYS   A O   1 
ATOM   1248 C  CB  . LYS   A 1 157 ? 5.23900   -18.50300 -8.13900  1.000 64.43748  ? 191 LYS   A CB  1 
ATOM   1249 C  CG  . LYS   A 1 157 ? 3.80900   -18.00400 -8.03400  1.000 61.75300  ? 191 LYS   A CG  1 
ATOM   1250 C  CD  . LYS   A 1 157 ? 2.92200   -18.66400 -9.07400  1.000 63.64280  ? 191 LYS   A CD  1 
ATOM   1251 C  CE  . LYS   A 1 157 ? 1.57300   -17.97300 -9.16200  1.000 70.10117  ? 191 LYS   A CE  1 
ATOM   1252 N  NZ  . LYS   A 1 157 ? 0.80900   -18.41300 -10.36200 1.000 98.88972  ? 191 LYS   A NZ  1 
ATOM   1253 N  N   . GLN   A 1 158 ? 5.18200   -16.81700 -5.33800  1.000 69.06692  ? 192 GLN   A N   1 
ATOM   1254 C  CA  . GLN   A 1 158 ? 4.72500   -16.83800 -3.95500  1.000 59.70890  ? 192 GLN   A CA  1 
ATOM   1255 C  C   . GLN   A 1 158 ? 3.57600   -17.83100 -3.81900  1.000 67.15531  ? 192 GLN   A C   1 
ATOM   1256 O  O   . GLN   A 1 158 ? 2.53300   -17.67200 -4.46100  1.000 70.48729  ? 192 GLN   A O   1 
ATOM   1257 C  CB  . GLN   A 1 158 ? 4.29300   -15.43900 -3.52100  1.000 67.10352  ? 192 GLN   A CB  1 
ATOM   1258 C  CG  . GLN   A 1 158 ? 3.78100   -15.35200 -2.09700  1.000 81.71663  ? 192 GLN   A CG  1 
ATOM   1259 C  CD  . GLN   A 1 158 ? 3.43100   -13.93300 -1.68900  1.000 96.69622  ? 192 GLN   A CD  1 
ATOM   1260 O  OE1 . GLN   A 1 158 ? 2.48400   -13.70800 -0.93500  1.000 96.27465  ? 192 GLN   A OE1 1 
ATOM   1261 N  NE2 . GLN   A 1 158 ? 4.19900   -12.96900 -2.18300  1.000 99.38899  ? 192 GLN   A NE2 1 
ATOM   1262 N  N   . TYR   A 1 159 ? 3.76600   -18.85600 -2.99000  1.000 65.48859  ? 193 TYR   A N   1 
ATOM   1263 C  CA  . TYR   A 1 159 ? 2.75800   -19.89100 -2.80800  1.000 67.41400  ? 193 TYR   A CA  1 
ATOM   1264 C  C   . TYR   A 1 159 ? 1.95200   -19.73000 -1.52600  1.000 63.87470  ? 193 TYR   A C   1 
ATOM   1265 O  O   . TYR   A 1 159 ? 1.00700   -20.49500 -1.31000  1.000 66.39411  ? 193 TYR   A O   1 
ATOM   1266 C  CB  . TYR   A 1 159 ? 3.40900   -21.28100 -2.82700  1.000 60.00409  ? 193 TYR   A CB  1 
ATOM   1267 C  CG  . TYR   A 1 159 ? 4.10600   -21.65000 -1.53800  1.000 59.85204  ? 193 TYR   A CG  1 
ATOM   1268 C  CD1 . TYR   A 1 159 ? 5.39900   -21.22000 -1.27800  1.000 60.40471  ? 193 TYR   A CD1 1 
ATOM   1269 C  CD2 . TYR   A 1 159 ? 3.47000   -22.43400 -0.58300  1.000 51.61318  ? 193 TYR   A CD2 1 
ATOM   1270 C  CE1 . TYR   A 1 159 ? 6.03900   -21.55700 -0.10000  1.000 54.88490  ? 193 TYR   A CE1 1 
ATOM   1271 C  CE2 . TYR   A 1 159 ? 4.10000   -22.77200 0.59700   1.000 59.47934  ? 193 TYR   A CE2 1 
ATOM   1272 C  CZ  . TYR   A 1 159 ? 5.38500   -22.33200 0.83300   1.000 69.57266  ? 193 TYR   A CZ  1 
ATOM   1273 O  OH  . TYR   A 1 159 ? 6.01800   -22.66900 2.00800   1.000 65.10880  ? 193 TYR   A OH  1 
ATOM   1274 N  N   . ARG   A 1 160 ? 2.29900   -18.76900 -0.67400  1.000 68.35039  ? 194 ARG   A N   1 
ATOM   1275 C  CA  . ARG   A 1 160 ? 1.53800   -18.52400 0.54200   1.000 72.42822  ? 194 ARG   A CA  1 
ATOM   1276 C  C   . ARG   A 1 160 ? 1.79900   -17.09800 1.00000   1.000 75.60016  ? 194 ARG   A C   1 
ATOM   1277 O  O   . ARG   A 1 160 ? 2.86300   -16.53200 0.73400   1.000 94.96454  ? 194 ARG   A O   1 
ATOM   1278 C  CB  . ARG   A 1 160 ? 1.90000   -19.52400 1.64800   1.000 62.48012  ? 194 ARG   A CB  1 
ATOM   1279 C  CG  . ARG   A 1 160 ? 3.26700   -19.30500 2.27400   1.000 70.54065  ? 194 ARG   A CG  1 
ATOM   1280 C  CD  . ARG   A 1 160 ? 3.60900   -20.40800 3.26300   1.000 69.98904  ? 194 ARG   A CD  1 
ATOM   1281 N  NE  . ARG   A 1 160 ? 4.83900   -20.12000 3.99100   1.000 75.28645  ? 194 ARG   A NE  1 
ATOM   1282 C  CZ  . ARG   A 1 160 ? 5.49600   -20.99900 4.73600   1.000 84.36607  ? 194 ARG   A CZ  1 
ATOM   1283 N  NH1 . ARG   A 1 160 ? 5.08400   -22.25100 4.85500   1.000 83.10183  ? 194 ARG   A NH1 1 
ATOM   1284 N  NH2 . ARG   A 1 160 ? 6.59600   -20.61200 5.37500   1.000 79.92567  ? 194 ARG   A NH2 1 
ATOM   1285 N  N   . ASP   A 1 161 ? 0.81600   -16.52600 1.68900   1.000 91.74788  ? 195 ASP   A N   1 
ATOM   1286 C  CA  . ASP   A 1 161 ? 0.95400   -15.16000 2.16800   1.000 96.80482  ? 195 ASP   A CA  1 
ATOM   1287 C  C   . ASP   A 1 161 ? 2.03700   -15.08900 3.24300   1.000 95.70361  ? 195 ASP   A C   1 
ATOM   1288 O  O   . ASP   A 1 161 ? 2.09600   -15.95100 4.12500   1.000 91.30982  ? 195 ASP   A O   1 
ATOM   1289 C  CB  . ASP   A 1 161 ? -0.37100  -14.64800 2.72700   1.000 99.33380  ? 195 ASP   A CB  1 
ATOM   1290 C  CG  . ASP   A 1 161 ? -0.29700  -13.19600 3.15800   1.000 105.93886 ? 195 ASP   A CG  1 
ATOM   1291 O  OD1 . ASP   A 1 161 ? -0.42000  -12.31000 2.28700   1.000 109.04462 ? 195 ASP   A OD1 1 
ATOM   1292 O  OD2 . ASP   A 1 161 ? -0.10700  -12.94000 4.36500   1.000 108.57766 ? 195 ASP   A OD2 1 
ATOM   1293 N  N   . PRO   A 1 162 ? 2.91000   -14.07900 3.19400   1.000 93.22531  ? 196 PRO   A N   1 
ATOM   1294 C  CA  . PRO   A 1 162 ? 4.00900   -14.01400 4.17100   1.000 97.87858  ? 196 PRO   A CA  1 
ATOM   1295 C  C   . PRO   A 1 162 ? 3.55600   -13.74100 5.59400   1.000 101.53613 ? 196 PRO   A C   1 
ATOM   1296 O  O   . PRO   A 1 162 ? 4.30200   -14.05600 6.53000   1.000 104.43994 ? 196 PRO   A O   1 
ATOM   1297 C  CB  . PRO   A 1 162 ? 4.88700   -12.87000 3.63900   1.000 101.62138 ? 196 PRO   A CB  1 
ATOM   1298 C  CG  . PRO   A 1 162 ? 4.47800   -12.69300 2.20400   1.000 99.40568  ? 196 PRO   A CG  1 
ATOM   1299 C  CD  . PRO   A 1 162 ? 3.02300   -13.03500 2.16400   1.000 97.57096  ? 196 PRO   A CD  1 
ATOM   1300 N  N   . ARG   A 1 163 ? 2.36600   -13.17600 5.79300   1.000 100.01780 ? 197 ARG   A N   1 
ATOM   1301 C  CA  . ARG   A 1 163 ? 1.90100   -12.81000 7.12700   1.000 99.34745  ? 197 ARG   A CA  1 
ATOM   1302 C  C   . ARG   A 1 163 ? 1.03700   -13.89600 7.76400   1.000 104.13948 ? 197 ARG   A C   1 
ATOM   1303 O  O   . ARG   A 1 163 ? 1.32500   -14.34600 8.87700   1.000 108.23263 ? 197 ARG   A O   1 
ATOM   1304 C  CB  . ARG   A 1 163 ? 1.12700   -11.49000 7.06200   1.000 102.11874 ? 197 ARG   A CB  1 
ATOM   1305 C  CG  . ARG   A 1 163 ? 1.94900   -10.30800 6.56900   1.000 105.02542 ? 197 ARG   A CG  1 
ATOM   1306 C  CD  . ARG   A 1 163 ? 2.37300   -9.40300  7.71600   1.000 120.73822 ? 197 ARG   A CD  1 
ATOM   1307 N  NE  . ARG   A 1 163 ? 3.10000   -10.12600 8.75300   1.000 131.40881 ? 197 ARG   A NE  1 
ATOM   1308 C  CZ  . ARG   A 1 163 ? 3.56100   -9.57400  9.86600   1.000 134.59874 ? 197 ARG   A CZ  1 
ATOM   1309 N  NH1 . ARG   A 1 163 ? 3.39400   -8.28600  10.12100  1.000 116.75674 ? 197 ARG   A NH1 1 
ATOM   1310 N  NH2 . ARG   A 1 163 ? 4.20700   -10.33300 10.74800  1.000 128.45242 ? 197 ARG   A NH2 1 
ATOM   1311 N  N   . THR   A 1 164 ? -0.02400  -14.32200 7.07800   1.000 103.03664 ? 198 THR   A N   1 
ATOM   1312 C  CA  . THR   A 1 164 ? -0.96500  -15.29000 7.62900   1.000 85.00147  ? 198 THR   A CA  1 
ATOM   1313 C  C   . THR   A 1 164 ? -0.63500  -16.73300 7.26200   1.000 101.39216 ? 198 THR   A C   1 
ATOM   1314 O  O   . THR   A 1 164 ? -1.19700  -17.65200 7.87300   1.000 107.41216 ? 198 THR   A O   1 
ATOM   1315 C  CB  . THR   A 1 164 ? -2.39200  -14.94900 7.17100   1.000 99.92493  ? 198 THR   A CB  1 
ATOM   1316 O  OG1 . THR   A 1 164 ? -3.28200  -16.03200 7.47500   1.000 116.16277 ? 198 THR   A OG1 1 
ATOM   1317 C  CG2 . THR   A 1 164 ? -2.42900  -14.66500 5.67800   1.000 89.50568  ? 198 THR   A CG2 1 
ATOM   1318 N  N   . LYS   A 1 165 ? 0.27100   -16.95000 6.30500   1.000 103.81244 ? 199 LYS   A N   1 
ATOM   1319 C  CA  . LYS   A 1 165 ? 0.63000   -18.28900 5.82900   1.000 94.11750  ? 199 LYS   A CA  1 
ATOM   1320 C  C   . LYS   A 1 165 ? -0.59000  -19.01500 5.26800   1.000 107.61044 ? 199 LYS   A C   1 
ATOM   1321 O  O   . LYS   A 1 165 ? -0.84900  -20.18200 5.57100   1.000 115.13496 ? 199 LYS   A O   1 
ATOM   1322 C  CB  . LYS   A 1 165 ? 1.29600   -19.11400 6.92700   1.000 84.00132  ? 199 LYS   A CB  1 
ATOM   1323 C  CG  . LYS   A 1 165 ? 2.46000   -18.43000 7.58800   1.000 91.31475  ? 199 LYS   A CG  1 
ATOM   1324 C  CD  . LYS   A 1 165 ? 3.46100   -17.95300 6.57000   1.000 98.66178  ? 199 LYS   A CD  1 
ATOM   1325 C  CE  . LYS   A 1 165 ? 4.81700   -17.76200 7.20000   1.000 89.85216  ? 199 LYS   A CE  1 
ATOM   1326 N  NZ  . LYS   A 1 165 ? 5.83300   -17.29000 6.24200   1.000 80.77232  ? 199 LYS   A NZ  1 
ATOM   1327 N  N   . GLN   A 1 166 ? -1.34800  -18.30500 4.44100   1.000 108.47016 ? 200 GLN   A N   1 
ATOM   1328 C  CA  . GLN   A 1 166 ? -2.50900  -18.86400 3.76300   1.000 91.96127  ? 200 GLN   A CA  1 
ATOM   1329 C  C   . GLN   A 1 166 ? -2.07400  -19.35200 2.38600   1.000 88.57616  ? 200 GLN   A C   1 
ATOM   1330 O  O   . GLN   A 1 166 ? -1.67800  -18.54600 1.53900   1.000 87.48626  ? 200 GLN   A O   1 
ATOM   1331 C  CB  . GLN   A 1 166 ? -3.62800  -17.82800 3.64700   1.000 97.14978  ? 200 GLN   A CB  1 
ATOM   1332 C  CG  . GLN   A 1 166 ? -4.98700  -18.40900 3.29900   1.000 89.25064  ? 200 GLN   A CG  1 
ATOM   1333 C  CD  . GLN   A 1 166 ? -5.67300  -19.05200 4.48800   1.000 121.39386 ? 200 GLN   A CD  1 
ATOM   1334 O  OE1 . GLN   A 1 166 ? -5.26000  -18.86000 5.63300   1.000 120.39987 ? 200 GLN   A OE1 1 
ATOM   1335 N  NE2 . GLN   A 1 166 ? -6.71700  -19.83000 4.22400   1.000 104.73187 ? 200 GLN   A NE2 1 
ATOM   1336 N  N   . HIS   A 1 167 ? -2.13500  -20.66500 2.17400   1.000 67.13899  ? 201 HIS   A N   1 
ATOM   1337 C  CA  . HIS   A 1 167 ? -1.70000  -21.24300 0.91200   1.000 63.76604  ? 201 HIS   A CA  1 
ATOM   1338 C  C   . HIS   A 1 167 ? -2.51900  -20.69000 -0.24700  1.000 70.50303  ? 201 HIS   A C   1 
ATOM   1339 O  O   . HIS   A 1 167 ? -3.68500  -20.31900 -0.10000  1.000 77.03421  ? 201 HIS   A O   1 
ATOM   1340 C  CB  . HIS   A 1 167 ? -1.82300  -22.76700 0.96100   1.000 72.54087  ? 201 HIS   A CB  1 
ATOM   1341 C  CG  . HIS   A 1 167 ? -0.87100  -23.48400 0.05500   1.000 69.73686  ? 201 HIS   A CG  1 
ATOM   1342 N  ND1 . HIS   A 1 167 ? -1.04700  -23.54700 -1.31000  1.000 66.55920  ? 201 HIS   A ND1 1 
ATOM   1343 C  CD2 . HIS   A 1 167 ? 0.26700   -24.16900 0.32000   1.000 55.37848  ? 201 HIS   A CD2 1 
ATOM   1344 C  CE1 . HIS   A 1 167 ? -0.05800  -24.23900 -1.84800  1.000 55.75233  ? 201 HIS   A CE1 1 
ATOM   1345 N  NE2 . HIS   A 1 167 ? 0.75200   -24.62800 -0.88000  1.000 60.06223  ? 201 HIS   A NE2 1 
ATOM   1346 N  N   . ILE   A 1 168 ? -1.88400  -20.62500 -1.41200  1.000 62.59364  ? 202 ILE   A N   1 
ATOM   1347 C  CA  . ILE   A 1 168 ? -2.53300  -20.16600 -2.64100  1.000 67.79892  ? 202 ILE   A CA  1 
ATOM   1348 C  C   . ILE   A 1 168 ? -3.63100  -21.15400 -3.01500  1.000 70.13799  ? 202 ILE   A C   1 
ATOM   1349 O  O   . ILE   A 1 168 ? -3.47700  -22.36400 -2.79200  1.000 77.86478  ? 202 ILE   A O   1 
ATOM   1350 C  CB  . ILE   A 1 168 ? -1.52700  -19.99900 -3.79600  1.000 60.83620  ? 202 ILE   A CB  1 
ATOM   1351 C  CG1 . ILE   A 1 168 ? -0.66900  -21.25800 -3.97300  1.000 59.66887  ? 202 ILE   A CG1 1 
ATOM   1352 C  CG2 . ILE   A 1 168 ? -0.66400  -18.75800 -3.59100  1.000 64.97305  ? 202 ILE   A CG2 1 
ATOM   1353 C  CD1 . ILE   A 1 168 ? 0.22700   -21.21600 -5.21400  1.000 68.29560  ? 202 ILE   A CD1 1 
ATOM   1354 N  N   . PRO   A 1 169 ? -4.74800  -20.69100 -3.56600  1.000 72.88080  ? 203 PRO   A N   1 
ATOM   1355 C  CA  . PRO   A 1 169 ? -5.82300  -21.61500 -3.93400  1.000 75.56271  ? 203 PRO   A CA  1 
ATOM   1356 C  C   . PRO   A 1 169 ? -5.38300  -22.57300 -5.02900  1.000 76.03500  ? 203 PRO   A C   1 
ATOM   1357 O  O   . PRO   A 1 169 ? -4.54600  -22.24900 -5.87200  1.000 72.05478  ? 203 PRO   A O   1 
ATOM   1358 C  CB  . PRO   A 1 169 ? -6.94200  -20.68500 -4.42200  1.000 73.48664  ? 203 PRO   A CB  1 
ATOM   1359 C  CG  . PRO   A 1 169 ? -6.62900  -19.35500 -3.81000  1.000 74.80608  ? 203 PRO   A CG  1 
ATOM   1360 C  CD  . PRO   A 1 169 ? -5.13200  -19.28300 -3.75900  1.000 70.83702  ? 203 PRO   A CD  1 
ATOM   1361 N  N   . TYR   A 1 170 ? -5.95000  -23.77300 -4.99400  1.000 78.06647  ? 204 TYR   A N   1 
ATOM   1362 C  CA  . TYR   A 1 170 ? -5.68600  -24.76700 -6.02100  1.000 69.21151  ? 204 TYR   A CA  1 
ATOM   1363 C  C   . TYR   A 1 170 ? -6.53900  -24.47500 -7.24800  1.000 70.48960  ? 204 TYR   A C   1 
ATOM   1364 O  O   . TYR   A 1 170 ? -7.75300  -24.28500 -7.13800  1.000 83.63649  ? 204 TYR   A O   1 
ATOM   1365 C  CB  . TYR   A 1 170 ? -5.97700  -26.16800 -5.48400  1.000 64.36358  ? 204 TYR   A CB  1 
ATOM   1366 C  CG  . TYR   A 1 170 ? -5.84900  -27.27300 -6.50600  1.000 63.93844  ? 204 TYR   A CG  1 
ATOM   1367 C  CD1 . TYR   A 1 170 ? -4.61000  -27.81600 -6.81800  1.000 80.75581  ? 204 TYR   A CD1 1 
ATOM   1368 C  CD2 . TYR   A 1 170 ? -6.96900  -27.78400 -7.14900  1.000 74.92814  ? 204 TYR   A CD2 1 
ATOM   1369 C  CE1 . TYR   A 1 170 ? -4.48900  -28.82900 -7.74700  1.000 76.16767  ? 204 TYR   A CE1 1 
ATOM   1370 C  CE2 . TYR   A 1 170 ? -6.85800  -28.79800 -8.08000  1.000 69.72880  ? 204 TYR   A CE2 1 
ATOM   1371 C  CZ  . TYR   A 1 170 ? -5.61600  -29.31600 -8.37500  1.000 64.78898  ? 204 TYR   A CZ  1 
ATOM   1372 O  OH  . TYR   A 1 170 ? -5.49500  -30.32700 -9.29900  1.000 79.37510  ? 204 TYR   A OH  1 
ATOM   1373 N  N   . ARG   A 1 171 ? -5.89800  -24.42000 -8.41400  1.000 68.53047  ? 205 ARG   A N   1 
ATOM   1374 C  CA  . ARG   A 1 171 ? -6.59700  -24.25900 -9.67900  1.000 83.69731  ? 205 ARG   A CA  1 
ATOM   1375 C  C   . ARG   A 1 171 ? -5.95900  -25.18800 -10.70200 1.000 64.98759  ? 205 ARG   A C   1 
ATOM   1376 O  O   . ARG   A 1 171 ? -4.96900  -25.87500 -10.42000 1.000 78.57015  ? 205 ARG   A O   1 
ATOM   1377 C  CB  . ARG   A 1 171 ? -6.57300  -22.80200 -10.16200 1.000 79.19765  ? 205 ARG   A CB  1 
ATOM   1378 C  CG  . ARG   A 1 171 ? -5.18600  -22.27600 -10.49200 1.000 79.74677  ? 205 ARG   A CG  1 
ATOM   1379 C  CD  . ARG   A 1 171 ? -5.25700  -21.00400 -11.32500 1.000 100.99845 ? 205 ARG   A CD  1 
ATOM   1380 N  NE  . ARG   A 1 171 ? -5.37400  -21.28300 -12.75200 1.000 109.11014 ? 205 ARG   A NE  1 
ATOM   1381 C  CZ  . ARG   A 1 171 ? -5.37000  -20.35400 -13.69800 1.000 112.05069 ? 205 ARG   A CZ  1 
ATOM   1382 N  NH1 . ARG   A 1 171 ? -5.27000  -19.06800 -13.40300 1.000 116.10631 ? 205 ARG   A NH1 1 
ATOM   1383 N  NH2 . ARG   A 1 171 ? -5.46600  -20.72300 -14.97200 1.000 109.71439 ? 205 ARG   A NH2 1 
ATOM   1384 N  N   . GLU   A 1 172 ? -6.54100  -25.21700 -11.90000 1.000 79.83993  ? 206 GLU   A N   1 
ATOM   1385 C  CA  . GLU   A 1 172 ? -6.06400  -26.06700 -12.98500 1.000 70.49902  ? 206 GLU   A CA  1 
ATOM   1386 C  C   . GLU   A 1 172 ? -6.07700  -25.25800 -14.27600 1.000 88.19294  ? 206 GLU   A C   1 
ATOM   1387 O  O   . GLU   A 1 172 ? -6.27100  -24.03800 -14.27100 1.000 89.77927  ? 206 GLU   A O   1 
ATOM   1388 C  CB  . GLU   A 1 172 ? -6.91000  -27.34300 -13.09900 1.000 84.62846  ? 206 GLU   A CB  1 
ATOM   1389 C  CG  . GLU   A 1 172 ? -6.95500  -28.12600 -11.80600 1.000 89.19105  ? 206 GLU   A CG  1 
ATOM   1390 C  CD  . GLU   A 1 172 ? -7.62500  -29.47400 -11.93100 1.000 97.72496  ? 206 GLU   A CD  1 
ATOM   1391 O  OE1 . GLU   A 1 172 ? -7.97900  -29.88100 -13.06100 1.000 109.57554 ? 206 GLU   A OE1 1 
ATOM   1392 O  OE2 . GLU   A 1 172 ? -7.77800  -30.14200 -10.89300 1.000 104.20931 ? 206 GLU   A OE2 1 
ATOM   1393 N  N   . LYS   A 1 173 ? -5.87700  -25.96000 -15.39200 1.000 84.95756  ? 207 LYS   A N   1 
ATOM   1394 C  CA  . LYS   A 1 173 ? -5.86700  -25.35900 -16.72600 1.000 91.11169  ? 207 LYS   A CA  1 
ATOM   1395 C  C   . LYS   A 1 173 ? -4.84600  -24.22500 -16.81600 1.000 93.06660  ? 207 LYS   A C   1 
ATOM   1396 O  O   . LYS   A 1 173 ? -5.14400  -23.11900 -17.26900 1.000 102.02162 ? 207 LYS   A O   1 
ATOM   1397 C  CB  . LYS   A 1 173 ? -7.26600  -24.87800 -17.12600 1.000 87.28720  ? 207 LYS   A CB  1 
ATOM   1398 C  CG  . LYS   A 1 173 ? -8.28800  -25.99700 -17.25800 1.000 75.44658  ? 207 LYS   A CG  1 
ATOM   1399 C  CD  . LYS   A 1 173 ? -9.49800  -25.54400 -18.05800 1.000 86.63511  ? 207 LYS   A CD  1 
ATOM   1400 C  CE  . LYS   A 1 173 ? -10.76500 -25.58200 -17.22000 1.000 85.54909  ? 207 LYS   A CE  1 
ATOM   1401 N  NZ  . LYS   A 1 173 ? -11.96500 -25.21500 -18.01900 1.000 98.07272  ? 207 LYS   A NZ  1 
ATOM   1402 N  N   . LYS   A 1 174 ? -3.62900  -24.50800 -16.36500 1.000 92.13868  ? 208 LYS   A N   1 
ATOM   1403 C  CA  . LYS   A 1 174 ? -2.52700  -23.56400 -16.44500 1.000 99.15103  ? 208 LYS   A CA  1 
ATOM   1404 C  C   . LYS   A 1 174 ? -1.61600  -23.91400 -17.61400 1.000 105.04579 ? 208 LYS   A C   1 
ATOM   1405 O  O   . LYS   A 1 174 ? -1.49300  -25.07800 -18.00400 1.000 100.31765 ? 208 LYS   A O   1 
ATOM   1406 C  CB  . LYS   A 1 174 ? -1.71900  -23.55200 -15.14700 1.000 90.98450  ? 208 LYS   A CB  1 
ATOM   1407 C  CG  . LYS   A 1 174 ? -2.36000  -22.75800 -14.02400 1.000 92.87918  ? 208 LYS   A CG  1 
ATOM   1408 C  CD  . LYS   A 1 174 ? -1.45000  -22.70200 -12.81000 1.000 91.40262  ? 208 LYS   A CD  1 
ATOM   1409 C  CE  . LYS   A 1 174 ? -1.67200  -21.42700 -12.01600 1.000 101.98449 ? 208 LYS   A CE  1 
ATOM   1410 N  NZ  . LYS   A 1 174 ? -1.32100  -20.21100 -12.80300 1.000 108.93272 ? 208 LYS   A NZ  1 
ATOM   1411 N  N   . SER   A 1 175 ? -0.97600  -22.88800 -18.17000 1.000 108.00809 ? 209 SER   A N   1 
ATOM   1412 C  CA  . SER   A 1 175 ? -0.02200  -23.10200 -19.24900 1.000 117.24156 ? 209 SER   A CA  1 
ATOM   1413 C  C   . SER   A 1 175 ? 1.20700   -23.83600 -18.72700 1.000 118.27955 ? 209 SER   A C   1 
ATOM   1414 O  O   . SER   A 1 175 ? 1.75900   -23.48200 -17.68100 1.000 113.01005 ? 209 SER   A O   1 
ATOM   1415 C  CB  . SER   A 1 175 ? 0.38300   -21.76900 -19.87600 1.000 124.68459 ? 209 SER   A CB  1 
ATOM   1416 O  OG  . SER   A 1 175 ? 1.34300   -21.96400 -20.90100 1.000 131.42799 ? 209 SER   A OG  1 
ATOM   1417 N  N   . LEU   A 1 176 ? 1.63500   -24.86300 -19.46000 1.000 117.62073 ? 210 LEU   A N   1 
ATOM   1418 C  CA  . LEU   A 1 176 ? 2.79400   -25.66100 -19.07200 1.000 106.85299 ? 210 LEU   A CA  1 
ATOM   1419 C  C   . LEU   A 1 176 ? 4.06000   -24.81600 -19.12900 1.000 110.15587 ? 210 LEU   A C   1 
ATOM   1420 O  O   . LEU   A 1 176 ? 4.54500   -24.48600 -20.21000 1.000 109.60444 ? 210 LEU   A O   1 
ATOM   1421 C  CB  . LEU   A 1 176 ? 2.92600   -26.89400 -19.97500 1.000 98.19525  ? 210 LEU   A CB  1 
ATOM   1422 C  CG  . LEU   A 1 176 ? 2.26600   -28.19200 -19.50800 1.000 99.70270  ? 210 LEU   A CG  1 
ATOM   1423 C  CD1 . LEU   A 1 176 ? 0.77400   -28.00900 -19.25200 1.000 96.99218  ? 210 LEU   A CD1 1 
ATOM   1424 C  CD2 . LEU   A 1 176 ? 2.50000   -29.30300 -20.52200 1.000 107.10256 ? 210 LEU   A CD2 1 
ATOM   1425 N  N   . SER   A 1 177 ? 4.59900   -24.45400 -17.97400 1.000 98.97831  ? 211 SER   A N   1 
ATOM   1426 C  CA  . SER   A 1 177 ? 5.81500   -23.66100 -17.88500 1.000 106.86400 ? 211 SER   A CA  1 
ATOM   1427 C  C   . SER   A 1 177 ? 6.87100   -24.49400 -17.17700 1.000 112.43931 ? 211 SER   A C   1 
ATOM   1428 O  O   . SER   A 1 177 ? 6.64000   -24.99400 -16.07400 1.000 103.63791 ? 211 SER   A O   1 
ATOM   1429 C  CB  . SER   A 1 177 ? 5.56000   -22.34700 -17.14900 1.000 110.20430 ? 211 SER   A CB  1 
ATOM   1430 O  OG  . SER   A 1 177 ? 5.41900   -22.52700 -15.74800 1.000 107.56473 ? 211 SER   A OG  1 
ATOM   1431 N  N   . GLY   A 1 178 ? 8.02500   -24.64900 -17.81100 1.000 108.24183 ? 212 GLY   A N   1 
ATOM   1432 C  CA  . GLY   A 1 178 ? 9.10400   -25.46600 -17.29500 1.000 85.15445  ? 212 GLY   A CA  1 
ATOM   1433 C  C   . GLY   A 1 178 ? 9.64400   -26.41700 -18.34500 1.000 79.78156  ? 212 GLY   A C   1 
ATOM   1434 O  O   . GLY   A 1 178 ? 9.10700   -26.55600 -19.44600 1.000 88.45893  ? 212 GLY   A O   1 
ATOM   1435 N  N   . THR   A 1 179 ? 10.74300  -27.06800 -17.97900 1.000 85.74558  ? 213 THR   A N   1 
ATOM   1436 C  CA  . THR   A 1 179 ? 11.36800  -28.07100 -18.81800 1.000 84.26554  ? 213 THR   A CA  1 
ATOM   1437 C  C   . THR   A 1 179 ? 10.71400  -29.42300 -18.57000 1.000 61.87327  ? 213 THR   A C   1 
ATOM   1438 O  O   . THR   A 1 179 ? 10.64400  -29.89500 -17.42800 1.000 56.46137  ? 213 THR   A O   1 
ATOM   1439 C  CB  . THR   A 1 179 ? 12.86800  -28.13600 -18.54100 1.000 78.10660  ? 213 THR   A CB  1 
ATOM   1440 O  OG1 . THR   A 1 179 ? 13.09000  -28.06900 -17.12100 1.000 77.71584  ? 213 THR   A OG1 1 
ATOM   1441 C  CG2 . THR   A 1 179 ? 13.59000  -26.99400 -19.21200 1.000 79.25806  ? 213 THR   A CG2 1 
ATOM   1442 N  N   . ALA   A 1 180 ? 10.24400  -30.04200 -19.65600 1.000 67.71514  ? 214 ALA   A N   1 
ATOM   1443 C  CA  . ALA   A 1 180 ? 9.40200   -31.22800 -19.57200 1.000 57.78072  ? 214 ALA   A CA  1 
ATOM   1444 C  C   . ALA   A 1 180 ? 10.13800  -32.45000 -19.03200 1.000 55.88851  ? 214 ALA   A C   1 
ATOM   1445 O  O   . ALA   A 1 180 ? 9.48900   -33.42300 -18.63400 1.000 55.52437  ? 214 ALA   A O   1 
ATOM   1446 C  CB  . ALA   A 1 180 ? 8.82200   -31.54100 -20.95200 1.000 56.73970  ? 214 ALA   A CB  1 
ATOM   1447 N  N   . ARG   A 1 181 ? 11.47200  -32.43400 -19.01300 1.000 52.43636  ? 215 ARG   A N   1 
ATOM   1448 C  CA  . ARG   A 1 181 ? 12.20100  -33.61900 -18.58200 1.000 52.51098  ? 215 ARG   A CA  1 
ATOM   1449 C  C   . ARG   A 1 181 ? 12.11300  -33.81900 -17.07500 1.000 49.04194  ? 215 ARG   A C   1 
ATOM   1450 O  O   . ARG   A 1 181 ? 12.19700  -34.95600 -16.60100 1.000 41.32772  ? 215 ARG   A O   1 
ATOM   1451 C  CB  . ARG   A 1 181 ? 13.66200  -33.52900 -19.01900 1.000 54.06040  ? 215 ARG   A CB  1 
ATOM   1452 C  CG  . ARG   A 1 181 ? 14.44600  -34.82100 -18.80100 1.000 59.43107  ? 215 ARG   A CG  1 
ATOM   1453 C  CD  . ARG   A 1 181 ? 15.93600  -34.60900 -18.99800 1.000 60.67075  ? 215 ARG   A CD  1 
ATOM   1454 N  NE  . ARG   A 1 181 ? 16.25700  -34.20500 -20.36100 1.000 57.96494  ? 215 ARG   A NE  1 
ATOM   1455 C  CZ  . ARG   A 1 181 ? 17.47700  -33.90300 -20.78200 1.000 51.30439  ? 215 ARG   A CZ  1 
ATOM   1456 N  NH1 . ARG   A 1 181 ? 18.51900  -33.94200 -19.96700 1.000 57.57930  ? 215 ARG   A NH1 1 
ATOM   1457 N  NH2 . ARG   A 1 181 ? 17.65700  -33.55300 -22.05200 1.000 53.19621  ? 215 ARG   A NH2 1 
ATOM   1458 N  N   . TYR   A 1 182 ? 11.93500  -32.74200 -16.30900 1.000 47.27894  ? 216 TYR   A N   1 
ATOM   1459 C  CA  . TYR   A 1 182 ? 11.96000  -32.83000 -14.85700 1.000 52.21177  ? 216 TYR   A CA  1 
ATOM   1460 C  C   . TYR   A 1 182 ? 10.67200  -32.39000 -14.17800 1.000 52.56733  ? 216 TYR   A C   1 
ATOM   1461 O  O   . TYR   A 1 182 ? 10.49600  -32.68400 -12.99100 1.000 57.85727  ? 216 TYR   A O   1 
ATOM   1462 C  CB  . TYR   A 1 182 ? 13.12100  -31.99500 -14.29100 1.000 46.72400  ? 216 TYR   A CB  1 
ATOM   1463 C  CG  . TYR   A 1 182 ? 14.44300  -32.24200 -14.98000 1.000 50.82239  ? 216 TYR   A CG  1 
ATOM   1464 C  CD1 . TYR   A 1 182 ? 15.13200  -33.43300 -14.79700 1.000 51.12938  ? 216 TYR   A CD1 1 
ATOM   1465 C  CD2 . TYR   A 1 182 ? 15.00200  -31.28200 -15.81100 1.000 45.72731  ? 216 TYR   A CD2 1 
ATOM   1466 C  CE1 . TYR   A 1 182 ? 16.34000  -33.66300 -15.42600 1.000 45.12402  ? 216 TYR   A CE1 1 
ATOM   1467 C  CE2 . TYR   A 1 182 ? 16.21000  -31.50100 -16.44400 1.000 51.25275  ? 216 TYR   A CE2 1 
ATOM   1468 C  CZ  . TYR   A 1 182 ? 16.87500  -32.69400 -16.24800 1.000 45.52950  ? 216 TYR   A CZ  1 
ATOM   1469 O  OH  . TYR   A 1 182 ? 18.07800  -32.92000 -16.87600 1.000 55.10907  ? 216 TYR   A OH  1 
ATOM   1470 N  N   . MET   A 1 183 ? 9.77300   -31.70400 -14.88100 1.000 55.04475  ? 217 MET   A N   1 
ATOM   1471 C  CA  . MET   A 1 183 ? 8.58300   -31.16300 -14.24000 1.000 55.33458  ? 217 MET   A CA  1 
ATOM   1472 C  C   . MET   A 1 183 ? 7.70300   -32.28700 -13.69800 1.000 56.80529  ? 217 MET   A C   1 
ATOM   1473 O  O   . MET   A 1 183 ? 7.71100   -33.41400 -14.19900 1.000 51.87899  ? 217 MET   A O   1 
ATOM   1474 C  CB  . MET   A 1 183 ? 7.79900   -30.29100 -15.22400 1.000 47.94383  ? 217 MET   A CB  1 
ATOM   1475 C  CG  . MET   A 1 183 ? 6.83600   -31.04800 -16.12000 1.000 58.56775  ? 217 MET   A CG  1 
ATOM   1476 S  SD  . MET   A 1 183 ? 6.47500   -30.20400 -17.67500 1.000 72.57984  ? 217 MET   A SD  1 
ATOM   1477 C  CE  . MET   A 1 183 ? 6.65200   -28.48700 -17.19700 1.000 72.94199  ? 217 MET   A CE  1 
ATOM   1478 N  N   . SER   A 1 184 ? 6.95100   -31.97200 -12.64700 1.000 56.86627  ? 218 SER   A N   1 
ATOM   1479 C  CA  . SER   A 1 184 ? 6.13800   -32.97400 -11.97700 1.000 62.12085  ? 218 SER   A CA  1 
ATOM   1480 C  C   . SER   A 1 184 ? 4.96700   -33.39900 -12.86200 1.000 52.28747  ? 218 SER   A C   1 
ATOM   1481 O  O   . SER   A 1 184 ? 4.63600   -32.75500 -13.86200 1.000 54.06488  ? 218 SER   A O   1 
ATOM   1482 C  CB  . SER   A 1 184 ? 5.62000   -32.43700 -10.64300 1.000 57.32396  ? 218 SER   A CB  1 
ATOM   1483 O  OG  . SER   A 1 184 ? 4.69700   -31.38400 -10.84900 1.000 61.72470  ? 218 SER   A OG  1 
ATOM   1484 N  N   . ILE   A 1 185 ? 4.33700   -34.51100 -12.47700 1.000 50.45766  ? 219 ILE   A N   1 
ATOM   1485 C  CA  . ILE   A 1 185 ? 3.15200   -34.98200 -13.18900 1.000 61.73382  ? 219 ILE   A CA  1 
ATOM   1486 C  C   . ILE   A 1 185 ? 2.03400   -33.95100 -13.09600 1.000 60.37129  ? 219 ILE   A C   1 
ATOM   1487 O  O   . ILE   A 1 185 ? 1.30000   -33.71800 -14.06400 1.000 56.84307  ? 219 ILE   A O   1 
ATOM   1488 C  CB  . ILE   A 1 185 ? 2.70800   -36.35200 -12.64200 1.000 56.50792  ? 219 ILE   A CB  1 
ATOM   1489 C  CG1 . ILE   A 1 185 ? 3.77800   -37.41000 -12.91600 1.000 50.23333  ? 219 ILE   A CG1 1 
ATOM   1490 C  CG2 . ILE   A 1 185 ? 1.37500   -36.77100 -13.24600 1.000 54.66911  ? 219 ILE   A CG2 1 
ATOM   1491 C  CD1 . ILE   A 1 185 ? 3.41200   -38.79000 -12.42000 1.000 57.88674  ? 219 ILE   A CD1 1 
ATOM   1492 N  N   . ASN   A 1 186 ? 1.89700   -33.30800 -11.93300 1.000 51.25917  ? 220 ASN   A N   1 
ATOM   1493 C  CA  . ASN   A 1 186 ? 0.85900   -32.29800 -11.76100 1.000 58.82585  ? 220 ASN   A CA  1 
ATOM   1494 C  C   . ASN   A 1 186 ? 1.05600   -31.12100 -12.70600 1.000 56.19018  ? 220 ASN   A C   1 
ATOM   1495 O  O   . ASN   A 1 186 ? 0.07800   -30.48800 -13.12000 1.000 71.50557  ? 220 ASN   A O   1 
ATOM   1496 C  CB  . ASN   A 1 186 ? 0.83100   -31.81400 -10.31000 1.000 58.14848  ? 220 ASN   A CB  1 
ATOM   1497 C  CG  . ASN   A 1 186 ? 0.60700   -32.94300 -9.32200  1.000 70.04532  ? 220 ASN   A CG  1 
ATOM   1498 O  OD1 . ASN   A 1 186 ? -0.50800  -33.44500 -9.17800  1.000 61.81674  ? 220 ASN   A OD1 1 
ATOM   1499 N  ND2 . ASN   A 1 186 ? 1.66700   -33.34400 -8.62900  1.000 73.14452  ? 220 ASN   A ND2 1 
ATOM   1500 N  N   . THR   A 1 187 ? 2.30600   -30.81100 -13.06200 1.000 58.76476  ? 221 THR   A N   1 
ATOM   1501 C  CA  . THR   A 1 187 ? 2.55000   -29.71900 -13.99600 1.000 60.03976  ? 221 THR   A CA  1 
ATOM   1502 C  C   . THR   A 1 187 ? 2.17200   -30.10800 -15.42000 1.000 55.06661  ? 221 THR   A C   1 
ATOM   1503 O  O   . THR   A 1 187 ? 1.69500   -29.26200 -16.18600 1.000 61.41906  ? 221 THR   A O   1 
ATOM   1504 C  CB  . THR   A 1 187 ? 4.01400   -29.28400 -13.93400 1.000 58.67951  ? 221 THR   A CB  1 
ATOM   1505 O  OG1 . THR   A 1 187 ? 4.41400   -29.14700 -12.56500 1.000 64.30692  ? 221 THR   A OG1 1 
ATOM   1506 C  CG2 . THR   A 1 187 ? 4.19600   -27.94700 -14.63200 1.000 59.70801  ? 221 THR   A CG2 1 
ATOM   1507 N  N   . HIS   A 1 188 ? 2.37600   -31.37600 -15.79200 1.000 57.22143  ? 222 HIS   A N   1 
ATOM   1508 C  CA  . HIS   A 1 188 ? 1.93000   -31.84100 -17.10200 1.000 62.88332  ? 222 HIS   A CA  1 
ATOM   1509 C  C   . HIS   A 1 188 ? 0.42000   -31.72700 -17.24900 1.000 66.37500  ? 222 HIS   A C   1 
ATOM   1510 O  O   . HIS   A 1 188 ? -0.08000  -31.46700 -18.34900 1.000 59.85268  ? 222 HIS   A O   1 
ATOM   1511 C  CB  . HIS   A 1 188 ? 2.36700   -33.28900 -17.33000 1.000 61.91859  ? 222 HIS   A CB  1 
ATOM   1512 C  CG  . HIS   A 1 188 ? 3.81500   -33.44000 -17.67500 1.000 63.26475  ? 222 HIS   A CG  1 
ATOM   1513 N  ND1 . HIS   A 1 188 ? 4.29700   -33.26000 -18.95400 1.000 56.85219  ? 222 HIS   A ND1 1 
ATOM   1514 C  CD2 . HIS   A 1 188 ? 4.88500   -33.76600 -16.91200 1.000 55.40659  ? 222 HIS   A CD2 1 
ATOM   1515 C  CE1 . HIS   A 1 188 ? 5.60200   -33.46300 -18.96300 1.000 63.51517  ? 222 HIS   A CE1 1 
ATOM   1516 N  NE2 . HIS   A 1 188 ? 5.98400   -33.77200 -17.73700 1.000 50.74906  ? 222 HIS   A NE2 1 
ATOM   1517 N  N   . LEU   A 1 189 ? -0.31900  -31.91400 -16.15800 1.000 58.87011  ? 223 LEU   A N   1 
ATOM   1518 C  CA  . LEU   A 1 189 ? -1.77300  -31.85200 -16.16900 1.000 73.79437  ? 223 LEU   A CA  1 
ATOM   1519 C  C   . LEU   A 1 189 ? -2.30500  -30.43500 -15.99700 1.000 74.13258  ? 223 LEU   A C   1 
ATOM   1520 O  O   . LEU   A 1 189 ? -3.51700  -30.25600 -15.84200 1.000 77.52723  ? 223 LEU   A O   1 
ATOM   1521 C  CB  . LEU   A 1 189 ? -2.33900  -32.76100 -15.07500 1.000 73.41832  ? 223 LEU   A CB  1 
ATOM   1522 C  CG  . LEU   A 1 189 ? -1.79300  -34.19000 -15.07700 1.000 62.93475  ? 223 LEU   A CG  1 
ATOM   1523 C  CD1 . LEU   A 1 189 ? -2.34700  -34.98500 -13.90700 1.000 53.93427  ? 223 LEU   A CD1 1 
ATOM   1524 C  CD2 . LEU   A 1 189 ? -2.09900  -34.88400 -16.39700 1.000 60.85511  ? 223 LEU   A CD2 1 
ATOM   1525 N  N   . GLY   A 1 190 ? -1.43200  -29.43000 -16.02000 1.000 66.51108  ? 224 GLY   A N   1 
ATOM   1526 C  CA  . GLY   A 1 190 ? -1.87000  -28.05400 -15.90900 1.000 65.23788  ? 224 GLY   A CA  1 
ATOM   1527 C  C   . GLY   A 1 190 ? -2.33000  -27.63700 -14.53200 1.000 69.50352  ? 224 GLY   A C   1 
ATOM   1528 O  O   . GLY   A 1 190 ? -3.04500  -26.64000 -14.40500 1.000 83.74251  ? 224 GLY   A O   1 
ATOM   1529 N  N   . ARG   A 1 191 ? -1.94000  -28.36700 -13.49400 1.000 60.81566  ? 225 ARG   A N   1 
ATOM   1530 C  CA  . ARG   A 1 191 ? -2.36100  -28.04200 -12.14000 1.000 64.49755  ? 225 ARG   A CA  1 
ATOM   1531 C  C   . ARG   A 1 191 ? -1.44000  -26.99300 -11.52800 1.000 64.01795  ? 225 ARG   A C   1 
ATOM   1532 O  O   . ARG   A 1 191 ? -0.26800  -26.87300 -11.89500 1.000 68.52793  ? 225 ARG   A O   1 
ATOM   1533 C  CB  . ARG   A 1 191 ? -2.37600  -29.29800 -11.27000 1.000 57.93597  ? 225 ARG   A CB  1 
ATOM   1534 C  CG  . ARG   A 1 191 ? -3.16000  -30.45100 -11.87600 1.000 73.39830  ? 225 ARG   A CG  1 
ATOM   1535 C  CD  . ARG   A 1 191 ? -3.12300  -31.68500 -10.99000 1.000 69.22324  ? 225 ARG   A CD  1 
ATOM   1536 N  NE  . ARG   A 1 191 ? -3.88300  -32.78500 -11.57100 1.000 79.13421  ? 225 ARG   A NE  1 
ATOM   1537 C  CZ  . ARG   A 1 191 ? -4.11400  -33.94100 -10.96300 1.000 77.55170  ? 225 ARG   A CZ  1 
ATOM   1538 N  NH1 . ARG   A 1 191 ? -3.66100  -34.18400 -9.74400  1.000 77.78324  ? 225 ARG   A NH1 1 
ATOM   1539 N  NH2 . ARG   A 1 191 ? -4.81900  -34.87600 -11.59300 1.000 78.57061  ? 225 ARG   A NH2 1 
ATOM   1540 N  N   . GLU   A 1 192 ? -1.99000  -26.22400 -10.58900 1.000 69.11146  ? 226 GLU   A N   1 
ATOM   1541 C  CA  . GLU   A 1 192 ? -1.19300  -25.24100 -9.86500  1.000 69.34716  ? 226 GLU   A CA  1 
ATOM   1542 C  C   . GLU   A 1 192 ? -0.07300  -25.93500 -9.10300  1.000 58.21749  ? 226 GLU   A C   1 
ATOM   1543 O  O   . GLU   A 1 192 ? -0.29300  -26.95000 -8.43700  1.000 73.27349  ? 226 GLU   A O   1 
ATOM   1544 C  CB  . GLU   A 1 192 ? -2.07800  -24.44800 -8.90200  1.000 62.98043  ? 226 GLU   A CB  1 
ATOM   1545 C  CG  . GLU   A 1 192 ? -1.31900  -23.44800 -8.03800  1.000 64.70365  ? 226 GLU   A CG  1 
ATOM   1546 C  CD  . GLU   A 1 192 ? -1.04300  -22.13900 -8.75500  1.000 70.16164  ? 226 GLU   A CD  1 
ATOM   1547 O  OE1 . GLU   A 1 192 ? -1.96400  -21.30000 -8.83500  1.000 82.19882  ? 226 GLU   A OE1 1 
ATOM   1548 O  OE2 . GLU   A 1 192 ? 0.09200   -21.95200 -9.24400  1.000 96.31276  ? 226 GLU   A OE2 1 
ATOM   1549 N  N   . GLN   A 1 193 ? 1.13300   -25.38800 -9.20600  1.000 61.46336  ? 227 GLN   A N   1 
ATOM   1550 C  CA  . GLN   A 1 193 ? 2.29400   -25.97500 -8.55700  1.000 51.63508  ? 227 GLN   A CA  1 
ATOM   1551 C  C   . GLN   A 1 193 ? 2.42100   -25.47400 -7.12500  1.000 52.94328  ? 227 GLN   A C   1 
ATOM   1552 O  O   . GLN   A 1 193 ? 2.01600   -24.35500 -6.79700  1.000 54.74859  ? 227 GLN   A O   1 
ATOM   1553 C  CB  . GLN   A 1 193 ? 3.56800   -25.65900 -9.34100  1.000 56.09023  ? 227 GLN   A CB  1 
ATOM   1554 C  CG  . GLN   A 1 193 ? 3.56200   -26.21600 -10.75400 1.000 55.38283  ? 227 GLN   A CG  1 
ATOM   1555 C  CD  . GLN   A 1 193 ? 4.81700   -25.87000 -11.52700 1.000 53.81855  ? 227 GLN   A CD  1 
ATOM   1556 O  OE1 . GLN   A 1 193 ? 4.75000   -25.31700 -12.62400 1.000 68.03183  ? 227 GLN   A OE1 1 
ATOM   1557 N  NE2 . GLN   A 1 193 ? 5.97100   -26.20200 -10.96200 1.000 60.26166  ? 227 GLN   A NE2 1 
ATOM   1558 N  N   . SER   A 1 194 ? 2.98400   -26.32000 -6.27100  1.000 50.67029  ? 228 SER   A N   1 
ATOM   1559 C  CA  . SER   A 1 194 ? 3.17200   -25.99600 -4.86100  1.000 49.31222  ? 228 SER   A CA  1 
ATOM   1560 C  C   . SER   A 1 194 ? 4.50200   -26.59700 -4.41600  1.000 49.66187  ? 228 SER   A C   1 
ATOM   1561 O  O   . SER   A 1 194 ? 5.37000   -26.91800 -5.23400  1.000 52.55168  ? 228 SER   A O   1 
ATOM   1562 C  CB  . SER   A 1 194 ? 1.97800   -26.49100 -4.03000  1.000 58.53167  ? 228 SER   A CB  1 
ATOM   1563 O  OG  . SER   A 1 194 ? 1.78500   -27.88500 -4.19400  1.000 56.26855  ? 228 SER   A OG  1 
ATOM   1564 N  N   . ARG   A 1 195 ? 4.66800   -26.75500 -3.09900  1.000 52.19474  ? 229 ARG   A N   1 
ATOM   1565 C  CA  . ARG   A 1 195 ? 5.92600   -27.26700 -2.56400  1.000 45.60826  ? 229 ARG   A CA  1 
ATOM   1566 C  C   . ARG   A 1 195 ? 6.18700   -28.69700 -3.01900  1.000 49.42351  ? 229 ARG   A C   1 
ATOM   1567 O  O   . ARG   A 1 195 ? 7.33800   -29.07900 -3.25800  1.000 47.17950  ? 229 ARG   A O   1 
ATOM   1568 C  CB  . ARG   A 1 195 ? 5.91500   -27.18700 -1.03700  1.000 40.28389  ? 229 ARG   A CB  1 
ATOM   1569 C  CG  . ARG   A 1 195 ? 6.02100   -25.77700 -0.48600  1.000 43.05543  ? 229 ARG   A CG  1 
ATOM   1570 C  CD  . ARG   A 1 195 ? 5.89400   -25.75800 1.02800   1.000 50.33491  ? 229 ARG   A CD  1 
ATOM   1571 N  NE  . ARG   A 1 195 ? 4.51100   -25.91100 1.46200   1.000 48.68674  ? 229 ARG   A NE  1 
ATOM   1572 C  CZ  . ARG   A 1 195 ? 4.08900   -25.71000 2.70300   1.000 63.15619  ? 229 ARG   A CZ  1 
ATOM   1573 N  NH1 . ARG   A 1 195 ? 4.92200   -25.34500 3.66500   1.000 63.49331  ? 229 ARG   A NH1 1 
ATOM   1574 N  NH2 . ARG   A 1 195 ? 2.80000   -25.87300 2.98600   1.000 64.79406  ? 229 ARG   A NH2 1 
ATOM   1575 N  N   . ARG   A 1 196 ? 5.12800   -29.50200 -3.14900  1.000 51.90992  ? 230 ARG   A N   1 
ATOM   1576 C  CA  . ARG   A 1 196 ? 5.30100   -30.90300 -3.51900  1.000 50.66032  ? 230 ARG   A CA  1 
ATOM   1577 C  C   . ARG   A 1 196 ? 5.88500   -31.05300 -4.91800  1.000 51.61356  ? 230 ARG   A C   1 
ATOM   1578 O  O   . ARG   A 1 196 ? 6.55300   -32.05300 -5.20800  1.000 47.61306  ? 230 ARG   A O   1 
ATOM   1579 C  CB  . ARG   A 1 196 ? 3.96300   -31.63700 -3.42700  1.000 52.49154  ? 230 ARG   A CB  1 
ATOM   1580 C  CG  . ARG   A 1 196 ? 2.91800   -31.13100 -4.41000  1.000 55.09025  ? 230 ARG   A CG  1 
ATOM   1581 C  CD  . ARG   A 1 196 ? 1.60500   -31.88000 -4.27400  1.000 59.69119  ? 230 ARG   A CD  1 
ATOM   1582 N  NE  . ARG   A 1 196 ? 0.61500   -31.41500 -5.23800  1.000 56.91525  ? 230 ARG   A NE  1 
ATOM   1583 C  CZ  . ARG   A 1 196 ? -0.63400  -31.85500 -5.30400  1.000 65.87513  ? 230 ARG   A CZ  1 
ATOM   1584 N  NH1 . ARG   A 1 196 ? -1.08700  -32.77600 -4.46900  1.000 50.80018  ? 230 ARG   A NH1 1 
ATOM   1585 N  NH2 . ARG   A 1 196 ? -1.45000  -31.35900 -6.22900  1.000 62.91377  ? 230 ARG   A NH2 1 
ATOM   1586 N  N   . ASP   A 1 197 ? 5.65200   -30.07600 -5.79500  1.000 51.22807  ? 231 ASP   A N   1 
ATOM   1587 C  CA  . ASP   A 1 197 ? 6.10200   -30.19700 -7.17600  1.000 43.98408  ? 231 ASP   A CA  1 
ATOM   1588 C  C   . ASP   A 1 197 ? 7.57700   -29.85100 -7.33200  1.000 50.85620  ? 231 ASP   A C   1 
ATOM   1589 O  O   . ASP   A 1 197 ? 8.22700   -30.34400 -8.26100  1.000 49.05048  ? 231 ASP   A O   1 
ATOM   1590 C  CB  . ASP   A 1 197 ? 5.24200   -29.31400 -8.07900  1.000 44.32143  ? 231 ASP   A CB  1 
ATOM   1591 C  CG  . ASP   A 1 197 ? 3.78600   -29.73300 -8.07400  1.000 54.05073  ? 231 ASP   A CG  1 
ATOM   1592 O  OD1 . ASP   A 1 197 ? 3.49700   -30.89700 -8.42200  1.000 57.59907  ? 231 ASP   A OD1 1 
ATOM   1593 O  OD2 . ASP   A 1 197 ? 2.93000   -28.90800 -7.69900  1.000 64.05698  ? 231 ASP   A OD2 1 
ATOM   1594 N  N   . ASP   A 1 198 ? 8.12000   -29.01200 -6.44800  1.000 47.64315  ? 232 ASP   A N   1 
ATOM   1595 C  CA  . ASP   A 1 198 ? 9.56100   -28.78700 -6.45000  1.000 48.28708  ? 232 ASP   A CA  1 
ATOM   1596 C  C   . ASP   A 1 198 ? 10.31500  -30.03700 -6.02000  1.000 50.68438  ? 232 ASP   A C   1 
ATOM   1597 O  O   . ASP   A 1 198 ? 11.44100  -30.26900 -6.47700  1.000 46.47019  ? 232 ASP   A O   1 
ATOM   1598 C  CB  . ASP   A 1 198 ? 9.92000   -27.61700 -5.53400  1.000 43.28471  ? 232 ASP   A CB  1 
ATOM   1599 C  CG  . ASP   A 1 198 ? 9.53300   -26.27700 -6.12300  1.000 42.71395  ? 232 ASP   A CG  1 
ATOM   1600 O  OD1 . ASP   A 1 198 ? 9.45600   -26.17200 -7.36300  1.000 42.93190  ? 232 ASP   A OD1 1 
ATOM   1601 O  OD2 . ASP   A 1 198 ? 9.31100   -25.32800 -5.34600  1.000 47.02292  ? 232 ASP   A OD2 1 
ATOM   1602 N  N   . LEU   A 1 199 ? 9.71200   -30.85400 -5.15500  1.000 48.83097  ? 233 LEU   A N   1 
ATOM   1603 C  CA  . LEU   A 1 199 ? 10.38500  -32.04700 -4.66000  1.000 44.31727  ? 233 LEU   A CA  1 
ATOM   1604 C  C   . LEU   A 1 199 ? 10.24400  -33.22500 -5.61500  1.000 44.03377  ? 233 LEU   A C   1 
ATOM   1605 O  O   . LEU   A 1 199 ? 11.16800  -34.03700 -5.72600  1.000 50.66867  ? 233 LEU   A O   1 
ATOM   1606 C  CB  . LEU   A 1 199 ? 9.84700   -32.42000 -3.27900  1.000 40.09501  ? 233 LEU   A CB  1 
ATOM   1607 C  CG  . LEU   A 1 199 ? 9.95400   -31.34000 -2.20000  1.000 49.34719  ? 233 LEU   A CG  1 
ATOM   1608 C  CD1 . LEU   A 1 199 ? 9.74800   -31.95200 -0.83100  1.000 56.65849  ? 233 LEU   A CD1 1 
ATOM   1609 C  CD2 . LEU   A 1 199 ? 11.29200  -30.61600 -2.26700  1.000 53.85745  ? 233 LEU   A CD2 1 
ATOM   1610 N  N   . GLU   A 1 200 ? 9.10400   -33.34300 -6.30100  1.000 47.18265  ? 234 GLU   A N   1 
ATOM   1611 C  CA  . GLU   A 1 200 ? 8.97600   -34.37900 -7.32000  1.000 50.80111  ? 234 GLU   A CA  1 
ATOM   1612 C  C   . GLU   A 1 200 ? 9.93100   -34.12000 -8.47700  1.000 49.81586  ? 234 GLU   A C   1 
ATOM   1613 O  O   . GLU   A 1 200 ? 10.49600  -35.06100 -9.04800  1.000 51.42210  ? 234 GLU   A O   1 
ATOM   1614 C  CB  . GLU   A 1 200 ? 7.53400   -34.46100 -7.82100  1.000 40.53488  ? 234 GLU   A CB  1 
ATOM   1615 C  CG  . GLU   A 1 200 ? 7.33500   -35.48200 -8.93000  1.000 53.86117  ? 234 GLU   A CG  1 
ATOM   1616 C  CD  . GLU   A 1 200 ? 5.88500   -35.63600 -9.33800  1.000 53.86319  ? 234 GLU   A CD  1 
ATOM   1617 O  OE1 . GLU   A 1 200 ? 5.00700   -35.08500 -8.64200  1.000 70.50003  ? 234 GLU   A OE1 1 
ATOM   1618 O  OE2 . GLU   A 1 200 ? 5.62300   -36.31200 -10.35600 1.000 48.43781  ? 234 GLU   A OE2 1 
ATOM   1619 N  N   . ALA   A 1 201 ? 10.12700  -32.84900 -8.83200  1.000 55.47600  ? 235 ALA   A N   1 
ATOM   1620 C  CA  . ALA   A 1 201 ? 11.10700  -32.51500 -9.85900  1.000 56.96037  ? 235 ALA   A CA  1 
ATOM   1621 C  C   . ALA   A 1 201 ? 12.51600  -32.87600 -9.40800  1.000 47.62511  ? 235 ALA   A C   1 
ATOM   1622 O  O   . ALA   A 1 201 ? 13.33700  -33.32900 -10.21300 1.000 50.94578  ? 235 ALA   A O   1 
ATOM   1623 C  CB  . ALA   A 1 201 ? 11.01400  -31.03100 -10.20900 1.000 46.67145  ? 235 ALA   A CB  1 
ATOM   1624 N  N   . LEU   A 1 202 ? 12.81300  -32.68500 -8.11900  1.000 41.58415  ? 236 LEU   A N   1 
ATOM   1625 C  CA  . LEU   A 1 202 ? 14.10300  -33.11200 -7.58600  1.000 44.40573  ? 236 LEU   A CA  1 
ATOM   1626 C  C   . LEU   A 1 202 ? 14.26700  -34.62300 -7.69200  1.000 52.60083  ? 236 LEU   A C   1 
ATOM   1627 O  O   . LEU   A 1 202 ? 15.34700  -35.11500 -8.04000  1.000 40.78255  ? 236 LEU   A O   1 
ATOM   1628 C  CB  . LEU   A 1 202 ? 14.25000  -32.66300 -6.13100  1.000 41.35481  ? 236 LEU   A CB  1 
ATOM   1629 C  CG  . LEU   A 1 202 ? 14.66300  -31.21500 -5.86400  1.000 49.29057  ? 236 LEU   A CG  1 
ATOM   1630 C  CD1 . LEU   A 1 202 ? 14.74700  -30.96800 -4.36800  1.000 48.08575  ? 236 LEU   A CD1 1 
ATOM   1631 C  CD2 . LEU   A 1 202 ? 15.99200  -30.90300 -6.53300  1.000 40.75095  ? 236 LEU   A CD2 1 
ATOM   1632 N  N   . GLY   A 1 203 ? 13.20300  -35.37500 -7.39600  1.000 46.03578  ? 237 GLY   A N   1 
ATOM   1633 C  CA  . GLY   A 1 203 ? 13.26500  -36.82100 -7.53500  1.000 37.05850  ? 237 GLY   A CA  1 
ATOM   1634 C  C   . GLY   A 1 203 ? 13.54700  -37.26500 -8.95800  1.000 45.40316  ? 237 GLY   A C   1 
ATOM   1635 O  O   . GLY   A 1 203 ? 14.24300  -38.26100 -9.17500  1.000 45.89845  ? 237 GLY   A O   1 
ATOM   1636 N  N   . HIS   A 1 204 ? 13.01500  -36.53900 -9.94500  1.000 37.54576  ? 238 HIS   A N   1 
ATOM   1637 C  CA  . HIS   A 1 204 ? 13.33800  -36.84200 -11.33600 1.000 38.24511  ? 238 HIS   A CA  1 
ATOM   1638 C  C   . HIS   A 1 204 ? 14.80500  -36.56200 -11.63100 1.000 50.40042  ? 238 HIS   A C   1 
ATOM   1639 O  O   . HIS   A 1 204 ? 15.44000  -37.29000 -12.40400 1.000 49.47018  ? 238 HIS   A O   1 
ATOM   1640 C  CB  . HIS   A 1 204 ? 12.44200  -36.03600 -12.27300 1.000 49.11296  ? 238 HIS   A CB  1 
ATOM   1641 C  CG  . HIS   A 1 204 ? 10.99300  -36.40300 -12.18800 1.000 62.63018  ? 238 HIS   A CG  1 
ATOM   1642 N  ND1 . HIS   A 1 204 ? 9.98800   -35.56200 -12.61200 1.000 48.94144  ? 238 HIS   A ND1 1 
ATOM   1643 C  CD2 . HIS   A 1 204 ? 10.38100  -37.52400 -11.73700 1.000 49.82628  ? 238 HIS   A CD2 1 
ATOM   1644 C  CE1 . HIS   A 1 204 ? 8.81800   -36.14600 -12.42100 1.000 64.57096  ? 238 HIS   A CE1 1 
ATOM   1645 N  NE2 . HIS   A 1 204 ? 9.02900   -37.33700 -11.89100 1.000 50.05417  ? 238 HIS   A NE2 1 
ATOM   1646 N  N   . VAL   A 1 205 ? 15.35700  -35.50600 -11.03000 1.000 44.22194  ? 239 VAL   A N   1 
ATOM   1647 C  CA  . VAL   A 1 205 ? 16.76700  -35.19200 -11.23100 1.000 45.83691  ? 239 VAL   A CA  1 
ATOM   1648 C  C   . VAL   A 1 205 ? 17.64700  -36.25000 -10.57800 1.000 40.99964  ? 239 VAL   A C   1 
ATOM   1649 O  O   . VAL   A 1 205 ? 18.72600  -36.57900 -11.08600 1.000 48.63307  ? 239 VAL   A O   1 
ATOM   1650 C  CB  . VAL   A 1 205 ? 17.08100  -33.78100 -10.70000 1.000 40.23265  ? 239 VAL   A CB  1 
ATOM   1651 C  CG1 . VAL   A 1 205 ? 18.55200  -33.45800 -10.87500 1.000 36.51628  ? 239 VAL   A CG1 1 
ATOM   1652 C  CG2 . VAL   A 1 205 ? 16.22700  -32.74500 -11.40900 1.000 35.87738  ? 239 VAL   A CG2 1 
ATOM   1653 N  N   . PHE   A 1 206 ? 17.20200  -36.80700 -9.45000  1.000 45.63804  ? 240 PHE   A N   1 
ATOM   1654 C  CA  . PHE   A 1 206 ? 17.99900  -37.81900 -8.76400  1.000 38.85505  ? 240 PHE   A CA  1 
ATOM   1655 C  C   . PHE   A 1 206 ? 18.12500  -39.08000 -9.61100  1.000 41.30342  ? 240 PHE   A C   1 
ATOM   1656 O  O   . PHE   A 1 206 ? 19.22300  -39.62500 -9.77200  1.000 49.82355  ? 240 PHE   A O   1 
ATOM   1657 C  CB  . PHE   A 1 206 ? 17.38600  -38.14200 -7.39900  1.000 46.28669  ? 240 PHE   A CB  1 
ATOM   1658 C  CG  . PHE   A 1 206 ? 17.26200  -36.95200 -6.48600  1.000 40.25337  ? 240 PHE   A CG  1 
ATOM   1659 C  CD1 . PHE   A 1 206 ? 18.07000  -35.83700 -6.65300  1.000 39.64974  ? 240 PHE   A CD1 1 
ATOM   1660 C  CD2 . PHE   A 1 206 ? 16.33300  -36.95000 -5.45900  1.000 33.31839  ? 240 PHE   A CD2 1 
ATOM   1661 C  CE1 . PHE   A 1 206 ? 17.94900  -34.74200 -5.81600  1.000 35.85046  ? 240 PHE   A CE1 1 
ATOM   1662 C  CE2 . PHE   A 1 206 ? 16.21000  -35.86200 -4.61700  1.000 46.27182  ? 240 PHE   A CE2 1 
ATOM   1663 C  CZ  . PHE   A 1 206 ? 17.01800  -34.75600 -4.79600  1.000 44.57577  ? 240 PHE   A CZ  1 
ATOM   1664 N  N   . PHE   A 1 207 ? 17.00600  -39.56000 -10.16300 1.000 49.33473  ? 241 PHE   A N   1 
ATOM   1665 C  CA  . PHE   A 1 207 ? 17.06300  -40.69100 -11.08300 1.000 46.55172  ? 241 PHE   A CA  1 
ATOM   1666 C  C   . PHE   A 1 207 ? 17.82400  -40.33900 -12.35200 1.000 39.60014  ? 241 PHE   A C   1 
ATOM   1667 O  O   . PHE   A 1 207 ? 18.49400  -41.20100 -12.93300 1.000 47.56758  ? 241 PHE   A O   1 
ATOM   1668 C  CB  . PHE   A 1 207 ? 15.65200  -41.16300 -11.43200 1.000 46.05285  ? 241 PHE   A CB  1 
ATOM   1669 C  CG  . PHE   A 1 207 ? 14.96300  -41.89700 -10.31900 1.000 47.57586  ? 241 PHE   A CG  1 
ATOM   1670 C  CD1 . PHE   A 1 207 ? 15.33300  -43.19200 -9.99400  1.000 52.02528  ? 241 PHE   A CD1 1 
ATOM   1671 C  CD2 . PHE   A 1 207 ? 13.93500  -41.30000 -9.60700  1.000 60.47756  ? 241 PHE   A CD2 1 
ATOM   1672 C  CE1 . PHE   A 1 207 ? 14.69800  -43.87200 -8.97300  1.000 58.39700  ? 241 PHE   A CE1 1 
ATOM   1673 C  CE2 . PHE   A 1 207 ? 13.29700  -41.97700 -8.58500  1.000 50.62585  ? 241 PHE   A CE2 1 
ATOM   1674 C  CZ  . PHE   A 1 207 ? 13.67900  -43.26400 -8.26900  1.000 59.56606  ? 241 PHE   A CZ  1 
ATOM   1675 N  N   . TYR   A 1 208 ? 17.72300  -39.08600 -12.79800 1.000 44.17179  ? 242 TYR   A N   1 
ATOM   1676 C  CA  . TYR   A 1 208 ? 18.50000  -38.63200 -13.94700 1.000 49.99070  ? 242 TYR   A CA  1 
ATOM   1677 C  C   . TYR   A 1 208 ? 19.99500  -38.75200 -13.67900 1.000 42.84019  ? 242 TYR   A C   1 
ATOM   1678 O  O   . TYR   A 1 208 ? 20.75600  -39.20000 -14.54400 1.000 46.35389  ? 242 TYR   A O   1 
ATOM   1679 C  CB  . TYR   A 1 208 ? 18.11000  -37.19000 -14.27900 1.000 39.46545  ? 242 TYR   A CB  1 
ATOM   1680 C  CG  . TYR   A 1 208 ? 18.98800  -36.47400 -15.28100 1.000 49.84103  ? 242 TYR   A CG  1 
ATOM   1681 C  CD1 . TYR   A 1 208 ? 18.84800  -36.69700 -16.64500 1.000 49.45867  ? 242 TYR   A CD1 1 
ATOM   1682 C  CD2 . TYR   A 1 208 ? 19.93000  -35.54300 -14.86300 1.000 39.54072  ? 242 TYR   A CD2 1 
ATOM   1683 C  CE1 . TYR   A 1 208 ? 19.63800  -36.02900 -17.56200 1.000 48.70401  ? 242 TYR   A CE1 1 
ATOM   1684 C  CE2 . TYR   A 1 208 ? 20.72300  -34.87000 -15.77200 1.000 41.40666  ? 242 TYR   A CE2 1 
ATOM   1685 C  CZ  . TYR   A 1 208 ? 20.57300  -35.11700 -17.11900 1.000 48.63296  ? 242 TYR   A CZ  1 
ATOM   1686 O  OH  . TYR   A 1 208 ? 21.35900  -34.44800 -18.02500 1.000 42.35464  ? 242 TYR   A OH  1 
ATOM   1687 N  N   . PHE   A 1 209 ? 20.43000  -38.37000 -12.47600 1.000 44.86374  ? 243 PHE   A N   1 
ATOM   1688 C  CA  . PHE   A 1 209 ? 21.83900  -38.49700 -12.11800 1.000 43.63160  ? 243 PHE   A CA  1 
ATOM   1689 C  C   . PHE   A 1 209 ? 22.24800  -39.95800 -11.97600 1.000 42.53701  ? 243 PHE   A C   1 
ATOM   1690 O  O   . PHE   A 1 209 ? 23.34200  -40.34700 -12.40100 1.000 44.84050  ? 243 PHE   A O   1 
ATOM   1691 C  CB  . PHE   A 1 209 ? 22.12100  -37.74500 -10.81700 1.000 42.65825  ? 243 PHE   A CB  1 
ATOM   1692 C  CG  . PHE   A 1 209 ? 22.10500  -36.24900 -10.95500 1.000 43.85991  ? 243 PHE   A CG  1 
ATOM   1693 C  CD1 . PHE   A 1 209 ? 22.28200  -35.64600 -12.19000 1.000 35.40602  ? 243 PHE   A CD1 1 
ATOM   1694 C  CD2 . PHE   A 1 209 ? 21.92600  -35.44500 -9.84100  1.000 36.39115  ? 243 PHE   A CD2 1 
ATOM   1695 C  CE1 . PHE   A 1 209 ? 22.27300  -34.27200 -12.31100 1.000 37.78213  ? 243 PHE   A CE1 1 
ATOM   1696 C  CE2 . PHE   A 1 209 ? 21.91700  -34.06700 -9.95600  1.000 30.60288  ? 243 PHE   A CE2 1 
ATOM   1697 C  CZ  . PHE   A 1 209 ? 22.09100  -33.48100 -11.19100 1.000 42.78352  ? 243 PHE   A CZ  1 
ATOM   1698 N  N   . LEU   A 1 210 ? 21.38100  -40.78400 -11.38400 1.000 44.32083  ? 244 LEU   A N   1 
ATOM   1699 C  CA  . LEU   A 1 210 ? 21.75700  -42.15900 -11.07200 1.000 41.78831  ? 244 LEU   A CA  1 
ATOM   1700 C  C   . LEU   A 1 210 ? 21.80800  -43.02600 -12.32300 1.000 41.03096  ? 244 LEU   A C   1 
ATOM   1701 O  O   . LEU   A 1 210 ? 22.73500  -43.82500 -12.49300 1.000 46.14889  ? 244 LEU   A O   1 
ATOM   1702 C  CB  . LEU   A 1 210 ? 20.78200  -42.74500 -10.05300 1.000 44.67343  ? 244 LEU   A CB  1 
ATOM   1703 C  CG  . LEU   A 1 210 ? 20.88700  -42.22200 -8.62000  1.000 50.40140  ? 244 LEU   A CG  1 
ATOM   1704 C  CD1 . LEU   A 1 210 ? 19.67300  -42.64400 -7.81000  1.000 49.31610  ? 244 LEU   A CD1 1 
ATOM   1705 C  CD2 . LEU   A 1 210 ? 22.16500  -42.72200 -7.96600  1.000 39.87403  ? 244 LEU   A CD2 1 
ATOM   1706 N  N   . ARG   A 1 211 ? 20.82000  -42.89000 -13.20500 1.000 51.71592  ? 245 ARG   A N   1 
ATOM   1707 C  CA  . ARG   A 1 211 ? 20.73300  -43.73000 -14.39300 1.000 66.62829  ? 245 ARG   A CA  1 
ATOM   1708 C  C   . ARG   A 1 211 ? 21.52300  -43.18300 -15.57200 1.000 50.62783  ? 245 ARG   A C   1 
ATOM   1709 O  O   . ARG   A 1 211 ? 21.95600  -43.95900 -16.43200 1.000 68.23855  ? 245 ARG   A O   1 
ATOM   1710 C  CB  . ARG   A 1 211 ? 19.27100  -43.89700 -14.81400 1.000 48.39119  ? 245 ARG   A CB  1 
ATOM   1711 C  CG  . ARG   A 1 211 ? 18.39800  -44.63600 -13.81600 1.000 50.84260  ? 245 ARG   A CG  1 
ATOM   1712 C  CD  . ARG   A 1 211 ? 16.92900  -44.42400 -14.14900 1.000 61.33635  ? 245 ARG   A CD  1 
ATOM   1713 N  NE  . ARG   A 1 211 ? 16.69000  -44.50100 -15.58600 1.000 61.79870  ? 245 ARG   A NE  1 
ATOM   1714 C  CZ  . ARG   A 1 211 ? 16.04600  -45.49000 -16.19000 1.000 57.32265  ? 245 ARG   A CZ  1 
ATOM   1715 N  NH1 . ARG   A 1 211 ? 15.51700  -46.49000 -15.50500 1.000 63.08415  ? 245 ARG   A NH1 1 
ATOM   1716 N  NH2 . ARG   A 1 211 ? 15.92300  -45.47100 -17.51400 1.000 53.89555  ? 245 ARG   A NH2 1 
ATOM   1717 N  N   . GLY   A 1 212 ? 21.71800  -41.86800 -15.63500 1.000 44.88619  ? 246 GLY   A N   1 
ATOM   1718 C  CA  . GLY   A 1 212 ? 22.26800  -41.22600 -16.80300 1.000 44.32271  ? 246 GLY   A CA  1 
ATOM   1719 C  C   . GLY   A 1 212 ? 21.23300  -40.73400 -17.79100 1.000 51.72302  ? 246 GLY   A C   1 
ATOM   1720 O  O   . GLY   A 1 212 ? 21.54300  -39.86300 -18.61200 1.000 55.74470  ? 246 GLY   A O   1 
ATOM   1721 N  N   . GLN   A 1 213 ? 20.01500  -41.26600 -17.73500 1.000 54.53535  ? 247 GLN   A N   1 
ATOM   1722 C  CA  . GLN   A 1 213 ? 18.92500  -40.79400 -18.57500 1.000 48.51511  ? 247 GLN   A CA  1 
ATOM   1723 C  C   . GLN   A 1 213 ? 17.60700  -41.16100 -17.91200 1.000 53.75737  ? 247 GLN   A C   1 
ATOM   1724 O  O   . GLN   A 1 213 ? 17.55900  -41.97700 -16.98800 1.000 59.04744  ? 247 GLN   A O   1 
ATOM   1725 C  CB  . GLN   A 1 213 ? 18.98500  -41.38700 -19.98600 1.000 46.99433  ? 247 GLN   A CB  1 
ATOM   1726 C  CG  . GLN   A 1 213 ? 18.43700  -42.80400 -20.07600 1.000 73.14028  ? 247 GLN   A CG  1 
ATOM   1727 C  CD  . GLN   A 1 213 ? 17.91600  -43.14600 -21.45900 1.000 87.24434  ? 247 GLN   A CD  1 
ATOM   1728 O  OE1 . GLN   A 1 213 ? 18.36600  -42.58900 -22.46100 1.000 76.60105  ? 247 GLN   A OE1 1 
ATOM   1729 N  NE2 . GLN   A 1 213 ? 16.95400  -44.06100 -21.52000 1.000 71.30229  ? 247 GLN   A NE2 1 
ATOM   1730 N  N   . LEU   A 1 214 ? 16.54100  -40.54200 -18.39800 1.000 62.65070  ? 248 LEU   A N   1 
ATOM   1731 C  CA  . LEU   A 1 214 ? 15.19000  -40.86800 -17.98900 1.000 52.77798  ? 248 LEU   A CA  1 
ATOM   1732 C  C   . LEU   A 1 214 ? 14.44300  -41.52700 -19.14400 1.000 53.58579  ? 248 LEU   A C   1 
ATOM   1733 O  O   . LEU   A 1 214 ? 14.67400  -41.19100 -20.31000 1.000 52.30069  ? 248 LEU   A O   1 
ATOM   1734 C  CB  . LEU   A 1 214 ? 14.43400  -39.61500 -17.53000 1.000 40.92255  ? 248 LEU   A CB  1 
ATOM   1735 C  CG  . LEU   A 1 214 ? 14.95700  -38.98400 -16.23800 1.000 42.12349  ? 248 LEU   A CG  1 
ATOM   1736 C  CD1 . LEU   A 1 214 ? 14.36200  -37.60300 -16.02500 1.000 47.41311  ? 248 LEU   A CD1 1 
ATOM   1737 C  CD2 . LEU   A 1 214 ? 14.65700  -39.88400 -15.04900 1.000 37.29395  ? 248 LEU   A CD2 1 
ATOM   1738 N  N   . PRO   A 1 215 ? 13.54400  -42.47400 -18.85700 1.000 49.93853  ? 249 PRO   A N   1 
ATOM   1739 C  CA  . PRO   A 1 215 ? 12.86900  -43.20600 -19.94100 1.000 53.51606  ? 249 PRO   A CA  1 
ATOM   1740 C  C   . PRO   A 1 215 ? 11.93700  -42.35000 -20.78300 1.000 60.02478  ? 249 PRO   A C   1 
ATOM   1741 O  O   . PRO   A 1 215 ? 11.45200  -42.83600 -21.81300 1.000 74.49722  ? 249 PRO   A O   1 
ATOM   1742 C  CB  . PRO   A 1 215 ? 12.09300  -44.30000 -19.19600 1.000 53.10343  ? 249 PRO   A CB  1 
ATOM   1743 C  CG  . PRO   A 1 215 ? 11.89400  -43.74900 -17.82600 1.000 49.28774  ? 249 PRO   A CG  1 
ATOM   1744 C  CD  . PRO   A 1 215 ? 13.12700  -42.94800 -17.52800 1.000 50.09753  ? 249 PRO   A CD  1 
ATOM   1745 N  N   . TRP   A 1 216 ? 11.66800  -41.10600 -20.39000 1.000 52.37441  ? 250 TRP   A N   1 
ATOM   1746 C  CA  . TRP   A 1 216 ? 10.84300  -40.20400 -21.18200 1.000 61.53798  ? 250 TRP   A CA  1 
ATOM   1747 C  C   . TRP   A 1 216 ? 11.67100  -39.18000 -21.95300 1.000 63.20952  ? 250 TRP   A C   1 
ATOM   1748 O  O   . TRP   A 1 216 ? 11.13500  -38.15100 -22.37700 1.000 67.93691  ? 250 TRP   A O   1 
ATOM   1749 C  CB  . TRP   A 1 216 ? 9.81700   -39.50200 -20.29300 1.000 58.31378  ? 250 TRP   A CB  1 
ATOM   1750 C  CG  . TRP   A 1 216 ? 10.37900  -38.95300 -19.02000 1.000 46.21537  ? 250 TRP   A CG  1 
ATOM   1751 C  CD1 . TRP   A 1 216 ? 11.05300  -37.77800 -18.86100 1.000 45.35467  ? 250 TRP   A CD1 1 
ATOM   1752 C  CD2 . TRP   A 1 216 ? 10.30100  -39.55100 -17.72100 1.000 44.70652  ? 250 TRP   A CD2 1 
ATOM   1753 N  NE1 . TRP   A 1 216 ? 11.40600  -37.61000 -17.54400 1.000 44.32503  ? 250 TRP   A NE1 1 
ATOM   1754 C  CE2 . TRP   A 1 216 ? 10.95600  -38.68500 -16.82300 1.000 38.54920  ? 250 TRP   A CE2 1 
ATOM   1755 C  CE3 . TRP   A 1 216 ? 9.74500   -40.73700 -17.23000 1.000 53.05280  ? 250 TRP   A CE3 1 
ATOM   1756 C  CZ2 . TRP   A 1 216 ? 11.06900  -38.96600 -15.46300 1.000 40.93305  ? 250 TRP   A CZ2 1 
ATOM   1757 C  CZ3 . TRP   A 1 216 ? 9.85800   -41.01400 -15.87900 1.000 41.04723  ? 250 TRP   A CZ3 1 
ATOM   1758 C  CH2 . TRP   A 1 216 ? 10.51500  -40.13300 -15.01200 1.000 54.87996  ? 250 TRP   A CH2 1 
ATOM   1759 N  N   . GLN   A 1 217 ? 12.96000  -39.44100 -22.14400 1.000 65.08377  ? 251 GLN   A N   1 
ATOM   1760 C  CA  . GLN   A 1 217 ? 13.80200  -38.59500 -22.97500 1.000 69.11843  ? 251 GLN   A CA  1 
ATOM   1761 C  C   . GLN   A 1 217 ? 13.80100  -39.09800 -24.41400 1.000 75.48108  ? 251 GLN   A C   1 
ATOM   1762 O  O   . GLN   A 1 217 ? 13.55300  -40.27400 -24.69000 1.000 72.23477  ? 251 GLN   A O   1 
ATOM   1763 C  CB  . GLN   A 1 217 ? 15.23600  -38.55500 -22.44400 1.000 51.79693  ? 251 GLN   A CB  1 
ATOM   1764 C  CG  . GLN   A 1 217 ? 15.39600  -37.89200 -21.08900 1.000 67.10066  ? 251 GLN   A CG  1 
ATOM   1765 C  CD  . GLN   A 1 217 ? 16.85300  -37.67400 -20.72500 1.000 52.71480  ? 251 GLN   A CD  1 
ATOM   1766 O  OE1 . GLN   A 1 217 ? 17.28400  -37.99800 -19.61800 1.000 59.64509  ? 251 GLN   A OE1 1 
ATOM   1767 N  NE2 . GLN   A 1 217 ? 17.61900  -37.11900 -21.65700 1.000 61.58298  ? 251 GLN   A NE2 1 
ATOM   1768 N  N   . GLY   A 1 218 ? 14.08800  -38.18300 -25.33800 1.000 76.03248  ? 252 GLY   A N   1 
ATOM   1769 C  CA  . GLY   A 1 218 ? 14.12200  -38.53900 -26.74400 1.000 63.90416  ? 252 GLY   A CA  1 
ATOM   1770 C  C   . GLY   A 1 218 ? 12.79000  -38.95600 -27.31900 1.000 79.65929  ? 252 GLY   A C   1 
ATOM   1771 O  O   . GLY   A 1 218 ? 12.75300  -39.65400 -28.33500 1.000 81.34158  ? 252 GLY   A O   1 
ATOM   1772 N  N   . LEU   A 1 219 ? 11.68800  -38.55300 -26.69200 1.000 82.89970  ? 253 LEU   A N   1 
ATOM   1773 C  CA  . LEU   A 1 219 ? 10.36200  -38.87900 -27.19700 1.000 70.91456  ? 253 LEU   A CA  1 
ATOM   1774 C  C   . LEU   A 1 219 ? 9.98400   -37.91500 -28.31400 1.000 77.85292  ? 253 LEU   A C   1 
ATOM   1775 O  O   . LEU   A 1 219 ? 10.17900  -36.70100 -28.19000 1.000 80.70356  ? 253 LEU   A O   1 
ATOM   1776 C  CB  . LEU   A 1 219 ? 9.33200   -38.82400 -26.06800 1.000 60.57065  ? 253 LEU   A CB  1 
ATOM   1777 C  CG  . LEU   A 1 219 ? 8.96600   -40.14600 -25.38600 1.000 60.85067  ? 253 LEU   A CG  1 
ATOM   1778 C  CD1 . LEU   A 1 219 ? 10.20000  -40.98600 -25.09600 1.000 77.67981  ? 253 LEU   A CD1 1 
ATOM   1779 C  CD2 . LEU   A 1 219 ? 8.18800   -39.88300 -24.10500 1.000 68.81831  ? 253 LEU   A CD2 1 
ATOM   1780 N  N   . LYS   A 1 220 ? 9.44800   -38.45500 -29.40200 1.000 63.16653  ? 254 LYS   A N   1 
ATOM   1781 C  CA  . LYS   A 1 220 ? 9.10500   -37.67000 -30.57700 1.000 77.24871  ? 254 LYS   A CA  1 
ATOM   1782 C  C   . LYS   A 1 220 ? 7.60600   -37.40200 -30.62400 1.000 85.87685  ? 254 LYS   A C   1 
ATOM   1783 O  O   . LYS   A 1 220 ? 6.80000   -38.17100 -30.09400 1.000 87.15988  ? 254 LYS   A O   1 
ATOM   1784 C  CB  . LYS   A 1 220 ? 9.54100   -38.38900 -31.85400 1.000 89.98230  ? 254 LYS   A CB  1 
ATOM   1785 C  CG  . LYS   A 1 220 ? 10.96700  -38.90200 -31.81500 1.000 88.59216  ? 254 LYS   A CG  1 
ATOM   1786 C  CD  . LYS   A 1 220 ? 11.12500  -40.13400 -32.68800 1.000 102.20883 ? 254 LYS   A CD  1 
ATOM   1787 C  CE  . LYS   A 1 220 ? 10.10700  -41.20500 -32.31500 1.000 99.54760  ? 254 LYS   A CE  1 
ATOM   1788 N  NZ  . LYS   A 1 220 ? 10.12000  -41.51200 -30.85600 1.000 100.63724 ? 254 LYS   A NZ  1 
ATOM   1789 N  N   . ALA   A 1 221 ? 7.24500   -36.29900 -31.27600 1.000 85.55540  ? 255 ALA   A N   1 
ATOM   1790 C  CA  . ALA   A 1 221 ? 5.85700   -35.89600 -31.46100 1.000 83.50616  ? 255 ALA   A CA  1 
ATOM   1791 C  C   . ALA   A 1 221 ? 5.78900   -34.81800 -32.53500 1.000 79.68059  ? 255 ALA   A C   1 
ATOM   1792 O  O   . ALA   A 1 221 ? 6.76800   -34.08900 -32.74200 1.000 88.27062  ? 255 ALA   A O   1 
ATOM   1793 C  CB  . ALA   A 1 221 ? 5.25600   -35.39300 -30.14800 1.000 75.15043  ? 255 ALA   A CB  1 
ATOM   1794 N  N   . PRO   A 1 222 ? 4.66200   -34.68500 -33.24200 1.000 85.80455  ? 256 PRO   A N   1 
ATOM   1795 C  CA  . PRO   A 1 222 ? 4.59500   -33.65100 -34.28900 1.000 85.35168  ? 256 PRO   A CA  1 
ATOM   1796 C  C   . PRO   A 1 222 ? 4.68400   -32.23900 -33.74200 1.000 86.38760  ? 256 PRO   A C   1 
ATOM   1797 O  O   . PRO   A 1 222 ? 5.28200   -31.36900 -34.38700 1.000 87.57453  ? 256 PRO   A O   1 
ATOM   1798 C  CB  . PRO   A 1 222 ? 3.24200   -33.92500 -34.96200 1.000 79.65424  ? 256 PRO   A CB  1 
ATOM   1799 C  CG  . PRO   A 1 222 ? 2.43900   -34.62800 -33.91900 1.000 77.70933  ? 256 PRO   A CG  1 
ATOM   1800 C  CD  . PRO   A 1 222 ? 3.41700   -35.46600 -33.15300 1.000 74.09730  ? 256 PRO   A CD  1 
ATOM   1801 N  N   . THR   A 1 223 ? 4.11300   -31.98300 -32.57100 1.000 82.92444  ? 257 THR   A N   1 
ATOM   1802 C  CA  . THR   A 1 223 ? 4.15100   -30.66800 -31.94800 1.000 83.36486  ? 257 THR   A CA  1 
ATOM   1803 C  C   . THR   A 1 223 ? 4.85000   -30.76100 -30.59600 1.000 82.44947  ? 257 THR   A C   1 
ATOM   1804 O  O   . THR   A 1 223 ? 5.20600   -31.84400 -30.12300 1.000 90.47180  ? 257 THR   A O   1 
ATOM   1805 C  CB  . THR   A 1 223 ? 2.74100   -30.09200 -31.77700 1.000 70.93849  ? 257 THR   A CB  1 
ATOM   1806 O  OG1 . THR   A 1 223 ? 2.09900   -30.71800 -30.65900 1.000 68.68374  ? 257 THR   A OG1 1 
ATOM   1807 C  CG2 . THR   A 1 223 ? 1.91200   -30.33400 -33.02000 1.000 75.79483  ? 257 THR   A CG2 1 
ATOM   1808 N  N   . ASN   A 1 224 ? 5.04000   -29.59900 -29.97100 1.000 78.24125  ? 258 ASN   A N   1 
ATOM   1809 C  CA  . ASN   A 1 224 ? 5.62200   -29.56500 -28.63600 1.000 75.19347  ? 258 ASN   A CA  1 
ATOM   1810 C  C   . ASN   A 1 224 ? 4.58500   -29.84900 -27.55800 1.000 78.71025  ? 258 ASN   A C   1 
ATOM   1811 O  O   . ASN   A 1 224 ? 4.92600   -30.40800 -26.51000 1.000 76.67288  ? 258 ASN   A O   1 
ATOM   1812 C  CB  . ASN   A 1 224 ? 6.28400   -28.21000 -28.37900 1.000 75.17566  ? 258 ASN   A CB  1 
ATOM   1813 C  CG  . ASN   A 1 224 ? 7.58300   -28.33200 -27.60500 1.000 94.63646  ? 258 ASN   A CG  1 
ATOM   1814 O  OD1 . ASN   A 1 224 ? 7.89700   -29.39100 -27.06200 1.000 100.83837 ? 258 ASN   A OD1 1 
ATOM   1815 N  ND2 . ASN   A 1 224 ? 8.34500   -27.24600 -27.55100 1.000 102.26116 ? 258 ASN   A ND2 1 
ATOM   1816 N  N   . LYS   A 1 225 ? 3.32300   -29.48000 -27.78700 1.000 81.21564  ? 259 LYS   A N   1 
ATOM   1817 C  CA  . LYS   A 1 225 ? 2.29000   -29.76000 -26.79400 1.000 87.63977  ? 259 LYS   A CA  1 
ATOM   1818 C  C   . LYS   A 1 225 ? 2.04900   -31.26000 -26.66600 1.000 84.03664  ? 259 LYS   A C   1 
ATOM   1819 O  O   . LYS   A 1 225 ? 1.89200   -31.77900 -25.55500 1.000 81.66594  ? 259 LYS   A O   1 
ATOM   1820 C  CB  . LYS   A 1 225 ? 0.99800   -29.02900 -27.16000 1.000 79.55465  ? 259 LYS   A CB  1 
ATOM   1821 C  CG  . LYS   A 1 225 ? 1.23500   -27.73400 -27.92100 1.000 95.07798  ? 259 LYS   A CG  1 
ATOM   1822 C  CD  . LYS   A 1 225 ? -0.03500  -27.19700 -28.55700 1.000 81.80712  ? 259 LYS   A CD  1 
ATOM   1823 C  CE  . LYS   A 1 225 ? 0.29300   -26.38400 -29.80300 1.000 86.99433  ? 259 LYS   A CE  1 
ATOM   1824 N  NZ  . LYS   A 1 225 ? -0.49900  -25.12600 -29.89300 1.000 92.67081  ? 259 LYS   A NZ  1 
ATOM   1825 N  N   . GLN   A 1 226 ? 2.02900   -31.97500 -27.79400 1.000 82.96582  ? 260 GLN   A N   1 
ATOM   1826 C  CA  . GLN   A 1 226 ? 1.88600   -33.42600 -27.75100 1.000 71.03390  ? 260 GLN   A CA  1 
ATOM   1827 C  C   . GLN   A 1 226 ? 3.15200   -34.11400 -27.25800 1.000 75.87065  ? 260 GLN   A C   1 
ATOM   1828 O  O   . GLN   A 1 226 ? 3.07200   -35.23400 -26.74200 1.000 70.91286  ? 260 GLN   A O   1 
ATOM   1829 C  CB  . GLN   A 1 226 ? 1.50200   -33.95700 -29.13200 1.000 68.60509  ? 260 GLN   A CB  1 
ATOM   1830 C  CG  . GLN   A 1 226 ? 0.28400   -33.27500 -29.73100 1.000 73.62755  ? 260 GLN   A CG  1 
ATOM   1831 C  CD  . GLN   A 1 226 ? 0.00400   -33.71500 -31.15300 1.000 76.52920  ? 260 GLN   A CD  1 
ATOM   1832 O  OE1 . GLN   A 1 226 ? 0.23400   -34.87000 -31.51500 1.000 81.82641  ? 260 GLN   A OE1 1 
ATOM   1833 N  NE2 . GLN   A 1 226 ? -0.49000  -32.79300 -31.97000 1.000 77.14936  ? 260 GLN   A NE2 1 
ATOM   1834 N  N   . LYS   A 1 227 ? 4.31300   -33.47100 -27.40400 1.000 78.29658  ? 261 LYS   A N   1 
ATOM   1835 C  CA  . LYS   A 1 227 ? 5.54200   -34.03700 -26.85800 1.000 73.68499  ? 261 LYS   A CA  1 
ATOM   1836 C  C   . LYS   A 1 227 ? 5.54700   -33.96400 -25.33700 1.000 68.69252  ? 261 LYS   A C   1 
ATOM   1837 O  O   . LYS   A 1 227 ? 5.93700   -34.92800 -24.66700 1.000 59.25724  ? 261 LYS   A O   1 
ATOM   1838 C  CB  . LYS   A 1 227 ? 6.75600   -33.31600 -27.44200 1.000 84.24581  ? 261 LYS   A CB  1 
ATOM   1839 C  CG  . LYS   A 1 227 ? 8.07800   -33.71600 -26.80900 1.000 72.44280  ? 261 LYS   A CG  1 
ATOM   1840 C  CD  . LYS   A 1 227 ? 9.25300   -33.08600 -27.53600 1.000 80.14283  ? 261 LYS   A CD  1 
ATOM   1841 C  CE  . LYS   A 1 227 ? 10.45200  -32.93100 -26.61400 1.000 78.28445  ? 261 LYS   A CE  1 
ATOM   1842 N  NZ  . LYS   A 1 227 ? 10.21700  -31.87900 -25.58500 1.000 90.73611  ? 261 LYS   A NZ  1 
ATOM   1843 N  N   . TYR   A 1 228 ? 5.11700   -32.83200 -24.77400 1.000 68.09346  ? 262 TYR   A N   1 
ATOM   1844 C  CA  . TYR   A 1 228 ? 4.95700   -32.74600 -23.32700 1.000 65.17607  ? 262 TYR   A CA  1 
ATOM   1845 C  C   . TYR   A 1 228 ? 3.92200   -33.74700 -22.82800 1.000 66.36773  ? 262 TYR   A C   1 
ATOM   1846 O  O   . TYR   A 1 228 ? 4.02700   -34.24000 -21.70000 1.000 68.07218  ? 262 TYR   A O   1 
ATOM   1847 C  CB  . TYR   A 1 228 ? 4.55700   -31.32700 -22.91200 1.000 69.18862  ? 262 TYR   A CB  1 
ATOM   1848 C  CG  . TYR   A 1 228 ? 5.66500   -30.28900 -22.97200 1.000 75.25479  ? 262 TYR   A CG  1 
ATOM   1849 C  CD1 . TYR   A 1 228 ? 6.69200   -30.38000 -23.90300 1.000 87.00170  ? 262 TYR   A CD1 1 
ATOM   1850 C  CD2 . TYR   A 1 228 ? 5.68100   -29.21700 -22.08700 1.000 85.74050  ? 262 TYR   A CD2 1 
ATOM   1851 C  CE1 . TYR   A 1 228 ? 7.69800   -29.43200 -23.95500 1.000 89.91809  ? 262 TYR   A CE1 1 
ATOM   1852 C  CE2 . TYR   A 1 228 ? 6.68400   -28.26500 -22.13200 1.000 89.24108  ? 262 TYR   A CE2 1 
ATOM   1853 C  CZ  . TYR   A 1 228 ? 7.69000   -28.37800 -23.06800 1.000 94.75726  ? 262 TYR   A CZ  1 
ATOM   1854 O  OH  . TYR   A 1 228 ? 8.69000   -27.43400 -23.11700 1.000 104.32414 ? 262 TYR   A OH  1 
ATOM   1855 N  N   . GLU   A 1 229 ? 2.92100   -34.06100 -23.65400 1.000 58.86951  ? 263 GLU   A N   1 
ATOM   1856 C  CA  . GLU   A 1 229 ? 1.91600   -35.04400 -23.26500 1.000 64.99987  ? 263 GLU   A CA  1 
ATOM   1857 C  C   . GLU   A 1 229 ? 2.50900   -36.44900 -23.22100 1.000 72.34258  ? 263 GLU   A C   1 
ATOM   1858 O  O   . GLU   A 1 229 ? 2.26700   -37.20400 -22.27200 1.000 68.81657  ? 263 GLU   A O   1 
ATOM   1859 C  CB  . GLU   A 1 229 ? 0.72700   -34.98300 -24.22600 1.000 64.44428  ? 263 GLU   A CB  1 
ATOM   1860 C  CG  . GLU   A 1 229 ? -0.23700  -36.15600 -24.10100 1.000 84.39150  ? 263 GLU   A CG  1 
ATOM   1861 C  CD  . GLU   A 1 229 ? -1.51000  -35.95600 -24.90300 1.000 95.82472  ? 263 GLU   A CD  1 
ATOM   1862 O  OE1 . GLU   A 1 229 ? -1.46600  -36.12200 -26.14000 1.000 97.31309  ? 263 GLU   A OE1 1 
ATOM   1863 O  OE2 . GLU   A 1 229 ? -2.55200  -35.62400 -24.29800 1.000 99.98450  ? 263 GLU   A OE2 1 
ATOM   1864 N  N   . LYS   A 1 230 ? 3.28700   -36.81800 -24.24300 1.000 69.09138  ? 264 LYS   A N   1 
ATOM   1865 C  CA  . LYS   A 1 230 ? 3.92000   -38.13500 -24.25400 1.000 58.60756  ? 264 LYS   A CA  1 
ATOM   1866 C  C   . LYS   A 1 230 ? 4.84100   -38.31500 -23.05600 1.000 63.65240  ? 264 LYS   A C   1 
ATOM   1867 O  O   . LYS   A 1 230 ? 4.88000   -39.39200 -22.44700 1.000 71.90249  ? 264 LYS   A O   1 
ATOM   1868 C  CB  . LYS   A 1 230 ? 4.70100   -38.33900 -25.55200 1.000 58.96614  ? 264 LYS   A CB  1 
ATOM   1869 C  CG  . LYS   A 1 230 ? 3.90900   -38.97200 -26.68500 1.000 62.00720  ? 264 LYS   A CG  1 
ATOM   1870 C  CD  . LYS   A 1 230 ? 4.85200   -39.48800 -27.76100 1.000 65.98363  ? 264 LYS   A CD  1 
ATOM   1871 C  CE  . LYS   A 1 230 ? 4.10300   -40.17100 -28.89100 1.000 78.59798  ? 264 LYS   A CE  1 
ATOM   1872 N  NZ  . LYS   A 1 230 ? 5.04100   -40.77400 -29.87900 1.000 85.20598  ? 264 LYS   A NZ  1 
ATOM   1873 N  N   . ILE   A 1 231 ? 5.59500   -37.27100 -22.70400 1.000 65.39063  ? 265 ILE   A N   1 
ATOM   1874 C  CA  . ILE   A 1 231 ? 6.50500   -37.35600 -21.56700 1.000 57.43195  ? 265 ILE   A CA  1 
ATOM   1875 C  C   . ILE   A 1 231 ? 5.72500   -37.55000 -20.27200 1.000 59.70367  ? 265 ILE   A C   1 
ATOM   1876 O  O   . ILE   A 1 231 ? 6.08200   -38.38900 -19.43600 1.000 67.96271  ? 265 ILE   A O   1 
ATOM   1877 C  CB  . ILE   A 1 231 ? 7.40400   -36.10800 -21.51600 1.000 56.99744  ? 265 ILE   A CB  1 
ATOM   1878 C  CG1 . ILE   A 1 231 ? 8.26100   -36.02300 -22.78000 1.000 54.20705  ? 265 ILE   A CG1 1 
ATOM   1879 C  CG2 . ILE   A 1 231 ? 8.28300   -36.13100 -20.28000 1.000 56.27999  ? 265 ILE   A CG2 1 
ATOM   1880 C  CD1 . ILE   A 1 231 ? 9.05700   -34.74100 -22.89600 1.000 61.09698  ? 265 ILE   A CD1 1 
ATOM   1881 N  N   . GLY   A 1 232 ? 4.64600   -36.78800 -20.08800 1.000 61.04454  ? 266 GLY   A N   1 
ATOM   1882 C  CA  . GLY   A 1 232 ? 3.83400   -36.94700 -18.89400 1.000 64.12032  ? 266 GLY   A CA  1 
ATOM   1883 C  C   . GLY   A 1 232 ? 3.13700   -38.29000 -18.81800 1.000 64.41661  ? 266 GLY   A C   1 
ATOM   1884 O  O   . GLY   A 1 232 ? 2.91200   -38.81700 -17.72400 1.000 59.50694  ? 266 GLY   A O   1 
ATOM   1885 N  N   . ASP   A 1 233 ? 2.78700   -38.86400 -19.97200 1.000 56.99999  ? 267 ASP   A N   1 
ATOM   1886 C  CA  . ASP   A 1 233 ? 2.14900   -40.17700 -19.98300 1.000 59.80511  ? 267 ASP   A CA  1 
ATOM   1887 C  C   . ASP   A 1 233 ? 3.13000   -41.27300 -19.58500 1.000 72.78560  ? 267 ASP   A C   1 
ATOM   1888 O  O   . ASP   A 1 233 ? 2.75800   -42.22500 -18.88900 1.000 64.29411  ? 267 ASP   A O   1 
ATOM   1889 C  CB  . ASP   A 1 233 ? 1.55500   -40.46400 -21.36200 1.000 66.08754  ? 267 ASP   A CB  1 
ATOM   1890 C  CG  . ASP   A 1 233 ? 0.29800   -39.66200 -21.63300 1.000 85.94213  ? 267 ASP   A CG  1 
ATOM   1891 O  OD1 . ASP   A 1 233 ? -0.40900  -39.31900 -20.66100 1.000 89.52378  ? 267 ASP   A OD1 1 
ATOM   1892 O  OD2 . ASP   A 1 233 ? 0.01100   -39.38000 -22.81500 1.000 76.39688  ? 267 ASP   A OD2 1 
ATOM   1893 N  N   . LYS   A 1 234 ? 4.38700   -41.16100 -20.02400 1.000 62.28830  ? 268 LYS   A N   1 
ATOM   1894 C  CA  . LYS   A 1 234 ? 5.39700   -42.12800 -19.61100 1.000 52.82454  ? 268 LYS   A CA  1 
ATOM   1895 C  C   . LYS   A 1 234 ? 5.67000   -42.04000 -18.11500 1.000 60.23479  ? 268 LYS   A C   1 
ATOM   1896 O  O   . LYS   A 1 234 ? 6.00200   -43.05000 -17.48500 1.000 59.80570  ? 268 LYS   A O   1 
ATOM   1897 C  CB  . LYS   A 1 234 ? 6.69000   -41.90900 -20.40100 1.000 57.09855  ? 268 LYS   A CB  1 
ATOM   1898 C  CG  . LYS   A 1 234 ? 7.80900   -42.89200 -20.07300 1.000 71.57964  ? 268 LYS   A CG  1 
ATOM   1899 C  CD  . LYS   A 1 234 ? 7.69000   -44.18000 -20.87700 1.000 50.45892  ? 268 LYS   A CD  1 
ATOM   1900 C  CE  . LYS   A 1 234 ? 7.96900   -43.93500 -22.35300 1.000 75.83981  ? 268 LYS   A CE  1 
ATOM   1901 N  NZ  . LYS   A 1 234 ? 7.98100   -45.19800 -23.14400 1.000 77.93689  ? 268 LYS   A NZ  1 
ATOM   1902 N  N   . LYS   A 1 235 ? 5.52000   -40.85000 -17.52700 1.000 56.21197  ? 269 LYS   A N   1 
ATOM   1903 C  CA  . LYS   A 1 235 ? 5.83500   -40.68100 -16.11200 1.000 62.22661  ? 269 LYS   A CA  1 
ATOM   1904 C  C   . LYS   A 1 235 ? 4.82000   -41.39000 -15.22300 1.000 62.55140  ? 269 LYS   A C   1 
ATOM   1905 O  O   . LYS   A 1 235 ? 5.19500   -42.00400 -14.21500 1.000 84.01931  ? 269 LYS   A O   1 
ATOM   1906 C  CB  . LYS   A 1 235 ? 5.91900   -39.19300 -15.76800 1.000 62.56356  ? 269 LYS   A CB  1 
ATOM   1907 C  CG  . LYS   A 1 235 ? 7.13600   -38.50400 -16.36900 1.000 64.98972  ? 269 LYS   A CG  1 
ATOM   1908 C  CD  . LYS   A 1 235 ? 7.18200   -37.02100 -16.04100 1.000 48.59933  ? 269 LYS   A CD  1 
ATOM   1909 C  CE  . LYS   A 1 235 ? 8.41700   -36.37800 -16.65300 1.000 57.53698  ? 269 LYS   A CE  1 
ATOM   1910 N  NZ  . LYS   A 1 235 ? 8.47500   -34.91500 -16.41700 1.000 46.72010  ? 269 LYS   A NZ  1 
ATOM   1911 N  N   . ARG   A 1 236 ? 3.53100   -41.31500 -15.57300 1.000 71.39901  ? 270 ARG   A N   1 
ATOM   1912 C  CA  . ARG   A 1 236 ? 2.51000   -42.04500 -14.82700 1.000 83.98713  ? 270 ARG   A CA  1 
ATOM   1913 C  C   . ARG   A 1 236 ? 2.57800   -43.54300 -15.08200 1.000 79.52861  ? 270 ARG   A C   1 
ATOM   1914 O  O   . ARG   A 1 236 ? 2.28600   -44.33700 -14.18000 1.000 81.81916  ? 270 ARG   A O   1 
ATOM   1915 C  CB  . ARG   A 1 236 ? 1.11300   -41.55400 -15.19600 1.000 74.90903  ? 270 ARG   A CB  1 
ATOM   1916 C  CG  . ARG   A 1 236 ? 0.98800   -40.08300 -15.52100 1.000 80.71422  ? 270 ARG   A CG  1 
ATOM   1917 C  CD  . ARG   A 1 236 ? -0.40500  -39.78000 -16.08200 1.000 87.46455  ? 270 ARG   A CD  1 
ATOM   1918 N  NE  . ARG   A 1 236 ? -0.74600  -40.65300 -17.20200 1.000 107.16800 ? 270 ARG   A NE  1 
ATOM   1919 C  CZ  . ARG   A 1 236 ? -1.51300  -41.73100 -17.11000 1.000 116.35271 ? 270 ARG   A CZ  1 
ATOM   1920 N  NH1 . ARG   A 1 236 ? -2.02400  -42.11900 -15.95300 1.000 123.90068 ? 270 ARG   A NH1 1 
ATOM   1921 N  NH2 . ARG   A 1 236 ? -1.76500  -42.44400 -18.20500 1.000 108.32980 ? 270 ARG   A NH2 1 
ATOM   1922 N  N   . THR   A 1 237 ? 2.94000   -43.94500 -16.30100 1.000 68.15558  ? 271 THR   A N   1 
ATOM   1923 C  CA  . THR   A 1 237 ? 3.01400   -45.36400 -16.62700 1.000 69.43355  ? 271 THR   A CA  1 
ATOM   1924 C  C   . THR   A 1 237 ? 4.18300   -46.04000 -15.92200 1.000 77.87291  ? 271 THR   A C   1 
ATOM   1925 O  O   . THR   A 1 237 ? 4.08300   -47.21200 -15.54400 1.000 85.53059  ? 271 THR   A O   1 
ATOM   1926 C  CB  . THR   A 1 237 ? 3.12000   -45.54800 -18.14400 1.000 69.55149  ? 271 THR   A CB  1 
ATOM   1927 O  OG1 . THR   A 1 237 ? 1.93900   -45.03100 -18.77200 1.000 78.77278  ? 271 THR   A OG1 1 
ATOM   1928 C  CG2 . THR   A 1 237 ? 3.27500   -47.02000 -18.51200 1.000 94.83821  ? 271 THR   A CG2 1 
ATOM   1929 N  N   . THR   A 1 238 ? 5.28200   -45.31400 -15.71300 1.000 73.44354  ? 272 THR   A N   1 
ATOM   1930 C  CA  . THR   A 1 238 ? 6.48000   -45.88700 -15.11600 1.000 72.42473  ? 272 THR   A CA  1 
ATOM   1931 C  C   . THR   A 1 238 ? 6.40400   -45.77200 -13.59900 1.000 68.85445  ? 272 THR   A C   1 
ATOM   1932 O  O   . THR   A 1 238 ? 6.46800   -44.65100 -13.07100 1.000 61.68212  ? 272 THR   A O   1 
ATOM   1933 C  CB  . THR   A 1 238 ? 7.72500   -45.18300 -15.63500 1.000 59.91376  ? 272 THR   A CB  1 
ATOM   1934 O  OG1 . THR   A 1 238 ? 7.76600   -45.27300 -17.06400 1.000 62.74895  ? 272 THR   A OG1 1 
ATOM   1935 C  CG2 . THR   A 1 238 ? 8.97600   -45.82300 -15.05500 1.000 60.59989  ? 272 THR   A CG2 1 
ATOM   1936 N  N   . PRO   A 1 239 ? 6.27200   -46.87400 -12.86500 1.000 74.32104  ? 273 PRO   A N   1 
ATOM   1937 C  CA  . PRO   A 1 239 ? 6.31100   -46.79400 -11.40300 1.000 58.16896  ? 273 PRO   A CA  1 
ATOM   1938 C  C   . PRO   A 1 239 ? 7.71000   -46.45600 -10.91300 1.000 62.64719  ? 273 PRO   A C   1 
ATOM   1939 O  O   . PRO   A 1 239 ? 8.70700   -46.63000 -11.61600 1.000 67.05754  ? 273 PRO   A O   1 
ATOM   1940 C  CB  . PRO   A 1 239 ? 5.89100   -48.20000 -10.95200 1.000 77.32076  ? 273 PRO   A CB  1 
ATOM   1941 C  CG  . PRO   A 1 239 ? 5.28100   -48.84300 -12.17200 1.000 55.08200  ? 273 PRO   A CG  1 
ATOM   1942 C  CD  . PRO   A 1 239 ? 6.00300   -48.24300 -13.33200 1.000 77.46072  ? 273 PRO   A CD  1 
ATOM   1943 N  N   . ALA   A 1 240 ? 7.77000   -45.96100 -9.67400  1.000 71.18396  ? 274 ALA   A N   1 
ATOM   1944 C  CA  . ALA   A 1 240 ? 9.05400   -45.57600 -9.09800  1.000 62.87478  ? 274 ALA   A CA  1 
ATOM   1945 C  C   . ALA   A 1 240 ? 9.98200   -46.77300 -8.94000  1.000 61.95974  ? 274 ALA   A C   1 
ATOM   1946 O  O   . ALA   A 1 240 ? 11.20600  -46.62500 -9.03000  1.000 65.52402  ? 274 ALA   A O   1 
ATOM   1947 C  CB  . ALA   A 1 240 ? 8.84100   -44.88500 -7.75200  1.000 57.11048  ? 274 ALA   A CB  1 
ATOM   1948 N  N   . VAL   A 1 241 ? 9.42200   -47.96200 -8.70600  1.000 66.93239  ? 275 VAL   A N   1 
ATOM   1949 C  CA  . VAL   A 1 241 ? 10.24200  -49.16400 -8.60100  1.000 63.06185  ? 275 VAL   A CA  1 
ATOM   1950 C  C   . VAL   A 1 241 ? 10.90300  -49.48700 -9.93700  1.000 66.38065  ? 275 VAL   A C   1 
ATOM   1951 O  O   . VAL   A 1 241 ? 12.04800  -49.95600 -9.97400  1.000 66.09393  ? 275 VAL   A O   1 
ATOM   1952 C  CB  . VAL   A 1 241 ? 9.38700   -50.33400 -8.07500  1.000 72.94206  ? 275 VAL   A CB  1 
ATOM   1953 C  CG1 . VAL   A 1 241 ? 9.99100   -51.67600 -8.46100  1.000 85.54097  ? 275 VAL   A CG1 1 
ATOM   1954 C  CG2 . VAL   A 1 241 ? 9.23900   -50.23300 -6.56300  1.000 59.03989  ? 275 VAL   A CG2 1 
ATOM   1955 N  N   . THR   A 1 242 ? 10.21300  -49.22500 -11.05000 1.000 62.35450  ? 276 THR   A N   1 
ATOM   1956 C  CA  . THR   A 1 242 ? 10.81800  -49.44200 -12.36100 1.000 65.43425  ? 276 THR   A CA  1 
ATOM   1957 C  C   . THR   A 1 242 ? 11.95200  -48.45500 -12.61500 1.000 76.89987  ? 276 THR   A C   1 
ATOM   1958 O  O   . THR   A 1 242 ? 13.00800  -48.83500 -13.13600 1.000 84.54848  ? 276 THR   A O   1 
ATOM   1959 C  CB  . THR   A 1 242 ? 9.75500   -49.33600 -13.45500 1.000 67.74608  ? 276 THR   A CB  1 
ATOM   1960 O  OG1 . THR   A 1 242 ? 8.75800   -50.34600 -13.25300 1.000 77.15328  ? 276 THR   A OG1 1 
ATOM   1961 C  CG2 . THR   A 1 242 ? 10.38100  -49.51800 -14.83000 1.000 52.32110  ? 276 THR   A CG2 1 
ATOM   1962 N  N   . LEU   A 1 243 ? 11.75300  -47.18400 -12.25400 1.000 67.12396  ? 277 LEU   A N   1 
ATOM   1963 C  CA  . LEU   A 1 243 ? 12.82900  -46.20400 -12.36400 1.000 67.00232  ? 277 LEU   A CA  1 
ATOM   1964 C  C   . LEU   A 1 243 ? 14.02500  -46.58500 -11.50400 1.000 65.10602  ? 277 LEU   A C   1 
ATOM   1965 O  O   . LEU   A 1 243 ? 15.17100  -46.30000 -11.87000 1.000 67.03082  ? 277 LEU   A O   1 
ATOM   1966 C  CB  . LEU   A 1 243 ? 12.32300  -44.81900 -11.96000 1.000 58.71835  ? 277 LEU   A CB  1 
ATOM   1967 C  CG  . LEU   A 1 243 ? 11.51700  -44.03300 -12.99100 1.000 65.04171  ? 277 LEU   A CG  1 
ATOM   1968 C  CD1 . LEU   A 1 243 ? 10.98600  -42.74800 -12.38100 1.000 57.27102  ? 277 LEU   A CD1 1 
ATOM   1969 C  CD2 . LEU   A 1 243 ? 12.38800  -43.73300 -14.18800 1.000 49.48468  ? 277 LEU   A CD2 1 
ATOM   1970 N  N   . CYS   A 1 244 ? 13.77900  -47.23100 -10.36600 1.000 58.42750  ? 278 CYS   A N   1 
ATOM   1971 C  CA  . CYS   A 1 244 ? 14.81000  -47.53400 -9.38700  1.000 53.28717  ? 278 CYS   A CA  1 
ATOM   1972 C  C   . CYS   A 1 244 ? 15.43000  -48.91100 -9.58900  1.000 56.93581  ? 278 CYS   A C   1 
ATOM   1973 O  O   . CYS   A 1 244 ? 16.04000  -49.44700 -8.65700  1.000 66.68897  ? 278 CYS   A O   1 
ATOM   1974 C  CB  . CYS   A 1 244 ? 14.22900  -47.42200 -7.97700  1.000 50.73986  ? 278 CYS   A CB  1 
ATOM   1975 S  SG  . CYS   A 1 244 ? 15.43400  -47.12300 -6.67700  1.000 57.76106  ? 278 CYS   A SG  1 
ATOM   1976 N  N   . ASP   A 1 245 ? 15.28500  -49.49300 -10.77600 1.000 67.67650  ? 279 ASP   A N   1 
ATOM   1977 C  CA  . ASP   A 1 245 ? 15.82700  -50.82200 -11.03000 1.000 82.23079  ? 279 ASP   A CA  1 
ATOM   1978 C  C   . ASP   A 1 245 ? 17.34600  -50.80300 -10.92800 1.000 67.01482  ? 279 ASP   A C   1 
ATOM   1979 O  O   . ASP   A 1 245 ? 18.02000  -50.07900 -11.66800 1.000 70.85016  ? 279 ASP   A O   1 
ATOM   1980 C  CB  . ASP   A 1 245 ? 15.38000  -51.31400 -12.40500 1.000 81.24820  ? 279 ASP   A CB  1 
ATOM   1981 C  CG  . ASP   A 1 245 ? 16.14300  -52.54000 -12.86200 1.000 94.32111  ? 279 ASP   A CG  1 
ATOM   1982 O  OD1 . ASP   A 1 245 ? 16.01100  -53.59900 -12.21200 1.000 101.95707 ? 279 ASP   A OD1 1 
ATOM   1983 O  OD2 . ASP   A 1 245 ? 16.89200  -52.44100 -13.85800 1.000 94.36463  ? 279 ASP   A OD2 1 
ATOM   1984 N  N   . GLY   A 1 246 ? 17.88200  -51.59900 -10.00400 1.000 71.44777  ? 280 GLY   A N   1 
ATOM   1985 C  CA  . GLY   A 1 246 ? 19.30700  -51.64700 -9.75500  1.000 63.91930  ? 280 GLY   A CA  1 
ATOM   1986 C  C   . GLY   A 1 246 ? 19.83700  -50.56500 -8.84200  1.000 58.09606  ? 280 GLY   A C   1 
ATOM   1987 O  O   . GLY   A 1 246 ? 21.03800  -50.56700 -8.54200  1.000 55.77941  ? 280 GLY   A O   1 
ATOM   1988 N  N   . LEU   A 1 247 ? 18.99000  -49.64900 -8.38800  1.000 57.68747  ? 281 LEU   A N   1 
ATOM   1989 C  CA  . LEU   A 1 247 ? 19.37300  -48.52700 -7.55000  1.000 57.63957  ? 281 LEU   A CA  1 
ATOM   1990 C  C   . LEU   A 1 247 ? 18.87400  -48.72000 -6.12300  1.000 54.93896  ? 281 LEU   A C   1 
ATOM   1991 O  O   . LEU   A 1 247 ? 17.99100  -49.54600 -5.86900  1.000 60.41066  ? 281 LEU   A O   1 
ATOM   1992 C  CB  . LEU   A 1 247 ? 18.80600  -47.22100 -8.12600  1.000 52.73533  ? 281 LEU   A CB  1 
ATOM   1993 C  CG  . LEU   A 1 247 ? 19.29500  -46.84400 -9.52500  1.000 42.61923  ? 281 LEU   A CG  1 
ATOM   1994 C  CD1 . LEU   A 1 247 ? 18.51800  -45.65300 -10.06300 1.000 58.40270  ? 281 LEU   A CD1 1 
ATOM   1995 C  CD2 . LEU   A 1 247 ? 20.78700  -46.55000 -9.50700  1.000 57.39917  ? 281 LEU   A CD2 1 
ATOM   1996 N  N   . PRO   A 1 248 ? 19.43600  -47.99100 -5.15700  1.000 59.94805  ? 282 PRO   A N   1 
ATOM   1997 C  CA  . PRO   A 1 248 ? 18.91900  -48.06600 -3.78400  1.000 58.85025  ? 282 PRO   A CA  1 
ATOM   1998 C  C   . PRO   A 1 248 ? 17.45800  -47.64300 -3.72300  1.000 58.40103  ? 282 PRO   A C   1 
ATOM   1999 O  O   . PRO   A 1 248 ? 17.08600  -46.56200 -4.18500  1.000 58.34907  ? 282 PRO   A O   1 
ATOM   2000 C  CB  . PRO   A 1 248 ? 19.82400  -47.10000 -3.01300  1.000 53.45804  ? 282 PRO   A CB  1 
ATOM   2001 C  CG  . PRO   A 1 248 ? 21.09200  -47.08000 -3.79600  1.000 58.94471  ? 282 PRO   A CG  1 
ATOM   2002 C  CD  . PRO   A 1 248 ? 20.67900  -47.20300 -5.23300  1.000 58.44482  ? 282 PRO   A CD  1 
ATOM   2003 N  N   . GLN   A 1 249 ? 16.63300  -48.50400 -3.12300  1.000 53.68115  ? 283 GLN   A N   1 
ATOM   2004 C  CA  . GLN   A 1 249 ? 15.18400  -48.34100 -3.16700  1.000 59.44874  ? 283 GLN   A CA  1 
ATOM   2005 C  C   . GLN   A 1 249 ? 14.69300  -47.09200 -2.44800  1.000 59.11067  ? 283 GLN   A C   1 
ATOM   2006 O  O   . GLN   A 1 249 ? 13.51800  -46.73700 -2.59700  1.000 46.36623  ? 283 GLN   A O   1 
ATOM   2007 C  CB  . GLN   A 1 249 ? 14.50600  -49.57700 -2.57300  1.000 49.12950  ? 283 GLN   A CB  1 
ATOM   2008 C  CG  . GLN   A 1 249 ? 13.20400  -49.93700 -3.25800  1.000 67.54461  ? 283 GLN   A CG  1 
ATOM   2009 C  CD  . GLN   A 1 249 ? 13.38600  -50.16500 -4.74600  1.000 79.18893  ? 283 GLN   A CD  1 
ATOM   2010 O  OE1 . GLN   A 1 249 ? 14.35800  -50.78700 -5.17600  1.000 70.28618  ? 283 GLN   A OE1 1 
ATOM   2011 N  NE2 . GLN   A 1 249 ? 12.45500  -49.65100 -5.54200  1.000 84.72293  ? 283 GLN   A NE2 1 
ATOM   2012 N  N   . GLN   A 1 250 ? 15.55000  -46.41900 -1.67700  1.000 54.20314  ? 284 GLN   A N   1 
ATOM   2013 C  CA  . GLN   A 1 250 ? 15.14100  -45.18700 -1.01400  1.000 52.21128  ? 284 GLN   A CA  1 
ATOM   2014 C  C   . GLN   A 1 250 ? 14.81700  -44.07600 -2.00400  1.000 53.69561  ? 284 GLN   A C   1 
ATOM   2015 O  O   . GLN   A 1 250 ? 14.05500  -43.16500 -1.66400  1.000 59.80099  ? 284 GLN   A O   1 
ATOM   2016 C  CB  . GLN   A 1 250 ? 16.23000  -44.71500 -0.04900  1.000 48.35697  ? 284 GLN   A CB  1 
ATOM   2017 C  CG  . GLN   A 1 250 ? 16.38000  -45.56100 1.21000   1.000 56.23948  ? 284 GLN   A CG  1 
ATOM   2018 C  CD  . GLN   A 1 250 ? 17.41500  -46.66400 1.07400   1.000 55.15144  ? 284 GLN   A CD  1 
ATOM   2019 O  OE1 . GLN   A 1 250 ? 17.70000  -47.13800 -0.02500  1.000 55.15967  ? 284 GLN   A OE1 1 
ATOM   2020 N  NE2 . GLN   A 1 250 ? 17.98900  -47.07300 2.19900   1.000 53.10416  ? 284 GLN   A NE2 1 
ATOM   2021 N  N   . PHE   A 1 251 ? 15.37600  -44.12600 -3.21600  1.000 51.56605  ? 285 PHE   A N   1 
ATOM   2022 C  CA  . PHE   A 1 251 ? 15.06900  -43.10000 -4.20700  1.000 51.67216  ? 285 PHE   A CA  1 
ATOM   2023 C  C   . PHE   A 1 251 ? 13.67500  -43.29600 -4.79000  1.000 56.88005  ? 285 PHE   A C   1 
ATOM   2024 O  O   . PHE   A 1 251 ? 12.97800  -42.31800 -5.08200  1.000 61.02942  ? 285 PHE   A O   1 
ATOM   2025 C  CB  . PHE   A 1 251 ? 16.12500  -43.10300 -5.31200  1.000 54.48469  ? 285 PHE   A CB  1 
ATOM   2026 C  CG  . PHE   A 1 251 ? 17.43800  -42.51100 -4.89300  1.000 46.88952  ? 285 PHE   A CG  1 
ATOM   2027 C  CD1 . PHE   A 1 251 ? 17.63700  -41.14000 -4.93000  1.000 62.28443  ? 285 PHE   A CD1 1 
ATOM   2028 C  CD2 . PHE   A 1 251 ? 18.47300  -43.32100 -4.45900  1.000 50.29924  ? 285 PHE   A CD2 1 
ATOM   2029 C  CE1 . PHE   A 1 251 ? 18.84500  -40.58800 -4.54300  1.000 47.30250  ? 285 PHE   A CE1 1 
ATOM   2030 C  CE2 . PHE   A 1 251 ? 19.68300  -42.77600 -4.07200  1.000 44.27307  ? 285 PHE   A CE2 1 
ATOM   2031 C  CZ  . PHE   A 1 251 ? 19.86900  -41.40900 -4.11400  1.000 50.83247  ? 285 PHE   A CZ  1 
ATOM   2032 N  N   . ALA   A 1 252 ? 13.25400  -44.55100 -4.97300  1.000 65.90625  ? 286 ALA   A N   1 
ATOM   2033 C  CA  . ALA   A 1 252 ? 11.88000  -44.81100 -5.39000  1.000 61.20395  ? 286 ALA   A CA  1 
ATOM   2034 C  C   . ALA   A 1 252 ? 10.90000  -44.45700 -4.28100  1.000 51.14701  ? 286 ALA   A C   1 
ATOM   2035 O  O   . ALA   A 1 252 ? 9.84000   -43.87600 -4.54200  1.000 57.43664  ? 286 ALA   A O   1 
ATOM   2036 C  CB  . ALA   A 1 252 ? 11.72000  -46.27400 -5.79800  1.000 60.79908  ? 286 ALA   A CB  1 
ATOM   2037 N  N   . GLU   A 1 253 ? 11.24000  -44.80300 -3.03700  1.000 60.09475  ? 287 GLU   A N   1 
ATOM   2038 C  CA  . GLU   A 1 253 ? 10.40800  -44.43000 -1.89800  1.000 60.22575  ? 287 GLU   A CA  1 
ATOM   2039 C  C   . GLU   A 1 253 ? 10.28100  -42.91800 -1.77400  1.000 58.68153  ? 287 GLU   A C   1 
ATOM   2040 O  O   . GLU   A 1 253 ? 9.22500   -42.41300 -1.37800  1.000 57.47810  ? 287 GLU   A O   1 
ATOM   2041 C  CB  . GLU   A 1 253 ? 10.98900  -45.03000 -0.61800  1.000 40.97772  ? 287 GLU   A CB  1 
ATOM   2042 C  CG  . GLU   A 1 253 ? 10.24700  -44.66300 0.65300   1.000 64.92291  ? 287 GLU   A CG  1 
ATOM   2043 C  CD  . GLU   A 1 253 ? 10.78900  -45.39400 1.86500   1.000 83.49987  ? 287 GLU   A CD  1 
ATOM   2044 O  OE1 . GLU   A 1 253 ? 11.51700  -46.39200 1.67600   1.000 78.43082  ? 287 GLU   A OE1 1 
ATOM   2045 O  OE2 . GLU   A 1 253 ? 10.49100  -44.97300 3.00200   1.000 92.78311  ? 287 GLU   A OE2 1 
ATOM   2046 N  N   . TYR   A 1 254 ? 11.34000  -42.18100 -2.11500  1.000 62.87462  ? 288 TYR   A N   1 
ATOM   2047 C  CA  . TYR   A 1 254 ? 11.26400  -40.72400 -2.09100  1.000 47.56366  ? 288 TYR   A CA  1 
ATOM   2048 C  C   . TYR   A 1 254 ? 10.29100  -40.20700 -3.14300  1.000 47.92383  ? 288 TYR   A C   1 
ATOM   2049 O  O   . TYR   A 1 254 ? 9.41500   -39.38600 -2.84600  1.000 49.82530  ? 288 TYR   A O   1 
ATOM   2050 C  CB  . TYR   A 1 254 ? 12.65200  -40.11600 -2.30200  1.000 43.69138  ? 288 TYR   A CB  1 
ATOM   2051 C  CG  . TYR   A 1 254 ? 12.62400  -38.62300 -2.54500  1.000 44.43268  ? 288 TYR   A CG  1 
ATOM   2052 C  CD1 . TYR   A 1 254 ? 12.55400  -37.73100 -1.48400  1.000 45.73485  ? 288 TYR   A CD1 1 
ATOM   2053 C  CD2 . TYR   A 1 254 ? 12.65900  -38.10700 -3.83500  1.000 37.55540  ? 288 TYR   A CD2 1 
ATOM   2054 C  CE1 . TYR   A 1 254 ? 12.52200  -36.36500 -1.69900  1.000 46.46180  ? 288 TYR   A CE1 1 
ATOM   2055 C  CE2 . TYR   A 1 254 ? 12.62600  -36.74300 -4.06000  1.000 45.07150  ? 288 TYR   A CE2 1 
ATOM   2056 C  CZ  . TYR   A 1 254 ? 12.55800  -35.87800 -2.98800  1.000 43.80016  ? 288 TYR   A CZ  1 
ATOM   2057 O  OH  . TYR   A 1 254 ? 12.52600  -34.52100 -3.20700  1.000 45.72029  ? 288 TYR   A OH  1 
ATOM   2058 N  N   . LEU   A 1 255 ? 10.43300  -40.67900 -4.38500  1.000 43.21193  ? 289 LEU   A N   1 
ATOM   2059 C  CA  . LEU   A 1 255 ? 9.59400   -40.17600 -5.46900  1.000 39.80702  ? 289 LEU   A CA  1 
ATOM   2060 C  C   . LEU   A 1 255 ? 8.12400   -40.49500 -5.22700  1.000 57.14973  ? 289 LEU   A C   1 
ATOM   2061 O  O   . LEU   A 1 255 ? 7.25300   -39.64800 -5.45600  1.000 56.99792  ? 289 LEU   A O   1 
ATOM   2062 C  CB  . LEU   A 1 255 ? 10.05700  -40.75700 -6.80400  1.000 53.38791  ? 289 LEU   A CB  1 
ATOM   2063 C  CG  . LEU   A 1 255 ? 9.28900   -40.29200 -8.04300  1.000 50.78500  ? 289 LEU   A CG  1 
ATOM   2064 C  CD1 . LEU   A 1 255 ? 9.42700   -38.78900 -8.23300  1.000 54.53647  ? 289 LEU   A CD1 1 
ATOM   2065 C  CD2 . LEU   A 1 255 ? 9.76000   -41.03900 -9.28100  1.000 55.25737  ? 289 LEU   A CD2 1 
ATOM   2066 N  N   . ASP   A 1 256 ? 7.82900   -41.71100 -4.76200  1.000 52.98311  ? 290 ASP   A N   1 
ATOM   2067 C  CA  . ASP   A 1 256 ? 6.44600   -42.06900 -4.46400  1.000 53.10839  ? 290 ASP   A CA  1 
ATOM   2068 C  C   . ASP   A 1 256 ? 5.89400   -41.24000 -3.31100  1.000 55.44197  ? 290 ASP   A C   1 
ATOM   2069 O  O   . ASP   A 1 256 ? 4.71200   -40.87700 -3.31100  1.000 58.13271  ? 290 ASP   A O   1 
ATOM   2070 C  CB  . ASP   A 1 256 ? 6.34200   -43.56100 -4.14600  1.000 72.04461  ? 290 ASP   A CB  1 
ATOM   2071 C  CG  . ASP   A 1 256 ? 6.32300   -44.42400 -5.39300  1.000 79.30264  ? 290 ASP   A CG  1 
ATOM   2072 O  OD1 . ASP   A 1 256 ? 5.89400   -43.92500 -6.45500  1.000 81.41267  ? 290 ASP   A OD1 1 
ATOM   2073 O  OD2 . ASP   A 1 256 ? 6.72900   -45.60300 -5.30900  1.000 75.81105  ? 290 ASP   A OD2 1 
ATOM   2074 N  N   . SER   A 1 257 ? 6.73400   -40.92700 -2.32300  1.000 52.72545  ? 291 SER   A N   1 
ATOM   2075 C  CA  . SER   A 1 257 ? 6.26900   -40.17000 -1.16500  1.000 48.86951  ? 291 SER   A CA  1 
ATOM   2076 C  C   . SER   A 1 257 ? 5.89500   -38.74400 -1.55100  1.000 55.26023  ? 291 SER   A C   1 
ATOM   2077 O  O   . SER   A 1 257 ? 4.82000   -38.25400 -1.18700  1.000 59.43990  ? 291 SER   A O   1 
ATOM   2078 C  CB  . SER   A 1 257 ? 7.33900   -40.17000 -0.07400  1.000 52.23212  ? 291 SER   A CB  1 
ATOM   2079 O  OG  . SER   A 1 257 ? 6.93000   -39.39700 1.04100   1.000 68.44229  ? 291 SER   A OG  1 
ATOM   2080 N  N   . VAL   A 1 258 ? 6.77300   -38.06000 -2.29100  1.000 56.39428  ? 292 VAL   A N   1 
ATOM   2081 C  CA  . VAL   A 1 258 ? 6.50100   -36.67800 -2.66800  1.000 53.99226  ? 292 VAL   A CA  1 
ATOM   2082 C  C   . VAL   A 1 258 ? 5.37900   -36.58300 -3.69300  1.000 58.14689  ? 292 VAL   A C   1 
ATOM   2083 O  O   . VAL   A 1 258 ? 4.74800   -35.52700 -3.81700  1.000 56.73614  ? 292 VAL   A O   1 
ATOM   2084 C  CB  . VAL   A 1 258 ? 7.78000   -35.99700 -3.19300  1.000 44.45098  ? 292 VAL   A CB  1 
ATOM   2085 C  CG1 . VAL   A 1 258 ? 8.88000   -36.06100 -2.14700  1.000 41.07765  ? 292 VAL   A CG1 1 
ATOM   2086 C  CG2 . VAL   A 1 258 ? 8.23500   -36.64000 -4.49100  1.000 52.62923  ? 292 VAL   A CG2 1 
ATOM   2087 N  N   . ARG   A 1 259 ? 5.11300   -37.66000 -4.43400  1.000 58.55473  ? 293 ARG   A N   1 
ATOM   2088 C  CA  . ARG   A 1 259 ? 3.97600   -37.68100 -5.34500  1.000 60.66028  ? 293 ARG   A CA  1 
ATOM   2089 C  C   . ARG   A 1 259 ? 2.65000   -37.84900 -4.61800  1.000 58.55758  ? 293 ARG   A C   1 
ATOM   2090 O  O   . ARG   A 1 259 ? 1.60000   -37.56100 -5.20100  1.000 69.57354  ? 293 ARG   A O   1 
ATOM   2091 C  CB  . ARG   A 1 259 ? 4.14200   -38.80000 -6.37400  1.000 60.70451  ? 293 ARG   A CB  1 
ATOM   2092 C  CG  . ARG   A 1 259 ? 5.08300   -38.45800 -7.51800  1.000 62.69795  ? 293 ARG   A CG  1 
ATOM   2093 C  CD  . ARG   A 1 259 ? 5.25700   -39.63300 -8.46800  1.000 57.64203  ? 293 ARG   A CD  1 
ATOM   2094 N  NE  . ARG   A 1 259 ? 5.99200   -39.25300 -9.66900  1.000 56.10436  ? 293 ARG   A NE  1 
ATOM   2095 C  CZ  . ARG   A 1 259 ? 6.39000   -40.10300 -10.60500 1.000 60.92812  ? 293 ARG   A CZ  1 
ATOM   2096 N  NH1 . ARG   A 1 259 ? 6.15800   -41.40100 -10.50400 1.000 53.40463  ? 293 ARG   A NH1 1 
ATOM   2097 N  NH2 . ARG   A 1 259 ? 7.04000   -39.63800 -11.66900 1.000 61.33174  ? 293 ARG   A NH2 1 
ATOM   2098 N  N   . SER   A 1 260 ? 2.67700   -38.29900 -3.36600  1.000 57.56013  ? 294 SER   A N   1 
ATOM   2099 C  CA  . SER   A 1 260 ? 1.47300   -38.51200 -2.57700  1.000 54.25351  ? 294 SER   A CA  1 
ATOM   2100 C  C   . SER   A 1 260 ? 1.16300   -37.35200 -1.64000  1.000 54.66057  ? 294 SER   A C   1 
ATOM   2101 O  O   . SER   A 1 260 ? 0.18800   -37.42700 -0.88700  1.000 67.49895  ? 294 SER   A O   1 
ATOM   2102 C  CB  . SER   A 1 260 ? 1.60100   -39.80500 -1.76400  1.000 58.79000  ? 294 SER   A CB  1 
ATOM   2103 O  OG  . SER   A 1 260 ? 1.92500   -40.90300 -2.60000  1.000 74.67740  ? 294 SER   A OG  1 
ATOM   2104 N  N   . LEU   A 1 261 ? 1.95900   -36.28900 -1.66900  1.000 66.88794  ? 295 LEU   A N   1 
ATOM   2105 C  CA  . LEU   A 1 261 ? 1.74000   -35.17200 -0.76300  1.000 57.42073  ? 295 LEU   A CA  1 
ATOM   2106 C  C   . LEU   A 1 261 ? 0.49600   -34.38700 -1.17500  1.000 62.91200  ? 295 LEU   A C   1 
ATOM   2107 O  O   . LEU   A 1 261 ? 0.26500   -34.17200 -2.36900  1.000 64.13890  ? 295 LEU   A O   1 
ATOM   2108 C  CB  . LEU   A 1 261 ? 2.95400   -34.24500 -0.75200  1.000 57.34169  ? 295 LEU   A CB  1 
ATOM   2109 C  CG  . LEU   A 1 261 ? 4.22300   -34.77100 -0.08100  1.000 56.03210  ? 295 LEU   A CG  1 
ATOM   2110 C  CD1 . LEU   A 1 261 ? 5.39700   -33.85200 -0.37200  1.000 52.87694  ? 295 LEU   A CD1 1 
ATOM   2111 C  CD2 . LEU   A 1 261 ? 4.01000   -34.91000 1.41800   1.000 42.70627  ? 295 LEU   A CD2 1 
ATOM   2112 N  N   . PRO   A 1 262 ? -0.32500  -33.95800 -0.21700  1.000 66.30780  ? 296 PRO   A N   1 
ATOM   2113 C  CA  . PRO   A 1 262 ? -1.43500  -33.05800 -0.54400  1.000 54.83017  ? 296 PRO   A CA  1 
ATOM   2114 C  C   . PRO   A 1 262 ? -0.92800  -31.74000 -1.11100  1.000 57.18460  ? 296 PRO   A C   1 
ATOM   2115 O  O   . PRO   A 1 262 ? 0.24800   -31.39000 -0.99200  1.000 60.89994  ? 296 PRO   A O   1 
ATOM   2116 C  CB  . PRO   A 1 262 ? -2.13900  -32.85300 0.80300   1.000 57.36841  ? 296 PRO   A CB  1 
ATOM   2117 C  CG  . PRO   A 1 262 ? -1.77100  -34.06000 1.60400   1.000 62.65434  ? 296 PRO   A CG  1 
ATOM   2118 C  CD  . PRO   A 1 262 ? -0.37200  -34.40900 1.18400   1.000 65.08264  ? 296 PRO   A CD  1 
ATOM   2119 N  N   . PHE   A 1 263 ? -1.84800  -30.99800 -1.73200  1.000 70.40025  ? 297 PHE   A N   1 
ATOM   2120 C  CA  . PHE   A 1 263 ? -1.45900  -29.79300 -2.45900  1.000 67.78005  ? 297 PHE   A CA  1 
ATOM   2121 C  C   . PHE   A 1 263 ? -0.85400  -28.74300 -1.53300  1.000 63.60748  ? 297 PHE   A C   1 
ATOM   2122 O  O   . PHE   A 1 263 ? 0.15500   -28.11400 -1.87300  1.000 67.94686  ? 297 PHE   A O   1 
ATOM   2123 C  CB  . PHE   A 1 263 ? -2.66300  -29.22000 -3.20600  1.000 62.05260  ? 297 PHE   A CB  1 
ATOM   2124 C  CG  . PHE   A 1 263 ? -2.40900  -27.87600 -3.82200  1.000 62.65041  ? 297 PHE   A CG  1 
ATOM   2125 C  CD1 . PHE   A 1 263 ? -1.62500  -27.75500 -4.95700  1.000 63.66755  ? 297 PHE   A CD1 1 
ATOM   2126 C  CD2 . PHE   A 1 263 ? -2.95900  -26.73100 -3.26800  1.000 65.10422  ? 297 PHE   A CD2 1 
ATOM   2127 C  CE1 . PHE   A 1 263 ? -1.39000  -26.51700 -5.52500  1.000 63.66274  ? 297 PHE   A CE1 1 
ATOM   2128 C  CE2 . PHE   A 1 263 ? -2.72800  -25.49100 -3.83200  1.000 58.94700  ? 297 PHE   A CE2 1 
ATOM   2129 C  CZ  . PHE   A 1 263 ? -1.94300  -25.38400 -4.96200  1.000 68.01420  ? 297 PHE   A CZ  1 
ATOM   2130 N  N   . ASP   A 1 264 ? -1.44600  -28.54300 -0.35700  1.000 73.47594  ? 298 ASP   A N   1 
ATOM   2131 C  CA  . ASP   A 1 264 ? -1.02800  -27.48700 0.55500   1.000 70.04859  ? 298 ASP   A CA  1 
ATOM   2132 C  C   . ASP   A 1 264 ? -0.20400  -28.00000 1.73100   1.000 65.81124  ? 298 ASP   A C   1 
ATOM   2133 O  O   . ASP   A 1 264 ? 0.08900   -27.22800 2.65100   1.000 73.58260  ? 298 ASP   A O   1 
ATOM   2134 C  CB  . ASP   A 1 264 ? -2.25200  -26.72100 1.06900   1.000 64.54638  ? 298 ASP   A CB  1 
ATOM   2135 C  CG  . ASP   A 1 264 ? -3.22300  -27.60300 1.84300   1.000 66.67963  ? 298 ASP   A CG  1 
ATOM   2136 O  OD1 . ASP   A 1 264 ? -3.00700  -28.83200 1.92400   1.000 71.68440  ? 298 ASP   A OD1 1 
ATOM   2137 O  OD2 . ASP   A 1 264 ? -4.21300  -27.06100 2.37800   1.000 77.81584  ? 298 ASP   A OD2 1 
ATOM   2138 N  N   . ALA   A 1 265 ? 0.18100   -29.27200 1.72100   1.000 62.24467  ? 299 ALA   A N   1 
ATOM   2139 C  CA  . ALA   A 1 265 ? 0.88200   -29.86500 2.85000   1.000 61.96369  ? 299 ALA   A CA  1 
ATOM   2140 C  C   . ALA   A 1 265 ? 2.34000   -29.42100 2.89200   1.000 65.62887  ? 299 ALA   A C   1 
ATOM   2141 O  O   . ALA   A 1 265 ? 2.96700   -29.17300 1.86000   1.000 59.09751  ? 299 ALA   A O   1 
ATOM   2142 C  CB  . ALA   A 1 265 ? 0.80800   -31.38900 2.78200   1.000 62.58782  ? 299 ALA   A CB  1 
ATOM   2143 N  N   . GLU   A 1 266 ? 2.87600   -29.32500 4.10900   1.000 70.70275  ? 300 GLU   A N   1 
ATOM   2144 C  CA  . GLU   A 1 266 ? 4.28900   -29.02700 4.29700   1.000 71.05769  ? 300 GLU   A CA  1 
ATOM   2145 C  C   . GLU   A 1 266 ? 5.08400   -30.32200 4.22400   1.000 62.11370  ? 300 GLU   A C   1 
ATOM   2146 O  O   . GLU   A 1 266 ? 4.86000   -31.21900 5.04900   1.000 73.33976  ? 300 GLU   A O   1 
ATOM   2147 C  CB  . GLU   A 1 266 ? 4.53100   -28.34200 5.63100   1.000 74.21131  ? 300 GLU   A CB  1 
ATOM   2148 C  CG  . GLU   A 1 266 ? 5.94700   -27.81700 5.80000   1.000 70.48717  ? 300 GLU   A CG  1 
ATOM   2149 C  CD  . GLU   A 1 266 ? 6.39700   -27.81500 7.24400   1.000 89.14330  ? 300 GLU   A CD  1 
ATOM   2150 O  OE1 . GLU   A 1 266 ? 6.02600   -28.75000 7.98400   1.000 100.04048 ? 300 GLU   A OE1 1 
ATOM   2151 O  OE2 . GLU   A 1 266 ? 7.12200   -26.88000 7.64100   1.000 94.45650  ? 300 GLU   A OE2 1 
ATOM   2152 N  N   . PRO   A 1 267 ? 6.00200   -30.46900 3.26800   1.000 61.77131  ? 301 PRO   A N   1 
ATOM   2153 C  CA  . PRO   A 1 267 ? 6.68000   -31.75100 3.10800   1.000 54.81848  ? 301 PRO   A CA  1 
ATOM   2154 C  C   . PRO   A 1 267 ? 7.64900   -32.00100 4.25000   1.000 60.41972  ? 301 PRO   A C   1 
ATOM   2155 O  O   . PRO   A 1 267 ? 8.19700   -31.05400 4.83700   1.000 62.31443  ? 301 PRO   A O   1 
ATOM   2156 C  CB  . PRO   A 1 267 ? 7.42500   -31.59200 1.76900   1.000 56.13353  ? 301 PRO   A CB  1 
ATOM   2157 C  CG  . PRO   A 1 267 ? 6.80500   -30.39400 1.10800   1.000 54.62666  ? 301 PRO   A CG  1 
ATOM   2158 C  CD  . PRO   A 1 267 ? 6.38200   -29.50600 2.22500   1.000 52.30017  ? 301 PRO   A CD  1 
ATOM   2159 N  N   . PRO   A 1 268 ? 7.88300   -33.26400 4.60700   1.000 63.04766  ? 302 PRO   A N   1 
ATOM   2160 C  CA  . PRO   A 1 268 ? 8.90100   -33.55800 5.62600   1.000 61.86476  ? 302 PRO   A CA  1 
ATOM   2161 C  C   . PRO   A 1 268 ? 10.31100  -33.54300 5.04400   1.000 56.18279  ? 302 PRO   A C   1 
ATOM   2162 O  O   . PRO   A 1 268 ? 10.84700  -34.58300 4.64700   1.000 55.87963  ? 302 PRO   A O   1 
ATOM   2163 C  CB  . PRO   A 1 268 ? 8.49400   -34.94800 6.12800   1.000 60.77684  ? 302 PRO   A CB  1 
ATOM   2164 C  CG  . PRO   A 1 268 ? 7.84100   -35.58600 4.94400   1.000 59.06329  ? 302 PRO   A CG  1 
ATOM   2165 C  CD  . PRO   A 1 268 ? 7.16100   -34.47700 4.18100   1.000 52.21390  ? 302 PRO   A CD  1 
ATOM   2166 N  N   . TYR   A 1 269 ? 10.92800  -32.35800 4.98800   1.000 55.99427  ? 303 TYR   A N   1 
ATOM   2167 C  CA  . TYR   A 1 269 ? 12.24100  -32.23500 4.35700   1.000 52.02864  ? 303 TYR   A CA  1 
ATOM   2168 C  C   . TYR   A 1 269 ? 13.28800  -33.06100 5.09100   1.000 59.41721  ? 303 TYR   A C   1 
ATOM   2169 O  O   . TYR   A 1 269 ? 14.07700  -33.77900 4.46600   1.000 61.85453  ? 303 TYR   A O   1 
ATOM   2170 C  CB  . TYR   A 1 269 ? 12.67000  -30.77100 4.29900   1.000 51.91824  ? 303 TYR   A CB  1 
ATOM   2171 C  CG  . TYR   A 1 269 ? 11.64700  -29.84800 3.67800   1.000 50.96730  ? 303 TYR   A CG  1 
ATOM   2172 C  CD1 . TYR   A 1 269 ? 11.62900  -29.61800 2.30700   1.000 35.77452  ? 303 TYR   A CD1 1 
ATOM   2173 C  CD2 . TYR   A 1 269 ? 10.70300  -29.20300 4.46300   1.000 41.18071  ? 303 TYR   A CD2 1 
ATOM   2174 C  CE1 . TYR   A 1 269 ? 10.69400  -28.77300 1.73800   1.000 48.74876  ? 303 TYR   A CE1 1 
ATOM   2175 C  CE2 . TYR   A 1 269 ? 9.76500   -28.35800 3.90400   1.000 44.34589  ? 303 TYR   A CE2 1 
ATOM   2176 C  CZ  . TYR   A 1 269 ? 9.76500   -28.14700 2.54200   1.000 44.01316  ? 303 TYR   A CZ  1 
ATOM   2177 O  OH  . TYR   A 1 269 ? 8.83000   -27.30500 1.98800   1.000 54.93359  ? 303 TYR   A OH  1 
ATOM   2178 N  N   . GLU   A 1 270 ? 13.31200  -32.96900 6.42300   1.000 52.46934  ? 304 GLU   A N   1 
ATOM   2179 C  CA  . GLU   A 1 270 ? 14.33100  -33.68100 7.18700   1.000 44.41426  ? 304 GLU   A CA  1 
ATOM   2180 C  C   . GLU   A 1 270 ? 14.12800  -35.18900 7.10300   1.000 58.56594  ? 304 GLU   A C   1 
ATOM   2181 O  O   . GLU   A 1 270 ? 15.10000  -35.95400 7.08400   1.000 63.57488  ? 304 GLU   A O   1 
ATOM   2182 C  CB  . GLU   A 1 270 ? 14.31800  -33.21200 8.64200   1.000 46.33700  ? 304 GLU   A CB  1 
ATOM   2183 C  CG  . GLU   A 1 270 ? 15.46900  -33.74800 9.49200   1.000 72.30504  ? 304 GLU   A CG  1 
ATOM   2184 C  CD  . GLU   A 1 270 ? 16.80200  -33.07400 9.19900   1.000 68.05552  ? 304 GLU   A CD  1 
ATOM   2185 O  OE1 . GLU   A 1 270 ? 17.21600  -33.02300 8.02200   1.000 52.29573  ? 304 GLU   A OE1 1 
ATOM   2186 O  OE2 . GLU   A 1 270 ? 17.43800  -32.58700 10.15700  1.000 88.82249  ? 304 GLU   A OE2 1 
ATOM   2187 N  N   . GLU   A 1 271 ? 12.87100  -35.63400 7.04900   1.000 59.63361  ? 305 GLU   A N   1 
ATOM   2188 C  CA  . GLU   A 1 271 ? 12.59700  -37.05300 6.86100   1.000 52.07224  ? 305 GLU   A CA  1 
ATOM   2189 C  C   . GLU   A 1 271 ? 13.08100  -37.53700 5.50000   1.000 58.00054  ? 305 GLU   A C   1 
ATOM   2190 O  O   . GLU   A 1 271 ? 13.52400  -38.68400 5.37300   1.000 55.93934  ? 305 GLU   A O   1 
ATOM   2191 C  CB  . GLU   A 1 271 ? 11.10100  -37.31600 7.02800   1.000 59.99869  ? 305 GLU   A CB  1 
ATOM   2192 C  CG  . GLU   A 1 271 ? 10.77100  -38.47600 7.94900   1.000 65.82348  ? 305 GLU   A CG  1 
ATOM   2193 C  CD  . GLU   A 1 271 ? 9.28900   -38.58100 8.24200   1.000 95.98999  ? 305 GLU   A CD  1 
ATOM   2194 O  OE1 . GLU   A 1 271 ? 8.71100   -37.60100 8.75900   1.000 99.99903  ? 305 GLU   A OE1 1 
ATOM   2195 O  OE2 . GLU   A 1 271 ? 8.70100   -39.64100 7.94700   1.000 96.92402  ? 305 GLU   A OE2 1 
ATOM   2196 N  N   . TYR   A 1 272 ? 13.01400  -36.67900 4.47900   1.000 47.32589  ? 306 TYR   A N   1 
ATOM   2197 C  CA  . TYR   A 1 272 ? 13.51500  -37.05500 3.16100   1.000 46.60469  ? 306 TYR   A CA  1 
ATOM   2198 C  C   . TYR   A 1 272 ? 15.03800  -37.11900 3.14400   1.000 55.23202  ? 306 TYR   A C   1 
ATOM   2199 O  O   . TYR   A 1 272 ? 15.61900  -38.02800 2.53900   1.000 43.72750  ? 306 TYR   A O   1 
ATOM   2200 C  CB  . TYR   A 1 272 ? 13.01000  -36.07200 2.10400   1.000 35.34130  ? 306 TYR   A CB  1 
ATOM   2201 C  CG  . TYR   A 1 272 ? 11.52000  -36.14100 1.86500   1.000 56.01671  ? 306 TYR   A CG  1 
ATOM   2202 C  CD1 . TYR   A 1 272 ? 10.83100  -37.34000 1.99500   1.000 46.28210  ? 306 TYR   A CD1 1 
ATOM   2203 C  CD2 . TYR   A 1 272 ? 10.80000  -35.00700 1.51000   1.000 55.50131  ? 306 TYR   A CD2 1 
ATOM   2204 C  CE1 . TYR   A 1 272 ? 9.46800   -37.40800 1.77700   1.000 55.33060  ? 306 TYR   A CE1 1 
ATOM   2205 C  CE2 . TYR   A 1 272 ? 9.43800   -35.06500 1.29100   1.000 52.80316  ? 306 TYR   A CE2 1 
ATOM   2206 C  CZ  . TYR   A 1 272 ? 8.77700   -36.26800 1.42600   1.000 55.60123  ? 306 TYR   A CZ  1 
ATOM   2207 O  OH  . TYR   A 1 272 ? 7.42000   -36.33200 1.20800   1.000 57.10875  ? 306 TYR   A OH  1 
ATOM   2208 N  N   . ARG   A 1 273 ? 15.70000  -36.15900 3.79500   1.000 45.01927  ? 307 ARG   A N   1 
ATOM   2209 C  CA  . ARG   A 1 273 ? 17.15800  -36.18100 3.85200   1.000 46.14580  ? 307 ARG   A CA  1 
ATOM   2210 C  C   . ARG   A 1 273 ? 17.65800  -37.38800 4.63400   1.000 57.80693  ? 307 ARG   A C   1 
ATOM   2211 O  O   . ARG   A 1 273 ? 18.66600  -38.00200 4.26500   1.000 54.00552  ? 307 ARG   A O   1 
ATOM   2212 C  CB  . ARG   A 1 273 ? 17.68400  -34.88500 4.46900   1.000 44.95861  ? 307 ARG   A CB  1 
ATOM   2213 C  CG  . ARG   A 1 273 ? 17.56400  -33.67300 3.56100   1.000 43.43973  ? 307 ARG   A CG  1 
ATOM   2214 C  CD  . ARG   A 1 273 ? 18.27600  -32.46800 4.15200   1.000 51.94534  ? 307 ARG   A CD  1 
ATOM   2215 N  NE  . ARG   A 1 273 ? 17.57100  -31.92400 5.30700   1.000 47.80169  ? 307 ARG   A NE  1 
ATOM   2216 C  CZ  . ARG   A 1 273 ? 16.71900  -30.91000 5.25100   1.000 53.40180  ? 307 ARG   A CZ  1 
ATOM   2217 N  NH1 . ARG   A 1 273 ? 16.44600  -30.30100 4.10800   1.000 52.16605  ? 307 ARG   A NH1 1 
ATOM   2218 N  NH2 . ARG   A 1 273 ? 16.13200  -30.49300 6.36900   1.000 45.42999  ? 307 ARG   A NH2 1 
ATOM   2219 N  N   . MET   A 1 274 ? 16.96700  -37.74400 5.72000   1.000 50.05841  ? 308 MET   A N   1 
ATOM   2220 C  CA  . MET   A 1 274 ? 17.32300  -38.95000 6.45800   1.000 52.20850  ? 308 MET   A CA  1 
ATOM   2221 C  C   . MET   A 1 274 ? 17.04600  -40.20500 5.64200   1.000 54.15255  ? 308 MET   A C   1 
ATOM   2222 O  O   . MET   A 1 274 ? 17.73800  -41.21700 5.80700   1.000 64.58646  ? 308 MET   A O   1 
ATOM   2223 C  CB  . MET   A 1 274 ? 16.56500  -38.99800 7.78500   1.000 47.85540  ? 308 MET   A CB  1 
ATOM   2224 C  CG  . MET   A 1 274 ? 16.99400  -37.93900 8.78800   1.000 68.66355  ? 308 MET   A CG  1 
ATOM   2225 S  SD  . MET   A 1 274 ? 18.71500  -38.12300 9.29000   1.000 89.11347  ? 308 MET   A SD  1 
ATOM   2226 C  CE  . MET   A 1 274 ? 18.69700  -39.79300 9.93800   1.000 82.13794  ? 308 MET   A CE  1 
ATOM   2227 N  N   . LEU   A 1 275 ? 16.04500  -40.15900 4.75900   1.000 50.78799  ? 309 LEU   A N   1 
ATOM   2228 C  CA  . LEU   A 1 275 ? 15.77100  -41.29900 3.89000   1.000 56.82348  ? 309 LEU   A CA  1 
ATOM   2229 C  C   . LEU   A 1 275 ? 16.89600  -41.50900 2.88500   1.000 56.46805  ? 309 LEU   A C   1 
ATOM   2230 O  O   . LEU   A 1 275 ? 17.33300  -42.64400 2.66100   1.000 58.19732  ? 309 LEU   A O   1 
ATOM   2231 C  CB  . LEU   A 1 275 ? 14.43800  -41.09800 3.17000   1.000 42.81471  ? 309 LEU   A CB  1 
ATOM   2232 C  CG  . LEU   A 1 275 ? 14.05600  -42.14800 2.12600   1.000 41.97726  ? 309 LEU   A CG  1 
ATOM   2233 C  CD1 . LEU   A 1 275 ? 13.81300  -43.49600 2.78300   1.000 48.36797  ? 309 LEU   A CD1 1 
ATOM   2234 C  CD2 . LEU   A 1 275 ? 12.83500  -41.70200 1.33700   1.000 53.93369  ? 309 LEU   A CD2 1 
ATOM   2235 N  N   . LEU   A 1 276 ? 17.37800  -40.42900 2.27000   1.000 55.87797  ? 310 LEU   A N   1 
ATOM   2236 C  CA  . LEU   A 1 276 ? 18.47300  -40.55900 1.31600   1.000 54.07915  ? 310 LEU   A CA  1 
ATOM   2237 C  C   . LEU   A 1 276 ? 19.79500  -40.83300 2.01900   1.000 56.67036  ? 310 LEU   A C   1 
ATOM   2238 O  O   . LEU   A 1 276 ? 20.68900  -41.45500 1.43400   1.000 54.37935  ? 310 LEU   A O   1 
ATOM   2239 C  CB  . LEU   A 1 276 ? 18.57400  -39.29600 0.46100   1.000 53.35898  ? 310 LEU   A CB  1 
ATOM   2240 C  CG  . LEU   A 1 276 ? 17.26200  -38.86800 -0.20500  1.000 44.42943  ? 310 LEU   A CG  1 
ATOM   2241 C  CD1 . LEU   A 1 276 ? 17.45300  -37.60500 -1.02700  1.000 55.79001  ? 310 LEU   A CD1 1 
ATOM   2242 C  CD2 . LEU   A 1 276 ? 16.70600  -39.99200 -1.06300  1.000 46.67740  ? 310 LEU   A CD2 1 
ATOM   2243 N  N   . LEU   A 1 277 ? 19.93600  -40.38500 3.26900   1.000 59.22451  ? 311 LEU   A N   1 
ATOM   2244 C  CA  . LEU   A 1 277 ? 21.16500  -40.63300 4.01200   1.000 57.59567  ? 311 LEU   A CA  1 
ATOM   2245 C  C   . LEU   A 1 277 ? 21.31400  -42.10100 4.38600   1.000 62.30050  ? 311 LEU   A C   1 
ATOM   2246 O  O   . LEU   A 1 277 ? 22.43900  -42.60700 4.46000   1.000 67.78453  ? 311 LEU   A O   1 
ATOM   2247 C  CB  . LEU   A 1 277 ? 21.20500  -39.75800 5.26500   1.000 52.95710  ? 311 LEU   A CB  1 
ATOM   2248 C  CG  . LEU   A 1 277 ? 22.08200  -38.50800 5.19500   1.000 65.15205  ? 311 LEU   A CG  1 
ATOM   2249 C  CD1 . LEU   A 1 277 ? 21.68000  -37.51200 6.26900   1.000 67.45508  ? 311 LEU   A CD1 1 
ATOM   2250 C  CD2 . LEU   A 1 277 ? 23.54600  -38.89000 5.34100   1.000 73.58261  ? 311 LEU   A CD2 1 
ATOM   2251 N  N   . SER   A 1 278 ? 20.20000  -42.80100 4.62100   1.000 57.40033  ? 312 SER   A N   1 
ATOM   2252 C  CA  . SER   A 1 278 ? 20.27000  -44.21800 4.95900   1.000 63.05280  ? 312 SER   A CA  1 
ATOM   2253 C  C   . SER   A 1 278 ? 20.80700  -45.05800 3.80900   1.000 61.35147  ? 312 SER   A C   1 
ATOM   2254 O  O   . SER   A 1 278 ? 21.19300  -46.21100 4.02900   1.000 63.96564  ? 312 SER   A O   1 
ATOM   2255 C  CB  . SER   A 1 278 ? 18.89300  -44.73400 5.38100   1.000 57.30348  ? 312 SER   A CB  1 
ATOM   2256 O  OG  . SER   A 1 278 ? 18.00900  -44.80000 4.27700   1.000 62.32187  ? 312 SER   A OG  1 
ATOM   2257 N  N   . VAL   A 1 279 ? 20.83000  -44.51100 2.59100   1.000 56.92364  ? 313 VAL   A N   1 
ATOM   2258 C  CA  . VAL   A 1 279 ? 21.46900  -45.20300 1.47600   1.000 53.23674  ? 313 VAL   A CA  1 
ATOM   2259 C  C   . VAL   A 1 279 ? 22.95000  -45.40700 1.75900   1.000 61.24139  ? 313 VAL   A C   1 
ATOM   2260 O  O   . VAL   A 1 279 ? 23.50700  -46.48100 1.50200   1.000 64.51806  ? 313 VAL   A O   1 
ATOM   2261 C  CB  . VAL   A 1 279 ? 21.25100  -44.42400 0.16600   1.000 50.14671  ? 313 VAL   A CB  1 
ATOM   2262 C  CG1 . VAL   A 1 279 ? 22.03100  -45.06200 -0.96300  1.000 42.02201  ? 313 VAL   A CG1 1 
ATOM   2263 C  CG2 . VAL   A 1 279 ? 19.77600  -44.35500 -0.17300  1.000 43.67493  ? 313 VAL   A CG2 1 
ATOM   2264 N  N   . LEU   A 1 280 ? 23.61100  -44.37900 2.29800   1.000 66.24094  ? 314 LEU   A N   1 
ATOM   2265 C  CA  . LEU   A 1 280 ? 25.03700  -44.48400 2.58200   1.000 64.20638  ? 314 LEU   A CA  1 
ATOM   2266 C  C   . LEU   A 1 280 ? 25.31800  -45.47600 3.70400   1.000 58.27982  ? 314 LEU   A C   1 
ATOM   2267 O  O   . LEU   A 1 280 ? 26.35600  -46.14500 3.68800   1.000 59.68309  ? 314 LEU   A O   1 
ATOM   2268 C  CB  . LEU   A 1 280 ? 25.60600  -43.10800 2.92700   1.000 60.12140  ? 314 LEU   A CB  1 
ATOM   2269 C  CG  . LEU   A 1 280 ? 25.44200  -42.03700 1.84600   1.000 51.10906  ? 314 LEU   A CG  1 
ATOM   2270 C  CD1 . LEU   A 1 280 ? 26.17000  -40.75900 2.23500   1.000 55.83362  ? 314 LEU   A CD1 1 
ATOM   2271 C  CD2 . LEU   A 1 280 ? 25.93500  -42.55300 0.50100   1.000 52.07340  ? 314 LEU   A CD2 1 
ATOM   2272 N  N   . ASP   A 1 281 ? 24.41300  -45.59100 4.68000   1.000 72.50472  ? 315 ASP   A N   1 
ATOM   2273 C  CA  . ASP   A 1 281 ? 24.60100  -46.59000 5.72700   1.000 73.11015  ? 315 ASP   A CA  1 
ATOM   2274 C  C   . ASP   A 1 281 ? 24.38500  -48.00200 5.20000   1.000 58.98134  ? 315 ASP   A C   1 
ATOM   2275 O  O   . ASP   A 1 281 ? 25.05700  -48.93800 5.64700   1.000 64.96093  ? 315 ASP   A O   1 
ATOM   2276 C  CB  . ASP   A 1 281 ? 23.66700  -46.31500 6.90600   1.000 73.19019  ? 315 ASP   A CB  1 
ATOM   2277 C  CG  . ASP   A 1 281 ? 24.03400  -45.04900 7.65900   1.000 86.51439  ? 315 ASP   A CG  1 
ATOM   2278 O  OD1 . ASP   A 1 281 ? 25.19100  -44.59000 7.52800   1.000 94.39451  ? 315 ASP   A OD1 1 
ATOM   2279 O  OD2 . ASP   A 1 281 ? 23.16400  -44.50500 8.37300   1.000 93.46614  ? 315 ASP   A OD2 1 
ATOM   2280 N  N   . ASP   A 1 282 ? 23.46000  -48.17500 4.25200   1.000 58.58294  ? 316 ASP   A N   1 
ATOM   2281 C  CA  . ASP   A 1 282 ? 23.24000  -49.49500 3.66900   1.000 75.84303  ? 316 ASP   A CA  1 
ATOM   2282 C  C   . ASP   A 1 282 ? 24.42300  -49.93700 2.81900   1.000 73.53092  ? 316 ASP   A C   1 
ATOM   2283 O  O   . ASP   A 1 282 ? 24.66600  -51.14100 2.67600   1.000 69.84523  ? 316 ASP   A O   1 
ATOM   2284 C  CB  . ASP   A 1 282 ? 21.96200  -49.50000 2.82900   1.000 63.49462  ? 316 ASP   A CB  1 
ATOM   2285 C  CG  . ASP   A 1 282 ? 20.70600  -49.37500 3.67200   1.000 71.77264  ? 316 ASP   A CG  1 
ATOM   2286 O  OD1 . ASP   A 1 282 ? 20.82300  -49.31800 4.91500   1.000 70.88810  ? 316 ASP   A OD1 1 
ATOM   2287 O  OD2 . ASP   A 1 282 ? 19.60100  -49.33600 3.09200   1.000 74.90948  ? 316 ASP   A OD2 1 
ATOM   2288 N  N   . LEU   A 1 283 ? 25.16500  -48.98800 2.25200   1.000 65.31021  ? 317 LEU   A N   1 
ATOM   2289 C  CA  . LEU   A 1 283 ? 26.28800  -49.29000 1.37600   1.000 71.25735  ? 317 LEU   A CA  1 
ATOM   2290 C  C   . LEU   A 1 283 ? 27.64000  -49.11200 2.05500   1.000 65.95162  ? 317 LEU   A C   1 
ATOM   2291 O  O   . LEU   A 1 283 ? 28.67300  -49.27900 1.39800   1.000 72.89147  ? 317 LEU   A O   1 
ATOM   2292 C  CB  . LEU   A 1 283 ? 26.22300  -48.41800 0.11800   1.000 72.43641  ? 317 LEU   A CB  1 
ATOM   2293 C  CG  . LEU   A 1 283 ? 24.93900  -48.54100 -0.70400  1.000 60.64920  ? 317 LEU   A CG  1 
ATOM   2294 C  CD1 . LEU   A 1 283 ? 24.96800  -47.59900 -1.89600  1.000 55.39702  ? 317 LEU   A CD1 1 
ATOM   2295 C  CD2 . LEU   A 1 283 ? 24.72800  -49.97800 -1.15600  1.000 65.48077  ? 317 LEU   A CD2 1 
ATOM   2296 N  N   . GLY   A 1 284 ? 27.66400  -48.78000 3.34200   1.000 60.01848  ? 318 GLY   A N   1 
ATOM   2297 C  CA  . GLY   A 1 284 ? 28.93200  -48.63400 4.04300   1.000 61.86265  ? 318 GLY   A CA  1 
ATOM   2298 C  C   . GLY   A 1 284 ? 29.76200  -47.46500 3.56200   1.000 69.70530  ? 318 GLY   A C   1 
ATOM   2299 O  O   . GLY   A 1 284 ? 30.98500  -47.59000 3.41600   1.000 75.34098  ? 318 GLY   A O   1 
ATOM   2300 N  N   . GLN   A 1 285 ? 29.12200  -46.32900 3.30900   1.000 59.87403  ? 319 GLN   A N   1 
ATOM   2301 C  CA  . GLN   A 1 285 ? 29.78700  -45.13300 2.82400   1.000 55.44224  ? 319 GLN   A CA  1 
ATOM   2302 C  C   . GLN   A 1 285 ? 29.55700  -43.98600 3.79900   1.000 66.07579  ? 319 GLN   A C   1 
ATOM   2303 O  O   . GLN   A 1 285 ? 28.54900  -43.94500 4.51100   1.000 60.66066  ? 319 GLN   A O   1 
ATOM   2304 C  CB  . GLN   A 1 285 ? 29.28200  -44.74000 1.42900   1.000 54.26910  ? 319 GLN   A CB  1 
ATOM   2305 C  CG  . GLN   A 1 285 ? 29.30900  -45.87500 0.41700   1.000 63.89907  ? 319 GLN   A CG  1 
ATOM   2306 C  CD  . GLN   A 1 285 ? 30.71000  -46.40100 0.16700   1.000 71.79116  ? 319 GLN   A CD  1 
ATOM   2307 O  OE1 . GLN   A 1 285 ? 31.68100  -45.64500 0.17800   1.000 73.61079  ? 319 GLN   A OE1 1 
ATOM   2308 N  NE2 . GLN   A 1 285 ? 30.82200  -47.70600 -0.05700  1.000 62.03023  ? 319 GLN   A NE2 1 
ATOM   2309 N  N   . ALA   A 1 286 ? 30.50500  -43.05600 3.82600   1.000 67.01579  ? 320 ALA   A N   1 
ATOM   2310 C  CA  . ALA   A 1 286 ? 30.43800  -41.88900 4.69000   1.000 46.51702  ? 320 ALA   A CA  1 
ATOM   2311 C  C   . ALA   A 1 286 ? 30.01400  -40.66400 3.89000   1.000 62.57619  ? 320 ALA   A C   1 
ATOM   2312 O  O   . ALA   A 1 286 ? 30.28700  -40.55600 2.69200   1.000 64.22199  ? 320 ALA   A O   1 
ATOM   2313 C  CB  . ALA   A 1 286 ? 31.78800  -41.62800 5.36300   1.000 53.40709  ? 320 ALA   A CB  1 
ATOM   2314 N  N   . CYS   A 1 287 ? 29.33500  -39.74000 4.56700   1.000 59.19059  ? 321 CYS   A N   1 
ATOM   2315 C  CA  . CYS   A 1 287 ? 28.93400  -38.47300 3.95500   1.000 59.59180  ? 321 CYS   A CA  1 
ATOM   2316 C  C   . CYS   A 1 287 ? 29.99900  -37.41800 4.25600   1.000 55.12069  ? 321 CYS   A C   1 
ATOM   2317 O  O   . CYS   A 1 287 ? 29.80200  -36.47200 5.02100   1.000 72.90131  ? 321 CYS   A O   1 
ATOM   2318 C  CB  . CYS   A 1 287 ? 27.55800  -38.05100 4.45400   1.000 60.00315  ? 321 CYS   A CB  1 
ATOM   2319 S  SG  . CYS   A 1 287 ? 26.83900  -36.65400 3.56300   1.000 66.42602  ? 321 CYS   A SG  1 
ATOM   2320 N  N   . ASP   A 1 288 ? 31.15700  -37.60700 3.62600   1.000 61.95927  ? 322 ASP   A N   1 
ATOM   2321 C  CA  . ASP   A 1 288 ? 32.33500  -36.78900 3.88400   1.000 53.82333  ? 322 ASP   A CA  1 
ATOM   2322 C  C   . ASP   A 1 288 ? 32.48600  -35.62100 2.91700   1.000 51.08515  ? 322 ASP   A C   1 
ATOM   2323 O  O   . ASP   A 1 288 ? 33.45900  -34.86900 3.02800   1.000 67.06051  ? 322 ASP   A O   1 
ATOM   2324 C  CB  . ASP   A 1 288 ? 33.59500  -37.66300 3.84300   1.000 62.42995  ? 322 ASP   A CB  1 
ATOM   2325 C  CG  . ASP   A 1 288 ? 33.70500  -38.48200 2.56400   1.000 62.84131  ? 322 ASP   A CG  1 
ATOM   2326 O  OD1 . ASP   A 1 288 ? 33.06500  -38.12100 1.55500   1.000 66.27296  ? 322 ASP   A OD1 1 
ATOM   2327 O  OD2 . ASP   A 1 288 ? 34.43200  -39.49800 2.57200   1.000 64.85543  ? 322 ASP   A OD2 1 
ATOM   2328 N  N   . GLY   A 1 289 ? 31.56000  -35.45100 1.98000   1.000 58.54817  ? 323 GLY   A N   1 
ATOM   2329 C  CA  . GLY   A 1 289 ? 31.63700  -34.36700 1.02400   1.000 61.95212  ? 323 GLY   A CA  1 
ATOM   2330 C  C   . GLY   A 1 289 ? 32.50000  -34.62600 -0.18900  1.000 68.04699  ? 323 GLY   A C   1 
ATOM   2331 O  O   . GLY   A 1 289 ? 32.76800  -33.68600 -0.94700  1.000 67.00148  ? 323 GLY   A O   1 
ATOM   2332 N  N   . ASP   A 1 290 ? 32.94400  -35.86300 -0.39900  1.000 53.46080  ? 324 ASP   A N   1 
ATOM   2333 C  CA  . ASP   A 1 290 ? 33.75000  -36.20000 -1.56600  1.000 50.24347  ? 324 ASP   A CA  1 
ATOM   2334 C  C   . ASP   A 1 290 ? 32.83400  -36.44100 -2.76000  1.000 48.88611  ? 324 ASP   A C   1 
ATOM   2335 O  O   . ASP   A 1 290 ? 31.93300  -37.28500 -2.69700  1.000 58.47755  ? 324 ASP   A O   1 
ATOM   2336 C  CB  . ASP   A 1 290 ? 34.60500  -37.43200 -1.28500  1.000 60.95563  ? 324 ASP   A CB  1 
ATOM   2337 C  CG  . ASP   A 1 290 ? 35.82000  -37.51400 -2.18400  1.000 72.73895  ? 324 ASP   A CG  1 
ATOM   2338 O  OD1 . ASP   A 1 290 ? 35.71900  -38.11300 -3.27400  1.000 71.56725  ? 324 ASP   A OD1 1 
ATOM   2339 O  OD2 . ASP   A 1 290 ? 36.87900  -36.97400 -1.79800  1.000 94.56052  ? 324 ASP   A OD2 1 
ATOM   2340 N  N   . MET   A 1 291 ? 33.07000  -35.71400 -3.85000  1.000 46.46028  ? 325 MET   A N   1 
ATOM   2341 C  CA  . MET   A 1 291 ? 32.23000  -35.77500 -5.03500  1.000 39.98740  ? 325 MET   A CA  1 
ATOM   2342 C  C   . MET   A 1 291 ? 33.02100  -36.32900 -6.21300  1.000 43.02840  ? 325 MET   A C   1 
ATOM   2343 O  O   . MET   A 1 291 ? 34.25400  -36.38100 -6.19400  1.000 39.84645  ? 325 MET   A O   1 
ATOM   2344 C  CB  . MET   A 1 291 ? 31.67000  -34.39000 -5.37800  1.000 43.97403  ? 325 MET   A CB  1 
ATOM   2345 C  CG  . MET   A 1 291 ? 31.04400  -33.67000 -4.19200  1.000 49.65941  ? 325 MET   A CG  1 
ATOM   2346 S  SD  . MET   A 1 291 ? 29.37200  -34.23500 -3.81400  1.000 58.04637  ? 325 MET   A SD  1 
ATOM   2347 C  CE  . MET   A 1 291 ? 29.17400  -33.58300 -2.15700  1.000 60.39487  ? 325 MET   A CE  1 
ATOM   2348 N  N   . ASP   A 1 292 ? 32.28700  -36.74100 -7.25100  1.000 40.49418  ? 326 ASP   A N   1 
ATOM   2349 C  CA  . ASP   A 1 292 ? 32.91900  -37.37500 -8.40500  1.000 36.98909  ? 326 ASP   A CA  1 
ATOM   2350 C  C   . ASP   A 1 292 ? 33.75700  -36.38500 -9.20100  1.000 50.61178  ? 326 ASP   A C   1 
ATOM   2351 O  O   . ASP   A 1 292 ? 34.86200  -36.71800 -9.64500  1.000 44.71428  ? 326 ASP   A O   1 
ATOM   2352 C  CB  . ASP   A 1 292 ? 31.85900  -38.00900 -9.30300  1.000 51.03883  ? 326 ASP   A CB  1 
ATOM   2353 C  CG  . ASP   A 1 292 ? 31.15400  -39.16700 -8.63800  1.000 45.48751  ? 326 ASP   A CG  1 
ATOM   2354 O  OD1 . ASP   A 1 292 ? 31.57300  -39.56100 -7.53200  1.000 58.94812  ? 326 ASP   A OD1 1 
ATOM   2355 O  OD2 . ASP   A 1 292 ? 30.17800  -39.67900 -9.22100  1.000 42.27969  ? 326 ASP   A OD2 1 
ATOM   2356 N  N   . TRP   A 1 293 ? 33.24800  -35.16600 -9.40100  1.000 55.05785  ? 327 TRP   A N   1 
ATOM   2357 C  CA  . TRP   A 1 293 ? 33.99100  -34.17500 -10.17000 1.000 47.94697  ? 327 TRP   A CA  1 
ATOM   2358 C  C   . TRP   A 1 293 ? 35.29100  -33.76900 -9.48900  1.000 40.97073  ? 327 TRP   A C   1 
ATOM   2359 O  O   . TRP   A 1 293 ? 36.17200  -33.21000 -10.14900 1.000 44.19414  ? 327 TRP   A O   1 
ATOM   2360 C  CB  . TRP   A 1 293 ? 33.12300  -32.94100 -10.42600 1.000 57.75839  ? 327 TRP   A CB  1 
ATOM   2361 C  CG  . TRP   A 1 293 ? 32.63300  -32.25200 -9.18600  1.000 49.66169  ? 327 TRP   A CG  1 
ATOM   2362 C  CD1 . TRP   A 1 293 ? 33.33500  -31.38700 -8.39600  1.000 39.35985  ? 327 TRP   A CD1 1 
ATOM   2363 C  CD2 . TRP   A 1 293 ? 31.32600  -32.35200 -8.60700  1.000 35.24331  ? 327 TRP   A CD2 1 
ATOM   2364 N  NE1 . TRP   A 1 293 ? 32.54900  -30.95200 -7.35600  1.000 46.92894  ? 327 TRP   A NE1 1 
ATOM   2365 C  CE2 . TRP   A 1 293 ? 31.31100  -31.52900 -7.46400  1.000 41.40080  ? 327 TRP   A CE2 1 
ATOM   2366 C  CE3 . TRP   A 1 293 ? 30.17000  -33.06200 -8.94300  1.000 43.74952  ? 327 TRP   A CE3 1 
ATOM   2367 C  CZ2 . TRP   A 1 293 ? 30.18500  -31.39500 -6.65600  1.000 34.63277  ? 327 TRP   A CZ2 1 
ATOM   2368 C  CZ3 . TRP   A 1 293 ? 29.05400  -32.92900 -8.13900  1.000 47.43057  ? 327 TRP   A CZ3 1 
ATOM   2369 C  CH2 . TRP   A 1 293 ? 29.07000  -32.10300 -7.00800  1.000 35.45313  ? 327 TRP   A CH2 1 
ATOM   2370 N  N   . MET   A 1 294 ? 35.43500  -34.04800 -8.19200  1.000 40.71723  ? 328 MET   A N   1 
ATOM   2371 C  CA  . MET   A 1 294 ? 36.67400  -33.74900 -7.48600  1.000 43.19896  ? 328 MET   A CA  1 
ATOM   2372 C  C   . MET   A 1 294 ? 37.82300  -34.66200 -7.89300  1.000 61.02918  ? 328 MET   A C   1 
ATOM   2373 O  O   . MET   A 1 294 ? 38.96800  -34.39000 -7.51400  1.000 58.79194  ? 328 MET   A O   1 
ATOM   2374 C  CB  . MET   A 1 294 ? 36.44700  -33.84100 -5.97500  1.000 42.53914  ? 328 MET   A CB  1 
ATOM   2375 C  CG  . MET   A 1 294 ? 35.46900  -32.81000 -5.42800  1.000 40.97551  ? 328 MET   A CG  1 
ATOM   2376 S  SD  . MET   A 1 294 ? 35.06400  -33.07400 -3.69000  1.000 56.34166  ? 328 MET   A SD  1 
ATOM   2377 C  CE  . MET   A 1 294 ? 36.69700  -33.17100 -2.96100  1.000 53.03243  ? 328 MET   A CE  1 
ATOM   2378 N  N   . HIS   A 1 295 ? 37.55300  -35.72800 -8.64400  1.000 49.60818  ? 329 HIS   A N   1 
ATOM   2379 C  CA  . HIS   A 1 295 ? 38.58700  -36.63800 -9.11900  1.000 62.46924  ? 329 HIS   A CA  1 
ATOM   2380 C  C   . HIS   A 1 295 ? 38.93000  -36.42900 -10.58700 1.000 61.90472  ? 329 HIS   A C   1 
ATOM   2381 O  O   . HIS   A 1 295 ? 39.75800  -37.17000 -11.12700 1.000 62.38165  ? 329 HIS   A O   1 
ATOM   2382 C  CB  . HIS   A 1 295 ? 38.15600  -38.09200 -8.89500  1.000 57.94225  ? 329 HIS   A CB  1 
ATOM   2383 C  CG  . HIS   A 1 295 ? 38.00900  -38.46300 -7.45200  1.000 54.17773  ? 329 HIS   A CG  1 
ATOM   2384 N  ND1 . HIS   A 1 295 ? 39.08800  -38.59000 -6.60300  1.000 65.17395  ? 329 HIS   A ND1 1 
ATOM   2385 C  CD2 . HIS   A 1 295 ? 36.91200  -38.74200 -6.71000  1.000 50.83842  ? 329 HIS   A CD2 1 
ATOM   2386 C  CE1 . HIS   A 1 295 ? 38.66000  -38.92600 -5.39900  1.000 47.14136  ? 329 HIS   A CE1 1 
ATOM   2387 N  NE2 . HIS   A 1 295 ? 37.34400  -39.02600 -5.43800  1.000 54.01290  ? 329 HIS   A NE2 1 
ATOM   2388 N  N   . LEU   A 1 296 ? 38.31600  -35.44700 -11.24200 1.000 52.96076  ? 330 LEU   A N   1 
ATOM   2389 C  CA  . LEU   A 1 296 ? 38.57900  -35.19800 -12.65100 1.000 59.55463  ? 330 LEU   A CA  1 
ATOM   2390 C  C   . LEU   A 1 296 ? 40.01600  -34.73800 -12.86500 1.000 59.33606  ? 330 LEU   A C   1 
ATOM   2391 O  O   . LEU   A 1 296 ? 40.62200  -34.09500 -12.00500 1.000 65.98760  ? 330 LEU   A O   1 
ATOM   2392 C  CB  . LEU   A 1 296 ? 37.61500  -34.14300 -13.19400 1.000 58.17051  ? 330 LEU   A CB  1 
ATOM   2393 C  CG  . LEU   A 1 296 ? 36.13400  -34.51000 -13.26000 1.000 61.35772  ? 330 LEU   A CG  1 
ATOM   2394 C  CD1 . LEU   A 1 296 ? 35.29900  -33.28100 -13.58400 1.000 61.78528  ? 330 LEU   A CD1 1 
ATOM   2395 C  CD2 . LEU   A 1 296 ? 35.90300  -35.60300 -14.29100 1.000 63.38368  ? 330 LEU   A CD2 1 
ATOM   2396 N  N   . ASN   A 1 297 ? 40.55900  -35.08800 -14.03300 1.000 63.95206  ? 331 ASN   A N   1 
ATOM   2397 C  CA  . ASN   A 1 297 ? 41.88000  -34.62900 -14.46700 1.000 71.08562  ? 331 ASN   A CA  1 
ATOM   2398 C  C   . ASN   A 1 297 ? 42.97100  -35.00200 -13.46400 1.000 83.30018  ? 331 ASN   A C   1 
ATOM   2399 O  O   . ASN   A 1 297 ? 43.90800  -34.23800 -13.22500 1.000 74.61425  ? 331 ASN   A O   1 
ATOM   2400 C  CB  . ASN   A 1 297 ? 41.87600  -33.12200 -14.73600 1.000 76.65742  ? 331 ASN   A CB  1 
ATOM   2401 C  CG  . ASN   A 1 297 ? 40.95400  -32.73700 -15.88200 1.000 60.28957  ? 331 ASN   A CG  1 
ATOM   2402 O  OD1 . ASN   A 1 297 ? 41.33600  -32.80300 -17.05000 1.000 97.95656  ? 331 ASN   A OD1 1 
ATOM   2403 N  ND2 . ASN   A 1 297 ? 39.73400  -32.33100 -15.55100 1.000 75.08951  ? 331 ASN   A ND2 1 
ATOM   2404 N  N   . GLY   A 1 298 ? 42.84900  -36.18800 -12.87200 1.000 73.66344  ? 332 GLY   A N   1 
ATOM   2405 C  CA  . GLY   A 1 298 ? 43.87000  -36.69800 -11.97700 1.000 74.10931  ? 332 GLY   A CA  1 
ATOM   2406 C  C   . GLY   A 1 298 ? 43.73000  -36.24700 -10.53700 1.000 72.27389  ? 332 GLY   A C   1 
ATOM   2407 O  O   . GLY   A 1 298 ? 44.71600  -35.84200 -9.91300  1.000 93.53331  ? 332 GLY   A O   1 
ATOM   2408 N  N   . GLY   A 1 299 ? 42.51700  -36.32800 -9.99200  1.000 92.76632  ? 333 GLY   A N   1 
ATOM   2409 C  CA  . GLY   A 1 299 ? 42.26100  -35.85200 -8.64500  1.000 92.06981  ? 333 GLY   A CA  1 
ATOM   2410 C  C   . GLY   A 1 299 ? 42.51900  -34.36600 -8.53300  1.000 86.36837  ? 333 GLY   A C   1 
ATOM   2411 O  O   . GLY   A 1 299 ? 43.25500  -33.91100 -7.65400  1.000 93.13757  ? 333 GLY   A O   1 
ATOM   2412 N  N   . ARG   A 1 300 ? 41.90000  -33.59800 -9.42600  1.000 96.58974  ? 334 ARG   A N   1 
ATOM   2413 C  CA  . ARG   A 1 300 ? 42.27300  -32.20700 -9.63400  1.000 73.53244  ? 334 ARG   A CA  1 
ATOM   2414 C  C   . ARG   A 1 300 ? 41.04800  -31.31200 -9.76800  1.000 83.58374  ? 334 ARG   A C   1 
ATOM   2415 O  O   . ARG   A 1 300 ? 41.04200  -30.17500 -9.28500  1.000 92.10074  ? 334 ARG   A O   1 
ATOM   2416 C  CB  . ARG   A 1 300 ? 43.15300  -32.10300 -10.87900 1.000 75.87118  ? 334 ARG   A CB  1 
ATOM   2417 C  CG  . ARG   A 1 300 ? 43.31000  -30.70900 -11.43700 1.000 89.26029  ? 334 ARG   A CG  1 
ATOM   2418 C  CD  . ARG   A 1 300 ? 44.72600  -30.21800 -11.24500 1.000 100.04408 ? 334 ARG   A CD  1 
ATOM   2419 N  NE  . ARG   A 1 300 ? 45.10600  -29.26800 -12.28200 1.000 104.61947 ? 334 ARG   A NE  1 
ATOM   2420 C  CZ  . ARG   A 1 300 ? 46.30600  -28.71700 -12.38800 1.000 126.04048 ? 334 ARG   A CZ  1 
ATOM   2421 N  NH1 . ARG   A 1 300 ? 47.26900  -28.98500 -11.52100 1.000 108.44126 ? 334 ARG   A NH1 1 
ATOM   2422 N  NH2 . ARG   A 1 300 ? 46.54700  -27.87700 -13.38900 1.000 127.76816 ? 334 ARG   A NH2 1 
ATOM   2423 N  N   . GLY   A 1 301 ? 40.01000  -31.82100 -10.41600 1.000 73.17065  ? 335 GLY   A N   1 
ATOM   2424 C  CA  . GLY   A 1 301 ? 38.81900  -31.05300 -10.71600 1.000 62.47227  ? 335 GLY   A CA  1 
ATOM   2425 C  C   . GLY   A 1 301 ? 38.73100  -30.72500 -12.19700 1.000 83.62037  ? 335 GLY   A C   1 
ATOM   2426 O  O   . GLY   A 1 301 ? 39.58900  -31.08900 -13.00200 1.000 82.23664  ? 335 GLY   A O   1 
ATOM   2427 N  N   . TRP   A 1 302 ? 37.65800  -30.01700 -12.53800 1.000 85.42554  ? 336 TRP   A N   1 
ATOM   2428 C  CA  . TRP   A 1 302 ? 37.39000  -29.61800 -13.91100 1.000 87.30332  ? 336 TRP   A CA  1 
ATOM   2429 C  C   . TRP   A 1 302 ? 38.44600  -28.62600 -14.40100 1.000 90.14253  ? 336 TRP   A C   1 
ATOM   2430 O  O   . TRP   A 1 302 ? 39.24800  -28.09700 -13.63000 1.000 105.06406 ? 336 TRP   A O   1 
ATOM   2431 C  CB  . TRP   A 1 302 ? 35.99200  -29.01000 -14.01400 1.000 95.41041  ? 336 TRP   A CB  1 
ATOM   2432 C  CG  . TRP   A 1 302 ? 35.68900  -28.02000 -12.92100 1.000 80.05499  ? 336 TRP   A CG  1 
ATOM   2433 C  CD1 . TRP   A 1 302 ? 35.32900  -28.30100 -11.63300 1.000 80.75737  ? 336 TRP   A CD1 1 
ATOM   2434 C  CD2 . TRP   A 1 302 ? 35.71800  -26.59100 -13.02400 1.000 78.05562  ? 336 TRP   A CD2 1 
ATOM   2435 N  NE1 . TRP   A 1 302 ? 35.13600  -27.13800 -10.92900 1.000 84.50429  ? 336 TRP   A NE1 1 
ATOM   2436 C  CE2 . TRP   A 1 302 ? 35.36700  -26.07300 -11.76000 1.000 70.46142  ? 336 TRP   A CE2 1 
ATOM   2437 C  CE3 . TRP   A 1 302 ? 36.00700  -25.69900 -14.06200 1.000 90.86687  ? 336 TRP   A CE3 1 
ATOM   2438 C  CZ2 . TRP   A 1 302 ? 35.30000  -24.70500 -11.50700 1.000 85.58472  ? 336 TRP   A CZ2 1 
ATOM   2439 C  CZ3 . TRP   A 1 302 ? 35.93800  -24.34100 -13.80800 1.000 90.13941  ? 336 TRP   A CZ3 1 
ATOM   2440 C  CH2 . TRP   A 1 302 ? 35.58500  -23.85800 -12.54200 1.000 92.84071  ? 336 TRP   A CH2 1 
ATOM   2441 N  N   . ASP   A 1 303 ? 38.43800  -28.37600 -15.70900 1.000 119.60652 ? 337 ASP   A N   1 
ATOM   2442 C  CA  . ASP   A 1 303 ? 39.39900  -27.46300 -16.31700 1.000 125.72201 ? 337 ASP   A CA  1 
ATOM   2443 C  C   . ASP   A 1 303 ? 38.97900  -27.15200 -17.74400 1.000 142.00429 ? 337 ASP   A C   1 
ATOM   2444 O  O   . ASP   A 1 303 ? 38.37400  -27.98700 -18.42100 1.000 145.26442 ? 337 ASP   A O   1 
ATOM   2445 C  CB  . ASP   A 1 303 ? 40.81900  -28.04800 -16.31500 1.000 138.89307 ? 337 ASP   A CB  1 
ATOM   2446 C  CG  . ASP   A 1 303 ? 41.66400  -27.51700 -15.18000 1.000 146.86125 ? 337 ASP   A CG  1 
ATOM   2447 O  OD1 . ASP   A 1 303 ? 41.57300  -26.30400 -14.89400 1.000 143.95060 ? 337 ASP   A OD1 1 
ATOM   2448 O  OD2 . ASP   A 1 303 ? 42.40500  -28.31300 -14.56700 1.000 149.73244 ? 337 ASP   A OD2 1 
ATOM   2449 N  N   . ALA   A 1 304 ? 39.31200  -25.94000 -18.18700 1.000 119.20144 ? 338 ALA   A N   1 
ATOM   2450 C  CA  . ALA   A 1 304 ? 39.24000  -25.53300 -19.58900 1.000 100.14795 ? 338 ALA   A CA  1 
ATOM   2451 C  C   . ALA   A 1 304 ? 37.82500  -25.56300 -20.15500 1.000 125.29080 ? 338 ALA   A C   1 
ATOM   2452 O  O   . ALA   A 1 304 ? 37.64600  -25.48400 -21.37400 1.000 122.30204 ? 338 ALA   A O   1 
ATOM   2453 C  CB  . ALA   A 1 304 ? 40.17000  -26.39100 -20.45600 1.000 91.80513  ? 338 ALA   A CB  1 
ATOM   2454 N  N   . THR   A 1 305 ? 36.81100  -25.68300 -19.30600 1.000 131.87946 ? 339 THR   A N   1 
ATOM   2455 C  CA  . THR   A 1 305 ? 35.43300  -25.67300 -19.78400 1.000 133.95305 ? 339 THR   A CA  1 
ATOM   2456 C  C   . THR   A 1 305 ? 34.49200  -25.10500 -18.72800 1.000 122.86549 ? 339 THR   A C   1 
ATOM   2457 O  O   . THR   A 1 305 ? 33.96900  -23.99900 -18.87900 1.000 127.50529 ? 339 THR   A O   1 
ATOM   2458 C  CB  . THR   A 1 305 ? 34.95300  -27.08200 -20.18300 1.000 130.44634 ? 339 THR   A CB  1 
ATOM   2459 O  OG1 . THR   A 1 305 ? 35.87300  -27.65900 -21.11800 1.000 131.89924 ? 339 THR   A OG1 1 
ATOM   2460 C  CG2 . THR   A 1 305 ? 33.57900  -27.00800 -20.82600 1.000 114.74690 ? 339 THR   A CG2 1 
HETATM 2461 C  C4  . A1BIN B 2 .   ? 21.99500  -20.17400 -15.80400 1.000 73.47957  ? 401 A1BIN A C4  1 
HETATM 2462 C  C14 . A1BIN B 2 .   ? 21.38400  -15.74900 -12.96600 1.000 62.61666  ? 401 A1BIN A C14 1 
HETATM 2463 C  C5  . A1BIN B 2 .   ? 23.86800  -19.39300 -14.51400 1.000 63.61069  ? 401 A1BIN A C5  1 
HETATM 2464 C  C6  . A1BIN B 2 .   ? 24.13100  -18.23000 -13.77900 1.000 50.34539  ? 401 A1BIN A C6  1 
HETATM 2465 C  C11 . A1BIN B 2 .   ? 25.37400  -17.36500 -11.79500 1.000 50.21993  ? 401 A1BIN A C11 1 
HETATM 2466 C  C7  . A1BIN B 2 .   ? 25.38800  -17.97300 -13.04600 1.000 53.20904  ? 401 A1BIN A C7  1 
HETATM 2467 C  C8  . A1BIN B 2 .   ? 26.61400  -18.38000 -13.55900 1.000 52.66221  ? 401 A1BIN A C8  1 
HETATM 2468 C  C9  . A1BIN B 2 .   ? 27.75500  -18.12800 -12.82500 1.000 50.22067  ? 401 A1BIN A C9  1 
HETATM 2469 C  C10 . A1BIN B 2 .   ? 26.57300  -17.16300 -11.14300 1.000 49.94296  ? 401 A1BIN A C10 1 
HETATM 2470 C  C12 . A1BIN B 2 .   ? 22.99600  -17.42600 -13.89100 1.000 65.12894  ? 401 A1BIN A C12 1 
HETATM 2471 C  C13 . A1BIN B 2 .   ? 22.67700  -16.07300 -13.38500 1.000 63.84552  ? 401 A1BIN A C13 1 
HETATM 2472 N  N1  . A1BIN B 2 .   ? 22.60300  -19.22500 -15.02600 1.000 66.52917  ? 401 A1BIN A N1  1 
HETATM 2473 N  N2  . A1BIN B 2 .   ? 27.75700  -17.53000 -11.63400 1.000 46.87828  ? 401 A1BIN A N2  1 
HETATM 2474 C  C3  . A1BIN B 2 .   ? 24.54400  -20.59500 -14.79600 1.000 44.74383  ? 401 A1BIN A C3  1 
HETATM 2475 N  N3  . A1BIN B 2 .   ? 22.07200  -18.03000 -14.66400 1.000 62.73198  ? 401 A1BIN A N3  1 
HETATM 2476 C  C1  . A1BIN B 2 .   ? 22.66900  -21.33100 -16.07400 1.000 69.59389  ? 401 A1BIN A C1  1 
HETATM 2477 C  C15 . A1BIN B 2 .   ? 21.08100  -14.47900 -12.51000 1.000 76.44401  ? 401 A1BIN A C15 1 
HETATM 2478 C  C16 . A1BIN B 2 .   ? 22.07200  -13.53600 -12.50500 1.000 69.65511  ? 401 A1BIN A C16 1 
HETATM 2479 C  C17 . A1BIN B 2 .   ? 23.34600  -13.79200 -12.93200 1.000 65.41534  ? 401 A1BIN A C17 1 
HETATM 2480 C  C18 . A1BIN B 2 .   ? 23.64500  -15.06500 -13.37900 1.000 66.11226  ? 401 A1BIN A C18 1 
HETATM 2481 C  C2  . A1BIN B 2 .   ? 23.94000  -21.54300 -15.57200 1.000 70.01125  ? 401 A1BIN A C2  1 
HETATM 2482 F  F1  . A1BIN B 2 .   ? 22.09200  -22.28300 -16.83900 1.000 82.94488  ? 401 A1BIN A F1  1 
HETATM 2483 F  F2  . A1BIN B 2 .   ? 21.77700  -12.28300 -12.06200 1.000 65.87217  ? 401 A1BIN A F2  1 
HETATM 2484 CL CL  . CL    C 3 .   ? 14.01900  -34.38600 -23.47400 1.000 74.02233  ? 402 CL    A CL  1 
HETATM 2485 CL CL  . CL    D 3 .   ? 1.73900   -18.00900 -13.35600 1.000 79.66330  ? 403 CL    A CL  1 
HETATM 2486 CL CL  . CL    E 3 .   ? 36.68500  -30.78900 -17.58700 1.000 88.08934  ? 404 CL    A CL  1 
HETATM 2487 O  O   . HOH   F 4 .   ? 8.26600   -27.33900 -9.57200  1.000 65.82652  ? 501 HOH   A O   1 
HETATM 2488 O  O   . HOH   F 4 .   ? 34.97400  -29.80200 -0.61500  1.000 57.93205  ? 502 HOH   A O   1 
HETATM 2489 O  O   . HOH   F 4 .   ? 41.679    -7.320    -4.290    1.000 45.24191  ? 503 HOH   A O   1 
HETATM 2490 O  O   . HOH   F 4 .   ? 31.58800  -13.35600 -5.50900  1.000 56.98075  ? 504 HOH   A O   1 
HETATM 2491 O  O   . HOH   F 4 .   ? 30.88200  -39.98300 -11.92300 1.000 58.50021  ? 505 HOH   A O   1 
HETATM 2492 O  O   . HOH   F 4 .   ? 0.25400   -29.69300 -7.85700  1.000 64.88966  ? 506 HOH   A O   1 
HETATM 2493 O  O   . HOH   F 4 .   ? 24.04300  -25.33600 -17.24700 1.000 57.63267  ? 507 HOH   A O   1 
HETATM 2494 O  O   . HOH   F 4 .   ? 23.99100  -15.90100 0.99200   1.000 69.33423  ? 508 HOH   A O   1 
HETATM 2495 O  O   . HOH   F 4 .   ? 2.71400   -29.32500 -0.96400  1.000 52.73158  ? 509 HOH   A O   1 
HETATM 2496 O  O   . HOH   F 4 .   ? -3.68100  -19.78100 -7.00900  1.000 67.62578  ? 510 HOH   A O   1 
HETATM 2497 O  O   . HOH   F 4 .   ? 0.68400   -20.53200 -23.28800 1.000 77.39477  ? 511 HOH   A O   1 
HETATM 2498 O  O   . HOH   F 4 .   ? -0.78100  -30.20600 -30.72800 1.000 60.63423  ? 512 HOH   A O   1 
HETATM 2499 O  O   . HOH   F 4 .   ? 12.02900  -35.63900 -21.26600 1.000 61.29911  ? 513 HOH   A O   1 
HETATM 2500 O  O   . HOH   F 4 .   ? 17.65900  -47.99100 -14.27600 1.000 62.17179  ? 514 HOH   A O   1 
HETATM 2501 O  O   . HOH   F 4 .   ? 3.85800   -33.93500 -6.25000  1.000 61.80668  ? 515 HOH   A O   1 
HETATM 2502 O  O   . HOH   F 4 .   ? 36.14100  -8.34600  -22.61700 1.000 70.43993  ? 516 HOH   A O   1 
HETATM 2503 O  O   . HOH   F 4 .   ? 5.64200   -31.60500 8.31100   1.000 70.51295  ? 517 HOH   A O   1 
HETATM 2504 O  O   . HOH   F 4 .   ? 25.94700  -33.14900 1.38900   1.000 57.69047  ? 518 HOH   A O   1 
HETATM 2505 O  O   . HOH   F 4 .   ? 26.42300  -41.96300 7.19500   1.000 74.40495  ? 519 HOH   A O   1 
HETATM 2506 O  O   . HOH   F 4 .   ? 31.96500  5.59400   -27.30800 1.000 85.44272  ? 520 HOH   A O   1 
HETATM 2507 O  O   . HOH   F 4 .   ? 7.52700   -29.49700 -11.18900 1.000 57.74566  ? 521 HOH   A O   1 
HETATM 2508 O  O   . HOH   F 4 .   ? 8.70600   -32.13500 -31.68100 1.000 76.51000  ? 522 HOH   A O   1 
HETATM 2509 O  O   . HOH   F 4 .   ? 14.10800  -19.80900 -13.78900 1.000 63.58232  ? 523 HOH   A O   1 
HETATM 2510 O  O   . HOH   F 4 .   ? 33.06900  -43.37700 1.48700   1.000 52.46999  ? 524 HOH   A O   1 
HETATM 2511 O  O   A HOH   F 4 .   ? 9.26200   -40.72000 5.24400   0.500 60.66385  ? 525 HOH   A O   1 
HETATM 2512 O  O   B HOH   F 4 .   ? 8.68000   -41.39900 3.45200   0.500 51.12951  ? 525 HOH   A O   1 
HETATM 2513 O  O   . HOH   F 4 .   ? 33.35000  -27.08700 -0.05900  1.000 57.88681  ? 526 HOH   A O   1 
HETATM 2514 O  O   . HOH   F 4 .   ? 31.25600  -24.34700 -17.47500 1.000 63.54633  ? 527 HOH   A O   1 
HETATM 2515 O  O   . HOH   F 4 .   ? 4.70100   -14.30700 -7.06600  1.000 59.22097  ? 528 HOH   A O   1 
HETATM 2516 O  O   . HOH   F 4 .   ? 2.03400   -22.98500 4.75100   1.000 70.39158  ? 529 HOH   A O   1 
HETATM 2517 O  O   . HOH   F 4 .   ? 39.02000  -30.80800 -6.96500  1.000 67.21493  ? 530 HOH   A O   1 
HETATM 2518 O  O   . HOH   F 4 .   ? 30.44900  -28.60200 -20.77200 1.000 72.17189  ? 531 HOH   A O   1 
HETATM 2519 O  O   . HOH   F 4 .   ? -3.18400  -19.55700 -16.81000 1.000 68.28839  ? 532 HOH   A O   1 
HETATM 2520 O  O   . HOH   F 4 .   ? 2.34900   -25.25800 6.04800   1.000 77.27313  ? 533 HOH   A O   1 
HETATM 2521 O  O   . HOH   F 4 .   ? 11.29900  -31.06100 7.97000   1.000 60.25338  ? 534 HOH   A O   1 
HETATM 2522 O  O   . HOH   F 4 .   ? 29.84400  -37.18100 -21.66900 1.000 66.29760  ? 535 HOH   A O   1 
HETATM 2523 O  O   . HOH   F 4 .   ? 2.15100   -41.93900 -5.61900  1.000 74.04431  ? 536 HOH   A O   1 
HETATM 2524 O  O   . HOH   F 4 .   ? 3.15300   -50.22200 -16.12300 1.000 64.57432  ? 537 HOH   A O   1 
HETATM 2525 O  O   . HOH   F 4 .   ? 34.51000  5.00300   -21.05300 1.000 99.60995  ? 538 HOH   A O   1 
HETATM 2526 O  O   . HOH   F 4 .   ? 7.57900   -35.32500 -35.61200 1.000 70.48936  ? 539 HOH   A O   1 
HETATM 2527 O  O   . HOH   F 4 .   ? 40.75700  -29.96500 -19.33300 1.000 84.06626  ? 540 HOH   A O   1 
HETATM 2528 O  O   . HOH   F 4 .   ? 17.68300  -51.34600 -1.97900  1.000 51.17771  ? 541 HOH   A O   1 
HETATM 2529 O  O   . HOH   F 4 .   ? 39.887    -9.264    -13.654   1.000 64.01741  ? 542 HOH   A O   1 
HETATM 2530 O  O   . HOH   F 4 .   ? 26.17700  -18.68000 0.67600   1.000 70.83132  ? 543 HOH   A O   1 
HETATM 2531 O  O   . HOH   F 4 .   ? 4.47200   -25.07000 6.97900   1.000 73.21828  ? 544 HOH   A O   1 
HETATM 2532 O  O   . HOH   F 4 .   ? 2.52000   -44.06200 -10.91000 1.000 71.35558  ? 545 HOH   A O   1 
HETATM 2533 O  O   . HOH   F 4 .   ? 34.60600  -39.09500 -16.53400 1.000 56.42288  ? 546 HOH   A O   1 
HETATM 2534 O  O   . HOH   F 4 .   ? -5.09000  -30.12800 -0.32500  1.000 75.52099  ? 547 HOH   A O   1 
HETATM 2535 O  O   . HOH   F 4 .   ? 6.96900   -15.93400 -13.55000 1.000 73.65624  ? 548 HOH   A O   1 
HETATM 2536 O  O   . HOH   F 4 .   ? -4.41500  -32.94200 -6.19800  1.000 57.35159  ? 549 HOH   A O   1 
HETATM 2537 O  O   . HOH   F 4 .   ? 30.80000  -7.40600  -4.18200  1.000 63.42056  ? 550 HOH   A O   1 
HETATM 2538 O  O   . HOH   F 4 .   ? 20.81800  -1.51800  -5.86400  1.000 69.21933  ? 551 HOH   A O   1 
HETATM 2539 O  O   . HOH   F 4 .   ? 29.65400  -31.44100 1.63900   1.000 51.89948  ? 552 HOH   A O   1 
HETATM 2540 O  O   . HOH   F 4 .   ? 16.22800  -25.24100 7.20600   1.000 65.15331  ? 553 HOH   A O   1 
HETATM 2541 O  O   . HOH   F 4 .   ? 27.46000  -52.83000 3.61900   1.000 67.72795  ? 554 HOH   A O   1 
HETATM 2542 O  O   . HOH   F 4 .   ? 20.78500  -4.94100  1.95600   1.000 60.35918  ? 555 HOH   A O   1 
HETATM 2543 O  O   . HOH   F 4 .   ? 36.39000  -12.67900 -12.56700 1.000 64.62522  ? 556 HOH   A O   1 
HETATM 2544 O  O   . HOH   F 4 .   ? 10.18700  -53.33800 -12.39900 1.000 74.95799  ? 557 HOH   A O   1 
HETATM 2545 O  O   . HOH   F 4 .   ? 20.45300  -34.19400 -23.93700 1.000 66.28396  ? 558 HOH   A O   1 
HETATM 2546 O  O   . HOH   F 4 .   ? 8.12100   -13.20600 -8.06400  1.000 70.13647  ? 559 HOH   A O   1 
HETATM 2547 O  O   . HOH   F 4 .   ? 18.83500  -16.19600 6.50300   1.000 74.25338  ? 560 HOH   A O   1 
HETATM 2548 O  O   . HOH   F 4 .   ? 16.34200  -35.47900 -25.05400 1.000 82.95441  ? 561 HOH   A O   1 
HETATM 2549 O  O   . HOH   F 4 .   ? 0.26900   -35.44200 -19.85500 1.000 71.31979  ? 562 HOH   A O   1 
HETATM 2550 O  O   . HOH   F 4 .   ? -3.22300  -36.35800 -1.64700  1.000 64.44170  ? 563 HOH   A O   1 
HETATM 2551 O  O   . HOH   F 4 .   ? 38.71000  -30.33600 -3.55000  1.000 57.48635  ? 564 HOH   A O   1 
HETATM 2552 O  O   . HOH   F 4 .   ? 39.99000  -35.50100 -4.00000  1.000 59.34502  ? 565 HOH   A O   1 
HETATM 2553 O  O   . HOH   F 4 .   ? 0.48100   -37.56000 -8.91700  1.000 55.12362  ? 566 HOH   A O   1 
HETATM 2554 O  O   . HOH   F 4 .   ? -3.92900  -16.56500 -1.14000  1.000 63.03399  ? 567 HOH   A O   1 
HETATM 2555 O  O   . HOH   F 4 .   ? 31.26000  -1.83400  -3.35800  1.000 66.97332  ? 568 HOH   A O   1 
HETATM 2556 O  O   . HOH   F 4 .   ? 23.76100  -21.27800 -19.84900 1.000 64.65745  ? 569 HOH   A O   1 
HETATM 2557 O  O   . HOH   F 4 .   ? 17.08400  -29.47500 -21.33800 1.000 68.54407  ? 570 HOH   A O   1 
HETATM 2558 O  O   . HOH   F 4 .   ? 34.138    -15.957   -5.145    1.000 58.05541  ? 571 HOH   A O   1 
HETATM 2559 O  O   . HOH   F 4 .   ? 9.73400   -12.08300 -3.21700  1.000 73.57641  ? 572 HOH   A O   1 
HETATM 2560 O  O   . HOH   F 4 .   ? 18.27300  -39.66400 -25.97800 1.000 74.98509  ? 573 HOH   A O   1 
HETATM 2561 O  O   . HOH   F 4 .   ? 27.33600  -1.76200  -22.29200 1.000 65.11583  ? 574 HOH   A O   1 
HETATM 2562 O  O   . HOH   F 4 .   ? -6.79800  -28.66200 -2.43300  1.000 62.17574  ? 575 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   . ASN A 1   ? 2.67862 1.87595 1.85867 -0.27695 0.08306  0.43936  35  ASN A N   
2    C CA  . ASN A 1   ? 2.56403 1.77901 1.85947 -0.24444 0.07265  0.39118  35  ASN A CA  
3    C C   . ASN A 1   ? 2.49634 1.80212 1.85191 -0.25279 0.12898  0.33914  35  ASN A C   
4    O O   . ASN A 1   ? 2.37256 1.72656 1.76881 -0.21917 0.12643  0.28911  35  ASN A O   
5    C CB  . ASN A 1   ? 2.38207 1.59732 1.68800 -0.19048 0.02127  0.36607  35  ASN A CB  
6    C CG  . ASN A 1   ? 2.47075 1.61060 1.74137 -0.16961 -0.03918 0.40885  35  ASN A CG  
7    O OD1 . ASN A 1   ? 2.47823 1.58331 1.78370 -0.17546 -0.04934 0.43413  35  ASN A OD1 
8    N ND2 . ASN A 1   ? 2.37953 1.52607 1.61301 -0.13695 -0.07906 0.40351  35  ASN A ND2 
9    N N   . ASN A 2   ? 2.50042 1.83070 1.86485 -0.29831 0.17837  0.35332  36  ASN A N   
10   C CA  . ASN A 2   ? 2.42924 1.85154 1.86008 -0.30290 0.23115  0.30399  36  ASN A CA  
11   C C   . ASN A 2   ? 2.36114 1.79764 1.91358 -0.27211 0.21360  0.26435  36  ASN A C   
12   O O   . ASN A 2   ? 2.31283 1.69445 1.90819 -0.26892 0.17920  0.28140  36  ASN A O   
13   C CB  . ASN A 2   ? 2.39477 1.85156 1.82089 -0.36060 0.28667  0.33145  36  ASN A CB  
14   C CG  . ASN A 2   ? 2.54764 2.02345 1.85003 -0.38982 0.31879  0.36079  36  ASN A CG  
15   O OD1 . ASN A 2   ? 2.67394 2.10716 1.88144 -0.37390 0.28661  0.37806  36  ASN A OD1 
16   N ND2 . ASN A 2   ? 2.50747 2.05744 1.81026 -0.43228 0.38265  0.36532  36  ASN A ND2 
17   N N   . SER A 3   ? 2.38146 1.88974 1.98554 -0.24736 0.23516  0.21025  37  SER A N   
18   C CA  . SER A 3   ? 2.10113 1.63183 1.80864 -0.21313 0.21695  0.17262  37  SER A CA  
19   C C   . SER A 3   ? 1.93035 1.40767 1.63597 -0.17669 0.15787  0.17907  37  SER A C   
20   O O   . SER A 3   ? 1.80596 1.24869 1.55641 -0.16803 0.12835  0.18788  37  SER A O   
21   C CB  . SER A 3   ? 2.00474 1.55270 1.79734 -0.23644 0.23212  0.17356  37  SER A CB  
22   O OG  . SER A 3   ? 1.83298 1.41133 1.71650 -0.20189 0.21478  0.13617  37  SER A OG  
23   N N   . SER A 4   ? 1.77514 1.25229 1.42895 -0.15500 0.14098  0.17064  38  SER A N   
24   C CA  . SER A 4   ? 1.72996 1.17372 1.37866 -0.12200 0.08770  0.17784  38  SER A CA  
25   C C   . SER A 4   ? 1.42839 0.90670 1.17148 -0.08912 0.07253  0.14708  38  SER A C   
26   O O   . SER A 4   ? 1.30605 0.83407 1.08723 -0.07835 0.08881  0.11460  38  SER A O   
27   C CB  . SER A 4   ? 1.84494 1.29221 1.42221 -0.11335 0.07421  0.17345  38  SER A CB  
28   O OG  . SER A 4   ? 2.06820 1.49070 1.54685 -0.14271 0.08842  0.20187  38  SER A OG  
29   N N   . VAL A 5   ? 1.47713 0.92753 1.25473 -0.07149 0.03988  0.15731  39  VAL A N   
30   C CA  . VAL A 5   ? 1.29162 0.77936 1.14751 -0.03839 0.02286  0.13165  39  VAL A CA  
31   C C   . VAL A 5   ? 1.16997 0.64368 1.01534 -0.00474 -0.02334 0.14110  39  VAL A C   
32   O O   . VAL A 5   ? 1.31854 0.73810 1.14263 0.00197  -0.05044 0.16193  39  VAL A O   
33   C CB  . VAL A 5   ? 1.16285 0.64756 1.07961 -0.04353 0.02796  0.12307  39  VAL A CB  
34   C CG1 . VAL A 5   ? 1.12613 0.65490 1.11016 -0.00593 0.00773  0.09680  39  VAL A CG1 
35   C CG2 . VAL A 5   ? 1.18730 0.70346 1.12690 -0.07687 0.07394  0.11290  39  VAL A CG2 
36   N N   . VAL A 6   ? 1.11804 0.64124 0.98265 0.01616  -0.03357 0.12665  40  VAL A N   
37   C CA  . VAL A 6   ? 1.03437 0.57108 0.90451 0.04843  -0.07371 0.13235  40  VAL A CA  
38   C C   . VAL A 6   ? 0.94467 0.53422 0.88944 0.07785  -0.08067 0.11227  40  VAL A C   
39   O O   . VAL A 6   ? 1.12201 0.74571 1.10975 0.07261  -0.05715 0.09469  40  VAL A O   
40   C CB  . VAL A 6   ? 1.29897 0.86193 1.14018 0.04530  -0.08355 0.13394  40  VAL A CB  
41   C CG1 . VAL A 6   ? 1.31505 0.82980 1.06998 0.01936  -0.07984 0.15119  40  VAL A CG1 
42   C CG2 . VAL A 6   ? 1.18919 0.80072 1.07149 0.03814  -0.06101 0.11136  40  VAL A CG2 
43   N N   . GLY A 7   ? 0.91785 0.52009 0.87681 0.11216  -0.11409 0.11419  41  GLY A N   
44   C CA  . GLY A 7   ? 0.90315 0.56749 0.92352 0.14360  -0.12053 0.09419  41  GLY A CA  
45   C C   . GLY A 7   ? 0.94472 0.59356 0.99580 0.14711  -0.11130 0.07488  41  GLY A C   
46   O O   . GLY A 7   ? 0.96357 0.67334 1.06096 0.16499  -0.10734 0.05546  41  GLY A O   
47   N N   . LEU A 8   ? 0.95652 0.52738 0.98173 0.12686  -0.10906 0.08185  42  LEU A N   
48   C CA  . LEU A 8   ? 0.94831 0.49320 1.00395 0.12224  -0.10554 0.06377  42  LEU A CA  
49   C C   . LEU A 8   ? 0.93602 0.52098 1.02530 0.09610  -0.07068 0.05074  42  LEU A C   
50   O O   . LEU A 8   ? 0.95642 0.50827 1.05522 0.06747  -0.05679 0.04842  42  LEU A O   
51   C CB  . LEU A 8   ? 0.90789 0.48015 1.00118 0.16907  -0.13369 0.03556  42  LEU A CB  
52   C CG  . LEU A 8   ? 1.17185 0.70131 1.24277 0.19768  -0.16748 0.03882  42  LEU A CG  
53   C CD1 . LEU A 8   ? 0.86085 0.45719 0.96621 0.24056  -0.18076 0.00344  42  LEU A CD1 
54   C CD2 . LEU A 8   ? 1.21320 0.64428 1.25978 0.16864  -0.17165 0.05113  42  LEU A CD2 
55   N N   . HIS A 9   ? 0.66071 0.31789 0.77297 0.10505  -0.05849 0.04401  43  HIS A N   
56   C CA  . HIS A 9   ? 0.75006 0.45265 0.90481 0.09414  -0.03436 0.02869  43  HIS A CA  
57   C C   . HIS A 9   ? 0.74391 0.46403 0.88955 0.07449  -0.00840 0.03694  43  HIS A C   
58   O O   . HIS A 9   ? 0.70385 0.46530 0.88849 0.07343  0.00747  0.02516  43  HIS A O   
59   C CB  . HIS A 9   ? 0.56929 0.34198 0.76669 0.12785  -0.04760 0.01107  43  HIS A CB  
60   C CG  . HIS A 9   ? 0.82863 0.59258 1.03714 0.15419  -0.07358 -0.00954 43  HIS A CG  
61   N ND1 . HIS A 9   ? 0.65589 0.34369 0.85175 0.14297  -0.08497 -0.01394 43  HIS A ND1 
62   C CD2 . HIS A 9   ? 0.90946 0.73026 1.13893 0.19211  -0.09142 -0.02909 43  HIS A CD2 
63   C CE1 . HIS A 9   ? 0.89006 0.57944 1.10134 0.17562  -0.11216 -0.04046 43  HIS A CE1 
64   N NE2 . HIS A 9   ? 0.71383 0.48959 0.94352 0.20777  -0.11472 -0.05252 43  HIS A NE2 
65   N N   . TYR A 10  ? 0.71143 0.40023 0.80654 0.06196  -0.00713 0.05391  44  TYR A N   
66   C CA  . TYR A 10  ? 0.72014 0.42466 0.80530 0.05045  0.00978  0.05379  44  TYR A CA  
67   C C   . TYR A 10  ? 0.84656 0.50792 0.87846 0.02072  0.03185  0.05906  44  TYR A C   
68   O O   . TYR A 10  ? 1.03426 0.65476 1.00931 0.01337  0.01932  0.07699  44  TYR A O   
69   C CB  . TYR A 10  ? 0.74331 0.47023 0.82057 0.06519  -0.01374 0.06392  44  TYR A CB  
70   C CG  . TYR A 10  ? 0.59707 0.38060 0.72300 0.09280  -0.03011 0.06203  44  TYR A CG  
71   C CD1 . TYR A 10  ? 0.59928 0.42730 0.77100 0.09801  -0.02043 0.05542  44  TYR A CD1 
72   C CD2 . TYR A 10  ? 0.64665 0.44271 0.77098 0.11674  -0.05537 0.06628  44  TYR A CD2 
73   C CE1 . TYR A 10  ? 0.66240 0.54975 0.86893 0.12182  -0.03346 0.05695  44  TYR A CE1 
74   C CE2 . TYR A 10  ? 0.68826 0.54904 0.85207 0.14403  -0.06604 0.06096  44  TYR A CE2 
75   C CZ  . TYR A 10  ? 0.60021 0.50825 0.80106 0.14421  -0.05390 0.05810  44  TYR A CZ  
76   O OH  . TYR A 10  ? 0.75895 0.73865 0.98946 0.16995  -0.06296 0.05625  44  TYR A OH  
77   N N   . LYS A 11  ? 0.82847 0.50588 0.87830 0.00634  0.06427  0.04346  45  LYS A N   
78   C CA  . LYS A 11  ? 1.01733 0.67342 1.02038 -0.02154 0.09432  0.04373  45  LYS A CA  
79   C C   . LYS A 11  ? 0.98059 0.63388 0.94298 -0.02101 0.09698  0.03417  45  LYS A C   
80   O O   . LYS A 11  ? 0.91923 0.59777 0.91902 -0.00747 0.09936  0.01418  45  LYS A O   
81   C CB  . LYS A 11  ? 0.93338 0.62409 0.98566 -0.03352 0.12931  0.02586  45  LYS A CB  
82   C CG  . LYS A 11  ? 1.07902 0.77549 1.09438 -0.05807 0.16961  0.01846  45  LYS A CG  
83   C CD  . LYS A 11  ? 1.12592 0.87812 1.21021 -0.06330 0.20291  -0.00376 45  LYS A CD  
84   C CE  . LYS A 11  ? 1.14159 0.91659 1.19295 -0.08815 0.24938  -0.01204 45  LYS A CE  
85   N NZ  . LYS A 11  ? 1.25079 0.98893 1.23482 -0.12627 0.25788  0.02339  45  LYS A NZ  
86   N N   . ILE A 12  ? 0.97387 0.59177 0.85816 -0.03572 0.09259  0.04844  46  ILE A N   
87   C CA  . ILE A 12  ? 1.12765 0.73931 0.96442 -0.03753 0.09088  0.03408  46  ILE A CA  
88   C C   . ILE A 12  ? 1.02628 0.65895 0.86524 -0.04443 0.13251  0.00228  46  ILE A C   
89   O O   . ILE A 12  ? 1.11115 0.75625 0.94168 -0.06179 0.16742  0.00365  46  ILE A O   
90   C CB  . ILE A 12  ? 1.34619 0.92015 1.09263 -0.05078 0.07341  0.05744  46  ILE A CB  
91   C CG1 . ILE A 12  ? 1.18176 0.74981 0.93380 -0.03348 0.02512  0.07389  46  ILE A CG1 
92   C CG2 . ILE A 12  ? 1.28401 0.85363 0.96138 -0.06313 0.08928  0.03614  46  ILE A CG2 
93   C CD1 . ILE A 12  ? 1.31485 0.90510 1.09582 -0.02412 0.00786  0.05341  46  ILE A CD1 
94   N N   . GLY A 13  ? 1.15654 0.79488 1.01121 -0.03086 0.12832  -0.02712 47  GLY A N   
95   C CA  . GLY A 13  ? 1.07104 0.73070 0.93987 -0.02607 0.16376  -0.06558 47  GLY A CA  
96   C C   . GLY A 13  ? 1.19966 0.83877 1.00661 -0.02578 0.16394  -0.09769 47  GLY A C   
97   O O   . GLY A 13  ? 1.52652 1.16048 1.25081 -0.04248 0.18008  -0.09890 47  GLY A O   
98   N N   . LYS A 14  ? 1.33029 0.95469 1.17333 -0.00800 0.14383  -0.12348 48  LYS A N   
99   C CA  . LYS A 14  ? 1.31938 0.91916 1.11814 -0.00309 0.14256  -0.16770 48  LYS A CA  
100  C C   . LYS A 14  ? 1.32956 0.88846 1.10312 -0.01117 0.09217  -0.15993 48  LYS A C   
101  O O   . LYS A 14  ? 1.26322 0.81702 1.09604 -0.00838 0.06128  -0.13646 48  LYS A O   
102  C CB  . LYS A 14  ? 1.28106 0.88578 1.14774 0.02440  0.15580  -0.20943 48  LYS A CB  
103  C CG  . LYS A 14  ? 1.41285 1.02326 1.23611 0.03595  0.18772  -0.26698 48  LYS A CG  
104  C CD  . LYS A 14  ? 1.68707 1.27129 1.57067 0.06859  0.17687  -0.31280 48  LYS A CD  
105  C CE  . LYS A 14  ? 1.56313 1.17104 1.55335 0.08800  0.17703  -0.29336 48  LYS A CE  
106  N NZ  . LYS A 14  ? 1.61914 1.18705 1.66832 0.12071  0.15637  -0.32806 48  LYS A NZ  
107  N N   . LYS A 15  ? 1.35957 0.89741 1.04606 -0.02261 0.08399  -0.18005 49  LYS A N   
108  C CA  . LYS A 15  ? 1.34520 0.85106 1.00842 -0.03419 0.03324  -0.17675 49  LYS A CA  
109  C C   . LYS A 15  ? 1.47207 0.94221 1.18607 -0.02516 0.01051  -0.21278 49  LYS A C   
110  O O   . LYS A 15  ? 1.40468 0.85808 1.11328 -0.00920 0.03019  -0.26403 49  LYS A O   
111  C CB  . LYS A 15  ? 1.54936 1.04544 1.09927 -0.04857 0.02784  -0.19072 49  LYS A CB  
112  C CG  . LYS A 15  ? 1.57402 1.04767 1.09706 -0.06364 -0.02884 -0.18534 49  LYS A CG  
113  C CD  . LYS A 15  ? 1.74629 1.21528 1.14819 -0.07495 -0.03336 -0.20092 49  LYS A CD  
114  C CE  . LYS A 15  ? 1.66326 1.15818 1.00920 -0.07834 0.00513  -0.16581 49  LYS A CE  
115  N NZ  . LYS A 15  ? 1.76597 1.26315 0.98648 -0.08728 0.01819  -0.18616 49  LYS A NZ  
116  N N   . ILE A 16  ? 1.33246 0.79164 1.09797 -0.03521 -0.03154 -0.18548 50  ILE A N   
117  C CA  . ILE A 16  ? 1.47166 0.88801 1.29153 -0.03444 -0.05967 -0.20666 50  ILE A CA  
118  C C   . ILE A 16  ? 1.42731 0.82902 1.24319 -0.06304 -0.11245 -0.19104 50  ILE A C   
119  O O   . ILE A 16  ? 1.45137 0.81763 1.31947 -0.07367 -0.14404 -0.19416 50  ILE A O   
120  C CB  . ILE A 16  ? 1.34252 0.77119 1.25911 -0.01963 -0.05249 -0.17935 50  ILE A CB  
121  C CG1 . ILE A 16  ? 1.22158 0.69890 1.17267 -0.03038 -0.06470 -0.11823 50  ILE A CG1 
122  C CG2 . ILE A 16  ? 1.24451 0.69482 1.17632 0.00858  -0.00461 -0.19926 50  ILE A CG2 
123  C CD1 . ILE A 16  ? 1.07208 0.57176 1.10602 -0.01618 -0.05850 -0.08918 50  ILE A CD1 
124  N N   . GLY A 17  ? 1.61854 1.04805 1.37616 -0.07711 -0.12484 -0.17180 51  GLY A N   
125  C CA  . GLY A 17  ? 1.68039 1.11964 1.44649 -0.10284 -0.17452 -0.14982 51  GLY A CA  
126  C C   . GLY A 17  ? 1.94884 1.35424 1.64235 -0.12015 -0.20694 -0.19259 51  GLY A C   
127  O O   . GLY A 17  ? 1.95709 1.32695 1.58800 -0.11048 -0.19077 -0.24485 51  GLY A O   
128  N N   . GLU A 18  ? 2.07797 1.50403 1.78257 -0.14536 -0.25448 -0.17179 52  GLU A N   
129  C CA  . GLU A 18  ? 2.14216 1.54636 1.78663 -0.16691 -0.29777 -0.20743 52  GLU A CA  
130  C C   . GLU A 18  ? 2.12180 1.57499 1.70118 -0.16806 -0.31348 -0.18056 52  GLU A C   
131  O O   . GLU A 18  ? 2.05867 1.55063 1.63752 -0.15065 -0.28911 -0.13808 52  GLU A O   
132  C CB  . GLU A 18  ? 2.11325 1.50231 1.83298 -0.20066 -0.34846 -0.20669 52  GLU A CB  
133  C CG  . GLU A 18  ? 2.11697 1.58077 1.90778 -0.21927 -0.37439 -0.14530 52  GLU A CG  
134  C CD  . GLU A 18  ? 1.95232 1.44187 1.84023 -0.21384 -0.35053 -0.09971 52  GLU A CD  
135  O OE1 . GLU A 18  ? 1.76001 1.25543 1.64447 -0.18229 -0.30446 -0.08848 52  GLU A OE1 
136  O OE2 . GLU A 18  ? 1.86608 1.37412 1.83336 -0.24399 -0.37899 -0.07373 52  GLU A OE2 
137  N N   . GLY A 19  ? 2.20453 1.65136 1.72903 -0.18778 -0.35946 -0.20684 53  GLY A N   
138  C CA  . GLY A 19  ? 2.25420 1.74288 1.71032 -0.18679 -0.38288 -0.18299 53  GLY A CA  
139  C C   . GLY A 19  ? 2.36650 1.90959 1.88314 -0.20783 -0.43950 -0.15216 53  GLY A C   
140  O O   . GLY A 19  ? 2.41922 2.00396 1.89378 -0.20246 -0.46595 -0.12763 53  GLY A O   
141  N N   . SER A 20  ? 2.45679 2.00398 2.07538 -0.23215 -0.45933 -0.15010 54  SER A N   
142  C CA  . SER A 20  ? 2.46871 2.08181 2.16019 -0.25873 -0.51069 -0.12171 54  SER A CA  
143  C C   . SER A 20  ? 2.32550 2.01256 2.11134 -0.24610 -0.49216 -0.06145 54  SER A C   
144  O O   . SER A 20  ? 2.25507 2.01882 2.06085 -0.23934 -0.51645 -0.02906 54  SER A O   
145  C CB  . SER A 20  ? 2.35897 1.93670 2.10608 -0.30258 -0.54861 -0.15269 54  SER A CB  
146  O OG  . SER A 20  ? 2.19066 1.72337 2.00267 -0.30401 -0.51624 -0.14984 54  SER A OG  
147  N N   . PHE A 21  ? 2.20023 1.86950 2.04357 -0.23898 -0.45114 -0.04840 55  PHE A N   
148  C CA  . PHE A 21  ? 2.12278 1.86343 2.05133 -0.22638 -0.43135 0.00294  55  PHE A CA  
149  C C   . PHE A 21  ? 2.02973 1.77044 1.92319 -0.18186 -0.38472 0.01860  55  PHE A C   
150  O O   . PHE A 21  ? 1.79352 1.55755 1.74359 -0.16711 -0.35335 0.04363  55  PHE A O   
151  C CB  . PHE A 21  ? 2.02986 1.75700 2.04464 -0.24948 -0.42149 0.01384  55  PHE A CB  
152  C CG  . PHE A 21  ? 1.84006 1.66630 1.95518 -0.26460 -0.43162 0.06406  55  PHE A CG  
153  C CD1 . PHE A 21  ? 1.69853 1.61698 1.82971 -0.23601 -0.42561 0.09514  55  PHE A CD1 
154  C CD2 . PHE A 21  ? 1.67825 1.50635 1.87186 -0.30724 -0.44734 0.08036  55  PHE A CD2 
155  C CE1 . PHE A 21  ? 1.54915 1.57390 1.77242 -0.24616 -0.43068 0.13651  55  PHE A CE1 
156  C CE2 . PHE A 21  ? 1.42499 1.35852 1.70907 -0.32486 -0.45177 0.13021  55  PHE A CE2 
157  C CZ  . PHE A 21  ? 1.47629 1.51544 1.77496 -0.29252 -0.44122 0.15579  55  PHE A CZ  
158  N N   . GLY A 22  ? 2.08519 1.79974 1.88427 -0.16297 -0.38168 0.00586  56  GLY A N   
159  C CA  . GLY A 22  ? 1.99343 1.69548 1.75667 -0.12872 -0.33982 0.02050  56  GLY A CA  
160  C C   . GLY A 22  ? 1.93187 1.57182 1.67410 -0.12387 -0.29280 -0.00557 56  GLY A C   
161  O O   . GLY A 22  ? 2.03342 1.65457 1.82883 -0.13600 -0.28538 -0.01948 56  GLY A O   
162  N N   . VAL A 23  ? 1.67732 1.28725 1.34550 -0.10663 -0.26187 -0.00993 57  VAL A N   
163  C CA  . VAL A 23  ? 1.76569 1.33176 1.41631 -0.10075 -0.21517 -0.03753 57  VAL A CA  
164  C C   . VAL A 23  ? 1.56255 1.14782 1.29508 -0.08514 -0.18414 -0.01654 57  VAL A C   
165  O O   . VAL A 23  ? 1.47773 1.09871 1.23782 -0.07029 -0.18214 0.01829  57  VAL A O   
166  C CB  . VAL A 23  ? 1.85992 1.40206 1.40789 -0.09370 -0.18953 -0.04358 57  VAL A CB  
167  C CG1 . VAL A 23  ? 1.91501 1.42616 1.44474 -0.08991 -0.14267 -0.08209 57  VAL A CG1 
168  C CG2 . VAL A 23  ? 1.95081 1.48635 1.40980 -0.10625 -0.22758 -0.05372 57  VAL A CG2 
169  N N   . ILE A 24  ? 1.30958 0.86994 1.08029 -0.08527 -0.16314 -0.04049 58  ILE A N   
170  C CA  . ILE A 24  ? 1.20401 0.78252 1.05019 -0.07064 -0.13761 -0.02362 58  ILE A CA  
171  C C   . ILE A 24  ? 1.28995 0.84546 1.11353 -0.05554 -0.09133 -0.04694 58  ILE A C   
172  O O   . ILE A 24  ? 1.29721 0.81763 1.07314 -0.05771 -0.07913 -0.08684 58  ILE A O   
173  C CB  . ILE A 24  ? 1.18571 0.75929 1.10594 -0.08251 -0.15626 -0.02320 58  ILE A CB  
174  C CG1 . ILE A 24  ? 1.12179 0.73766 1.07541 -0.10296 -0.19840 0.00567  58  ILE A CG1 
175  C CG2 . ILE A 24  ? 1.12270 0.71382 1.11016 -0.06524 -0.13080 -0.00583 58  ILE A CG2 
176  C CD1 . ILE A 24  ? 1.02686 0.63989 1.05355 -0.12428 -0.21833 0.01668  58  ILE A CD1 
177  N N   . PHE A 25  ? 1.19578 0.77798 1.05536 -0.03992 -0.06600 -0.02542 59  PHE A N   
178  C CA  . PHE A 25  ? 1.14003 0.71669 0.99201 -0.02886 -0.02227 -0.04228 59  PHE A CA  
179  C C   . PHE A 25  ? 1.04109 0.63957 0.97691 -0.01315 -0.00865 -0.03570 59  PHE A C   
180  O O   . PHE A 25  ? 0.97786 0.60328 0.96577 -0.00959 -0.02816 -0.00810 59  PHE A O   
181  C CB  . PHE A 25  ? 1.14612 0.73107 0.95049 -0.02990 -0.00568 -0.02173 59  PHE A CB  
182  C CG  . PHE A 25  ? 1.20710 0.76909 0.91472 -0.04387 -0.01047 -0.02728 59  PHE A CG  
183  C CD1 . PHE A 25  ? 1.28776 0.84774 0.96114 -0.05019 -0.05146 -0.00798 59  PHE A CD1 
184  C CD2 . PHE A 25  ? 1.28157 0.83357 0.93173 -0.04977 0.02612  -0.05081 59  PHE A CD2 
185  C CE1 . PHE A 25  ? 1.41528 0.95598 0.99315 -0.06173 -0.06034 -0.01042 59  PHE A CE1 
186  C CE2 . PHE A 25  ? 1.37203 0.90846 0.92211 -0.06320 0.02229  -0.05275 59  PHE A CE2 
187  C CZ  . PHE A 25  ? 1.45198 0.97889 0.96298 -0.06898 -0.02318 -0.03165 59  PHE A CZ  
188  N N   . GLU A 26  ? 1.05655 0.65175 1.00392 -0.00260 0.02534  -0.06188 60  GLU A N   
189  C CA  . GLU A 26  ? 1.04149 0.66579 1.05996 0.01432  0.04131  -0.05488 60  GLU A CA  
190  C C   . GLU A 26  ? 0.97684 0.63030 0.99224 0.01369  0.05694  -0.03336 60  GLU A C   
191  O O   . GLU A 26  ? 1.01676 0.65989 0.97291 0.00082  0.06725  -0.02957 60  GLU A O   
192  C CB  . GLU A 26  ? 1.14589 0.76461 1.18637 0.02903  0.06949  -0.09369 60  GLU A CB  
193  C CG  . GLU A 26  ? 1.18184 0.77410 1.27270 0.04225  0.04921  -0.10613 60  GLU A CG  
194  C CD  . GLU A 26  ? 1.29591 0.89002 1.42230 0.06740  0.07540  -0.14468 60  GLU A CD  
195  O OE1 . GLU A 26  ? 1.43531 1.05806 1.54042 0.07003  0.11310  -0.16683 60  GLU A OE1 
196  O OE2 . GLU A 26  ? 1.31379 0.88354 1.49219 0.08458  0.05771  -0.15068 60  GLU A OE2 
197  N N   . GLY A 27  ? 0.93463 0.62073 1.01189 0.02691  0.05561  -0.01852 61  GLY A N   
198  C CA  . GLY A 27  ? 0.95944 0.66642 1.04139 0.02704  0.06364  -0.00319 61  GLY A CA  
199  C C   . GLY A 27  ? 0.62784 0.37230 0.77868 0.04236  0.07340  -0.00718 61  GLY A C   
200  O O   . GLY A 27  ? 0.79931 0.55628 0.99513 0.05623  0.06846  -0.01284 61  GLY A O   
201  N N   . THR A 28  ? 0.82732 0.58569 0.98570 0.03881  0.08334  -0.00309 62  THR A N   
202  C CA  . THR A 28  ? 0.66393 0.46290 0.88571 0.05105  0.08813  -0.00924 62  THR A CA  
203  C C   . THR A 28  ? 0.66357 0.46845 0.88680 0.05268  0.07165  0.00372  62  THR A C   
204  O O   . THR A 28  ? 0.71791 0.49203 0.90479 0.03619  0.07566  0.00960  62  THR A O   
205  C CB  . THR A 28  ? 0.80229 0.61785 1.04613 0.04189  0.12281  -0.03168 62  THR A CB  
206  O OG1 . THR A 28  ? 0.98211 0.79564 1.23148 0.05068  0.13618  -0.05223 62  THR A OG1 
207  C CG2 . THR A 28  ? 0.65351 0.51679 0.96624 0.05204  0.12186  -0.03838 62  THR A CG2 
208  N N   . ASN A 29  ? 0.57456 0.41614 0.83593 0.07366  0.05150  0.00818  63  ASN A N   
209  C CA  . ASN A 29  ? 0.60372 0.45598 0.87220 0.08194  0.03538  0.00868  63  ASN A CA  
210  C C   . ASN A 29  ? 0.54876 0.40194 0.84414 0.06793  0.05043  -0.00813 63  ASN A C   
211  O O   . ASN A 29  ? 0.57412 0.46527 0.91742 0.07087  0.06119  -0.02171 63  ASN A O   
212  C CB  . ASN A 29  ? 0.43493 0.34054 0.73476 0.10866  0.01444  0.01317  63  ASN A CB  
213  C CG  . ASN A 29  ? 0.68925 0.60758 0.98599 0.12485  -0.00589 0.00730  63  ASN A CG  
214  O OD1 . ASN A 29  ? 0.67408 0.57345 0.97782 0.11890  -0.00621 -0.00924 63  ASN A OD1 
215  N ND2 . ASN A 29  ? 0.65757 0.60992 0.94655 0.14504  -0.02350 0.01905  63  ASN A ND2 
216  N N   . ILE A 30  ? 0.50429 0.31518 0.77246 0.05111  0.04883  -0.00507 64  ILE A N   
217  C CA  . ILE A 30  ? 0.52960 0.33584 0.82376 0.02612  0.06385  -0.01564 64  ILE A CA  
218  C C   . ILE A 30  ? 0.58557 0.42248 0.93032 0.03851  0.04337  -0.03478 64  ILE A C   
219  O O   . ILE A 30  ? 0.60593 0.44149 0.98184 0.01453  0.04975  -0.04540 64  ILE A O   
220  C CB  . ILE A 30  ? 0.79677 0.53551 1.04100 -0.00235 0.06659  0.00181  64  ILE A CB  
221  C CG1 . ILE A 30  ? 0.85149 0.54956 1.07158 0.01749  0.02942  0.00798  64  ILE A CG1 
222  C CG2 . ILE A 30  ? 0.79557 0.51133 0.98239 -0.01690 0.08780  0.01797  64  ILE A CG2 
223  C CD1 . ILE A 30  ? 0.95078 0.57031 1.12156 -0.00614 0.02363  0.03037  64  ILE A CD1 
224  N N   . ILE A 31  ? 0.61386 0.48360 0.96707 0.07268  0.01878  -0.03983 65  ILE A N   
225  C CA  . ILE A 31  ? 0.47934 0.38739 0.87212 0.08939  -0.00302 -0.06284 65  ILE A CA  
226  C C   . ILE A 31  ? 0.51836 0.49719 0.95864 0.10247  0.00112  -0.07023 65  ILE A C   
227  O O   . ILE A 31  ? 0.51087 0.52336 0.99774 0.09826  -0.00406 -0.09104 65  ILE A O   
228  C CB  . ILE A 31  ? 0.52472 0.43511 0.89178 0.12259  -0.03279 -0.06648 65  ILE A CB  
229  C CG1 . ILE A 31  ? 0.63186 0.47513 0.97912 0.11639  -0.05037 -0.07665 65  ILE A CG1 
230  C CG2 . ILE A 31  ? 0.67049 0.65339 1.06754 0.15173  -0.05088 -0.08545 65  ILE A CG2 
231  C CD1 . ILE A 31  ? 0.73638 0.50806 1.03787 0.09532  -0.04074 -0.05023 65  ILE A CD1 
232  N N   . ASN A 32  ? 0.61397 0.61335 1.04573 0.11750  0.00665  -0.05214 66  ASN A N   
233  C CA  . ASN A 32  ? 0.51070 0.56714 0.98348 0.13491  0.00412  -0.05210 66  ASN A CA  
234  C C   . ASN A 32  ? 0.57647 0.62387 1.06047 0.12919  0.02655  -0.04331 66  ASN A C   
235  O O   . ASN A 32  ? 0.65619 0.74206 1.18034 0.14564  0.02298  -0.04360 66  ASN A O   
236  C CB  . ASN A 32  ? 0.57335 0.66867 1.03151 0.16403  -0.01876 -0.03647 66  ASN A CB  
237  C CG  . ASN A 32  ? 0.64598 0.71390 1.05923 0.16386  -0.01777 -0.01170 66  ASN A CG  
238  O OD1 . ASN A 32  ? 0.67338 0.69579 1.06907 0.14624  -0.00187 -0.00298 66  ASN A OD1 
239  N ND2 . ASN A 32  ? 0.67721 0.78155 1.07240 0.18379  -0.03515 -0.00268 66  ASN A ND2 
240  N N   . GLY A 33  ? 0.59632 0.59334 1.04406 0.10992  0.04633  -0.03755 67  GLY A N   
241  C CA  . GLY A 33  ? 0.40538 0.39184 0.86019 0.10675  0.06814  -0.04011 67  GLY A CA  
242  C C   . GLY A 33  ? 0.57952 0.55416 1.02343 0.12301  0.05642  -0.02258 67  GLY A C   
243  O O   . GLY A 33  ? 0.66111 0.62746 1.12293 0.12914  0.06726  -0.03057 67  GLY A O   
244  N N   . VAL A 34  ? 0.56399 0.53881 0.98258 0.12978  0.03415  0.00007  68  VAL A N   
245  C CA  . VAL A 34  ? 0.69704 0.65964 1.10842 0.13574  0.02185  0.02290  68  VAL A CA  
246  C C   . VAL A 34  ? 0.65445 0.56193 1.02129 0.11639  0.03101  0.02179  68  VAL A C   
247  O O   . VAL A 34  ? 0.51795 0.40673 0.84604 0.10277  0.03598  0.01879  68  VAL A O   
248  C CB  . VAL A 34  ? 0.59241 0.59403 0.99822 0.14652  -0.00195 0.05057  68  VAL A CB  
249  C CG1 . VAL A 34  ? 0.54555 0.60575 0.98096 0.16595  -0.01212 0.04512  68  VAL A CG1 
250  C CG2 . VAL A 34  ? 0.61789 0.61191 0.98181 0.13804  -0.00648 0.05605  68  VAL A CG2 
251  N N   . PRO A 35  ? 0.70298 0.57887 1.07236 0.11566  0.03017  0.02222  69  PRO A N   
252  C CA  . PRO A 35  ? 0.47571 0.30116 0.79854 0.09743  0.03416  0.01601  69  PRO A CA  
253  C C   . PRO A 35  ? 0.50054 0.32535 0.79802 0.08685  0.01070  0.04418  69  PRO A C   
254  O O   . PRO A 35  ? 0.52945 0.38728 0.85110 0.09302  -0.00746 0.07126  69  PRO A O   
255  C CB  . PRO A 35  ? 0.61297 0.40502 0.95669 0.10524  0.03514  0.00091  69  PRO A CB  
256  C CG  . PRO A 35  ? 0.57059 0.38979 0.96705 0.12453  0.01719  0.02213  69  PRO A CG  
257  C CD  . PRO A 35  ? 0.44454 0.32357 0.85959 0.13357  0.02182  0.02538  69  PRO A CD  
258  N N   . VAL A 36  ? 0.49785 0.29310 0.74584 0.07034  0.01136  0.03922  70  VAL A N   
259  C CA  . VAL A 36  ? 0.51834 0.32131 0.74599 0.06030  -0.01162 0.06218  70  VAL A CA  
260  C C   . VAL A 36  ? 0.66135 0.41542 0.84649 0.04088  -0.01724 0.05072  70  VAL A C   
261  O O   . VAL A 36  ? 0.59666 0.31361 0.75381 0.03707  0.00082  0.02310  70  VAL A O   
262  C CB  . VAL A 36  ? 0.58576 0.41638 0.79514 0.06698  -0.01529 0.06966  70  VAL A CB  
263  C CG1 . VAL A 36  ? 0.48461 0.36767 0.73270 0.08767  -0.01582 0.07571  70  VAL A CG1 
264  C CG2 . VAL A 36  ? 0.50710 0.29919 0.67372 0.05958  0.00146  0.05172  70  VAL A CG2 
265  N N   . ALA A 37  ? 0.60109 0.36425 0.78248 0.02815  -0.04276 0.07058  71  ALA A N   
266  C CA  . ALA A 37  ? 0.82589 0.55227 0.96413 0.00812  -0.05708 0.06060  71  ALA A CA  
267  C C   . ALA A 37  ? 0.75791 0.50989 0.86475 0.00785  -0.06981 0.07414  71  ALA A C   
268  O O   . ALA A 37  ? 0.77078 0.57712 0.90770 0.01446  -0.08408 0.09864  71  ALA A O   
269  C CB  . ALA A 37  ? 0.76530 0.48119 0.93188 -0.01071 -0.08287 0.07209  71  ALA A CB  
270  N N   . ILE A 38  ? 0.80235 0.51910 0.84814 0.00288  -0.06475 0.05884  72  ILE A N   
271  C CA  . ILE A 38  ? 0.97501 0.70249 0.98509 0.00692  -0.07979 0.07262  72  ILE A CA  
272  C C   . ILE A 38  ? 0.98695 0.69735 0.95471 -0.01160 -0.10650 0.06916  72  ILE A C   
273  O O   . ILE A 38  ? 1.05553 0.72084 0.97334 -0.02476 -0.09941 0.04585  72  ILE A O   
274  C CB  . ILE A 38  ? 1.00566 0.70393 0.97448 0.01316  -0.05723 0.06728  72  ILE A CB  
275  C CG1 . ILE A 38  ? 0.90804 0.62332 0.92445 0.02667  -0.03307 0.06375  72  ILE A CG1 
276  C CG2 . ILE A 38  ? 1.07273 0.77225 1.01085 0.02242  -0.07914 0.08651  72  ILE A CG2 
277  C CD1 . ILE A 38  ? 0.81345 0.49997 0.80052 0.02310  -0.00833 0.05784  72  ILE A CD1 
278  N N   . LYS A 39  ? 0.98082 0.73525 0.96905 -0.01138 -0.13767 0.08914  73  LYS A N   
279  C CA  . LYS A 39  ? 0.93028 0.68323 0.89310 -0.03104 -0.17082 0.08698  73  LYS A CA  
280  C C   . LYS A 39  ? 1.13562 0.89705 1.05387 -0.01835 -0.19195 0.09931  73  LYS A C   
281  O O   . LYS A 39  ? 0.98735 0.79323 0.93686 0.00517  -0.19968 0.11835  73  LYS A O   
282  C CB  . LYS A 39  ? 0.93102 0.73821 0.96291 -0.04597 -0.19390 0.10302  73  LYS A CB  
283  C CG  . LYS A 39  ? 1.07873 0.89652 1.09884 -0.07055 -0.23395 0.10123  73  LYS A CG  
284  C CD  . LYS A 39  ? 0.94189 0.77997 1.02570 -0.10161 -0.24996 0.10940  73  LYS A CD  
285  C CE  . LYS A 39  ? 0.93385 0.82560 1.03969 -0.12517 -0.29318 0.12035  73  LYS A CE  
286  N NZ  . LYS A 39  ? 0.89720 0.87610 1.09257 -0.13832 -0.29841 0.15582  73  LYS A NZ  
287  N N   . PHE A 40  ? 1.18191 0.90055 1.02489 -0.03072 -0.20315 0.08717  74  PHE A N   
288  C CA  . PHE A 40  ? 1.18823 0.90433 0.97749 -0.01961 -0.22866 0.10274  74  PHE A CA  
289  C C   . PHE A 40  ? 1.35777 1.11602 1.15661 -0.03014 -0.27651 0.10637  74  PHE A C   
290  O O   . PHE A 40  ? 1.39836 1.16472 1.21940 -0.05634 -0.28866 0.09032  74  PHE A O   
291  C CB  . PHE A 40  ? 1.28498 0.93629 0.97523 -0.02812 -0.21284 0.09352  74  PHE A CB  
292  C CG  . PHE A 40  ? 1.44788 1.06699 1.12973 -0.02094 -0.16846 0.09568  74  PHE A CG  
293  C CD1 . PHE A 40  ? 1.32274 0.96495 1.07686 -0.00360 -0.15216 0.10352  74  PHE A CD1 
294  C CD2 . PHE A 40  ? 1.46745 1.04093 1.06845 -0.03375 -0.14344 0.08955  74  PHE A CD2 
295  C CE1 . PHE A 40  ? 1.31747 0.93353 1.06963 -0.00092 -0.11598 0.10325  74  PHE A CE1 
296  C CE2 . PHE A 40  ? 1.53090 1.08443 1.13306 -0.03334 -0.10263 0.09352  74  PHE A CE2 
297  C CZ  . PHE A 40  ? 1.44451 1.01719 1.12545 -0.01777 -0.09110 0.09945  74  PHE A CZ  
298  N N   . GLU A 41  ? 1.29497 1.07858 1.08124 -0.00914 -0.30724 0.12740  75  GLU A N   
299  C CA  . GLU A 41  ? 1.35933 1.19430 1.15701 -0.01509 -0.35694 0.13236  75  GLU A CA  
300  C C   . GLU A 41  ? 1.43736 1.25915 1.17718 0.01193  -0.38586 0.15244  75  GLU A C   
301  O O   . GLU A 41  ? 1.47522 1.28826 1.22478 0.04469  -0.37591 0.16970  75  GLU A O   
302  C CB  . GLU A 41  ? 1.27160 1.20306 1.17732 -0.01038 -0.36954 0.14383  75  GLU A CB  
303  C CG  . GLU A 41  ? 1.36240 1.36199 1.29496 -0.02363 -0.42087 0.14754  75  GLU A CG  
304  C CD  . GLU A 41  ? 1.25405 1.36892 1.28877 -0.00559 -0.43224 0.16636  75  GLU A CD  
305  O OE1 . GLU A 41  ? 1.31835 1.45408 1.37417 0.03644  -0.41638 0.17672  75  GLU A OE1 
306  O OE2 . GLU A 41  ? 1.27427 1.46243 1.36961 -0.03437 -0.45705 0.16897  75  GLU A OE2 
307  N N   . PRO A 42  ? 1.43264 1.24715 1.11027 0.00008  -0.42481 0.15045  76  PRO A N   
308  C CA  . PRO A 42  ? 1.53118 1.33366 1.15397 0.02834  -0.46024 0.17635  76  PRO A CA  
309  C C   . PRO A 42  ? 1.56372 1.44151 1.27268 0.06801  -0.48794 0.19474  76  PRO A C   
310  O O   . PRO A 42  ? 1.50105 1.46779 1.30052 0.06353  -0.49950 0.18760  76  PRO A O   
311  C CB  . PRO A 42  ? 1.34603 1.15051 0.90219 0.00446  -0.50308 0.16549  76  PRO A CB  
312  C CG  . PRO A 42  ? 1.57399 1.34859 1.11213 -0.03585 -0.47405 0.12864  76  PRO A CG  
313  C CD  . PRO A 42  ? 1.46970 1.27491 1.11412 -0.03885 -0.43987 0.12217  76  PRO A CD  
314  N N   . ARG A 43  ? 1.85197 1.69419 1.53379 0.10713  -0.49816 0.21861  77  ARG A N   
315  C CA  . ARG A 43  ? 1.82076 1.73470 1.58843 0.15281  -0.50668 0.22395  77  ARG A CA  
316  C C   . ARG A 43  ? 1.80044 1.80457 1.60209 0.16037  -0.54556 0.22293  77  ARG A C   
317  O O   . ARG A 43  ? 1.82908 1.93776 1.72044 0.15879  -0.55098 0.21214  77  ARG A O   
318  C CB  . ARG A 43  ? 1.80956 1.65576 1.54652 0.18660  -0.49270 0.23985  77  ARG A CB  
319  C CG  . ARG A 43  ? 1.86582 1.77928 1.68079 0.23552  -0.49991 0.23947  77  ARG A CG  
320  C CD  . ARG A 43  ? 1.79714 1.80164 1.71309 0.24856  -0.47785 0.21993  77  ARG A CD  
321  N NE  . ARG A 43  ? 2.05997 2.14623 2.04753 0.29199  -0.48544 0.21773  77  ARG A NE  
322  C CZ  . ARG A 43  ? 1.92688 2.10422 2.00070 0.30888  -0.46532 0.20433  77  ARG A CZ  
323  N NH1 . ARG A 43  ? 1.67700 1.87882 1.77854 0.28895  -0.43678 0.19349  77  ARG A NH1 
324  N NH2 . ARG A 43  ? 1.89016 2.13407 2.02324 0.34523  -0.47513 0.20331  77  ARG A NH2 
325  N N   . LYS A 44  ? 1.33592 1.30668 1.06810 0.16710  -0.57171 0.23661  78  LYS A N   
326  C CA  . LYS A 44  ? 1.52328 1.57843 1.28178 0.17605  -0.61219 0.23677  78  LYS A CA  
327  C C   . LYS A 44  ? 1.70066 1.77384 1.43413 0.12581  -0.63488 0.21845  78  LYS A C   
328  O O   . LYS A 44  ? 1.68999 1.71687 1.33137 0.10613  -0.65640 0.21896  78  LYS A O   
329  C CB  . LYS A 44  ? 1.47763 1.48856 1.17210 0.20323  -0.63378 0.26149  78  LYS A CB  
330  C CG  . LYS A 44  ? 1.43167 1.54057 1.17113 0.22669  -0.67492 0.26555  78  LYS A CG  
331  C CD  . LYS A 44  ? 1.53418 1.62437 1.18534 0.20366  -0.71158 0.27032  78  LYS A CD  
332  C CE  . LYS A 44  ? 1.63543 1.60894 1.17308 0.20780  -0.70682 0.29889  78  LYS A CE  
333  N NZ  . LYS A 44  ? 1.74123 1.69639 1.17733 0.18175  -0.73588 0.30203  78  LYS A NZ  
334  N N   . THR A 45  ? 1.50050 1.64296 1.31834 0.10244  -0.62949 0.20134  79  THR A N   
335  C CA  . THR A 45  ? 1.49133 1.64432 1.30381 0.04748  -0.64950 0.18070  79  THR A CA  
336  C C   . THR A 45  ? 1.61135 1.89315 1.52357 0.04013  -0.67630 0.17236  79  THR A C   
337  O O   . THR A 45  ? 1.54567 1.91861 1.54068 0.07734  -0.66979 0.18018  79  THR A O   
338  C CB  . THR A 45  ? 1.59223 1.70384 1.41947 0.01297  -0.62083 0.17168  79  THR A CB  
339  O OG1 . THR A 45  ? 1.64375 1.75547 1.46881 -0.04170 -0.63616 0.14620  79  THR A OG1 
340  C CG2 . THR A 45  ? 1.40069 1.59333 1.34660 0.02995  -0.59302 0.18012  79  THR A CG2 
341  N N   . GLU A 46  ? 1.68892 1.97886 1.59049 -0.00875 -0.70578 0.15235  80  GLU A N   
342  C CA  . GLU A 46  ? 1.68694 2.09482 1.68242 -0.02633 -0.73272 0.14289  80  GLU A CA  
343  C C   . GLU A 46  ? 1.60936 2.08514 1.72002 -0.05302 -0.70728 0.14492  80  GLU A C   
344  O O   . GLU A 46  ? 1.59896 2.19170 1.80545 -0.05378 -0.71583 0.14483  80  GLU A O   
345  C CB  . GLU A 46  ? 1.69622 2.08152 1.64023 -0.07279 -0.77367 0.11710  80  GLU A CB  
346  C CG  . GLU A 46  ? 1.58077 2.08295 1.59579 -0.07927 -0.81324 0.10797  80  GLU A CG  
347  C CD  . GLU A 46  ? 1.67835 2.21299 1.65089 -0.02790 -0.84119 0.11831  80  GLU A CD  
348  O OE1 . GLU A 46  ? 1.77327 2.30456 1.73923 0.02697  -0.82107 0.14259  80  GLU A OE1 
349  O OE2 . GLU A 46  ? 1.81274 2.37409 1.75818 -0.04291 -0.88466 0.10226  80  GLU A OE2 
350  N N   . ALA A 47  ? 1.61973 2.02881 1.72246 -0.07477 -0.67554 0.14818  81  ALA A N   
351  C CA  . ALA A 47  ? 1.58239 2.04788 1.78598 -0.10419 -0.64802 0.15712  81  ALA A CA  
352  C C   . ALA A 47  ? 1.54153 1.98114 1.74924 -0.07054 -0.60224 0.17348  81  ALA A C   
353  O O   . ALA A 47  ? 1.59734 1.94738 1.76647 -0.08902 -0.57583 0.16922  81  ALA A O   
354  C CB  . ALA A 47  ? 1.44363 1.85401 1.64443 -0.17424 -0.66039 0.14179  81  ALA A CB  
355  N N   . PRO A 48  ? 1.49502 2.00543 1.74455 -0.01546 -0.58227 0.18227  82  PRO A N   
356  C CA  . PRO A 48  ? 1.39286 1.88639 1.65219 0.01769  -0.53797 0.19160  82  PRO A CA  
357  C C   . PRO A 48  ? 1.31120 1.86384 1.65196 -0.01647 -0.50638 0.20260  82  PRO A C   
358  O O   . PRO A 48  ? 1.27586 1.93664 1.69585 -0.02957 -0.50341 0.20616  82  PRO A O   
359  C CB  . PRO A 48  ? 1.39582 1.95328 1.67660 0.08650  -0.53456 0.18644  82  PRO A CB  
360  C CG  . PRO A 48  ? 1.52014 2.09800 1.77634 0.09406  -0.57989 0.18007  82  PRO A CG  
361  C CD  . PRO A 48  ? 1.45166 2.04857 1.72886 0.02638  -0.60379 0.17682  82  PRO A CD  
362  N N   . GLN A 49  ? 1.27560 1.75174 1.59135 -0.03004 -0.47735 0.20692  83  GLN A N   
363  C CA  . GLN A 49  ? 1.14684 1.66116 1.52640 -0.06268 -0.44455 0.22090  83  GLN A CA  
364  C C   . GLN A 49  ? 1.00551 1.46956 1.36483 -0.03650 -0.39444 0.22071  83  GLN A C   
365  O O   . GLN A 49  ? 0.84361 1.36851 1.26134 -0.04776 -0.36801 0.23858  83  GLN A O   
366  C CB  . GLN A 49  ? 1.23558 1.68709 1.60731 -0.12897 -0.45631 0.21520  83  GLN A CB  
367  C CG  . GLN A 49  ? 1.31482 1.85826 1.75872 -0.17674 -0.49742 0.22607  83  GLN A CG  
368  C CD  . GLN A 49  ? 1.24847 1.71623 1.69203 -0.24301 -0.50814 0.21902  83  GLN A CD  
369  O OE1 . GLN A 49  ? 1.32892 1.66959 1.70616 -0.24597 -0.48951 0.19857  83  GLN A OE1 
370  N NE2 . GLN A 49  ? 1.14383 1.68238 1.65908 -0.29215 -0.53182 0.23139  83  GLN A NE2 
371  N N   . LEU A 50  ? 1.07968 1.02915 1.66730 0.13219  -0.09486 0.16432  84  LEU A N   
372  C CA  . LEU A 50  ? 0.98020 0.90868 1.56633 0.12192  -0.08108 0.14152  84  LEU A CA  
373  C C   . LEU A 50  ? 0.85854 0.77158 1.49011 0.13589  -0.07664 0.10768  84  LEU A C   
374  O O   . LEU A 50  ? 0.92274 0.83059 1.54681 0.12902  -0.06663 0.07715  84  LEU A O   
375  C CB  . LEU A 50  ? 0.88042 0.77669 1.46430 0.10919  -0.08089 0.17057  84  LEU A CB  
376  C CG  . LEU A 50  ? 0.91769 0.80022 1.49365 0.09306  -0.06775 0.15293  84  LEU A CG  
377  C CD1 . LEU A 50  ? 0.79040 0.70504 1.32546 0.08487  -0.05918 0.12839  84  LEU A CD1 
378  C CD2 . LEU A 50  ? 0.95032 0.81261 1.51489 0.07727  -0.06418 0.18723  84  LEU A CD2 
379  N N   . ARG A 51  ? 0.86955 0.77462 1.54797 0.15576  -0.08437 0.11169  85  ARG A N   
380  C CA  . ARG A 51  ? 0.73074 0.61931 1.45105 0.17033  -0.07776 0.07637  85  ARG A CA  
381  C C   . ARG A 51  ? 0.77048 0.69079 1.47239 0.17369  -0.06575 0.03800  85  ARG A C   
382  O O   . ARG A 51  ? 0.77201 0.68068 1.46997 0.17123  -0.05565 0.00292  85  ARG A O   
383  C CB  . ARG A 51  ? 0.86784 0.74913 1.62153 0.18434  -0.08446 0.08671  85  ARG A CB  
384  C CG  . ARG A 51  ? 0.86586 0.72789 1.64854 0.19423  -0.07487 0.05000  85  ARG A CG  
385  C CD  . ARG A 51  ? 0.96002 0.85126 1.75881 0.21207  -0.06983 0.03326  85  ARG A CD  
386  N NE  . ARG A 51  ? 1.21076 1.08327 2.03423 0.22254  -0.05859 -0.00173 85  ARG A NE  
387  C CZ  . ARG A 51  ? 1.13621 1.03003 1.97388 0.23774  -0.04815 -0.02414 85  ARG A CZ  
388  N NH1 . ARG A 51  ? 1.25047 1.18661 2.08449 0.24357  -0.04822 -0.01532 85  ARG A NH1 
389  N NH2 . ARG A 51  ? 1.08610 0.95885 1.94204 0.24650  -0.03676 -0.05640 85  ARG A NH2 
390  N N   . ASP A 52  ? 0.87963 0.84003 1.56821 0.17789  -0.06742 0.04491  86  ASP A N   
391  C CA  . ASP A 52  ? 0.80165 0.79341 1.47409 0.18043  -0.05445 0.01229  86  ASP A CA  
392  C C   . ASP A 52  ? 0.72087 0.72060 1.33743 0.15986  -0.04683 -0.00058 86  ASP A C   
393  O O   . ASP A 52  ? 0.70611 0.71832 1.30653 0.15973  -0.03478 -0.03212 86  ASP A O   
394  C CB  . ASP A 52  ? 0.77579 0.80889 1.45595 0.18876  -0.05925 0.02557  86  ASP A CB  
395  C CG  . ASP A 52  ? 0.96610 1.00475 1.69412 0.20969  -0.05533 0.01347  86  ASP A CG  
396  O OD1 . ASP A 52  ? 0.98231 0.99167 1.72689 0.21607  -0.04677 -0.00840 86  ASP A OD1 
397  O OD2 . ASP A 52  ? 1.18261 1.25450 1.92171 0.21561  -0.06010 0.02498  86  ASP A OD2 
398  N N   . GLU A 53  ? 0.76284 0.75583 1.34950 0.14290  -0.05289 0.02402  87  GLU A N   
399  C CA  . GLU A 53  ? 0.80223 0.80032 1.34405 0.12474  -0.04592 0.01261  87  GLU A CA  
400  C C   . GLU A 53  ? 0.64537 0.61477 1.19583 0.12113  -0.04118 -0.01334 87  GLU A C   
401  O O   . GLU A 53  ? 0.57601 0.55343 1.09929 0.11333  -0.03483 -0.03731 87  GLU A O   
402  C CB  . GLU A 53  ? 0.70697 0.70489 1.21929 0.10909  -0.05090 0.04474  87  GLU A CB  
403  C CG  . GLU A 53  ? 0.87620 0.88196 1.34750 0.09181  -0.04328 0.03517  87  GLU A CG  
404  C CD  . GLU A 53  ? 0.78748 0.79864 1.22643 0.07830  -0.04441 0.06400  87  GLU A CD  
405  O OE1 . GLU A 53  ? 1.01813 1.03290 1.45595 0.08155  -0.05249 0.09039  87  GLU A OE1 
406  O OE2 . GLU A 53  ? 0.81216 0.82398 1.22645 0.06475  -0.03738 0.05978  87  GLU A OE2 
407  N N   . TYR A 54  ? 0.77151 0.70618 1.36019 0.12602  -0.04602 -0.00814 88  TYR A N   
408  C CA  . TYR A 54  ? 0.60512 0.51020 1.20794 0.12297  -0.04404 -0.03593 88  TYR A CA  
409  C C   . TYR A 54  ? 0.64106 0.55232 1.24436 0.13495  -0.03616 -0.07680 88  TYR A C   
410  O O   . TYR A 54  ? 0.67060 0.57503 1.25491 0.12738  -0.03352 -0.10564 88  TYR A O   
411  C CB  . TYR A 54  ? 0.72708 0.59186 1.37681 0.12713  -0.05086 -0.02184 88  TYR A CB  
412  C CG  . TYR A 54  ? 0.69291 0.52349 1.36752 0.12773  -0.05064 -0.05515 88  TYR A CG  
413  C CD1 . TYR A 54  ? 0.70132 0.52071 1.36193 0.10949  -0.05218 -0.06808 88  TYR A CD1 
414  C CD2 . TYR A 54  ? 0.78152 0.59190 1.49317 0.14551  -0.04960 -0.07419 88  TYR A CD2 
415  C CE1 . TYR A 54  ? 0.92725 0.71460 1.60951 0.10832  -0.05528 -0.09988 88  TYR A CE1 
416  C CE2 . TYR A 54  ? 0.77797 0.56034 1.49780 0.14137  -0.04944 -0.10571 88  TYR A CE2 
417  C CZ  . TYR A 54  ? 0.79502 0.56382 1.50303 0.12362  -0.05371 -0.11917 88  TYR A CZ  
418  O OH  . TYR A 54  ? 1.06317 0.80618 1.77775 0.11823  -0.05660 -0.15052 88  TYR A OH  
419  N N   . ARG A 55  ? 0.84835 0.77364 1.47305 0.15360  -0.03220 -0.07953 89  ARG A N   
420  C CA  . ARG A 55  ? 0.67077 0.60407 1.29532 0.16583  -0.02010 -0.11808 89  ARG A CA  
421  C C   . ARG A 55  ? 0.63695 0.60624 1.21165 0.15747  -0.01148 -0.12991 89  ARG A C   
422  O O   . ARG A 55  ? 0.66668 0.63877 1.22485 0.16109  -0.00069 -0.16380 89  ARG A O   
423  C CB  . ARG A 55  ? 0.74568 0.68592 1.41650 0.18914  -0.01635 -0.11599 89  ARG A CB  
424  C CG  . ARG A 55  ? 0.90031 0.80952 1.60879 0.19261  -0.02775 -0.09114 89  ARG A CG  
425  C CD  . ARG A 55  ? 0.95049 0.85233 1.68965 0.20879  -0.02205 -0.10259 89  ARG A CD  
426  N NE  . ARG A 55  ? 1.18890 1.05800 1.96058 0.20969  -0.03351 -0.07919 89  ARG A NE  
427  C CZ  . ARG A 55  ? 1.28841 1.12099 2.07877 0.21086  -0.03219 -0.09718 89  ARG A CZ  
428  N NH1 . ARG A 55  ? 1.25629 1.07959 2.03431 0.21234  -0.02064 -0.13984 89  ARG A NH1 
429  N NH2 . ARG A 55  ? 1.04723 0.85181 1.86720 0.21000  -0.04300 -0.07154 89  ARG A NH2 
430  N N   . THR A 56  ? 0.69937 0.69418 1.24799 0.14622  -0.01559 -0.10294 90  THR A N   
431  C CA  . THR A 56  ? 0.62325 0.64785 1.12601 0.13664  -0.00842 -0.11207 90  THR A CA  
432  C C   . THR A 56  ? 0.65839 0.66833 1.12802 0.12157  -0.01011 -0.12865 90  THR A C   
433  O O   . THR A 56  ? 0.75160 0.77214 1.19043 0.11925  -0.00278 -0.15238 90  THR A O   
434  C CB  . THR A 56  ? 0.60679 0.65835 1.09268 0.12842  -0.01331 -0.08054 90  THR A CB  
435  O OG1 . THR A 56  ? 0.57619 0.64319 1.09509 0.14196  -0.01581 -0.06467 90  THR A OG1 
436  C CG2 . THR A 56  ? 0.48858 0.56843 0.93186 0.11902  -0.00558 -0.08980 90  THR A CG2 
437  N N   . TYR A 57  ? 0.46598 0.45254 0.94266 0.11082  -0.02007 -0.11501 91  TYR A N   
438  C CA  . TYR A 57  ? 0.54572 0.51925 1.00130 0.09678  -0.02438 -0.13028 91  TYR A CA  
439  C C   . TYR A 57  ? 0.56433 0.51583 1.02535 0.10278  -0.02359 -0.16776 91  TYR A C   
440  O O   . TYR A 57  ? 0.65529 0.60907 1.08370 0.09547  -0.02455 -0.19011 91  TYR A O   
441  C CB  . TYR A 57  ? 0.53801 0.49211 1.01051 0.08452  -0.03315 -0.10741 91  TYR A CB  
442  C CG  . TYR A 57  ? 0.45667 0.43044 0.91211 0.07550  -0.03239 -0.07468 91  TYR A CG  
443  C CD1 . TYR A 57  ? 0.64319 0.64048 1.06095 0.06594  -0.02962 -0.07507 91  TYR A CD1 
444  C CD2 . TYR A 57  ? 0.55536 0.52164 1.03035 0.07640  -0.03457 -0.04356 91  TYR A CD2 
445  C CE1 . TYR A 57  ? 0.53476 0.54695 0.93592 0.05804  -0.02766 -0.04879 91  TYR A CE1 
446  C CE2 . TYR A 57  ? 0.49316 0.47534 0.94588 0.06772  -0.03304 -0.01631 91  TYR A CE2 
447  C CZ  . TYR A 57  ? 0.59116 0.59585 1.00757 0.05874  -0.02891 -0.02078 91  TYR A CZ  
448  O OH  . TYR A 57  ? 0.52789 0.54555 0.92125 0.05049  -0.02615 0.00288  91  TYR A OH  
449  N N   . LYS A 58  ? 0.68601 0.61423 1.18688 0.11623  -0.02273 -0.17535 92  LYS A N   
450  C CA  . LYS A 58  ? 0.66854 0.57306 1.17380 0.12348  -0.02020 -0.21490 92  LYS A CA  
451  C C   . LYS A 58  ? 0.71848 0.64710 1.19033 0.13211  -0.00560 -0.24013 92  LYS A C   
452  O O   . LYS A 58  ? 0.81578 0.73415 1.25953 0.12996  -0.00387 -0.27370 92  LYS A O   
453  C CB  . LYS A 58  ? 0.57983 0.45397 1.13965 0.13835  -0.02042 -0.21632 92  LYS A CB  
454  C CG  . LYS A 58  ? 0.82124 0.65148 1.40591 0.13040  -0.03223 -0.22826 92  LYS A CG  
455  C CD  . LYS A 58  ? 0.78515 0.61238 1.37312 0.11095  -0.04404 -0.19673 92  LYS A CD  
456  C CE  . LYS A 58  ? 0.94779 0.73262 1.56824 0.10140  -0.05565 -0.20719 92  LYS A CE  
457  N NZ  . LYS A 58  ? 0.95283 0.72521 1.54985 0.09525  -0.06107 -0.25066 92  LYS A NZ  
458  N N   . HIS A 59  ? 0.71995 0.68093 1.19356 0.14090  0.00482  -0.22393 93  HIS A N   
459  C CA  . HIS A 59  ? 0.79916 0.78696 1.24408 0.14755  0.02155  -0.24358 93  HIS A CA  
460  C C   . HIS A 59  ? 0.62710 0.63029 1.01435 0.13093  0.01981  -0.24713 93  HIS A C   
461  O O   . HIS A 59  ? 0.74308 0.74958 1.09452 0.13149  0.02921  -0.27451 93  HIS A O   
462  C CB  . HIS A 59  ? 0.76443 0.78548 1.23282 0.15843  0.03051  -0.22166 93  HIS A CB  
463  C CG  . HIS A 59  ? 0.90567 0.95499 1.35871 0.16715  0.05126  -0.24080 93  HIS A CG  
464  N ND1 . HIS A 59  ? 1.03333 1.07423 1.45362 0.16861  0.06369  -0.27718 93  HIS A ND1 
465  C CD2 . HIS A 59  ? 0.81158 0.89821 1.27780 0.17394  0.06241  -0.22815 93  HIS A CD2 
466  C CE1 . HIS A 59  ? 0.90262 0.97455 1.31545 0.17617  0.08450  -0.28503 93  HIS A CE1 
467  N NE2 . HIS A 59  ? 0.88022 0.98116 1.32441 0.17931  0.08391  -0.25563 93  HIS A NE2 
468  N N   . LEU A 60  ? 0.59724 0.60879 0.97404 0.11648  0.00834  -0.21940 94  LEU A N   
469  C CA  . LEU A 60  ? 0.62591 0.65062 0.95533 0.10134  0.00456  -0.21848 94  LEU A CA  
470  C C   . LEU A 60  ? 0.66375 0.66275 0.98203 0.08934  -0.01089 -0.23109 94  LEU A C   
471  O O   . LEU A 60  ? 0.79307 0.80086 1.08273 0.07611  -0.01869 -0.22383 94  LEU A O   
472  C CB  . LEU A 60  ? 0.66018 0.70759 0.98635 0.09284  0.00165  -0.18406 94  LEU A CB  
473  C CG  . LEU A 60  ? 0.58495 0.66234 0.91847 0.10065  0.01296  -0.16987 94  LEU A CG  
474  C CD1 . LEU A 60  ? 0.62608 0.71645 0.96040 0.09169  0.00613  -0.13717 94  LEU A CD1 
475  C CD2 . LEU A 60  ? 0.62048 0.72047 0.91892 0.10052  0.02639  -0.18459 94  LEU A CD2 
476  N N   . GLN A 61  ? 0.68410 0.65153 1.02833 0.09354  -0.01650 -0.24966 95  GLN A N   
477  C CA  . GLN A 61  ? 0.76243 0.70554 1.10391 0.08067  -0.03380 -0.26168 95  GLN A CA  
478  C C   . GLN A 61  ? 0.76602 0.71228 1.05509 0.07484  -0.03713 -0.28867 95  GLN A C   
479  O O   . GLN A 61  ? 0.67743 0.62609 0.94073 0.08440  -0.02445 -0.31309 95  GLN A O   
480  C CB  . GLN A 61  ? 0.88018 0.78609 1.26393 0.08620  -0.03898 -0.27722 95  GLN A CB  
481  C CG  . GLN A 61  ? 0.81489 0.69505 1.20685 0.07096  -0.05889 -0.28769 95  GLN A CG  
482  C CD  . GLN A 61  ? 0.92948 0.77240 1.37468 0.07373  -0.06442 -0.29203 95  GLN A CD  
483  O OE1 . GLN A 61  ? 0.96032 0.79891 1.44454 0.07185  -0.06529 -0.26134 95  GLN A OE1 
484  N NE2 . GLN A 61  ? 0.88395 0.69766 1.32901 0.07781  -0.06783 -0.33030 95  GLN A NE2 
485  N N   . GLY A 62  ? 0.81854 0.76545 1.09206 0.05922  -0.05397 -0.28324 96  GLY A N   
486  C CA  . GLY A 62  ? 0.81549 0.76735 1.03678 0.05194  -0.06175 -0.30176 96  GLY A CA  
487  C C   . GLY A 62  ? 0.84635 0.82989 1.03272 0.04754  -0.05679 -0.28080 96  GLY A C   
488  O O   . GLY A 62  ? 0.99370 0.98158 1.13838 0.03949  -0.06701 -0.28859 96  GLY A O   
489  N N   . CYS A 63  ? 0.85881 0.86290 1.06078 0.05214  -0.04313 -0.25429 97  CYS A N   
490  C CA  . CYS A 63  ? 0.83259 0.86387 1.00636 0.04719  -0.03840 -0.23406 97  CYS A CA  
491  C C   . CYS A 63  ? 0.76778 0.80104 0.95176 0.03451  -0.05386 -0.21364 97  CYS A C   
492  O O   . CYS A 63  ? 0.60279 0.62747 0.82693 0.03186  -0.05849 -0.20043 97  CYS A O   
493  C CB  . CYS A 63  ? 0.86541 0.91698 1.05421 0.05544  -0.02041 -0.21522 97  CYS A CB  
494  S SG  . CYS A 63  ? 0.95809 1.01598 1.14387 0.07170  0.00125  -0.23602 97  CYS A SG  
495  N N   . ASP A 64  ? 0.90105 0.94569 1.05005 0.02703  -0.06063 -0.21002 98  ASP A N   
496  C CA  . ASP A 64  ? 0.67453 0.72450 0.83573 0.01683  -0.07311 -0.19033 98  ASP A CA  
497  C C   . ASP A 64  ? 0.64370 0.70842 0.82369 0.01779  -0.06011 -0.16311 98  ASP A C   
498  O O   . ASP A 64  ? 0.70859 0.78938 0.86720 0.02079  -0.04755 -0.15501 98  ASP A O   
499  C CB  . ASP A 64  ? 0.77361 0.83163 0.89307 0.01061  -0.08374 -0.19170 98  ASP A CB  
500  C CG  . ASP A 64  ? 1.17086 1.21521 1.29111 0.00270  -0.10903 -0.20565 98  ASP A CG  
501  O OD1 . ASP A 64  ? 1.12135 1.15942 1.28576 -0.00262 -0.11947 -0.19932 98  ASP A OD1 
502  O OD2 . ASP A 64  ? 1.29230 1.33273 1.36898 0.00102  -0.11873 -0.22250 98  ASP A OD2 
503  N N   . GLY A 65  ? 0.59692 0.65571 0.81579 0.01424  -0.06283 -0.14932 99  GLY A N   
504  C CA  . GLY A 65  ? 0.56961 0.63899 0.80226 0.01422  -0.05136 -0.12499 99  GLY A CA  
505  C C   . GLY A 65  ? 0.53426 0.59631 0.79334 0.02046  -0.04297 -0.11850 99  GLY A C   
506  O O   . GLY A 65  ? 0.62831 0.69529 0.89923 0.01883  -0.03628 -0.09759 99  GLY A O   
507  N N   . ILE A 66  ? 0.63768 0.68696 0.90510 0.02795  -0.04321 -0.13550 100 ILE A N   
508  C CA  . ILE A 66  ? 0.65495 0.69400 0.95300 0.03518  -0.03785 -0.12841 100 ILE A CA  
509  C C   . ILE A 66  ? 0.57301 0.58786 0.90590 0.03002  -0.04752 -0.13050 100 ILE A C   
510  O O   . ILE A 66  ? 0.58594 0.58631 0.91976 0.02824  -0.05744 -0.15357 100 ILE A O   
511  C CB  . ILE A 66  ? 0.72329 0.76220 1.01792 0.04830  -0.03045 -0.14545 100 ILE A CB  
512  C CG1 . ILE A 66  ? 0.58377 0.64908 0.84749 0.05126  -0.01999 -0.14330 100 ILE A CG1 
513  C CG2 . ILE A 66  ? 0.43682 0.46527 0.76826 0.05710  -0.02713 -0.13460 100 ILE A CG2 
514  C CD1 . ILE A 66  ? 0.56185 0.64412 0.82833 0.04910  -0.01520 -0.11636 100 ILE A CD1 
515  N N   . PRO A 67  ? 0.48736 0.49648 0.84764 0.02637  -0.04518 -0.10745 101 PRO A N   
516  C CA  . PRO A 67  ? 0.52105 0.50737 0.91899 0.01956  -0.05286 -0.10705 101 PRO A CA  
517  C C   . PRO A 67  ? 0.60229 0.56394 1.02256 0.02799  -0.05609 -0.12375 101 PRO A C   
518  O O   . PRO A 67  ? 0.75988 0.72252 1.17688 0.04077  -0.04914 -0.12591 101 PRO A O   
519  C CB  . PRO A 67  ? 0.51403 0.50236 0.92850 0.01490  -0.04451 -0.07478 101 PRO A CB  
520  C CG  . PRO A 67  ? 0.48286 0.48611 0.87448 0.02403  -0.03541 -0.06292 101 PRO A CG  
521  C CD  . PRO A 67  ? 0.45575 0.47779 0.81224 0.02744  -0.03529 -0.08051 101 PRO A CD  
522  N N   . ASN A 68  ? 0.56031 0.49960 1.00756 0.02071  -0.06720 -0.13651 102 ASN A N   
523  C CA  . ASN A 68  ? 0.46895 0.37882 0.94226 0.02760  -0.07094 -0.15419 102 ASN A CA  
524  C C   . ASN A 68  ? 0.49568 0.39081 1.00557 0.03130  -0.06466 -0.12773 102 ASN A C   
525  O O   . ASN A 68  ? 0.55509 0.45279 1.08034 0.02174  -0.06198 -0.09963 102 ASN A O   
526  C CB  . ASN A 68  ? 0.49718 0.38559 0.98966 0.01635  -0.08719 -0.17647 102 ASN A CB  
527  C CG  . ASN A 68  ? 0.58966 0.48252 1.04293 0.01674  -0.09623 -0.21018 102 ASN A CG  
528  O OD1 . ASN A 68  ? 0.73051 0.63306 1.14908 0.02850  -0.08749 -0.22313 102 ASN A OD1 
529  N ND2 . ASN A 68  ? 0.72715 0.61379 1.18596 0.00327  -0.11409 -0.22370 102 ASN A ND2 
530  N N   . ALA A 69  ? 0.67998 0.55963 1.20349 0.04577  -0.06152 -0.13600 103 ALA A N   
531  C CA  . ALA A 69  ? 0.64132 0.50052 1.20362 0.05074  -0.05925 -0.11249 103 ALA A CA  
532  C C   . ALA A 69  ? 0.59472 0.41440 1.19860 0.04715  -0.06838 -0.12887 103 ALA A C   
533  O O   . ALA A 69  ? 0.82518 0.62953 1.42836 0.05367  -0.07253 -0.16453 103 ALA A O   
534  C CB  . ALA A 69  ? 0.67706 0.54336 1.23820 0.07008  -0.05194 -0.10904 103 ALA A CB  
535  N N   . TYR A 70  ? 0.55330 0.35554 1.19225 0.03598  -0.07052 -0.10349 104 TYR A N   
536  C CA  . TYR A 70  ? 0.65518 0.41912 1.33884 0.02840  -0.08016 -0.11618 104 TYR A CA  
537  C C   . TYR A 70  ? 0.64249 0.37478 1.36748 0.03728  -0.07843 -0.09910 104 TYR A C   
538  O O   . TYR A 70  ? 0.66132 0.37305 1.40435 0.03772  -0.08411 -0.11852 104 TYR A O   
539  C CB  . TYR A 70  ? 0.63934 0.40536 1.34151 0.00609  -0.08429 -0.10135 104 TYR A CB  
540  C CG  . TYR A 70  ? 0.66292 0.45600 1.33455 -0.00348 -0.09046 -0.12010 104 TYR A CG  
541  C CD1 . TYR A 70  ? 0.66774 0.45126 1.33163 -0.00535 -0.10475 -0.16059 104 TYR A CD1 
542  C CD2 . TYR A 70  ? 0.58505 0.41149 1.23462 -0.01041 -0.08276 -0.09731 104 TYR A CD2 
543  C CE1 . TYR A 70  ? 0.66003 0.46762 1.29524 -0.01386 -0.11336 -0.17474 104 TYR A CE1 
544  C CE2 . TYR A 70  ? 0.51069 0.36046 1.13699 -0.01787 -0.08968 -0.11232 104 TYR A CE2 
545  C CZ  . TYR A 70  ? 0.61948 0.46024 1.23893 -0.01961 -0.10607 -0.14939 104 TYR A CZ  
546  O OH  . TYR A 70  ? 0.86992 0.73326 1.46531 -0.02682 -0.11586 -0.16150 104 TYR A OH  
547  N N   . TYR A 71  ? 0.63832 0.37768 1.36483 0.04284  -0.07069 -0.06043 105 TYR A N   
548  C CA  . TYR A 71  ? 0.64378 0.36111 1.40120 0.04869  -0.07042 -0.03736 105 TYR A CA  
549  C C   . TYR A 71  ? 0.67051 0.40017 1.41769 0.06346  -0.06543 -0.00654 105 TYR A C   
550  O O   . TYR A 71  ? 0.69920 0.45839 1.41223 0.05938  -0.06017 0.01263  105 TYR A O   
551  C CB  . TYR A 71  ? 0.67106 0.37506 1.45470 0.02928  -0.07053 -0.01030 105 TYR A CB  
552  C CG  . TYR A 71  ? 0.71112 0.39851 1.51622 0.03362  -0.06849 0.02544  105 TYR A CG  
553  C CD1 . TYR A 71  ? 0.73634 0.39951 1.56880 0.04219  -0.07364 0.01434  105 TYR A CD1 
554  C CD2 . TYR A 71  ? 0.80011 0.49525 1.59478 0.02922  -0.06152 0.07049  105 TYR A CD2 
555  C CE1 . TYR A 71  ? 0.83201 0.47923 1.68452 0.04635  -0.07332 0.04805  105 TYR A CE1 
556  C CE2 . TYR A 71  ? 0.77004 0.44996 1.57873 0.03285  -0.06147 0.10445  105 TYR A CE2 
557  C CZ  . TYR A 71  ? 0.76059 0.41659 1.60006 0.04146  -0.06806 0.09361  105 TYR A CZ  
558  O OH  . TYR A 71  ? 1.11846 0.75824 1.97296 0.04519  -0.06938 0.12846  105 TYR A OH  
559  N N   . PHE A 72  ? 0.80072 0.51878 1.56618 0.07780  -0.06721 -0.00211 106 PHE A N   
560  C CA  . PHE A 72  ? 0.65854 0.38649 1.42126 0.09015  -0.06689 0.03251  106 PHE A CA  
561  C C   . PHE A 72  ? 0.80360 0.50617 1.59955 0.09544  -0.07120 0.04744  106 PHE A C   
562  O O   . PHE A 72  ? 0.80635 0.49239 1.62360 0.10243  -0.07261 0.01826  106 PHE A O   
563  C CB  . PHE A 72  ? 0.88438 0.63988 1.62950 0.10930  -0.06500 0.01564  106 PHE A CB  
564  C CG  . PHE A 72  ? 0.99402 0.76039 1.74445 0.12340  -0.06867 0.04642  106 PHE A CG  
565  C CD1 . PHE A 72  ? 0.98596 0.76090 1.72102 0.11778  -0.07193 0.09039  106 PHE A CD1 
566  C CD2 . PHE A 72  ? 0.89950 0.66799 1.66885 0.14167  -0.06922 0.03165  106 PHE A CD2 
567  C CE1 . PHE A 72  ? 0.86633 0.65220 1.60312 0.12950  -0.07929 0.11897  106 PHE A CE1 
568  C CE2 . PHE A 72  ? 1.00806 0.78867 1.78569 0.15391  -0.07525 0.06036  106 PHE A CE2 
569  C CZ  . PHE A 72  ? 0.93126 0.72079 1.69181 0.14750  -0.08207 0.10401  106 PHE A CZ  
570  N N   . GLY A 73  ? 0.90991 0.60850 1.70758 0.09209  -0.07308 0.09269  107 GLY A N   
571  C CA  . GLY A 73  ? 0.93353 0.60767 1.76196 0.09694  -0.07814 0.11175  107 GLY A CA  
572  C C   . GLY A 73  ? 0.95266 0.62835 1.76864 0.09295  -0.08057 0.16445  107 GLY A C   
573  O O   . GLY A 73  ? 0.96738 0.66320 1.74896 0.08671  -0.07767 0.18505  107 GLY A O   
574  N N   . GLN A 74  ? 1.10357 0.75642 1.94555 0.09658  -0.08605 0.18609  108 GLN A N   
575  C CA  . GLN A 74  ? 1.22752 0.87728 2.05610 0.09300  -0.08992 0.23718  108 GLN A CA  
576  C C   . GLN A 74  ? 1.20705 0.83266 2.04671 0.07336  -0.08396 0.25784  108 GLN A C   
577  O O   . GLN A 74  ? 1.26764 0.86823 2.14553 0.07099  -0.08439 0.24183  108 GLN A O   
578  C CB  . GLN A 74  ? 1.33941 0.98217 2.18884 0.11182  -0.10163 0.25151  108 GLN A CB  
579  C CG  . GLN A 74  ? 1.34303 1.01505 2.18366 0.13108  -0.10752 0.23842  108 GLN A CG  
580  C CD  . GLN A 74  ? 1.53299 1.20200 2.39363 0.14765  -0.12043 0.26103  108 GLN A CD  
581  O OE1 . GLN A 74  ? 1.42405 1.08969 2.26918 0.14400  -0.12893 0.30445  108 GLN A OE1 
582  N NE2 . GLN A 74  ? 1.69318 1.36333 2.58717 0.16587  -0.12156 0.23160  108 GLN A NE2 
583  N N   . GLU A 75  ? 1.19793 0.83189 2.00343 0.05906  -0.07739 0.29271  109 GLU A N   
584  C CA  . GLU A 75  ? 1.30924 0.92481 2.12136 0.04000  -0.06874 0.31787  109 GLU A CA  
585  C C   . GLU A 75  ? 1.44415 1.06241 2.21687 0.03649  -0.06824 0.36881  109 GLU A C   
586  O O   . GLU A 75  ? 1.41494 1.05535 2.14119 0.03044  -0.06172 0.38231  109 GLU A O   
587  C CB  . GLU A 75  ? 1.26704 0.89283 2.07525 0.02122  -0.05518 0.30040  109 GLU A CB  
588  C CG  . GLU A 75  ? 1.08496 0.70920 1.92377 0.02341  -0.05823 0.24912  109 GLU A CG  
589  C CD  . GLU A 75  ? 1.12141 0.74487 1.97653 0.00280  -0.04939 0.23709  109 GLU A CD  
590  O OE1 . GLU A 75  ? 1.19696 0.82820 2.03600 -0.01268 -0.03713 0.26590  109 GLU A OE1 
591  O OE2 . GLU A 75  ? 1.23921 0.85540 2.12244 0.00211  -0.05469 0.19836  109 GLU A OE2 
592  N N   . GLY A 76  ? 1.48640 1.08108 2.27480 0.04006  -0.07537 0.39655  110 GLY A N   
593  C CA  . GLY A 76  ? 1.58364 1.17933 2.32977 0.03873  -0.07849 0.44425  110 GLY A CA  
594  C C   . GLY A 76  ? 1.63174 1.24886 2.35308 0.05685  -0.09404 0.44708  110 GLY A C   
595  O O   . GLY A 76  ? 1.44801 1.06628 2.20227 0.07525  -0.10624 0.42445  110 GLY A O   
596  N N   . LEU A 77  ? 1.68998 1.32576 2.35187 0.05119  -0.09298 0.47404  111 LEU A N   
597  C CA  . LEU A 77  ? 1.65953 1.32050 2.29248 0.06542  -0.10880 0.47794  111 LEU A CA  
598  C C   . LEU A 77  ? 1.59326 1.28453 2.20320 0.06419  -0.10228 0.45100  111 LEU A C   
599  O O   . LEU A 77  ? 1.57410 1.28905 2.13777 0.06601  -0.10922 0.46344  111 LEU A O   
600  C CB  . LEU A 77  ? 1.81805 1.47937 2.39523 0.06076  -0.11639 0.52505  111 LEU A CB  
601  C CG  . LEU A 77  ? 1.74543 1.40861 2.26152 0.03897  -0.09788 0.54897  111 LEU A CG  
602  C CD1 . LEU A 77  ? 1.71210 1.38928 2.15896 0.03916  -0.11002 0.58045  111 LEU A CD1 
603  C CD2 . LEU A 77  ? 1.80158 1.43406 2.33119 0.02476  -0.08348 0.56931  111 LEU A CD2 
604  N N   . HIS A 78  ? 1.50576 1.19624 2.14639 0.06075  -0.09046 0.41380  112 HIS A N   
605  C CA  . HIS A 78  ? 1.26824 0.98405 1.88971 0.05862  -0.08311 0.38813  112 HIS A CA  
606  C C   . HIS A 78  ? 1.08984 0.80669 1.75676 0.06971  -0.08419 0.33995  112 HIS A C   
607  O O   . HIS A 78  ? 1.28210 0.97677 1.99040 0.06782  -0.08103 0.32205  112 HIS A O   
608  C CB  . HIS A 78  ? 1.10068 0.81721 1.69643 0.03624  -0.06190 0.39428  112 HIS A CB  
609  C CG  . HIS A 78  ? 1.33388 1.06261 1.86478 0.02592  -0.05638 0.43025  112 HIS A CG  
610  N ND1 . HIS A 78  ? 1.27190 1.02714 1.75912 0.03031  -0.06207 0.43162  112 HIS A ND1 
611  C CD2 . HIS A 78  ? 1.34713 1.06539 1.84565 0.01080  -0.04471 0.46412  112 HIS A CD2 
612  C CE1 . HIS A 78  ? 1.31620 1.07601 1.74378 0.01793  -0.05476 0.46331  112 HIS A CE1 
613  N NE2 . HIS A 78  ? 1.57441 1.31196 2.00639 0.00636  -0.04306 0.48316  112 HIS A NE2 
614  N N   . ASN A 79  ? 1.17792 0.92121 1.83380 0.08075  -0.08861 0.31846  113 ASN A N   
615  C CA  . ASN A 79  ? 1.03388 0.78286 1.71707 0.08830  -0.08521 0.27040  113 ASN A CA  
616  C C   . ASN A 79  ? 1.06180 0.81711 1.72721 0.07260  -0.07125 0.25571  113 ASN A C   
617  O O   . ASN A 79  ? 0.91123 0.68987 1.52561 0.06065  -0.06413 0.27035  113 ASN A O   
618  C CB  . ASN A 79  ? 1.06777 0.84529 1.74934 0.10787  -0.09475 0.25357  113 ASN A CB  
619  C CG  . ASN A 79  ? 1.24908 1.01991 1.96594 0.12519  -0.10545 0.25085  113 ASN A CG  
620  O OD1 . ASN A 79  ? 1.26379 1.05028 1.97330 0.13511  -0.11802 0.27234  113 ASN A OD1 
621  N ND2 . ASN A 79  ? 1.35501 1.10274 2.11072 0.12843  -0.10113 0.22367  113 ASN A ND2 
622  N N   . ILE A 80  ? 0.99434 0.73869 1.68861 0.06937  -0.06610 0.21898  114 ILE A N   
623  C CA  . ILE A 80  ? 0.83717 0.59088 1.51647 0.05126  -0.05388 0.20107  114 ILE A CA  
624  C C   . ILE A 80  ? 0.85307 0.62438 1.53117 0.05783  -0.05464 0.15132  114 ILE A C   
625  O O   . ILE A 80  ? 0.77708 0.53037 1.49069 0.07018  -0.06091 0.12546  114 ILE A O   
626  C CB  . ILE A 80  ? 0.94462 0.66890 1.65784 0.03518  -0.04841 0.20820  114 ILE A CB  
627  C CG1 . ILE A 80  ? 0.93296 0.65251 1.62705 0.02291  -0.04088 0.25650  114 ILE A CG1 
628  C CG2 . ILE A 80  ? 0.74140 0.47136 1.46104 0.02094  -0.04131 0.17922  114 ILE A CG2 
629  C CD1 . ILE A 80  ? 1.00806 0.70338 1.73477 0.01208  -0.03798 0.26730  114 ILE A CD1 
630  N N   . LEU A 81  ? 0.64594 0.45073 1.28169 0.04982  -0.04755 0.13819  115 LEU A N   
631  C CA  . LEU A 81  ? 0.72927 0.55103 1.35654 0.05215  -0.04724 0.09484  115 LEU A CA  
632  C C   . LEU A 81  ? 0.69057 0.51936 1.30849 0.03310  -0.04006 0.08632  115 LEU A C   
633  O O   . LEU A 81  ? 0.68615 0.53100 1.27700 0.02190  -0.03115 0.10811  115 LEU A O   
634  C CB  . LEU A 81  ? 0.64278 0.50076 1.23116 0.06224  -0.04726 0.08623  115 LEU A CB  
635  C CG  . LEU A 81  ? 0.70725 0.58405 1.27966 0.06350  -0.04529 0.04541  115 LEU A CG  
636  C CD1 . LEU A 81  ? 0.56975 0.42347 1.17711 0.07374  -0.04985 0.01377  115 LEU A CD1 
637  C CD2 . LEU A 81  ? 0.73881 0.65112 1.27555 0.07124  -0.04375 0.04159  115 LEU A CD2 
638  N N   . VAL A 82  ? 0.70844 0.52537 1.34943 0.02976  -0.04437 0.05394  116 VAL A N   
639  C CA  . VAL A 82  ? 0.61130 0.43514 1.25344 0.01244  -0.04171 0.04354  116 VAL A CA  
640  C C   . VAL A 82  ? 0.50931 0.35529 1.12436 0.01597  -0.04588 0.00663  116 VAL A C   
641  O O   . VAL A 82  ? 0.61016 0.44551 1.23207 0.02586  -0.05338 -0.02350 116 VAL A O   
642  C CB  . VAL A 82  ? 0.55505 0.34486 1.24967 0.00182  -0.04698 0.03932  116 VAL A CB  
643  C CG1 . VAL A 82  ? 0.54040 0.34235 1.24218 -0.01631 -0.04630 0.02950  116 VAL A CG1 
644  C CG2 . VAL A 82  ? 0.58589 0.35115 1.30719 -0.00178 -0.04193 0.07941  116 VAL A CG2 
645  N N   . ILE A 83  ? 0.58290 0.45816 1.16605 0.00827  -0.04004 0.00921  117 ILE A N   
646  C CA  . ILE A 83  ? 0.63966 0.53575 1.19556 0.00927  -0.04419 -0.02037 117 ILE A CA  
647  C C   . ILE A 83  ? 0.47818 0.38619 1.03817 -0.00670 -0.04342 -0.01969 117 ILE A C   
648  O O   . ILE A 83  ? 0.52840 0.43104 1.11272 -0.01797 -0.03686 0.00276  117 ILE A O   
649  C CB  . ILE A 83  ? 0.42208 0.34585 0.93327 0.01941  -0.03879 -0.01891 117 ILE A CB  
650  C CG1 . ILE A 83  ? 0.50738 0.44691 0.99843 0.01355  -0.02815 0.01312  117 ILE A CG1 
651  C CG2 . ILE A 83  ? 0.52970 0.44658 1.04413 0.03642  -0.04088 -0.02508 117 ILE A CG2 
652  C CD1 . ILE A 83  ? 0.49172 0.46090 0.93879 0.01664  -0.02400 0.00990  117 ILE A CD1 
653  N N   . ASP A 84  ? 0.49030 0.41546 1.02780 -0.00728 -0.04964 -0.04334 118 ASP A N   
654  C CA  . ASP A 84  ? 0.40214 0.34230 0.94548 -0.02015 -0.05110 -0.04326 118 ASP A CA  
655  C C   . ASP A 84  ? 0.43064 0.38993 0.96049 -0.02420 -0.03454 -0.01459 118 ASP A C   
656  O O   . ASP A 84  ? 0.37189 0.34031 0.86930 -0.01644 -0.02561 -0.00244 118 ASP A O   
657  C CB  . ASP A 84  ? 0.49041 0.44590 1.00426 -0.01789 -0.06183 -0.07017 118 ASP A CB  
658  C CG  . ASP A 84  ? 0.42036 0.35681 0.94693 -0.01867 -0.07950 -0.10127 118 ASP A CG  
659  O OD1 . ASP A 84  ? 0.74376 0.66229 1.31321 -0.02867 -0.08766 -0.10321 118 ASP A OD1 
660  O OD2 . ASP A 84  ? 0.58676 0.52569 1.07958 -0.01013 -0.08466 -0.12440 118 ASP A OD2 
661  N N   . LEU A 85  ? 0.39560 0.36125 0.95224 -0.03675 -0.03035 -0.00494 119 LEU A N   
662  C CA  . LEU A 85  ? 0.42501 0.40921 0.96882 -0.04088 -0.01235 0.01741  119 LEU A CA  
663  C C   . LEU A 85  ? 0.48676 0.49503 1.00639 -0.03938 -0.01503 0.00435  119 LEU A C   
664  O O   . LEU A 85  ? 0.44556 0.45808 0.98008 -0.04253 -0.02995 -0.01445 119 LEU A O   
665  C CB  . LEU A 85  ? 0.40749 0.38819 0.99723 -0.05454 -0.00199 0.03581  119 LEU A CB  
666  C CG  . LEU A 85  ? 0.52971 0.52705 1.10676 -0.05877 0.02176  0.05912  119 LEU A CG  
667  C CD1 . LEU A 85  ? 0.41995 0.41124 0.95455 -0.05231 0.03372  0.07886  119 LEU A CD1 
668  C CD2 . LEU A 85  ? 0.37887 0.37553 1.00798 -0.07288 0.03409  0.07524  119 LEU A CD2 
669  N N   . LEU A 86  ? 0.47223 0.49459 0.95387 -0.03495 -0.00216 0.01477  120 LEU A N   
670  C CA  . LEU A 86  ? 0.45397 0.49601 0.91011 -0.03246 -0.00342 0.00485  120 LEU A CA  
671  C C   . LEU A 86  ? 0.50502 0.55955 0.95623 -0.03651 0.01665  0.02218  120 LEU A C   
672  O O   . LEU A 86  ? 0.49690 0.54577 0.95681 -0.04113 0.03246  0.04166  120 LEU A O   
673  C CB  . LEU A 86  ? 0.42916 0.47470 0.84059 -0.02215 -0.00856 -0.00544 120 LEU A CB  
674  C CG  . LEU A 86  ? 0.45613 0.49120 0.86842 -0.01666 -0.02497 -0.02657 120 LEU A CG  
675  C CD1 . LEU A 86  ? 0.42434 0.46456 0.79918 -0.00637 -0.02406 -0.03182 120 LEU A CD1 
676  C CD2 . LEU A 86  ? 0.34118 0.38083 0.76094 -0.02025 -0.04023 -0.04603 120 LEU A CD2 
677  N N   . GLY A 87  ? 0.55960 0.62967 0.99526 -0.03462 0.01688  0.01494  121 GLY A N   
678  C CA  . GLY A 87  ? 0.45610 0.53714 0.88979 -0.03722 0.03622  0.02621  121 GLY A CA  
679  C C   . GLY A 87  ? 0.40247 0.48361 0.78695 -0.03328 0.04924  0.03404  121 GLY A C   
680  O O   . GLY A 87  ? 0.48569 0.55859 0.84516 -0.02987 0.04557  0.03751  121 GLY A O   
681  N N   . PRO A 88  ? 0.58939 0.67970 0.96160 -0.03356 0.06368  0.03612  122 PRO A N   
682  C CA  . PRO A 88  ? 0.65558 0.74445 0.97974 -0.03176 0.07564  0.04186  122 PRO A CA  
683  C C   . PRO A 88  ? 0.38294 0.47379 0.67284 -0.02601 0.06069  0.03076  122 PRO A C   
684  O O   . PRO A 88  ? 0.34975 0.44474 0.64780 -0.02294 0.04512  0.01791  122 PRO A O   
685  C CB  . PRO A 88  ? 0.59082 0.68729 0.91813 -0.03318 0.09440  0.04175  122 PRO A CB  
686  C CG  . PRO A 88  ? 0.50533 0.60886 0.89029 -0.03622 0.09544  0.04171  122 PRO A CG  
687  C CD  . PRO A 88  ? 0.43406 0.53582 0.83927 -0.03540 0.06940  0.03284  122 PRO A CD  
688  N N   . SER A 89  ? 0.34638 0.43485 0.59662 -0.02544 0.06563  0.03655  123 SER A N   
689  C CA  . SER A 89  ? 0.48571 0.57874 0.70669 -0.02147 0.05409  0.02784  123 SER A CA  
690  C C   . SER A 89  ? 0.51365 0.61232 0.72052 -0.02194 0.05854  0.01898  123 SER A C   
691  O O   . SER A 89  ? 0.42008 0.51810 0.63442 -0.02419 0.07267  0.02021  123 SER A O   
692  C CB  . SER A 89  ? 0.41824 0.50815 0.60749 -0.02152 0.05397  0.03799  123 SER A CB  
693  O OG  . SER A 89  ? 0.44060 0.52689 0.60354 -0.02650 0.06956  0.04622  123 SER A OG  
694  N N   . LEU A 90  ? 0.54454 0.64842 0.73411 -0.01952 0.04747  0.01024  124 LEU A N   
695  C CA  . LEU A 90  ? 0.43496 0.54096 0.60987 -0.02056 0.05070  0.00360  124 LEU A CA  
696  C C   . LEU A 90  ? 0.43239 0.53317 0.57833 -0.02457 0.06403  0.00704  124 LEU A C   
697  O O   . LEU A 90  ? 0.53374 0.63133 0.67409 -0.02573 0.07237  0.00165  124 LEU A O   
698  C CB  . LEU A 90  ? 0.41934 0.53174 0.58101 -0.01884 0.03770  -0.00389 124 LEU A CB  
699  C CG  . LEU A 90  ? 0.35397 0.47001 0.53466 -0.01528 0.02536  -0.01044 124 LEU A CG  
700  C CD1 . LEU A 90  ? 0.35616 0.47912 0.51850 -0.01418 0.01724  -0.01652 124 LEU A CD1 
701  C CD2 . LEU A 90  ? 0.40328 0.51798 0.60571 -0.01532 0.02515  -0.01223 124 LEU A CD2 
702  N N   . GLU A 91  ? 0.54427 0.64246 0.67068 -0.02657 0.06532  0.01568  125 GLU A N   
703  C CA  . GLU A 91  ? 0.52373 0.61499 0.61690 -0.03146 0.07778  0.01888  125 GLU A CA  
704  C C   . GLU A 91  ? 0.59762 0.68262 0.70168 -0.03285 0.09893  0.02263  125 GLU A C   
705  O O   . GLU A 91  ? 0.55134 0.63024 0.63612 -0.03530 0.11408  0.01731  125 GLU A O   
706  C CB  . GLU A 91  ? 0.55162 0.64224 0.62001 -0.03326 0.07027  0.02986  125 GLU A CB  
707  C CG  . GLU A 91  ? 0.60907 0.69123 0.63445 -0.03948 0.08053  0.03394  125 GLU A CG  
708  C CD  . GLU A 91  ? 0.71865 0.80004 0.71584 -0.04363 0.07755  0.02075  125 GLU A CD  
709  O OE1 . GLU A 91  ? 0.76686 0.85687 0.77503 -0.04230 0.06376  0.01352  125 GLU A OE1 
710  O OE2 . GLU A 91  ? 0.59987 0.67098 0.56344 -0.04884 0.09002  0.01708  125 GLU A OE2 
711  N N   . ASP A 92  ? 0.51203 0.59829 0.64970 -0.03158 0.10142  0.03076  126 ASP A N   
712  C CA  . ASP A 92  ? 0.53788 0.62211 0.69609 -0.03340 0.12307  0.03528  126 ASP A CA  
713  C C   . ASP A 92  ? 0.45645 0.54492 0.63946 -0.03035 0.12934  0.02334  126 ASP A C   
714  O O   . ASP A 92  ? 0.53112 0.61625 0.70882 -0.03092 0.15044  0.02027  126 ASP A O   
715  C CB  . ASP A 92  ? 0.56230 0.64776 0.75963 -0.03408 0.12126  0.04622  126 ASP A CB  
716  C CG  . ASP A 92  ? 0.61300 0.69079 0.78972 -0.03669 0.11856  0.06182  126 ASP A CG  
717  O OD1 . ASP A 92  ? 0.66435 0.73611 0.79797 -0.04000 0.12821  0.06890  126 ASP A OD1 
718  O OD2 . ASP A 92  ? 0.57418 0.65047 0.77712 -0.03534 0.10570  0.06689  126 ASP A OD2 
719  N N   . LEU A 93  ? 0.43103 0.52610 0.64075 -0.02655 0.11129  0.01665  127 LEU A N   
720  C CA  . LEU A 93  ? 0.44029 0.53890 0.67452 -0.02287 0.11258  0.00812  127 LEU A CA  
721  C C   . LEU A 93  ? 0.56107 0.65225 0.76213 -0.02252 0.11824  -0.00052 127 LEU A C   
722  O O   . LEU A 93  ? 0.54156 0.63064 0.75875 -0.01944 0.12932  -0.00615 127 LEU A O   
723  C CB  . LEU A 93  ? 0.40611 0.51155 0.66438 -0.01989 0.08873  0.00428  127 LEU A CB  
724  C CG  . LEU A 93  ? 0.39054 0.50023 0.68007 -0.02114 0.07917  0.00904  127 LEU A CG  
725  C CD1 . LEU A 93  ? 0.48516 0.59789 0.77715 -0.01890 0.05438  0.00200  127 LEU A CD1 
726  C CD2 . LEU A 93  ? 0.37483 0.49084 0.71422 -0.02190 0.08941  0.01291  127 LEU A CD2 
727  N N   . PHE A 94  ? 0.60583 0.69279 0.76507 -0.02563 0.11007  -0.00198 128 PHE A N   
728  C CA  . PHE A 94  ? 0.45467 0.53260 0.58119 -0.02779 0.11462  -0.01087 128 PHE A CA  
729  C C   . PHE A 94  ? 0.55840 0.62652 0.66942 -0.02946 0.14009  -0.01380 128 PHE A C   
730  O O   . PHE A 94  ? 0.58717 0.64736 0.70205 -0.02727 0.15172  -0.02376 128 PHE A O   
731  C CB  . PHE A 94  ? 0.55167 0.63023 0.64154 -0.03232 0.10016  -0.01025 128 PHE A CB  
732  C CG  . PHE A 94  ? 0.58015 0.65104 0.64321 -0.03625 0.09804  -0.02025 128 PHE A CG  
733  C CD1 . PHE A 94  ? 0.50476 0.57432 0.58339 -0.03442 0.09179  -0.02617 128 PHE A CD1 
734  C CD2 . PHE A 94  ? 0.55453 0.61857 0.57616 -0.04284 0.10018  -0.02281 128 PHE A CD2 
735  C CE1 . PHE A 94  ? 0.53471 0.59499 0.59227 -0.03942 0.08978  -0.03455 128 PHE A CE1 
736  C CE2 . PHE A 94  ? 0.55820 0.61403 0.55779 -0.04825 0.09636  -0.03346 128 PHE A CE2 
737  C CZ  . PHE A 94  ? 0.52201 0.57544 0.54167 -0.04674 0.09200  -0.03936 128 PHE A CZ  
738  N N   . ASP A 95  ? 0.46658 0.53376 0.55954 -0.03301 0.15017  -0.00489 129 ASP A N   
739  C CA  . ASP A 95  ? 0.64366 0.70161 0.71568 -0.03521 0.17764  -0.00698 129 ASP A CA  
740  C C   . ASP A 95  ? 0.60854 0.66981 0.72714 -0.02952 0.19822  -0.01056 129 ASP A C   
741  O O   . ASP A 95  ? 0.73634 0.78852 0.84543 -0.02808 0.22039  -0.02125 129 ASP A O   
742  C CB  . ASP A 95  ? 0.64899 0.70645 0.69785 -0.04018 0.18410  0.00833  129 ASP A CB  
743  C CG  . ASP A 95  ? 0.80668 0.85621 0.79538 -0.04636 0.17375  0.00934  129 ASP A CG  
744  O OD1 . ASP A 95  ? 0.97848 1.01817 0.93284 -0.04907 0.17680  -0.00479 129 ASP A OD1 
745  O OD2 . ASP A 95  ? 1.00697 1.05949 0.98514 -0.04859 0.16121  0.02420  129 ASP A OD2 
746  N N   . TRP A 96  ? 0.50701 0.58138 0.67862 -0.02606 0.19069  -0.00283 130 TRP A N   
747  C CA  . TRP A 96  ? 0.57966 0.66169 0.80495 -0.02096 0.20785  -0.00374 130 TRP A CA  
748  C C   . TRP A 96  ? 0.49165 0.57163 0.73968 -0.01378 0.20358  -0.01576 130 TRP A C   
749  O O   . TRP A 96  ? 0.47672 0.56006 0.76338 -0.00809 0.22251  -0.01942 130 TRP A O   
750  C CB  . TRP A 96  ? 0.51070 0.60730 0.78677 -0.02126 0.19661  0.00793  130 TRP A CB  
751  C CG  . TRP A 96  ? 0.72686 0.82289 0.98947 -0.02807 0.20329  0.02192  130 TRP A CG  
752  C CD1 . TRP A 96  ? 0.76791 0.85529 0.98927 -0.03296 0.22598  0.02756  130 TRP A CD1 
753  C CD2 . TRP A 96  ? 0.75995 0.86163 1.04825 -0.03099 0.18642  0.03266  130 TRP A CD2 
754  N NE1 . TRP A 96  ? 0.87482 0.96242 1.09660 -0.03857 0.22399  0.04423  130 TRP A NE1 
755  C CE2 . TRP A 96  ? 0.82938 0.92489 1.09453 -0.03727 0.20018  0.04669  130 TRP A CE2 
756  C CE3 . TRP A 96  ? 0.51822 0.62753 0.84443 -0.02919 0.16076  0.03118  130 TRP A CE3 
757  C CZ2 . TRP A 96  ? 0.81293 0.90840 1.09752 -0.04124 0.18935  0.05974  130 TRP A CZ2 
758  C CZ3 . TRP A 96  ? 0.69239 0.80159 1.03516 -0.03338 0.15049  0.04074  130 TRP A CZ3 
759  C CH2 . TRP A 96  ? 0.84094 0.94271 1.16594 -0.03908 0.16489  0.05513  130 TRP A CH2 
760  N N   . CYS A 97  ? 0.63039 0.70513 0.85854 -0.01371 0.18017  -0.02064 131 CYS A N   
761  C CA  . CYS A 97  ? 0.44864 0.51792 0.69432 -0.00779 0.17426  -0.02904 131 CYS A CA  
762  C C   . CYS A 97  ? 0.46047 0.51025 0.66540 -0.00927 0.18668  -0.04244 131 CYS A C   
763  O O   . CYS A 97  ? 0.55195 0.59237 0.76055 -0.00658 0.17763  -0.04877 131 CYS A O   
764  C CB  . CYS A 97  ? 0.61813 0.69244 0.86784 -0.00781 0.14275  -0.02509 131 CYS A CB  
765  S SG  . CYS A 97  ? 0.45438 0.54786 0.75368 -0.00570 0.12445  -0.01444 131 CYS A SG  
766  N N   . GLY A 98  ? 0.51134 0.55305 0.67592 -0.01428 0.20642  -0.04667 132 GLY A N   
767  C CA  . GLY A 98  ? 0.59249 0.61366 0.71354 -0.01722 0.21707  -0.06227 132 GLY A CA  
768  C C   . GLY A 98  ? 0.67790 0.69252 0.75091 -0.02602 0.19512  -0.06431 132 GLY A C   
769  O O   . GLY A 98  ? 0.72117 0.71818 0.76597 -0.02943 0.19649  -0.07838 132 GLY A O   
770  N N   . ARG A 99  ? 0.62119 0.64957 0.68834 -0.02979 0.17494  -0.05139 133 ARG A N   
771  C CA  . ARG A 99  ? 0.62679 0.65469 0.65784 -0.03743 0.15337  -0.05122 133 ARG A CA  
772  C C   . ARG A 99  ? 0.67822 0.70002 0.71798 -0.03783 0.13950  -0.05836 133 ARG A C   
773  O O   . ARG A 99  ? 0.54332 0.55477 0.55196 -0.04520 0.13318  -0.06702 133 ARG A O   
774  C CB  . ARG A 99  ? 0.62709 0.64390 0.60167 -0.04564 0.16059  -0.05709 133 ARG A CB  
775  C CG  . ARG A 99  ? 0.55082 0.57359 0.51072 -0.04674 0.17096  -0.04470 133 ARG A CG  
776  C CD  . ARG A 99  ? 0.79283 0.80661 0.69036 -0.05591 0.16920  -0.04630 133 ARG A CD  
777  N NE  . ARG A 99  ? 0.85530 0.87501 0.73744 -0.06150 0.14019  -0.04438 133 ARG A NE  
778  C CZ  . ARG A 99  ? 0.84916 0.88422 0.74084 -0.06106 0.12145  -0.02881 133 ARG A CZ  
779  N NH1 . ARG A 99  ? 0.79461 0.83797 0.70983 -0.05608 0.12643  -0.01389 133 ARG A NH1 
780  N NH2 . ARG A 99  ? 0.80789 0.84997 0.68921 -0.06577 0.09770  -0.02868 133 ARG A NH2 
781  N N   . ARG A 100 ? 0.60373 0.63192 0.68681 -0.03076 0.13349  -0.05340 134 ARG A N   
782  C CA  . ARG A 100 ? 0.53876 0.56276 0.63231 -0.03107 0.11862  -0.05441 134 ARG A CA  
783  C C   . ARG A 100 ? 0.55504 0.59125 0.69015 -0.02368 0.10775  -0.04397 134 ARG A C   
784  O O   . ARG A 100 ? 0.61902 0.65670 0.78895 -0.01600 0.11697  -0.04260 134 ARG A O   
785  C CB  . ARG A 100 ? 0.67348 0.67476 0.76622 -0.03053 0.13040  -0.06745 134 ARG A CB  
786  C CG  . ARG A 100 ? 0.71029 0.70286 0.80540 -0.03425 0.11523  -0.06727 134 ARG A CG  
787  C CD  . ARG A 100 ? 0.94706 0.92023 1.07078 -0.02730 0.12410  -0.07275 134 ARG A CD  
788  N NE  . ARG A 100 ? 0.92542 0.88058 1.04003 -0.03420 0.11549  -0.07659 134 ARG A NE  
789  C CZ  . ARG A 100 ? 1.05414 0.98778 1.14273 -0.04173 0.12301  -0.09276 134 ARG A CZ  
790  N NH1 . ARG A 100 ? 1.06295 0.99010 1.12515 -0.04303 0.13945  -0.10712 134 ARG A NH1 
791  N NH2 . ARG A 100 ? 1.18673 1.10385 1.27399 -0.04911 0.11371  -0.09453 134 ARG A NH2 
792  N N   . PHE A 101 ? 0.45084 0.49675 0.58299 -0.02613 0.08822  -0.03704 135 PHE A N   
793  C CA  . PHE A 101 ? 0.52448 0.58016 0.68604 -0.02058 0.07486  -0.02837 135 PHE A CA  
794  C C   . PHE A 101 ? 0.48860 0.53385 0.65645 -0.02015 0.06679  -0.02624 135 PHE A C   
795  O O   . PHE A 101 ? 0.57112 0.60721 0.71623 -0.02700 0.06533  -0.02918 135 PHE A O   
796  C CB  . PHE A 101 ? 0.46113 0.53268 0.61276 -0.02284 0.06040  -0.02291 135 PHE A CB  
797  C CG  . PHE A 101 ? 0.49236 0.57355 0.65363 -0.02081 0.06406  -0.02077 135 PHE A CG  
798  C CD1 . PHE A 101 ? 0.50858 0.58912 0.69735 -0.01653 0.07630  -0.02026 135 PHE A CD1 
799  C CD2 . PHE A 101 ? 0.45598 0.54680 0.60326 -0.02311 0.05613  -0.01851 135 PHE A CD2 
800  C CE1 . PHE A 101 ? 0.52280 0.61114 0.72304 -0.01635 0.08040  -0.01628 135 PHE A CE1 
801  C CE2 . PHE A 101 ? 0.50131 0.59749 0.65982 -0.02162 0.05897  -0.01507 135 PHE A CE2 
802  C CZ  . PHE A 101 ? 0.47755 0.57200 0.66165 -0.01913 0.07101  -0.01332 135 PHE A CZ  
803  N N   . SER A 102 ? 0.46258 0.50916 0.66341 -0.01276 0.06021  -0.01969 136 SER A N   
804  C CA  . SER A 102 ? 0.52326 0.55936 0.73116 -0.01165 0.04987  -0.01311 136 SER A CA  
805  C C   . SER A 102 ? 0.54291 0.58592 0.72405 -0.01837 0.03458  -0.00624 136 SER A C   
806  O O   . SER A 102 ? 0.61037 0.66849 0.77623 -0.02108 0.03007  -0.00694 136 SER A O   
807  C CB  . SER A 102 ? 0.44807 0.48728 0.69807 -0.00185 0.04184  -0.00508 136 SER A CB  
808  O OG  . SER A 102 ? 0.42466 0.48251 0.68084 -0.00091 0.02790  -0.00004 136 SER A OG  
809  N N   . VAL A 103 ? 0.52572 0.55662 0.70305 -0.02082 0.02816  0.00090  137 VAL A N   
810  C CA  . VAL A 103 ? 0.58180 0.61930 0.73391 -0.02782 0.01736  0.00878  137 VAL A CA  
811  C C   . VAL A 103 ? 0.49414 0.54745 0.64652 -0.02369 0.00301  0.01535  137 VAL A C   
812  O O   . VAL A 103 ? 0.43855 0.50527 0.56862 -0.02765 -0.00045 0.01435  137 VAL A O   
813  C CB  . VAL A 103 ? 0.47066 0.48964 0.62145 -0.03182 0.01436  0.01830  137 VAL A CB  
814  C CG1 . VAL A 103 ? 0.34096 0.36845 0.46620 -0.03936 0.00591  0.02881  137 VAL A CG1 
815  C CG2 . VAL A 103 ? 0.39020 0.39160 0.53808 -0.03796 0.02747  0.00811  137 VAL A CG2 
816  N N   . LYS A 104 ? 0.46922 0.52131 0.64867 -0.01555 -0.00595 0.02089  138 LYS A N   
817  C CA  . LYS A 104 ? 0.54827 0.61354 0.72747 -0.01268 -0.02293 0.02535  138 LYS A CA  
818  C C   . LYS A 104 ? 0.53665 0.61695 0.71422 -0.01279 -0.01960 0.01429  138 LYS A C   
819  O O   . LYS A 104 ? 0.55450 0.64457 0.71269 -0.01461 -0.02868 0.01267  138 LYS A O   
820  C CB  . LYS A 104 ? 0.43495 0.49745 0.65115 -0.00429 -0.03531 0.03337  138 LYS A CB  
821  C CG  . LYS A 104 ? 0.48931 0.56528 0.70992 -0.00202 -0.05588 0.03566  138 LYS A CG  
822  C CD  . LYS A 104 ? 0.46704 0.54291 0.73289 0.00617  -0.06967 0.04428  138 LYS A CD  
823  C CE  . LYS A 104 ? 0.53475 0.62439 0.80710 0.00682  -0.09357 0.04498  138 LYS A CE  
824  N NZ  . LYS A 104 ? 0.58225 0.67479 0.90350 0.01449  -0.11113 0.05535  138 LYS A NZ  
825  N N   . THR A 105 ? 0.49410 0.57467 0.69074 -0.01082 -0.00556 0.00667  139 THR A N   
826  C CA  . THR A 105 ? 0.52563 0.61754 0.72205 -0.01140 -0.00179 -0.00089 139 THR A CA  
827  C C   . THR A 105 ? 0.47179 0.56822 0.63422 -0.01711 0.00205  -0.00507 139 THR A C   
828  O O   . THR A 105 ? 0.42185 0.52779 0.57725 -0.01705 -0.00338 -0.00867 139 THR A O   
829  C CB  . THR A 105 ? 0.44583 0.53577 0.66575 -0.00905 0.01488  -0.00524 139 THR A CB  
830  O OG1 . THR A 105 ? 0.58167 0.67427 0.84320 -0.00296 0.01077  -0.00178 139 THR A OG1 
831  C CG2 . THR A 105 ? 0.39758 0.49545 0.61044 -0.01135 0.02100  -0.01004 139 THR A CG2 
832  N N   . VAL A 106 ? 0.48753 0.57723 0.63245 -0.02201 0.01066  -0.00525 140 VAL A N   
833  C CA  . VAL A 106 ? 0.40783 0.50519 0.52790 -0.02762 0.01332  -0.00826 140 VAL A CA  
834  C C   . VAL A 106 ? 0.39533 0.50151 0.50003 -0.02860 0.00373  -0.00525 140 VAL A C   
835  O O   . VAL A 106 ? 0.46998 0.58790 0.56521 -0.02868 0.00366  -0.00969 140 VAL A O   
836  C CB  . VAL A 106 ? 0.39465 0.48302 0.50293 -0.03447 0.02178  -0.00936 140 VAL A CB  
837  C CG1 . VAL A 106 ? 0.39259 0.49273 0.48208 -0.04098 0.02141  -0.01037 140 VAL A CG1 
838  C CG2 . VAL A 106 ? 0.27721 0.35747 0.39054 -0.03394 0.03314  -0.01574 140 VAL A CG2 
839  N N   . VAL A 107 ? 0.40464 0.50456 0.50598 -0.02883 -0.00383 0.00269  141 VAL A N   
840  C CA  . VAL A 107 ? 0.39676 0.50364 0.47558 -0.03068 -0.01086 0.00633  141 VAL A CA  
841  C C   . VAL A 107 ? 0.59574 0.71107 0.67427 -0.02551 -0.01983 -0.00069 141 VAL A C   
842  O O   . VAL A 107 ? 0.62493 0.75023 0.68667 -0.02589 -0.01801 -0.00689 141 VAL A O   
843  C CB  . VAL A 107 ? 0.51150 0.60709 0.58406 -0.03232 -0.01854 0.01960  141 VAL A CB  
844  C CG1 . VAL A 107 ? 0.40639 0.50827 0.45072 -0.03335 -0.02725 0.02375  141 VAL A CG1 
845  C CG2 . VAL A 107 ? 0.50618 0.59233 0.57552 -0.03967 -0.00897 0.02563  141 VAL A CG2 
846  N N   . GLN A 108 ? 0.58119 0.69257 0.68187 -0.02067 -0.02933 -0.00085 142 GLN A N   
847  C CA  . GLN A 108 ? 0.52529 0.64224 0.62891 -0.01739 -0.04064 -0.00855 142 GLN A CA  
848  C C   . GLN A 108 ? 0.54450 0.66779 0.65431 -0.01622 -0.03197 -0.01923 142 GLN A C   
849  O O   . GLN A 108 ? 0.50647 0.63415 0.60568 -0.01484 -0.03628 -0.02818 142 GLN A O   
850  C CB  . GLN A 108 ? 0.37954 0.49312 0.51493 -0.01378 -0.05312 -0.00542 142 GLN A CB  
851  C CG  . GLN A 108 ? 0.61399 0.72117 0.74767 -0.01322 -0.06622 0.00710  142 GLN A CG  
852  C CD  . GLN A 108 ? 0.49485 0.60210 0.67076 -0.00859 -0.07833 0.01089  142 GLN A CD  
853  O OE1 . GLN A 108 ? 0.71508 0.82215 0.89250 -0.00734 -0.09941 0.01747  142 GLN A OE1 
854  N NE2 . GLN A 108 ? 0.51036 0.61901 0.72137 -0.00623 -0.06503 0.00748  142 GLN A NE2 
855  N N   . VAL A 109 ? 0.46812 0.59018 0.59358 -0.01650 -0.01987 -0.01842 143 VAL A N   
856  C CA  . VAL A 109 ? 0.31517 0.44189 0.44483 -0.01550 -0.01267 -0.02452 143 VAL A CA  
857  C C   . VAL A 109 ? 0.54625 0.68120 0.65349 -0.01680 -0.00786 -0.02759 143 VAL A C   
858  O O   . VAL A 109 ? 0.53107 0.67116 0.64009 -0.01375 -0.00722 -0.03422 143 VAL A O   
859  C CB  . VAL A 109 ? 0.33719 0.45976 0.48109 -0.01643 -0.00107 -0.02104 143 VAL A CB  
860  C CG1 . VAL A 109 ? 0.56176 0.68849 0.70186 -0.01645 0.00547  -0.02303 143 VAL A CG1 
861  C CG2 . VAL A 109 ? 0.56401 0.68264 0.73822 -0.01410 -0.00248 -0.01950 143 VAL A CG2 
862  N N   . ALA A 110 ? 0.52954 0.66599 0.61992 -0.02121 -0.00414 -0.02252 144 ALA A N   
863  C CA  . ALA A 110 ? 0.41951 0.56745 0.49584 -0.02343 0.00243  -0.02425 144 ALA A CA  
864  C C   . ALA A 110 ? 0.51413 0.66879 0.57605 -0.02034 -0.00021 -0.03097 144 ALA A C   
865  O O   . ALA A 110 ? 0.47140 0.63671 0.53390 -0.01746 0.00546  -0.03766 144 ALA A O   
866  C CB  . ALA A 110 ? 0.40444 0.55151 0.47065 -0.03096 0.00748  -0.01629 144 ALA A CB  
867  N N   . ILE A 111 ? 0.42546 0.57375 0.47362 -0.02049 -0.00896 -0.02963 145 ILE A N   
868  C CA  . ILE A 111 ? 0.55635 0.70902 0.58132 -0.01851 -0.01076 -0.03763 145 ILE A CA  
869  C C   . ILE A 111 ? 0.53326 0.68461 0.56947 -0.01200 -0.01546 -0.05229 145 ILE A C   
870  O O   . ILE A 111 ? 0.66444 0.82037 0.68634 -0.00869 -0.01165 -0.06401 145 ILE A O   
871  C CB  . ILE A 111 ? 0.50916 0.65388 0.51063 -0.02128 -0.02204 -0.03072 145 ILE A CB  
872  C CG1 . ILE A 111 ? 0.65725 0.79161 0.67802 -0.01902 -0.03890 -0.02960 145 ILE A CG1 
873  C CG2 . ILE A 111 ? 0.56593 0.70936 0.55747 -0.02798 -0.01610 -0.01486 145 ILE A CG2 
874  C CD1 . ILE A 111 ? 0.72976 0.85693 0.73146 -0.02099 -0.05465 -0.02054 145 ILE A CD1 
875  N N   . GLN A 112 ? 0.56139 0.70556 0.62465 -0.01025 -0.02208 -0.05232 146 GLN A N   
876  C CA  . GLN A 112 ? 0.50999 0.65069 0.58955 -0.00534 -0.02573 -0.06443 146 GLN A CA  
877  C C   . GLN A 112 ? 0.47059 0.61795 0.56332 -0.00165 -0.01396 -0.06628 146 GLN A C   
878  O O   . GLN A 112 ? 0.50824 0.65462 0.60650 0.00386  -0.01330 -0.07806 146 GLN A O   
879  C CB  . GLN A 112 ? 0.37574 0.50766 0.48356 -0.00609 -0.03552 -0.06148 146 GLN A CB  
880  C CG  . GLN A 112 ? 0.59699 0.72419 0.70053 -0.00858 -0.05156 -0.05992 146 GLN A CG  
881  C CD  . GLN A 112 ? 0.53600 0.65839 0.67682 -0.00919 -0.06084 -0.05860 146 GLN A CD  
882  O OE1 . GLN A 112 ? 0.63930 0.75885 0.80339 -0.00808 -0.05781 -0.06331 146 GLN A OE1 
883  N NE2 . GLN A 112 ? 0.58064 0.70255 0.73114 -0.01095 -0.07187 -0.05070 146 GLN A NE2 
884  N N   . MET A 113 ? 0.42894 0.58200 0.52727 -0.00443 -0.00607 -0.05527 147 MET A N   
885  C CA  . MET A 113 ? 0.48991 0.65155 0.59964 -0.00138 0.00163  -0.05473 147 MET A CA  
886  C C   . MET A 113 ? 0.48849 0.66411 0.58761 0.00120  0.00937  -0.06120 147 MET A C   
887  O O   . MET A 113 ? 0.38167 0.56320 0.49498 0.00804  0.01311  -0.06745 147 MET A O   
888  C CB  . MET A 113 ? 0.34333 0.50713 0.45641 -0.00664 0.00547  -0.04263 147 MET A CB  
889  C CG  . MET A 113 ? 0.38316 0.53473 0.50822 -0.00808 0.00315  -0.03692 147 MET A CG  
890  S SD  . MET A 113 ? 0.53415 0.68347 0.65110 -0.01549 0.00894  -0.02716 147 MET A SD  
891  C CE  . MET A 113 ? 0.35346 0.50566 0.47560 -0.01467 0.01110  -0.02192 147 MET A CE  
892  N N   . LEU A 114 ? 0.59093 0.77202 0.66779 -0.00390 0.01307  -0.05872 148 LEU A N   
893  C CA  . LEU A 114 ? 0.54723 0.74327 0.61360 -0.00233 0.02416  -0.06432 148 LEU A CA  
894  C C   . LEU A 114 ? 0.54135 0.73331 0.59961 0.00549  0.02461  -0.08143 148 LEU A C   
895  O O   . LEU A 114 ? 0.54259 0.74623 0.60675 0.01169  0.03578  -0.09066 148 LEU A O   
896  C CB  . LEU A 114 ? 0.52242 0.72206 0.56409 -0.01096 0.02855  -0.05553 148 LEU A CB  
897  C CG  . LEU A 114 ? 0.52697 0.73180 0.57712 -0.01958 0.03129  -0.04165 148 LEU A CG  
898  C CD1 . LEU A 114 ? 0.48185 0.68282 0.50878 -0.02824 0.03319  -0.03163 148 LEU A CD1 
899  C CD2 . LEU A 114 ? 0.44475 0.67060 0.51495 -0.01925 0.04086  -0.04185 148 LEU A CD2 
900  N N   . THR A 115 ? 0.66972 0.84524 0.71671 0.00537  0.01229  -0.08713 149 THR A N   
901  C CA  . THR A 115 ? 0.55299 0.72062 0.59049 0.01158  0.00993  -0.10647 149 THR A CA  
902  C C   . THR A 115 ? 0.51926 0.68224 0.59062 0.01995  0.01001  -0.11512 149 THR A C   
903  O O   . THR A 115 ? 0.58900 0.75176 0.66160 0.02783  0.01694  -0.13173 149 THR A O   
904  C CB  . THR A 115 ? 0.46122 0.61312 0.48113 0.00751  -0.00762 -0.10949 149 THR A CB  
905  O OG1 . THR A 115 ? 0.63155 0.78648 0.61892 0.00075  -0.00871 -0.09930 149 THR A OG1 
906  C CG2 . THR A 115 ? 0.53099 0.67196 0.53837 0.01235  -0.01270 -0.13248 149 THR A CG2 
907  N N   . LEU A 116 ? 0.59129 0.74915 0.68988 0.01864  0.00354  -0.10368 150 LEU A N   
908  C CA  . LEU A 116 ? 0.42383 0.57557 0.55461 0.02580  0.00304  -0.10683 150 LEU A CA  
909  C C   . LEU A 116 ? 0.43680 0.60474 0.58204 0.03282  0.01515  -0.10600 150 LEU A C   
910  O O   . LEU A 116 ? 0.54497 0.71003 0.70771 0.04259  0.01879  -0.11792 150 LEU A O   
911  C CB  . LEU A 116 ? 0.33701 0.48109 0.48788 0.02140  -0.00395 -0.09136 150 LEU A CB  
912  C CG  . LEU A 116 ? 0.52741 0.65611 0.68209 0.01652  -0.01588 -0.09295 150 LEU A CG  
913  C CD1 . LEU A 116 ? 0.44576 0.57193 0.61703 0.01148  -0.01644 -0.07573 150 LEU A CD1 
914  C CD2 . LEU A 116 ? 0.58530 0.69871 0.75655 0.02121  -0.02223 -0.10831 150 LEU A CD2 
915  N N   . VAL A 117 ? 0.44270 0.62769 0.58492 0.02801  0.02069  -0.09237 151 VAL A N   
916  C CA  . VAL A 117 ? 0.48379 0.68850 0.64570 0.03346  0.02981  -0.08984 151 VAL A CA  
917  C C   . VAL A 117 ? 0.46942 0.68506 0.62451 0.03989  0.04355  -0.10598 151 VAL A C   
918  O O   . VAL A 117 ? 0.53588 0.76178 0.71754 0.05029  0.05122  -0.11233 151 VAL A O   
919  C CB  . VAL A 117 ? 0.45212 0.67197 0.61151 0.02419  0.03055  -0.07321 151 VAL A CB  
920  C CG1 . VAL A 117 ? 0.39333 0.63789 0.57683 0.02842  0.03807  -0.07076 151 VAL A CG1 
921  C CG2 . VAL A 117 ? 0.36799 0.57617 0.53216 0.01932  0.01983  -0.05987 151 VAL A CG2 
922  N N   . GLU A 118 ? 0.47786 0.69131 0.59720 0.03439  0.04750  -0.11243 152 GLU A N   
923  C CA  . GLU A 118 ? 0.50579 0.72747 0.60981 0.03986  0.06306  -0.12906 152 GLU A CA  
924  C C   . GLU A 118 ? 0.60646 0.81295 0.72138 0.05188  0.06289  -0.15062 152 GLU A C   
925  O O   . GLU A 118 ? 0.67464 0.89140 0.80601 0.06250  0.07779  -0.16329 152 GLU A O   
926  C CB  . GLU A 118 ? 0.46185 0.67927 0.51777 0.03079  0.06419  -0.12988 152 GLU A CB  
927  C CG  . GLU A 118 ? 0.60673 0.83127 0.63651 0.03527  0.08252  -0.14720 152 GLU A CG  
928  C CD  . GLU A 118 ? 0.70308 0.92008 0.67826 0.02603  0.08080  -0.14620 152 GLU A CD  
929  O OE1 . GLU A 118 ? 0.74461 0.95121 0.70815 0.01713  0.06406  -0.13170 152 GLU A OE1 
930  O OE2 . GLU A 118 ? 0.70465 0.92586 0.64813 0.02813  0.09658  -0.15949 152 GLU A OE2 
931  N N   . GLU A 119 ? 0.61439 0.79611 0.72470 0.05035  0.04650  -0.15558 153 GLU A N   
932  C CA  . GLU A 119 ? 0.71806 0.88071 0.84131 0.06005  0.04403  -0.17676 153 GLU A CA  
933  C C   . GLU A 119 ? 0.57230 0.73872 0.74477 0.07167  0.04822  -0.17406 153 GLU A C   
934  O O   . GLU A 119 ? 0.65086 0.81084 0.83915 0.08373  0.05632  -0.19329 153 GLU A O   
935  C CB  . GLU A 119 ? 0.80266 0.94026 0.92157 0.05373  0.02359  -0.17838 153 GLU A CB  
936  C CG  . GLU A 119 ? 0.91704 1.04499 0.99032 0.04685  0.01640  -0.19147 153 GLU A CG  
937  C CD  . GLU A 119 ? 0.92498 1.04304 0.97850 0.05449  0.02434  -0.22163 153 GLU A CD  
938  O OE1 . GLU A 119 ? 0.93417 1.04371 1.01896 0.06528  0.02995  -0.23506 153 GLU A OE1 
939  O OE2 . GLU A 119 ? 1.02691 1.14423 1.03208 0.04993  0.02516  -0.23195 153 GLU A OE2 
940  N N   . VAL A 120 ? 0.50404 0.67961 0.70031 0.06862  0.04221  -0.15050 154 VAL A N   
941  C CA  . VAL A 120 ? 0.50376 0.68565 0.74483 0.07926  0.04355  -0.14342 154 VAL A CA  
942  C C   . VAL A 120 ? 0.61603 0.82351 0.87146 0.08863  0.06170  -0.15104 154 VAL A C   
943  O O   . VAL A 120 ? 0.61640 0.82352 0.90652 0.10311  0.06773  -0.16078 154 VAL A O   
944  C CB  . VAL A 120 ? 0.44349 0.63124 0.69644 0.07206  0.03256  -0.11621 154 VAL A CB  
945  C CG1 . VAL A 120 ? 0.45224 0.65147 0.74722 0.08234  0.03186  -0.10569 154 VAL A CG1 
946  C CG2 . VAL A 120 ? 0.47658 0.63915 0.72477 0.06525  0.01870  -0.10954 154 VAL A CG2 
947  N N   . HIS A 121 ? 0.58416 0.81420 0.81715 0.08070  0.07174  -0.14633 155 HIS A N   
948  C CA  . HIS A 121 ? 0.53049 0.78883 0.77996 0.08776  0.09191  -0.15229 155 HIS A CA  
949  C C   . HIS A 121 ? 0.52219 0.77338 0.75839 0.09788  0.10921  -0.18097 155 HIS A C   
950  O O   . HIS A 121 ? 0.60536 0.87445 0.87104 0.11024  0.12727  -0.19105 155 HIS A O   
951  C CB  . HIS A 121 ? 0.44861 0.73018 0.67657 0.07420  0.09887  -0.13893 155 HIS A CB  
952  C CG  . HIS A 121 ? 0.49640 0.78634 0.73811 0.06459  0.08412  -0.11443 155 HIS A CG  
953  N ND1 . HIS A 121 ? 0.41290 0.71718 0.63758 0.05044  0.08590  -0.10117 155 HIS A ND1 
954  C CD2 . HIS A 121 ? 0.46465 0.74850 0.73236 0.06658  0.06748  -0.10139 155 HIS A CD2 
955  C CE1 . HIS A 121 ? 0.41914 0.72539 0.65809 0.04429  0.07087  -0.08391 155 HIS A CE1 
956  N NE2 . HIS A 121 ? 0.41033 0.70508 0.67275 0.05380  0.05971  -0.08307 155 HIS A NE2 
957  N N   . ARG A 122 ? 0.60116 0.82696 0.79405 0.09294  0.10387  -0.19522 156 ARG A N   
958  C CA  . ARG A 122 ? 0.59006 0.80505 0.76072 0.10115  0.11859  -0.22546 156 ARG A CA  
959  C C   . ARG A 122 ? 0.64626 0.84854 0.86164 0.11888  0.12159  -0.24252 156 ARG A C   
960  O O   . ARG A 122 ? 0.65497 0.86155 0.87496 0.13114  0.14299  -0.26574 156 ARG A O   
961  C CB  . ARG A 122 ? 0.72503 0.91302 0.84264 0.09115  0.10484  -0.23603 156 ARG A CB  
962  C CG  . ARG A 122 ? 0.89138 1.08908 0.96357 0.07534  0.10214  -0.22009 156 ARG A CG  
963  C CD  . ARG A 122 ? 0.90087 1.12146 0.94712 0.07524  0.12856  -0.22497 156 ARG A CD  
964  N NE  . ARG A 122 ? 1.21866 1.42457 1.20223 0.07087  0.13128  -0.24278 156 ARG A NE  
965  C CZ  . ARG A 122 ? 1.47183 1.68496 1.42738 0.07621  0.15658  -0.26239 156 ARG A CZ  
966  N NH1 . ARG A 122 ? 1.25486 1.49105 1.24669 0.08747  0.18307  -0.26825 156 ARG A NH1 
967  N NH2 . ARG A 122 ? 1.46464 1.66214 1.35432 0.07028  0.15529  -0.27648 156 ARG A NH2 
968  N N   . HIS A 123 ? 0.63363 0.81931 0.88304 0.12078  0.10189  -0.23085 157 HIS A N   
969  C CA  . HIS A 123 ? 0.78341 0.95217 1.07911 0.13705  0.10141  -0.24273 157 HIS A CA  
970  C C   . HIS A 123 ? 0.56840 0.76277 0.92211 0.14920  0.10758  -0.22709 157 HIS A C   
971  O O   . HIS A 123 ? 0.83086 1.01130 1.23074 0.16237  0.10200  -0.22760 157 HIS A O   
972  C CB  . HIS A 123 ? 0.75152 0.88710 1.05523 0.13205  0.07719  -0.23616 157 HIS A CB  
973  C CG  . HIS A 123 ? 0.73831 0.84822 0.99662 0.12170  0.06814  -0.25413 157 HIS A CG  
974  N ND1 . HIS A 123 ? 0.62143 0.73912 0.83112 0.10637  0.06336  -0.24760 157 HIS A ND1 
975  C CD2 . HIS A 123 ? 0.76902 0.84540 1.02571 0.12417  0.06087  -0.27829 157 HIS A CD2 
976  C CE1 . HIS A 123 ? 0.59832 0.69069 0.77857 0.10018  0.05214  -0.26587 157 HIS A CE1 
977  N NE2 . HIS A 123 ? 0.80328 0.87031 1.01054 0.10993  0.05022  -0.28566 157 HIS A NE2 
978  N N   . ASP A 124 ? 0.61015 0.84112 0.96468 0.14452  0.11735  -0.21237 158 ASP A N   
979  C CA  . ASP A 124 ? 0.55739 0.81978 0.96828 0.15499  0.12336  -0.19888 158 ASP A CA  
980  C C   . ASP A 124 ? 0.62747 0.88932 1.06772 0.15183  0.09839  -0.16861 158 ASP A C   
981  O O   . ASP A 124 ? 0.78598 1.05861 1.28061 0.16479  0.09438  -0.15897 158 ASP A O   
982  C CB  . ASP A 124 ? 0.58970 0.85121 1.04532 0.17757  0.14042  -0.22131 158 ASP A CB  
983  C CG  . ASP A 124 ? 0.70060 0.95055 1.11747 0.18105  0.16341  -0.25619 158 ASP A CG  
984  O OD1 . ASP A 124 ? 0.82902 1.09146 1.19555 0.16811  0.17427  -0.25858 158 ASP A OD1 
985  O OD2 . ASP A 124 ? 0.86877 1.09354 1.30049 0.19540  0.16906  -0.27984 158 ASP A OD2 
986  N N   . LEU A 125 ? 0.52633 0.77594 0.93048 0.13503  0.08171  -0.15309 159 LEU A N   
987  C CA  . LEU A 125 ? 0.53139 0.77956 0.95063 0.12952  0.06020  -0.12486 159 LEU A CA  
988  C C   . LEU A 125 ? 0.61388 0.88167 1.00418 0.11190  0.05597  -0.10773 159 LEU A C   
989  O O   . LEU A 125 ? 0.52740 0.79572 0.87651 0.10100  0.06384  -0.11527 159 LEU A O   
990  C CB  . LEU A 125 ? 0.55594 0.76578 0.96367 0.12617  0.04449  -0.12171 159 LEU A CB  
991  C CG  . LEU A 125 ? 0.65392 0.83622 1.09761 0.14084  0.04030  -0.12931 159 LEU A CG  
992  C CD1 . LEU A 125 ? 0.64257 0.83983 1.14226 0.15598  0.03679  -0.11531 159 LEU A CD1 
993  C CD2 . LEU A 125 ? 0.75992 0.92566 1.19491 0.14860  0.05468  -0.16352 159 LEU A CD2 
994  N N   . ILE A 126 ? 0.47568 0.75795 0.88729 0.10915  0.04228  -0.08458 160 ILE A N   
995  C CA  . ILE A 126 ? 0.38084 0.67258 0.76490 0.09169  0.03337  -0.06767 160 ILE A CA  
996  C C   . ILE A 126 ? 0.46507 0.73410 0.84043 0.08692  0.01404  -0.05002 160 ILE A C   
997  O O   . ILE A 126 ? 0.52790 0.78875 0.93311 0.09706  0.00412  -0.04092 160 ILE A O   
998  C CB  . ILE A 126 ? 0.46160 0.79131 0.87226 0.08929  0.03365  -0.05704 160 ILE A CB  
999  C CG1 . ILE A 126 ? 0.49704 0.83986 0.96367 0.10446  0.02461  -0.04807 160 ILE A CG1 
1000 C CG2 . ILE A 126 ? 0.54036 0.89276 0.94781 0.08773  0.05631  -0.07158 160 ILE A CG2 
1001 C CD1 . ILE A 126 ? 0.31849 0.70180 0.81951 0.10196  0.02144  -0.03713 160 ILE A CD1 
1002 N N   . TYR A 127 ? 0.43852 0.69663 0.77364 0.07183  0.00999  -0.04443 161 TYR A N   
1003 C CA  . TYR A 127 ? 0.47787 0.71277 0.79972 0.06656  -0.00301 -0.03006 161 TYR A CA  
1004 C C   . TYR A 127 ? 0.51618 0.76252 0.84551 0.06314  -0.01733 -0.00828 161 TYR A C   
1005 O O   . TYR A 127 ? 0.56144 0.79471 0.90264 0.06793  -0.02831 0.00576  161 TYR A O   
1006 C CB  . TYR A 127 ? 0.44534 0.66620 0.72634 0.05315  -0.00036 -0.03309 161 TYR A CB  
1007 C CG  . TYR A 127 ? 0.38947 0.58601 0.65939 0.04837  -0.00819 -0.02169 161 TYR A CG  
1008 C CD1 . TYR A 127 ? 0.34193 0.51550 0.62470 0.05436  -0.00904 -0.02605 161 TYR A CD1 
1009 C CD2 . TYR A 127 ? 0.48520 0.68114 0.73242 0.03718  -0.01325 -0.00742 161 TYR A CD2 
1010 C CE1 . TYR A 127 ? 0.52107 0.67434 0.79765 0.04877  -0.01369 -0.01388 161 TYR A CE1 
1011 C CE2 . TYR A 127 ? 0.53749 0.71286 0.77417 0.03275  -0.01624 0.00309  161 TYR A CE2 
1012 C CZ  . TYR A 127 ? 0.49388 0.64929 0.74685 0.03827  -0.01592 0.00113  161 TYR A CZ  
1013 O OH  . TYR A 127 ? 0.39996 0.53693 0.64588 0.03257  -0.01653 0.01341  161 TYR A OH  
1014 N N   . ARG A 128 ? 0.38308 0.65232 0.70389 0.05380  -0.01852 -0.00463 162 ARG A N   
1015 C CA  . ARG A 128 ? 0.53903 0.82385 0.86632 0.04907  -0.03422 0.01277  162 ARG A CA  
1016 C C   . ARG A 128 ? 0.50295 0.76694 0.79683 0.03974  -0.04573 0.02773  162 ARG A C   
1017 O O   . ARG A 128 ? 0.64433 0.91649 0.93749 0.03625  -0.06161 0.04307  162 ARG A O   
1018 C CB  . ARG A 128 ? 0.37313 0.67347 0.74916 0.06383  -0.04329 0.02064  162 ARG A CB  
1019 C CG  . ARG A 128 ? 0.52295 0.84893 0.93833 0.07426  -0.02972 0.00623  162 ARG A CG  
1020 C CD  . ARG A 128 ? 0.64850 0.99588 1.11812 0.08769  -0.04157 0.01727  162 ARG A CD  
1021 N NE  . ARG A 128 ? 0.52822 0.85099 1.01231 0.10013  -0.05156 0.02710  162 ARG A NE  
1022 C CZ  . ARG A 128 ? 0.64816 0.97914 1.16897 0.10989  -0.06998 0.04551  162 ARG A CZ  
1023 N NH1 . ARG A 128 ? 0.61683 0.98227 1.16525 0.10855  -0.08274 0.05559  162 ARG A NH1 
1024 N NH2 . ARG A 128 ? 0.59164 0.89538 1.12389 0.12065  -0.07736 0.05540  162 ARG A NH2 
1025 N N   . ASP A 129 ? 0.65743 0.89590 0.92366 0.03531  -0.03823 0.02382  163 ASP A N   
1026 C CA  . ASP A 129 ? 0.69696 0.91657 0.93104 0.02628  -0.04380 0.03676  163 ASP A CA  
1027 C C   . ASP A 129 ? 0.58255 0.78854 0.78618 0.01657  -0.03191 0.02694  163 ASP A C   
1028 O O   . ASP A 129 ? 0.59491 0.77999 0.78356 0.01379  -0.02831 0.03144  163 ASP A O   
1029 C CB  . ASP A 129 ? 0.75931 0.95875 1.00453 0.03408  -0.04860 0.04972  163 ASP A CB  
1030 C CG  . ASP A 129 ? 0.88224 1.06966 1.09669 0.02571  -0.05680 0.06918  163 ASP A CG  
1031 O OD1 . ASP A 129 ? 0.71895 0.91681 0.90775 0.01592  -0.06309 0.07219  163 ASP A OD1 
1032 O OD2 . ASP A 129 ? 0.81219 0.97860 1.02657 0.02808  -0.05633 0.08113  163 ASP A OD2 
1033 N N   . ILE A 130 ? 0.44336 0.66171 0.64109 0.01141  -0.02532 0.01484  164 ILE A N   
1034 C CA  . ILE A 130 ? 0.41357 0.61976 0.58782 0.00390  -0.01555 0.00628  164 ILE A CA  
1035 C C   . ILE A 130 ? 0.50860 0.70216 0.65334 -0.00624 -0.01689 0.01407  164 ILE A C   
1036 O O   . ILE A 130 ? 0.37683 0.57816 0.50827 -0.01348 -0.02376 0.01880  164 ILE A O   
1037 C CB  . ILE A 130 ? 0.47214 0.69357 0.64512 -0.00023 -0.00946 -0.00411 164 ILE A CB  
1038 C CG1 . ILE A 130 ? 0.40968 0.63888 0.60317 0.00982  -0.00277 -0.01502 164 ILE A CG1 
1039 C CG2 . ILE A 130 ? 0.55741 0.76589 0.70500 -0.00928 -0.00317 -0.00832 164 ILE A CG2 
1040 C CD1 . ILE A 130 ? 0.40810 0.61769 0.59617 0.01377  0.00173  -0.02339 164 ILE A CD1 
1041 N N   . LYS A 131 ? 0.46558 0.63989 0.60107 -0.00710 -0.00993 0.01427  165 LYS A N   
1042 C CA  . LYS A 131 ? 0.52905 0.69005 0.63741 -0.01544 -0.00578 0.01945  165 LYS A CA  
1043 C C   . LYS A 131 ? 0.55465 0.70107 0.66642 -0.01509 0.00495  0.01496  165 LYS A C   
1044 O O   . LYS A 131 ? 0.51052 0.65370 0.64451 -0.00859 0.00507  0.01244  165 LYS A O   
1045 C CB  . LYS A 131 ? 0.55750 0.71273 0.65539 -0.01563 -0.01196 0.03508  165 LYS A CB  
1046 C CG  . LYS A 131 ? 0.54373 0.68767 0.66148 -0.00814 -0.01072 0.04384  165 LYS A CG  
1047 C CD  . LYS A 131 ? 0.61976 0.75450 0.72065 -0.01007 -0.01511 0.06305  165 LYS A CD  
1048 C CE  . LYS A 131 ? 0.68318 0.83127 0.78935 -0.00626 -0.03279 0.07280  165 LYS A CE  
1049 N NZ  . LYS A 131 ? 0.79787 0.93509 0.88562 -0.00757 -0.03973 0.09487  165 LYS A NZ  
1050 N N   . PRO A 132 ? 0.47267 0.61022 0.56616 -0.02179 0.01346  0.01276  166 PRO A N   
1051 C CA  . PRO A 132 ? 0.51223 0.63928 0.61695 -0.02094 0.02286  0.00952  166 PRO A CA  
1052 C C   . PRO A 132 ? 0.54646 0.66389 0.66375 -0.01873 0.02698  0.01915  166 PRO A C   
1053 O O   . PRO A 132 ? 0.48397 0.59624 0.62267 -0.01725 0.03130  0.01656  166 PRO A O   
1054 C CB  . PRO A 132 ? 0.52892 0.64911 0.61323 -0.02760 0.03220  0.00589  166 PRO A CB  
1055 C CG  . PRO A 132 ? 0.60238 0.72357 0.65819 -0.03307 0.02869  0.00987  166 PRO A CG  
1056 C CD  . PRO A 132 ? 0.50311 0.63944 0.56808 -0.03024 0.01458  0.01169  166 PRO A CD  
1057 N N   . ASP A 133 ? 0.50057 0.61547 0.60645 -0.01923 0.02449  0.03161  167 ASP A N   
1058 C CA  . ASP A 133 ? 0.45412 0.55790 0.57033 -0.01843 0.02927  0.04469  167 ASP A CA  
1059 C C   . ASP A 133 ? 0.52725 0.62924 0.67955 -0.01140 0.02231  0.04345  167 ASP A C   
1060 O O   . ASP A 133 ? 0.40037 0.49142 0.57172 -0.01190 0.02746  0.05077  167 ASP A O   
1061 C CB  . ASP A 133 ? 0.61868 0.71949 0.70906 -0.02065 0.02520  0.06081  167 ASP A CB  
1062 C CG  . ASP A 133 ? 0.55146 0.65284 0.60009 -0.02836 0.02895  0.05856  167 ASP A CG  
1063 O OD1 . ASP A 133 ? 0.69295 0.80462 0.73381 -0.02967 0.02091  0.04802  167 ASP A OD1 
1064 O OD2 . ASP A 133 ? 0.71199 0.80261 0.73522 -0.03378 0.04095  0.06665  167 ASP A OD2 
1065 N N   . ASN A 134 ? 0.54203 0.65380 0.70481 -0.00543 0.01203  0.03356  168 ASN A N   
1066 C CA  . ASN A 134 ? 0.44475 0.55307 0.63812 0.00217  0.00578  0.02848  168 ASN A CA  
1067 C C   . ASN A 134 ? 0.34952 0.45895 0.55516 0.00302  0.00580  0.01086  168 ASN A C   
1068 O O   . ASN A 134 ? 0.53759 0.64228 0.76459 0.00860  0.00061  0.00224  168 ASN A O   
1069 C CB  . ASN A 134 ? 0.40219 0.52079 0.60107 0.00985  -0.00386 0.02852  168 ASN A CB  
1070 C CG  . ASN A 134 ? 0.65053 0.76591 0.84465 0.01077  -0.00932 0.04855  168 ASN A CG  
1071 O OD1 . ASN A 134 ? 0.70106 0.80211 0.89132 0.00695  -0.00519 0.06297  168 ASN A OD1 
1072 N ND2 . ASN A 134 ? 0.42415 0.55383 0.61968 0.01554  -0.01892 0.05100  168 ASN A ND2 
1073 N N   . PHE A 135 ? 0.45373 0.56774 0.64544 -0.00216 0.01037  0.00508  169 PHE A N   
1074 C CA  . PHE A 135 ? 0.42852 0.54268 0.62928 -0.00220 0.00794  -0.00807 169 PHE A CA  
1075 C C   . PHE A 135 ? 0.46075 0.56642 0.67850 -0.00681 0.01289  -0.00404 169 PHE A C   
1076 O O   . PHE A 135 ? 0.36970 0.47564 0.57854 -0.01132 0.02234  0.00229  169 PHE A O   
1077 C CB  . PHE A 135 ? 0.54843 0.67283 0.72797 -0.00430 0.00826  -0.01464 169 PHE A CB  
1078 C CG  . PHE A 135 ? 0.42721 0.56305 0.59773 -0.00042 0.00458  -0.02060 169 PHE A CG  
1079 C CD1 . PHE A 135 ? 0.42342 0.56812 0.58347 -0.00122 0.00536  -0.01391 169 PHE A CD1 
1080 C CD2 . PHE A 135 ? 0.37548 0.51427 0.54825 0.00355  0.00057  -0.03324 169 PHE A CD2 
1081 C CE1 . PHE A 135 ? 0.50627 0.66526 0.66616 0.00216  0.00329  -0.01873 169 PHE A CE1 
1082 C CE2 . PHE A 135 ? 0.42975 0.58109 0.59642 0.00729  0.00142  -0.03885 169 PHE A CE2 
1083 C CZ  . PHE A 135 ? 0.43302 0.59584 0.59725 0.00674  0.00335  -0.03110 169 PHE A CZ  
1084 N N   . LEU A 136 ? 0.48707 0.58536 0.73175 -0.00586 0.00713  -0.00882 170 LEU A N   
1085 C CA  . LEU A 136 ? 0.49129 0.58353 0.76288 -0.01093 0.01118  -0.00375 170 LEU A CA  
1086 C C   . LEU A 136 ? 0.39023 0.48522 0.67745 -0.01204 0.00094  -0.01643 170 LEU A C   
1087 O O   . LEU A 136 ? 0.37420 0.46962 0.65417 -0.00872 -0.01090 -0.02986 170 LEU A O   
1088 C CB  . LEU A 136 ? 0.45405 0.53361 0.75109 -0.01138 0.01095  0.00379  170 LEU A CB  
1089 C CG  . LEU A 136 ? 0.47951 0.55292 0.76976 -0.01317 0.02210  0.02370  170 LEU A CG  
1090 C CD1 . LEU A 136 ? 0.42002 0.49984 0.67429 -0.00946 0.02225  0.02790  170 LEU A CD1 
1091 C CD2 . LEU A 136 ? 0.44946 0.50759 0.76785 -0.01241 0.01784  0.03008  170 LEU A CD2 
1092 N N   . ILE A 137 ? 0.39360 0.49110 0.70241 -0.01659 0.00553  -0.01195 171 ILE A N   
1093 C CA  . ILE A 137 ? 0.40623 0.50696 0.73757 -0.01822 -0.00797 -0.02137 171 ILE A CA  
1094 C C   . ILE A 137 ? 0.55845 0.65110 0.92842 -0.02220 -0.01484 -0.02298 171 ILE A C   
1095 O O   . ILE A 137 ? 0.48350 0.56677 0.86136 -0.02305 -0.00761 -0.01546 171 ILE A O   
1096 C CB  . ILE A 137 ? 0.38438 0.49402 0.72866 -0.01999 -0.00168 -0.01611 171 ILE A CB  
1097 C CG1 . ILE A 137 ? 0.46727 0.57691 0.83728 -0.02391 0.01762  -0.00308 171 ILE A CG1 
1098 C CG2 . ILE A 137 ? 0.49985 0.61345 0.80748 -0.01674 0.00295  -0.01633 171 ILE A CG2 
1099 C CD1 . ILE A 137 ? 0.47303 0.59228 0.86983 -0.02454 0.02509  0.00008  171 ILE A CD1 
1100 N N   . GLY A 138 ? 0.53449 0.62966 0.92962 -0.02528 -0.03061 -0.03196 172 GLY A N   
1101 C CA  . GLY A 138 ? 0.48424 0.57151 0.92058 -0.03111 -0.03987 -0.03546 172 GLY A CA  
1102 C C   . GLY A 138 ? 0.44919 0.54190 0.93090 -0.03789 -0.02671 -0.02046 172 GLY A C   
1103 O O   . GLY A 138 ? 0.44970 0.54997 0.92638 -0.03708 -0.00691 -0.00756 172 GLY A O   
1104 N N   . ARG A 139 ? 0.54887 0.63726 1.07645 -0.04532 -0.03706 -0.02336 173 ARG A N   
1105 C CA  . ARG A 139 ? 0.50767 0.60349 1.08823 -0.05339 -0.02470 -0.00943 173 ARG A CA  
1106 C C   . ARG A 139 ? 0.53478 0.64861 1.15172 -0.05610 -0.03820 -0.01398 173 ARG A C   
1107 O O   . ARG A 139 ? 0.68918 0.80498 1.29362 -0.05404 -0.06304 -0.02864 173 ARG A O   
1108 C CB  . ARG A 139 ? 0.56928 0.64975 1.18739 -0.06174 -0.02719 -0.00699 173 ARG A CB  
1109 C CG  . ARG A 139 ? 0.44631 0.50643 1.03206 -0.05736 -0.02082 -0.00388 173 ARG A CG  
1110 C CD  . ARG A 139 ? 0.67662 0.71859 1.30384 -0.06576 -0.02003 0.00327  173 ARG A CD  
1111 N NE  . ARG A 139 ? 0.76337 0.80726 1.40902 -0.07162 0.00643  0.02945  173 ARG A NE  
1112 C CZ  . ARG A 139 ? 0.66913 0.71797 1.37145 -0.08336 0.01408  0.04021  173 ARG A CZ  
1113 N NH1 . ARG A 139 ? 0.37436 0.42674 1.12234 -0.09017 -0.00577 0.02689  173 ARG A NH1 
1114 N NH2 . ARG A 139 ? 0.56826 0.61846 1.27810 -0.08821 0.04218  0.06504  173 ARG A NH2 
1115 N N   . ARG A 140 ? 0.55883 0.68649 1.22113 -0.06047 -0.02101 -0.00025 174 ARG A N   
1116 C CA  . ARG A 140 ? 0.68902 0.83374 1.38688 -0.06012 -0.03129 -0.00148 174 ARG A CA  
1117 C C   . ARG A 140 ? 0.63042 0.76926 1.35060 -0.06498 -0.06295 -0.01354 174 ARG A C   
1118 O O   . ARG A 140 ? 0.69011 0.81453 1.42394 -0.07168 -0.06857 -0.01700 174 ARG A O   
1119 C CB  . ARG A 140 ? 0.56155 0.71283 1.28846 -0.06014 -0.00295 0.01465  174 ARG A CB  
1120 C CG  . ARG A 140 ? 0.85374 1.01898 1.60585 -0.05496 -0.00781 0.01521  174 ARG A CG  
1121 C CD  . ARG A 140 ? 0.91301 1.08634 1.64467 -0.04662 0.01531  0.02032  174 ARG A CD  
1122 N NE  . ARG A 140 ? 1.11155 1.28011 1.82718 -0.04829 0.05013  0.03079  174 ARG A NE  
1123 C CZ  . ARG A 140 ? 1.05760 1.22910 1.74960 -0.04267 0.07603  0.03464  174 ARG A CZ  
1124 N NH1 . ARG A 140 ? 0.69745 0.87597 1.38448 -0.03432 0.07270  0.02927  174 ARG A NH1 
1125 N NH2 . ARG A 140 ? 1.03308 1.19835 1.70405 -0.04574 0.10545  0.04429  174 ARG A NH2 
1126 N N   . GLY A 141 ? 0.60685 0.75542 1.32940 -0.06158 -0.08462 -0.01971 175 GLY A N   
1127 C CA  . GLY A 141 ? 0.82298 0.96752 1.56148 -0.06622 -0.11665 -0.03113 175 GLY A CA  
1128 C C   . GLY A 141 ? 0.79343 0.92354 1.49673 -0.06889 -0.14173 -0.05101 175 GLY A C   
1129 O O   . GLY A 141 ? 0.79198 0.91739 1.49851 -0.07270 -0.17024 -0.06319 175 GLY A O   
1130 N N   . ALA A 142 ? 0.82688 0.94955 1.49607 -0.06695 -0.13204 -0.05583 176 ALA A N   
1131 C CA  . ALA A 142 ? 0.69346 0.79942 1.32368 -0.06730 -0.15166 -0.07688 176 ALA A CA  
1132 C C   . ALA A 142 ? 0.80378 0.91440 1.38119 -0.06031 -0.16873 -0.08557 176 ALA A C   
1133 O O   . ALA A 142 ? 0.78063 0.90624 1.35144 -0.05480 -0.16286 -0.07371 176 ALA A O   
1134 C CB  . ALA A 142 ? 0.66061 0.74882 1.25650 -0.06201 -0.12852 -0.07511 176 ALA A CB  
1135 N N   . THR A 143 ? 0.97926 1.07494 1.51810 -0.06071 -0.18901 -0.10668 177 THR A N   
1136 C CA  . THR A 143 ? 0.92756 1.02554 1.40949 -0.05530 -0.20426 -0.11442 177 THR A CA  
1137 C C   . THR A 143 ? 0.88157 0.98029 1.31359 -0.04485 -0.17884 -0.10565 177 THR A C   
1138 O O   . THR A 143 ? 1.01843 1.12632 1.42131 -0.04039 -0.18176 -0.09889 177 THR A O   
1139 C CB  . THR A 143 ? 1.08606 1.16631 1.53367 -0.05852 -0.22778 -0.14108 177 THR A CB  
1140 O OG1 . THR A 143 ? 1.18933 1.26425 1.68902 -0.06994 -0.24851 -0.15110 177 THR A OG1 
1141 C CG2 . THR A 143 ? 1.09641 1.18162 1.49343 -0.05662 -0.25016 -0.14683 177 THR A CG2 
1142 N N   . ASP A 144 ? 0.80615 0.89494 1.23027 -0.04139 -0.15541 -0.10458 178 ASP A N   
1143 C CA  . ASP A 144 ? 0.79250 0.88328 1.17682 -0.03292 -0.13193 -0.09590 178 ASP A CA  
1144 C C   . ASP A 144 ? 0.56811 0.66768 0.97947 -0.03221 -0.10816 -0.07493 178 ASP A C   
1145 O O   . ASP A 144 ? 0.72220 0.81778 1.11789 -0.02829 -0.08756 -0.06839 178 ASP A O   
1146 C CB  . ASP A 144 ? 0.74905 0.82480 1.10527 -0.02841 -0.12345 -0.10823 178 ASP A CB  
1147 C CG  . ASP A 144 ? 0.93906 1.00171 1.33577 -0.03177 -0.11762 -0.10814 178 ASP A CG  
1148 O OD1 . ASP A 144 ? 0.80328 0.86938 1.24872 -0.03895 -0.11809 -0.09784 178 ASP A OD1 
1149 O OD2 . ASP A 144 ? 1.09067 1.13945 1.47317 -0.02702 -0.11167 -0.11743 178 ASP A OD2 
1150 N N   . GLU A 145 ? 0.64998 0.76209 1.10210 -0.03578 -0.11079 -0.06455 179 GLU A N   
1151 C CA  . GLU A 145 ? 0.69190 0.81142 1.17163 -0.03565 -0.08567 -0.04705 179 GLU A CA  
1152 C C   . GLU A 145 ? 0.65904 0.78094 1.09732 -0.02860 -0.06721 -0.03935 179 GLU A C   
1153 O O   . GLU A 145 ? 0.69898 0.81848 1.13192 -0.02761 -0.04422 -0.03007 179 GLU A O   
1154 C CB  . GLU A 145 ? 0.65805 0.79289 1.19424 -0.03960 -0.09160 -0.03957 179 GLU A CB  
1155 C CG  . GLU A 145 ? 0.51975 0.66342 1.08433 -0.03888 -0.06232 -0.02327 179 GLU A CG  
1156 C CD  . GLU A 145 ? 0.60743 0.76918 1.23631 -0.04158 -0.06646 -0.01672 179 GLU A CD  
1157 O OE1 . GLU A 145 ? 0.79737 0.96484 1.45219 -0.04530 -0.09558 -0.02379 179 GLU A OE1 
1158 O OE2 . GLU A 145 ? 0.71588 0.88659 1.36960 -0.03988 -0.04070 -0.00511 179 GLU A OE2 
1159 N N   . ASN A 146 ? 0.71203 0.83747 1.11938 -0.02467 -0.07794 -0.04249 180 ASN A N   
1160 C CA  . ASN A 146 ? 0.55367 0.68045 0.92630 -0.01958 -0.06276 -0.03570 180 ASN A CA  
1161 C C   . ASN A 146 ? 0.64071 0.76143 0.96005 -0.01674 -0.06490 -0.04350 180 ASN A C   
1162 O O   . ASN A 146 ? 0.68587 0.80801 0.97589 -0.01401 -0.05655 -0.03893 180 ASN A O   
1163 C CB  . ASN A 146 ? 0.65849 0.79354 1.04321 -0.01728 -0.06942 -0.02914 180 ASN A CB  
1164 C CG  . ASN A 146 ? 0.62866 0.77292 1.07047 -0.01819 -0.06049 -0.02051 180 ASN A CG  
1165 O OD1 . ASN A 146 ? 0.54409 0.68789 0.99822 -0.01899 -0.03661 -0.01493 180 ASN A OD1 
1166 N ND2 . ASN A 146 ? 0.68295 0.83662 1.16036 -0.01812 -0.07951 -0.01875 180 ASN A ND2 
1167 N N   . ASN A 147 ? 0.65016 0.76400 0.95941 -0.01746 -0.07467 -0.05583 181 ASN A N   
1168 C CA  . ASN A 147 ? 0.59324 0.70339 0.85809 -0.01382 -0.07216 -0.06399 181 ASN A CA  
1169 C C   . ASN A 147 ? 0.64247 0.75032 0.90346 -0.01136 -0.05281 -0.05898 181 ASN A C   
1170 O O   . ASN A 147 ? 0.53829 0.64237 0.82751 -0.01309 -0.04518 -0.05278 181 ASN A O   
1171 C CB  . ASN A 147 ? 0.65822 0.76060 0.91309 -0.01430 -0.08885 -0.08203 181 ASN A CB  
1172 C CG  . ASN A 147 ? 0.72432 0.82883 0.96833 -0.01700 -0.11136 -0.08731 181 ASN A CG  
1173 O OD1 . ASN A 147 ? 0.78389 0.89564 1.01784 -0.01663 -0.11349 -0.07666 181 ASN A OD1 
1174 N ND2 . ASN A 147 ? 0.65595 0.75242 0.90098 -0.01988 -0.12975 -0.10373 181 ASN A ND2 
1175 N N   . VAL A 148 ? 0.67147 0.78236 0.89811 -0.00790 -0.04558 -0.06016 182 VAL A N   
1176 C CA  . VAL A 148 ? 0.49610 0.60763 0.71727 -0.00545 -0.03080 -0.05414 182 VAL A CA  
1177 C C   . VAL A 148 ? 0.60894 0.71380 0.83401 -0.00128 -0.03294 -0.06421 182 VAL A C   
1178 O O   . VAL A 148 ? 0.49596 0.59846 0.70848 0.00107  -0.04118 -0.07913 182 VAL A O   
1179 C CB  . VAL A 148 ? 0.55442 0.67459 0.74468 -0.00470 -0.02306 -0.05010 182 VAL A CB  
1180 C CG1 . VAL A 148 ? 0.37358 0.49627 0.56058 -0.00321 -0.01164 -0.04314 182 VAL A CG1 
1181 C CG2 . VAL A 148 ? 0.57484 0.69719 0.76368 -0.00813 -0.02183 -0.04187 182 VAL A CG2 
1182 N N   . HIS A 149 ? 0.57678 0.67700 0.81816 -0.00005 -0.02515 -0.05594 183 HIS A N   
1183 C CA  . HIS A 149 ? 0.45440 0.54603 0.70627 0.00530  -0.02616 -0.06229 183 HIS A CA  
1184 C C   . HIS A 149 ? 0.56695 0.66463 0.81033 0.00961  -0.01659 -0.05158 183 HIS A C   
1185 O O   . HIS A 149 ? 0.51693 0.62226 0.74829 0.00637  -0.00970 -0.03884 183 HIS A O   
1186 C CB  . HIS A 149 ? 0.52523 0.60211 0.81310 0.00217  -0.02970 -0.05940 183 HIS A CB  
1187 C CG  . HIS A 149 ? 0.43672 0.50912 0.74059 -0.00347 -0.04226 -0.06965 183 HIS A CG  
1188 N ND1 . HIS A 149 ? 0.49680 0.57716 0.80885 -0.00955 -0.04354 -0.06242 183 HIS A ND1 
1189 C CD2 . HIS A 149 ? 0.58331 0.64413 0.89856 -0.00401 -0.05568 -0.08731 183 HIS A CD2 
1190 C CE1 . HIS A 149 ? 0.45031 0.52664 0.78049 -0.01380 -0.05905 -0.07329 183 HIS A CE1 
1191 N NE2 . HIS A 149 ? 0.61219 0.67580 0.94191 -0.01137 -0.06728 -0.08928 183 HIS A NE2 
1192 N N   . LEU A 150 ? 0.42985 0.52356 0.68108 0.01718  -0.01727 -0.05775 184 LEU A N   
1193 C CA  . LEU A 150 ? 0.48265 0.58358 0.73271 0.02239  -0.01206 -0.04716 184 LEU A CA  
1194 C C   . LEU A 150 ? 0.50862 0.59431 0.78741 0.02767  -0.01436 -0.04183 184 LEU A C   
1195 O O   . LEU A 150 ? 0.45939 0.53255 0.75527 0.03247  -0.01859 -0.05642 184 LEU A O   
1196 C CB  . LEU A 150 ? 0.58714 0.70330 0.82273 0.02854  -0.00932 -0.05814 184 LEU A CB  
1197 C CG  . LEU A 150 ? 0.65361 0.78331 0.89182 0.03298  -0.00618 -0.04677 184 LEU A CG  
1198 C CD1 . LEU A 150 ? 0.44510 0.58091 0.66734 0.02449  -0.00496 -0.02957 184 LEU A CD1 
1199 C CD2 . LEU A 150 ? 0.55228 0.70001 0.78339 0.03822  -0.00112 -0.05838 184 LEU A CD2 
1200 N N   . ILE A 151 ? 0.44109 0.52571 0.72311 0.02645  -0.01209 -0.02093 185 ILE A N   
1201 C CA  . ILE A 151 ? 0.52184 0.59041 0.82983 0.03068  -0.01467 -0.00932 185 ILE A CA  
1202 C C   . ILE A 151 ? 0.56777 0.64616 0.87026 0.03599  -0.01592 0.00689  185 ILE A C   
1203 O O   . ILE A 151 ? 0.52659 0.62429 0.80722 0.03506  -0.01483 0.00713  185 ILE A O   
1204 C CB  . ILE A 151 ? 0.45811 0.51156 0.77742 0.02141  -0.01187 0.00521  185 ILE A CB  
1205 C CG1 . ILE A 151 ? 0.46813 0.53237 0.76063 0.01258  -0.00387 0.01826  185 ILE A CG1 
1206 C CG2 . ILE A 151 ? 0.60585 0.64846 0.94452 0.01721  -0.01523 -0.01096 185 ILE A CG2 
1207 C CD1 . ILE A 151 ? 0.56563 0.62951 0.84382 0.01175  -0.00113 0.04175  185 ILE A CD1 
1208 N N   . ASP A 152 ? 0.47703 0.54112 0.80179 0.04095  -0.01998 0.02159  186 ASP A N   
1209 C CA  . ASP A 152 ? 0.63669 0.70787 0.96030 0.04628  -0.02552 0.04094  186 ASP A CA  
1210 C C   . ASP A 152 ? 0.58236 0.67410 0.91309 0.05680  -0.02868 0.02888  186 ASP A C   
1211 O O   . ASP A 152 ? 0.50951 0.62303 0.81767 0.05299  -0.02728 0.02572  186 ASP A O   
1212 C CB  . ASP A 152 ? 0.60630 0.68550 0.89428 0.03564  -0.02338 0.05905  186 ASP A CB  
1213 C CG  . ASP A 152 ? 0.67102 0.75432 0.95391 0.03910  -0.03300 0.08199  186 ASP A CG  
1214 O OD1 . ASP A 152 ? 0.67972 0.75840 0.99297 0.05044  -0.04147 0.08749  186 ASP A OD1 
1215 O OD2 . ASP A 152 ? 0.93258 1.02288 1.18102 0.03069  -0.03308 0.09416  186 ASP A OD2 
1216 N N   . PHE A 153 ? 0.62177 0.70653 0.98723 0.06998  -0.03177 0.02217  187 PHE A N   
1217 C CA  . PHE A 153 ? 0.52839 0.63396 0.90936 0.08174  -0.03173 0.01070  187 PHE A CA  
1218 C C   . PHE A 153 ? 0.45609 0.56549 0.86547 0.09264  -0.04225 0.03072  187 PHE A C   
1219 O O   . PHE A 153 ? 0.61786 0.73356 1.06202 0.10735  -0.04207 0.02138  187 PHE A O   
1220 C CB  . PHE A 153 ? 0.49795 0.59548 0.89679 0.09033  -0.02440 -0.01832 187 PHE A CB  
1221 C CG  . PHE A 153 ? 0.53715 0.63622 0.90568 0.08059  -0.01722 -0.03811 187 PHE A CG  
1222 C CD1 . PHE A 153 ? 0.51257 0.59045 0.87379 0.07124  -0.01871 -0.04030 187 PHE A CD1 
1223 C CD2 . PHE A 153 ? 0.49451 0.61698 0.84445 0.08036  -0.00973 -0.05250 187 PHE A CD2 
1224 C CE1 . PHE A 153 ? 0.61268 0.69301 0.94896 0.06297  -0.01560 -0.05645 187 PHE A CE1 
1225 C CE2 . PHE A 153 ? 0.60783 0.73019 0.92831 0.07166  -0.00530 -0.06740 187 PHE A CE2 
1226 C CZ  . PHE A 153 ? 0.47936 0.58080 0.79316 0.06351  -0.00963 -0.06936 187 PHE A CZ  
1227 N N   . GLY A 154 ? 0.61906 0.72489 1.01368 0.08599  -0.05145 0.05860  188 GLY A N   
1228 C CA  . GLY A 154 ? 0.69567 0.80624 1.11272 0.09527  -0.06563 0.08143  188 GLY A CA  
1229 C C   . GLY A 154 ? 0.63390 0.77969 1.05698 0.09953  -0.07159 0.07991  188 GLY A C   
1230 O O   . GLY A 154 ? 0.58261 0.73735 1.03810 0.11100  -0.08436 0.09408  188 GLY A O   
1231 N N   . MET A 155 ? 0.62628 0.79242 1.02281 0.09026  -0.06349 0.06443  189 MET A N   
1232 C CA  . MET A 155 ? 0.55470 0.75565 0.96036 0.09182  -0.06687 0.06084  189 MET A CA  
1233 C C   . MET A 155 ? 0.54228 0.75814 0.97136 0.10029  -0.05153 0.03374  189 MET A C   
1234 O O   . MET A 155 ? 0.57593 0.82275 1.01661 0.10078  -0.05015 0.02910  189 MET A O   
1235 C CB  . MET A 155 ? 0.69790 0.91083 1.05757 0.07407  -0.06860 0.06447  189 MET A CB  
1236 C CG  . MET A 155 ? 0.63288 0.83449 0.96232 0.06511  -0.08263 0.08978  189 MET A CG  
1237 S SD  . MET A 155 ? 0.98994 1.21032 1.34572 0.07281  -0.10849 0.11456  189 MET A SD  
1238 C CE  . MET A 155 ? 0.95358 1.19037 1.25939 0.05339  -0.11898 0.11980  189 MET A CE  
1239 N N   . ALA A 156 ? 0.49389 0.68855 0.92886 0.10586  -0.03974 0.01557  190 ALA A N   
1240 C CA  . ALA A 156 ? 0.50759 0.71337 0.95512 0.11327  -0.02355 -0.01181 190 ALA A CA  
1241 C C   . ALA A 156 ? 0.55204 0.77724 1.05247 0.13126  -0.02288 -0.01376 190 ALA A C   
1242 O O   . ALA A 156 ? 0.58935 0.80381 1.12534 0.14307  -0.03369 -0.00036 190 ALA A O   
1243 C CB  . ALA A 156 ? 0.56814 0.74353 1.00861 0.11505  -0.01482 -0.03145 190 ALA A CB  
1244 N N   . LYS A 157 ? 0.46039 0.71464 0.96875 0.13355  -0.00921 -0.02933 191 LYS A N   
1245 C CA  . LYS A 157 ? 0.48983 0.76985 1.05328 0.15033  -0.00490 -0.03247 191 LYS A CA  
1246 C C   . LYS A 157 ? 0.46613 0.75684 1.03162 0.15639  0.02119  -0.06266 191 LYS A C   
1247 O O   . LYS A 157 ? 0.64352 0.93793 1.16580 0.14333  0.03236  -0.07370 191 LYS A O   
1248 C CB  . LYS A 157 ? 0.51751 0.83458 1.09624 0.14471  -0.01732 -0.01257 191 LYS A CB  
1249 C CG  . LYS A 157 ? 0.45054 0.79899 1.09680 0.16233  -0.01581 -0.01194 191 LYS A CG  
1250 C CD  . LYS A 157 ? 0.45757 0.83894 1.12163 0.15535  -0.03661 0.01198  191 LYS A CD  
1251 C CE  . LYS A 157 ? 0.51213 0.91584 1.23555 0.17177  -0.04009 0.01723  191 LYS A CE  
1252 N NZ  . LYS A 157 ? 0.86564 1.29254 1.59918 0.16409  -0.06768 0.04295  191 LYS A NZ  
1253 N N   . GLN A 158 ? 0.57173 0.86602 1.18648 0.17667  0.03139  -0.07558 192 GLN A N   
1254 C CA  . GLN A 158 ? 0.44802 0.75454 1.06611 0.18433  0.05933  -0.10522 192 GLN A CA  
1255 C C   . GLN A 158 ? 0.52062 0.87528 1.15570 0.18047  0.06951  -0.10063 192 GLN A C   
1256 O O   . GLN A 158 ? 0.54139 0.91838 1.21842 0.18666  0.06053  -0.08363 192 GLN A O   
1257 C CB  . GLN A 158 ? 0.53420 0.82324 1.19219 0.20588  0.06788  -0.12016 192 GLN A CB  
1258 C CG  . GLN A 158 ? 0.72044 1.01568 1.36873 0.21261  0.09799  -0.15007 192 GLN A CG  
1259 C CD  . GLN A 158 ? 0.90977 1.17928 1.58497 0.23101  0.10509  -0.16456 192 GLN A CD  
1260 O OE1 . GLN A 158 ? 0.89479 1.17884 1.58438 0.24113  0.12600  -0.17816 192 GLN A OE1 
1261 N NE2 . GLN A 158 ? 0.95427 1.18479 1.63727 0.23489  0.08854  -0.16130 192 GLN A NE2 
1262 N N   . TYR A 159 ? 0.51089 0.87568 1.10169 0.16678  0.08585  -0.11186 193 TYR A N   
1263 C CA  . TYR A 159 ? 0.51625 0.92476 1.12041 0.15957  0.09712  -0.10664 193 TYR A CA  
1264 C C   . TYR A 159 ? 0.46345 0.88740 1.07609 0.16888  0.12915  -0.12770 193 TYR A C   
1265 O O   . TYR A 159 ? 0.48011 0.93825 1.10431 0.16274  0.14059  -0.12093 193 TYR A O   
1266 C CB  . TYR A 159 ? 0.44245 0.85001 0.98742 0.13519  0.09314  -0.09830 193 TYR A CB  
1267 C CG  . TYR A 159 ? 0.46406 0.85598 0.95407 0.12884  0.11342  -0.11894 193 TYR A CG  
1268 C CD1 . TYR A 159 ? 0.49868 0.85017 0.94625 0.12736  0.10696  -0.12890 193 TYR A CD1 
1269 C CD2 . TYR A 159 ? 0.35394 0.77221 0.83491 0.12339  0.13802  -0.12688 193 TYR A CD2 
1270 C CE1 . TYR A 159 ? 0.45049 0.78829 0.84660 0.12119  0.12126  -0.14674 193 TYR A CE1 
1271 C CE2 . TYR A 159 ? 0.47722 0.88024 0.90249 0.11727  0.15462  -0.14334 193 TYR A CE2 
1272 C CZ  . TYR A 159 ? 0.63284 0.99563 1.01497 0.11644  0.14450  -0.15343 193 TYR A CZ  
1273 O OH  . TYR A 159 ? 0.60009 0.94823 0.92552 0.10998  0.15693  -0.16888 193 TYR A OH  
1274 N N   . ARG A 160 ? 0.53362 0.92935 1.13404 0.18151  0.14311  -0.15143 194 ARG A N   
1275 C CA  . ARG A 160 ? 0.58329 0.98716 1.18149 0.19028  0.17351  -0.17077 194 ARG A CA  
1276 C C   . ARG A 160 ? 0.63398 1.00152 1.23696 0.20793  0.17808  -0.19210 194 ARG A C   
1277 O O   . ARG A 160 ? 0.89563 1.22797 1.48462 0.20840  0.16263  -0.19785 194 ARG A O   
1278 C CB  . ARG A 160 ? 0.47439 0.88407 1.01550 0.17635  0.19546  -0.18459 194 ARG A CB  
1279 C CG  . ARG A 160 ? 0.60729 0.98001 1.09292 0.17286  0.19486  -0.20682 194 ARG A CG  
1280 C CD  . ARG A 160 ? 0.61785 0.99859 1.04283 0.15718  0.21205  -0.21494 194 ARG A CD  
1281 N NE  . ARG A 160 ? 0.71833 1.05984 1.08236 0.15351  0.20812  -0.23462 194 ARG A NE  
1282 C CZ  . ARG A 160 ? 0.85804 1.19198 1.15551 0.13756  0.21090  -0.23581 194 ARG A CZ  
1283 N NH1 . ARG A 160 ? 0.83807 1.19901 1.12042 0.12352  0.21963  -0.21877 194 ARG A NH1 
1284 N NH2 . ARG A 160 ? 0.83062 1.12840 1.07779 0.13520  0.20301  -0.25356 194 ARG A NH2 
1285 N N   . ASP A 161 ? 0.82838 1.20453 1.45309 0.22195  0.19960  -0.20385 195 ASP A N   
1286 C CA  . ASP A 161 ? 0.90176 1.24316 1.53323 0.23887  0.20552  -0.22585 195 ASP A CA  
1287 C C   . ASP A 161 ? 0.92031 1.22839 1.48759 0.23321  0.21647  -0.25521 195 ASP A C   
1288 O O   . ASP A 161 ? 0.87606 1.19645 1.39685 0.22288  0.23510  -0.26466 195 ASP A O   
1289 C CB  . ASP A 161 ? 0.91521 1.27616 1.58286 0.25523  0.22874  -0.23358 195 ASP A CB  
1290 C CG  . ASP A 161 ? 1.00710 1.33130 1.68680 0.27346  0.23428  -0.25632 195 ASP A CG  
1291 O OD1 . ASP A 161 ? 1.03538 1.34639 1.76143 0.28395  0.21454  -0.24449 195 ASP A OD1 
1292 O OD2 . ASP A 161 ? 1.05947 1.36620 1.69979 0.27657  0.25760  -0.28555 195 ASP A OD2 
1293 N N   . PRO A 162 ? 0.90507 1.16998 1.46709 0.23855  0.20368  -0.26895 196 PRO A N   
1294 C CA  . PRO A 162 ? 0.99552 1.22802 1.49539 0.23123  0.20861  -0.29720 196 PRO A CA  
1295 C C   . PRO A 162 ? 1.05459 1.28197 1.52135 0.23784  0.23866  -0.32632 196 PRO A C   
1296 O O   . PRO A 162 ? 1.11817 1.32920 1.52087 0.22801  0.24500  -0.34659 196 PRO A O   
1297 C CB  . PRO A 162 ? 1.05185 1.24053 1.56877 0.23610  0.18571  -0.30155 196 PRO A CB  
1298 C CG  . PRO A 162 ? 0.99985 1.20098 1.57613 0.24069  0.16519  -0.26810 196 PRO A CG  
1299 C CD  . PRO A 162 ? 0.95136 1.19446 1.56143 0.24846  0.18038  -0.25591 196 PRO A CD  
1300 N N   . ARG A 163 ? 1.01774 1.25873 1.52375 0.25414  0.25664  -0.32863 197 ARG A N   
1301 C CA  . ARG A 163 ? 1.02145 1.25570 1.49760 0.26277  0.28700  -0.35707 197 ARG A CA  
1302 C C   . ARG A 163 ? 1.07460 1.35056 1.53166 0.25766  0.31414  -0.35065 197 ARG A C   
1303 O O   . ARG A 163 ? 1.15050 1.42011 1.54175 0.24989  0.33196  -0.36750 197 ARG A O   
1304 C CB  . ARG A 163 ? 1.04224 1.26502 1.57279 0.28517  0.29345  -0.36629 197 ARG A CB  
1305 C CG  . ARG A 163 ? 1.08863 1.26511 1.63675 0.29017  0.26949  -0.37381 197 ARG A CG  
1306 C CD  . ARG A 163 ? 1.31482 1.44933 1.82335 0.29607  0.28217  -0.41237 197 ARG A CD  
1307 N NE  . ARG A 163 ? 1.47997 1.60658 1.90639 0.28095  0.29089  -0.43108 197 ARG A NE  
1308 C CZ  . ARG A 163 ? 1.54938 1.64106 1.92370 0.28170  0.30043  -0.46485 197 ARG A CZ  
1309 N NH1 . ARG A 163 ? 1.32667 1.38666 1.72289 0.29688  0.30437  -0.48622 197 ARG A NH1 
1310 N NH2 . ARG A 163 ? 1.49893 1.58618 1.79550 0.26645  0.30482  -0.47706 197 ARG A NH2 
1311 N N   . THR A 164 ? 1.02800 1.34606 1.54087 0.26101  0.31627  -0.32514 198 THR A N   
1312 C CA  . THR A 164 ? 0.78772 1.14770 1.29424 0.25648  0.34239  -0.31672 198 THR A CA  
1313 C C   . THR A 164 ? 0.99531 1.37880 1.47832 0.23415  0.33325  -0.29344 198 THR A C   
1314 O O   . THR A 164 ? 1.06874 1.48055 1.53189 0.22603  0.35524  -0.28719 198 THR A O   
1315 C CB  . THR A 164 ? 0.93890 1.33463 1.52316 0.27206  0.35026  -0.30354 198 THR A CB  
1316 O OG1 . THR A 164 ? 1.12800 1.56986 1.71580 0.26410  0.37025  -0.28902 198 THR A OG1 
1317 C CG2 . THR A 164 ? 0.78486 1.18533 1.43061 0.27428  0.31627  -0.27878 198 THR A CG2 
1318 N N   . LYS A 165 ? 1.02964 1.40096 1.51380 0.22399  0.30239  -0.28051 199 LYS A N   
1319 C CA  . LYS A 165 ? 0.90601 1.29777 1.37225 0.20326  0.29105  -0.25857 199 LYS A CA  
1320 C C   . LYS A 165 ? 1.04404 1.48361 1.56106 0.20051  0.29489  -0.23207 199 LYS A C   
1321 O O   . LYS A 165 ? 1.13787 1.60228 1.63446 0.18551  0.30627  -0.22050 199 LYS A O   
1322 C CB  . LYS A 165 ? 0.80736 1.19014 1.19416 0.18808  0.30573  -0.27016 199 LYS A CB  
1323 C CG  . LYS A 165 ? 0.93314 1.27061 1.26579 0.18938  0.30034  -0.29797 199 LYS A CG  
1324 C CD  . LYS A 165 ? 1.02782 1.34175 1.37913 0.18897  0.26726  -0.29526 199 LYS A CD  
1325 C CE  . LYS A 165 ? 0.95001 1.22582 1.23814 0.18176  0.25734  -0.31765 199 LYS A CE  
1326 N NZ  . LYS A 165 ? 0.83604 1.08858 1.14437 0.18124  0.22641  -0.31478 199 LYS A NZ  
1327 N N   . GLN A 166 ? 1.02852 1.48005 1.61280 0.21442  0.28351  -0.22170 200 GLN A N   
1328 C CA  . GLN A 166 ? 0.78599 1.28281 1.42532 0.21226  0.28003  -0.19673 200 GLN A CA  
1329 C C   . GLN A 166 ? 0.73632 1.23693 1.39224 0.20039  0.24456  -0.17204 200 GLN A C   
1330 O O   . GLN A 166 ? 0.72238 1.20182 1.39988 0.20857  0.22022  -0.16791 200 GLN A O   
1331 C CB  . GLN A 166 ? 0.82642 1.33620 1.52863 0.23400  0.28567  -0.19917 200 GLN A CB  
1332 C CG  . GLN A 166 ? 0.69096 1.25272 1.44743 0.23227  0.28928  -0.17934 200 GLN A CG  
1333 C CD  . GLN A 166 ? 1.09498 1.68341 1.83402 0.22856  0.32653  -0.18718 200 GLN A CD  
1334 O OE1 . GLN A 166 ? 1.10679 1.67324 1.79462 0.23167  0.35177  -0.20955 200 GLN A OE1 
1335 N NE2 . GLN A 166 ? 0.85489 1.49031 1.63414 0.22080  0.32926  -0.16849 200 GLN A NE2 
1336 N N   . HIS A 167 ? 0.46071 0.98601 1.10426 0.18064  0.24198  -0.15537 201 HIS A N   
1337 C CA  . HIS A 167 ? 0.41411 0.94262 1.06609 0.16754  0.20963  -0.13366 201 HIS A CA  
1338 C C   . HIS A 167 ? 0.47267 1.01793 1.18819 0.17710  0.18582  -0.11568 201 HIS A C   
1339 O O   . HIS A 167 ? 0.53213 1.10242 1.29240 0.18820  0.19559  -0.11455 201 HIS A O   
1340 C CB  . HIS A 167 ? 0.52315 1.07702 1.15605 0.14457  0.21359  -0.11994 201 HIS A CB  
1341 C CG  . HIS A 167 ? 0.49853 1.04168 1.10947 0.12800  0.18698  -0.10774 201 HIS A CG  
1342 N ND1 . HIS A 167 ? 0.44383 0.99634 1.08878 0.12474  0.15567  -0.08774 201 HIS A ND1 
1343 C CD2 . HIS A 167 ? 0.34127 0.86562 0.89724 0.11383  0.18659  -0.11335 201 HIS A CD2 
1344 C CE1 . HIS A 167 ? 0.32218 0.86139 0.93476 0.10956  0.13898  -0.08231 201 HIS A CE1 
1345 N NE2 . HIS A 167 ? 0.40038 0.92246 0.95925 0.10286  0.15681  -0.09720 201 HIS A NE2 
1346 N N   . ILE A 168 ? 0.37665 0.90756 1.09407 0.17267  0.15373  -0.10138 202 ILE A N   
1347 C CA  . ILE A 168 ? 0.42212 0.96478 1.18915 0.17904  0.12555  -0.08113 202 ILE A CA  
1348 C C   . ILE A 168 ? 0.42696 1.01499 1.22298 0.16675  0.12095  -0.06469 202 ILE A C   
1349 O O   . ILE A 168 ? 0.52896 1.13062 1.29892 0.14754  0.12726  -0.06180 202 ILE A O   
1350 C CB  . ILE A 168 ? 0.34807 0.86368 1.09975 0.17424  0.09306  -0.06760 202 ILE A CB  
1351 C CG1 . ILE A 168 ? 0.34814 0.86329 1.05572 0.15181  0.08746  -0.06313 202 ILE A CG1 
1352 C CG2 . ILE A 168 ? 0.41861 0.89059 1.15948 0.18914  0.09348  -0.08096 202 ILE A CG2 
1353 C CD1 . ILE A 168 ? 0.46892 0.96278 1.16322 0.14569  0.05540  -0.04709 202 ILE A CD1 
1354 N N   . PRO A 169 ? 0.43570 1.04707 1.28636 0.17638  0.10953  -0.05414 203 PRO A N   
1355 C CA  . PRO A 169 ? 0.44470 1.09991 1.32643 0.16356  0.10298  -0.04029 203 PRO A CA  
1356 C C   . PRO A 169 ? 0.45730 1.11326 1.31842 0.14227  0.07228  -0.02289 203 PRO A C   
1357 O O   . PRO A 169 ? 0.42298 1.05104 1.26373 0.14227  0.04791  -0.01519 203 PRO A O   
1358 C CB  . PRO A 169 ? 0.39168 1.06397 1.33651 0.18110  0.09164  -0.03336 203 PRO A CB  
1359 C CG  . PRO A 169 ? 0.41777 1.05976 1.36476 0.20428  0.10747  -0.04959 203 PRO A CG  
1360 C CD  . PRO A 169 ? 0.40122 0.99987 1.29040 0.19967  0.10449  -0.05637 203 PRO A CD  
1361 N N   . TYR A 170 ? 0.47126 1.15817 1.33674 0.12330  0.07459  -0.01716 204 TYR A N   
1362 C CA  . TYR A 170 ? 0.36402 1.05321 1.21250 0.10157  0.04584  -0.00291 204 TYR A CA  
1363 C C   . TYR A 170 ? 0.36114 1.06652 1.25063 0.10367  0.01180  0.01288  204 TYR A C   
1364 O O   . TYR A 170 ? 0.50015 1.23712 1.44054 0.10996  0.01530  0.01457  204 TYR A O   
1365 C CB  . TYR A 170 ? 0.29839 1.01056 1.13656 0.07920  0.06134  -0.00381 204 TYR A CB  
1366 C CG  . TYR A 170 ? 0.29673 1.01144 1.12120 0.05527  0.03265  0.00808  204 TYR A CG  
1367 C CD1 . TYR A 170 ? 0.53664 1.22166 1.31005 0.04296  0.02363  0.00887  204 TYR A CD1 
1368 C CD2 . TYR A 170 ? 0.41281 1.15830 1.27582 0.04471  0.01469  0.01706  204 TYR A CD2 
1369 C CE1 . TYR A 170 ? 0.48406 1.16763 1.24233 0.02122  -0.00176 0.01776  204 TYR A CE1 
1370 C CE2 . TYR A 170 ? 0.35308 1.09633 1.19997 0.02230  -0.01205 0.02500  204 TYR A CE2 
1371 C CZ  . TYR A 170 ? 0.31924 1.03022 1.11222 0.01080  -0.01972 0.02489  204 TYR A CZ  
1372 O OH  . TYR A 170 ? 0.51241 1.21725 1.28623 -0.01122 -0.04550 0.03111  204 TYR A OH  
1373 N N   . ARG A 171 ? 0.35141 1.03475 1.21769 0.09869  -0.02102 0.02498  205 ARG A N   
1374 C CA  . ARG A 171 ? 0.53107 1.22553 1.42352 0.09763  -0.05722 0.04193  205 ARG A CA  
1375 C C   . ARG A 171 ? 0.31305 0.99422 1.16196 0.07570  -0.08522 0.05164  205 ARG A C   
1376 O O   . ARG A 171 ? 0.50600 1.16922 1.31009 0.06322  -0.07576 0.04556  205 ARG A O   
1377 C CB  . ARG A 171 ? 0.47426 1.14954 1.38535 0.12079  -0.07082 0.04962  205 ARG A CB  
1378 C CG  . ARG A 171 ? 0.51151 1.14246 1.37604 0.12469  -0.07805 0.05203  205 ARG A CG  
1379 C CD  . ARG A 171 ? 0.78111 1.39311 1.66327 0.14201  -0.10098 0.06686  205 ARG A CD  
1380 N NE  . ARG A 171 ? 0.88843 1.49995 1.75731 0.13096  -0.14030 0.08850  205 ARG A NE  
1381 C CZ  . ARG A 171 ? 0.93019 1.52370 1.80353 0.14123  -0.16596 0.10695  205 ARG A CZ  
1382 N NH1 . ARG A 171 ? 0.98059 1.55418 1.87673 0.16279  -0.15742 0.10680  205 ARG A NH1 
1383 N NH2 . ARG A 171 ? 0.90785 1.50113 1.75967 0.12889  -0.20103 0.12600  205 ARG A NH2 
1384 N N   . GLU A 172 ? 0.49436 1.18374 1.35545 0.07089  -0.12017 0.06661  206 GLU A N   
1385 C CA  . GLU A 172 ? 0.39491 1.07116 1.21257 0.05010  -0.14946 0.07543  206 GLU A CA  
1386 C C   . GLU A 172 ? 0.62602 1.28734 1.43757 0.05800  -0.18532 0.09394  206 GLU A C   
1387 O O   . GLU A 172 ? 0.63893 1.29493 1.47734 0.07947  -0.18569 0.10011  206 GLU A O   
1388 C CB  . GLU A 172 ? 0.55959 1.26470 1.39121 0.02814  -0.15549 0.07274  206 GLU A CB  
1389 C CG  . GLU A 172 ? 0.61039 1.32984 1.44863 0.01978  -0.11887 0.05774  206 GLU A CG  
1390 C CD  . GLU A 172 ? 0.70839 1.44939 1.55533 -0.00490 -0.12430 0.05574  206 GLU A CD  
1391 O OE1 . GLU A 172 ? 0.85932 1.60198 1.70207 -0.01697 -0.15811 0.06354  206 GLU A OE1 
1392 O OE2 . GLU A 172 ? 0.78342 1.53757 1.63849 -0.01302 -0.09459 0.04637  206 GLU A OE2 
1393 N N   . LYS A 173 ? 0.60077 1.25329 1.37393 0.03982  -0.21538 0.10288  207 LYS A N   
1394 C CA  . LYS A 173 ? 0.69003 1.32718 1.44462 0.04313  -0.25164 0.12231  207 LYS A CA  
1395 C C   . LYS A 173 ? 0.73427 1.33650 1.46534 0.05956  -0.24839 0.13092  207 LYS A C   
1396 O O   . LYS A 173 ? 0.84299 1.43888 1.59449 0.07610  -0.26181 0.14520  207 LYS A O   
1397 C CB  . LYS A 173 ? 0.61288 1.27945 1.42419 0.05212  -0.27023 0.13192  207 LYS A CB  
1398 C CG  . LYS A 173 ? 0.44398 1.14433 1.27832 0.03373  -0.27993 0.12628  207 LYS A CG  
1399 C CD  . LYS A 173 ? 0.56350 1.28744 1.44080 0.03964  -0.31018 0.14065  207 LYS A CD  
1400 C CE  . LYS A 173 ? 0.50932 1.27720 1.46395 0.04561  -0.29292 0.13334  207 LYS A CE  
1401 N NZ  . LYS A 173 ? 0.64389 1.43768 1.64474 0.05016  -0.32443 0.14780  207 LYS A NZ  
1402 N N   . LYS A 174 ? 0.74384 1.32284 1.43417 0.05448  -0.23024 0.12278  208 LYS A N   
1403 C CA  . LYS A 174 ? 0.85259 1.39702 1.51768 0.06666  -0.22643 0.13024  208 LYS A CA  
1404 C C   . LYS A 174 ? 0.95835 1.47642 1.55649 0.05178  -0.25014 0.14437  208 LYS A C   
1405 O O   . LYS A 174 ? 0.90939 1.43095 1.47127 0.03044  -0.25876 0.14010  208 LYS A O   
1406 C CB  . LYS A 174 ? 0.75210 1.28780 1.41710 0.07201  -0.19012 0.11205  208 LYS A CB  
1407 C CG  . LYS A 174 ? 0.75346 1.30227 1.47326 0.09239  -0.16434 0.09938  208 LYS A CG  
1408 C CD  . LYS A 174 ? 0.74342 1.27771 1.45175 0.09708  -0.13068 0.08072  208 LYS A CD  
1409 C CE  . LYS A 174 ? 0.86769 1.39434 1.61292 0.12140  -0.11137 0.07172  208 LYS A CE  
1410 N NZ  . LYS A 174 ? 0.96518 1.46249 1.71128 0.13482  -0.13010 0.08810  208 LYS A NZ  
1411 N N   . SER A 175 ? 1.01130 1.50099 1.59153 0.06273  -0.25926 0.16106  209 SER A N   
1412 C CA  . SER A 175 ? 1.16019 1.62269 1.67176 0.04971  -0.27751 0.17605  209 SER A CA  
1413 C C   . SER A 175 ? 1.19668 1.63831 1.65909 0.03794  -0.25179 0.15940  209 SER A C   
1414 O O   . SER A 175 ? 1.13002 1.55971 1.60414 0.04784  -0.22174 0.14503  209 SER A O   
1415 C CB  . SER A 175 ? 1.26610 1.70023 1.77112 0.06450  -0.28811 0.19884  209 SER A CB  
1416 O OG  . SER A 175 ? 1.38433 1.79159 1.81774 0.05139  -0.30192 0.21446  209 SER A OG  
1417 N N   . LEU A 176 ? 1.21384 1.64311 1.61210 0.01676  -0.25980 0.15665  210 LEU A N   
1418 C CA  . LEU A 176 ? 1.10492 1.50688 1.44813 0.00505  -0.23261 0.13773  210 LEU A CA  
1419 C C   . LEU A 176 ? 1.17083 1.53367 1.48091 0.01354  -0.21696 0.14295  210 LEU A C   
1420 O O   . LEU A 176 ? 1.18594 1.52649 1.45204 0.01005  -0.23035 0.15969  210 LEU A O   
1421 C CB  . LEU A 176 ? 1.01704 1.41238 1.30155 -0.01817 -0.24626 0.13371  210 LEU A CB  
1422 C CG  . LEU A 176 ? 1.02252 1.44245 1.32327 -0.03325 -0.24445 0.11617  210 LEU A CG  
1423 C CD1 . LEU A 176 ? 0.94729 1.41356 1.32441 -0.02816 -0.26208 0.12218  210 LEU A CD1 
1424 C CD2 . LEU A 176 ? 1.14221 1.54728 1.37992 -0.05563 -0.25934 0.11115  210 LEU A CD2 
1425 N N   . SER A 177 ? 1.02537 1.37976 1.35560 0.02375  -0.18884 0.12910  211 SER A N   
1426 C CA  . SER A 177 ? 1.14454 1.46359 1.45222 0.03071  -0.17318 0.13155  211 SER A CA  
1427 C C   . SER A 177 ? 1.23195 1.53480 1.50543 0.02128  -0.14663 0.11038  211 SER A C   
1428 O O   . SER A 177 ? 1.10827 1.42581 1.40368 0.02174  -0.13118 0.09223  211 SER A O   
1429 C CB  . SER A 177 ? 1.16738 1.48750 1.53239 0.05221  -0.16694 0.13363  211 SER A CB  
1430 O OG  . SER A 177 ? 1.11921 1.45200 1.51576 0.05805  -0.14387 0.11034  211 SER A OG  
1431 N N   . GLY A 178 ? 1.20620 1.47954 1.42696 0.01290  -0.14096 0.11391  212 GLY A N   
1432 C CA  . GLY A 178 ? 0.92971 1.18694 1.11883 0.00412  -0.11852 0.09651  212 GLY A CA  
1433 C C   . GLY A 178 ? 0.88598 1.12902 1.01634 -0.01225 -0.12150 0.09778  212 GLY A C   
1434 O O   . GLY A 178 ? 1.00192 1.24884 1.11028 -0.01889 -0.14196 0.10989  212 GLY A O   
1435 N N   . THR A 179 ? 0.97582 1.20152 1.08060 -0.01830 -0.10092 0.08429  213 THR A N   
1436 C CA  . THR A 179 ? 0.97988 1.19005 1.03177 -0.03256 -0.09749 0.08015  213 THR A CA  
1437 C C   . THR A 179 ? 0.69230 0.91695 0.74165 -0.04374 -0.10111 0.06500  213 THR A C   
1438 O O   . THR A 179 ? 0.61227 0.84603 0.68698 -0.04250 -0.08976 0.05195  213 THR A O   
1439 C CB  . THR A 179 ? 0.91567 1.10179 0.95023 -0.03257 -0.07344 0.07340  213 THR A CB  
1440 O OG1 . THR A 179 ? 0.89692 1.08862 0.96731 -0.02527 -0.06077 0.06107  213 THR A OG1 
1441 C CG2 . THR A 179 ? 0.93960 1.10755 0.96430 -0.02745 -0.07070 0.09091  213 THR A CG2 
1442 N N   . ALA A 180 ? 0.83452 0.98079 0.75756 -0.00206 -0.05807 0.02643  214 ALA A N   
1443 C CA  . ALA A 180 ? 0.69447 0.86477 0.63616 -0.00912 -0.06994 0.00677  214 ALA A CA  
1444 C C   . ALA A 180 ? 0.66933 0.83536 0.61881 -0.02480 -0.05691 -0.00518 214 ALA A C   
1445 O O   . ALA A 180 ? 0.65131 0.83282 0.62554 -0.03445 -0.06360 -0.01939 214 ALA A O   
1446 C CB  . ALA A 180 ? 0.68841 0.86720 0.60024 -0.00140 -0.09047 0.00145  214 ALA A CB  
1447 N N   . ARG A 181 ? 0.63812 0.78412 0.57010 -0.02765 -0.03891 0.00134  215 ARG A N   
1448 C CA  . ARG A 181 ? 0.63852 0.77962 0.57704 -0.03897 -0.02846 -0.00968 215 ARG A CA  
1449 C C   . ARG A 181 ? 0.58045 0.72609 0.55683 -0.04862 -0.02151 -0.01117 215 ARG A C   
1450 O O   . ARG A 181 ? 0.47827 0.62417 0.46783 -0.05854 -0.01950 -0.02126 215 ARG A O   
1451 C CB  . ARG A 181 ? 0.67193 0.79674 0.58538 -0.03721 -0.01109 -0.00206 215 ARG A CB  
1452 C CG  . ARG A 181 ? 0.74065 0.86012 0.65734 -0.04407 -0.00224 -0.01480 215 ARG A CG  
1453 C CD  . ARG A 181 ? 0.76329 0.87426 0.66766 -0.04179 0.01756  -0.00563 215 ARG A CD  
1454 N NE  . ARG A 181 ? 0.74277 0.85237 0.60726 -0.03182 0.02140  0.00085  215 ARG A NE  
1455 C CZ  . ARG A 181 ? 0.66347 0.77125 0.51461 -0.02904 0.04054  0.01177  215 ARG A CZ  
1456 N NH1 . ARG A 181 ? 0.73384 0.84201 0.61190 -0.03538 0.05510  0.01611  215 ARG A NH1 
1457 N NH2 . ARG A 181 ? 0.70089 0.80916 0.51116 -0.01960 0.04516  0.01937  215 ARG A NH2 
1458 N N   . TYR A 182 ? 0.55267 0.69958 0.54414 -0.04495 -0.01820 -0.00139 216 TYR A N   
1459 C CA  . TYR A 182 ? 0.60488 0.75524 0.62369 -0.05180 -0.01001 -0.00255 216 TYR A CA  
1460 C C   . TYR A 182 ? 0.59404 0.76485 0.63843 -0.04811 -0.01632 -0.00446 216 TYR A C   
1461 O O   . TYR A 182 ? 0.65147 0.83053 0.71630 -0.05407 -0.00919 -0.00704 216 TYR A O   
1462 C CB  . TYR A 182 ? 0.54261 0.67510 0.55759 -0.05104 0.00221  0.00714  216 TYR A CB  
1463 C CG  . TYR A 182 ? 0.60560 0.72430 0.60111 -0.05325 0.01102  0.01152  216 TYR A CG  
1464 C CD1 . TYR A 182 ? 0.60919 0.72680 0.60669 -0.06017 0.01716  0.00445  216 TYR A CD1 
1465 C CD2 . TYR A 182 ? 0.55108 0.65852 0.52783 -0.04764 0.01432  0.02403  216 TYR A CD2 
1466 C CE1 . TYR A 182 ? 0.54032 0.65044 0.52375 -0.05948 0.02696  0.00731  216 TYR A CE1 
1467 C CE2 . TYR A 182 ? 0.62804 0.72927 0.59005 -0.04959 0.02586  0.02922  216 TYR A CE2 
1468 C CZ  . TYR A 182 ? 0.55285 0.65771 0.51935 -0.05455 0.03248  0.01962  216 TYR A CZ  
1469 O OH  . TYR A 182 ? 0.67831 0.78187 0.63370 -0.05386 0.04560  0.02360  216 TYR A OH  
1470 N N   . MET A 183 ? 0.62227 0.80345 0.66573 -0.03700 -0.02890 -0.00265 217 MET A N   
1471 C CA  . MET A 183 ? 0.60888 0.81303 0.68055 -0.02967 -0.03350 -0.00447 217 MET A CA  
1472 C C   . MET A 183 ? 0.60764 0.84099 0.70971 -0.04150 -0.03451 -0.01401 217 MET A C   
1473 O O   . MET A 183 ? 0.54525 0.78035 0.64556 -0.05325 -0.03981 -0.02038 217 MET A O   
1474 C CB  . MET A 183 ? 0.51501 0.72565 0.58099 -0.01346 -0.04975 -0.00006 217 MET A CB  
1475 C CG  . MET A 183 ? 0.63893 0.87500 0.71138 -0.01518 -0.06784 -0.00796 217 MET A CG  
1476 S SD  . MET A 183 ? 0.82803 1.05926 0.87041 0.00349  -0.08900 0.00036  217 MET A SD  
1477 C CE  . MET A 183 ? 0.83994 1.04998 0.88154 0.02168  -0.08255 0.01571  217 MET A CE  
1478 N N   . SER A 184 ? 0.59167 0.84697 0.72202 -0.03850 -0.02839 -0.01499 218 SER A N   
1479 C CA  . SER A 184 ? 0.63745 0.92268 0.80018 -0.05172 -0.02473 -0.01992 218 SER A CA  
1480 C C   . SER A 184 ? 0.49512 0.81071 0.68085 -0.05384 -0.04296 -0.02581 218 SER A C   
1481 O O   . SER A 184 ? 0.51991 0.83767 0.69664 -0.04058 -0.05897 -0.02600 218 SER A O   
1482 C CB  . SER A 184 ? 0.56284 0.86814 0.74707 -0.04544 -0.01069 -0.01881 218 SER A CB  
1483 O OG  . SER A 184 ? 0.60635 0.93249 0.80642 -0.02635 -0.01799 -0.02021 218 SER A OG  
1484 N N   . ILE A 185 ? 0.45396 0.79283 0.67038 -0.07163 -0.04171 -0.02970 219 ILE A N   
1485 C CA  . ILE A 185 ? 0.57492 0.94788 0.82281 -0.07734 -0.06055 -0.03682 219 ILE A CA  
1486 C C   . ILE A 185 ? 0.53452 0.94697 0.81235 -0.05941 -0.06565 -0.03574 219 ILE A C   
1487 O O   . ILE A 185 ? 0.47988 0.91211 0.76778 -0.05145 -0.08783 -0.04023 219 ILE A O   
1488 C CB  . ILE A 185 ? 0.49222 0.88104 0.77378 -0.10319 -0.05592 -0.03893 219 ILE A CB  
1489 C CG1 . ILE A 185 ? 0.43699 0.78269 0.68896 -0.11753 -0.05550 -0.04200 219 ILE A CG1 
1490 C CG2 . ILE A 185 ? 0.44021 0.87133 0.76563 -0.11149 -0.07604 -0.04669 219 ILE A CG2 
1491 C CD1 . ILE A 185 ? 0.52196 0.87279 0.80469 -0.14354 -0.05255 -0.04244 219 ILE A CD1 
1492 N N   . ASN A 186 ? 0.41082 0.83519 0.70160 -0.05051 -0.04624 -0.03081 220 ASN A N   
1493 C CA  . ASN A 186 ? 0.48440 0.94572 0.80500 -0.02956 -0.04876 -0.03140 220 ASN A CA  
1494 C C   . ASN A 186 ? 0.46753 0.90681 0.76064 -0.00537 -0.06534 -0.02984 220 ASN A C   
1495 O O   . ASN A 186 ? 0.64306 1.11268 0.96115 0.01197  -0.07951 -0.03121 220 ASN A O   
1496 C CB  . ASN A 186 ? 0.46968 0.94058 0.79912 -0.02203 -0.02293 -0.02901 220 ASN A CB  
1497 C CG  . ASN A 186 ? 0.60496 1.09829 0.95815 -0.04522 -0.00434 -0.02607 220 ASN A CG  
1498 O OD1 . ASN A 186 ? 0.46797 1.01106 0.86972 -0.05411 -0.00354 -0.02627 220 ASN A OD1 
1499 N ND2 . ASN A 186 ? 0.66679 1.12461 0.98775 -0.05545 0.01044  -0.02165 220 ASN A ND2 
1500 N N   . THR A 187 ? 0.53359 0.92161 0.77758 -0.00369 -0.06378 -0.02525 221 THR A N   
1501 C CA  . THR A 187 ? 0.56757 0.93077 0.78290 0.01666  -0.07791 -0.01947 221 THR A CA  
1502 C C   . THR A 187 ? 0.50497 0.87602 0.71129 0.01595  -0.10330 -0.02085 221 THR A C   
1503 O O   . THR A 187 ? 0.58613 0.96030 0.78721 0.03598  -0.12085 -0.01619 221 THR A O   
1504 C CB  . THR A 187 ? 0.58295 0.89320 0.75341 0.01580  -0.06658 -0.01231 221 THR A CB  
1505 O OG1 . THR A 187 ? 0.65412 0.95814 0.83110 0.01279  -0.04563 -0.01411 221 THR A OG1 
1506 C CG2 . THR A 187 ? 0.61272 0.89631 0.75960 0.03731  -0.07658 -0.00254 221 THR A CG2 
1507 N N   . HIS A 188 ? 0.53341 0.90528 0.73546 -0.00552 -0.10714 -0.02779 222 HIS A N   
1508 C CA  . HIS A 188 ? 0.60479 0.98658 0.79791 -0.00668 -0.13358 -0.03375 222 HIS A CA  
1509 C C   . HIS A 188 ? 0.61488 1.04988 0.85718 0.00044  -0.15307 -0.03892 222 HIS A C   
1510 O O   . HIS A 188 ? 0.53227 0.97700 0.76486 0.01225  -0.17952 -0.04007 222 HIS A O   
1511 C CB  . HIS A 188 ? 0.59885 0.97021 0.78357 -0.03128 -0.13390 -0.04429 222 HIS A CB  
1512 C CG  . HIS A 188 ? 0.64958 0.97277 0.78142 -0.03368 -0.12272 -0.04107 222 HIS A CG  
1513 N ND1 . HIS A 188 ? 0.59150 0.89299 0.67563 -0.02446 -0.13525 -0.04035 222 HIS A ND1 
1514 C CD2 . HIS A 188 ? 0.56275 0.85914 0.68331 -0.04340 -0.09990 -0.03796 222 HIS A CD2 
1515 C CE1 . HIS A 188 ? 0.69929 0.96531 0.74869 -0.02872 -0.11832 -0.03707 222 HIS A CE1 
1516 N NE2 . HIS A 188 ? 0.53110 0.79351 0.60362 -0.04006 -0.09827 -0.03597 222 HIS A NE2 
1517 N N   . LEU A 189 ? 0.48956 0.96234 0.78490 -0.00578 -0.14035 -0.04134 223 LEU A N   
1518 C CA  . LEU A 189 ? 0.63922 1.17190 0.99272 -0.00035 -0.15518 -0.04607 223 LEU A CA  
1519 C C   . LEU A 189 ? 0.63459 1.18167 1.00044 0.03184  -0.15653 -0.03948 223 LEU A C   
1520 O O   . LEU A 189 ? 0.64103 1.24309 1.06156 0.04079  -0.16495 -0.04288 223 LEU A O   
1521 C CB  . LEU A 189 ? 0.60363 1.17460 1.01133 -0.02311 -0.13748 -0.04981 223 LEU A CB  
1522 C CG  . LEU A 189 ? 0.48080 1.03094 0.87949 -0.05527 -0.13404 -0.05487 223 LEU A CG  
1523 C CD1 . LEU A 189 ? 0.33782 0.92259 0.78885 -0.07727 -0.11367 -0.05298 223 LEU A CD1 
1524 C CD2 . LEU A 189 ? 0.45524 1.00764 0.84933 -0.06467 -0.16711 -0.06654 223 LEU A CD2 
1525 N N   . GLY A 190 ? 0.56931 1.06853 0.88928 0.04941  -0.14876 -0.03030 224 GLY A N   
1526 C CA  . GLY A 190 ? 0.54968 1.05157 0.87750 0.08125  -0.15197 -0.02433 224 GLY A CA  
1527 C C   . GLY A 190 ? 0.58196 1.10945 0.94940 0.09011  -0.12847 -0.02805 224 GLY A C   
1528 O O   . GLY A 190 ? 0.74858 1.29403 1.13922 0.11830  -0.13341 -0.02762 224 GLY A O   
1529 N N   . ARG A 191 ? 0.46946 0.99841 0.84285 0.06890  -0.10302 -0.03171 225 ARG A N   
1530 C CA  . ARG A 191 ? 0.49704 1.05216 0.90141 0.07712  -0.07829 -0.03571 225 ARG A CA  
1531 C C   . ARG A 191 ? 0.52180 1.02460 0.88600 0.09330  -0.06396 -0.03395 225 ARG A C   
1532 O O   . ARG A 191 ? 0.61352 1.06101 0.92921 0.08650  -0.06556 -0.02829 225 ARG A O   
1533 C CB  . ARG A 191 ? 0.39893 0.97838 0.82399 0.04731  -0.05765 -0.03780 225 ARG A CB  
1534 C CG  . ARG A 191 ? 0.56711 1.18975 1.03194 0.02484  -0.07282 -0.04002 225 ARG A CG  
1535 C CD  . ARG A 191 ? 0.50250 1.14100 0.98666 -0.00611 -0.05151 -0.03861 225 ARG A CD  
1536 N NE  . ARG A 191 ? 0.60155 1.27728 1.12791 -0.03013 -0.06779 -0.04151 225 ARG A NE  
1537 C CZ  . ARG A 191 ? 0.56465 1.26103 1.12094 -0.05970 -0.05415 -0.03871 225 ARG A CZ  
1538 N NH1 . ARG A 191 ? 0.57456 1.26066 1.12019 -0.06782 -0.02321 -0.03131 225 ARG A NH1 
1539 N NH2 . ARG A 191 ? 0.55847 1.27604 1.15082 -0.08117 -0.07291 -0.04180 225 ARG A NH2 
1540 N N   . GLU A 192 ? 0.57217 1.09455 0.95919 0.11512  -0.05000 -0.04005 226 GLU A N   
1541 C CA  . GLU A 192 ? 0.60281 1.07657 0.95550 0.12999  -0.03713 -0.04262 226 GLU A CA  
1542 C C   . GLU A 192 ? 0.48223 0.92701 0.80276 0.10459  -0.01812 -0.04228 226 GLU A C   
1543 O O   . GLU A 192 ? 0.65619 1.13370 0.99418 0.08541  -0.00274 -0.04351 226 GLU A O   
1544 C CB  . GLU A 192 ? 0.50097 1.00672 0.88528 0.15832  -0.02383 -0.05359 226 GLU A CB  
1545 C CG  . GLU A 192 ? 0.55124 1.00647 0.90073 0.17410  -0.01150 -0.06116 226 GLU A CG  
1546 C CD  . GLU A 192 ? 0.64444 1.04790 0.97349 0.19874  -0.03125 -0.05799 226 GLU A CD  
1547 O OE1 . GLU A 192 ? 0.78167 1.20322 1.13829 0.23049  -0.03867 -0.06308 226 GLU A OE1 
1548 O OE2 . GLU A 192 ? 1.00887 1.35418 1.29640 0.18662  -0.03891 -0.04911 226 GLU A OE2 
1549 N N   . GLN A 193 ? 0.55861 0.94245 0.83426 0.10412  -0.01986 -0.03901 227 GLN A N   
1550 C CA  . GLN A 193 ? 0.45388 0.80878 0.69924 0.08221  -0.00568 -0.03832 227 GLN A CA  
1551 C C   . GLN A 193 ? 0.47386 0.82453 0.71321 0.09256  0.01334  -0.04894 227 GLN A C   
1552 O O   . GLN A 193 ? 0.49701 0.84215 0.74104 0.11901  0.01299  -0.05742 227 GLN A O   
1553 C CB  . GLN A 193 ? 0.54283 0.84047 0.74787 0.07515  -0.01602 -0.02972 227 GLN A CB  
1554 C CG  . GLN A 193 ? 0.53493 0.83422 0.73515 0.06529  -0.03295 -0.02027 227 GLN A CG  
1555 C CD  . GLN A 193 ? 0.54571 0.79331 0.70583 0.05965  -0.03881 -0.01007 227 GLN A CD  
1556 O OE1 . GLN A 193 ? 0.73472 0.96767 0.88251 0.06962  -0.05411 -0.00099 227 GLN A OE1 
1557 N NE2 . GLN A 193 ? 0.64238 0.86468 0.78261 0.04385  -0.02639 -0.01007 227 GLN A NE2 
1558 N N   . SER A 194 ? 0.44903 0.80066 0.67556 0.07307  0.02893  -0.04909 228 SER A N   
1559 C CA  . SER A 194 ? 0.43740 0.78612 0.65012 0.08093  0.04676  -0.05930 228 SER A CA  
1560 C C   . SER A 194 ? 0.46468 0.77953 0.64271 0.05934  0.05110  -0.05527 228 SER A C   
1561 O O   . SER A 194 ? 0.51560 0.80153 0.67959 0.04427  0.04001  -0.04663 228 SER A O   
1562 C CB  . SER A 194 ? 0.52292 0.93323 0.76779 0.08482  0.06573  -0.06286 228 SER A CB  
1563 O OG  . SER A 194 ? 0.47879 0.91831 0.74085 0.05773  0.07041  -0.05136 228 SER A OG  
1564 N N   . ARG A 195 ? 0.49975 0.82048 0.66293 0.05950  0.06755  -0.06158 229 ARG A N   
1565 C CA  . ARG A 195 ? 0.43727 0.72775 0.56788 0.04232  0.06957  -0.05831 229 ARG A CA  
1566 C C   . ARG A 195 ? 0.48012 0.78034 0.61742 0.01591  0.06991  -0.04346 229 ARG A C   
1567 O O   . ARG A 195 ? 0.46881 0.73746 0.58633 0.00205  0.06323  -0.03807 229 ARG A O   
1568 C CB  . ARG A 195 ? 0.37368 0.67310 0.48383 0.05006  0.08608  -0.06767 229 ARG A CB  
1569 C CG  . ARG A 195 ? 0.42316 0.69734 0.51541 0.07511  0.08284  -0.08686 229 ARG A CG  
1570 C CD  . ARG A 195 ? 0.51900 0.80713 0.58637 0.08503  0.09995  -0.09842 229 ARG A CD  
1571 N NE  . ARG A 195 ? 0.47176 0.81519 0.56292 0.09838  0.12008  -0.10033 229 ARG A NE  
1572 C CZ  . ARG A 195 ? 0.65396 1.01886 0.72683 0.11436  0.13898  -0.11209 229 ARG A CZ  
1573 N NH1 . ARG A 195 ? 0.68422 1.01752 0.71072 0.11969  0.13772  -0.12491 229 ARG A NH1 
1574 N NH2 . ARG A 195 ? 0.64598 1.06797 0.74793 0.12571  0.15950  -0.11160 229 ARG A NH2 
1575 N N   . ARG A 196 ? 0.48669 0.83065 0.65500 0.00881  0.07718  -0.03747 230 ARG A N   
1576 C CA  . ARG A 196 ? 0.46633 0.81586 0.64267 -0.01661 0.07680  -0.02521 230 ARG A CA  
1577 C C   . ARG A 196 ? 0.48834 0.81107 0.66167 -0.02441 0.05775  -0.02226 230 ARG A C   
1578 O O   . ARG A 196 ? 0.44548 0.75283 0.61077 -0.04254 0.05515  -0.01556 230 ARG A O   
1579 C CB  . ARG A 196 ? 0.45841 0.86074 0.67529 -0.02406 0.08652  -0.02020 230 ARG A CB  
1580 C CG  . ARG A 196 ? 0.47024 0.90033 0.72261 -0.01303 0.07459  -0.02500 230 ARG A CG  
1581 C CD  . ARG A 196 ? 0.49307 0.98137 0.79355 -0.02289 0.08360  -0.02022 230 ARG A CD  
1582 N NE  . ARG A 196 ? 0.43552 0.95397 0.77303 -0.01160 0.06841  -0.02534 230 ARG A NE  
1583 C CZ  . ARG A 196 ? 0.51260 1.08831 0.90205 -0.01716 0.07136  -0.02340 230 ARG A CZ  
1584 N NH1 . ARG A 196 ? 0.30302 0.91213 0.71503 -0.03571 0.09156  -0.01472 230 ARG A NH1 
1585 N NH2 . ARG A 196 ? 0.45598 1.05733 0.87713 -0.00427 0.05314  -0.02878 230 ARG A NH2 
1586 N N   . ASP A 197 ? 0.48443 0.80022 0.66179 -0.00935 0.04481  -0.02672 231 ASP A N   
1587 C CA  . ASP A 197 ? 0.40194 0.69671 0.57255 -0.01500 0.02830  -0.02260 231 ASP A CA  
1588 C C   . ASP A 197 ? 0.51551 0.76393 0.65286 -0.01762 0.02527  -0.02027 231 ASP A C   
1589 O O   . ASP A 197 ? 0.50176 0.73353 0.62841 -0.02762 0.01798  -0.01534 231 ASP A O   
1590 C CB  . ASP A 197 ? 0.39721 0.70372 0.58309 0.00260  0.01492  -0.02470 231 ASP A CB  
1591 C CG  . ASP A 197 ? 0.48908 0.84845 0.71616 0.00375  0.01516  -0.02690 231 ASP A CG  
1592 O OD1 . ASP A 197 ? 0.52254 0.90058 0.76539 -0.01527 0.01255  -0.02415 231 ASP A OD1 
1593 O OD2 . ASP A 197 ? 0.60141 0.98434 0.84813 0.02364  0.01791  -0.03212 231 ASP A OD2 
1594 N N   . ASP A 198 ? 0.48637 0.71539 0.60846 -0.00869 0.03054  -0.02486 232 ASP A N   
1595 C CA  . ASP A 198 ? 0.51533 0.70614 0.61322 -0.01495 0.02795  -0.02253 232 ASP A CA  
1596 C C   . ASP A 198 ? 0.54838 0.73851 0.63889 -0.03264 0.03406  -0.01816 232 ASP A C   
1597 O O   . ASP A 198 ? 0.50632 0.67410 0.58524 -0.04105 0.03039  -0.01365 232 ASP A O   
1598 C CB  . ASP A 198 ? 0.46284 0.63303 0.54875 -0.00257 0.02900  -0.03129 232 ASP A CB  
1599 C CG  . ASP A 198 ? 0.45977 0.61389 0.54928 0.01483  0.01984  -0.03374 232 ASP A CG  
1600 O OD1 . ASP A 198 ? 0.46329 0.61200 0.55593 0.01458  0.01118  -0.02468 232 ASP A OD1 
1601 O OD2 . ASP A 198 ? 0.51850 0.66308 0.60508 0.02998  0.02069  -0.04485 232 ASP A OD2 
1602 N N   . LEU A 199 ? 0.51396 0.72899 0.61241 -0.03778 0.04408  -0.01795 233 LEU A N   
1603 C CA  . LEU A 199 ? 0.46090 0.67148 0.55147 -0.05293 0.04913  -0.01161 233 LEU A CA  
1604 C C   . LEU A 199 ? 0.45179 0.66666 0.55463 -0.06666 0.04518  -0.00590 233 LEU A C   
1605 O O   . LEU A 199 ? 0.54481 0.74189 0.63847 -0.07636 0.04395  -0.00166 233 LEU A O   
1606 C CB  . LEU A 199 ? 0.40095 0.63235 0.49013 -0.05314 0.06264  -0.01051 233 LEU A CB  
1607 C CG  . LEU A 199 ? 0.52557 0.75284 0.59656 -0.03781 0.06682  -0.01998 233 LEU A CG  
1608 C CD1 . LEU A 199 ? 0.61706 0.86055 0.67516 -0.04015 0.08090  -0.01598 233 LEU A CD1 
1609 C CD2 . LEU A 199 ? 0.60137 0.79215 0.65282 -0.03541 0.05558  -0.02488 233 LEU A CD2 
1610 N N   . GLU A 200 ? 0.47664 0.71490 0.60118 -0.06663 0.04165  -0.00731 234 GLU A N   
1611 C CA  . GLU A 200 ? 0.51936 0.75774 0.65311 -0.07901 0.03378  -0.00597 234 GLU A CA  
1612 C C   . GLU A 200 ? 0.52239 0.73364 0.63674 -0.07591 0.02398  -0.00742 234 GLU A C   
1613 O O   . GLU A 200 ? 0.54942 0.74690 0.65748 -0.08507 0.02082  -0.00736 234 GLU A O   
1614 C CB  . GLU A 200 ? 0.36811 0.64051 0.53151 -0.07935 0.02845  -0.00888 234 GLU A CB  
1615 C CG  . GLU A 200 ? 0.53448 0.80568 0.70632 -0.09204 0.01611  -0.01140 234 GLU A CG  
1616 C CD  . GLU A 200 ? 0.50999 0.81944 0.71712 -0.09497 0.00809  -0.01499 234 GLU A CD  
1617 O OE1 . GLU A 200 ? 0.70253 1.04401 0.93215 -0.08799 0.01595  -0.01368 234 GLU A OE1 
1618 O OE2 . GLU A 200 ? 0.43924 0.74855 0.65262 -0.10349 -0.00670 -0.02049 234 GLU A OE2 
1619 N N   . ALA A 201 ? 0.60037 0.80268 0.70479 -0.06249 0.02016  -0.00823 235 ALA A N   
1620 C CA  . ALA A 201 ? 0.63385 0.81173 0.71865 -0.06030 0.01473  -0.00580 235 ALA A CA  
1621 C C   . ALA A 201 ? 0.52667 0.68378 0.59910 -0.06688 0.02127  -0.00304 235 ALA A C   
1622 O O   . ALA A 201 ? 0.57637 0.72097 0.63837 -0.07040 0.02039  -0.00155 235 ALA A O   
1623 C CB  . ALA A 201 ? 0.50846 0.67763 0.58722 -0.04603 0.01015  -0.00369 235 ALA A CB  
1624 N N   . LEU A 202 ? 0.45045 0.60604 0.52351 -0.06702 0.02749  -0.00311 236 LEU A N   
1625 C CA  . LEU A 202 ? 0.49390 0.63444 0.55887 -0.07275 0.03082  -0.00058 236 LEU A CA  
1626 C C   . LEU A 202 ? 0.59659 0.73759 0.66441 -0.08240 0.03238  0.00116  236 LEU A C   
1627 O O   . LEU A 202 ? 0.45294 0.58088 0.51574 -0.08472 0.03240  0.00265  236 LEU A O   
1628 C CB  . LEU A 202 ? 0.45652 0.59712 0.51765 -0.06993 0.03419  -0.00239 236 LEU A CB  
1629 C CG  . LEU A 202 ? 0.56339 0.69063 0.61880 -0.06174 0.03055  -0.00648 236 LEU A CG  
1630 C CD1 . LEU A 202 ? 0.55084 0.67880 0.59740 -0.05843 0.03238  -0.01202 236 LEU A CD1 
1631 C CD2 . LEU A 202 ? 0.46182 0.57080 0.51573 -0.06587 0.02695  -0.00238 236 LEU A CD2 
1632 N N   . GLY A 203 ? 0.50479 0.66072 0.58364 -0.08802 0.03392  0.00112  237 GLY A N   
1633 C CA  . GLY A 203 ? 0.39131 0.54172 0.47502 -0.09848 0.03368  0.00277  237 GLY A CA  
1634 C C   . GLY A 203 ? 0.50179 0.64184 0.58148 -0.09884 0.02686  -0.00307 237 GLY A C   
1635 O O   . GLY A 203 ? 0.51446 0.63862 0.59085 -0.10243 0.02648  -0.00403 237 GLY A O   
1636 N N   . HIS A 204 ? 0.40041 0.54840 0.47776 -0.09309 0.02101  -0.00737 238 HIS A N   
1637 C CA  . HIS A 204 ? 0.41666 0.55520 0.48128 -0.09083 0.01494  -0.01320 238 HIS A CA  
1638 C C   . HIS A 204 ? 0.58113 0.70374 0.63011 -0.08514 0.02104  -0.01027 238 HIS A C   
1639 O O   . HIS A 204 ? 0.57617 0.68830 0.61517 -0.08415 0.02138  -0.01516 238 HIS A O   
1640 C CB  . HIS A 204 ? 0.55109 0.70243 0.61254 -0.08413 0.00610  -0.01567 238 HIS A CB  
1641 C CG  . HIS A 204 ? 0.70764 0.88111 0.79091 -0.08981 -0.00188 -0.02009 238 HIS A CG  
1642 N ND1 . HIS A 204 ? 0.52543 0.71840 0.61572 -0.08210 -0.01030 -0.02065 238 HIS A ND1 
1643 C CD2 . HIS A 204 ? 0.53627 0.71697 0.63994 -0.10303 -0.00299 -0.02298 238 HIS A CD2 
1644 C CE1 . HIS A 204 ? 0.70653 0.92303 0.82385 -0.09033 -0.01609 -0.02484 238 HIS A CE1 
1645 N NE2 . HIS A 204 ? 0.52231 0.73111 0.64841 -0.10466 -0.01116 -0.02569 238 HIS A NE2 
1646 N N   . VAL A 205 ? 0.50325 0.62500 0.55198 -0.08120 0.02586  -0.00345 239 VAL A N   
1647 C CA  . VAL A 205 ? 0.52911 0.64097 0.57151 -0.07850 0.03179  0.00072  239 VAL A CA  
1648 C C   . VAL A 205 ? 0.46766 0.57349 0.51665 -0.08175 0.03516  0.00012  239 VAL A C   
1649 O O   . VAL A 205 ? 0.56650 0.66787 0.61347 -0.07878 0.03972  -0.00001 239 VAL A O   
1650 C CB  . VAL A 205 ? 0.45785 0.56802 0.50279 -0.07602 0.03293  0.00690  239 VAL A CB  
1651 C CG1 . VAL A 205 ? 0.41226 0.51639 0.45880 -0.07671 0.03865  0.01227  239 VAL A CG1 
1652 C CG2 . VAL A 205 ? 0.40448 0.51593 0.44276 -0.07016 0.02851  0.00901  239 VAL A CG2 
1653 N N   . PHE A 206 ? 0.52340 0.63025 0.58039 -0.08659 0.03370  0.00098  240 PHE A N   
1654 C CA  . PHE A 206 ? 0.43889 0.53706 0.50037 -0.08818 0.03490  0.00319  240 PHE A CA  
1655 C C   . PHE A 206 ? 0.47408 0.56091 0.53436 -0.08802 0.03398  -0.00303 240 PHE A C   
1656 O O   . PHE A 206 ? 0.58416 0.66305 0.64586 -0.08270 0.03630  -0.00390 240 PHE A O   
1657 C CB  . PHE A 206 ? 0.53108 0.63170 0.59591 -0.09339 0.03444  0.00855  240 PHE A CB  
1658 C CG  . PHE A 206 ? 0.45268 0.56251 0.51425 -0.09095 0.03506  0.01076  240 PHE A CG  
1659 C CD1 . PHE A 206 ? 0.44577 0.55467 0.50607 -0.08629 0.03379  0.00946  240 PHE A CD1 
1660 C CD2 . PHE A 206 ? 0.36230 0.48122 0.42243 -0.09345 0.03751  0.01362  240 PHE A CD2 
1661 C CE1 . PHE A 206 ? 0.39795 0.50964 0.45456 -0.08370 0.03205  0.00819  240 PHE A CE1 
1662 C CE2 . PHE A 206 ? 0.52641 0.65198 0.57973 -0.08838 0.03811  0.01197  240 PHE A CE2 
1663 C CZ  . PHE A 206 ? 0.50777 0.62712 0.55878 -0.08325 0.03391  0.00784  240 PHE A CZ  
1664 N N   . PHE A 207 ? 0.57611 0.66260 0.63578 -0.09304 0.02946  -0.00907 241 PHE A N   
1665 C CA  . PHE A 207 ? 0.54708 0.61893 0.60274 -0.09256 0.02589  -0.01938 241 PHE A CA  
1666 C C   . PHE A 207 ? 0.46425 0.53628 0.50410 -0.08193 0.02928  -0.02631 241 PHE A C   
1667 O O   . PHE A 207 ? 0.57137 0.63040 0.60558 -0.07572 0.03074  -0.03481 241 PHE A O   
1668 C CB  . PHE A 207 ? 0.53819 0.61232 0.59929 -0.10218 0.01722  -0.02591 241 PHE A CB  
1669 C CG  . PHE A 207 ? 0.55234 0.62409 0.63124 -0.11471 0.01653  -0.01840 241 PHE A CG  
1670 C CD1 . PHE A 207 ? 0.61518 0.66240 0.69914 -0.11895 0.01518  -0.01767 241 PHE A CD1 
1671 C CD2 . PHE A 207 ? 0.70451 0.79827 0.79509 -0.12135 0.01833  -0.01101 241 PHE A CD2 
1672 C CE1 . PHE A 207 ? 0.69223 0.73554 0.79105 -0.13195 0.01602  -0.00653 241 PHE A CE1 
1673 C CE2 . PHE A 207 ? 0.57410 0.66935 0.68010 -0.13348 0.02124  -0.00147 241 PHE A CE2 
1674 C CZ  . PHE A 207 ? 0.69486 0.76416 0.80422 -0.14000 0.02025  0.00231  241 PHE A CZ  
1675 N N   . TYR A 208 ? 0.52036 0.60601 0.55196 -0.07873 0.03147  -0.02218 242 TYR A N   
1676 C CA  . TYR A 208 ? 0.59893 0.68686 0.61364 -0.06952 0.03803  -0.02356 242 TYR A CA  
1677 C C   . TYR A 208 ? 0.50553 0.59354 0.52866 -0.06421 0.04864  -0.01937 242 TYR A C   
1678 O O   . TYR A 208 ? 0.55350 0.64042 0.56732 -0.05553 0.05583  -0.02543 242 TYR A O   
1679 C CB  . TYR A 208 ? 0.46463 0.56320 0.47168 -0.06854 0.03810  -0.01481 242 TYR A CB  
1680 C CG  . TYR A 208 ? 0.60026 0.70214 0.59133 -0.06141 0.04799  -0.00875 242 TYR A CG  
1681 C CD1 . TYR A 208 ? 0.60475 0.70611 0.56834 -0.05418 0.04831  -0.01490 242 TYR A CD1 
1682 C CD2 . TYR A 208 ? 0.46446 0.57067 0.46724 -0.06282 0.05676  0.00373  242 TYR A CD2 
1683 C CE1 . TYR A 208 ? 0.59941 0.70581 0.54531 -0.04784 0.06048  -0.00603 242 TYR A CE1 
1684 C CE2 . TYR A 208 ? 0.49005 0.60109 0.48213 -0.05910 0.06804  0.01279  242 TYR A CE2 
1685 C CZ  . TYR A 208 ? 0.59118 0.70300 0.55365 -0.05130 0.07150  0.00930  242 TYR A CZ  
1686 O OH  . TYR A 208 ? 0.51401 0.63246 0.46281 -0.04770 0.08577  0.02140  242 TYR A OH  
1687 N N   . PHE A 209 ? 0.52390 0.61564 0.56507 -0.06818 0.04923  -0.01018 243 PHE A N   
1688 C CA  . PHE A 209 ? 0.50195 0.59825 0.55760 -0.06363 0.05583  -0.00624 243 PHE A CA  
1689 C C   . PHE A 209 ? 0.49035 0.57461 0.55126 -0.05782 0.05455  -0.01354 243 PHE A C   
1690 O O   . PHE A 209 ? 0.51594 0.60458 0.58321 -0.04802 0.06203  -0.01634 243 PHE A O   
1691 C CB  . PHE A 209 ? 0.48257 0.58465 0.55360 -0.06931 0.05207  0.00304  243 PHE A CB  
1692 C CG  . PHE A 209 ? 0.49539 0.60499 0.56609 -0.07317 0.05381  0.00967  243 PHE A CG  
1693 C CD1 . PHE A 209 ? 0.39002 0.50397 0.45128 -0.07088 0.06177  0.01240  243 PHE A CD1 
1694 C CD2 . PHE A 209 ? 0.39861 0.50811 0.47597 -0.07830 0.04732  0.01337  243 PHE A CD2 
1695 C CE1 . PHE A 209 ? 0.41958 0.53463 0.48134 -0.07501 0.06271  0.02116  243 PHE A CE1 
1696 C CE2 . PHE A 209 ? 0.32491 0.43471 0.40315 -0.08139 0.04728  0.01811  243 PHE A CE2 
1697 C CZ  . PHE A 209 ? 0.48078 0.59185 0.55294 -0.08043 0.05473  0.02325  243 PHE A CZ  
1698 N N   . LEU A 210 ? 0.51816 0.58714 0.57868 -0.06336 0.04581  -0.01589 244 LEU A N   
1699 C CA  . LEU A 210 ? 0.48999 0.54049 0.55729 -0.05872 0.04272  -0.01976 244 LEU A CA  
1700 C C   . LEU A 210 ? 0.48876 0.52578 0.54445 -0.05022 0.04428  -0.03590 244 LEU A C   
1701 O O   . LEU A 210 ? 0.55456 0.58290 0.61598 -0.03798 0.04742  -0.04161 244 LEU A O   
1702 C CB  . LEU A 210 ? 0.53001 0.56673 0.60064 -0.06980 0.03434  -0.01391 244 LEU A CB  
1703 C CG  . LEU A 210 ? 0.59741 0.64296 0.67465 -0.07434 0.03275  0.00063  244 LEU A CG  
1704 C CD1 . LEU A 210 ? 0.58655 0.62468 0.66255 -0.08643 0.02898  0.00730  244 LEU A CD1 
1705 C CD2 . LEU A 210 ? 0.46207 0.50341 0.54955 -0.06481 0.03113  0.00638  244 LEU A CD2 
1706 N N   . ARG A 211 ? 0.63027 0.66564 0.66906 -0.05472 0.04083  -0.04492 245 ARG A N   
1707 C CA  . ARG A 211 ? 0.82990 0.84996 0.85171 -0.04692 0.03900  -0.06386 245 ARG A CA  
1708 C C   . ARG A 211 ? 0.62817 0.66385 0.63160 -0.03324 0.05141  -0.06933 245 ARG A C   
1709 O O   . ARG A 211 ? 0.85945 0.88430 0.84900 -0.02029 0.05467  -0.08564 245 ARG A O   
1710 C CB  . ARG A 211 ? 0.60454 0.61745 0.61666 -0.05845 0.02610  -0.07241 245 ARG A CB  
1711 C CG  . ARG A 211 ? 0.63410 0.63185 0.66584 -0.07366 0.01583  -0.06783 245 ARG A CG  
1712 C CD  . ARG A 211 ? 0.76451 0.77020 0.79580 -0.08695 0.00464  -0.07222 245 ARG A CD  
1713 N NE  . ARG A 211 ? 0.77905 0.78258 0.78645 -0.08028 -0.00201 -0.09137 245 ARG A NE  
1714 C CZ  . ARG A 211 ? 0.73005 0.71371 0.73423 -0.08536 -0.01615 -0.10991 245 ARG A CZ  
1715 N NH1 . ARG A 211 ? 0.80196 0.76519 0.82975 -0.09970 -0.02444 -0.10984 245 ARG A NH1 
1716 N NH2 . ARG A 211 ? 0.69642 0.67957 0.67180 -0.07653 -0.02284 -0.12857 245 ARG A NH2 
1717 N N   . GLY A 212 ? 0.54799 0.60743 0.55005 -0.03551 0.05917  -0.05590 246 GLY A N   
1718 C CA  . GLY A 212 ? 0.54244 0.61748 0.52414 -0.02601 0.07198  -0.05633 246 GLY A CA  
1719 C C   . GLY A 212 ? 0.64629 0.72182 0.59713 -0.02798 0.06564  -0.06043 246 GLY A C   
1720 O O   . GLY A 212 ? 0.69874 0.78862 0.63068 -0.02309 0.07593  -0.05291 246 GLY A O   
1721 N N   . GLN A 213 ? 0.68792 0.74941 0.63476 -0.03542 0.04845  -0.07058 247 GLN A N   
1722 C CA  . GLN A 213 ? 0.61850 0.68378 0.54107 -0.03744 0.03768  -0.07442 247 GLN A CA  
1723 C C   . GLN A 213 ? 0.68075 0.74003 0.62176 -0.05147 0.01951  -0.07792 247 GLN A C   
1724 O O   . GLN A 213 ? 0.74371 0.79093 0.70889 -0.05902 0.01643  -0.07937 247 GLN A O   
1725 C CB  . GLN A 213 ? 0.61440 0.67234 0.49883 -0.02484 0.03637  -0.09391 247 GLN A CB  
1726 C CG  . GLN A 213 ? 0.95350 0.98706 0.83843 -0.02691 0.02069  -0.11797 247 GLN A CG  
1727 C CD  . GLN A 213 ? 1.14812 1.17522 0.99155 -0.01862 0.00923  -0.13962 247 GLN A CD  
1728 O OE1 . GLN A 213 ? 1.02164 1.06023 0.82862 -0.00522 0.01941  -0.13870 247 GLN A OE1 
1729 N NE2 . GLN A 213 ? 0.95071 0.95966 0.79880 -0.02739 -0.01263 -0.15873 247 GLN A NE2 
1730 N N   . LEU A 214 ? 0.79339 0.86307 0.72398 -0.05449 0.00798  -0.07744 248 LEU A N   
1731 C CA  . LEU A 214 ? 0.66112 0.73295 0.61125 -0.06723 -0.00930 -0.08215 248 LEU A CA  
1732 C C   . LEU A 214 ? 0.68037 0.74628 0.60936 -0.06594 -0.02718 -0.10317 248 LEU A C   
1733 O O   . LEU A 214 ? 0.67582 0.74376 0.56762 -0.05346 -0.02760 -0.10877 248 LEU A O   
1734 C CB  . LEU A 214 ? 0.49966 0.59275 0.46246 -0.07073 -0.01149 -0.06632 248 LEU A CB  
1735 C CG  . LEU A 214 ? 0.50603 0.60339 0.49109 -0.07390 0.00165  -0.04934 248 LEU A CG  
1736 C CD1 . LEU A 214 ? 0.56620 0.67973 0.55556 -0.07199 0.00029  -0.03681 248 LEU A CD1 
1737 C CD2 . LEU A 214 ? 0.43708 0.52922 0.45070 -0.08590 0.00053  -0.04979 248 LEU A CD2 
1738 N N   . PRO A 215 ? 0.62929 0.68779 0.58036 -0.07937 -0.04272 -0.11493 249 PRO A N   
1739 C CA  . PRO A 215 ? 0.68339 0.73329 0.61669 -0.07987 -0.06354 -0.13896 249 PRO A CA  
1740 C C   . PRO A 215 ? 0.76335 0.83701 0.68030 -0.07601 -0.07902 -0.13948 249 PRO A C   
1741 O O   . PRO A 215 ? 0.95585 1.02455 0.85016 -0.07365 -0.09842 -0.16041 249 PRO A O   
1742 C CB  . PRO A 215 ? 0.66872 0.70723 0.64174 -0.10014 -0.07558 -0.14580 249 PRO A CB  
1743 C CG  . PRO A 215 ? 0.60271 0.65852 0.61148 -0.10985 -0.06350 -0.12146 249 PRO A CG  
1744 C CD  . PRO A 215 ? 0.61795 0.67491 0.61061 -0.09568 -0.04195 -0.10637 249 PRO A CD  
1745 N N   . TRP A 216 ? 0.65544 0.75268 0.58187 -0.07395 -0.07319 -0.11839 250 TRP A N   
1746 C CA  . TRP A 216 ? 0.76982 0.88811 0.68023 -0.06665 -0.08807 -0.11570 250 TRP A CA  
1747 C C   . TRP A 216 ? 0.80600 0.92339 0.67229 -0.04857 -0.07559 -0.10310 250 TRP A C   
1748 O O   . TRP A 216 ? 0.86457 0.99713 0.71959 -0.04089 -0.08329 -0.09171 250 TRP A O   
1749 C CB  . TRP A 216 ? 0.70606 0.85065 0.65895 -0.07467 -0.09251 -0.10171 250 TRP A CB  
1750 C CG  . TRP A 216 ? 0.54513 0.69001 0.52083 -0.07711 -0.07032 -0.08262 250 TRP A CG  
1751 C CD1 . TRP A 216 ? 0.53859 0.68345 0.50123 -0.06649 -0.05561 -0.06505 250 TRP A CD1 
1752 C CD2 . TRP A 216 ? 0.51361 0.65763 0.52740 -0.09149 -0.06196 -0.07930 250 TRP A CD2 
1753 N NE1 . TRP A 216 ? 0.51673 0.66109 0.50633 -0.07279 -0.04064 -0.05429 250 TRP A NE1 
1754 C CE2 . TRP A 216 ? 0.43385 0.57861 0.45223 -0.08707 -0.04354 -0.06185 250 TRP A CE2 
1755 C CE3 . TRP A 216 ? 0.61046 0.75147 0.65383 -0.10843 -0.06864 -0.08831 250 TRP A CE3 
1756 C CZ2 . TRP A 216 ? 0.45496 0.59949 0.50082 -0.09666 -0.03221 -0.05414 250 TRP A CZ2 
1757 C CZ3 . TRP A 216 ? 0.44919 0.58926 0.52116 -0.11886 -0.05500 -0.07695 250 TRP A CZ3 
1758 C CH2 . TRP A 216 ? 0.62404 0.76682 0.69433 -0.11181 -0.03722 -0.06052 250 TRP A CH2 
1759 N N   . GLN A 217 ? 0.84284 0.94365 0.68640 -0.04145 -0.05615 -0.10343 251 GLN A N   
1760 C CA  . GLN A 217 ? 0.90763 1.00910 0.70946 -0.02625 -0.04175 -0.09103 251 GLN A CA  
1761 C C   . GLN A 217 ? 1.00783 1.10322 0.75689 -0.01388 -0.05136 -0.10978 251 GLN A C   
1762 O O   . GLN A 217 ? 0.97206 1.05537 0.71716 -0.01627 -0.06435 -0.13604 251 GLN A O   
1763 C CB  . GLN A 217 ? 0.68822 0.78251 0.49732 -0.02459 -0.01390 -0.08056 251 GLN A CB  
1764 C CG  . GLN A 217 ? 0.86607 0.96571 0.71774 -0.03429 -0.00436 -0.06159 251 GLN A CG  
1765 C CD  . GLN A 217 ? 0.68296 0.78008 0.53989 -0.03171 0.02006  -0.05012 251 GLN A CD  
1766 O OE1 . GLN A 217 ? 0.76083 0.85496 0.65044 -0.03898 0.02627  -0.04817 251 GLN A OE1 
1767 N NE2 . GLN A 217 ? 0.80458 0.90530 0.62999 -0.02147 0.03383  -0.04126 251 GLN A NE2 
1768 N N   . GLY A 218 ? 1.02716 1.12875 0.73298 -0.00036 -0.04508 -0.09582 252 GLY A N   
1769 C CA  . GLY A 218 ? 0.89485 0.99262 0.54060 0.01417  -0.05251 -0.11154 252 GLY A CA  
1770 C C   . GLY A 218 ? 1.09677 1.19811 0.73182 0.01313  -0.08836 -0.13213 252 GLY A C   
1771 O O   . GLY A 218 ? 1.13577 1.22903 0.72581 0.02260  -0.09995 -0.15613 252 GLY A O   
1772 N N   . LEU A 219 ? 1.11927 1.23456 0.79598 0.00242  -0.10689 -0.12497 253 LEU A N   
1773 C CA  . LEU A 219 ? 0.96384 1.09000 0.64059 0.00002  -0.14298 -0.14291 253 LEU A CA  
1774 C C   . LEU A 219 ? 1.06490 1.20231 0.69085 0.01743  -0.15620 -0.13092 253 LEU A C   
1775 O O   . LEU A 219 ? 1.10013 1.24329 0.72295 0.02428  -0.14356 -0.10078 253 LEU A O   
1776 C CB  . LEU A 219 ? 0.80387 0.94723 0.55031 -0.01724 -0.15497 -0.13863 253 LEU A CB  
1777 C CG  . LEU A 219 ? 0.79492 0.93115 0.58598 -0.03700 -0.16349 -0.16104 253 LEU A CG  
1778 C CD1 . LEU A 219 ? 1.02040 1.12768 0.80340 -0.03816 -0.14014 -0.16900 253 LEU A CD1 
1779 C CD2 . LEU A 219 ? 0.86648 1.02323 0.72507 -0.05278 -0.16324 -0.14767 253 LEU A CD2 
1780 N N   . LYS A 220 ? 0.89252 1.03033 0.47720 0.02483  -0.18317 -0.15445 254 LYS A N   
1781 C CA  . LYS A 220 ? 1.08753 1.23423 0.61334 0.04366  -0.19880 -0.14474 254 LYS A CA  
1782 C C   . LYS A 220 ? 1.17903 1.35047 0.73342 0.04093  -0.23791 -0.14786 254 LYS A C   
1783 O O   . LYS A 220 ? 1.17440 1.35575 0.78153 0.02419  -0.25783 -0.16868 254 LYS A O   
1784 C CB  . LYS A 220 ? 1.27856 1.41143 0.72893 0.05781  -0.20420 -0.16965 254 LYS A CB  
1785 C CG  . LYS A 220 ? 1.27462 1.38734 0.70413 0.06138  -0.16708 -0.17406 254 LYS A CG  
1786 C CD  . LYS A 220 ? 1.46827 1.56456 0.85064 0.06921  -0.17903 -0.21497 254 LYS A CD  
1787 C CE  . LYS A 220 ? 1.42037 1.51092 0.85107 0.05059  -0.21285 -0.24701 254 LYS A CE  
1788 N NZ  . LYS A 220 ? 1.40770 1.49670 0.91936 0.02915  -0.20194 -0.24151 254 LYS A NZ  
1789 N N   . ALA A 221 ? 1.18248 1.36479 0.70344 0.05773  -0.24859 -0.12533 255 ALA A N   
1790 C CA  . ALA A 221 ? 1.14002 1.34959 0.68325 0.06102  -0.28700 -0.12523 255 ALA A CA  
1791 C C   . ALA A 221 ? 1.11289 1.32175 0.59286 0.08460  -0.29526 -0.10044 255 ALA A C   
1792 O O   . ALA A 221 ? 1.24166 1.43371 0.67851 0.09573  -0.26674 -0.07428 255 ALA A O   
1793 C CB  . ALA A 221 ? 0.99990 1.22808 0.62739 0.04899  -0.28253 -0.11027 255 ALA A CB  
1794 N N   . PRO A 222 ? 1.18551 1.40780 0.66687 0.08845  -0.32869 -0.10315 256 PRO A N   
1795 C CA  . PRO A 222 ? 1.20069 1.41613 0.62615 0.10819  -0.33347 -0.07533 256 PRO A CA  
1796 C C   . PRO A 222 ? 1.20902 1.42587 0.64744 0.12042  -0.32186 -0.03651 256 PRO A C   
1797 O O   . PRO A 222 ? 1.24871 1.44556 0.63316 0.13401  -0.30637 -0.00678 256 PRO A O   
1798 C CB  . PRO A 222 ? 1.11700 1.35306 0.55644 0.10717  -0.37550 -0.09041 256 PRO A CB  
1799 C CG  . PRO A 222 ? 1.05553 1.31686 0.58021 0.08780  -0.39014 -0.11303 256 PRO A CG  
1800 C CD  . PRO A 222 ? 1.01200 1.25684 0.54652 0.07387  -0.36262 -0.12956 256 PRO A CD  
1801 N N   . THR A 223 ? 1.13399 1.37278 0.64397 0.11543  -0.32775 -0.03533 257 THR A N   
1802 C CA  . THR A 223 ? 1.13327 1.36914 0.66507 0.12605  -0.31572 -0.00091 257 THR A CA  
1803 C C   . THR A 223 ? 1.10671 1.33164 0.69436 0.10665  -0.27851 0.00089  257 THR A C   
1804 O O   . THR A 223 ? 1.20110 1.42623 0.81019 0.08803  -0.26694 -0.02343 257 THR A O   
1805 C CB  . THR A 223 ? 0.94935 1.21568 0.53031 0.13604  -0.34967 0.00288  257 THR A CB  
1806 O OG1 . THR A 223 ? 0.88313 1.17816 0.54838 0.11797  -0.35285 -0.01915 257 THR A OG1 
1807 C CG2 . THR A 223 ? 1.01745 1.29099 0.57142 0.14040  -0.38102 -0.00568 257 THR A CG2 
1808 N N   . ASN A 224 ? 1.05007 1.26286 0.65989 0.11213  -0.26165 0.02995  258 ASN A N   
1809 C CA  . ASN A 224 ? 0.99688 1.20070 0.65943 0.09572  -0.23045 0.03178  258 ASN A CA  
1810 C C   . ASN A 224 ? 1.00491 1.23941 0.74632 0.08682  -0.24223 0.01535  258 ASN A C   
1811 O O   . ASN A 224 ? 0.96514 1.20022 0.74786 0.06865  -0.22211 0.00432  258 ASN A O   
1812 C CB  . ASN A 224 ? 1.00902 1.18410 0.66321 0.10384  -0.20847 0.06672  258 ASN A CB  
1813 C CG  . ASN A 224 ? 1.25914 1.41260 0.92401 0.08703  -0.17014 0.07048  258 ASN A CG  
1814 O OD1 . ASN A 224 ? 1.32757 1.48888 1.01496 0.07063  -0.15984 0.04767  258 ASN A OD1 
1815 N ND2 . ASN A 224 ? 1.36976 1.49513 1.02057 0.09074  -0.15045 0.10002  258 ASN A ND2 
1816 N N   . LYS A 225 ? 1.01975 1.28244 0.78363 0.09995  -0.27395 0.01461  259 LYS A N   
1817 C CA  . LYS A 225 ? 1.06265 1.36213 0.90513 0.09178  -0.28306 -0.00029 259 LYS A CA  
1818 C C   . LYS A 225 ? 1.00251 1.32191 0.86859 0.06897  -0.29017 -0.03159 259 LYS A C   
1819 O O   . LYS A 225 ? 0.94898 1.28205 0.87190 0.05130  -0.27647 -0.04170 259 LYS A O   
1820 C CB  . LYS A 225 ? 0.94285 1.27312 0.80674 0.11320  -0.31659 0.00599  259 LYS A CB  
1821 C CG  . LYS A 225 ? 1.16594 1.46846 0.97813 0.13943  -0.32153 0.03652  259 LYS A CG  
1822 C CD  . LYS A 225 ? 0.98436 1.31747 0.80646 0.16332  -0.36195 0.04077  259 LYS A CD  
1823 C CE  . LYS A 225 ? 1.08657 1.38920 0.82962 0.18632  -0.37437 0.06731  259 LYS A CE  
1824 N NZ  . LYS A 225 ? 1.15218 1.45735 0.91154 0.21443  -0.39350 0.09025  259 LYS A NZ  
1825 N N   . GLN A 226 ? 1.00456 1.32290 0.82486 0.06918  -0.31166 -0.04710 260 GLN A N   
1826 C CA  . GLN A 226 ? 0.84444 1.17207 0.68245 0.04711  -0.31974 -0.07836 260 GLN A CA  
1827 C C   . GLN A 226 ? 0.92162 1.21557 0.74555 0.03139  -0.28499 -0.08320 260 GLN A C   
1828 O O   . GLN A 226 ? 0.84613 1.14379 0.70445 0.01036  -0.28334 -0.10421 260 GLN A O   
1829 C CB  . GLN A 226 ? 0.82843 1.16125 0.61701 0.05412  -0.35566 -0.09700 260 GLN A CB  
1830 C CG  . GLN A 226 ? 0.87831 1.24172 0.67748 0.07065  -0.39121 -0.08994 260 GLN A CG  
1831 C CD  . GLN A 226 ? 0.93657 1.28854 0.68265 0.07314  -0.41481 -0.10052 260 GLN A CD  
1832 O OE1 . GLN A 226 ? 1.01352 1.35234 0.74318 0.05741  -0.41746 -0.12598 260 GLN A OE1 
1833 N NE2 . GLN A 226 ? 0.95254 1.30805 0.67074 0.09364  -0.43229 -0.08112 260 GLN A NE2 
1834 N N   . LYS A 227 ? 0.97856 1.24043 0.75592 0.04085  -0.25788 -0.06304 261 LYS A N   
1835 C CA  . LYS A 227 ? 0.93098 1.16600 0.70272 0.02782  -0.22456 -0.06574 261 LYS A CA  
1836 C C   . LYS A 227 ? 0.84416 1.08483 0.68102 0.01386  -0.20408 -0.06008 261 LYS A C   
1837 O O   . LYS A 227 ? 0.71923 0.95316 0.57912 -0.00350 -0.19094 -0.07346 261 LYS A O   
1838 C CB  . LYS A 227 ? 1.09467 1.30076 0.80553 0.04078  -0.20132 -0.04415 261 LYS A CB  
1839 C CG  . LYS A 227 ? 0.95199 1.13571 0.66479 0.02952  -0.16582 -0.04315 261 LYS A CG  
1840 C CD  . LYS A 227 ? 1.07612 1.23811 0.73083 0.04097  -0.14353 -0.02273 261 LYS A CD  
1841 C CE  . LYS A 227 ? 1.05021 1.19714 0.72710 0.03108  -0.10841 -0.01099 261 LYS A CE  
1842 N NZ  . LYS A 227 ? 1.19290 1.34041 0.91424 0.02858  -0.10286 0.00883  261 LYS A NZ  
1843 N N   . TYR A 228 ? 0.82393 1.07503 0.68828 0.02281  -0.20165 -0.04061 262 TYR A N   
1844 C CA  . TYR A 228 ? 0.76391 1.02487 0.68761 0.01199  -0.18498 -0.03801 262 TYR A CA  
1845 C C   . TYR A 228 ? 0.75010 1.04353 0.72804 -0.00422 -0.19929 -0.05819 262 TYR A C   
1846 O O   . TYR A 228 ? 0.75763 1.05413 0.77467 -0.01993 -0.18195 -0.06136 262 TYR A O   
1847 C CB  . TYR A 228 ? 0.80719 1.07345 0.74821 0.02831  -0.18344 -0.01746 262 TYR A CB  
1848 C CG  . TYR A 228 ? 0.90828 1.13819 0.81286 0.03778  -0.16272 0.00537  262 TYR A CG  
1849 C CD1 . TYR A 228 ? 1.08500 1.28865 0.93202 0.03942  -0.15468 0.01186  262 TYR A CD1 
1850 C CD2 . TYR A 228 ? 1.03520 1.25770 0.96485 0.04461  -0.15071 0.01976  262 TYR A CD2 
1851 C CE1 . TYR A 228 ? 1.14073 1.31452 0.96123 0.04484  -0.13474 0.03487  262 TYR A CE1 
1852 C CE2 . TYR A 228 ? 1.10061 1.28788 1.00226 0.05008  -0.13383 0.04027  262 TYR A CE2 
1853 C CZ  . TYR A 228 ? 1.19544 1.35980 1.04510 0.04874  -0.12559 0.04917  262 TYR A CZ  
1854 O OH  . TYR A 228 ? 1.33453 1.46693 1.16238 0.05109  -0.10772 0.07171  262 TYR A OH  
1855 N N   . GLU A 229 ? 0.64565 0.96416 0.62697 -0.00152 -0.23148 -0.07089 263 GLU A N   
1856 C CA  . GLU A 229 ? 0.69353 1.04490 0.73127 -0.02025 -0.24692 -0.08979 263 GLU A CA  
1857 C C   . GLU A 229 ? 0.79647 1.12521 0.82701 -0.04189 -0.24073 -0.10854 263 GLU A C   
1858 O O   . GLU A 229 ? 0.73248 1.07030 0.81194 -0.06247 -0.23155 -0.11420 263 GLU A O   
1859 C CB  . GLU A 229 ? 0.67296 1.05817 0.71746 -0.01180 -0.28680 -0.09953 263 GLU A CB  
1860 C CG  . GLU A 229 ? 0.89703 1.31400 0.99546 -0.03492 -0.30785 -0.12243 263 GLU A CG  
1861 C CD  . GLU A 229 ? 1.02080 1.48083 1.13927 -0.02615 -0.34914 -0.13076 263 GLU A CD  
1862 O OE1 . GLU A 229 ? 1.06113 1.50907 1.12726 -0.01746 -0.37530 -0.14161 263 GLU A OE1 
1863 O OE2 . GLU A 229 ? 1.03533 1.54253 1.22109 -0.02668 -0.35488 -0.12618 263 GLU A OE2 
1864 N N   . LYS A 230 ? 0.78613 1.08432 0.75471 -0.03629 -0.24493 -0.11772 264 LYS A N   
1865 C CA  . LYS A 230 ? 0.66566 0.93714 0.62402 -0.05258 -0.23912 -0.13729 264 LYS A CA  
1866 C C   . LYS A 230 ? 0.73035 0.98153 0.70662 -0.06237 -0.20389 -0.12641 264 LYS A C   
1867 O O   . LYS A 230 ? 0.82787 1.07064 0.83346 -0.08174 -0.19932 -0.13751 264 LYS A O   
1868 C CB  . LYS A 230 ? 0.70490 0.94797 0.58758 -0.03903 -0.24473 -0.14801 264 LYS A CB  
1869 C CG  . LYS A 230 ? 0.74663 0.99906 0.61030 -0.03877 -0.28357 -0.17411 264 LYS A CG  
1870 C CD  . LYS A 230 ? 0.83343 1.05183 0.62181 -0.02801 -0.28222 -0.19024 264 LYS A CD  
1871 C CE  . LYS A 230 ? 0.99988 1.22364 0.76284 -0.02720 -0.32314 -0.22076 264 LYS A CE  
1872 N NZ  . LYS A 230 ? 1.12023 1.30943 0.80778 -0.01551 -0.31941 -0.24066 264 LYS A NZ  
1873 N N   . ILE A 231 ? 0.76137 1.00276 0.72041 -0.04955 -0.18042 -0.10415 265 ILE A N   
1874 C CA  . ILE A 231 ? 0.66136 0.88542 0.63537 -0.05729 -0.14989 -0.09398 265 ILE A CA  
1875 C C   . ILE A 231 ? 0.66134 0.90875 0.69838 -0.07231 -0.14550 -0.09081 265 ILE A C   
1876 O O   . ILE A 231 ? 0.76285 0.99889 0.82053 -0.08767 -0.13203 -0.09347 265 ILE A O   
1877 C CB  . ILE A 231 ? 0.66984 0.88043 0.61538 -0.04164 -0.12983 -0.07184 265 ILE A CB  
1878 C CG1 . ILE A 231 ? 0.66247 0.85185 0.54530 -0.02887 -0.12890 -0.07250 265 ILE A CG1 
1879 C CG2 . ILE A 231 ? 0.65886 0.85581 0.62371 -0.04964 -0.10244 -0.06251 265 ILE A CG2 
1880 C CD1 . ILE A 231 ? 0.76253 0.94007 0.61881 -0.01552 -0.11140 -0.04797 265 ILE A CD1 
1881 N N   . GLY A 232 ? 0.65672 0.93809 0.72460 -0.06673 -0.15610 -0.08416 266 GLY A N   
1882 C CA  . GLY A 232 ? 0.66605 0.97641 0.79382 -0.07939 -0.14958 -0.08100 266 GLY A CA  
1883 C C   . GLY A 232 ? 0.65332 0.97646 0.81777 -0.10285 -0.16236 -0.09663 266 GLY A C   
1884 O O   . GLY A 232 ? 0.57457 0.90703 0.77939 -0.11949 -0.14830 -0.09253 266 GLY A O   
1885 N N   . ASP A 233 ? 0.56465 0.88682 0.71427 -0.10514 -0.18964 -0.11440 267 ASP A N   
1886 C CA  . ASP A 233 ? 0.58619 0.91470 0.77143 -0.12977 -0.20531 -0.13164 267 ASP A CA  
1887 C C   . ASP A 233 ? 0.76963 1.05442 0.94147 -0.14391 -0.18944 -0.13675 267 ASP A C   
1888 O O   . ASP A 233 ? 0.64746 0.93356 0.86186 -0.16731 -0.18708 -0.13892 267 ASP A O   
1889 C CB  . ASP A 233 ? 0.66902 1.00487 0.83713 -0.12699 -0.24234 -0.15269 267 ASP A CB  
1890 C CG  . ASP A 233 ? 0.89214 1.27989 1.09338 -0.11824 -0.26419 -0.14932 267 ASP A CG  
1891 O OD1 . ASP A 233 ? 0.90610 1.33085 1.16454 -0.12367 -0.25331 -0.13673 267 ASP A OD1 
1892 O OD2 . ASP A 233 ? 0.78010 1.17320 0.94943 -0.10430 -0.29229 -0.15928 267 ASP A OD2 
1893 N N   . LYS A 234 ? 0.66838 0.91493 0.78337 -0.12964 -0.17811 -0.13733 268 LYS A N   
1894 C CA  . LYS A 234 ? 0.56570 0.77203 0.66937 -0.13842 -0.16212 -0.14106 268 LYS A CA  
1895 C C   . LYS A 234 ? 0.64851 0.85685 0.78329 -0.14663 -0.13510 -0.12058 268 LYS A C   
1896 O O   . LYS A 234 ? 0.64581 0.83141 0.79513 -0.16158 -0.12690 -0.12137 268 LYS A O   
1897 C CB  . LYS A 234 ? 0.65165 0.82573 0.69211 -0.11866 -0.15339 -0.14467 268 LYS A CB  
1898 C CG  . LYS A 234 ? 0.85243 0.98650 0.88078 -0.12279 -0.13788 -0.15016 268 LYS A CG  
1899 C CD  . LYS A 234 ? 0.59722 0.70542 0.61457 -0.13022 -0.15843 -0.17871 268 LYS A CD  
1900 C CE  . LYS A 234 ? 0.94035 1.04212 0.89909 -0.11063 -0.17150 -0.19566 268 LYS A CE  
1901 N NZ  . LYS A 234 ? 0.98326 1.05432 0.92367 -0.11460 -0.19096 -0.22787 268 LYS A NZ  
1902 N N   . LYS A 235 ? 0.58650 0.81960 0.72970 -0.13607 -0.12232 -0.10253 269 LYS A N   
1903 C CA  . LYS A 235 ? 0.65539 0.88982 0.81912 -0.14079 -0.09718 -0.08491 269 LYS A CA  
1904 C C   . LYS A 235 ? 0.63338 0.89154 0.85174 -0.16302 -0.09642 -0.08147 269 LYS A C   
1905 O O   . LYS A 235 ? 0.90627 1.15012 1.13597 -0.17471 -0.07981 -0.07206 269 LYS A O   
1906 C CB  . LYS A 235 ? 0.65670 0.90787 0.81256 -0.12234 -0.08589 -0.07036 269 LYS A CB  
1907 C CG  . LYS A 235 ? 0.71322 0.93686 0.81923 -0.10459 -0.07930 -0.06723 269 LYS A CG  
1908 C CD  . LYS A 235 ? 0.50366 0.73795 0.60495 -0.08846 -0.07061 -0.05303 269 LYS A CD  
1909 C CE  . LYS A 235 ? 0.64091 0.84772 0.69751 -0.07505 -0.06314 -0.04737 269 LYS A CE  
1910 N NZ  . LYS A 235 ? 0.50431 0.71435 0.55648 -0.06079 -0.05723 -0.03359 269 LYS A NZ  
1911 N N   . ARG A 236 ? 0.72073 1.01737 0.97474 -0.16920 -0.11410 -0.08723 270 ARG A N   
1912 C CA  . ARG A 236 ? 0.85147 1.17595 1.16371 -0.19337 -0.11318 -0.08338 270 ARG A CA  
1913 C C   . ARG A 236 ? 0.80207 1.09610 1.12356 -0.21702 -0.12453 -0.09511 270 ARG A C   
1914 O O   . ARG A 236 ? 0.81888 1.11364 1.17624 -0.23905 -0.11370 -0.08517 270 ARG A O   
1915 C CB  . ARG A 236 ? 0.70398 1.08351 1.05871 -0.19328 -0.13080 -0.08737 270 ARG A CB  
1916 C CG  . ARG A 236 ? 0.77598 1.17743 1.11336 -0.16482 -0.13254 -0.08326 270 ARG A CG  
1917 C CD  . ARG A 236 ? 0.82924 1.28390 1.21011 -0.16383 -0.15679 -0.09026 270 ARG A CD  
1918 N NE  . ARG A 236 ? 1.08046 1.52929 1.46214 -0.17671 -0.18863 -0.11021 270 ARG A NE  
1919 C CZ  . ARG A 236 ? 1.17491 1.63984 1.60613 -0.20474 -0.20025 -0.11786 270 ARG A CZ  
1920 N NH1 . ARG A 236 ? 1.24957 1.73029 1.72781 -0.22105 -0.17888 -0.10044 270 ARG A NH1 
1921 N NH2 . ARG A 236 ? 1.08365 1.53019 1.50220 -0.21197 -0.23047 -0.13508 270 ARG A NH2 
1922 N N   . THR A 237 ? 0.67858 0.94418 0.96685 -0.21241 -0.14619 -0.11603 271 THR A N   
1923 C CA  . THR A 237 ? 0.70450 0.93479 0.99887 -0.23259 -0.15997 -0.13178 271 THR A CA  
1924 C C   . THR A 237 ? 0.83440 1.01631 1.10810 -0.23435 -0.13889 -0.12337 271 THR A C   
1925 O O   . THR A 237 ? 0.93151 1.08870 1.22956 -0.25627 -0.14074 -0.12432 271 THR A O   
1926 C CB  . THR A 237 ? 0.72453 0.93707 0.98105 -0.22271 -0.18875 -0.15958 271 THR A CB  
1927 O OG1 . THR A 237 ? 0.81783 1.07695 1.09823 -0.22272 -0.21300 -0.16710 271 THR A OG1 
1928 C CG2 . THR A 237 ? 1.05908 1.22726 1.31708 -0.24090 -0.20421 -0.18043 271 THR A CG2 
1929 N N   . THR A 238 ? 0.79660 0.96483 1.02909 -0.21209 -0.11981 -0.11386 272 THR A N   
1930 C CA  . THR A 238 ? 0.80475 0.93046 1.01660 -0.20974 -0.10236 -0.10677 272 THR A CA  
1931 C C   . THR A 238 ? 0.74628 0.88524 0.98463 -0.21864 -0.07927 -0.08043 272 THR A C   
1932 O O   . THR A 238 ? 0.64833 0.81396 0.88135 -0.20589 -0.06494 -0.06702 272 THR A O   
1933 C CB  . THR A 238 ? 0.66926 0.77836 0.82883 -0.18304 -0.09380 -0.10939 272 THR A CB  
1934 O OG1 . THR A 238 ? 0.71866 0.81799 0.84753 -0.17332 -0.11325 -0.13280 272 THR A OG1 
1935 C CG2 . THR A 238 ? 0.69637 0.76591 0.84024 -0.17931 -0.07820 -0.10354 272 THR A CG2 
1936 N N   . PRO A 239 ? 0.81354 0.93277 1.07755 -0.23942 -0.07517 -0.07211 273 PRO A N   
1937 C CA  . PRO A 239 ? 0.60074 0.72974 0.87968 -0.24561 -0.05164 -0.04525 273 PRO A CA  
1938 C C   . PRO A 239 ? 0.67932 0.78281 0.91818 -0.22563 -0.03607 -0.03663 273 PRO A C   
1939 O O   . PRO A 239 ? 0.75638 0.82797 0.96353 -0.21163 -0.04159 -0.04961 273 PRO A O   
1940 C CB  . PRO A 239 ? 0.84028 0.94549 1.15207 -0.27357 -0.05442 -0.03858 273 PRO A CB  
1941 C CG  . PRO A 239 ? 0.55657 0.65273 0.88357 -0.28545 -0.08220 -0.06428 273 PRO A CG  
1942 C CD  . PRO A 239 ? 0.85881 0.94480 1.13954 -0.25916 -0.09303 -0.08639 273 PRO A CD  
1943 N N   . ALA A 240 ? 0.78068 0.90176 1.02223 -0.22397 -0.01634 -0.01505 274 ALA A N   
1944 C CA  . ALA A 240 ? 0.69296 0.79516 0.90084 -0.20630 -0.00384 -0.00655 274 ALA A CA  
1945 C C   . ALA A 240 ? 0.70123 0.75450 0.89846 -0.20871 -0.00534 -0.00431 274 ALA A C   
1946 O O   . ALA A 240 ? 0.76251 0.79501 0.93210 -0.19124 -0.00295 -0.00693 274 ALA A O   
1947 C CB  . ALA A 240 ? 0.60972 0.73950 0.82071 -0.20484 0.01494  0.01381  274 ALA A CB  
1948 N N   . VAL A 241 ? 0.76217 0.79666 0.98429 -0.23007 -0.00958 0.00112  275 VAL A N   
1949 C CA  . VAL A 241 ? 0.73338 0.71526 0.94742 -0.23130 -0.01333 0.00284  275 VAL A CA  
1950 C C   . VAL A 241 ? 0.79148 0.74403 0.98665 -0.21813 -0.02867 -0.02509 275 VAL A C   
1951 O O   . VAL A 241 ? 0.80622 0.72359 0.98146 -0.20366 -0.02810 -0.02784 275 VAL A O   
1952 C CB  . VAL A 241 ? 0.85261 0.81821 1.10064 -0.25984 -0.01497 0.01656  275 VAL A CB  
1953 C CG1 . VAL A 241 ? 1.03379 0.93747 1.27890 -0.26242 -0.02757 0.00826  275 VAL A CG1 
1954 C CG2 . VAL A 241 ? 0.67021 0.65094 0.92209 -0.26669 0.00526  0.04939  275 VAL A CG2 
1955 N N   . THR A 242 ? 0.73355 0.70249 0.93314 -0.22070 -0.04242 -0.04640 276 THR A N   
1956 C CA  . THR A 242 ? 0.78917 0.73421 0.96283 -0.20570 -0.05552 -0.07402 276 THR A CA  
1957 C C   . THR A 242 ? 0.94253 0.89799 1.08133 -0.17865 -0.04458 -0.07518 276 THR A C   
1958 O O   . THR A 242 ? 1.05637 0.98386 1.17223 -0.16224 -0.04461 -0.08713 276 THR A O   
1959 C CB  . THR A 242 ? 0.80927 0.77281 0.99197 -0.21448 -0.07476 -0.09527 276 THR A CB  
1960 O OG1 . THR A 242 ? 0.91926 0.87157 1.14064 -0.24251 -0.08666 -0.09548 276 THR A OG1 
1961 C CG2 . THR A 242 ? 0.63362 0.57385 0.78050 -0.19661 -0.08734 -0.12457 276 THR A CG2 
1962 N N   . LEU A 243 ? 0.80589 0.80156 0.94295 -0.17366 -0.03475 -0.06311 277 LEU A N   
1963 C CA  . LEU A 243 ? 0.81037 0.81509 0.92032 -0.15200 -0.02385 -0.06064 277 LEU A CA  
1964 C C   . LEU A 243 ? 0.79542 0.77826 0.90005 -0.14394 -0.01293 -0.04845 277 LEU A C   
1965 O O   . LEU A 243 ? 0.82795 0.80555 0.91337 -0.12616 -0.00758 -0.05293 277 LEU A O   
1966 C CB  . LEU A 243 ? 0.69077 0.73612 0.80414 -0.15019 -0.01670 -0.04894 277 LEU A CB  
1967 C CG  . LEU A 243 ? 0.76383 0.83452 0.87294 -0.14726 -0.02683 -0.06020 277 LEU A CG  
1968 C CD1 . LEU A 243 ? 0.65082 0.75667 0.76855 -0.14453 -0.01929 -0.04701 277 LEU A CD1 
1969 C CD2 . LEU A 243 ? 0.58183 0.64164 0.65672 -0.12969 -0.02897 -0.07338 277 LEU A CD2 
1970 N N   . CYS A 244 ? 0.70848 0.68067 0.83082 -0.15660 -0.00957 -0.03168 278 CYS A N   
1971 C CA  . CYS A 244 ? 0.65083 0.60584 0.76800 -0.14878 -0.00141 -0.01634 278 CYS A CA  
1972 C C   . CYS A 244 ? 0.71231 0.62093 0.83006 -0.14571 -0.00821 -0.02244 278 CYS A C   
1973 O O   . CYS A 244 ? 0.84187 0.73095 0.96105 -0.14286 -0.00481 -0.00632 278 CYS A O   
1974 C CB  . CYS A 244 ? 0.61000 0.57894 0.73894 -0.16158 0.00694  0.00807  278 CYS A CB  
1975 S SG  . CYS A 244 ? 0.70467 0.67178 0.81820 -0.14793 0.01622  0.02780  278 CYS A SG  
1976 N N   . ASP A 245 ? 0.85593 0.74485 0.97062 -0.14457 -0.01904 -0.04599 279 ASP A N   
1977 C CA  . ASP A 245 ? 1.05648 0.89633 1.17159 -0.13970 -0.02675 -0.05588 279 ASP A CA  
1978 C C   . ASP A 245 ? 0.87112 0.70256 0.97258 -0.11406 -0.01918 -0.05514 279 ASP A C   
1979 O O   . ASP A 245 ? 0.91808 0.77041 1.00350 -0.09697 -0.01352 -0.06715 279 ASP A O   
1980 C CB  . ASP A 245 ? 1.05173 0.87468 1.16065 -0.14085 -0.04088 -0.08650 279 ASP A CB  
1981 C CG  . ASP A 245 ? 1.23668 1.00791 1.33919 -0.12798 -0.04811 -0.10382 279 ASP A CG  
1982 O OD1 . ASP A 245 ? 1.34066 1.07242 1.46082 -0.13866 -0.05375 -0.09423 279 ASP A OD1 
1983 O OD2 . ASP A 245 ? 1.24562 1.01494 1.32487 -0.10601 -0.04703 -0.12611 279 ASP A OD2 
1984 N N   . GLY A 246 ? 0.93410 0.73676 1.04383 -0.11153 -0.01905 -0.03917 280 GLY A N   
1985 C CA  . GLY A 246 ? 0.84218 0.64018 0.94629 -0.08721 -0.01397 -0.03591 280 GLY A CA  
1986 C C   . GLY A 246 ? 0.75631 0.59279 0.85828 -0.08240 -0.00437 -0.01592 280 GLY A C   
1987 O O   . GLY A 246 ? 0.72628 0.56426 0.82882 -0.06351 -0.00199 -0.01169 280 GLY A O   
1988 N N   . LEU A 247 ? 0.74084 0.60879 0.84223 -0.09789 0.00000  -0.00512 281 LEU A N   
1989 C CA  . LEU A 247 ? 0.73020 0.63279 0.82705 -0.09436 0.00737  0.00977  281 LEU A CA  
1990 C C   . LEU A 247 ? 0.69639 0.59637 0.79466 -0.10675 0.00840  0.03508  281 LEU A C   
1991 O O   . LEU A 247 ? 0.77019 0.64910 0.87604 -0.12280 0.00611  0.04290  281 LEU A O   
1992 C CB  . LEU A 247 ? 0.65754 0.59726 0.74890 -0.09881 0.01233  0.00137  281 LEU A CB  
1993 C CG  . LEU A 247 ? 0.52955 0.47692 0.61287 -0.08642 0.01370  -0.01960 281 LEU A CG  
1994 C CD1 . LEU A 247 ? 0.72157 0.69912 0.79834 -0.09269 0.01615  -0.02404 281 LEU A CD1 
1995 C CD2 . LEU A 247 ? 0.71393 0.66980 0.79717 -0.06749 0.01919  -0.01896 281 LEU A CD2 
1996 N N   . PRO A 248 ? 0.75551 0.67635 0.84590 -0.10014 0.01174  0.04864  282 PRO A N   
1997 C CA  . PRO A 248 ? 0.74329 0.66591 0.82684 -0.11031 0.01446  0.07239  282 PRO A CA  
1998 C C   . PRO A 248 ? 0.72961 0.67252 0.81684 -0.12948 0.02174  0.07434  282 PRO A C   
1999 O O   . PRO A 248 ? 0.71899 0.69193 0.80609 -0.12953 0.02537  0.06255  282 PRO A O   
2000 C CB  . PRO A 248 ? 0.67090 0.61794 0.74233 -0.09743 0.01444  0.07783  282 PRO A CB  
2001 C CG  . PRO A 248 ? 0.73819 0.68353 0.81791 -0.07984 0.00961  0.06369  282 PRO A CG  
2002 C CD  . PRO A 248 ? 0.73067 0.67151 0.81845 -0.08254 0.01206  0.04339  282 PRO A CD  
2003 N N   . GLN A 249 ? 0.67321 0.60028 0.76615 -0.14556 0.02418  0.09115  283 GLN A N   
2004 C CA  . GLN A 249 ? 0.73493 0.68234 0.84151 -0.16559 0.03114  0.09295  283 GLN A CA  
2005 C C   . GLN A 249 ? 0.71948 0.71016 0.81629 -0.16485 0.04207  0.09803  283 GLN A C   
2006 O O   . GLN A 249 ? 0.54446 0.56130 0.65595 -0.17719 0.04837  0.09583  283 GLN A O   
2007 C CB  . GLN A 249 ? 0.60901 0.53043 0.72725 -0.18475 0.03325  0.11409  283 GLN A CB  
2008 C CG  . GLN A 249 ? 0.83057 0.75771 0.97810 -0.20722 0.03265  0.10674  283 GLN A CG  
2009 C CD  . GLN A 249 ? 0.98052 0.89100 1.13729 -0.20307 0.01847  0.07723  283 GLN A CD  
2010 O OE1 . GLN A 249 ? 0.88265 0.75662 1.03129 -0.19018 0.00958  0.06854  283 GLN A OE1 
2011 N NE2 . GLN A 249 ? 1.03595 0.97489 1.20824 -0.21179 0.01611  0.06113  283 GLN A NE2 
2012 N N   . GLN A 250 ? 0.66198 0.66128 0.73621 -0.14991 0.04315  0.10307  284 GLN A N   
2013 C CA  . GLN A 250 ? 0.62876 0.66431 0.69073 -0.14664 0.05187  0.10338  284 GLN A CA  
2014 C C   . GLN A 250 ? 0.63635 0.69585 0.70800 -0.14281 0.05097  0.08166  284 GLN A C   
2015 O O   . GLN A 250 ? 0.70430 0.79316 0.77471 -0.14313 0.05883  0.07991  284 GLN A O   
2016 C CB  . GLN A 250 ? 0.58893 0.62429 0.62412 -0.13130 0.04847  0.10940  284 GLN A CB  
2017 C CG  . GLN A 250 ? 0.70041 0.71979 0.71665 -0.13299 0.05051  0.13505  284 GLN A CG  
2018 C CD  . GLN A 250 ? 0.69852 0.68024 0.71675 -0.12670 0.03834  0.14222  284 GLN A CD  
2019 O OE1 . GLN A 250 ? 0.69775 0.66169 0.73637 -0.12610 0.03191  0.12927  284 GLN A OE1 
2020 N NE2 . GLN A 250 ? 0.68448 0.65390 0.67934 -0.11969 0.03456  0.16235  284 GLN A NE2 
2021 N N   . PHE A 251 ? 0.61088 0.65816 0.69024 -0.13750 0.04217  0.06573  285 PHE A N   
2022 C CA  . PHE A 251 ? 0.60385 0.67097 0.68849 -0.13360 0.04089  0.04852  285 PHE A CA  
2023 C C   . PHE A 251 ? 0.65876 0.73935 0.76307 -0.14689 0.04171  0.04414  285 PHE A C   
2024 O O   . PHE A 251 ? 0.70090 0.80799 0.80995 -0.14491 0.04352  0.03705  285 PHE A O   
2025 C CB  . PHE A 251 ? 0.64504 0.69754 0.72760 -0.12316 0.03358  0.03508  285 PHE A CB  
2026 C CG  . PHE A 251 ? 0.55242 0.60521 0.62395 -0.11001 0.03255  0.03650  285 PHE A CG  
2027 C CD1 . PHE A 251 ? 0.74273 0.81466 0.80913 -0.10392 0.03386  0.03111  285 PHE A CD1 
2028 C CD2 . PHE A 251 ? 0.60270 0.63620 0.67225 -0.10386 0.02860  0.04331  285 PHE A CD2 
2029 C CE1 . PHE A 251 ? 0.55403 0.62737 0.61589 -0.09490 0.03098  0.03174  285 PHE A CE1 
2030 C CE2 . PHE A 251 ? 0.52583 0.56502 0.59132 -0.09258 0.02539  0.04405  285 PHE A CE2 
2031 C CZ  . PHE A 251 ? 0.60288 0.66280 0.66573 -0.08959 0.02645  0.03790  285 PHE A CZ  
2032 N N   . ALA A 252 ? 0.77451 0.83647 0.89316 -0.16040 0.03863  0.04795  286 ALA A N   
2033 C CA  . ALA A 252 ? 0.70109 0.77941 0.84497 -0.17649 0.03777  0.04506  286 ALA A CA  
2034 C C   . ALA A 252 ? 0.55992 0.67024 0.71319 -0.18466 0.05154  0.06050  286 ALA A C   
2035 O O   . ALA A 252 ? 0.62208 0.76613 0.79412 -0.18855 0.05366  0.05514  286 ALA A O   
2036 C CB  . ALA A 252 ? 0.70165 0.74757 0.86087 -0.19118 0.02959  0.04492  286 ALA A CB  
2037 N N   . GLU A 253 ? 0.68060 0.78272 0.82000 -0.18555 0.06121  0.07996  287 GLU A N   
2038 C CA  . GLU A 253 ? 0.67123 0.80537 0.81170 -0.19013 0.07770  0.09506  287 GLU A CA  
2039 C C   . GLU A 253 ? 0.64465 0.81078 0.77420 -0.17363 0.08212  0.08353  287 GLU A C   
2040 O O   . GLU A 253 ? 0.61278 0.81561 0.75551 -0.17581 0.09372  0.08574  287 GLU A O   
2041 C CB  . GLU A 253 ? 0.44182 0.55707 0.55808 -0.19015 0.08543  0.11796  287 GLU A CB  
2042 C CG  . GLU A 253 ? 0.73731 0.88494 0.84453 -0.19216 0.10503  0.13463  287 GLU A CG  
2043 C CD  . GLU A 253 ? 0.98935 1.11524 1.06803 -0.19303 0.11125  0.16027  287 GLU A CD  
2044 O OE1 . GLU A 253 ? 0.93954 1.02426 1.01622 -0.19644 0.10035  0.16788  287 GLU A OE1 
2045 O OE2 . GLU A 253 ? 1.10673 1.25585 1.16276 -0.18842 0.12660  0.17256  287 GLU A OE2 
2046 N N   . TYR A 254 ? 0.70918 0.86202 0.81775 -0.15699 0.07333  0.07121  288 TYR A N   
2047 C CA  . TYR A 254 ? 0.51081 0.68581 0.61059 -0.14210 0.07496  0.05939  288 TYR A CA  
2048 C C   . TYR A 254 ? 0.49958 0.69697 0.62434 -0.14303 0.07109  0.04668  288 TYR A C   
2049 O O   . TYR A 254 ? 0.51047 0.73900 0.64366 -0.13763 0.07848  0.04390  288 TYR A O   
2050 C CB  . TYR A 254 ? 0.47610 0.62998 0.55399 -0.12809 0.06542  0.05089  288 TYR A CB  
2051 C CG  . TYR A 254 ? 0.48253 0.65024 0.55547 -0.11492 0.06377  0.03761  288 TYR A CG  
2052 C CD1 . TYR A 254 ? 0.50056 0.68027 0.55688 -0.10532 0.07001  0.03677  288 TYR A CD1 
2053 C CD2 . TYR A 254 ? 0.39300 0.55877 0.47516 -0.11133 0.05548  0.02603  288 TYR A CD2 
2054 C CE1 . TYR A 254 ? 0.50886 0.69456 0.56191 -0.09302 0.06707  0.02386  288 TYR A CE1 
2055 C CE2 . TYR A 254 ? 0.48719 0.66023 0.56509 -0.09964 0.05345  0.01693  288 TYR A CE2 
2056 C CZ  . TYR A 254 ? 0.47257 0.65369 0.53796 -0.09081 0.05879  0.01547  288 TYR A CZ  
2057 O OH  . TYR A 254 ? 0.49766 0.67952 0.55999 -0.07890 0.05534  0.00559  288 TYR A OH  
2058 N N   . LEU A 255 ? 0.44140 0.62371 0.57674 -0.14773 0.05865  0.03798  289 LEU A N   
2059 C CA  . LEU A 255 ? 0.38553 0.58748 0.53948 -0.14665 0.05089  0.02563  289 LEU A CA  
2060 C C   . LEU A 255 ? 0.58253 0.81876 0.77014 -0.15945 0.05644  0.03034  289 LEU A C   
2061 O O   . LEU A 255 ? 0.56468 0.83302 0.76796 -0.15261 0.05641  0.02423  289 LEU A O   
2062 C CB  . LEU A 255 ? 0.56613 0.74398 0.71838 -0.14907 0.03629  0.01492  289 LEU A CB  
2063 C CG  . LEU A 255 ? 0.52360 0.71836 0.68763 -0.14654 0.02438  0.00192  289 LEU A CG  
2064 C CD1 . LEU A 255 ? 0.57180 0.77794 0.72240 -0.12840 0.02476  -0.00178 289 LEU A CD1 
2065 C CD2 . LEU A 255 ? 0.59168 0.76064 0.74721 -0.14894 0.01084  -0.00962 289 LEU A CD2 
2066 N N   . ASP A 256 ? 0.52672 0.75733 0.72906 -0.17809 0.06125  0.04236  290 ASP A N   
2067 C CA  . ASP A 256 ? 0.50332 0.77048 0.74407 -0.19385 0.06883  0.04974  290 ASP A CA  
2068 C C   . ASP A 256 ? 0.52067 0.82511 0.76076 -0.18488 0.08873  0.05821  290 ASP A C   
2069 O O   . ASP A 256 ? 0.52908 0.87785 0.80184 -0.18665 0.09444  0.05691  290 ASP A O   
2070 C CB  . ASP A 256 ? 0.74481 0.99187 1.00068 -0.21778 0.07088  0.06416  290 ASP A CB  
2071 C CG  . ASP A 256 ? 0.83966 1.06192 1.11156 -0.22998 0.05019  0.05112  290 ASP A CG  
2072 O OD1 . ASP A 256 ? 0.85737 1.09560 1.14034 -0.22497 0.03617  0.03335  290 ASP A OD1 
2073 O OD2 . ASP A 256 ? 0.80805 0.99301 1.07941 -0.24334 0.04689  0.05818  290 ASP A OD2 
2074 N N   . SER A 257 ? 0.50365 0.79262 0.70705 -0.17372 0.09866  0.06535  291 SER A N   
2075 C CA  . SER A 257 ? 0.44709 0.76791 0.64182 -0.16306 0.11782  0.07083  291 SER A CA  
2076 C C   . SER A 257 ? 0.51920 0.86335 0.71709 -0.14231 0.11464  0.05301  291 SER A C   
2077 O O   . SER A 257 ? 0.55042 0.93773 0.77030 -0.13735 0.12700  0.05233  291 SER A O   
2078 C CB  . SER A 257 ? 0.51344 0.80824 0.66290 -0.15491 0.12416  0.07974  291 SER A CB  
2079 O OG  . SER A 257 ? 0.71460 1.03784 0.84806 -0.14207 0.14169  0.08146  291 SER A OG  
2080 N N   . VAL A 258 ? 0.54956 0.86581 0.72736 -0.12938 0.09888  0.03954  292 VAL A N   
2081 C CA  . VAL A 258 ? 0.51458 0.84414 0.69274 -0.10933 0.09439  0.02496  292 VAL A CA  
2082 C C   . VAL A 258 ? 0.54430 0.90332 0.76169 -0.11141 0.08593  0.01870  292 VAL A C   
2083 O O   . VAL A 258 ? 0.51523 0.89743 0.74305 -0.09456 0.08567  0.01007  292 VAL A O   
2084 C CB  . VAL A 258 ? 0.41683 0.70728 0.56482 -0.09804 0.08077  0.01610  292 VAL A CB  
2085 C CG1 . VAL A 258 ? 0.39347 0.65985 0.50744 -0.09570 0.08591  0.02099  292 VAL A CG1 
2086 C CG2 . VAL A 258 ? 0.52614 0.79454 0.67900 -0.10758 0.06535  0.01408  292 VAL A CG2 
2087 N N   . ARG A 259 ? 0.54259 0.90000 0.78223 -0.13062 0.07685  0.02170  293 ARG A N   
2088 C CA  . ARG A 259 ? 0.54509 0.93490 0.82482 -0.13480 0.06610  0.01538  293 ARG A CA  
2089 C C   . ARG A 259 ? 0.48657 0.92995 0.80840 -0.14184 0.08184  0.02275  293 ARG A C   
2090 O O   . ARG A 259 ? 0.60047 1.08235 0.96066 -0.13965 0.07421  0.01649  293 ARG A O   
2091 C CB  . ARG A 259 ? 0.55003 0.91824 0.83822 -0.15354 0.04884  0.01275  293 ARG A CB  
2092 C CG  . ARG A 259 ? 0.59788 0.92956 0.85479 -0.14293 0.03106  0.00154  293 ARG A CG  
2093 C CD  . ARG A 259 ? 0.54019 0.84925 0.80070 -0.15932 0.01548  -0.00407 293 ARG A CD  
2094 N NE  . ARG A 259 ? 0.53924 0.82232 0.77016 -0.14724 0.00024  -0.01542 293 ARG A NE  
2095 C CZ  . ARG A 259 ? 0.61239 0.86946 0.83315 -0.15468 -0.01326 -0.02436 293 ARG A CZ  
2096 N NH1 . ARG A 259 ? 0.51416 0.76153 0.75344 -0.17486 -0.01618 -0.02454 293 ARG A NH1 
2097 N NH2 . ARG A 259 ? 0.63384 0.87254 0.82395 -0.14120 -0.02344 -0.03322 293 ARG A NH2 
2098 N N   . SER A 260 ? 0.47393 0.92336 0.78974 -0.14948 0.10377  0.03689  294 SER A N   
2099 C CA  . SER A 260 ? 0.40623 0.89907 0.75609 -0.15416 0.12271  0.04639  294 SER A CA  
2100 C C   . SER A 260 ? 0.40529 0.92784 0.74372 -0.12963 0.14170  0.04290  294 SER A C   
2101 O O   . SER A 260 ? 0.55081 1.10360 0.91024 -0.12796 0.15994  0.04944  294 SER A O   
2102 C CB  . SER A 260 ? 0.47362 0.94266 0.81746 -0.17408 0.13528  0.06522  294 SER A CB  
2103 O OG  . SER A 260 ? 0.68238 1.11908 1.03595 -0.19487 0.11755  0.06611  294 SER A OG  
2104 N N   . LEU A 261 ? 0.57870 1.08170 0.88104 -0.10805 0.13640  0.03083  295 LEU A N   
2105 C CA  . LEU A 261 ? 0.45779 0.97982 0.74412 -0.08247 0.15223  0.02351  295 LEU A CA  
2106 C C   . LEU A 261 ? 0.49587 1.06792 0.82658 -0.06656 0.15209  0.01327  295 LEU A C   
2107 O O   . LEU A 261 ? 0.50433 1.07540 0.85725 -0.06497 0.13014  0.00575  295 LEU A O   
2108 C CB  . LEU A 261 ? 0.49017 0.96233 0.72623 -0.06377 0.14098  0.01146  295 LEU A CB  
2109 C CG  . LEU A 261 ? 0.50313 0.93250 0.69334 -0.07215 0.14256  0.01934  295 LEU A CG  
2110 C CD1 . LEU A 261 ? 0.49020 0.87415 0.64473 -0.05747 0.12626  0.00638  295 LEU A CD1 
2111 C CD2 . LEU A 261 ? 0.33445 0.78381 0.50438 -0.06899 0.16750  0.02765  295 LEU A CD2 
2112 N N   . PRO A 262 ? 0.52265 1.13329 0.86346 -0.05224 0.17468  0.01275  296 PRO A N   
2113 C CA  . PRO A 262 ? 0.35072 1.00236 0.73022 -0.03021 0.17340  0.00092  296 PRO A CA  
2114 C C   . PRO A 262 ? 0.39527 1.02326 0.75422 -0.00250 0.15612  -0.01749 296 PRO A C   
2115 O O   . PRO A 262 ? 0.47790 1.04991 0.78611 0.00189  0.14850  -0.02190 296 PRO A O   
2116 C CB  . PRO A 262 ? 0.37609 1.05212 0.75153 -0.01770 0.20272  0.00314  296 PRO A CB  
2117 C CG  . PRO A 262 ? 0.45683 1.11356 0.81020 -0.04322 0.21711  0.02251  296 PRO A CG  
2118 C CD  . PRO A 262 ? 0.51578 1.12518 0.83189 -0.05562 0.20041  0.02458  296 PRO A CD  
2119 N N   . PHE A 263 ? 0.53870 1.19962 0.93657 0.01669  0.14721  -0.02698 297 PHE A N   
2120 C CA  . PHE A 263 ? 0.52439 1.14767 0.90328 0.04167  0.12535  -0.04047 297 PHE A CA  
2121 C C   . PHE A 263 ? 0.49758 1.08825 0.83097 0.06665  0.13533  -0.05313 297 PHE A C   
2122 O O   . PHE A 263 ? 0.58481 1.11708 0.87978 0.07283  0.11928  -0.05883 297 PHE A O   
2123 C CB  . PHE A 263 ? 0.41915 1.08794 0.85063 0.06018  0.11405  -0.04646 297 PHE A CB  
2124 C CG  . PHE A 263 ? 0.44506 1.07698 0.85839 0.09015  0.09432  -0.05800 297 PHE A CG  
2125 C CD1 . PHE A 263 ? 0.48312 1.06429 0.87167 0.08393  0.06785  -0.05476 297 PHE A CD1 
2126 C CD2 . PHE A 263 ? 0.46883 1.11554 0.88929 0.12533  0.10320  -0.07145 297 PHE A CD2 
2127 C CE1 . PHE A 263 ? 0.50089 1.04553 0.87248 0.10971  0.05078  -0.06119 297 PHE A CE1 
2128 C CE2 . PHE A 263 ? 0.40957 1.01588 0.81427 0.15252  0.08399  -0.08039 297 PHE A CE2 
2129 C CZ  . PHE A 263 ? 0.54967 1.10436 0.93021 0.14344  0.05780  -0.07347 297 PHE A CZ  
2130 N N   . ASP A 264 ? 0.60900 1.23692 0.94584 0.08069  0.16189  -0.05822 298 ASP A N   
2131 C CA  . ASP A 264 ? 0.58861 1.18949 0.88342 0.10809  0.17040  -0.07522 298 ASP A CA  
2132 C C   . ASP A 264 ? 0.55835 1.13897 0.80321 0.09617  0.18707  -0.07150 298 ASP A C   
2133 O O   . ASP A 264 ? 0.67511 1.23856 0.88213 0.11787  0.19572  -0.08726 298 ASP A O   
2134 C CB  . ASP A 264 ? 0.49061 1.14503 0.81683 0.14042  0.18790  -0.08861 298 ASP A CB  
2135 C CG  . ASP A 264 ? 0.49319 1.19650 0.84383 0.12578  0.21422  -0.07458 298 ASP A CG  
2136 O OD1 . ASP A 264 ? 0.55610 1.26109 0.90649 0.09225  0.21931  -0.05509 298 ASP A OD1 
2137 O OD2 . ASP A 264 ? 0.61878 1.35015 0.98772 0.14718  0.22883  -0.08211 298 ASP A OD2 
2138 N N   . ALA A 265 ? 0.51439 1.09404 0.75658 0.06367  0.18975  -0.05195 299 ALA A N   
2139 C CA  . ALA A 265 ? 0.53086 1.09576 0.72771 0.05263  0.20510  -0.04445 299 ALA A CA  
2140 C C   . ALA A 265 ? 0.61794 1.11407 0.76158 0.05431  0.18594  -0.05294 299 ALA A C   
2141 O O   . ALA A 265 ? 0.54703 1.00532 0.69309 0.04953  0.16160  -0.05482 299 ALA A O   
2142 C CB  . ALA A 265 ? 0.52713 1.10897 0.74195 0.01785  0.21229  -0.01906 299 ALA A CB  
2143 N N   . GLU A 266 ? 0.70265 1.18564 0.79808 0.06101  0.19734  -0.05761 300 GLU A N   
2144 C CA  . GLU A 266 ? 0.74268 1.16656 0.79063 0.05948  0.17912  -0.06464 300 GLU A CA  
2145 C C   . GLU A 266 ? 0.63806 1.04597 0.67601 0.02985  0.17489  -0.04252 300 GLU A C   
2146 O O   . GLU A 266 ? 0.77618 1.20719 0.80321 0.01958  0.19367  -0.02700 300 GLU A O   
2147 C CB  . GLU A 266 ? 0.80174 1.21769 0.80026 0.08095  0.18879  -0.08211 300 GLU A CB  
2148 C CG  . GLU A 266 ? 0.78858 1.14502 0.74459 0.08154  0.16554  -0.09429 300 GLU A CG  
2149 C CD  . GLU A 266 ? 1.04555 1.39666 0.94483 0.09005  0.17396  -0.10195 300 GLU A CD  
2150 O OE1 . GLU A 266 ? 1.17677 1.56058 1.06372 0.08231  0.19540  -0.08475 300 GLU A OE1 
2151 O OE2 . GLU A 266 ? 1.13656 1.44978 1.00257 0.10387  0.15824  -0.12467 300 GLU A OE2 
2152 N N   . PRO A 267 ? 0.64557 1.01474 0.68673 0.01664  0.15203  -0.03934 301 PRO A N   
2153 C CA  . PRO A 267 ? 0.56321 0.91884 0.60080 -0.00891 0.14821  -0.01943 301 PRO A CA  
2154 C C   . PRO A 267 ? 0.65768 0.99144 0.64656 -0.00944 0.14928  -0.01675 301 PRO A C   
2155 O O   . PRO A 267 ? 0.69927 1.01275 0.65565 0.00705  0.14255  -0.03424 301 PRO A O   
2156 C CB  . PRO A 267 ? 0.58677 0.90825 0.63780 -0.01615 0.12442  -0.02175 301 PRO A CB  
2157 C CG  . PRO A 267 ? 0.55940 0.88596 0.63020 0.00212  0.11827  -0.03691 301 PRO A CG  
2158 C CD  . PRO A 267 ? 0.53245 0.87097 0.58375 0.02490  0.13048  -0.05195 301 PRO A CD  
2159 N N   . PRO A 268 ? 0.69272 1.02801 0.67479 -0.02773 0.15565  0.00467  302 PRO A N   
2160 C CA  . PRO A 268 ? 0.70133 1.01344 0.63581 -0.02756 0.15220  0.00943  302 PRO A CA  
2161 C C   . PRO A 268 ? 0.64593 0.91499 0.57377 -0.03333 0.12649  0.00595  302 PRO A C   
2162 O O   . PRO A 268 ? 0.64381 0.89903 0.58033 -0.04961 0.12038  0.02210  302 PRO A O   
2163 C CB  . PRO A 268 ? 0.68115 1.01130 0.61679 -0.04487 0.16936  0.03737  302 PRO A CB  
2164 C CG  . PRO A 268 ? 0.63770 0.97971 0.62672 -0.06219 0.16911  0.04628  302 PRO A CG  
2165 C CD  . PRO A 268 ? 0.53598 0.89443 0.55348 -0.04874 0.16586  0.02578  302 PRO A CD  
2166 N N   . TYR A 269 ? 0.65498 0.90259 0.56997 -0.01987 0.11158  -0.01538 303 TYR A N   
2167 C CA  . TYR A 269 ? 0.61570 0.82854 0.53262 -0.02621 0.08894  -0.01852 303 TYR A CA  
2168 C C   . TYR A 269 ? 0.72306 0.92164 0.61289 -0.03302 0.08159  -0.00687 303 TYR A C   
2169 O O   . TYR A 269 ? 0.75425 0.93760 0.65835 -0.04496 0.07148  0.00371  303 TYR A O   
2170 C CB  . TYR A 269 ? 0.62358 0.81592 0.53315 -0.01249 0.07515  -0.04219 303 TYR A CB  
2171 C CG  . TYR A 269 ? 0.60047 0.80302 0.53303 -0.00113 0.08060  -0.05382 303 TYR A CG  
2172 C CD1 . TYR A 269 ? 0.40008 0.59388 0.36530 -0.00654 0.07256  -0.05165 303 TYR A CD1 
2173 C CD2 . TYR A 269 ? 0.47438 0.69608 0.39422 0.01730  0.09371  -0.06685 303 TYR A CD2 
2174 C CE1 . TYR A 269 ? 0.55488 0.75720 0.54015 0.00587  0.07499  -0.06048 303 TYR A CE1 
2175 C CE2 . TYR A 269 ? 0.50305 0.73491 0.44698 0.03080  0.09744  -0.07748 303 TYR A CE2 
2176 C CZ  . TYR A 269 ? 0.49135 0.71262 0.46833 0.02490  0.08677  -0.07341 303 TYR A CZ  
2177 O OH  . TYR A 269 ? 0.61887 0.84953 0.61883 0.04028  0.08808  -0.08226 303 TYR A OH  
2178 N N   . GLU A 270 ? 0.64699 0.85084 0.49576 -0.02336 0.08609  -0.00910 304 GLU A N   
2179 C CA  . GLU A 270 ? 0.55949 0.74955 0.37850 -0.02687 0.07567  0.00214  304 GLU A CA  
2180 C C   . GLU A 270 ? 0.73368 0.92935 0.56221 -0.04153 0.08600  0.03119  304 GLU A C   
2181 O O   . GLU A 270 ? 0.80412 0.98143 0.63001 -0.04806 0.07299  0.04324  304 GLU A O   
2182 C CB  . GLU A 270 ? 0.59980 0.79495 0.36585 -0.01137 0.07763  -0.00744 304 GLU A CB  
2183 C CG  . GLU A 270 ? 0.94580 1.12559 0.67587 -0.01139 0.06071  0.00088  304 GLU A CG  
2184 C CD  . GLU A 270 ? 0.89767 1.05284 0.63529 -0.01100 0.03074  -0.01654 304 GLU A CD  
2185 O OE1 . GLU A 270 ? 0.68678 0.83210 0.46812 -0.02094 0.02310  -0.01688 304 GLU A OE1 
2186 O OE2 . GLU A 270 ? 1.17600 1.32333 0.87552 -0.00105 0.01472  -0.03008 304 GLU A OE2 
2187 N N   . GLU A 271 ? 0.73395 0.95469 0.57717 -0.04684 0.10866  0.04261  305 GLU A N   
2188 C CA  . GLU A 271 ? 0.63237 0.85438 0.49176 -0.06401 0.11764  0.06975  305 GLU A CA  
2189 C C   . GLU A 271 ? 0.70082 0.90325 0.59969 -0.07609 0.10401  0.07058  305 GLU A C   
2190 O O   . GLU A 271 ? 0.67875 0.86420 0.58248 -0.08686 0.09996  0.08835  305 GLU A O   
2191 C CB  . GLU A 271 ? 0.71556 0.97302 0.59110 -0.06941 0.14434  0.07995  305 GLU A CB  
2192 C CG  . GLU A 271 ? 0.79318 1.05798 0.64983 -0.07950 0.16115  0.11003  305 GLU A CG  
2193 C CD  . GLU A 271 ? 1.15506 1.46285 1.02927 -0.08439 0.19052  0.11958  305 GLU A CD  
2194 O OE1 . GLU A 271 ? 1.20143 1.53674 1.06134 -0.06759 0.20303  0.10385  305 GLU A OE1 
2195 O OE2 . GLU A 271 ? 1.15428 1.46886 1.05953 -0.10496 0.20091  0.14196  305 GLU A OE2 
2196 N N   . TYR A 272 ? 0.55703 0.75965 0.48149 -0.07290 0.09690  0.05172  306 TYR A N   
2197 C CA  . TYR A 272 ? 0.54344 0.72876 0.49856 -0.08188 0.08490  0.05083  306 TYR A CA  
2198 C C   . TYR A 272 ? 0.66523 0.82423 0.60911 -0.07912 0.06656  0.04900  306 TYR A C   
2199 O O   . TYR A 272 ? 0.51999 0.66328 0.47818 -0.08666 0.06018  0.05753  306 TYR A O   
2200 C CB  . TYR A 272 ? 0.38973 0.58327 0.36981 -0.07787 0.08284  0.03399  306 TYR A CB  
2201 C CG  . TYR A 272 ? 0.63389 0.85719 0.63730 -0.08135 0.09767  0.03603  306 TYR A CG  
2202 C CD1 . TYR A 272 ? 0.50187 0.73728 0.51936 -0.09601 0.10885  0.05365  306 TYR A CD1 
2203 C CD2 . TYR A 272 ? 0.61801 0.85757 0.63322 -0.07015 0.09948  0.02099  306 TYR A CD2 
2204 C CE1 . TYR A 272 ? 0.59585 0.86419 0.64227 -0.10118 0.12158  0.05564  306 TYR A CE1 
2205 C CE2 . TYR A 272 ? 0.56379 0.83642 0.60607 -0.07187 0.11166  0.02258  306 TYR A CE2 
2206 C CZ  . TYR A 272 ? 0.58775 0.87743 0.64742 -0.08827 0.12277  0.03964  306 TYR A CZ  
2207 O OH  . TYR A 272 ? 0.58263 0.91069 0.67655 -0.09197 0.13413  0.04136  306 TYR A OH  
2208 N N   . ARG A 273 ? 0.54491 0.69976 0.46586 -0.06785 0.05714  0.03642  307 ARG A N   
2209 C CA  . ARG A 273 ? 0.56695 0.70335 0.48302 -0.06593 0.03846  0.03455  307 ARG A CA  
2210 C C   . ARG A 273 ? 0.72325 0.85196 0.62119 -0.06771 0.03570  0.05396  307 ARG A C   
2211 O O   . ARG A 273 ? 0.67560 0.79048 0.58589 -0.06948 0.02388  0.05961  307 ARG A O   
2212 C CB  . ARG A 273 ? 0.55911 0.69295 0.45616 -0.05551 0.02669  0.01568  307 ARG A CB  
2213 C CG  . ARG A 273 ? 0.53362 0.66439 0.45250 -0.05401 0.02389  -0.00174 307 ARG A CG  
2214 C CD  . ARG A 273 ? 0.64976 0.77010 0.55383 -0.04648 0.00827  -0.02042 307 ARG A CD  
2215 N NE  . ARG A 273 ? 0.60680 0.73370 0.47575 -0.03456 0.01356  -0.03112 307 ARG A NE  
2216 C CZ  . ARG A 273 ? 0.67732 0.80628 0.54543 -0.02562 0.02041  -0.04649 307 ARG A CZ  
2217 N NH1 . ARG A 273 ? 0.65314 0.77644 0.55249 -0.02783 0.02115  -0.05095 307 ARG A NH1 
2218 N NH2 . ARG A 273 ? 0.58550 0.72209 0.41854 -0.01219 0.02665  -0.05753 307 ARG A NH2 
2219 N N   . MET A 274 ? 0.63187 0.76992 0.50020 -0.06593 0.04732  0.06562  308 MET A N   
2220 C CA  . MET A 274 ? 0.66907 0.79682 0.51779 -0.06796 0.04601  0.08908  308 MET A CA  
2221 C C   . MET A 274 ? 0.68742 0.80374 0.56639 -0.08114 0.05228  0.10592  308 MET A C   
2222 O O   . MET A 274 ? 0.82705 0.92376 0.70318 -0.08201 0.04395  0.12196  308 MET A O   
2223 C CB  . MET A 274 ? 0.62320 0.76517 0.42992 -0.06354 0.06051  0.10010  308 MET A CB  
2224 C CG  . MET A 274 ? 0.89864 1.04595 0.66432 -0.04800 0.05055  0.08301  308 MET A CG  
2225 S SD  . MET A 274 ? 1.17046 1.29780 0.91764 -0.04026 0.01877  0.08345  308 MET A SD  
2226 C CE  . MET A 274 ? 1.09277 1.20882 0.81927 -0.04434 0.02466  0.12225  308 MET A CE  
2227 N N   . LEU A 275 ? 0.63152 0.75831 0.53989 -0.09046 0.06476  0.10138  309 LEU A N   
2228 C CA  . LEU A 275 ? 0.70238 0.81594 0.64071 -0.10374 0.06745  0.11227  309 LEU A CA  
2229 C C   . LEU A 275 ? 0.69824 0.79110 0.65619 -0.10094 0.05119  0.10319  309 LEU A C   
2230 O O   . LEU A 275 ? 0.72491 0.79520 0.69112 -0.10447 0.04625  0.11475  309 LEU A O   
2231 C CB  . LEU A 275 ? 0.50897 0.64290 0.47489 -0.11362 0.08094  0.10638  309 LEU A CB  
2232 C CG  . LEU A 275 ? 0.49148 0.61256 0.49090 -0.12847 0.08054  0.11132  309 LEU A CG  
2233 C CD1 . LEU A 275 ? 0.57878 0.68449 0.57449 -0.14045 0.08703  0.13749  309 LEU A CD1 
2234 C CD2 . LEU A 275 ? 0.62495 0.77134 0.65295 -0.13553 0.08827  0.10050  309 LEU A CD2 
2235 N N   . LEU A 276 ? 0.68575 0.78538 0.65197 -0.09403 0.04377  0.08313  310 LEU A N   
2236 C CA  . LEU A 276 ? 0.66109 0.74727 0.64641 -0.09086 0.03191  0.07538  310 LEU A CA  
2237 C C   . LEU A 276 ? 0.70112 0.77735 0.67474 -0.08171 0.01798  0.08123  310 LEU A C   
2238 O O   . LEU A 276 ? 0.67059 0.73439 0.66118 -0.07851 0.01028  0.08192  310 LEU A O   
2239 C CB  . LEU A 276 ? 0.64410 0.74116 0.64214 -0.08801 0.02999  0.05629  310 LEU A CB  
2240 C CG  . LEU A 276 ? 0.52313 0.63299 0.53199 -0.09363 0.04061  0.04987  310 LEU A CG  
2241 C CD1 . LEU A 276 ? 0.66223 0.77743 0.68011 -0.08909 0.03703  0.03445  310 LEU A CD1 
2242 C CD2 . LEU A 276 ? 0.54803 0.65023 0.57526 -0.10333 0.04450  0.05502  310 LEU A CD2 
2243 N N   . LEU A 277 ? 0.74087 0.82404 0.68535 -0.07577 0.01381  0.08436  311 LEU A N   
2244 C CA  . LEU A 277 ? 0.72644 0.80317 0.65876 -0.06629 -0.00312 0.08999  311 LEU A CA  
2245 C C   . LEU A 277 ? 0.79463 0.85168 0.72082 -0.06580 -0.00439 0.11296  311 LEU A C   
2246 O O   . LEU A 277 ? 0.86491 0.91260 0.79800 -0.05710 -0.01931 0.11759  311 LEU A O   
2247 C CB  . LEU A 277 ? 0.67577 0.76387 0.57249 -0.05942 -0.00939 0.08512  311 LEU A CB  
2248 C CG  . LEU A 277 ? 0.82468 0.92160 0.72919 -0.05455 -0.02487 0.06386  311 LEU A CG  
2249 C CD1 . LEU A 277 ? 0.86332 0.96857 0.73110 -0.04917 -0.02687 0.05285  311 LEU A CD1 
2250 C CD2 . LEU A 277 ? 0.92825 1.02269 0.84487 -0.04810 -0.04588 0.06696  311 LEU A CD2 
2251 N N   . SER A 278 ? 0.73787 0.78850 0.65458 -0.07506 0.01076  0.12842  312 SER A N   
2252 C CA  . SER A 278 ? 0.81944 0.84484 0.73144 -0.07676 0.00999  0.15285  312 SER A CA  
2253 C C   . SER A 278 ? 0.79349 0.79716 0.74042 -0.07673 0.00432  0.14940  312 SER A C   
2254 O O   . SER A 278 ? 0.83571 0.81251 0.78218 -0.07350 -0.00172 0.16668  312 SER A O   
2255 C CB  . SER A 278 ? 0.75035 0.77551 0.65141 -0.09074 0.02953  0.17078  312 SER A CB  
2256 O OG  . SER A 278 ? 0.80192 0.83032 0.73570 -0.10403 0.04058  0.16106  312 SER A OG  
2257 N N   . VAL A 279 ? 0.72516 0.73810 0.69957 -0.07877 0.00634  0.12770  313 VAL A N   
2258 C CA  . VAL A 279 ? 0.67483 0.67039 0.67753 -0.07487 0.00128  0.12039  313 VAL A CA  
2259 C C   . VAL A 279 ? 0.77600 0.76810 0.78280 -0.05803 -0.01481 0.12205  313 VAL A C   
2260 O O   . VAL A 279 ? 0.82136 0.78968 0.84035 -0.05044 -0.02078 0.12836  313 VAL A O   
2261 C CB  . VAL A 279 ? 0.62368 0.63431 0.64736 -0.07854 0.00713  0.09770  313 VAL A CB  
2262 C CG1 . VAL A 279 ? 0.51774 0.51415 0.56476 -0.07112 0.00315  0.08808  313 VAL A CG1 
2263 C CG2 . VAL A 279 ? 0.53982 0.55492 0.56471 -0.09369 0.01989  0.09634  313 VAL A CG2 
2264 N N   . LEU A 280 ? 0.83387 0.84972 0.83326 -0.05138 -0.02345 0.11535  314 LEU A N   
2265 C CA  . LEU A 280 ? 0.80310 0.82355 0.81290 -0.03616 -0.04096 0.11585  314 LEU A CA  
2266 C C   . LEU A 280 ? 0.74188 0.74279 0.72970 -0.02741 -0.05223 0.13924  314 LEU A C   
2267 O O   . LEU A 280 ? 0.75690 0.75008 0.76071 -0.01304 -0.06553 0.14406  314 LEU A O   
2268 C CB  . LEU A 280 ? 0.74170 0.79166 0.75098 -0.03457 -0.04987 0.10220  314 LEU A CB  
2269 C CG  . LEU A 280 ? 0.61485 0.68152 0.64554 -0.04250 -0.04017 0.08222  314 LEU A CG  
2270 C CD1 . LEU A 280 ? 0.66554 0.75526 0.70063 -0.04164 -0.05222 0.07029  314 LEU A CD1 
2271 C CD2 . LEU A 280 ? 0.61682 0.68047 0.68126 -0.03914 -0.03417 0.07577  314 LEU A CD2 
2272 N N   . ASP A 281 ? 0.93656 0.93042 0.88787 -0.03451 -0.04644 0.15530  315 ASP A N   
2273 C CA  . ASP A 281 ? 0.96031 0.93187 0.88567 -0.02698 -0.05540 0.18231  315 ASP A CA  
2274 C C   . ASP A 281 ? 0.78866 0.72227 0.73009 -0.02878 -0.05072 0.19660  315 ASP A C   
2275 O O   . ASP A 281 ? 0.87349 0.78343 0.81131 -0.01591 -0.06405 0.21446  315 ASP A O   
2276 C CB  . ASP A 281 ? 0.97515 0.95186 0.85388 -0.03427 -0.04681 0.19725  315 ASP A CB  
2277 C CG  . ASP A 281 ? 1.14197 1.14857 0.99661 -0.02785 -0.05698 0.18331  315 ASP A CG  
2278 O OD1 . ASP A 281 ? 1.23151 1.25112 1.10393 -0.01720 -0.07623 0.16928  315 ASP A OD1 
2279 O OD2 . ASP A 281 ? 1.23776 1.25572 1.05780 -0.03346 -0.04568 0.18512  315 ASP A OD2 
2280 N N   . ASP A 282 ? 0.78029 0.70573 0.73987 -0.04383 -0.03418 0.18826  316 ASP A N   
2281 C CA  . ASP A 282 ? 1.00637 0.89195 0.98337 -0.04697 -0.03187 0.19705  316 ASP A CA  
2282 C C   . ASP A 282 ? 0.97034 0.84537 0.97812 -0.02892 -0.04372 0.18311  316 ASP A C   
2283 O O   . ASP A 282 ? 0.93358 0.76986 0.95037 -0.02202 -0.04937 0.19336  316 ASP A O   
2284 C CB  . ASP A 282 ? 0.84613 0.72970 0.83668 -0.06801 -0.01457 0.18766  316 ASP A CB  
2285 C CG  . ASP A 282 ? 0.95611 0.84756 0.92337 -0.08587 -0.00023 0.20592  316 ASP A CG  
2286 O OD1 . ASP A 282 ? 0.95450 0.84988 0.88904 -0.08130 -0.00219 0.22647  316 ASP A OD1 
2287 O OD2 . ASP A 282 ? 0.98938 0.88582 0.97102 -0.10368 0.01302  0.19965  316 ASP A OD2 
2288 N N   . LEU A 283 ? 0.84921 0.75763 0.87466 -0.02079 -0.04665 0.16034  317 LEU A N   
2289 C CA  . LEU A 283 ? 0.91366 0.82218 0.97161 -0.00333 -0.05347 0.14553  317 LEU A CA  
2290 C C   . LEU A 283 ? 0.83785 0.76554 0.90247 0.01673  -0.07189 0.15011  317 LEU A C   
2291 O O   . LEU A 283 ? 0.91191 0.84904 1.00859 0.03305  -0.07686 0.13817  317 LEU A O   
2292 C CB  . LEU A 283 ? 0.91305 0.84772 0.99148 -0.00883 -0.04184 0.11859  317 LEU A CB  
2293 C CG  . LEU A 283 ? 0.76941 0.69006 0.84493 -0.02676 -0.02702 0.11040  317 LEU A CG  
2294 C CD1 . LEU A 283 ? 0.68896 0.63687 0.77901 -0.02930 -0.01778 0.08644  317 LEU A CD1 
2295 C CD2 . LEU A 283 ? 0.84325 0.71851 0.92621 -0.02454 -0.02799 0.11348  317 LEU A CD2 
2296 N N   . GLY A 284 ? 0.76940 0.70589 0.80513 0.01675  -0.08236 0.16619  318 GLY A N   
2297 C CA  . GLY A 284 ? 0.78425 0.74017 0.82608 0.03560  -0.10437 0.17031  318 GLY A CA  
2298 C C   . GLY A 284 ? 0.85837 0.85988 0.93024 0.03753  -0.10792 0.14710  318 GLY A C   
2299 O O   . GLY A 284 ? 0.91282 0.93228 1.01751 0.05465  -0.12127 0.14269  318 GLY A O   
2300 N N   . GLN A 285 ? 0.72979 0.75085 0.79430 0.02028  -0.09608 0.13317  319 GLN A N   
2301 C CA  . GLN A 285 ? 0.65156 0.71115 0.74385 0.01770  -0.09756 0.11310  319 GLN A CA  
2302 C C   . GLN A 285 ? 0.78946 0.86678 0.85433 0.00872  -0.10630 0.11024  319 GLN A C   
2303 O O   . GLN A 285 ? 0.73960 0.80231 0.76292 0.00098  -0.10124 0.11878  319 GLN A O   
2304 C CB  . GLN A 285 ? 0.62940 0.69229 0.74029 0.00675  -0.07560 0.09661  319 GLN A CB  
2305 C CG  . GLN A 285 ? 0.75280 0.79324 0.88183 0.01501  -0.06559 0.09529  319 GLN A CG  
2306 C CD  . GLN A 285 ? 0.83610 0.88945 1.00219 0.03628  -0.07542 0.09335  319 GLN A CD  
2307 O OE1 . GLN A 285 ? 0.83756 0.92848 1.03084 0.04009  -0.08261 0.08632  319 GLN A OE1 
2308 N NE2 . GLN A 285 ? 0.72123 0.74364 0.89200 0.05037  -0.07612 0.09930  319 GLN A NE2 
2309 N N   . ALA A 286 ? 0.78227 0.89182 0.87220 0.00983  -0.11911 0.09735  320 ALA A N   
2310 C CA  . ALA A 286 ? 0.52482 0.64968 0.59294 0.00226  -0.13101 0.08925  320 ALA A CA  
2311 C C   . ALA A 286 ? 0.72008 0.85614 0.80139 -0.01357 -0.11652 0.07103  320 ALA A C   
2312 O O   . ALA A 286 ? 0.72569 0.87059 0.84386 -0.01675 -0.10381 0.06397  320 ALA A O   
2313 C CB  . ALA A 286 ? 0.59649 0.74770 0.68504 0.01217  -0.16017 0.08658  320 ALA A CB  
2314 N N   . CYS A 287 ? 0.68883 0.82319 0.73695 -0.02179 -0.11818 0.06385  321 CYS A N   
2315 C CA  . CYS A 287 ? 0.68851 0.82942 0.74629 -0.03503 -0.10813 0.04710  321 CYS A CA  
2316 C C   . CYS A 287 ? 0.61657 0.77928 0.69849 -0.03831 -0.12927 0.03334  321 CYS A C   
2317 O O   . CYS A 287 ? 0.84982 1.01146 0.90864 -0.04249 -0.14067 0.02173  321 CYS A O   
2318 C CB  . CYS A 287 ? 0.71366 0.83972 0.72647 -0.04023 -0.09696 0.04501  321 CYS A CB  
2319 S SG  . CYS A 287 ? 0.79112 0.91797 0.81480 -0.05302 -0.08208 0.02744  321 CYS A SG  
2320 N N   . ASP A 288 ? 0.67958 0.86316 0.81142 -0.03627 -0.13442 0.03379  322 ASP A N   
2321 C CA  . ASP A 288 ? 0.55588 0.76591 0.72325 -0.04062 -0.15630 0.02347  322 ASP A CA  
2322 C C   . ASP A 288 ? 0.50609 0.72590 0.70901 -0.05706 -0.14562 0.01240  322 ASP A C   
2323 O O   . ASP A 288 ? 0.68861 0.93065 0.92873 -0.06496 -0.16215 0.00432  322 ASP A O   
2324 C CB  . ASP A 288 ? 0.64314 0.87759 0.85133 -0.02800 -0.16903 0.03191  322 ASP A CB  
2325 C CG  . ASP A 288 ? 0.63730 0.87434 0.87605 -0.02239 -0.14484 0.03939  322 ASP A CG  
2326 O OD1 . ASP A 288 ? 0.68337 0.91168 0.92302 -0.03209 -0.12075 0.03580  322 ASP A OD1 
2327 O OD2 . ASP A 288 ? 0.65251 0.89932 0.91238 -0.00635 -0.15104 0.04807  322 ASP A OD2 
2328 N N   . GLY A 289 ? 0.60901 0.81291 0.80265 -0.06301 -0.11982 0.01308  323 GLY A N   
2329 C CA  . GLY A 289 ? 0.64109 0.84993 0.86287 -0.07755 -0.10857 0.00662  323 GLY A CA  
2330 C C   . GLY A 289 ? 0.69350 0.92649 0.96548 -0.07879 -0.09446 0.01299  323 GLY A C   
2331 O O   . GLY A 289 ? 0.66834 0.90948 0.96793 -0.09211 -0.08610 0.01089  323 GLY A O   
2332 N N   . ASP A 290 ? 0.50130 0.74489 0.78507 -0.06446 -0.09062 0.02121  324 ASP A N   
2333 C CA  . ASP A 290 ? 0.43728 0.70596 0.76578 -0.06151 -0.07424 0.02555  324 ASP A CA  
2334 C C   . ASP A 290 ? 0.43318 0.68320 0.74107 -0.06137 -0.04647 0.02751  324 ASP A C   
2335 O O   . ASP A 290 ? 0.57521 0.79964 0.84703 -0.05307 -0.04133 0.02940  324 ASP A O   
2336 C CB  . ASP A 290 ? 0.56030 0.84590 0.90983 -0.04247 -0.08289 0.03101  324 ASP A CB  
2337 C CG  . ASP A 290 ? 0.67601 1.00215 1.08559 -0.03899 -0.07245 0.03251  324 ASP A CG  
2338 O OD1 . ASP A 290 ? 0.66031 0.98585 1.07307 -0.03062 -0.04850 0.03423  324 ASP A OD1 
2339 O OD2 . ASP A 290 ? 0.92591 1.28659 1.38036 -0.04460 -0.08827 0.03110  324 ASP A OD2 
2340 N N   . MET A 291 ? 0.39038 0.65355 0.72135 -0.07118 -0.02942 0.02800  325 MET A N   
2341 C CA  . MET A 291 ? 0.32099 0.56843 0.62991 -0.07156 -0.00557 0.02927  325 MET A CA  
2342 C C   . MET A 291 ? 0.34155 0.61376 0.67958 -0.06287 0.01424  0.03233  325 MET A C   
2343 O O   . MET A 291 ? 0.27454 0.58130 0.65814 -0.06007 0.01232  0.03449  325 MET A O   
2344 C CB  . MET A 291 ? 0.37821 0.61453 0.67808 -0.08851 -0.00082 0.02897  325 MET A CB  
2345 C CG  . MET A 291 ? 0.46499 0.68063 0.74122 -0.09560 -0.02030 0.02269  325 MET A CG  
2346 S SD  . MET A 291 ? 0.60152 0.78336 0.82062 -0.08804 -0.01808 0.01979  325 MET A SD  
2347 C CE  . MET A 291 ? 0.64114 0.81273 0.84086 -0.09108 -0.04247 0.01158  325 MET A CE  
2348 N N   . ASP A 292 ? 0.32354 0.58011 0.63494 -0.05772 0.03321  0.03133  326 ASP A N   
2349 C CA  . ASP A 292 ? 0.26698 0.54327 0.59517 -0.04567 0.05369  0.03113  326 ASP A CA  
2350 C C   . ASP A 292 ? 0.41714 0.72656 0.77932 -0.05617 0.06941  0.03826  326 ASP A C   
2351 O O   . ASP A 292 ? 0.31776 0.66289 0.71828 -0.04770 0.08072  0.04003  326 ASP A O   
2352 C CB  . ASP A 292 ? 0.46830 0.71691 0.75403 -0.03842 0.06679  0.02572  326 ASP A CB  
2353 C CG  . ASP A 292 ? 0.41645 0.63476 0.67711 -0.02868 0.05427  0.02047  326 ASP A CG  
2354 O OD1 . ASP A 292 ? 0.58218 0.80168 0.85589 -0.02443 0.03750  0.02283  326 ASP A OD1 
2355 O OD2 . ASP A 292 ? 0.39504 0.58823 0.62317 -0.02608 0.06028  0.01498  326 ASP A OD2 
2356 N N   . TRP A 293 ? 0.48096 0.77945 0.83154 -0.07415 0.07139  0.04359  327 TRP A N   
2357 C CA  . TRP A 293 ? 0.37161 0.69677 0.75338 -0.08715 0.08726  0.05440  327 TRP A CA  
2358 C C   . TRP A 293 ? 0.25106 0.61270 0.69293 -0.09609 0.07654  0.05795  327 TRP A C   
2359 O O   . TRP A 293 ? 0.26759 0.66257 0.74902 -0.10541 0.09259  0.06822  327 TRP A O   
2360 C CB  . TRP A 293 ? 0.51357 0.81148 0.86950 -0.10393 0.08782  0.06053  327 TRP A CB  
2361 C CG  . TRP A 293 ? 0.42118 0.69504 0.77070 -0.11478 0.06209  0.05530  327 TRP A CG  
2362 C CD1 . TRP A 293 ? 0.27550 0.55912 0.66088 -0.12992 0.04614  0.05605  327 TRP A CD1 
2363 C CD2 . TRP A 293 ? 0.26574 0.50326 0.57009 -0.11086 0.04981  0.04702  327 TRP A CD2 
2364 N NE1 . TRP A 293 ? 0.39019 0.64305 0.74985 -0.13345 0.02462  0.04684  327 TRP A NE1 
2365 C CE2 . TRP A 293 ? 0.34515 0.57178 0.65611 -0.12155 0.02829  0.04230  327 TRP A CE2 
2366 C CE3 . TRP A 293 ? 0.39521 0.61056 0.65652 -0.09975 0.05479  0.04241  327 TRP A CE3 
2367 C CZ2 . TRP A 293 ? 0.28178 0.47850 0.55561 -0.11919 0.01505  0.03373  327 TRP A CZ2 
2368 C CZ3 . TRP A 293 ? 0.46091 0.64934 0.69190 -0.10001 0.04118  0.03585  327 TRP A CZ3 
2369 C CH2 . TRP A 293 ? 0.31011 0.49055 0.54640 -0.10854 0.02314  0.03189  327 TRP A CH2 
2370 N N   . MET A 294 ? 0.24628 0.60452 0.69627 -0.09376 0.04961  0.05053  328 MET A N   
2371 C CA  . MET A 294 ? 0.24610 0.64124 0.75403 -0.10078 0.03415  0.05165  328 MET A CA  
2372 C C   . MET A 294 ? 0.44155 0.88272 0.99457 -0.08425 0.04558  0.05338  328 MET A C   
2373 O O   . MET A 294 ? 0.37960 0.86239 0.99184 -0.09031 0.03624  0.05591  328 MET A O   
2374 C CB  . MET A 294 ? 0.24826 0.62530 0.74274 -0.09984 0.00026  0.04257  328 MET A CB  
2375 C CG  . MET A 294 ? 0.25364 0.59164 0.71160 -0.11529 -0.01249 0.03827  328 MET A CG  
2376 S SD  . MET A 294 ? 0.46596 0.78186 0.89291 -0.10910 -0.04755 0.02675  328 MET A SD  
2377 C CE  . MET A 294 ? 0.38669 0.75035 0.87795 -0.10960 -0.07104 0.02559  328 MET A CE  
2378 N N   . HIS A 295 ? 0.30676 0.74229 0.83583 -0.06298 0.06423  0.05054  329 HIS A N   
2379 C CA  . HIS A 295 ? 0.44287 0.91935 1.01132 -0.04262 0.07786  0.04970  329 HIS A CA  
2380 C C   . HIS A 295 ? 0.42342 0.92658 1.00210 -0.04204 0.11480  0.05608  329 HIS A C   
2381 O O   . HIS A 295 ? 0.40732 0.94677 1.01613 -0.02259 0.13159  0.05396  329 HIS A O   
2382 C CB  . HIS A 295 ? 0.40536 0.85481 0.94137 -0.01567 0.07172  0.03975  329 HIS A CB  
2383 C CG  . HIS A 295 ? 0.36645 0.79660 0.89545 -0.01243 0.03792  0.03715  329 HIS A CG  
2384 N ND1 . HIS A 295 ? 0.47759 0.94248 1.05625 -0.00714 0.01742  0.03855  329 HIS A ND1 
2385 C CD2 . HIS A 295 ? 0.35740 0.73968 0.83454 -0.01316 0.02150  0.03443  329 HIS A CD2 
2386 C CE1 . HIS A 295 ? 0.26779 0.70394 0.81943 -0.00396 -0.01085 0.03716  329 HIS A CE1 
2387 N NE2 . HIS A 295 ? 0.39174 0.77830 0.88220 -0.00793 -0.00709 0.03528  329 HIS A NE2 
2388 N N   . LEU A 296 ? 0.32456 0.81067 0.87703 -0.06083 0.12817  0.06426  330 LEU A N   
2389 C CA  . LEU A 296 ? 0.40322 0.90868 0.95091 -0.06045 0.16260  0.07190  330 LEU A CA  
2390 C C   . LEU A 296 ? 0.37003 0.92007 0.96440 -0.06797 0.16960  0.07571  330 LEU A C   
2391 O O   . LEU A 296 ? 0.43868 0.99985 1.06870 -0.08423 0.14854  0.07711  330 LEU A O   
2392 C CB  . LEU A 296 ? 0.41257 0.88235 0.91529 -0.07956 0.16883  0.08095  330 LEU A CB  
2393 C CG  . LEU A 296 ? 0.49177 0.91046 0.92909 -0.07224 0.16240  0.07317  330 LEU A CG  
2394 C CD1 . LEU A 296 ? 0.51694 0.90634 0.92428 -0.09228 0.16324  0.08432  330 LEU A CD1 
2395 C CD2 . LEU A 296 ? 0.52956 0.94646 0.93228 -0.04779 0.18279  0.06390  330 LEU A CD2 
2396 N N   . ASN A 297 ? 0.42005 0.99666 1.01318 -0.05559 0.19971  0.07604  331 ASN A N   
2397 C CA  . ASN A 297 ? 0.48098 1.10341 1.11654 -0.06367 0.21350  0.08107  331 ASN A CA  
2398 C C   . ASN A 297 ? 0.60217 1.26316 1.29969 -0.05848 0.19306  0.07479  331 ASN A C   
2399 O O   . ASN A 297 ? 0.46825 1.15833 1.20842 -0.07700 0.18806  0.08005  331 ASN A O   
2400 C CB  . ASN A 297 ? 0.55714 1.16715 1.18834 -0.09607 0.21615  0.09587  331 ASN A CB  
2401 C CG  . ASN A 297 ? 0.38032 0.95831 0.95210 -0.09877 0.23815  0.10452  331 ASN A CG  
2402 O OD1 . ASN A 297 ? 0.85454 1.45210 1.41526 -0.09298 0.26761  0.10906  331 ASN A OD1 
2403 N ND2 . ASN A 297 ? 0.59702 1.12673 1.12931 -0.10667 0.22336  0.10662  331 ASN A ND2 
2404 N N   . GLY A 298 ? 0.47850 1.13887 1.18150 -0.03266 0.18013  0.06394  332 GLY A N   
2405 C CA  . GLY A 298 ? 0.45363 1.15054 1.21164 -0.02167 0.15982  0.05816  332 GLY A CA  
2406 C C   . GLY A 298 ? 0.43114 1.11221 1.20274 -0.03708 0.12039  0.05872  332 GLY A C   
2407 O O   . GLY A 298 ? 0.67417 1.38793 1.49173 -0.04687 0.10355  0.05881  332 GLY A O   
2408 N N   . GLY A 299 ? 0.72016 1.35291 1.45163 -0.03884 0.10501  0.05785  333 GLY A N   
2409 C CA  . GLY A 299 ? 0.71691 1.33024 1.45108 -0.05342 0.06814  0.05664  333 GLY A CA  
2410 C C   . GLY A 299 ? 0.64276 1.25438 1.38447 -0.08620 0.06233  0.06121  333 GLY A C   
2411 O O   . GLY A 299 ? 0.71146 1.34080 1.48654 -0.09703 0.03752  0.05823  333 GLY A O   
2412 N N   . ARG A 300 ? 0.79102 1.37862 1.50033 -0.10126 0.08398  0.06828  334 ARG A N   
2413 C CA  . ARG A 300 ? 0.49542 1.08257 1.21590 -0.13013 0.08623  0.07517  334 ARG A CA  
2414 C C   . ARG A 300 ? 0.65700 1.19024 1.32856 -0.14632 0.08583  0.07950  334 ARG A C   
2415 O O   . ARG A 300 ? 0.76979 1.28420 1.44543 -0.16892 0.07019  0.08027  334 ARG A O   
2416 C CB  . ARG A 300 ? 0.50483 1.13051 1.24742 -0.13085 0.11973  0.08343  334 ARG A CB  
2417 C CG  . ARG A 300 ? 0.67709 1.29383 1.42056 -0.15977 0.13084  0.09530  334 ARG A CG  
2418 C CD  . ARG A 300 ? 0.77689 1.44110 1.58323 -0.17439 0.12762  0.09734  334 ARG A CD  
2419 N NE  . ARG A 300 ? 0.83036 1.50182 1.64288 -0.19465 0.15400  0.11225  334 ARG A NE  
2420 C CZ  . ARG A 300 ? 1.06952 1.78309 1.93635 -0.21145 0.15907  0.11778  334 ARG A CZ  
2421 N NH1 . ARG A 300 ? 0.81501 1.56934 1.73593 -0.21045 0.13815  0.10855  334 ARG A NH1 
2422 N NH2 . ARG A 300 ? 1.09044 1.80629 1.95788 -0.22988 0.18535  0.13390  334 ARG A NH2 
2423 N N   . GLY A 301 ? 0.54864 1.05666 1.17485 -0.13373 0.10205  0.08130  335 GLY A N   
2424 C CA  . GLY A 301 ? 0.44454 0.90541 1.02370 -0.14540 0.10485  0.08642  335 GLY A CA  
2425 C C   . GLY A 301 ? 0.72003 1.18071 1.27645 -0.14713 0.13792  0.09864  335 GLY A C   
2426 O O   . GLY A 301 ? 0.68398 1.18141 1.25923 -0.13985 0.16032  0.10219  335 GLY A O   
2427 N N   . TRP A 302 ? 0.77104 1.18980 1.28494 -0.15581 0.13996  0.10497  336 TRP A N   
2428 C CA  . TRP A 302 ? 0.80785 1.21879 1.29049 -0.15732 0.16752  0.11832  336 TRP A CA  
2429 C C   . TRP A 302 ? 0.82722 1.25712 1.34066 -0.17650 0.17908  0.13106  336 TRP A C   
2430 O O   . TRP A 302 ? 0.99725 1.44020 1.55451 -0.19148 0.16316  0.12889  336 TRP A O   
2431 C CB  . TRP A 302 ? 0.94310 1.30434 1.37772 -0.16206 0.16164  0.12293  336 TRP A CB  
2432 C CG  . TRP A 302 ? 0.75512 1.08638 1.20023 -0.17960 0.13397  0.11992  336 TRP A CG  
2433 C CD1 . TRP A 302 ? 0.76533 1.08610 1.21698 -0.17768 0.10719  0.10560  336 TRP A CD1 
2434 C CD2 . TRP A 302 ? 0.73716 1.04312 1.18547 -0.20056 0.13033  0.13063  336 TRP A CD2 
2435 N NE1 . TRP A 302 ? 0.82086 1.11231 1.27761 -0.19509 0.08713  0.10410  336 TRP A NE1 
2436 C CE2 . TRP A 302 ? 0.64675 0.92709 1.10337 -0.20928 0.10055  0.11920  336 TRP A CE2 
2437 C CE3 . TRP A 302 ? 0.90257 1.20339 1.34657 -0.21240 0.14930  0.14918  336 TRP A CE3 
2438 C CZ2 . TRP A 302 ? 0.84711 1.09527 1.30945 -0.22837 0.08883  0.12355  336 TRP A CZ2 
2439 C CZ3 . TRP A 302 ? 0.90172 1.17003 1.35314 -0.23257 0.13773  0.15652  336 TRP A CZ3 
2440 C CH2 . TRP A 302 ? 0.94165 1.18303 1.40284 -0.23992 0.10754  0.14272  336 TRP A CH2 
2441 N N   . ASP A 303 ? 1.20795 1.63959 1.69696 -0.17633 0.20692  0.14479  337 ASP A N   
2442 C CA  . ASP A 303 ? 1.27050 1.72046 1.78591 -0.19501 0.22252  0.16021  337 ASP A CA  
2443 C C   . ASP A 303 ? 1.49631 1.93349 1.96572 -0.19300 0.25031  0.17700  337 ASP A C   
2444 O O   . ASP A 303 ? 1.55230 1.98762 1.97946 -0.17197 0.26349  0.17286  337 ASP A O   
2445 C CB  . ASP A 303 ? 1.39981 1.90902 1.96847 -0.19112 0.23288  0.15543  337 ASP A CB  
2446 C CG  . ASP A 303 ? 1.47642 2.00082 2.10282 -0.20919 0.20866  0.15070  337 ASP A CG  
2447 O OD1 . ASP A 303 ? 1.44689 1.94351 2.07907 -0.23290 0.19692  0.15883  337 ASP A OD1 
2448 O OD2 . ASP A 303 ? 1.48715 2.04972 2.15228 -0.19864 0.19995  0.13829  337 ASP A OD2 
2449 N N   . ALA A 304 ? 1.20829 1.63554 1.68528 -0.21503 0.25804  0.19605  338 ALA A N   
2450 C CA  . ALA A 304 ? 0.98009 1.40349 1.42158 -0.21621 0.28677  0.21634  338 ALA A CA  
2451 C C   . ALA A 304 ? 1.33580 1.71615 1.70853 -0.20337 0.28673  0.22061  338 ALA A C   
2452 O O   . ALA A 304 ? 1.31217 1.69064 1.64410 -0.19764 0.30967  0.23464  338 ALA A O   
2453 C CB  . ALA A 304 ? 0.85367 1.33004 1.30446 -0.20268 0.31688  0.21484  338 ALA A CB  
2454 N N   . THR A 305 ? 1.43501 1.78270 1.79311 -0.19826 0.26132  0.20888  339 THR A N   
2455 C CA  . THR A 305 ? 1.49417 1.80367 1.79177 -0.18679 0.25912  0.21302  339 THR A CA  
2456 C C   . THR A 305 ? 1.36771 1.63539 1.66523 -0.19377 0.22944  0.20803  339 THR A C   
2457 O O   . THR A 305 ? 1.44392 1.67415 1.72656 -0.20499 0.22351  0.22312  339 THR A O   
2458 C CB  . THR A 305 ? 1.45609 1.78096 1.71932 -0.15971 0.26758  0.19767  339 THR A CB  
2459 O OG1 . THR A 305 ? 1.46093 1.82532 1.72532 -0.15070 0.29515  0.19852  339 THR A OG1 
2460 C CG2 . THR A 305 ? 1.29017 1.57999 1.48970 -0.14888 0.26624  0.20370  339 THR A CG2 
# 
