data_9EDX
# 
_entry.id   9EDX 
# 
_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   9EDX         pdb_00009edx 10.2210/pdb9edx/pdb 
WWPDB D_1000290239 ?            ?                   
# 
_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                        9EDX 
_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 2a: 2-(4-fluorophenyl)-3-(pyridin-4-yl)pyrazolo[1,5-a]pyridine-6-carbonitrile
;
_citation.year                      ? 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      ? 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
_citation_author.citation_id        primary 
_citation_author.name               'Stogios, P.J.' 
_citation_author.ordinal            1 
_citation_author.identifier_ORCID   ? 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man 'non-specific serine/threonine protein kinase'                              35397.254 1  2.7.11.1 ? ? ? 
2 non-polymer syn '2-(4-fluorophenyl)-3-(pyridin-4-yl)pyrazolo[1,5-a]pyridine-6-carbonitrile' 314.316   1  ?        ? ? ? 
3 non-polymer syn 'CHLORIDE ION'                                                              35.453    2  ?        ? ? ? 
4 water       nat water                                                                       18.015    77 ?        ? ? ? 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;SSVVGLHYKIGKKIGEGSFGVIFEGTNIINGVPVAIKFEPRKTEAPQLRDEYRTYKHLQGCDGIPNAYYFGQEGLHNILV
IDLLGPSLEDLFDWCGRRFSVKTVVQVAIQMLTLVEEVHRHDLIYRDIKPDNFLIGRRGATDENNVHLIDFGMAKQYRDP
RTKQHIPYREKKSLSGTARYMSINTHLGREQSRRDDLEALGHVFFYFLRGQLPWQGLKAPTNKQKYEKIGDKKRTTPAVT
LCDGLPQQFAEYLDSVRSLPFDAEPPYEEYRMLLLSVLDDLGQACDGDMDWMHLNGGRGWDATINKKPN
;
_entity_poly.pdbx_seq_one_letter_code_can   
;SSVVGLHYKIGKKIGEGSFGVIFEGTNIINGVPVAIKFEPRKTEAPQLRDEYRTYKHLQGCDGIPNAYYFGQEGLHNILV
IDLLGPSLEDLFDWCGRRFSVKTVVQVAIQMLTLVEEVHRHDLIYRDIKPDNFLIGRRGATDENNVHLIDFGMAKQYRDP
RTKQHIPYREKKSLSGTARYMSINTHLGREQSRRDDLEALGHVFFYFLRGQLPWQGLKAPTNKQKYEKIGDKKRTTPAVT
LCDGLPQQFAEYLDSVRSLPFDAEPPYEEYRMLLLSVLDDLGQACDGDMDWMHLNGGRGWDATINKKPN
;
_entity_poly.pdbx_strand_id                 A 
_entity_poly.pdbx_target_identifier         IDP97431 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 '2-(4-fluorophenyl)-3-(pyridin-4-yl)pyrazolo[1,5-a]pyridine-6-carbonitrile' A1BIO 
3 'CHLORIDE ION'                                                              CL    
4 water                                                                       HOH   
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   SER n 
1 2   SER n 
1 3   VAL n 
1 4   VAL n 
1 5   GLY n 
1 6   LEU n 
1 7   HIS n 
1 8   TYR n 
1 9   LYS n 
1 10  ILE n 
1 11  GLY n 
1 12  LYS n 
1 13  LYS n 
1 14  ILE n 
1 15  GLY n 
1 16  GLU n 
1 17  GLY n 
1 18  SER n 
1 19  PHE n 
1 20  GLY n 
1 21  VAL n 
1 22  ILE n 
1 23  PHE n 
1 24  GLU n 
1 25  GLY n 
1 26  THR n 
1 27  ASN n 
1 28  ILE n 
1 29  ILE n 
1 30  ASN n 
1 31  GLY n 
1 32  VAL n 
1 33  PRO n 
1 34  VAL n 
1 35  ALA n 
1 36  ILE n 
1 37  LYS n 
1 38  PHE n 
1 39  GLU n 
1 40  PRO n 
1 41  ARG n 
1 42  LYS n 
1 43  THR n 
1 44  GLU n 
1 45  ALA n 
1 46  PRO n 
1 47  GLN n 
1 48  LEU n 
1 49  ARG n 
1 50  ASP n 
1 51  GLU n 
1 52  TYR n 
1 53  ARG n 
1 54  THR n 
1 55  TYR n 
1 56  LYS n 
1 57  HIS n 
1 58  LEU n 
1 59  GLN n 
1 60  GLY n 
1 61  CYS n 
1 62  ASP n 
1 63  GLY n 
1 64  ILE n 
1 65  PRO n 
1 66  ASN n 
1 67  ALA n 
1 68  TYR n 
1 69  TYR n 
1 70  PHE n 
1 71  GLY n 
1 72  GLN n 
1 73  GLU n 
1 74  GLY n 
1 75  LEU n 
1 76  HIS n 
1 77  ASN n 
1 78  ILE n 
1 79  LEU n 
1 80  VAL n 
1 81  ILE n 
1 82  ASP n 
1 83  LEU n 
1 84  LEU n 
1 85  GLY n 
1 86  PRO n 
1 87  SER n 
1 88  LEU n 
1 89  GLU n 
1 90  ASP n 
1 91  LEU n 
1 92  PHE n 
1 93  ASP n 
1 94  TRP n 
1 95  CYS n 
1 96  GLY n 
1 97  ARG n 
1 98  ARG n 
1 99  PHE n 
1 100 SER n 
1 101 VAL n 
1 102 LYS n 
1 103 THR n 
1 104 VAL n 
1 105 VAL n 
1 106 GLN n 
1 107 VAL n 
1 108 ALA n 
1 109 ILE n 
1 110 GLN n 
1 111 MET n 
1 112 LEU n 
1 113 THR n 
1 114 LEU n 
1 115 VAL n 
1 116 GLU n 
1 117 GLU n 
1 118 VAL n 
1 119 HIS n 
1 120 ARG n 
1 121 HIS n 
1 122 ASP n 
1 123 LEU n 
1 124 ILE n 
1 125 TYR n 
1 126 ARG n 
1 127 ASP n 
1 128 ILE n 
1 129 LYS n 
1 130 PRO n 
1 131 ASP n 
1 132 ASN n 
1 133 PHE n 
1 134 LEU n 
1 135 ILE n 
1 136 GLY n 
1 137 ARG n 
1 138 ARG n 
1 139 GLY n 
1 140 ALA n 
1 141 THR n 
1 142 ASP n 
1 143 GLU n 
1 144 ASN n 
1 145 ASN n 
1 146 VAL n 
1 147 HIS n 
1 148 LEU n 
1 149 ILE n 
1 150 ASP n 
1 151 PHE n 
1 152 GLY n 
1 153 MET n 
1 154 ALA n 
1 155 LYS n 
1 156 GLN n 
1 157 TYR n 
1 158 ARG n 
1 159 ASP n 
1 160 PRO n 
1 161 ARG n 
1 162 THR n 
1 163 LYS n 
1 164 GLN n 
1 165 HIS n 
1 166 ILE n 
1 167 PRO n 
1 168 TYR n 
1 169 ARG n 
1 170 GLU n 
1 171 LYS n 
1 172 LYS n 
1 173 SER n 
1 174 LEU n 
1 175 SER n 
1 176 GLY n 
1 177 THR n 
1 178 ALA n 
1 179 ARG n 
1 180 TYR n 
1 181 MET n 
1 182 SER n 
1 183 ILE n 
1 184 ASN n 
1 185 THR n 
1 186 HIS n 
1 187 LEU n 
1 188 GLY n 
1 189 ARG n 
1 190 GLU n 
1 191 GLN n 
1 192 SER n 
1 193 ARG n 
1 194 ARG n 
1 195 ASP n 
1 196 ASP n 
1 197 LEU n 
1 198 GLU n 
1 199 ALA n 
1 200 LEU n 
1 201 GLY n 
1 202 HIS n 
1 203 VAL n 
1 204 PHE n 
1 205 PHE n 
1 206 TYR n 
1 207 PHE n 
1 208 LEU n 
1 209 ARG n 
1 210 GLY n 
1 211 GLN n 
1 212 LEU n 
1 213 PRO n 
1 214 TRP n 
1 215 GLN n 
1 216 GLY n 
1 217 LEU n 
1 218 LYS n 
1 219 ALA n 
1 220 PRO n 
1 221 THR n 
1 222 ASN n 
1 223 LYS n 
1 224 GLN n 
1 225 LYS n 
1 226 TYR n 
1 227 GLU n 
1 228 LYS n 
1 229 ILE n 
1 230 GLY n 
1 231 ASP n 
1 232 LYS n 
1 233 LYS n 
1 234 ARG n 
1 235 THR n 
1 236 THR n 
1 237 PRO n 
1 238 ALA n 
1 239 VAL n 
1 240 THR n 
1 241 LEU n 
1 242 CYS n 
1 243 ASP n 
1 244 GLY n 
1 245 LEU n 
1 246 PRO n 
1 247 GLN n 
1 248 GLN n 
1 249 PHE n 
1 250 ALA n 
1 251 GLU n 
1 252 TYR n 
1 253 LEU n 
1 254 ASP n 
1 255 SER n 
1 256 VAL n 
1 257 ARG n 
1 258 SER n 
1 259 LEU n 
1 260 PRO n 
1 261 PHE n 
1 262 ASP n 
1 263 ALA n 
1 264 GLU n 
1 265 PRO n 
1 266 PRO n 
1 267 TYR n 
1 268 GLU n 
1 269 GLU n 
1 270 TYR n 
1 271 ARG n 
1 272 MET n 
1 273 LEU n 
1 274 LEU n 
1 275 LEU n 
1 276 SER n 
1 277 VAL n 
1 278 LEU n 
1 279 ASP n 
1 280 ASP n 
1 281 LEU n 
1 282 GLY n 
1 283 GLN n 
1 284 ALA n 
1 285 CYS n 
1 286 ASP n 
1 287 GLY n 
1 288 ASP n 
1 289 MET n 
1 290 ASP n 
1 291 TRP n 
1 292 MET n 
1 293 HIS n 
1 294 LEU n 
1 295 ASN n 
1 296 GLY n 
1 297 GLY n 
1 298 ARG n 
1 299 GLY n 
1 300 TRP n 
1 301 ASP n 
1 302 ALA n 
1 303 THR n 
1 304 ILE n 
1 305 ASN n 
1 306 LYS n 
1 307 LYS n 
1 308 PRO n 
1 309 ASN n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   309 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 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 
A1BIO non-polymer         . '2-(4-fluorophenyl)-3-(pyridin-4-yl)pyrazolo[1,5-a]pyridine-6-carbonitrile' ? 'C19 H11 F N4'   314.316 
ALA   'L-peptide linking' y ALANINE                                                                     ? 'C3 H7 N O2'     89.093  
ARG   'L-peptide linking' y ARGININE                                                                    ? 'C6 H15 N4 O2 1' 175.209 
ASN   'L-peptide linking' y ASPARAGINE                                                                  ? 'C4 H8 N2 O3'    132.118 
ASP   'L-peptide linking' y 'ASPARTIC ACID'                                                             ? 'C4 H7 N O4'     133.103 
CL    non-polymer         . 'CHLORIDE ION'                                                              ? 'Cl -1'          35.453  
CYS   'L-peptide linking' y CYSTEINE                                                                    ? 'C3 H7 N O2 S'   121.158 
GLN   'L-peptide linking' y GLUTAMINE                                                                   ? 'C5 H10 N2 O3'   146.144 
GLU   'L-peptide linking' y 'GLUTAMIC ACID'                                                             ? 'C5 H9 N O4'     147.129 
GLY   'peptide linking'   y GLYCINE                                                                     ? 'C2 H5 N O2'     75.067  
HIS   'L-peptide linking' y HISTIDINE                                                                   ? 'C6 H10 N3 O2 1' 156.162 
HOH   non-polymer         . WATER                                                                       ? 'H2 O'           18.015  
ILE   'L-peptide linking' y ISOLEUCINE                                                                  ? 'C6 H13 N O2'    131.173 
LEU   'L-peptide linking' y LEUCINE                                                                     ? 'C6 H13 N O2'    131.173 
LYS   'L-peptide linking' y LYSINE                                                                      ? 'C6 H15 N2 O2 1' 147.195 
MET   'L-peptide linking' y METHIONINE                                                                  ? 'C5 H11 N O2 S'  149.211 
PHE   'L-peptide linking' y PHENYLALANINE                                                               ? 'C9 H11 N O2'    165.189 
PRO   'L-peptide linking' y PROLINE                                                                     ? 'C5 H9 N O2'     115.130 
SER   'L-peptide linking' y SERINE                                                                      ? 'C3 H7 N O3'     105.093 
THR   'L-peptide linking' y THREONINE                                                                   ? 'C4 H9 N O3'     119.119 
TRP   'L-peptide linking' y TRYPTOPHAN                                                                  ? 'C11 H12 N2 O2'  204.225 
TYR   'L-peptide linking' y TYROSINE                                                                    ? 'C9 H11 N O3'    181.189 
VAL   'L-peptide linking' y VALINE                                                                      ? 'C5 H11 N O2'    117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   SER 1   37  37  SER SER A . n 
A 1 2   SER 2   38  38  SER SER A . n 
A 1 3   VAL 3   39  39  VAL VAL A . n 
A 1 4   VAL 4   40  40  VAL VAL A . n 
A 1 5   GLY 5   41  41  GLY GLY A . n 
A 1 6   LEU 6   42  42  LEU LEU A . n 
A 1 7   HIS 7   43  43  HIS HIS A . n 
A 1 8   TYR 8   44  44  TYR TYR A . n 
A 1 9   LYS 9   45  45  LYS LYS A . n 
A 1 10  ILE 10  46  46  ILE ILE A . n 
A 1 11  GLY 11  47  47  GLY GLY A . n 
A 1 12  LYS 12  48  48  LYS LYS A . n 
A 1 13  LYS 13  49  49  LYS LYS A . n 
A 1 14  ILE 14  50  50  ILE ILE A . n 
A 1 15  GLY 15  51  51  GLY GLY A . n 
A 1 16  GLU 16  52  52  GLU GLU A . n 
A 1 17  GLY 17  53  53  GLY GLY A . n 
A 1 18  SER 18  54  54  SER SER A . n 
A 1 19  PHE 19  55  55  PHE PHE A . n 
A 1 20  GLY 20  56  56  GLY GLY A . n 
A 1 21  VAL 21  57  57  VAL VAL A . n 
A 1 22  ILE 22  58  58  ILE ILE A . n 
A 1 23  PHE 23  59  59  PHE PHE A . n 
A 1 24  GLU 24  60  60  GLU GLU A . n 
A 1 25  GLY 25  61  61  GLY GLY A . n 
A 1 26  THR 26  62  62  THR THR A . n 
A 1 27  ASN 27  63  63  ASN ASN A . n 
A 1 28  ILE 28  64  64  ILE ILE A . n 
A 1 29  ILE 29  65  65  ILE ILE A . n 
A 1 30  ASN 30  66  66  ASN ASN A . n 
A 1 31  GLY 31  67  67  GLY GLY A . n 
A 1 32  VAL 32  68  68  VAL VAL A . n 
A 1 33  PRO 33  69  69  PRO PRO A . n 
A 1 34  VAL 34  70  70  VAL VAL A . n 
A 1 35  ALA 35  71  71  ALA ALA A . n 
A 1 36  ILE 36  72  72  ILE ILE A . n 
A 1 37  LYS 37  73  73  LYS LYS A . n 
A 1 38  PHE 38  74  74  PHE PHE A . n 
A 1 39  GLU 39  75  75  GLU GLU A . n 
A 1 40  PRO 40  76  76  PRO PRO A . n 
A 1 41  ARG 41  77  77  ARG ARG A . n 
A 1 42  LYS 42  78  78  LYS LYS A . n 
A 1 43  THR 43  79  79  THR THR A . n 
A 1 44  GLU 44  80  80  GLU GLU A . n 
A 1 45  ALA 45  81  81  ALA ALA A . n 
A 1 46  PRO 46  82  82  PRO PRO A . n 
A 1 47  GLN 47  83  83  GLN GLN A . n 
A 1 48  LEU 48  84  84  LEU LEU A . n 
A 1 49  ARG 49  85  85  ARG ARG A . n 
A 1 50  ASP 50  86  86  ASP ASP A . n 
A 1 51  GLU 51  87  87  GLU GLU A . n 
A 1 52  TYR 52  88  88  TYR TYR A . n 
A 1 53  ARG 53  89  89  ARG ARG A . n 
A 1 54  THR 54  90  90  THR THR A . n 
A 1 55  TYR 55  91  91  TYR TYR A . n 
A 1 56  LYS 56  92  92  LYS LYS A . n 
A 1 57  HIS 57  93  93  HIS HIS A . n 
A 1 58  LEU 58  94  94  LEU LEU A . n 
A 1 59  GLN 59  95  95  GLN GLN A . n 
A 1 60  GLY 60  96  96  GLY GLY A . n 
A 1 61  CYS 61  97  97  CYS CYS A . n 
A 1 62  ASP 62  98  98  ASP ASP A . n 
A 1 63  GLY 63  99  99  GLY GLY A . n 
A 1 64  ILE 64  100 100 ILE ILE A . n 
A 1 65  PRO 65  101 101 PRO PRO A . n 
A 1 66  ASN 66  102 102 ASN ASN A . n 
A 1 67  ALA 67  103 103 ALA ALA A . n 
A 1 68  TYR 68  104 104 TYR TYR A . n 
A 1 69  TYR 69  105 105 TYR TYR A . n 
A 1 70  PHE 70  106 106 PHE PHE A . n 
A 1 71  GLY 71  107 107 GLY GLY A . n 
A 1 72  GLN 72  108 108 GLN GLN A . n 
A 1 73  GLU 73  109 109 GLU GLU A . n 
A 1 74  GLY 74  110 110 GLY GLY A . n 
A 1 75  LEU 75  111 111 LEU LEU A . n 
A 1 76  HIS 76  112 112 HIS HIS A . n 
A 1 77  ASN 77  113 113 ASN ASN A . n 
A 1 78  ILE 78  114 114 ILE ILE A . n 
A 1 79  LEU 79  115 115 LEU LEU A . n 
A 1 80  VAL 80  116 116 VAL VAL A . n 
A 1 81  ILE 81  117 117 ILE ILE A . n 
A 1 82  ASP 82  118 118 ASP ASP A . n 
A 1 83  LEU 83  119 119 LEU LEU A . n 
A 1 84  LEU 84  120 120 LEU LEU A . n 
A 1 85  GLY 85  121 121 GLY GLY A . n 
A 1 86  PRO 86  122 122 PRO PRO A . n 
A 1 87  SER 87  123 123 SER SER A . n 
A 1 88  LEU 88  124 124 LEU LEU A . n 
A 1 89  GLU 89  125 125 GLU GLU A . n 
A 1 90  ASP 90  126 126 ASP ASP A . n 
A 1 91  LEU 91  127 127 LEU LEU A . n 
A 1 92  PHE 92  128 128 PHE PHE A . n 
A 1 93  ASP 93  129 129 ASP ASP A . n 
A 1 94  TRP 94  130 130 TRP TRP A . n 
A 1 95  CYS 95  131 131 CYS CYS A . n 
A 1 96  GLY 96  132 132 GLY GLY A . n 
A 1 97  ARG 97  133 133 ARG ARG A . n 
A 1 98  ARG 98  134 134 ARG ARG A . n 
A 1 99  PHE 99  135 135 PHE PHE A . n 
A 1 100 SER 100 136 136 SER SER A . n 
A 1 101 VAL 101 137 137 VAL VAL A . n 
A 1 102 LYS 102 138 138 LYS LYS A . n 
A 1 103 THR 103 139 139 THR THR A . n 
A 1 104 VAL 104 140 140 VAL VAL A . n 
A 1 105 VAL 105 141 141 VAL VAL A . n 
A 1 106 GLN 106 142 142 GLN GLN A . n 
A 1 107 VAL 107 143 143 VAL VAL A . n 
A 1 108 ALA 108 144 144 ALA ALA A . n 
A 1 109 ILE 109 145 145 ILE ILE A . n 
A 1 110 GLN 110 146 146 GLN GLN A . n 
A 1 111 MET 111 147 147 MET MET A . n 
A 1 112 LEU 112 148 148 LEU LEU A . n 
A 1 113 THR 113 149 149 THR THR A . n 
A 1 114 LEU 114 150 150 LEU LEU A . n 
A 1 115 VAL 115 151 151 VAL VAL A . n 
A 1 116 GLU 116 152 152 GLU GLU A . n 
A 1 117 GLU 117 153 153 GLU GLU A . n 
A 1 118 VAL 118 154 154 VAL VAL A . n 
A 1 119 HIS 119 155 155 HIS HIS A . n 
A 1 120 ARG 120 156 156 ARG ARG A . n 
A 1 121 HIS 121 157 157 HIS HIS A . n 
A 1 122 ASP 122 158 158 ASP ASP A . n 
A 1 123 LEU 123 159 159 LEU LEU A . n 
A 1 124 ILE 124 160 160 ILE ILE A . n 
A 1 125 TYR 125 161 161 TYR TYR A . n 
A 1 126 ARG 126 162 162 ARG ARG A . n 
A 1 127 ASP 127 163 163 ASP ASP A . n 
A 1 128 ILE 128 164 164 ILE ILE A . n 
A 1 129 LYS 129 165 165 LYS LYS A . n 
A 1 130 PRO 130 166 166 PRO PRO A . n 
A 1 131 ASP 131 167 167 ASP ASP A . n 
A 1 132 ASN 132 168 168 ASN ASN A . n 
A 1 133 PHE 133 169 169 PHE PHE A . n 
A 1 134 LEU 134 170 170 LEU LEU A . n 
A 1 135 ILE 135 171 171 ILE ILE A . n 
A 1 136 GLY 136 172 172 GLY GLY A . n 
A 1 137 ARG 137 173 173 ARG ARG A . n 
A 1 138 ARG 138 174 174 ARG ARG A . n 
A 1 139 GLY 139 175 175 GLY GLY A . n 
A 1 140 ALA 140 176 176 ALA ALA A . n 
A 1 141 THR 141 177 177 THR THR A . n 
A 1 142 ASP 142 178 178 ASP ASP A . n 
A 1 143 GLU 143 179 179 GLU GLU A . n 
A 1 144 ASN 144 180 180 ASN ASN A . n 
A 1 145 ASN 145 181 181 ASN ASN A . n 
A 1 146 VAL 146 182 182 VAL VAL A . n 
A 1 147 HIS 147 183 183 HIS HIS A . n 
A 1 148 LEU 148 184 184 LEU LEU A . n 
A 1 149 ILE 149 185 185 ILE ILE A . n 
A 1 150 ASP 150 186 186 ASP ASP A . n 
A 1 151 PHE 151 187 187 PHE PHE A . n 
A 1 152 GLY 152 188 188 GLY GLY A . n 
A 1 153 MET 153 189 189 MET MET A . n 
A 1 154 ALA 154 190 190 ALA ALA A . n 
A 1 155 LYS 155 191 191 LYS LYS A . n 
A 1 156 GLN 156 192 192 GLN GLN A . n 
A 1 157 TYR 157 193 193 TYR TYR A . n 
A 1 158 ARG 158 194 194 ARG ARG A . n 
A 1 159 ASP 159 195 195 ASP ASP A . n 
A 1 160 PRO 160 196 196 PRO PRO A . n 
A 1 161 ARG 161 197 197 ARG ARG A . n 
A 1 162 THR 162 198 198 THR THR A . n 
A 1 163 LYS 163 199 199 LYS LYS A . n 
A 1 164 GLN 164 200 200 GLN GLN A . n 
A 1 165 HIS 165 201 201 HIS HIS A . n 
A 1 166 ILE 166 202 202 ILE ILE A . n 
A 1 167 PRO 167 203 203 PRO PRO A . n 
A 1 168 TYR 168 204 204 TYR TYR A . n 
A 1 169 ARG 169 205 205 ARG ARG A . n 
A 1 170 GLU 170 206 206 GLU GLU A . n 
A 1 171 LYS 171 207 207 LYS LYS A . n 
A 1 172 LYS 172 208 208 LYS LYS A . n 
A 1 173 SER 173 209 209 SER SER A . n 
A 1 174 LEU 174 210 210 LEU LEU A . n 
A 1 175 SER 175 211 211 SER SER A . n 
A 1 176 GLY 176 212 212 GLY GLY A . n 
A 1 177 THR 177 213 213 THR THR A . n 
A 1 178 ALA 178 214 214 ALA ALA A . n 
A 1 179 ARG 179 215 215 ARG ARG A . n 
A 1 180 TYR 180 216 216 TYR TYR A . n 
A 1 181 MET 181 217 217 MET MET A . n 
A 1 182 SER 182 218 218 SER SER A . n 
A 1 183 ILE 183 219 219 ILE ILE A . n 
A 1 184 ASN 184 220 220 ASN ASN A . n 
A 1 185 THR 185 221 221 THR THR A . n 
A 1 186 HIS 186 222 222 HIS HIS A . n 
A 1 187 LEU 187 223 223 LEU LEU A . n 
A 1 188 GLY 188 224 224 GLY GLY A . n 
A 1 189 ARG 189 225 225 ARG ARG A . n 
A 1 190 GLU 190 226 226 GLU GLU A . n 
A 1 191 GLN 191 227 227 GLN GLN A . n 
A 1 192 SER 192 228 228 SER SER A . n 
A 1 193 ARG 193 229 229 ARG ARG A . n 
A 1 194 ARG 194 230 230 ARG ARG A . n 
A 1 195 ASP 195 231 231 ASP ASP A . n 
A 1 196 ASP 196 232 232 ASP ASP A . n 
A 1 197 LEU 197 233 233 LEU LEU A . n 
A 1 198 GLU 198 234 234 GLU GLU A . n 
A 1 199 ALA 199 235 235 ALA ALA A . n 
A 1 200 LEU 200 236 236 LEU LEU A . n 
A 1 201 GLY 201 237 237 GLY GLY A . n 
A 1 202 HIS 202 238 238 HIS HIS A . n 
A 1 203 VAL 203 239 239 VAL VAL A . n 
A 1 204 PHE 204 240 240 PHE PHE A . n 
A 1 205 PHE 205 241 241 PHE PHE A . n 
A 1 206 TYR 206 242 242 TYR TYR A . n 
A 1 207 PHE 207 243 243 PHE PHE A . n 
A 1 208 LEU 208 244 244 LEU LEU A . n 
A 1 209 ARG 209 245 245 ARG ARG A . n 
A 1 210 GLY 210 246 246 GLY GLY A . n 
A 1 211 GLN 211 247 247 GLN GLN A . n 
A 1 212 LEU 212 248 248 LEU LEU A . n 
A 1 213 PRO 213 249 249 PRO PRO A . n 
A 1 214 TRP 214 250 250 TRP TRP A . n 
A 1 215 GLN 215 251 251 GLN GLN A . n 
A 1 216 GLY 216 252 252 GLY GLY A . n 
A 1 217 LEU 217 253 253 LEU LEU A . n 
A 1 218 LYS 218 254 254 LYS LYS A . n 
A 1 219 ALA 219 255 255 ALA ALA A . n 
A 1 220 PRO 220 256 256 PRO PRO A . n 
A 1 221 THR 221 257 257 THR THR A . n 
A 1 222 ASN 222 258 258 ASN ASN A . n 
A 1 223 LYS 223 259 259 LYS LYS A . n 
A 1 224 GLN 224 260 260 GLN GLN A . n 
A 1 225 LYS 225 261 261 LYS LYS A . n 
A 1 226 TYR 226 262 262 TYR TYR A . n 
A 1 227 GLU 227 263 263 GLU GLU A . n 
A 1 228 LYS 228 264 264 LYS LYS A . n 
A 1 229 ILE 229 265 265 ILE ILE A . n 
A 1 230 GLY 230 266 266 GLY GLY A . n 
A 1 231 ASP 231 267 267 ASP ASP A . n 
A 1 232 LYS 232 268 268 LYS LYS A . n 
A 1 233 LYS 233 269 269 LYS LYS A . n 
A 1 234 ARG 234 270 270 ARG ARG A . n 
A 1 235 THR 235 271 271 THR THR A . n 
A 1 236 THR 236 272 272 THR THR A . n 
A 1 237 PRO 237 273 273 PRO PRO A . n 
A 1 238 ALA 238 274 274 ALA ALA A . n 
A 1 239 VAL 239 275 275 VAL VAL A . n 
A 1 240 THR 240 276 276 THR THR A . n 
A 1 241 LEU 241 277 277 LEU LEU A . n 
A 1 242 CYS 242 278 278 CYS CYS A . n 
A 1 243 ASP 243 279 279 ASP ASP A . n 
A 1 244 GLY 244 280 280 GLY GLY A . n 
A 1 245 LEU 245 281 281 LEU LEU A . n 
A 1 246 PRO 246 282 282 PRO PRO A . n 
A 1 247 GLN 247 283 283 GLN GLN A . n 
A 1 248 GLN 248 284 284 GLN GLN A . n 
A 1 249 PHE 249 285 285 PHE PHE A . n 
A 1 250 ALA 250 286 286 ALA ALA A . n 
A 1 251 GLU 251 287 287 GLU GLU A . n 
A 1 252 TYR 252 288 288 TYR TYR A . n 
A 1 253 LEU 253 289 289 LEU LEU A . n 
A 1 254 ASP 254 290 290 ASP ASP A . n 
A 1 255 SER 255 291 291 SER SER A . n 
A 1 256 VAL 256 292 292 VAL VAL A . n 
A 1 257 ARG 257 293 293 ARG ARG A . n 
A 1 258 SER 258 294 294 SER SER A . n 
A 1 259 LEU 259 295 295 LEU LEU A . n 
A 1 260 PRO 260 296 296 PRO PRO A . n 
A 1 261 PHE 261 297 297 PHE PHE A . n 
A 1 262 ASP 262 298 298 ASP ASP A . n 
A 1 263 ALA 263 299 299 ALA ALA A . n 
A 1 264 GLU 264 300 300 GLU GLU A . n 
A 1 265 PRO 265 301 301 PRO PRO A . n 
A 1 266 PRO 266 302 302 PRO PRO A . n 
A 1 267 TYR 267 303 303 TYR TYR A . n 
A 1 268 GLU 268 304 304 GLU GLU A . n 
A 1 269 GLU 269 305 305 GLU GLU A . n 
A 1 270 TYR 270 306 306 TYR TYR A . n 
A 1 271 ARG 271 307 307 ARG ARG A . n 
A 1 272 MET 272 308 308 MET MET A . n 
A 1 273 LEU 273 309 309 LEU LEU A . n 
A 1 274 LEU 274 310 310 LEU LEU A . n 
A 1 275 LEU 275 311 311 LEU LEU A . n 
A 1 276 SER 276 312 312 SER SER A . n 
A 1 277 VAL 277 313 313 VAL VAL A . n 
A 1 278 LEU 278 314 314 LEU LEU A . n 
A 1 279 ASP 279 315 315 ASP ASP A . n 
A 1 280 ASP 280 316 316 ASP ASP A . n 
A 1 281 LEU 281 317 317 LEU LEU A . n 
A 1 282 GLY 282 318 318 GLY GLY A . n 
A 1 283 GLN 283 319 319 GLN GLN A . n 
A 1 284 ALA 284 320 320 ALA ALA A . n 
A 1 285 CYS 285 321 321 CYS CYS A . n 
A 1 286 ASP 286 322 322 ASP ASP A . n 
A 1 287 GLY 287 323 323 GLY GLY A . n 
A 1 288 ASP 288 324 324 ASP ASP A . n 
A 1 289 MET 289 325 325 MET MET A . n 
A 1 290 ASP 290 326 326 ASP ASP A . n 
A 1 291 TRP 291 327 327 TRP TRP A . n 
A 1 292 MET 292 328 328 MET MET A . n 
A 1 293 HIS 293 329 329 HIS HIS A . n 
A 1 294 LEU 294 330 330 LEU LEU A . n 
A 1 295 ASN 295 331 331 ASN ASN A . n 
A 1 296 GLY 296 332 332 GLY GLY A . n 
A 1 297 GLY 297 333 333 GLY GLY A . n 
A 1 298 ARG 298 334 334 ARG ARG A . n 
A 1 299 GLY 299 335 335 GLY GLY A . n 
A 1 300 TRP 300 336 336 TRP TRP A . n 
A 1 301 ASP 301 337 337 ASP ASP A . n 
A 1 302 ALA 302 338 338 ALA ALA A . n 
A 1 303 THR 303 339 339 THR THR A . n 
A 1 304 ILE 304 340 340 ILE ILE A . n 
A 1 305 ASN 305 341 341 ASN ASN A . n 
A 1 306 LYS 306 342 342 LYS LYS A . n 
A 1 307 LYS 307 343 ?   ?   ?   A . n 
A 1 308 PRO 308 344 ?   ?   ?   A . n 
A 1 309 ASN 309 345 ?   ?   ?   A . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1BIO 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1BIO 
_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 A1BIO 1  401 401 A1BIO LIG A . 
C 3 CL    1  402 1   CL    CL  A . 
D 3 CL    1  403 2   CL    CL  A . 
E 4 HOH   1  501 54  HOH   HOH A . 
E 4 HOH   2  502 58  HOH   HOH A . 
E 4 HOH   3  503 3   HOH   HOH A . 
E 4 HOH   4  504 12  HOH   HOH A . 
E 4 HOH   5  505 31  HOH   HOH A . 
E 4 HOH   6  506 47  HOH   HOH A . 
E 4 HOH   7  507 68  HOH   HOH A . 
E 4 HOH   8  508 52  HOH   HOH A . 
E 4 HOH   9  509 67  HOH   HOH A . 
E 4 HOH   10 510 6   HOH   HOH A . 
E 4 HOH   11 511 29  HOH   HOH A . 
E 4 HOH   12 512 33  HOH   HOH A . 
E 4 HOH   13 513 42  HOH   HOH A . 
E 4 HOH   14 514 20  HOH   HOH A . 
E 4 HOH   15 515 65  HOH   HOH A . 
E 4 HOH   16 516 69  HOH   HOH A . 
E 4 HOH   17 517 15  HOH   HOH A . 
E 4 HOH   18 518 27  HOH   HOH A . 
E 4 HOH   19 519 25  HOH   HOH A . 
E 4 HOH   20 520 43  HOH   HOH A . 
E 4 HOH   21 521 66  HOH   HOH A . 
E 4 HOH   22 522 18  HOH   HOH A . 
E 4 HOH   23 523 83  HOH   HOH A . 
E 4 HOH   24 524 39  HOH   HOH A . 
E 4 HOH   25 525 8   HOH   HOH A . 
E 4 HOH   26 526 13  HOH   HOH A . 
E 4 HOH   27 527 24  HOH   HOH A . 
E 4 HOH   28 528 16  HOH   HOH A . 
E 4 HOH   29 529 32  HOH   HOH A . 
E 4 HOH   30 530 40  HOH   HOH A . 
E 4 HOH   31 531 11  HOH   HOH A . 
E 4 HOH   32 532 37  HOH   HOH A . 
E 4 HOH   33 533 80  HOH   HOH A . 
E 4 HOH   34 534 7   HOH   HOH A . 
E 4 HOH   35 535 48  HOH   HOH A . 
E 4 HOH   36 536 35  HOH   HOH A . 
E 4 HOH   37 537 34  HOH   HOH A . 
E 4 HOH   38 538 28  HOH   HOH A . 
E 4 HOH   39 539 74  HOH   HOH A . 
E 4 HOH   40 540 17  HOH   HOH A . 
E 4 HOH   41 541 70  HOH   HOH A . 
E 4 HOH   42 542 21  HOH   HOH A . 
E 4 HOH   43 543 82  HOH   HOH A . 
E 4 HOH   44 544 44  HOH   HOH A . 
E 4 HOH   45 545 9   HOH   HOH A . 
E 4 HOH   46 546 26  HOH   HOH A . 
E 4 HOH   47 547 76  HOH   HOH A . 
E 4 HOH   48 548 46  HOH   HOH A . 
E 4 HOH   49 549 79  HOH   HOH A . 
E 4 HOH   50 550 72  HOH   HOH A . 
E 4 HOH   51 551 73  HOH   HOH A . 
E 4 HOH   52 552 75  HOH   HOH A . 
E 4 HOH   53 553 23  HOH   HOH A . 
E 4 HOH   54 554 84  HOH   HOH A . 
E 4 HOH   55 555 77  HOH   HOH A . 
E 4 HOH   56 556 50  HOH   HOH A . 
E 4 HOH   57 557 81  HOH   HOH A . 
E 4 HOH   58 558 1   HOH   HOH A . 
E 4 HOH   59 559 56  HOH   HOH A . 
E 4 HOH   60 560 87  HOH   HOH A . 
E 4 HOH   61 561 4   HOH   HOH A . 
E 4 HOH   62 562 5   HOH   HOH A . 
E 4 HOH   63 563 36  HOH   HOH A . 
E 4 HOH   64 564 53  HOH   HOH A . 
E 4 HOH   65 565 49  HOH   HOH A . 
E 4 HOH   66 566 85  HOH   HOH A . 
E 4 HOH   67 567 38  HOH   HOH A . 
E 4 HOH   68 568 57  HOH   HOH A . 
E 4 HOH   69 569 86  HOH   HOH A . 
E 4 HOH   70 570 59  HOH   HOH A . 
E 4 HOH   71 571 64  HOH   HOH A . 
E 4 HOH   72 572 71  HOH   HOH A . 
E 4 HOH   73 573 78  HOH   HOH A . 
E 4 HOH   74 574 63  HOH   HOH A . 
E 4 HOH   75 575 45  HOH   HOH A . 
E 4 HOH   76 576 41  HOH   HOH A . 
E 4 HOH   77 577 22  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                     9EDX 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     91.710 
_cell.length_a_esd                 ? 
_cell.length_b                     91.710 
_cell.length_b_esd                 ? 
_cell.length_c                     118.950 
_cell.length_c_esd                 ? 
_cell.volume                       866419.992 
_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                         9EDX 
_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                   9EDX 
_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             2.72 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          54.77 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              8 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '0.1 M Tris pH 8, 25 mM Magnesium chloride, 20% (w/v) PEG3350' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            298 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     298 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS EIGER X 9M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2023-06-28 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   1.18077 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'CLSI BEAMLINE 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                          50.23 
_reflns.entry_id                                       9EDX 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.03 
_reflns.d_resolution_low                               29.11 
_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                                     24095 
_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                           100 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                10.2 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          19.2 
_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                                0.029 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   1.00 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.059 
_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                                    2.03 
_reflns_shell.d_res_low                                     2.08 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           1.0 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             1774 
_reflns_shell.percent_possible_obs                          ? 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               10.4 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               ? 
_reflns_shell.pdbx_Rpim_I_all                               1.044 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.439 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          99.9 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  2.138 
_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                               71.90 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  ? 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 9EDX 
_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                            2.03 
_refine.ls_d_res_low                             29.11 
_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                     24095 
_refine.ls_number_reflns_R_free                  1205 
_refine.ls_number_reflns_R_work                  22890 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.99 
_refine.ls_percent_reflns_R_free                 5.00 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2167 
_refine.ls_R_factor_R_free                       0.2386 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2156 
_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                 34.0845 
_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                            0.3133 
_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                       2.03 
_refine_hist.d_res_low                        29.11 
_refine_hist.number_atoms_solvent             77 
_refine_hist.number_atoms_total               2572 
_refine_hist.number_reflns_all                ? 
_refine_hist.number_reflns_obs                ? 
_refine_hist.number_reflns_R_free             ? 
_refine_hist.number_reflns_R_work             ? 
_refine_hist.R_factor_all                     ? 
_refine_hist.R_factor_obs                     ? 
_refine_hist.R_factor_R_free                  ? 
_refine_hist.R_factor_R_work                  ? 
_refine_hist.pdbx_number_residues_total       ? 
_refine_hist.pdbx_B_iso_mean_ligand           ? 
_refine_hist.pdbx_B_iso_mean_solvent          ? 
_refine_hist.pdbx_number_atoms_protein        2469 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         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' ? 0.0029  ? 2555 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.5134  ? 3453 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 0.0385  ? 358  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.0055  ? 451  ? f_plane_restr      ? ? 
'X-RAY DIFFRACTION' ? 13.6986 ? 956  ? f_dihedral_angle_d ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 2.03 2.11  . . 167 2507 100.00 . . . . 0.3560 . . . . . . . . . . . 0.3454 
'X-RAY DIFFRACTION' 2.11 2.21  . . 161 2542 100.00 . . . . 0.3017 . . . . . . . . . . . 0.3482 
'X-RAY DIFFRACTION' 2.21 2.32  . . 83  2550 99.96  . . . . 0.2909 . . . . . . . . . . . 0.3139 
'X-RAY DIFFRACTION' 2.32 2.47  . . 114 2567 100.00 . . . . 0.2466 . . . . . . . . . . . 0.2461 
'X-RAY DIFFRACTION' 2.47 2.66  . . 149 2530 100.00 . . . . 0.2568 . . . . . . . . . . . 0.2727 
'X-RAY DIFFRACTION' 2.66 2.93  . . 162 2505 100.00 . . . . 0.2647 . . . . . . . . . . . 0.2996 
'X-RAY DIFFRACTION' 2.93 3.35  . . 129 2552 100.00 . . . . 0.2346 . . . . . . . . . . . 0.2407 
'X-RAY DIFFRACTION' 3.35 4.22  . . 94  2594 100.00 . . . . 0.1920 . . . . . . . . . . . 0.2354 
'X-RAY DIFFRACTION' 4.22 29.11 . . 146 2543 100.00 . . . . 0.1829 . . . . . . . . . . . 0.1998 
# 
_struct.entry_id                     9EDX 
_struct.title                        
;Crystal structure of Yck2 from Candida albicans in complex with inhibitor 2a: 2-(4-fluorophenyl)-3-(pyridin-4-yl)pyrazolo[1,5-a]pyridine-6-carbonitrile
;
_struct.pdbx_model_details           ? 
_struct.pdbx_formula_weight          ? 
_struct.pdbx_formula_weight_method   ? 
_struct.pdbx_model_type_details      ? 
_struct.pdbx_CASP_flag               N 
# 
_struct_keywords.entry_id        9EDX 
_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 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   
;SSVVGLHYKIGKKIGEGSFGVIFEGTNIINGVPVAIKFEPRKTEAPQLRDEYRTYKHLQGCDGIPNAYYFGQEGLHNILV
IDLLGPSLEDLFDWCGRRFSVKTVVQVAIQMLTLVEEVHRHDLIYRDIKPDNFLIGRRGATDENNVHLIDFGMAKQYRDP
RTKQHIPYREKKSLSGTARYMSINTHLGREQSRRDDLEALGHVFFYFLRGQLPWQGLKAPTNKQKYEKIGDKKRTTPAVT
LCDGLPQQFAEYLDSVRSLPFDAEPPYEEYRMLLLSVLDDLGQACDGDMDWMHLNGGRGWDATINKKPN
;
_struct_ref.pdbx_align_begin           37 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              9EDX 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 1 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 309 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             A0A8H6C375 
_struct_ref_seq.db_align_beg                  37 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  345 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       37 
_struct_ref_seq.pdbx_auth_seq_align_end       345 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'gel filtration' 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 GLN A 47  ? LEU A 58  ? GLN A 83  LEU A 94  1 ? 12 
HELX_P HELX_P2  AA2 SER A 87  ? CYS A 95  ? SER A 123 CYS A 131 1 ? 9  
HELX_P HELX_P3  AA3 SER A 100 ? HIS A 121 ? SER A 136 HIS A 157 1 ? 22 
HELX_P HELX_P4  AA4 SER A 182 ? LEU A 187 ? SER A 218 LEU A 223 1 ? 6  
HELX_P HELX_P5  AA5 SER A 192 ? GLY A 210 ? SER A 228 GLY A 246 1 ? 19 
HELX_P HELX_P6  AA6 THR A 221 ? THR A 236 ? THR A 257 THR A 272 1 ? 16 
HELX_P HELX_P7  AA7 PRO A 237 ? CYS A 242 ? PRO A 273 CYS A 278 1 ? 6  
HELX_P HELX_P8  AA8 GLN A 247 ? SER A 258 ? GLN A 283 SER A 294 1 ? 12 
HELX_P HELX_P9  AA9 PRO A 266 ? LEU A 281 ? PRO A 302 LEU A 317 1 ? 16 
HELX_P HELX_P10 AB1 MET A 289 ? ARG A 298 ? MET A 325 ARG A 334 5 ? 10 
HELX_P HELX_P11 AB2 ASP A 301 ? LYS A 306 ? ASP A 337 LYS A 342 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 3   ? VAL A 4   ? VAL A 39  VAL A 40  
AA1 2 TYR A 8   ? GLY A 17  ? TYR A 44  GLY A 53  
AA1 3 GLY A 20  ? ASN A 27  ? GLY A 56  ASN A 63  
AA1 4 PRO A 33  ? PRO A 40  ? PRO A 69  PRO A 76  
AA1 5 HIS A 76  ? ASP A 82  ? HIS A 112 ASP A 118 
AA1 6 ALA A 67  ? GLY A 71  ? ALA A 103 GLY A 107 
AA2 1 LEU A 123 ? ILE A 124 ? LEU A 159 ILE A 160 
AA2 2 LYS A 155 ? GLN A 156 ? LYS A 191 GLN A 192 
AA3 1 PHE A 133 ? LEU A 134 ? PHE A 169 LEU A 170 
AA3 2 HIS A 147 ? LEU A 148 ? HIS A 183 LEU A 184 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N VAL A 4   ? N VAL A 40  O TYR A 8   ? O TYR A 44  
AA1 2 3 N LYS A 12  ? N LYS A 48  O GLU A 24  ? O GLU A 60  
AA1 3 4 N VAL A 21  ? N VAL A 57  O PHE A 38  ? O PHE A 74  
AA1 4 5 N GLU A 39  ? N GLU A 75  O ASN A 77  ? O ASN A 113 
AA1 5 6 O VAL A 80  ? O VAL A 116 N TYR A 68  ? N TYR A 104 
AA2 1 2 N ILE A 124 ? N ILE A 160 O LYS A 155 ? O LYS A 191 
AA3 1 2 N LEU A 134 ? N LEU A 170 O HIS A 147 ? O HIS A 183 
# 
_pdbx_entry_details.entry_id                   9EDX 
_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  ? ? 70.60   -41.74 
2 1 GLU A 52  ? ? -166.36 73.70  
3 1 ASP A 163 ? ? -142.46 39.97  
4 1 ASP A 186 ? ? 61.10   90.83  
# 
_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 23.1220312988 -8.46930253796 -12.6548766363 0.545875278661 ? 0.127653958849    ? -0.152566547289 ? 
0.515284839175 ? -0.0680163797969  ? 0.830448676675 ? 5.33223430002 ? 2.43188644994  ? -1.64544776521  ? 4.94315046169 ? 
-0.234128676786 ? 3.48210880363 ? -0.227738587111 ? 0.584427326937  ? 0.343408772109  ? -0.613893493822 ? 0.0894944192857  ? 
0.913757006786   ? -0.494584375259 ? -0.721659606583 ? 0.122106054103   ? 
2 'X-RAY DIFFRACTION' ? refined 16.9110316393 -25.7542587425 -6.83515101095 0.348340927372 ? -0.00624101865254 ? 0.0244223470047 ? 
0.441060070162 ? 0.000835592179168 ? 0.452544014934 ? 6.35279825698 ? -1.87222638818 ? -1.30124207833  ? 4.56671201552 ? 
-0.225987323629 ? 1.74907268179 ? 0.0991526456731 ? 0.0517548850389 ? 0.630115493365  ? 0.127828266614  ? 0.00931575373839 ? 
-0.0487268156773 ? -0.264675812905 ? -0.263406250402 ? -0.112314000769  ? 
3 'X-RAY DIFFRACTION' ? refined 14.9578557845 -36.881281275  -9.67536819714 0.319823397877 ? -0.0667327012855  ? 0.0133041664717 ? 
0.402095612922 ? -0.00383414935547 ? 0.341196850114 ? 4.04261246844 ? -1.21576312933 ? 0.0849748316053 ? 3.16009749454 ? 
-0.108104681248 ? 2.59232148493 ? 0.0724309797273 ? -0.037663682825 ? -0.285212990035 ? -0.126994207766 ? -0.0885664124524 ? 
0.115055977922   ? 0.186885925241  ? -0.291078303303 ? 0.00827619125905 ? 
# 
loop_
_pdbx_refine_tls_group.id 
_pdbx_refine_tls_group.pdbx_refine_id 
_pdbx_refine_tls_group.refine_tls_id 
_pdbx_refine_tls_group.beg_label_asym_id 
_pdbx_refine_tls_group.beg_label_seq_id 
_pdbx_refine_tls_group.beg_auth_asym_id 
_pdbx_refine_tls_group.beg_auth_seq_id 
_pdbx_refine_tls_group.beg_PDB_ins_code 
_pdbx_refine_tls_group.end_label_asym_id 
_pdbx_refine_tls_group.end_label_seq_id 
_pdbx_refine_tls_group.end_auth_asym_id 
_pdbx_refine_tls_group.end_auth_seq_id 
_pdbx_refine_tls_group.end_PDB_ins_code 
_pdbx_refine_tls_group.selection 
_pdbx_refine_tls_group.selection_details 
1 'X-RAY DIFFRACTION' 1 A 1   A 37  ? A 82  A 118 ? ? 
;chain 'A' and (resid 37 through 118 )
;
2 'X-RAY DIFFRACTION' 2 A 83  A 119 ? A 177 A 213 ? ? 
;chain 'A' and (resid 119 through 213 )
;
3 'X-RAY DIFFRACTION' 3 A 178 A 214 ? A 306 A 342 ? ? 
;chain 'A' and (resid 214 through 342 )
;
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1 1 Y 1 A LYS 343 ? A LYS 307 
2 1 Y 1 A PRO 344 ? A PRO 308 
3 1 Y 1 A ASN 345 ? A ASN 309 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
A1BIO C13  C  Y N 1   
A1BIO C15  C  N N 2   
A1BIO C17  C  Y N 3   
A1BIO C20  C  Y N 4   
A1BIO C21  C  Y N 5   
A1BIO C24  C  Y N 6   
A1BIO C02  C  Y N 7   
A1BIO C03  C  Y N 8   
A1BIO C04  C  Y N 9   
A1BIO C05  C  Y N 10  
A1BIO C06  C  Y N 11  
A1BIO C07  C  Y N 12  
A1BIO C08  C  Y N 13  
A1BIO C11  C  Y N 14  
A1BIO C12  C  Y N 15  
A1BIO C14  C  Y N 16  
A1BIO C18  C  Y N 17  
A1BIO C19  C  Y N 18  
A1BIO C23  C  Y N 19  
A1BIO F01  F  N N 20  
A1BIO N09  N  Y N 21  
A1BIO N10  N  Y N 22  
A1BIO N16  N  N N 23  
A1BIO N22  N  Y N 24  
A1BIO H131 H  N N 25  
A1BIO H171 H  N N 26  
A1BIO H201 H  N N 27  
A1BIO H211 H  N N 28  
A1BIO H241 H  N N 29  
A1BIO H031 H  N N 30  
A1BIO H041 H  N N 31  
A1BIO H051 H  N N 32  
A1BIO H061 H  N N 33  
A1BIO H121 H  N N 34  
A1BIO H231 H  N N 35  
ALA   N    N  N N 36  
ALA   CA   C  N S 37  
ALA   C    C  N N 38  
ALA   O    O  N N 39  
ALA   CB   C  N N 40  
ALA   OXT  O  N N 41  
ALA   H    H  N N 42  
ALA   H2   H  N N 43  
ALA   HA   H  N N 44  
ALA   HB1  H  N N 45  
ALA   HB2  H  N N 46  
ALA   HB3  H  N N 47  
ALA   HXT  H  N N 48  
ARG   N    N  N N 49  
ARG   CA   C  N S 50  
ARG   C    C  N N 51  
ARG   O    O  N N 52  
ARG   CB   C  N N 53  
ARG   CG   C  N N 54  
ARG   CD   C  N N 55  
ARG   NE   N  N N 56  
ARG   CZ   C  N N 57  
ARG   NH1  N  N N 58  
ARG   NH2  N  N N 59  
ARG   OXT  O  N N 60  
ARG   H    H  N N 61  
ARG   H2   H  N N 62  
ARG   HA   H  N N 63  
ARG   HB2  H  N N 64  
ARG   HB3  H  N N 65  
ARG   HG2  H  N N 66  
ARG   HG3  H  N N 67  
ARG   HD2  H  N N 68  
ARG   HD3  H  N N 69  
ARG   HE   H  N N 70  
ARG   HH11 H  N N 71  
ARG   HH12 H  N N 72  
ARG   HH21 H  N N 73  
ARG   HH22 H  N N 74  
ARG   HXT  H  N N 75  
ASN   N    N  N N 76  
ASN   CA   C  N S 77  
ASN   C    C  N N 78  
ASN   O    O  N N 79  
ASN   CB   C  N N 80  
ASN   CG   C  N N 81  
ASN   OD1  O  N N 82  
ASN   ND2  N  N N 83  
ASN   OXT  O  N N 84  
ASN   H    H  N N 85  
ASN   H2   H  N N 86  
ASN   HA   H  N N 87  
ASN   HB2  H  N N 88  
ASN   HB3  H  N N 89  
ASN   HD21 H  N N 90  
ASN   HD22 H  N N 91  
ASN   HXT  H  N N 92  
ASP   N    N  N N 93  
ASP   CA   C  N S 94  
ASP   C    C  N N 95  
ASP   O    O  N N 96  
ASP   CB   C  N N 97  
ASP   CG   C  N N 98  
ASP   OD1  O  N N 99  
ASP   OD2  O  N N 100 
ASP   OXT  O  N N 101 
ASP   H    H  N N 102 
ASP   H2   H  N N 103 
ASP   HA   H  N N 104 
ASP   HB2  H  N N 105 
ASP   HB3  H  N N 106 
ASP   HD2  H  N N 107 
ASP   HXT  H  N N 108 
CL    CL   CL N N 109 
CYS   N    N  N N 110 
CYS   CA   C  N R 111 
CYS   C    C  N N 112 
CYS   O    O  N N 113 
CYS   CB   C  N N 114 
CYS   SG   S  N N 115 
CYS   OXT  O  N N 116 
CYS   H    H  N N 117 
CYS   H2   H  N N 118 
CYS   HA   H  N N 119 
CYS   HB2  H  N N 120 
CYS   HB3  H  N N 121 
CYS   HG   H  N N 122 
CYS   HXT  H  N N 123 
GLN   N    N  N N 124 
GLN   CA   C  N S 125 
GLN   C    C  N N 126 
GLN   O    O  N N 127 
GLN   CB   C  N N 128 
GLN   CG   C  N N 129 
GLN   CD   C  N N 130 
GLN   OE1  O  N N 131 
GLN   NE2  N  N N 132 
GLN   OXT  O  N N 133 
GLN   H    H  N N 134 
GLN   H2   H  N N 135 
GLN   HA   H  N N 136 
GLN   HB2  H  N N 137 
GLN   HB3  H  N N 138 
GLN   HG2  H  N N 139 
GLN   HG3  H  N N 140 
GLN   HE21 H  N N 141 
GLN   HE22 H  N N 142 
GLN   HXT  H  N N 143 
GLU   N    N  N N 144 
GLU   CA   C  N S 145 
GLU   C    C  N N 146 
GLU   O    O  N N 147 
GLU   CB   C  N N 148 
GLU   CG   C  N N 149 
GLU   CD   C  N N 150 
GLU   OE1  O  N N 151 
GLU   OE2  O  N N 152 
GLU   OXT  O  N N 153 
GLU   H    H  N N 154 
GLU   H2   H  N N 155 
GLU   HA   H  N N 156 
GLU   HB2  H  N N 157 
GLU   HB3  H  N N 158 
GLU   HG2  H  N N 159 
GLU   HG3  H  N N 160 
GLU   HE2  H  N N 161 
GLU   HXT  H  N N 162 
GLY   N    N  N N 163 
GLY   CA   C  N N 164 
GLY   C    C  N N 165 
GLY   O    O  N N 166 
GLY   OXT  O  N N 167 
GLY   H    H  N N 168 
GLY   H2   H  N N 169 
GLY   HA2  H  N N 170 
GLY   HA3  H  N N 171 
GLY   HXT  H  N N 172 
HIS   N    N  N N 173 
HIS   CA   C  N S 174 
HIS   C    C  N N 175 
HIS   O    O  N N 176 
HIS   CB   C  N N 177 
HIS   CG   C  Y N 178 
HIS   ND1  N  Y N 179 
HIS   CD2  C  Y N 180 
HIS   CE1  C  Y N 181 
HIS   NE2  N  Y N 182 
HIS   OXT  O  N N 183 
HIS   H    H  N N 184 
HIS   H2   H  N N 185 
HIS   HA   H  N N 186 
HIS   HB2  H  N N 187 
HIS   HB3  H  N N 188 
HIS   HD1  H  N N 189 
HIS   HD2  H  N N 190 
HIS   HE1  H  N N 191 
HIS   HE2  H  N N 192 
HIS   HXT  H  N N 193 
HOH   O    O  N N 194 
HOH   H1   H  N N 195 
HOH   H2   H  N N 196 
ILE   N    N  N N 197 
ILE   CA   C  N S 198 
ILE   C    C  N N 199 
ILE   O    O  N N 200 
ILE   CB   C  N S 201 
ILE   CG1  C  N N 202 
ILE   CG2  C  N N 203 
ILE   CD1  C  N N 204 
ILE   OXT  O  N N 205 
ILE   H    H  N N 206 
ILE   H2   H  N N 207 
ILE   HA   H  N N 208 
ILE   HB   H  N N 209 
ILE   HG12 H  N N 210 
ILE   HG13 H  N N 211 
ILE   HG21 H  N N 212 
ILE   HG22 H  N N 213 
ILE   HG23 H  N N 214 
ILE   HD11 H  N N 215 
ILE   HD12 H  N N 216 
ILE   HD13 H  N N 217 
ILE   HXT  H  N N 218 
LEU   N    N  N N 219 
LEU   CA   C  N S 220 
LEU   C    C  N N 221 
LEU   O    O  N N 222 
LEU   CB   C  N N 223 
LEU   CG   C  N N 224 
LEU   CD1  C  N N 225 
LEU   CD2  C  N N 226 
LEU   OXT  O  N N 227 
LEU   H    H  N N 228 
LEU   H2   H  N N 229 
LEU   HA   H  N N 230 
LEU   HB2  H  N N 231 
LEU   HB3  H  N N 232 
LEU   HG   H  N N 233 
LEU   HD11 H  N N 234 
LEU   HD12 H  N N 235 
LEU   HD13 H  N N 236 
LEU   HD21 H  N N 237 
LEU   HD22 H  N N 238 
LEU   HD23 H  N N 239 
LEU   HXT  H  N N 240 
LYS   N    N  N N 241 
LYS   CA   C  N S 242 
LYS   C    C  N N 243 
LYS   O    O  N N 244 
LYS   CB   C  N N 245 
LYS   CG   C  N N 246 
LYS   CD   C  N N 247 
LYS   CE   C  N N 248 
LYS   NZ   N  N N 249 
LYS   OXT  O  N N 250 
LYS   H    H  N N 251 
LYS   H2   H  N N 252 
LYS   HA   H  N N 253 
LYS   HB2  H  N N 254 
LYS   HB3  H  N N 255 
LYS   HG2  H  N N 256 
LYS   HG3  H  N N 257 
LYS   HD2  H  N N 258 
LYS   HD3  H  N N 259 
LYS   HE2  H  N N 260 
LYS   HE3  H  N N 261 
LYS   HZ1  H  N N 262 
LYS   HZ2  H  N N 263 
LYS   HZ3  H  N N 264 
LYS   HXT  H  N N 265 
MET   N    N  N N 266 
MET   CA   C  N S 267 
MET   C    C  N N 268 
MET   O    O  N N 269 
MET   CB   C  N N 270 
MET   CG   C  N N 271 
MET   SD   S  N N 272 
MET   CE   C  N N 273 
MET   OXT  O  N N 274 
MET   H    H  N N 275 
MET   H2   H  N N 276 
MET   HA   H  N N 277 
MET   HB2  H  N N 278 
MET   HB3  H  N N 279 
MET   HG2  H  N N 280 
MET   HG3  H  N N 281 
MET   HE1  H  N N 282 
MET   HE2  H  N N 283 
MET   HE3  H  N N 284 
MET   HXT  H  N N 285 
PHE   N    N  N N 286 
PHE   CA   C  N S 287 
PHE   C    C  N N 288 
PHE   O    O  N N 289 
PHE   CB   C  N N 290 
PHE   CG   C  Y N 291 
PHE   CD1  C  Y N 292 
PHE   CD2  C  Y N 293 
PHE   CE1  C  Y N 294 
PHE   CE2  C  Y N 295 
PHE   CZ   C  Y N 296 
PHE   OXT  O  N N 297 
PHE   H    H  N N 298 
PHE   H2   H  N N 299 
PHE   HA   H  N N 300 
PHE   HB2  H  N N 301 
PHE   HB3  H  N N 302 
PHE   HD1  H  N N 303 
PHE   HD2  H  N N 304 
PHE   HE1  H  N N 305 
PHE   HE2  H  N N 306 
PHE   HZ   H  N N 307 
PHE   HXT  H  N N 308 
PRO   N    N  N N 309 
PRO   CA   C  N S 310 
PRO   C    C  N N 311 
PRO   O    O  N N 312 
PRO   CB   C  N N 313 
PRO   CG   C  N N 314 
PRO   CD   C  N N 315 
PRO   OXT  O  N N 316 
PRO   H    H  N N 317 
PRO   HA   H  N N 318 
PRO   HB2  H  N N 319 
PRO   HB3  H  N N 320 
PRO   HG2  H  N N 321 
PRO   HG3  H  N N 322 
PRO   HD2  H  N N 323 
PRO   HD3  H  N N 324 
PRO   HXT  H  N N 325 
SER   N    N  N N 326 
SER   CA   C  N S 327 
SER   C    C  N N 328 
SER   O    O  N N 329 
SER   CB   C  N N 330 
SER   OG   O  N N 331 
SER   OXT  O  N N 332 
SER   H    H  N N 333 
SER   H2   H  N N 334 
SER   HA   H  N N 335 
SER   HB2  H  N N 336 
SER   HB3  H  N N 337 
SER   HG   H  N N 338 
SER   HXT  H  N N 339 
THR   N    N  N N 340 
THR   CA   C  N S 341 
THR   C    C  N N 342 
THR   O    O  N N 343 
THR   CB   C  N R 344 
THR   OG1  O  N N 345 
THR   CG2  C  N N 346 
THR   OXT  O  N N 347 
THR   H    H  N N 348 
THR   H2   H  N N 349 
THR   HA   H  N N 350 
THR   HB   H  N N 351 
THR   HG1  H  N N 352 
THR   HG21 H  N N 353 
THR   HG22 H  N N 354 
THR   HG23 H  N N 355 
THR   HXT  H  N N 356 
TRP   N    N  N N 357 
TRP   CA   C  N S 358 
TRP   C    C  N N 359 
TRP   O    O  N N 360 
TRP   CB   C  N N 361 
TRP   CG   C  Y N 362 
TRP   CD1  C  Y N 363 
TRP   CD2  C  Y N 364 
TRP   NE1  N  Y N 365 
TRP   CE2  C  Y N 366 
TRP   CE3  C  Y N 367 
TRP   CZ2  C  Y N 368 
TRP   CZ3  C  Y N 369 
TRP   CH2  C  Y N 370 
TRP   OXT  O  N N 371 
TRP   H    H  N N 372 
TRP   H2   H  N N 373 
TRP   HA   H  N N 374 
TRP   HB2  H  N N 375 
TRP   HB3  H  N N 376 
TRP   HD1  H  N N 377 
TRP   HE1  H  N N 378 
TRP   HE3  H  N N 379 
TRP   HZ2  H  N N 380 
TRP   HZ3  H  N N 381 
TRP   HH2  H  N N 382 
TRP   HXT  H  N N 383 
TYR   N    N  N N 384 
TYR   CA   C  N S 385 
TYR   C    C  N N 386 
TYR   O    O  N N 387 
TYR   CB   C  N N 388 
TYR   CG   C  Y N 389 
TYR   CD1  C  Y N 390 
TYR   CD2  C  Y N 391 
TYR   CE1  C  Y N 392 
TYR   CE2  C  Y N 393 
TYR   CZ   C  Y N 394 
TYR   OH   O  N N 395 
TYR   OXT  O  N N 396 
TYR   H    H  N N 397 
TYR   H2   H  N N 398 
TYR   HA   H  N N 399 
TYR   HB2  H  N N 400 
TYR   HB3  H  N N 401 
TYR   HD1  H  N N 402 
TYR   HD2  H  N N 403 
TYR   HE1  H  N N 404 
TYR   HE2  H  N N 405 
TYR   HH   H  N N 406 
TYR   HXT  H  N N 407 
VAL   N    N  N N 408 
VAL   CA   C  N S 409 
VAL   C    C  N N 410 
VAL   O    O  N N 411 
VAL   CB   C  N N 412 
VAL   CG1  C  N N 413 
VAL   CG2  C  N N 414 
VAL   OXT  O  N N 415 
VAL   H    H  N N 416 
VAL   H2   H  N N 417 
VAL   HA   H  N N 418 
VAL   HB   H  N N 419 
VAL   HG11 H  N N 420 
VAL   HG12 H  N N 421 
VAL   HG13 H  N N 422 
VAL   HG21 H  N N 423 
VAL   HG22 H  N N 424 
VAL   HG23 H  N N 425 
VAL   HXT  H  N N 426 
# 
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 
A1BIO C02 F01  sing N N 1   
A1BIO C04 C03  doub Y N 2   
A1BIO C03 C02  sing Y N 3   
A1BIO C05 C02  doub Y N 4   
A1BIO C06 C05  sing Y N 5   
A1BIO C07 C06  doub Y N 6   
A1BIO C08 C07  sing N N 7   
A1BIO N09 C08  doub Y N 8   
A1BIO N10 N09  sing Y N 9   
A1BIO C11 N10  sing Y N 10  
A1BIO C13 C12  doub Y N 11  
A1BIO C14 C13  sing Y N 12  
A1BIO N16 C15  trip N N 13  
A1BIO C15 C14  sing N N 14  
A1BIO C17 C14  doub Y N 15  
A1BIO C12 C11  sing Y N 16  
A1BIO C18 C11  doub Y N 17  
A1BIO C19 C18  sing N N 18  
A1BIO C20 C19  doub Y N 19  
A1BIO C21 C20  sing Y N 20  
A1BIO N22 C21  doub Y N 21  
A1BIO C23 N22  sing Y N 22  
A1BIO C24 C23  doub Y N 23  
A1BIO C04 C07  sing Y N 24  
A1BIO C08 C18  sing Y N 25  
A1BIO N10 C17  sing Y N 26  
A1BIO C19 C24  sing Y N 27  
A1BIO C13 H131 sing N N 28  
A1BIO C17 H171 sing N N 29  
A1BIO C20 H201 sing N N 30  
A1BIO C21 H211 sing N N 31  
A1BIO C24 H241 sing N N 32  
A1BIO C03 H031 sing N N 33  
A1BIO C04 H041 sing N N 34  
A1BIO C05 H051 sing N N 35  
A1BIO C06 H061 sing N N 36  
A1BIO C12 H121 sing N N 37  
A1BIO C23 H231 sing N N 38  
ALA   N   CA   sing N N 39  
ALA   N   H    sing N N 40  
ALA   N   H2   sing N N 41  
ALA   CA  C    sing N N 42  
ALA   CA  CB   sing N N 43  
ALA   CA  HA   sing N N 44  
ALA   C   O    doub N N 45  
ALA   C   OXT  sing N N 46  
ALA   CB  HB1  sing N N 47  
ALA   CB  HB2  sing N N 48  
ALA   CB  HB3  sing N N 49  
ALA   OXT HXT  sing N N 50  
ARG   N   CA   sing N N 51  
ARG   N   H    sing N N 52  
ARG   N   H2   sing N N 53  
ARG   CA  C    sing N N 54  
ARG   CA  CB   sing N N 55  
ARG   CA  HA   sing N N 56  
ARG   C   O    doub N N 57  
ARG   C   OXT  sing N N 58  
ARG   CB  CG   sing N N 59  
ARG   CB  HB2  sing N N 60  
ARG   CB  HB3  sing N N 61  
ARG   CG  CD   sing N N 62  
ARG   CG  HG2  sing N N 63  
ARG   CG  HG3  sing N N 64  
ARG   CD  NE   sing N N 65  
ARG   CD  HD2  sing N N 66  
ARG   CD  HD3  sing N N 67  
ARG   NE  CZ   sing N N 68  
ARG   NE  HE   sing N N 69  
ARG   CZ  NH1  sing N N 70  
ARG   CZ  NH2  doub N N 71  
ARG   NH1 HH11 sing N N 72  
ARG   NH1 HH12 sing N N 73  
ARG   NH2 HH21 sing N N 74  
ARG   NH2 HH22 sing N N 75  
ARG   OXT HXT  sing N N 76  
ASN   N   CA   sing N N 77  
ASN   N   H    sing N N 78  
ASN   N   H2   sing N N 79  
ASN   CA  C    sing N N 80  
ASN   CA  CB   sing N N 81  
ASN   CA  HA   sing N N 82  
ASN   C   O    doub N N 83  
ASN   C   OXT  sing N N 84  
ASN   CB  CG   sing N N 85  
ASN   CB  HB2  sing N N 86  
ASN   CB  HB3  sing N N 87  
ASN   CG  OD1  doub N N 88  
ASN   CG  ND2  sing N N 89  
ASN   ND2 HD21 sing N N 90  
ASN   ND2 HD22 sing N N 91  
ASN   OXT HXT  sing N N 92  
ASP   N   CA   sing N N 93  
ASP   N   H    sing N N 94  
ASP   N   H2   sing N N 95  
ASP   CA  C    sing N N 96  
ASP   CA  CB   sing N N 97  
ASP   CA  HA   sing N N 98  
ASP   C   O    doub N N 99  
ASP   C   OXT  sing N N 100 
ASP   CB  CG   sing N N 101 
ASP   CB  HB2  sing N N 102 
ASP   CB  HB3  sing N N 103 
ASP   CG  OD1  doub N N 104 
ASP   CG  OD2  sing N N 105 
ASP   OD2 HD2  sing N N 106 
ASP   OXT HXT  sing N N 107 
CYS   N   CA   sing N N 108 
CYS   N   H    sing N N 109 
CYS   N   H2   sing N N 110 
CYS   CA  C    sing N N 111 
CYS   CA  CB   sing N N 112 
CYS   CA  HA   sing N N 113 
CYS   C   O    doub N N 114 
CYS   C   OXT  sing N N 115 
CYS   CB  SG   sing N N 116 
CYS   CB  HB2  sing N N 117 
CYS   CB  HB3  sing N N 118 
CYS   SG  HG   sing N N 119 
CYS   OXT HXT  sing N N 120 
GLN   N   CA   sing N N 121 
GLN   N   H    sing N N 122 
GLN   N   H2   sing N N 123 
GLN   CA  C    sing N N 124 
GLN   CA  CB   sing N N 125 
GLN   CA  HA   sing N N 126 
GLN   C   O    doub N N 127 
GLN   C   OXT  sing N N 128 
GLN   CB  CG   sing N N 129 
GLN   CB  HB2  sing N N 130 
GLN   CB  HB3  sing N N 131 
GLN   CG  CD   sing N N 132 
GLN   CG  HG2  sing N N 133 
GLN   CG  HG3  sing N N 134 
GLN   CD  OE1  doub N N 135 
GLN   CD  NE2  sing N N 136 
GLN   NE2 HE21 sing N N 137 
GLN   NE2 HE22 sing N N 138 
GLN   OXT HXT  sing N N 139 
GLU   N   CA   sing N N 140 
GLU   N   H    sing N N 141 
GLU   N   H2   sing N N 142 
GLU   CA  C    sing N N 143 
GLU   CA  CB   sing N N 144 
GLU   CA  HA   sing N N 145 
GLU   C   O    doub N N 146 
GLU   C   OXT  sing N N 147 
GLU   CB  CG   sing N N 148 
GLU   CB  HB2  sing N N 149 
GLU   CB  HB3  sing N N 150 
GLU   CG  CD   sing N N 151 
GLU   CG  HG2  sing N N 152 
GLU   CG  HG3  sing N N 153 
GLU   CD  OE1  doub N N 154 
GLU   CD  OE2  sing N N 155 
GLU   OE2 HE2  sing N N 156 
GLU   OXT HXT  sing N N 157 
GLY   N   CA   sing N N 158 
GLY   N   H    sing N N 159 
GLY   N   H2   sing N N 160 
GLY   CA  C    sing N N 161 
GLY   CA  HA2  sing N N 162 
GLY   CA  HA3  sing N N 163 
GLY   C   O    doub N N 164 
GLY   C   OXT  sing N N 165 
GLY   OXT HXT  sing N N 166 
HIS   N   CA   sing N N 167 
HIS   N   H    sing N N 168 
HIS   N   H2   sing N N 169 
HIS   CA  C    sing N N 170 
HIS   CA  CB   sing N N 171 
HIS   CA  HA   sing N N 172 
HIS   C   O    doub N N 173 
HIS   C   OXT  sing N N 174 
HIS   CB  CG   sing N N 175 
HIS   CB  HB2  sing N N 176 
HIS   CB  HB3  sing N N 177 
HIS   CG  ND1  sing Y N 178 
HIS   CG  CD2  doub Y N 179 
HIS   ND1 CE1  doub Y N 180 
HIS   ND1 HD1  sing N N 181 
HIS   CD2 NE2  sing Y N 182 
HIS   CD2 HD2  sing N N 183 
HIS   CE1 NE2  sing Y N 184 
HIS   CE1 HE1  sing N N 185 
HIS   NE2 HE2  sing N N 186 
HIS   OXT HXT  sing N N 187 
HOH   O   H1   sing N N 188 
HOH   O   H2   sing N N 189 
ILE   N   CA   sing N N 190 
ILE   N   H    sing N N 191 
ILE   N   H2   sing N N 192 
ILE   CA  C    sing N N 193 
ILE   CA  CB   sing N N 194 
ILE   CA  HA   sing N N 195 
ILE   C   O    doub N N 196 
ILE   C   OXT  sing N N 197 
ILE   CB  CG1  sing N N 198 
ILE   CB  CG2  sing N N 199 
ILE   CB  HB   sing N N 200 
ILE   CG1 CD1  sing N N 201 
ILE   CG1 HG12 sing N N 202 
ILE   CG1 HG13 sing N N 203 
ILE   CG2 HG21 sing N N 204 
ILE   CG2 HG22 sing N N 205 
ILE   CG2 HG23 sing N N 206 
ILE   CD1 HD11 sing N N 207 
ILE   CD1 HD12 sing N N 208 
ILE   CD1 HD13 sing N N 209 
ILE   OXT HXT  sing N N 210 
LEU   N   CA   sing N N 211 
LEU   N   H    sing N N 212 
LEU   N   H2   sing N N 213 
LEU   CA  C    sing N N 214 
LEU   CA  CB   sing N N 215 
LEU   CA  HA   sing N N 216 
LEU   C   O    doub N N 217 
LEU   C   OXT  sing N N 218 
LEU   CB  CG   sing N N 219 
LEU   CB  HB2  sing N N 220 
LEU   CB  HB3  sing N N 221 
LEU   CG  CD1  sing N N 222 
LEU   CG  CD2  sing N N 223 
LEU   CG  HG   sing N N 224 
LEU   CD1 HD11 sing N N 225 
LEU   CD1 HD12 sing N N 226 
LEU   CD1 HD13 sing N N 227 
LEU   CD2 HD21 sing N N 228 
LEU   CD2 HD22 sing N N 229 
LEU   CD2 HD23 sing N N 230 
LEU   OXT HXT  sing N N 231 
LYS   N   CA   sing N N 232 
LYS   N   H    sing N N 233 
LYS   N   H2   sing N N 234 
LYS   CA  C    sing N N 235 
LYS   CA  CB   sing N N 236 
LYS   CA  HA   sing N N 237 
LYS   C   O    doub N N 238 
LYS   C   OXT  sing N N 239 
LYS   CB  CG   sing N N 240 
LYS   CB  HB2  sing N N 241 
LYS   CB  HB3  sing N N 242 
LYS   CG  CD   sing N N 243 
LYS   CG  HG2  sing N N 244 
LYS   CG  HG3  sing N N 245 
LYS   CD  CE   sing N N 246 
LYS   CD  HD2  sing N N 247 
LYS   CD  HD3  sing N N 248 
LYS   CE  NZ   sing N N 249 
LYS   CE  HE2  sing N N 250 
LYS   CE  HE3  sing N N 251 
LYS   NZ  HZ1  sing N N 252 
LYS   NZ  HZ2  sing N N 253 
LYS   NZ  HZ3  sing N N 254 
LYS   OXT HXT  sing N N 255 
MET   N   CA   sing N N 256 
MET   N   H    sing N N 257 
MET   N   H2   sing N N 258 
MET   CA  C    sing N N 259 
MET   CA  CB   sing N N 260 
MET   CA  HA   sing N N 261 
MET   C   O    doub N N 262 
MET   C   OXT  sing N N 263 
MET   CB  CG   sing N N 264 
MET   CB  HB2  sing N N 265 
MET   CB  HB3  sing N N 266 
MET   CG  SD   sing N N 267 
MET   CG  HG2  sing N N 268 
MET   CG  HG3  sing N N 269 
MET   SD  CE   sing N N 270 
MET   CE  HE1  sing N N 271 
MET   CE  HE2  sing N N 272 
MET   CE  HE3  sing N N 273 
MET   OXT HXT  sing N N 274 
PHE   N   CA   sing N N 275 
PHE   N   H    sing N N 276 
PHE   N   H2   sing N N 277 
PHE   CA  C    sing N N 278 
PHE   CA  CB   sing N N 279 
PHE   CA  HA   sing N N 280 
PHE   C   O    doub N N 281 
PHE   C   OXT  sing N N 282 
PHE   CB  CG   sing N N 283 
PHE   CB  HB2  sing N N 284 
PHE   CB  HB3  sing N N 285 
PHE   CG  CD1  doub Y N 286 
PHE   CG  CD2  sing Y N 287 
PHE   CD1 CE1  sing Y N 288 
PHE   CD1 HD1  sing N N 289 
PHE   CD2 CE2  doub Y N 290 
PHE   CD2 HD2  sing N N 291 
PHE   CE1 CZ   doub Y N 292 
PHE   CE1 HE1  sing N N 293 
PHE   CE2 CZ   sing Y N 294 
PHE   CE2 HE2  sing N N 295 
PHE   CZ  HZ   sing N N 296 
PHE   OXT HXT  sing N N 297 
PRO   N   CA   sing N N 298 
PRO   N   CD   sing N N 299 
PRO   N   H    sing N N 300 
PRO   CA  C    sing N N 301 
PRO   CA  CB   sing N N 302 
PRO   CA  HA   sing N N 303 
PRO   C   O    doub N N 304 
PRO   C   OXT  sing N N 305 
PRO   CB  CG   sing N N 306 
PRO   CB  HB2  sing N N 307 
PRO   CB  HB3  sing N N 308 
PRO   CG  CD   sing N N 309 
PRO   CG  HG2  sing N N 310 
PRO   CG  HG3  sing N N 311 
PRO   CD  HD2  sing N N 312 
PRO   CD  HD3  sing N N 313 
PRO   OXT HXT  sing N N 314 
SER   N   CA   sing N N 315 
SER   N   H    sing N N 316 
SER   N   H2   sing N N 317 
SER   CA  C    sing N N 318 
SER   CA  CB   sing N N 319 
SER   CA  HA   sing N N 320 
SER   C   O    doub N N 321 
SER   C   OXT  sing N N 322 
SER   CB  OG   sing N N 323 
SER   CB  HB2  sing N N 324 
SER   CB  HB3  sing N N 325 
SER   OG  HG   sing N N 326 
SER   OXT HXT  sing N N 327 
THR   N   CA   sing N N 328 
THR   N   H    sing N N 329 
THR   N   H2   sing N N 330 
THR   CA  C    sing N N 331 
THR   CA  CB   sing N N 332 
THR   CA  HA   sing N N 333 
THR   C   O    doub N N 334 
THR   C   OXT  sing N N 335 
THR   CB  OG1  sing N N 336 
THR   CB  CG2  sing N N 337 
THR   CB  HB   sing N N 338 
THR   OG1 HG1  sing N N 339 
THR   CG2 HG21 sing N N 340 
THR   CG2 HG22 sing N N 341 
THR   CG2 HG23 sing N N 342 
THR   OXT HXT  sing N N 343 
TRP   N   CA   sing N N 344 
TRP   N   H    sing N N 345 
TRP   N   H2   sing N N 346 
TRP   CA  C    sing N N 347 
TRP   CA  CB   sing N N 348 
TRP   CA  HA   sing N N 349 
TRP   C   O    doub N N 350 
TRP   C   OXT  sing N N 351 
TRP   CB  CG   sing N N 352 
TRP   CB  HB2  sing N N 353 
TRP   CB  HB3  sing N N 354 
TRP   CG  CD1  doub Y N 355 
TRP   CG  CD2  sing Y N 356 
TRP   CD1 NE1  sing Y N 357 
TRP   CD1 HD1  sing N N 358 
TRP   CD2 CE2  doub Y N 359 
TRP   CD2 CE3  sing Y N 360 
TRP   NE1 CE2  sing Y N 361 
TRP   NE1 HE1  sing N N 362 
TRP   CE2 CZ2  sing Y N 363 
TRP   CE3 CZ3  doub Y N 364 
TRP   CE3 HE3  sing N N 365 
TRP   CZ2 CH2  doub Y N 366 
TRP   CZ2 HZ2  sing N N 367 
TRP   CZ3 CH2  sing Y N 368 
TRP   CZ3 HZ3  sing N N 369 
TRP   CH2 HH2  sing N N 370 
TRP   OXT HXT  sing N N 371 
TYR   N   CA   sing N N 372 
TYR   N   H    sing N N 373 
TYR   N   H2   sing N N 374 
TYR   CA  C    sing N N 375 
TYR   CA  CB   sing N N 376 
TYR   CA  HA   sing N N 377 
TYR   C   O    doub N N 378 
TYR   C   OXT  sing N N 379 
TYR   CB  CG   sing N N 380 
TYR   CB  HB2  sing N N 381 
TYR   CB  HB3  sing N N 382 
TYR   CG  CD1  doub Y N 383 
TYR   CG  CD2  sing Y N 384 
TYR   CD1 CE1  sing Y N 385 
TYR   CD1 HD1  sing N N 386 
TYR   CD2 CE2  doub Y N 387 
TYR   CD2 HD2  sing N N 388 
TYR   CE1 CZ   doub Y N 389 
TYR   CE1 HE1  sing N N 390 
TYR   CE2 CZ   sing Y N 391 
TYR   CE2 HE2  sing N N 392 
TYR   CZ  OH   sing N N 393 
TYR   OH  HH   sing N N 394 
TYR   OXT HXT  sing N N 395 
VAL   N   CA   sing N N 396 
VAL   N   H    sing N N 397 
VAL   N   H2   sing N N 398 
VAL   CA  C    sing N N 399 
VAL   CA  CB   sing N N 400 
VAL   CA  HA   sing N N 401 
VAL   C   O    doub N N 402 
VAL   C   OXT  sing N N 403 
VAL   CB  CG1  sing N N 404 
VAL   CB  CG2  sing N N 405 
VAL   CB  HB   sing N N 406 
VAL   CG1 HG11 sing N N 407 
VAL   CG1 HG12 sing N N 408 
VAL   CG1 HG13 sing N N 409 
VAL   CG2 HG21 sing N N 410 
VAL   CG2 HG22 sing N N 411 
VAL   CG2 HG23 sing N N 412 
VAL   OXT HXT  sing N N 413 
# 
_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                    9EDX 
_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]   0.010904 
_atom_sites.fract_transf_matrix[1][2]   0.006295 
_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]   0.012591 
_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]   0.008407 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
_atom_type.scat_dispersion_real 
_atom_type.scat_dispersion_imag 
_atom_type.scat_Cromer_Mann_a1 
_atom_type.scat_Cromer_Mann_a2 
_atom_type.scat_Cromer_Mann_a3 
_atom_type.scat_Cromer_Mann_a4 
_atom_type.scat_Cromer_Mann_b1 
_atom_type.scat_Cromer_Mann_b2 
_atom_type.scat_Cromer_Mann_b3 
_atom_type.scat_Cromer_Mann_b4 
_atom_type.scat_Cromer_Mann_c 
_atom_type.scat_source 
_atom_type.scat_dispersion_source 
C  ? ? 3.54356 2.42580 ? ? 25.62398 1.50364  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
CL ? ? 9.50761 7.44341 ? ? 1.04373  23.83732 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
F  ? ? 4.90428 4.07044 ? ? 12.99538 1.63651  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
N  ? ? 4.01032 2.96436 ? ? 19.97189 1.75589  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
O  ? ? 4.49882 3.47563 ? ? 15.80542 1.70748  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
S  ? ? 9.55732 6.39887 ? ? 1.23737  29.19336 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N   . SER   A 1 1   ? 31.22300  2.58800   -22.20200 1.000 107.13964 ? 37  SER   A N   1 
ATOM   2    C  CA  . SER   A 1 1   ? 32.10200  2.48300   -21.04300 1.000 110.19381 ? 37  SER   A CA  1 
ATOM   3    C  C   . SER   A 1 1   ? 32.22700  1.02700   -20.60300 1.000 110.72991 ? 37  SER   A C   1 
ATOM   4    O  O   . SER   A 1 1   ? 31.32700  0.22000   -20.83600 1.000 111.58826 ? 37  SER   A O   1 
ATOM   5    C  CB  . SER   A 1 1   ? 31.58000  3.35000   -19.89500 1.000 110.43949 ? 37  SER   A CB  1 
ATOM   6    O  OG  . SER   A 1 1   ? 32.53800  3.46000   -18.85600 1.000 109.14804 ? 37  SER   A OG  1 
ATOM   7    N  N   . SER   A 1 2   ? 33.35100  0.69600   -19.96500 1.000 106.22826 ? 38  SER   A N   1 
ATOM   8    C  CA  . SER   A 1 2   ? 33.63200  -0.67900  -19.57100 1.000 104.56589 ? 38  SER   A CA  1 
ATOM   9    C  C   . SER   A 1 2   ? 33.06000  -1.05000  -18.20800 1.000 97.87851  ? 38  SER   A C   1 
ATOM   10   O  O   . SER   A 1 2   ? 32.99000  -2.24200  -17.88700 1.000 88.23951  ? 38  SER   A O   1 
ATOM   11   C  CB  . SER   A 1 2   ? 35.14500  -0.92600  -19.56800 1.000 102.60604 ? 38  SER   A CB  1 
ATOM   12   O  OG  . SER   A 1 2   ? 35.82200  0.03700   -18.77800 1.000 107.04377 ? 38  SER   A OG  1 
ATOM   13   N  N   . VAL   A 1 3   ? 32.64600  -0.07000  -17.40600 1.000 100.50885 ? 39  VAL   A N   1 
ATOM   14   C  CA  . VAL   A 1 3   ? 32.17000  -0.29800  -16.04500 1.000 89.16254  ? 39  VAL   A CA  1 
ATOM   15   C  C   . VAL   A 1 3   ? 30.66700  -0.06200  -16.00200 1.000 88.99159  ? 39  VAL   A C   1 
ATOM   16   O  O   . VAL   A 1 3   ? 30.17900  0.96500   -16.48900 1.000 95.92693  ? 39  VAL   A O   1 
ATOM   17   C  CB  . VAL   A 1 3   ? 32.88900  0.61300   -15.03500 1.000 85.52808  ? 39  VAL   A CB  1 
ATOM   18   C  CG1 . VAL   A 1 3   ? 32.29800  0.43700   -13.64200 1.000 76.34754  ? 39  VAL   A CG1 1 
ATOM   19   C  CG2 . VAL   A 1 3   ? 34.38400  0.33300   -15.02900 1.000 85.46391  ? 39  VAL   A CG2 1 
ATOM   20   N  N   . VAL   A 1 4   ? 29.93900  -1.00600  -15.41000 1.000 79.38281  ? 40  VAL   A N   1 
ATOM   21   C  CA  . VAL   A 1 4   ? 28.51500  -0.84900  -15.15200 1.000 83.50318  ? 40  VAL   A CA  1 
ATOM   22   C  C   . VAL   A 1 4   ? 28.29800  -0.87500  -13.64500 1.000 80.06209  ? 40  VAL   A C   1 
ATOM   23   O  O   . VAL   A 1 4   ? 29.08500  -1.46200  -12.89500 1.000 72.37015  ? 40  VAL   A O   1 
ATOM   24   C  CB  . VAL   A 1 4   ? 27.66900  -1.93700  -15.85500 1.000 85.45277  ? 40  VAL   A CB  1 
ATOM   25   C  CG1 . VAL   A 1 4   ? 28.05200  -2.03800  -17.32800 1.000 87.42810  ? 40  VAL   A CG1 1 
ATOM   26   C  CG2 . VAL   A 1 4   ? 27.82200  -3.28200  -15.16100 1.000 79.92258  ? 40  VAL   A CG2 1 
ATOM   27   N  N   . GLY   A 1 5   ? 27.23600  -0.20700  -13.20000 1.000 77.34913  ? 41  GLY   A N   1 
ATOM   28   C  CA  . GLY   A 1 5   ? 26.91600  -0.17000  -11.78200 1.000 72.38745  ? 41  GLY   A CA  1 
ATOM   29   C  C   . GLY   A 1 5   ? 27.97900  0.46600   -10.91400 1.000 73.00647  ? 41  GLY   A C   1 
ATOM   30   O  O   . GLY   A 1 5   ? 28.13000  0.07700   -9.75000  1.000 69.29431  ? 41  GLY   A O   1 
ATOM   31   N  N   . LEU   A 1 6   ? 28.73300  1.42400   -11.45800 1.000 69.24730  ? 42  LEU   A N   1 
ATOM   32   C  CA  . LEU   A 1 6   ? 29.75700  2.17500   -10.73300 1.000 66.00860  ? 42  LEU   A CA  1 
ATOM   33   C  C   . LEU   A 1 6   ? 30.98800  1.34100   -10.38600 1.000 66.62708  ? 42  LEU   A C   1 
ATOM   34   O  O   . LEU   A 1 6   ? 32.11600  1.82700   -10.51000 1.000 61.36423  ? 42  LEU   A O   1 
ATOM   35   C  CB  . LEU   A 1 6   ? 29.18200  2.78800   -9.45000  1.000 70.58495  ? 42  LEU   A CB  1 
ATOM   36   C  CG  . LEU   A 1 6   ? 28.48700  4.14800   -9.50000  1.000 75.74870  ? 42  LEU   A CG  1 
ATOM   37   C  CD1 . LEU   A 1 6   ? 27.38600  4.19500   -10.54800 1.000 81.74802  ? 42  LEU   A CD1 1 
ATOM   38   C  CD2 . LEU   A 1 6   ? 27.93000  4.45600   -8.12500  1.000 84.52702  ? 42  LEU   A CD2 1 
ATOM   39   N  N   . HIS   A 1 7   ? 30.80100  0.09300   -9.95100  1.000 53.60743  ? 43  HIS   A N   1 
ATOM   40   C  CA  . HIS   A 1 7   ? 31.89800  -0.66300  -9.35900  1.000 61.72963  ? 43  HIS   A CA  1 
ATOM   41   C  C   . HIS   A 1 7   ? 32.18400  -1.99300  -10.04600 1.000 59.25358  ? 43  HIS   A C   1 
ATOM   42   O  O   . HIS   A 1 7   ? 32.98000  -2.78100  -9.52300  1.000 53.83382  ? 43  HIS   A O   1 
ATOM   43   C  CB  . HIS   A 1 7   ? 31.61800  -0.91400  -7.87300  1.000 56.98458  ? 43  HIS   A CB  1 
ATOM   44   C  CG  . HIS   A 1 7   ? 31.28800  0.32900   -7.11100  1.000 59.53919  ? 43  HIS   A CG  1 
ATOM   45   N  ND1 . HIS   A 1 7   ? 30.12500  0.47000   -6.38500  1.000 67.71521  ? 43  HIS   A ND1 1 
ATOM   46   C  CD2 . HIS   A 1 7   ? 31.96400  1.49400   -6.97000  1.000 59.34141  ? 43  HIS   A CD2 1 
ATOM   47   C  CE1 . HIS   A 1 7   ? 30.09900  1.66800   -5.82800  1.000 70.30172  ? 43  HIS   A CE1 1 
ATOM   48   N  NE2 . HIS   A 1 7   ? 31.20400  2.30900   -6.16500  1.000 68.86677  ? 43  HIS   A NE2 1 
ATOM   49   N  N   . TYR   A 1 8   ? 31.57600  -2.27100  -11.19600 1.000 59.05504  ? 44  TYR   A N   1 
ATOM   50   C  CA  . TYR   A 1 8   ? 31.66400  -3.59600  -11.80200 1.000 62.24140  ? 44  TYR   A CA  1 
ATOM   51   C  C   . TYR   A 1 8   ? 32.09300  -3.47200  -13.25700 1.000 69.68466  ? 44  TYR   A C   1 
ATOM   52   O  O   . TYR   A 1 8   ? 31.36700  -2.90200  -14.07900 1.000 70.43581  ? 44  TYR   A O   1 
ATOM   53   C  CB  . TYR   A 1 8   ? 30.33400  -4.33500  -11.67200 1.000 55.72638  ? 44  TYR   A CB  1 
ATOM   54   C  CG  . TYR   A 1 8   ? 29.85700  -4.37500  -10.24000 1.000 57.94646  ? 44  TYR   A CG  1 
ATOM   55   C  CD1 . TYR   A 1 8   ? 30.42500  -5.25200  -9.32400  1.000 56.14471  ? 44  TYR   A CD1 1 
ATOM   56   C  CD2 . TYR   A 1 8   ? 28.86100  -3.51900  -9.79600  1.000 64.37464  ? 44  TYR   A CD2 1 
ATOM   57   C  CE1 . TYR   A 1 8   ? 30.00200  -5.28400  -8.01100  1.000 58.36149  ? 44  TYR   A CE1 1 
ATOM   58   C  CE2 . TYR   A 1 8   ? 28.43200  -3.54200  -8.48400  1.000 63.33154  ? 44  TYR   A CE2 1 
ATOM   59   C  CZ  . TYR   A 1 8   ? 29.00300  -4.42600  -7.59800  1.000 63.96314  ? 44  TYR   A CZ  1 
ATOM   60   O  OH  . TYR   A 1 8   ? 28.56900  -4.44200  -6.29400  1.000 73.78790  ? 44  TYR   A OH  1 
ATOM   61   N  N   . LYS   A 1 9   ? 33.27000  -4.01000  -13.56500 1.000 63.19349  ? 45  LYS   A N   1 
ATOM   62   C  CA  . LYS   A 1 9   ? 33.80400  -4.01400  -14.91800 1.000 70.31341  ? 45  LYS   A CA  1 
ATOM   63   C  C   . LYS   A 1 9   ? 33.42200  -5.30700  -15.62400 1.000 67.43655  ? 45  LYS   A C   1 
ATOM   64   O  O   . LYS   A 1 9   ? 33.49500  -6.39100  -15.03900 1.000 61.18406  ? 45  LYS   A O   1 
ATOM   65   C  CB  . LYS   A 1 9   ? 35.32700  -3.86000  -14.89600 1.000 68.21266  ? 45  LYS   A CB  1 
ATOM   66   C  CG  . LYS   A 1 9   ? 35.96200  -3.73600  -16.27400 1.000 80.88075  ? 45  LYS   A CG  1 
ATOM   67   C  CD  . LYS   A 1 9   ? 37.47700  -3.87800  -16.20400 1.000 82.26320  ? 45  LYS   A CD  1 
ATOM   68   C  CE  . LYS   A 1 9   ? 38.10900  -3.76500  -17.58500 1.000 83.43697  ? 45  LYS   A CE  1 
ATOM   69   N  NZ  . LYS   A 1 9   ? 39.54500  -4.16400  -17.57500 1.000 64.07943  ? 45  LYS   A NZ  1 
ATOM   70   N  N   . ILE   A 1 10  ? 33.01800  -5.18700  -16.88700 1.000 68.81025  ? 46  ILE   A N   1 
ATOM   71   C  CA  . ILE   A 1 10  ? 32.58800  -6.33600  -17.67600 1.000 74.72712  ? 46  ILE   A CA  1 
ATOM   72   C  C   . ILE   A 1 10  ? 33.77100  -7.25200  -17.95200 1.000 78.43007  ? 46  ILE   A C   1 
ATOM   73   O  O   . ILE   A 1 10  ? 34.92700  -6.89400  -17.69700 1.000 85.10686  ? 46  ILE   A O   1 
ATOM   74   C  CB  . ILE   A 1 10  ? 31.92400  -5.89200  -18.99200 1.000 76.69427  ? 46  ILE   A CB  1 
ATOM   75   C  CG1 . ILE   A 1 10  ? 32.89200  -5.05100  -19.83300 1.000 88.84490  ? 46  ILE   A CG1 1 
ATOM   76   C  CG2 . ILE   A 1 10  ? 30.64400  -5.12500  -18.70400 1.000 76.27616  ? 46  ILE   A CG2 1 
ATOM   77   C  CD1 . ILE   A 1 10  ? 33.62000  -5.82500  -20.92900 1.000 89.91287  ? 46  ILE   A CD1 1 
ATOM   78   N  N   . GLY   A 1 11  ? 33.48900  -8.43400  -18.49000 1.000 83.81646  ? 47  GLY   A N   1 
ATOM   79   C  CA  . GLY   A 1 11  ? 34.53000  -9.38800  -18.80700 1.000 84.23992  ? 47  GLY   A CA  1 
ATOM   80   C  C   . GLY   A 1 11  ? 34.10200  -10.37400 -19.87200 1.000 94.33866  ? 47  GLY   A C   1 
ATOM   81   O  O   . GLY   A 1 11  ? 33.40100  -10.00800 -20.82100 1.000 94.77853  ? 47  GLY   A O   1 
ATOM   82   N  N   . LYS   A 1 12  ? 34.51800  -11.62800 -19.72200 1.000 97.90927  ? 48  LYS   A N   1 
ATOM   83   C  CA  . LYS   A 1 12  ? 34.16600  -12.66100 -20.68600 1.000 96.14160  ? 48  LYS   A CA  1 
ATOM   84   C  C   . LYS   A 1 12  ? 32.66900  -12.94300 -20.64500 1.000 94.29779  ? 48  LYS   A C   1 
ATOM   85   O  O   . LYS   A 1 12  ? 32.04200  -12.91200 -19.58200 1.000 90.94290  ? 48  LYS   A O   1 
ATOM   86   C  CB  . LYS   A 1 12  ? 34.95100  -13.94300 -20.39800 1.000 92.49335  ? 48  LYS   A CB  1 
ATOM   87   C  CG  . LYS   A 1 12  ? 34.71400  -15.07400 -21.39200 1.000 99.20733  ? 48  LYS   A CG  1 
ATOM   88   C  CD  . LYS   A 1 12  ? 35.17900  -16.41400 -20.83400 1.000 96.33208  ? 48  LYS   A CD  1 
ATOM   89   C  CE  . LYS   A 1 12  ? 33.99800  -17.33400 -20.55400 1.000 94.84410  ? 48  LYS   A CE  1 
ATOM   90   N  NZ  . LYS   A 1 12  ? 34.40300  -18.59600 -19.87300 1.000 98.17558  ? 48  LYS   A NZ  1 
ATOM   91   N  N   . LYS   A 1 13  ? 32.09600  -13.21600 -21.81400 1.000 94.94230  ? 49  LYS   A N   1 
ATOM   92   C  CA  . LYS   A 1 13  ? 30.69300  -13.59500 -21.90300 1.000 90.35743  ? 49  LYS   A CA  1 
ATOM   93   C  C   . LYS   A 1 13  ? 30.53900  -15.08100 -21.60800 1.000 91.56994  ? 49  LYS   A C   1 
ATOM   94   O  O   . LYS   A 1 13  ? 31.20000  -15.91700 -22.23200 1.000 97.66518  ? 49  LYS   A O   1 
ATOM   95   C  CB  . LYS   A 1 13  ? 30.14200  -13.27300 -23.29100 1.000 94.52507  ? 49  LYS   A CB  1 
ATOM   96   C  CG  . LYS   A 1 13  ? 28.68500  -13.65400 -23.48000 1.000 98.51890  ? 49  LYS   A CG  1 
ATOM   97   C  CD  . LYS   A 1 13  ? 28.28100  -13.56500 -24.94200 1.000 103.29788 ? 49  LYS   A CD  1 
ATOM   98   C  CE  . LYS   A 1 13  ? 28.54700  -12.17900 -25.50300 1.000 104.02395 ? 49  LYS   A CE  1 
ATOM   99   N  NZ  . LYS   A 1 13  ? 28.14900  -12.07900 -26.93400 1.000 110.35562 ? 49  LYS   A NZ  1 
ATOM   100  N  N   . ILE   A 1 14  ? 29.66700  -15.41000 -20.65600 1.000 84.01185  ? 50  ILE   A N   1 
ATOM   101  C  CA  . ILE   A 1 14  ? 29.41900  -16.79600 -20.27300 1.000 92.94502  ? 50  ILE   A CA  1 
ATOM   102  C  C   . ILE   A 1 14  ? 28.05200  -17.28700 -20.70900 1.000 93.56417  ? 50  ILE   A C   1 
ATOM   103  O  O   . ILE   A 1 14  ? 27.69300  -18.43300 -20.40000 1.000 89.22806  ? 50  ILE   A O   1 
ATOM   104  C  CB  . ILE   A 1 14  ? 29.59900  -17.00300 -18.75800 1.000 88.25640  ? 50  ILE   A CB  1 
ATOM   105  C  CG1 . ILE   A 1 14  ? 29.05400  -15.80200 -17.98400 1.000 83.63156  ? 50  ILE   A CG1 1 
ATOM   106  C  CG2 . ILE   A 1 14  ? 31.06100  -17.26600 -18.42100 1.000 90.33418  ? 50  ILE   A CG2 1 
ATOM   107  C  CD1 . ILE   A 1 14  ? 29.21300  -15.92100 -16.48600 1.000 80.51538  ? 50  ILE   A CD1 1 
ATOM   108  N  N   . GLY   A 1 15  ? 27.27800  -16.47100 -21.41200 1.000 93.91737  ? 51  GLY   A N   1 
ATOM   109  C  CA  . GLY   A 1 15  ? 25.97000  -16.90200 -21.86400 1.000 100.13293 ? 51  GLY   A CA  1 
ATOM   110  C  C   . GLY   A 1 15  ? 25.26100  -15.78500 -22.60000 1.000 108.98170 ? 51  GLY   A C   1 
ATOM   111  O  O   . GLY   A 1 15  ? 25.55600  -14.59900 -22.41300 1.000 108.77008 ? 51  GLY   A O   1 
ATOM   112  N  N   . GLU   A 1 16  ? 24.31400  -16.19400 -23.44400 1.000 117.94613 ? 52  GLU   A N   1 
ATOM   113  C  CA  . GLU   A 1 16  ? 23.48800  -15.26900 -24.21100 1.000 122.99745 ? 52  GLU   A CA  1 
ATOM   114  C  C   . GLU   A 1 16  ? 22.30200  -16.01900 -24.80600 1.000 126.43417 ? 52  GLU   A C   1 
ATOM   115  O  O   . GLU   A 1 16  ? 22.27200  -16.28600 -26.01200 1.000 128.91970 ? 52  GLU   A O   1 
ATOM   116  C  CB  . GLU   A 1 16  ? 24.31100  -14.59000 -25.31300 1.000 120.39041 ? 52  GLU   A CB  1 
ATOM   117  C  CG  . GLU   A 1 16  ? 23.66100  -13.35100 -25.92200 1.000 118.70193 ? 52  GLU   A CG  1 
ATOM   118  C  CD  . GLU   A 1 16  ? 23.03000  -13.61600 -27.27800 1.000 120.80150 ? 52  GLU   A CD  1 
ATOM   119  O  OE1 . GLU   A 1 16  ? 23.45700  -14.57100 -27.95900 1.000 122.94133 ? 52  GLU   A OE1 1 
ATOM   120  O  OE2 . GLU   A 1 16  ? 22.10700  -12.86700 -27.66200 1.000 119.38476 ? 52  GLU   A OE2 1 
ATOM   121  N  N   . GLY   A 1 17  ? 21.32600  -16.37300 -23.97200 1.000 132.60606 ? 53  GLY   A N   1 
ATOM   122  C  CA  . GLY   A 1 17  ? 20.20700  -17.16800 -24.44100 1.000 140.16180 ? 53  GLY   A CA  1 
ATOM   123  C  C   . GLY   A 1 17  ? 18.90800  -16.99100 -23.67900 1.000 146.16891 ? 53  GLY   A C   1 
ATOM   124  O  O   . GLY   A 1 17  ? 18.31600  -15.90800 -23.68500 1.000 148.81633 ? 53  GLY   A O   1 
ATOM   125  N  N   . SER   A 1 18  ? 18.46200  -18.06000 -23.01200 1.000 144.67122 ? 54  SER   A N   1 
ATOM   126  C  CA  . SER   A 1 18  ? 17.12900  -18.09200 -22.41700 1.000 142.64475 ? 54  SER   A CA  1 
ATOM   127  C  C   . SER   A 1 18  ? 16.94500  -17.07300 -21.30000 1.000 147.41537 ? 54  SER   A C   1 
ATOM   128  O  O   . SER   A 1 18  ? 15.80300  -16.79100 -20.92000 1.000 143.54631 ? 54  SER   A O   1 
ATOM   129  C  CB  . SER   A 1 18  ? 16.83000  -19.49400 -21.88300 1.000 138.15139 ? 54  SER   A CB  1 
ATOM   130  O  OG  . SER   A 1 18  ? 15.66600  -19.49600 -21.07400 1.000 137.43731 ? 54  SER   A OG  1 
ATOM   131  N  N   . PHE   A 1 19  ? 18.03200  -16.51700 -20.75900 1.000 162.86556 ? 55  PHE   A N   1 
ATOM   132  C  CA  . PHE   A 1 19  ? 17.93200  -15.59400 -19.63400 1.000 158.19689 ? 55  PHE   A CA  1 
ATOM   133  C  C   . PHE   A 1 19  ? 18.70500  -14.30200 -19.88000 1.000 159.74641 ? 55  PHE   A C   1 
ATOM   134  O  O   . PHE   A 1 19  ? 19.01900  -13.58300 -18.92500 1.000 160.61262 ? 55  PHE   A O   1 
ATOM   135  C  CB  . PHE   A 1 19  ? 18.40900  -16.27300 -18.34700 1.000 157.21144 ? 55  PHE   A CB  1 
ATOM   136  C  CG  . PHE   A 1 19  ? 17.78900  -17.62500 -18.11200 1.000 164.34447 ? 55  PHE   A CG  1 
ATOM   137  C  CD1 . PHE   A 1 19  ? 16.46500  -17.73700 -17.71800 1.000 153.78618 ? 55  PHE   A CD1 1 
ATOM   138  C  CD2 . PHE   A 1 19  ? 18.52900  -18.78400 -18.29100 1.000 160.44055 ? 55  PHE   A CD2 1 
ATOM   139  C  CE1 . PHE   A 1 19  ? 15.89000  -18.97900 -17.50600 1.000 146.10507 ? 55  PHE   A CE1 1 
ATOM   140  C  CE2 . PHE   A 1 19  ? 17.96000  -20.02800 -18.08000 1.000 152.57096 ? 55  PHE   A CE2 1 
ATOM   141  C  CZ  . PHE   A 1 19  ? 16.63900  -20.12500 -17.68600 1.000 145.13977 ? 55  PHE   A CZ  1 
ATOM   142  N  N   . GLY   A 1 20  ? 19.01200  -13.99000 -21.13300 1.000 149.58042 ? 56  GLY   A N   1 
ATOM   143  C  CA  . GLY   A 1 20  ? 19.67600  -12.74800 -21.47700 1.000 140.18786 ? 56  GLY   A CA  1 
ATOM   144  C  C   . GLY   A 1 20  ? 21.16700  -12.91900 -21.68600 1.000 127.62349 ? 56  GLY   A C   1 
ATOM   145  O  O   . GLY   A 1 20  ? 21.71800  -14.02300 -21.68300 1.000 127.90894 ? 56  GLY   A O   1 
ATOM   146  N  N   . VAL   A 1 21  ? 21.82600  -11.78000 -21.87500 1.000 120.44204 ? 57  VAL   A N   1 
ATOM   147  C  CA  . VAL   A 1 21  ? 23.27100  -11.75100 -22.07500 1.000 115.36516 ? 57  VAL   A CA  1 
ATOM   148  C  C   . VAL   A 1 21  ? 23.94600  -11.76400 -20.70900 1.000 110.34927 ? 57  VAL   A C   1 
ATOM   149  O  O   . VAL   A 1 21  ? 23.71400  -10.87500 -19.88300 1.000 115.25263 ? 57  VAL   A O   1 
ATOM   150  C  CB  . VAL   A 1 21  ? 23.69000  -10.52000 -22.89100 1.000 114.87334 ? 57  VAL   A CB  1 
ATOM   151  C  CG1 . VAL   A 1 21  ? 25.04000  -10.75200 -23.54900 1.000 113.66394 ? 57  VAL   A CG1 1 
ATOM   152  C  CG2 . VAL   A 1 21  ? 22.63200  -10.18500 -23.93000 1.000 116.82440 ? 57  VAL   A CG2 1 
ATOM   153  N  N   . ILE   A 1 22  ? 24.77700  -12.77500 -20.46400 1.000 105.75934 ? 58  ILE   A N   1 
ATOM   154  C  CA  . ILE   A 1 22  ? 25.44900  -12.95200 -19.18200 1.000 97.72355  ? 58  ILE   A CA  1 
ATOM   155  C  C   . ILE   A 1 22  ? 26.95300  -12.86600 -19.40400 1.000 92.62837  ? 58  ILE   A C   1 
ATOM   156  O  O   . ILE   A 1 22  ? 27.49300  -13.52900 -20.29800 1.000 91.39819  ? 58  ILE   A O   1 
ATOM   157  C  CB  . ILE   A 1 22  ? 25.06900  -14.28900 -18.51800 1.000 92.98046  ? 58  ILE   A CB  1 
ATOM   158  C  CG1 . ILE   A 1 22  ? 23.54800  -14.45800 -18.50600 1.000 100.45206 ? 58  ILE   A CG1 1 
ATOM   159  C  CG2 . ILE   A 1 22  ? 25.62900  -14.35900 -17.10500 1.000 87.11695  ? 58  ILE   A CG2 1 
ATOM   160  C  CD1 . ILE   A 1 22  ? 23.05300  -15.54900 -17.57700 1.000 99.48915  ? 58  ILE   A CD1 1 
ATOM   161  N  N   . PHE   A 1 23  ? 27.62200  -12.05600 -18.59000 1.000 86.20339  ? 59  PHE   A N   1 
ATOM   162  C  CA  . PHE   A 1 23  ? 29.06000  -11.85000 -18.66300 1.000 84.53281  ? 59  PHE   A CA  1 
ATOM   163  C  C   . PHE   A 1 23  ? 29.72000  -12.24200 -17.34800 1.000 76.72617  ? 59  PHE   A C   1 
ATOM   164  O  O   . PHE   A 1 23  ? 29.06300  -12.41500 -16.31800 1.000 78.66442  ? 59  PHE   A O   1 
ATOM   165  C  CB  . PHE   A 1 23  ? 29.39800  -10.38600 -18.97500 1.000 83.77919  ? 59  PHE   A CB  1 
ATOM   166  C  CG  . PHE   A 1 23  ? 29.10700  -9.97700  -20.38500 1.000 89.03704  ? 59  PHE   A CG  1 
ATOM   167  C  CD1 . PHE   A 1 23  ? 30.06200  -10.13600 -21.37400 1.000 92.45698  ? 59  PHE   A CD1 1 
ATOM   168  C  CD2 . PHE   A 1 23  ? 27.88900  -9.41300  -20.71900 1.000 92.85212  ? 59  PHE   A CD2 1 
ATOM   169  C  CE1 . PHE   A 1 23  ? 29.80200  -9.75400  -22.67300 1.000 98.15975  ? 59  PHE   A CE1 1 
ATOM   170  C  CE2 . PHE   A 1 23  ? 27.62500  -9.02600  -22.01500 1.000 98.43180  ? 59  PHE   A CE2 1 
ATOM   171  C  CZ  . PHE   A 1 23  ? 28.58100  -9.19800  -22.99500 1.000 99.84453  ? 59  PHE   A CZ  1 
ATOM   172  N  N   . GLU   A 1 24  ? 31.04200  -12.37900 -17.40000 1.000 71.98906  ? 60  GLU   A N   1 
ATOM   173  C  CA  . GLU   A 1 24  ? 31.86200  -12.39000 -16.20000 1.000 69.97304  ? 60  GLU   A CA  1 
ATOM   174  C  C   . GLU   A 1 24  ? 32.20700  -10.95400 -15.82700 1.000 71.00097  ? 60  GLU   A C   1 
ATOM   175  O  O   . GLU   A 1 24  ? 32.24800  -10.06400 -16.68000 1.000 70.22131  ? 60  GLU   A O   1 
ATOM   176  C  CB  . GLU   A 1 24  ? 33.14400  -13.20500 -16.40100 1.000 72.52850  ? 60  GLU   A CB  1 
ATOM   177  C  CG  . GLU   A 1 24  ? 32.93200  -14.71400 -16.46400 1.000 82.76096  ? 60  GLU   A CG  1 
ATOM   178  C  CD  . GLU   A 1 24  ? 34.23400  -15.50700 -16.48300 1.000 81.31638  ? 60  GLU   A CD  1 
ATOM   179  O  OE1 . GLU   A 1 24  ? 35.32000  -14.89000 -16.52700 1.000 65.45773  ? 60  GLU   A OE1 1 
ATOM   180  O  OE2 . GLU   A 1 24  ? 34.16600  -16.75600 -16.45200 1.000 81.08208  ? 60  GLU   A OE2 1 
ATOM   181  N  N   . GLY   A 1 25  ? 32.44200  -10.73000 -14.53700 1.000 65.01859  ? 61  GLY   A N   1 
ATOM   182  C  CA  . GLY   A 1 25  ? 32.72500  -9.39000  -14.06900 1.000 63.59708  ? 61  GLY   A CA  1 
ATOM   183  C  C   . GLY   A 1 25  ? 33.67800  -9.40700  -12.89600 1.000 59.84928  ? 61  GLY   A C   1 
ATOM   184  O  O   . GLY   A 1 25  ? 33.96200  -10.45300 -12.30900 1.000 51.76058  ? 61  GLY   A O   1 
ATOM   185  N  N   . THR   A 1 26  ? 34.16400  -8.21500  -12.55900 1.000 55.17740  ? 62  THR   A N   1 
ATOM   186  C  CA  . THR   A 1 26  ? 35.08800  -8.03000  -11.44800 1.000 53.54861  ? 62  THR   A CA  1 
ATOM   187  C  C   . THR   A 1 26  ? 34.73100  -6.73900  -10.73200 1.000 52.66830  ? 62  THR   A C   1 
ATOM   188  O  O   . THR   A 1 26  ? 34.66400  -5.67700  -11.35800 1.000 50.95489  ? 62  THR   A O   1 
ATOM   189  C  CB  . THR   A 1 26  ? 36.54100  -7.99100  -11.93300 1.000 61.71540  ? 62  THR   A CB  1 
ATOM   190  O  OG1 . THR   A 1 26  ? 36.90300  -9.27100  -12.46600 1.000 64.91041  ? 62  THR   A OG1 1 
ATOM   191  C  CG2 . THR   A 1 26  ? 37.48100  -7.63900  -10.78600 1.000 62.53889  ? 62  THR   A CG2 1 
ATOM   192  N  N   . ASN   A 1 27  ? 34.49100  -6.83700  -9.42700  1.000 43.95266  ? 63  ASN   A N   1 
ATOM   193  C  CA  . ASN   A 1 27  ? 34.28800  -5.65600  -8.60200  1.000 52.06301  ? 63  ASN   A CA  1 
ATOM   194  C  C   . ASN   A 1 27  ? 35.56500  -4.82500  -8.58200  1.000 55.83423  ? 63  ASN   A C   1 
ATOM   195  O  O   . ASN   A 1 27  ? 36.63300  -5.32400  -8.21400  1.000 49.81495  ? 63  ASN   A O   1 
ATOM   196  C  CB  . ASN   A 1 27  ? 33.88300  -6.08500  -7.19100  1.000 50.58580  ? 63  ASN   A CB  1 
ATOM   197  C  CG  . ASN   A 1 27  ? 33.48500  -4.91900  -6.30500  1.000 58.12729  ? 63  ASN   A CG  1 
ATOM   198  O  OD1 . ASN   A 1 27  ? 34.21900  -3.94400  -6.17300  1.000 55.72479  ? 63  ASN   A OD1 1 
ATOM   199  N  ND2 . ASN   A 1 27  ? 32.31700  -5.02600  -5.67900  1.000 56.80945  ? 63  ASN   A ND2 1 
ATOM   200  N  N   . ILE   A 1 28  ? 35.46000  -3.55400  -8.99100  1.000 44.39809  ? 64  ILE   A N   1 
ATOM   201  C  CA  . ILE   A 1 28  ? 36.65000  -2.71800  -9.15300  1.000 50.24424  ? 64  ILE   A CA  1 
ATOM   202  C  C   . ILE   A 1 28  ? 37.15600  -2.15000  -7.83900  1.000 47.85819  ? 64  ILE   A C   1 
ATOM   203  O  O   . ILE   A 1 28  ? 38.21700  -1.51100  -7.82000  1.000 45.83431  ? 64  ILE   A O   1 
ATOM   204  C  CB  . ILE   A 1 28  ? 36.38000  -1.56800  -10.14400 1.000 52.80039  ? 64  ILE   A CB  1 
ATOM   205  C  CG1 . ILE   A 1 28  ? 35.55000  -0.46600  -9.48300  1.000 49.00114  ? 64  ILE   A CG1 1 
ATOM   206  C  CG2 . ILE   A 1 28  ? 35.66800  -2.09800  -11.38000 1.000 62.52204  ? 64  ILE   A CG2 1 
ATOM   207  C  CD1 . ILE   A 1 28  ? 35.18100  0.66800   -10.42800 1.000 62.09962  ? 64  ILE   A CD1 1 
ATOM   208  N  N   . ILE   A 1 29  ? 36.43100  -2.35900  -6.74400  1.000 49.02209  ? 65  ILE   A N   1 
ATOM   209  C  CA  . ILE   A 1 29  ? 36.89300  -1.94300  -5.42500  1.000 50.19307  ? 65  ILE   A CA  1 
ATOM   210  C  C   . ILE   A 1 29  ? 37.75100  -3.02000  -4.77400  1.000 50.67543  ? 65  ILE   A C   1 
ATOM   211  O  O   . ILE   A 1 29  ? 38.82400  -2.73000  -4.23800  1.000 51.61147  ? 65  ILE   A O   1 
ATOM   212  C  CB  . ILE   A 1 29  ? 35.68800  -1.57300  -4.53300  1.000 54.56766  ? 65  ILE   A CB  1 
ATOM   213  C  CG1 . ILE   A 1 29  ? 34.96500  -0.33700  -5.08300  1.000 57.49364  ? 65  ILE   A CG1 1 
ATOM   214  C  CG2 . ILE   A 1 29  ? 36.13800  -1.33900  -3.09800  1.000 52.57712  ? 65  ILE   A CG2 1 
ATOM   215  C  CD1 . ILE   A 1 29  ? 35.79100  0.93000   -5.03900  1.000 59.69746  ? 65  ILE   A CD1 1 
ATOM   216  N  N   . ASN   A 1 30  ? 37.30700  -4.28000  -4.81600  1.000 56.26125  ? 66  ASN   A N   1 
ATOM   217  C  CA  . ASN   A 1 30  ? 38.00100  -5.35700  -4.12300  1.000 55.40381  ? 66  ASN   A CA  1 
ATOM   218  C  C   . ASN   A 1 30  ? 38.49500  -6.48300  -5.02100  1.000 61.34618  ? 66  ASN   A C   1 
ATOM   219  O  O   . ASN   A 1 30  ? 39.22600  -7.35400  -4.53500  1.000 64.15057  ? 66  ASN   A O   1 
ATOM   220  C  CB  . ASN   A 1 30  ? 37.10200  -5.96100  -3.03100  1.000 53.41061  ? 66  ASN   A CB  1 
ATOM   221  C  CG  . ASN   A 1 30  ? 35.75700  -6.42200  -3.56300  1.000 61.07979  ? 66  ASN   A CG  1 
ATOM   222  O  OD1 . ASN   A 1 30  ? 35.65000  -6.92300  -4.68200  1.000 57.27139  ? 66  ASN   A OD1 1 
ATOM   223  N  ND2 . ASN   A 1 30  ? 34.71700  -6.24900  -2.75600  1.000 63.09261  ? 66  ASN   A ND2 1 
ATOM   224  N  N   . GLY   A 1 31  ? 38.11900  -6.50600  -6.29800  1.000 58.72244  ? 67  GLY   A N   1 
ATOM   225  C  CA  . GLY   A 1 31  ? 38.56700  -7.55000  -7.19600  1.000 55.42111  ? 67  GLY   A CA  1 
ATOM   226  C  C   . GLY   A 1 31  ? 37.73100  -8.81300  -7.20700  1.000 52.55977  ? 67  GLY   A C   1 
ATOM   227  O  O   . GLY   A 1 31  ? 38.00800  -9.70700  -8.01900  1.000 49.97476  ? 67  GLY   A O   1 
ATOM   228  N  N   . VAL   A 1 32  ? 36.72600  -8.91900  -6.34700  1.000 53.70412  ? 68  VAL   A N   1 
ATOM   229  C  CA  . VAL   A 1 32  ? 35.92400  -10.14900 -6.27900  1.000 54.39700  ? 68  VAL   A CA  1 
ATOM   230  C  C   . VAL   A 1 32  ? 35.14300  -10.31500 -7.57900  1.000 52.93896  ? 68  VAL   A C   1 
ATOM   231  O  O   . VAL   A 1 32  ? 34.51600  -9.34600  -8.05200  1.000 56.19681  ? 68  VAL   A O   1 
ATOM   232  C  CB  . VAL   A 1 32  ? 34.98900  -10.10900 -5.06900  1.000 61.56667  ? 68  VAL   A CB  1 
ATOM   233  C  CG1 . VAL   A 1 32  ? 33.85500  -11.12100 -5.22400  1.000 60.60336  ? 68  VAL   A CG1 1 
ATOM   234  C  CG2 . VAL   A 1 32  ? 35.77500  -10.38500 -3.79600  1.000 63.77602  ? 68  VAL   A CG2 1 
ATOM   235  N  N   . PRO   A 1 33  ? 35.15700  -11.49400 -8.19700  1.000 52.34854  ? 69  PRO   A N   1 
ATOM   236  C  CA  . PRO   A 1 33  ? 34.42700  -11.67000 -9.45400  1.000 47.77276  ? 69  PRO   A CA  1 
ATOM   237  C  C   . PRO   A 1 33  ? 32.92500  -11.66300 -9.23400  1.000 55.11211  ? 69  PRO   A C   1 
ATOM   238  O  O   . PRO   A 1 33  ? 32.42400  -12.00400 -8.16000  1.000 50.91016  ? 69  PRO   A O   1 
ATOM   239  C  CB  . PRO   A 1 33  ? 34.91100  -13.03300 -9.95700  1.000 61.86539  ? 69  PRO   A CB  1 
ATOM   240  C  CG  . PRO   A 1 33  ? 35.30200  -13.75900 -8.71600  1.000 57.86552  ? 69  PRO   A CG  1 
ATOM   241  C  CD  . PRO   A 1 33  ? 35.88400  -12.71600 -7.80600  1.000 55.08272  ? 69  PRO   A CD  1 
ATOM   242  N  N   . VAL   A 1 34  ? 32.20500  -11.25700 -10.27600 1.000 54.82544  ? 70  VAL   A N   1 
ATOM   243  C  CA  . VAL   A 1 34  ? 30.75200  -11.18400 -10.25300 1.000 54.95660  ? 70  VAL   A CA  1 
ATOM   244  C  C   . VAL   A 1 34  ? 30.21900  -11.71900 -11.57500 1.000 59.22343  ? 70  VAL   A C   1 
ATOM   245  O  O   . VAL   A 1 34  ? 30.95800  -11.90500 -12.54500 1.000 58.72869  ? 70  VAL   A O   1 
ATOM   246  C  CB  . VAL   A 1 34  ? 30.23600  -9.74800  -10.00200 1.000 53.07182  ? 70  VAL   A CB  1 
ATOM   247  C  CG1 . VAL   A 1 34  ? 30.51900  -9.31100  -8.56500  1.000 46.53260  ? 70  VAL   A CG1 1 
ATOM   248  C  CG2 . VAL   A 1 34  ? 30.86100  -8.76900  -10.99200 1.000 43.93836  ? 70  VAL   A CG2 1 
ATOM   249  N  N   . ALA   A 1 35  ? 28.91800  -11.99400 -11.59100 1.000 57.41687  ? 71  ALA   A N   1 
ATOM   250  C  CA  . ALA   A 1 35  ? 28.18600  -12.33700 -12.80100 1.000 62.24387  ? 71  ALA   A CA  1 
ATOM   251  C  C   . ALA   A 1 35  ? 27.26800  -11.17700 -13.15300 1.000 68.59916  ? 71  ALA   A C   1 
ATOM   252  O  O   . ALA   A 1 35  ? 26.49700  -10.71400 -12.30600 1.000 65.55146  ? 71  ALA   A O   1 
ATOM   253  C  CB  . ALA   A 1 35  ? 27.37400  -13.62000 -12.61400 1.000 61.39172  ? 71  ALA   A CB  1 
ATOM   254  N  N   . ILE   A 1 36  ? 27.35500  -10.70600 -14.39300 1.000 71.59438  ? 72  ILE   A N   1 
ATOM   255  C  CA  . ILE   A 1 36  ? 26.59400  -9.55000  -14.85500 1.000 76.55270  ? 72  ILE   A CA  1 
ATOM   256  C  C   . ILE   A 1 36  ? 25.58400  -10.02500 -15.88900 1.000 82.32119  ? 72  ILE   A C   1 
ATOM   257  O  O   . ILE   A 1 36  ? 25.96300  -10.56800 -16.93500 1.000 84.87186  ? 72  ILE   A O   1 
ATOM   258  C  CB  . ILE   A 1 36  ? 27.51400  -8.46500  -15.43500 1.000 73.36308  ? 72  ILE   A CB  1 
ATOM   259  C  CG1 . ILE   A 1 36  ? 28.68500  -8.21000  -14.48200 1.000 63.83297  ? 72  ILE   A CG1 1 
ATOM   260  C  CG2 . ILE   A 1 36  ? 26.73400  -7.18300  -15.69700 1.000 75.50123  ? 72  ILE   A CG2 1 
ATOM   261  C  CD1 . ILE   A 1 36  ? 29.58500  -7.07200  -14.89600 1.000 66.95862  ? 72  ILE   A CD1 1 
ATOM   262  N  N   . LYS   A 1 37  ? 24.30000  -9.82000  -15.60200 1.000 83.16972  ? 73  LYS   A N   1 
ATOM   263  C  CA  . LYS   A 1 37  ? 23.22400  -10.19000 -16.51200 1.000 93.02664  ? 73  LYS   A CA  1 
ATOM   264  C  C   . LYS   A 1 37  ? 22.68500  -8.95400  -17.21700 1.000 101.56864 ? 73  LYS   A C   1 
ATOM   265  O  O   . LYS   A 1 37  ? 22.34000  -7.96100  -16.56900 1.000 96.59003  ? 73  LYS   A O   1 
ATOM   266  C  CB  . LYS   A 1 37  ? 22.09200  -10.90300 -15.77300 1.000 92.94267  ? 73  LYS   A CB  1 
ATOM   267  C  CG  . LYS   A 1 37  ? 22.16600  -12.40600 -15.88600 1.000 96.98127  ? 73  LYS   A CG  1 
ATOM   268  C  CD  . LYS   A 1 37  ? 20.78400  -13.02800 -15.97400 1.000 101.33462 ? 73  LYS   A CD  1 
ATOM   269  C  CE  . LYS   A 1 37  ? 20.03000  -12.88200 -14.67300 1.000 98.53241  ? 73  LYS   A CE  1 
ATOM   270  N  NZ  . LYS   A 1 37  ? 18.83700  -13.77400 -14.64400 1.000 98.62132  ? 73  LYS   A NZ  1 
ATOM   271  N  N   . PHE   A 1 38  ? 22.61000  -9.02100  -18.54100 1.000 104.84750 ? 74  PHE   A N   1 
ATOM   272  C  CA  . PHE   A 1 38  ? 22.06500  -7.94500  -19.35600 1.000 108.61207 ? 74  PHE   A CA  1 
ATOM   273  C  C   . PHE   A 1 38  ? 20.70200  -8.35500  -19.89400 1.000 114.78878 ? 74  PHE   A C   1 
ATOM   274  O  O   . PHE   A 1 38  ? 20.54500  -9.45500  -20.43200 1.000 119.13093 ? 74  PHE   A O   1 
ATOM   275  C  CB  . PHE   A 1 38  ? 23.01100  -7.59500  -20.50600 1.000 107.16121 ? 74  PHE   A CB  1 
ATOM   276  C  CG  . PHE   A 1 38  ? 24.13900  -6.69400  -20.10300 1.000 100.05223 ? 74  PHE   A CG  1 
ATOM   277  C  CD1 . PHE   A 1 38  ? 23.98200  -5.31900  -20.12600 1.000 102.07060 ? 74  PHE   A CD1 1 
ATOM   278  C  CD2 . PHE   A 1 38  ? 25.35000  -7.21900  -19.69100 1.000 92.90980  ? 74  PHE   A CD2 1 
ATOM   279  C  CE1 . PHE   A 1 38  ? 25.01400  -4.48300  -19.75100 1.000 98.40602  ? 74  PHE   A CE1 1 
ATOM   280  C  CE2 . PHE   A 1 38  ? 26.38700  -6.39000  -19.31500 1.000 87.66597  ? 74  PHE   A CE2 1 
ATOM   281  C  CZ  . PHE   A 1 38  ? 26.22000  -5.02000  -19.34400 1.000 93.72948  ? 74  PHE   A CZ  1 
ATOM   282  N  N   . GLU   A 1 39  ? 19.71800  -7.47000  -19.74000 1.000 116.20135 ? 75  GLU   A N   1 
ATOM   283  C  CA  . GLU   A 1 39  ? 18.37800  -7.70100  -20.26100 1.000 124.24434 ? 75  GLU   A CA  1 
ATOM   284  C  C   . GLU   A 1 39  ? 17.92700  -6.40200  -20.92100 1.000 128.35994 ? 75  GLU   A C   1 
ATOM   285  O  O   . GLU   A 1 39  ? 18.09400  -5.32500  -20.32600 1.000 126.77595 ? 75  GLU   A O   1 
ATOM   286  C  CB  . GLU   A 1 39  ? 17.40200  -8.11100  -19.15800 1.000 123.74111 ? 75  GLU   A CB  1 
ATOM   287  C  CG  . GLU   A 1 39  ? 15.94100  -8.04800  -19.56600 1.000 128.75644 ? 75  GLU   A CG  1 
ATOM   288  C  CD  . GLU   A 1 39  ? 15.00600  -7.90900  -18.37700 1.000 130.19418 ? 75  GLU   A CD  1 
ATOM   289  O  OE1 . GLU   A 1 39  ? 15.23600  -7.01200  -17.54100 1.000 127.94557 ? 75  GLU   A OE1 1 
ATOM   290  O  OE2 . GLU   A 1 39  ? 14.05000  -8.70600  -18.27100 1.000 134.99404 ? 75  GLU   A OE2 1 
ATOM   291  N  N   . PRO   A 1 40  ? 17.34400  -6.45600  -22.12200 1.000 137.21042 ? 76  PRO   A N   1 
ATOM   292  C  CA  . PRO   A 1 40  ? 16.95800  -5.21500  -22.80700 1.000 137.11086 ? 76  PRO   A CA  1 
ATOM   293  C  C   . PRO   A 1 40  ? 15.90500  -4.45300  -22.02100 1.000 131.05600 ? 76  PRO   A C   1 
ATOM   294  O  O   . PRO   A 1 40  ? 15.29000  -4.98500  -21.09600 1.000 133.79028 ? 76  PRO   A O   1 
ATOM   295  C  CB  . PRO   A 1 40  ? 16.40500  -5.69700  -24.15400 1.000 133.70001 ? 76  PRO   A CB  1 
ATOM   296  C  CG  . PRO   A 1 40  ? 16.94800  -7.02100  -24.33000 1.000 137.06185 ? 76  PRO   A CG  1 
ATOM   297  C  CD  . PRO   A 1 40  ? 17.12900  -7.63300  -22.97800 1.000 136.51120 ? 76  PRO   A CD  1 
ATOM   298  N  N   . ARG   A 1 41  ? 15.70800  -3.18000  -22.39400 1.000 127.15858 ? 77  ARG   A N   1 
ATOM   299  C  CA  . ARG   A 1 41  ? 14.79600  -2.32100  -21.63300 1.000 128.97609 ? 77  ARG   A CA  1 
ATOM   300  C  C   . ARG   A 1 41  ? 13.34000  -2.65500  -21.94600 1.000 128.01265 ? 77  ARG   A C   1 
ATOM   301  O  O   . ARG   A 1 41  ? 12.62100  -3.17200  -21.08900 1.000 127.43516 ? 77  ARG   A O   1 
ATOM   302  C  CB  . ARG   A 1 41  ? 15.10600  -0.83800  -21.89300 1.000 126.70224 ? 77  ARG   A CB  1 
ATOM   303  C  CG  . ARG   A 1 41  ? 15.95800  -0.19800  -20.79000 1.000 121.81746 ? 77  ARG   A CG  1 
ATOM   304  C  CD  . ARG   A 1 41  ? 15.38200  -0.39700  -19.38400 1.000 117.99498 ? 77  ARG   A CD  1 
ATOM   305  N  NE  . ARG   A 1 41  ? 13.95700  -0.09700  -19.32800 1.000 116.43820 ? 77  ARG   A NE  1 
ATOM   306  C  CZ  . ARG   A 1 41  ? 13.04200  -0.96400  -18.92200 1.000 115.27290 ? 77  ARG   A CZ  1 
ATOM   307  N  NH1 . ARG   A 1 41  ? 13.38200  -2.15100  -18.44400 1.000 110.78627 ? 77  ARG   A NH1 1 
ATOM   308  N  NH2 . ARG   A 1 41  ? 11.75300  -0.66700  -19.06500 1.000 117.27711 ? 77  ARG   A NH2 1 
ATOM   309  N  N   . LYS   A 1 42  ? 12.89700  -2.42100  -23.18000 1.000 128.85672 ? 78  LYS   A N   1 
ATOM   310  C  CA  . LYS   A 1 42  ? 11.53900  -2.78400  -23.57800 1.000 137.26756 ? 78  LYS   A CA  1 
ATOM   311  C  C   . LYS   A 1 42  ? 11.54800  -4.20200  -24.13900 1.000 138.17078 ? 78  LYS   A C   1 
ATOM   312  O  O   . LYS   A 1 42  ? 11.97000  -4.44000  -25.27600 1.000 137.79120 ? 78  LYS   A O   1 
ATOM   313  C  CB  . LYS   A 1 42  ? 10.98300  -1.77200  -24.57300 1.000 141.57262 ? 78  LYS   A CB  1 
ATOM   314  C  CG  . LYS   A 1 42  ? 10.58100  -0.43100  -23.93100 1.000 148.71542 ? 78  LYS   A CG  1 
ATOM   315  C  CD  . LYS   A 1 42  ? 9.66400   -0.65700  -22.75100 1.000 146.16194 ? 78  LYS   A CD  1 
ATOM   316  C  CE  . LYS   A 1 42  ? 8.32900   -1.24800  -23.17500 1.000 145.96361 ? 78  LYS   A CE  1 
ATOM   317  N  NZ  . LYS   A 1 42  ? 7.63100   -1.90400  -22.03300 1.000 148.20093 ? 78  LYS   A NZ  1 
ATOM   318  N  N   . THR   A 1 43  ? 11.07000  -5.14300  -23.33000 1.000 135.56091 ? 79  THR   A N   1 
ATOM   319  C  CA  . THR   A 1 43  ? 10.96600  -6.53100  -23.72500 1.000 134.21938 ? 79  THR   A CA  1 
ATOM   320  C  C   . THR   A 1 43  ? 9.54200   -7.02400  -23.51300 1.000 139.19018 ? 79  THR   A C   1 
ATOM   321  O  O   . THR   A 1 43  ? 8.74000   -6.41300  -22.80000 1.000 140.32234 ? 79  THR   A O   1 
ATOM   322  C  CB  . THR   A 1 43  ? 11.93600  -7.42400  -22.94000 1.000 135.99590 ? 79  THR   A CB  1 
ATOM   323  O  OG1 . THR   A 1 43  ? 11.40100  -7.68600  -21.63800 1.000 143.87215 ? 79  THR   A OG1 1 
ATOM   324  C  CG2 . THR   A 1 43  ? 13.29600  -6.76200  -22.79600 1.000 131.43459 ? 79  THR   A CG2 1 
ATOM   325  N  N   . GLU   A 1 44  ? 9.24300   -8.16500  -24.13900 1.000 140.39085 ? 80  GLU   A N   1 
ATOM   326  C  CA  . GLU   A 1 44  ? 7.92700   -8.77100  -23.97600 1.000 143.27897 ? 80  GLU   A CA  1 
ATOM   327  C  C   . GLU   A 1 44  ? 7.74600   -9.34400  -22.57600 1.000 148.63519 ? 80  GLU   A C   1 
ATOM   328  O  O   . GLU   A 1 44  ? 6.62600   -9.35500  -22.05400 1.000 151.75056 ? 80  GLU   A O   1 
ATOM   329  C  CB  . GLU   A 1 44  ? 7.71900   -9.85400  -25.03600 1.000 140.34611 ? 80  GLU   A CB  1 
ATOM   330  C  CG  . GLU   A 1 44  ? 6.27200   -10.28000 -25.24500 1.000 142.72814 ? 80  GLU   A CG  1 
ATOM   331  C  CD  . GLU   A 1 44  ? 6.05800   -10.94100 -26.59500 1.000 141.83801 ? 80  GLU   A CD  1 
ATOM   332  O  OE1 . GLU   A 1 44  ? 6.84700   -11.84200 -26.95500 1.000 140.53809 ? 80  GLU   A OE1 1 
ATOM   333  O  OE2 . GLU   A 1 44  ? 5.11200   -10.54500 -27.30600 1.000 141.99542 ? 80  GLU   A OE2 1 
ATOM   334  N  N   . ALA   A 1 45  ? 8.82700   -9.80600  -21.95200 1.000 152.62548 ? 81  ALA   A N   1 
ATOM   335  C  CA  . ALA   A 1 45  ? 8.77200   -10.43500 -20.63300 1.000 160.95665 ? 81  ALA   A CA  1 
ATOM   336  C  C   . ALA   A 1 45  ? 9.80400   -9.79900  -19.71000 1.000 165.31442 ? 81  ALA   A C   1 
ATOM   337  O  O   . ALA   A 1 45  ? 11.01000  -10.08200 -19.83100 1.000 163.68837 ? 81  ALA   A O   1 
ATOM   338  C  CB  . ALA   A 1 45  ? 9.00000   -11.93800 -20.73700 1.000 161.13555 ? 81  ALA   A CB  1 
ATOM   339  N  N   . PRO   A 1 46  ? 9.38000   -8.93400  -18.78500 1.000 177.88481 ? 82  PRO   A N   1 
ATOM   340  C  CA  . PRO   A 1 46  ? 10.32300  -8.37400  -17.80600 1.000 167.24557 ? 82  PRO   A CA  1 
ATOM   341  C  C   . PRO   A 1 46  ? 10.44300  -9.23500  -16.55500 1.000 160.60415 ? 82  PRO   A C   1 
ATOM   342  O  O   . PRO   A 1 46  ? 9.55800   -9.21800  -15.69400 1.000 160.20024 ? 82  PRO   A O   1 
ATOM   343  C  CB  . PRO   A 1 46  ? 9.71600   -7.00200  -17.49200 1.000 171.66969 ? 82  PRO   A CB  1 
ATOM   344  C  CG  . PRO   A 1 46  ? 8.24000   -7.20500  -17.68000 1.000 175.45768 ? 82  PRO   A CG  1 
ATOM   345  C  CD  . PRO   A 1 46  ? 8.06300   -8.27400  -18.73500 1.000 171.52941 ? 82  PRO   A CD  1 
ATOM   346  N  N   . GLN   A 1 47  ? 11.53900  -9.98800  -16.43700 1.000 150.52392 ? 83  GLN   A N   1 
ATOM   347  C  CA  . GLN   A 1 47  ? 11.72200  -10.91800 -15.32900 1.000 142.25890 ? 83  GLN   A CA  1 
ATOM   348  C  C   . GLN   A 1 47  ? 12.93900  -10.62100 -14.46300 1.000 120.32068 ? 83  GLN   A C   1 
ATOM   349  O  O   . GLN   A 1 47  ? 13.17400  -11.34600 -13.48900 1.000 114.98217 ? 83  GLN   A O   1 
ATOM   350  C  CB  . GLN   A 1 47  ? 11.82100  -12.35800 -15.85300 1.000 143.98044 ? 83  GLN   A CB  1 
ATOM   351  C  CG  . GLN   A 1 47  ? 10.51400  -12.92200 -16.38800 1.000 142.02135 ? 83  GLN   A CG  1 
ATOM   352  C  CD  . GLN   A 1 47  ? 10.57300  -14.42300 -16.60900 1.000 127.64160 ? 83  GLN   A CD  1 
ATOM   353  O  OE1 . GLN   A 1 47  ? 11.53800  -14.94300 -17.17000 1.000 130.01591 ? 83  GLN   A OE1 1 
ATOM   354  N  NE2 . GLN   A 1 47  ? 9.54200   -15.12700 -16.15800 1.000 122.16289 ? 83  GLN   A NE2 1 
ATOM   355  N  N   . LEU   A 1 48  ? 13.71200  -9.58200  -14.77800 1.000 115.62595 ? 84  LEU   A N   1 
ATOM   356  C  CA  . LEU   A 1 48  ? 14.94300  -9.31500  -14.04100 1.000 108.11555 ? 84  LEU   A CA  1 
ATOM   357  C  C   . LEU   A 1 48  ? 14.66200  -8.60200  -12.72200 1.000 102.06467 ? 84  LEU   A C   1 
ATOM   358  O  O   . LEU   A 1 48  ? 15.14700  -9.02400  -11.66600 1.000 97.00944  ? 84  LEU   A O   1 
ATOM   359  C  CB  . LEU   A 1 48  ? 15.90000  -8.49200  -14.91000 1.000 103.31244 ? 84  LEU   A CB  1 
ATOM   360  C  CG  . LEU   A 1 48  ? 17.39900  -8.52000  -14.59500 1.000 94.46854  ? 84  LEU   A CG  1 
ATOM   361  C  CD1 . LEU   A 1 48  ? 18.18600  -7.84300  -15.69800 1.000 96.49964  ? 84  LEU   A CD1 1 
ATOM   362  C  CD2 . LEU   A 1 48  ? 17.70300  -7.85700  -13.27200 1.000 86.67193  ? 84  LEU   A CD2 1 
ATOM   363  N  N   . ARG   A 1 49  ? 13.89900  -7.50700  -12.77300 1.000 93.27308  ? 85  ARG   A N   1 
ATOM   364  C  CA  . ARG   A 1 49  ? 13.64700  -6.71100  -11.57600 1.000 96.34466  ? 85  ARG   A CA  1 
ATOM   365  C  C   . ARG   A 1 49  ? 13.04900  -7.55100  -10.45500 1.000 99.31279  ? 85  ARG   A C   1 
ATOM   366  O  O   . ARG   A 1 49  ? 13.35600  -7.32700  -9.27900  1.000 92.23184  ? 85  ARG   A O   1 
ATOM   367  C  CB  . ARG   A 1 49  ? 12.72900  -5.53500  -11.92100 1.000 86.92472  ? 85  ARG   A CB  1 
ATOM   368  C  CG  . ARG   A 1 49  ? 12.47800  -4.57100  -10.77000 1.000 99.63144  ? 85  ARG   A CG  1 
ATOM   369  C  CD  . ARG   A 1 49  ? 11.09900  -4.77400  -10.16000 1.000 106.06248 ? 85  ARG   A CD  1 
ATOM   370  N  NE  . ARG   A 1 49  ? 11.01400  -4.18400  -8.83000  1.000 107.01891 ? 85  ARG   A NE  1 
ATOM   371  C  CZ  . ARG   A 1 49  ? 11.43800  -4.78100  -7.72500  1.000 103.88554 ? 85  ARG   A CZ  1 
ATOM   372  N  NH1 . ARG   A 1 49  ? 11.97300  -5.99100  -7.75600  1.000 99.56545  ? 85  ARG   A NH1 1 
ATOM   373  N  NH2 . ARG   A 1 49  ? 11.32800  -4.14800  -6.56100  1.000 100.45381 ? 85  ARG   A NH2 1 
ATOM   374  N  N   . ASP   A 1 50  ? 12.21000  -8.52800  -10.79700 1.000 110.16893 ? 86  ASP   A N   1 
ATOM   375  C  CA  . ASP   A 1 50  ? 11.66100  -9.41900  -9.78400  1.000 108.51049 ? 86  ASP   A CA  1 
ATOM   376  C  C   . ASP   A 1 50  ? 12.68700  -10.43600 -9.31100  1.000 102.32888 ? 86  ASP   A C   1 
ATOM   377  O  O   . ASP   A 1 50  ? 12.60800  -10.90800 -8.17100  1.000 103.12412 ? 86  ASP   A O   1 
ATOM   378  C  CB  . ASP   A 1 50  ? 10.42500  -10.12800 -10.33200 1.000 114.36848 ? 86  ASP   A CB  1 
ATOM   379  C  CG  . ASP   A 1 50  ? 9.39400   -9.15900  -10.85800 1.000 116.69688 ? 86  ASP   A CG  1 
ATOM   380  O  OD1 . ASP   A 1 50  ? 9.16200   -8.12700  -10.19500 1.000 115.32193 ? 86  ASP   A OD1 1 
ATOM   381  O  OD2 . ASP   A 1 50  ? 8.82800   -9.41800  -11.94000 1.000 130.65322 ? 86  ASP   A OD2 1 
ATOM   382  N  N   . GLU   A 1 51  ? 13.65300  -10.78400 -10.16100 1.000 87.55206  ? 87  GLU   A N   1 
ATOM   383  C  CA  . GLU   A 1 51  ? 14.70300  -11.70100 -9.73500  1.000 91.38428  ? 87  GLU   A CA  1 
ATOM   384  C  C   . GLU   A 1 51  ? 15.64400  -11.03900 -8.73800  1.000 85.79549  ? 87  GLU   A C   1 
ATOM   385  O  O   . GLU   A 1 51  ? 16.04600  -11.66200 -7.74700  1.000 74.24715  ? 87  GLU   A O   1 
ATOM   386  C  CB  . GLU   A 1 51  ? 15.48400  -12.20400 -10.94200 1.000 87.38956  ? 87  GLU   A CB  1 
ATOM   387  C  CG  . GLU   A 1 51  ? 16.81800  -12.79200 -10.56700 1.000 87.47050  ? 87  GLU   A CG  1 
ATOM   388  C  CD  . GLU   A 1 51  ? 17.36800  -13.68500 -11.64100 1.000 92.78894  ? 87  GLU   A CD  1 
ATOM   389  O  OE1 . GLU   A 1 51  ? 17.48100  -13.23300 -12.79900 1.000 101.33562 ? 87  GLU   A OE1 1 
ATOM   390  O  OE2 . GLU   A 1 51  ? 17.67100  -14.85400 -11.32500 1.000 92.15691  ? 87  GLU   A OE2 1 
ATOM   391  N  N   . TYR   A 1 52  ? 16.02400  -9.78600  -8.99400  1.000 87.75705  ? 88  TYR   A N   1 
ATOM   392  C  CA  . TYR   A 1 52  ? 16.82600  -9.04900  -8.02500  1.000 78.64528  ? 88  TYR   A CA  1 
ATOM   393  C  C   . TYR   A 1 52  ? 16.14700  -9.02200  -6.66400  1.000 78.23470  ? 88  TYR   A C   1 
ATOM   394  O  O   . TYR   A 1 52  ? 16.80000  -9.21000  -5.63000  1.000 72.17387  ? 88  TYR   A O   1 
ATOM   395  C  CB  . TYR   A 1 52  ? 17.08200  -7.62900  -8.52900  1.000 77.84655  ? 88  TYR   A CB  1 
ATOM   396  C  CG  . TYR   A 1 52  ? 17.60300  -6.68700  -7.46900  1.000 81.17716  ? 88  TYR   A CG  1 
ATOM   397  C  CD1 . TYR   A 1 52  ? 18.94500  -6.68300  -7.11400  1.000 85.84234  ? 88  TYR   A CD1 1 
ATOM   398  C  CD2 . TYR   A 1 52  ? 16.75100  -5.80200  -6.82100  1.000 83.74317  ? 88  TYR   A CD2 1 
ATOM   399  C  CE1 . TYR   A 1 52  ? 19.42400  -5.82300  -6.14600  1.000 91.22718  ? 88  TYR   A CE1 1 
ATOM   400  C  CE2 . TYR   A 1 52  ? 17.22000  -4.94000  -5.85100  1.000 86.13017  ? 88  TYR   A CE2 1 
ATOM   401  C  CZ  . TYR   A 1 52  ? 18.55700  -4.95500  -5.51800  1.000 89.95609  ? 88  TYR   A CZ  1 
ATOM   402  O  OH  . TYR   A 1 52  ? 19.03100  -4.09600  -4.55200  1.000 98.91436  ? 88  TYR   A OH  1 
ATOM   403  N  N   . ARG   A 1 53  ? 14.83000  -8.80400  -6.64500  1.000 80.68862  ? 89  ARG   A N   1 
ATOM   404  C  CA  . ARG   A 1 53  ? 14.10000  -8.81800  -5.38400  1.000 76.46373  ? 89  ARG   A CA  1 
ATOM   405  C  C   . ARG   A 1 53  ? 14.12000  -10.19900 -4.74400  1.000 79.85159  ? 89  ARG   A C   1 
ATOM   406  O  O   . ARG   A 1 53  ? 14.18500  -10.30900 -3.51400  1.000 82.25507  ? 89  ARG   A O   1 
ATOM   407  C  CB  . ARG   A 1 53  ? 12.66100  -8.35100  -5.60400  1.000 88.41183  ? 89  ARG   A CB  1 
ATOM   408  C  CG  . ARG   A 1 53  ? 11.90700  -8.03200  -4.32500  1.000 94.01226  ? 89  ARG   A CG  1 
ATOM   409  C  CD  . ARG   A 1 53  ? 10.62200  -7.26300  -4.61200  1.000 104.21187 ? 89  ARG   A CD  1 
ATOM   410  N  NE  . ARG   A 1 53  ? 10.05800  -6.68000  -3.40000  1.000 107.30492 ? 89  ARG   A NE  1 
ATOM   411  C  CZ  . ARG   A 1 53  ? 9.02400   -5.85000  -3.37700  1.000 110.64905 ? 89  ARG   A CZ  1 
ATOM   412  N  NH1 . ARG   A 1 53  ? 8.40600   -5.48400  -4.48900  1.000 115.04933 ? 89  ARG   A NH1 1 
ATOM   413  N  NH2 . ARG   A 1 53  ? 8.60200   -5.37100  -2.21000  1.000 103.85957 ? 89  ARG   A NH2 1 
ATOM   414  N  N   . THR   A 1 54  ? 14.07600  -11.25900 -5.55500  1.000 84.65581  ? 90  THR   A N   1 
ATOM   415  C  CA  . THR   A 1 54  ? 14.10800  -12.61000 -5.00300  1.000 79.54824  ? 90  THR   A CA  1 
ATOM   416  C  C   . THR   A 1 54  ? 15.44100  -12.89600 -4.31900  1.000 73.38753  ? 90  THR   A C   1 
ATOM   417  O  O   . THR   A 1 54  ? 15.47100  -13.49300 -3.23600  1.000 71.93800  ? 90  THR   A O   1 
ATOM   418  C  CB  . THR   A 1 54  ? 13.82700  -13.63400 -6.10300  1.000 74.54278  ? 90  THR   A CB  1 
ATOM   419  O  OG1 . THR   A 1 54  ? 12.63100  -13.26500 -6.80100  1.000 72.58398  ? 90  THR   A OG1 1 
ATOM   420  C  CG2 . THR   A 1 54  ? 13.63800  -15.01900 -5.50200  1.000 71.41317  ? 90  THR   A CG2 1 
ATOM   421  N  N   . TYR   A 1 55  ? 16.55300  -12.47400 -4.92800  1.000 71.74286  ? 91  TYR   A N   1 
ATOM   422  C  CA  . TYR   A 1 55  ? 17.84500  -12.63400 -4.26700  1.000 72.08336  ? 91  TYR   A CA  1 
ATOM   423  C  C   . TYR   A 1 55  ? 17.93200  -11.79400 -2.99900  1.000 70.91200  ? 91  TYR   A C   1 
ATOM   424  O  O   . TYR   A 1 55  ? 18.57500  -12.20800 -2.02800  1.000 72.93973  ? 91  TYR   A O   1 
ATOM   425  C  CB  . TYR   A 1 55  ? 18.98500  -12.27300 -5.22000  1.000 63.20134  ? 91  TYR   A CB  1 
ATOM   426  C  CG  . TYR   A 1 55  ? 19.25800  -13.31100 -6.28900  1.000 68.71600  ? 91  TYR   A CG  1 
ATOM   427  C  CD1 . TYR   A 1 55  ? 19.63400  -14.60700 -5.95000  1.000 67.59469  ? 91  TYR   A CD1 1 
ATOM   428  C  CD2 . TYR   A 1 55  ? 19.16400  -12.99000 -7.63600  1.000 63.40759  ? 91  TYR   A CD2 1 
ATOM   429  C  CE1 . TYR   A 1 55  ? 19.88700  -15.55700 -6.92400  1.000 66.55019  ? 91  TYR   A CE1 1 
ATOM   430  C  CE2 . TYR   A 1 55  ? 19.41900  -13.93400 -8.61600  1.000 68.27236  ? 91  TYR   A CE2 1 
ATOM   431  C  CZ  . TYR   A 1 55  ? 19.77700  -15.21400 -8.25500  1.000 68.05756  ? 91  TYR   A CZ  1 
ATOM   432  O  OH  . TYR   A 1 55  ? 20.03000  -16.15100 -9.23100  1.000 66.95597  ? 91  TYR   A OH  1 
ATOM   433  N  N   . LYS   A 1 56  ? 17.28900  -10.62300 -2.98300  1.000 75.52880  ? 92  LYS   A N   1 
ATOM   434  C  CA  . LYS   A 1 56  ? 17.29800  -9.79600  -1.78000  1.000 73.79959  ? 92  LYS   A CA  1 
ATOM   435  C  C   . LYS   A 1 56  ? 16.48400  -10.43600 -0.66100  1.000 78.11743  ? 92  LYS   A C   1 
ATOM   436  O  O   . LYS   A 1 56  ? 16.87200  -10.36700 0.51100   1.000 79.11501  ? 92  LYS   A O   1 
ATOM   437  C  CB  . LYS   A 1 56  ? 16.77300  -8.39500  -2.10000  1.000 83.32653  ? 92  LYS   A CB  1 
ATOM   438  C  CG  . LYS   A 1 56  ? 17.82500  -7.29700  -1.99200  1.000 87.62909  ? 92  LYS   A CG  1 
ATOM   439  C  CD  . LYS   A 1 56  ? 18.95700  -7.50100  -2.98700  1.000 80.31439  ? 92  LYS   A CD  1 
ATOM   440  C  CE  . LYS   A 1 56  ? 20.11600  -6.55400  -2.71200  1.000 83.54704  ? 92  LYS   A CE  1 
ATOM   441  N  NZ  . LYS   A 1 56  ? 20.72900  -6.79400  -1.37600  1.000 90.53118  ? 92  LYS   A NZ  1 
ATOM   442  N  N   . HIS   A 1 57  ? 15.35200  -11.06000 -0.99700  1.000 81.38638  ? 93  HIS   A N   1 
ATOM   443  C  CA  . HIS   A 1 57  ? 14.56700  -11.76100 0.01600   1.000 83.61499  ? 93  HIS   A CA  1 
ATOM   444  C  C   . HIS   A 1 57  ? 15.34100  -12.94900 0.57300   1.000 83.53952  ? 93  HIS   A C   1 
ATOM   445  O  O   . HIS   A 1 57  ? 15.43000  -13.13000 1.79300   1.000 85.90372  ? 93  HIS   A O   1 
ATOM   446  C  CB  . HIS   A 1 57  ? 13.22900  -12.21200 -0.57300  1.000 88.23805  ? 93  HIS   A CB  1 
ATOM   447  C  CG  . HIS   A 1 57  ? 12.28600  -12.79800 0.43400   1.000 93.37648  ? 93  HIS   A CG  1 
ATOM   448  N  ND1 . HIS   A 1 57  ? 12.57800  -12.87500 1.77900   1.000 97.26129  ? 93  HIS   A ND1 1 
ATOM   449  C  CD2 . HIS   A 1 57  ? 11.05100  -13.33500 0.28700   1.000 89.96305  ? 93  HIS   A CD2 1 
ATOM   450  C  CE1 . HIS   A 1 57  ? 11.56700  -13.43600 2.41700   1.000 92.12060  ? 93  HIS   A CE1 1 
ATOM   451  N  NE2 . HIS   A 1 57  ? 10.62700  -13.72400 1.53500   1.000 95.32589  ? 93  HIS   A NE2 1 
ATOM   452  N  N   . LEU   A 1 58  ? 15.91700  -13.76400 -0.30900  1.000 80.79714  ? 94  LEU   A N   1 
ATOM   453  C  CA  . LEU   A 1 58  ? 16.71600  -14.91500 0.08200   1.000 82.63353  ? 94  LEU   A CA  1 
ATOM   454  C  C   . LEU   A 1 58  ? 18.13800  -14.53800 0.48000   1.000 78.57711  ? 94  LEU   A C   1 
ATOM   455  O  O   . LEU   A 1 58  ? 19.00400  -15.41700 0.54800   1.000 72.67242  ? 94  LEU   A O   1 
ATOM   456  C  CB  . LEU   A 1 58  ? 16.74100  -15.94100 -1.05600  1.000 80.20779  ? 94  LEU   A CB  1 
ATOM   457  C  CG  . LEU   A 1 58  ? 15.38400  -16.49300 -1.50200  1.000 81.19456  ? 94  LEU   A CG  1 
ATOM   458  C  CD1 . LEU   A 1 58  ? 15.48400  -17.14200 -2.87200  1.000 73.95511  ? 94  LEU   A CD1 1 
ATOM   459  C  CD2 . LEU   A 1 58  ? 14.85000  -17.48800 -0.48400  1.000 71.48908  ? 94  LEU   A CD2 1 
ATOM   460  N  N   . GLN   A 1 59  ? 18.39400  -13.25800 0.73900   1.000 84.05518  ? 95  GLN   A N   1 
ATOM   461  C  CA  . GLN   A 1 59  ? 19.73200  -12.81500 1.10300   1.000 79.24934  ? 95  GLN   A CA  1 
ATOM   462  C  C   . GLN   A 1 59  ? 20.15100  -13.42300 2.43400   1.000 81.26432  ? 95  GLN   A C   1 
ATOM   463  O  O   . GLN   A 1 59  ? 19.34800  -13.54500 3.36300   1.000 86.98958  ? 95  GLN   A O   1 
ATOM   464  C  CB  . GLN   A 1 59  ? 19.78100  -11.29000 1.18200   1.000 85.78531  ? 95  GLN   A CB  1 
ATOM   465  C  CG  . GLN   A 1 59  ? 21.16200  -10.71600 1.42600   1.000 83.33761  ? 95  GLN   A CG  1 
ATOM   466  C  CD  . GLN   A 1 59  ? 21.64600  -9.86900  0.26800   1.000 85.42856  ? 95  GLN   A CD  1 
ATOM   467  O  OE1 . GLN   A 1 59  ? 21.55200  -10.27200 -0.89400  1.000 79.46386  ? 95  GLN   A OE1 1 
ATOM   468  N  NE2 . GLN   A 1 59  ? 22.15800  -8.68300  0.57700   1.000 81.04017  ? 95  GLN   A NE2 1 
ATOM   469  N  N   . GLY   A 1 60  ? 21.42100  -13.81300 2.51900   1.000 77.86167  ? 96  GLY   A N   1 
ATOM   470  C  CA  . GLY   A 1 60  ? 21.96000  -14.43600 3.70300   1.000 85.43344  ? 96  GLY   A CA  1 
ATOM   471  C  C   . GLY   A 1 60  ? 21.80700  -15.94000 3.75700   1.000 82.72049  ? 96  GLY   A C   1 
ATOM   472  O  O   . GLY   A 1 60  ? 22.51900  -16.59400 4.52800   1.000 85.57882  ? 96  GLY   A O   1 
ATOM   473  N  N   . CYS   A 1 61  ? 20.89900  -16.50800 2.96800   1.000 77.90883  ? 97  CYS   A N   1 
ATOM   474  C  CA  . CYS   A 1 61  ? 20.73300  -17.95400 2.94200   1.000 84.35849  ? 97  CYS   A CA  1 
ATOM   475  C  C   . CYS   A 1 61  ? 21.92900  -18.60300 2.25800   1.000 79.26628  ? 97  CYS   A C   1 
ATOM   476  O  O   . CYS   A 1 61  ? 22.37300  -18.15100 1.19800   1.000 72.05877  ? 97  CYS   A O   1 
ATOM   477  C  CB  . CYS   A 1 61  ? 19.43900  -18.33000 2.22100   1.000 77.95296  ? 97  CYS   A CB  1 
ATOM   478  S  SG  . CYS   A 1 61  ? 17.94000  -17.71300 3.01700   1.000 93.48853  ? 97  CYS   A SG  1 
ATOM   479  N  N   . ASP   A 1 62  ? 22.45600  -19.65900 2.87100   1.000 84.03116  ? 98  ASP   A N   1 
ATOM   480  C  CA  . ASP   A 1 62  ? 23.59100  -20.36600 2.29600   1.000 79.21471  ? 98  ASP   A CA  1 
ATOM   481  C  C   . ASP   A 1 62  ? 23.16800  -21.10400 1.03300   1.000 76.24012  ? 98  ASP   A C   1 
ATOM   482  O  O   . ASP   A 1 62  ? 22.13100  -21.77500 1.01000   1.000 61.03377  ? 98  ASP   A O   1 
ATOM   483  C  CB  . ASP   A 1 62  ? 24.17800  -21.34100 3.31200   1.000 88.50589  ? 98  ASP   A CB  1 
ATOM   484  C  CG  . ASP   A 1 62  ? 24.92800  -20.63700 4.42100   1.000 93.26169  ? 98  ASP   A CG  1 
ATOM   485  O  OD1 . ASP   A 1 62  ? 25.79400  -19.79100 4.11100   1.000 92.46925  ? 98  ASP   A OD1 1 
ATOM   486  O  OD2 . ASP   A 1 62  ? 24.64100  -20.91900 5.60200   1.000 100.98026 ? 98  ASP   A OD2 1 
ATOM   487  N  N   . GLY   A 1 63  ? 23.98000  -20.98000 -0.01500  1.000 73.21164  ? 99  GLY   A N   1 
ATOM   488  C  CA  . GLY   A 1 63  ? 23.67400  -21.54100 -1.31000  1.000 65.35096  ? 99  GLY   A CA  1 
ATOM   489  C  C   . GLY   A 1 63  ? 23.01800  -20.57500 -2.27200  1.000 65.31493  ? 99  GLY   A C   1 
ATOM   490  O  O   . GLY   A 1 63  ? 22.95400  -20.87000 -3.47100  1.000 62.58349  ? 99  GLY   A O   1 
ATOM   491  N  N   . ILE   A 1 64  ? 22.53000  -19.44100 -1.78700  1.000 63.62973  ? 100 ILE   A N   1 
ATOM   492  C  CA  . ILE   A 1 64  ? 21.91500  -18.41800 -2.62700  1.000 67.01239  ? 100 ILE   A CA  1 
ATOM   493  C  C   . ILE   A 1 64  ? 22.93000  -17.29300 -2.80000  1.000 67.68817  ? 100 ILE   A C   1 
ATOM   494  O  O   . ILE   A 1 64  ? 23.42900  -16.76600 -1.79200  1.000 53.47603  ? 100 ILE   A O   1 
ATOM   495  C  CB  . ILE   A 1 64  ? 20.60600  -17.89300 -2.01600  1.000 73.35925  ? 100 ILE   A CB  1 
ATOM   496  C  CG1 . ILE   A 1 64  ? 19.69100  -19.05200 -1.60400  1.000 72.40248  ? 100 ILE   A CG1 1 
ATOM   497  C  CG2 . ILE   A 1 64  ? 19.89000  -16.97500 -2.99500  1.000 64.35883  ? 100 ILE   A CG2 1 
ATOM   498  C  CD1 . ILE   A 1 64  ? 19.01700  -19.76700 -2.76300  1.000 58.42988  ? 100 ILE   A CD1 1 
ATOM   499  N  N   . PRO   A 1 65  ? 23.27100  -16.90700 -4.02600  1.000 64.18793  ? 101 PRO   A N   1 
ATOM   500  C  CA  . PRO   A 1 65  ? 24.28300  -15.86500 -4.21400  1.000 62.36321  ? 101 PRO   A CA  1 
ATOM   501  C  C   . PRO   A 1 65  ? 23.75400  -14.49800 -3.81200  1.000 64.91671  ? 101 PRO   A C   1 
ATOM   502  O  O   . PRO   A 1 65  ? 22.56300  -14.20400 -3.93400  1.000 66.14147  ? 101 PRO   A O   1 
ATOM   503  C  CB  . PRO   A 1 65  ? 24.57700  -15.93000 -5.71500  1.000 60.49481  ? 101 PRO   A CB  1 
ATOM   504  C  CG  . PRO   A 1 65  ? 23.30500  -16.44400 -6.31000  1.000 62.99011  ? 101 PRO   A CG  1 
ATOM   505  C  CD  . PRO   A 1 65  ? 22.74400  -17.41000 -5.30700  1.000 65.14603  ? 101 PRO   A CD  1 
ATOM   506  N  N   . ASN   A 1 66  ? 24.66100  -13.65700 -3.32200  1.000 63.86295  ? 102 ASN   A N   1 
ATOM   507  C  CA  . ASN   A 1 66  ? 24.29600  -12.31200 -2.90100  1.000 65.30694  ? 102 ASN   A CA  1 
ATOM   508  C  C   . ASN   A 1 66  ? 24.01900  -11.42600 -4.10900  1.000 63.90164  ? 102 ASN   A C   1 
ATOM   509  O  O   . ASN   A 1 66  ? 24.74000  -11.47300 -5.10900  1.000 59.66883  ? 102 ASN   A O   1 
ATOM   510  C  CB  . ASN   A 1 66  ? 25.40700  -11.69500 -2.04700  1.000 62.32833  ? 102 ASN   A CB  1 
ATOM   511  C  CG  . ASN   A 1 66  ? 25.43500  -12.24500 -0.63100  1.000 67.48751  ? 102 ASN   A CG  1 
ATOM   512  O  OD1 . ASN   A 1 66  ? 24.39400  -12.53600 -0.04300  1.000 75.01848  ? 102 ASN   A OD1 1 
ATOM   513  N  ND2 . ASN   A 1 66  ? 26.63300  -12.38400 -0.07600  1.000 65.43145  ? 102 ASN   A ND2 1 
ATOM   514  N  N   . ALA   A 1 67  ? 22.96800  -10.61700 -4.01000  1.000 60.36779  ? 103 ALA   A N   1 
ATOM   515  C  CA  . ALA   A 1 67  ? 22.67000  -9.60900  -5.01800  1.000 63.03526  ? 103 ALA   A CA  1 
ATOM   516  C  C   . ALA   A 1 67  ? 23.36200  -8.30400  -4.64300  1.000 70.88770  ? 103 ALA   A C   1 
ATOM   517  O  O   . ALA   A 1 67  ? 23.21300  -7.82000  -3.51600  1.000 73.55380  ? 103 ALA   A O   1 
ATOM   518  C  CB  . ALA   A 1 67  ? 21.16300  -9.38900  -5.14000  1.000 66.27382  ? 103 ALA   A CB  1 
ATOM   519  N  N   . TYR   A 1 68  ? 24.10500  -7.72900  -5.59100  1.000 62.33400  ? 104 TYR   A N   1 
ATOM   520  C  CA  . TYR   A 1 68  ? 24.88800  -6.52800  -5.32800  1.000 64.32976  ? 104 TYR   A CA  1 
ATOM   521  C  C   . TYR   A 1 68  ? 24.35700  -5.26700  -5.99500  1.000 67.77727  ? 104 TYR   A C   1 
ATOM   522  O  O   . TYR   A 1 68  ? 24.56100  -4.17500  -5.45700  1.000 70.52268  ? 104 TYR   A O   1 
ATOM   523  C  CB  . TYR   A 1 68  ? 26.34400  -6.73600  -5.76300  1.000 62.83727  ? 104 TYR   A CB  1 
ATOM   524  C  CG  . TYR   A 1 68  ? 27.02900  -7.84500  -5.00700  1.000 62.62351  ? 104 TYR   A CG  1 
ATOM   525  C  CD1 . TYR   A 1 68  ? 27.41000  -7.67400  -3.68300  1.000 64.66303  ? 104 TYR   A CD1 1 
ATOM   526  C  CD2 . TYR   A 1 68  ? 27.27900  -9.06700  -5.60900  1.000 57.98060  ? 104 TYR   A CD2 1 
ATOM   527  C  CE1 . TYR   A 1 68  ? 28.02900  -8.68800  -2.98300  1.000 69.20560  ? 104 TYR   A CE1 1 
ATOM   528  C  CE2 . TYR   A 1 68  ? 27.89700  -10.08800 -4.91800  1.000 64.09156  ? 104 TYR   A CE2 1 
ATOM   529  C  CZ  . TYR   A 1 68  ? 28.26900  -9.89300  -3.60500  1.000 64.59576  ? 104 TYR   A CZ  1 
ATOM   530  O  OH  . TYR   A 1 68  ? 28.88200  -10.90700 -2.90700  1.000 69.18227  ? 104 TYR   A OH  1 
ATOM   531  N  N   . TYR   A 1 69  ? 23.68100  -5.37500  -7.13900  1.000 63.30910  ? 105 TYR   A N   1 
ATOM   532  C  CA  . TYR   A 1 69  ? 23.29200  -4.17400  -7.86700  1.000 77.65386  ? 105 TYR   A CA  1 
ATOM   533  C  C   . TYR   A 1 69  ? 22.19400  -4.48200  -8.87600  1.000 77.31168  ? 105 TYR   A C   1 
ATOM   534  O  O   . TYR   A 1 69  ? 22.18300  -5.55100  -9.49300  1.000 76.61555  ? 105 TYR   A O   1 
ATOM   535  C  CB  . TYR   A 1 69  ? 24.49900  -3.55100  -8.57900  1.000 74.60501  ? 105 TYR   A CB  1 
ATOM   536  C  CG  . TYR   A 1 69  ? 24.15400  -2.43400  -9.54000  1.000 81.66280  ? 105 TYR   A CG  1 
ATOM   537  C  CD1 . TYR   A 1 69  ? 23.91200  -1.14500  -9.08500  1.000 76.55402  ? 105 TYR   A CD1 1 
ATOM   538  C  CD2 . TYR   A 1 69  ? 24.09400  -2.66700  -10.90800 1.000 84.44968  ? 105 TYR   A CD2 1 
ATOM   539  C  CE1 . TYR   A 1 69  ? 23.60900  -0.12300  -9.96400  1.000 87.04864  ? 105 TYR   A CE1 1 
ATOM   540  C  CE2 . TYR   A 1 69  ? 23.78900  -1.65500  -11.79400 1.000 80.62840  ? 105 TYR   A CE2 1 
ATOM   541  C  CZ  . TYR   A 1 69  ? 23.55000  -0.38500  -11.31800 1.000 84.18610  ? 105 TYR   A CZ  1 
ATOM   542  O  OH  . TYR   A 1 69  ? 23.25200  0.62700   -12.20100 1.000 92.12289  ? 105 TYR   A OH  1 
ATOM   543  N  N   . PHE   A 1 70  ? 21.27300  -3.53200  -9.02700  1.000 77.64453  ? 106 PHE   A N   1 
ATOM   544  C  CA  . PHE   A 1 70  ? 20.27600  -3.55000  -10.08900 1.000 85.34095  ? 106 PHE   A CA  1 
ATOM   545  C  C   . PHE   A 1 70  ? 20.17400  -2.14600  -10.65800 1.000 85.50227  ? 106 PHE   A C   1 
ATOM   546  O  O   . PHE   A 1 70  ? 19.95300  -1.18500  -9.91100  1.000 88.70187  ? 106 PHE   A O   1 
ATOM   547  C  CB  . PHE   A 1 70  ? 18.91300  -4.03100  -9.58400  1.000 82.54397  ? 106 PHE   A CB  1 
ATOM   548  C  CG  . PHE   A 1 70  ? 17.81200  -3.92800  -10.61500 1.000 85.10458  ? 106 PHE   A CG  1 
ATOM   549  C  CD1 . PHE   A 1 70  ? 17.86500  -4.65200  -11.79800 1.000 85.45289  ? 106 PHE   A CD1 1 
ATOM   550  C  CD2 . PHE   A 1 70  ? 16.72300  -3.10000  -10.39600 1.000 81.73328  ? 106 PHE   A CD2 1 
ATOM   551  C  CE1 . PHE   A 1 70  ? 16.85200  -4.55000  -12.73900 1.000 90.54989  ? 106 PHE   A CE1 1 
ATOM   552  C  CE2 . PHE   A 1 70  ? 15.71300  -2.99600  -11.33100 1.000 88.76026  ? 106 PHE   A CE2 1 
ATOM   553  C  CZ  . PHE   A 1 70  ? 15.77600  -3.72000  -12.50100 1.000 91.17436  ? 106 PHE   A CZ  1 
ATOM   554  N  N   . GLY   A 1 71  ? 20.34200  -2.03200  -11.97700 1.000 91.66516  ? 107 GLY   A N   1 
ATOM   555  C  CA  . GLY   A 1 71  ? 20.43800  -0.74100  -12.62300 1.000 100.68811 ? 107 GLY   A CA  1 
ATOM   556  C  C   . GLY   A 1 71  ? 19.70100  -0.69200  -13.94700 1.000 117.63095 ? 107 GLY   A C   1 
ATOM   557  O  O   . GLY   A 1 71  ? 19.05300  -1.65600  -14.36100 1.000 114.49759 ? 107 GLY   A O   1 
ATOM   558  N  N   . GLN   A 1 72  ? 19.81800  0.46500   -14.60600 1.000 139.67962 ? 108 GLN   A N   1 
ATOM   559  C  CA  . GLN   A 1 72  ? 19.07600  0.77600   -15.82100 1.000 143.67898 ? 108 GLN   A CA  1 
ATOM   560  C  C   . GLN   A 1 72  ? 19.97300  1.39400   -16.88700 1.000 144.13774 ? 108 GLN   A C   1 
ATOM   561  O  O   . GLN   A 1 72  ? 19.48900  2.14800   -17.74100 1.000 159.24786 ? 108 GLN   A O   1 
ATOM   562  C  CB  . GLN   A 1 72  ? 17.92400  1.73900   -15.52200 1.000 153.87717 ? 108 GLN   A CB  1 
ATOM   563  C  CG  . GLN   A 1 72  ? 17.04700  1.37800   -14.33600 1.000 154.94255 ? 108 GLN   A CG  1 
ATOM   564  C  CD  . GLN   A 1 72  ? 16.14100  2.52300   -13.92300 1.000 167.80029 ? 108 GLN   A CD  1 
ATOM   565  O  OE1 . GLN   A 1 72  ? 16.49000  3.69100   -14.08400 1.000 176.68324 ? 108 GLN   A OE1 1 
ATOM   566  N  NE2 . GLN   A 1 72  ? 14.96500  2.19300   -13.39400 1.000 173.83284 ? 108 GLN   A NE2 1 
ATOM   567  N  N   . GLU   A 1 73  ? 21.26800  1.09200   -16.85400 1.000 132.99898 ? 109 GLU   A N   1 
ATOM   568  C  CA  . GLU   A 1 73  ? 22.22600  1.75300   -17.72900 1.000 130.99216 ? 109 GLU   A CA  1 
ATOM   569  C  C   . GLU   A 1 73  ? 21.90400  1.47800   -19.19100 1.000 132.94503 ? 109 GLU   A C   1 
ATOM   570  O  O   . GLU   A 1 73  ? 21.89200  0.32300   -19.62800 1.000 132.50297 ? 109 GLU   A O   1 
ATOM   571  C  CB  . GLU   A 1 73  ? 23.64100  1.28200   -17.40000 1.000 124.06973 ? 109 GLU   A CB  1 
ATOM   572  C  CG  . GLU   A 1 73  ? 24.07900  1.60800   -15.98800 1.000 117.36548 ? 109 GLU   A CG  1 
ATOM   573  C  CD  . GLU   A 1 73  ? 25.56500  1.42100   -15.78300 1.000 104.44551 ? 109 GLU   A CD  1 
ATOM   574  O  OE1 . GLU   A 1 73  ? 26.26000  1.06700   -16.75800 1.000 102.81069 ? 109 GLU   A OE1 1 
ATOM   575  O  OE2 . GLU   A 1 73  ? 26.03800  1.63500   -14.64700 1.000 108.70589 ? 109 GLU   A OE2 1 
ATOM   576  N  N   . GLY   A 1 74  ? 21.64200  2.54800   -19.94300 1.000 134.75886 ? 110 GLY   A N   1 
ATOM   577  C  CA  . GLY   A 1 74  ? 21.33600  2.42000   -21.35300 1.000 135.77951 ? 110 GLY   A CA  1 
ATOM   578  C  C   . GLY   A 1 74  ? 19.99800  1.73800   -21.58600 1.000 132.24559 ? 110 GLY   A C   1 
ATOM   579  O  O   . GLY   A 1 74  ? 19.05700  1.85400   -20.79500 1.000 129.27489 ? 110 GLY   A O   1 
ATOM   580  N  N   . LEU   A 1 75  ? 19.91600  1.01000   -22.70000 1.000 131.50238 ? 111 LEU   A N   1 
ATOM   581  C  CA  . LEU   A 1 75  ? 18.73200  0.23300   -23.03600 1.000 132.72722 ? 111 LEU   A CA  1 
ATOM   582  C  C   . LEU   A 1 75  ? 18.76300  -1.16800  -22.42800 1.000 131.81212 ? 111 LEU   A C   1 
ATOM   583  O  O   . LEU   A 1 75  ? 18.06100  -2.06300  -22.91400 1.000 131.75192 ? 111 LEU   A O   1 
ATOM   584  C  CB  . LEU   A 1 75  ? 18.55600  0.15800   -24.55800 1.000 137.39149 ? 111 LEU   A CB  1 
ATOM   585  C  CG  . LEU   A 1 75  ? 19.40100  -0.78300  -25.42600 1.000 139.41928 ? 111 LEU   A CG  1 
ATOM   586  C  CD1 . LEU   A 1 75  ? 18.94000  -0.70000  -26.87600 1.000 134.01885 ? 111 LEU   A CD1 1 
ATOM   587  C  CD2 . LEU   A 1 75  ? 20.89300  -0.49400  -25.32200 1.000 135.91097 ? 111 LEU   A CD2 1 
ATOM   588  N  N   . HIS   A 1 76  ? 19.53800  -1.36800  -21.36300 1.000 129.82838 ? 112 HIS   A N   1 
ATOM   589  C  CA  . HIS   A 1 76  ? 19.67500  -2.66700  -20.72100 1.000 127.47395 ? 112 HIS   A CA  1 
ATOM   590  C  C   . HIS   A 1 76  ? 19.44200  -2.55100  -19.22200 1.000 122.30618 ? 112 HIS   A C   1 
ATOM   591  O  O   . HIS   A 1 76  ? 19.83400  -1.56200  -18.59600 1.000 120.86912 ? 112 HIS   A O   1 
ATOM   592  C  CB  . HIS   A 1 76  ? 21.06400  -3.27100  -20.97800 1.000 122.33779 ? 112 HIS   A CB  1 
ATOM   593  C  CG  . HIS   A 1 76  ? 21.17500  -4.00300  -22.27900 1.000 125.42127 ? 112 HIS   A CG  1 
ATOM   594  N  ND1 . HIS   A 1 76  ? 20.38000  -5.08400  -22.59200 1.000 129.49283 ? 112 HIS   A ND1 1 
ATOM   595  C  CD2 . HIS   A 1 76  ? 21.99400  -3.81900  -23.34200 1.000 126.29434 ? 112 HIS   A CD2 1 
ATOM   596  C  CE1 . HIS   A 1 76  ? 20.69800  -5.53000  -23.79400 1.000 131.18736 ? 112 HIS   A CE1 1 
ATOM   597  N  NE2 . HIS   A 1 76  ? 21.67500  -4.78000  -24.27000 1.000 131.71884 ? 112 HIS   A NE2 1 
ATOM   598  N  N   . ASN   A 1 77  ? 18.79800  -3.56800  -18.65400 1.000 120.47092 ? 113 ASN   A N   1 
ATOM   599  C  CA  . ASN   A 1 77  ? 18.72100  -3.74500  -17.21100 1.000 114.12801 ? 113 ASN   A CA  1 
ATOM   600  C  C   . ASN   A 1 77  ? 19.81600  -4.70200  -16.76400 1.000 107.79004 ? 113 ASN   A C   1 
ATOM   601  O  O   . ASN   A 1 77  ? 20.07000  -5.72100  -17.41400 1.000 108.64786 ? 113 ASN   A O   1 
ATOM   602  C  CB  . ASN   A 1 77  ? 17.35900  -4.28400  -16.78400 1.000 113.58157 ? 113 ASN   A CB  1 
ATOM   603  C  CG  . ASN   A 1 77  ? 16.27300  -3.23700  -16.84000 1.000 114.56137 ? 113 ASN   A CG  1 
ATOM   604  O  OD1 . ASN   A 1 77  ? 15.07900  -3.54500  -16.85000 1.000 110.75473 ? 113 ASN   A OD1 1 
ATOM   605  N  ND2 . ASN   A 1 77  ? 16.68800  -1.98400  -16.89600 1.000 119.68303 ? 113 ASN   A ND2 1 
ATOM   606  N  N   . ILE   A 1 78  ? 20.45900  -4.37000  -15.64800 1.000 104.32720 ? 114 ILE   A N   1 
ATOM   607  C  CA  . ILE   A 1 78  ? 21.67100  -5.04500  -15.20500 1.000 95.86179  ? 114 ILE   A CA  1 
ATOM   608  C  C   . ILE   A 1 78  ? 21.45100  -5.60900  -13.80800 1.000 89.59508  ? 114 ILE   A C   1 
ATOM   609  O  O   . ILE   A 1 78  ? 20.88800  -4.93600  -12.93700 1.000 85.07001  ? 114 ILE   A O   1 
ATOM   610  C  CB  . ILE   A 1 78  ? 22.87800  -4.08300  -15.23100 1.000 91.42181  ? 114 ILE   A CB  1 
ATOM   611  C  CG1 . ILE   A 1 78  ? 23.15700  -3.62700  -16.66500 1.000 96.02924  ? 114 ILE   A CG1 1 
ATOM   612  C  CG2 . ILE   A 1 78  ? 24.11100  -4.74100  -14.63500 1.000 83.35051  ? 114 ILE   A CG2 1 
ATOM   613  C  CD1 . ILE   A 1 78  ? 24.12900  -2.47900  -16.76200 1.000 94.89055  ? 114 ILE   A CD1 1 
ATOM   614  N  N   . LEU   A 1 79  ? 21.88700  -6.85300  -13.60500 1.000 81.49719  ? 115 LEU   A N   1 
ATOM   615  C  CA  . LEU   A 1 79  ? 21.90200  -7.49800  -12.29800 1.000 78.94385  ? 115 LEU   A CA  1 
ATOM   616  C  C   . LEU   A 1 79  ? 23.29300  -8.05400  -12.04400 1.000 74.39645  ? 115 LEU   A C   1 
ATOM   617  O  O   . LEU   A 1 79  ? 23.84200  -8.76700  -12.89100 1.000 72.47524  ? 115 LEU   A O   1 
ATOM   618  C  CB  . LEU   A 1 79  ? 20.87000  -8.62400  -12.21100 1.000 76.49999  ? 115 LEU   A CB  1 
ATOM   619  C  CG  . LEU   A 1 79  ? 20.76200  -9.33700  -10.86300 1.000 75.62702  ? 115 LEU   A CG  1 
ATOM   620  C  CD1 . LEU   A 1 79  ? 20.58000  -8.33000  -9.74800  1.000 67.52214  ? 115 LEU   A CD1 1 
ATOM   621  C  CD2 . LEU   A 1 79  ? 19.61900  -10.34200 -10.87100 1.000 77.66537  ? 115 LEU   A CD2 1 
ATOM   622  N  N   . VAL   A 1 80  ? 23.85500  -7.73400  -10.88100 1.000 70.29571  ? 116 VAL   A N   1 
ATOM   623  C  CA  . VAL   A 1 80  ? 25.19000  -8.17400  -10.49100 1.000 64.70472  ? 116 VAL   A CA  1 
ATOM   624  C  C   . VAL   A 1 80  ? 25.06200  -9.01800  -9.23100  1.000 64.51271  ? 116 VAL   A C   1 
ATOM   625  O  O   . VAL   A 1 80  ? 24.57300  -8.53400  -8.20200  1.000 64.95335  ? 116 VAL   A O   1 
ATOM   626  C  CB  . VAL   A 1 80  ? 26.13600  -6.98600  -10.25400 1.000 65.27234  ? 116 VAL   A CB  1 
ATOM   627  C  CG1 . VAL   A 1 80  ? 27.48300  -7.47600  -9.74700  1.000 49.55485  ? 116 VAL   A CG1 1 
ATOM   628  C  CG2 . VAL   A 1 80  ? 26.29900  -6.17000  -11.52800 1.000 68.65040  ? 116 VAL   A CG2 1 
ATOM   629  N  N   . ILE   A 1 81  ? 25.49600  -10.27700 -9.31200  1.000 56.22279  ? 117 ILE   A N   1 
ATOM   630  C  CA  . ILE   A 1 81  ? 25.54300  -11.19200 -8.17800  1.000 60.64496  ? 117 ILE   A CA  1 
ATOM   631  C  C   . ILE   A 1 81  ? 26.86600  -11.94700 -8.22600  1.000 51.69482  ? 117 ILE   A C   1 
ATOM   632  O  O   . ILE   A 1 81  ? 27.68800  -11.74600 -9.12400  1.000 49.27440  ? 117 ILE   A O   1 
ATOM   633  C  CB  . ILE   A 1 81  ? 24.36200  -12.18600 -8.16400  1.000 62.26598  ? 117 ILE   A CB  1 
ATOM   634  C  CG1 . ILE   A 1 81  ? 24.39400  -13.05600 -9.41900  1.000 62.66115  ? 117 ILE   A CG1 1 
ATOM   635  C  CG2 . ILE   A 1 81  ? 23.03100  -11.45800 -8.03300  1.000 64.27201  ? 117 ILE   A CG2 1 
ATOM   636  C  CD1 . ILE   A 1 81  ? 23.62100  -14.34300 -9.29200  1.000 75.20758  ? 117 ILE   A CD1 1 
ATOM   637  N  N   . ASP   A 1 82  ? 27.06000  -12.83500 -7.25400  1.000 59.13142  ? 118 ASP   A N   1 
ATOM   638  C  CA  . ASP   A 1 82  ? 28.28500  -13.61800 -7.18500  1.000 53.34272  ? 118 ASP   A CA  1 
ATOM   639  C  C   . ASP   A 1 82  ? 28.45300  -14.47500 -8.43300  1.000 53.29566  ? 118 ASP   A C   1 
ATOM   640  O  O   . ASP   A 1 82  ? 27.48200  -14.94400 -9.03200  1.000 55.48379  ? 118 ASP   A O   1 
ATOM   641  C  CB  . ASP   A 1 82  ? 28.28000  -14.50500 -5.94100  1.000 57.66538  ? 118 ASP   A CB  1 
ATOM   642  C  CG  . ASP   A 1 82  ? 28.34900  -13.70600 -4.65400  1.000 64.46990  ? 118 ASP   A CG  1 
ATOM   643  O  OD1 . ASP   A 1 82  ? 29.22200  -12.82000 -4.54400  1.000 56.42033  ? 118 ASP   A OD1 1 
ATOM   644  O  OD2 . ASP   A 1 82  ? 27.52200  -13.96200 -3.75100  1.000 66.11452  ? 118 ASP   A OD2 1 
ATOM   645  N  N   . LEU   A 1 83  ? 29.70800  -14.66300 -8.83000  1.000 66.04184  ? 119 LEU   A N   1 
ATOM   646  C  CA  . LEU   A 1 83  ? 30.06000  -15.56900 -9.91500  1.000 57.78831  ? 119 LEU   A CA  1 
ATOM   647  C  C   . LEU   A 1 83  ? 30.33600  -16.94500 -9.32300  1.000 61.67106  ? 119 LEU   A C   1 
ATOM   648  O  O   . LEU   A 1 83  ? 31.17800  -17.08400 -8.42900  1.000 69.42833  ? 119 LEU   A O   1 
ATOM   649  C  CB  . LEU   A 1 83  ? 31.27800  -15.04800 -10.67900 1.000 66.58347  ? 119 LEU   A CB  1 
ATOM   650  C  CG  . LEU   A 1 83  ? 31.68300  -15.81400 -11.93900 1.000 68.86435  ? 119 LEU   A CG  1 
ATOM   651  C  CD1 . LEU   A 1 83  ? 30.55300  -15.79500 -12.95400 1.000 74.23578  ? 119 LEU   A CD1 1 
ATOM   652  C  CD2 . LEU   A 1 83  ? 32.95000  -15.22900 -12.53900 1.000 77.58653  ? 119 LEU   A CD2 1 
ATOM   653  N  N   . LEU   A 1 84  ? 29.62900  -17.95400 -9.81400  1.000 52.40944  ? 120 LEU   A N   1 
ATOM   654  C  CA  . LEU   A 1 84  ? 29.73500  -19.31600 -9.31700  1.000 63.38139  ? 120 LEU   A CA  1 
ATOM   655  C  C   . LEU   A 1 84  ? 30.37000  -20.21200 -10.37600 1.000 64.44415  ? 120 LEU   A C   1 
ATOM   656  O  O   . LEU   A 1 84  ? 30.69900  -19.77400 -11.48300 1.000 62.10288  ? 120 LEU   A O   1 
ATOM   657  C  CB  . LEU   A 1 84  ? 28.35700  -19.83100 -8.89900  1.000 59.15558  ? 120 LEU   A CB  1 
ATOM   658  C  CG  . LEU   A 1 84  ? 27.70800  -19.02300 -7.77500  1.000 56.94159  ? 120 LEU   A CG  1 
ATOM   659  C  CD1 . LEU   A 1 84  ? 26.26400  -19.45100 -7.54400  1.000 48.07223  ? 120 LEU   A CD1 1 
ATOM   660  C  CD2 . LEU   A 1 84  ? 28.52200  -19.17400 -6.50100  1.000 57.85437  ? 120 LEU   A CD2 1 
ATOM   661  N  N   . GLY   A 1 85  ? 30.54600  -21.48400 -10.02000 1.000 58.30171  ? 121 GLY   A N   1 
ATOM   662  C  CA  . GLY   A 1 85  ? 31.16800  -22.44800 -10.89500 1.000 52.78787  ? 121 GLY   A CA  1 
ATOM   663  C  C   . GLY   A 1 85  ? 30.18400  -23.13600 -11.82200 1.000 54.27409  ? 121 GLY   A C   1 
ATOM   664  O  O   . GLY   A 1 85  ? 29.08200  -22.64000 -12.07700 1.000 57.73092  ? 121 GLY   A O   1 
ATOM   665  N  N   . PRO   A 1 86  ? 30.57000  -24.29900 -12.34200 1.000 47.32453  ? 122 PRO   A N   1 
ATOM   666  C  CA  . PRO   A 1 86  ? 29.71900  -24.99800 -13.31300 1.000 57.81657  ? 122 PRO   A CA  1 
ATOM   667  C  C   . PRO   A 1 86  ? 28.45400  -25.54700 -12.67400 1.000 44.90359  ? 122 PRO   A C   1 
ATOM   668  O  O   . PRO   A 1 86  ? 28.36100  -25.73600 -11.45900 1.000 44.10512  ? 122 PRO   A O   1 
ATOM   669  C  CB  . PRO   A 1 86  ? 30.61200  -26.13900 -13.82000 1.000 54.27564  ? 122 PRO   A CB  1 
ATOM   670  C  CG  . PRO   A 1 86  ? 32.00300  -25.74700 -13.44100 1.000 65.86016  ? 122 PRO   A CG  1 
ATOM   671  C  CD  . PRO   A 1 86  ? 31.86900  -24.96500 -12.17200 1.000 63.39006  ? 122 PRO   A CD  1 
ATOM   672  N  N   . SER   A 1 87  ? 27.47000  -25.81600 -13.52600 1.000 47.49684  ? 123 SER   A N   1 
ATOM   673  C  CA  . SER   A 1 87  ? 26.22000  -26.39900 -13.07000 1.000 48.18206  ? 123 SER   A CA  1 
ATOM   674  C  C   . SER   A 1 87  ? 26.39400  -27.89500 -12.82600 1.000 50.63476  ? 123 SER   A C   1 
ATOM   675  O  O   . SER   A 1 87  ? 27.36600  -28.51700 -13.26700 1.000 46.83258  ? 123 SER   A O   1 
ATOM   676  C  CB  . SER   A 1 87  ? 25.11600  -26.16900 -14.09600 1.000 49.69833  ? 123 SER   A CB  1 
ATOM   677  O  OG  . SER   A 1 87  ? 25.33600  -26.97500 -15.24200 1.000 52.16288  ? 123 SER   A OG  1 
ATOM   678  N  N   . LEU   A 1 88  ? 25.42600  -28.48100 -12.11600 1.000 46.16140  ? 124 LEU   A N   1 
ATOM   679  C  CA  . LEU   A 1 88  ? 25.43500  -29.92900 -11.94500 1.000 47.81999  ? 124 LEU   A CA  1 
ATOM   680  C  C   . LEU   A 1 88  ? 25.32700  -30.64000 -13.28600 1.000 48.51810  ? 124 LEU   A C   1 
ATOM   681  O  O   . LEU   A 1 88  ? 25.90700  -31.71700 -13.46200 1.000 44.47320  ? 124 LEU   A O   1 
ATOM   682  C  CB  . LEU   A 1 88  ? 24.30500  -30.36500 -11.01100 1.000 44.74618  ? 124 LEU   A CB  1 
ATOM   683  C  CG  . LEU   A 1 88  ? 24.48700  -30.02500 -9.53000  1.000 42.11757  ? 124 LEU   A CG  1 
ATOM   684  C  CD1 . LEU   A 1 88  ? 23.35900  -30.62900 -8.70400  1.000 40.06789  ? 124 LEU   A CD1 1 
ATOM   685  C  CD2 . LEU   A 1 88  ? 25.83700  -30.51000 -9.03100  1.000 45.99527  ? 124 LEU   A CD2 1 
ATOM   686  N  N   . GLU   A 1 89  ? 24.60700  -30.05300 -14.24900 1.000 45.67910  ? 125 GLU   A N   1 
ATOM   687  C  CA  . GLU   A 1 89  ? 24.57800  -30.63200 -15.58900 1.000 46.66989  ? 125 GLU   A CA  1 
ATOM   688  C  C   . GLU   A 1 89  ? 25.96300  -30.61300 -16.22700 1.000 48.69198  ? 125 GLU   A C   1 
ATOM   689  O  O   . GLU   A 1 89  ? 26.34800  -31.57300 -16.90300 1.000 51.26116  ? 125 GLU   A O   1 
ATOM   690  C  CB  . GLU   A 1 89  ? 23.56600  -29.89700 -16.46900 1.000 39.60224  ? 125 GLU   A CB  1 
ATOM   691  C  CG  . GLU   A 1 89  ? 23.52200  -30.37600 -17.92300 1.000 47.60340  ? 125 GLU   A CG  1 
ATOM   692  C  CD  . GLU   A 1 89  ? 23.00900  -31.80500 -18.08200 1.000 53.59308  ? 125 GLU   A CD  1 
ATOM   693  O  OE1 . GLU   A 1 89  ? 22.31900  -32.30900 -17.17000 1.000 53.13724  ? 125 GLU   A OE1 1 
ATOM   694  O  OE2 . GLU   A 1 89  ? 23.29400  -32.42400 -19.13000 1.000 55.32676  ? 125 GLU   A OE2 1 
ATOM   695  N  N   . ASP   A 1 90  ? 26.73100  -29.53900 -16.01400 1.000 50.08859  ? 126 ASP   A N   1 
ATOM   696  C  CA  . ASP   A 1 90  ? 28.08700  -29.47300 -16.55800 1.000 48.41925  ? 126 ASP   A CA  1 
ATOM   697  C  C   . ASP   A 1 90  ? 28.97700  -30.54500 -15.95100 1.000 49.36190  ? 126 ASP   A C   1 
ATOM   698  O  O   . ASP   A 1 90  ? 29.70900  -31.24100 -16.66400 1.000 53.20042  ? 126 ASP   A O   1 
ATOM   699  C  CB  . ASP   A 1 90  ? 28.70100  -28.09800 -16.30400 1.000 51.71773  ? 126 ASP   A CB  1 
ATOM   700  C  CG  . ASP   A 1 90  ? 28.01900  -27.00300 -17.07600 1.000 57.10100  ? 126 ASP   A CG  1 
ATOM   701  O  OD1 . ASP   A 1 90  ? 27.55700  -27.26400 -18.20600 1.000 63.33115  ? 126 ASP   A OD1 1 
ATOM   702  O  OD2 . ASP   A 1 90  ? 27.95300  -25.87300 -16.54900 1.000 56.88137  ? 126 ASP   A OD2 1 
ATOM   703  N  N   . LEU   A 1 91  ? 28.96000  -30.65900 -14.62200 1.000 40.40146  ? 127 LEU   A N   1 
ATOM   704  C  CA  . LEU   A 1 91  ? 29.75100  -31.68900 -13.96200 1.000 50.58133  ? 127 LEU   A CA  1 
ATOM   705  C  C   . LEU   A 1 91  ? 29.26100  -33.08100 -14.33400 1.000 52.96663  ? 127 LEU   A C   1 
ATOM   706  O  O   . LEU   A 1 91  ? 30.05300  -34.03400 -14.36300 1.000 44.48669  ? 127 LEU   A O   1 
ATOM   707  C  CB  . LEU   A 1 91  ? 29.70000  -31.48800 -12.44900 1.000 50.99749  ? 127 LEU   A CB  1 
ATOM   708  C  CG  . LEU   A 1 91  ? 30.17200  -30.10900 -11.98700 1.000 50.65879  ? 127 LEU   A CG  1 
ATOM   709  C  CD1 . LEU   A 1 91  ? 29.80000  -29.89300 -10.53600 1.000 54.39303  ? 127 LEU   A CD1 1 
ATOM   710  C  CD2 . LEU   A 1 91  ? 31.67600  -29.99100 -12.18000 1.000 49.50665  ? 127 LEU   A CD2 1 
ATOM   711  N  N   . PHE   A 1 92  ? 27.96500  -33.20900 -14.62400 1.000 43.68905  ? 128 PHE   A N   1 
ATOM   712  C  CA  . PHE   A 1 92  ? 27.40000  -34.48500 -15.04800 1.000 47.53830  ? 128 PHE   A CA  1 
ATOM   713  C  C   . PHE   A 1 92  ? 28.01100  -34.95100 -16.36400 1.000 47.87798  ? 128 PHE   A C   1 
ATOM   714  O  O   . PHE   A 1 92  ? 28.43500  -36.10500 -16.48400 1.000 51.28692  ? 128 PHE   A O   1 
ATOM   715  C  CB  . PHE   A 1 92  ? 25.88200  -34.35300 -15.16500 1.000 42.62062  ? 128 PHE   A CB  1 
ATOM   716  C  CG  . PHE   A 1 92  ? 25.16300  -35.65700 -15.33800 1.000 42.43216  ? 128 PHE   A CG  1 
ATOM   717  C  CD1 . PHE   A 1 92  ? 25.20900  -36.62200 -14.34700 1.000 46.60829  ? 128 PHE   A CD1 1 
ATOM   718  C  CD2 . PHE   A 1 92  ? 24.41800  -35.90900 -16.47700 1.000 44.70363  ? 128 PHE   A CD2 1 
ATOM   719  C  CE1 . PHE   A 1 92  ? 24.54400  -37.82200 -14.49600 1.000 41.83872  ? 128 PHE   A CE1 1 
ATOM   720  C  CE2 . PHE   A 1 92  ? 23.74300  -37.11200 -16.63200 1.000 48.08604  ? 128 PHE   A CE2 1 
ATOM   721  C  CZ  . PHE   A 1 92  ? 23.80400  -38.06600 -15.63700 1.000 36.67620  ? 128 PHE   A CZ  1 
ATOM   722  N  N   . ASP   A 1 93  ? 28.06900  -34.06300 -17.36500 1.000 44.96955  ? 129 ASP   A N   1 
ATOM   723  C  CA  . ASP   A 1 93  ? 28.65800  -34.43300 -18.65100 1.000 52.94272  ? 129 ASP   A CA  1 
ATOM   724  C  C   . ASP   A 1 93  ? 30.13200  -34.79400 -18.50700 1.000 56.63472  ? 129 ASP   A C   1 
ATOM   725  O  O   . ASP   A 1 93  ? 30.63000  -35.69100 -19.20000 1.000 61.46310  ? 129 ASP   A O   1 
ATOM   726  C  CB  . ASP   A 1 93  ? 28.50400  -33.29200 -19.65700 1.000 59.95582  ? 129 ASP   A CB  1 
ATOM   727  C  CG  . ASP   A 1 93  ? 27.15100  -33.28100 -20.33400 1.000 65.50008  ? 129 ASP   A CG  1 
ATOM   728  O  OD1 . ASP   A 1 93  ? 26.49700  -34.34400 -20.39600 1.000 70.94813  ? 129 ASP   A OD1 1 
ATOM   729  O  OD2 . ASP   A 1 93  ? 26.74600  -32.20400 -20.81800 1.000 73.88399  ? 129 ASP   A OD2 1 
ATOM   730  N  N   . TRP   A 1 94  ? 30.85100  -34.09400 -17.62400 1.000 56.55340  ? 130 TRP   A N   1 
ATOM   731  C  CA  . TRP   A 1 94  ? 32.29200  -34.30600 -17.51300 1.000 57.03580  ? 130 TRP   A CA  1 
ATOM   732  C  C   . TRP   A 1 94  ? 32.61700  -35.61500 -16.80700 1.000 49.58234  ? 130 TRP   A C   1 
ATOM   733  O  O   . TRP   A 1 94  ? 33.68700  -36.19100 -17.03200 1.000 51.48485  ? 130 TRP   A O   1 
ATOM   734  C  CB  . TRP   A 1 94  ? 32.93700  -33.12700 -16.78500 1.000 50.90452  ? 130 TRP   A CB  1 
ATOM   735  C  CG  . TRP   A 1 94  ? 32.73300  -31.82500 -17.49300 1.000 63.48510  ? 130 TRP   A CG  1 
ATOM   736  C  CD1 . TRP   A 1 94  ? 32.49300  -31.65000 -18.82400 1.000 70.80734  ? 130 TRP   A CD1 1 
ATOM   737  C  CD2 . TRP   A 1 94  ? 32.73200  -30.51600 -16.90900 1.000 67.19940  ? 130 TRP   A CD2 1 
ATOM   738  N  NE1 . TRP   A 1 94  ? 32.35200  -30.31400 -19.10900 1.000 79.80728  ? 130 TRP   A NE1 1 
ATOM   739  C  CE2 . TRP   A 1 94  ? 32.49200  -29.59600 -17.95000 1.000 77.97255  ? 130 TRP   A CE2 1 
ATOM   740  C  CE3 . TRP   A 1 94  ? 32.91200  -30.03200 -15.61000 1.000 68.27214  ? 130 TRP   A CE3 1 
ATOM   741  C  CZ2 . TRP   A 1 94  ? 32.43000  -28.22100 -17.73300 1.000 72.31245  ? 130 TRP   A CZ2 1 
ATOM   742  C  CZ3 . TRP   A 1 94  ? 32.85000  -28.66400 -15.39800 1.000 68.51428  ? 130 TRP   A CZ3 1 
ATOM   743  C  CH2 . TRP   A 1 94  ? 32.61200  -27.77600 -16.45400 1.000 64.48780  ? 130 TRP   A CH2 1 
ATOM   744  N  N   . CYS   A 1 95  ? 31.71300  -36.09700 -15.95700 1.000 50.72166  ? 131 CYS   A N   1 
ATOM   745  C  CA  . CYS   A 1 95  ? 31.87100  -37.36400 -15.26300 1.000 52.93352  ? 131 CYS   A CA  1 
ATOM   746  C  C   . CYS   A 1 95  ? 31.28300  -38.53400 -16.04100 1.000 56.12299  ? 131 CYS   A C   1 
ATOM   747  O  O   . CYS   A 1 95  ? 31.08700  -39.61100 -15.46900 1.000 48.36515  ? 131 CYS   A O   1 
ATOM   748  C  CB  . CYS   A 1 95  ? 31.23700  -37.28000 -13.87400 1.000 51.42340  ? 131 CYS   A CB  1 
ATOM   749  S  SG  . CYS   A 1 95  ? 32.07200  -36.12300 -12.76900 1.000 46.10419  ? 131 CYS   A SG  1 
ATOM   750  N  N   . GLY   A 1 96  ? 30.99700  -38.34800 -17.32800 1.000 51.98681  ? 132 GLY   A N   1 
ATOM   751  C  CA  . GLY   A 1 96  ? 30.48000  -39.43100 -18.14100 1.000 53.94221  ? 132 GLY   A CA  1 
ATOM   752  C  C   . GLY   A 1 96  ? 28.98000  -39.60600 -18.09900 1.000 53.79680  ? 132 GLY   A C   1 
ATOM   753  O  O   . GLY   A 1 96  ? 28.48800  -40.70200 -18.38900 1.000 55.54390  ? 132 GLY   A O   1 
ATOM   754  N  N   . ARG   A 1 97  ? 28.23600  -38.55300 -17.76300 1.000 44.56920  ? 133 ARG   A N   1 
ATOM   755  C  CA  . ARG   A 1 97  ? 26.77400  -38.60000 -17.65400 1.000 47.48309  ? 133 ARG   A CA  1 
ATOM   756  C  C   . ARG   A 1 97  ? 26.32600  -39.70600 -16.70000 1.000 54.64876  ? 133 ARG   A C   1 
ATOM   757  O  O   . ARG   A 1 97  ? 25.39700  -40.47400 -16.97400 1.000 50.11166  ? 133 ARG   A O   1 
ATOM   758  C  CB  . ARG   A 1 97  ? 26.11700  -38.74300 -19.03100 1.000 49.49328  ? 133 ARG   A CB  1 
ATOM   759  C  CG  . ARG   A 1 97  ? 26.32000  -37.51700 -19.91700 1.000 52.49862  ? 133 ARG   A CG  1 
ATOM   760  C  CD  . ARG   A 1 97  ? 25.39600  -37.49700 -21.12700 1.000 60.33745  ? 133 ARG   A CD  1 
ATOM   761  N  NE  . ARG   A 1 97  ? 23.99600  -37.29500 -20.76700 1.000 61.84518  ? 133 ARG   A NE  1 
ATOM   762  C  CZ  . ARG   A 1 97  ? 23.47300  -36.13200 -20.40200 1.000 62.43013  ? 133 ARG   A CZ  1 
ATOM   763  N  NH1 . ARG   A 1 97  ? 24.21600  -35.04100 -20.29200 1.000 56.47707  ? 133 ARG   A NH1 1 
ATOM   764  N  NH2 . ARG   A 1 97  ? 22.17100  -36.06100 -20.13400 1.000 58.81781  ? 133 ARG   A NH2 1 
ATOM   765  N  N   . ARG   A 1 98  ? 27.00300  -39.77700 -15.55400 1.000 51.37870  ? 134 ARG   A N   1 
ATOM   766  C  CA  . ARG   A 1 98  ? 26.59400  -40.64900 -14.46200 1.000 48.63234  ? 134 ARG   A CA  1 
ATOM   767  C  C   . ARG   A 1 98  ? 27.28400  -40.21500 -13.17400 1.000 52.06813  ? 134 ARG   A C   1 
ATOM   768  O  O   . ARG   A 1 98  ? 28.50400  -40.01600 -13.15600 1.000 54.31878  ? 134 ARG   A O   1 
ATOM   769  C  CB  . ARG   A 1 98  ? 26.92000  -42.11200 -14.77600 1.000 55.74014  ? 134 ARG   A CB  1 
ATOM   770  C  CG  . ARG   A 1 98  ? 25.99900  -43.11000 -14.09700 1.000 54.67846  ? 134 ARG   A CG  1 
ATOM   771  C  CD  . ARG   A 1 98  ? 26.55400  -44.51800 -14.21100 1.000 70.00171  ? 134 ARG   A CD  1 
ATOM   772  N  NE  . ARG   A 1 98  ? 25.49700  -45.52100 -14.23300 1.000 69.94452  ? 134 ARG   A NE  1 
ATOM   773  C  CZ  . ARG   A 1 98  ? 24.99500  -46.05000 -15.34100 1.000 77.61411  ? 134 ARG   A CZ  1 
ATOM   774  N  NH1 . ARG   A 1 98  ? 25.43800  -45.69900 -16.53700 1.000 82.33718  ? 134 ARG   A NH1 1 
ATOM   775  N  NH2 . ARG   A 1 98  ? 24.02700  -46.95700 -15.24600 1.000 67.93572  ? 134 ARG   A NH2 1 
ATOM   776  N  N   . PHE   A 1 99  ? 26.51900  -40.04400 -12.10000 1.000 45.39710  ? 135 PHE   A N   1 
ATOM   777  C  CA  . PHE   A 1 99  ? 27.07800  -39.77200 -10.78300 1.000 47.85796  ? 135 PHE   A CA  1 
ATOM   778  C  C   . PHE   A 1 99  ? 26.99500  -41.03100 -9.93000  1.000 49.53982  ? 135 PHE   A C   1 
ATOM   779  O  O   . PHE   A 1 99  ? 26.04300  -41.80900 -10.04300 1.000 41.23531  ? 135 PHE   A O   1 
ATOM   780  C  CB  . PHE   A 1 99  ? 26.34400  -38.62300 -10.08500 1.000 45.88860  ? 135 PHE   A CB  1 
ATOM   781  C  CG  . PHE   A 1 99  ? 26.75900  -37.25100 -10.54800 1.000 47.00188  ? 135 PHE   A CG  1 
ATOM   782  C  CD1 . PHE   A 1 99  ? 28.02900  -37.01700 -11.05900 1.000 44.21347  ? 135 PHE   A CD1 1 
ATOM   783  C  CD2 . PHE   A 1 99  ? 25.87600  -36.18500 -10.45300 1.000 41.55221  ? 135 PHE   A CD2 1 
ATOM   784  C  CE1 . PHE   A 1 99  ? 28.40300  -35.74800 -11.47900 1.000 47.04488  ? 135 PHE   A CE1 1 
ATOM   785  C  CE2 . PHE   A 1 99  ? 26.24500  -34.91600 -10.87200 1.000 41.87420  ? 135 PHE   A CE2 1 
ATOM   786  C  CZ  . PHE   A 1 99  ? 27.50900  -34.69600 -11.38100 1.000 45.34690  ? 135 PHE   A CZ  1 
ATOM   787  N  N   . SER   A 1 100 ? 28.00500  -41.23600 -9.08800  1.000 45.46294  ? 136 SER   A N   1 
ATOM   788  C  CA  . SER   A 1 100 ? 27.98100  -42.35400 -8.16100  1.000 44.46939  ? 136 SER   A CA  1 
ATOM   789  C  C   . SER   A 1 100 ? 26.85500  -42.17300 -7.15000  1.000 43.95034  ? 136 SER   A C   1 
ATOM   790  O  O   . SER   A 1 100 ? 26.30300  -41.08400 -6.97900  1.000 43.81963  ? 136 SER   A O   1 
ATOM   791  C  CB  . SER   A 1 100 ? 29.32000  -42.49000 -7.43400  1.000 52.65262  ? 136 SER   A CB  1 
ATOM   792  O  OG  . SER   A 1 100 ? 29.59800  -41.34500 -6.64100  1.000 46.44139  ? 136 SER   A OG  1 
ATOM   793  N  N   . VAL   A 1 101 ? 26.51100  -43.27000 -6.47900  1.000 45.99459  ? 137 VAL   A N   1 
ATOM   794  C  CA  . VAL   A 1 101 ? 25.45400  -43.21500 -5.47800  1.000 50.04161  ? 137 VAL   A CA  1 
ATOM   795  C  C   . VAL   A 1 101 ? 25.82700  -42.23900 -4.36900  1.000 45.18623  ? 137 VAL   A C   1 
ATOM   796  O  O   . VAL   A 1 101 ? 24.98900  -41.45800 -3.89900  1.000 46.44467  ? 137 VAL   A O   1 
ATOM   797  C  CB  . VAL   A 1 101 ? 25.16900  -44.62600 -4.93500  1.000 44.40550  ? 137 VAL   A CB  1 
ATOM   798  C  CG1 . VAL   A 1 101 ? 24.05800  -44.58000 -3.90500  1.000 45.02163  ? 137 VAL   A CG1 1 
ATOM   799  C  CG2 . VAL   A 1 101 ? 24.79600  -45.54900 -6.08400  1.000 50.71249  ? 137 VAL   A CG2 1 
ATOM   800  N  N   . LYS   A 1 102 ? 27.09600  -42.24800 -3.95700  1.000 44.56180  ? 138 LYS   A N   1 
ATOM   801  C  CA  . LYS   A 1 102 ? 27.55000  -41.35600 -2.89400  1.000 49.59782  ? 138 LYS   A CA  1 
ATOM   802  C  C   . LYS   A 1 102 ? 27.43000  -39.89300 -3.30600  1.000 47.18299  ? 138 LYS   A C   1 
ATOM   803  O  O   . LYS   A 1 102 ? 26.98000  -39.05500 -2.51500  1.000 41.30236  ? 138 LYS   A O   1 
ATOM   804  C  CB  . LYS   A 1 102 ? 28.99000  -41.69600 -2.51700  1.000 49.91000  ? 138 LYS   A CB  1 
ATOM   805  C  CG  . LYS   A 1 102 ? 29.62700  -40.76700 -1.49700  1.000 58.46762  ? 138 LYS   A CG  1 
ATOM   806  C  CD  . LYS   A 1 102 ? 31.04300  -41.23000 -1.15600  1.000 52.94408  ? 138 LYS   A CD  1 
ATOM   807  C  CE  . LYS   A 1 102 ? 31.77500  -40.18700 -0.31600  1.000 58.32344  ? 138 LYS   A CE  1 
ATOM   808  N  NZ  . LYS   A 1 102 ? 33.13100  -40.63200 0.12300   1.000 60.68145  ? 138 LYS   A NZ  1 
ATOM   809  N  N   . THR   A 1 103 ? 27.82300  -39.56800 -4.53800  1.000 44.15247  ? 139 THR   A N   1 
ATOM   810  C  CA  . THR   A 1 103 ? 27.68100  -38.19700 -5.01600  1.000 45.72018  ? 139 THR   A CA  1 
ATOM   811  C  C   . THR   A 1 103 ? 26.21600  -37.78700 -5.09800  1.000 47.75306  ? 139 THR   A C   1 
ATOM   812  O  O   . THR   A 1 103 ? 25.86300  -36.66400 -4.72200  1.000 44.34603  ? 139 THR   A O   1 
ATOM   813  C  CB  . THR   A 1 103 ? 28.35500  -38.03900 -6.37700  1.000 45.26736  ? 139 THR   A CB  1 
ATOM   814  O  OG1 . THR   A 1 103 ? 29.77200  -38.14100 -6.21600  1.000 46.88351  ? 139 THR   A OG1 1 
ATOM   815  C  CG2 . THR   A 1 103 ? 28.01100  -36.69300 -6.99800  1.000 44.12551  ? 139 THR   A CG2 1 
ATOM   816  N  N   . VAL   A 1 104 ? 25.34400  -38.67900 -5.57500  1.000 45.56631  ? 140 VAL   A N   1 
ATOM   817  C  CA  . VAL   A 1 104 ? 23.93300  -38.32000 -5.69800  1.000 41.05141  ? 140 VAL   A CA  1 
ATOM   818  C  C   . VAL   A 1 104 ? 23.33400  -38.04000 -4.32900  1.000 39.43123  ? 140 VAL   A C   1 
ATOM   819  O  O   . VAL   A 1 104 ? 22.60000  -37.06100 -4.14700  1.000 39.43204  ? 140 VAL   A O   1 
ATOM   820  C  CB  . VAL   A 1 104 ? 23.14400  -39.41600 -6.43500  1.000 33.17725  ? 140 VAL   A CB  1 
ATOM   821  C  CG1 . VAL   A 1 104 ? 21.65400  -39.09600 -6.38200  1.000 41.72659  ? 140 VAL   A CG1 1 
ATOM   822  C  CG2 . VAL   A 1 104 ? 23.60700  -39.52600 -7.86900  1.000 39.26815  ? 140 VAL   A CG2 1 
ATOM   823  N  N   . VAL   A 1 105 ? 23.64000  -38.88600 -3.34600  1.000 38.86084  ? 141 VAL   A N   1 
ATOM   824  C  CA  . VAL   A 1 105 ? 23.07700  -38.70000 -2.01200  1.000 38.07647  ? 141 VAL   A CA  1 
ATOM   825  C  C   . VAL   A 1 105 ? 23.53700  -37.37200 -1.42000  1.000 44.91777  ? 141 VAL   A C   1 
ATOM   826  O  O   . VAL   A 1 105 ? 22.72700  -36.58200 -0.92200  1.000 43.61117  ? 141 VAL   A O   1 
ATOM   827  C  CB  . VAL   A 1 105 ? 23.44500  -39.88700 -1.10400  1.000 46.05665  ? 141 VAL   A CB  1 
ATOM   828  C  CG1 . VAL   A 1 105 ? 23.15700  -39.55400 0.34800   1.000 44.72438  ? 141 VAL   A CG1 1 
ATOM   829  C  CG2 . VAL   A 1 105 ? 22.66400  -41.13000 -1.52500  1.000 43.07006  ? 141 VAL   A CG2 1 
ATOM   830  N  N   . GLN   A 1 106 ? 24.84400  -37.09700 -1.47900  1.000 35.83779  ? 142 GLN   A N   1 
ATOM   831  C  CA  . GLN   A 1 106 ? 25.37200  -35.88800 -0.84800  1.000 41.37770  ? 142 GLN   A CA  1 
ATOM   832  C  C   . GLN   A 1 106 ? 24.87500  -34.63500 -1.55800  1.000 41.49686  ? 142 GLN   A C   1 
ATOM   833  O  O   . GLN   A 1 106 ? 24.59000  -33.61500 -0.91900  1.000 54.08155  ? 142 GLN   A O   1 
ATOM   834  C  CB  . GLN   A 1 106 ? 26.90100  -35.93200 -0.83400  1.000 43.60923  ? 142 GLN   A CB  1 
ATOM   835  C  CG  . GLN   A 1 106 ? 27.48500  -37.04300 0.03200   1.000 51.51339  ? 142 GLN   A CG  1 
ATOM   836  C  CD  . GLN   A 1 106 ? 28.99600  -37.16900 -0.09700  1.000 57.27955  ? 142 GLN   A CD  1 
ATOM   837  O  OE1 . GLN   A 1 106 ? 29.72100  -37.12200 0.89700   1.000 59.17064  ? 142 GLN   A OE1 1 
ATOM   838  N  NE2 . GLN   A 1 106 ? 29.47500  -37.34200 -1.32200  1.000 51.77066  ? 142 GLN   A NE2 1 
ATOM   839  N  N   . VAL   A 1 107 ? 24.76700  -34.69900 -2.88300  1.000 37.27578  ? 143 VAL   A N   1 
ATOM   840  C  CA  . VAL   A 1 107 ? 24.19900  -33.60000 -3.65100  1.000 37.16440  ? 143 VAL   A CA  1 
ATOM   841  C  C   . VAL   A 1 107 ? 22.70100  -33.47100 -3.38000  1.000 42.67804  ? 143 VAL   A C   1 
ATOM   842  O  O   . VAL   A 1 107 ? 22.16800  -32.35800 -3.30200  1.000 42.11237  ? 143 VAL   A O   1 
ATOM   843  C  CB  . VAL   A 1 107 ? 24.51700  -33.81400 -5.14500  1.000 42.13494  ? 143 VAL   A CB  1 
ATOM   844  C  CG1 . VAL   A 1 107 ? 23.53100  -33.11400 -6.03200  1.000 50.68996  ? 143 VAL   A CG1 1 
ATOM   845  C  CG2 . VAL   A 1 107 ? 25.94100  -33.33200 -5.44700  1.000 50.78138  ? 143 VAL   A CG2 1 
ATOM   846  N  N   . ALA   A 1 108 ? 22.00300  -34.59700 -3.19800  1.000 43.38161  ? 144 ALA   A N   1 
ATOM   847  C  CA  . ALA   A 1 108 ? 20.55400  -34.53800 -3.00700  1.000 45.83664  ? 144 ALA   A CA  1 
ATOM   848  C  C   . ALA   A 1 108 ? 20.18700  -33.84300 -1.70100  1.000 45.28184  ? 144 ALA   A C   1 
ATOM   849  O  O   . ALA   A 1 108 ? 19.22200  -33.07100 -1.65400  1.000 44.56139  ? 144 ALA   A O   1 
ATOM   850  C  CB  . ALA   A 1 108 ? 19.95200  -35.94100 -3.05200  1.000 42.09158  ? 144 ALA   A CB  1 
ATOM   851  N  N   . ILE   A 1 109 ? 20.94900  -34.09100 -0.63200  1.000 39.82113  ? 145 ILE   A N   1 
ATOM   852  C  CA  . ILE   A 1 109 ? 20.59900  -33.49200 0.65200   1.000 42.62849  ? 145 ILE   A CA  1 
ATOM   853  C  C   . ILE   A 1 109 ? 20.89200  -31.99300 0.65500   1.000 48.53668  ? 145 ILE   A C   1 
ATOM   854  O  O   . ILE   A 1 109 ? 20.22100  -31.22900 1.36100   1.000 47.76141  ? 145 ILE   A O   1 
ATOM   855  C  CB  . ILE   A 1 109 ? 21.31600  -34.22100 1.80400   1.000 44.77649  ? 145 ILE   A CB  1 
ATOM   856  C  CG1 . ILE   A 1 109 ? 22.82800  -34.00500 1.73400   1.000 50.60218  ? 145 ILE   A CG1 1 
ATOM   857  C  CG2 . ILE   A 1 109 ? 20.99300  -35.71300 1.77100   1.000 51.12560  ? 145 ILE   A CG2 1 
ATOM   858  C  CD1 . ILE   A 1 109 ? 23.58600  -34.70600 2.83900   1.000 56.09030  ? 145 ILE   A CD1 1 
ATOM   859  N  N   . GLN   A 1 110 ? 21.87600  -31.53900 -0.13100  1.000 46.25499  ? 146 GLN   A N   1 
ATOM   860  C  CA  . GLN   A 1 110 ? 22.07400  -30.09900 -0.28000  1.000 41.78776  ? 146 GLN   A CA  1 
ATOM   861  C  C   . GLN   A 1 110 ? 20.98600  -29.47900 -1.14600  1.000 47.17663  ? 146 GLN   A C   1 
ATOM   862  O  O   . GLN   A 1 110 ? 20.52500  -28.36600 -0.86600  1.000 46.80122  ? 146 GLN   A O   1 
ATOM   863  C  CB  . GLN   A 1 110 ? 23.45200  -29.79800 -0.87300  1.000 42.32423  ? 146 GLN   A CB  1 
ATOM   864  C  CG  . GLN   A 1 110 ? 24.61100  -30.26500 -0.00500  1.000 42.05584  ? 146 GLN   A CG  1 
ATOM   865  C  CD  . GLN   A 1 110 ? 25.96900  -29.79300 -0.50800  1.000 51.31089  ? 146 GLN   A CD  1 
ATOM   866  O  OE1 . GLN   A 1 110 ? 26.09900  -28.70200 -1.06700  1.000 53.07073  ? 146 GLN   A OE1 1 
ATOM   867  N  NE2 . GLN   A 1 110 ? 26.99000  -30.61300 -0.29800  1.000 54.36877  ? 146 GLN   A NE2 1 
ATOM   868  N  N   . MET   A 1 111 ? 20.56600  -30.17600 -2.20500  1.000 41.73070  ? 147 MET   A N   1 
ATOM   869  C  CA  . MET   A 1 111 ? 19.48000  -29.65600 -3.02600  1.000 39.58152  ? 147 MET   A CA  1 
ATOM   870  C  C   . MET   A 1 111 ? 18.18500  -29.57200 -2.22500  1.000 46.22051  ? 147 MET   A C   1 
ATOM   871  O  O   . MET   A 1 111 ? 17.44300  -28.58700 -2.33700  1.000 44.54951  ? 147 MET   A O   1 
ATOM   872  C  CB  . MET   A 1 111 ? 19.32000  -30.51900 -4.27800  1.000 37.51039  ? 147 MET   A CB  1 
ATOM   873  C  CG  . MET   A 1 111 ? 20.56800  -30.50100 -5.16300  1.000 42.68704  ? 147 MET   A CG  1 
ATOM   874  S  SD  . MET   A 1 111 ? 20.53000  -31.66800 -6.53800  1.000 46.65293  ? 147 MET   A SD  1 
ATOM   875  C  CE  . MET   A 1 111 ? 19.59600  -30.77100 -7.76000  1.000 47.75561  ? 147 MET   A CE  1 
ATOM   876  N  N   . LEU   A 1 112 ? 17.91900  -30.57400 -1.38000  1.000 38.74908  ? 148 LEU   A N   1 
ATOM   877  C  CA  . LEU   A 1 112 ? 16.72600  -30.54100 -0.53600  1.000 46.15111  ? 148 LEU   A CA  1 
ATOM   878  C  C   . LEU   A 1 112 ? 16.79000  -29.39600 0.46800   1.000 49.16001  ? 148 LEU   A C   1 
ATOM   879  O  O   . LEU   A 1 112 ? 15.77000  -28.76400 0.76800   1.000 45.93794  ? 148 LEU   A O   1 
ATOM   880  C  CB  . LEU   A 1 112 ? 16.56000  -31.87800 0.18500   1.000 39.76544  ? 148 LEU   A CB  1 
ATOM   881  C  CG  . LEU   A 1 112 ? 16.05000  -33.06300 -0.63800  1.000 42.90192  ? 148 LEU   A CG  1 
ATOM   882  C  CD1 . LEU   A 1 112 ? 16.27500  -34.37100 0.11100   1.000 42.28493  ? 148 LEU   A CD1 1 
ATOM   883  C  CD2 . LEU   A 1 112 ? 14.57000  -32.88600 -0.96300  1.000 48.54623  ? 148 LEU   A CD2 1 
ATOM   884  N  N   . THR   A 1 113 ? 17.97900  -29.12600 1.01100   1.000 42.91070  ? 149 THR   A N   1 
ATOM   885  C  CA  . THR   A 1 113 ? 18.14200  -28.00100 1.92500   1.000 48.97446  ? 149 THR   A CA  1 
ATOM   886  C  C   . THR   A 1 113 ? 17.94000  -26.67300 1.20200   1.000 52.25445  ? 149 THR   A C   1 
ATOM   887  O  O   . THR   A 1 113 ? 17.29100  -25.76300 1.73300   1.000 51.34621  ? 149 THR   A O   1 
ATOM   888  C  CB  . THR   A 1 113 ? 19.52400  -28.06300 2.58000   1.000 46.59186  ? 149 THR   A CB  1 
ATOM   889  O  OG1 . THR   A 1 113 ? 19.68300  -29.33100 3.23100   1.000 47.68906  ? 149 THR   A OG1 1 
ATOM   890  C  CG2 . THR   A 1 113 ? 19.69300  -26.94700 3.60900   1.000 56.18236  ? 149 THR   A CG2 1 
ATOM   891  N  N   . LEU   A 1 114 ? 18.48200  -26.54500 -0.01100  1.000 45.46305  ? 150 LEU   A N   1 
ATOM   892  C  CA  . LEU   A 1 114 ? 18.28600  -25.32100 -0.78000  1.000 43.65204  ? 150 LEU   A CA  1 
ATOM   893  C  C   . LEU   A 1 114 ? 16.80700  -25.07300 -1.04100  1.000 49.20662  ? 150 LEU   A C   1 
ATOM   894  O  O   . LEU   A 1 114 ? 16.28600  -23.99100 -0.74500  1.000 45.91107  ? 150 LEU   A O   1 
ATOM   895  C  CB  . LEU   A 1 114 ? 19.05400  -25.39900 -2.09700  1.000 46.20172  ? 150 LEU   A CB  1 
ATOM   896  C  CG  . LEU   A 1 114 ? 20.54500  -25.07500 -2.01700  1.000 52.77282  ? 150 LEU   A CG  1 
ATOM   897  C  CD1 . LEU   A 1 114 ? 21.26300  -25.64000 -3.22600  1.000 55.60786  ? 150 LEU   A CD1 1 
ATOM   898  C  CD2 . LEU   A 1 114 ? 20.75100  -23.57200 -1.92600  1.000 51.67349  ? 150 LEU   A CD2 1 
ATOM   899  N  N   . VAL   A 1 115 ? 16.11200  -26.07400 -1.58500  1.000 45.79458  ? 151 VAL   A N   1 
ATOM   900  C  CA  . VAL   A 1 115 ? 14.70100  -25.91600 -1.92200  1.000 45.26992  ? 151 VAL   A CA  1 
ATOM   901  C  C   . VAL   A 1 115 ? 13.87600  -25.63900 -0.67000  1.000 46.41057  ? 151 VAL   A C   1 
ATOM   902  O  O   . VAL   A 1 115 ? 12.95000  -24.81800 -0.68900  1.000 52.20979  ? 151 VAL   A O   1 
ATOM   903  C  CB  . VAL   A 1 115 ? 14.20100  -27.16000 -2.67900  1.000 43.84775  ? 151 VAL   A CB  1 
ATOM   904  C  CG1 . VAL   A 1 115 ? 12.70200  -27.07700 -2.92000  1.000 45.47806  ? 151 VAL   A CG1 1 
ATOM   905  C  CG2 . VAL   A 1 115 ? 14.94500  -27.30500 -3.99700  1.000 38.20504  ? 151 VAL   A CG2 1 
ATOM   906  N  N   . GLU   A 1 116 ? 14.20300  -26.30900 0.43800   1.000 43.39631  ? 152 GLU   A N   1 
ATOM   907  C  CA  . GLU   A 1 116 ? 13.50300  -26.04500 1.69200   1.000 54.13564  ? 152 GLU   A CA  1 
ATOM   908  C  C   . GLU   A 1 116 ? 13.62800  -24.58000 2.08600   1.000 59.53376  ? 152 GLU   A C   1 
ATOM   909  O  O   . GLU   A 1 116 ? 12.62800  -23.91700 2.37700   1.000 55.90346  ? 152 GLU   A O   1 
ATOM   910  C  CB  . GLU   A 1 116 ? 14.04300  -26.94000 2.80900   1.000 48.79174  ? 152 GLU   A CB  1 
ATOM   911  C  CG  . GLU   A 1 116 ? 13.40600  -26.65000 4.16400   1.000 55.02792  ? 152 GLU   A CG  1 
ATOM   912  C  CD  . GLU   A 1 116 ? 14.01400  -27.45100 5.29800   1.000 61.34308  ? 152 GLU   A CD  1 
ATOM   913  O  OE1 . GLU   A 1 116 ? 14.95400  -28.23400 5.04800   1.000 56.32701  ? 152 GLU   A OE1 1 
ATOM   914  O  OE2 . GLU   A 1 116 ? 13.55100  -27.29200 6.44700   1.000 63.62501  ? 152 GLU   A OE2 1 
ATOM   915  N  N   . GLU   A 1 117 ? 14.85800  -24.05500 2.08900   1.000 54.88144  ? 153 GLU   A N   1 
ATOM   916  C  CA  . GLU   A 1 117 ? 15.07200  -22.66600 2.48000   1.000 59.59279  ? 153 GLU   A CA  1 
ATOM   917  C  C   . GLU   A 1 117 ? 14.32500  -21.70400 1.56600   1.000 58.70902  ? 153 GLU   A C   1 
ATOM   918  O  O   . GLU   A 1 117 ? 13.89000  -20.63500 2.01100   1.000 61.10158  ? 153 GLU   A O   1 
ATOM   919  C  CB  . GLU   A 1 117 ? 16.56800  -22.35000 2.49000   1.000 63.12730  ? 153 GLU   A CB  1 
ATOM   920  C  CG  . GLU   A 1 117 ? 16.94100  -21.13000 3.32300   1.000 76.33287  ? 153 GLU   A CG  1 
ATOM   921  C  CD  . GLU   A 1 117 ? 16.60900  -21.30200 4.79500   1.000 79.63298  ? 153 GLU   A CD  1 
ATOM   922  O  OE1 . GLU   A 1 117 ? 16.75100  -22.43000 5.31400   1.000 82.35374  ? 153 GLU   A OE1 1 
ATOM   923  O  OE2 . GLU   A 1 117 ? 16.20100  -20.30900 5.43300   1.000 87.10842  ? 153 GLU   A OE2 1 
ATOM   924  N  N   . VAL   A 1 118 ? 14.16100  -22.06000 0.29100   1.000 47.90645  ? 154 VAL   A N   1 
ATOM   925  C  CA  . VAL   A 1 118 ? 13.31500  -21.25500 -0.58300  1.000 53.25226  ? 154 VAL   A CA  1 
ATOM   926  C  C   . VAL   A 1 118 ? 11.86400  -21.32400 -0.12100  1.000 58.68100  ? 154 VAL   A C   1 
ATOM   927  O  O   . VAL   A 1 118 ? 11.15900  -20.30800 -0.09200  1.000 58.47546  ? 154 VAL   A O   1 
ATOM   928  C  CB  . VAL   A 1 118 ? 13.47200  -21.70500 -2.04600  1.000 49.23452  ? 154 VAL   A CB  1 
ATOM   929  C  CG1 . VAL   A 1 118 ? 12.50700  -20.94300 -2.93900  1.000 52.30017  ? 154 VAL   A CG1 1 
ATOM   930  C  CG2 . VAL   A 1 118 ? 14.90300  -21.49100 -2.51000  1.000 55.93693  ? 154 VAL   A CG2 1 
ATOM   931  N  N   . HIS   A 1 119 ? 11.40300  -22.51400 0.27400   1.000 51.50672  ? 155 HIS   A N   1 
ATOM   932  C  CA  . HIS   A 1 119 ? 10.03100  -22.65400 0.75500   1.000 61.42882  ? 155 HIS   A CA  1 
ATOM   933  C  C   . HIS   A 1 119 ? 9.81400   -21.92300 2.07300   1.000 58.10427  ? 155 HIS   A C   1 
ATOM   934  O  O   . HIS   A 1 119 ? 8.71500   -21.41400 2.31900   1.000 64.06652  ? 155 HIS   A O   1 
ATOM   935  C  CB  . HIS   A 1 119 ? 9.67300   -24.13200 0.90400   1.000 49.07667  ? 155 HIS   A CB  1 
ATOM   936  C  CG  . HIS   A 1 119 ? 9.64300   -24.87900 -0.39200  1.000 53.07150  ? 155 HIS   A CG  1 
ATOM   937  N  ND1 . HIS   A 1 119 ? 9.53600   -26.25200 -0.45700  1.000 47.95446  ? 155 HIS   A ND1 1 
ATOM   938  C  CD2 . HIS   A 1 119 ? 9.70400   -24.44600 -1.67300  1.000 49.24569  ? 155 HIS   A CD2 1 
ATOM   939  C  CE1 . HIS   A 1 119 ? 9.53000   -26.63100 -1.72200  1.000 49.02933  ? 155 HIS   A CE1 1 
ATOM   940  N  NE2 . HIS   A 1 119 ? 9.63000   -25.55500 -2.48100  1.000 48.48682  ? 155 HIS   A NE2 1 
ATOM   941  N  N   . ARG   A 1 120 ? 10.83500  -21.86600 2.93500   1.000 62.83868  ? 156 ARG   A N   1 
ATOM   942  C  CA  . ARG   A 1 120 ? 10.70900  -21.10400 4.17500   1.000 67.33917  ? 156 ARG   A CA  1 
ATOM   943  C  C   . ARG   A 1 120 ? 10.45100  -19.63100 3.89300   1.000 69.52170  ? 156 ARG   A C   1 
ATOM   944  O  O   . ARG   A 1 120 ? 9.80000   -18.94800 4.69200   1.000 72.32587  ? 156 ARG   A O   1 
ATOM   945  C  CB  . ARG   A 1 120 ? 11.96900  -21.25600 5.03000   1.000 73.42224  ? 156 ARG   A CB  1 
ATOM   946  C  CG  . ARG   A 1 120 ? 12.51900  -22.67200 5.10100   1.000 83.94890  ? 156 ARG   A CG  1 
ATOM   947  C  CD  . ARG   A 1 120 ? 12.15600  -23.38200 6.39200   1.000 90.98499  ? 156 ARG   A CD  1 
ATOM   948  N  NE  . ARG   A 1 120 ? 12.92000  -22.87200 7.52400   1.000 103.81548 ? 156 ARG   A NE  1 
ATOM   949  C  CZ  . ARG   A 1 120 ? 14.05700  -23.40200 7.95700   1.000 104.98179 ? 156 ARG   A CZ  1 
ATOM   950  N  NH1 . ARG   A 1 120 ? 14.57500  -24.48100 7.39400   1.000 93.88789  ? 156 ARG   A NH1 1 
ATOM   951  N  NH2 . ARG   A 1 120 ? 14.68700  -22.83600 8.98300   1.000 104.67933 ? 156 ARG   A NH2 1 
ATOM   952  N  N   . HIS   A 1 121 ? 10.95200  -19.12600 2.76400   1.000 66.69401  ? 157 HIS   A N   1 
ATOM   953  C  CA  . HIS   A 1 121 ? 10.74200  -17.74200 2.35900   1.000 74.09224  ? 157 HIS   A CA  1 
ATOM   954  C  C   . HIS   A 1 121 ? 9.51300   -17.57000 1.47500   1.000 67.90652  ? 157 HIS   A C   1 
ATOM   955  O  O   . HIS   A 1 121 ? 9.46100   -16.63100 0.66700   1.000 66.11921  ? 157 HIS   A O   1 
ATOM   956  C  CB  . HIS   A 1 121 ? 11.99200  -17.20900 1.65900   1.000 74.07514  ? 157 HIS   A CB  1 
ATOM   957  C  CG  . HIS   A 1 121 ? 13.15100  -16.99700 2.58200   1.000 78.96944  ? 157 HIS   A CG  1 
ATOM   958  N  ND1 . HIS   A 1 121 ? 13.74000  -18.02500 3.28600   1.000 75.76727  ? 157 HIS   A ND1 1 
ATOM   959  C  CD2 . HIS   A 1 121 ? 13.82000  -15.87200 2.92900   1.000 79.47811  ? 157 HIS   A CD2 1 
ATOM   960  C  CE1 . HIS   A 1 121 ? 14.72500  -17.54300 4.02300   1.000 77.05133  ? 157 HIS   A CE1 1 
ATOM   961  N  NE2 . HIS   A 1 121 ? 14.79600  -16.24000 3.82300   1.000 79.56164  ? 157 HIS   A NE2 1 
ATOM   962  N  N   . ASP   A 1 122 ? 8.52900   -18.46300 1.60400   1.000 69.84040  ? 158 ASP   A N   1 
ATOM   963  C  CA  . ASP   A 1 122 ? 7.20700   -18.34400 0.99200   1.000 66.31878  ? 158 ASP   A CA  1 
ATOM   964  C  C   . ASP   A 1 122 ? 7.23500   -18.44200 -0.52900  1.000 67.14649  ? 158 ASP   A C   1 
ATOM   965  O  O   . ASP   A 1 122 ? 6.30700   -17.96700 -1.19300  1.000 64.85939  ? 158 ASP   A O   1 
ATOM   966  C  CB  . ASP   A 1 122 ? 6.51700   -17.03700 1.40700   1.000 70.16443  ? 158 ASP   A CB  1 
ATOM   967  C  CG  . ASP   A 1 122 ? 6.71200   -16.71200 2.87400   1.000 76.56308  ? 158 ASP   A CG  1 
ATOM   968  O  OD1 . ASP   A 1 122 ? 6.58200   -17.62500 3.71500   1.000 75.35262  ? 158 ASP   A OD1 1 
ATOM   969  O  OD2 . ASP   A 1 122 ? 7.00400   -15.53700 3.18300   1.000 80.00752  ? 158 ASP   A OD2 1 
ATOM   970  N  N   . LEU   A 1 123 ? 8.26400   -19.06100 -1.10700  1.000 59.01000  ? 159 LEU   A N   1 
ATOM   971  C  CA  . LEU   A 1 123 ? 8.39800   -19.16600 -2.55400  1.000 59.94447  ? 159 LEU   A CA  1 
ATOM   972  C  C   . LEU   A 1 123 ? 8.53800   -20.62300 -2.97400  1.000 59.56762  ? 159 LEU   A C   1 
ATOM   973  O  O   . LEU   A 1 123 ? 9.08500   -21.44800 -2.23800  1.000 54.31901  ? 159 LEU   A O   1 
ATOM   974  C  CB  . LEU   A 1 123 ? 9.61700   -18.38200 -3.06200  1.000 62.43357  ? 159 LEU   A CB  1 
ATOM   975  C  CG  . LEU   A 1 123 ? 9.71300   -16.92200 -2.62800  1.000 66.49220  ? 159 LEU   A CG  1 
ATOM   976  C  CD1 . LEU   A 1 123 ? 10.93900  -16.26800 -3.24600  1.000 69.69708  ? 159 LEU   A CD1 1 
ATOM   977  C  CD2 . LEU   A 1 123 ? 8.44800   -16.17600 -3.00600  1.000 68.49798  ? 159 LEU   A CD2 1 
ATOM   978  N  N   . ILE   A 1 124 ? 8.04100   -20.92700 -4.17200  1.000 48.41905  ? 160 ILE   A N   1 
ATOM   979  C  CA  . ILE   A 1 124 ? 8.30800   -22.19600 -4.83700  1.000 55.52554  ? 160 ILE   A CA  1 
ATOM   980  C  C   . ILE   A 1 124 ? 9.14600   -21.91000 -6.07500  1.000 60.85585  ? 160 ILE   A C   1 
ATOM   981  O  O   . ILE   A 1 124 ? 9.02400   -20.85200 -6.70300  1.000 58.97573  ? 160 ILE   A O   1 
ATOM   982  C  CB  . ILE   A 1 124 ? 7.01900   -22.96200 -5.20900  1.000 52.06140  ? 160 ILE   A CB  1 
ATOM   983  C  CG1 . ILE   A 1 124 ? 6.04900   -22.05700 -5.97000  1.000 55.95380  ? 160 ILE   A CG1 1 
ATOM   984  C  CG2 . ILE   A 1 124 ? 6.36400   -23.54300 -3.97000  1.000 53.23533  ? 160 ILE   A CG2 1 
ATOM   985  C  CD1 . ILE   A 1 124 ? 4.77100   -22.75200 -6.37900  1.000 51.50845  ? 160 ILE   A CD1 1 
ATOM   986  N  N   . TYR   A 1 125 ? 10.00500  -22.86800 -6.43000  1.000 54.24880  ? 161 TYR   A N   1 
ATOM   987  C  CA  . TYR   A 1 125 ? 10.99900  -22.63000 -7.47300  1.000 51.17887  ? 161 TYR   A CA  1 
ATOM   988  C  C   . TYR   A 1 125 ? 10.41500  -22.83800 -8.86400  1.000 53.91065  ? 161 TYR   A C   1 
ATOM   989  O  O   . TYR   A 1 125 ? 10.58500  -21.99100 -9.74900  1.000 56.96865  ? 161 TYR   A O   1 
ATOM   990  C  CB  . TYR   A 1 125 ? 12.20600  -23.54200 -7.26100  1.000 50.99209  ? 161 TYR   A CB  1 
ATOM   991  C  CG  . TYR   A 1 125 ? 13.39700  -23.16400 -8.10600  1.000 51.32910  ? 161 TYR   A CG  1 
ATOM   992  C  CD1 . TYR   A 1 125 ? 14.14600  -22.03200 -7.81300  1.000 54.12424  ? 161 TYR   A CD1 1 
ATOM   993  C  CD2 . TYR   A 1 125 ? 13.77400  -23.93400 -9.19700  1.000 55.49071  ? 161 TYR   A CD2 1 
ATOM   994  C  CE1 . TYR   A 1 125 ? 15.24200  -21.68000 -8.58300  1.000 55.37591  ? 161 TYR   A CE1 1 
ATOM   995  C  CE2 . TYR   A 1 125 ? 14.86400  -23.58800 -9.97300  1.000 56.50698  ? 161 TYR   A CE2 1 
ATOM   996  C  CZ  . TYR   A 1 125 ? 15.59300  -22.46300 -9.66200  1.000 51.21722  ? 161 TYR   A CZ  1 
ATOM   997  O  OH  . TYR   A 1 125 ? 16.67500  -22.13000 -10.44100 1.000 52.25663  ? 161 TYR   A OH  1 
ATOM   998  N  N   . ARG   A 1 126 ? 9.75600   -23.97500 -9.08000  1.000 52.77434  ? 162 ARG   A N   1 
ATOM   999  C  CA  . ARG   A 1 126 ? 9.00500   -24.28400 -10.29400 1.000 54.14300  ? 162 ARG   A CA  1 
ATOM   1000 C  C   . ARG   A 1 126 ? 9.88400   -24.42300 -11.53200 1.000 58.51219  ? 162 ARG   A C   1 
ATOM   1001 O  O   . ARG   A 1 126 ? 9.36000   -24.49200 -12.65100 1.000 64.27915  ? 162 ARG   A O   1 
ATOM   1002 C  CB  . ARG   A 1 126 ? 7.91000   -23.23900 -10.55600 1.000 55.49811  ? 162 ARG   A CB  1 
ATOM   1003 C  CG  . ARG   A 1 126 ? 6.92500   -23.07900 -9.41600  1.000 59.20439  ? 162 ARG   A CG  1 
ATOM   1004 C  CD  . ARG   A 1 126 ? 5.64900   -22.40600 -9.88300  1.000 56.43018  ? 162 ARG   A CD  1 
ATOM   1005 N  NE  . ARG   A 1 126 ? 5.91400   -21.16400 -10.59700 1.000 62.98137  ? 162 ARG   A NE  1 
ATOM   1006 C  CZ  . ARG   A 1 126 ? 4.99500   -20.45800 -11.24200 1.000 73.07288  ? 162 ARG   A CZ  1 
ATOM   1007 N  NH1 . ARG   A 1 126 ? 3.73100   -20.84900 -11.29300 1.000 66.32075  ? 162 ARG   A NH1 1 
ATOM   1008 N  NH2 . ARG   A 1 126 ? 5.35300   -19.33100 -11.85100 1.000 73.54554  ? 162 ARG   A NH2 1 
ATOM   1009 N  N   . ASP   A 1 127 ? 11.20300  -24.47300 -11.37400 1.000 63.85922  ? 163 ASP   A N   1 
ATOM   1010 C  CA  . ASP   A 1 127 ? 12.10300  -24.63900 -12.51100 1.000 64.32963  ? 163 ASP   A CA  1 
ATOM   1011 C  C   . ASP   A 1 127 ? 13.27400  -25.53400 -12.13000 1.000 61.21950  ? 163 ASP   A C   1 
ATOM   1012 O  O   . ASP   A 1 127 ? 14.42100  -25.28800 -12.51700 1.000 53.34259  ? 163 ASP   A O   1 
ATOM   1013 C  CB  . ASP   A 1 127 ? 12.59600  -23.28800 -13.02600 1.000 65.60723  ? 163 ASP   A CB  1 
ATOM   1014 C  CG  . ASP   A 1 127 ? 13.14200  -23.36800 -14.43500 1.000 73.77832  ? 163 ASP   A CG  1 
ATOM   1015 O  OD1 . ASP   A 1 127 ? 12.77200  -24.31500 -15.16100 1.000 69.38035  ? 163 ASP   A OD1 1 
ATOM   1016 O  OD2 . ASP   A 1 127 ? 13.95000  -22.49300 -14.81300 1.000 79.76325  ? 163 ASP   A OD2 1 
ATOM   1017 N  N   . ILE   A 1 128 ? 12.99400  -26.58600 -11.36300 1.000 46.40309  ? 164 ILE   A N   1 
ATOM   1018 C  CA  . ILE   A 1 128 ? 14.03600  -27.48800 -10.88700 1.000 44.12408  ? 164 ILE   A CA  1 
ATOM   1019 C  C   . ILE   A 1 128 ? 14.69500  -28.17300 -12.07800 1.000 45.29178  ? 164 ILE   A C   1 
ATOM   1020 O  O   . ILE   A 1 128 ? 14.02300  -28.81100 -12.89700 1.000 39.23827  ? 164 ILE   A O   1 
ATOM   1021 C  CB  . ILE   A 1 128 ? 13.46000  -28.52100 -9.91200  1.000 42.75365  ? 164 ILE   A CB  1 
ATOM   1022 C  CG1 . ILE   A 1 128 ? 13.03800  -27.85700 -8.59900  1.000 44.70371  ? 164 ILE   A CG1 1 
ATOM   1023 C  CG2 . ILE   A 1 128 ? 14.47200  -29.63800 -9.66800  1.000 41.80587  ? 164 ILE   A CG2 1 
ATOM   1024 C  CD1 . ILE   A 1 128 ? 14.17000  -27.19600 -7.84100  1.000 39.35702  ? 164 ILE   A CD1 1 
ATOM   1025 N  N   . LYS   A 1 129 ? 16.01700  -28.05400 -12.16800 1.000 49.28466  ? 165 LYS   A N   1 
ATOM   1026 C  CA  . LYS   A 1 129 ? 16.79800  -28.66700 -13.23400 1.000 47.67954  ? 165 LYS   A CA  1 
ATOM   1027 C  C   . LYS   A 1 129 ? 18.25600  -28.64300 -12.81300 1.000 42.75324  ? 165 LYS   A C   1 
ATOM   1028 O  O   . LYS   A 1 129 ? 18.67000  -27.72100 -12.10300 1.000 44.46923  ? 165 LYS   A O   1 
ATOM   1029 C  CB  . LYS   A 1 129 ? 16.60700  -27.91800 -14.56300 1.000 50.35468  ? 165 LYS   A CB  1 
ATOM   1030 C  CG  . LYS   A 1 129 ? 17.04700  -26.46000 -14.51000 1.000 56.35529  ? 165 LYS   A CG  1 
ATOM   1031 C  CD  . LYS   A 1 129 ? 16.55000  -25.67100 -15.71100 1.000 57.77440  ? 165 LYS   A CD  1 
ATOM   1032 C  CE  . LYS   A 1 129 ? 17.17700  -26.16600 -16.99900 1.000 57.98568  ? 165 LYS   A CE  1 
ATOM   1033 N  NZ  . LYS   A 1 129 ? 16.90000  -25.24200 -18.13600 1.000 75.92378  ? 165 LYS   A NZ  1 
ATOM   1034 N  N   . PRO   A 1 130 ? 19.05600  -29.63900 -13.21100 1.000 48.61691  ? 166 PRO   A N   1 
ATOM   1035 C  CA  . PRO   A 1 130 ? 20.47400  -29.62900 -12.81900 1.000 45.30805  ? 166 PRO   A CA  1 
ATOM   1036 C  C   . PRO   A 1 130 ? 21.23700  -28.44300 -13.37700 1.000 47.55462  ? 166 PRO   A C   1 
ATOM   1037 O  O   . PRO   A 1 130 ? 22.28800  -28.08600 -12.83100 1.000 49.38857  ? 166 PRO   A O   1 
ATOM   1038 C  CB  . PRO   A 1 130 ? 21.00500  -30.95700 -13.37600 1.000 45.53615  ? 166 PRO   A CB  1 
ATOM   1039 C  CG  . PRO   A 1 130 ? 20.05900  -31.32700 -14.46400 1.000 50.32627  ? 166 PRO   A CG  1 
ATOM   1040 C  CD  . PRO   A 1 130 ? 18.71600  -30.81500 -14.03300 1.000 43.19572  ? 166 PRO   A CD  1 
ATOM   1041 N  N   . ASP   A 1 131 ? 20.73200  -27.81200 -14.43800 1.000 46.95681  ? 167 ASP   A N   1 
ATOM   1042 C  CA  . ASP   A 1 131 ? 21.40600  -26.66800 -15.03700 1.000 51.41619  ? 167 ASP   A CA  1 
ATOM   1043 C  C   . ASP   A 1 131 ? 21.41100  -25.44800 -14.12600 1.000 50.82604  ? 167 ASP   A C   1 
ATOM   1044 O  O   . ASP   A 1 131 ? 22.28100  -24.58300 -14.27500 1.000 43.79309  ? 167 ASP   A O   1 
ATOM   1045 C  CB  . ASP   A 1 131 ? 20.73600  -26.32700 -16.36400 1.000 57.44129  ? 167 ASP   A CB  1 
ATOM   1046 C  CG  . ASP   A 1 131 ? 20.38800  -27.56500 -17.16800 1.000 61.02858  ? 167 ASP   A CG  1 
ATOM   1047 O  OD1 . ASP   A 1 131 ? 19.52500  -28.34900 -16.70900 1.000 58.37199  ? 167 ASP   A OD1 1 
ATOM   1048 O  OD2 . ASP   A 1 131 ? 20.99500  -27.76900 -18.23900 1.000 58.57557  ? 167 ASP   A OD2 1 
ATOM   1049 N  N   . ASN   A 1 132 ? 20.47800  -25.36000 -13.18000 1.000 44.65671  ? 168 ASN   A N   1 
ATOM   1050 C  CA  . ASN   A 1 132 ? 20.39400  -24.20100 -12.30300 1.000 49.47879  ? 168 ASN   A CA  1 
ATOM   1051 C  C   . ASN   A 1 132 ? 21.06300  -24.41200 -10.95200 1.000 49.26892  ? 168 ASN   A C   1 
ATOM   1052 O  O   . ASN   A 1 132 ? 21.12800  -23.46400 -10.16100 1.000 50.78802  ? 168 ASN   A O   1 
ATOM   1053 C  CB  . ASN   A 1 132 ? 18.93100  -23.80700 -12.08700 1.000 51.43254  ? 168 ASN   A CB  1 
ATOM   1054 C  CG  . ASN   A 1 132 ? 18.27100  -23.32200 -13.35500 1.000 56.61080  ? 168 ASN   A CG  1 
ATOM   1055 O  OD1 . ASN   A 1 132 ? 18.94400  -22.98800 -14.33000 1.000 57.44842  ? 168 ASN   A OD1 1 
ATOM   1056 N  ND2 . ASN   A 1 132 ? 16.94700  -23.28000 -13.35100 1.000 55.72571  ? 168 ASN   A ND2 1 
ATOM   1057 N  N   . PHE   A 1 133 ? 21.54900  -25.61600 -10.66400 1.000 40.80748  ? 169 PHE   A N   1 
ATOM   1058 C  CA  . PHE   A 1 133 ? 22.29700  -25.89200 -9.44200  1.000 39.93730  ? 169 PHE   A CA  1 
ATOM   1059 C  C   . PHE   A 1 133 ? 23.78300  -25.83700 -9.77800  1.000 46.48188  ? 169 PHE   A C   1 
ATOM   1060 O  O   . PHE   A 1 133 ? 24.27600  -26.64900 -10.56500 1.000 44.28947  ? 169 PHE   A O   1 
ATOM   1061 C  CB  . PHE   A 1 133 ? 21.91600  -27.24800 -8.85700  1.000 41.02011  ? 169 PHE   A CB  1 
ATOM   1062 C  CG  . PHE   A 1 133 ? 20.53000  -27.29600 -8.27400  1.000 41.55600  ? 169 PHE   A CG  1 
ATOM   1063 C  CD1 . PHE   A 1 133 ? 19.43600  -27.59000 -9.07200  1.000 46.36425  ? 169 PHE   A CD1 1 
ATOM   1064 C  CD2 . PHE   A 1 133 ? 20.32600  -27.06300 -6.92200  1.000 45.23596  ? 169 PHE   A CD2 1 
ATOM   1065 C  CE1 . PHE   A 1 133 ? 18.16300  -27.64500 -8.53500  1.000 45.31512  ? 169 PHE   A CE1 1 
ATOM   1066 C  CE2 . PHE   A 1 133 ? 19.05300  -27.11900 -6.38100  1.000 46.65665  ? 169 PHE   A CE2 1 
ATOM   1067 C  CZ  . PHE   A 1 133 ? 17.97400  -27.40900 -7.18900  1.000 41.33993  ? 169 PHE   A CZ  1 
ATOM   1068 N  N   . LEU   A 1 134 ? 24.49100  -24.88300 -9.18000  1.000 53.06028  ? 170 LEU   A N   1 
ATOM   1069 C  CA  . LEU   A 1 134 ? 25.88300  -24.60800 -9.49900  1.000 50.61529  ? 170 LEU   A CA  1 
ATOM   1070 C  C   . LEU   A 1 134 ? 26.75900  -24.80300 -8.26900  1.000 52.25815  ? 170 LEU   A C   1 
ATOM   1071 O  O   . LEU   A 1 134 ? 26.34000  -24.53900 -7.13900  1.000 53.48545  ? 170 LEU   A O   1 
ATOM   1072 C  CB  . LEU   A 1 134 ? 26.06300  -23.17300 -10.01800 1.000 51.90823  ? 170 LEU   A CB  1 
ATOM   1073 C  CG  . LEU   A 1 134 ? 25.75600  -22.82200 -11.47700 1.000 52.71752  ? 170 LEU   A CG  1 
ATOM   1074 C  CD1 . LEU   A 1 134 ? 24.33700  -23.18600 -11.87100 1.000 44.58155  ? 170 LEU   A CD1 1 
ATOM   1075 C  CD2 . LEU   A 1 134 ? 26.00600  -21.33400 -11.70300 1.000 57.43616  ? 170 LEU   A CD2 1 
ATOM   1076 N  N   . ILE   A 1 135 ? 27.99400  -25.24400 -8.49800  1.000 52.46512  ? 171 ILE   A N   1 
ATOM   1077 C  CA  . ILE   A 1 135 ? 28.97700  -25.30700 -7.42300  1.000 52.92228  ? 171 ILE   A CA  1 
ATOM   1078 C  C   . ILE   A 1 135 ? 29.69900  -23.96800 -7.35100  1.000 54.07964  ? 171 ILE   A C   1 
ATOM   1079 O  O   . ILE   A 1 135 ? 29.39600  -23.04600 -8.11600  1.000 51.02586  ? 171 ILE   A O   1 
ATOM   1080 C  CB  . ILE   A 1 135 ? 29.96700  -26.46700 -7.62800  1.000 54.61716  ? 171 ILE   A CB  1 
ATOM   1081 C  CG1 . ILE   A 1 135 ? 30.66700  -26.32900 -8.97900  1.000 53.22676  ? 171 ILE   A CG1 1 
ATOM   1082 C  CG2 . ILE   A 1 135 ? 29.24900  -27.80400 -7.52200  1.000 53.50845  ? 171 ILE   A CG2 1 
ATOM   1083 C  CD1 . ILE   A 1 135 ? 31.94100  -27.13100 -9.09200  1.000 61.00490  ? 171 ILE   A CD1 1 
ATOM   1084 N  N   . GLY   A 1 136 ? 30.65600  -23.84900 -6.43300  1.000 54.77851  ? 172 GLY   A N   1 
ATOM   1085 C  CA  . GLY   A 1 136 ? 31.42100  -22.63200 -6.27200  1.000 64.99247  ? 172 GLY   A CA  1 
ATOM   1086 C  C   . GLY   A 1 136 ? 32.65600  -22.61100 -7.15100  1.000 67.01589  ? 172 GLY   A C   1 
ATOM   1087 O  O   . GLY   A 1 136 ? 32.86000  -23.46100 -8.02000  1.000 69.29992  ? 172 GLY   A O   1 
ATOM   1088 N  N   . ARG   A 1 137 ? 33.49300  -21.60900 -6.91700  1.000 71.09828  ? 173 ARG   A N   1 
ATOM   1089 C  CA  . ARG   A 1 137 ? 34.74000  -21.47100 -7.65200  1.000 76.40075  ? 173 ARG   A CA  1 
ATOM   1090 C  C   . ARG   A 1 137 ? 35.89100  -22.07300 -6.84900  1.000 69.89393  ? 173 ARG   A C   1 
ATOM   1091 O  O   . ARG   A 1 137 ? 35.75400  -22.41000 -5.67100  1.000 72.34072  ? 173 ARG   A O   1 
ATOM   1092 C  CB  . ARG   A 1 137 ? 34.99700  -20.00000 -7.99400  1.000 78.34844  ? 173 ARG   A CB  1 
ATOM   1093 C  CG  . ARG   A 1 137 ? 34.12200  -19.49700 -9.14100  1.000 69.72311  ? 173 ARG   A CG  1 
ATOM   1094 C  CD  . ARG   A 1 137 ? 34.18200  -17.98900 -9.32200  1.000 73.24328  ? 173 ARG   A CD  1 
ATOM   1095 N  NE  . ARG   A 1 137 ? 35.48600  -17.52100 -9.77400  1.000 82.60011  ? 173 ARG   A NE  1 
ATOM   1096 C  CZ  . ARG   A 1 137 ? 35.83900  -17.39400 -11.04700 1.000 76.22627  ? 173 ARG   A CZ  1 
ATOM   1097 N  NH1 . ARG   A 1 137 ? 35.02100  -17.73700 -12.02900 1.000 80.11481  ? 173 ARG   A NH1 1 
ATOM   1098 N  NH2 . ARG   A 1 137 ? 37.04200  -16.91100 -11.34100 1.000 71.67949  ? 173 ARG   A NH2 1 
ATOM   1099 N  N   . ARG   A 1 138 ? 37.03200  -22.22300 -7.51300  1.000 80.18015  ? 174 ARG   A N   1 
ATOM   1100 C  CA  . ARG   A 1 138 ? 38.16600  -22.90500 -6.90600  1.000 79.92374  ? 174 ARG   A CA  1 
ATOM   1101 C  C   . ARG   A 1 138 ? 38.78000  -22.07900 -5.78400  1.000 79.64827  ? 174 ARG   A C   1 
ATOM   1102 O  O   . ARG   A 1 138 ? 38.75200  -20.84600 -5.79700  1.000 88.34528  ? 174 ARG   A O   1 
ATOM   1103 C  CB  . ARG   A 1 138 ? 39.22800  -23.21100 -7.95600  1.000 83.28847  ? 174 ARG   A CB  1 
ATOM   1104 C  CG  . ARG   A 1 138 ? 38.91800  -24.42600 -8.78400  1.000 90.03665  ? 174 ARG   A CG  1 
ATOM   1105 C  CD  . ARG   A 1 138 ? 39.70400  -25.62100 -8.29900  1.000 93.47345  ? 174 ARG   A CD  1 
ATOM   1106 N  NE  . ARG   A 1 138 ? 39.22300  -26.83800 -8.93500  1.000 95.63208  ? 174 ARG   A NE  1 
ATOM   1107 C  CZ  . ARG   A 1 138 ? 39.49500  -27.18500 -10.18500 1.000 89.64242  ? 174 ARG   A CZ  1 
ATOM   1108 N  NH1 . ARG   A 1 138 ? 40.27200  -26.44200 -10.95500 1.000 91.34678  ? 174 ARG   A NH1 1 
ATOM   1109 N  NH2 . ARG   A 1 138 ? 38.97100  -28.30300 -10.67500 1.000 85.72742  ? 174 ARG   A NH2 1 
ATOM   1110 N  N   . GLY   A 1 139 ? 39.35200  -22.78400 -4.80700  1.000 77.80451  ? 175 GLY   A N   1 
ATOM   1111 C  CA  . GLY   A 1 139 ? 39.95800  -22.15600 -3.65400  1.000 86.10726  ? 175 GLY   A CA  1 
ATOM   1112 C  C   . GLY   A 1 139 ? 38.98600  -21.57200 -2.66000  1.000 80.66327  ? 175 GLY   A C   1 
ATOM   1113 O  O   . GLY   A 1 139 ? 39.40400  -21.20300 -1.55500  1.000 87.37905  ? 175 GLY   A O   1 
ATOM   1114 N  N   . ALA   A 1 140 ? 37.70700  -21.47400 -3.00500  1.000 80.49798  ? 176 ALA   A N   1 
ATOM   1115 C  CA  . ALA   A 1 140 ? 36.72500  -20.90700 -2.10200  1.000 76.96142  ? 176 ALA   A CA  1 
ATOM   1116 C  C   . ALA   A 1 140 ? 36.31500  -21.93100 -1.04900  1.000 86.90107  ? 176 ALA   A C   1 
ATOM   1117 O  O   . ALA   A 1 140 ? 36.50400  -23.14200 -1.20700  1.000 81.37304  ? 176 ALA   A O   1 
ATOM   1118 C  CB  . ALA   A 1 140 ? 35.49900  -20.42300 -2.87600  1.000 82.91709  ? 176 ALA   A CB  1 
ATOM   1119 N  N   . THR   A 1 141 ? 35.75000  -21.42200 0.04600   1.000 96.25916  ? 177 THR   A N   1 
ATOM   1120 C  CA  . THR   A 1 141 ? 35.27000  -22.29000 1.11300   1.000 97.01125  ? 177 THR   A CA  1 
ATOM   1121 C  C   . THR   A 1 141 ? 34.05700  -23.10700 0.68300   1.000 90.14304  ? 177 THR   A C   1 
ATOM   1122 O  O   . THR   A 1 141 ? 33.80100  -24.16900 1.26100   1.000 101.34948 ? 177 THR   A O   1 
ATOM   1123 C  CB  . THR   A 1 141 ? 34.93600  -21.45400 2.35100   1.000 98.95339  ? 177 THR   A CB  1 
ATOM   1124 O  OG1 . THR   A 1 141 ? 35.93900  -20.44500 2.52800   1.000 105.17279 ? 177 THR   A OG1 1 
ATOM   1125 C  CG2 . THR   A 1 141 ? 34.89900  -22.33000 3.59500   1.000 103.95800 ? 177 THR   A CG2 1 
ATOM   1126 N  N   . ASP   A 1 142 ? 33.31400  -22.64300 -0.31900  1.000 76.75867  ? 178 ASP   A N   1 
ATOM   1127 C  CA  . ASP   A 1 142 ? 32.16400  -23.35600 -0.86600  1.000 77.40416  ? 178 ASP   A CA  1 
ATOM   1128 C  C   . ASP   A 1 142 ? 32.42200  -23.78900 -2.30700  1.000 70.52794  ? 178 ASP   A C   1 
ATOM   1129 O  O   . ASP   A 1 142 ? 31.55300  -23.67500 -3.17400  1.000 69.08412  ? 178 ASP   A O   1 
ATOM   1130 C  CB  . ASP   A 1 142 ? 30.90800  -22.49500 -0.78100  1.000 75.59980  ? 178 ASP   A CB  1 
ATOM   1131 C  CG  . ASP   A 1 142 ? 31.04000  -21.19700 -1.55200  1.000 72.63564  ? 178 ASP   A CG  1 
ATOM   1132 O  OD1 . ASP   A 1 142 ? 32.18500  -20.80400 -1.85300  1.000 78.77985  ? 178 ASP   A OD1 1 
ATOM   1133 O  OD2 . ASP   A 1 142 ? 30.00100  -20.57300 -1.85700  1.000 76.38274  ? 178 ASP   A OD2 1 
ATOM   1134 N  N   . GLU   A 1 143 ? 33.63200  -24.28700 -2.57200  1.000 66.24653  ? 179 GLU   A N   1 
ATOM   1135 C  CA  . GLU   A 1 143 ? 34.00800  -24.66100 -3.93200  1.000 63.69813  ? 179 GLU   A CA  1 
ATOM   1136 C  C   . GLU   A 1 143 ? 33.11500  -25.76900 -4.47400  1.000 62.25373  ? 179 GLU   A C   1 
ATOM   1137 O  O   . GLU   A 1 143 ? 32.62700  -25.69000 -5.60700  1.000 63.88207  ? 179 GLU   A O   1 
ATOM   1138 C  CB  . GLU   A 1 143 ? 35.47400  -25.09300 -3.96500  1.000 70.85087  ? 179 GLU   A CB  1 
ATOM   1139 C  CG  . GLU   A 1 143 ? 35.92600  -25.64200 -5.30700  1.000 72.22006  ? 179 GLU   A CG  1 
ATOM   1140 C  CD  . GLU   A 1 143 ? 37.37800  -26.07600 -5.29600  1.000 71.09464  ? 179 GLU   A CD  1 
ATOM   1141 O  OE1 . GLU   A 1 143 ? 38.13100  -25.61400 -4.41300  1.000 64.89485  ? 179 GLU   A OE1 1 
ATOM   1142 O  OE2 . GLU   A 1 143 ? 37.76000  -26.88700 -6.16500  1.000 77.55066  ? 179 GLU   A OE2 1 
ATOM   1143 N  N   . ASN   A 1 144 ? 32.89800  -26.81900 -3.68400  1.000 55.18160  ? 180 ASN   A N   1 
ATOM   1144 C  CA  . ASN   A 1 144 ? 32.10900  -27.96200 -4.12400  1.000 59.78590  ? 180 ASN   A CA  1 
ATOM   1145 C  C   . ASN   A 1 144 ? 30.74300  -28.02700 -3.45200  1.000 58.65008  ? 180 ASN   A C   1 
ATOM   1146 O  O   . ASN   A 1 144 ? 30.07500  -29.06500 -3.52300  1.000 58.62182  ? 180 ASN   A O   1 
ATOM   1147 C  CB  . ASN   A 1 144 ? 32.88300  -29.25900 -3.88700  1.000 53.86529  ? 180 ASN   A CB  1 
ATOM   1148 C  CG  . ASN   A 1 144 ? 34.17600  -29.31700 -4.68200  1.000 60.96993  ? 180 ASN   A CG  1 
ATOM   1149 O  OD1 . ASN   A 1 144 ? 34.16100  -29.43100 -5.90700  1.000 67.02287  ? 180 ASN   A OD1 1 
ATOM   1150 N  ND2 . ASN   A 1 144 ? 35.30300  -29.23900 -3.98600  1.000 67.24410  ? 180 ASN   A ND2 1 
ATOM   1151 N  N   . ASN   A 1 145 ? 30.31900  -26.95000 -2.79700  1.000 59.95762  ? 181 ASN   A N   1 
ATOM   1152 C  CA  . ASN   A 1 145 ? 28.97500  -26.87800 -2.24700  1.000 61.68784  ? 181 ASN   A CA  1 
ATOM   1153 C  C   . ASN   A 1 145 ? 27.97900  -26.49800 -3.33400  1.000 60.93021  ? 181 ASN   A C   1 
ATOM   1154 O  O   . ASN   A 1 145 ? 28.30600  -25.78400 -4.28600  1.000 58.09872  ? 181 ASN   A O   1 
ATOM   1155 C  CB  . ASN   A 1 145 ? 28.90200  -25.86000 -1.11000  1.000 60.94524  ? 181 ASN   A CB  1 
ATOM   1156 C  CG  . ASN   A 1 145 ? 29.55000  -26.35800 0.15800   1.000 67.77022  ? 181 ASN   A CG  1 
ATOM   1157 O  OD1 . ASN   A 1 145 ? 29.69600  -27.56400 0.35900   1.000 68.55210  ? 181 ASN   A OD1 1 
ATOM   1158 N  ND2 . ASN   A 1 145 ? 29.93900  -25.43400 1.02800   1.000 69.00437  ? 181 ASN   A ND2 1 
ATOM   1159 N  N   . VAL   A 1 146 ? 26.75500  -26.97100 -3.17900  1.000 55.26967  ? 182 VAL   A N   1 
ATOM   1160 C  CA  . VAL   A 1 146 ? 25.72700  -26.73000 -4.18200  1.000 49.18286  ? 182 VAL   A CA  1 
ATOM   1161 C  C   . VAL   A 1 146 ? 25.09100  -25.37100 -3.93700  1.000 50.49328  ? 182 VAL   A C   1 
ATOM   1162 O  O   . VAL   A 1 146 ? 24.84700  -24.97800 -2.78900  1.000 51.24445  ? 182 VAL   A O   1 
ATOM   1163 C  CB  . VAL   A 1 146 ? 24.68300  -27.85800 -4.15800  1.000 51.71720  ? 182 VAL   A CB  1 
ATOM   1164 C  CG1 . VAL   A 1 146 ? 23.66900  -27.67000 -5.27600  1.000 47.17822  ? 182 VAL   A CG1 1 
ATOM   1165 C  CG2 . VAL   A 1 146 ? 25.37700  -29.21900 -4.26900  1.000 45.99211  ? 182 VAL   A CG2 1 
ATOM   1166 N  N   . HIS   A 1 147 ? 24.82600  -24.64600 -5.01900  1.000 48.79722  ? 183 HIS   A N   1 
ATOM   1167 C  CA  . HIS   A 1 147 ? 24.14000  -23.36300 -4.98100  1.000 54.34680  ? 183 HIS   A CA  1 
ATOM   1168 C  C   . HIS   A 1 147 ? 22.90300  -23.42300 -5.86800  1.000 50.06924  ? 183 HIS   A C   1 
ATOM   1169 O  O   . HIS   A 1 147 ? 22.73900  -24.33500 -6.68000  1.000 55.51172  ? 183 HIS   A O   1 
ATOM   1170 C  CB  . HIS   A 1 147 ? 25.06000  -22.22100 -5.43900  1.000 51.69121  ? 183 HIS   A CB  1 
ATOM   1171 C  CG  . HIS   A 1 147 ? 26.35800  -22.15300 -4.69700  1.000 54.25694  ? 183 HIS   A CG  1 
ATOM   1172 N  ND1 . HIS   A 1 147 ? 27.39000  -23.03800 -4.92000  1.000 60.72030  ? 183 HIS   A ND1 1 
ATOM   1173 C  CD2 . HIS   A 1 147 ? 26.79200  -21.30400 -3.73500  1.000 54.64034  ? 183 HIS   A CD2 1 
ATOM   1174 C  CE1 . HIS   A 1 147 ? 28.40500  -22.73600 -4.12900  1.000 62.55220  ? 183 HIS   A CE1 1 
ATOM   1175 N  NE2 . HIS   A 1 147 ? 28.06600  -21.69000 -3.39800  1.000 59.19607  ? 183 HIS   A NE2 1 
ATOM   1176 N  N   . LEU   A 1 148 ? 22.02800  -22.43200 -5.71200  1.000 50.85142  ? 184 LEU   A N   1 
ATOM   1177 C  CA  . LEU   A 1 148 ? 20.82300  -22.32800 -6.52400  1.000 48.91672  ? 184 LEU   A CA  1 
ATOM   1178 C  C   . LEU   A 1 148 ? 20.72800  -20.92200 -7.09700  1.000 54.52547  ? 184 LEU   A C   1 
ATOM   1179 O  O   . LEU   A 1 148 ? 20.82700  -19.93900 -6.35600  1.000 56.64180  ? 184 LEU   A O   1 
ATOM   1180 C  CB  . LEU   A 1 148 ? 19.56800  -22.65600 -5.70400  1.000 49.53248  ? 184 LEU   A CB  1 
ATOM   1181 C  CG  . LEU   A 1 148 ? 18.24200  -22.59100 -6.46600  1.000 47.82597  ? 184 LEU   A CG  1 
ATOM   1182 C  CD1 . LEU   A 1 148 ? 18.23800  -23.56600 -7.64000  1.000 46.12012  ? 184 LEU   A CD1 1 
ATOM   1183 C  CD2 . LEU   A 1 148 ? 17.05900  -22.86700 -5.53600  1.000 51.40691  ? 184 LEU   A CD2 1 
ATOM   1184 N  N   . ILE   A 1 149 ? 20.53800  -20.82500 -8.41100  1.000 47.87990  ? 185 ILE   A N   1 
ATOM   1185 C  CA  . ILE   A 1 149 ? 20.43700  -19.54900 -9.10100  1.000 59.28556  ? 185 ILE   A CA  1 
ATOM   1186 C  C   . ILE   A 1 149 ? 19.18900  -19.56300 -9.98100  1.000 63.62264  ? 185 ILE   A C   1 
ATOM   1187 O  O   . ILE   A 1 149 ? 18.44900  -20.54500 -10.02700 1.000 57.46740  ? 185 ILE   A O   1 
ATOM   1188 C  CB  . ILE   A 1 149 ? 21.70700  -19.22600 -9.92100  1.000 65.07126  ? 185 ILE   A CB  1 
ATOM   1189 C  CG1 . ILE   A 1 149 ? 22.09100  -20.39000 -10.83600 1.000 61.87198  ? 185 ILE   A CG1 1 
ATOM   1190 C  CG2 . ILE   A 1 149 ? 22.87100  -18.90800 -8.99600  1.000 62.84944  ? 185 ILE   A CG2 1 
ATOM   1191 C  CD1 . ILE   A 1 149 ? 21.56900  -20.26800 -12.24800 1.000 67.49537  ? 185 ILE   A CD1 1 
ATOM   1192 N  N   . ASP   A 1 150 ? 18.95400  -18.44000 -10.66500 1.000 62.71033  ? 186 ASP   A N   1 
ATOM   1193 C  CA  . ASP   A 1 150 ? 17.86700  -18.29600 -11.63000 1.000 66.00269  ? 186 ASP   A CA  1 
ATOM   1194 C  C   . ASP   A 1 150 ? 16.50300  -18.49200 -10.97700 1.000 68.11739  ? 186 ASP   A C   1 
ATOM   1195 O  O   . ASP   A 1 150 ? 15.98300  -19.61200 -10.92200 1.000 60.16127  ? 186 ASP   A O   1 
ATOM   1196 C  CB  . ASP   A 1 150 ? 18.05000  -19.27200 -12.79500 1.000 69.90714  ? 186 ASP   A CB  1 
ATOM   1197 C  CG  . ASP   A 1 150 ? 17.30000  -18.84500 -14.04000 1.000 81.97121  ? 186 ASP   A CG  1 
ATOM   1198 O  OD1 . ASP   A 1 150 ? 16.08500  -18.57400 -13.94900 1.000 87.96629  ? 186 ASP   A OD1 1 
ATOM   1199 O  OD2 . ASP   A 1 150 ? 17.93100  -18.77700 -15.11300 1.000 100.57119 ? 186 ASP   A OD2 1 
ATOM   1200 N  N   . PHE   A 1 151 ? 15.90600  -17.40200 -10.50100 1.000 66.64005  ? 187 PHE   A N   1 
ATOM   1201 C  CA  . PHE   A 1 151 ? 14.60300  -17.42700 -9.84800  1.000 64.40076  ? 187 PHE   A CA  1 
ATOM   1202 C  C   . PHE   A 1 151 ? 13.55000  -16.68800 -10.67200 1.000 70.97604  ? 187 PHE   A C   1 
ATOM   1203 O  O   . PHE   A 1 151 ? 12.63100  -16.06600 -10.13100 1.000 69.98788  ? 187 PHE   A O   1 
ATOM   1204 C  CB  . PHE   A 1 151 ? 14.69600  -16.84200 -8.44200  1.000 61.46335  ? 187 PHE   A CB  1 
ATOM   1205 C  CG  . PHE   A 1 151 ? 15.51100  -17.67600 -7.49600  1.000 65.90478  ? 187 PHE   A CG  1 
ATOM   1206 C  CD1 . PHE   A 1 151 ? 14.91800  -18.69000 -6.76200  1.000 60.77538  ? 187 PHE   A CD1 1 
ATOM   1207 C  CD2 . PHE   A 1 151 ? 16.87100  -17.45200 -7.33900  1.000 63.45039  ? 187 PHE   A CD2 1 
ATOM   1208 C  CE1 . PHE   A 1 151 ? 15.66200  -19.46300 -5.89100  1.000 62.76167  ? 187 PHE   A CE1 1 
ATOM   1209 C  CE2 . PHE   A 1 151 ? 17.62000  -18.22400 -6.46700  1.000 61.80544  ? 187 PHE   A CE2 1 
ATOM   1210 C  CZ  . PHE   A 1 151 ? 17.01400  -19.23200 -5.74500  1.000 54.26547  ? 187 PHE   A CZ  1 
ATOM   1211 N  N   . GLY   A 1 152 ? 13.67200  -16.75100 -12.00100 1.000 73.92020  ? 188 GLY   A N   1 
ATOM   1212 C  CA  . GLY   A 1 152 ? 12.70800  -16.10100 -12.87300 1.000 76.83564  ? 188 GLY   A CA  1 
ATOM   1213 C  C   . GLY   A 1 152 ? 11.37000  -16.80000 -12.97000 1.000 79.31498  ? 188 GLY   A C   1 
ATOM   1214 O  O   . GLY   A 1 152 ? 10.39900  -16.19500 -13.43500 1.000 75.56193  ? 188 GLY   A O   1 
ATOM   1215 N  N   . MET   A 1 153 ? 11.29200  -18.05600 -12.53600 1.000 72.49081  ? 189 MET   A N   1 
ATOM   1216 C  CA  . MET   A 1 153 ? 10.05300  -18.82000 -12.55200 1.000 67.69075  ? 189 MET   A CA  1 
ATOM   1217 C  C   . MET   A 1 153 ? 9.46400   -18.99600 -11.16100 1.000 66.84973  ? 189 MET   A C   1 
ATOM   1218 O  O   . MET   A 1 153 ? 8.45600   -19.69300 -11.00900 1.000 62.45201  ? 189 MET   A O   1 
ATOM   1219 C  CB  . MET   A 1 153 ? 10.28900  -20.18700 -13.19800 1.000 73.50956  ? 189 MET   A CB  1 
ATOM   1220 C  CG  . MET   A 1 153 ? 10.74300  -20.10800 -14.64500 1.000 78.07634  ? 189 MET   A CG  1 
ATOM   1221 S  SD  . MET   A 1 153 ? 9.34800   -20.15600 -15.78100 1.000 103.29984 ? 189 MET   A SD  1 
ATOM   1222 C  CE  . MET   A 1 153 ? 9.92700   -19.07800 -17.08700 1.000 87.24874  ? 189 MET   A CE  1 
ATOM   1223 N  N   . ALA   A 1 154 ? 10.06300  -18.37500 -10.14900 1.000 61.46025  ? 190 ALA   A N   1 
ATOM   1224 C  CA  . ALA   A 1 154 ? 9.58400   -18.52100 -8.78400  1.000 65.21544  ? 190 ALA   A CA  1 
ATOM   1225 C  C   . ALA   A 1 154 ? 8.29300   -17.73700 -8.58000  1.000 65.24093  ? 190 ALA   A C   1 
ATOM   1226 O  O   . ALA   A 1 154 ? 8.05700   -16.70600 -9.21600  1.000 65.80609  ? 190 ALA   A O   1 
ATOM   1227 C  CB  . ALA   A 1 154 ? 10.65000  -18.05000 -7.79300  1.000 60.67038  ? 190 ALA   A CB  1 
ATOM   1228 N  N   . LYS   A 1 155 ? 7.45400   -18.23800 -7.67600  1.000 60.85520  ? 191 LYS   A N   1 
ATOM   1229 C  CA  . LYS   A 1 155 ? 6.17300   -17.61400 -7.38200  1.000 65.75019  ? 191 LYS   A CA  1 
ATOM   1230 C  C   . LYS   A 1 155 ? 5.86300   -17.80600 -5.90500  1.000 65.70967  ? 191 LYS   A C   1 
ATOM   1231 O  O   . LYS   A 1 155 ? 6.19600   -18.84100 -5.32200  1.000 62.45524  ? 191 LYS   A O   1 
ATOM   1232 C  CB  . LYS   A 1 155 ? 5.05400   -18.20300 -8.25500  1.000 62.37836  ? 191 LYS   A CB  1 
ATOM   1233 C  CG  . LYS   A 1 155 ? 3.64400   -17.73800 -7.90400  1.000 75.43887  ? 191 LYS   A CG  1 
ATOM   1234 C  CD  . LYS   A 1 155 ? 2.60100   -18.31100 -8.86300  1.000 78.44053  ? 191 LYS   A CD  1 
ATOM   1235 C  CE  . LYS   A 1 155 ? 2.80800   -17.79100 -10.28300 1.000 88.76340  ? 191 LYS   A CE  1 
ATOM   1236 N  NZ  . LYS   A 1 155 ? 1.82500   -18.34800 -11.26000 1.000 86.36677  ? 191 LYS   A NZ  1 
ATOM   1237 N  N   . GLN   A 1 156 ? 5.24000   -16.79600 -5.30500  1.000 65.78727  ? 192 GLN   A N   1 
ATOM   1238 C  CA  . GLN   A 1 156 ? 4.81700   -16.88800 -3.91300  1.000 69.58056  ? 192 GLN   A CA  1 
ATOM   1239 C  C   . GLN   A 1 156 ? 3.66100   -17.87500 -3.79000  1.000 67.75912  ? 192 GLN   A C   1 
ATOM   1240 O  O   . GLN   A 1 156 ? 2.64600   -17.74000 -4.48200  1.000 74.10850  ? 192 GLN   A O   1 
ATOM   1241 C  CB  . GLN   A 1 156 ? 4.41200   -15.50600 -3.40300  1.000 74.70529  ? 192 GLN   A CB  1 
ATOM   1242 C  CG  . GLN   A 1 156 ? 3.77200   -15.50700 -2.03000  1.000 76.58094  ? 192 GLN   A CG  1 
ATOM   1243 C  CD  . GLN   A 1 156 ? 3.45500   -14.10700 -1.53400  1.000 84.01210  ? 192 GLN   A CD  1 
ATOM   1244 O  OE1 . GLN   A 1 156 ? 2.38400   -13.86100 -0.98300  1.000 84.13465  ? 192 GLN   A OE1 1 
ATOM   1245 N  NE2 . GLN   A 1 156 ? 4.39100   -13.18500 -1.72400  1.000 89.86436  ? 192 GLN   A NE2 1 
ATOM   1246 N  N   . TYR   A 1 157 ? 3.81200   -18.87300 -2.91500  1.000 68.77575  ? 193 TYR   A N   1 
ATOM   1247 C  CA  . TYR   A 1 157 ? 2.78700   -19.89200 -2.72500  1.000 68.16322  ? 193 TYR   A CA  1 
ATOM   1248 C  C   . TYR   A 1 157 ? 1.99500   -19.71700 -1.43600  1.000 71.80080  ? 193 TYR   A C   1 
ATOM   1249 O  O   . TYR   A 1 157 ? 1.03300   -20.46200 -1.21600  1.000 73.20793  ? 193 TYR   A O   1 
ATOM   1250 C  CB  . TYR   A 1 157 ? 3.41300   -21.29500 -2.74300  1.000 52.52863  ? 193 TYR   A CB  1 
ATOM   1251 C  CG  . TYR   A 1 157 ? 4.17100   -21.65100 -1.48300  1.000 63.29015  ? 193 TYR   A CG  1 
ATOM   1252 C  CD1 . TYR   A 1 157 ? 5.50000   -21.28200 -1.31900  1.000 65.36331  ? 193 TYR   A CD1 1 
ATOM   1253 C  CD2 . TYR   A 1 157 ? 3.56000   -22.36400 -0.45900  1.000 60.20667  ? 193 TYR   A CD2 1 
ATOM   1254 C  CE1 . TYR   A 1 157 ? 6.19600   -21.60900 -0.16800  1.000 61.87154  ? 193 TYR   A CE1 1 
ATOM   1255 C  CE2 . TYR   A 1 157 ? 4.24400   -22.69100 0.69500   1.000 62.90334  ? 193 TYR   A CE2 1 
ATOM   1256 C  CZ  . TYR   A 1 157 ? 5.56100   -22.31200 0.83600   1.000 65.09655  ? 193 TYR   A CZ  1 
ATOM   1257 O  OH  . TYR   A 1 157 ? 6.24200   -22.64000 1.98700   1.000 62.08622  ? 193 TYR   A OH  1 
ATOM   1258 N  N   . ARG   A 1 158 ? 2.37200   -18.76900 -0.58100  1.000 67.77286  ? 194 ARG   A N   1 
ATOM   1259 C  CA  . ARG   A 1 158 ? 1.65200   -18.53800 0.66300   1.000 71.48397  ? 194 ARG   A CA  1 
ATOM   1260 C  C   . ARG   A 1 158 ? 1.90200   -17.10900 1.11600   1.000 77.56346  ? 194 ARG   A C   1 
ATOM   1261 O  O   . ARG   A 1 158 ? 2.94400   -16.52200 0.81100   1.000 83.02095  ? 194 ARG   A O   1 
ATOM   1262 C  CB  . ARG   A 1 158 ? 2.07200   -19.52700 1.75600   1.000 77.94505  ? 194 ARG   A CB  1 
ATOM   1263 C  CG  . ARG   A 1 158 ? 3.50000   -19.36000 2.24800   1.000 73.22233  ? 194 ARG   A CG  1 
ATOM   1264 C  CD  . ARG   A 1 158 ? 3.82200   -20.37700 3.33200   1.000 74.51050  ? 194 ARG   A CD  1 
ATOM   1265 N  NE  . ARG   A 1 158 ? 5.16000   -20.19100 3.88000   1.000 77.04014  ? 194 ARG   A NE  1 
ATOM   1266 C  CZ  . ARG   A 1 158 ? 5.70200   -20.96300 4.81200   1.000 77.88914  ? 194 ARG   A CZ  1 
ATOM   1267 N  NH1 . ARG   A 1 158 ? 5.04900   -21.99600 5.32000   1.000 76.92288  ? 194 ARG   A NH1 1 
ATOM   1268 N  NH2 . ARG   A 1 158 ? 6.92800   -20.68900 5.25000   1.000 75.99520  ? 194 ARG   A NH2 1 
ATOM   1269 N  N   . ASP   A 1 159 ? 0.93900   -16.56200 1.84500   1.000 84.82381  ? 195 ASP   A N   1 
ATOM   1270 C  CA  . ASP   A 1 159 ? 1.04100   -15.18500 2.30400   1.000 84.40777  ? 195 ASP   A CA  1 
ATOM   1271 C  C   . ASP   A 1 159 ? 2.21500   -15.03900 3.26800   1.000 89.34552  ? 195 ASP   A C   1 
ATOM   1272 O  O   . ASP   A 1 159 ? 2.34100   -15.83500 4.20900   1.000 90.70499  ? 195 ASP   A O   1 
ATOM   1273 C  CB  . ASP   A 1 159 ? -0.25700  -14.76300 2.98400   1.000 90.01927  ? 195 ASP   A CB  1 
ATOM   1274 C  CG  . ASP   A 1 159 ? -0.21900  -13.33700 3.46300   1.000 91.98146  ? 195 ASP   A CG  1 
ATOM   1275 O  OD1 . ASP   A 1 159 ? -0.40100  -12.42800 2.62800   1.000 97.58123  ? 195 ASP   A OD1 1 
ATOM   1276 O  OD2 . ASP   A 1 159 ? 0.00400   -13.12300 4.67100   1.000 98.44419  ? 195 ASP   A OD2 1 
ATOM   1277 N  N   . PRO   A 1 160 ? 3.09100   -14.04600 3.07600   1.000 93.49864  ? 196 PRO   A N   1 
ATOM   1278 C  CA  . PRO   A 1 160 ? 4.26200   -13.91600 3.95800   1.000 91.66479  ? 196 PRO   A CA  1 
ATOM   1279 C  C   . PRO   A 1 160 ? 3.90900   -13.56400 5.38800   1.000 97.94617  ? 196 PRO   A C   1 
ATOM   1280 O  O   . PRO   A 1 160 ? 4.81000   -13.54000 6.23800   1.000 101.19348 ? 196 PRO   A O   1 
ATOM   1281 C  CB  . PRO   A 1 160 ? 5.07500   -12.78700 3.30600   1.000 93.41685  ? 196 PRO   A CB  1 
ATOM   1282 C  CG  . PRO   A 1 160 ? 4.54200   -12.68300 1.89500   1.000 90.71514  ? 196 PRO   A CG  1 
ATOM   1283 C  CD  . PRO   A 1 160 ? 3.09600   -13.04300 1.99900   1.000 89.91993  ? 196 PRO   A CD  1 
ATOM   1284 N  N   . ARG   A 1 161 ? 2.64300   -13.27300 5.68000   1.000 98.60288  ? 197 ARG   A N   1 
ATOM   1285 C  CA  . ARG   A 1 161 ? 2.24000   -12.84100 7.01200   1.000 98.50798  ? 197 ARG   A CA  1 
ATOM   1286 C  C   . ARG   A 1 161 ? 1.26600   -13.80900 7.65500   1.000 102.15464 ? 197 ARG   A C   1 
ATOM   1287 O  O   . ARG   A 1 161 ? 1.47400   -14.20000 8.80500   1.000 109.88380 ? 197 ARG   A O   1 
ATOM   1288 C  CB  . ARG   A 1 161 ? 1.62300   -11.42900 6.97800   1.000 100.86195 ? 197 ARG   A CB  1 
ATOM   1289 C  CG  . ARG   A 1 161 ? 1.11200   -10.90500 8.32200   1.000 112.65863 ? 197 ARG   A CG  1 
ATOM   1290 C  CD  . ARG   A 1 161 ? 1.26600   -9.38500  8.34800   1.000 118.56516 ? 197 ARG   A CD  1 
ATOM   1291 N  NE  . ARG   A 1 161 ? 0.79200   -8.81800  9.60300   1.000 125.59451 ? 197 ARG   A NE  1 
ATOM   1292 C  CZ  . ARG   A 1 161 ? 1.55600   -8.75900  10.67900  1.000 124.94591 ? 197 ARG   A CZ  1 
ATOM   1293 N  NH1 . ARG   A 1 161 ? 2.77600   -9.27300  10.67500  1.000 119.23539 ? 197 ARG   A NH1 1 
ATOM   1294 N  NH2 . ARG   A 1 161 ? 1.09800   -8.15600  11.77300  1.000 124.23314 ? 197 ARG   A NH2 1 
ATOM   1295 N  N   . THR   A 1 162 ? 0.21500   -14.21900 6.94000   1.000 100.23305 ? 198 THR   A N   1 
ATOM   1296 C  CA  . THR   A 1 162 ? -0.77800  -15.14700 7.46800   1.000 96.00872  ? 198 THR   A CA  1 
ATOM   1297 C  C   . THR   A 1 162 ? -0.43200  -16.61100 7.21500   1.000 95.69862  ? 198 THR   A C   1 
ATOM   1298 O  O   . THR   A 1 162 ? -1.08800  -17.48900 7.78500   1.000 98.84285  ? 198 THR   A O   1 
ATOM   1299 C  CB  . THR   A 1 162 ? -2.15300  -14.84700 6.86200   1.000 91.81023  ? 198 THR   A CB  1 
ATOM   1300 O  OG1 . THR   A 1 162 ? -2.17700  -15.28700 5.49800   1.000 87.05601  ? 198 THR   A OG1 1 
ATOM   1301 C  CG2 . THR   A 1 162 ? -2.43600  -13.35300 6.90500   1.000 92.60681  ? 198 THR   A CG2 1 
ATOM   1302 N  N   . LYS   A 1 163 ? 0.56200   -16.88900 6.36700   1.000 91.17254  ? 199 LYS   A N   1 
ATOM   1303 C  CA  . LYS   A 1 163 ? 0.98700   -18.25600 6.04600   1.000 91.88296  ? 199 LYS   A CA  1 
ATOM   1304 C  C   . LYS   A 1 163 ? -0.15500  -19.08500 5.46100   1.000 88.30969  ? 199 LYS   A C   1 
ATOM   1305 O  O   . LYS   A 1 163 ? -0.24200  -20.29500 5.68100   1.000 87.33249  ? 199 LYS   A O   1 
ATOM   1306 C  CB  . LYS   A 1 163 ? 1.58900   -18.95300 7.26900   1.000 94.98583  ? 199 LYS   A CB  1 
ATOM   1307 C  CG  . LYS   A 1 163 ? 2.91600   -18.37500 7.70000   1.000 94.44497  ? 199 LYS   A CG  1 
ATOM   1308 C  CD  . LYS   A 1 163 ? 3.96200   -18.60500 6.63000   1.000 92.24782  ? 199 LYS   A CD  1 
ATOM   1309 C  CE  . LYS   A 1 163 ? 4.94400   -17.46100 6.60500   1.000 88.65810  ? 199 LYS   A CE  1 
ATOM   1310 N  NZ  . LYS   A 1 163 ? 4.20600   -16.17800 6.66000   1.000 99.21008  ? 199 LYS   A NZ  1 
ATOM   1311 N  N   . GLN   A 1 164 ? -1.03300  -18.43800 4.70000   1.000 83.36764  ? 200 GLN   A N   1 
ATOM   1312 C  CA  . GLN   A 1 164 ? -2.13900  -19.13300 4.05600   1.000 83.11419  ? 200 GLN   A CA  1 
ATOM   1313 C  C   . GLN   A 1 164 ? -1.74000  -19.57200 2.65200   1.000 78.00472  ? 200 GLN   A C   1 
ATOM   1314 O  O   . GLN   A 1 164 ? -1.32100  -18.74900 1.83400   1.000 83.31390  ? 200 GLN   A O   1 
ATOM   1315 C  CB  . GLN   A 1 164 ? -3.38000  -18.24700 3.99000   1.000 86.16370  ? 200 GLN   A CB  1 
ATOM   1316 C  CG  . GLN   A 1 164 ? -4.44400  -18.81100 3.07600   1.000 85.07274  ? 200 GLN   A CG  1 
ATOM   1317 C  CD  . GLN   A 1 164 ? -5.83600  -18.61100 3.61900   1.000 94.35887  ? 200 GLN   A CD  1 
ATOM   1318 O  OE1 . GLN   A 1 164 ? -6.11500  -17.62300 4.29800   1.000 103.11908 ? 200 GLN   A OE1 1 
ATOM   1319 N  NE2 . GLN   A 1 164 ? -6.72500  -19.55400 3.32300   1.000 100.21845 ? 200 GLN   A NE2 1 
ATOM   1320 N  N   . HIS   A 1 165 ? -1.88700  -20.86700 2.37800   1.000 80.57849  ? 201 HIS   A N   1 
ATOM   1321 C  CA  . HIS   A 1 165 ? -1.50100  -21.42300 1.08800   1.000 76.29528  ? 201 HIS   A CA  1 
ATOM   1322 C  C   . HIS   A 1 165 ? -2.39700  -20.88700 -0.02300  1.000 76.63260  ? 201 HIS   A C   1 
ATOM   1323 O  O   . HIS   A 1 165 ? -3.57300  -20.57800 0.19000   1.000 77.01429  ? 201 HIS   A O   1 
ATOM   1324 C  CB  . HIS   A 1 165 ? -1.57900  -22.95000 1.12800   1.000 76.24150  ? 201 HIS   A CB  1 
ATOM   1325 C  CG  . HIS   A 1 165 ? -0.75200  -23.63400 0.08100   1.000 74.58554  ? 201 HIS   A CG  1 
ATOM   1326 N  ND1 . HIS   A 1 165 ? -1.13900  -23.71500 -1.24000  1.000 71.10549  ? 201 HIS   A ND1 1 
ATOM   1327 C  CD2 . HIS   A 1 165 ? 0.43000   -24.29000 0.16700   1.000 63.02959  ? 201 HIS   A CD2 1 
ATOM   1328 C  CE1 . HIS   A 1 165 ? -0.22500  -24.38100 -1.92400  1.000 69.79520  ? 201 HIS   A CE1 1 
ATOM   1329 N  NE2 . HIS   A 1 165 ? 0.73600   -24.74200 -1.09400  1.000 63.68012  ? 201 HIS   A NE2 1 
ATOM   1330 N  N   . ILE   A 1 166 ? -1.82600  -20.77800 -1.21900  1.000 72.30035  ? 202 ILE   A N   1 
ATOM   1331 C  CA  . ILE   A 1 166 ? -2.56100  -20.30000 -2.38600  1.000 77.20374  ? 202 ILE   A CA  1 
ATOM   1332 C  C   . ILE   A 1 166 ? -3.64600  -21.31700 -2.72000  1.000 77.13303  ? 202 ILE   A C   1 
ATOM   1333 O  O   . ILE   A 1 166 ? -3.49100  -22.50700 -2.40500  1.000 75.42855  ? 202 ILE   A O   1 
ATOM   1334 C  CB  . ILE   A 1 166 ? -1.62500  -20.06000 -3.58200  1.000 71.79153  ? 202 ILE   A CB  1 
ATOM   1335 C  CG1 . ILE   A 1 166 ? -0.74700  -21.29100 -3.83200  1.000 74.13768  ? 202 ILE   A CG1 1 
ATOM   1336 C  CG2 . ILE   A 1 166 ? -0.78200  -18.81500 -3.35500  1.000 68.01372  ? 202 ILE   A CG2 1 
ATOM   1337 C  CD1 . ILE   A 1 166 ? 0.12600   -21.17600 -5.06500  1.000 65.98973  ? 202 ILE   A CD1 1 
ATOM   1338 N  N   . PRO   A 1 167 ? -4.75500  -20.90800 -3.33400  1.000 76.42529  ? 203 PRO   A N   1 
ATOM   1339 C  CA  . PRO   A 1 167 ? -5.79400  -21.88100 -3.68100  1.000 82.40234  ? 203 PRO   A CA  1 
ATOM   1340 C  C   . PRO   A 1 167 ? -5.34000  -22.80100 -4.80200  1.000 78.80568  ? 203 PRO   A C   1 
ATOM   1341 O  O   . PRO   A 1 167 ? -4.50000  -22.44800 -5.63500  1.000 70.86273  ? 203 PRO   A O   1 
ATOM   1342 C  CB  . PRO   A 1 167 ? -6.97100  -21.00500 -4.12100  1.000 78.30294  ? 203 PRO   A CB  1 
ATOM   1343 C  CG  . PRO   A 1 167 ? -6.33600  -19.74700 -4.59300  1.000 85.09238  ? 203 PRO   A CG  1 
ATOM   1344 C  CD  . PRO   A 1 167 ? -5.13800  -19.53600 -3.70600  1.000 78.08364  ? 203 PRO   A CD  1 
ATOM   1345 N  N   . TYR   A 1 168 ? -5.91000  -24.00100 -4.80400  1.000 78.70744  ? 204 TYR   A N   1 
ATOM   1346 C  CA  . TYR   A 1 168 ? -5.64200  -24.98000 -5.84300  1.000 74.14386  ? 204 TYR   A CA  1 
ATOM   1347 C  C   . TYR   A 1 168 ? -6.44900  -24.64900 -7.09200  1.000 82.81176  ? 204 TYR   A C   1 
ATOM   1348 O  O   . TYR   A 1 168 ? -7.65600  -24.40100 -7.01300  1.000 75.91950  ? 204 TYR   A O   1 
ATOM   1349 C  CB  . TYR   A 1 168 ? -5.98900  -26.38200 -5.33900  1.000 70.15191  ? 204 TYR   A CB  1 
ATOM   1350 C  CG  . TYR   A 1 168 ? -5.99200  -27.45700 -6.40100  1.000 69.52641  ? 204 TYR   A CG  1 
ATOM   1351 C  CD1 . TYR   A 1 168 ? -4.80400  -28.01000 -6.85800  1.000 75.39549  ? 204 TYR   A CD1 1 
ATOM   1352 C  CD2 . TYR   A 1 168 ? -7.18400  -27.93300 -6.93200  1.000 75.91199  ? 204 TYR   A CD2 1 
ATOM   1353 C  CE1 . TYR   A 1 168 ? -4.80200  -28.99700 -7.82200  1.000 75.19050  ? 204 TYR   A CE1 1 
ATOM   1354 C  CE2 . TYR   A 1 168 ? -7.19200  -28.91800 -7.89800  1.000 75.74853  ? 204 TYR   A CE2 1 
ATOM   1355 C  CZ  . TYR   A 1 168 ? -5.99800  -29.44600 -8.33800  1.000 79.76916  ? 204 TYR   A CZ  1 
ATOM   1356 O  OH  . TYR   A 1 168 ? -5.99600  -30.42900 -9.30000  1.000 83.89242  ? 204 TYR   A OH  1 
ATOM   1357 N  N   . ARG   A 1 169 ? -5.77800  -24.62400 -8.24300  1.000 82.41581  ? 205 ARG   A N   1 
ATOM   1358 C  CA  . ARG   A 1 169 ? -6.44300  -24.41600 -9.52100  1.000 78.86692  ? 205 ARG   A CA  1 
ATOM   1359 C  C   . ARG   A 1 169 ? -5.82500  -25.34300 -10.55700 1.000 82.87971  ? 205 ARG   A C   1 
ATOM   1360 O  O   . ARG   A 1 169 ? -4.80800  -25.99900 -10.31300 1.000 81.52164  ? 205 ARG   A O   1 
ATOM   1361 C  CB  . ARG   A 1 169 ? -6.35200  -22.95600 -9.98700  1.000 82.30075  ? 205 ARG   A CB  1 
ATOM   1362 C  CG  . ARG   A 1 169 ? -4.93300  -22.47700 -10.24800 1.000 87.70517  ? 205 ARG   A CG  1 
ATOM   1363 C  CD  . ARG   A 1 169 ? -4.90600  -21.14400 -10.98700 1.000 92.69444  ? 205 ARG   A CD  1 
ATOM   1364 N  NE  . ARG   A 1 169 ? -5.05000  -21.30200 -12.43000 1.000 98.42256  ? 205 ARG   A NE  1 
ATOM   1365 C  CZ  . ARG   A 1 169 ? -4.98200  -20.30500 -13.30300 1.000 106.70296 ? 205 ARG   A CZ  1 
ATOM   1366 N  NH1 . ARG   A 1 169 ? -4.77200  -19.05800 -12.91300 1.000 110.22539 ? 205 ARG   A NH1 1 
ATOM   1367 N  NH2 . ARG   A 1 169 ? -5.12600  -20.56500 -14.59900 1.000 108.76606 ? 205 ARG   A NH2 1 
ATOM   1368 N  N   . GLU   A 1 170 ? -6.45400  -25.39000 -11.72400 1.000 84.79451  ? 206 GLU   A N   1 
ATOM   1369 C  CA  . GLU   A 1 170 ? -6.01300  -26.25100 -12.81400 1.000 84.22533  ? 206 GLU   A CA  1 
ATOM   1370 C  C   . GLU   A 1 170 ? -6.02200  -25.42600 -14.09900 1.000 87.10004  ? 206 GLU   A C   1 
ATOM   1371 O  O   . GLU   A 1 170 ? -6.07400  -24.19000 -14.07700 1.000 91.17775  ? 206 GLU   A O   1 
ATOM   1372 C  CB  . GLU   A 1 170 ? -6.90100  -27.49800 -12.90300 1.000 85.38963  ? 206 GLU   A CB  1 
ATOM   1373 C  CG  . GLU   A 1 170 ? -6.91400  -28.34300 -11.64000 1.000 81.78411  ? 206 GLU   A CG  1 
ATOM   1374 C  CD  . GLU   A 1 170 ? -7.84300  -29.53300 -11.74700 1.000 87.04910  ? 206 GLU   A CD  1 
ATOM   1375 O  OE1 . GLU   A 1 170 ? -8.52600  -29.66200 -12.78400 1.000 89.61790  ? 206 GLU   A OE1 1 
ATOM   1376 O  OE2 . GLU   A 1 170 ? -7.88900  -30.34000 -10.79500 1.000 88.15832  ? 206 GLU   A OE2 1 
ATOM   1377 N  N   . LYS   A 1 171 ? -5.97000  -26.11800 -15.24100 1.000 84.45714  ? 207 LYS   A N   1 
ATOM   1378 C  CA  . LYS   A 1 171 ? -6.04800  -25.49400 -16.56400 1.000 95.25086  ? 207 LYS   A CA  1 
ATOM   1379 C  C   . LYS   A 1 171 ? -4.93600  -24.47000 -16.78300 1.000 97.70532  ? 207 LYS   A C   1 
ATOM   1380 O  O   . LYS   A 1 171 ? -5.11400  -23.49100 -17.51200 1.000 103.46917 ? 207 LYS   A O   1 
ATOM   1381 C  CB  . LYS   A 1 171 ? -7.41600  -24.84100 -16.79500 1.000 93.21883  ? 207 LYS   A CB  1 
ATOM   1382 C  CG  . LYS   A 1 171 ? -8.61700  -25.67400 -16.35000 1.000 103.31947 ? 207 LYS   A CG  1 
ATOM   1383 C  CD  . LYS   A 1 171 ? -8.82200  -26.91300 -17.21200 1.000 108.38421 ? 207 LYS   A CD  1 
ATOM   1384 C  CE  . LYS   A 1 171 ? -10.10400 -27.64300 -16.81400 1.000 113.41578 ? 207 LYS   A CE  1 
ATOM   1385 N  NZ  . LYS   A 1 171 ? -10.20100 -29.01400 -17.39100 1.000 110.97443 ? 207 LYS   A NZ  1 
ATOM   1386 N  N   . LYS   A 1 172 ? -3.78500  -24.67900 -16.15500 1.000 93.97149  ? 208 LYS   A N   1 
ATOM   1387 C  CA  . LYS   A 1 172 ? -2.65700  -23.77500 -16.30900 1.000 98.22577  ? 208 LYS   A CA  1 
ATOM   1388 C  C   . LYS   A 1 172 ? -1.75500  -24.23800 -17.44800 1.000 105.00775 ? 208 LYS   A C   1 
ATOM   1389 O  O   . LYS   A 1 172 ? -1.78300  -25.39700 -17.86900 1.000 104.78397 ? 208 LYS   A O   1 
ATOM   1390 C  CB  . LYS   A 1 172 ? -1.85600  -23.68000 -15.01100 1.000 96.16151  ? 208 LYS   A CB  1 
ATOM   1391 C  CG  . LYS   A 1 172 ? -2.67200  -23.21800 -13.81700 1.000 95.37607  ? 208 LYS   A CG  1 
ATOM   1392 C  CD  . LYS   A 1 172 ? -1.83000  -23.17700 -12.55400 1.000 92.09028  ? 208 LYS   A CD  1 
ATOM   1393 C  CE  . LYS   A 1 172 ? -0.84500  -22.02000 -12.57300 1.000 93.68491  ? 208 LYS   A CE  1 
ATOM   1394 N  NZ  . LYS   A 1 172 ? -1.53600  -20.70000 -12.52700 1.000 99.71212  ? 208 LYS   A NZ  1 
ATOM   1395 N  N   . SER   A 1 173 ? -0.94600  -23.30800 -17.94400 1.000 109.60171 ? 209 SER   A N   1 
ATOM   1396 C  CA  . SER   A 1 173 ? -0.06000  -23.59100 -19.06200 1.000 110.46614 ? 209 SER   A CA  1 
ATOM   1397 C  C   . SER   A 1 173 ? 1.15500   -24.38400 -18.60100 1.000 110.51687 ? 209 SER   A C   1 
ATOM   1398 O  O   . SER   A 1 173 ? 1.70800   -24.13500 -17.52600 1.000 112.01453 ? 209 SER   A O   1 
ATOM   1399 C  CB  . SER   A 1 173 ? 0.37900   -22.28700 -19.72600 1.000 118.21574 ? 209 SER   A CB  1 
ATOM   1400 O  OG  . SER   A 1 173 ? 0.59000   -21.27600 -18.75400 1.000 132.33290 ? 209 SER   A OG  1 
ATOM   1401 N  N   . LEU   A 1 174 ? 1.56600   -25.34900 -19.42200 1.000 110.71573 ? 210 LEU   A N   1 
ATOM   1402 C  CA  . LEU   A 1 174 ? 2.73200   -26.17900 -19.12200 1.000 110.71555 ? 210 LEU   A CA  1 
ATOM   1403 C  C   . LEU   A 1 174 ? 3.99000   -25.36400 -19.38900 1.000 115.18116 ? 210 LEU   A C   1 
ATOM   1404 O  O   . LEU   A 1 174 ? 4.41200   -25.20300 -20.53600 1.000 116.05837 ? 210 LEU   A O   1 
ATOM   1405 C  CB  . LEU   A 1 174 ? 2.72500   -27.45700 -19.95400 1.000 103.99920 ? 210 LEU   A CB  1 
ATOM   1406 C  CG  . LEU   A 1 174 ? 1.68100   -28.52900 -19.63900 1.000 101.12312 ? 210 LEU   A CG  1 
ATOM   1407 C  CD1 . LEU   A 1 174 ? 0.41200   -28.31300 -20.45200 1.000 95.43857  ? 210 LEU   A CD1 1 
ATOM   1408 C  CD2 . LEU   A 1 174 ? 2.25800   -29.91600 -19.88700 1.000 88.44845  ? 210 LEU   A CD2 1 
ATOM   1409 N  N   . SER   A 1 175 ? 4.59500   -24.84700 -18.32400 1.000 118.05910 ? 211 SER   A N   1 
ATOM   1410 C  CA  . SER   A 1 175 ? 5.82600   -24.07600 -18.41300 1.000 118.03480 ? 211 SER   A CA  1 
ATOM   1411 C  C   . SER   A 1 175 ? 6.89500   -24.74600 -17.56400 1.000 118.43258 ? 211 SER   A C   1 
ATOM   1412 O  O   . SER   A 1 175 ? 6.65100   -25.07900 -16.39900 1.000 109.88361 ? 211 SER   A O   1 
ATOM   1413 C  CB  . SER   A 1 175 ? 5.60700   -22.63000 -17.96000 1.000 122.13046 ? 211 SER   A CB  1 
ATOM   1414 O  OG  . SER   A 1 175 ? 4.71700   -21.95500 -18.83300 1.000 129.95464 ? 211 SER   A OG  1 
ATOM   1415 N  N   . GLY   A 1 176 ? 8.06900   -24.94300 -18.15000 1.000 106.72076 ? 212 GLY   A N   1 
ATOM   1416 C  CA  . GLY   A 1 176 ? 9.18400   -25.58100 -17.49100 1.000 89.27593  ? 212 GLY   A CA  1 
ATOM   1417 C  C   . GLY   A 1 176 ? 9.86800   -26.54000 -18.43800 1.000 84.57808  ? 212 GLY   A C   1 
ATOM   1418 O  O   . GLY   A 1 176 ? 9.65200   -26.51000 -19.64900 1.000 84.10461  ? 212 GLY   A O   1 
ATOM   1419 N  N   . THR   A 1 177 ? 10.71100  -27.40200 -17.87400 1.000 78.55722  ? 213 THR   A N   1 
ATOM   1420 C  CA  . THR   A 1 177 ? 11.41200  -28.42400 -18.63900 1.000 69.97251  ? 213 THR   A CA  1 
ATOM   1421 C  C   . THR   A 1 177 ? 10.71400  -29.75900 -18.42400 1.000 63.47397  ? 213 THR   A C   1 
ATOM   1422 O  O   . THR   A 1 177 ? 10.62100  -30.24200 -17.28800 1.000 59.93488  ? 213 THR   A O   1 
ATOM   1423 C  CB  . THR   A 1 177 ? 12.88000  -28.52600 -18.23000 1.000 66.34833  ? 213 THR   A CB  1 
ATOM   1424 O  OG1 . THR   A 1 177 ? 13.00200  -29.43700 -17.13100 1.000 69.09257  ? 213 THR   A OG1 1 
ATOM   1425 C  CG2 . THR   A 1 177 ? 13.40900  -27.16500 -17.81400 1.000 59.35126  ? 213 THR   A CG2 1 
ATOM   1426 N  N   . ALA   A 1 178 ? 10.24800  -30.36000 -19.51800 1.000 62.73391  ? 214 ALA   A N   1 
ATOM   1427 C  CA  . ALA   A 1 178 ? 9.43200   -31.56400 -19.43200 1.000 66.41907  ? 214 ALA   A CA  1 
ATOM   1428 C  C   . ALA   A 1 178 ? 10.19900  -32.76600 -18.89700 1.000 56.00756  ? 214 ALA   A C   1 
ATOM   1429 O  O   . ALA   A 1 178 ? 9.57300   -33.71600 -18.41500 1.000 58.69463  ? 214 ALA   A O   1 
ATOM   1430 C  CB  . ALA   A 1 178 ? 8.84600   -31.89600 -20.80500 1.000 72.44042  ? 214 ALA   A CB  1 
ATOM   1431 N  N   . ARG   A 1 179 ? 11.53000  -32.76000 -18.97300 1.000 51.06999  ? 215 ARG   A N   1 
ATOM   1432 C  CA  . ARG   A 1 179 ? 12.27500  -33.93000 -18.52500 1.000 54.31748  ? 215 ARG   A CA  1 
ATOM   1433 C  C   . ARG   A 1 179 ? 12.16200  -34.12900 -17.01800 1.000 48.96562  ? 215 ARG   A C   1 
ATOM   1434 O  O   . ARG   A 1 179 ? 12.15100  -35.27300 -16.54600 1.000 52.01219  ? 215 ARG   A O   1 
ATOM   1435 C  CB  . ARG   A 1 179 ? 13.74000  -33.81500 -18.94300 1.000 47.43870  ? 215 ARG   A CB  1 
ATOM   1436 C  CG  . ARG   A 1 179 ? 14.53700  -35.09200 -18.73800 1.000 48.87861  ? 215 ARG   A CG  1 
ATOM   1437 C  CD  . ARG   A 1 179 ? 16.02100  -34.83500 -18.92100 1.000 54.13209  ? 215 ARG   A CD  1 
ATOM   1438 N  NE  . ARG   A 1 179 ? 16.33800  -34.38300 -20.27100 1.000 54.70602  ? 215 ARG   A NE  1 
ATOM   1439 C  CZ  . ARG   A 1 179 ? 17.55400  -34.05400 -20.67900 1.000 56.77863  ? 215 ARG   A CZ  1 
ATOM   1440 N  NH1 . ARG   A 1 179 ? 18.59000  -34.08300 -19.85700 1.000 54.00852  ? 215 ARG   A NH1 1 
ATOM   1441 N  NH2 . ARG   A 1 179 ? 17.73700  -33.68900 -21.94500 1.000 51.66692  ? 215 ARG   A NH2 1 
ATOM   1442 N  N   . TYR   A 1 180 ? 12.04300  -33.04400 -16.25100 1.000 48.40513  ? 216 TYR   A N   1 
ATOM   1443 C  CA  . TYR   A 1 180 ? 12.04900  -33.13500 -14.79900 1.000 44.24438  ? 216 TYR   A CA  1 
ATOM   1444 C  C   . TYR   A 1 180 ? 10.73300  -32.75000 -14.12600 1.000 48.48405  ? 216 TYR   A C   1 
ATOM   1445 O  O   . TYR   A 1 180 ? 10.53700  -33.12100 -12.96300 1.000 40.46419  ? 216 TYR   A O   1 
ATOM   1446 C  CB  . TYR   A 1 180 ? 13.18100  -32.26500 -14.22000 1.000 44.11504  ? 216 TYR   A CB  1 
ATOM   1447 C  CG  . TYR   A 1 180 ? 14.51300  -32.48400 -14.92000 1.000 41.98933  ? 216 TYR   A CG  1 
ATOM   1448 C  CD1 . TYR   A 1 180 ? 15.24000  -33.65200 -14.72600 1.000 42.34509  ? 216 TYR   A CD1 1 
ATOM   1449 C  CD2 . TYR   A 1 180 ? 15.03500  -31.52800 -15.78500 1.000 47.93568  ? 216 TYR   A CD2 1 
ATOM   1450 C  CE1 . TYR   A 1 180 ? 16.45500  -33.86000 -15.36800 1.000 47.88919  ? 216 TYR   A CE1 1 
ATOM   1451 C  CE2 . TYR   A 1 180 ? 16.25000  -31.72800 -16.43400 1.000 49.87229  ? 216 TYR   A CE2 1 
ATOM   1452 C  CZ  . TYR   A 1 180 ? 16.95300  -32.89800 -16.21800 1.000 45.00416  ? 216 TYR   A CZ  1 
ATOM   1453 O  OH  . TYR   A 1 180 ? 18.15400  -33.10800 -16.86200 1.000 52.70389  ? 216 TYR   A OH  1 
ATOM   1454 N  N   . MET   A 1 181 ? 9.82700   -32.05000 -14.81100 1.000 46.73572  ? 217 MET   A N   1 
ATOM   1455 C  CA  . MET   A 1 181 ? 8.67300   -31.45800 -14.14000 1.000 51.21149  ? 217 MET   A CA  1 
ATOM   1456 C  C   . MET   A 1 181 ? 7.76700   -32.53400 -13.54400 1.000 50.16715  ? 217 MET   A C   1 
ATOM   1457 O  O   . MET   A 1 181 ? 7.72000   -33.67700 -14.00900 1.000 44.33856  ? 217 MET   A O   1 
ATOM   1458 C  CB  . MET   A 1 181 ? 7.86800   -30.58800 -15.10700 1.000 54.11486  ? 217 MET   A CB  1 
ATOM   1459 C  CG  . MET   A 1 181 ? 7.18200   -31.37100 -16.21100 1.000 52.15754  ? 217 MET   A CG  1 
ATOM   1460 S  SD  . MET   A 1 181 ? 6.08100   -30.37000 -17.23300 1.000 60.95650  ? 217 MET   A SD  1 
ATOM   1461 C  CE  . MET   A 1 181 ? 7.07500   -28.89400 -17.45000 1.000 74.50798  ? 217 MET   A CE  1 
ATOM   1462 N  N   . SER   A 1 182 ? 7.03800   -32.14900 -12.49700 1.000 48.02667  ? 218 SER   A N   1 
ATOM   1463 C  CA  . SER   A 1 182 ? 6.17600   -33.08300 -11.79000 1.000 51.87938  ? 218 SER   A CA  1 
ATOM   1464 C  C   . SER   A 1 182 ? 5.01600   -33.52900 -12.67500 1.000 56.41382  ? 218 SER   A C   1 
ATOM   1465 O  O   . SER   A 1 182 ? 4.67500   -32.88800 -13.67500 1.000 55.70467  ? 218 SER   A O   1 
ATOM   1466 C  CB  . SER   A 1 182 ? 5.62800   -32.45000 -10.51000 1.000 54.85775  ? 218 SER   A CB  1 
ATOM   1467 O  OG  . SER   A 1 182 ? 4.68100   -31.43700 -10.80900 1.000 51.36701  ? 218 SER   A OG  1 
ATOM   1468 N  N   . ILE   A 1 183 ? 4.40600   -34.65300 -12.28800 1.000 54.99665  ? 219 ILE   A N   1 
ATOM   1469 C  CA  . ILE   A 1 183 ? 3.21500   -35.13000 -12.98500 1.000 57.71658  ? 219 ILE   A CA  1 
ATOM   1470 C  C   . ILE   A 1 183 ? 2.09400   -34.10200 -12.88600 1.000 60.19568  ? 219 ILE   A C   1 
ATOM   1471 O  O   . ILE   A 1 183 ? 1.35000   -33.87900 -13.84800 1.000 62.58255  ? 219 ILE   A O   1 
ATOM   1472 C  CB  . ILE   A 1 183 ? 2.78500   -36.50000 -12.42800 1.000 60.71235  ? 219 ILE   A CB  1 
ATOM   1473 C  CG1 . ILE   A 1 183 ? 3.83200   -37.56600 -12.75700 1.000 57.87152  ? 219 ILE   A CG1 1 
ATOM   1474 C  CG2 . ILE   A 1 183 ? 1.42800   -36.90800 -12.98400 1.000 60.11288  ? 219 ILE   A CG2 1 
ATOM   1475 C  CD1 . ILE   A 1 183 ? 3.46600   -38.95000 -12.26500 1.000 59.52249  ? 219 ILE   A CD1 1 
ATOM   1476 N  N   . ASN   A 1 184 ? 1.96400   -33.44600 -11.72800 1.000 58.74421  ? 220 ASN   A N   1 
ATOM   1477 C  CA  . ASN   A 1 184 ? 0.92600   -32.43100 -11.57500 1.000 59.73442  ? 220 ASN   A CA  1 
ATOM   1478 C  C   . ASN   A 1 184 ? 1.13000   -31.27300 -12.54000 1.000 61.71758  ? 220 ASN   A C   1 
ATOM   1479 O  O   . ASN   A 1 184 ? 0.15500   -30.67400 -13.00700 1.000 52.21428  ? 220 ASN   A O   1 
ATOM   1480 C  CB  . ASN   A 1 184 ? 0.89300   -31.92000 -10.13600 1.000 61.79394  ? 220 ASN   A CB  1 
ATOM   1481 C  CG  . ASN   A 1 184 ? 0.58000   -33.01200 -9.13800  1.000 64.58442  ? 220 ASN   A CG  1 
ATOM   1482 O  OD1 . ASN   A 1 184 ? -0.33100  -33.81300 -9.34200  1.000 58.83030  ? 220 ASN   A OD1 1 
ATOM   1483 N  ND2 . ASN   A 1 184 ? 1.34400   -33.05700 -8.05300  1.000 65.72179  ? 220 ASN   A ND2 1 
ATOM   1484 N  N   . THR   A 1 185 ? 2.38600   -30.94700 -12.85500 1.000 51.53785  ? 221 THR   A N   1 
ATOM   1485 C  CA  . THR   A 1 185 ? 2.65300   -29.88600 -13.81900 1.000 54.67006  ? 221 THR   A CA  1 
ATOM   1486 C  C   . THR   A 1 185 ? 2.23900   -30.30300 -15.22500 1.000 60.56139  ? 221 THR   A C   1 
ATOM   1487 O  O   . THR   A 1 185 ? 1.73800   -29.47900 -16.00100 1.000 67.15623  ? 221 THR   A O   1 
ATOM   1488 C  CB  . THR   A 1 185 ? 4.13300   -29.50700 -13.78200 1.000 53.84890  ? 221 THR   A CB  1 
ATOM   1489 O  OG1 . THR   A 1 185 ? 4.52700   -29.25500 -12.42700 1.000 52.59780  ? 221 THR   A OG1 1 
ATOM   1490 C  CG2 . THR   A 1 185 ? 4.38300   -28.25900 -14.61500 1.000 54.22525  ? 221 THR   A CG2 1 
ATOM   1491 N  N   . HIS   A 1 186 ? 2.44100   -31.57700 -15.57400 1.000 57.57626  ? 222 HIS   A N   1 
ATOM   1492 C  CA  . HIS   A 1 186 ? 1.99100   -32.06000 -16.87500 1.000 60.36274  ? 222 HIS   A CA  1 
ATOM   1493 C  C   . HIS   A 1 186 ? 0.48100   -31.93700 -17.02400 1.000 65.18102  ? 222 HIS   A C   1 
ATOM   1494 O  O   . HIS   A 1 186 ? -0.01900  -31.73300 -18.13600 1.000 62.67267  ? 222 HIS   A O   1 
ATOM   1495 C  CB  . HIS   A 1 186 ? 2.42700   -33.51200 -17.08200 1.000 61.99312  ? 222 HIS   A CB  1 
ATOM   1496 C  CG  . HIS   A 1 186 ? 3.85700   -33.66100 -17.49800 1.000 62.58282  ? 222 HIS   A CG  1 
ATOM   1497 N  ND1 . HIS   A 1 186 ? 4.29200   -33.38500 -18.77600 1.000 70.40676  ? 222 HIS   A ND1 1 
ATOM   1498 C  CD2 . HIS   A 1 186 ? 4.94900   -34.06800 -16.80900 1.000 60.02329  ? 222 HIS   A CD2 1 
ATOM   1499 C  CE1 . HIS   A 1 186 ? 5.59200   -33.60700 -18.85500 1.000 67.40645  ? 222 HIS   A CE1 1 
ATOM   1500 N  NE2 . HIS   A 1 186 ? 6.01500   -34.02300 -17.67600 1.000 62.16257  ? 222 HIS   A NE2 1 
ATOM   1501 N  N   . LEU   A 1 187 ? -0.25700  -32.04300 -15.92100 1.000 57.25518  ? 223 LEU   A N   1 
ATOM   1502 C  CA  . LEU   A 1 187 ? -1.71100  -31.97300 -15.93400 1.000 70.86495  ? 223 LEU   A CA  1 
ATOM   1503 C  C   . LEU   A 1 187 ? -2.23900  -30.55100 -15.78300 1.000 69.03805  ? 223 LEU   A C   1 
ATOM   1504 O  O   . LEU   A 1 187 ? -3.44700  -30.36900 -15.59600 1.000 75.55910  ? 223 LEU   A O   1 
ATOM   1505 C  CB  . LEU   A 1 187 ? -2.28200  -32.86200 -14.82700 1.000 73.16737  ? 223 LEU   A CB  1 
ATOM   1506 C  CG  . LEU   A 1 187 ? -1.84200  -34.32600 -14.88700 1.000 68.90933  ? 223 LEU   A CG  1 
ATOM   1507 C  CD1 . LEU   A 1 187 ? -2.38800  -35.11400 -13.70500 1.000 75.61541  ? 223 LEU   A CD1 1 
ATOM   1508 C  CD2 . LEU   A 1 187 ? -2.27500  -34.95700 -16.20500 1.000 64.57188  ? 223 LEU   A CD2 1 
ATOM   1509 N  N   . GLY   A 1 188 ? -1.37000  -29.54500 -15.86000 1.000 68.76513  ? 224 GLY   A N   1 
ATOM   1510 C  CA  . GLY   A 1 188 ? -1.81000  -28.16800 -15.76200 1.000 79.55341  ? 224 GLY   A CA  1 
ATOM   1511 C  C   . GLY   A 1 188 ? -2.30300  -27.74400 -14.39800 1.000 84.65253  ? 224 GLY   A C   1 
ATOM   1512 O  O   . GLY   A 1 188 ? -2.99700  -26.73000 -14.28900 1.000 88.71998  ? 224 GLY   A O   1 
ATOM   1513 N  N   . ARG   A 1 189 ? -1.96400  -28.48900 -13.35100 1.000 84.00146  ? 225 ARG   A N   1 
ATOM   1514 C  CA  . ARG   A 1 189 ? -2.38700  -28.14400 -12.00400 1.000 87.42710  ? 225 ARG   A CA  1 
ATOM   1515 C  C   . ARG   A 1 189 ? -1.46600  -27.08500 -11.40500 1.000 95.61176  ? 225 ARG   A C   1 
ATOM   1516 O  O   . ARG   A 1 189 ? -0.31100  -26.92500 -11.81100 1.000 97.57863  ? 225 ARG   A O   1 
ATOM   1517 C  CB  . ARG   A 1 189 ? -2.40400  -29.38600 -11.11500 1.000 77.81931  ? 225 ARG   A CB  1 
ATOM   1518 C  CG  . ARG   A 1 189 ? -3.28300  -30.50800 -11.63800 1.000 84.00318  ? 225 ARG   A CG  1 
ATOM   1519 C  CD  . ARG   A 1 189 ? -3.16700  -31.73800 -10.76100 1.000 85.66233  ? 225 ARG   A CD  1 
ATOM   1520 N  NE  . ARG   A 1 189 ? -3.99500  -32.83600 -11.24300 1.000 90.22611  ? 225 ARG   A NE  1 
ATOM   1521 C  CZ  . ARG   A 1 189 ? -4.00400  -34.05100 -10.71200 1.000 92.34804  ? 225 ARG   A CZ  1 
ATOM   1522 N  NH1 . ARG   A 1 189 ? -3.23100  -34.36000 -9.68200  1.000 88.43784  ? 225 ARG   A NH1 1 
ATOM   1523 N  NH2 . ARG   A 1 189 ? -4.80500  -34.97800 -11.22700 1.000 90.83031  ? 225 ARG   A NH2 1 
ATOM   1524 N  N   . GLU   A 1 190 ? -1.99600  -26.35400 -10.42600 1.000 81.33964  ? 226 GLU   A N   1 
ATOM   1525 C  CA  . GLU   A 1 190 ? -1.19400  -25.37100 -9.71100  1.000 74.98124  ? 226 GLU   A CA  1 
ATOM   1526 C  C   . GLU   A 1 190 ? -0.06800  -26.06400 -8.95300  1.000 72.10714  ? 226 GLU   A C   1 
ATOM   1527 O  O   . GLU   A 1 190 ? -0.29100  -27.06900 -8.26900  1.000 58.61458  ? 226 GLU   A O   1 
ATOM   1528 C  CB  . GLU   A 1 190 ? -2.06700  -24.57300 -8.74400  1.000 71.43432  ? 226 GLU   A CB  1 
ATOM   1529 C  CG  . GLU   A 1 190 ? -1.31900  -23.48100 -7.99600  1.000 73.31312  ? 226 GLU   A CG  1 
ATOM   1530 C  CD  . GLU   A 1 190 ? -1.02200  -22.27900 -8.86600  1.000 76.95178  ? 226 GLU   A CD  1 
ATOM   1531 O  OE1 . GLU   A 1 190 ? -1.97400  -21.54900 -9.20900  1.000 86.59775  ? 226 GLU   A OE1 1 
ATOM   1532 O  OE2 . GLU   A 1 190 ? 0.15700   -22.06900 -9.21500  1.000 71.76027  ? 226 GLU   A OE2 1 
ATOM   1533 N  N   . GLN   A 1 191 ? 1.14200   -25.52900 -9.07300  1.000 62.78698  ? 227 GLN   A N   1 
ATOM   1534 C  CA  . GLN   A 1 191 ? 2.29700   -26.11400 -8.41200  1.000 55.71500  ? 227 GLN   A CA  1 
ATOM   1535 C  C   . GLN   A 1 191 ? 2.40500   -25.62100 -6.97400  1.000 53.52087  ? 227 GLN   A C   1 
ATOM   1536 O  O   . GLN   A 1 191 ? 2.00000   -24.50300 -6.64500  1.000 59.14109  ? 227 GLN   A O   1 
ATOM   1537 C  CB  . GLN   A 1 191 ? 3.58200   -25.78600 -9.17300  1.000 54.23017  ? 227 GLN   A CB  1 
ATOM   1538 C  CG  . GLN   A 1 191 ? 3.58500   -26.28100 -10.60500 1.000 56.01802  ? 227 GLN   A CG  1 
ATOM   1539 C  CD  . GLN   A 1 191 ? 4.89200   -26.00400 -11.31300 1.000 61.59463  ? 227 GLN   A CD  1 
ATOM   1540 O  OE1 . GLN   A 1 191 ? 5.96900   -26.10800 -10.72000 1.000 55.75590  ? 227 GLN   A OE1 1 
ATOM   1541 N  NE2 . GLN   A 1 191 ? 4.80700   -25.64200 -12.58800 1.000 55.98988  ? 227 GLN   A NE2 1 
ATOM   1542 N  N   . SER   A 1 192 ? 2.96000   -26.47200 -6.11900  1.000 51.31586  ? 228 SER   A N   1 
ATOM   1543 C  CA  . SER   A 1 192 ? 3.18900   -26.13500 -4.71900  1.000 52.15766  ? 228 SER   A CA  1 
ATOM   1544 C  C   . SER   A 1 192 ? 4.52200   -26.75200 -4.30800  1.000 49.69189  ? 228 SER   A C   1 
ATOM   1545 O  O   . SER   A 1 192 ? 5.33800   -27.14100 -5.15100  1.000 46.06170  ? 228 SER   A O   1 
ATOM   1546 C  CB  . SER   A 1 192 ? 2.01000   -26.59800 -3.84900  1.000 57.53851  ? 228 SER   A CB  1 
ATOM   1547 O  OG  . SER   A 1 192 ? 1.84300   -28.00600 -3.91300  1.000 54.18534  ? 228 SER   A OG  1 
ATOM   1548 N  N   . ARG   A 1 193 ? 4.75600   -26.84500 -2.99600  1.000 48.02737  ? 229 ARG   A N   1 
ATOM   1549 C  CA  . ARG   A 1 193 ? 6.04500   -27.32400 -2.50800  1.000 55.49719  ? 229 ARG   A CA  1 
ATOM   1550 C  C   . ARG   A 1 193 ? 6.32100   -28.75200 -2.95000  1.000 50.95902  ? 229 ARG   A C   1 
ATOM   1551 O  O   . ARG   A 1 193 ? 7.47600   -29.10800 -3.21400  1.000 48.48804  ? 229 ARG   A O   1 
ATOM   1552 C  CB  . ARG   A 1 193 ? 6.10100   -27.22200 -0.98400  1.000 53.79557  ? 229 ARG   A CB  1 
ATOM   1553 C  CG  . ARG   A 1 193 ? 6.24000   -25.80300 -0.46800  1.000 57.28592  ? 229 ARG   A CG  1 
ATOM   1554 C  CD  . ARG   A 1 193 ? 6.09600   -25.74500 1.04300   1.000 58.05636  ? 229 ARG   A CD  1 
ATOM   1555 N  NE  . ARG   A 1 193 ? 4.72600   -26.00400 1.47000   1.000 56.72411  ? 229 ARG   A NE  1 
ATOM   1556 C  CZ  . ARG   A 1 193 ? 4.27900   -25.81900 2.70500   1.000 66.35141  ? 229 ARG   A CZ  1 
ATOM   1557 N  NH1 . ARG   A 1 193 ? 5.07200   -25.37500 3.66700   1.000 58.72205  ? 229 ARG   A NH1 1 
ATOM   1558 N  NH2 . ARG   A 1 193 ? 3.00300   -26.08000 2.98100   1.000 63.41281  ? 229 ARG   A NH2 1 
ATOM   1559 N  N   . ARG   A 1 194 ? 5.27600   -29.57700 -3.04800  1.000 48.39479  ? 230 ARG   A N   1 
ATOM   1560 C  CA  . ARG   A 1 194 ? 5.46300   -30.97300 -3.42400  1.000 50.54451  ? 230 ARG   A CA  1 
ATOM   1561 C  C   . ARG   A 1 194 ? 6.05000   -31.10800 -4.82200  1.000 40.92064  ? 230 ARG   A C   1 
ATOM   1562 O  O   . ARG   A 1 194 ? 6.79000   -32.06000 -5.09300  1.000 47.09250  ? 230 ARG   A O   1 
ATOM   1563 C  CB  . ARG   A 1 194 ? 4.13300   -31.72600 -3.32800  1.000 43.58772  ? 230 ARG   A CB  1 
ATOM   1564 C  CG  . ARG   A 1 194 ? 3.07300   -31.25900 -4.31000  1.000 44.90778  ? 230 ARG   A CG  1 
ATOM   1565 C  CD  . ARG   A 1 194 ? 1.76200   -32.00700 -4.11000  1.000 57.40292  ? 230 ARG   A CD  1 
ATOM   1566 N  NE  . ARG   A 1 194 ? 0.75200   -31.58700 -5.07200  1.000 56.45311  ? 230 ARG   A NE  1 
ATOM   1567 C  CZ  . ARG   A 1 194 ? -0.45800  -32.11900 -5.17500  1.000 58.57802  ? 230 ARG   A CZ  1 
ATOM   1568 N  NH1 . ARG   A 1 194 ? -0.85700  -33.09500 -4.37300  1.000 58.33672  ? 230 ARG   A NH1 1 
ATOM   1569 N  NH2 . ARG   A 1 194 ? -1.29000  -31.65900 -6.10500  1.000 60.16325  ? 230 ARG   A NH2 1 
ATOM   1570 N  N   . ASP   A 1 195 ? 5.74300   -30.17000 -5.71600  1.000 41.22733  ? 231 ASP   A N   1 
ATOM   1571 C  CA  . ASP   A 1 195 ? 6.18800   -30.29600 -7.09700  1.000 42.40943  ? 231 ASP   A CA  1 
ATOM   1572 C  C   . ASP   A 1 195 ? 7.66500   -29.95600 -7.26000  1.000 45.57612  ? 231 ASP   A C   1 
ATOM   1573 O  O   . ASP   A 1 195 ? 8.31800   -30.50400 -8.15400  1.000 42.87464  ? 231 ASP   A O   1 
ATOM   1574 C  CB  . ASP   A 1 195 ? 5.32400   -29.41900 -8.00300  1.000 46.84549  ? 231 ASP   A CB  1 
ATOM   1575 C  CG  . ASP   A 1 195 ? 3.87500   -29.88300 -8.04700  1.000 50.53057  ? 231 ASP   A CG  1 
ATOM   1576 O  OD1 . ASP   A 1 195 ? 3.61000   -30.98200 -8.58300  1.000 50.29349  ? 231 ASP   A OD1 1 
ATOM   1577 O  OD2 . ASP   A 1 195 ? 3.00100   -29.16200 -7.52700  1.000 56.33684  ? 231 ASP   A OD2 1 
ATOM   1578 N  N   . ASP   A 1 196 ? 8.21100   -29.06800 -6.42300  1.000 47.81365  ? 232 ASP   A N   1 
ATOM   1579 C  CA  . ASP   A 1 196 ? 9.65600   -28.85000 -6.44900  1.000 45.47529  ? 232 ASP   A CA  1 
ATOM   1580 C  C   . ASP   A 1 196 ? 10.40300  -30.11100 -6.01900  1.000 44.94663  ? 232 ASP   A C   1 
ATOM   1581 O  O   . ASP   A 1 196 ? 11.44800  -30.44600 -6.59000  1.000 44.98135  ? 232 ASP   A O   1 
ATOM   1582 C  CB  . ASP   A 1 196 ? 10.03900  -27.66300 -5.56000  1.000 40.97469  ? 232 ASP   A CB  1 
ATOM   1583 C  CG  . ASP   A 1 196 ? 9.66200   -26.31100 -6.17000  1.000 49.05624  ? 232 ASP   A CG  1 
ATOM   1584 O  OD1 . ASP   A 1 196 ? 9.43200   -26.23400 -7.39800  1.000 43.55542  ? 232 ASP   A OD1 1 
ATOM   1585 O  OD2 . ASP   A 1 196 ? 9.60900   -25.31800 -5.41300  1.000 42.80723  ? 232 ASP   A OD2 1 
ATOM   1586 N  N   . LEU   A 1 197 ? 9.86400   -30.83800 -5.03200  1.000 46.45341  ? 233 LEU   A N   1 
ATOM   1587 C  CA  . LEU   A 1 197 ? 10.52700  -32.03700 -4.52300  1.000 46.24070  ? 233 LEU   A CA  1 
ATOM   1588 C  C   . LEU   A 1 197 ? 10.38000  -33.22200 -5.47000  1.000 44.43686  ? 233 LEU   A C   1 
ATOM   1589 O  O   . LEU   A 1 197 ? 11.29500  -34.04700 -5.57600  1.000 46.97751  ? 233 LEU   A O   1 
ATOM   1590 C  CB  . LEU   A 1 197 ? 9.97300   -32.41000 -3.14800  1.000 41.30553  ? 233 LEU   A CB  1 
ATOM   1591 C  CG  . LEU   A 1 197 ? 10.09600  -31.36800 -2.03800  1.000 50.11721  ? 233 LEU   A CG  1 
ATOM   1592 C  CD1 . LEU   A 1 197 ? 9.94800   -32.05100 -0.69500  1.000 57.12306  ? 233 LEU   A CD1 1 
ATOM   1593 C  CD2 . LEU   A 1 197 ? 11.41200  -30.62400 -2.12000  1.000 40.81623  ? 233 LEU   A CD2 1 
ATOM   1594 N  N   . GLU   A 1 198 ? 9.23000   -33.35000 -6.13800  1.000 43.02634  ? 234 GLU   A N   1 
ATOM   1595 C  CA  . GLU   A 1 198 ? 9.08100   -34.41200 -7.12800  1.000 44.33651  ? 234 GLU   A CA  1 
ATOM   1596 C  C   . GLU   A 1 198 ? 10.07100  -34.22700 -8.26800  1.000 44.79720  ? 234 GLU   A C   1 
ATOM   1597 O  O   . GLU   A 1 198 ? 10.69300  -35.19400 -8.72500  1.000 44.93598  ? 234 GLU   A O   1 
ATOM   1598 C  CB  . GLU   A 1 198 ? 7.64800   -34.45400 -7.66200  1.000 38.71046  ? 234 GLU   A CB  1 
ATOM   1599 C  CG  . GLU   A 1 198 ? 7.43400   -35.47600 -8.77300  1.000 47.24389  ? 234 GLU   A CG  1 
ATOM   1600 C  CD  . GLU   A 1 198 ? 5.97500   -35.59600 -9.18400  1.000 56.09896  ? 234 GLU   A CD  1 
ATOM   1601 O  OE1 . GLU   A 1 198 ? 5.10300   -35.08600 -8.44800  1.000 51.18404  ? 234 GLU   A OE1 1 
ATOM   1602 O  OE2 . GLU   A 1 198 ? 5.70400   -36.19600 -10.24800 1.000 56.13623  ? 234 GLU   A OE2 1 
ATOM   1603 N  N   . ALA   A 1 199 ? 10.24200  -32.98600 -8.72800  1.000 40.89753  ? 235 ALA   A N   1 
ATOM   1604 C  CA  . ALA   A 1 199 ? 11.20800  -32.71700 -9.78600  1.000 47.97398  ? 235 ALA   A CA  1 
ATOM   1605 C  C   . ALA   A 1 199 ? 12.62000  -33.07500 -9.34100  1.000 41.94682  ? 235 ALA   A C   1 
ATOM   1606 O  O   . ALA   A 1 199 ? 13.39900  -33.64000 -10.11800 1.000 41.82079  ? 235 ALA   A O   1 
ATOM   1607 C  CB  . ALA   A 1 199 ? 11.12600  -31.25100 -10.20900 1.000 46.26695  ? 235 ALA   A CB  1 
ATOM   1608 N  N   . LEU   A 1 200 ? 12.97100  -32.75400 -8.09200  1.000 41.33711  ? 236 LEU   A N   1 
ATOM   1609 C  CA  . LEU   A 1 200 ? 14.24200  -33.21900 -7.54700  1.000 47.05086  ? 236 LEU   A CA  1 
ATOM   1610 C  C   . LEU   A 1 200 ? 14.34700  -34.73700 -7.62900  1.000 42.38033  ? 236 LEU   A C   1 
ATOM   1611 O  O   . LEU   A 1 200 ? 15.39400  -35.27200 -8.00800  1.000 44.08959  ? 236 LEU   A O   1 
ATOM   1612 C  CB  . LEU   A 1 200 ? 14.40500  -32.74700 -6.10100  1.000 41.96509  ? 236 LEU   A CB  1 
ATOM   1613 C  CG  . LEU   A 1 200 ? 14.66800  -31.26100 -5.85300  1.000 41.28867  ? 236 LEU   A CG  1 
ATOM   1614 C  CD1 . LEU   A 1 200 ? 14.56400  -30.96500 -4.37000  1.000 43.32943  ? 236 LEU   A CD1 1 
ATOM   1615 C  CD2 . LEU   A 1 200 ? 16.03200  -30.83600 -6.38800  1.000 35.95268  ? 236 LEU   A CD2 1 
ATOM   1616 N  N   . GLY   A 1 201 ? 13.26800  -35.44800 -7.28600  1.000 43.20152  ? 237 GLY   A N   1 
ATOM   1617 C  CA  . GLY   A 1 201 ? 13.29200  -36.90000 -7.37300  1.000 41.08907  ? 237 GLY   A CA  1 
ATOM   1618 C  C   . GLY   A 1 201 ? 13.57700  -37.40400 -8.77200  1.000 44.21278  ? 237 GLY   A C   1 
ATOM   1619 O  O   . GLY   A 1 201 ? 14.23500  -38.43500 -8.94600  1.000 48.75517  ? 237 GLY   A O   1 
ATOM   1620 N  N   . HIS   A 1 202 ? 13.09200  -36.68700 -9.78700  1.000 42.50797  ? 238 HIS   A N   1 
ATOM   1621 C  CA  . HIS   A 1 202 ? 13.40000  -37.04600 -11.16500 1.000 43.75675  ? 238 HIS   A CA  1 
ATOM   1622 C  C   . HIS   A 1 202 ? 14.87300  -36.81700 -11.47700 1.000 43.73246  ? 238 HIS   A C   1 
ATOM   1623 O  O   . HIS   A 1 202 ? 15.50800  -37.64100 -12.14800 1.000 42.02261  ? 238 HIS   A O   1 
ATOM   1624 C  CB  . HIS   A 1 202 ? 12.51300  -36.24500 -12.11500 1.000 45.29874  ? 238 HIS   A CB  1 
ATOM   1625 C  CG  . HIS   A 1 202 ? 11.05600  -36.56300 -11.98500 1.000 48.18190  ? 238 HIS   A CG  1 
ATOM   1626 N  ND1 . HIS   A 1 202 ? 10.06500  -35.64300 -12.25000 1.000 45.50793  ? 238 HIS   A ND1 1 
ATOM   1627 C  CD2 . HIS   A 1 202 ? 10.42400  -37.70200 -11.61600 1.000 51.89625  ? 238 HIS   A CD2 1 
ATOM   1628 C  CE1 . HIS   A 1 202 ? 8.88500   -36.20200 -12.04900 1.000 54.23847  ? 238 HIS   A CE1 1 
ATOM   1629 N  NE2 . HIS   A 1 202 ? 9.07400   -37.45100 -11.66400 1.000 51.26941  ? 238 HIS   A NE2 1 
ATOM   1630 N  N   . VAL   A 1 203 ? 15.43100  -35.70300 -10.99800 1.000 44.00291  ? 239 VAL   A N   1 
ATOM   1631 C  CA  . VAL   A 1 203 ? 16.84400  -35.41700 -11.21600 1.000 37.57135  ? 239 VAL   A CA  1 
ATOM   1632 C  C   . VAL   A 1 203 ? 17.71600  -36.47000 -10.54700 1.000 38.52046  ? 239 VAL   A C   1 
ATOM   1633 O  O   . VAL   A 1 203 ? 18.74700  -36.87900 -11.09500 1.000 42.20470  ? 239 VAL   A O   1 
ATOM   1634 C  CB  . VAL   A 1 203 ? 17.18600  -34.00400 -10.71000 1.000 35.79987  ? 239 VAL   A CB  1 
ATOM   1635 C  CG1 . VAL   A 1 203 ? 18.65900  -33.69900 -10.95100 1.000 36.45824  ? 239 VAL   A CG1 1 
ATOM   1636 C  CG2 . VAL   A 1 203 ? 16.30700  -32.96800 -11.39100 1.000 44.85155  ? 239 VAL   A CG2 1 
ATOM   1637 N  N   . PHE   A 1 204 ? 17.33300  -36.91100 -9.34600  1.000 36.76080  ? 240 PHE   A N   1 
ATOM   1638 C  CA  . PHE   A 1 204 ? 18.13300  -37.90600 -8.63600  1.000 38.34348  ? 240 PHE   A CA  1 
ATOM   1639 C  C   . PHE   A 1 204 ? 18.24100  -39.19200 -9.44600  1.000 46.25589  ? 240 PHE   A C   1 
ATOM   1640 O  O   . PHE   A 1 204 ? 19.32500  -39.77300 -9.56900  1.000 44.25910  ? 240 PHE   A O   1 
ATOM   1641 C  CB  . PHE   A 1 204 ? 17.53200  -38.19700 -7.25900  1.000 39.87140  ? 240 PHE   A CB  1 
ATOM   1642 C  CG  . PHE   A 1 204 ? 17.41300  -36.99200 -6.37400  1.000 42.81557  ? 240 PHE   A CG  1 
ATOM   1643 C  CD1 . PHE   A 1 204 ? 18.20900  -35.87100 -6.57800  1.000 39.21131  ? 240 PHE   A CD1 1 
ATOM   1644 C  CD2 . PHE   A 1 204 ? 16.49600  -36.97400 -5.33900  1.000 41.67182  ? 240 PHE   A CD2 1 
ATOM   1645 C  CE1 . PHE   A 1 204 ? 18.08900  -34.76200 -5.76500  1.000 39.12400  ? 240 PHE   A CE1 1 
ATOM   1646 C  CE2 . PHE   A 1 204 ? 16.36900  -35.86600 -4.52100  1.000 42.71987  ? 240 PHE   A CE2 1 
ATOM   1647 C  CZ  . PHE   A 1 204 ? 17.16500  -34.75700 -4.73400  1.000 40.58755  ? 240 PHE   A CZ  1 
ATOM   1648 N  N   . PHE   A 1 205 ? 17.12100  -39.65600 -10.01100 1.000 44.65440  ? 241 PHE   A N   1 
ATOM   1649 C  CA  . PHE   A 1 205 ? 17.17700  -40.81500 -10.89600 1.000 43.41288  ? 241 PHE   A CA  1 
ATOM   1650 C  C   . PHE   A 1 205 ? 17.91100  -40.49300 -12.19100 1.000 47.36354  ? 241 PHE   A C   1 
ATOM   1651 O  O   . PHE   A 1 205 ? 18.56800  -41.36900 -12.76500 1.000 42.00774  ? 241 PHE   A O   1 
ATOM   1652 C  CB  . PHE   A 1 205 ? 15.76800  -41.32400 -11.19300 1.000 47.15751  ? 241 PHE   A CB  1 
ATOM   1653 C  CG  . PHE   A 1 205 ? 15.15400  -42.08200 -10.05800 1.000 53.64598  ? 241 PHE   A CG  1 
ATOM   1654 C  CD1 . PHE   A 1 205 ? 15.63400  -43.33200 -9.71000  1.000 47.02669  ? 241 PHE   A CD1 1 
ATOM   1655 C  CD2 . PHE   A 1 205 ? 14.10200  -41.54800 -9.33700  1.000 46.21515  ? 241 PHE   A CD2 1 
ATOM   1656 C  CE1 . PHE   A 1 205 ? 15.07800  -44.03600 -8.66500  1.000 55.53151  ? 241 PHE   A CE1 1 
ATOM   1657 C  CE2 . PHE   A 1 205 ? 13.54000  -42.24600 -8.29000  1.000 48.23210  ? 241 PHE   A CE2 1 
ATOM   1658 C  CZ  . PHE   A 1 205 ? 14.02600  -43.49400 -7.95400  1.000 57.67073  ? 241 PHE   A CZ  1 
ATOM   1659 N  N   . TYR   A 1 206 ? 17.81000  -39.24500 -12.65900 1.000 45.57332  ? 242 TYR   A N   1 
ATOM   1660 C  CA  . TYR   A 1 206 ? 18.57300  -38.81300 -13.82700 1.000 42.73283  ? 242 TYR   A CA  1 
ATOM   1661 C  C   . TYR   A 1 206 ? 20.07200  -38.92600 -13.57500 1.000 47.26405  ? 242 TYR   A C   1 
ATOM   1662 O  O   . TYR   A 1 206 ? 20.81100  -39.45600 -14.41400 1.000 48.36733  ? 242 TYR   A O   1 
ATOM   1663 C  CB  . TYR   A 1 206 ? 18.17300  -37.38000 -14.18300 1.000 45.25924  ? 242 TYR   A CB  1 
ATOM   1664 C  CG  . TYR   A 1 206 ? 19.02100  -36.67300 -15.22500 1.000 43.52255  ? 242 TYR   A CG  1 
ATOM   1665 C  CD1 . TYR   A 1 206 ? 18.84600  -36.91700 -16.58200 1.000 46.45924  ? 242 TYR   A CD1 1 
ATOM   1666 C  CD2 . TYR   A 1 206 ? 19.96400  -35.72100 -14.85000 1.000 47.71764  ? 242 TYR   A CD2 1 
ATOM   1667 C  CE1 . TYR   A 1 206 ? 19.60600  -36.25600 -17.53700 1.000 48.12398  ? 242 TYR   A CE1 1 
ATOM   1668 C  CE2 . TYR   A 1 206 ? 20.73200  -35.05700 -15.79800 1.000 41.27027  ? 242 TYR   A CE2 1 
ATOM   1669 C  CZ  . TYR   A 1 206 ? 20.54500  -35.32400 -17.13700 1.000 47.10914  ? 242 TYR   A CZ  1 
ATOM   1670 O  OH  . TYR   A 1 206 ? 21.29700  -34.66400 -18.08200 1.000 51.95169  ? 242 TYR   A OH  1 
ATOM   1671 N  N   . PHE   A 1 207 ? 20.54000  -38.43700 -12.42000 1.000 44.49532  ? 243 PHE   A N   1 
ATOM   1672 C  CA  . PHE   A 1 207 ? 21.95600  -38.56100 -12.07700 1.000 43.99562  ? 243 PHE   A CA  1 
ATOM   1673 C  C   . PHE   A 1 207 ? 22.36400  -40.02000 -11.92800 1.000 48.07070  ? 243 PHE   A C   1 
ATOM   1674 O  O   . PHE   A 1 207 ? 23.44200  -40.41900 -12.38200 1.000 44.11866  ? 243 PHE   A O   1 
ATOM   1675 C  CB  . PHE   A 1 207 ? 22.26100  -37.80800 -10.78300 1.000 38.32965  ? 243 PHE   A CB  1 
ATOM   1676 C  CG  . PHE   A 1 207 ? 22.23700  -36.31700 -10.92000 1.000 39.91663  ? 243 PHE   A CG  1 
ATOM   1677 C  CD1 . PHE   A 1 207 ? 22.39400  -35.71600 -12.15500 1.000 37.91593  ? 243 PHE   A CD1 1 
ATOM   1678 C  CD2 . PHE   A 1 207 ? 22.06600  -35.51500 -9.80500  1.000 40.67234  ? 243 PHE   A CD2 1 
ATOM   1679 C  CE1 . PHE   A 1 207 ? 22.37500  -34.34200 -12.28000 1.000 41.63696  ? 243 PHE   A CE1 1 
ATOM   1680 C  CE2 . PHE   A 1 207 ? 22.04700  -34.13500 -9.92000  1.000 45.53039  ? 243 PHE   A CE2 1 
ATOM   1681 C  CZ  . PHE   A 1 207 ? 22.20100  -33.54800 -11.16000 1.000 40.04945  ? 243 PHE   A CZ  1 
ATOM   1682 N  N   . LEU   A 1 208 ? 21.52100  -40.82700 -11.28400 1.000 42.83770  ? 244 LEU   A N   1 
ATOM   1683 C  CA  . LEU   A 1 208 ? 21.89000  -42.20600 -10.98100 1.000 48.58280  ? 244 LEU   A CA  1 
ATOM   1684 C  C   . LEU   A 1 208 ? 21.93300  -43.05900 -12.24000 1.000 48.36784  ? 244 LEU   A C   1 
ATOM   1685 O  O   . LEU   A 1 208 ? 22.86800  -43.84200 -12.44100 1.000 50.51894  ? 244 LEU   A O   1 
ATOM   1686 C  CB  . LEU   A 1 208 ? 20.90400  -42.80000 -9.97700  1.000 50.51891  ? 244 LEU   A CB  1 
ATOM   1687 C  CG  . LEU   A 1 208 ? 21.01100  -42.32200 -8.53200  1.000 48.94875  ? 244 LEU   A CG  1 
ATOM   1688 C  CD1 . LEU   A 1 208 ? 19.79300  -42.77300 -7.73700  1.000 50.49778  ? 244 LEU   A CD1 1 
ATOM   1689 C  CD2 . LEU   A 1 208 ? 22.28400  -42.85600 -7.90700  1.000 45.30187  ? 244 LEU   A CD2 1 
ATOM   1690 N  N   . ARG   A 1 209 ? 20.92400  -42.92800 -13.09500 1.000 45.84921  ? 245 ARG   A N   1 
ATOM   1691 C  CA  . ARG   A 1 209 ? 20.78800  -43.80500 -14.25000 1.000 57.28634  ? 245 ARG   A CA  1 
ATOM   1692 C  C   . ARG   A 1 209 ? 21.49800  -43.28700 -15.48800 1.000 52.33224  ? 245 ARG   A C   1 
ATOM   1693 O  O   . ARG   A 1 209 ? 21.74900  -44.06900 -16.41300 1.000 55.49602  ? 245 ARG   A O   1 
ATOM   1694 C  CB  . ARG   A 1 209 ? 19.30800  -44.01300 -14.58100 1.000 52.28201  ? 245 ARG   A CB  1 
ATOM   1695 C  CG  . ARG   A 1 209 ? 18.49700  -44.62600 -13.45900 1.000 52.09424  ? 245 ARG   A CG  1 
ATOM   1696 C  CD  . ARG   A 1 209 ? 17.00800  -44.44300 -13.71400 1.000 60.16660  ? 245 ARG   A CD  1 
ATOM   1697 N  NE  . ARG   A 1 209 ? 16.61900  -44.85600 -15.05800 1.000 67.17498  ? 245 ARG   A NE  1 
ATOM   1698 C  CZ  . ARG   A 1 209 ? 16.19000  -46.07000 -15.37600 1.000 69.01733  ? 245 ARG   A CZ  1 
ATOM   1699 N  NH1 . ARG   A 1 209 ? 16.11800  -47.03500 -14.47400 1.000 71.52035  ? 245 ARG   A NH1 1 
ATOM   1700 N  NH2 . ARG   A 1 209 ? 15.82400  -46.32200 -16.62900 1.000 70.58484  ? 245 ARG   A NH2 1 
ATOM   1701 N  N   . GLY   A 1 210 ? 21.82200  -42.00000 -15.53500 1.000 51.20480  ? 246 GLY   A N   1 
ATOM   1702 C  CA  . GLY   A 1 210 ? 22.33800  -41.40000 -16.74100 1.000 48.79344  ? 246 GLY   A CA  1 
ATOM   1703 C  C   . GLY   A 1 210 ? 21.28200  -40.98500 -17.73900 1.000 57.45884  ? 246 GLY   A C   1 
ATOM   1704 O  O   . GLY   A 1 210 ? 21.61500  -40.30900 -18.72000 1.000 50.73737  ? 246 GLY   A O   1 
ATOM   1705 N  N   . GLN   A 1 211 ? 20.02300  -41.36000 -17.52400 1.000 50.68948  ? 247 GLN   A N   1 
ATOM   1706 C  CA  . GLN   A 1 211 ? 18.94100  -40.99300 -18.42600 1.000 56.91784  ? 247 GLN   A CA  1 
ATOM   1707 C  C   . GLN   A 1 211 ? 17.61600  -41.20600 -17.71000 1.000 54.63796  ? 247 GLN   A C   1 
ATOM   1708 O  O   . GLN   A 1 211 ? 17.54800  -41.85200 -16.66100 1.000 57.59159  ? 247 GLN   A O   1 
ATOM   1709 C  CB  . GLN   A 1 211 ? 18.99100  -41.80400 -19.72700 1.000 53.94665  ? 247 GLN   A CB  1 
ATOM   1710 C  CG  . GLN   A 1 211 ? 19.04000  -43.32100 -19.53100 1.000 63.42107  ? 247 GLN   A CG  1 
ATOM   1711 C  CD  . GLN   A 1 211 ? 17.67500  -43.94700 -19.27800 1.000 70.95408  ? 247 GLN   A CD  1 
ATOM   1712 O  OE1 . GLN   A 1 211 ? 17.28600  -44.17800 -18.13300 1.000 74.31518  ? 247 GLN   A OE1 1 
ATOM   1713 N  NE2 . GLN   A 1 211 ? 16.93700  -44.20900 -20.35200 1.000 65.18467  ? 247 GLN   A NE2 1 
ATOM   1714 N  N   . LEU   A 1 212 ? 16.55800  -40.66100 -18.29800 1.000 58.18124  ? 248 LEU   A N   1 
ATOM   1715 C  CA  . LEU   A 1 212 ? 15.22400  -41.00100 -17.84700 1.000 58.60819  ? 248 LEU   A CA  1 
ATOM   1716 C  C   . LEU   A 1 212 ? 14.47800  -41.72300 -18.96300 1.000 57.13959  ? 248 LEU   A C   1 
ATOM   1717 O  O   . LEU   A 1 212 ? 14.70400  -41.43300 -20.14400 1.000 54.17428  ? 248 LEU   A O   1 
ATOM   1718 C  CB  . LEU   A 1 212 ? 14.45200  -39.74900 -17.41200 1.000 53.88285  ? 248 LEU   A CB  1 
ATOM   1719 C  CG  . LEU   A 1 212 ? 15.05700  -39.07300 -16.17800 1.000 51.00940  ? 248 LEU   A CG  1 
ATOM   1720 C  CD1 . LEU   A 1 212 ? 14.36000  -37.77100 -15.84700 1.000 46.42909  ? 248 LEU   A CD1 1 
ATOM   1721 C  CD2 . LEU   A 1 212 ? 15.01500  -40.02100 -14.99100 1.000 58.01680  ? 248 LEU   A CD2 1 
ATOM   1722 N  N   . PRO   A 1 213 ? 13.61000  -42.68300 -18.63100 1.000 62.19612  ? 249 PRO   A N   1 
ATOM   1723 C  CA  . PRO   A 1 213 ? 12.93800  -43.46000 -19.68500 1.000 60.12274  ? 249 PRO   A CA  1 
ATOM   1724 C  C   . PRO   A 1 213 ? 11.98100  -42.64700 -20.53700 1.000 55.70331  ? 249 PRO   A C   1 
ATOM   1725 O  O   . PRO   A 1 213 ? 11.49300  -43.16800 -21.54800 1.000 63.81635  ? 249 PRO   A O   1 
ATOM   1726 C  CB  . PRO   A 1 213 ? 12.19600  -44.55300 -18.90400 1.000 57.61719  ? 249 PRO   A CB  1 
ATOM   1727 C  CG  . PRO   A 1 213 ? 12.03200  -44.00100 -17.54000 1.000 57.05676  ? 249 PRO   A CG  1 
ATOM   1728 C  CD  . PRO   A 1 213 ? 13.24200  -43.14300 -17.28300 1.000 59.73391  ? 249 PRO   A CD  1 
ATOM   1729 N  N   . TRP   A 1 214 ? 11.69400  -41.39800 -20.17400 1.000 57.67932  ? 250 TRP   A N   1 
ATOM   1730 C  CA  . TRP   A 1 214 ? 10.86200  -40.53200 -20.99500 1.000 60.52409  ? 250 TRP   A CA  1 
ATOM   1731 C  C   . TRP   A 1 214 ? 11.68600  -39.53500 -21.80600 1.000 64.07251  ? 250 TRP   A C   1 
ATOM   1732 O  O   . TRP   A 1 214 ? 11.13300  -38.56200 -22.33000 1.000 65.51114  ? 250 TRP   A O   1 
ATOM   1733 C  CB  . TRP   A 1 214 ? 9.83000   -39.80700 -20.12900 1.000 55.83476  ? 250 TRP   A CB  1 
ATOM   1734 C  CG  . TRP   A 1 214 ? 10.39100  -39.19400 -18.88800 1.000 59.83994  ? 250 TRP   A CG  1 
ATOM   1735 C  CD1 . TRP   A 1 214 ? 11.08000  -38.02200 -18.79400 1.000 55.14621  ? 250 TRP   A CD1 1 
ATOM   1736 C  CD2 . TRP   A 1 214 ? 10.29700  -39.71400 -17.55400 1.000 54.73963  ? 250 TRP   A CD2 1 
ATOM   1737 N  NE1 . TRP   A 1 214 ? 11.42800  -37.78100 -17.48700 1.000 59.81536  ? 250 TRP   A NE1 1 
ATOM   1738 C  CE2 . TRP   A 1 214 ? 10.95800  -38.80400 -16.70600 1.000 54.73277  ? 250 TRP   A CE2 1 
ATOM   1739 C  CE3 . TRP   A 1 214 ? 9.72100   -40.86000 -16.99600 1.000 58.88714  ? 250 TRP   A CE3 1 
ATOM   1740 C  CZ2 . TRP   A 1 214 ? 11.06100  -39.00500 -15.33200 1.000 54.50220  ? 250 TRP   A CZ2 1 
ATOM   1741 C  CZ3 . TRP   A 1 214 ? 9.82300   -41.05600 -15.63000 1.000 53.89547  ? 250 TRP   A CZ3 1 
ATOM   1742 C  CH2 . TRP   A 1 214 ? 10.48700  -40.13400 -14.81400 1.000 52.36658  ? 250 TRP   A CH2 1 
ATOM   1743 N  N   . GLN   A 1 215 ? 12.99300  -39.75900 -21.91900 1.000 62.97175  ? 251 GLN   A N   1 
ATOM   1744 C  CA  . GLN   A 1 215 ? 13.84300  -38.96600 -22.79400 1.000 64.70348  ? 251 GLN   A CA  1 
ATOM   1745 C  C   . GLN   A 1 215 ? 13.79100  -39.51600 -24.21400 1.000 66.87067  ? 251 GLN   A C   1 
ATOM   1746 O  O   . GLN   A 1 215 ? 13.55100  -40.70700 -24.43200 1.000 64.29854  ? 251 GLN   A O   1 
ATOM   1747 C  CB  . GLN   A 1 215 ? 15.29300  -38.95800 -22.30100 1.000 60.92675  ? 251 GLN   A CB  1 
ATOM   1748 C  CG  . GLN   A 1 215 ? 15.51200  -38.28900 -20.95100 1.000 58.62165  ? 251 GLN   A CG  1 
ATOM   1749 C  CD  . GLN   A 1 215 ? 16.98700  -38.14700 -20.60100 1.000 58.19981  ? 251 GLN   A CD  1 
ATOM   1750 O  OE1 . GLN   A 1 215 ? 17.37000  -38.22300 -19.43400 1.000 57.71020  ? 251 GLN   A OE1 1 
ATOM   1751 N  NE2 . GLN   A 1 215 ? 17.81800  -37.93300 -21.61400 1.000 56.47033  ? 251 GLN   A NE2 1 
ATOM   1752 N  N   . GLY   A 1 216 ? 14.01900  -38.63200 -25.18200 1.000 72.53583  ? 252 GLY   A N   1 
ATOM   1753 C  CA  . GLY   A 1 216 ? 14.06500  -39.04600 -26.57000 1.000 65.76068  ? 252 GLY   A CA  1 
ATOM   1754 C  C   . GLY   A 1 216 ? 12.73300  -39.42300 -27.17300 1.000 72.71596  ? 252 GLY   A C   1 
ATOM   1755 O  O   . GLY   A 1 216 ? 12.70100  -40.11400 -28.19400 1.000 69.48571  ? 252 GLY   A O   1 
ATOM   1756 N  N   . LEU   A 1 217 ? 11.62800  -38.99100 -26.57300 1.000 71.31794  ? 253 LEU   A N   1 
ATOM   1757 C  CA  . LEU   A 1 217 ? 10.31700  -39.29200 -27.12300 1.000 70.61409  ? 253 LEU   A CA  1 
ATOM   1758 C  C   . LEU   A 1 217 ? 10.00200  -38.36700 -28.29200 1.000 74.50732  ? 253 LEU   A C   1 
ATOM   1759 O  O   . LEU   A 1 217 ? 10.40100  -37.19900 -28.31600 1.000 78.16430  ? 253 LEU   A O   1 
ATOM   1760 C  CB  . LEU   A 1 217 ? 9.23600   -39.16500 -26.04800 1.000 68.81798  ? 253 LEU   A CB  1 
ATOM   1761 C  CG  . LEU   A 1 217 ? 9.36100   -40.10900 -24.85200 1.000 68.48014  ? 253 LEU   A CG  1 
ATOM   1762 C  CD1 . LEU   A 1 217 ? 8.08700   -40.09600 -24.02100 1.000 65.96462  ? 253 LEU   A CD1 1 
ATOM   1763 C  CD2 . LEU   A 1 217 ? 9.69700   -41.52100 -25.30700 1.000 72.20777  ? 253 LEU   A CD2 1 
ATOM   1764 N  N   . LYS   A 1 218 ? 9.28400   -38.90700 -29.27100 1.000 75.32411  ? 254 LYS   A N   1 
ATOM   1765 C  CA  . LYS   A 1 218 ? 8.89400   -38.17600 -30.46500 1.000 83.07546  ? 254 LYS   A CA  1 
ATOM   1766 C  C   . LYS   A 1 218 ? 7.40600   -37.85300 -30.43100 1.000 83.82287  ? 254 LYS   A C   1 
ATOM   1767 O  O   . LYS   A 1 218 ? 6.61100   -38.57000 -29.81700 1.000 79.06075  ? 254 LYS   A O   1 
ATOM   1768 C  CB  . LYS   A 1 218 ? 9.21200   -38.97600 -31.73200 1.000 87.16181  ? 254 LYS   A CB  1 
ATOM   1769 C  CG  . LYS   A 1 218 ? 10.45200  -38.51300 -32.47900 1.000 94.49825  ? 254 LYS   A CG  1 
ATOM   1770 C  CD  . LYS   A 1 218 ? 11.71700  -39.13900 -31.92400 1.000 89.51370  ? 254 LYS   A CD  1 
ATOM   1771 C  CE  . LYS   A 1 218 ? 12.91200  -38.77000 -32.78600 1.000 95.05599  ? 254 LYS   A CE  1 
ATOM   1772 N  NZ  . LYS   A 1 218 ? 14.13800  -39.52400 -32.41100 1.000 95.44220  ? 254 LYS   A NZ  1 
ATOM   1773 N  N   . ALA   A 1 219 ? 7.04100   -36.76300 -31.10800 1.000 87.27989  ? 255 ALA   A N   1 
ATOM   1774 C  CA  . ALA   A 1 219 ? 5.65700   -36.33200 -31.26000 1.000 88.52956  ? 255 ALA   A CA  1 
ATOM   1775 C  C   . ALA   A 1 219 ? 5.57600   -35.25900 -32.33900 1.000 89.20958  ? 255 ALA   A C   1 
ATOM   1776 O  O   . ALA   A 1 219 ? 6.56400   -34.55400 -32.58400 1.000 99.77724  ? 255 ALA   A O   1 
ATOM   1777 C  CB  . ALA   A 1 219 ? 5.09600   -35.80600 -29.93900 1.000 87.92214  ? 255 ALA   A CB  1 
ATOM   1778 N  N   . PRO   A 1 220 ? 4.43000   -35.11000 -33.01100 1.000 88.02075  ? 256 PRO   A N   1 
ATOM   1779 C  CA  . PRO   A 1 220 ? 4.33000   -34.06900 -34.05000 1.000 89.28959  ? 256 PRO   A CA  1 
ATOM   1780 C  C   . PRO   A 1 220 ? 4.56000   -32.66100 -33.52600 1.000 87.75011  ? 256 PRO   A C   1 
ATOM   1781 O  O   . PRO   A 1 220 ? 5.23900   -31.86500 -34.18600 1.000 85.11228  ? 256 PRO   A O   1 
ATOM   1782 C  CB  . PRO   A 1 220 ? 2.90300   -34.25200 -34.58600 1.000 84.14494  ? 256 PRO   A CB  1 
ATOM   1783 C  CG  . PRO   A 1 220 ? 2.56700   -35.67400 -34.28800 1.000 85.56708  ? 256 PRO   A CG  1 
ATOM   1784 C  CD  . PRO   A 1 220 ? 3.24600   -35.98500 -32.98600 1.000 84.51526  ? 256 PRO   A CD  1 
ATOM   1785 N  N   . THR   A 1 221 ? 4.01400   -32.32800 -32.36200 1.000 85.82468  ? 257 THR   A N   1 
ATOM   1786 C  CA  . THR   A 1 221 ? 4.13400   -30.99800 -31.77800 1.000 84.73882  ? 257 THR   A CA  1 
ATOM   1787 C  C   . THR   A 1 221 ? 4.80800   -31.09000 -30.41300 1.000 84.69064  ? 257 THR   A C   1 
ATOM   1788 O  O   . THR   A 1 221 ? 5.16000   -32.17200 -29.93600 1.000 88.34711  ? 257 THR   A O   1 
ATOM   1789 C  CB  . THR   A 1 221 ? 2.76400   -30.32500 -31.64400 1.000 78.08406  ? 257 THR   A CB  1 
ATOM   1790 O  OG1 . THR   A 1 221 ? 2.04200   -30.92400 -30.56000 1.000 79.96543  ? 257 THR   A OG1 1 
ATOM   1791 C  CG2 . THR   A 1 221 ? 1.96400   -30.48800 -32.91800 1.000 73.44794  ? 257 THR   A CG2 1 
ATOM   1792 N  N   . ASN   A 1 222 ? 4.98300   -29.93000 -29.78000 1.000 83.65447  ? 258 ASN   A N   1 
ATOM   1793 C  CA  . ASN   A 1 222 ? 5.55300   -29.90200 -28.43900 1.000 84.72776  ? 258 ASN   A CA  1 
ATOM   1794 C  C   . ASN   A 1 222 ? 4.51400   -30.22500 -27.37400 1.000 83.21685  ? 258 ASN   A C   1 
ATOM   1795 O  O   . ASN   A 1 222 ? 4.85600   -30.80300 -26.33700 1.000 80.26485  ? 258 ASN   A O   1 
ATOM   1796 C  CB  . ASN   A 1 222 ? 6.18800   -28.53800 -28.16600 1.000 88.06313  ? 258 ASN   A CB  1 
ATOM   1797 C  CG  . ASN   A 1 222 ? 7.70000   -28.61000 -28.05800 1.000 90.05899  ? 258 ASN   A CG  1 
ATOM   1798 O  OD1 . ASN   A 1 222 ? 8.30100   -29.66300 -28.27900 1.000 92.53339  ? 258 ASN   A OD1 1 
ATOM   1799 N  ND2 . ASN   A 1 222 ? 8.32400   -27.48800 -27.72000 1.000 89.41923  ? 258 ASN   A ND2 1 
ATOM   1800 N  N   . LYS   A 1 223 ? 3.24900   -29.86900 -27.61300 1.000 80.74014  ? 259 LYS   A N   1 
ATOM   1801 C  CA  . LYS   A 1 223 ? 2.19100   -30.18800 -26.65900 1.000 82.66961  ? 259 LYS   A CA  1 
ATOM   1802 C  C   . LYS   A 1 223 ? 2.01600   -31.69600 -26.52000 1.000 81.56273  ? 259 LYS   A C   1 
ATOM   1803 O  O   . LYS   A 1 223 ? 1.91500   -32.22100 -25.40500 1.000 77.48944  ? 259 LYS   A O   1 
ATOM   1804 C  CB  . LYS   A 1 223 ? 0.88100   -29.53000 -27.09300 1.000 88.24531  ? 259 LYS   A CB  1 
ATOM   1805 C  CG  . LYS   A 1 223 ? -0.33600  -29.99500 -26.31000 1.000 92.53812  ? 259 LYS   A CG  1 
ATOM   1806 C  CD  . LYS   A 1 223 ? -1.61200  -29.35400 -26.83000 1.000 99.89524  ? 259 LYS   A CD  1 
ATOM   1807 C  CE  . LYS   A 1 223 ? -2.84200  -30.02700 -26.24100 1.000 107.34056 ? 259 LYS   A CE  1 
ATOM   1808 N  NZ  . LYS   A 1 223 ? -2.93100  -31.45800 -26.64600 1.000 106.56227 ? 259 LYS   A NZ  1 
ATOM   1809 N  N   . GLN   A 1 224 ? 1.97700   -32.40900 -27.64800 1.000 81.34931  ? 260 GLN   A N   1 
ATOM   1810 C  CA  . GLN   A 1 224 ? 1.85700   -33.86200 -27.60000 1.000 74.92553  ? 260 GLN   A CA  1 
ATOM   1811 C  C   . GLN   A 1 224 ? 3.12200   -34.51000 -27.05300 1.000 79.81534  ? 260 GLN   A C   1 
ATOM   1812 O  O   . GLN   A 1 224 ? 3.05300   -35.58300 -26.44200 1.000 78.06876  ? 260 GLN   A O   1 
ATOM   1813 C  CB  . GLN   A 1 224 ? 1.53300   -34.40300 -28.99200 1.000 78.31249  ? 260 GLN   A CB  1 
ATOM   1814 C  CG  . GLN   A 1 224 ? 0.31500   -33.75100 -29.63000 1.000 72.43719  ? 260 GLN   A CG  1 
ATOM   1815 C  CD  . GLN   A 1 224 ? 0.08800   -34.19800 -31.06000 1.000 77.52092  ? 260 GLN   A CD  1 
ATOM   1816 O  OE1 . GLN   A 1 224 ? 0.56400   -35.25500 -31.47600 1.000 83.99747  ? 260 GLN   A OE1 1 
ATOM   1817 N  NE2 . GLN   A 1 224 ? -0.64000  -33.39100 -31.82400 1.000 73.01719  ? 260 GLN   A NE2 1 
ATOM   1818 N  N   . LYS   A 1 225 ? 4.28200   -33.88000 -27.26100 1.000 79.67341  ? 261 LYS   A N   1 
ATOM   1819 C  CA  . LYS   A 1 225 ? 5.52000   -34.39500 -26.68500 1.000 81.37422  ? 261 LYS   A CA  1 
ATOM   1820 C  C   . LYS   A 1 225 ? 5.49600   -34.30400 -25.16500 1.000 77.43027  ? 261 LYS   A C   1 
ATOM   1821 O  O   . LYS   A 1 225 ? 5.89500   -35.24900 -24.47500 1.000 71.67972  ? 261 LYS   A O   1 
ATOM   1822 C  CB  . LYS   A 1 225 ? 6.71700   -33.63400 -27.25600 1.000 77.36566  ? 261 LYS   A CB  1 
ATOM   1823 C  CG  . LYS   A 1 225 ? 8.01700   -33.84400 -26.50300 1.000 77.46370  ? 261 LYS   A CG  1 
ATOM   1824 C  CD  . LYS   A 1 225 ? 9.15300   -33.07500 -27.15900 1.000 80.95453  ? 261 LYS   A CD  1 
ATOM   1825 C  CE  . LYS   A 1 225 ? 10.36300  -32.97400 -26.24600 1.000 78.87831  ? 261 LYS   A CE  1 
ATOM   1826 N  NZ  . LYS   A 1 225 ? 10.87600  -34.31000 -25.83600 1.000 83.21854  ? 261 LYS   A NZ  1 
ATOM   1827 N  N   . TYR   A 1 226 ? 5.02800   -33.17600 -24.62700 1.000 82.29957  ? 262 TYR   A N   1 
ATOM   1828 C  CA  . TYR   A 1 226 ? 4.89800   -33.04500 -23.18000 1.000 81.36160  ? 262 TYR   A CA  1 
ATOM   1829 C  C   . TYR   A 1 226 ? 3.88000   -34.03100 -22.62200 1.000 80.13426  ? 262 TYR   A C   1 
ATOM   1830 O  O   . TYR   A 1 226 ? 3.99500   -34.45600 -21.46700 1.000 85.33560  ? 262 TYR   A O   1 
ATOM   1831 C  CB  . TYR   A 1 226 ? 4.51400   -31.60800 -22.81700 1.000 84.67291  ? 262 TYR   A CB  1 
ATOM   1832 C  CG  . TYR   A 1 226 ? 5.67600   -30.63400 -22.80900 1.000 94.10669  ? 262 TYR   A CG  1 
ATOM   1833 C  CD1 . TYR   A 1 226 ? 6.65600   -30.67700 -23.79400 1.000 99.07929  ? 262 TYR   A CD1 1 
ATOM   1834 C  CD2 . TYR   A 1 226 ? 5.78600   -29.66300 -21.82100 1.000 97.46644  ? 262 TYR   A CD2 1 
ATOM   1835 C  CE1 . TYR   A 1 226 ? 7.71700   -29.78700 -23.79100 1.000 102.23536 ? 262 TYR   A CE1 1 
ATOM   1836 C  CE2 . TYR   A 1 226 ? 6.84200   -28.76700 -21.81100 1.000 102.80964 ? 262 TYR   A CE2 1 
ATOM   1837 C  CZ  . TYR   A 1 226 ? 7.80400   -28.83400 -22.79800 1.000 112.62706 ? 262 TYR   A CZ  1 
ATOM   1838 O  OH  . TYR   A 1 226 ? 8.85700   -27.94600 -22.79100 1.000 113.75039 ? 262 TYR   A OH  1 
ATOM   1839 N  N   . GLU   A 1 227 ? 2.88500   -34.41400 -23.42400 1.000 74.90337  ? 263 GLU   A N   1 
ATOM   1840 C  CA  . GLU   A 1 227 ? 1.89500   -35.38300 -22.96700 1.000 74.85314  ? 263 GLU   A CA  1 
ATOM   1841 C  C   . GLU   A 1 227 ? 2.45900   -36.80000 -22.95700 1.000 73.65471  ? 263 GLU   A C   1 
ATOM   1842 O  O   . GLU   A 1 227 ? 2.20100   -37.56400 -22.02000 1.000 67.48346  ? 263 GLU   A O   1 
ATOM   1843 C  CB  . GLU   A 1 227 ? 0.64700   -35.31100 -23.84500 1.000 77.86873  ? 263 GLU   A CB  1 
ATOM   1844 C  CG  . GLU   A 1 227 ? -0.44200  -36.28700 -23.44600 1.000 79.17650  ? 263 GLU   A CG  1 
ATOM   1845 C  CD  . GLU   A 1 227 ? -1.69800  -36.11600 -24.27000 1.000 76.59700  ? 263 GLU   A CD  1 
ATOM   1846 O  OE1 . GLU   A 1 227 ? -1.83300  -35.06900 -24.93600 1.000 86.57888  ? 263 GLU   A OE1 1 
ATOM   1847 O  OE2 . GLU   A 1 227 ? -2.54700  -37.03100 -24.25700 1.000 83.07384  ? 263 GLU   A OE2 1 
ATOM   1848 N  N   . LYS   A 1 228 ? 3.22500   -37.16900 -23.98900 1.000 68.42119  ? 264 LYS   A N   1 
ATOM   1849 C  CA  . LYS   A 1 228 ? 3.84800   -38.48900 -24.01000 1.000 69.26263  ? 264 LYS   A CA  1 
ATOM   1850 C  C   . LYS   A 1 228 ? 4.83800   -38.64800 -22.86500 1.000 69.24519  ? 264 LYS   A C   1 
ATOM   1851 O  O   . LYS   A 1 228 ? 4.95900   -39.73200 -22.28100 1.000 64.89882  ? 264 LYS   A O   1 
ATOM   1852 C  CB  . LYS   A 1 228 ? 4.54600   -38.72600 -25.34800 1.000 69.18408  ? 264 LYS   A CB  1 
ATOM   1853 C  CG  . LYS   A 1 228 ? 3.63100   -39.20300 -26.45900 1.000 74.83113  ? 264 LYS   A CG  1 
ATOM   1854 C  CD  . LYS   A 1 228 ? 4.43900   -39.63700 -27.66800 1.000 72.39797  ? 264 LYS   A CD  1 
ATOM   1855 C  CE  . LYS   A 1 228 ? 3.55200   -40.25200 -28.73800 1.000 78.81320  ? 264 LYS   A CE  1 
ATOM   1856 N  NZ  . LYS   A 1 228 ? 4.35500   -40.74800 -29.88900 1.000 83.01574  ? 264 LYS   A NZ  1 
ATOM   1857 N  N   . ILE   A 1 229 ? 5.56200   -37.57800 -22.53500 1.000 67.49047  ? 265 ILE   A N   1 
ATOM   1858 C  CA  . ILE   A 1 229 ? 6.48400   -37.62100 -21.40600 1.000 64.90598  ? 265 ILE   A CA  1 
ATOM   1859 C  C   . ILE   A 1 229 ? 5.71700   -37.81800 -20.10300 1.000 63.22236  ? 265 ILE   A C   1 
ATOM   1860 O  O   . ILE   A 1 229 ? 6.03900   -38.70200 -19.30100 1.000 63.27628  ? 265 ILE   A O   1 
ATOM   1861 C  CB  . ILE   A 1 229 ? 7.34900   -36.34600 -21.37800 1.000 61.31531  ? 265 ILE   A CB  1 
ATOM   1862 C  CG1 . ILE   A 1 229 ? 8.28500   -36.31500 -22.59100 1.000 66.36607  ? 265 ILE   A CG1 1 
ATOM   1863 C  CG2 . ILE   A 1 229 ? 8.13900   -36.26300 -20.08600 1.000 63.42375  ? 265 ILE   A CG2 1 
ATOM   1864 C  CD1 . ILE   A 1 229 ? 9.18300   -35.09400 -22.65400 1.000 62.04086  ? 265 ILE   A CD1 1 
ATOM   1865 N  N   . GLY   A 1 230 ? 4.67800   -37.00900 -19.88000 1.000 66.79881  ? 266 GLY   A N   1 
ATOM   1866 C  CA  . GLY   A 1 230 ? 3.86100   -37.17400 -18.68900 1.000 66.44567  ? 266 GLY   A CA  1 
ATOM   1867 C  C   . GLY   A 1 230 ? 3.18100   -38.52700 -18.60800 1.000 67.00494  ? 266 GLY   A C   1 
ATOM   1868 O  O   . GLY   A 1 230 ? 3.01500   -39.07600 -17.51500 1.000 64.26369  ? 266 GLY   A O   1 
ATOM   1869 N  N   . ASP   A 1 231 ? 2.78500   -39.08400 -19.75700 1.000 66.09323  ? 267 ASP   A N   1 
ATOM   1870 C  CA  . ASP   A 1 231 ? 2.18100   -40.41400 -19.77700 1.000 65.54130  ? 267 ASP   A CA  1 
ATOM   1871 C  C   . ASP   A 1 231 ? 3.17100   -41.48300 -19.33200 1.000 69.04105  ? 267 ASP   A C   1 
ATOM   1872 O  O   . ASP   A 1 231 ? 2.80500   -42.41000 -18.59900 1.000 69.68676  ? 267 ASP   A O   1 
ATOM   1873 C  CB  . ASP   A 1 231 ? 1.65100   -40.72900 -21.17700 1.000 64.61422  ? 267 ASP   A CB  1 
ATOM   1874 C  CG  . ASP   A 1 231 ? 0.29300   -40.10500 -21.44500 1.000 79.86349  ? 267 ASP   A CG  1 
ATOM   1875 O  OD1 . ASP   A 1 231 ? -0.54700  -40.08700 -20.52100 1.000 81.04846  ? 267 ASP   A OD1 1 
ATOM   1876 O  OD2 . ASP   A 1 231 ? 0.06300   -39.63600 -22.58100 1.000 81.06523  ? 267 ASP   A OD2 1 
ATOM   1877 N  N   . LYS   A 1 232 ? 4.42700   -41.38000 -19.77400 1.000 62.41771  ? 268 LYS   A N   1 
ATOM   1878 C  CA  . LYS   A 1 232 ? 5.43600   -42.34100 -19.34400 1.000 66.29219  ? 268 LYS   A CA  1 
ATOM   1879 C  C   . LYS   A 1 232 ? 5.71000   -42.22700 -17.85000 1.000 66.07109  ? 268 LYS   A C   1 
ATOM   1880 O  O   . LYS   A 1 232 ? 5.96800   -43.24000 -17.18800 1.000 66.69231  ? 268 LYS   A O   1 
ATOM   1881 C  CB  . LYS   A 1 232 ? 6.72500   -42.14000 -20.14200 1.000 65.32232  ? 268 LYS   A CB  1 
ATOM   1882 C  CG  . LYS   A 1 232 ? 7.79500   -43.19600 -19.90200 1.000 68.16145  ? 268 LYS   A CG  1 
ATOM   1883 C  CD  . LYS   A 1 232 ? 7.47000   -44.50900 -20.60000 1.000 67.92159  ? 268 LYS   A CD  1 
ATOM   1884 C  CE  . LYS   A 1 232 ? 8.70000   -45.40700 -20.64400 1.000 72.49353  ? 268 LYS   A CE  1 
ATOM   1885 N  NZ  . LYS   A 1 232 ? 8.45400   -46.69300 -21.35400 1.000 77.40869  ? 268 LYS   A NZ  1 
ATOM   1886 N  N   . LYS   A 1 233 ? 5.65000   -41.01000 -17.30300 1.000 66.62914  ? 269 LYS   A N   1 
ATOM   1887 C  CA  . LYS   A 1 233 ? 5.86500   -40.82600 -15.87200 1.000 57.95596  ? 269 LYS   A CA  1 
ATOM   1888 C  C   . LYS   A 1 233 ? 4.79700   -41.54400 -15.05500 1.000 69.76253  ? 269 LYS   A C   1 
ATOM   1889 O  O   . LYS   A 1 233 ? 5.11100   -42.19600 -14.05200 1.000 72.08127  ? 269 LYS   A O   1 
ATOM   1890 C  CB  . LYS   A 1 233 ? 5.90100   -39.33500 -15.53500 1.000 60.24051  ? 269 LYS   A CB  1 
ATOM   1891 C  CG  . LYS   A 1 233 ? 7.13100   -38.61100 -16.08100 1.000 59.51117  ? 269 LYS   A CG  1 
ATOM   1892 C  CD  . LYS   A 1 233 ? 7.11500   -37.12500 -15.75300 1.000 58.82897  ? 269 LYS   A CD  1 
ATOM   1893 C  CE  . LYS   A 1 233 ? 8.36700   -36.43400 -16.28200 1.000 57.81302  ? 269 LYS   A CE  1 
ATOM   1894 N  NZ  . LYS   A 1 233 ? 8.34600   -34.96600 -16.03400 1.000 55.47826  ? 269 LYS   A NZ  1 
ATOM   1895 N  N   . ARG   A 1 234 ? 3.53400   -41.45000 -15.47100 1.000 67.76826  ? 270 ARG   A N   1 
ATOM   1896 C  CA  . ARG   A 1 234 ? 2.46300   -42.15800 -14.78000 1.000 68.23620  ? 270 ARG   A CA  1 
ATOM   1897 C  C   . ARG   A 1 234 ? 2.44200   -43.64600 -15.10000 1.000 69.51376  ? 270 ARG   A C   1 
ATOM   1898 O  O   . ARG   A 1 234 ? 1.76800   -44.40600 -14.39700 1.000 78.46640  ? 270 ARG   A O   1 
ATOM   1899 C  CB  . ARG   A 1 234 ? 1.10800   -41.53700 -15.12900 1.000 71.12744  ? 270 ARG   A CB  1 
ATOM   1900 C  CG  . ARG   A 1 234 ? 1.04400   -40.03800 -14.90300 1.000 69.96828  ? 270 ARG   A CG  1 
ATOM   1901 C  CD  . ARG   A 1 234 ? -0.34400  -39.49200 -15.18900 1.000 82.63241  ? 270 ARG   A CD  1 
ATOM   1902 N  NE  . ARG   A 1 234 ? -0.85400  -39.96100 -16.47200 1.000 89.06498  ? 270 ARG   A NE  1 
ATOM   1903 C  CZ  . ARG   A 1 234 ? -1.86000  -39.40100 -17.12900 1.000 87.39295  ? 270 ARG   A CZ  1 
ATOM   1904 N  NH1 . ARG   A 1 234 ? -2.47700  -38.32700 -16.66400 1.000 93.01321  ? 270 ARG   A NH1 1 
ATOM   1905 N  NH2 . ARG   A 1 234 ? -2.25100  -39.92800 -18.28600 1.000 90.96797  ? 270 ARG   A NH2 1 
ATOM   1906 N  N   . THR   A 1 235 ? 3.15700   -44.07500 -16.14000 1.000 71.83760  ? 271 THR   A N   1 
ATOM   1907 C  CA  . THR   A 1 235 ? 3.22900   -45.48300 -16.50300 1.000 71.19146  ? 271 THR   A CA  1 
ATOM   1908 C  C   . THR   A 1 235 ? 4.41300   -46.19700 -15.86700 1.000 72.77651  ? 271 THR   A C   1 
ATOM   1909 O  O   . THR   A 1 235 ? 4.36300   -47.41900 -15.68700 1.000 66.29024  ? 271 THR   A O   1 
ATOM   1910 C  CB  . THR   A 1 235 ? 3.31100   -45.62700 -18.02800 1.000 72.63682  ? 271 THR   A CB  1 
ATOM   1911 O  OG1 . THR   A 1 235 ? 2.39500   -44.71300 -18.64400 1.000 78.58491  ? 271 THR   A OG1 1 
ATOM   1912 C  CG2 . THR   A 1 235 ? 2.95600   -47.04400 -18.46000 1.000 89.97027  ? 271 THR   A CG2 1 
ATOM   1913 N  N   . THR   A 1 236 ? 5.46600   -45.46600 -15.50800 1.000 71.51351  ? 272 THR   A N   1 
ATOM   1914 C  CA  . THR   A 1 236 ? 6.67300   -46.07200 -14.97100 1.000 70.94527  ? 272 THR   A CA  1 
ATOM   1915 C  C   . THR   A 1 236 ? 6.64100   -46.02400 -13.45200 1.000 69.95055  ? 272 THR   A C   1 
ATOM   1916 O  O   . THR   A 1 236 ? 6.72400   -44.92700 -12.87600 1.000 69.55497  ? 272 THR   A O   1 
ATOM   1917 C  CB  . THR   A 1 236 ? 7.90900   -45.34900 -15.49900 1.000 68.35764  ? 272 THR   A CB  1 
ATOM   1918 O  OG1 . THR   A 1 236 ? 7.90800   -45.39100 -16.93200 1.000 68.70086  ? 272 THR   A OG1 1 
ATOM   1919 C  CG2 . THR   A 1 236 ? 9.17800   -46.00500 -14.97400 1.000 70.64169  ? 272 THR   A CG2 1 
ATOM   1920 N  N   . PRO   A 1 237 ? 6.52200   -47.15700 -12.76400 1.000 68.70426  ? 273 PRO   A N   1 
ATOM   1921 C  CA  . PRO   A 1 237 ? 6.57800   -47.14100 -11.29900 1.000 67.11860  ? 273 PRO   A CA  1 
ATOM   1922 C  C   . PRO   A 1 237 ? 7.94100   -46.68000 -10.80400 1.000 68.39756  ? 273 PRO   A C   1 
ATOM   1923 O  O   . PRO   A 1 237 ? 8.95200   -46.76000 -11.50600 1.000 70.90297  ? 273 PRO   A O   1 
ATOM   1924 C  CB  . PRO   A 1 237 ? 6.31400   -48.60100 -10.91100 1.000 68.28338  ? 273 PRO   A CB  1 
ATOM   1925 C  CG  . PRO   A 1 237 ? 5.67800   -49.21800 -12.12100 1.000 68.35057  ? 273 PRO   A CG  1 
ATOM   1926 C  CD  . PRO   A 1 237 ? 6.27600   -48.50900 -13.29200 1.000 71.91035  ? 273 PRO   A CD  1 
ATOM   1927 N  N   . ALA   A 1 238 ? 7.95200   -46.18600 -9.56300  1.000 61.73946  ? 274 ALA   A N   1 
ATOM   1928 C  CA  . ALA   A 1 238 ? 9.20000   -45.73400 -8.96000  1.000 64.92983  ? 274 ALA   A CA  1 
ATOM   1929 C  C   . ALA   A 1 238 ? 10.18000  -46.88300 -8.76400  1.000 70.82705  ? 274 ALA   A C   1 
ATOM   1930 O  O   . ALA   A 1 238 ? 11.39600  -46.68100 -8.86100  1.000 64.30756  ? 274 ALA   A O   1 
ATOM   1931 C  CB  . ALA   A 1 238 ? 8.92300   -45.04100 -7.62600  1.000 56.48595  ? 274 ALA   A CB  1 
ATOM   1932 N  N   . VAL   A 1 239 ? 9.67800   -48.08900 -8.48700  1.000 65.65493  ? 275 VAL   A N   1 
ATOM   1933 C  CA  . VAL   A 1 239 ? 10.57200  -49.23300 -8.34800  1.000 69.42275  ? 275 VAL   A CA  1 
ATOM   1934 C  C   . VAL   A 1 239 ? 11.20100  -49.58100 -9.69100  1.000 69.54494  ? 275 VAL   A C   1 
ATOM   1935 O  O   . VAL   A 1 239 ? 12.36100  -50.00900 -9.74900  1.000 71.46650  ? 275 VAL   A O   1 
ATOM   1936 C  CB  . VAL   A 1 239 ? 9.81500   -50.42800 -7.74100  1.000 72.01446  ? 275 VAL   A CB  1 
ATOM   1937 C  CG1 . VAL   A 1 239 ? 10.75100  -51.61000 -7.53900  1.000 77.56112  ? 275 VAL   A CG1 1 
ATOM   1938 C  CG2 . VAL   A 1 239 ? 9.17700   -50.02400 -6.42400  1.000 67.63583  ? 275 VAL   A CG2 1 
ATOM   1939 N  N   . THR   A 1 240 ? 10.46400  -49.39000 -10.78900 1.000 70.21261  ? 276 THR   A N   1 
ATOM   1940 C  CA  . THR   A 1 240 ? 11.04300  -49.59800 -12.11200 1.000 70.59191  ? 276 THR   A CA  1 
ATOM   1941 C  C   . THR   A 1 240 ? 12.16600  -48.60300 -12.38500 1.000 68.86659  ? 276 THR   A C   1 
ATOM   1942 O  O   . THR   A 1 240 ? 13.19800  -48.96700 -12.96000 1.000 78.19389  ? 276 THR   A O   1 
ATOM   1943 C  CB  . THR   A 1 240 ? 9.95700   -49.49500 -13.18400 1.000 71.69123  ? 276 THR   A CB  1 
ATOM   1944 O  OG1 . THR   A 1 240 ? 8.91100   -50.43400 -12.89900 1.000 66.14553  ? 276 THR   A OG1 1 
ATOM   1945 C  CG2 . THR   A 1 240 ? 10.53400  -49.80000 -14.55700 1.000 70.57397  ? 276 THR   A CG2 1 
ATOM   1946 N  N   . LEU   A 1 241 ? 11.98400  -47.34200 -11.98000 1.000 68.39383  ? 277 LEU   A N   1 
ATOM   1947 C  CA  . LEU   A 1 241 ? 13.06400  -46.36600 -12.09400 1.000 63.47538  ? 277 LEU   A CA  1 
ATOM   1948 C  C   . LEU   A 1 241 ? 14.24700  -46.74500 -11.22000 1.000 63.25861  ? 277 LEU   A C   1 
ATOM   1949 O  O   . LEU   A 1 241 ? 15.40100  -46.47900 -11.57800 1.000 61.45731  ? 277 LEU   A O   1 
ATOM   1950 C  CB  . LEU   A 1 241 ? 12.56800  -44.97400 -11.70500 1.000 59.89474  ? 277 LEU   A CB  1 
ATOM   1951 C  CG  . LEU   A 1 241 ? 11.58500  -44.29400 -12.65000 1.000 61.69659  ? 277 LEU   A CG  1 
ATOM   1952 C  CD1 . LEU   A 1 241 ? 11.11800  -42.97100 -12.06700 1.000 61.88380  ? 277 LEU   A CD1 1 
ATOM   1953 C  CD2 . LEU   A 1 241 ? 12.23900  -44.08700 -13.99300 1.000 57.62587  ? 277 LEU   A CD2 1 
ATOM   1954 N  N   . CYS   A 1 242 ? 13.97800  -47.36200 -10.07100 1.000 60.54436  ? 278 CYS   A N   1 
ATOM   1955 C  CA  . CYS   A 1 242 ? 14.99100  -47.68000 -9.08000  1.000 62.71545  ? 278 CYS   A CA  1 
ATOM   1956 C  C   . CYS   A 1 242 ? 15.61700  -49.05200 -9.30300  1.000 63.71640  ? 278 CYS   A C   1 
ATOM   1957 O  O   . CYS   A 1 242 ? 16.13500  -49.64700 -8.35100  1.000 63.28844  ? 278 CYS   A O   1 
ATOM   1958 C  CB  . CYS   A 1 242 ? 14.38300  -47.59500 -7.67900  1.000 57.63295  ? 278 CYS   A CB  1 
ATOM   1959 S  SG  . CYS   A 1 242 ? 15.50000  -47.01400 -6.40600  1.000 62.71461  ? 278 CYS   A SG  1 
ATOM   1960 N  N   . ASP   A 1 243 ? 15.57500  -49.56400 -10.53300 1.000 66.75208  ? 279 ASP   A N   1 
ATOM   1961 C  CA  . ASP   A 1 243 ? 16.11800  -50.88500 -10.83000 1.000 74.48612  ? 279 ASP   A CA  1 
ATOM   1962 C  C   . ASP   A 1 243 ? 17.62800  -50.88000 -10.63100 1.000 67.77852  ? 279 ASP   A C   1 
ATOM   1963 O  O   . ASP   A 1 243 ? 18.34300  -50.09500 -11.26300 1.000 64.96325  ? 279 ASP   A O   1 
ATOM   1964 C  CB  . ASP   A 1 243 ? 15.76700  -51.29400 -12.26000 1.000 78.08256  ? 279 ASP   A CB  1 
ATOM   1965 C  CG  . ASP   A 1 243 ? 16.01500  -52.77000 -12.52800 1.000 82.63992  ? 279 ASP   A CG  1 
ATOM   1966 O  OD1 . ASP   A 1 243 ? 16.11700  -53.54900 -11.55600 1.000 85.89387  ? 279 ASP   A OD1 1 
ATOM   1967 O  OD2 . ASP   A 1 243 ? 16.11000  -53.15300 -13.71300 1.000 87.51681  ? 279 ASP   A OD2 1 
ATOM   1968 N  N   . GLY   A 1 244 ? 18.11200  -51.75100 -9.75000  1.000 62.69555  ? 280 GLY   A N   1 
ATOM   1969 C  CA  . GLY   A 1 244 ? 19.52400  -51.77800 -9.43600  1.000 64.23351  ? 280 GLY   A CA  1 
ATOM   1970 C  C   . GLY   A 1 244 ? 20.02900  -50.59100 -8.65100  1.000 61.28494  ? 280 GLY   A C   1 
ATOM   1971 O  O   . GLY   A 1 244 ? 21.24400  -50.39800 -8.56700  1.000 60.03027  ? 280 GLY   A O   1 
ATOM   1972 N  N   . LEU   A 1 245 ? 19.14100  -49.78900 -8.07500  1.000 58.36514  ? 281 LEU   A N   1 
ATOM   1973 C  CA  . LEU   A 1 245 ? 19.50300  -48.62200 -7.28900  1.000 59.51768  ? 281 LEU   A CA  1 
ATOM   1974 C  C   . LEU   A 1 245 ? 18.94800  -48.75100 -5.87700  1.000 58.68184  ? 281 LEU   A C   1 
ATOM   1975 O  O   . LEU   A 1 245 ? 18.00700  -49.51800 -5.64100  1.000 62.91974  ? 281 LEU   A O   1 
ATOM   1976 C  CB  . LEU   A 1 245 ? 18.97000  -47.34100 -7.94600  1.000 55.51303  ? 281 LEU   A CB  1 
ATOM   1977 C  CG  . LEU   A 1 245 ? 19.52200  -47.07100 -9.34500  1.000 54.02048  ? 281 LEU   A CG  1 
ATOM   1978 C  CD1 . LEU   A 1 245 ? 18.83200  -45.86800 -9.96600  1.000 57.98877  ? 281 LEU   A CD1 1 
ATOM   1979 C  CD2 . LEU   A 1 245 ? 21.02600  -46.86100 -9.28900  1.000 53.47030  ? 281 LEU   A CD2 1 
ATOM   1980 N  N   . PRO   A 1 246 ? 19.52300  -48.03800 -4.90700  1.000 56.48565  ? 282 PRO   A N   1 
ATOM   1981 C  CA  . PRO   A 1 246 ? 18.98300  -48.08400 -3.53800  1.000 52.41230  ? 282 PRO   A CA  1 
ATOM   1982 C  C   . PRO   A 1 246 ? 17.53400  -47.62100 -3.50700  1.000 59.09032  ? 282 PRO   A C   1 
ATOM   1983 O  O   . PRO   A 1 246 ? 17.20500  -46.52000 -3.95300  1.000 55.87529  ? 282 PRO   A O   1 
ATOM   1984 C  CB  . PRO   A 1 246 ? 19.90300  -47.13300 -2.76500  1.000 55.13577  ? 282 PRO   A CB  1 
ATOM   1985 C  CG  . PRO   A 1 246 ? 21.18000  -47.14800 -3.53700  1.000 56.97509  ? 282 PRO   A CG  1 
ATOM   1986 C  CD  . PRO   A 1 246 ? 20.78100  -47.27200 -4.97700  1.000 57.76346  ? 282 PRO   A CD  1 
ATOM   1987 N  N   . GLN   A 1 247 ? 16.66300  -48.47200 -2.95700  1.000 57.28430  ? 283 GLN   A N   1 
ATOM   1988 C  CA  . GLN   A 1 247 ? 15.22400  -48.23800 -3.03200  1.000 64.87545  ? 283 GLN   A CA  1 
ATOM   1989 C  C   . GLN   A 1 247 ? 14.76800  -47.01200 -2.25100  1.000 58.93777  ? 283 GLN   A C   1 
ATOM   1990 O  O   . GLN   A 1 247 ? 13.60500  -46.61500 -2.38900  1.000 62.69314  ? 283 GLN   A O   1 
ATOM   1991 C  CB  . GLN   A 1 247 ? 14.46300  -49.47300 -2.54700  1.000 62.17687  ? 283 GLN   A CB  1 
ATOM   1992 C  CG  . GLN   A 1 247 ? 14.46800  -50.62500 -3.54100  1.000 72.56168  ? 283 GLN   A CG  1 
ATOM   1993 C  CD  . GLN   A 1 247 ? 13.70700  -50.30600 -4.81600  1.000 73.67234  ? 283 GLN   A CD  1 
ATOM   1994 O  OE1 . GLN   A 1 247 ? 12.61500  -49.73700 -4.77500  1.000 74.67217  ? 283 GLN   A OE1 1 
ATOM   1995 N  NE2 . GLN   A 1 247 ? 14.28400  -50.66700 -5.95700  1.000 74.26319  ? 283 GLN   A NE2 1 
ATOM   1996 N  N   . GLN   A 1 248 ? 15.63900  -46.40200 -1.44400  1.000 59.92544  ? 284 GLN   A N   1 
ATOM   1997 C  CA  . GLN   A 1 248 ? 15.27600  -45.14700 -0.79600  1.000 60.19801  ? 284 GLN   A CA  1 
ATOM   1998 C  C   . GLN   A 1 248 ? 14.97600  -44.04400 -1.80300  1.000 51.12866  ? 284 GLN   A C   1 
ATOM   1999 O  O   . GLN   A 1 248 ? 14.24600  -43.10400 -1.47200  1.000 51.50994  ? 284 GLN   A O   1 
ATOM   2000 C  CB  . GLN   A 1 248 ? 16.38700  -44.68400 0.15200   1.000 56.94818  ? 284 GLN   A CB  1 
ATOM   2001 C  CG  . GLN   A 1 248 ? 16.53900  -45.52300 1.41500   1.000 58.06435  ? 284 GLN   A CG  1 
ATOM   2002 C  CD  . GLN   A 1 248 ? 17.59500  -46.59900 1.28100   1.000 55.57000  ? 284 GLN   A CD  1 
ATOM   2003 O  OE1 . GLN   A 1 248 ? 17.83000  -47.12600 0.19400   1.000 62.45327  ? 284 GLN   A OE1 1 
ATOM   2004 N  NE2 . GLN   A 1 248 ? 18.24700  -46.92500 2.38800   1.000 58.62784  ? 284 GLN   A NE2 1 
ATOM   2005 N  N   . PHE   A 1 249 ? 15.52500  -44.12700 -3.01800  1.000 54.16368  ? 285 PHE   A N   1 
ATOM   2006 C  CA  . PHE   A 1 249 ? 15.23200  -43.10700 -4.02000  1.000 52.11043  ? 285 PHE   A CA  1 
ATOM   2007 C  C   . PHE   A 1 249 ? 13.83500  -43.28600 -4.59600  1.000 53.31501  ? 285 PHE   A C   1 
ATOM   2008 O  O   . PHE   A 1 249 ? 13.15800  -42.30100 -4.91300  1.000 48.95567  ? 285 PHE   A O   1 
ATOM   2009 C  CB  . PHE   A 1 249 ? 16.27700  -43.14100 -5.13200  1.000 52.35146  ? 285 PHE   A CB  1 
ATOM   2010 C  CG  . PHE   A 1 249 ? 17.58300  -42.52100 -4.74700  1.000 48.01401  ? 285 PHE   A CG  1 
ATOM   2011 C  CD1 . PHE   A 1 249 ? 17.73100  -41.14500 -4.73100  1.000 48.09751  ? 285 PHE   A CD1 1 
ATOM   2012 C  CD2 . PHE   A 1 249 ? 18.66500  -43.31300 -4.40600  1.000 50.15838  ? 285 PHE   A CD2 1 
ATOM   2013 C  CE1 . PHE   A 1 249 ? 18.93600  -40.57000 -4.37700  1.000 46.97541  ? 285 PHE   A CE1 1 
ATOM   2014 C  CE2 . PHE   A 1 249 ? 19.87000  -42.74700 -4.05400  1.000 44.24952  ? 285 PHE   A CE2 1 
ATOM   2015 C  CZ  . PHE   A 1 249 ? 20.00500  -41.37200 -4.03800  1.000 50.02909  ? 285 PHE   A CZ  1 
ATOM   2016 N  N   . ALA   A 1 250 ? 13.39800  -44.53700 -4.76100  1.000 52.34585  ? 286 ALA   A N   1 
ATOM   2017 C  CA  . ALA   A 1 250 ? 12.01700  -44.78600 -5.15600  1.000 55.85661  ? 286 ALA   A CA  1 
ATOM   2018 C  C   . ALA   A 1 250 ? 11.06400  -44.46200 -4.01700  1.000 58.03534  ? 286 ALA   A C   1 
ATOM   2019 O  O   . ALA   A 1 250 ? 9.97200   -43.92300 -4.24100  1.000 61.38918  ? 286 ALA   A O   1 
ATOM   2020 C  CB  . ALA   A 1 250 ? 11.85100  -46.23900 -5.59200  1.000 55.87875  ? 286 ALA   A CB  1 
ATOM   2021 N  N   . GLU   A 1 251 ? 11.46000  -44.79400 -2.78800  1.000 52.82053  ? 287 GLU   A N   1 
ATOM   2022 C  CA  . GLU   A 1 251 ? 10.65600  -44.43600 -1.62700  1.000 58.21802  ? 287 GLU   A CA  1 
ATOM   2023 C  C   . GLU   A 1 251 ? 10.51000  -42.92600 -1.50300  1.000 58.55924  ? 287 GLU   A C   1 
ATOM   2024 O  O   . GLU   A 1 251 ? 9.44700   -42.43100 -1.11000  1.000 47.90430  ? 287 GLU   A O   1 
ATOM   2025 C  CB  . GLU   A 1 251 ? 11.29000  -45.02400 -0.36900  1.000 56.51761  ? 287 GLU   A CB  1 
ATOM   2026 C  CG  . GLU   A 1 251 ? 10.41800  -44.97700 0.85600   1.000 67.69238  ? 287 GLU   A CG  1 
ATOM   2027 C  CD  . GLU   A 1 251 ? 11.03100  -45.73500 2.01000   1.000 74.92297  ? 287 GLU   A CD  1 
ATOM   2028 O  OE1 . GLU   A 1 251 ? 12.06700  -46.40300 1.79700   1.000 70.92898  ? 287 GLU   A OE1 1 
ATOM   2029 O  OE2 . GLU   A 1 251 ? 10.48100  -45.66300 3.12800   1.000 81.60969  ? 287 GLU   A OE2 1 
ATOM   2030 N  N   . TYR   A 1 252 ? 11.55900  -42.18000 -1.84700  1.000 50.48782  ? 288 TYR   A N   1 
ATOM   2031 C  CA  . TYR   A 1 252 ? 11.46800  -40.72500 -1.83400  1.000 52.86750  ? 288 TYR   A CA  1 
ATOM   2032 C  C   . TYR   A 1 252 ? 10.46900  -40.22400 -2.87100  1.000 46.51932  ? 288 TYR   A C   1 
ATOM   2033 O  O   . TYR   A 1 252 ? 9.61100   -39.38700 -2.56600  1.000 49.66165  ? 288 TYR   A O   1 
ATOM   2034 C  CB  . TYR   A 1 252 ? 12.84400  -40.10400 -2.07800  1.000 47.77272  ? 288 TYR   A CB  1 
ATOM   2035 C  CG  . TYR   A 1 252 ? 12.77500  -38.61400 -2.34300  1.000 47.20794  ? 288 TYR   A CG  1 
ATOM   2036 C  CD1 . TYR   A 1 252 ? 12.74800  -37.70200 -1.29500  1.000 47.35317  ? 288 TYR   A CD1 1 
ATOM   2037 C  CD2 . TYR   A 1 252 ? 12.73100  -38.12100 -3.64100  1.000 47.18977  ? 288 TYR   A CD2 1 
ATOM   2038 C  CE1 . TYR   A 1 252 ? 12.68400  -36.34600 -1.53300  1.000 42.00879  ? 288 TYR   A CE1 1 
ATOM   2039 C  CE2 . TYR   A 1 252 ? 12.66300  -36.76700 -3.88800  1.000 47.02651  ? 288 TYR   A CE2 1 
ATOM   2040 C  CZ  . TYR   A 1 252 ? 12.64000  -35.88400 -2.83100  1.000 44.00236  ? 288 TYR   A CZ  1 
ATOM   2041 O  OH  . TYR   A 1 252 ? 12.56700  -34.52700 -3.07400  1.000 43.65629  ? 288 TYR   A OH  1 
ATOM   2042 N  N   . LEU   A 1 253 ? 10.56500  -40.72300 -4.10900  1.000 43.54930  ? 289 LEU   A N   1 
ATOM   2043 C  CA  . LEU   A 1 253 ? 9.71500   -40.19900 -5.17400  1.000 48.23585  ? 289 LEU   A CA  1 
ATOM   2044 C  C   . LEU   A 1 253 ? 8.24600   -40.51800 -4.92000  1.000 51.94077  ? 289 LEU   A C   1 
ATOM   2045 O  O   . LEU   A 1 253 ? 7.37800   -39.66400 -5.13000  1.000 48.02033  ? 289 LEU   A O   1 
ATOM   2046 C  CB  . LEU   A 1 253 ? 10.16200  -40.74800 -6.52900  1.000 45.90367  ? 289 LEU   A CB  1 
ATOM   2047 C  CG  . LEU   A 1 253 ? 9.47700   -40.12000 -7.74800  1.000 45.83423  ? 289 LEU   A CG  1 
ATOM   2048 C  CD1 . LEU   A 1 253 ? 9.64900   -38.61100 -7.74100  1.000 45.62781  ? 289 LEU   A CD1 1 
ATOM   2049 C  CD2 . LEU   A 1 253 ? 10.01000  -40.71600 -9.04300  1.000 47.52720  ? 289 LEU   A CD2 1 
ATOM   2050 N  N   . ASP   A 1 254 ? 7.94700   -41.73600 -4.45900  1.000 51.44728  ? 290 ASP   A N   1 
ATOM   2051 C  CA  . ASP   A 1 254 ? 6.56300   -42.07900 -4.14800  1.000 54.39036  ? 290 ASP   A CA  1 
ATOM   2052 C  C   . ASP   A 1 254 ? 6.02000   -41.24900 -2.99600  1.000 53.70266  ? 290 ASP   A C   1 
ATOM   2053 O  O   . ASP   A 1 254 ? 4.82500   -40.93600 -2.97000  1.000 54.69086  ? 290 ASP   A O   1 
ATOM   2054 C  CB  . ASP   A 1 254 ? 6.44200   -43.56500 -3.81900  1.000 56.75551  ? 290 ASP   A CB  1 
ATOM   2055 C  CG  . ASP   A 1 254 ? 6.52800   -44.44200 -5.04800  1.000 61.66624  ? 290 ASP   A CG  1 
ATOM   2056 O  OD1 . ASP   A 1 254 ? 6.18000   -43.96300 -6.14800  1.000 62.56043  ? 290 ASP   A OD1 1 
ATOM   2057 O  OD2 . ASP   A 1 254 ? 6.93900   -45.61400 -4.91100  1.000 64.30922  ? 290 ASP   A OD2 1 
ATOM   2058 N  N   . SER   A 1 255 ? 6.87200   -40.89100 -2.03300  1.000 51.58936  ? 291 SER   A N   1 
ATOM   2059 C  CA  . SER   A 1 255 ? 6.40700   -40.09100 -0.90600  1.000 58.27591  ? 291 SER   A CA  1 
ATOM   2060 C  C   . SER   A 1 255 ? 6.03500   -38.68200 -1.35200  1.000 60.66460  ? 291 SER   A C   1 
ATOM   2061 O  O   . SER   A 1 255 ? 4.94100   -38.19300 -1.04200  1.000 56.91015  ? 291 SER   A O   1 
ATOM   2062 C  CB  . SER   A 1 255 ? 7.47400   -40.05200 0.18800   1.000 59.83200  ? 291 SER   A CB  1 
ATOM   2063 O  OG  . SER   A 1 255 ? 7.07300   -39.21000 1.25400   1.000 58.46357  ? 291 SER   A OG  1 
ATOM   2064 N  N   . VAL   A 1 256 ? 6.92800   -38.01800 -2.09600  1.000 52.57006  ? 292 VAL   A N   1 
ATOM   2065 C  CA  . VAL   A 1 256 ? 6.66400   -36.64700 -2.53000  1.000 50.60012  ? 292 VAL   A CA  1 
ATOM   2066 C  C   . VAL   A 1 256 ? 5.52500   -36.58300 -3.54000  1.000 53.50914  ? 292 VAL   A C   1 
ATOM   2067 O  O   . VAL   A 1 256 ? 4.85100   -35.55100 -3.64900  1.000 51.66417  ? 292 VAL   A O   1 
ATOM   2068 C  CB  . VAL   A 1 256 ? 7.93800   -35.99600 -3.10300  1.000 50.94573  ? 292 VAL   A CB  1 
ATOM   2069 C  CG1 . VAL   A 1 256 ? 9.03600   -35.95900 -2.05100  1.000 50.18321  ? 292 VAL   A CG1 1 
ATOM   2070 C  CG2 . VAL   A 1 256 ? 8.40900   -36.72400 -4.35100  1.000 50.22483  ? 292 VAL   A CG2 1 
ATOM   2071 N  N   . ARG   A 1 257 ? 5.29700   -37.65900 -4.29600  1.000 52.32915  ? 293 ARG   A N   1 
ATOM   2072 C  CA  . ARG   A 1 257 ? 4.15200   -37.71000 -5.19600  1.000 58.63963  ? 293 ARG   A CA  1 
ATOM   2073 C  C   . ARG   A 1 257 ? 2.83500   -37.87400 -4.45200  1.000 59.74437  ? 293 ARG   A C   1 
ATOM   2074 O  O   . ARG   A 1 257 ? 1.78000   -37.56500 -5.01400  1.000 62.70026  ? 293 ARG   A O   1 
ATOM   2075 C  CB  . ARG   A 1 257 ? 4.31900   -38.84900 -6.20400  1.000 59.25132  ? 293 ARG   A CB  1 
ATOM   2076 C  CG  . ARG   A 1 257 ? 5.26300   -38.52800 -7.34800  1.000 55.84903  ? 293 ARG   A CG  1 
ATOM   2077 C  CD  . ARG   A 1 257 ? 5.37100   -39.69200 -8.31600  1.000 58.00489  ? 293 ARG   A CD  1 
ATOM   2078 N  NE  . ARG   A 1 257 ? 6.16100   -39.34600 -9.49100  1.000 48.87010  ? 293 ARG   A NE  1 
ATOM   2079 C  CZ  . ARG   A 1 257 ? 6.45700   -40.19500 -10.46300 1.000 49.69300  ? 293 ARG   A CZ  1 
ATOM   2080 N  NH1 . ARG   A 1 257 ? 6.05100   -41.45400 -10.42900 1.000 58.51384  ? 293 ARG   A NH1 1 
ATOM   2081 N  NH2 . ARG   A 1 257 ? 7.17800   -39.77100 -11.49800 1.000 48.98705  ? 293 ARG   A NH2 1 
ATOM   2082 N  N   . SER   A 1 258 ? 2.87300   -38.33800 -3.20300  1.000 60.15194  ? 294 SER   A N   1 
ATOM   2083 C  CA  . SER   A 1 258 ? 1.67300   -38.56200 -2.41100  1.000 61.79861  ? 294 SER   A CA  1 
ATOM   2084 C  C   . SER   A 1 258 ? 1.35800   -37.40900 -1.46800  1.000 65.20772  ? 294 SER   A C   1 
ATOM   2085 O  O   . SER   A 1 258 ? 0.35300   -37.47000 -0.75400  1.000 60.60301  ? 294 SER   A O   1 
ATOM   2086 C  CB  . SER   A 1 258 ? 1.81100   -39.86200 -1.61100  1.000 65.17226  ? 294 SER   A CB  1 
ATOM   2087 O  OG  . SER   A 1 258 ? 2.08400   -40.95500 -2.47100  1.000 70.12821  ? 294 SER   A OG  1 
ATOM   2088 N  N   . LEU   A 1 259 ? 2.18300   -36.36700 -1.45200  1.000 54.71980  ? 295 LEU   A N   1 
ATOM   2089 C  CA  . LEU   A 1 259 ? 1.94500   -35.23600 -0.56700  1.000 57.33744  ? 295 LEU   A CA  1 
ATOM   2090 C  C   . LEU   A 1 259 ? 0.69600   -34.46900 -1.00100  1.000 55.65962  ? 295 LEU   A C   1 
ATOM   2091 O  O   . LEU   A 1 259 ? 0.46600   -34.28400 -2.20100  1.000 55.81051  ? 295 LEU   A O   1 
ATOM   2092 C  CB  . LEU   A 1 259 ? 3.15100   -34.29600 -0.56800  1.000 52.58896  ? 295 LEU   A CB  1 
ATOM   2093 C  CG  . LEU   A 1 259 ? 4.39900   -34.75200 0.18900   1.000 54.66336  ? 295 LEU   A CG  1 
ATOM   2094 C  CD1 . LEU   A 1 259 ? 5.58500   -33.86200 -0.15400  1.000 52.55480  ? 295 LEU   A CD1 1 
ATOM   2095 C  CD2 . LEU   A 1 259 ? 4.14400   -34.74900 1.68600   1.000 50.70436  ? 295 LEU   A CD2 1 
ATOM   2096 N  N   . PRO   A 1 260 ? -0.12900  -34.01600 -0.05500  1.000 63.39772  ? 296 PRO   A N   1 
ATOM   2097 C  CA  . PRO   A 1 260 ? -1.23700  -33.11500 -0.39900  1.000 54.06266  ? 296 PRO   A CA  1 
ATOM   2098 C  C   . PRO   A 1 260 ? -0.73300  -31.80300 -0.98500  1.000 62.80081  ? 296 PRO   A C   1 
ATOM   2099 O  O   . PRO   A 1 260 ? 0.45500   -31.47500 -0.94800  1.000 57.72000  ? 296 PRO   A O   1 
ATOM   2100 C  CB  . PRO   A 1 260 ? -1.94300  -32.88800 0.94200   1.000 63.68788  ? 296 PRO   A CB  1 
ATOM   2101 C  CG  . PRO   A 1 260 ? -1.57800  -34.06800 1.76900   1.000 68.81880  ? 296 PRO   A CG  1 
ATOM   2102 C  CD  . PRO   A 1 260 ? -0.18700  -34.45000 1.35200   1.000 59.55812  ? 296 PRO   A CD  1 
ATOM   2103 N  N   . PHE   A 1 261 ? -1.68300  -31.02900 -1.51500  1.000 64.20120  ? 297 PHE   A N   1 
ATOM   2104 C  CA  . PHE   A 1 261 ? -1.35200  -29.79800 -2.22900  1.000 63.29568  ? 297 PHE   A CA  1 
ATOM   2105 C  C   . PHE   A 1 261 ? -0.73600  -28.75700 -1.30100  1.000 63.56349  ? 297 PHE   A C   1 
ATOM   2106 O  O   . PHE   A 1 261 ? 0.28100   -28.14000 -1.63400  1.000 58.87609  ? 297 PHE   A O   1 
ATOM   2107 C  CB  . PHE   A 1 261 ? -2.60300  -29.23200 -2.90600  1.000 54.84145  ? 297 PHE   A CB  1 
ATOM   2108 C  CG  . PHE   A 1 261 ? -2.37800  -27.91000 -3.58800  1.000 61.70197  ? 297 PHE   A CG  1 
ATOM   2109 C  CD1 . PHE   A 1 261 ? -1.57100  -27.82800 -4.71100  1.000 61.02512  ? 297 PHE   A CD1 1 
ATOM   2110 C  CD2 . PHE   A 1 261 ? -2.97600  -26.75400 -3.11500  1.000 66.60169  ? 297 PHE   A CD2 1 
ATOM   2111 C  CE1 . PHE   A 1 261 ? -1.36000  -26.61900 -5.34400  1.000 65.21054  ? 297 PHE   A CE1 1 
ATOM   2112 C  CE2 . PHE   A 1 261 ? -2.77300  -25.54000 -3.75000  1.000 63.76463  ? 297 PHE   A CE2 1 
ATOM   2113 C  CZ  . PHE   A 1 261 ? -1.96200  -25.47400 -4.86600  1.000 64.19946  ? 297 PHE   A CZ  1 
ATOM   2114 N  N   . ASP   A 1 262 ? -1.35200  -28.52600 -0.14400  1.000 59.76633  ? 298 ASP   A N   1 
ATOM   2115 C  CA  . ASP   A 1 262 ? -0.89800  -27.48800 0.77200   1.000 66.42189  ? 298 ASP   A CA  1 
ATOM   2116 C  C   . ASP   A 1 262 ? -0.04100  -28.03000 1.90900   1.000 70.15445  ? 298 ASP   A C   1 
ATOM   2117 O  O   . ASP   A 1 262 ? 0.22600   -27.30000 2.86900   1.000 74.71402  ? 298 ASP   A O   1 
ATOM   2118 C  CB  . ASP   A 1 262 ? -2.09800  -26.72600 1.34100   1.000 71.13178  ? 298 ASP   A CB  1 
ATOM   2119 C  CG  . ASP   A 1 262 ? -3.06400  -27.62800 2.08600   1.000 73.77846  ? 298 ASP   A CG  1 
ATOM   2120 O  OD1 . ASP   A 1 262 ? -2.88300  -28.86300 2.04300   1.000 74.50614  ? 298 ASP   A OD1 1 
ATOM   2121 O  OD2 . ASP   A 1 262 ? -4.00500  -27.10200 2.71800   1.000 78.17541  ? 298 ASP   A OD2 1 
ATOM   2122 N  N   . ALA   A 1 263 ? 0.39800   -29.28100 1.82700   1.000 65.17506  ? 299 ALA   A N   1 
ATOM   2123 C  CA  . ALA   A 1 263 ? 1.11300   -29.89600 2.93400   1.000 68.91490  ? 299 ALA   A CA  1 
ATOM   2124 C  C   . ALA   A 1 263 ? 2.56600   -29.43900 2.97500   1.000 61.98375  ? 299 ALA   A C   1 
ATOM   2125 O  O   . ALA   A 1 263 ? 3.19600   -29.19800 1.94200   1.000 62.92319  ? 299 ALA   A O   1 
ATOM   2126 C  CB  . ALA   A 1 263 ? 1.05300   -31.41900 2.82900   1.000 66.17559  ? 299 ALA   A CB  1 
ATOM   2127 N  N   . GLU   A 1 264 ? 3.09300   -29.31500 4.18900   1.000 66.50572  ? 300 GLU   A N   1 
ATOM   2128 C  CA  . GLU   A 1 264 ? 4.50700   -29.00900 4.36200   1.000 73.85105  ? 300 GLU   A CA  1 
ATOM   2129 C  C   . GLU   A 1 264 ? 5.31300   -30.30000 4.30000   1.000 68.44203  ? 300 GLU   A C   1 
ATOM   2130 O  O   . GLU   A 1 264 ? 5.11600   -31.18000 5.14600   1.000 68.53583  ? 300 GLU   A O   1 
ATOM   2131 C  CB  . GLU   A 1 264 ? 4.75900   -28.30300 5.68600   1.000 76.47610  ? 300 GLU   A CB  1 
ATOM   2132 C  CG  . GLU   A 1 264 ? 6.21800   -27.90200 5.88100   1.000 74.98205  ? 300 GLU   A CG  1 
ATOM   2133 C  CD  . GLU   A 1 264 ? 6.54600   -27.56400 7.32100   1.000 86.57501  ? 300 GLU   A CD  1 
ATOM   2134 O  OE1 . GLU   A 1 264 ? 5.67600   -27.76800 8.19400   1.000 103.58115 ? 300 GLU   A OE1 1 
ATOM   2135 O  OE2 . GLU   A 1 264 ? 7.67600   -27.09900 7.58000   1.000 90.48215  ? 300 GLU   A OE2 1 
ATOM   2136 N  N   . PRO   A 1 265 ? 6.21700   -30.45600 3.33300   1.000 64.87857  ? 301 PRO   A N   1 
ATOM   2137 C  CA  . PRO   A 1 265 ? 6.90600   -31.73600 3.18400   1.000 65.46230  ? 301 PRO   A CA  1 
ATOM   2138 C  C   . PRO   A 1 265 ? 7.86300   -31.97700 4.33300   1.000 58.20719  ? 301 PRO   A C   1 
ATOM   2139 O  O   . PRO   A 1 265 ? 8.40500   -31.02400 4.92200   1.000 53.96598  ? 301 PRO   A O   1 
ATOM   2140 C  CB  . PRO   A 1 265 ? 7.66000   -31.57900 1.85100   1.000 57.21814  ? 301 PRO   A CB  1 
ATOM   2141 C  CG  . PRO   A 1 265 ? 7.04400   -30.38200 1.17600   1.000 60.04864  ? 301 PRO   A CG  1 
ATOM   2142 C  CD  . PRO   A 1 265 ? 6.59600   -29.49200 2.28800   1.000 61.49615  ? 301 PRO   A CD  1 
ATOM   2143 N  N   . PRO   A 1 266 ? 8.09500   -33.23900 4.70900   1.000 58.95072  ? 302 PRO   A N   1 
ATOM   2144 C  CA  . PRO   A 1 266 ? 9.07800   -33.52700 5.76000   1.000 53.68557  ? 302 PRO   A CA  1 
ATOM   2145 C  C   . PRO   A 1 266 ? 10.49800  -33.52100 5.21900   1.000 57.15081  ? 302 PRO   A C   1 
ATOM   2146 O  O   . PRO   A 1 266 ? 11.04500  -34.57400 4.87100   1.000 55.78285  ? 302 PRO   A O   1 
ATOM   2147 C  CB  . PRO   A 1 266 ? 8.66200   -34.91600 6.25800   1.000 58.45916  ? 302 PRO   A CB  1 
ATOM   2148 C  CG  . PRO   A 1 266 ? 8.01500   -35.55000 5.07500   1.000 58.71149  ? 302 PRO   A CG  1 
ATOM   2149 C  CD  . PRO   A 1 266 ? 7.34700   -34.44100 4.29900   1.000 59.12922  ? 302 PRO   A CD  1 
ATOM   2150 N  N   . TYR   A 1 267 ? 11.10000  -32.33200 5.15100   1.000 51.64564  ? 303 TYR   A N   1 
ATOM   2151 C  CA  . TYR   A 1 267 ? 12.41200  -32.19400 4.52300   1.000 57.16863  ? 303 TYR   A CA  1 
ATOM   2152 C  C   . TYR   A 1 267 ? 13.46400  -33.02400 5.24600   1.000 52.88323  ? 303 TYR   A C   1 
ATOM   2153 O  O   . TYR   A 1 267 ? 14.20000  -33.79400 4.61800   1.000 55.68229  ? 303 TYR   A O   1 
ATOM   2154 C  CB  . TYR   A 1 267 ? 12.82500  -30.72400 4.48500   1.000 56.19394  ? 303 TYR   A CB  1 
ATOM   2155 C  CG  . TYR   A 1 267 ? 11.83800  -29.81900 3.78200   1.000 56.52249  ? 303 TYR   A CG  1 
ATOM   2156 C  CD1 . TYR   A 1 267 ? 11.83700  -29.70400 2.39800   1.000 51.05179  ? 303 TYR   A CD1 1 
ATOM   2157 C  CD2 . TYR   A 1 267 ? 10.91500  -29.07300 4.50200   1.000 55.76829  ? 303 TYR   A CD2 1 
ATOM   2158 C  CE1 . TYR   A 1 267 ? 10.94100  -28.87600 1.75100   1.000 53.22071  ? 303 TYR   A CE1 1 
ATOM   2159 C  CE2 . TYR   A 1 267 ? 10.01600  -28.23900 3.86400   1.000 57.94392  ? 303 TYR   A CE2 1 
ATOM   2160 C  CZ  . TYR   A 1 267 ? 10.03500  -28.14700 2.48800   1.000 58.42394  ? 303 TYR   A CZ  1 
ATOM   2161 O  OH  . TYR   A 1 267 ? 9.14700   -27.31700 1.84300   1.000 52.40854  ? 303 TYR   A OH  1 
ATOM   2162 N  N   . GLU   A 1 268 ? 13.55500  -32.87900 6.57100   1.000 53.09415  ? 304 GLU   A N   1 
ATOM   2163 C  CA  . GLU   A 1 268 ? 14.59900  -33.58700 7.30600   1.000 58.27346  ? 304 GLU   A CA  1 
ATOM   2164 C  C   . GLU   A 1 268 ? 14.40200  -35.09600 7.24000   1.000 57.27502  ? 304 GLU   A C   1 
ATOM   2165 O  O   . GLU   A 1 268 ? 15.38300  -35.84800 7.23400   1.000 58.36095  ? 304 GLU   A O   1 
ATOM   2166 C  CB  . GLU   A 1 268 ? 14.64500  -33.11000 8.75900   1.000 62.31976  ? 304 GLU   A CB  1 
ATOM   2167 C  CG  . GLU   A 1 268 ? 15.85700  -33.61300 9.55000   1.000 63.47735  ? 304 GLU   A CG  1 
ATOM   2168 C  CD  . GLU   A 1 268 ? 17.18100  -33.04300 9.05400   1.000 73.47167  ? 304 GLU   A CD  1 
ATOM   2169 O  OE1 . GLU   A 1 268 ? 17.16900  -32.09400 8.24000   1.000 71.42420  ? 304 GLU   A OE1 1 
ATOM   2170 O  OE2 . GLU   A 1 268 ? 18.24000  -33.54400 9.48700   1.000 79.16089  ? 304 GLU   A OE2 1 
ATOM   2171 N  N   . GLU   A 1 269 ? 13.14900  -35.55500 7.17500   1.000 55.13781  ? 305 GLU   A N   1 
ATOM   2172 C  CA  . GLU   A 1 269 ? 12.89100  -36.98100 7.00300   1.000 55.43920  ? 305 GLU   A CA  1 
ATOM   2173 C  C   . GLU   A 1 269 ? 13.41700  -37.47500 5.66000   1.000 55.56914  ? 305 GLU   A C   1 
ATOM   2174 O  O   . GLU   A 1 269 ? 13.99400  -38.56600 5.57600   1.000 54.26546  ? 305 GLU   A O   1 
ATOM   2175 C  CB  . GLU   A 1 269 ? 11.39200  -37.26300 7.13800   1.000 54.48858  ? 305 GLU   A CB  1 
ATOM   2176 C  CG  . GLU   A 1 269 ? 11.05900  -38.53800 7.90300   1.000 62.45618  ? 305 GLU   A CG  1 
ATOM   2177 C  CD  . GLU   A 1 269 ? 9.63300   -38.55100 8.43200   1.000 71.71035  ? 305 GLU   A CD  1 
ATOM   2178 O  OE1 . GLU   A 1 269 ? 8.69400   -38.33400 7.63700   1.000 74.52586  ? 305 GLU   A OE1 1 
ATOM   2179 O  OE2 . GLU   A 1 269 ? 9.45500   -38.76500 9.65000   1.000 74.12985  ? 305 GLU   A OE2 1 
ATOM   2180 N  N   . TYR   A 1 270 ? 13.22900  -36.68600 4.59700   1.000 49.07689  ? 306 TYR   A N   1 
ATOM   2181 C  CA  . TYR   A 1 270 ? 13.73800  -37.08300 3.28800   1.000 57.48756  ? 306 TYR   A CA  1 
ATOM   2182 C  C   . TYR   A 1 270 ? 15.26000  -37.09600 3.26900   1.000 52.33146  ? 306 TYR   A C   1 
ATOM   2183 O  O   . TYR   A 1 270 ? 15.86900  -37.97600 2.65100   1.000 50.81692  ? 306 TYR   A O   1 
ATOM   2184 C  CB  . TYR   A 1 270 ? 13.20000  -36.15000 2.20400   1.000 50.83690  ? 306 TYR   A CB  1 
ATOM   2185 C  CG  . TYR   A 1 270 ? 11.70600  -36.23800 2.00800   1.000 50.55555  ? 306 TYR   A CG  1 
ATOM   2186 C  CD1 . TYR   A 1 270 ? 11.03500  -37.44400 2.15200   1.000 55.32613  ? 306 TYR   A CD1 1 
ATOM   2187 C  CD2 . TYR   A 1 270 ? 10.96600  -35.11000 1.67900   1.000 50.98052  ? 306 TYR   A CD2 1 
ATOM   2188 C  CE1 . TYR   A 1 270 ? 9.66000   -37.52000 1.97200   1.000 56.85677  ? 306 TYR   A CE1 1 
ATOM   2189 C  CE2 . TYR   A 1 270 ? 9.60800   -35.17500 1.49600   1.000 54.64372  ? 306 TYR   A CE2 1 
ATOM   2190 C  CZ  . TYR   A 1 270 ? 8.95500   -36.37900 1.64400   1.000 58.39185  ? 306 TYR   A CZ  1 
ATOM   2191 O  OH  . TYR   A 1 270 ? 7.59800   -36.43000 1.45600   1.000 58.71855  ? 306 TYR   A OH  1 
ATOM   2192 N  N   . ARG   A 1 271 ? 15.89200  -36.12200 3.93200   1.000 46.56943  ? 307 ARG   A N   1 
ATOM   2193 C  CA  . ARG   A 1 271 ? 17.34900  -36.11700 4.02500   1.000 55.23036  ? 307 ARG   A CA  1 
ATOM   2194 C  C   . ARG   A 1 271 ? 17.85200  -37.32500 4.80500   1.000 55.37872  ? 307 ARG   A C   1 
ATOM   2195 O  O   . ARG   A 1 271 ? 18.87200  -37.92400 4.44300   1.000 54.57093  ? 307 ARG   A O   1 
ATOM   2196 C  CB  . ARG   A 1 271 ? 17.83300  -34.81500 4.67000   1.000 48.68474  ? 307 ARG   A CB  1 
ATOM   2197 C  CG  . ARG   A 1 271 ? 17.72400  -33.58900 3.77100   1.000 47.35923  ? 307 ARG   A CG  1 
ATOM   2198 C  CD  . ARG   A 1 271 ? 18.39900  -32.37400 4.39900   1.000 47.79979  ? 307 ARG   A CD  1 
ATOM   2199 N  NE  . ARG   A 1 271 ? 17.62900  -31.84300 5.51800   1.000 56.62074  ? 307 ARG   A NE  1 
ATOM   2200 C  CZ  . ARG   A 1 271 ? 16.75200  -30.85100 5.42100   1.000 59.69343  ? 307 ARG   A CZ  1 
ATOM   2201 N  NH1 . ARG   A 1 271 ? 16.53800  -30.22800 4.27300   1.000 52.17207  ? 307 ARG   A NH1 1 
ATOM   2202 N  NH2 . ARG   A 1 271 ? 16.07300  -30.47500 6.50100   1.000 56.83179  ? 307 ARG   A NH2 1 
ATOM   2203 N  N   . MET   A 1 272 ? 17.14900  -37.69600 5.87800   1.000 50.07565  ? 308 MET   A N   1 
ATOM   2204 C  CA  . MET   A 1 272 ? 17.52300  -38.88400 6.63700   1.000 53.37346  ? 308 MET   A CA  1 
ATOM   2205 C  C   . MET   A 1 272 ? 17.24500  -40.16000 5.85300   1.000 59.71357  ? 308 MET   A C   1 
ATOM   2206 O  O   . MET   A 1 272 ? 17.92600  -41.17200 6.05700   1.000 57.72568  ? 308 MET   A O   1 
ATOM   2207 C  CB  . MET   A 1 272 ? 16.78100  -38.91000 7.97300   1.000 58.38507  ? 308 MET   A CB  1 
ATOM   2208 C  CG  . MET   A 1 272 ? 17.26100  -37.86200 8.95500   1.000 69.04005  ? 308 MET   A CG  1 
ATOM   2209 S  SD  . MET   A 1 272 ? 19.00600  -38.08000 9.35700   1.000 87.33090  ? 308 MET   A SD  1 
ATOM   2210 C  CE  . MET   A 1 272 ? 19.39900  -36.47700 10.05200  1.000 78.73071  ? 308 MET   A CE  1 
ATOM   2211 N  N   . LEU   A 1 273 ? 16.24800  -40.13700 4.96400   1.000 52.82936  ? 309 LEU   A N   1 
ATOM   2212 C  CA  . LEU   A 1 273 ? 15.98100  -41.30000 4.12500   1.000 56.87461  ? 309 LEU   A CA  1 
ATOM   2213 C  C   . LEU   A 1 273 ? 17.11200  -41.52600 3.13000   1.000 54.63932  ? 309 LEU   A C   1 
ATOM   2214 O  O   . LEU   A 1 273 ? 17.55700  -42.66300 2.93300   1.000 56.16399  ? 309 LEU   A O   1 
ATOM   2215 C  CB  . LEU   A 1 273 ? 14.64700  -41.12600 3.39800   1.000 48.84336  ? 309 LEU   A CB  1 
ATOM   2216 C  CG  . LEU   A 1 273 ? 14.21400  -42.25400 2.45600   1.000 56.98519  ? 309 LEU   A CG  1 
ATOM   2217 C  CD1 . LEU   A 1 273 ? 13.95100  -43.53300 3.23200   1.000 58.70988  ? 309 LEU   A CD1 1 
ATOM   2218 C  CD2 . LEU   A 1 273 ? 12.98500  -41.85100 1.64300   1.000 52.02608  ? 309 LEU   A CD2 1 
ATOM   2219 N  N   . LEU   A 1 274 ? 17.59700  -40.45600 2.49900   1.000 55.47711  ? 310 LEU   A N   1 
ATOM   2220 C  CA  . LEU   A 1 274 ? 18.68200  -40.60100 1.53800   1.000 52.49911  ? 310 LEU   A CA  1 
ATOM   2221 C  C   . LEU   A 1 274 ? 20.02200  -40.85300 2.22000   1.000 50.32679  ? 310 LEU   A C   1 
ATOM   2222 O  O   . LEU   A 1 274 ? 20.86600  -41.56500 1.66500   1.000 51.16701  ? 310 LEU   A O   1 
ATOM   2223 C  CB  . LEU   A 1 274 ? 18.75500  -39.36500 0.63900   1.000 50.80240  ? 310 LEU   A CB  1 
ATOM   2224 C  CG  . LEU   A 1 274 ? 17.50200  -39.14000 -0.21300  1.000 47.95484  ? 310 LEU   A CG  1 
ATOM   2225 C  CD1 . LEU   A 1 274 ? 17.70100  -37.99100 -1.18300  1.000 37.95833  ? 310 LEU   A CD1 1 
ATOM   2226 C  CD2 . LEU   A 1 274 ? 17.11800  -40.40700 -0.95700  1.000 40.03267  ? 310 LEU   A CD2 1 
ATOM   2227 N  N   . LEU   A 1 275 ? 20.23600  -40.29500 3.41500   1.000 52.52338  ? 311 LEU   A N   1 
ATOM   2228 C  CA  . LEU   A 1 275 ? 21.46800  -40.57100 4.14800   1.000 54.20381  ? 311 LEU   A CA  1 
ATOM   2229 C  C   . LEU   A 1 275 ? 21.58600  -42.04400 4.51800   1.000 57.98422  ? 311 LEU   A C   1 
ATOM   2230 O  O   . LEU   A 1 275 ? 22.69600  -42.58800 4.53000   1.000 55.25847  ? 311 LEU   A O   1 
ATOM   2231 C  CB  . LEU   A 1 275 ? 21.54600  -39.70600 5.40700   1.000 60.09629  ? 311 LEU   A CB  1 
ATOM   2232 C  CG  . LEU   A 1 275 ? 22.10200  -38.29000 5.24500   1.000 61.10007  ? 311 LEU   A CG  1 
ATOM   2233 C  CD1 . LEU   A 1 275 ? 22.09900  -37.54700 6.57500   1.000 63.49819  ? 311 LEU   A CD1 1 
ATOM   2234 C  CD2 . LEU   A 1 275 ? 23.50600  -38.34400 4.67100   1.000 63.66317  ? 311 LEU   A CD2 1 
ATOM   2235 N  N   . SER   A 1 276 ? 20.46300  -42.70500 4.81600   1.000 53.44769  ? 312 SER   A N   1 
ATOM   2236 C  CA  . SER   A 1 276 ? 20.50600  -44.12600 5.14100   1.000 59.98545  ? 312 SER   A CA  1 
ATOM   2237 C  C   . SER   A 1 276 ? 21.07700  -44.96100 4.00300   1.000 58.53982  ? 312 SER   A C   1 
ATOM   2238 O  O   . SER   A 1 276 ? 21.53300  -46.08500 4.24400   1.000 57.28865  ? 312 SER   A O   1 
ATOM   2239 C  CB  . SER   A 1 276 ? 19.10700  -44.63200 5.49100   1.000 54.45338  ? 312 SER   A CB  1 
ATOM   2240 O  OG  . SER   A 1 276 ? 18.27600  -44.62400 4.34600   1.000 55.61355  ? 312 SER   A OG  1 
ATOM   2241 N  N   . VAL   A 1 277 ? 21.04900  -44.44800 2.77000   1.000 56.12034  ? 313 VAL   A N   1 
ATOM   2242 C  CA  . VAL   A 1 277 ? 21.67200  -45.16000 1.65800   1.000 56.56297  ? 313 VAL   A CA  1 
ATOM   2243 C  C   . VAL   A 1 277 ? 23.15800  -45.35600 1.92200   1.000 56.25652  ? 313 VAL   A C   1 
ATOM   2244 O  O   . VAL   A 1 277 ? 23.71500  -46.43100 1.66600   1.000 57.50505  ? 313 VAL   A O   1 
ATOM   2245 C  CB  . VAL   A 1 277 ? 21.43400  -44.40800 0.33700   1.000 57.12285  ? 313 VAL   A CB  1 
ATOM   2246 C  CG1 . VAL   A 1 277 ? 22.16200  -45.10300 -0.79900  1.000 52.77588  ? 313 VAL   A CG1 1 
ATOM   2247 C  CG2 . VAL   A 1 277 ? 19.94900  -44.30100 0.04000   1.000 51.97883  ? 313 VAL   A CG2 1 
ATOM   2248 N  N   . LEU   A 1 278 ? 23.82300  -44.32300 2.44400   1.000 56.44077  ? 314 LEU   A N   1 
ATOM   2249 C  CA  . LEU   A 1 278 ? 25.25300  -44.42300 2.70900   1.000 60.16122  ? 314 LEU   A CA  1 
ATOM   2250 C  C   . LEU   A 1 278 ? 25.54600  -45.38600 3.85300   1.000 65.21201  ? 314 LEU   A C   1 
ATOM   2251 O  O   . LEU   A 1 278 ? 26.62700  -45.98500 3.89500   1.000 64.35507  ? 314 LEU   A O   1 
ATOM   2252 C  CB  . LEU   A 1 278 ? 25.82900  -43.03800 3.00700   1.000 57.90337  ? 314 LEU   A CB  1 
ATOM   2253 C  CG  . LEU   A 1 278 ? 25.66400  -42.00900 1.88300   1.000 56.48306  ? 314 LEU   A CG  1 
ATOM   2254 C  CD1 . LEU   A 1 278 ? 26.29800  -40.67500 2.25500   1.000 63.22367  ? 314 LEU   A CD1 1 
ATOM   2255 C  CD2 . LEU   A 1 278 ? 26.25300  -42.54000 0.58400   1.000 58.10582  ? 314 LEU   A CD2 1 
ATOM   2256 N  N   . ASP   A 1 279 ? 24.60100  -45.55500 4.78100   1.000 67.05077  ? 315 ASP   A N   1 
ATOM   2257 C  CA  . ASP   A 1 279 ? 24.78800  -46.53700 5.84500   1.000 68.09962  ? 315 ASP   A CA  1 
ATOM   2258 C  C   . ASP   A 1 279 ? 24.67000  -47.95800 5.30700   1.000 67.49546  ? 315 ASP   A C   1 
ATOM   2259 O  O   . ASP   A 1 279 ? 25.45500  -48.83600 5.68100   1.000 64.26025  ? 315 ASP   A O   1 
ATOM   2260 C  CB  . ASP   A 1 279 ? 23.78100  -46.29600 6.97100   1.000 69.37750  ? 315 ASP   A CB  1 
ATOM   2261 C  CG  . ASP   A 1 279 ? 24.10800  -45.05800 7.79100   1.000 79.58653  ? 315 ASP   A CG  1 
ATOM   2262 O  OD1 . ASP   A 1 279 ? 25.28900  -44.65300 7.80400   1.000 96.35329  ? 315 ASP   A OD1 1 
ATOM   2263 O  OD2 . ASP   A 1 279 ? 23.19000  -44.49300 8.42600   1.000 80.22432  ? 315 ASP   A OD2 1 
ATOM   2264 N  N   . ASP   A 1 280 ? 23.70400  -48.19600 4.41500   1.000 64.84875  ? 316 ASP   A N   1 
ATOM   2265 C  CA  . ASP   A 1 280 ? 23.53400  -49.52400 3.83200   1.000 68.25970  ? 316 ASP   A CA  1 
ATOM   2266 C  C   . ASP   A 1 280 ? 24.72700  -49.92400 2.97100   1.000 68.45565  ? 316 ASP   A C   1 
ATOM   2267 O  O   . ASP   A 1 280 ? 25.03500  -51.11600 2.85900   1.000 67.78042  ? 316 ASP   A O   1 
ATOM   2268 C  CB  . ASP   A 1 280 ? 22.25100  -49.57200 2.99900   1.000 69.87957  ? 316 ASP   A CB  1 
ATOM   2269 C  CG  . ASP   A 1 280 ? 21.00700  -49.26200 3.81300   1.000 68.59134  ? 316 ASP   A CG  1 
ATOM   2270 O  OD1 . ASP   A 1 280 ? 21.11600  -49.07800 5.04600   1.000 67.96742  ? 316 ASP   A OD1 1 
ATOM   2271 O  OD2 . ASP   A 1 280 ? 19.91400  -49.20100 3.21300   1.000 65.07698  ? 316 ASP   A OD2 1 
ATOM   2272 N  N   . LEU   A 1 281 ? 25.40000  -48.95400 2.35700   1.000 63.76500  ? 317 LEU   A N   1 
ATOM   2273 C  CA  . LEU   A 1 281 ? 26.52700  -49.20500 1.46900   1.000 71.50929  ? 317 LEU   A CA  1 
ATOM   2274 C  C   . LEU   A 1 281 ? 27.87700  -49.01900 2.15100   1.000 64.95418  ? 317 LEU   A C   1 
ATOM   2275 O  O   . LEU   A 1 281 ? 28.91200  -49.14700 1.49000   1.000 65.69277  ? 317 LEU   A O   1 
ATOM   2276 C  CB  . LEU   A 1 281 ? 26.44200  -48.28900 0.24200   1.000 68.92015  ? 317 LEU   A CB  1 
ATOM   2277 C  CG  . LEU   A 1 281 ? 25.13400  -48.33000 -0.55000  1.000 60.91151  ? 317 LEU   A CG  1 
ATOM   2278 C  CD1 . LEU   A 1 281 ? 25.11800  -47.25900 -1.62400  1.000 64.26547  ? 317 LEU   A CD1 1 
ATOM   2279 C  CD2 . LEU   A 1 281 ? 24.92400  -49.70400 -1.16200  1.000 74.45524  ? 317 LEU   A CD2 1 
ATOM   2280 N  N   . GLY   A 1 282 ? 27.89300  -48.71700 3.44700   1.000 63.77571  ? 318 GLY   A N   1 
ATOM   2281 C  CA  . GLY   A 1 282 ? 29.14600  -48.55500 4.16000   1.000 64.73752  ? 318 GLY   A CA  1 
ATOM   2282 C  C   . GLY   A 1 282 ? 29.96000  -47.35400 3.73700   1.000 71.31885  ? 318 GLY   A C   1 
ATOM   2283 O  O   . GLY   A 1 282 ? 31.19000  -47.37300 3.85500   1.000 69.48907  ? 318 GLY   A O   1 
ATOM   2284 N  N   . GLN   A 1 283 ? 29.30800  -46.30600 3.24800   1.000 59.83707  ? 319 GLN   A N   1 
ATOM   2285 C  CA  . GLN   A 1 283 ? 29.98000  -45.10100 2.79200   1.000 65.93995  ? 319 GLN   A CA  1 
ATOM   2286 C  C   . GLN   A 1 283 ? 29.79200  -43.98200 3.80800   1.000 68.61585  ? 319 GLN   A C   1 
ATOM   2287 O  O   . GLN   A 1 283 ? 28.85200  -43.98800 4.60800   1.000 68.25973  ? 319 GLN   A O   1 
ATOM   2288 C  CB  . GLN   A 1 283 ? 29.44900  -44.66800 1.42200   1.000 67.70557  ? 319 GLN   A CB  1 
ATOM   2289 C  CG  . GLN   A 1 283 ? 29.40700  -45.79700 0.40600   1.000 66.18391  ? 319 GLN   A CG  1 
ATOM   2290 C  CD  . GLN   A 1 283 ? 30.77500  -46.40000 0.15700   1.000 70.05120  ? 319 GLN   A CD  1 
ATOM   2291 O  OE1 . GLN   A 1 283 ? 31.78500  -45.69600 0.15500   1.000 69.05002  ? 319 GLN   A OE1 1 
ATOM   2292 N  NE2 . GLN   A 1 283 ? 30.81600  -47.71100 -0.05100  1.000 71.05753  ? 319 GLN   A NE2 1 
ATOM   2293 N  N   . ALA   A 1 284 ? 30.70800  -43.02000 3.77400   1.000 70.13971  ? 320 ALA   A N   1 
ATOM   2294 C  CA  . ALA   A 1 284 ? 30.66700  -41.87400 4.66600   1.000 59.92896  ? 320 ALA   A CA  1 
ATOM   2295 C  C   . ALA   A 1 284 ? 30.25000  -40.62900 3.89600   1.000 65.36011  ? 320 ALA   A C   1 
ATOM   2296 O  O   . ALA   A 1 284 ? 30.50000  -40.50500 2.69400   1.000 63.17941  ? 320 ALA   A O   1 
ATOM   2297 C  CB  . ALA   A 1 284 ? 32.02200  -41.64200 5.33800   1.000 64.76395  ? 320 ALA   A CB  1 
ATOM   2298 N  N   . CYS   A 1 285 ? 29.60100  -39.70900 4.60300   1.000 66.06488  ? 321 CYS   A N   1 
ATOM   2299 C  CA  . CYS   A 1 285 ? 29.18300  -38.43700 4.02200   1.000 58.87372  ? 321 CYS   A CA  1 
ATOM   2300 C  C   . CYS   A 1 285 ? 30.24000  -37.37700 4.33200   1.000 65.09222  ? 321 CYS   A C   1 
ATOM   2301 O  O   . CYS   A 1 285 ? 30.05700  -36.47900 5.15300   1.000 67.07621  ? 321 CYS   A O   1 
ATOM   2302 C  CB  . CYS   A 1 285 ? 27.80600  -38.04200 4.54900   1.000 65.57682  ? 321 CYS   A CB  1 
ATOM   2303 S  SG  . CYS   A 1 285 ? 27.07400  -36.60400 3.73700   1.000 61.93356  ? 321 CYS   A SG  1 
ATOM   2304 N  N   . ASP   A 1 286 ? 31.37900  -37.51300 3.65200   1.000 65.73215  ? 322 ASP   A N   1 
ATOM   2305 C  CA  . ASP   A 1 286 ? 32.52500  -36.64600 3.89300   1.000 63.27119  ? 322 ASP   A CA  1 
ATOM   2306 C  C   . ASP   A 1 286 ? 32.60700  -35.47600 2.92300   1.000 66.32105  ? 322 ASP   A C   1 
ATOM   2307 O  O   . ASP   A 1 286 ? 33.45100  -34.59400 3.11500   1.000 70.71034  ? 322 ASP   A O   1 
ATOM   2308 C  CB  . ASP   A 1 286 ? 33.82500  -37.45900 3.83300   1.000 69.63599  ? 322 ASP   A CB  1 
ATOM   2309 C  CG  . ASP   A 1 286 ? 33.93600  -38.30700 2.57600   1.000 62.69694  ? 322 ASP   A CG  1 
ATOM   2310 O  OD1 . ASP   A 1 286 ? 33.20500  -38.04100 1.60000   1.000 58.27486  ? 322 ASP   A OD1 1 
ATOM   2311 O  OD2 . ASP   A 1 286 ? 34.76000  -39.24700 2.56600   1.000 74.04056  ? 322 ASP   A OD2 1 
ATOM   2312 N  N   . GLY   A 1 287 ? 31.76000  -35.44400 1.89900   1.000 60.11911  ? 323 GLY   A N   1 
ATOM   2313 C  CA  . GLY   A 1 287 ? 31.78000  -34.37700 0.92000   1.000 62.00215  ? 323 GLY   A CA  1 
ATOM   2314 C  C   . GLY   A 1 287 ? 32.62600  -34.63400 -0.30800  1.000 64.34908  ? 323 GLY   A C   1 
ATOM   2315 O  O   . GLY   A 1 287 ? 32.90000  -33.68800 -1.05700  1.000 58.85966  ? 323 GLY   A O   1 
ATOM   2316 N  N   . ASP   A 1 288 ? 33.04300  -35.87700 -0.54400  1.000 61.10679  ? 324 ASP   A N   1 
ATOM   2317 C  CA  . ASP   A 1 288 ? 33.86600  -36.22000 -1.69800  1.000 60.70777  ? 324 ASP   A CA  1 
ATOM   2318 C  C   . ASP   A 1 288 ? 32.95900  -36.50700 -2.89100  1.000 62.21283  ? 324 ASP   A C   1 
ATOM   2319 O  O   . ASP   A 1 288 ? 32.13800  -37.43100 -2.84500  1.000 55.43508  ? 324 ASP   A O   1 
ATOM   2320 C  CB  . ASP   A 1 288 ? 34.75600  -37.42300 -1.38100  1.000 57.18310  ? 324 ASP   A CB  1 
ATOM   2321 C  CG  . ASP   A 1 288 ? 35.76200  -37.72100 -2.48200  1.000 65.31336  ? 324 ASP   A CG  1 
ATOM   2322 O  OD1 . ASP   A 1 288 ? 36.60700  -36.85100 -2.77600  1.000 60.88328  ? 324 ASP   A OD1 1 
ATOM   2323 O  OD2 . ASP   A 1 288 ? 35.71800  -38.83600 -3.04200  1.000 69.93230  ? 324 ASP   A OD2 1 
ATOM   2324 N  N   . MET   A 1 289 ? 33.10800  -35.72000 -3.95400  1.000 57.07911  ? 325 MET   A N   1 
ATOM   2325 C  CA  . MET   A 1 289 ? 32.26000  -35.81600 -5.13400  1.000 55.61807  ? 325 MET   A CA  1 
ATOM   2326 C  C   . MET   A 1 289 ? 33.03800  -36.40500 -6.30400  1.000 50.23344  ? 325 MET   A C   1 
ATOM   2327 O  O   . MET   A 1 289 ? 34.27300  -36.40800 -6.33100  1.000 54.98218  ? 325 MET   A O   1 
ATOM   2328 C  CB  . MET   A 1 289 ? 31.69600  -34.44400 -5.52200  1.000 43.96053  ? 325 MET   A CB  1 
ATOM   2329 C  CG  . MET   A 1 289 ? 31.05700  -33.69300 -4.37900  1.000 43.56338  ? 325 MET   A CG  1 
ATOM   2330 S  SD  . MET   A 1 289 ? 29.44500  -34.33200 -3.89100  1.000 50.28613  ? 325 MET   A SD  1 
ATOM   2331 C  CE  . MET   A 1 289 ? 29.64700  -34.21900 -2.12100  1.000 53.91029  ? 325 MET   A CE  1 
ATOM   2332 N  N   . ASP   A 1 290 ? 32.28600  -36.90100 -7.29000  1.000 43.24831  ? 326 ASP   A N   1 
ATOM   2333 C  CA  . ASP   A 1 290 ? 32.91200  -37.53300 -8.44700  1.000 48.16023  ? 326 ASP   A CA  1 
ATOM   2334 C  C   . ASP   A 1 290 ? 33.76400  -36.54200 -9.22700  1.000 46.57901  ? 326 ASP   A C   1 
ATOM   2335 O  O   . ASP   A 1 290 ? 34.86700  -36.88000 -9.67400  1.000 44.52355  ? 326 ASP   A O   1 
ATOM   2336 C  CB  . ASP   A 1 290 ? 31.84900  -38.14500 -9.35700  1.000 47.58293  ? 326 ASP   A CB  1 
ATOM   2337 C  CG  . ASP   A 1 290 ? 31.09300  -39.27400 -8.69500  1.000 52.28542  ? 326 ASP   A CG  1 
ATOM   2338 O  OD1 . ASP   A 1 290 ? 31.38700  -39.58200 -7.52100  1.000 47.70395  ? 326 ASP   A OD1 1 
ATOM   2339 O  OD2 . ASP   A 1 290 ? 30.19400  -39.84600 -9.34600  1.000 50.70239  ? 326 ASP   A OD2 1 
ATOM   2340 N  N   . TRP   A 1 291 ? 33.27800  -35.31200 -9.40100  1.000 44.98323  ? 327 TRP   A N   1 
ATOM   2341 C  CA  . TRP   A 1 291 ? 34.01200  -34.36500 -10.23100 1.000 51.03311  ? 327 TRP   A CA  1 
ATOM   2342 C  C   . TRP   A 1 291 ? 35.31700  -33.90600 -9.59600  1.000 46.92163  ? 327 TRP   A C   1 
ATOM   2343 O  O   . TRP   A 1 291 ? 36.13700  -33.29800 -10.29100 1.000 45.98467  ? 327 TRP   A O   1 
ATOM   2344 C  CB  . TRP   A 1 291 ? 33.12700  -33.16000 -10.56000 1.000 50.17145  ? 327 TRP   A CB  1 
ATOM   2345 C  CG  . TRP   A 1 291 ? 32.62000  -32.42500 -9.36600  1.000 49.95526  ? 327 TRP   A CG  1 
ATOM   2346 C  CD1 . TRP   A 1 291 ? 33.30600  -31.51700 -8.61200  1.000 50.98358  ? 327 TRP   A CD1 1 
ATOM   2347 C  CD2 . TRP   A 1 291 ? 31.31200  -32.51600 -8.79600  1.000 44.04070  ? 327 TRP   A CD2 1 
ATOM   2348 N  NE1 . TRP   A 1 291 ? 32.50600  -31.04200 -7.60200  1.000 54.80051  ? 327 TRP   A NE1 1 
ATOM   2349 C  CE2 . TRP   A 1 291 ? 31.27600  -31.63900 -7.69200  1.000 45.76565  ? 327 TRP   A CE2 1 
ATOM   2350 C  CE3 . TRP   A 1 291 ? 30.16500  -33.25100 -9.11100  1.000 45.40068  ? 327 TRP   A CE3 1 
ATOM   2351 C  CZ2 . TRP   A 1 291 ? 30.14300  -31.47600 -6.90400  1.000 44.36986  ? 327 TRP   A CZ2 1 
ATOM   2352 C  CZ3 . TRP   A 1 291 ? 29.03800  -33.09200 -8.32300  1.000 45.98753  ? 327 TRP   A CZ3 1 
ATOM   2353 C  CH2 . TRP   A 1 291 ? 29.03500  -32.21100 -7.23200  1.000 49.87504  ? 327 TRP   A CH2 1 
ATOM   2354 N  N   . MET   A 1 292 ? 35.53800  -34.19100 -8.31100  1.000 42.18873  ? 328 MET   A N   1 
ATOM   2355 C  CA  . MET   A 1 292 ? 36.79200  -33.83500 -7.65900  1.000 55.56612  ? 328 MET   A CA  1 
ATOM   2356 C  C   . MET   A 1 292 ? 37.95100  -34.70900 -8.11100  1.000 57.45200  ? 328 MET   A C   1 
ATOM   2357 O  O   . MET   A 1 292 ? 39.10800  -34.33500 -7.89300  1.000 56.57997  ? 328 MET   A O   1 
ATOM   2358 C  CB  . MET   A 1 292 ? 36.64300  -33.92500 -6.13900  1.000 49.45137  ? 328 MET   A CB  1 
ATOM   2359 C  CG  . MET   A 1 292 ? 35.25900  -33.52400 -5.64200  1.000 51.77578  ? 328 MET   A CG  1 
ATOM   2360 S  SD  . MET   A 1 292 ? 35.21200  -32.73400 -4.02400  1.000 56.96233  ? 328 MET   A SD  1 
ATOM   2361 C  CE  . MET   A 1 292 ? 36.29600  -33.75900 -3.05600  1.000 62.48606  ? 328 MET   A CE  1 
ATOM   2362 N  N   . HIS   A 1 293 ? 37.67200  -35.85400 -8.73100  1.000 52.09810  ? 329 HIS   A N   1 
ATOM   2363 C  CA  . HIS   A 1 293 ? 38.71200  -36.73200 -9.24600  1.000 57.31131  ? 329 HIS   A CA  1 
ATOM   2364 C  C   . HIS   A 1 293 ? 38.98900  -36.51400 -10.72800 1.000 58.28021  ? 329 HIS   A C   1 
ATOM   2365 O  O   . HIS   A 1 293 ? 39.82600  -37.22200 -11.29700 1.000 52.60582  ? 329 HIS   A O   1 
ATOM   2366 C  CB  . HIS   A 1 293 ? 38.33600  -38.19800 -8.99700  1.000 53.43638  ? 329 HIS   A CB  1 
ATOM   2367 C  CG  . HIS   A 1 293 ? 38.14100  -38.53400 -7.55000  1.000 53.61503  ? 329 HIS   A CG  1 
ATOM   2368 N  ND1 . HIS   A 1 293 ? 39.19400  -38.78300 -6.69600  1.000 47.22209  ? 329 HIS   A ND1 1 
ATOM   2369 C  CD2 . HIS   A 1 293 ? 37.01600  -38.65500 -6.80600  1.000 48.22721  ? 329 HIS   A CD2 1 
ATOM   2370 C  CE1 . HIS   A 1 293 ? 38.72600  -39.04600 -5.48900  1.000 56.29843  ? 329 HIS   A CE1 1 
ATOM   2371 N  NE2 . HIS   A 1 293 ? 37.40800  -38.97900 -5.52900  1.000 49.14812  ? 329 HIS   A NE2 1 
ATOM   2372 N  N   . LEU   A 1 294 ? 38.31800  -35.55600 -11.36500 1.000 56.97992  ? 330 LEU   A N   1 
ATOM   2373 C  CA  . LEU   A 1 294 ? 38.54500  -35.30200 -12.78100 1.000 57.65135  ? 330 LEU   A CA  1 
ATOM   2374 C  C   . LEU   A 1 294 ? 39.98100  -34.86200 -13.03300 1.000 61.49870  ? 330 LEU   A C   1 
ATOM   2375 O  O   . LEU   A 1 294 ? 40.62800  -34.25200 -12.17700 1.000 59.11553  ? 330 LEU   A O   1 
ATOM   2376 C  CB  . LEU   A 1 294 ? 37.58300  -34.23300 -13.29700 1.000 57.31176  ? 330 LEU   A CB  1 
ATOM   2377 C  CG  . LEU   A 1 294 ? 36.10700  -34.62100 -13.32600 1.000 58.68229  ? 330 LEU   A CG  1 
ATOM   2378 C  CD1 . LEU   A 1 294 ? 35.26300  -33.42100 -13.72000 1.000 54.76287  ? 330 LEU   A CD1 1 
ATOM   2379 C  CD2 . LEU   A 1 294 ? 35.88400  -35.78200 -14.28100 1.000 56.58523  ? 330 LEU   A CD2 1 
ATOM   2380 N  N   . ASN   A 1 295 ? 40.47600  -35.19100 -14.22800 1.000 67.87097  ? 331 ASN   A N   1 
ATOM   2381 C  CA  . ASN   A 1 295 ? 41.78500  -34.74800 -14.71000 1.000 68.14812  ? 331 ASN   A CA  1 
ATOM   2382 C  C   . ASN   A 1 295 ? 42.89500  -35.09900 -13.71600 1.000 71.30104  ? 331 ASN   A C   1 
ATOM   2383 O  O   . ASN   A 1 295 ? 43.56900  -34.23100 -13.16100 1.000 66.36309  ? 331 ASN   A O   1 
ATOM   2384 C  CB  . ASN   A 1 295 ? 41.77100  -33.24300 -15.01100 1.000 69.19108  ? 331 ASN   A CB  1 
ATOM   2385 C  CG  . ASN   A 1 295 ? 40.82400  -32.87800 -16.14400 1.000 74.28661  ? 331 ASN   A CG  1 
ATOM   2386 O  OD1 . ASN   A 1 295 ? 40.83400  -33.50000 -17.20800 1.000 77.44086  ? 331 ASN   A OD1 1 
ATOM   2387 N  ND2 . ASN   A 1 295 ? 40.00300  -31.85800 -15.91900 1.000 72.76226  ? 331 ASN   A ND2 1 
ATOM   2388 N  N   . GLY   A 1 296 ? 43.06500  -36.40100 -13.49000 1.000 71.21968  ? 332 GLY   A N   1 
ATOM   2389 C  CA  . GLY   A 1 296 ? 44.12300  -36.89100 -12.62600 1.000 68.14895  ? 332 GLY   A CA  1 
ATOM   2390 C  C   . GLY   A 1 296 ? 44.05700  -36.40700 -11.19000 1.000 68.57183  ? 332 GLY   A C   1 
ATOM   2391 O  O   . GLY   A 1 296 ? 45.00700  -36.59300 -10.42300 1.000 72.84497  ? 332 GLY   A O   1 
ATOM   2392 N  N   . GLY   A 1 297 ? 42.94500  -35.78700 -10.80600 1.000 66.17037  ? 333 GLY   A N   1 
ATOM   2393 C  CA  . GLY   A 1 297 ? 42.79900  -35.21000 -9.48500  1.000 67.42459  ? 333 GLY   A CA  1 
ATOM   2394 C  C   . GLY   A 1 297 ? 42.73700  -33.69700 -9.45500  1.000 69.60481  ? 333 GLY   A C   1 
ATOM   2395 O  O   . GLY   A 1 297 ? 42.34400  -33.13800 -8.42300  1.000 72.70238  ? 333 GLY   A O   1 
ATOM   2396 N  N   . ARG   A 1 298 ? 43.10900  -33.01300 -10.54300 1.000 68.91993  ? 334 ARG   A N   1 
ATOM   2397 C  CA  . ARG   A 1 298 ? 42.98700  -31.55600 -10.57800 1.000 73.84183  ? 334 ARG   A CA  1 
ATOM   2398 C  C   . ARG   A 1 298 ? 41.54000  -31.11000 -10.42400 1.000 76.87675  ? 334 ARG   A C   1 
ATOM   2399 O  O   . ARG   A 1 298 ? 41.26400  -30.07400 -9.80600  1.000 76.31696  ? 334 ARG   A O   1 
ATOM   2400 C  CB  . ARG   A 1 298 ? 43.54800  -31.00200 -11.88700 1.000 76.11431  ? 334 ARG   A CB  1 
ATOM   2401 C  CG  . ARG   A 1 298 ? 45.04700  -31.00400 -11.98800 1.000 84.09429  ? 334 ARG   A CG  1 
ATOM   2402 C  CD  . ARG   A 1 298 ? 45.50700  -31.79600 -13.18800 1.000 88.99957  ? 334 ARG   A CD  1 
ATOM   2403 N  NE  . ARG   A 1 298 ? 46.85900  -32.28600 -12.96800 1.000 102.88350 ? 334 ARG   A NE  1 
ATOM   2404 C  CZ  . ARG   A 1 298 ? 47.53600  -33.05300 -13.80800 1.000 96.41525  ? 334 ARG   A CZ  1 
ATOM   2405 N  NH1 . ARG   A 1 298 ? 47.01400  -33.45800 -14.95400 1.000 102.73583 ? 334 ARG   A NH1 1 
ATOM   2406 N  NH2 . ARG   A 1 298 ? 48.77200  -33.42000 -13.48900 1.000 90.21546  ? 334 ARG   A NH2 1 
ATOM   2407 N  N   . GLY   A 1 299 ? 40.60700  -31.86900 -10.98700 1.000 67.95444  ? 335 GLY   A N   1 
ATOM   2408 C  CA  . GLY   A 1 299 ? 39.23400  -31.43300 -11.12600 1.000 64.88364  ? 335 GLY   A CA  1 
ATOM   2409 C  C   . GLY   A 1 299 ? 38.94200  -30.94900 -12.53400 1.000 77.95657  ? 335 GLY   A C   1 
ATOM   2410 O  O   . GLY   A 1 299 ? 39.72700  -31.12900 -13.47000 1.000 70.02495  ? 335 GLY   A O   1 
ATOM   2411 N  N   . TRP   A 1 300 ? 37.77900  -30.31600 -12.67800 1.000 74.40109  ? 336 TRP   A N   1 
ATOM   2412 C  CA  . TRP   A 1 300 ? 37.35600  -29.81200 -13.97900 1.000 78.66108  ? 336 TRP   A CA  1 
ATOM   2413 C  C   . TRP   A 1 300 ? 38.24300  -28.65500 -14.42900 1.000 84.03042  ? 336 TRP   A C   1 
ATOM   2414 O  O   . TRP   A 1 300 ? 38.66100  -27.82000 -13.62100 1.000 74.32067  ? 336 TRP   A O   1 
ATOM   2415 C  CB  . TRP   A 1 300 ? 35.90000  -29.35400 -13.91800 1.000 74.89687  ? 336 TRP   A CB  1 
ATOM   2416 C  CG  . TRP   A 1 300 ? 35.68900  -28.27900 -12.91000 1.000 73.88172  ? 336 TRP   A CG  1 
ATOM   2417 C  CD1 . TRP   A 1 300 ? 35.59500  -28.43400 -11.56000 1.000 76.84366  ? 336 TRP   A CD1 1 
ATOM   2418 C  CD2 . TRP   A 1 300 ? 35.57000  -26.87500 -13.16300 1.000 77.73431  ? 336 TRP   A CD2 1 
ATOM   2419 N  NE1 . TRP   A 1 300 ? 35.41900  -27.21600 -10.95300 1.000 76.50544  ? 336 TRP   A NE1 1 
ATOM   2420 C  CE2 . TRP   A 1 300 ? 35.39800  -26.24200 -11.91500 1.000 78.53124  ? 336 TRP   A CE2 1 
ATOM   2421 C  CE3 . TRP   A 1 300 ? 35.57900  -26.09300 -14.32200 1.000 78.71566  ? 336 TRP   A CE3 1 
ATOM   2422 C  CZ2 . TRP   A 1 300 ? 35.24600  -24.86400 -11.79200 1.000 83.05133  ? 336 TRP   A CZ2 1 
ATOM   2423 C  CZ3 . TRP   A 1 300 ? 35.43000  -24.72100 -14.19800 1.000 79.66396  ? 336 TRP   A CZ3 1 
ATOM   2424 C  CH2 . TRP   A 1 300 ? 35.26500  -24.12200 -12.94200 1.000 81.68269  ? 336 TRP   A CH2 1 
ATOM   2425 N  N   . ASP   A 1 301 ? 38.52700  -28.60600 -15.73000 1.000 95.82456  ? 337 ASP   A N   1 
ATOM   2426 C  CA  . ASP   A 1 301 ? 39.30600  -27.52400 -16.31400 1.000 96.95109  ? 337 ASP   A CA  1 
ATOM   2427 C  C   . ASP   A 1 301 ? 38.62100  -27.06100 -17.59400 1.000 105.51405 ? 337 ASP   A C   1 
ATOM   2428 O  O   . ASP   A 1 301 ? 37.68100  -27.69200 -18.08600 1.000 109.07655 ? 337 ASP   A O   1 
ATOM   2429 C  CB  . ASP   A 1 301 ? 40.75600  -27.95100 -16.57900 1.000 98.60124  ? 337 ASP   A CB  1 
ATOM   2430 C  CG  . ASP   A 1 301 ? 41.70300  -26.76900 -16.67300 1.000 107.48437 ? 337 ASP   A CG  1 
ATOM   2431 O  OD1 . ASP   A 1 301 ? 41.44000  -25.85900 -17.48700 1.000 112.76874 ? 337 ASP   A OD1 1 
ATOM   2432 O  OD2 . ASP   A 1 301 ? 42.70000  -26.74100 -15.92100 1.000 110.18213 ? 337 ASP   A OD2 1 
ATOM   2433 N  N   . ALA   A 1 302 ? 39.10600  -25.94500 -18.14100 1.000 111.60842 ? 338 ALA   A N   1 
ATOM   2434 C  CA  . ALA   A 1 302 ? 38.38900  -25.27300 -19.22000 1.000 117.69218 ? 338 ALA   A CA  1 
ATOM   2435 C  C   . ALA   A 1 302 ? 38.65200  -25.91700 -20.57800 1.000 122.46588 ? 338 ALA   A C   1 
ATOM   2436 O  O   . ALA   A 1 302 ? 37.71300  -26.17100 -21.34100 1.000 125.44849 ? 338 ALA   A O   1 
ATOM   2437 C  CB  . ALA   A 1 302 ? 38.76400  -23.79000 -19.25200 1.000 121.53272 ? 338 ALA   A CB  1 
ATOM   2438 N  N   . THR   A 1 303 ? 39.92000  -26.19100 -20.89700 1.000 122.40946 ? 339 THR   A N   1 
ATOM   2439 C  CA  . THR   A 1 303 ? 40.27500  -26.57700 -22.26100 1.000 126.60847 ? 339 THR   A CA  1 
ATOM   2440 C  C   . THR   A 1 303 ? 39.71400  -27.94700 -22.63100 1.000 131.68208 ? 339 THR   A C   1 
ATOM   2441 O  O   . THR   A 1 303 ? 39.26200  -28.15100 -23.76500 1.000 132.12256 ? 339 THR   A O   1 
ATOM   2442 C  CB  . THR   A 1 303 ? 41.79600  -26.56700 -22.43500 1.000 125.17866 ? 339 THR   A CB  1 
ATOM   2443 O  OG1 . THR   A 1 303 ? 42.33500  -25.35300 -21.89900 1.000 127.54396 ? 339 THR   A OG1 1 
ATOM   2444 C  CG2 . THR   A 1 303 ? 42.16700  -26.66600 -23.91100 1.000 121.72750 ? 339 THR   A CG2 1 
ATOM   2445 N  N   . ILE   A 1 304 ? 39.72600  -28.89300 -21.69600 1.000 125.06222 ? 340 ILE   A N   1 
ATOM   2446 C  CA  . ILE   A 1 304 ? 39.40800  -30.28100 -22.02200 1.000 120.95633 ? 340 ILE   A CA  1 
ATOM   2447 C  C   . ILE   A 1 304 ? 37.92100  -30.57800 -21.86200 1.000 118.26723 ? 340 ILE   A C   1 
ATOM   2448 O  O   . ILE   A 1 304 ? 37.32000  -31.23400 -22.71600 1.000 120.05269 ? 340 ILE   A O   1 
ATOM   2449 C  CB  . ILE   A 1 304 ? 40.26400  -31.22700 -21.15700 1.000 115.25345 ? 340 ILE   A CB  1 
ATOM   2450 C  CG1 . ILE   A 1 304 ? 41.75200  -30.95200 -21.37700 1.000 117.20241 ? 340 ILE   A CG1 1 
ATOM   2451 C  CG2 . ILE   A 1 304 ? 39.93100  -32.68100 -21.46300 1.000 111.60130 ? 340 ILE   A CG2 1 
ATOM   2452 C  CD1 . ILE   A 1 304 ? 42.20200  -31.13200 -22.81000 1.000 118.52594 ? 340 ILE   A CD1 1 
ATOM   2453 N  N   . ASN   A 1 305 ? 37.30700  -30.10400 -20.77800 1.000 118.77372 ? 341 ASN   A N   1 
ATOM   2454 C  CA  . ASN   A 1 305 ? 35.96800  -30.56400 -20.42000 1.000 107.03217 ? 341 ASN   A CA  1 
ATOM   2455 C  C   . ASN   A 1 305 ? 34.90500  -29.99300 -21.35400 1.000 112.68548 ? 341 ASN   A C   1 
ATOM   2456 O  O   . ASN   A 1 305 ? 34.21100  -30.74100 -22.05300 1.000 114.68361 ? 341 ASN   A O   1 
ATOM   2457 C  CB  . ASN   A 1 305 ? 35.67100  -30.20600 -18.96400 1.000 95.24628  ? 341 ASN   A CB  1 
ATOM   2458 C  CG  . ASN   A 1 305 ? 36.45200  -31.06200 -17.98800 1.000 87.80678  ? 341 ASN   A CG  1 
ATOM   2459 O  OD1 . ASN   A 1 305 ? 37.17400  -30.55100 -17.13400 1.000 82.15593  ? 341 ASN   A OD1 1 
ATOM   2460 N  ND2 . ASN   A 1 305 ? 36.31600  -32.37700 -18.11600 1.000 85.58652  ? 341 ASN   A ND2 1 
ATOM   2461 N  N   . LYS   A 1 306 ? 34.75300  -28.67200 -21.37400 1.000 131.44653 ? 342 LYS   A N   1 
ATOM   2462 C  CA  . LYS   A 1 306 ? 33.70600  -28.04900 -22.18200 1.000 133.52709 ? 342 LYS   A CA  1 
ATOM   2463 C  C   . LYS   A 1 306 ? 34.07600  -28.05600 -23.66300 1.000 138.99176 ? 342 LYS   A C   1 
ATOM   2464 O  O   . LYS   A 1 306 ? 33.25300  -28.39000 -24.51600 1.000 142.97413 ? 342 LYS   A O   1 
ATOM   2465 C  CB  . LYS   A 1 306 ? 33.44000  -26.61600 -21.71700 1.000 123.77692 ? 342 LYS   A CB  1 
ATOM   2466 C  CG  . LYS   A 1 306 ? 31.99800  -26.16100 -21.90800 1.000 126.02410 ? 342 LYS   A CG  1 
ATOM   2467 C  CD  . LYS   A 1 306 ? 31.16800  -26.43200 -20.65900 1.000 119.29428 ? 342 LYS   A CD  1 
ATOM   2468 C  CE  . LYS   A 1 306 ? 29.67600  -26.28500 -20.92300 1.000 113.02461 ? 342 LYS   A CE  1 
ATOM   2469 N  NZ  . LYS   A 1 306 ? 29.12900  -27.45300 -21.66800 1.000 118.37037 ? 342 LYS   A NZ  1 
HETATM 2470 C  C13 . A1BIO B 2 .   ? 24.03800  -21.76100 -15.90900 1.000 81.25312  ? 401 A1BIO A C13 1 
HETATM 2471 C  C15 . A1BIO B 2 .   ? 22.15800  -22.67100 -17.34100 1.000 79.78365  ? 401 A1BIO A C15 1 
HETATM 2472 C  C17 . A1BIO B 2 .   ? 22.06600  -20.44700 -16.15700 1.000 91.24392  ? 401 A1BIO A C17 1 
HETATM 2473 C  C20 . A1BIO B 2 .   ? 26.58400  -18.18900 -13.87300 1.000 74.24080  ? 401 A1BIO A C20 1 
HETATM 2474 C  C21 . A1BIO B 2 .   ? 27.70900  -17.90000 -13.11700 1.000 71.60363  ? 401 A1BIO A C21 1 
HETATM 2475 C  C24 . A1BIO B 2 .   ? 25.27100  -17.78800 -11.91400 1.000 73.63529  ? 401 A1BIO A C24 1 
HETATM 2476 C  C02 . A1BIO B 2 .   ? 22.35100  -13.79700 -12.31200 1.000 90.21069  ? 401 A1BIO A C02 1 
HETATM 2477 C  C03 . A1BIO B 2 .   ? 21.44500  -14.81900 -12.08700 1.000 86.20901  ? 401 A1BIO A C03 1 
HETATM 2478 C  C04 . A1BIO B 2 .   ? 21.63500  -16.05200 -12.69000 1.000 83.28111  ? 401 A1BIO A C04 1 
HETATM 2479 C  C05 . A1BIO B 2 .   ? 23.44500  -14.00800 -13.13500 1.000 87.17562  ? 401 A1BIO A C05 1 
HETATM 2480 C  C06 . A1BIO B 2 .   ? 23.63500  -15.23800 -13.74100 1.000 88.51144  ? 401 A1BIO A C06 1 
HETATM 2481 C  C07 . A1BIO B 2 .   ? 22.73000  -16.26100 -13.51600 1.000 85.98740  ? 401 A1BIO A C07 1 
HETATM 2482 C  C08 . A1BIO B 2 .   ? 22.93600  -17.62200 -14.17000 1.000 86.40525  ? 401 A1BIO A C08 1 
HETATM 2483 C  C11 . A1BIO B 2 .   ? 23.81500  -19.59900 -14.82600 1.000 83.56525  ? 401 A1BIO A C11 1 
HETATM 2484 C  C12 . A1BIO B 2 .   ? 24.56600  -20.77400 -15.10400 1.000 83.69901  ? 401 A1BIO A C12 1 
HETATM 2485 C  C14 . A1BIO B 2 .   ? 22.77900  -21.60100 -16.44200 1.000 82.28343  ? 401 A1BIO A C14 1 
HETATM 2486 C  C18 . A1BIO B 2 .   ? 24.06700  -18.44000 -14.05800 1.000 84.37685  ? 401 A1BIO A C18 1 
HETATM 2487 C  C19 . A1BIO B 2 .   ? 25.33900  -18.13000 -13.26100 1.000 77.09003  ? 401 A1BIO A C19 1 
HETATM 2488 C  C23 . A1BIO B 2 .   ? 26.44800  -17.51500 -11.23400 1.000 65.91616  ? 401 A1BIO A C23 1 
HETATM 2489 F  F01 . A1BIO B 2 .   ? 22.17400  -12.58100 -11.72200 1.000 93.93237  ? 401 A1BIO A F01 1 
HETATM 2490 N  N09 . A1BIO B 2 .   ? 22.04600  -18.24800 -14.95600 1.000 89.32369  ? 401 A1BIO A N09 1 
HETATM 2491 N  N10 . A1BIO B 2 .   ? 22.61600  -19.47600 -15.35000 1.000 89.69046  ? 401 A1BIO A N10 1 
HETATM 2492 N  N16 . A1BIO B 2 .   ? 21.68100  -23.45300 -18.00800 1.000 76.08188  ? 401 A1BIO A N16 1 
HETATM 2493 N  N22 . A1BIO B 2 .   ? 27.61800  -17.57400 -11.84200 1.000 65.22477  ? 401 A1BIO A N22 1 
HETATM 2494 CL CL  . CL    C 3 .   ? 14.51600  -34.96100 -23.94300 1.000 76.80573  ? 402 CL    A CL  1 
HETATM 2495 CL CL  . CL    D 3 .   ? 3.14400   -17.75500 -14.07800 1.000 100.26229 ? 403 CL    A CL  1 
HETATM 2496 O  O   . HOH   E 4 .   ? 13.58100  -28.68800 8.31900   1.000 68.54553  ? 501 HOH   A O   1 
HETATM 2497 O  O   . HOH   E 4 .   ? 18.72600  -24.82600 -19.69500 1.000 71.39196  ? 502 HOH   A O   1 
HETATM 2498 O  O   . HOH   E 4 .   ? 19.38000  -31.17400 -17.91800 1.000 54.08263  ? 503 HOH   A O   1 
HETATM 2499 O  O   . HOH   E 4 .   ? 31.29100  -39.33900 -4.57700  1.000 41.15078  ? 504 HOH   A O   1 
HETATM 2500 O  O   . HOH   E 4 .   ? 24.52300  -25.91400 -0.42300  1.000 56.75330  ? 505 HOH   A O   1 
HETATM 2501 O  O   . HOH   E 4 .   ? 7.97300   -27.29300 -9.53600  1.000 52.25393  ? 506 HOH   A O   1 
HETATM 2502 O  O   . HOH   E 4 .   ? 30.86000  -40.26800 -12.02400 1.000 50.86414  ? 507 HOH   A O   1 
HETATM 2503 O  O   . HOH   E 4 .   ? 39.269    -9.099    -2.573    1.000 59.22616  ? 508 HOH   A O   1 
HETATM 2504 O  O   . HOH   E 4 .   ? 21.26700  -13.33300 -1.81900  1.000 64.99821  ? 509 HOH   A O   1 
HETATM 2505 O  O   . HOH   E 4 .   ? 13.58400  -2.71900  -6.79800  1.000 76.59581  ? 510 HOH   A O   1 
HETATM 2506 O  O   . HOH   E 4 .   ? 34.78700  -38.64100 -16.83200 1.000 63.68378  ? 511 HOH   A O   1 
HETATM 2507 O  O   . HOH   E 4 .   ? 14.43500  -40.19300 -6.02000  1.000 45.67704  ? 512 HOH   A O   1 
HETATM 2508 O  O   . HOH   E 4 .   ? 4.41600   -33.95800 -5.79600  1.000 45.24298  ? 513 HOH   A O   1 
HETATM 2509 O  O   . HOH   E 4 .   ? -0.65400  -30.61100 -30.52300 1.000 70.32664  ? 514 HOH   A O   1 
HETATM 2510 O  O   . HOH   E 4 .   ? 19.79500  -49.24900 0.45000   1.000 59.22398  ? 515 HOH   A O   1 
HETATM 2511 O  O   . HOH   E 4 .   ? 32.79900  -19.92000 -4.81500  1.000 67.69547  ? 516 HOH   A O   1 
HETATM 2512 O  O   . HOH   E 4 .   ? 7.45700   -43.92200 0.21200   1.000 60.73867  ? 517 HOH   A O   1 
HETATM 2513 O  O   . HOH   E 4 .   ? 30.41300  -36.85500 -21.75900 1.000 66.67568  ? 518 HOH   A O   1 
HETATM 2514 O  O   . HOH   E 4 .   ? 12.06700  -30.86400 7.86600   1.000 64.14318  ? 519 HOH   A O   1 
HETATM 2515 O  O   . HOH   E 4 .   ? 34.32100  -31.32300 -0.40100  1.000 63.06325  ? 520 HOH   A O   1 
HETATM 2516 O  O   . HOH   E 4 .   ? 10.40200  -27.58900 -10.76600 1.000 51.93170  ? 521 HOH   A O   1 
HETATM 2517 O  O   . HOH   E 4 .   ? 16.23800  -13.90600 4.69000   1.000 83.20462  ? 522 HOH   A O   1 
HETATM 2518 O  O   . HOH   E 4 .   ? -9.32100  -20.85400 3.36600   1.000 86.99834  ? 523 HOH   A O   1 
HETATM 2519 O  O   . HOH   E 4 .   ? 35.16000  -36.30500 -19.54600 1.000 74.22259  ? 524 HOH   A O   1 
HETATM 2520 O  O   . HOH   E 4 .   ? 2.25400   -24.15400 5.05100   1.000 74.34131  ? 525 HOH   A O   1 
HETATM 2521 O  O   . HOH   E 4 .   ? 17.77600  -50.92600 -1.75300  1.000 52.74600  ? 526 HOH   A O   1 
HETATM 2522 O  O   . HOH   E 4 .   ? 34.69200  -39.69700 -10.55200 1.000 50.11096  ? 527 HOH   A O   1 
HETATM 2523 O  O   . HOH   E 4 .   ? 32.85900  -43.21100 1.55700   1.000 57.79550  ? 528 HOH   A O   1 
HETATM 2524 O  O   . HOH   E 4 .   ? 36.23200  -29.28400 -8.03000  1.000 59.07879  ? 529 HOH   A O   1 
HETATM 2525 O  O   . HOH   E 4 .   ? 25.59500  -42.96200 -18.58800 1.000 60.07778  ? 530 HOH   A O   1 
HETATM 2526 O  O   . HOH   E 4 .   ? -4.92600  -30.59500 0.71400   1.000 64.76731  ? 531 HOH   A O   1 
HETATM 2527 O  O   . HOH   E 4 .   ? 32.97600  -45.77400 5.73200   1.000 70.88594  ? 532 HOH   A O   1 
HETATM 2528 O  O   . HOH   E 4 .   ? -5.03200  -25.01800 0.74500   1.000 71.64050  ? 533 HOH   A O   1 
HETATM 2529 O  O   . HOH   E 4 .   ? -3.18900  -19.50100 -16.72300 1.000 87.37502  ? 534 HOH   A O   1 
HETATM 2530 O  O   . HOH   E 4 .   ? 39.92400  -8.72800  -12.87200 1.000 64.38369  ? 535 HOH   A O   1 
HETATM 2531 O  O   . HOH   E 4 .   ? 27.17900  -53.31300 2.42300   1.000 74.18065  ? 536 HOH   A O   1 
HETATM 2532 O  O   . HOH   E 4 .   ? 20.90700  -34.32600 8.01400   1.000 75.96051  ? 537 HOH   A O   1 
HETATM 2533 O  O   . HOH   E 4 .   ? 3.73600   -38.97700 1.82800   1.000 67.43753  ? 538 HOH   A O   1 
HETATM 2534 O  O   . HOH   E 4 .   ? 4.91500   -24.71800 7.09400   1.000 80.97138  ? 539 HOH   A O   1 
HETATM 2535 O  O   . HOH   E 4 .   ? 33.74200  -27.13000 -0.54700  1.000 65.44617  ? 540 HOH   A O   1 
HETATM 2536 O  O   . HOH   E 4 .   ? 24.497    3.653     -11.861   1.000 84.39013  ? 541 HOH   A O   1 
HETATM 2537 O  O   . HOH   E 4 .   ? 14.03700  -13.94900 -19.07700 1.000 109.94075 ? 542 HOH   A O   1 
HETATM 2538 O  O   . HOH   E 4 .   ? -7.05700  -20.88500 0.32500   1.000 82.16330  ? 543 HOH   A O   1 
HETATM 2539 O  O   . HOH   E 4 .   ? 1.15300   -30.49100 6.61100   1.000 67.39635  ? 544 HOH   A O   1 
HETATM 2540 O  O   . HOH   E 4 .   ? 37.19400  -12.54100 -13.02400 1.000 77.80999  ? 545 HOH   A O   1 
HETATM 2541 O  O   . HOH   E 4 .   ? 31.90300  -10.64500 -1.50800  1.000 74.75936  ? 546 HOH   A O   1 
HETATM 2542 O  O   . HOH   E 4 .   ? -2.33000  -35.20500 -6.52600  1.000 71.05391  ? 547 HOH   A O   1 
HETATM 2543 O  O   . HOH   E 4 .   ? 37.32400  -37.02300 2.63800   1.000 84.65177  ? 548 HOH   A O   1 
HETATM 2544 O  O   . HOH   E 4 .   ? 13.55800  -31.69800 -21.51700 1.000 66.83915  ? 549 HOH   A O   1 
HETATM 2545 O  O   . HOH   E 4 .   ? 10.55200  -28.84500 -13.18300 1.000 66.27416  ? 550 HOH   A O   1 
HETATM 2546 O  O   . HOH   E 4 .   ? 43.74000  -28.39000 -8.00700  1.000 78.18568  ? 551 HOH   A O   1 
HETATM 2547 O  O   . HOH   E 4 .   ? -4.67300  -32.57700 -6.29400  1.000 77.48278  ? 552 HOH   A O   1 
HETATM 2548 O  O   . HOH   E 4 .   ? 10.68800  -48.61800 -2.00600  1.000 75.15104  ? 553 HOH   A O   1 
HETATM 2549 O  O   . HOH   E 4 .   ? 20.67200  -1.23900  -6.28800  1.000 76.46341  ? 554 HOH   A O   1 
HETATM 2550 O  O   . HOH   E 4 .   ? -2.44400  -36.38000 -2.99000  1.000 67.84640  ? 555 HOH   A O   1 
HETATM 2551 O  O   . HOH   E 4 .   ? 38.87900  -30.68700 -7.05200  1.000 61.20269  ? 556 HOH   A O   1 
HETATM 2552 O  O   . HOH   E 4 .   ? -7.84700  -23.58100 -1.65300  1.000 82.58643  ? 557 HOH   A O   1 
HETATM 2553 O  O   . HOH   E 4 .   ? 31.75700  -2.31100  -3.17300  1.000 65.30630  ? 558 HOH   A O   1 
HETATM 2554 O  O   . HOH   E 4 .   ? 8.99900   -32.04700 -31.13300 1.000 81.77827  ? 559 HOH   A O   1 
HETATM 2555 O  O   . HOH   E 4 .   ? 11.60400  -52.98700 -13.69500 1.000 74.40508  ? 560 HOH   A O   1 
HETATM 2556 O  O   . HOH   E 4 .   ? 34.09500  -21.19800 -13.29300 1.000 65.10490  ? 561 HOH   A O   1 
HETATM 2557 O  O   . HOH   E 4 .   ? 35.22700  -20.31100 -15.53200 1.000 77.18769  ? 562 HOH   A O   1 
HETATM 2558 O  O   . HOH   E 4 .   ? 22.65800  -25.90600 1.18000   1.000 63.24701  ? 563 HOH   A O   1 
HETATM 2559 O  O   . HOH   E 4 .   ? 7.50000   -35.42200 -36.28600 1.000 75.29741  ? 564 HOH   A O   1 
HETATM 2560 O  O   . HOH   E 4 .   ? 43.85700  -23.75800 -25.19400 1.000 104.14575 ? 565 HOH   A O   1 
HETATM 2561 O  O   . HOH   E 4 .   ? 15.30900  -3.84800  -3.11200  1.000 71.19461  ? 566 HOH   A O   1 
HETATM 2562 O  O   . HOH   E 4 .   ? 29.40700  -39.23900 -22.06000 1.000 70.27362  ? 567 HOH   A O   1 
HETATM 2563 O  O   . HOH   E 4 .   ? 22.71400  -24.55200 5.30100   1.000 79.36439  ? 568 HOH   A O   1 
HETATM 2564 O  O   . HOH   E 4 .   ? 30.98800  -13.61500 -0.57500  1.000 71.42302  ? 569 HOH   A O   1 
HETATM 2565 O  O   . HOH   E 4 .   ? 40.38500  -35.51700 -3.85800  1.000 67.81219  ? 570 HOH   A O   1 
HETATM 2566 O  O   . HOH   E 4 .   ? 21.24900  -52.06200 -4.75500  1.000 70.24094  ? 571 HOH   A O   1 
HETATM 2567 O  O   . HOH   E 4 .   ? 20.97300  -37.18000 -24.32500 1.000 65.91666  ? 572 HOH   A O   1 
HETATM 2568 O  O   . HOH   E 4 .   ? 0.79700   -38.03700 -9.51200  1.000 65.73797  ? 573 HOH   A O   1 
HETATM 2569 O  O   . HOH   E 4 .   ? 16.97100  -29.44300 -20.92100 1.000 72.49787  ? 574 HOH   A O   1 
HETATM 2570 O  O   . HOH   E 4 .   ? 5.81200   0.60600   -25.23000 1.000 88.47671  ? 575 HOH   A O   1 
HETATM 2571 O  O   . HOH   E 4 .   ? 10.84800  -9.33300  -28.22800 1.000 85.46090  ? 576 HOH   A O   1 
HETATM 2572 O  O   . HOH   E 4 .   ? 14.38300  -28.23000 -22.62700 1.000 71.69113  ? 577 HOH   A O   1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1    N N   . SER A 1   ? 1.64729 1.10017 1.32336 0.04003  -0.19551 0.18284  37  SER A N   
2    C CA  . SER A 1   ? 1.67536 1.12508 1.38643 0.03662  -0.16161 0.15149  37  SER A CA  
3    C C   . SER A 1   ? 1.65480 1.16071 1.39172 0.02914  -0.15034 0.11580  37  SER A C   
4    O O   . SER A 1   ? 1.64803 1.19443 1.39738 0.03619  -0.16946 0.11144  37  SER A O   
5    C CB  . SER A 1   ? 1.66591 1.09549 1.43480 0.06582  -0.16120 0.15176  37  SER A CB  
6    O OG  . SER A 1   ? 1.64641 1.06597 1.43475 0.05590  -0.13034 0.12577  37  SER A OG  
7    N N   . SER A 2   ? 1.59300 1.10180 1.34138 0.01421  -0.11972 0.09189  38  SER A N   
8    C CA  . SER A 2   ? 1.54726 1.10359 1.32218 0.00667  -0.10590 0.06235  38  SER A CA  
9    C C   . SER A 2   ? 1.43124 1.01708 1.27062 0.02810  -0.10713 0.04553  38  SER A C   
10   O O   . SER A 2   ? 1.28692 0.91315 1.15263 0.02649  -0.10139 0.02608  38  SER A O   
11   C CB  . SER A 2   ? 1.52754 1.07950 1.29152 -0.01893 -0.07361 0.04857  38  SER A CB  
12   O OG  . SER A 2   ? 1.58821 1.11280 1.36617 -0.01945 -0.06141 0.05060  38  SER A OG  
13   N N   . VAL A 3   ? 1.46357 1.02756 1.32775 0.04658  -0.11172 0.05191  39  VAL A N   
14   C CA  . VAL A 3   ? 1.29402 0.88152 1.21224 0.06284  -0.10802 0.03440  39  VAL A CA  
15   C C   . VAL A 3   ? 1.27951 0.87571 1.22606 0.09021  -0.13072 0.04349  39  VAL A C   
16   O O   . VAL A 3   ? 1.38157 0.94458 1.31864 0.10289  -0.14455 0.06609  39  VAL A O   
17   C CB  . VAL A 3   ? 1.25468 0.81295 1.18205 0.05877  -0.08988 0.02743  39  VAL A CB  
18   C CG1 . VAL A 3   ? 1.11533 0.69627 1.08926 0.07280  -0.08583 0.00917  39  VAL A CG1 
19   C CG2 . VAL A 3   ? 1.25881 0.81931 1.16912 0.03122  -0.06944 0.01908  39  VAL A CG2 
20   N N   . VAL A 4   ? 1.12959 0.77081 1.11579 0.09961  -0.13380 0.02772  40  VAL A N   
21   C CA  . VAL A 4   ? 1.16210 0.82074 1.18990 0.12554  -0.15093 0.03168  40  VAL A CA  
22   C C   . VAL A 4   ? 1.09981 0.76999 1.17220 0.13486  -0.13316 0.01041  40  VAL A C   
23   O O   . VAL A 4   ? 0.99853 0.68095 1.07025 0.11969  -0.11472 -0.00676 40  VAL A O   
24   C CB  . VAL A 4   ? 1.16884 0.87391 1.20407 0.12539  -0.17092 0.03143  40  VAL A CB  
25   C CG1 . VAL A 4   ? 1.21641 0.91147 1.19399 0.10713  -0.18446 0.04738  40  VAL A CG1 
26   C CG2 . VAL A 4   ? 1.07795 0.82251 1.13624 0.11539  -0.15546 0.00566  40  VAL A CG2 
27   N N   . GLY A 5   ? 1.05350 0.72005 1.16537 0.15933  -0.13812 0.01285  41  GLY A N   
28   C CA  . GLY A 5   ? 0.97474 0.65078 1.12487 0.16644  -0.11835 -0.00943 41  GLY A CA  
29   C C   . GLY A 5   ? 1.00104 0.64258 1.13029 0.15123  -0.09412 -0.02225 41  GLY A C   
30   O O   . GLY A 5   ? 0.94391 0.60378 1.08517 0.14302  -0.07713 -0.04320 41  GLY A O   
31   N N   . LEU A 6   ? 0.98076 0.57404 1.07628 0.14410  -0.09279 -0.00934 42  LEU A N   
32   C CA  . LEU A 6   ? 0.95858 0.51588 1.03356 0.12628  -0.07111 -0.02136 42  LEU A CA  
33   C C   . LEU A 6   ? 0.96525 0.54835 1.01793 0.09778  -0.06242 -0.03205 42  LEU A C   
34   O O   . LEU A 6   ? 0.91686 0.47424 0.94046 0.07750  -0.05392 -0.03042 42  LEU A O   
35   C CB  . LEU A 6   ? 1.01018 0.55596 1.11577 0.13544  -0.05230 -0.04303 42  LEU A CB  
36   C CG  . LEU A 6   ? 1.08590 0.57972 1.21248 0.15740  -0.04640 -0.03766 42  LEU A CG  
37   C CD1 . LEU A 6   ? 1.15049 0.65091 1.30465 0.18744  -0.07140 -0.01029 42  LEU A CD1 
38   C CD2 . LEU A 6   ? 1.18696 0.68000 1.34468 0.16201  -0.02149 -0.06770 42  LEU A CD2 
39   N N   . HIS A 7   ? 0.77732 0.41141 0.84811 0.09594  -0.06392 -0.04133 43  HIS A N   
40   C CA  . HIS A 7   ? 0.87398 0.53461 0.93686 0.07280  -0.05467 -0.04989 43  HIS A CA  
41   C C   . HIS A 7   ? 0.82990 0.52662 0.89484 0.06800  -0.06148 -0.04337 43  HIS A C   
42   O O   . HIS A 7   ? 0.74987 0.47429 0.82128 0.05367  -0.05440 -0.04762 43  HIS A O   
43   C CB  . HIS A 7   ? 0.79954 0.48371 0.88190 0.06992  -0.04391 -0.06800 43  HIS A CB  
44   C CG  . HIS A 7   ? 0.84440 0.49259 0.92523 0.07202  -0.03122 -0.08150 43  HIS A CG  
45   N ND1 . HIS A 7   ? 0.93749 0.59055 1.04483 0.08776  -0.02365 -0.09485 43  HIS A ND1 
46   C CD2 . HIS A 7   ? 0.86407 0.46836 0.92227 0.05894  -0.02106 -0.08628 43  HIS A CD2 
47   C CE1 . HIS A 7   ? 0.98608 0.59778 1.08729 0.08528  -0.00768 -0.10870 43  HIS A CE1 
48   N NE2 . HIS A 7   ? 0.98873 0.56880 1.05909 0.06718  -0.00646 -0.10386 43  HIS A NE2 
49   N N   . TYR A 8   ? 0.82863 0.52595 0.88924 0.07826  -0.07467 -0.03306 44  TYR A N   
50   C CA  . TYR A 8   ? 0.85678 0.58676 0.92135 0.07273  -0.07753 -0.03317 44  TYR A CA  
51   C C   . TYR A 8   ? 0.96979 0.68025 0.99766 0.06390  -0.08275 -0.02165 44  TYR A C   
52   O O   . TYR A 8   ? 0.99056 0.68352 1.00215 0.07334  -0.09843 -0.00966 44  TYR A O   
53   C CB  . TYR A 8   ? 0.75359 0.51464 0.84912 0.08803  -0.08725 -0.03819 44  TYR A CB  
54   C CG  . TYR A 8   ? 0.76588 0.54335 0.89248 0.09477  -0.07878 -0.04959 44  TYR A CG  
55   C CD1 . TYR A 8   ? 0.73034 0.53343 0.86947 0.08333  -0.06693 -0.05631 44  TYR A CD1 
56   C CD2 . TYR A 8   ? 0.84521 0.61187 0.98886 0.11184  -0.08107 -0.05250 44  TYR A CD2 
57   C CE1 . TYR A 8   ? 0.74730 0.56510 0.90507 0.08518  -0.05877 -0.06547 44  TYR A CE1 
58   C CE2 . TYR A 8   ? 0.81971 0.60007 0.98654 0.11445  -0.06845 -0.06632 44  TYR A CE2 
59   C CZ  . TYR A 8   ? 0.81857 0.62450 0.98723 0.09928  -0.05787 -0.07271 44  TYR A CZ  
60   O OH  . TYR A 8   ? 0.93387 0.75323 1.11650 0.09803  -0.04512 -0.08525 44  TYR A OH  
61   N N   . LYS A 9   ? 0.88975 0.60516 0.90616 0.04526  -0.06920 -0.02403 45  LYS A N   
62   C CA  . LYS A 9   ? 0.99822 0.69708 0.97629 0.03153  -0.06718 -0.01717 45  LYS A CA  
63   C C   . LYS A 9   ? 0.95180 0.67775 0.93273 0.02794  -0.06798 -0.02536 45  LYS A C   
64   O O   . LYS A 9   ? 0.85083 0.60674 0.86715 0.02826  -0.05853 -0.03711 45  LYS A O   
65   C CB  . LYS A 9   ? 0.97727 0.66746 0.94704 0.01168  -0.04681 -0.01824 45  LYS A CB  
66   C CG  . LYS A 9   ? 1.15934 0.82838 1.08538 -0.00587 -0.03877 -0.01242 45  LYS A CG  
67   C CD  . LYS A 9   ? 1.17250 0.84634 1.10679 -0.02552 -0.01418 -0.01731 45  LYS A CD  
68   C CE  . LYS A 9   ? 1.20958 0.86206 1.09859 -0.04565 -0.00052 -0.01411 45  LYS A CE  
69   N NZ  . LYS A 9   ? 0.95204 0.61967 0.86302 -0.06368 0.02766  -0.02229 45  LYS A NZ  
70   N N   . ILE A 10  ? 0.98649 0.70016 0.92783 0.02237  -0.07914 -0.01851 46  ILE A N   
71   C CA  . ILE A 10  ? 1.05611 0.79215 0.99103 0.01367  -0.08037 -0.02965 46  ILE A CA  
72   C C   . ILE A 10  ? 1.10095 0.84205 1.03698 -0.00555 -0.05074 -0.04451 46  ILE A C   
73   O O   . ILE A 10  ? 1.18871 0.91803 1.12693 -0.01266 -0.03290 -0.04226 46  ILE A O   
74   C CB  . ILE A 10  ? 1.10266 0.82563 0.98574 0.00740  -0.10218 -0.01689 46  ILE A CB  
75   C CG1 . ILE A 10  ? 1.28760 0.97266 1.11544 -0.00966 -0.09330 -0.00384 46  ILE A CG1 
76   C CG2 . ILE A 10  ? 1.09101 0.81674 0.99040 0.03095  -0.13247 -0.00067 46  ILE A CG2 
77   C CD1 . ILE A 10  ? 1.31486 0.99930 1.10212 -0.03847 -0.07282 -0.01738 46  ILE A CD1 
78   N N   . GLY A 11  ? 1.16228 0.92135 1.10101 -0.01489 -0.04386 -0.06086 47  GLY A N   
79   C CA  . GLY A 11  ? 1.16360 0.92564 1.11149 -0.03120 -0.01155 -0.07744 47  GLY A CA  
80   C C   . GLY A 11  ? 1.29781 1.06489 1.22174 -0.04872 -0.00504 -0.09680 47  GLY A C   
81   O O   . GLY A 11  ? 1.32316 1.08333 1.19466 -0.05861 -0.02482 -0.09315 47  GLY A O   
82   N N   . LYS A 12  ? 1.32630 1.10507 1.28873 -0.05389 0.02238  -0.11680 48  LYS A N   
83   C CA  . LYS A 12  ? 1.31014 1.09011 1.25270 -0.07417 0.03506  -0.14172 48  LYS A CA  
84   C C   . LYS A 12  ? 1.28016 1.07954 1.22318 -0.06981 0.00529  -0.14430 48  LYS A C   
85   O O   . LYS A 12  ? 1.21675 1.03385 1.20482 -0.04819 -0.01053 -0.13445 48  LYS A O   
86   C CB  . LYS A 12  ? 1.24435 1.02820 1.24177 -0.07672 0.07460  -0.16164 48  LYS A CB  
87   C CG  . LYS A 12  ? 1.33727 1.11525 1.31690 -0.10101 0.09706  -0.19396 48  LYS A CG  
88   C CD  . LYS A 12  ? 1.27522 1.05670 1.32826 -0.09527 0.13202  -0.20999 48  LYS A CD  
89   C CE  . LYS A 12  ? 1.24447 1.03822 1.32095 -0.09455 0.12211  -0.22246 48  LYS A CE  
90   N NZ  . LYS A 12  ? 1.26131 1.05428 1.41463 -0.08549 0.15418  -0.23116 48  LYS A NZ  
91   N N   . LYS A 13  ? 1.30565 1.10440 1.19732 -0.09320 -0.00186 -0.15831 49  LYS A N   
92   C CA  . LYS A 13  ? 1.23812 1.06191 1.13314 -0.09443 -0.02971 -0.16375 49  LYS A CA  
93   C C   . LYS A 13  ? 1.23441 1.06839 1.17643 -0.10152 -0.00440 -0.19232 49  LYS A C   
94   O O   . LYS A 13  ? 1.32043 1.13860 1.25179 -0.12327 0.03025  -0.21807 49  LYS A O   
95   C CB  . LYS A 13  ? 1.31675 1.14038 1.13439 -0.12066 -0.05204 -0.16518 49  LYS A CB  
96   C CG  . LYS A 13  ? 1.35441 1.21189 1.17696 -0.12566 -0.08470 -0.17040 49  LYS A CG  
97   C CD  . LYS A 13  ? 1.44098 1.30188 1.18199 -0.15991 -0.10398 -0.17554 49  LYS A CD  
98   C CE  . LYS A 13  ? 1.47567 1.31877 1.15799 -0.15690 -0.12705 -0.14110 49  LYS A CE  
99   N NZ  . LYS A 13  ? 1.58319 1.43143 1.17839 -0.19278 -0.14928 -0.14097 49  LYS A NZ  
100  N N   . ILE A 14  ? 1.11293 0.97058 1.10856 -0.08390 -0.01833 -0.18846 50  ILE A N   
101  C CA  . ILE A 14  ? 1.20736 1.07232 1.25181 -0.08951 0.00431  -0.21140 50  ILE A CA  
102  C C   . ILE A 14  ? 1.20883 1.09906 1.24712 -0.10527 -0.01740 -0.22674 50  ILE A C   
103  O O   . ILE A 14  ? 1.13851 1.03430 1.21745 -0.11247 0.00002  -0.24659 50  ILE A O   
104  C CB  . ILE A 14  ? 1.12220 0.99412 1.23702 -0.06178 0.01256  -0.19615 50  ILE A CB  
105  C CG1 . ILE A 14  ? 1.05696 0.94444 1.17622 -0.03765 -0.02056 -0.16840 50  ILE A CG1 
106  C CG2 . ILE A 14  ? 1.14748 0.99843 1.28638 -0.05631 0.04700  -0.19323 50  ILE A CG2 
107  C CD1 . ILE A 14  ? 0.99602 0.89143 1.17177 -0.01537 -0.01345 -0.15414 50  ILE A CD1 
108  N N   . GLY A 15  ? 1.22303 1.12990 1.21551 -0.11155 -0.05541 -0.21649 51  GLY A N   
109  C CA  . GLY A 15  ? 1.29166 1.23130 1.28164 -0.12854 -0.08068 -0.22936 51  GLY A CA  
110  C C   . GLY A 15  ? 1.41278 1.37248 1.35555 -0.12964 -0.12765 -0.20698 51  GLY A C   
111  O O   . GLY A 15  ? 1.41768 1.36694 1.34815 -0.10759 -0.14299 -0.17683 51  GLY A O   
112  N N   . GLU A 16  ? 1.52473 1.51360 1.44309 -0.15699 -0.15085 -0.22131 52  GLU A N   
113  C CA  . GLU A 16  ? 1.59246 1.60963 1.47125 -0.16051 -0.20158 -0.19731 52  GLU A CA  
114  C C   . GLU A 16  ? 1.62087 1.68344 1.49961 -0.19027 -0.22583 -0.21758 52  GLU A C   
115  O O   . GLU A 16  ? 1.67463 1.74026 1.48347 -0.22978 -0.23436 -0.23287 52  GLU A O   
116  C CB  . GLU A 16  ? 1.59939 1.58611 1.38879 -0.17852 -0.20325 -0.18681 52  GLU A CB  
117  C CG  . GLU A 16  ? 1.58395 1.58990 1.33628 -0.17150 -0.25632 -0.14699 52  GLU A CG  
118  C CD  . GLU A 16  ? 1.62456 1.65797 1.30738 -0.21407 -0.28692 -0.15443 52  GLU A CD  
119  O OE1 . GLU A 16  ? 1.67146 1.69196 1.30778 -0.25460 -0.25837 -0.19269 52  GLU A OE1 
120  O OE2 . GLU A 16  ? 1.59720 1.66580 1.27308 -0.20780 -0.33936 -0.12187 52  GLU A OE2 
121  N N   . GLY A 17  ? 1.66151 1.76093 1.61598 -0.17527 -0.23586 -0.21945 53  GLY A N   
122  C CA  . GLY A 17  ? 1.73820 1.88413 1.70317 -0.20564 -0.25587 -0.24176 53  GLY A CA  
123  C C   . GLY A 17  ? 1.76908 1.96981 1.81486 -0.18286 -0.28562 -0.22736 53  GLY A C   
124  O O   . GLY A 17  ? 1.78876 2.01798 1.84761 -0.15858 -0.32631 -0.19215 53  GLY A O   
125  N N   . SER A 18  ? 1.72607 1.94019 1.83058 -0.19037 -0.26258 -0.25417 54  SER A N   
126  C CA  . SER A 18  ? 1.65524 1.92813 1.83648 -0.17889 -0.28721 -0.24835 54  SER A CA  
127  C C   . SER A 18  ? 1.69456 1.97296 1.93359 -0.12809 -0.29366 -0.21439 54  SER A C   
128  O O   . SER A 18  ? 1.60709 1.93833 1.90869 -0.11374 -0.31941 -0.20320 54  SER A O   
129  C CB  . SER A 18  ? 1.58174 1.85735 1.81003 -0.19979 -0.25282 -0.28470 54  SER A CB  
130  O OG  . SER A 18  ? 1.52812 1.85514 1.83873 -0.18421 -0.26696 -0.27791 54  SER A OG  
131  N N   . PHE A 19  ? 1.91298 2.13983 2.13534 -0.10238 -0.26920 -0.19992 55  PHE A N   
132  C CA  . PHE A 19  ? 1.83765 2.06335 2.10976 -0.05874 -0.26887 -0.17382 55  PHE A CA  
133  C C   . PHE A 19  ? 1.88391 2.07463 2.11109 -0.03708 -0.27948 -0.14430 55  PHE A C   
134  O O   . PHE A 19  ? 1.89288 2.06348 2.14618 -0.00534 -0.26724 -0.12843 55  PHE A O   
135  C CB  . PHE A 19  ? 1.82023 2.02060 2.13249 -0.04866 -0.22358 -0.18664 55  PHE A CB  
136  C CG  . PHE A 19  ? 1.88983 2.11287 2.24164 -0.07282 -0.20653 -0.21528 55  PHE A CG  
137  C CD1 . PHE A 19  ? 1.71650 1.99443 2.13225 -0.07000 -0.22278 -0.21688 55  PHE A CD1 
138  C CD2 . PHE A 19  ? 1.85918 2.04752 2.18932 -0.09859 -0.17174 -0.24085 55  PHE A CD2 
139  C CE1 . PHE A 19  ? 1.60061 1.89766 2.05305 -0.09526 -0.20541 -0.24348 55  PHE A CE1 
140  C CE2 . PHE A 19  ? 1.74223 1.94482 2.10995 -0.12193 -0.15357 -0.26691 55  PHE A CE2 
141  C CZ  . PHE A 19  ? 1.61053 1.86712 2.03700 -0.12167 -0.17078 -0.26823 55  PHE A CZ  
142  N N   . GLY A 20  ? 1.78142 1.96332 1.93863 -0.05660 -0.30069 -0.13739 56  GLY A N   
143  C CA  . GLY A 20  ? 1.68873 1.83724 1.80053 -0.03972 -0.31254 -0.10705 56  GLY A CA  
144  C C   . GLY A 20  ? 1.56862 1.65950 1.62099 -0.05257 -0.27663 -0.11722 56  GLY A C   
145  O O   . GLY A 20  ? 1.57996 1.65592 1.62408 -0.07485 -0.24316 -0.14757 56  GLY A O   
146  N N   . VAL A 21  ? 1.50096 1.55854 1.51675 -0.03759 -0.28254 -0.09039 57  VAL A N   
147  C CA  . VAL A 21  ? 1.47112 1.47704 1.43519 -0.04774 -0.24979 -0.09591 57  VAL A CA  
148  C C   . VAL A 21  ? 1.39876 1.38247 1.41155 -0.02355 -0.21586 -0.09926 57  VAL A C   
149  O O   . VAL A 21  ? 1.44953 1.43178 1.49777 0.00662  -0.22381 -0.07940 57  VAL A O   
150  C CB  . VAL A 21  ? 1.49449 1.47394 1.39623 -0.04624 -0.27013 -0.06490 57  VAL A CB  
151  C CG1 . VAL A 21  ? 1.51559 1.45283 1.35029 -0.07222 -0.23837 -0.07779 57  VAL A CG1 
152  C CG2 . VAL A 21  ? 1.51660 1.53136 1.39083 -0.05731 -0.31925 -0.04609 57  VAL A CG2 
153  N N   . ILE A 22  ? 1.34532 1.31206 1.36099 -0.03765 -0.17770 -0.12414 58  ILE A N   
154  C CA  . ILE A 22  ? 1.23359 1.18513 1.29433 -0.01911 -0.14773 -0.12580 58  ILE A CA  
155  C C   . ILE A 22  ? 1.19373 1.10591 1.21981 -0.02707 -0.11927 -0.12702 58  ILE A C   
156  O O   . ILE A 22  ? 1.19411 1.09393 1.18467 -0.05294 -0.10195 -0.14521 58  ILE A O   
157  C CB  . ILE A 22  ? 1.14989 1.12056 1.26239 -0.02465 -0.12779 -0.14851 58  ILE A CB  
158  C CG1 . ILE A 22  ? 1.21901 1.23377 1.36393 -0.02389 -0.15519 -0.15114 58  ILE A CG1 
159  C CG2 . ILE A 22  ? 1.06391 1.02457 1.22157 -0.00416 -0.10440 -0.14227 58  ILE A CG2 
160  C CD1 . ILE A 22  ? 1.18067 1.21406 1.38541 -0.02413 -0.13619 -0.16738 58  ILE A CD1 
161  N N   . PHE A 23  ? 1.11430 1.00837 1.15266 -0.00697 -0.11251 -0.11003 59  PHE A N   
162  C CA  . PHE A 23  ? 1.11089 0.97380 1.12718 -0.01253 -0.08724 -0.10828 59  PHE A CA  
163  C C   . PHE A 23  ? 0.99446 0.85809 1.06269 0.00062  -0.06397 -0.10887 59  PHE A C   
164  O O   . PHE A 23  ? 0.99812 0.88086 1.10991 0.01562  -0.06918 -0.10658 59  PHE A O   
165  C CB  . PHE A 23  ? 1.12260 0.96163 1.09900 -0.00573 -0.10247 -0.08457 59  PHE A CB  
166  C CG  . PHE A 23  ? 1.21291 1.04425 1.12584 -0.02304 -0.12201 -0.07810 59  PHE A CG  
167  C CD1 . PHE A 23  ? 1.28143 1.09024 1.14128 -0.04854 -0.10252 -0.08605 59  PHE A CD1 
168  C CD2 . PHE A 23  ? 1.25744 1.10601 1.16451 -0.01451 -0.15978 -0.06222 59  PHE A CD2 
169  C CE1 . PHE A 23  ? 1.37886 1.18042 1.17034 -0.06858 -0.12082 -0.07839 59  PHE A CE1 
170  C CE2 . PHE A 23  ? 1.35012 1.19465 1.19518 -0.03190 -0.18238 -0.05075 59  PHE A CE2 
171  C CZ  . PHE A 23  ? 1.39734 1.21724 1.17906 -0.06063 -0.16320 -0.05876 59  PHE A CZ  
172  N N   . GLU A 24  ? 0.94226 0.78744 1.00556 -0.00668 -0.03821 -0.11070 60  GLU A N   
173  C CA  . GLU A 24  ? 0.90271 0.74916 1.00678 0.00548  -0.02332 -0.10223 60  GLU A CA  
174  C C   . GLU A 24  ? 0.92683 0.75919 1.01169 0.01497  -0.03601 -0.08357 60  GLU A C   
175  O O   . GLU A 24  ? 0.93887 0.75161 0.97761 0.00934  -0.04641 -0.07680 60  GLU A O   
176  C CB  . GLU A 24  ? 0.93216 0.77126 1.05232 -0.00551 0.00962  -0.11102 60  GLU A CB  
177  C CG  . GLU A 24  ? 1.04712 0.89489 1.20253 -0.01180 0.02949  -0.12929 60  GLU A CG  
178  C CD  . GLU A 24  ? 1.01995 0.86070 1.20900 -0.01648 0.06481  -0.13467 60  GLU A CD  
179  O OE1 . GLU A 24  ? 0.82317 0.65715 1.00678 -0.01708 0.07318  -0.12543 60  GLU A OE1 
180  O OE2 . GLU A 24  ? 1.00408 0.84616 1.23051 -0.01946 0.08554  -0.14799 60  GLU A OE2 
181  N N   . GLY A 25  ? 0.83730 0.67797 0.95515 0.02715  -0.03465 -0.07502 61  GLY A N   
182  C CA  . GLY A 25  ? 0.82968 0.65498 0.93175 0.03355  -0.04388 -0.06193 61  GLY A CA  
183  C C   . GLY A 25  ? 0.76980 0.60392 0.90028 0.03391  -0.03217 -0.05650 61  GLY A C   
184  O O   . GLY A 25  ? 0.64792 0.50320 0.81555 0.03381  -0.02088 -0.05805 61  GLY A O   
185  N N   . THR A 26  ? 0.72222 0.53950 0.83476 0.03300  -0.03610 -0.04857 62  THR A N   
186  C CA  . THR A 26  ? 0.69154 0.51942 0.82364 0.02863  -0.02955 -0.04317 62  THR A CA  
187  C C   . THR A 26  ? 0.69159 0.50279 0.80677 0.03258  -0.03965 -0.04134 62  THR A C   
188  O O   . THR A 26  ? 0.69096 0.47047 0.77463 0.03206  -0.04430 -0.03893 62  THR A O   
189  C CB  . THR A 26  ? 0.79671 0.62105 0.92714 0.01378  -0.01501 -0.03981 62  THR A CB  
190  O OG1 . THR A 26  ? 0.82355 0.66324 0.97951 0.01123  0.00030  -0.04434 62  THR A OG1 
191  C CG2 . THR A 26  ? 0.79530 0.63565 0.94525 0.00659  -0.01398 -0.03244 62  THR A CG2 
192  N N   . ASN A 27  ? 0.56853 0.39824 0.70323 0.03529  -0.04105 -0.04250 63  ASN A N   
193  C CA  . ASN A 27  ? 0.68172 0.49499 0.80144 0.03471  -0.04423 -0.04596 63  ASN A CA  
194  C C   . ASN A 27  ? 0.74045 0.53848 0.84252 0.01725  -0.03946 -0.04292 63  ASN A C   
195  O O   . ASN A 27  ? 0.65060 0.47355 0.76859 0.00426  -0.03514 -0.03758 63  ASN A O   
196  C CB  . ASN A 27  ? 0.64774 0.48795 0.78633 0.03499  -0.04322 -0.04949 63  ASN A CB  
197  C CG  . ASN A 27  ? 0.75505 0.57672 0.87680 0.03319  -0.04163 -0.05970 63  ASN A CG  
198  O OD1 . ASN A 27  ? 0.73877 0.53898 0.83953 0.02053  -0.03910 -0.06201 63  ASN A OD1 
199  N ND2 . ASN A 27  ? 0.73209 0.56134 0.86507 0.04403  -0.03990 -0.06822 63  ASN A ND2 
200  N N   . ILE A 28  ? 0.61847 0.37617 0.69229 0.01683  -0.04028 -0.04465 64  ILE A N   
201  C CA  . ILE A 28  ? 0.70521 0.44326 0.76058 -0.00238 -0.03389 -0.04240 64  ILE A CA  
202  C C   . ILE A 28  ? 0.67291 0.41736 0.72812 -0.01856 -0.03129 -0.05025 64  ILE A C   
203  O O   . ILE A 28  ? 0.65376 0.38922 0.69852 -0.03903 -0.02637 -0.05015 64  ILE A O   
204  C CB  . ILE A 28  ? 0.76555 0.45199 0.78863 0.00125  -0.03450 -0.03820 64  ILE A CB  
205  C CG1 . ILE A 28  ? 0.73032 0.38473 0.74676 0.01025  -0.03548 -0.04569 64  ILE A CG1 
206  C CG2 . ILE A 28  ? 0.89198 0.57563 0.90794 0.01546  -0.04193 -0.03018 64  ILE A CG2 
207  C CD1 . ILE A 28  ? 0.92240 0.52287 0.91424 0.01831  -0.03758 -0.03592 64  ILE A CD1 
208  N N   . ILE A 29  ? 0.67925 0.44012 0.74325 -0.01340 -0.03352 -0.05831 65  ILE A N   
209  C CA  . ILE A 29  ? 0.69260 0.46512 0.74939 -0.03379 -0.03143 -0.06747 65  ILE A CA  
210  C C   . ILE A 29  ? 0.67296 0.50020 0.75228 -0.04667 -0.03753 -0.05626 65  ILE A C   
211  O O   . ILE A 29  ? 0.68015 0.52416 0.75670 -0.07071 -0.03989 -0.05471 65  ILE A O   
212  C CB  . ILE A 29  ? 0.75390 0.51524 0.80418 -0.02513 -0.02698 -0.08321 65  ILE A CB  
213  C CG1 . ILE A 29  ? 0.81422 0.51922 0.85105 -0.01211 -0.02000 -0.09223 65  ILE A CG1 
214  C CG2 . ILE A 29  ? 0.72742 0.50726 0.76301 -0.05111 -0.02420 -0.09446 65  ILE A CG2 
215  C CD1 . ILE A 29  ? 0.86363 0.52939 0.87521 -0.03319 -0.01187 -0.10005 65  ILE A CD1 
216  N N   . ASN A 30  ? 0.72512 0.58182 0.83074 -0.03157 -0.04087 -0.04660 66  ASN A N   
217  C CA  . ASN A 30  ? 0.68853 0.59482 0.82174 -0.03975 -0.04689 -0.03126 66  ASN A CA  
218  C C   . ASN A 30  ? 0.74534 0.66993 0.91560 -0.02929 -0.04447 -0.01657 66  ASN A C   
219  O O   . ASN A 30  ? 0.75672 0.72093 0.95978 -0.03411 -0.04850 0.00005  66  ASN A O   
220  C CB  . ASN A 30  ? 0.65595 0.58283 0.79058 -0.03565 -0.04937 -0.03140 66  ASN A CB  
221  C CG  . ASN A 30  ? 0.75518 0.66750 0.89807 -0.01148 -0.04420 -0.03759 66  ASN A CG  
222  O OD1 . ASN A 30  ? 0.70390 0.60908 0.86307 0.00219  -0.04251 -0.03392 66  ASN A OD1 
223  N ND2 . ASN A 30  ? 0.78520 0.69529 0.91674 -0.00876 -0.04056 -0.04882 66  ASN A ND2 
224  N N   . GLY A 31  ? 0.72240 0.61972 0.88907 -0.01610 -0.03752 -0.02170 67  GLY A N   
225  C CA  . GLY A 31  ? 0.66636 0.57591 0.86348 -0.00953 -0.02972 -0.01401 67  GLY A CA  
226  C C   . GLY A 31  ? 0.61756 0.54031 0.83916 0.00598  -0.02777 -0.01201 67  GLY A C   
227  O O   . GLY A 31  ? 0.57545 0.50198 0.82138 0.01081  -0.01731 -0.01028 67  GLY A O   
228  N N   . VAL A 32  ? 0.63192 0.56012 0.84846 0.01180  -0.03411 -0.01439 68  VAL A N   
229  C CA  . VAL A 32  ? 0.62769 0.56918 0.86997 0.02353  -0.03088 -0.01214 68  VAL A CA  
230  C C   . VAL A 32  ? 0.61932 0.53822 0.85390 0.03354  -0.02656 -0.02519 68  VAL A C   
231  O O   . VAL A 32  ? 0.67887 0.57368 0.88267 0.03693  -0.03234 -0.03518 68  VAL A O   
232  C CB  . VAL A 32  ? 0.71751 0.66945 0.95230 0.02439  -0.03600 -0.01342 68  VAL A CB  
233  C CG1 . VAL A 32  ? 0.69714 0.65365 0.95186 0.03622  -0.03126 -0.01690 68  VAL A CG1 
234  C CG2 . VAL A 32  ? 0.73203 0.71490 0.97627 0.01144  -0.04127 0.00428  68  VAL A CG2 
235  N N   . PRO A 33  ? 0.60086 0.52590 0.86224 0.03717  -0.01680 -0.02513 69  PRO A N   
236  C CA  . PRO A 33  ? 0.55366 0.46049 0.80099 0.04082  -0.01431 -0.03953 69  PRO A CA  
237  C C   . PRO A 33  ? 0.64746 0.55626 0.89029 0.04937  -0.02382 -0.04762 69  PRO A C   
238  O O   . PRO A 33  ? 0.58259 0.50843 0.84333 0.05262  -0.02476 -0.04367 69  PRO A O   
239  C CB  . PRO A 33  ? 0.71827 0.63210 1.00023 0.03892  0.00319  -0.04027 69  PRO A CB  
240  C CG  . PRO A 33  ? 0.64582 0.58437 0.96844 0.04157  0.00549  -0.02296 69  PRO A CG  
241  C CD  . PRO A 33  ? 0.61274 0.56035 0.91980 0.03683  -0.00690 -0.01147 69  PRO A CD  
242  N N   . VAL A 34  ? 0.65677 0.55049 0.87586 0.05176  -0.03125 -0.05763 70  VAL A N   
243  C CA  . VAL A 34  ? 0.65530 0.55576 0.87704 0.06056  -0.04242 -0.06491 70  VAL A CA  
244  C C   . VAL A 34  ? 0.71288 0.61127 0.92608 0.05625  -0.04575 -0.07507 70  VAL A C   
245  O O   . VAL A 34  ? 0.71743 0.60240 0.91159 0.04602  -0.03865 -0.07793 70  VAL A O   
246  C CB  . VAL A 34  ? 0.64251 0.52971 0.84427 0.06962  -0.05533 -0.06325 70  VAL A CB  
247  C CG1 . VAL A 34  ? 0.55603 0.44793 0.76407 0.06963  -0.05001 -0.05980 70  VAL A CG1 
248  C CG2 . VAL A 34  ? 0.54895 0.40703 0.71348 0.06603  -0.06075 -0.05868 70  VAL A CG2 
249  N N   . ALA A 35  ? 0.67971 0.59437 0.90750 0.06139  -0.05536 -0.08212 71  ALA A N   
250  C CA  . ALA A 35  ? 0.74324 0.66222 0.95952 0.05495  -0.06551 -0.09210 71  ALA A CA  
251  C C   . ALA A 35  ? 0.82833 0.74776 1.03036 0.06620  -0.09021 -0.08599 71  ALA A C   
252  O O   . ALA A 35  ? 0.77724 0.70879 1.00463 0.08043  -0.09579 -0.08338 71  ALA A O   
253  C CB  . ALA A 35  ? 0.71281 0.65532 0.96447 0.04962  -0.05901 -0.10444 71  ALA A CB  
254  N N   . ILE A 36  ? 0.88390 0.78963 1.04674 0.05970  -0.10350 -0.08255 72  ILE A N   
255  C CA  . ILE A 36  ? 0.95235 0.85482 1.10148 0.07164  -0.12943 -0.06968 72  ILE A CA  
256  C C   . ILE A 36  ? 1.01862 0.94594 1.16327 0.06326  -0.15063 -0.07412 72  ILE A C   
257  O O   . ILE A 36  ? 1.06485 0.98712 1.17277 0.04212  -0.14938 -0.08139 72  ILE A O   
258  C CB  . ILE A 36  ? 0.94007 0.80505 1.04234 0.06953  -0.13150 -0.05523 72  ILE A CB  
259  C CG1 . ILE A 36  ? 0.82442 0.67037 0.93057 0.06974  -0.10887 -0.05496 72  ILE A CG1 
260  C CG2 . ILE A 36  ? 0.97173 0.82754 1.06943 0.08679  -0.15645 -0.03677 72  ILE A CG2 
261  C CD1 . ILE A 36  ? 0.88955 0.69848 0.95608 0.06636  -0.10816 -0.04202 72  ILE A CD1 
262  N N   . LYS A 37  ? 1.00691 0.96345 1.18971 0.07766  -0.16911 -0.07127 73  LYS A N   
263  C CA  . LYS A 37  ? 1.11946 1.10933 1.30580 0.06961  -0.19499 -0.07335 73  LYS A CA  
264  C C   . LYS A 37  ? 1.23306 1.22126 1.40482 0.08317  -0.22817 -0.04820 73  LYS A C   
265  O O   . LYS A 37  ? 1.16210 1.14395 1.36393 0.10899  -0.23254 -0.03430 73  LYS A O   
266  C CB  . LYS A 37  ? 1.08338 1.11568 1.33233 0.07473  -0.19421 -0.08616 73  LYS A CB  
267  C CG  . LYS A 37  ? 1.12869 1.17387 1.38229 0.05011  -0.17692 -0.10981 73  LYS A CG  
268  C CD  . LYS A 37  ? 1.15283 1.24711 1.45032 0.04444  -0.19225 -0.12039 73  LYS A CD  
269  C CE  . LYS A 37  ? 1.08881 1.20517 1.44980 0.06519  -0.18371 -0.11956 73  LYS A CE  
270  N NZ  . LYS A 37  ? 1.05805 1.22208 1.46704 0.05388  -0.18885 -0.13476 73  LYS A NZ  
271  N N   . PHE A 38  ? 1.28871 1.28111 1.41391 0.06473  -0.25040 -0.04197 74  PHE A N   
272  C CA  . PHE A 38  ? 1.34180 1.33571 1.44926 0.07486  -0.28720 -0.01209 74  PHE A CA  
273  C C   . PHE A 38  ? 1.39131 1.44235 1.52779 0.07054  -0.32164 -0.01064 74  PHE A C   
274  O O   . PHE A 38  ? 1.44366 1.51918 1.56359 0.04165  -0.32211 -0.03205 74  PHE A O   
275  C CB  . PHE A 38  ? 1.36341 1.32081 1.38742 0.05397  -0.29056 -0.00029 74  PHE A CB  
276  C CG  . PHE A 38  ? 1.29842 1.20252 1.30059 0.06415  -0.26873 0.01063  74  PHE A CG  
277  C CD1 . PHE A 38  ? 1.33211 1.21157 1.33453 0.08658  -0.28561 0.04179  74  PHE A CD1 
278  C CD2 . PHE A 38  ? 1.22120 1.10068 1.20827 0.05111  -0.23122 -0.00956 74  PHE A CD2 
279  C CE1 . PHE A 38  ? 1.30912 1.13823 1.29163 0.09207  -0.26424 0.04926  74  PHE A CE1 
280  C CE2 . PHE A 38  ? 1.17466 1.01123 1.14502 0.05722  -0.21291 -0.00037 74  PHE A CE2 
281  C CZ  . PHE A 38  ? 1.26184 1.07216 1.22730 0.07588  -0.22877 0.02735  74  PHE A CZ  
282  N N   . GLU A 39  ? 1.38587 1.45886 1.57039 0.09865  -0.34923 0.01364  75  GLU A N   
283  C CA  . GLU A 39  ? 1.45453 1.58947 1.67672 0.09753  -0.38771 0.02103  75  GLU A CA  
284  C C   . GLU A 39  ? 1.50753 1.64129 1.72827 0.11905  -0.42768 0.06507  75  GLU A C   
285  O O   . GLU A 39  ? 1.49058 1.58988 1.73645 0.15070  -0.41873 0.08323  75  GLU A O   
286  C CB  . GLU A 39  ? 1.40299 1.58082 1.71779 0.11490  -0.37738 0.00445  75  GLU A CB  
287  C CG  . GLU A 39  ? 1.42396 1.67022 1.79798 0.12243  -0.41900 0.01828  75  GLU A CG  
288  C CD  . GLU A 39  ? 1.39765 1.67637 1.87277 0.15195  -0.40618 0.01168  75  GLU A CD  
289  O OE1 . GLU A 39  ? 1.37221 1.61628 1.87286 0.18235  -0.38571 0.01973  75  GLU A OE1 
290  O OE2 . GLU A 39  ? 1.42104 1.75915 1.94897 0.14195  -0.41368 -0.00411 75  GLU A OE2 
291  N N   . PRO A 40  ? 1.61690 1.78665 1.80982 0.10207  -0.47194 0.08404  76  PRO A N   
292  C CA  . PRO A 40  ? 1.61797 1.78476 1.80685 0.12267  -0.51327 0.13357  76  PRO A CA  
293  C C   . PRO A 40  ? 1.49634 1.69024 1.79295 0.16847  -0.52442 0.15237  76  PRO A C   
294  O O   . PRO A 40  ? 1.49426 1.72323 1.86592 0.17860  -0.50666 0.12625  76  PRO A O   
295  C CB  . PRO A 40  ? 1.57354 1.78983 1.71662 0.08915  -0.56037 0.14502  76  PRO A CB  
296  C CG  . PRO A 40  ? 1.63270 1.84966 1.72536 0.04639  -0.53354 0.09954  76  PRO A CG  
297  C CD  . PRO A 40  ? 1.60849 1.81705 1.76126 0.05905  -0.48560 0.06221  76  PRO A CD  
298  N N   . ARG A 41  ? 1.45047 1.62491 1.75607 0.19635  -0.55118 0.19874  77  ARG A N   
299  C CA  . ARG A 41  ? 1.43253 1.62210 1.84587 0.24418  -0.55509 0.21706  77  ARG A CA  
300  C C   . ARG A 41  ? 1.36638 1.64556 1.85195 0.24876  -0.59110 0.22660  77  ARG A C   
301  O O   . ARG A 41  ? 1.31891 1.64069 1.88235 0.25732  -0.57102 0.19843  77  ARG A O   
302  C CB  . ARG A 41  ? 1.42697 1.55783 1.82931 0.27291  -0.56281 0.26224  77  ARG A CB  
303  C CG  . ARG A 41  ? 1.38779 1.44424 1.79647 0.29203  -0.51098 0.24485  77  ARG A CG  
304  C CD  . ARG A 41  ? 1.30120 1.37910 1.80296 0.31423  -0.47410 0.20984  77  ARG A CD  
305  N NE  . ARG A 41  ? 1.23476 1.37156 1.81780 0.33641  -0.48150 0.22205  77  ARG A NE  
306  C CZ  . ARG A 41  ? 1.17693 1.38262 1.82029 0.33250  -0.48030 0.19802  77  ARG A CZ  
307  N NH1 . ARG A 41  ? 1.11711 1.33870 1.75357 0.30933  -0.46788 0.15927  77  ARG A NH1 
308  N NH2 . ARG A 41  ? 1.16101 1.42258 1.87240 0.35096  -0.49369 0.21438  77  ARG A NH2 
309  N N   . LYS A 42  ? 1.37886 1.68884 1.82827 0.23697  -0.63423 0.26182  78  LYS A N   
310  C CA  . LYS A 42  ? 1.43750 1.83646 1.94159 0.23463  -0.66267 0.26741  78  LYS A CA  
311  C C   . LYS A 42  ? 1.44833 1.89444 1.90708 0.18401  -0.68311 0.23737  78  LYS A C   
312  O O   . LYS A 42  ? 1.47590 1.91890 1.84064 0.14829  -0.71222 0.24835  78  LYS A O   
313  C CB  . LYS A 42  ? 1.49110 1.90272 1.98530 0.25015  -0.69846 0.31976  78  LYS A CB  
314  C CG  . LYS A 42  ? 1.56696 1.94866 2.13489 0.30330  -0.67686 0.34447  78  LYS A CG  
315  C CD  . LYS A 42  ? 1.48397 1.90641 2.16311 0.32738  -0.64701 0.31557  78  LYS A CD  
316  C CE  . LYS A 42  ? 1.43000 1.95199 2.16397 0.32037  -0.67978 0.31685  78  LYS A CE  
317  N NZ  . LYS A 42  ? 1.41480 1.97880 2.23735 0.32673  -0.64721 0.27716  78  LYS A NZ  
318  N N   . THR A 43  ? 1.38018 1.86743 1.90309 0.17821  -0.66346 0.19699  79  THR A N   
319  C CA  . THR A 43  ? 1.35758 1.88981 1.85233 0.13020  -0.67594 0.16203  79  THR A CA  
320  C C   . THR A 43  ? 1.36103 1.98175 1.94581 0.13155  -0.68305 0.15133  79  THR A C   
321  O O   . THR A 43  ? 1.33833 1.97984 2.01344 0.17103  -0.66865 0.16258  79  THR A O   
322  C CB  . THR A 43  ? 1.40655 1.89008 1.87060 0.11165  -0.62294 0.11225  79  THR A CB  
323  O OG1 . THR A 43  ? 1.46709 1.97019 2.02920 0.13494  -0.58921 0.08767  79  THR A OG1 
324  C CG2 . THR A 43  ? 1.40395 1.79485 1.79511 0.12101  -0.59070 0.11906  79  THR A CG2 
325  N N   . GLU A 44  ? 1.36901 2.03990 1.92530 0.08448  -0.70219 0.12600  80  GLU A N   
326  C CA  . GLU A 44  ? 1.34980 2.10733 1.98682 0.07826  -0.70877 0.11137  80  GLU A CA  
327  C C   . GLU A 44  ? 1.39029 2.14802 2.10915 0.08990  -0.66161 0.07492  80  GLU A C   
328  O O   . GLU A 44  ? 1.38058 2.19514 2.19010 0.10644  -0.65421 0.07396  80  GLU A O   
329  C CB  . GLU A 44  ? 1.31703 2.12177 1.89372 0.01978  -0.73780 0.08898  80  GLU A CB  
330  C CG  . GLU A 44  ? 1.29095 2.19428 1.93779 0.01116  -0.75945 0.08372  80  GLU A CG  
331  C CD  . GLU A 44  ? 1.29171 2.23522 1.86227 -0.04050 -0.79861 0.07233  80  GLU A CD  
332  O OE1 . GLU A 44  ? 1.31376 2.22341 1.80263 -0.08780 -0.78755 0.03707  80  GLU A OE1 
333  O OE2 . GLU A 44  ? 1.26689 2.27063 1.85766 -0.03369 -0.83904 0.09685  80  GLU A OE2 
334  N N   . ALA A 45  ? 1.47225 2.16721 2.15961 0.08195  -0.62818 0.04482  81  ALA A N   
335  C CA  . ALA A 45  ? 1.55796 2.24786 2.30980 0.08925  -0.58011 0.00752  81  ALA A CA  
336  C C   . ALA A 45  ? 1.64828 2.25389 2.37903 0.11975  -0.53419 0.00752  81  ALA A C   
337  O O   . ALA A 45  ? 1.68004 2.21946 2.31991 0.10129  -0.50888 -0.00550 81  ALA A O   
338  C CB  . ALA A 45  ? 1.57216 2.26582 2.28443 0.03858  -0.55917 -0.03829 81  ALA A CB  
339  N N   . PRO A 46  ? 1.78237 2.38624 2.59020 0.16370  -0.51697 0.02045  82  PRO A N   
340  C CA  . PRO A 46  ? 1.67870 2.20664 2.46923 0.18800  -0.47201 0.01487  82  PRO A CA  
341  C C   . PRO A 46  ? 1.58975 2.10860 2.40388 0.17927  -0.41837 -0.02486 82  PRO A C   
342  O O   . PRO A 46  ? 1.54330 2.09931 2.44426 0.19616  -0.40098 -0.03387 82  PRO A O   
343  C CB  . PRO A 46  ? 1.71783 2.24220 2.56264 0.23234  -0.47026 0.04657  82  PRO A CB  
344  C CG  . PRO A 46  ? 1.71485 2.32085 2.63089 0.23232  -0.48626 0.05266  82  PRO A CG  
345  C CD  . PRO A 46  ? 1.65929 2.31617 2.54187 0.18912  -0.52568 0.04491  82  PRO A CD  
346  N N   . GLN A 47  ? 1.50505 1.97323 2.24095 0.15231  -0.38910 -0.04682 83  GLN A N   
347  C CA  . GLN A 47  ? 1.39910 1.85717 2.14892 0.14005  -0.34176 -0.07944 83  GLN A CA  
348  C C   . GLN A 47  ? 1.16142 1.54600 1.86421 0.14952  -0.30085 -0.08406 83  GLN A C   
349  O O   . GLN A 47  ? 1.09555 1.46862 1.80463 0.14001  -0.26269 -0.10586 83  GLN A O   
350  C CB  . GLN A 47  ? 1.42733 1.90037 2.14290 0.09552  -0.34058 -0.10447 83  GLN A CB  
351  C CG  . GLN A 47  ? 1.35595 1.91004 2.13017 0.07817  -0.37137 -0.11072 83  GLN A CG  
352  C CD  . GLN A 47  ? 1.17895 1.74087 1.92998 0.03293  -0.35689 -0.14342 83  GLN A CD  
353  O OE1 . GLN A 47  ? 1.25065 1.76755 1.92182 0.00808  -0.34879 -0.15359 83  GLN A OE1 
354  N NE2 . GLN A 47  ? 1.06656 1.68381 1.89126 0.02155  -0.35000 -0.16129 83  GLN A NE2 
355  N N   . LEU A 48  ? 1.13349 1.46980 1.78997 0.16606  -0.30860 -0.06262 84  LEU A N   
356  C CA  . LEU A 48  ? 1.07654 1.34678 1.68458 0.16977  -0.27324 -0.06750 84  LEU A CA  
357  C C   . LEU A 48  ? 0.98566 1.24688 1.64545 0.19740  -0.24435 -0.07122 84  LEU A C   
358  O O   . LEU A 48  ? 0.93151 1.17184 1.58257 0.19040  -0.20739 -0.08902 84  LEU A O   
359  C CB  . LEU A 48  ? 1.05546 1.27712 1.59282 0.17210  -0.29026 -0.04526 84  LEU A CB  
360  C CG  . LEU A 48  ? 0.98720 1.14596 1.45622 0.16174  -0.26117 -0.05152 84  LEU A CG  
361  C CD1 . LEU A 48  ? 1.04786 1.16952 1.44917 0.15760  -0.28160 -0.03008 84  LEU A CD1 
362  C CD2 . LEU A 48  ? 0.89148 1.02039 1.38127 0.18192  -0.22927 -0.05583 84  LEU A CD2 
363  N N   . ARG A 49  ? 0.85190 1.12726 1.56479 0.22812  -0.26004 -0.05383 85  ARG A N   
364  C CA  . ARG A 49  ? 0.88001 1.14042 1.64023 0.25415  -0.22858 -0.06051 85  ARG A CA  
365  C C   . ARG A 49  ? 0.89051 1.18487 1.69805 0.24515  -0.19533 -0.08823 85  ARG A C   
366  O O   . ARG A 49  ? 0.81071 1.07742 1.61626 0.24884  -0.15671 -0.10320 85  ARG A O   
367  C CB  . ARG A 49  ? 0.73509 1.01182 1.55583 0.28748  -0.24917 -0.03704 85  ARG A CB  
368  C CG  . ARG A 49  ? 0.89788 1.14488 1.74279 0.30718  -0.20682 -0.04419 85  ARG A CG  
369  C CD  . ARG A 49  ? 0.93666 1.23763 1.85560 0.31227  -0.18958 -0.05520 85  ARG A CD  
370  N NE  . ARG A 49  ? 0.95404 1.22621 1.88597 0.32115  -0.14089 -0.07429 85  ARG A NE  
371  C CZ  . ARG A 49  ? 0.92490 1.18478 1.83750 0.30362  -0.10436 -0.10240 85  ARG A CZ  
372  N NH1 . ARG A 49  ? 0.87518 1.14735 1.76051 0.27920  -0.10838 -0.11367 85  ARG A NH1 
373  N NH2 . ARG A 49  ? 0.88740 1.12190 1.80749 0.30975  -0.06243 -0.11945 85  ARG A NH2 
374  N N   . ASP A 50  ? 0.99546 1.34908 1.84138 0.22966  -0.20908 -0.09570 86  ASP A N   
375  C CA  . ASP A 50  ? 0.95062 1.33484 1.83744 0.21658  -0.17631 -0.12070 86  ASP A CA  
376  C C   . ASP A 50  ? 0.90680 1.25515 1.72608 0.18721  -0.15034 -0.13469 86  ASP A C   
377  O O   . ASP A 50  ? 0.91255 1.26116 1.74454 0.17927  -0.11409 -0.15084 86  ASP A O   
378  C CB  . ASP A 50  ? 0.97825 1.43730 1.92993 0.20650  -0.19913 -0.12406 86  ASP A CB  
379  C CG  . ASP A 50  ? 0.98372 1.47170 1.97852 0.22957  -0.22281 -0.10110 86  ASP A CG  
380  O OD1 . ASP A 50  ? 0.96808 1.43306 1.98056 0.25450  -0.20031 -0.09531 86  ASP A OD1 
381  O OD2 . ASP A 50  ? 1.14003 1.67405 2.15014 0.22147  -0.26374 -0.08878 86  ASP A OD2 
382  N N   . GLU A 51  ? 0.75318 1.07096 1.50245 0.17077  -0.16706 -0.12734 87  GLU A N   
383  C CA  . GLU A 51  ? 0.83218 1.11428 1.52572 0.14710  -0.14224 -0.13711 87  GLU A CA  
384  C C   . GLU A 51  ? 0.78969 1.02207 1.44807 0.15691  -0.11522 -0.13506 87  GLU A C   
385  O O   . GLU A 51  ? 0.65158 0.87198 1.29750 0.14422  -0.08553 -0.14405 87  GLU A O   
386  C CB  . GLU A 51  ? 0.80752 1.07081 1.44207 0.12774  -0.16331 -0.13231 87  GLU A CB  
387  C CG  . GLU A 51  ? 0.84321 1.05914 1.42113 0.11251  -0.13865 -0.13590 87  GLU A CG  
388  C CD  . GLU A 51  ? 0.92718 1.13392 1.46446 0.08772  -0.14837 -0.14060 87  GLU A CD  
389  O OE1 . GLU A 51  ? 1.04632 1.25033 1.55364 0.08663  -0.17613 -0.13226 87  GLU A OE1 
390  O OE2 . GLU A 51  ? 0.92182 1.12257 1.45715 0.06820  -0.12640 -0.15265 87  GLU A OE2 
391  N N   . TYR A 52  ? 0.83065 1.03319 1.47052 0.17704  -0.12606 -0.12194 88  TYR A N   
392  C CA  . TYR A 52  ? 0.73992 0.89809 1.35016 0.18401  -0.10067 -0.12327 88  TYR A CA  
393  C C   . TYR A 52  ? 0.71504 0.88998 1.36754 0.18804  -0.06788 -0.13954 88  TYR A C   
394  O O   . TYR A 52  ? 0.65635 0.80892 1.27701 0.17604  -0.04058 -0.14700 88  TYR A O   
395  C CB  . TYR A 52  ? 0.74470 0.87049 1.34263 0.20603  -0.11604 -0.10826 88  TYR A CB  
396  C CG  . TYR A 52  ? 0.80550 0.89062 1.38825 0.21438  -0.08814 -0.11473 88  TYR A CG  
397  C CD1 . TYR A 52  ? 0.89979 0.94343 1.41839 0.19875  -0.07605 -0.11480 88  TYR A CD1 
398  C CD2 . TYR A 52  ? 0.81879 0.90871 1.45436 0.23621  -0.07256 -0.12259 88  TYR A CD2 
399  C CE1 . TYR A 52  ? 0.98543 0.99452 1.48626 0.20102  -0.05208 -0.12311 88  TYR A CE1 
400  C CE2 . TYR A 52  ? 0.86855 0.91825 1.48575 0.23935  -0.04385 -0.13365 88  TYR A CE2 
401  C CZ  . TYR A 52  ? 0.95388 0.96376 1.50028 0.21988  -0.03513 -0.13418 88  TYR A CZ  
402  O OH  . TYR A 52  ? 1.08728 1.05954 1.61147 0.21786  -0.00808 -0.14741 88  TYR A OH  
403  N N   . ARG A 53  ? 0.70771 0.92539 1.43270 0.20315  -0.07002 -0.14464 89  ARG A N   
404  C CA  . ARG A 53  ? 0.63310 0.87036 1.40182 0.20485  -0.03431 -0.16308 89  ARG A CA  
405  C C   . ARG A 53  ? 0.67345 0.92839 1.43216 0.17644  -0.01432 -0.17329 89  ARG A C   
406  O O   . ARG A 53  ? 0.70949 0.95673 1.45910 0.16716  0.02028  -0.18492 89  ARG A O   
407  C CB  . ARG A 53  ? 0.73951 1.02407 1.59567 0.22663  -0.04101 -0.16477 89  ARG A CB  
408  C CG  . ARG A 53  ? 0.79806 1.08985 1.68413 0.22807  0.00097  -0.18194 89  ARG A CG  
409  C CD  . ARG A 53  ? 0.89716 1.21743 1.84498 0.24912  -0.00536 -0.17501 89  ARG A CD  
410  N NE  . ARG A 53  ? 0.93083 1.24502 1.90124 0.25378  0.03784  -0.19289 89  ARG A NE  
411  C CZ  . ARG A 53  ? 0.94977 1.27947 1.97492 0.27434  0.04356  -0.19053 89  ARG A CZ  
412  N NH1 . ARG A 53  ? 0.98358 1.33916 2.04861 0.29354  0.00692  -0.16765 89  ARG A NH1 
413  N NH2 . ARG A 53  ? 0.86177 1.18191 1.90251 0.27510  0.08750  -0.21139 89  ARG A NH2 
414  N N   . THR A 54  ? 0.72791 1.00362 1.48501 0.16031  -0.03430 -0.16894 90  THR A N   
415  C CA  . THR A 54  ? 0.66178 0.94793 1.41276 0.13351  -0.01435 -0.17633 90  THR A CA  
416  C C   . THR A 54  ? 0.62256 0.86157 1.30426 0.11988  0.00283  -0.17000 90  THR A C   
417  O O   . THR A 54  ? 0.60629 0.84520 1.28183 0.10494  0.03113  -0.17384 90  THR A O   
418  C CB  . THR A 54  ? 0.58591 0.89758 1.34880 0.11770  -0.03810 -0.17593 90  THR A CB  
419  O OG1 . THR A 54  ? 0.52334 0.88469 1.34984 0.12992  -0.06136 -0.17821 90  THR A OG1 
420  C CG2 . THR A 54  ? 0.53928 0.86268 1.31142 0.09116  -0.01376 -0.18464 90  THR A CG2 
421  N N   . TYR A 55  ? 0.63140 0.83274 1.26176 0.12370  -0.01447 -0.15821 91  TYR A N   
422  C CA  . TYR A 55  ? 0.66769 0.83065 1.24049 0.11243  -0.00084 -0.15034 91  TYR A CA  
423  C C   . TYR A 55  ? 0.66154 0.81126 1.22153 0.11634  0.02304  -0.15593 91  TYR A C   
424  O O   . TYR A 55  ? 0.70258 0.83972 1.22908 0.10032  0.04120  -0.15202 91  TYR A O   
425  C CB  . TYR A 55  ? 0.58151 0.71101 1.10884 0.11535  -0.02253 -0.13841 91  TYR A CB  
426  C CG  . TYR A 55  ? 0.65245 0.78485 1.17359 0.10261  -0.03690 -0.13532 91  TYR A CG  
427  C CD1 . TYR A 55  ? 0.63985 0.77069 1.15775 0.08386  -0.02172 -0.13412 91  TYR A CD1 
428  C CD2 . TYR A 55  ? 0.58650 0.72007 1.10263 0.10782  -0.06399 -0.13329 91  TYR A CD2 
429  C CE1 . TYR A 55  ? 0.62871 0.75678 1.14311 0.07107  -0.02919 -0.13592 91  TYR A CE1 
430  C CE2 . TYR A 55  ? 0.65191 0.78606 1.15607 0.09173  -0.07323 -0.13551 91  TYR A CE2 
431  C CZ  . TYR A 55  ? 0.65019 0.78022 1.15547 0.07359  -0.05378 -0.13924 91  TYR A CZ  
432  O OH  . TYR A 55  ? 0.64095 0.76646 1.13661 0.05661  -0.05768 -0.14587 91  TYR A OH  
433  N N   . LYS A 56  ? 0.71033 0.86249 1.29693 0.13627  0.02389  -0.16475 92  LYS A N   
434  C CA  . LYS A 56  ? 0.69739 0.83429 1.27236 0.13737  0.05195  -0.17662 92  LYS A CA  
435  C C   . LYS A 56  ? 0.73410 0.90026 1.33374 0.12368  0.08357  -0.18968 92  LYS A C   
436  O O   . LYS A 56  ? 0.76391 0.91630 1.32581 0.10800  0.10892  -0.19514 92  LYS A O   
437  C CB  . LYS A 56  ? 0.81068 0.93826 1.41709 0.16419  0.04879  -0.18373 92  LYS A CB  
438  C CG  . LYS A 56  ? 0.89916 0.97611 1.45424 0.16731  0.04868  -0.18151 92  LYS A CG  
439  C CD  . LYS A 56  ? 0.82907 0.88341 1.33910 0.16255  0.01913  -0.16141 92  LYS A CD  
440  C CE  . LYS A 56  ? 0.90378 0.91081 1.35982 0.15824  0.02292  -0.16017 92  LYS A CE  
441  N NZ  . LYS A 56  ? 1.00778 1.00857 1.42343 0.13433  0.04730  -0.16883 92  LYS A NZ  
442  N N   . HIS A 57  ? 0.74117 0.94955 1.40159 0.12621  0.08260  -0.19476 93  HIS A N   
443  C CA  . HIS A 57  ? 0.75155 0.98877 1.43667 0.11003  0.11462  -0.20627 93  HIS A CA  
444  C C   . HIS A 57  ? 0.77105 0.99636 1.40672 0.08208  0.12230  -0.19276 93  HIS A C   
445  O O   . HIS A 57  ? 0.81172 1.03288 1.41935 0.06436  0.15099  -0.19540 93  HIS A O   
446  C CB  . HIS A 57  ? 0.76609 1.05464 1.53192 0.11659  0.10889  -0.21370 93  HIS A CB  
447  C CG  . HIS A 57  ? 0.80831 1.12976 1.60982 0.10099  0.14536  -0.22802 93  HIS A CG  
448  N ND1 . HIS A 57  ? 0.87757 1.18203 1.63589 0.08222  0.18127  -0.23324 93  HIS A ND1 
449  C CD2 . HIS A 57  ? 0.72354 1.09601 1.59864 0.09855  0.15184  -0.23798 93  HIS A CD2 
450  C CE1 . HIS A 57  ? 0.78636 1.12657 1.58723 0.06908  0.21078  -0.24551 93  HIS A CE1 
451  N NE2 . HIS A 57  ? 0.78788 1.17044 1.66362 0.07911  0.19432  -0.24930 93  HIS A NE2 
452  N N   . LEU A 58  ? 0.74240 0.96097 1.36655 0.07725  0.09780  -0.17729 94  LEU A N   
453  C CA  . LEU A 58  ? 0.78287 0.98664 1.37019 0.05528  0.10302  -0.16042 94  LEU A CA  
454  C C   . LEU A 58  ? 0.76563 0.93235 1.28760 0.05170  0.09810  -0.14529 94  LEU A C   
455  O O   . LEU A 58  ? 0.70402 0.85672 1.20048 0.03917  0.09432  -0.12593 94  LEU A O   
456  C CB  . LEU A 58  ? 0.74346 0.95262 1.35146 0.05133  0.08360  -0.15423 94  LEU A CB  
457  C CG  . LEU A 58  ? 0.72061 0.97116 1.39326 0.04815  0.08514  -0.16872 94  LEU A CG  
458  C CD1 . LEU A 58  ? 0.62468 0.87692 1.30836 0.04521  0.05965  -0.16820 94  LEU A CD1 
459  C CD2 . LEU A 58  ? 0.58796 0.85256 1.27573 0.02618  0.11624  -0.16880 94  LEU A CD2 
460  N N   . GLN A 59  ? 0.84757 0.99885 1.34730 0.06206  0.09869  -0.15365 95  GLN A N   
461  C CA  . GLN A 59  ? 0.81689 0.93724 1.25698 0.05581  0.09263  -0.14169 95  GLN A CA  
462  C C   . GLN A 59  ? 0.85479 0.97612 1.25676 0.03084  0.11126  -0.13006 95  GLN A C   
463  O O   . GLN A 59  ? 0.91987 1.05764 1.32770 0.01967  0.13722  -0.14032 95  GLN A O   
464  C CB  . GLN A 59  ? 0.91017 1.01198 1.33730 0.06861  0.09434  -0.15734 95  GLN A CB  
465  C CG  . GLN A 59  ? 0.90886 0.97998 1.27761 0.06051  0.08568  -0.14799 95  GLN A CG  
466  C CD  . GLN A 59  ? 0.94332 0.99085 1.31172 0.07884  0.06281  -0.14663 95  GLN A CD  
467  O OE1 . GLN A 59  ? 0.85824 0.91050 1.25053 0.09009  0.04321  -0.13871 95  GLN A OE1 
468  N NE2 . GLN A 59  ? 0.90699 0.92729 1.24488 0.07895  0.06661  -0.15522 95  GLN A NE2 
469  N N   . GLY A 60  ? 0.82949 0.93537 1.19353 0.02132  0.09780  -0.10668 96  GLY A N   
470  C CA  . GLY A 60  ? 0.93694 1.04571 1.26343 -0.00220 0.10764  -0.08683 96  GLY A CA  
471  C C   . GLY A 60  ? 0.89172 1.01052 1.24076 -0.01118 0.11175  -0.06534 96  GLY A C   
472  O O   . GLY A 60  ? 0.93782 1.05525 1.25854 -0.02754 0.11182  -0.03774 96  GLY A O   
473  N N   . CYS A 61  ? 0.81025 0.93923 1.21070 -0.00225 0.11449  -0.07588 97  CYS A N   
474  C CA  . CYS A 61  ? 0.88236 1.01495 1.30793 -0.01227 0.12116  -0.05855 97  CYS A CA  
475  C C   . CYS A 61  ? 0.82496 0.93738 1.24942 -0.00767 0.10266  -0.03545 97  CYS A C   
476  O O   . CYS A 61  ? 0.73536 0.83768 1.16487 0.00699  0.08491  -0.04387 97  CYS A O   
477  C CB  . CYS A 61  ? 0.77622 0.92743 1.25821 -0.00741 0.12818  -0.08045 97  CYS A CB  
478  S SG  . CYS A 61  ? 0.95578 1.13765 1.45871 -0.01162 0.15527  -0.10760 97  CYS A SG  
479  N N   . ASP A 62  ? 0.88908 0.99507 1.30865 -0.02023 0.10848  -0.00495 98  ASP A N   
480  C CA  . ASP A 62  ? 0.83084 0.91820 1.26076 -0.01448 0.09591  0.01834  98  ASP A CA  
481  C C   . ASP A 62  ? 0.78055 0.85919 1.25703 -0.00763 0.09792  0.00277  98  ASP A C   
482  O O   . ASP A 62  ? 0.57581 0.66169 1.08151 -0.01594 0.11323  -0.00772 98  ASP A O   
483  C CB  . ASP A 62  ? 0.95263 1.03596 1.37423 -0.02781 0.10198  0.05910  98  ASP A CB  
484  C CG  . ASP A 62  ? 1.02729 1.12036 1.39587 -0.03740 0.09226  0.07864  98  ASP A CG  
485  O OD1 . ASP A 62  ? 1.02390 1.11562 1.37389 -0.02938 0.07410  0.07546  98  ASP A OD1 
486  O OD2 . ASP A 62  ? 1.13058 1.23321 1.47300 -0.05609 0.10330  0.09624  98  ASP A OD2 
487  N N   . GLY A 63  ? 0.74550 0.80941 1.22679 0.00417  0.08386  -0.00033 99  GLY A N   
488  C CA  . GLY A 63  ? 0.63819 0.69280 1.15204 0.00725  0.08465  -0.01972 99  GLY A CA  
489  C C   . GLY A 63  ? 0.63505 0.70095 1.14566 0.01545  0.07111  -0.05109 99  GLY A C   
490  O O   . GLY A 63  ? 0.59802 0.65681 1.12306 0.01626  0.06620  -0.06689 99  GLY A O   
491  N N   . ILE A 64  ? 0.61444 0.69660 1.10659 0.02058  0.06573  -0.05989 100 ILE A N   
492  C CA  . ILE A 64  ? 0.65342 0.74588 1.14687 0.03193  0.05105  -0.08346 100 ILE A CA  
493  C C   . ILE A 64  ? 0.67987 0.75606 1.13590 0.04272  0.03624  -0.07826 100 ILE A C   
494  O O   . ILE A 64  ? 0.50975 0.58311 0.93898 0.04087  0.03986  -0.06735 100 ILE A O   
495  C CB  . ILE A 64  ? 0.71888 0.83870 1.22973 0.03275  0.05920  -0.09846 100 ILE A CB  
496  C CG1 . ILE A 64  ? 0.68924 0.82599 1.23574 0.01751  0.07851  -0.10061 100 ILE A CG1 
497  C CG2 . ILE A 64  ? 0.59513 0.72856 1.12166 0.04703  0.04164  -0.11813 100 ILE A CG2 
498  C CD1 . ILE A 64  ? 0.49614 0.64350 1.08044 0.01279  0.07240  -0.11664 100 ILE A CD1 
499  N N   . PRO A 65  ? 0.64137 0.70657 1.09091 0.05045  0.02044  -0.08583 101 PRO A N   
500  C CA  . PRO A 65  ? 0.63592 0.68303 1.05057 0.05813  0.00876  -0.08000 101 PRO A CA  
501  C C   . PRO A 65  ? 0.67107 0.72208 1.07338 0.06766  0.00432  -0.08930 101 PRO A C   
502  O O   . PRO A 65  ? 0.67283 0.74100 1.09924 0.07421  0.00370  -0.10322 101 PRO A O   
503  C CB  . PRO A 65  ? 0.61722 0.65234 1.02897 0.06062  -0.00353 -0.08730 101 PRO A CB  
504  C CG  . PRO A 65  ? 0.63239 0.68712 1.07383 0.05776  -0.00573 -0.10345 101 PRO A CG  
505  C CD  . PRO A 65  ? 0.64549 0.71468 1.11509 0.04853  0.01302  -0.10061 101 PRO A CD  
506  N N   . ASN A 66  ? 0.67398 0.70938 1.04315 0.06789  0.00247  -0.08211 102 ASN A N   
507  C CA  . ASN A 66  ? 0.69855 0.72866 1.05415 0.07540  0.00283  -0.09295 102 ASN A CA  
508  C C   . ASN A 66  ? 0.68380 0.70197 1.04220 0.09082  -0.01347 -0.10053 102 ASN A C   
509  O O   . ASN A 66  ? 0.63974 0.64343 0.98397 0.09110  -0.02601 -0.09402 102 ASN A O   
510  C CB  . ASN A 66  ? 0.67887 0.69434 0.99499 0.06592  0.00559  -0.08495 102 ASN A CB  
511  C CG  . ASN A 66  ? 0.74243 0.77317 1.04862 0.04964  0.02035  -0.07753 102 ASN A CG  
512  O OD1 . ASN A 66  ? 0.82681 0.87378 1.14976 0.04750  0.03468  -0.08611 102 ASN A OD1 
513  N ND2 . ASN A 66  ? 0.72620 0.75456 1.00533 0.03658  0.01635  -0.05988 102 ASN A ND2 
514  N N   . ALA A 67  ? 0.63027 0.65483 1.00860 0.10348  -0.01209 -0.11286 103 ALA A N   
515  C CA  . ALA A 67  ? 0.66695 0.67881 1.04930 0.12034  -0.02897 -0.11446 103 ALA A CA  
516  C C   . ALA A 67  ? 0.78812 0.76625 1.13905 0.12363  -0.02518 -0.11489 103 ALA A C   
517  O O   . ALA A 67  ? 0.82411 0.79886 1.17174 0.12068  -0.00664 -0.12514 103 ALA A O   
518  C CB  . ALA A 67  ? 0.68239 0.72085 1.11487 0.13536  -0.03049 -0.12441 103 ALA A CB  
519  N N   . TYR A 68  ? 0.69707 0.64878 1.02256 0.12675  -0.04047 -0.10561 104 TYR A N   
520  C CA  . TYR A 68  ? 0.74493 0.66049 1.03882 0.12597  -0.03650 -0.10564 104 TYR A CA  
521  C C   . TYR A 68  ? 0.79359 0.68466 1.09698 0.14587  -0.04531 -0.10464 104 TYR A C   
522  O O   . TYR A 68  ? 0.84206 0.70323 1.13425 0.14801  -0.03368 -0.11161 104 TYR A O   
523  C CB  . TYR A 68  ? 0.74398 0.64340 1.00015 0.11115  -0.04268 -0.09391 104 TYR A CB  
524  C CG  . TYR A 68  ? 0.73599 0.65605 0.98737 0.09370  -0.03416 -0.08992 104 TYR A CG  
525  C CD1 . TYR A 68  ? 0.76582 0.68863 1.00245 0.08076  -0.02119 -0.09352 104 TYR A CD1 
526  C CD2 . TYR A 68  ? 0.66836 0.60441 0.93023 0.08913  -0.03871 -0.08179 104 TYR A CD2 
527  C CE1 . TYR A 68  ? 0.81724 0.76122 1.05103 0.06561  -0.01728 -0.08319 104 TYR A CE1 
528  C CE2 . TYR A 68  ? 0.73911 0.69146 1.00462 0.07638  -0.03072 -0.07363 104 TYR A CE2 
529  C CZ  . TYR A 68  ? 0.74809 0.70592 1.00034 0.06564  -0.02214 -0.07140 104 TYR A CZ  
530  O OH  . TYR A 68  ? 0.79845 0.77470 1.05547 0.05361  -0.01799 -0.05681 104 TYR A OH  
531  N N   . TYR A 69  ? 0.72659 0.62861 1.05026 0.15919  -0.06570 -0.09532 105 TYR A N   
532  C CA  . TYR A 69  ? 0.91418 0.79114 1.24517 0.17867  -0.07862 -0.08592 105 TYR A CA  
533  C C   . TYR A 69  ? 0.88779 0.79571 1.25399 0.19285  -0.10304 -0.07594 105 TYR A C   
534  O O   . TYR A 69  ? 0.87187 0.80660 1.23257 0.18111  -0.11507 -0.07375 105 TYR A O   
535  C CB  . TYR A 69  ? 0.90631 0.74141 1.18693 0.17034  -0.08619 -0.07277 105 TYR A CB  
536  C CG  . TYR A 69  ? 1.00468 0.81129 1.28685 0.18856  -0.10349 -0.05545 105 TYR A CG  
537  C CD1 . TYR A 69  ? 0.94690 0.71800 1.24381 0.20397  -0.09236 -0.05727 105 TYR A CD1 
538  C CD2 . TYR A 69  ? 1.04329 0.85574 1.30967 0.18857  -0.12993 -0.03644 105 TYR A CD2 
539  C CE1 . TYR A 69  ? 1.08805 0.82920 1.39020 0.22245  -0.10846 -0.03613 105 TYR A CE1 
540  C CE2 . TYR A 69  ? 1.00423 0.79112 1.26817 0.20414  -0.14879 -0.01445 105 TYR A CE2 
541  C CZ  . TYR A 69  ? 1.05449 0.80504 1.33915 0.22273  -0.13864 -0.01206 105 TYR A CZ  
542  O OH  . TYR A 69  ? 1.16426 0.88557 1.45042 0.24014  -0.15768 0.01490  105 TYR A OH  
543  N N   . PHE A 70  ? 0.88011 0.78464 1.28539 0.21732  -0.10982 -0.07022 106 PHE A N   
544  C CA  . PHE A 70  ? 0.95664 0.89004 1.39588 0.23256  -0.14009 -0.05396 106 PHE A CA  
545  C C   . PHE A 70  ? 0.96970 0.86584 1.41316 0.25471  -0.15311 -0.03290 106 PHE A C   
546  O O   . PHE A 70  ? 1.00974 0.87974 1.48079 0.27146  -0.13315 -0.03948 106 PHE A O   
547  C CB  . PHE A 70  ? 0.87990 0.86598 1.39042 0.24381  -0.13627 -0.06582 106 PHE A CB  
548  C CG  . PHE A 70  ? 0.88482 0.90803 1.44073 0.26061  -0.17071 -0.04741 106 PHE A CG  
549  C CD1 . PHE A 70  ? 0.89086 0.93664 1.41932 0.24528  -0.20167 -0.03531 106 PHE A CD1 
550  C CD2 . PHE A 70  ? 0.81329 0.85076 1.44144 0.29064  -0.17175 -0.04250 106 PHE A CD2 
551  C CE1 . PHE A 70  ? 0.92951 1.01509 1.49588 0.25687  -0.23771 -0.01682 106 PHE A CE1 
552  C CE2 . PHE A 70  ? 0.87248 0.95119 1.54881 0.30666  -0.20775 -0.02122 106 PHE A CE2 
553  C CZ  . PHE A 70  ? 0.90562 1.01033 1.54826 0.28844  -0.24312 -0.00743 106 PHE A CZ  
554  N N   . GLY A 71  ? 1.05936 0.95015 1.47335 0.25307  -0.18454 -0.00775 107 GLY A N   
555  C CA  . GLY A 71  ? 1.19087 1.03867 1.59616 0.27022  -0.19845 0.01879  107 GLY A CA  
556  C C   . GLY A 71  ? 1.39337 1.26768 1.80839 0.27969  -0.24139 0.04992  107 GLY A C   
557  O O   . GLY A 71  ? 1.32976 1.25958 1.76105 0.27173  -0.26071 0.04735  107 GLY A O   
558  N N   . GLN A 72  ? 1.69052 1.52323 2.09344 0.29467  -0.25666 0.08066  108 GLN A N   
559  C CA  . GLN A 72  ? 1.73049 1.58385 2.14480 0.30751  -0.30093 0.11877  108 GLN A CA  
560  C C   . GLN A 72  ? 1.77889 1.58176 2.11593 0.29529  -0.31682 0.14923  108 GLN A C   
561  O O   . GLN A 72  ? 1.96994 1.76606 2.31469 0.31208  -0.34900 0.18935  108 GLN A O   
562  C CB  . GLN A 72  ? 1.82798 1.68802 2.33063 0.34789  -0.30590 0.13558  108 GLN A CB  
563  C CG  . GLN A 72  ? 1.80395 1.70663 2.37654 0.35692  -0.27483 0.10282  108 GLN A CG  
564  C CD  . GLN A 72  ? 1.94993 1.84648 2.57924 0.38568  -0.25565 0.11182  108 GLN A CD  
565  O OE1 . GLN A 72  ? 2.08700 1.92691 2.69925 0.39789  -0.24780 0.13023  108 GLN A OE1 
566  N NE2 . GLN A 72  ? 1.98458 1.93769 2.68259 0.39631  -0.24689 0.09819  108 GLN A NE2 
567  N N   . GLU A 73  ? 1.67297 1.44200 1.93838 0.26615  -0.29485 0.13321  109 GLU A N   
568  C CA  . GLU A 73  ? 1.68968 1.40498 1.88245 0.25236  -0.30063 0.15817  109 GLU A CA  
569  C C   . GLU A 73  ? 1.71966 1.46023 1.87142 0.24049  -0.34309 0.18927  109 GLU A C   
570  O O   . GLU A 73  ? 1.70833 1.49247 1.83371 0.21597  -0.35193 0.17388  109 GLU A O   
571  C CB  . GLU A 73  ? 1.63023 1.31956 1.76430 0.22104  -0.26824 0.13115  109 GLU A CB  
572  C CG  . GLU A 73  ? 1.54449 1.20855 1.70632 0.22647  -0.22971 0.10299  109 GLU A CG  
573  C CD  . GLU A 73  ? 1.40955 1.04394 1.51497 0.19699  -0.20356 0.08660  109 GLU A CD  
574  O OE1 . GLU A 73  ? 1.40932 1.03948 1.45753 0.17428  -0.21145 0.09624  109 GLU A OE1 
575  O OE2 . GLU A 73  ? 1.46449 1.08220 1.58364 0.19503  -0.17473 0.06370  109 GLU A OE2 
576  N N   . GLY A 74  ? 1.75476 1.46589 1.89957 0.25627  -0.36875 0.23353  110 GLY A N   
577  C CA  . GLY A 74  ? 1.77606 1.50917 1.87378 0.24302  -0.41271 0.26900  110 GLY A CA  
578  C C   . GLY A 74  ? 1.68641 1.49938 1.83894 0.25217  -0.44872 0.27239  110 GLY A C   
579  O O   . GLY A 74  ? 1.60816 1.45088 1.85282 0.28289  -0.44755 0.26583  110 GLY A O   
580  N N   . LEU A 75  ? 1.68418 1.53378 1.77853 0.22202  -0.47949 0.28064  111 LEU A N   
581  C CA  . LEU A 75  ? 1.65912 1.58966 1.79425 0.22040  -0.51561 0.28026  111 LEU A CA  
582  C C   . LEU A 75  ? 1.62984 1.60077 1.77766 0.19886  -0.48979 0.22610  111 LEU A C   
583  O O   . LEU A 75  ? 1.60657 1.63985 1.75955 0.18089  -0.51531 0.21781  111 LEU A O   
584  C CB  . LEU A 75  ? 1.73510 1.68743 1.79772 0.19425  -0.56422 0.31574  111 LEU A CB  
585  C CG  . LEU A 75  ? 1.79768 1.74798 1.75164 0.14120  -0.55783 0.29374  111 LEU A CG  
586  C CD1 . LEU A 75  ? 1.74010 1.71997 1.63204 0.11866  -0.61263 0.33397  111 LEU A CD1 
587  C CD2 . LEU A 75  ? 1.80167 1.67605 1.68628 0.12583  -0.51361 0.28163  111 LEU A CD2 
588  N N   . HIS A 76  ? 1.61353 1.55090 1.76845 0.19941  -0.44092 0.19080  112 HIS A N   
589  C CA  . HIS A 76  ? 1.57008 1.53701 1.73634 0.18032  -0.41344 0.14407  112 HIS A CA  
590  C C   . HIS A 76  ? 1.47960 1.44488 1.72260 0.20651  -0.38061 0.12150  112 HIS A C   
591  O O   . HIS A 76  ? 1.47330 1.39066 1.72851 0.22726  -0.36095 0.12853  112 HIS A O   
592  C CB  . HIS A 76  ? 1.54473 1.47506 1.62848 0.14530  -0.38410 0.12177  112 HIS A CB  
593  C CG  . HIS A 76  ? 1.60062 1.55083 1.61399 0.10825  -0.40488 0.12190  112 HIS A CG  
594  N ND1 . HIS A 76  ? 1.62727 1.63673 1.65614 0.09056  -0.42159 0.10376  112 HIS A ND1 
595  C CD2 . HIS A 76  ? 1.65232 1.56999 1.57630 0.08180  -0.40855 0.13489  112 HIS A CD2 
596  C CE1 . HIS A 76  ? 1.67432 1.68610 1.62410 0.05405  -0.43504 0.10384  112 HIS A CE1 
597  N NE2 . HIS A 76  ? 1.72123 1.67819 1.60529 0.04830  -0.42672 0.12288  112 HIS A NE2 
598  N N   . ASN A 77  ? 1.42327 1.43963 1.71444 0.20220  -0.37317 0.09319  113 ASN A N   
599  C CA  . ASN A 77  ? 1.32436 1.34088 1.67110 0.21596  -0.33603 0.06535  113 ASN A CA  
600  C C   . ASN A 77  ? 1.26532 1.26311 1.56710 0.18838  -0.30151 0.03446  113 ASN A C   
601  O O   . ASN A 77  ? 1.28310 1.29803 1.54700 0.15990  -0.30590 0.02282  113 ASN A O   
602  C CB  . ASN A 77  ? 1.26743 1.35050 1.69766 0.22717  -0.34503 0.05468  113 ASN A CB  
603  C CG  . ASN A 77  ? 1.24974 1.35169 1.75138 0.26347  -0.36922 0.08272  113 ASN A CG  
604  O OD1 . ASN A 77  ? 1.15743 1.32188 1.72887 0.27280  -0.38823 0.08353  113 ASN A OD1 
605  N ND2 . ASN A 77  ? 1.33672 1.38459 1.82610 0.28417  -0.36797 0.10684  113 ASN A ND2 
606  N N   . ILE A 78  ? 1.23083 1.19397 1.53916 0.19623  -0.26691 0.02128  114 ILE A N   
607  C CA  . ILE A 78  ? 1.14528 1.08502 1.41201 0.17376  -0.23647 0.00053  114 ILE A CA  
608  C C   . ILE A 78  ? 1.04466 1.00244 1.35710 0.17732  -0.20803 -0.02397 114 ILE A C   
609  O O   . ILE A 78  ? 0.97254 0.92978 1.32995 0.19865  -0.19844 -0.02579 114 ILE A O   
610  C CB  . ILE A 78  ? 1.12520 1.00507 1.34335 0.17258  -0.22388 0.01132  114 ILE A CB  
611  C CG1 . ILE A 78  ? 1.20824 1.06871 1.37173 0.16379  -0.24951 0.03679  114 ILE A CG1 
612  C CG2 . ILE A 78  ? 1.03769 0.90164 1.22761 0.15214  -0.19318 -0.00852 114 ILE A CG2 
613  C CD1 . ILE A 78  ? 1.22696 1.02774 1.35071 0.16540  -0.23998 0.05251  114 ILE A CD1 
614  N N   . LEU A 79  ? 0.94129 0.91328 1.24195 0.15555  -0.19273 -0.04241 115 LEU A N   
615  C CA  . LEU A 79  ? 0.89512 0.87897 1.22542 0.15342  -0.16468 -0.06147 115 LEU A CA  
616  C C   . LEU A 79  ? 0.85958 0.81810 1.14904 0.13430  -0.14353 -0.06766 115 LEU A C   
617  O O   . LEU A 79  ? 0.84603 0.80249 1.10521 0.11655  -0.14635 -0.06912 115 LEU A O   
618  C CB  . LEU A 79  ? 0.83314 0.86679 1.20672 0.14719  -0.16719 -0.07461 115 LEU A CB  
619  C CG  . LEU A 79  ? 0.80745 0.85460 1.21144 0.14355  -0.13829 -0.09085 115 LEU A CG  
620  C CD1 . LEU A 79  ? 0.70215 0.73655 1.12684 0.16189  -0.12287 -0.09167 115 LEU A CD1 
621  C CD2 . LEU A 79  ? 0.80146 0.89717 1.25230 0.13699  -0.14146 -0.10241 115 LEU A CD2 
622  N N   . VAL A 80  ? 0.81288 0.75444 1.10360 0.13676  -0.12188 -0.07191 116 VAL A N   
623  C CA  . VAL A 80  ? 0.75759 0.68143 1.01946 0.12075  -0.10405 -0.07394 116 VAL A CA  
624  C C   . VAL A 80  ? 0.73889 0.68442 1.02788 0.11587  -0.08484 -0.08371 116 VAL A C   
625  O O   . VAL A 80  ? 0.73691 0.68656 1.04446 0.12406  -0.07553 -0.08868 116 VAL A O   
626  C CB  . VAL A 80  ? 0.78794 0.67301 1.01910 0.12230  -0.09893 -0.06673 116 VAL A CB  
627  C CG1 . VAL A 80  ? 0.59762 0.47544 0.80980 0.10541  -0.08258 -0.06772 116 VAL A CG1 
628  C CG2 . VAL A 80  ? 0.84959 0.70890 1.04992 0.12519  -0.11658 -0.05311 116 VAL A CG2 
629  N N   . ILE A 81  ? 0.62952 0.58643 0.92027 0.10164  -0.07675 -0.08622 117 ILE A N   
630  C CA  . ILE A 81  ? 0.67296 0.64633 0.98495 0.09473  -0.05900 -0.08901 117 ILE A CA  
631  C C   . ILE A 81  ? 0.56767 0.53054 0.86596 0.08187  -0.04899 -0.08202 117 ILE A C   
632  O O   . ILE A 81  ? 0.55107 0.49568 0.82545 0.07780  -0.05280 -0.07900 117 ILE A O   
633  C CB  . ILE A 81  ? 0.67057 0.67486 1.02039 0.09292  -0.05742 -0.09813 117 ILE A CB  
634  C CG1 . ILE A 81  ? 0.67575 0.68251 1.02258 0.08240  -0.06427 -0.10292 117 ILE A CG1 
635  C CG2 . ILE A 81  ? 0.68088 0.70355 1.05762 0.10723  -0.06588 -0.10429 117 ILE A CG2 
636  C CD1 . ILE A 81  ? 0.81489 0.84610 1.19655 0.07250  -0.05573 -0.11285 117 ILE A CD1 
637  N N   . ASP A 82  ? 0.65149 0.62700 0.96823 0.07551  -0.03507 -0.07779 118 ASP A N   
638  C CA  . ASP A 82  ? 0.57973 0.54962 0.89743 0.06666  -0.02533 -0.06704 118 ASP A CA  
639  C C   . ASP A 82  ? 0.57921 0.54254 0.90324 0.06123  -0.02207 -0.07411 118 ASP A C   
640  O O   . ASP A 82  ? 0.60055 0.57207 0.93551 0.05938  -0.02485 -0.08676 118 ASP A O   
641  C CB  . ASP A 82  ? 0.62154 0.60754 0.96194 0.06175  -0.01336 -0.05646 118 ASP A CB  
642  C CG  . ASP A 82  ? 0.71138 0.70313 1.03505 0.06051  -0.01383 -0.05024 118 ASP A CG  
643  O OD1 . ASP A 82  ? 0.62131 0.60233 0.92008 0.05868  -0.01933 -0.04589 118 ASP A OD1 
644  O OD2 . ASP A 82  ? 0.72391 0.73065 1.05749 0.05841  -0.00671 -0.05171 118 ASP A OD2 
645  N N   . LEU A 83  ? 0.59381 0.48558 1.42989 -0.07406 0.12488  0.01887  119 LEU A N   
646  C CA  . LEU A 83  ? 0.49478 0.40602 1.29489 -0.06605 0.14074  0.05949  119 LEU A CA  
647  C C   . LEU A 83  ? 0.55526 0.49334 1.29462 -0.07235 0.11009  0.03554  119 LEU A C   
648  O O   . LEU A 83  ? 0.63955 0.58464 1.41377 -0.08720 0.08616  0.00156  119 LEU A O   
649  C CB  . LEU A 83  ? 0.58027 0.48834 1.46125 -0.06723 0.16748  0.08598  119 LEU A CB  
650  C CG  . LEU A 83  ? 0.61403 0.53883 1.46367 -0.05538 0.19214  0.13125  119 LEU A CG  
651  C CD1 . LEU A 83  ? 0.70236 0.62489 1.49337 -0.03501 0.21612  0.17357  119 LEU A CD1 
652  C CD2 . LEU A 83  ? 0.70159 0.62877 1.61757 -0.04840 0.21320  0.14804  119 LEU A CD2 
653  N N   . LEU A 84  ? 0.46140 0.41555 1.11437 -0.06044 0.11009  0.05288  120 LEU A N   
654  C CA  . LEU A 84  ? 0.61251 0.58925 1.20644 -0.06394 0.08539  0.03525  120 LEU A CA  
655  C C   . LEU A 84  ? 0.62591 0.61776 1.20491 -0.05892 0.10202  0.06517  120 LEU A C   
656  O O   . LEU A 84  ? 0.58856 0.57540 1.19568 -0.05134 0.13278  0.09975  120 LEU A O   
657  C CB  . LEU A 84  ? 0.58420 0.56627 1.09718 -0.05587 0.07118  0.02463  120 LEU A CB  
658  C CG  . LEU A 84  ? 0.55807 0.52650 1.07895 -0.05871 0.05621  -0.00770 120 LEU A CG  
659  C CD1 . LEU A 84  ? 0.46809 0.44209 0.91634 -0.04825 0.05046  -0.00982 120 LEU A CD1 
660  C CD2 . LEU A 84  ? 0.56073 0.53539 1.10208 -0.07193 0.02733  -0.04824 120 LEU A CD2 
661  N N   . GLY A 85  ? 0.55686 0.56703 1.09131 -0.06146 0.08357  0.05249  121 GLY A N   
662  C CA  . GLY A 85  ? 0.48742 0.51135 1.00693 -0.05694 0.09731  0.07346  121 GLY A CA  
663  C C   . GLY A 85  ? 0.52913 0.55995 0.97309 -0.04230 0.10839  0.09213  121 GLY A C   
664  O O   . GLY A 85  ? 0.58443 0.60971 0.99938 -0.03359 0.11231  0.09943  121 GLY A O   
665  N N   . PRO A 86  ? 0.44633 0.49079 0.86100 -0.03895 0.11258  0.09800  122 PRO A N   
666  C CA  . PRO A 86  ? 0.59882 0.65223 0.94572 -0.02535 0.12187  0.11068  122 PRO A CA  
667  C C   . PRO A 86  ? 0.45173 0.50926 0.74514 -0.02617 0.09869  0.09051  122 PRO A C   
668  O O   . PRO A 86  ? 0.44086 0.49664 0.73829 -0.03604 0.07656  0.06746  122 PRO A O   
669  C CB  . PRO A 86  ? 0.55235 0.61668 0.89320 -0.02419 0.13042  0.11353  122 PRO A CB  
670  C CG  . PRO A 86  ? 0.67510 0.73647 1.09082 -0.03386 0.13510  0.11505  122 PRO A CG  
671  C CD  . PRO A 86  ? 0.63515 0.68817 1.08522 -0.04622 0.11134  0.09389  122 PRO A CD  
672  N N   . SER A 87  ? 0.49852 0.56436 0.74178 -0.01423 0.10442  0.10008  123 SER A N   
673  C CA  . SER A 87  ? 0.51957 0.59227 0.71886 -0.01466 0.08564  0.08335  123 SER A CA  
674  C C   . SER A 87  ? 0.55547 0.63652 0.73190 -0.02038 0.07553  0.06711  123 SER A C   
675  O O   . SER A 87  ? 0.50360 0.58696 0.68886 -0.02059 0.08498  0.07052  123 SER A O   
676  C CB  . SER A 87  ? 0.54778 0.63122 0.70931 0.00012  0.09225  0.09758  123 SER A CB  
677  O OG  . SER A 87  ? 0.58499 0.68213 0.71483 0.00900  0.10233  0.10437  123 SER A OG  
678  N N   . LEU A 88  ? 0.50583 0.59077 0.65733 -0.02417 0.05892  0.05092  124 LEU A N   
679  C CA  . LEU A 88  ? 0.53064 0.62175 0.66455 -0.02840 0.05241  0.03840  124 LEU A CA  
680  C C   . LEU A 88  ? 0.54481 0.64600 0.65266 -0.02058 0.06327  0.04121  124 LEU A C   
681  O O   . LEU A 88  ? 0.49335 0.59535 0.60108 -0.02275 0.06656  0.03420  124 LEU A O   
682  C CB  . LEU A 88  ? 0.49660 0.59027 0.61327 -0.03244 0.03751  0.02502  124 LEU A CB  
683  C CG  . LEU A 88  ? 0.46079 0.54724 0.59225 -0.03842 0.02563  0.01719  124 LEU A CG  
684  C CD1 . LEU A 88  ? 0.44037 0.53114 0.55089 -0.03955 0.01711  0.00829  124 LEU A CD1 
685  C CD2 . LEU A 88  ? 0.50290 0.58730 0.65741 -0.04332 0.02234  0.01562  124 LEU A CD2 
686  N N   . GLU A 89  ? 0.51340 0.62354 0.59866 -0.00966 0.06878  0.05072  125 GLU A N   
687  C CA  . GLU A 89  ? 0.53191 0.65533 0.58600 0.00097  0.07810  0.05146  125 GLU A CA  
688  C C   . GLU A 89  ? 0.55466 0.67330 0.62212 0.00584  0.09923  0.06438  125 GLU A C   
689  O O   . GLU A 89  ? 0.59103 0.71502 0.64164 0.00958  0.10680  0.05562  125 GLU A O   
690  C CB  . GLU A 89  ? 0.44686 0.58569 0.47215 0.01529  0.07788  0.06267  125 GLU A CB  
691  C CG  . GLU A 89  ? 0.55572 0.71349 0.53951 0.03048  0.08567  0.06277  125 GLU A CG  
692  C CD  . GLU A 89  ? 0.63487 0.80332 0.59810 0.02495  0.07210  0.03113  125 GLU A CD  
693  O OE1 . GLU A 89  ? 0.62499 0.79050 0.60349 0.01164  0.05598  0.01430  125 GLU A OE1 
694  O OE2 . GLU A 89  ? 0.66298 0.84244 0.59674 0.03468  0.07944  0.02265  125 GLU A OE2 
695  N N   . ASP A 90  ? 0.56381 0.67209 0.66725 0.00567  0.11042  0.08372  126 ASP A N   
696  C CA  . ASP A 90  ? 0.53551 0.64027 0.66393 0.00949  0.13316  0.09850  126 ASP A CA  
697  C C   . ASP A 90  ? 0.54118 0.64171 0.69264 -0.00126 0.12907  0.08311  126 ASP A C   
698  O O   . ASP A 90  ? 0.58980 0.69379 0.73779 0.00462  0.14534  0.08415  126 ASP A O   
699  C CB  . ASP A 90  ? 0.56432 0.65801 0.74271 0.00811  0.14440  0.11986  126 ASP A CB  
700  C CG  . ASP A 90  ? 0.63667 0.73302 0.79989 0.02273  0.15635  0.14362  126 ASP A CG  
701  O OD1 . ASP A 90  ? 0.72699 0.83824 0.84107 0.03930  0.16549  0.15263  126 ASP A OD1 
702  O OD2 . ASP A 90  ? 0.62514 0.70942 0.82667 0.01888  0.15627  0.15271  126 ASP A OD2 
703  N N   . LEU A 91  ? 0.42186 0.51580 0.59741 -0.01485 0.10873  0.07029  127 LEU A N   
704  C CA  . LEU A 91  ? 0.54396 0.63647 0.74144 -0.02256 0.10271  0.05935  127 LEU A CA  
705  C C   . LEU A 91  ? 0.58423 0.68037 0.74789 -0.02034 0.10170  0.04416  127 LEU A C   
706  O O   . LEU A 91  ? 0.47200 0.56689 0.65140 -0.02081 0.10824  0.03995  127 LEU A O   
707  C CB  . LEU A 91  ? 0.54312 0.63184 0.76270 -0.03365 0.07948  0.05009  127 LEU A CB  
708  C CG  . LEU A 91  ? 0.52705 0.61115 0.78659 -0.03773 0.07717  0.05684  127 LEU A CG  
709  C CD1 . LEU A 91  ? 0.57372 0.65628 0.83668 -0.04556 0.05190  0.04145  127 LEU A CD1 
710  C CD2 . LEU A 91  ? 0.49387 0.57993 0.80722 -0.03947 0.08896  0.06643  127 LEU A CD2 
711  N N   . PHE A 92  ? 0.47825 0.57928 0.60245 -0.01795 0.09373  0.03485  128 PHE A N   
712  C CA  . PHE A 92  ? 0.53406 0.63902 0.63316 -0.01719 0.09183  0.01595  128 PHE A CA  
713  C C   . PHE A 92  ? 0.54208 0.65151 0.62556 -0.00614 0.11215  0.01418  128 PHE A C   
714  O O   . PHE A 92  ? 0.58429 0.68959 0.67478 -0.00722 0.11781  0.00048  128 PHE A O   
715  C CB  . PHE A 92  ? 0.47905 0.59308 0.54726 -0.01673 0.07805  0.00636  128 PHE A CB  
716  C CG  . PHE A 92  ? 0.47924 0.59702 0.53597 -0.02033 0.07144  -0.01741 128 PHE A CG  
717  C CD1 . PHE A 92  ? 0.52705 0.63478 0.60908 -0.03060 0.06609  -0.02537 128 PHE A CD1 
718  C CD2 . PHE A 92  ? 0.51402 0.64678 0.53773 -0.01268 0.07005  -0.03183 128 PHE A CD2 
719  C CE1 . PHE A 92  ? 0.46602 0.57437 0.54929 -0.03504 0.06286  -0.04654 128 PHE A CE1 
720  C CE2 . PHE A 92  ? 0.55589 0.69212 0.57904 -0.01807 0.06248  -0.05891 128 PHE A CE2 
721  C CZ  . PHE A 92  ? 0.40475 0.52670 0.46208 -0.03026 0.06044  -0.06585 128 PHE A CZ  
722  N N   . ASP A 93  ? 0.50963 0.62722 0.57178 0.00657  0.12567  0.02921  129 ASP A N   
723  C CA  . ASP A 93  ? 0.61609 0.74025 0.65525 0.02097  0.14829  0.02942  129 ASP A CA  
724  C C   . ASP A 93  ? 0.65211 0.76680 0.73296 0.01960  0.16720  0.03709  129 ASP A C   
725  O O   . ASP A 93  ? 0.71627 0.83162 0.78742 0.02689  0.18275  0.02561  129 ASP A O   
726  C CB  . ASP A 93  ? 0.71078 0.84655 0.72072 0.03790  0.16234  0.05284  129 ASP A CB  
727  C CG  . ASP A 93  ? 0.79299 0.94696 0.74875 0.04725  0.14789  0.04142  129 ASP A CG  
728  O OD1 . ASP A 93  ? 0.86639 1.02595 0.80336 0.04278  0.13276  0.01019  129 ASP A OD1 
729  O OD2 . ASP A 93  ? 0.90208 1.06592 0.83926 0.05962  0.15173  0.06428  129 ASP A OD2 
730  N N   . TRP A 94  ? 0.63691 0.74433 0.76753 0.01095  0.16575  0.05441  130 TRP A N   
731  C CA  . TRP A 94  ? 0.62805 0.73163 0.80742 0.01035  0.18263  0.06430  130 TRP A CA  
732  C C   . TRP A 94  ? 0.52845 0.62639 0.72907 0.00254  0.17313  0.04671  130 TRP A C   
733  O O   . TRP A 94  ? 0.54293 0.63997 0.77329 0.00645  0.19035  0.04945  130 TRP A O   
734  C CB  . TRP A 94  ? 0.53344 0.63453 0.76617 0.00275  0.18008  0.08415  130 TRP A CB  
735  C CG  . TRP A 94  ? 0.69479 0.79789 0.91947 0.01139  0.19509  0.10631  130 TRP A CG  
736  C CD1 . TRP A 94  ? 0.79968 0.90997 0.98071 0.02923  0.21815  0.11821  130 TRP A CD1 
737  C CD2 . TRP A 94  ? 0.73124 0.82918 0.99285 0.00455  0.18896  0.11996  130 TRP A CD2 
738  N NE1 . TRP A 94  ? 0.91074 1.02052 1.10106 0.03500  0.22870  0.14406  130 TRP A NE1 
739  C CE2 . TRP A 94  ? 0.87292 0.97307 1.11661 0.01889  0.21172  0.14414  130 TRP A CE2 
740  C CE3 . TRP A 94  ? 0.73145 0.82365 1.03893 -0.01090 0.16656  0.11277  130 TRP A CE3 
741  C CZ2 . TRP A 94  ? 0.79192 0.88497 1.07066 0.01693  0.21511  0.16274  130 TRP A CZ2 
742  C CZ3 . TRP A 94  ? 0.72601 0.81185 1.06537 -0.01378 0.16780  0.12511  130 TRP A CZ3 
743  C CH2 . TRP A 94  ? 0.67890 0.76333 1.00801 -0.00062 0.19305  0.15057  130 TRP A CH2 
744  N N   . CYS A 95  ? 0.54775 0.64210 0.73734 -0.00694 0.14864  0.03158  131 CYS A N   
745  C CA  . CYS A 95  ? 0.57140 0.65931 0.78052 -0.01257 0.14111  0.01909  131 CYS A CA  
746  C C   . CYS A 95  ? 0.62284 0.70725 0.80233 -0.00828 0.14821  -0.00420 131 CYS A C   
747  O O   . CYS A 95  ? 0.52221 0.59856 0.71689 -0.01372 0.14159  -0.01589 131 CYS A O   
748  C CB  . CYS A 95  ? 0.55050 0.63653 0.76682 -0.02336 0.11471  0.01848  131 CYS A CB  
749  S SG  . CYS A 95  ? 0.46764 0.55851 0.72560 -0.02900 0.10157  0.03594  131 CYS A SG  
750  N N   . GLY A 96  ? 0.58170 0.67278 0.72077 0.00235  0.16161  -0.01155 132 GLY A N   
751  C CA  . GLY A 96  ? 0.61612 0.70638 0.72705 0.00697  0.16635  -0.04058 132 GLY A CA  
752  C C   . GLY A 96  ? 0.62240 0.71789 0.70374 0.00093  0.14457  -0.06072 132 GLY A C   
753  O O   . GLY A 96  ? 0.64692 0.73889 0.72461 -0.00124 0.14231  -0.08951 132 GLY A O   
754  N N   . ARG A 97  ? 0.50768 0.61168 0.57407 -0.00185 0.12937  -0.04762 133 ARG A N   
755  C CA  . ARG A 97  ? 0.54870 0.66110 0.59435 -0.00738 0.10838  -0.06323 133 ARG A CA  
756  C C   . ARG A 97  ? 0.63241 0.73319 0.71081 -0.02108 0.09816  -0.07784 133 ARG A C   
757  O O   . ARG A 97  ? 0.57519 0.67953 0.64930 -0.02527 0.08983  -0.10367 133 ARG A O   
758  C CB  . ARG A 97  ? 0.58422 0.71412 0.58219 0.00412  0.10814  -0.08498 133 ARG A CB  
759  C CG  . ARG A 97  ? 0.62993 0.77462 0.59016 0.02078  0.11786  -0.06288 133 ARG A CG  
760  C CD  . ARG A 97  ? 0.73925 0.90881 0.64449 0.03439  0.10959  -0.08120 133 ARG A CD  
761  N NE  . ARG A 97  ? 0.75497 0.93750 0.65737 0.02714  0.08268  -0.08992 133 ARG A NE  
762  C CZ  . ARG A 97  ? 0.76055 0.94961 0.66190 0.02858  0.07464  -0.06456 133 ARG A CZ  
763  N NH1 . ARG A 97  ? 0.68580 0.86738 0.59269 0.03507  0.09025  -0.02979 133 ARG A NH1 
764  N NH2 . ARG A 97  ? 0.71003 0.91301 0.61177 0.02316  0.05163  -0.07499 133 ARG A NH2 
765  N N   . ARG A 98  ? 0.58297 0.67138 0.69781 -0.02731 0.09887  -0.06000 134 ARG A N   
766  C CA  . ARG A 98  ? 0.54143 0.61976 0.68662 -0.03742 0.09114  -0.06274 134 ARG A CA  
767  C C   . ARG A 98  ? 0.57855 0.65226 0.74754 -0.03967 0.08668  -0.03686 134 ARG A C   
768  O O   . ARG A 98  ? 0.60202 0.67400 0.78784 -0.03526 0.09478  -0.02423 134 ARG A O   
769  C CB  . ARG A 98  ? 0.62727 0.69309 0.79751 -0.03805 0.10339  -0.08143 134 ARG A CB  
770  C CG  . ARG A 98  ? 0.60753 0.66510 0.80490 -0.04793 0.09761  -0.09172 134 ARG A CG  
771  C CD  . ARG A 98  ? 0.79461 0.83438 1.03076 -0.04802 0.11321  -0.10396 134 ARG A CD  
772  N NE  . ARG A 98  ? 0.78803 0.82120 1.04834 -0.05713 0.11145  -0.12772 134 ARG A NE  
773  C CZ  . ARG A 98  ? 0.88643 0.92209 1.14046 -0.05857 0.11185  -0.16590 134 ARG A CZ  
774  N NH1 . ARG A 98  ? 0.95608 1.00127 1.17109 -0.04882 0.11549  -0.18287 134 ARG A NH1 
775  N NH2 . ARG A 98  ? 0.75407 0.78392 1.04326 -0.06924 0.10900  -0.18813 134 ARG A NH2 
776  N N   . PHE A 99  ? 0.49315 0.56757 0.66416 -0.04544 0.07354  -0.02989 135 PHE A N   
777  C CA  . PHE A 99  ? 0.51922 0.59214 0.70702 -0.04581 0.06627  -0.00990 135 PHE A CA  
778  C C   . PHE A 99  ? 0.53482 0.59916 0.74831 -0.04725 0.06876  -0.00529 135 PHE A C   
779  O O   . PHE A 99  ? 0.42969 0.48927 0.64779 -0.05162 0.07224  -0.01626 135 PHE A O   
780  C CB  . PHE A 99  ? 0.49858 0.57869 0.66628 -0.04765 0.05230  -0.00365 135 PHE A CB  
781  C CG  . PHE A 99  ? 0.51446 0.60000 0.67140 -0.04498 0.05065  0.00084  135 PHE A CG  
782  C CD1 . PHE A 99  ? 0.47358 0.55881 0.64752 -0.04149 0.05949  0.00712  135 PHE A CD1 
783  C CD2 . PHE A 99  ? 0.45051 0.54092 0.58737 -0.04537 0.04286  0.00084  135 PHE A CD2 
784  C CE1 . PHE A 99  ? 0.50848 0.59716 0.68185 -0.03922 0.06178  0.01450  135 PHE A CE1 
785  C CE2 . PHE A 99  ? 0.45458 0.54703 0.58941 -0.04236 0.04431  0.00758  135 PHE A CE2 
786  C CZ  . PHE A 99  ? 0.49250 0.58358 0.64689 -0.03970 0.05429  0.01508  135 PHE A CZ  
787  N N   . SER A 100 ? 0.47610 0.53999 0.71130 -0.04283 0.06719  0.01213  136 SER A N   
788  C CA  . SER A 100 ? 0.45775 0.51512 0.71676 -0.04042 0.07044  0.02472  136 SER A CA  
789  C C   . SER A 100 ? 0.45581 0.51668 0.69742 -0.04195 0.06251  0.03233  136 SER A C   
790  O O   . SER A 100 ? 0.46088 0.53020 0.67386 -0.04394 0.05172  0.02891  136 SER A O   
791  C CB  . SER A 100 ? 0.55170 0.61443 0.83443 -0.03217 0.06654  0.04456  136 SER A CB  
792  O OG  . SER A 100 ? 0.47382 0.55135 0.73939 -0.03039 0.04772  0.05247  136 SER A OG  
793  N N   . VAL A 101 ? 0.47714 0.53046 0.73998 -0.03977 0.07122  0.04448  137 VAL A N   
794  C CA  . VAL A 101 ? 0.53163 0.58851 0.78121 -0.03898 0.06944  0.05597  137 VAL A CA  
795  C C   . VAL A 101 ? 0.47538 0.54687 0.69463 -0.03070 0.05313  0.07036  137 VAL A C   
796  O O   . VAL A 101 ? 0.49852 0.57686 0.68931 -0.03121 0.04678  0.06823  137 VAL A O   
797  C CB  . VAL A 101 ? 0.45218 0.49734 0.73769 -0.03590 0.08652  0.07283  137 VAL A CB  
798  C CG1 . VAL A 101 ? 0.46247 0.51229 0.73586 -0.03339 0.08984  0.08857  137 VAL A CG1 
799  C CG2 . VAL A 101 ? 0.52536 0.55516 0.84633 -0.04588 0.10076  0.05003  137 VAL A CG2 
800  N N   . LYS A 102 ? 0.46254 0.54056 0.69004 -0.02260 0.04518  0.08222  138 LYS A N   
801  C CA  . LYS A 102 ? 0.52912 0.62422 0.73115 -0.01451 0.02545  0.09019  138 LYS A CA  
802  C C   . LYS A 102 ? 0.50418 0.60421 0.68434 -0.02180 0.01301  0.06959  138 LYS A C   
803  O O   . LYS A 102 ? 0.43678 0.54503 0.58749 -0.01889 0.00169  0.06706  138 LYS A O   
804  C CB  . LYS A 102 ? 0.52193 0.62711 0.74732 -0.00517 0.01673  0.10395  138 LYS A CB  
805  C CG  . LYS A 102 ? 0.62963 0.75709 0.83479 0.00269  -0.00913 0.10560  138 LYS A CG  
806  C CD  . LYS A 102 ? 0.54415 0.68639 0.78110 0.01266  -0.01955 0.12009  138 LYS A CD  
807  C CE  . LYS A 102 ? 0.60766 0.77581 0.83255 0.01768  -0.05039 0.11261  138 LYS A CE  
808  N NZ  . LYS A 102 ? 0.61896 0.80869 0.87797 0.02897  -0.06521 0.12726  138 LYS A NZ  
809  N N   . THR A 103 ? 0.46282 0.55732 0.65746 -0.02958 0.01731  0.05572  139 THR A N   
810  C CA  . THR A 103 ? 0.48678 0.58379 0.66659 -0.03514 0.01001  0.04118  139 THR A CA  
811  C C   . THR A 103 ? 0.52246 0.61623 0.67571 -0.03872 0.01312  0.03331  139 THR A C   
812  O O   . THR A 103 ? 0.48411 0.58194 0.61890 -0.03865 0.00385  0.02739  139 THR A O   
813  C CB  . THR A 103 ? 0.47618 0.56872 0.67505 -0.03941 0.01940  0.03382  139 THR A CB  
814  O OG1 . THR A 103 ? 0.48433 0.58331 0.71372 -0.03598 0.01540  0.04123  139 THR A OG1 
815  C CG2 . THR A 103 ? 0.46630 0.55927 0.65100 -0.04342 0.01744  0.02412  139 THR A CG2 
816  N N   . VAL A 104 ? 0.49575 0.58286 0.65271 -0.04189 0.02593  0.03152  140 VAL A N   
817  C CA  . VAL A 104 ? 0.44372 0.53199 0.58405 -0.04537 0.02796  0.02401  140 VAL A CA  
818  C C   . VAL A 104 ? 0.42766 0.52110 0.54944 -0.03960 0.02387  0.03349  140 VAL A C   
819  O O   . VAL A 104 ? 0.43271 0.53010 0.53543 -0.03933 0.01963  0.02719  140 VAL A O   
820  C CB  . VAL A 104 ? 0.33982 0.42301 0.49775 -0.05101 0.04016  0.01687  140 VAL A CB  
821  C CG1 . VAL A 104 ? 0.44892 0.53824 0.59826 -0.05412 0.04048  0.01116  140 VAL A CG1 
822  C CG2 . VAL A 104 ? 0.41564 0.49648 0.57989 -0.05429 0.04349  0.00203  140 VAL A CG2 
823  N N   . VAL A 105 ? 0.41882 0.51292 0.54479 -0.03260 0.02676  0.05019  141 VAL A N   
824  C CA  . VAL A 105 ? 0.41480 0.51599 0.51594 -0.02330 0.02582  0.06155  141 VAL A CA  
825  C C   . VAL A 105 ? 0.50780 0.61753 0.58134 -0.01855 0.00770  0.05198  141 VAL A C   
826  O O   . VAL A 105 ? 0.49825 0.61112 0.54765 -0.01565 0.00666  0.04565  141 VAL A O   
827  C CB  . VAL A 105 ? 0.51284 0.61517 0.62193 -0.01292 0.03339  0.08654  141 VAL A CB  
828  C CG1 . VAL A 105 ? 0.50444 0.61881 0.57607 0.00175  0.02991  0.09962  141 VAL A CG1 
829  C CG2 . VAL A 105 ? 0.46751 0.55858 0.61037 -0.01836 0.05522  0.09464  141 VAL A CG2 
830  N N   . GLN A 106 ? 0.38838 0.50202 0.47128 -0.01797 -0.00620 0.04871  142 GLN A N   
831  C CA  . GLN A 106 ? 0.46093 0.58339 0.52783 -0.01461 -0.02553 0.03588  142 GLN A CA  
832  C C   . GLN A 106 ? 0.46492 0.58007 0.53171 -0.02288 -0.02562 0.01753  142 GLN A C   
833  O O   . GLN A 106 ? 0.62970 0.74731 0.67784 -0.01970 -0.03425 0.00496  142 GLN A O   
834  C CB  . GLN A 106 ? 0.47838 0.60917 0.56940 -0.01379 -0.04036 0.03629  142 GLN A CB  
835  C CG  . GLN A 106 ? 0.57475 0.71706 0.66546 -0.00153 -0.04399 0.05700  142 GLN A CG  
836  C CD  . GLN A 106 ? 0.63275 0.78581 0.75780 -0.00084 -0.05790 0.05871  142 GLN A CD  
837  O OE1 . GLN A 106 ? 0.65206 0.82528 0.77087 0.00990  -0.07834 0.06182  142 GLN A OE1 
838  N NE2 . GLN A 106 ? 0.55435 0.69685 0.71585 -0.01074 -0.04696 0.05661  142 GLN A NE2 
839  N N   . VAL A 107 ? 0.40762 0.51420 0.49449 -0.03163 -0.01536 0.01595  143 VAL A N   
840  C CA  . VAL A 107 ? 0.40812 0.50921 0.49475 -0.03642 -0.01267 0.00518  143 VAL A CA  
841  C C   . VAL A 107 ? 0.48462 0.58589 0.55106 -0.03408 -0.00534 0.00417  143 VAL A C   
842  O O   . VAL A 107 ? 0.48054 0.58001 0.53953 -0.03284 -0.00710 -0.00457 143 VAL A O   
843  C CB  . VAL A 107 ? 0.46604 0.56252 0.57238 -0.04227 -0.00334 0.00664  143 VAL A CB  
844  C CG1 . VAL A 107 ? 0.57735 0.67203 0.67661 -0.04361 0.00310  0.00248  143 VAL A CG1 
845  C CG2 . VAL A 107 ? 0.56727 0.66355 0.69865 -0.04411 -0.00833 0.00610  143 VAL A CG2 
846  N N   . ALA A 108 ? 0.49361 0.59686 0.55783 -0.03311 0.00460  0.01369  144 ALA A N   
847  C CA  . ALA A 108 ? 0.52664 0.63264 0.58231 -0.03168 0.01377  0.01403  144 ALA A CA  
848  C C   . ALA A 108 ? 0.52731 0.63670 0.55650 -0.02216 0.01148  0.01235  144 ALA A C   
849  O O   . ALA A 108 ? 0.52004 0.63027 0.54282 -0.02016 0.01569  0.00610  144 ALA A O   
850  C CB  . ALA A 108 ? 0.47376 0.58077 0.54476 -0.03390 0.02675  0.02471  144 ALA A CB  
851  N N   . ILE A 109 ? 0.46244 0.57574 0.47483 -0.01429 0.00444  0.01704  145 ILE A N   
852  C CA  . ILE A 109 ? 0.50731 0.62638 0.48600 -0.00235 0.00211  0.01254  145 ILE A CA  
853  C C   . ILE A 109 ? 0.58480 0.69991 0.55946 -0.00336 -0.01113 -0.01100 145 ILE A C   
854  O O   . ILE A 109 ? 0.58212 0.69771 0.53488 0.00433  -0.00879 -0.02175 145 ILE A O   
855  C CB  . ILE A 109 ? 0.53855 0.66783 0.49492 0.00975  -0.00367 0.02509  145 ILE A CB  
856  C CG1 . ILE A 109 ? 0.60757 0.74066 0.57442 0.00748  -0.02583 0.01664  145 ILE A CG1 
857  C CG2 . ILE A 109 ? 0.61431 0.74354 0.58468 0.01108  0.01403  0.05188  145 ILE A CG2 
858  C CD1 . ILE A 109 ? 0.67885 0.82734 0.62499 0.02169  -0.03570 0.03015  145 ILE A CD1 
859  N N   . GLN A 110 ? 0.54910 0.65907 0.54931 -0.01227 -0.02226 -0.01918 146 GLN A N   
860  C CA  . GLN A 110 ? 0.49158 0.59415 0.50201 -0.01493 -0.03023 -0.03925 146 GLN A CA  
861  C C   . GLN A 110 ? 0.55892 0.65328 0.58029 -0.01776 -0.01663 -0.03853 146 GLN A C   
862  O O   . GLN A 110 ? 0.55671 0.64487 0.57666 -0.01426 -0.01595 -0.05209 146 GLN A O   
863  C CB  . GLN A 110 ? 0.48821 0.58843 0.53150 -0.02316 -0.04209 -0.04399 146 GLN A CB  
864  C CG  . GLN A 110 ? 0.48169 0.59453 0.52171 -0.01955 -0.06004 -0.04671 146 GLN A CG  
865  C CD  . GLN A 110 ? 0.58459 0.69743 0.66756 -0.02807 -0.07197 -0.05410 146 GLN A CD  
866  O OE1 . GLN A 110 ? 0.60102 0.70314 0.71229 -0.03478 -0.07038 -0.06493 146 GLN A OE1 
867  N NE2 . GLN A 110 ? 0.61557 0.74093 0.70926 -0.02687 -0.08204 -0.04587 146 GLN A NE2 
868  N N   . MET A 111 ? 0.48537 0.58091 0.51929 -0.02293 -0.00670 -0.02430 147 MET A N   
869  C CA  . MET A 111 ? 0.45559 0.54997 0.49836 -0.02319 0.00290  -0.02225 147 MET A CA  
870  C C   . MET A 111 ? 0.54331 0.64243 0.57042 -0.01562 0.01180  -0.02318 147 MET A C   
871  O O   . MET A 111 ? 0.52130 0.61764 0.55374 -0.01155 0.01637  -0.02838 147 MET A O   
872  C CB  . MET A 111 ? 0.42335 0.52302 0.47886 -0.02903 0.00778  -0.01153 147 MET A CB  
873  C CG  . MET A 111 ? 0.48562 0.58067 0.55563 -0.03401 0.00379  -0.00969 147 MET A CG  
874  S SD  . MET A 111 ? 0.53144 0.63315 0.60801 -0.03854 0.00951  -0.00304 147 MET A SD  
875  C CE  . MET A 111 ? 0.54300 0.65147 0.62003 -0.03426 0.01275  -0.00077 147 MET A CE  
876  N N   . LEU A 112 ? 0.45180 0.55792 0.46257 -0.01201 0.01696  -0.01584 148 LEU A N   
877  C CA  . LEU A 112 ? 0.54829 0.66008 0.54516 -0.00308 0.02997  -0.01372 148 LEU A CA  
878  C C   . LEU A 112 ? 0.59590 0.70252 0.56944 0.00691  0.02691  -0.03072 148 LEU A C   
879  O O   . LEU A 112 ? 0.55579 0.66274 0.52690 0.01408  0.03807  -0.03519 148 LEU A O   
880  C CB  . LEU A 112 ? 0.46826 0.58764 0.45500 0.00039  0.03971  0.00258  148 LEU A CB  
881  C CG  . LEU A 112 ? 0.49605 0.62020 0.51383 -0.00871 0.04858  0.01610  148 LEU A CG  
882  C CD1 . LEU A 112 ? 0.48870 0.61497 0.50296 -0.00518 0.05804  0.03417  148 LEU A CD1 
883  C CD2 . LEU A 112 ? 0.55764 0.69041 0.59648 -0.00910 0.06083  0.01727  148 LEU A CD2 
884  N N   . THR A 113 ? 0.52260 0.62579 0.48202 0.00796  0.01133  -0.04277 149 THR A N   
885  C CA  . THR A 113 ? 0.60730 0.70567 0.54784 0.01631  0.00450  -0.06693 149 THR A CA  
886  C C   . THR A 113 ? 0.64338 0.72757 0.61448 0.01188  0.00507  -0.08048 149 THR A C   
887  O O   . THR A 113 ? 0.63604 0.71425 0.60063 0.02020  0.01177  -0.09588 149 THR A O   
888  C CB  . THR A 113 ? 0.58027 0.68279 0.50722 0.01700  -0.01708 -0.07927 149 THR A CB  
889  O OG1 . THR A 113 ? 0.59854 0.71520 0.49823 0.02415  -0.01581 -0.06058 149 THR A OG1 
890  C CG2 . THR A 113 ? 0.70948 0.80964 0.61555 0.02596  -0.02751 -0.11144 149 THR A CG2 
891  N N   . LEU A 114 ? 0.54794 0.62631 0.55314 0.00079  0.00075  -0.07317 150 LEU A N   
892  C CA  . LEU A 114 ? 0.51870 0.58391 0.55596 -0.00111 0.00473  -0.07812 150 LEU A CA  
893  C C   . LEU A 114 ? 0.58712 0.65518 0.62732 0.00595  0.02097  -0.06932 150 LEU A C   
894  O O   . LEU A 114 ? 0.54572 0.60395 0.59475 0.01295  0.02751  -0.08141 150 LEU A O   
895  C CB  . LEU A 114 ? 0.54193 0.60438 0.60914 -0.01090 0.00181  -0.06439 150 LEU A CB  
896  C CG  . LEU A 114 ? 0.62094 0.67661 0.70758 -0.01804 -0.01153 -0.07540 150 LEU A CG  
897  C CD1 . LEU A 114 ? 0.64951 0.70810 0.75523 -0.02556 -0.01006 -0.05635 150 LEU A CD1 
898  C CD2 . LEU A 114 ? 0.60219 0.64057 0.72060 -0.01791 -0.01143 -0.09286 150 LEU A CD2 
899  N N   . VAL A 115 ? 0.53971 0.62201 0.57826 0.00429  0.02740  -0.04997 151 VAL A N   
900  C CA  . VAL A 115 ? 0.52629 0.61725 0.57652 0.01016  0.04013  -0.04088 151 VAL A CA  
901  C C   . VAL A 115 ? 0.54645 0.63802 0.57892 0.02151  0.05202  -0.05055 151 VAL A C   
902  O O   . VAL A 115 ? 0.61532 0.70563 0.66279 0.02964  0.06261  -0.05247 151 VAL A O   
903  C CB  . VAL A 115 ? 0.50003 0.60873 0.55725 0.00421  0.04136  -0.02385 151 VAL A CB  
904  C CG1 . VAL A 115 ? 0.50961 0.63320 0.58515 0.00995  0.05188  -0.01633 151 VAL A CG1 
905  C CG2 . VAL A 115 ? 0.42430 0.53298 0.49434 -0.00364 0.03179  -0.01698 151 VAL A CG2 
906  N N   . GLU A 116 ? 0.51829 0.61290 0.51767 0.02464  0.05199  -0.05514 152 GLU A N   
907  C CA  . GLU A 116 ? 0.66246 0.75875 0.63570 0.03872  0.06553  -0.06442 152 GLU A CA  
908  C C   . GLU A 116 ? 0.73602 0.81580 0.71019 0.04564  0.06400  -0.09076 152 GLU A C   
909  O O   . GLU A 116 ? 0.68867 0.76659 0.66882 0.05615  0.07992  -0.09588 152 GLU A O   
910  C CB  . GLU A 116 ? 0.60658 0.71005 0.53723 0.04410  0.06364  -0.06328 152 GLU A CB  
911  C CG  . GLU A 116 ? 0.69707 0.80408 0.58966 0.06247  0.07899  -0.07308 152 GLU A CG  
912  C CD  . GLU A 116 ? 0.79031 0.90728 0.63317 0.07224  0.07586  -0.06966 152 GLU A CD  
913  O OE1 . GLU A 116 ? 0.72550 0.84584 0.56883 0.06400  0.06096  -0.05944 152 GLU A OE1 
914  O OE2 . GLU A 116 ? 0.83094 0.95367 0.63286 0.09041  0.08936  -0.07601 152 GLU A OE2 
915  N N   . GLU A 117 ? 0.68075 0.74813 0.65637 0.03959  0.04579  -0.10878 153 GLU A N   
916  C CA  . GLU A 117 ? 0.74311 0.79220 0.72895 0.04414  0.04339  -0.13845 153 GLU A CA  
917  C C   . GLU A 117 ? 0.72049 0.75822 0.75197 0.04499  0.05576  -0.13143 153 GLU A C   
918  O O   . GLU A 117 ? 0.75206 0.77586 0.79367 0.05414  0.06499  -0.15125 153 GLU A O   
919  C CB  . GLU A 117 ? 0.78770 0.82796 0.78288 0.03423  0.02061  -0.15708 153 GLU A CB  
920  C CG  . GLU A 117 ? 0.95923 0.98379 0.95728 0.03909  0.01373  -0.19790 153 GLU A CG  
921  C CD  . GLU A 117 ? 1.01713 1.05175 0.95682 0.05496  0.01464  -0.22009 153 GLU A CD  
922  O OE1 . GLU A 117 ? 1.05942 1.11407 0.95558 0.05932  0.01058  -0.20628 153 GLU A OE1 
923  O OE2 . GLU A 117 ? 1.11680 1.13909 1.05382 0.06485  0.02134  -0.25045 153 GLU A OE2 
924  N N   . VAL A 118 ? 0.57238 0.61681 0.63104 0.03756  0.05624  -0.10377 154 VAL A N   
925  C CA  . VAL A 118 ? 0.62846 0.66916 0.72572 0.04256  0.06780  -0.09078 154 VAL A CA  
926  C C   . VAL A 118 ? 0.69467 0.74745 0.78749 0.05508  0.08552  -0.08625 154 VAL A C   
927  O O   . VAL A 118 ? 0.68688 0.73066 0.80427 0.06553  0.09818  -0.09083 154 VAL A O   
928  C CB  . VAL A 118 ? 0.56728 0.61850 0.68490 0.03470  0.06200  -0.06291 154 VAL A CB  
929  C CG1 . VAL A 118 ? 0.59349 0.64791 0.74577 0.04381  0.07218  -0.04537 154 VAL A CG1 
930  C CG2 . VAL A 118 ? 0.65294 0.69084 0.78158 0.02437  0.05003  -0.06581 154 VAL A CG2 
931  N N   . HIS A 119 ? 0.60559 0.67830 0.67313 0.05485  0.08913  -0.07618 155 HIS A N   
932  C CA  . HIS A 119 ? 0.72589 0.81245 0.79568 0.06638  0.10905  -0.06974 155 HIS A CA  
933  C C   . HIS A 119 ? 0.69593 0.77004 0.74173 0.08076  0.12274  -0.09483 155 HIS A C   
934  O O   . HIS A 119 ? 0.76507 0.84206 0.82710 0.09338  0.14228  -0.09444 155 HIS A O   
935  C CB  . HIS A 119 ? 0.56659 0.67532 0.62277 0.06181  0.11248  -0.05202 155 HIS A CB  
936  C CG  . HIS A 119 ? 0.60332 0.72681 0.68635 0.04931  0.10100  -0.03234 155 HIS A CG  
937  N ND1 . HIS A 119 ? 0.53396 0.67323 0.61486 0.04128  0.10074  -0.01934 155 HIS A ND1 
938  C CD2 . HIS A 119 ? 0.54475 0.67012 0.65625 0.04508  0.09008  -0.02448 155 HIS A CD2 
939  C CE1 . HIS A 119 ? 0.53553 0.68570 0.64167 0.03165  0.08828  -0.00963 155 HIS A CE1 
940  N NE2 . HIS A 119 ? 0.52596 0.66977 0.64655 0.03491  0.08141  -0.01128 155 HIS A NE2 
941  N N   . ARG A 120 ? 0.77248 0.83516 0.77995 0.08044  0.11229  -0.11836 156 ARG A N   
942  C CA  . ARG A 120 ? 0.84266 0.89416 0.82176 0.09543  0.12210  -0.14936 156 ARG A CA  
943  C C   . ARG A 120 ? 0.86417 0.89335 0.88399 0.10038  0.12843  -0.16738 156 ARG A C   
944  O O   . ARG A 120 ? 0.90479 0.92652 0.91674 0.11594  0.14613  -0.18758 156 ARG A O   
945  C CB  . ARG A 120 ? 0.93615 0.98337 0.87019 0.09368  0.10234  -0.17478 156 ARG A CB  
946  C CG  . ARG A 120 ? 1.07317 1.13908 0.97742 0.08699  0.09188  -0.15322 156 ARG A CG  
947  C CD  . ARG A 120 ? 1.17641 1.25807 1.02254 0.10357  0.10498  -0.15154 156 ARG A CD  
948  N NE  . ARG A 120 ? 1.35612 1.43400 1.15439 0.11419  0.09176  -0.18802 156 ARG A NE  
949  C CZ  . ARG A 120 ? 1.37885 1.46553 1.14446 0.11204  0.06827  -0.19389 156 ARG A CZ  
950  N NH1 . ARG A 120 ? 1.23180 1.32840 1.00711 0.10026  0.05890  -0.16425 156 ARG A NH1 
951  N NH2 . ARG A 120 ? 1.38875 1.47578 1.11281 0.12293  0.05294  -0.23227 156 ARG A NH2 
952  N N   . HIS A 121 ? 0.81721 0.83485 0.88201 0.08902  0.11699  -0.15890 157 HIS A N   
953  C CA  . HIS A 121 ? 0.90223 0.89697 1.01597 0.09393  0.12514  -0.16836 157 HIS A CA  
954  C C   . HIS A 121 ? 0.80655 0.81253 0.96106 0.10145  0.14097  -0.13674 157 HIS A C   
955  O O   . HIS A 121 ? 0.77236 0.76438 0.97549 0.10338  0.14411  -0.12793 157 HIS A O   
956  C CB  . HIS A 121 ? 0.89798 0.87386 1.04268 0.08010  0.10770  -0.17306 157 HIS A CB  
957  C CG  . HIS A 121 ? 0.97173 0.93458 1.09417 0.07449  0.09143  -0.21246 157 HIS A CG  
958  N ND1 . HIS A 121 ? 0.94332 0.92339 1.01210 0.07075  0.07630  -0.21965 157 HIS A ND1 
959  C CD2 . HIS A 121 ? 0.97751 0.91386 1.12844 0.07264  0.08659  -0.24802 157 HIS A CD2 
960  C CE1 . HIS A 121 ? 0.96594 0.93450 1.02716 0.06768  0.05995  -0.25822 157 HIS A CE1 
961  N NE2 . HIS A 121 ? 0.98959 0.93116 1.10223 0.06742  0.06535  -0.27853 157 HIS A NE2 
962  N N   . ASP A 122 ? 0.82682 0.85965 0.96715 0.10643  0.15096  -0.11783 158 ASP A N   
963  C CA  . ASP A 122 ? 0.76309 0.81356 0.94316 0.11587  0.16557  -0.09254 158 ASP A CA  
964  C C   . ASP A 122 ? 0.75754 0.82045 0.97328 0.10849  0.15179  -0.06197 158 ASP A C   
965  O O   . ASP A 122 ? 0.71091 0.78526 0.96819 0.11855  0.15939  -0.04281 158 ASP A O   
966  C CB  . ASP A 122 ? 0.80785 0.84016 1.01791 0.13336  0.18675  -0.10740 158 ASP A CB  
967  C CG  . ASP A 122 ? 0.90819 0.92284 1.07802 0.14213  0.19813  -0.14651 158 ASP A CG  
968  O OD1 . ASP A 122 ? 0.90356 0.93401 1.02549 0.14403  0.20261  -0.14981 158 ASP A OD1 
969  O OD2 . ASP A 122 ? 0.95602 0.94114 1.14277 0.14822  0.20307  -0.17434 158 ASP A OD2 
970  N N   . LEU A 123 ? 0.65971 0.72347 0.85893 0.09326  0.13188  -0.05620 159 LEU A N   
971  C CA  . LEU A 123 ? 0.65955 0.73552 0.88255 0.08832  0.11933  -0.02937 159 LEU A CA  
972  C C   . LEU A 123 ? 0.65399 0.75516 0.85415 0.07574  0.10548  -0.01783 159 LEU A C   
973  O O   . LEU A 123 ? 0.59962 0.69869 0.76557 0.06714  0.10201  -0.02996 159 LEU A O   
974  C CB  . LEU A 123 ? 0.69614 0.74565 0.93040 0.08307  0.11187  -0.03216 159 LEU A CB  
975  C CG  . LEU A 123 ? 0.74795 0.76543 1.01302 0.09234  0.12514  -0.04853 159 LEU A CG  
976  C CD1 . LEU A 123 ? 0.78889 0.78276 1.07652 0.08484  0.11904  -0.04654 159 LEU A CD1 
977  C CD2 . LEU A 123 ? 0.75759 0.78214 1.06288 0.11013  0.14086  -0.03066 159 LEU A CD2 
978  N N   . ILE A 124 ? 0.49780 0.62365 0.71826 0.07614  0.09715  0.00512  160 ILE A N   
979  C CA  . ILE A 124 ? 0.58591 0.73259 0.79122 0.06368  0.08179  0.01303  160 ILE A CA  
980  C C   . ILE A 124 ? 0.65431 0.79763 0.86030 0.06159  0.06949  0.02561  160 ILE A C   
981  O O   . ILE A 124 ? 0.62450 0.76305 0.85326 0.07295  0.07294  0.03897  160 ILE A O   
982  C CB  . ILE A 124 ? 0.52246 0.70619 0.74945 0.06527  0.08001  0.02388  160 ILE A CB  
983  C CG1 . ILE A 124 ? 0.55328 0.75439 0.81832 0.08078  0.08075  0.04020  160 ILE A CG1 
984  C CG2 . ILE A 124 ? 0.53690 0.72451 0.76130 0.06483  0.09550  0.01488  160 ILE A CG2 
985  C CD1 . ILE A 124 ? 0.47289 0.71589 0.76831 0.08230  0.07500  0.04859  160 ILE A CD1 
986  N N   . TYR A 125 ? 0.57771 0.72341 0.76008 0.04874  0.05784  0.02370  161 TYR A N   
987  C CA  . TYR A 125 ? 0.54255 0.68167 0.72035 0.04704  0.05051  0.03426  161 TYR A CA  
988  C C   . TYR A 125 ? 0.56506 0.73473 0.74857 0.05423  0.04092  0.05348  161 TYR A C   
989  O O   . TYR A 125 ? 0.60104 0.76994 0.79357 0.06546  0.04251  0.07218  161 TYR A O   
990  C CB  . TYR A 125 ? 0.55209 0.68130 0.70407 0.03222  0.04370  0.02352  161 TYR A CB  
991  C CG  . TYR A 125 ? 0.56066 0.67760 0.71201 0.03066  0.04168  0.03266  161 TYR A CG  
992  C CD1 . TYR A 125 ? 0.59930 0.68904 0.76814 0.03246  0.04943  0.03074  161 TYR A CD1 
993  C CD2 . TYR A 125 ? 0.61286 0.74539 0.75014 0.02774  0.03388  0.04194  161 TYR A CD2 
994  C CE1 . TYR A 125 ? 0.61593 0.69491 0.79319 0.03093  0.05145  0.04217  161 TYR A CE1 
995  C CE2 . TYR A 125 ? 0.62925 0.75156 0.76620 0.02832  0.03661  0.05305  161 TYR A CE2 
996  C CZ  . TYR A 125 ? 0.56358 0.65947 0.72297 0.02971  0.04641  0.05533  161 TYR A CZ  
997  O OH  . TYR A 125 ? 0.57719 0.66378 0.74455 0.03016  0.05268  0.06940  161 TYR A OH  
998  N N   . ARG A 126 ? 0.54267 0.74042 0.72209 0.04865  0.03081  0.04898  162 ARG A N   
999  C CA  . ARG A 126 ? 0.54564 0.78019 0.73136 0.05561  0.01685  0.05961  162 ARG A CA  
1000 C C   . ARG A 126 ? 0.60782 0.84669 0.76869 0.05748  0.00792  0.06852  162 ARG A C   
1001 O O   . ARG A 126 ? 0.67119 0.94189 0.82924 0.06782  -0.00483 0.07832  162 ARG A O   
1002 C CB  . ARG A 126 ? 0.54753 0.79826 0.76289 0.07410  0.01960  0.07609  162 ARG A CB  
1003 C CG  . ARG A 126 ? 0.58545 0.83577 0.82828 0.07523  0.03135  0.06828  162 ARG A CG  
1004 C CD  . ARG A 126 ? 0.52846 0.80818 0.80745 0.09303  0.02938  0.08438  162 ARG A CD  
1005 N NE  . ARG A 126 ? 0.61273 0.88381 0.89646 0.11052  0.03292  0.10712  162 ARG A NE  
1006 C CZ  . ARG A 126 ? 0.72237 1.01946 1.03460 0.13040  0.02967  0.12859  162 ARG A CZ  
1007 N NH1 . ARG A 126 ? 0.61398 0.95065 0.95525 0.13459  0.02012  0.12778  162 ARG A NH1 
1008 N NH2 . ARG A 126 ? 0.73091 1.01527 1.04822 0.14723  0.03694  0.15347  162 ARG A NH2 
1009 N N   . ASP A 127 ? 0.69100 0.90185 0.83352 0.04930  0.01409  0.06526  163 ASP A N   
1010 C CA  . ASP A 127 ? 0.70364 0.91753 0.82306 0.05186  0.01053  0.07455  163 ASP A CA  
1011 C C   . ASP A 127 ? 0.67596 0.87098 0.77913 0.03543  0.01179  0.05924  163 ASP A C   
1012 O O   . ASP A 127 ? 0.58440 0.76365 0.67873 0.03542  0.01850  0.06681  163 ASP A O   
1013 C CB  . ASP A 127 ? 0.72217 0.92140 0.84920 0.06648  0.02294  0.09983  163 ASP A CB  
1014 C CG  . ASP A 127 ? 0.82911 1.04324 0.93089 0.07700  0.02131  0.11762  163 ASP A CG  
1015 O OD1 . ASP A 127 ? 0.77131 1.01569 0.84914 0.07764  0.00608  0.10929  163 ASP A OD1 
1016 O OD2 . ASP A 127 ? 0.90912 1.10489 1.01663 0.08507  0.03649  0.13891  163 ASP A OD2 
1017 N N   . ILE A 128 ? 0.48722 0.68453 0.59135 0.02237  0.00723  0.04029  164 ILE A N   
1018 C CA  . ILE A 128 ? 0.46769 0.64826 0.56056 0.00854  0.00864  0.02810  164 ILE A CA  
1019 C C   . ILE A 128 ? 0.48551 0.67573 0.55964 0.00809  0.00362  0.02791  164 ILE A C   
1020 O O   . ILE A 128 ? 0.40204 0.61834 0.47049 0.01026  -0.00688 0.02191  164 ILE A O   
1021 C CB  . ILE A 128 ? 0.44662 0.63058 0.54724 -0.00199 0.00746  0.01377  164 ILE A CB  
1022 C CG1 . ILE A 128 ? 0.47244 0.64348 0.58262 0.00024  0.01652  0.01303  164 ILE A CG1 
1023 C CG2 . ILE A 128 ? 0.44183 0.61407 0.53253 -0.01369 0.00764  0.00492  164 ILE A CG2 
1024 C CD1 . ILE A 128 ? 0.41683 0.55981 0.51874 -0.00092 0.02206  0.01080  164 ILE A CD1 
1025 N N   . LYS A 129 ? 0.54501 0.71580 0.61178 0.00561  0.01095  0.03203  165 LYS A N   
1026 C CA  . LYS A 129 ? 0.52896 0.70551 0.57713 0.00666  0.01127  0.03220  165 LYS A CA  
1027 C C   . LYS A 129 ? 0.47290 0.62462 0.52691 -0.00020 0.02095  0.03404  165 LYS A C   
1028 O O   . LYS A 129 ? 0.49487 0.62852 0.56624 -0.00095 0.02660  0.04020  165 LYS A O   
1029 C CB  . LYS A 129 ? 0.56235 0.75591 0.59499 0.02425  0.01284  0.05054  165 LYS A CB  
1030 C CG  . LYS A 129 ? 0.63911 0.81543 0.68671 0.03349  0.02666  0.07448  165 LYS A CG  
1031 C CD  . LYS A 129 ? 0.65459 0.85107 0.68951 0.05474  0.02905  0.09889  165 LYS A CD  
1032 C CE  . LYS A 129 ? 0.66376 0.87499 0.66445 0.06407  0.03243  0.10519  165 LYS A CE  
1033 N NZ  . LYS A 129 ? 0.89031 1.11948 0.87496 0.08901  0.03915  0.13674  165 LYS A NZ  
1034 N N   . PRO A 130 ? 0.55041 0.70155 0.59526 -0.00526 0.02244  0.02652  166 PRO A N   
1035 C CA  . PRO A 130 ? 0.51086 0.64228 0.56836 -0.01108 0.03086  0.02946  166 PRO A CA  
1036 C C   . PRO A 130 ? 0.53871 0.66205 0.60611 -0.00275 0.04359  0.04946  166 PRO A C   
1037 O O   . PRO A 130 ? 0.55919 0.66619 0.65116 -0.00854 0.04897  0.05191  166 PRO A O   
1038 C CB  . PRO A 130 ? 0.51579 0.65181 0.56256 -0.01471 0.03204  0.01867  166 PRO A CB  
1039 C CG  . PRO A 130 ? 0.57685 0.73544 0.59988 -0.00710 0.02637  0.01229  166 PRO A CG  
1040 C CD  . PRO A 130 ? 0.48150 0.65046 0.50928 -0.00569 0.01626  0.01248  166 PRO A CD  
1041 N N   . ASP A 131 ? 0.53167 0.66771 0.58476 0.01152  0.04862  0.06515  167 ASP A N   
1042 C CA  . ASP A 131 ? 0.58630 0.71421 0.65307 0.02177  0.06568  0.09051  167 ASP A CA  
1043 C C   . ASP A 131 ? 0.57282 0.68099 0.67735 0.01854  0.06855  0.09592  167 ASP A C   
1044 O O   . ASP A 131 ? 0.47854 0.57197 0.61343 0.02042  0.08367  0.11181  167 ASP A O   
1045 C CB  . ASP A 131 ? 0.66513 0.81508 0.70230 0.04169  0.06979  0.10935  167 ASP A CB  
1046 C CG  . ASP A 131 ? 0.71619 0.89017 0.71245 0.04488  0.05993  0.09330  167 ASP A CG  
1047 O OD1 . ASP A 131 ? 0.68085 0.86451 0.67252 0.03607  0.04201  0.07001  167 ASP A OD1 
1048 O OD2 . ASP A 131 ? 0.69039 0.87305 0.66216 0.05616  0.07157  0.10254  167 ASP A OD2 
1049 N N   . ASN A 132 ? 0.49407 0.60113 0.60155 0.01380  0.05616  0.08170  168 ASN A N   
1050 C CA  . ASN A 132 ? 0.55049 0.63863 0.69084 0.01223  0.05885  0.08120  168 ASN A CA  
1051 C C   . ASN A 132 ? 0.54753 0.62013 0.70433 -0.00273 0.05078  0.05821  168 ASN A C   
1052 O O   . ASN A 132 ? 0.56308 0.61935 0.74728 -0.00483 0.05141  0.05095  168 ASN A O   
1053 C CB  . ASN A 132 ? 0.57418 0.67141 0.70861 0.02003  0.05326  0.08076  168 ASN A CB  
1054 C CG  . ASN A 132 ? 0.63730 0.75203 0.76163 0.03826  0.05924  0.10650  168 ASN A CG  
1055 O OD1 . ASN A 132 ? 0.64796 0.76287 0.77195 0.04714  0.07195  0.12845  168 ASN A OD1 
1056 N ND2 . ASN A 132 ? 0.62278 0.75502 0.73952 0.04576  0.05079  0.10595  168 ASN A ND2 
1057 N N   . PHE A 133 ? 0.44366 0.52188 0.58496 -0.01158 0.04280  0.04591  169 PHE A N   
1058 C CA  . PHE A 133 ? 0.43180 0.50057 0.58507 -0.02257 0.03351  0.02791  169 PHE A CA  
1059 C C   . PHE A 133 ? 0.50754 0.57009 0.68848 -0.02721 0.03933  0.03354  169 PHE A C   
1060 O O   . PHE A 133 ? 0.48038 0.55083 0.65159 -0.02652 0.04500  0.04146  169 PHE A O   
1061 C CB  . PHE A 133 ? 0.45114 0.53026 0.57717 -0.02724 0.02332  0.01605  169 PHE A CB  
1062 C CG  . PHE A 133 ? 0.46157 0.54668 0.57069 -0.02416 0.01929  0.00962  169 PHE A CG  
1063 C CD1 . PHE A 133 ? 0.52201 0.62177 0.61785 -0.01875 0.02121  0.01614  169 PHE A CD1 
1064 C CD2 . PHE A 133 ? 0.51085 0.58986 0.61805 -0.02554 0.01347  -0.00389 169 PHE A CD2 
1065 C CE1 . PHE A 133 ? 0.50808 0.61578 0.59791 -0.01627 0.01893  0.01129  169 PHE A CE1 
1066 C CE2 . PHE A 133 ? 0.53122 0.61643 0.62509 -0.02127 0.01425  -0.00768 169 PHE A CE2 
1067 C CZ  . PHE A 133 ? 0.46060 0.55989 0.55024 -0.01740 0.01775  0.00090  169 PHE A CZ  
1068 N N   . LEU A 134 ? 0.58239 0.63145 0.80221 -0.03192 0.03840  0.02726  170 LEU A N   
1069 C CA  . LEU A 134 ? 0.53907 0.58293 0.80115 -0.03682 0.04563  0.03373  170 LEU A CA  
1070 C C   . LEU A 134 ? 0.55274 0.59641 0.83642 -0.04742 0.02725  0.01087  170 LEU A C   
1071 O O   . LEU A 134 ? 0.57175 0.61286 0.84759 -0.04944 0.01204  -0.01018 170 LEU A O   
1072 C CB  . LEU A 134 ? 0.54541 0.57471 0.85215 -0.03321 0.06229  0.04827  170 LEU A CB  
1073 C CG  . LEU A 134 ? 0.55725 0.58880 0.85698 -0.01965 0.08576  0.08121  170 LEU A CG  
1074 C CD1 . LEU A 134 ? 0.46784 0.51192 0.71413 -0.00884 0.08214  0.08586  170 LEU A CD1 
1075 C CD2 . LEU A 134 ? 0.60434 0.61753 0.96044 -0.01663 0.10313  0.09631  170 LEU A CD2 
1076 N N   . ILE A 135 ? 0.54455 0.59339 0.85549 -0.05232 0.02879  0.01517  171 ILE A N   
1077 C CA  . ILE A 135 ? 0.53861 0.59201 0.88019 -0.06109 0.00935  -0.00466 171 ILE A CA  
1078 C C   . ILE A 135 ? 0.53454 0.57688 0.94336 -0.06749 0.01220  -0.01042 171 ILE A C   
1079 O O   . ILE A 135 ? 0.49347 0.52223 0.92305 -0.06406 0.03227  0.00486  171 ILE A O   
1080 C CB  . ILE A 135 ? 0.55375 0.62058 0.90087 -0.06278 0.00831  0.00230  171 ILE A CB  
1081 C CG1 . ILE A 135 ? 0.52661 0.59120 0.90456 -0.06069 0.03447  0.02621  171 ILE A CG1 
1082 C CG2 . ILE A 135 ? 0.55609 0.63083 0.84616 -0.05781 0.00444  0.00379  171 ILE A CG2 
1083 C CD1 . ILE A 135 ? 0.61122 0.68741 1.01928 -0.06343 0.03541  0.03060  171 ILE A CD1 
1084 N N   . GLY A 136 ? 0.52816 0.57747 0.97570 -0.07615 -0.00817 -0.03213 172 GLY A N   
1085 C CA  . GLY A 136 ? 0.63512 0.67544 1.15886 -0.08501 -0.00874 -0.04389 172 GLY A CA  
1086 C C   . GLY A 136 ? 0.63823 0.68219 1.22588 -0.08960 0.00895  -0.02301 172 GLY A C   
1087 O O   . GLY A 136 ? 0.67155 0.72275 1.23879 -0.08382 0.02556  0.00220  172 GLY A O   
1088 N N   . ARG A 137 ? 0.66398 0.70277 1.33467 -0.10005 0.00668  -0.03549 173 ARG A N   
1089 C CA  . ARG A 137 ? 0.70409 0.74731 1.45148 -0.10555 0.02513  -0.01627 173 ARG A CA  
1090 C C   . ARG A 137 ? 0.60117 0.66997 1.38451 -0.11416 -0.00361 -0.03735 173 ARG A C   
1091 O O   . ARG A 137 ? 0.63792 0.72000 1.39070 -0.11559 -0.03913 -0.06826 173 ARG A O   
1092 C CB  . ARG A 137 ? 0.70731 0.72951 1.54007 -0.11211 0.04483  -0.01228 173 ARG A CB  
1093 C CG  . ARG A 137 ? 0.61323 0.61472 1.42121 -0.09926 0.08220  0.02472  173 ARG A CG  
1094 C CD  . ARG A 137 ? 0.64387 0.62129 1.51775 -0.09810 0.09963  0.02798  173 ARG A CD  
1095 N NE  . ARG A 137 ? 0.73950 0.71861 1.68032 -0.09432 0.11444  0.03966  173 ARG A NE  
1096 C CZ  . ARG A 137 ? 0.65600 0.63186 1.60840 -0.08059 0.15198  0.08287  173 ARG A CZ  
1097 N NH1 . ARG A 137 ? 0.72511 0.69856 1.62033 -0.06829 0.17715  0.11883  173 ARG A NH1 
1098 N NH2 . ARG A 137 ? 0.57497 0.55186 1.59667 -0.07745 0.16432  0.08979  173 ARG A NH2 
1099 N N   . ARG A 138 ? 0.71118 0.78724 1.54806 -0.11444 0.01316  -0.01759 174 ARG A N   
1100 C CA  . ARG A 138 ? 0.69228 0.79273 1.55172 -0.11611 -0.01088 -0.03032 174 ARG A CA  
1101 C C   . ARG A 138 ? 0.67280 0.77749 1.57598 -0.12245 -0.04312 -0.06800 174 ARG A C   
1102 O O   . ARG A 138 ? 0.77636 0.86161 1.71875 -0.12479 -0.03585 -0.07768 174 ARG A O   
1103 C CB  . ARG A 138 ? 0.72230 0.82434 1.61794 -0.10951 0.01886  0.00094  174 ARG A CB  
1104 C CG  . ARG A 138 ? 0.82153 0.93068 1.66877 -0.10190 0.04034  0.02859  174 ARG A CG  
1105 C CD  . ARG A 138 ? 0.85561 0.99054 1.70541 -0.10087 0.02093  0.02353  174 ARG A CD  
1106 N NE  . ARG A 138 ? 0.89848 1.03878 1.69632 -0.09328 0.03851  0.04325  174 ARG A NE  
1107 C CZ  . ARG A 138 ? 0.82573 0.95984 1.62043 -0.08411 0.07683  0.07142  174 ARG A CZ  
1108 N NH1 . ARG A 138 ? 0.83748 0.95933 1.67395 -0.07926 0.10216  0.08740  174 ARG A NH1 
1109 N NH2 . ARG A 138 ? 0.79932 0.93217 1.52576 -0.07353 0.08794  0.08057  174 ARG A NH2 
1110 N N   . GLY A 139 ? 0.64232 0.77460 1.53930 -0.12349 -0.07877 -0.08886 175 GLY A N   
1111 C CA  . GLY A 139 ? 0.73342 0.87682 1.66144 -0.12770 -0.11412 -0.12746 175 GLY A CA  
1112 C C   . GLY A 139 ? 0.67967 0.81748 1.56769 -0.12945 -0.13839 -0.16348 175 GLY A C   
1113 O O   . GLY A 139 ? 0.75703 0.90915 1.65383 -0.13059 -0.17230 -0.20001 175 GLY A O   
1114 N N   . ALA A 140 ? 0.69899 0.81739 1.54217 -0.12852 -0.12200 -0.15550 176 ALA A N   
1115 C CA  . ALA A 140 ? 0.67005 0.78020 1.47393 -0.12846 -0.14111 -0.18959 176 ALA A CA  
1116 C C   . ALA A 140 ? 0.81097 0.94859 1.54228 -0.12209 -0.17586 -0.20726 176 ALA A C   
1117 O O   . ALA A 140 ? 0.74450 0.90118 1.44612 -0.11619 -0.17721 -0.18418 176 ALA A O   
1118 C CB  . ALA A 140 ? 0.76140 0.84082 1.54825 -0.12861 -0.10968 -0.17260 176 ALA A CB  
1119 N N   . THR A 141 ? 0.94184 1.07927 1.63630 -0.11870 -0.20018 -0.24578 177 THR A N   
1120 C CA  . THR A 141 ? 0.97124 1.13277 1.58197 -0.10640 -0.22906 -0.25970 177 THR A CA  
1121 C C   . THR A 141 ? 0.91855 1.06514 1.44133 -0.09377 -0.20165 -0.22449 177 THR A C   
1122 O O   . THR A 141 ? 1.07695 1.24193 1.53193 -0.08105 -0.21279 -0.21529 177 THR A O   
1123 C CB  . THR A 141 ? 1.00446 1.16657 1.58875 -0.10219 -0.25504 -0.30829 177 THR A CB  
1124 O OG1 . THR A 141 ? 1.06097 1.21998 1.71514 -0.10944 -0.26144 -0.32955 177 THR A OG1 
1125 C CG2 . THR A 141 ? 1.08177 1.27902 1.58914 -0.08653 -0.28996 -0.32269 177 THR A CG2 
1126 N N   . ASP A 142 ? 0.75800 0.87355 1.28493 -0.09630 -0.16637 -0.20363 178 ASP A N   
1127 C CA  . ASP A 142 ? 0.79387 0.89726 1.24988 -0.08615 -0.14105 -0.17211 178 ASP A CA  
1128 C C   . ASP A 142 ? 0.70129 0.79659 1.18186 -0.08887 -0.11026 -0.13187 178 ASP A C   
1129 O O   . ASP A 142 ? 0.69655 0.77315 1.15518 -0.08534 -0.08312 -0.11026 178 ASP A O   
1130 C CB  . ASP A 142 ? 0.78834 0.86743 1.21668 -0.08247 -0.12821 -0.18268 178 ASP A CB  
1131 C CG  . ASP A 142 ? 0.73499 0.78892 1.23591 -0.09191 -0.10885 -0.18314 178 ASP A CG  
1132 O OD1 . ASP A 142 ? 0.78599 0.84298 1.36431 -0.10300 -0.11137 -0.18592 178 ASP A OD1 
1133 O OD2 . ASP A 142 ? 0.79488 0.82675 1.28057 -0.08741 -0.08963 -0.17831 178 ASP A OD2 
1134 N N   . GLU A 143 ? 0.62629 0.73835 1.15243 -0.09352 -0.11476 -0.12233 179 GLU A N   
1135 C CA  . GLU A 143 ? 0.58756 0.69338 1.13930 -0.09457 -0.08390 -0.08699 179 GLU A CA  
1136 C C   . GLU A 143 ? 0.59492 0.69725 1.07319 -0.08418 -0.06698 -0.06204 179 GLU A C   
1137 O O   . GLU A 143 ? 0.62356 0.71119 1.09247 -0.08151 -0.03842 -0.03948 179 GLU A O   
1138 C CB  . GLU A 143 ? 0.65020 0.77796 1.26385 -0.09971 -0.09291 -0.08349 179 GLU A CB  
1139 C CG  . GLU A 143 ? 0.66218 0.78636 1.29549 -0.09783 -0.05956 -0.04782 179 GLU A CG  
1140 C CD  . GLU A 143 ? 0.61792 0.76525 1.31810 -0.10179 -0.06676 -0.04402 179 GLU A CD  
1141 O OE1 . GLU A 143 ? 0.51597 0.68089 1.26885 -0.10933 -0.09636 -0.06945 179 GLU A OE1 
1142 O OE2 . GLU A 143 ? 0.69857 0.84819 1.39982 -0.09663 -0.04364 -0.01763 179 GLU A OE2 
1143 N N   . ASN A 144 ? 0.51712 0.63430 0.94523 -0.07733 -0.08433 -0.06554 180 ASN A N   
1144 C CA  . ASN A 144 ? 0.59566 0.71000 0.96593 -0.06924 -0.06945 -0.04493 180 ASN A CA  
1145 C C   . ASN A 144 ? 0.60441 0.71331 0.91072 -0.06279 -0.07405 -0.05304 180 ASN A C   
1146 O O   . ASN A 144 ? 0.61826 0.72829 0.88081 -0.05664 -0.06682 -0.04008 180 ASN A O   
1147 C CB  . ASN A 144 ? 0.51431 0.64693 0.88540 -0.06512 -0.07731 -0.03470 180 ASN A CB  
1148 C CG  . ASN A 144 ? 0.58089 0.71938 1.01631 -0.06985 -0.06691 -0.02301 180 ASN A CG  
1149 O OD1 . ASN A 144 ? 0.65900 0.78623 1.10133 -0.06975 -0.03878 -0.00506 180 ASN A OD1 
1150 N ND2 . ASN A 144 ? 0.63769 0.79672 1.12057 -0.07258 -0.08967 -0.03344 180 ASN A ND2 
1151 N N   . ASN A 145 ? 0.62332 0.72597 0.92883 -0.06398 -0.08415 -0.07502 181 ASN A N   
1152 C CA  . ASN A 145 ? 0.66581 0.76214 0.91591 -0.05687 -0.08309 -0.08164 181 ASN A CA  
1153 C C   . ASN A 145 ? 0.66448 0.74308 0.90750 -0.05654 -0.05758 -0.06646 181 ASN A C   
1154 O O   . ASN A 145 ? 0.61882 0.68681 0.90186 -0.06110 -0.04362 -0.05800 181 ASN A O   
1155 C CB  . ASN A 145 ? 0.65612 0.75262 0.90690 -0.05621 -0.10264 -0.11445 181 ASN A CB  
1156 C CG  . ASN A 145 ? 0.74039 0.86081 0.97376 -0.05082 -0.13179 -0.13082 181 ASN A CG  
1157 O OD1 . ASN A 145 ? 0.75451 0.88951 0.96065 -0.04423 -0.13441 -0.11304 181 ASN A OD1 
1158 N ND2 . ASN A 145 ? 0.74876 0.87432 0.99877 -0.05229 -0.15436 -0.16540 181 ASN A ND2 
1159 N N   . VAL A 146 ? 0.60929 0.68708 0.80363 -0.04975 -0.05118 -0.06121 182 VAL A N   
1160 C CA  . VAL A 146 ? 0.53864 0.60632 0.72376 -0.04760 -0.03113 -0.04692 182 VAL A CA  
1161 C C   . VAL A 146 ? 0.55628 0.61086 0.75138 -0.04576 -0.02867 -0.05981 182 VAL A C   
1162 O O   . VAL A 146 ? 0.57028 0.62466 0.75211 -0.04308 -0.04056 -0.08177 182 VAL A O   
1163 C CB  . VAL A 146 ? 0.58303 0.65793 0.72406 -0.04241 -0.02567 -0.03681 182 VAL A CB  
1164 C CG1 . VAL A 146 ? 0.52878 0.59975 0.66402 -0.03997 -0.00953 -0.02389 182 VAL A CG1 
1165 C CG2 . VAL A 146 ? 0.50826 0.59288 0.64636 -0.04389 -0.02758 -0.02654 182 VAL A CG2 
1166 N N   . HIS A 147 ? 0.53080 0.57476 0.74851 -0.04514 -0.01203 -0.04567 183 HIS A N   
1167 C CA  . HIS A 147 ? 0.60065 0.62987 0.83442 -0.04148 -0.00472 -0.05174 183 HIS A CA  
1168 C C   . HIS A 147 ? 0.55322 0.58427 0.76492 -0.03292 0.01052  -0.03075 183 HIS A C   
1169 O O   . HIS A 147 ? 0.62515 0.66792 0.81612 -0.03142 0.01528  -0.01345 183 HIS A O   
1170 C CB  . HIS A 147 ? 0.55109 0.56562 0.84733 -0.04680 0.00218  -0.05096 183 HIS A CB  
1171 C CG  . HIS A 147 ? 0.57129 0.58855 0.90168 -0.05664 -0.01511 -0.07261 183 HIS A CG  
1172 N ND1 . HIS A 147 ? 0.64606 0.67709 0.98394 -0.06168 -0.02066 -0.06455 183 HIS A ND1 
1173 C CD2 . HIS A 147 ? 0.56775 0.57815 0.93018 -0.06181 -0.02979 -0.10443 183 HIS A CD2 
1174 C CE1 . HIS A 147 ? 0.65549 0.69073 1.03048 -0.06939 -0.03929 -0.08803 183 HIS A CE1 
1175 N NE2 . HIS A 147 ? 0.61214 0.63560 1.00144 -0.07007 -0.04654 -0.11453 183 HIS A NE2 
1176 N N   . LEU A 148 ? 0.56403 0.58476 0.78333 -0.02658 0.01717  -0.03447 184 LEU A N   
1177 C CA  . LEU A 148 ? 0.54225 0.56817 0.74819 -0.01664 0.02927  -0.01455 184 LEU A CA  
1178 C C   . LEU A 148 ? 0.60491 0.61427 0.85254 -0.01047 0.04374  -0.00306 184 LEU A C   
1179 O O   . LEU A 148 ? 0.62794 0.61931 0.90488 -0.01158 0.04399  -0.02166 184 LEU A O   
1180 C CB  . LEU A 148 ? 0.55819 0.59201 0.73180 -0.01130 0.02582  -0.02554 184 LEU A CB  
1181 C CG  . LEU A 148 ? 0.53540 0.58025 0.70152 -0.00109 0.03493  -0.00719 184 LEU A CG  
1182 C CD1 . LEU A 148 ? 0.51303 0.57651 0.66281 -0.00145 0.03426  0.01192  184 LEU A CD1 
1183 C CD2 . LEU A 148 ? 0.58524 0.63791 0.73008 0.00355  0.03432  -0.01868 184 LEU A CD2 
1184 N N   . ILE A 149 ? 0.51763 0.53329 0.76830 -0.00250 0.05631  0.02727  185 ILE A N   
1185 C CA  . ILE A 149 ? 0.65346 0.65514 0.94397 0.00694  0.07386  0.04806  185 ILE A CA  
1186 C C   . ILE A 149 ? 0.71043 0.72945 0.97750 0.02297  0.07975  0.07289  185 ILE A C   
1187 O O   . ILE A 149 ? 0.63873 0.67993 0.86484 0.02408  0.06910  0.06945  185 ILE A O   
1188 C CB  . ILE A 149 ? 0.71753 0.71095 1.04394 0.00421  0.08682  0.06741  185 ILE A CB  
1189 C CG1 . ILE A 149 ? 0.68223 0.69704 0.97158 0.00502  0.08627  0.08322  185 ILE A CG1 
1190 C CG2 . ILE A 149 ? 0.68097 0.65751 1.04951 -0.01124 0.07989  0.04078  185 ILE A CG2 
1191 C CD1 . ILE A 149 ? 0.75489 0.78359 1.02603 0.02255  0.10070  0.11895  185 ILE A CD1 
1192 N N   . ASP A 150 ? 0.69120 0.70092 0.99059 0.03600  0.09666  0.09840  186 ASP A N   
1193 C CA  . ASP A 150 ? 0.73179 0.76151 1.01450 0.05495  0.10172  0.12739  186 ASP A CA  
1194 C C   . ASP A 150 ? 0.76010 0.80224 1.02582 0.05869  0.09108  0.11222  186 ASP A C   
1195 O O   . ASP A 150 ? 0.66426 0.73029 0.89130 0.05494  0.07661  0.10197  186 ASP A O   
1196 C CB  . ASP A 150 ? 0.78613 0.84341 1.02661 0.05975  0.09806  0.14569  186 ASP A CB  
1197 C CG  . ASP A 150 ? 0.93551 1.01350 1.16552 0.08312  0.10574  0.18239  186 ASP A CG  
1198 O OD1 . ASP A 150 ? 1.00746 1.09815 1.23671 0.09360  0.10013  0.18515  186 ASP A OD1 
1199 O OD2 . ASP A 150 ? 1.17166 1.25559 1.39400 0.09287  0.11796  0.20991  186 ASP A OD2 
1200 N N   . PHE A 151 ? 0.73528 0.76088 1.03586 0.06657  0.10061  0.11131  187 PHE A N   
1201 C CA  . PHE A 151 ? 0.70591 0.74160 0.99942 0.07231  0.09575  0.09881  187 PHE A CA  
1202 C C   . PHE A 151 ? 0.77860 0.82776 1.09040 0.09451  0.10462  0.13095  187 PHE A C   
1203 O O   . PHE A 151 ? 0.76015 0.80461 1.09446 0.10321  0.11053  0.12608  187 PHE A O   
1204 C CB  . PHE A 151 ? 0.67088 0.67819 0.98625 0.06490  0.09908  0.06496  187 PHE A CB  
1205 C CG  . PHE A 151 ? 0.73724 0.74032 1.02653 0.04673  0.08578  0.03270  187 PHE A CG  
1206 C CD1 . PHE A 151 ? 0.67952 0.70018 0.92949 0.04264  0.07506  0.01545  187 PHE A CD1 
1207 C CD2 . PHE A 151 ? 0.70616 0.68971 1.01496 0.03488  0.08473  0.02217  187 PHE A CD2 
1208 C CE1 . PHE A 151 ? 0.71375 0.73239 0.93852 0.02939  0.06369  -0.00890 187 PHE A CE1 
1209 C CE2 . PHE A 151 ? 0.69283 0.67710 0.97839 0.02064  0.06998  -0.00546 187 PHE A CE2 
1210 C CZ  . PHE A 151 ? 0.60651 0.60829 0.84703 0.01905  0.05950  -0.01956 187 PHE A CZ  
1211 N N   . GLY A 152 ? 0.81315 0.88145 1.11403 0.10625  0.10605  0.16518  188 GLY A N   
1212 C CA  . GLY A 152 ? 0.83940 0.92717 1.15283 0.13079  0.11158  0.20021  188 GLY A CA  
1213 C C   . GLY A 152 ? 0.86515 0.99317 1.15529 0.13747  0.09369  0.19648  188 GLY A C   
1214 O O   . GLY A 152 ? 0.80542 0.95143 1.11416 0.15819  0.09590  0.22061  188 GLY A O   
1215 N N   . MET A 153 ? 0.78472 0.92808 1.04152 0.12082  0.07664  0.16802  189 MET A N   
1216 C CA  . MET A 153 ? 0.71517 0.89648 0.96029 0.12327  0.06011  0.16051  189 MET A CA  
1217 C C   . MET A 153 ? 0.70344 0.87427 0.96228 0.11287  0.06263  0.13179  189 MET A C   
1218 O O   . MET A 153 ? 0.63843 0.83851 0.89596 0.11207  0.05223  0.12366  189 MET A O   
1219 C CB  . MET A 153 ? 0.79350 1.00271 0.99682 0.11379  0.04119  0.15161  189 MET A CB  
1220 C CG  . MET A 153 ? 0.85329 1.08024 1.03301 0.12796  0.03846  0.17879  189 MET A CG  
1221 S SD  . MET A 153 ? 1.15566 1.44013 1.32913 0.15185  0.01897  0.19887  189 MET A SD  
1222 C CE  . MET A 153 ? 0.95543 1.24056 1.11906 0.17977  0.03323  0.24743  189 MET A CE  
1223 N N   . ALA A 154 ? 0.64337 0.77495 0.91689 0.10583  0.07670  0.11566  190 ALA A N   
1224 C CA  . ALA A 154 ? 0.69313 0.81466 0.97010 0.09892  0.08120  0.08770  190 ALA A CA  
1225 C C   . ALA A 154 ? 0.67909 0.80874 0.99103 0.11622  0.09148  0.09598  190 ALA A C   
1226 O O   . ALA A 154 ? 0.67707 0.80344 1.01983 0.13300  0.09992  0.12021  190 ALA A O   
1227 C CB  . ALA A 154 ? 0.64865 0.72930 0.92725 0.08834  0.08984  0.06388  190 ALA A CB  
1228 N N   . LYS A 155 ? 0.62047 0.76108 0.93067 0.11355  0.09330  0.07834  191 LYS A N   
1229 C CA  . LYS A 155 ? 0.66698 0.81821 1.01302 0.12975  0.10499  0.08413  191 LYS A CA  
1230 C C   . LYS A 155 ? 0.67343 0.81115 1.01209 0.12493  0.11825  0.05526  191 LYS A C   
1231 O O   . LYS A 155 ? 0.64248 0.78302 0.94751 0.11041  0.11272  0.03874  191 LYS A O   
1232 C CB  . LYS A 155 ? 0.60333 0.80465 0.96211 0.13742  0.09091  0.10396  191 LYS A CB  
1233 C CG  . LYS A 155 ? 0.74816 0.96809 1.15008 0.15331  0.10193  0.10987  191 LYS A CG  
1234 C CD  . LYS A 155 ? 0.76132 1.03646 1.18260 0.16034  0.08258  0.12825  191 LYS A CD  
1235 C CE  . LYS A 155 ? 0.88642 1.17783 1.30836 0.17507  0.06856  0.15855  191 LYS A CE  
1236 N NZ  . LYS A 155 ? 0.83152 1.18238 1.26764 0.18353  0.04394  0.17250  191 LYS A NZ  
1237 N N   . GLN A 156 ? 0.66916 0.79188 1.03858 0.13929  0.13765  0.05057  192 GLN A N   
1238 C CA  . GLN A 156 ? 0.72377 0.83656 1.08342 0.13997  0.15398  0.02416  192 GLN A CA  
1239 C C   . GLN A 156 ? 0.68569 0.83857 1.05028 0.14060  0.15419  0.03175  192 GLN A C   
1240 O O   . GLN A 156 ? 0.74286 0.92595 1.14698 0.15172  0.15256  0.05349  192 GLN A O   
1241 C CB  . GLN A 156 ? 0.78551 0.87180 1.18115 0.15721  0.17659  0.01597  192 GLN A CB  
1242 C CG  . GLN A 156 ? 0.81439 0.89488 1.20046 0.16376  0.19742  -0.00977 192 GLN A CG  
1243 C CD  . GLN A 156 ? 0.90668 0.95671 1.32868 0.18112  0.22072  -0.02350 192 GLN A CD  
1244 O OE1 . GLN A 156 ? 0.89851 0.95697 1.34125 0.19622  0.24148  -0.02611 192 GLN A OE1 
1245 N NE2 . GLN A 156 ? 0.98847 1.00212 1.42384 0.17905  0.21939  -0.03294 192 GLN A NE2 
1246 N N   . TYR A 157 ? 0.70954 0.86468 1.03894 0.12939  0.15627  0.01549  193 TYR A N   
1247 C CA  . TYR A 157 ? 0.68611 0.87660 1.02718 0.12771  0.16002  0.02300  193 TYR A CA  
1248 C C   . TYR A 157 ? 0.73220 0.91909 1.07681 0.13918  0.18907  0.01144  193 TYR A C   
1249 O O   . TYR A 157 ? 0.73315 0.94950 1.09891 0.13976  0.19829  0.02046  193 TYR A O   
1250 C CB  . TYR A 157 ? 0.49661 0.69588 0.80336 0.10839  0.14567  0.02020  193 TYR A CB  
1251 C CG  . TYR A 157 ? 0.65748 0.83189 0.91537 0.10326  0.15576  0.00015  193 TYR A CG  
1252 C CD1 . TYR A 157 ? 0.70577 0.84949 0.92825 0.09748  0.14633  -0.01498 193 TYR A CD1 
1253 C CD2 . TYR A 157 ? 0.61789 0.80258 0.86711 0.10562  0.17484  -0.00185 193 TYR A CD2 
1254 C CE1 . TYR A 157 ? 0.68244 0.80935 0.85905 0.09484  0.15116  -0.03395 193 TYR A CE1 
1255 C CE2 . TYR A 157 ? 0.67521 0.84144 0.87339 0.10499  0.18330  -0.01698 193 TYR A CE2 
1256 C CZ  . TYR A 157 ? 0.72472 0.86359 0.88506 0.09989  0.16914  -0.03418 193 TYR A CZ  
1257 O OH  . TYR A 157 ? 0.70814 0.83430 0.81655 0.10121  0.17341  -0.04992 193 TYR A OH  
1258 N N   . ARG A 158 ? 0.69857 0.85104 1.02546 0.14859  0.20476  -0.00962 194 ARG A N   
1259 C CA  . ARG A 158 ? 0.74849 0.89658 1.07100 0.16283  0.23476  -0.02352 194 ARG A CA  
1260 C C   . ARG A 158 ? 0.83642 0.94796 1.16268 0.17653  0.24784  -0.04597 194 ARG A C   
1261 O O   . ARG A 158 ? 0.91789 1.00176 1.23477 0.17015  0.23350  -0.05736 194 ARG A O   
1262 C CB  . ARG A 158 ? 0.85003 0.99618 1.11535 0.15636  0.24135  -0.03655 194 ARG A CB  
1263 C CG  . ARG A 158 ? 0.81945 0.93383 1.02884 0.14897  0.22823  -0.06226 194 ARG A CG  
1264 C CD  . ARG A 158 ? 0.85329 0.97204 1.00573 0.14695  0.23471  -0.06942 194 ARG A CD  
1265 N NE  . ARG A 158 ? 0.91103 1.00475 1.01140 0.14217  0.21962  -0.09595 194 ARG A NE  
1266 C CZ  . ARG A 158 ? 0.93999 1.03584 0.98360 0.14215  0.21947  -0.10348 194 ARG A CZ  
1267 N NH1 . ARG A 158 ? 0.92467 1.04277 0.95528 0.14661  0.23736  -0.08388 194 ARG A NH1 
1268 N NH2 . ARG A 158 ? 0.93581 1.01259 0.93907 0.13849  0.20134  -0.12972 194 ARG A NH2 
1269 N N   . ASP A 159 ? 0.92200 1.03324 1.26768 0.19530  0.27694  -0.05307 195 ASP A N   
1270 C CA  . ASP A 159 ? 0.92471 1.00024 1.28217 0.21003  0.29286  -0.07789 195 ASP A CA  
1271 C C   . ASP A 159 ? 1.01888 1.06121 1.31463 0.20449  0.28860  -0.11792 195 ASP A C   
1272 O O   . ASP A 159 ? 1.05194 1.10214 1.29230 0.20357  0.29380  -0.13004 195 ASP A O   
1273 C CB  . ASP A 159 ? 0.98320 1.06730 1.36981 0.23255  0.32803  -0.07956 195 ASP A CB  
1274 C CG  . ASP A 159 ? 1.01510 1.06048 1.41929 0.24910  0.34711  -0.10833 195 ASP A CG  
1275 O OD1 . ASP A 159 ? 1.06941 1.10541 1.53282 0.25544  0.34554  -0.09414 195 ASP A OD1 
1276 O OD2 . ASP A 159 ? 1.11905 1.14348 1.47790 0.25696  0.36380  -0.14552 195 ASP A OD2 
1277 N N   . PRO A 160 ? 1.07962 1.08671 1.38619 0.20155  0.27909  -0.13834 196 PRO A N   
1278 C CA  . PRO A 160 ? 1.08284 1.06296 1.33704 0.19466  0.26927  -0.18020 196 PRO A CA  
1279 C C   . PRO A 160 ? 1.17844 1.14714 1.39592 0.21223  0.29313  -0.21910 196 PRO A C   
1280 O O   . PRO A 160 ? 1.24196 1.19527 1.40766 0.20913  0.28288  -0.25714 196 PRO A O   
1281 C CB  . PRO A 160 ? 1.10160 1.04752 1.40029 0.18871  0.25839  -0.19019 196 PRO A CB  
1282 C CG  . PRO A 160 ? 1.04265 1.00423 1.39988 0.18911  0.25595  -0.14257 196 PRO A CG  
1283 C CD  . PRO A 160 ? 1.01753 1.01030 1.38872 0.20412  0.27566  -0.12139 196 PRO A CD  
1284 N N   . ARG A 161 ? 1.17542 1.15318 1.41787 0.23201  0.32417  -0.21204 197 ARG A N   
1285 C CA  . ARG A 161 ? 1.18962 1.15561 1.39763 0.25259  0.35194  -0.24989 197 ARG A CA  
1286 C C   . ARG A 161 ? 1.23471 1.23516 1.41154 0.26454  0.37636  -0.23031 197 ARG A C   
1287 O O   . ARG A 161 ? 1.35564 1.35815 1.46130 0.27319  0.38543  -0.25390 197 ARG A O   
1288 C CB  . ARG A 161 ? 1.20795 1.14664 1.47770 0.27019  0.37603  -0.26630 197 ARG A CB  
1289 C CG  . ARG A 161 ? 1.37272 1.29859 1.60920 0.29404  0.40762  -0.30802 197 ARG A CG  
1290 C CD  . ARG A 161 ? 1.44762 1.33274 1.72457 0.29815  0.40551  -0.33752 197 ARG A CD  
1291 N NE  . ARG A 161 ? 1.55333 1.42843 1.79026 0.31804  0.42359  -0.37389 197 ARG A NE  
1292 C CZ  . ARG A 161 ? 1.57446 1.43516 1.73775 0.32095  0.41400  -0.42313 197 ARG A CZ  
1293 N NH1 . ARG A 161 ? 1.51592 1.37377 1.64072 0.30361  0.38634  -0.44026 197 ARG A NH1 
1294 N NH2 . ARG A 161 ? 1.58085 1.43124 1.70820 0.34243  0.43049  -0.45594 197 ARG A NH2 
1295 N N   . THR A 162 ? 1.18269 1.21266 1.41304 0.26600  0.38707  -0.18672 198 THR A N   
1296 C CA  . THR A 162 ? 1.12147 1.18578 1.34064 0.27573  0.41311  -0.16391 198 THR A CA  
1297 C C   . THR A 162 ? 1.11770 1.20959 1.30883 0.25680  0.39406  -0.13584 198 THR A C   
1298 O O   . THR A 162 ? 1.15384 1.27130 1.33043 0.26336  0.41656  -0.11798 198 THR A O   
1299 C CB  . THR A 162 ? 1.03292 1.11905 1.33640 0.28703  0.43435  -0.13351 198 THR A CB  
1300 O OG1 . THR A 162 ? 0.94865 1.05697 1.30211 0.26896  0.40549  -0.09739 198 THR A OG1 
1301 C CG2 . THR A 162 ? 1.04056 1.09713 1.38095 0.30171  0.44486  -0.15530 198 THR A CG2 
1302 N N   . LYS A 163 ? 1.06297 1.14949 1.25169 0.23443  0.35643  -0.13028 199 LYS A N   
1303 C CA  . LYS A 163 ? 1.07198 1.18060 1.23855 0.21568  0.33693  -0.10646 199 LYS A CA  
1304 C C   . LYS A 163 ? 0.99562 1.14265 1.21710 0.21279  0.34682  -0.06714 199 LYS A C   
1305 O O   . LYS A 163 ? 0.98147 1.14952 1.18725 0.20540  0.34978  -0.04903 199 LYS A O   
1306 C CB  . LYS A 163 ? 1.13931 1.24580 1.22393 0.21952  0.34268  -0.12155 199 LYS A CB  
1307 C CG  . LYS A 163 ? 1.16003 1.23639 1.19206 0.21654  0.32052  -0.16071 199 LYS A CG  
1308 C CD  . LYS A 163 ? 1.12908 1.19967 1.17624 0.19190  0.28205  -0.15278 199 LYS A CD  
1309 C CE  . LYS A 163 ? 1.09538 1.13234 1.14089 0.18888  0.26401  -0.18966 199 LYS A CE  
1310 N NZ  . LYS A 163 ? 1.22093 1.23991 1.30870 0.20458  0.28553  -0.20578 199 LYS A NZ  
1311 N N   . GLN A 164 ? 0.90600 1.06352 1.19806 0.21883  0.35122  -0.05359 200 GLN A N   
1312 C CA  . GLN A 164 ? 0.86808 1.06663 1.22325 0.21567  0.35521  -0.02004 200 GLN A CA  
1313 C C   . GLN A 164 ? 0.78963 1.00285 1.17135 0.19516  0.31615  -0.00251 200 GLN A C   
1314 O O   . GLN A 164 ? 0.85652 1.05600 1.25303 0.19431  0.29659  -0.00457 200 GLN A O   
1315 C CB  . GLN A 164 ? 0.88100 1.09084 1.30199 0.23593  0.37973  -0.01299 200 GLN A CB  
1316 C CG  . GLN A 164 ? 0.82571 1.08197 1.32469 0.23110  0.37330  0.01971  200 GLN A CG  
1317 C CD  . GLN A 164 ? 0.92205 1.19727 1.46588 0.24658  0.40429  0.02930  200 GLN A CD  
1318 O OE1 . GLN A 164 ? 1.04473 1.29608 1.57724 0.26339  0.42478  0.01353  200 GLN A OE1 
1319 N NE2 . GLN A 164 ? 0.96829 1.28196 1.55759 0.23605  0.40046  0.05256  200 GLN A NE2 
1320 N N   . HIS A 165 ? 0.81042 1.05131 1.19988 0.18005  0.30727  0.01495  201 HIS A N   
1321 C CA  . HIS A 165 ? 0.74483 1.00156 1.15249 0.16103  0.27075  0.02720  201 HIS A CA  
1322 C C   . HIS A 165 ? 0.71604 1.00104 1.19461 0.16710  0.25926  0.04377  201 HIS A C   
1323 O O   . HIS A 165 ? 0.69641 1.00266 1.22713 0.18130  0.28027  0.05297  201 HIS A O   
1324 C CB  . HIS A 165 ? 0.73603 1.01559 1.14521 0.14465  0.26784  0.03865  201 HIS A CB  
1325 C CG  . HIS A 165 ? 0.71712 1.00029 1.11650 0.12409  0.23156  0.04061  201 HIS A CG  
1326 N ND1 . HIS A 165 ? 0.64788 0.95942 1.09438 0.11764  0.20549  0.05079  201 HIS A ND1 
1327 C CD2 . HIS A 165 ? 0.59444 0.85863 0.94177 0.11035  0.21774  0.03327  201 HIS A CD2 
1328 C CE1 . HIS A 165 ? 0.64123 0.94896 1.06170 0.10094  0.17905  0.04778  201 HIS A CE1 
1329 N NE2 . HIS A 165 ? 0.59235 0.87081 0.95640 0.09574  0.18670  0.03808  201 HIS A NE2 
1330 N N   . ILE A 166 ? 0.65991 0.94748 1.13970 0.15822  0.22616  0.04914  202 ILE A N   
1331 C CA  . ILE A 166 ? 0.69235 1.01074 1.23030 0.16603  0.20963  0.06751  202 ILE A CA  
1332 C C   . ILE A 166 ? 0.65621 1.02545 1.24905 0.15951  0.20422  0.08000  202 ILE A C   
1333 O O   . ILE A 166 ? 0.63669 1.01243 1.21682 0.14300  0.20421  0.07561  202 ILE A O   
1334 C CB  . ILE A 166 ? 0.63328 0.94462 1.14985 0.15954  0.17708  0.07234  202 ILE A CB  
1335 C CG1 . ILE A 166 ? 0.67674 0.98830 1.15185 0.13661  0.15688  0.06515  202 ILE A CG1 
1336 C CG2 . ILE A 166 ? 0.60976 0.87481 1.09964 0.16893  0.18550  0.06380  202 ILE A CG2 
1337 C CD1 . ILE A 166 ? 0.58111 0.89074 1.03546 0.13113  0.12726  0.07113  202 ILE A CD1 
1338 N N   . PRO A 167 ? 0.61216 1.01916 1.27250 0.17207  0.19973  0.09561  203 PRO A N   
1339 C CA  . PRO A 167 ? 0.64936 1.10892 1.37263 0.16412  0.19109  0.10387  203 PRO A CA  
1340 C C   . PRO A 167 ? 0.59929 1.08127 1.31369 0.14504  0.15053  0.10120  203 PRO A C   
1341 O O   . PRO A 167 ? 0.51610 0.98590 1.19046 0.14472  0.12584  0.10123  203 PRO A O   
1342 C CB  . PRO A 167 ? 0.56177 1.05590 1.35748 0.18564  0.19217  0.12061  203 PRO A CB  
1343 C CG  . PRO A 167 ? 0.66747 1.13265 1.43301 0.20077  0.18489  0.12561  203 PRO A CG  
1344 C CD  . PRO A 167 ? 0.62406 1.02882 1.31395 0.19497  0.20313  0.10687  203 PRO A CD  
1345 N N   . TYR A 168 ? 0.57348 1.08795 1.32910 0.12951  0.14639  0.09825  204 TYR A N   
1346 C CA  . TYR A 168 ? 0.50624 1.04633 1.26455 0.11105  0.10883  0.09020  204 TYR A CA  
1347 C C   . TYR A 168 ? 0.58053 1.17436 1.39157 0.12065  0.07484  0.09761  204 TYR A C   
1348 O O   . TYR A 168 ? 0.45619 1.08751 1.34089 0.13127  0.08136  0.10722  204 TYR A O   
1349 C CB  . TYR A 168 ? 0.43944 0.99252 1.23349 0.09066  0.11933  0.08265  204 TYR A CB  
1350 C CG  . TYR A 168 ? 0.41181 0.99838 1.23149 0.07136  0.08170  0.06936  204 TYR A CG  
1351 C CD1 . TYR A 168 ? 0.51495 1.07723 1.27251 0.05758  0.06264  0.05635  204 TYR A CD1 
1352 C CD2 . TYR A 168 ? 0.44357 1.08719 1.35355 0.06699  0.06527  0.06688  204 TYR A CD2 
1353 C CE1 . TYR A 168 ? 0.49544 1.08661 1.27485 0.04100  0.02964  0.03953  204 TYR A CE1 
1354 C CE2 . TYR A 168 ? 0.42282 1.09771 1.35756 0.04914  0.02880  0.04786  204 TYR A CE2 
1355 C CZ  . TYR A 168 ? 0.50575 1.15276 1.37236 0.03663  0.01196  0.03336  204 TYR A CZ  
1356 O OH  . TYR A 168 ? 0.54061 1.21700 1.42992 0.01991  -0.02314 0.00999  204 TYR A OH  
1357 N N   . ARG A 169 ? 0.58635 1.18629 1.35879 0.11920  0.03908  0.09445  205 ARG A N   
1358 C CA  . ARG A 169 ? 0.51043 1.16614 1.32001 0.12988  0.00131  0.10071  205 ARG A CA  
1359 C C   . ARG A 169 ? 0.56687 1.23832 1.34386 0.11418  -0.03633 0.08287  205 ARG A C   
1360 O O   . ARG A 169 ? 0.57942 1.21354 1.30449 0.09695  -0.03096 0.06915  205 ARG A O   
1361 C CB  . ARG A 169 ? 0.56210 1.21152 1.35344 0.15783  -0.00024 0.12416  205 ARG A CB  
1362 C CG  . ARG A 169 ? 0.67521 1.27538 1.38181 0.15917  -0.00021 0.12659  205 ARG A CG  
1363 C CD  . ARG A 169 ? 0.73960 1.34246 1.43991 0.18702  -0.00641 0.15353  205 ARG A CD  
1364 N NE  . ARG A 169 ? 0.79703 1.44988 1.49270 0.19581  -0.04782 0.16162  205 ARG A NE  
1365 C CZ  . ARG A 169 ? 0.90209 1.56573 1.58641 0.22173  -0.05838 0.18963  205 ARG A CZ  
1366 N NH1 . ARG A 169 ? 0.95919 1.58430 1.64457 0.23972  -0.03012 0.21182  205 ARG A NH1 
1367 N NH2 . ARG A 169 ? 0.91534 1.62978 1.58749 0.23109  -0.09749 0.19536  205 ARG A NH2 
1368 N N   . GLU A 170 ? 0.56151 1.29095 1.36935 0.12204  -0.07522 0.08222  206 GLU A N   
1369 C CA  . GLU A 170 ? 0.55576 1.30888 1.33555 0.11045  -0.11419 0.06101  206 GLU A CA  
1370 C C   . GLU A 170 ? 0.59006 1.37739 1.34196 0.13618  -0.14686 0.07696  206 GLU A C   
1371 O O   . GLU A 170 ? 0.64792 1.42516 1.39126 0.16058  -0.13412 0.10675  206 GLU A O   
1372 C CB  . GLU A 170 ? 0.52958 1.32900 1.38584 0.08999  -0.13230 0.03464  206 GLU A CB  
1373 C CG  . GLU A 170 ? 0.48450 1.25078 1.37215 0.06694  -0.09565 0.02559  206 GLU A CG  
1374 C CD  . GLU A 170 ? 0.51437 1.31748 1.47562 0.04611  -0.10838 0.00227  206 GLU A CD  
1375 O OE1 . GLU A 170 ? 0.52418 1.37656 1.50433 0.04877  -0.14642 -0.00907 206 GLU A OE1 
1376 O OE2 . GLU A 170 ? 0.53145 1.30486 1.51331 0.02729  -0.07760 -0.00239 206 GLU A OE2 
1377 N N   . LYS A 171 ? 0.54768 1.37621 1.28510 0.13238  -0.18852 0.05712  207 LYS A N   
1378 C CA  . LYS A 171 ? 0.67995 1.55208 1.38707 0.15906  -0.22398 0.07143  207 LYS A CA  
1379 C C   . LYS A 171 ? 0.75359 1.57899 1.37977 0.17767  -0.20618 0.10106  207 LYS A C   
1380 O O   . LYS A 171 ? 0.82315 1.67191 1.43630 0.20761  -0.21704 0.13138  207 LYS A O   
1381 C CB  . LYS A 171 ? 0.61912 1.53238 1.39040 0.17827  -0.23700 0.08637  207 LYS A CB  
1382 C CG  . LYS A 171 ? 0.70512 1.64987 1.57067 0.15955  -0.24370 0.06003  207 LYS A CG  
1383 C CD  . LYS A 171 ? 0.75674 1.73127 1.63010 0.13703  -0.28442 0.02995  207 LYS A CD  
1384 C CE  . LYS A 171 ? 0.77735 1.79630 1.73563 0.11714  -0.28193 0.02321  207 LYS A CE  
1385 N NZ  . LYS A 171 ? 0.74272 1.77122 1.70258 0.08900  -0.30876 -0.01667 207 LYS A NZ  
1386 N N   . LYS A 172 ? 0.74430 1.50495 1.32124 0.16101  -0.17820 0.09454  208 LYS A N   
1387 C CA  . LYS A 172 ? 0.83598 1.55003 1.34613 0.17460  -0.15967 0.11931  208 LYS A CA  
1388 C C   . LYS A 172 ? 0.94256 1.66438 1.38287 0.17565  -0.18295 0.11066  208 LYS A C   
1389 O O   . LYS A 172 ? 0.93278 1.67968 1.36886 0.15941  -0.20737 0.07763  208 LYS A O   
1390 C CB  . LYS A 172 ? 0.83816 1.48123 1.33431 0.15783  -0.11863 0.11619  208 LYS A CB  
1391 C CG  . LYS A 172 ? 0.81254 1.44390 1.36742 0.15870  -0.09089 0.12255  208 LYS A CG  
1392 C CD  . LYS A 172 ? 0.80116 1.36662 1.33123 0.14400  -0.05429 0.11531  208 LYS A CD  
1393 C CE  . LYS A 172 ? 0.85103 1.37065 1.33792 0.15753  -0.03697 0.13516  208 LYS A CE  
1394 N NZ  . LYS A 172 ? 0.91344 1.43728 1.43789 0.18346  -0.02438 0.16209  208 LYS A NZ  
1395 N N   . SER A 173 ? 1.02558 1.72438 1.41441 0.19568  -0.17250 0.14065  209 SER A N   
1396 C CA  . SER A 173 ? 1.05761 1.76347 1.37613 0.20229  -0.18867 0.13937  209 SER A CA  
1397 C C   . SER A 173 ? 1.08810 1.74256 1.36848 0.17537  -0.17192 0.11498  209 SER A C   
1398 O O   . SER A 173 ? 1.12303 1.72276 1.41025 0.16217  -0.14019 0.11760  209 SER A O   
1399 C CB  . SER A 173 ? 1.16965 1.86787 1.45414 0.23464  -0.17743 0.18621  209 SER A CB  
1400 O OG  . SER A 173 ? 1.35668 2.00290 1.66847 0.23616  -0.13999 0.20917  209 SER A OG  
1401 N N   . LEU A 174 ? 1.09730 1.77165 1.33774 0.16864  -0.19445 0.08956  210 LEU A N   
1402 C CA  . LEU A 174 ? 1.12351 1.75410 1.32907 0.14540  -0.18070 0.06672  210 LEU A CA  
1403 C C   . LEU A 174 ? 1.21150 1.80199 1.36287 0.15827  -0.15711 0.09628  210 LEU A C   
1404 O O   . LEU A 174 ? 1.23278 1.84322 1.33369 0.17745  -0.16736 0.10814  210 LEU A O   
1405 C CB  . LEU A 174 ? 1.03354 1.69844 1.21951 0.13565  -0.21108 0.02765  210 LEU A CB  
1406 C CG  . LEU A 174 ? 0.96548 1.66251 1.21424 0.11491  -0.23215 -0.01030 210 LEU A CG  
1407 C CD1 . LEU A 174 ? 0.85984 1.62900 1.13739 0.13354  -0.26917 -0.01135 210 LEU A CD1 
1408 C CD2 . LEU A 174 ? 0.81281 1.50251 1.04532 0.09275  -0.24123 -0.05284 210 LEU A CD2 
1409 N N   . SER A 175 ? 1.26233 1.79773 1.42566 0.14846  -0.12484 0.10767  211 SER A N   
1410 C CA  . SER A 175 ? 1.28782 1.78085 1.41611 0.15606  -0.09998 0.13271  211 SER A CA  
1411 C C   . SER A 175 ? 1.31207 1.75704 1.43079 0.12940  -0.08267 0.11088  211 SER A C   
1412 O O   . SER A 175 ? 1.19972 1.62478 1.35058 0.11092  -0.07427 0.09424  211 SER A O   
1413 C CB  . SER A 175 ? 1.33664 1.80887 1.49489 0.17230  -0.07839 0.16758  211 SER A CB  
1414 O OG  . SER A 175 ? 1.41830 1.93535 1.58403 0.20114  -0.09302 0.19465  211 SER A OG  
1415 N N   . GLY A 176 ? 1.18375 1.61274 1.25842 0.12966  -0.07647 0.11311  212 GLY A N   
1416 C CA  . GLY A 176 ? 0.97977 1.36784 1.04446 0.10749  -0.06203 0.09532  212 GLY A CA  
1417 C C   . GLY A 176 ? 0.93054 1.33088 0.95216 0.10547  -0.07186 0.07918  212 GLY A C   
1418 O O   . GLY A 176 ? 0.92310 1.35938 0.91311 0.12439  -0.08629 0.08566  212 GLY A O   
1419 N N   . THR A 177 ? 0.86492 1.23616 0.88373 0.08426  -0.06354 0.05786  213 THR A N   
1420 C CA  . THR A 177 ? 0.76578 1.14296 0.74989 0.08008  -0.06940 0.03780  213 THR A CA  
1421 C C   . THR A 177 ? 0.67052 1.06539 0.67581 0.06218  -0.08813 -0.00056 213 THR A C   
1422 O O   . THR A 177 ? 0.62144 0.99444 0.66137 0.04273  -0.08109 -0.01207 213 THR A O   
1423 C CB  . THR A 177 ? 0.73762 1.07171 0.71160 0.06992  -0.04657 0.04131  213 THR A CB  
1424 O OG1 . THR A 177 ? 0.77072 1.08323 0.77125 0.04601  -0.04467 0.01779  213 THR A OG1 
1425 C CG2 . THR A 177 ? 0.65466 0.96084 0.63958 0.07799  -0.02541 0.07449  213 THR A CG2 
1426 N N   . ALA A 178 ? 0.78435 0.91226 0.68699 0.03564  -0.03144 -0.00391 214 ALA A N   
1427 C CA  . ALA A 178 ? 0.82154 0.96657 0.73551 0.02501  -0.04576 -0.02183 214 ALA A CA  
1428 C C   . ALA A 178 ? 0.69169 0.82376 0.61259 0.00909  -0.03970 -0.03042 214 ALA A C   
1429 O O   . ALA A 178 ? 0.71547 0.85778 0.65688 -0.00418 -0.04783 -0.04211 214 ALA A O   
1430 C CB  . ALA A 178 ? 0.90264 1.05887 0.79090 0.03619  -0.06227 -0.03011 214 ALA A CB  
1431 N N   . ARG A 179 ? 0.64082 0.75135 0.54826 0.01028  -0.02538 -0.02369 215 ARG A N   
1432 C CA  . ARG A 179 ? 0.68384 0.78211 0.59787 -0.00183 -0.02066 -0.03133 215 ARG A CA  
1433 C C   . ARG A 179 ? 0.60463 0.70601 0.54984 -0.01639 -0.01715 -0.02996 215 ARG A C   
1434 O O   . ARG A 179 ? 0.64017 0.73856 0.59750 -0.02829 -0.01952 -0.03761 215 ARG A O   
1435 C CB  . ARG A 179 ? 0.60876 0.68827 0.50543 0.00456  -0.00545 -0.02344 215 ARG A CB  
1436 C CG  . ARG A 179 ? 0.63023 0.69692 0.53001 -0.00308 -0.00179 -0.03235 215 ARG A CG  
1437 C CD  . ARG A 179 ? 0.70339 0.75739 0.59599 0.00288  0.01539  -0.02223 215 ARG A CD  
1438 N NE  . ARG A 179 ? 0.72152 0.77443 0.58263 0.01889  0.02115  -0.01753 215 ARG A NE  
1439 C CZ  . ARG A 179 ? 0.75258 0.79876 0.60599 0.02620  0.03831  -0.00642 215 ARG A CZ  
1440 N NH1 . ARG A 179 ? 0.71109 0.75208 0.58891 0.01879  0.04927  -0.00024 215 ARG A NH1 
1441 N NH2 . ARG A 179 ? 0.69829 0.74549 0.51932 0.04188  0.04474  -0.00059 215 ARG A NH2 
1442 N N   . TYR A 180 ? 0.59182 0.69833 0.54902 -0.01471 -0.01171 -0.02045 216 TYR A N   
1443 C CA  . TYR A 180 ? 0.53046 0.64042 0.51021 -0.02545 -0.00699 -0.01900 216 TYR A CA  
1444 C C   . TYR A 180 ? 0.57035 0.70310 0.56872 -0.02700 -0.01210 -0.02061 216 TYR A C   
1445 O O   . TYR A 180 ? 0.46086 0.60092 0.47567 -0.03648 -0.00863 -0.02070 216 TYR A O   
1446 C CB  . TYR A 180 ? 0.53309 0.62959 0.51349 -0.02299 0.00449  -0.01000 216 TYR A CB  
1447 C CG  . TYR A 180 ? 0.51642 0.59543 0.48356 -0.02005 0.01197  -0.00615 216 TYR A CG  
1448 C CD1 . TYR A 180 ? 0.52300 0.59428 0.49164 -0.02686 0.01407  -0.00994 216 TYR A CD1 
1449 C CD2 . TYR A 180 ? 0.59855 0.66943 0.55335 -0.00945 0.01828  0.00284  216 TYR A CD2 
1450 C CE1 . TYR A 180 ? 0.60048 0.65938 0.55971 -0.02224 0.02235  -0.00689 216 TYR A CE1 
1451 C CE2 . TYR A 180 ? 0.63017 0.68946 0.57530 -0.00630 0.02806  0.00785  216 TYR A CE2 
1452 C CZ  . TYR A 180 ? 0.56904 0.62394 0.51697 -0.01227 0.03005  0.00189  216 TYR A CZ  
1453 O OH  . TYR A 180 ? 0.67162 0.71841 0.61247 -0.00729 0.04105  0.00630  216 TYR A OH  
1454 N N   . MET A 181 ? 0.54448 0.69061 0.54065 -0.01666 -0.01960 -0.02093 217 MET A N   
1455 C CA  . MET A 181 ? 0.58670 0.75601 0.60309 -0.01439 -0.02195 -0.02126 217 MET A CA  
1456 C C   . MET A 181 ? 0.55840 0.74946 0.59826 -0.02835 -0.02614 -0.02779 217 MET A C   
1457 O O   . MET A 181 ? 0.48480 0.67421 0.52566 -0.03801 -0.03285 -0.03413 217 MET A O   
1458 C CB  . MET A 181 ? 0.62150 0.80225 0.63236 0.00138  -0.03110 -0.01963 217 MET A CB  
1459 C CG  . MET A 181 ? 0.59375 0.78840 0.59960 0.00131  -0.04660 -0.02779 217 MET A CG  
1460 S SD  . MET A 181 ? 0.69983 0.91520 0.70104 0.02194  -0.06070 -0.02510 217 MET A SD  
1461 C CE  . MET A 181 ? 0.88897 1.07461 0.86739 0.03846  -0.04751 -0.00800 217 MET A CE  
1462 N N   . SER A 182 ? 0.51784 0.72895 0.57800 -0.02913 -0.02118 -0.02620 218 SER A N   
1463 C CA  . SER A 182 ? 0.55014 0.78454 0.63650 -0.04296 -0.02085 -0.02822 218 SER A CA  
1464 C C   . SER A 182 ? 0.59364 0.85227 0.69756 -0.04529 -0.03564 -0.03541 218 SER A C   
1465 O O   . SER A 182 ? 0.58576 0.84970 0.68106 -0.03217 -0.04633 -0.03830 218 SER A O   
1466 C CB  . SER A 182 ? 0.57618 0.83062 0.67754 -0.03975 -0.00997 -0.02448 218 SER A CB  
1467 O OG  . SER A 182 ? 0.52148 0.79732 0.63291 -0.02530 -0.01426 -0.02652 218 SER A OG  
1468 N N   . ILE A 183 ? 0.56184 0.83564 0.69214 -0.06245 -0.03688 -0.03757 219 ILE A N   
1469 C CA  . ILE A 183 ? 0.57821 0.87999 0.73477 -0.06797 -0.05232 -0.04617 219 ILE A CA  
1470 C C   . ILE A 183 ? 0.59085 0.92930 0.76701 -0.05509 -0.05440 -0.04493 219 ILE A C   
1471 O O   . ILE A 183 ? 0.61226 0.97007 0.79552 -0.04763 -0.07119 -0.05201 219 ILE A O   
1472 C CB  . ILE A 183 ? 0.60270 0.91259 0.79150 -0.09143 -0.05055 -0.04639 219 ILE A CB  
1473 C CG1 . ILE A 183 ? 0.58574 0.85690 0.75622 -0.10142 -0.05227 -0.05008 219 ILE A CG1 
1474 C CG2 . ILE A 183 ? 0.57040 0.91613 0.79748 -0.09941 -0.06649 -0.05566 219 ILE A CG2 
1475 C CD1 . ILE A 183 ? 0.59572 0.86719 0.79868 -0.12458 -0.05092 -0.04902 219 ILE A CD1 
1476 N N   . ASN A 184 ? 0.56637 0.91551 0.75013 -0.05015 -0.03814 -0.03684 220 ASN A N   
1477 C CA  . ASN A 184 ? 0.56118 0.94413 0.76433 -0.03500 -0.03822 -0.03645 220 ASN A CA  
1478 C C   . ASN A 184 ? 0.59870 0.96896 0.77733 -0.01274 -0.04803 -0.03765 220 ASN A C   
1479 O O   . ASN A 184 ? 0.46339 0.86181 0.65871 0.00039  -0.05788 -0.03951 220 ASN A O   
1480 C CB  . ASN A 184 ? 0.58266 0.97421 0.79102 -0.03120 -0.01765 -0.02997 220 ASN A CB  
1481 C CG  . ASN A 184 ? 0.60442 1.01287 0.83663 -0.05114 -0.00557 -0.02431 220 ASN A CG  
1482 O OD1 . ASN A 184 ? 0.51013 0.94705 0.77810 -0.06467 -0.01107 -0.02502 220 ASN A OD1 
1483 N ND2 . ASN A 184 ? 0.63084 1.02196 0.84432 -0.05329 0.01044  -0.01786 220 ASN A ND2 
1484 N N   . THR A 185 ? 0.49584 0.82517 0.63719 -0.00780 -0.04506 -0.03483 221 THR A N   
1485 C CA  . THR A 185 ? 0.54863 0.86255 0.66604 0.01221  -0.05220 -0.03197 221 THR A CA  
1486 C C   . THR A 185 ? 0.62234 0.94547 0.73325 0.01500  -0.07236 -0.03705 221 THR A C   
1487 O O   . THR A 185 ? 0.70444 1.03721 0.80998 0.03365  -0.08278 -0.03443 221 THR A O   
1488 C CB  . THR A 185 ? 0.56355 0.83413 0.64834 0.01400  -0.04205 -0.02628 221 THR A CB  
1489 O OG1 . THR A 185 ? 0.54796 0.81207 0.63845 0.00985  -0.02659 -0.02487 221 THR A OG1 
1490 C CG2 . THR A 185 ? 0.58062 0.83445 0.64524 0.03467  -0.04501 -0.01899 221 THR A CG2 
1491 N N   . HIS A 186 ? 0.58616 0.90540 0.69608 -0.00197 -0.07910 -0.04493 222 HIS A N   
1492 C CA  . HIS A 186 ? 0.62014 0.95004 0.72333 0.00029  -0.10071 -0.05445 222 HIS A CA  
1493 C C   . HIS A 186 ? 0.65323 1.03021 0.79314 0.00389  -0.11591 -0.05973 222 HIS A C   
1494 O O   . HIS A 186 ? 0.61976 1.01092 0.75060 0.01644  -0.13582 -0.06460 222 HIS A O   
1495 C CB  . HIS A 186 ? 0.64627 0.96189 0.74730 -0.01972 -0.10504 -0.06538 222 HIS A CB  
1496 C CG  . HIS A 186 ? 0.68144 0.95528 0.74114 -0.01722 -0.09720 -0.06318 222 HIS A CG  
1497 N ND1 . HIS A 186 ? 0.79765 1.05831 0.81918 -0.00209 -0.10592 -0.06491 222 HIS A ND1 
1498 C CD2 . HIS A 186 ? 0.66114 0.90662 0.71284 -0.02683 -0.08102 -0.05864 222 HIS A CD2 
1499 C CE1 . HIS A 186 ? 0.77991 1.00693 0.77430 -0.00304 -0.09357 -0.06153 222 HIS A CE1 
1500 N NE2 . HIS A 186 ? 0.71027 0.92778 0.72384 -0.01796 -0.07955 -0.05825 222 HIS A NE2 
1501 N N   . LEU A 187 ? 0.52992 0.93432 0.71120 -0.00557 -0.10667 -0.05817 223 LEU A N   
1502 C CA  . LEU A 187 ? 0.67059 1.12581 0.89614 -0.00370 -0.11836 -0.06245 223 LEU A CA  
1503 C C   . LEU A 187 ? 0.64030 1.11251 0.87032 0.02182  -0.11510 -0.05419 223 LEU A C   
1504 O O   . LEU A 187 ? 0.69377 1.21183 0.96530 0.02600  -0.12075 -0.05604 223 LEU A O   
1505 C CB  . LEU A 187 ? 0.67614 1.15603 0.94785 -0.02699 -0.10727 -0.06302 223 LEU A CB  
1506 C CG  . LEU A 187 ? 0.62757 1.08862 0.90205 -0.05317 -0.10999 -0.07000 223 LEU A CG  
1507 C CD1 . LEU A 187 ? 0.68985 1.17308 1.01011 -0.07527 -0.09522 -0.06475 223 LEU A CD1 
1508 C CD2 . LEU A 187 ? 0.56841 1.03885 0.84618 -0.05687 -0.13878 -0.08637 223 LEU A CD2 
1509 N N   . GLY A 188 ? 0.66133 1.09788 0.85354 0.03891  -0.10595 -0.04513 224 GLY A N   
1510 C CA  . GLY A 188 ? 0.79410 1.23884 0.98973 0.06430  -0.10328 -0.03751 224 GLY A CA  
1511 C C   . GLY A 188 ? 0.84190 1.30597 1.06854 0.06566  -0.08492 -0.03621 224 GLY A C   
1512 O O   . GLY A 188 ? 0.88240 1.36452 1.12403 0.08711  -0.08484 -0.03339 224 GLY A O   
1513 N N   . ARG A 189 ? 0.83202 1.29280 1.06686 0.04533  -0.06893 -0.03787 225 ARG A N   
1514 C CA  . ARG A 189 ? 0.86127 1.34138 1.11919 0.04745  -0.04956 -0.03678 225 ARG A CA  
1515 C C   . ARG A 189 ? 0.98829 1.42907 1.21545 0.06111  -0.03520 -0.03383 225 ARG A C   
1516 O O   . ARG A 189 ? 1.03967 1.43652 1.23135 0.06016  -0.03612 -0.03106 225 ARG A O   
1517 C CB  . ARG A 189 ? 0.72918 1.22212 1.00548 0.02119  -0.03794 -0.03707 225 ARG A CB  
1518 C CG  . ARG A 189 ? 0.78329 1.31187 1.09659 0.00339  -0.05186 -0.04103 225 ARG A CG  
1519 C CD  . ARG A 189 ? 0.79768 1.32961 1.12748 -0.02341 -0.03848 -0.03775 225 ARG A CD  
1520 N NE  . ARG A 189 ? 0.83158 1.39408 1.20252 -0.04329 -0.05203 -0.04228 225 ARG A NE  
1521 C CZ  . ARG A 189 ? 0.85067 1.41518 1.24295 -0.06924 -0.04430 -0.03872 225 ARG A CZ  
1522 N NH1 . ARG A 189 ? 0.81582 1.35554 1.18887 -0.07702 -0.02331 -0.02908 225 ARG A NH1 
1523 N NH2 . ARG A 189 ? 0.80828 1.39966 1.24320 -0.08766 -0.05903 -0.04476 225 ARG A NH2 
1524 N N   . GLU A 190 ? 0.79624 1.25461 1.03968 0.07408  -0.02175 -0.03561 226 GLU A N   
1525 C CA  . GLU A 190 ? 0.73591 1.15856 0.95447 0.08594  -0.00897 -0.03702 226 GLU A CA  
1526 C C   . GLU A 190 ? 0.71620 1.11193 0.91162 0.06629  0.00196  -0.03718 226 GLU A C   
1527 O O   . GLU A 190 ? 0.53385 0.95148 0.74176 0.04938  0.00994  -0.03642 226 GLU A O   
1528 C CB  . GLU A 190 ? 0.67432 1.12477 0.91509 0.10426  0.00353  -0.04252 226 GLU A CB  
1529 C CG  . GLU A 190 ? 0.71864 1.13147 0.93545 0.11830  0.01428  -0.04854 226 GLU A CG  
1530 C CD  . GLU A 190 ? 0.78038 1.15826 0.98517 0.13829  0.00410  -0.04600 226 GLU A CD  
1531 O OE1 . GLU A 190 ? 0.88896 1.28672 1.11464 0.16015  -0.00081 -0.04569 226 GLU A OE1 
1532 O OE2 . GLU A 190 ? 0.73938 1.07101 0.91617 0.13255  0.00155  -0.04266 226 GLU A OE2 
1533 N N   . GLN A 191 ? 0.62405 0.97325 0.78832 0.06862  0.00235  -0.03666 227 GLN A N   
1534 C CA  . GLN A 191 ? 0.55004 0.87385 0.69303 0.05224  0.01021  -0.03684 227 GLN A CA  
1535 C C   . GLN A 191 ? 0.52321 0.84803 0.66230 0.05816  0.02472  -0.04410 227 GLN A C   
1536 O O   . GLN A 191 ? 0.59260 0.91832 0.73617 0.07770  0.02805  -0.05084 227 GLN A O   
1537 C CB  . GLN A 191 ? 0.55544 0.83354 0.67151 0.05121  0.00441  -0.03317 227 GLN A CB  
1538 C CG  . GLN A 191 ? 0.58061 0.85599 0.69183 0.04755  -0.00882 -0.02685 227 GLN A CG  
1539 C CD  . GLN A 191 ? 0.67403 0.90775 0.75854 0.04675  -0.01034 -0.02120 227 GLN A CD  
1540 O OE1 . GLN A 191 ? 0.61167 0.82225 0.68455 0.03789  -0.00282 -0.02201 227 GLN A OE1 
1541 N NE2 . GLN A 191 ? 0.60857 0.83508 0.68371 0.05685  -0.01985 -0.01447 227 GLN A NE2 
1542 N N   . SER A 192 ? 0.49902 0.82282 0.62793 0.04269  0.03275  -0.04318 228 SER A N   
1543 C CA  . SER A 192 ? 0.51326 0.83800 0.63050 0.04781  0.04533  -0.05043 228 SER A CA  
1544 C C   . SER A 192 ? 0.49931 0.79658 0.59218 0.03300  0.04551  -0.04820 228 SER A C   
1545 O O   . SER A 192 ? 0.46398 0.73655 0.54960 0.02281  0.03684  -0.04282 228 SER A O   
1546 C CB  . SER A 192 ? 0.55902 0.93139 0.69579 0.04865  0.05849  -0.04902 228 SER A CB  
1547 O OG  . SER A 192 ? 0.50707 0.89670 0.65502 0.02741  0.06013  -0.03729 228 SER A OG  
1548 N N   . ARG A 193 ? 0.48076 0.78430 0.55976 0.03356  0.05550  -0.05236 229 ARG A N   
1549 C CA  . ARG A 193 ? 0.59105 0.87063 0.64696 0.02278  0.05390  -0.05101 229 ARG A CA  
1550 C C   . ARG A 193 ? 0.53213 0.81213 0.59196 0.00302  0.05192  -0.03666 229 ARG A C   
1551 O O   . ARG A 193 ? 0.51396 0.76701 0.56135 -0.00552 0.04562  -0.03406 229 ARG A O   
1552 C CB  . ARG A 193 ? 0.57143 0.86369 0.60887 0.02927  0.06403  -0.05761 229 ARG A CB  
1553 C CG  . ARG A 193 ? 0.62351 0.90288 0.65021 0.04818  0.06285  -0.07709 229 ARG A CG  
1554 C CD  . ARG A 193 ? 0.63406 0.93265 0.63916 0.05751  0.07340  -0.08577 229 ARG A CD  
1555 N NE  . ARG A 193 ? 0.59862 0.94043 0.61621 0.06462  0.08917  -0.08069 229 ARG A NE  
1556 C CZ  . ARG A 193 ? 0.71785 1.08440 0.71880 0.07779  0.10263  -0.08799 229 ARG A CZ  
1557 N NH1 . ARG A 193 ? 0.63731 0.98898 0.60488 0.08606  0.09992  -0.10298 229 ARG A NH1 
1558 N NH2 . ARG A 193 ? 0.66038 1.06995 0.67907 0.08339  0.11909  -0.08073 229 ARG A NH2 
1559 N N   . ARG A 194 ? 0.48268 0.79290 0.56320 -0.00435 0.05712  -0.02793 230 ARG A N   
1560 C CA  . ARG A 194 ? 0.50831 0.81630 0.59585 -0.02357 0.05502  -0.01593 230 ARG A CA  
1561 C C   . ARG A 194 ? 0.39535 0.67675 0.48270 -0.02861 0.04105  -0.01696 230 ARG A C   
1562 O O   . ARG A 194 ? 0.48140 0.74491 0.56300 -0.04108 0.03768  -0.01129 230 ARG A O   
1563 C CB  . ARG A 194 ? 0.39748 0.74362 0.51503 -0.03159 0.06229  -0.00784 230 ARG A CB  
1564 C CG  . ARG A 194 ? 0.39859 0.76477 0.54293 -0.02570 0.05485  -0.01315 230 ARG A CG  
1565 C CD  . ARG A 194 ? 0.53021 0.93943 0.71140 -0.03527 0.06217  -0.00559 230 ARG A CD  
1566 N NE  . ARG A 194 ? 0.50102 0.93333 0.71062 -0.02908 0.05194  -0.01145 230 ARG A NE  
1567 C CZ  . ARG A 194 ? 0.50070 0.97391 0.75109 -0.03715 0.05353  -0.00751 230 ARG A CZ  
1568 N NH1 . ARG A 194 ? 0.48396 0.97886 0.75371 -0.05300 0.06751  0.00419  230 ARG A NH1 
1569 N NH2 . ARG A 194 ? 0.50583 0.99991 0.78019 -0.02911 0.04062  -0.01417 230 ARG A NH2 
1570 N N   . ASP A 195 ? 0.39876 0.67704 0.49065 -0.01729 0.03358  -0.02339 231 ASP A N   
1571 C CA  . ASP A 195 ? 0.42185 0.67934 0.51017 -0.01988 0.02177  -0.02285 231 ASP A CA  
1572 C C   . ASP A 195 ? 0.48163 0.70257 0.54749 -0.01907 0.01998  -0.02332 231 ASP A C   
1573 O O   . ASP A 195 ? 0.45556 0.65885 0.51463 -0.02539 0.01438  -0.02044 231 ASP A O   
1574 C CB  . ASP A 195 ? 0.47078 0.73931 0.56983 -0.00629 0.01445  -0.02623 231 ASP A CB  
1575 C CG  . ASP A 195 ? 0.49421 0.80331 0.62241 -0.00879 0.01332  -0.02589 231 ASP A CG  
1576 O OD1 . ASP A 195 ? 0.48471 0.80179 0.62443 -0.02297 0.00699  -0.02385 231 ASP A OD1 
1577 O OD2 . ASP A 195 ? 0.55476 0.88855 0.69723 0.00332  0.01878  -0.02865 231 ASP A OD2 
1578 N N   . ASP A 196 ? 0.51674 0.72727 0.57269 -0.01126 0.02443  -0.02814 232 ASP A N   
1579 C CA  . ASP A 196 ? 0.50195 0.68227 0.54364 -0.01358 0.02253  -0.02849 232 ASP A CA  
1580 C C   . ASP A 196 ? 0.49850 0.67525 0.53402 -0.02698 0.02390  -0.02284 232 ASP A C   
1581 O O   . ASP A 196 ? 0.50753 0.66402 0.53754 -0.03193 0.02079  -0.01974 232 ASP A O   
1582 C CB  . ASP A 196 ? 0.44984 0.62099 0.48602 -0.00378 0.02445  -0.03799 232 ASP A CB  
1583 C CG  . ASP A 196 ? 0.55349 0.71441 0.59602 0.01017  0.02209  -0.04229 232 ASP A CG  
1584 O OD1 . ASP A 196 ? 0.48416 0.64016 0.53058 0.01236  0.01823  -0.03531 232 ASP A OD1 
1585 O OD2 . ASP A 196 ? 0.47599 0.63237 0.51812 0.02018  0.02364  -0.05290 232 ASP A OD2 
1586 N N   . LEU A 197 ? 0.51022 0.70719 0.54761 -0.03189 0.02972  -0.01974 233 LEU A N   
1587 C CA  . LEU A 197 ? 0.51108 0.70323 0.54263 -0.04287 0.03142  -0.01166 233 LEU A CA  
1588 C C   . LEU A 197 ? 0.48646 0.67400 0.52794 -0.05408 0.02824  -0.00524 233 LEU A C   
1589 O O   . LEU A 197 ? 0.52608 0.69640 0.56244 -0.06058 0.02649  -0.00056 233 LEU A O   
1590 C CB  . LEU A 197 ? 0.44216 0.65682 0.47045 -0.04341 0.04049  -0.00704 233 LEU A CB  
1591 C CG  . LEU A 197 ? 0.55665 0.77768 0.56989 -0.03096 0.04353  -0.01634 233 LEU A CG  
1592 C CD1 . LEU A 197 ? 0.64360 0.88245 0.64438 -0.03219 0.05242  -0.00802 233 LEU A CD1 
1593 C CD2 . LEU A 197 ? 0.45104 0.64622 0.45357 -0.02697 0.03476  -0.02527 233 LEU A CD2 
1594 N N   . GLU A 198 ? 0.45805 0.66153 0.51523 -0.05582 0.02640  -0.00634 234 GLU A N   
1595 C CA  . GLU A 198 ? 0.47365 0.67095 0.53998 -0.06600 0.02022  -0.00496 234 GLU A CA  
1596 C C   . GLU A 198 ? 0.49278 0.66405 0.54525 -0.06184 0.01339  -0.00911 234 GLU A C   
1597 O O   . GLU A 198 ? 0.50115 0.65568 0.55053 -0.06855 0.01089  -0.00807 234 GLU A O   
1598 C CB  . GLU A 198 ? 0.38660 0.60962 0.47460 -0.06778 0.01632  -0.00803 234 GLU A CB  
1599 C CG  . GLU A 198 ? 0.49364 0.71034 0.59107 -0.07776 0.00618  -0.01147 234 GLU A CG  
1600 C CD  . GLU A 198 ? 0.58643 0.83385 0.71123 -0.08152 -0.00000 -0.01543 234 GLU A CD  
1601 O OE1 . GLU A 198 ? 0.50937 0.78557 0.64982 -0.07822 0.00702  -0.01241 234 GLU A OE1 
1602 O OE2 . GLU A 198 ? 0.58568 0.83025 0.71699 -0.08688 -0.01244 -0.02287 234 GLU A OE2 
1603 N N   . ALA A 199 ? 0.44751 0.61436 0.49205 -0.04991 0.01173  -0.01293 235 ALA A N   
1604 C CA  . ALA A 199 ? 0.54906 0.69338 0.58036 -0.04519 0.00870  -0.01350 235 ALA A CA  
1605 C C   . ALA A 199 ? 0.48136 0.60700 0.50542 -0.04883 0.01273  -0.01027 235 ALA A C   
1606 O O   . ALA A 199 ? 0.48695 0.59740 0.50465 -0.05010 0.01191  -0.00956 235 ALA A O   
1607 C CB  . ALA A 199 ? 0.52973 0.67133 0.55688 -0.03213 0.00831  -0.01433 235 ALA A CB  
1608 N N   . LEU A 200 ? 0.47248 0.60104 0.49710 -0.04902 0.01657  -0.00926 236 LEU A N   
1609 C CA  . LEU A 200 ? 0.55025 0.66651 0.57096 -0.05244 0.01791  -0.00604 236 LEU A CA  
1610 C C   . LEU A 200 ? 0.49194 0.60374 0.51458 -0.06084 0.01767  -0.00114 236 LEU A C   
1611 O O   . LEU A 200 ? 0.51939 0.61595 0.53987 -0.06130 0.01742  0.00066  236 LEU A O   
1612 C CB  . LEU A 200 ? 0.48388 0.60859 0.50201 -0.05059 0.01938  -0.00728 236 LEU A CB  
1613 C CG  . LEU A 200 ? 0.47657 0.59811 0.49411 -0.04258 0.01821  -0.01512 236 LEU A CG  
1614 C CD1 . LEU A 200 ? 0.50066 0.63411 0.51155 -0.03972 0.01846  -0.01997 236 LEU A CD1 
1615 C CD2 . LEU A 200 ? 0.41388 0.51704 0.43512 -0.04248 0.01631  -0.01506 236 LEU A CD2 
1616 N N   . GLY A 201 ? 0.49560 0.62028 0.52558 -0.06743 0.01841  0.00134  237 GLY A N   
1617 C CA  . GLY A 201 ? 0.46971 0.58584 0.50564 -0.07667 0.01792  0.00616  237 GLY A CA  
1618 C C   . GLY A 201 ? 0.51525 0.61494 0.54970 -0.07667 0.01289  -0.00039 237 GLY A C   
1619 O O   . GLY A 201 ? 0.57841 0.66084 0.61322 -0.07974 0.01247  0.00113  237 GLY A O   
1620 N N   . HIS A 202 ? 0.49325 0.59782 0.52404 -0.07123 0.00895  -0.00787 238 HIS A N   
1621 C CA  . HIS A 202 ? 0.51659 0.60741 0.53856 -0.06792 0.00436  -0.01506 238 HIS A CA  
1622 C C   . HIS A 202 ? 0.52572 0.59980 0.53612 -0.06042 0.00946  -0.01291 238 HIS A C   
1623 O O   . HIS A 202 ? 0.51091 0.56980 0.51595 -0.05916 0.00942  -0.01645 238 HIS A O   
1624 C CB  . HIS A 202 ? 0.53359 0.63662 0.55093 -0.06142 -0.00151 -0.02101 238 HIS A CB  
1625 C CG  . HIS A 202 ? 0.55754 0.68121 0.59194 -0.06871 -0.00803 -0.02463 238 HIS A CG  
1626 N ND1 . HIS A 202 ? 0.51546 0.65976 0.55388 -0.06242 -0.01228 -0.02651 238 HIS A ND1 
1627 C CD2 . HIS A 202 ? 0.59698 0.72496 0.64988 -0.08203 -0.01065 -0.02569 238 HIS A CD2 
1628 C CE1 . HIS A 202 ? 0.61206 0.77646 0.67230 -0.07159 -0.01741 -0.02944 238 HIS A CE1 
1629 N NE2 . HIS A 202 ? 0.57447 0.72885 0.64469 -0.08477 -0.01609 -0.02861 238 HIS A NE2 
1630 N N   . VAL A 203 ? 0.52848 0.60572 0.53771 -0.05530 0.01398  -0.00816 239 VAL A N   
1631 C CA  . VAL A 203 ? 0.45182 0.51768 0.45804 -0.05008 0.01932  -0.00498 239 VAL A CA  
1632 C C   . VAL A 203 ? 0.46430 0.52245 0.47685 -0.05374 0.02048  -0.00179 239 VAL A C   
1633 O O   . VAL A 203 ? 0.51469 0.56247 0.52643 -0.04946 0.02403  -0.00151 239 VAL A O   
1634 C CB  . VAL A 203 ? 0.42649 0.49693 0.43681 -0.04661 0.02189  -0.00196 239 VAL A CB  
1635 C CG1 . VAL A 203 ? 0.43612 0.49799 0.45114 -0.04356 0.02747  0.00199  239 VAL A CG1 
1636 C CG2 . VAL A 203 ? 0.54142 0.61635 0.54638 -0.04081 0.02084  -0.00316 239 VAL A CG2 
1637 N N   . PHE A 204 ? 0.43793 0.50221 0.45660 -0.05999 0.01845  0.00207  240 PHE A N   
1638 C CA  . PHE A 204 ? 0.45891 0.51553 0.48244 -0.06167 0.01872  0.00815  240 PHE A CA  
1639 C C   . PHE A 204 ? 0.56460 0.60407 0.58884 -0.06244 0.01835  0.00536  240 PHE A C   
1640 O O   . PHE A 204 ? 0.54220 0.57030 0.56914 -0.05752 0.02022  0.00708  240 PHE A O   
1641 C CB  . PHE A 204 ? 0.47423 0.54098 0.49972 -0.06726 0.01783  0.01551  240 PHE A CB  
1642 C CG  . PHE A 204 ? 0.50742 0.59029 0.52909 -0.06459 0.01761  0.01480  240 PHE A CG  
1643 C CD1 . PHE A 204 ? 0.46154 0.54457 0.48374 -0.05899 0.01674  0.00971  240 PHE A CD1 
1644 C CD2 . PHE A 204 ? 0.48898 0.58654 0.50782 -0.06753 0.01906  0.01872  240 PHE A CD2 
1645 C CE1 . PHE A 204 ? 0.45757 0.55146 0.47750 -0.05651 0.01499  0.00571  240 PHE A CE1 
1646 C CE2 . PHE A 204 ? 0.49974 0.61110 0.51232 -0.06285 0.01877  0.01470  240 PHE A CE2 
1647 C CZ  . PHE A 204 ? 0.47379 0.58148 0.48687 -0.05737 0.01555  0.00672  240 PHE A CZ  
1648 N N   . PHE A 205 ? 0.54492 0.58281 0.56893 -0.06800 0.01505  -0.00061 241 PHE A N   
1649 C CA  . PHE A 205 ? 0.53555 0.55449 0.55946 -0.06839 0.01262  -0.00824 241 PHE A CA  
1650 C C   . PHE A 205 ? 0.59232 0.60464 0.60264 -0.05713 0.01505  -0.01701 241 PHE A C   
1651 O O   . PHE A 205 ? 0.53100 0.52618 0.53892 -0.05202 0.01631  -0.02260 241 PHE A O   
1652 C CB  . PHE A 205 ? 0.57987 0.60137 0.61053 -0.07849 0.00598  -0.01491 241 PHE A CB  
1653 C CG  . PHE A 205 ? 0.65596 0.67869 0.70365 -0.09053 0.00653  -0.00441 241 PHE A CG  
1654 C CD1 . PHE A 205 ? 0.57666 0.57727 0.63288 -0.09375 0.00740  0.00111  241 PHE A CD1 
1655 C CD2 . PHE A 205 ? 0.55145 0.59745 0.60706 -0.09733 0.00767  0.00153  241 PHE A CD2 
1656 C CE1 . PHE A 205 ? 0.67934 0.67986 0.75075 -0.10466 0.00983  0.01495  241 PHE A CE1 
1657 C CE2 . PHE A 205 ? 0.57081 0.62043 0.64136 -0.10793 0.01132  0.01414  241 PHE A CE2 
1658 C CZ  . PHE A 205 ? 0.69563 0.72191 0.77369 -0.11221 0.01262  0.02218  241 PHE A CZ  
1659 N N   . TYR A 206 ? 0.56847 0.59357 0.56954 -0.05197 0.01697  -0.01736 242 TYR A N   
1660 C CA  . TYR A 206 ? 0.53843 0.55977 0.52545 -0.04049 0.02269  -0.02069 242 TYR A CA  
1661 C C   . TYR A 206 ? 0.59488 0.61138 0.58956 -0.03473 0.03128  -0.01440 242 TYR A C   
1662 O O   . TYR A 206 ? 0.61415 0.62141 0.60218 -0.02596 0.03674  -0.01905 242 TYR A O   
1663 C CB  . TYR A 206 ? 0.56860 0.60308 0.54796 -0.03679 0.02405  -0.01717 242 TYR A CB  
1664 C CG  . TYR A 206 ? 0.55133 0.58430 0.51803 -0.02538 0.03348  -0.01383 242 TYR A CG  
1665 C CD1 . TYR A 206 ? 0.59750 0.62647 0.54128 -0.01616 0.03378  -0.02095 242 TYR A CD1 
1666 C CD2 . TYR A 206 ? 0.59939 0.63629 0.57738 -0.02394 0.04208  -0.00324 242 TYR A CD2 
1667 C CE1 . TYR A 206 ? 0.62310 0.65262 0.55276 -0.00463 0.04532  -0.01451 242 TYR A CE1 
1668 C CE2 . TYR A 206 ? 0.52021 0.55687 0.49101 -0.01499 0.05333  0.00326  242 TYR A CE2 
1669 C CZ  . TYR A 206 ? 0.60376 0.63716 0.54901 -0.00481 0.05632  -0.00079 242 TYR A CZ  
1670 O OH  . TYR A 206 ? 0.66786 0.70271 0.60336 0.00518  0.07026  0.00882  242 TYR A OH  
1671 N N   . PHE A 207 ? 0.55218 0.57704 0.56140 -0.03845 0.03203  -0.00506 243 PHE A N   
1672 C CA  . PHE A 207 ? 0.54146 0.56646 0.56371 -0.03361 0.03734  0.00067  243 PHE A CA  
1673 C C   . PHE A 207 ? 0.59619 0.60709 0.62319 -0.03122 0.03606  -0.00077 243 PHE A C   
1674 O O   . PHE A 207 ? 0.54568 0.55260 0.57803 -0.02201 0.04242  -0.00117 243 PHE A O   
1675 C CB  . PHE A 207 ? 0.46093 0.49871 0.49671 -0.03842 0.03396  0.00792  243 PHE A CB  
1676 C CG  . PHE A 207 ? 0.47729 0.52465 0.51472 -0.03902 0.03633  0.00897  243 PHE A CG  
1677 C CD1 . PHE A 207 ? 0.45471 0.50017 0.48575 -0.03362 0.04445  0.00908  243 PHE A CD1 
1678 C CD2 . PHE A 207 ? 0.48148 0.53819 0.52569 -0.04388 0.03073  0.01009  243 PHE A CD2 
1679 C CE1 . PHE A 207 ? 0.49897 0.54909 0.53396 -0.03422 0.04727  0.01268  243 PHE A CE1 
1680 C CE2 . PHE A 207 ? 0.54027 0.60090 0.58878 -0.04428 0.03231  0.00973  243 PHE A CE2 
1681 C CZ  . PHE A 207 ? 0.47331 0.52933 0.51907 -0.04002 0.04075  0.01225  243 PHE A CZ  
1682 N N   . LEU A 208 ? 0.53227 0.53542 0.55995 -0.03893 0.02901  -0.00041 244 LEU A N   
1683 C CA  . LEU A 208 ? 0.60831 0.59394 0.64368 -0.03725 0.02743  0.00125  244 LEU A CA  
1684 C C   . LEU A 208 ? 0.61462 0.58092 0.64222 -0.03070 0.02933  -0.01219 244 LEU A C   
1685 O O   . LEU A 208 ? 0.64412 0.59779 0.67758 -0.02099 0.03293  -0.01354 244 LEU A O   
1686 C CB  . LEU A 208 ? 0.63267 0.61444 0.67238 -0.04863 0.02138  0.00814  244 LEU A CB  
1687 C CG  . LEU A 208 ? 0.60604 0.60385 0.64995 -0.05174 0.01963  0.02195  244 LEU A CG  
1688 C CD1 . LEU A 208 ? 0.62529 0.62347 0.66993 -0.06306 0.01737  0.02915  244 LEU A CD1 
1689 C CD2 . LEU A 208 ? 0.55806 0.55214 0.61106 -0.04314 0.01918  0.03113  244 LEU A CD2 
1690 N N   . ARG A 209 ? 0.58778 0.55241 0.60187 -0.03436 0.02594  -0.02365 245 ARG A N   
1691 C CA  . ARG A 209 ? 0.74264 0.68812 0.74585 -0.02871 0.02427  -0.04045 245 ARG A CA  
1692 C C   . ARG A 209 ? 0.68439 0.63499 0.66901 -0.01380 0.03296  -0.04806 245 ARG A C   
1693 O O   . ARG A 209 ? 0.73362 0.66828 0.70670 -0.00405 0.03415  -0.06267 245 ARG A O   
1694 C CB  . ARG A 209 ? 0.68140 0.62480 0.68027 -0.03997 0.01338  -0.05098 245 ARG A CB  
1695 C CG  . ARG A 209 ? 0.67355 0.61273 0.69306 -0.05576 0.00733  -0.04253 245 ARG A CG  
1696 C CD  . ARG A 209 ? 0.77163 0.72150 0.79293 -0.06777 -0.00200 -0.05002 245 ARG A CD  
1697 N NE  . ARG A 209 ? 0.86803 0.80785 0.87647 -0.06411 -0.01016 -0.07215 245 ARG A NE  
1698 C CZ  . ARG A 209 ? 0.89560 0.81282 0.91393 -0.07081 -0.01889 -0.08607 245 ARG A CZ  
1699 N NH1 . ARG A 209 ? 0.92494 0.82453 0.96798 -0.08177 -0.01870 -0.07713 245 ARG A NH1 
1700 N NH2 . ARG A 209 ? 0.92271 0.83383 0.92536 -0.06607 -0.02857 -0.10946 245 ARG A NH2 
1701 N N   . GLY A 210 ? 0.66432 0.63563 0.64560 -0.01132 0.03981  -0.03849 246 GLY A N   
1702 C CA  . GLY A 210 ? 0.63777 0.61587 0.60028 0.00160  0.04998  -0.04162 246 GLY A CA  
1703 C C   . GLY A 210 ? 0.75526 0.73639 0.69152 0.00282  0.04435  -0.05094 246 GLY A C   
1704 O O   . GLY A 210 ? 0.67408 0.66315 0.59055 0.01408  0.05346  -0.04945 246 GLY A O   
1705 N N   . GLN A 211 ? 0.67067 0.64787 0.60742 -0.00796 0.02985  -0.05901 247 GLN A N   
1706 C CA  . GLN A 211 ? 0.75450 0.73838 0.66973 -0.00667 0.02085  -0.06871 247 GLN A CA  
1707 C C   . GLN A 211 ? 0.71870 0.70655 0.65074 -0.02287 0.00640  -0.07107 247 GLN A C   
1708 O O   . GLN A 211 ? 0.75055 0.73148 0.70619 -0.03417 0.00448  -0.06678 247 GLN A O   
1709 C CB  . GLN A 211 ? 0.72999 0.70110 0.61864 0.00537  0.01795  -0.08916 247 GLN A CB  
1710 C CG  . GLN A 211 ? 0.85418 0.80075 0.75478 0.00126  0.01125  -0.10459 247 GLN A CG  
1711 C CD  . GLN A 211 ? 0.94687 0.88833 0.86073 -0.01486 -0.00757 -0.11617 247 GLN A CD  
1712 O OE1 . GLN A 211 ? 0.98000 0.92083 0.92281 -0.03029 -0.01041 -0.10585 247 GLN A OE1 
1713 N NE2 . GLN A 211 ? 0.88111 0.82138 0.77423 -0.01111 -0.02049 -0.13731 247 GLN A NE2 
1714 N N   . LEU A 212 ? 0.76308 0.76418 0.68336 -0.02288 -0.00314 -0.07644 248 LEU A N   
1715 C CA  . LEU A 212 ? 0.76005 0.76827 0.69852 -0.03729 -0.01734 -0.08199 248 LEU A CA  
1716 C C   . LEU A 212 ? 0.74738 0.75123 0.67243 -0.03567 -0.03279 -0.10472 248 LEU A C   
1717 O O   . LEU A 212 ? 0.72016 0.72502 0.61320 -0.02045 -0.03353 -0.11305 248 LEU A O   
1718 C CB  . LEU A 212 ? 0.69003 0.72241 0.63486 -0.03975 -0.01842 -0.07011 248 LEU A CB  
1719 C CG  . LEU A 212 ? 0.64729 0.68355 0.60729 -0.04305 -0.00646 -0.05190 248 LEU A CG  
1720 C CD1 . LEU A 212 ? 0.58138 0.63780 0.54491 -0.04215 -0.00691 -0.04317 248 LEU A CD1 
1721 C CD2 . LEU A 212 ? 0.73023 0.75962 0.71452 -0.05651 -0.00647 -0.04857 248 LEU A CD2 
1722 N N   . PRO A 213 ? 0.80512 0.80414 0.75391 -0.05096 -0.04536 -0.11526 249 PRO A N   
1723 C CA  . PRO A 213 ? 0.78388 0.77683 0.72368 -0.05097 -0.06314 -0.14113 249 PRO A CA  
1724 C C   . PRO A 213 ? 0.72471 0.74385 0.64792 -0.04452 -0.07651 -0.14791 249 PRO A C   
1725 O O   . PRO A 213 ? 0.83287 0.85021 0.74165 -0.04103 -0.09338 -0.17132 249 PRO A O   
1726 C CB  . PRO A 213 ? 0.74174 0.72544 0.72201 -0.07298 -0.07186 -0.14560 249 PRO A CB  
1727 C CG  . PRO A 213 ? 0.72118 0.72001 0.72671 -0.08320 -0.06086 -0.12030 249 PRO A CG  
1728 C CD  . PRO A 213 ? 0.76203 0.76027 0.74732 -0.06901 -0.04350 -0.10385 249 PRO A CD  
1729 N N   . TRP A 214 ? 0.74149 0.78416 0.66590 -0.04155 -0.07101 -0.12944 250 TRP A N   
1730 C CA  . TRP A 214 ? 0.77512 0.84218 0.68234 -0.03164 -0.08286 -0.13239 250 TRP A CA  
1731 C C   . TRP A 214 ? 0.83393 0.90069 0.69985 -0.00963 -0.07151 -0.12222 250 TRP A C   
1732 O O   . TRP A 214 ? 0.85076 0.93666 0.70170 0.00100  -0.07699 -0.11618 250 TRP A O   
1733 C CB  . TRP A 214 ? 0.69633 0.79013 0.63500 -0.04130 -0.08557 -0.11958 250 TRP A CB  
1734 C CG  . TRP A 214 ? 0.74252 0.83464 0.69649 -0.04523 -0.06647 -0.09738 250 TRP A CG  
1735 C CD1 . TRP A 214 ? 0.68825 0.78076 0.62629 -0.03315 -0.05279 -0.08086 250 TRP A CD1 
1736 C CD2 . TRP A 214 ? 0.66732 0.75732 0.65522 -0.06226 -0.05989 -0.08973 250 TRP A CD2 
1737 N NE1 . TRP A 214 ? 0.74071 0.83179 0.70022 -0.04150 -0.04036 -0.06695 250 TRP A NE1 
1738 C CE2 . TRP A 214 ? 0.66728 0.75790 0.65441 -0.05813 -0.04399 -0.07121 250 TRP A CE2 
1739 C CE3 . TRP A 214 ? 0.71047 0.79758 0.72940 -0.08057 -0.06570 -0.09585 250 TRP A CE3 
1740 C CZ2 . TRP A 214 ? 0.65662 0.74722 0.66700 -0.06944 -0.03484 -0.05996 250 TRP A CZ2 
1741 C CZ3 . TRP A 214 ? 0.63944 0.72579 0.68255 -0.09212 -0.05393 -0.08063 250 TRP A CZ3 
1742 C CH2 . TRP A 214 ? 0.62154 0.71072 0.65742 -0.08543 -0.03918 -0.06350 250 TRP A CH2 
1743 N N   . GLN A 215 ? 0.83217 0.87850 0.68197 -0.00219 -0.05507 -0.11851 251 GLN A N   
1744 C CA  . GLN A 215 ? 0.86679 0.91264 0.67901 0.01803  -0.04195 -0.10880 251 GLN A CA  
1745 C C   . GLN A 215 ? 0.90902 0.95142 0.68034 0.03321  -0.05186 -0.12994 251 GLN A C   
1746 O O   . GLN A 215 ? 0.87958 0.91013 0.65334 0.02788  -0.06465 -0.15435 251 GLN A O   
1747 C CB  . GLN A 215 ? 0.82222 0.85300 0.63973 0.01969  -0.01907 -0.09544 251 GLN A CB  
1748 C CG  . GLN A 215 ? 0.78047 0.81526 0.63163 0.00792  -0.00938 -0.07527 251 GLN A CG  
1749 C CD  . GLN A 215 ? 0.77678 0.80169 0.63286 0.01148  0.01088  -0.06243 251 GLN A CD  
1750 O OE1 . GLN A 215 ? 0.76206 0.78411 0.64656 0.00068  0.01561  -0.05442 251 GLN A OE1 
1751 N NE2 . GLN A 215 ? 0.76479 0.78736 0.59347 0.02741  0.02293  -0.05997 251 GLN A NE2 
1752 N N   . GLY A 216 ? 0.99060 1.04224 0.72318 0.05286  -0.04584 -0.12034 252 GLY A N   
1753 C CA  . GLY A 216 ? 0.92114 0.97173 0.60574 0.07146  -0.05298 -0.13869 252 GLY A CA  
1754 C C   . GLY A 216 ? 1.00779 1.07168 0.68341 0.07106  -0.08356 -0.16221 252 GLY A C   
1755 O O   . GLY A 216 ? 0.98010 1.03963 0.62040 0.08294  -0.09497 -0.18686 252 GLY A O   
1756 N N   . LEU A 217 ? 0.97336 1.05532 0.68108 0.05844  -0.09779 -0.15684 253 LEU A N   
1757 C CA  . LEU A 217 ? 0.95853 1.05924 0.66525 0.05724  -0.12843 -0.17837 253 LEU A CA  
1758 C C   . LEU A 217 ? 1.01744 1.13759 0.67591 0.08208  -0.13588 -0.17182 253 LEU A C   
1759 O O   . LEU A 217 ? 1.06707 1.19138 0.71144 0.09407  -0.11855 -0.14277 253 LEU A O   
1760 C CB  . LEU A 217 ? 0.91142 1.02932 0.67403 0.03585  -0.13909 -0.17361 253 LEU A CB  
1761 C CG  . LEU A 217 ? 0.89648 0.99814 0.70732 0.01077  -0.13352 -0.17777 253 LEU A CG  
1762 C CD1 . LEU A 217 ? 0.83992 0.96488 0.70156 -0.00844 -0.14685 -0.17686 253 LEU A CD1 
1763 C CD2 . LEU A 217 ? 0.95436 1.03148 0.75773 0.00685  -0.14169 -0.20644 253 LEU A CD2 
1764 N N   . LYS A 218 ? 1.03251 1.16363 0.66583 0.09003  -0.16282 -0.19912 254 LYS A N   
1765 C CA  . LYS A 218 ? 1.14093 1.29248 0.72307 0.11574  -0.17478 -0.19597 254 LYS A CA  
1766 C C   . LYS A 218 ? 1.13103 1.31506 0.73879 0.11113  -0.20469 -0.20113 254 LYS A C   
1767 O O   . LYS A 218 ? 1.05179 1.24296 0.70920 0.08852  -0.22227 -0.21973 254 LYS A O   
1768 C CB  . LYS A 218 ? 1.21420 1.35820 0.73935 0.13355  -0.18540 -0.22519 254 LYS A CB  
1769 C CG  . LYS A 218 ? 1.33036 1.46265 0.79749 0.15871  -0.15708 -0.20752 254 LYS A CG  
1770 C CD  . LYS A 218 ? 1.27224 1.37514 0.75373 0.15021  -0.12916 -0.20705 254 LYS A CD  
1771 C CE  . LYS A 218 ? 1.36332 1.45997 0.78840 0.17626  -0.10139 -0.19240 254 LYS A CE  
1772 N NZ  . LYS A 218 ? 1.37263 1.44437 0.80937 0.17172  -0.07721 -0.19759 254 LYS A NZ  
1773 N N   . ALA A 219 ? 1.17874 1.38339 0.75412 0.13348  -0.20953 -0.18275 255 ALA A N   
1774 C CA  . ALA A 219 ? 1.17688 1.41688 0.76996 0.13603  -0.23882 -0.18567 255 ALA A CA  
1775 C C   . ALA A 219 ? 1.19933 1.45255 0.73768 0.16776  -0.24059 -0.16478 255 ALA A C   
1776 O O   . ALA A 219 ? 1.35147 1.58854 0.85108 0.18415  -0.21387 -0.13848 255 ALA A O   
1777 C CB  . ALA A 219 ? 1.14345 1.39383 0.80336 0.11680  -0.23217 -0.16768 255 ALA A CB  
1778 N N   . PRO A 220 ? 1.17465 1.45257 0.71717 0.17404  -0.26658 -0.17107 256 PRO A N   
1779 C CA  . PRO A 220 ? 1.20323 1.48852 0.70084 0.20233  -0.26450 -0.14628 256 PRO A CA  
1780 C C   . PRO A 220 ? 1.18292 1.46861 0.68257 0.21423  -0.24501 -0.10581 256 PRO A C   
1781 O O   . PRO A 220 ? 1.16878 1.44108 0.62401 0.23502  -0.22503 -0.07825 256 PRO A O   
1782 C CB  . PRO A 220 ? 1.12145 1.43740 0.63828 0.20214  -0.29975 -0.16374 256 PRO A CB  
1783 C CG  . PRO A 220 ? 1.12814 1.44295 0.68007 0.17615  -0.31719 -0.20282 256 PRO A CG  
1784 C CD  . PRO A 220 ? 1.10929 1.40720 0.69470 0.15589  -0.29822 -0.20203 256 PRO A CD  
1785 N N   . THR A 221 ? 1.13610 1.43639 0.68846 0.20151  -0.24926 -0.10082 257 THR A N   
1786 C CA  . THR A 221 ? 1.11918 1.41546 0.68505 0.20992  -0.23022 -0.06376 257 THR A CA  
1787 C C   . THR A 221 ? 1.11056 1.38203 0.72527 0.18350  -0.20222 -0.05761 257 THR A C   
1788 O O   . THR A 221 ? 1.15404 1.41479 0.78795 0.16162  -0.19928 -0.07974 257 THR A O   
1789 C CB  . THR A 221 ? 1.01235 1.34386 0.61063 0.21785  -0.25440 -0.05880 257 THR A CB  
1790 O OG1 . THR A 221 ? 1.00766 1.35518 0.67548 0.19028  -0.26338 -0.07850 257 THR A OG1 
1791 C CG2 . THR A 221 ? 0.95591 1.30477 0.53001 0.23115  -0.27899 -0.07003 257 THR A CG2 
1792 N N   . ASN A 222 ? 1.09428 1.35559 0.72862 0.18676  -0.18260 -0.02740 258 ASN A N   
1793 C CA  . ASN A 222 ? 1.09949 1.34052 0.77926 0.16379  -0.15884 -0.02189 258 ASN A CA  
1794 C C   . ASN A 222 ? 1.05230 1.31593 0.79363 0.14452  -0.17201 -0.03699 258 ASN A C   
1795 O O   . ASN A 222 ? 1.00706 1.25985 0.78279 0.12115  -0.16002 -0.04508 258 ASN A O   
1796 C CB  . ASN A 222 ? 1.14980 1.36877 0.82742 0.17407  -0.13342 0.01317  258 ASN A CB  
1797 C CG  . ASN A 222 ? 1.19139 1.37723 0.85322 0.16749  -0.10349 0.02397  258 ASN A CG  
1798 O OD1 . ASN A 222 ? 1.22994 1.40933 0.87658 0.15906  -0.10096 0.00637  258 ASN A OD1 
1799 N ND2 . ASN A 222 ? 1.18800 1.35282 0.85670 0.17152  -0.08110 0.05228  258 ASN A ND2 
1800 N N   . LYS A 223 ? 1.00476 1.30199 0.76101 0.15493  -0.19594 -0.03963 259 LYS A N   
1801 C CA  . LYS A 223 ? 0.99943 1.32460 0.81704 0.13757  -0.20749 -0.05327 259 LYS A CA  
1802 C C   . LYS A 223 ? 0.97652 1.30907 0.81342 0.11336  -0.22010 -0.08414 259 LYS A C   
1803 O O   . LYS A 223 ? 0.90951 1.24220 0.79253 0.08957  -0.21152 -0.09071 259 LYS A O   
1804 C CB  . LYS A 223 ? 1.05294 1.41719 0.88279 0.15632  -0.23224 -0.05037 259 LYS A CB  
1805 C CG  . LYS A 223 ? 1.07278 1.47578 0.96748 0.13941  -0.24747 -0.06729 259 LYS A CG  
1806 C CD  . LYS A 223 ? 1.14708 1.59319 1.05529 0.16044  -0.27364 -0.06490 259 LYS A CD  
1807 C CE  . LYS A 223 ? 1.20405 1.69576 1.17865 0.14190  -0.29167 -0.08543 259 LYS A CE  
1808 N NZ  . LYS A 223 ? 1.19079 1.68991 1.16818 0.12105  -0.31081 -0.11563 259 LYS A NZ  
1809 N N   . GLN A 224 ? 0.98422 1.32158 0.78510 0.11986  -0.24058 -0.10333 260 GLN A N   
1810 C CA  . GLN A 224 ? 0.89675 1.23492 0.71515 0.09733  -0.25370 -0.13468 260 GLN A CA  
1811 C C   . GLN A 224 ? 0.97426 1.27181 0.78656 0.08170  -0.22745 -0.13507 260 GLN A C   
1812 O O   . GLN A 224 ? 0.94224 1.23483 0.78919 0.05732  -0.22909 -0.15275 260 GLN A O   
1813 C CB  . GLN A 224 ? 0.94917 1.30049 0.72585 0.11103  -0.28377 -0.15816 260 GLN A CB  
1814 C CG  . GLN A 224 ? 0.85978 1.25416 0.63834 0.12990  -0.31303 -0.15740 260 GLN A CG  
1815 C CD  . GLN A 224 ? 0.93892 1.33197 0.67455 0.14167  -0.33272 -0.17358 260 GLN A CD  
1816 O OE1 . GLN A 224 ? 1.03429 1.40632 0.75091 0.13206  -0.33484 -0.19671 260 GLN A OE1 
1817 N NE2 . GLN A 224 ? 0.87996 1.29342 0.60094 0.16303  -0.34589 -0.16102 260 GLN A NE2 
1818 N N   . LYS A 225 ? 0.99549 1.26452 0.76722 0.09539  -0.20308 -0.11447 261 LYS A N   
1819 C CA  . LYS A 225 ? 1.02894 1.26327 0.79965 0.08221  -0.17759 -0.11244 261 LYS A CA  
1820 C C   . LYS A 225 ? 0.96208 1.19326 0.78666 0.06128  -0.16191 -0.10272 261 LYS A C   
1821 O O   . LYS A 225 ? 0.88689 1.10312 0.73349 0.04134  -0.15465 -0.11274 261 LYS A O   
1822 C CB  . LYS A 225 ? 1.00231 1.21310 0.72414 0.10163  -0.15479 -0.09035 261 LYS A CB  
1823 C CG  . LYS A 225 ? 1.01111 1.19120 0.74096 0.08969  -0.12594 -0.08156 261 LYS A CG  
1824 C CD  . LYS A 225 ? 1.07571 1.23777 0.76243 0.10839  -0.10363 -0.05907 261 LYS A CD  
1825 C CE  . LYS A 225 ? 1.05079 1.18876 0.75747 0.09638  -0.07544 -0.04552 261 LYS A CE  
1826 N NZ  . LYS A 225 ? 1.10567 1.23077 0.82549 0.08019  -0.07361 -0.06641 261 LYS A NZ  
1827 N N   . TYR A 226 ? 1.01270 1.25718 0.85714 0.06724  -0.15663 -0.08331 262 TYR A N   
1828 C CA  . TYR A 226 ? 0.98462 1.23021 0.87655 0.05009  -0.14304 -0.07614 262 TYR A CA  
1829 C C   . TYR A 226 ? 0.94569 1.21526 0.88379 0.02932  -0.15801 -0.09485 262 TYR A C   
1830 O O   . TYR A 226 ? 1.00213 1.26667 0.97357 0.01046  -0.14541 -0.09355 262 TYR A O   
1831 C CB  . TYR A 226 ? 1.02003 1.27535 0.92180 0.06405  -0.13641 -0.05513 262 TYR A CB  
1832 C CG  . TYR A 226 ? 1.15851 1.38303 1.03408 0.07517  -0.11357 -0.03305 262 TYR A CG  
1833 C CD1 . TYR A 226 ? 1.24379 1.44706 1.07371 0.08575  -0.10704 -0.02797 262 TYR A CD1 
1834 C CD2 . TYR A 226 ? 1.19575 1.41345 1.09408 0.07512  -0.09826 -0.01804 262 TYR A CD2 
1835 C CE1 . TYR A 226 ? 1.29799 1.47551 1.11097 0.09375  -0.08503 -0.00613 262 TYR A CE1 
1836 C CE2 . TYR A 226 ? 1.27888 1.46779 1.15963 0.08287  -0.07896 0.00084  262 TYR A CE2 
1837 C CZ  . TYR A 226 ? 1.42296 1.59266 1.26370 0.09110  -0.07204 0.00795  262 TYR A CZ  
1838 O OH  . TYR A 226 ? 1.44958 1.59291 1.27950 0.09670  -0.05167 0.02835  262 TYR A OH  
1839 N N   . GLU A 227 ? 0.86919 1.16595 0.81084 0.03224  -0.18503 -0.11163 263 GLU A N   
1840 C CA  . GLU A 227 ? 0.84371 1.16488 0.83549 0.01027  -0.20004 -0.12952 263 GLU A CA  
1841 C C   . GLU A 227 ? 0.83684 1.13255 0.82915 -0.00913 -0.20036 -0.14787 263 GLU A C   
1842 O O   . GLU A 227 ? 0.74363 1.04051 0.77992 -0.03253 -0.19544 -0.15126 263 GLU A O   
1843 C CB  . GLU A 227 ? 0.86568 1.22688 0.86610 0.01923  -0.23161 -0.14309 263 GLU A CB  
1844 C CG  . GLU A 227 ? 0.85251 1.24352 0.91232 -0.00499 -0.24871 -0.16180 263 GLU A CG  
1845 C CD  . GLU A 227 ? 0.79973 1.23636 0.87424 0.00449  -0.28163 -0.17489 263 GLU A CD  
1846 O OE1 . GLU A 227 ? 0.93284 1.38103 0.97573 0.03171  -0.28828 -0.16402 263 GLU A OE1 
1847 O OE2 . GLU A 227 ? 0.85856 1.31966 0.97821 -0.01529 -0.30153 -0.19537 263 GLU A OE2 
1848 N N   . LYS A 228 ? 0.79467 1.06676 0.73826 0.00154  -0.20503 -0.15898 264 LYS A N   
1849 C CA  . LYS A 228 ? 0.81555 1.05873 0.75738 -0.01351 -0.20418 -0.17727 264 LYS A CA  
1850 C C   . LYS A 228 ? 0.82090 1.03539 0.77472 -0.02514 -0.17514 -0.16112 264 LYS A C   
1851 O O   . LYS A 228 ? 0.76188 0.96105 0.74293 -0.04529 -0.17276 -0.16988 264 LYS A O   
1852 C CB  . LYS A 228 ? 0.84079 1.06533 0.72256 0.00515  -0.21157 -0.19163 264 LYS A CB  
1853 C CG  . LYS A 228 ? 0.90835 1.15447 0.78042 0.00999  -0.24622 -0.22004 264 LYS A CG  
1854 C CD  . LYS A 228 ? 0.90598 1.12908 0.71573 0.02757  -0.25055 -0.23757 264 LYS A CD  
1855 C CE  . LYS A 228 ? 0.98434 1.22691 0.78329 0.03122  -0.28822 -0.27172 264 LYS A CE  
1856 N NZ  . LYS A 228 ? 1.06690 1.28607 0.80125 0.04975  -0.29158 -0.29215 264 LYS A NZ  
1857 N N   . ILE A 229 ? 0.80778 1.01400 0.74254 -0.01246 -0.15389 -0.13726 265 ILE A N   
1858 C CA  . ILE A 229 ? 0.77852 0.96218 0.72543 -0.02220 -0.12888 -0.12220 265 ILE A CA  
1859 C C   . ILE A 229 ? 0.73418 0.93464 0.73334 -0.04182 -0.12572 -0.11669 265 ILE A C   
1860 O O   . ILE A 229 ? 0.73284 0.91804 0.75333 -0.05891 -0.11733 -0.11719 265 ILE A O   
1861 C CB  . ILE A 229 ? 0.74538 0.91930 0.66502 -0.00511 -0.10980 -0.09981 265 ILE A CB  
1862 C CG1 . ILE A 229 ? 0.83241 0.98771 0.70149 0.01241  -0.10700 -0.10224 265 ILE A CG1 
1863 C CG2 . ILE A 229 ? 0.77112 0.92918 0.70951 -0.01562 -0.08793 -0.08547 265 ILE A CG2 
1864 C CD1 . ILE A 229 ? 0.78879 0.93354 0.63494 0.02744  -0.08710 -0.07853 265 ILE A CD1 
1865 N N   . GLY A 230 ? 0.76155 0.99470 0.78179 -0.03813 -0.13161 -0.11027 266 GLY A N   
1866 C CA  . GLY A 230 ? 0.73336 0.98833 0.80295 -0.05479 -0.12705 -0.10494 266 GLY A CA  
1867 C C   . GLY A 230 ? 0.72587 0.98814 0.83187 -0.07724 -0.13977 -0.12073 266 GLY A C   
1868 O O   . GLY A 230 ? 0.67915 0.94276 0.81982 -0.09538 -0.12855 -0.11373 266 GLY A O   
1869 N N   . ASP A 231 ? 0.71548 0.98181 0.81395 -0.07630 -0.16345 -0.14204 267 ASP A N   
1870 C CA  . ASP A 231 ? 0.69543 0.96387 0.83097 -0.09915 -0.17804 -0.16035 267 ASP A CA  
1871 C C   . ASP A 231 ? 0.75507 0.98082 0.88735 -0.11232 -0.16509 -0.16131 267 ASP A C   
1872 O O   . ASP A 231 ? 0.74974 0.97317 0.92488 -0.13525 -0.16265 -0.16114 267 ASP A O   
1873 C CB  . ASP A 231 ? 0.68474 0.96387 0.80644 -0.09270 -0.20886 -0.18690 267 ASP A CB  
1874 C CG  . ASP A 231 ? 0.85150 1.18152 1.00144 -0.08860 -0.22803 -0.18944 267 ASP A CG  
1875 O OD1 . ASP A 231 ? 0.83892 1.19782 1.04273 -0.10344 -0.22264 -0.17994 267 ASP A OD1 
1876 O OD2 . ASP A 231 ? 0.87296 1.21611 0.99104 -0.06918 -0.24809 -0.20009 267 ASP A OD2 
1877 N N   . LYS A 232 ? 0.69841 0.89080 0.78238 -0.09753 -0.15602 -0.16084 268 LYS A N   
1878 C CA  . LYS A 232 ? 0.76168 0.91446 0.84266 -0.10646 -0.14324 -0.16054 268 LYS A CA  
1879 C C   . LYS A 232 ? 0.75163 0.90215 0.85662 -0.11673 -0.12018 -0.13563 268 LYS A C   
1880 O O   . LYS A 232 ? 0.75937 0.88874 0.88589 -0.13248 -0.11359 -0.13318 268 LYS A O   
1881 C CB  . LYS A 232 ? 0.77697 0.90148 0.80351 -0.08592 -0.13660 -0.16386 268 LYS A CB  
1882 C CG  . LYS A 232 ? 0.82786 0.91204 0.84992 -0.09117 -0.12626 -0.16747 268 LYS A CG  
1883 C CD  . LYS A 232 ? 0.82780 0.89430 0.85861 -0.10065 -0.14572 -0.19647 268 LYS A CD  
1884 C CE  . LYS A 232 ? 0.90552 0.92887 0.92002 -0.09705 -0.13531 -0.20218 268 LYS A CE  
1885 N NZ  . LYS A 232 ? 0.97344 0.97323 0.99451 -0.10439 -0.15435 -0.23360 268 LYS A NZ  
1886 N N   . LYS A 233 ? 0.75342 0.92434 0.85385 -0.10696 -0.10841 -0.11733 269 LYS A N   
1887 C CA  . LYS A 233 ? 0.63718 0.80929 0.75560 -0.11435 -0.08804 -0.09602 269 LYS A CA  
1888 C C   . LYS A 233 ? 0.76331 0.95514 0.93221 -0.13629 -0.08863 -0.09262 269 LYS A C   
1889 O O   . LYS A 233 ? 0.79208 0.97023 0.97645 -0.14860 -0.07509 -0.08018 269 LYS A O   
1890 C CB  . LYS A 233 ? 0.66481 0.85497 0.76908 -0.09848 -0.07825 -0.08202 269 LYS A CB  
1891 C CG  . LYS A 233 ? 0.67777 0.84518 0.73821 -0.07991 -0.07150 -0.07873 269 LYS A CG  
1892 C CD  . LYS A 233 ? 0.66738 0.84871 0.71915 -0.06584 -0.06302 -0.06566 269 LYS A CD  
1893 C CE  . LYS A 233 ? 0.67457 0.83257 0.68949 -0.05041 -0.05486 -0.06019 269 LYS A CE  
1894 N NZ  . LYS A 233 ? 0.64401 0.81053 0.65338 -0.03743 -0.04788 -0.04829 269 LYS A NZ  
1895 N N   . ARG A 234 ? 0.71752 0.94318 0.91419 -0.14119 -0.10394 -0.10204 270 ARG A N   
1896 C CA  . ARG A 234 ? 0.69746 0.94615 0.94906 -0.16377 -0.10409 -0.09855 270 ARG A CA  
1897 C C   . ARG A 234 ? 0.71458 0.93825 0.98837 -0.18393 -0.11490 -0.11225 270 ARG A C   
1898 O O   . ARG A 234 ? 0.80892 1.04208 1.13036 -0.20596 -0.11065 -0.10501 270 ARG A O   
1899 C CB  . ARG A 234 ? 0.70800 1.00604 0.98848 -0.16197 -0.11772 -0.10448 270 ARG A CB  
1900 C CG  . ARG A 234 ? 0.69238 1.01289 0.95320 -0.14000 -0.10897 -0.09295 270 ARG A CG  
1901 C CD  . ARG A 234 ? 0.82438 1.19577 1.11951 -0.13711 -0.12229 -0.09775 270 ARG A CD  
1902 N NE  . ARG A 234 ? 0.90149 1.28068 1.20189 -0.13920 -0.15147 -0.12062 270 ARG A NE  
1903 C CZ  . ARG A 234 ? 0.86162 1.28103 1.17788 -0.12998 -0.17060 -0.12915 270 ARG A CZ  
1904 N NH1 . ARG A 234 ? 0.91660 1.37097 1.24651 -0.11688 -0.16271 -0.11644 270 ARG A NH1 
1905 N NH2 . ARG A 234 ? 0.90462 1.32944 1.22231 -0.13229 -0.19945 -0.15222 270 ARG A NH2 
1906 N N   . THR A 235 ? 0.76559 0.95701 1.00690 -0.17647 -0.12770 -0.13159 271 THR A N   
1907 C CA  . THR A 235 ? 0.76177 0.92258 1.02060 -0.19302 -0.13893 -0.14844 271 THR A CA  
1908 C C   . THR A 235 ? 0.80134 0.91680 1.04703 -0.19509 -0.12135 -0.13681 271 THR A C   
1909 O O   . THR A 235 ? 0.71820 0.80803 0.99249 -0.21317 -0.12393 -0.14121 271 THR A O   
1910 C CB  . THR A 235 ? 0.79324 0.94441 1.02222 -0.18159 -0.16391 -0.17983 271 THR A CB  
1911 O OG1 . THR A 235 ? 0.85415 1.04878 1.08294 -0.17209 -0.17955 -0.18677 271 THR A OG1 
1912 C CG2 . THR A 235 ? 1.00982 1.13884 1.26980 -0.20172 -0.18217 -0.20390 271 THR A CG2 
1913 N N   . THR A 236 ? 0.80179 0.90691 1.00849 -0.17719 -0.10431 -0.12166 272 THR A N   
1914 C CA  . THR A 236 ? 0.81256 0.87818 1.00486 -0.17549 -0.08968 -0.11125 272 THR A CA  
1915 C C   . THR A 236 ? 0.79019 0.86417 1.00344 -0.18460 -0.06939 -0.08173 272 THR A C   
1916 O O   . THR A 236 ? 0.78212 0.87929 0.98136 -0.17419 -0.05804 -0.06705 272 THR A O   
1917 C CB  . THR A 236 ? 0.80166 0.85320 0.94241 -0.15103 -0.08393 -0.11289 272 THR A CB  
1918 O OG1 . THR A 236 ? 0.81597 0.86215 0.93220 -0.14053 -0.10122 -0.13905 272 THR A OG1 
1919 C CG2 . THR A 236 ? 0.84647 0.86092 0.97667 -0.14805 -0.07039 -0.10318 272 THR A CG2 
1920 N N   . PRO A 237 ? 0.77013 0.82527 1.01505 -0.20273 -0.06412 -0.07202 273 PRO A N   
1921 C CA  . PRO A 237 ? 0.74354 0.80593 1.00073 -0.20856 -0.04343 -0.04150 273 PRO A CA  
1922 C C   . PRO A 237 ? 0.77880 0.82422 0.99577 -0.19003 -0.03061 -0.02898 273 PRO A C   
1923 O O   . PRO A 237 ? 0.82882 0.84771 1.01747 -0.17687 -0.03515 -0.04105 273 PRO A O   
1924 C CB  . PRO A 237 ? 0.75414 0.79013 1.05019 -0.23040 -0.04239 -0.03478 273 PRO A CB  
1925 C CG  . PRO A 237 ? 0.75046 0.77875 1.06779 -0.24096 -0.06503 -0.06462 273 PRO A CG  
1926 C CD  . PRO A 237 ? 0.81158 0.83730 1.08339 -0.21878 -0.07725 -0.08838 273 PRO A CD  
1927 N N   . ALA A 238 ? 0.68871 0.75262 0.90449 -0.18864 -0.01438 -0.00508 274 ALA A N   
1928 C CA  . ALA A 238 ? 0.74419 0.79639 0.92646 -0.17259 -0.00412 0.00676  274 ALA A CA  
1929 C C   . ALA A 238 ? 0.83331 0.84420 1.01360 -0.17321 -0.00188 0.01337  274 ALA A C   
1930 O O   . ALA A 238 ? 0.76528 0.75953 0.91858 -0.15785 -0.00047 0.01238  274 ALA A O   
1931 C CB  . ALA A 238 ? 0.62810 0.70930 0.80881 -0.17098 0.01078  0.02835  274 ALA A CB  
1932 N N   . VAL A 239 ? 0.76285 0.75689 0.97484 -0.19058 -0.00125 0.02098  275 VAL A N   
1933 C CA  . VAL A 239 ? 0.82487 0.77532 1.03756 -0.18988 0.00006  0.02726  275 VAL A CA  
1934 C C   . VAL A 239 ? 0.84032 0.76160 1.04047 -0.18113 -0.01341 -0.00100 275 VAL A C   
1935 O O   . VAL A 239 ? 0.87977 0.77153 1.06411 -0.16859 -0.01162 -0.00047 275 VAL A O   
1936 C CB  . VAL A 239 ? 0.84879 0.78528 1.10215 -0.21174 0.00472  0.04393  275 VAL A CB  
1937 C CG1 . VAL A 239 ? 0.93486 0.82251 1.18960 -0.20904 0.00645  0.05306  275 VAL A CG1 
1938 C CG2 . VAL A 239 ? 0.77926 0.74984 1.04076 -0.21806 0.02105  0.07308  275 VAL A CG2 
1939 N N   . THR A 240 ? 0.84359 0.77507 1.04910 -0.18554 -0.02706 -0.02625 276 THR A N   
1940 C CA  . THR A 240 ? 0.86279 0.77134 1.04804 -0.17389 -0.03924 -0.05466 276 THR A CA  
1941 C C   . THR A 240 ? 0.85226 0.76800 0.99635 -0.15032 -0.03352 -0.05553 276 THR A C   
1942 O O   . THR A 240 ? 0.98529 0.87481 1.11091 -0.13660 -0.03381 -0.06583 276 THR A O   
1943 C CB  . THR A 240 ? 0.86807 0.79229 1.06358 -0.18195 -0.05670 -0.08069 276 THR A CB  
1944 O OG1 . THR A 240 ? 0.78389 0.70340 1.02594 -0.20663 -0.06229 -0.07972 276 THR A OG1 
1945 C CG2 . THR A 240 ? 0.87072 0.77040 1.04037 -0.16846 -0.06934 -0.11126 276 THR A CG2 
1946 N N   . LEU A 241 ? 0.83846 0.78952 0.97067 -0.14530 -0.02758 -0.04499 277 LEU A N   
1947 C CA  . LEU A 241 ? 0.78475 0.74211 0.88492 -0.12587 -0.02089 -0.04246 277 LEU A CA  
1948 C C   . LEU A 241 ? 0.78917 0.72859 0.88577 -0.11912 -0.01051 -0.02531 277 LEU A C   
1949 O O   . LEU A 241 ? 0.77550 0.70695 0.85265 -0.10350 -0.00716 -0.02847 277 LEU A O   
1950 C CB  . LEU A 241 ? 0.72920 0.72386 0.82266 -0.12342 -0.01710 -0.03432 277 LEU A CB  
1951 C CG  . LEU A 241 ? 0.74538 0.76247 0.83633 -0.12326 -0.02750 -0.04978 277 LEU A CG  
1952 C CD1 . LEU A 241 ? 0.73750 0.78778 0.82603 -0.11975 -0.02196 -0.03900 277 LEU A CD1 
1953 C CD2 . LEU A 241 ? 0.70727 0.71253 0.76972 -0.10822 -0.03328 -0.06747 277 LEU A CD2 
1954 N N   . CYS A 242 ? 0.74963 0.68498 0.86580 -0.13002 -0.00505 -0.00566 278 CYS A N   
1955 C CA  . CYS A 242 ? 0.78243 0.70577 0.89470 -0.12291 0.00332  0.01419  278 CYS A CA  
1956 C C   . CYS A 242 ? 0.80556 0.68758 0.92779 -0.12120 0.00143  0.01252  278 CYS A C   
1957 O O   . CYS A 242 ? 0.80272 0.67128 0.93068 -0.11944 0.00707  0.03320  278 CYS A O   
1958 C CB  . CYS A 242 ? 0.70849 0.65034 0.83096 -0.13255 0.01136  0.03903  278 CYS A CB  
1959 S SG  . CYS A 242 ? 0.77579 0.72936 0.87772 -0.11825 0.01920  0.06010  278 CYS A SG  
1960 N N   . ASP A 243 ? 0.85077 0.71190 0.97360 -0.11999 -0.00694 -0.01203 279 ASP A N   
1961 C CA  . ASP A 243 ? 0.95962 0.77768 1.09283 -0.11706 -0.00944 -0.01805 279 ASP A CA  
1962 C C   . ASP A 243 ? 0.88270 0.69141 1.00116 -0.09617 -0.00279 -0.01077 279 ASP A C   
1963 O O   . ASP A 243 ? 0.84923 0.67253 0.94655 -0.08138 -0.00101 -0.02149 279 ASP A O   
1964 C CB  . ASP A 243 ? 1.01155 0.81266 1.14257 -0.11734 -0.02103 -0.05113 279 ASP A CB  
1965 C CG  . ASP A 243 ? 1.07974 0.83211 1.22810 -0.11844 -0.02556 -0.06075 279 ASP A CG  
1966 O OD1 . ASP A 243 ? 1.12070 0.85234 1.29054 -0.12489 -0.02035 -0.03837 279 ASP A OD1 
1967 O OD2 . ASP A 243 ? 1.15091 0.88438 1.28995 -0.11160 -0.03433 -0.09076 279 ASP A OD2 
1968 N N   . GLY A 244 ? 0.82144 0.60742 0.95329 -0.09470 0.00117  0.00917  280 GLY A N   
1969 C CA  . GLY A 244 ? 0.84532 0.62681 0.96845 -0.07458 0.00603  0.01841  280 GLY A CA  
1970 C C   . GLY A 244 ? 0.79990 0.61993 0.90872 -0.06796 0.01076  0.03396  280 GLY A C   
1971 O O   . GLY A 244 ? 0.78445 0.60893 0.88750 -0.05108 0.01309  0.03703  280 GLY A O   
1972 N N   . LEU A 245 ? 0.75452 0.60324 0.85984 -0.08033 0.01178  0.04240  281 LEU A N   
1973 C CA  . LEU A 245 ? 0.76210 0.64559 0.85371 -0.07509 0.01476  0.05385  281 LEU A CA  
1974 C C   . LEU A 245 ? 0.74721 0.64072 0.84171 -0.08362 0.01813  0.07937  281 LEU A C   
1975 O O   . LEU A 245 ? 0.80042 0.68080 0.90945 -0.09759 0.01992  0.08766  281 LEU A O   
1976 C CB  . LEU A 245 ? 0.70606 0.61723 0.78595 -0.07809 0.01396  0.03813  281 LEU A CB  
1977 C CG  . LEU A 245 ? 0.69183 0.59779 0.76291 -0.06791 0.01271  0.01592  281 LEU A CG  
1978 C CD1 . LEU A 245 ? 0.73775 0.66835 0.79721 -0.07131 0.01165  0.00450  281 LEU A CD1 
1979 C CD2 . LEU A 245 ? 0.68521 0.59354 0.75288 -0.05103 0.01631  0.01926  281 LEU A CD2 
1980 N N   . PRO A 246 ? 0.71587 0.63304 0.79728 -0.07537 0.01924  0.09240  282 PRO A N   
1981 C CA  . PRO A 246 ? 0.66134 0.59197 0.73811 -0.08080 0.02346  0.11632  282 PRO A CA  
1982 C C   . PRO A 246 ? 0.73864 0.68806 0.81846 -0.09652 0.02801  0.11384  282 PRO A C   
1983 O O   . PRO A 246 ? 0.69280 0.66464 0.76557 -0.09707 0.02666  0.09786  282 PRO A O   
1984 C CB  . PRO A 246 ? 0.69318 0.65010 0.75163 -0.06734 0.02036  0.12042  282 PRO A CB  
1985 C CG  . PRO A 246 ? 0.71819 0.66519 0.78142 -0.05433 0.01528  0.10792  282 PRO A CG  
1986 C CD  . PRO A 246 ? 0.73040 0.66198 0.80237 -0.05994 0.01638  0.08656  282 PRO A CD  
1987 N N   . GLN A 247 ? 0.71414 0.65497 0.80743 -0.10900 0.03417  0.13158  283 GLN A N   
1988 C CA  . GLN A 247 ? 0.80011 0.75873 0.90614 -0.12551 0.03908  0.12937  283 GLN A CA  
1989 C C   . GLN A 247 ? 0.71708 0.71669 0.80559 -0.12269 0.04433  0.13263  283 GLN A C   
1990 O O   . GLN A 247 ? 0.75404 0.77452 0.85349 -0.13332 0.04824  0.12775  283 GLN A O   
1991 C CB  . GLN A 247 ? 0.76383 0.70470 0.89390 -0.14066 0.04648  0.15103  283 GLN A CB  
1992 C CG  . GLN A 247 ? 0.90054 0.80024 1.05624 -0.14885 0.04004  0.13996  283 GLN A CG  
1993 C CD  . GLN A 247 ? 0.90828 0.81350 1.07743 -0.15867 0.03189  0.10997  283 GLN A CD  
1994 O OE1 . GLN A 247 ? 0.90784 0.84325 1.08611 -0.16960 0.03443  0.10752  283 GLN A OE1 
1995 N NE2 . GLN A 247 ? 0.92479 0.80286 1.09401 -0.15287 0.02190  0.08681  283 GLN A NE2 
1996 N N   . GLN A 248 ? 0.73368 0.74611 0.79711 -0.10801 0.04348  0.13892  284 GLN A N   
1997 C CA  . GLN A 248 ? 0.73133 0.77949 0.77643 -0.10335 0.04650  0.13565  284 GLN A CA  
1998 C C   . GLN A 248 ? 0.61160 0.67206 0.65900 -0.10359 0.04154  0.10948  284 GLN A C   
1999 O O   . GLN A 248 ? 0.60936 0.69700 0.65078 -0.10342 0.04546  0.10495  284 GLN A O   
2000 C CB  . GLN A 248 ? 0.69598 0.75314 0.71465 -0.08720 0.04221  0.14183  284 GLN A CB  
2001 C CG  . GLN A 248 ? 0.71470 0.76975 0.72174 -0.08336 0.04772  0.17120  284 GLN A CG  
2002 C CD  . GLN A 248 ? 0.69135 0.71511 0.70494 -0.07730 0.04162  0.18189  284 GLN A CD  
2003 O OE1 . GLN A 248 ? 0.78026 0.77826 0.81442 -0.08138 0.03783  0.17080  284 GLN A OE1 
2004 N NE2 . GLN A 248 ? 0.73549 0.76209 0.73001 -0.06539 0.04010  0.20284  284 GLN A NE2 
2005 N N   . PHE A 249 ? 0.65411 0.69531 0.70856 -0.10211 0.03382  0.09301  285 PHE A N   
2006 C CA  . PHE A 249 ? 0.62471 0.67637 0.67888 -0.10113 0.02975  0.07165  285 PHE A CA  
2007 C C   . PHE A 249 ? 0.63144 0.69051 0.70379 -0.11398 0.03096  0.06601  285 PHE A C   
2008 O O   . PHE A 249 ? 0.56947 0.64965 0.64097 -0.11321 0.03028  0.05546  285 PHE A O   
2009 C CB  . PHE A 249 ? 0.63495 0.66664 0.68752 -0.09377 0.02322  0.05795  285 PHE A CB  
2010 C CG  . PHE A 249 ? 0.58299 0.61814 0.62319 -0.08113 0.02098  0.05848  285 PHE A CG  
2011 C CD1 . PHE A 249 ? 0.58083 0.63450 0.61215 -0.07585 0.01972  0.04948  285 PHE A CD1 
2012 C CD2 . PHE A 249 ? 0.61491 0.63471 0.65617 -0.07453 0.01924  0.06773  285 PHE A CD2 
2013 C CE1 . PHE A 249 ? 0.56698 0.62471 0.59316 -0.06660 0.01622  0.04864  285 PHE A CE1 
2014 C CE2 . PHE A 249 ? 0.53941 0.56693 0.57494 -0.06361 0.01541  0.06741  285 PHE A CE2 
2015 C CZ  . PHE A 249 ? 0.60821 0.65523 0.63743 -0.06085 0.01361  0.05729  285 PHE A CZ  
2016 N N   . ALA A 250 ? 0.61849 0.65992 0.71050 -0.12573 0.03160  0.07237  286 ALA A N   
2017 C CA  . ALA A 250 ? 0.65118 0.70376 0.76737 -0.14046 0.03174  0.06829  286 ALA A CA  
2018 C C   . ALA A 250 ? 0.66635 0.75042 0.78831 -0.14568 0.04322  0.08445  286 ALA A C   
2019 O O   . ALA A 250 ? 0.69545 0.80602 0.83104 -0.15093 0.04406  0.07762  286 ALA A O   
2020 C CB  . ALA A 250 ? 0.65357 0.67596 0.79361 -0.15323 0.02856  0.06979  286 ALA A CB  
2021 N N   . GLU A 251 ? 0.60413 0.68771 0.71510 -0.14260 0.05245  0.10641  287 GLU A N   
2022 C CA  . GLU A 251 ? 0.66243 0.77815 0.77144 -0.14387 0.06581  0.12248  287 GLU A CA  
2023 C C   . GLU A 251 ? 0.66328 0.80815 0.75356 -0.13149 0.06537  0.10834  287 GLU A C   
2024 O O   . GLU A 251 ? 0.51512 0.69137 0.61365 -0.13363 0.07407  0.11019  287 GLU A O   
2025 C CB  . GLU A 251 ? 0.64930 0.75752 0.74059 -0.13856 0.07409  0.14832  287 GLU A CB  
2026 C CG  . GLU A 251 ? 0.78150 0.92005 0.87045 -0.14084 0.09113  0.16994  287 GLU A CG  
2027 C CD  . GLU A 251 ? 0.88302 1.01077 0.95295 -0.13541 0.09868  0.19878  287 GLU A CD  
2028 O OE1 . GLU A 251 ? 0.84490 0.93967 0.91041 -0.13150 0.08971  0.20204  287 GLU A OE1 
2029 O OE2 . GLU A 251 ? 0.96301 1.11644 1.02135 -0.13328 0.11399  0.21886  287 GLU A OE2 
2030 N N   . TYR A 252 ? 0.57167 0.70644 0.64019 -0.11846 0.05594  0.09419  288 TYR A N   
2031 C CA  . TYR A 252 ? 0.59960 0.75520 0.65392 -0.10738 0.05422  0.07935  288 TYR A CA  
2032 C C   . TYR A 252 ? 0.50877 0.67657 0.58218 -0.11176 0.05078  0.06440  288 TYR A C   
2033 O O   . TYR A 252 ? 0.53858 0.73405 0.61429 -0.10795 0.05585  0.06074  288 TYR A O   
2034 C CB  . TYR A 252 ? 0.54696 0.68664 0.58155 -0.09546 0.04474  0.06866  288 TYR A CB  
2035 C CG  . TYR A 252 ? 0.53817 0.69097 0.56455 -0.08614 0.04140  0.05164  288 TYR A CG  
2036 C CD1 . TYR A 252 ? 0.53955 0.71070 0.54895 -0.07665 0.04473  0.04992  288 TYR A CD1 
2037 C CD2 . TYR A 252 ? 0.53785 0.68303 0.57211 -0.08570 0.03484  0.03737  288 TYR A CD2 
2038 C CE1 . TYR A 252 ? 0.47109 0.64911 0.47595 -0.06807 0.04138  0.03382  288 TYR A CE1 
2039 C CE2 . TYR A 252 ? 0.53498 0.68838 0.56343 -0.07683 0.03250  0.02498  288 TYR A CE2 
2040 C CZ  . TYR A 252 ? 0.49595 0.66404 0.51190 -0.06859 0.03568  0.02293  288 TYR A CZ  
2041 O OH  . TYR A 252 ? 0.49142 0.66293 0.50439 -0.05961 0.03305  0.00986  288 TYR A OH  
2042 N N   . LEU A 253 ? 0.47340 0.62182 0.55945 -0.11782 0.04149  0.05483  289 LEU A N   
2043 C CA  . LEU A 253 ? 0.52428 0.68472 0.62374 -0.11918 0.03485  0.03966  289 LEU A CA  
2044 C C   . LEU A 253 ? 0.55230 0.74037 0.68085 -0.13076 0.04039  0.04520  289 LEU A C   
2045 O O   . LEU A 253 ? 0.49102 0.70570 0.62783 -0.12656 0.03985  0.03754  289 LEU A O   
2046 C CB  . LEU A 253 ? 0.50269 0.63715 0.60429 -0.12166 0.02323  0.02741  289 LEU A CB  
2047 C CG  . LEU A 253 ? 0.49654 0.64184 0.60312 -0.11893 0.01347  0.01092  289 LEU A CG  
2048 C CD1 . LEU A 253 ? 0.49562 0.65332 0.58470 -0.10389 0.01447  0.00632  289 LEU A CD1 
2049 C CD2 . LEU A 253 ? 0.52847 0.64778 0.62957 -0.11892 0.00274  -0.00176 289 LEU A CD2 
2050 N N   . ASP A 254 ? 0.54138 0.72428 0.68911 -0.14517 0.04632  0.05974  290 ASP A N   
2051 C CA  . ASP A 254 ? 0.55744 0.76970 0.73945 -0.15841 0.05386  0.06777  290 ASP A CA  
2052 C C   . ASP A 254 ? 0.53912 0.78713 0.71421 -0.14994 0.06911  0.07763  290 ASP A C   
2053 O O   . ASP A 254 ? 0.53148 0.81429 0.73223 -0.15348 0.07402  0.07678  290 ASP A O   
2054 C CB  . ASP A 254 ? 0.58516 0.78039 0.79090 -0.17654 0.05910  0.08468  290 ASP A CB  
2055 C CG  . ASP A 254 ? 0.65084 0.81710 0.87510 -0.18766 0.04341  0.07029  290 ASP A CG  
2056 O OD1 . ASP A 254 ? 0.65834 0.83172 0.88695 -0.18536 0.02968  0.04871  290 ASP A OD1 
2057 O OD2 . ASP A 254 ? 0.69163 0.82717 0.92465 -0.19735 0.04442  0.08028  290 ASP A OD2 
2058 N N   . SER A 255 ? 0.52559 0.76764 0.66693 -0.13768 0.07614  0.08568  291 SER A N   
2059 C CA  . SER A 255 ? 0.60363 0.87826 0.73233 -0.12702 0.09024  0.09185  291 SER A CA  
2060 C C   . SER A 255 ? 0.62921 0.92200 0.75377 -0.11335 0.08490  0.07148  291 SER A C   
2061 O O   . SER A 255 ? 0.56454 0.89279 0.70499 -0.11055 0.09411  0.07132  291 SER A O   
2062 C CB  . SER A 255 ? 0.64011 0.90275 0.73049 -0.11605 0.09501  0.10198  291 SER A CB  
2063 O OG  . SER A 255 ? 0.61875 0.91183 0.69077 -0.10308 0.10712  0.10347  291 SER A OG  
2064 N N   . VAL A 256 ? 0.54086 0.80992 0.64665 -0.10415 0.07105  0.05548  292 VAL A N   
2065 C CA  . VAL A 256 ? 0.51379 0.79389 0.61489 -0.09024 0.06599  0.03853  292 VAL A CA  
2066 C C   . VAL A 256 ? 0.53397 0.83248 0.66665 -0.09511 0.06013  0.03131  292 VAL A C   
2067 O O   . VAL A 256 ? 0.50176 0.82170 0.63954 -0.08359 0.06037  0.02252  292 VAL A O   
2068 C CB  . VAL A 256 ? 0.53659 0.78565 0.61347 -0.08103 0.05425  0.02686  292 VAL A CB  
2069 C CG1 . VAL A 256 ? 0.54016 0.77696 0.58961 -0.07528 0.05741  0.03177  292 VAL A CG1 
2070 C CG2 . VAL A 256 ? 0.53358 0.75724 0.61750 -0.08977 0.04292  0.02387  292 VAL A CG2 
2071 N N   . ARG A 257 ? 0.51441 0.80466 0.66920 -0.11092 0.05324  0.03347  293 ARG A N   
2072 C CA  . ARG A 257 ? 0.57603 0.88824 0.76377 -0.11692 0.04519  0.02584  293 ARG A CA  
2073 C C   . ARG A 257 ? 0.56442 0.91965 0.78594 -0.12344 0.05840  0.03565  293 ARG A C   
2074 O O   . ARG A 257 ? 0.58240 0.96689 0.83304 -0.12342 0.05279  0.02836  293 ARG A O   
2075 C CB  . ARG A 257 ? 0.58687 0.87628 0.78813 -0.13221 0.03205  0.02166  293 ARG A CB  
2076 C CG  . ARG A 257 ? 0.56294 0.82131 0.73776 -0.12322 0.01741  0.00770  293 ARG A CG  
2077 C CD  . ARG A 257 ? 0.59369 0.83061 0.77963 -0.13637 0.00489  0.00052  293 ARG A CD  
2078 N NE  . ARG A 257 ? 0.49485 0.70792 0.65407 -0.12553 -0.00739 -0.01310 293 ARG A NE  
2079 C CZ  . ARG A 257 ? 0.51322 0.70376 0.67113 -0.13125 -0.01900 -0.02370 293 ARG A CZ  
2080 N NH1 . ARG A 257 ? 0.61815 0.80247 0.80264 -0.14898 -0.02206 -0.02392 293 ARG A NH1 
2081 N NH2 . ARG A 257 ? 0.51959 0.69259 0.64910 -0.11852 -0.02700 -0.03439 293 ARG A NH2 
2082 N N   . SER A 258 ? 0.56823 0.93057 0.78669 -0.12779 0.07624  0.05310  294 SER A N   
2083 C CA  . SER A 258 ? 0.56417 0.96934 0.81455 -0.13424 0.09341  0.06632  294 SER A CA  
2084 C C   . SER A 258 ? 0.60343 1.03762 0.83654 -0.11399 0.10793  0.06546  294 SER A C   
2085 O O   . SER A 258 ? 0.52357 0.99832 0.78075 -0.11559 0.12535  0.07624  294 SER A O   
2086 C CB  . SER A 258 ? 0.60700 1.00378 0.86546 -0.15141 0.10687  0.08982  294 SER A CB  
2087 O OG  . SER A 258 ? 0.67383 1.04020 0.95052 -0.16956 0.09323  0.08849  294 SER A OG  
2088 N N   . LEU A 259 ? 0.49002 0.90472 0.68436 -0.09509 0.10178  0.05232  295 LEU A N   
2089 C CA  . LEU A 259 ? 0.52203 0.95864 0.69789 -0.07449 0.11355  0.04711  295 LEU A CA  
2090 C C   . LEU A 259 ? 0.47762 0.95167 0.68552 -0.06572 0.11380  0.03755  295 LEU A C   
2091 O O   . LEU A 259 ? 0.47509 0.94437 0.70109 -0.06733 0.09689  0.02733  295 LEU A O   
2092 C CB  . LEU A 259 ? 0.48738 0.88995 0.62081 -0.05873 0.10359  0.03285  295 LEU A CB  
2093 C CG  . LEU A 259 ? 0.53479 0.90956 0.63261 -0.06031 0.10491  0.04037  295 LEU A CG  
2094 C CD1 . LEU A 259 ? 0.52877 0.86997 0.59810 -0.04912 0.09057  0.02426  295 LEU A CD1 
2095 C CD2 . LEU A 259 ? 0.48249 0.88206 0.56198 -0.05241 0.12418  0.05048  295 LEU A CD2 
2096 N N   . PRO A 260 ? 0.56029 1.07367 0.77487 -0.05451 0.13272  0.04079  296 PRO A N   
2097 C CA  . PRO A 260 ? 0.42063 0.96985 0.66366 -0.04060 0.13305  0.02994  296 PRO A CA  
2098 C C   . PRO A 260 ? 0.54787 1.07115 0.76712 -0.02001 0.11784  0.00961  296 PRO A C   
2099 O O   . PRO A 260 ? 0.51016 0.99215 0.69079 -0.01558 0.11019  0.00322  296 PRO A O   
2100 C CB  . PRO A 260 ? 0.52856 1.11940 0.77188 -0.02936 0.15993  0.03741  296 PRO A CB  
2101 C CG  . PRO A 260 ? 0.59830 1.18528 0.83122 -0.04623 0.17397  0.05930  296 PRO A CG  
2102 C CD  . PRO A 260 ? 0.51049 1.04191 0.71054 -0.05446 0.15616  0.05722  296 PRO A CD  
2103 N N   . PHE A 261 ? 0.54763 1.09748 0.79424 -0.00694 0.11391  0.00061  297 PHE A N   
2104 C CA  . PHE A 261 ? 0.54947 1.07462 0.78086 0.01226  0.09895  -0.01543 297 PHE A CA  
2105 C C   . PHE A 261 ? 0.57175 1.07816 0.76521 0.03256  0.10713  -0.02647 297 PHE A C   
2106 O O   . PHE A 261 ? 0.53619 0.99946 0.70137 0.03817  0.09534  -0.03545 297 PHE A O   
2107 C CB  . PHE A 261 ? 0.41683 0.97872 0.68818 0.02413  0.09366  -0.02032 297 PHE A CB  
2108 C CG  . PHE A 261 ? 0.51643 1.05395 0.77401 0.04662  0.08032  -0.03341 297 PHE A CG  
2109 C CD1 . PHE A 261 ? 0.52719 1.02393 0.76756 0.04256  0.06068  -0.03511 297 PHE A CD1 
2110 C CD2 . PHE A 261 ? 0.57124 1.12577 0.83354 0.07274  0.08865  -0.04296 297 PHE A CD2 
2111 C CE1 . PHE A 261 ? 0.59207 1.06486 0.82078 0.06267  0.05028  -0.04297 297 PHE A CE1 
2112 C CE2 . PHE A 261 ? 0.54765 1.07526 0.79986 0.09340  0.07659  -0.05289 297 PHE A CE2 
2113 C CZ  . PHE A 261 ? 0.57240 1.05877 0.80812 0.08760  0.05767  -0.05130 297 PHE A CZ  
2114 N N   . ASP A 262 ? 0.51256 1.05200 0.70629 0.04417  0.12734  -0.02695 298 ASP A N   
2115 C CA  . ASP A 262 ? 0.61348 1.13849 0.77175 0.06594  0.13411  -0.04205 298 ASP A CA  
2116 C C   . ASP A 262 ? 0.67766 1.19075 0.79714 0.05967  0.14365  -0.03734 298 ASP A C   
2117 O O   . ASP A 262 ? 0.74687 1.25627 0.83566 0.07758  0.15091  -0.05068 298 ASP A O   
2118 C CB  . ASP A 262 ? 0.65244 1.22084 0.82940 0.08908  0.15007  -0.04993 298 ASP A CB  
2119 C CG  . ASP A 262 ? 0.65976 1.28296 0.86052 0.08116  0.17308  -0.03345 298 ASP A CG  
2120 O OD1 . ASP A 262 ? 0.66588 1.29121 0.87380 0.05602  0.17467  -0.01488 298 ASP A OD1 
2121 O OD2 . ASP A 262 ? 0.69744 1.36132 0.91155 0.10047  0.19074  -0.03839 298 ASP A OD2 
2122 N N   . ALA A 263 ? 0.61698 1.12314 0.73623 0.03623  0.14258  -0.01970 299 ALA A N   
2123 C CA  . ALA A 263 ? 0.67806 1.17785 0.76254 0.03144  0.15215  -0.01096 299 ALA A CA  
2124 C C   . ALA A 263 ? 0.61927 1.07116 0.66467 0.03480  0.13619  -0.02361 299 ALA A C   
2125 O O   . ALA A 263 ? 0.64059 1.05936 0.69084 0.02945  0.11804  -0.02965 299 ALA A O   
2126 C CB  . ALA A 263 ? 0.63524 1.14195 0.73717 0.00590  0.15677  0.01409  299 ALA A CB  
2127 N N   . GLU A 264 ? 0.68964 1.14075 0.69652 0.04426  0.14326  -0.02742 300 GLU A N   
2128 C CA  . GLU A 264 ? 0.80725 1.21834 0.78042 0.04536  0.12746  -0.03852 300 GLU A CA  
2129 C C   . GLU A 264 ? 0.74574 1.14194 0.71281 0.02525  0.12312  -0.01814 300 GLU A C   
2130 O O   . GLU A 264 ? 0.74383 1.16034 0.69988 0.02114  0.13698  -0.00009 300 GLU A O   
2131 C CB  . GLU A 264 ? 0.85190 1.26895 0.78489 0.06546  0.13296  -0.05473 300 GLU A CB  
2132 C CG  . GLU A 264 ? 0.85563 1.23424 0.75911 0.06635  0.11364  -0.06945 300 GLU A CG  
2133 C CD  . GLU A 264 ? 1.01429 1.40245 0.87272 0.08309  0.11726  -0.08249 300 GLU A CD  
2134 O OE1 . GLU A 264 ? 1.22176 1.64665 1.06721 0.09381  0.13756  -0.07630 300 GLU A OE1 
2135 O OE2 . GLU A 264 ? 1.08019 1.44118 0.91654 0.08575  0.09974  -0.09910 300 GLU A OE2 
2136 N N   . PRO A 265 ? 0.70995 1.07132 0.68383 0.01377  0.10565  -0.01903 301 PRO A N   
2137 C CA  . PRO A 265 ? 0.72234 1.06965 0.69528 -0.00391 0.10218  0.00001  301 PRO A CA  
2138 C C   . PRO A 265 ? 0.64520 0.98620 0.58022 0.00088  0.10128  0.00267  301 PRO A C   
2139 O O   . PRO A 265 ? 0.60216 0.93654 0.51177 0.01522  0.09464  -0.01644 301 PRO A O   
2140 C CB  . PRO A 265 ? 0.62472 0.93789 0.61142 -0.01188 0.08437  -0.00664 301 PRO A CB  
2141 C CG  . PRO A 265 ? 0.65492 0.96993 0.65673 -0.00114 0.08109  -0.02287 301 PRO A CG  
2142 C CD  . PRO A 265 ? 0.67258 1.00671 0.65728 0.01729  0.09023  -0.03553 301 PRO A CD  
2143 N N   . PRO A 266 ? 0.65572 0.99816 0.58598 -0.01006 0.10666  0.02578  302 PRO A N   
2144 C CA  . PRO A 266 ? 0.60355 0.93992 0.49634 -0.00411 0.10311  0.03053  302 PRO A CA  
2145 C C   . PRO A 266 ? 0.65994 0.96163 0.54991 -0.00859 0.08224  0.02318  302 PRO A C   
2146 O O   . PRO A 266 ? 0.64505 0.93124 0.54320 -0.02041 0.07863  0.03993  302 PRO A O   
2147 C CB  . PRO A 266 ? 0.65870 1.00898 0.55350 -0.01415 0.11855  0.06226  302 PRO A CB  
2148 C CG  . PRO A 266 ? 0.64855 0.99399 0.58823 -0.03231 0.12041  0.07112  302 PRO A CG  
2149 C CD  . PRO A 266 ? 0.64470 0.99733 0.60461 -0.02705 0.11710  0.04904  302 PRO A CD  
2150 N N   . TYR A 267 ? 0.59717 0.88656 0.47857 0.00103  0.06912  -0.00191 303 TYR A N   
2151 C CA  . TYR A 267 ? 0.67509 0.93486 0.56220 -0.00413 0.05075  -0.00955 303 TYR A CA  
2152 C C   . TYR A 267 ? 0.62903 0.88464 0.49565 -0.00471 0.04369  0.00248  303 TYR A C   
2153 O O   . TYR A 267 ? 0.66575 0.90352 0.54640 -0.01468 0.03728  0.01353  303 TYR A O   
2154 C CB  . TYR A 267 ? 0.66734 0.91622 0.55156 0.00568  0.03930  -0.03766 303 TYR A CB  
2155 C CG  . TYR A 267 ? 0.66450 0.91479 0.56831 0.00947  0.04500  -0.04893 303 TYR A CG  
2156 C CD1 . TYR A 267 ? 0.59159 0.82423 0.52391 0.00078  0.04127  -0.04717 303 TYR A CD1 
2157 C CD2 . TYR A 267 ? 0.65218 0.92242 0.54434 0.02403  0.05412  -0.06116 303 TYR A CD2 
2158 C CE1 . TYR A 267 ? 0.61286 0.84743 0.56186 0.00635  0.04492  -0.05550 303 TYR A CE1 
2159 C CE2 . TYR A 267 ? 0.67243 0.94446 0.58471 0.02986  0.05858  -0.07076 303 TYR A CE2 
2160 C CZ  . TYR A 267 ? 0.67501 0.92896 0.61587 0.02087  0.05314  -0.06699 303 TYR A CZ  
2161 O OH  . TYR A 267 ? 0.59178 0.84800 0.55151 0.02861  0.05605  -0.07460 303 TYR A OH  
2162 N N   . GLU A 268 ? 0.63761 0.91038 0.46935 0.00799  0.04438  0.00013  304 GLU A N   
2163 C CA  . GLU A 268 ? 0.71129 0.98199 0.52085 0.01049  0.03475  0.01122  304 GLU A CA  
2164 C C   . GLU A 268 ? 0.69675 0.96668 0.51276 0.00083  0.04561  0.04446  304 GLU A C   
2165 O O   . GLU A 268 ? 0.71509 0.97161 0.53075 -0.00185 0.03578  0.05628  304 GLU A O   
2166 C CB  . GLU A 268 ? 0.77024 1.06217 0.53545 0.02838  0.03281  0.00138  304 GLU A CB  
2167 C CG  . GLU A 268 ? 0.79362 1.08511 0.53312 0.03440  0.01683  0.00769  304 GLU A CG  
2168 C CD  . GLU A 268 ? 0.92069 1.19274 0.67816 0.03105  -0.00775 -0.01263 304 GLU A CD  
2169 O OE1 . GLU A 268 ? 0.89063 1.14899 0.67417 0.02588  -0.01195 -0.03361 304 GLU A OE1 
2170 O OE2 . GLU A 268 ? 0.99619 1.26798 0.74359 0.03401  -0.02254 -0.00605 304 GLU A OE2 
2171 N N   . GLU A 269 ? 0.66169 0.94547 0.48783 -0.00461 0.06553  0.05968  305 GLU A N   
2172 C CA  . GLU A 269 ? 0.66245 0.94097 0.50301 -0.01690 0.07591  0.09044  305 GLU A CA  
2173 C C   . GLU A 269 ? 0.66254 0.91138 0.53746 -0.03095 0.06618  0.09014  305 GLU A C   
2174 O O   . GLU A 269 ? 0.64995 0.88216 0.52972 -0.03661 0.06368  0.10859  305 GLU A O   
2175 C CB  . GLU A 269 ? 0.63836 0.94045 0.49151 -0.02212 0.09883  0.10416  305 GLU A CB  
2176 C CG  . GLU A 269 ? 0.73894 1.04943 0.58468 -0.02642 0.11481  0.13955  305 GLU A CG  
2177 C CD  . GLU A 269 ? 0.84318 1.18806 0.69343 -0.02667 0.13987  0.15177  305 GLU A CD  
2178 O OE1 . GLU A 269 ? 0.86390 1.21700 0.75074 -0.03646 0.14611  0.14451  305 GLU A OE1 
2179 O OE2 . GLU A 269 ? 0.87777 1.24416 0.69466 -0.01587 0.15348  0.16903  305 GLU A OE2 
2180 N N   . TYR A 270 ? 0.57536 0.81669 0.47265 -0.03489 0.06105  0.06972  306 TYR A N   
2181 C CA  . TYR A 270 ? 0.68154 0.89671 0.60601 -0.04567 0.05262  0.06773  306 TYR A CA  
2182 C C   . TYR A 270 ? 0.62462 0.82188 0.54185 -0.04131 0.03702  0.06327  306 TYR A C   
2183 O O   . TYR A 270 ? 0.60730 0.78488 0.53863 -0.04762 0.03319  0.07237  306 TYR A O   
2184 C CB  . TYR A 270 ? 0.59117 0.80481 0.53559 -0.04794 0.05089  0.04871  306 TYR A CB  
2185 C CG  . TYR A 270 ? 0.57570 0.80855 0.53663 -0.05325 0.06404  0.05307  306 TYR A CG  
2186 C CD1 . TYR A 270 ? 0.62983 0.86862 0.60369 -0.06420 0.07485  0.07419  306 TYR A CD1 
2187 C CD2 . TYR A 270 ? 0.57462 0.82006 0.54234 -0.04732 0.06533  0.03659  306 TYR A CD2 
2188 C CE1 . TYR A 270 ? 0.63445 0.89532 0.63053 -0.07058 0.08636  0.07791  306 TYR A CE1 
2189 C CE2 . TYR A 270 ? 0.60711 0.87477 0.59432 -0.05102 0.07625  0.04024  306 TYR A CE2 
2190 C CZ  . TYR A 270 ? 0.64613 0.92357 0.64892 -0.06335 0.08662  0.06048  306 TYR A CZ  
2191 O OH  . TYR A 270 ? 0.63278 0.93659 0.66167 -0.06839 0.09689  0.06368  306 TYR A OH  
2192 N N   . ARG A 271 ? 0.55559 0.76021 0.45363 -0.03020 0.02735  0.04773  307 ARG A N   
2193 C CA  . ARG A 271 ? 0.66968 0.86352 0.56530 -0.02629 0.01138  0.04344  307 ARG A CA  
2194 C C   . ARG A 271 ? 0.67621 0.87049 0.55745 -0.02311 0.01044  0.06646  307 ARG A C   
2195 O O   . ARG A 271 ? 0.66685 0.84663 0.55997 -0.02409 0.00167  0.07235  307 ARG A O   
2196 C CB  . ARG A 271 ? 0.58863 0.79201 0.46915 -0.01624 -0.00047 0.02012  307 ARG A CB  
2197 C CG  . ARG A 271 ? 0.56825 0.76243 0.46876 -0.01908 -0.00311 -0.00181 307 ARG A CG  
2198 C CD  . ARG A 271 ? 0.57574 0.77322 0.46721 -0.01100 -0.01753 -0.02571 307 ARG A CD  
2199 N NE  . ARG A 271 ? 0.69133 0.90716 0.55284 0.00039  -0.01383 -0.03535 307 ARG A NE  
2200 C CZ  . ARG A 271 ? 0.72935 0.94719 0.59154 0.00466  -0.00756 -0.05112 307 ARG A CZ  
2201 N NH1 . ARG A 271 ? 0.63002 0.83188 0.52040 -0.00154 -0.00572 -0.05798 307 ARG A NH1 
2202 N NH2 . ARG A 271 ? 0.69665 0.93352 0.52917 0.01735  -0.00249 -0.05955 307 ARG A NH2 
2203 N N   . MET A 272 ? 0.61177 0.82323 0.46765 -0.01788 0.02052  0.08122  308 MET A N   
2204 C CA  . MET A 272 ? 0.65898 0.86943 0.49954 -0.01400 0.02166  0.10819  308 MET A CA  
2205 C C   . MET A 272 ? 0.73741 0.92628 0.60515 -0.02683 0.03097  0.12932  308 MET A C   
2206 O O   . MET A 272 ? 0.71683 0.89236 0.58412 -0.02462 0.02725  0.14852  308 MET A O   
2207 C CB  . MET A 272 ? 0.72619 0.96193 0.53025 -0.00440 0.03309  0.12087  308 MET A CB  
2208 C CG  . MET A 272 ? 0.86630 1.12158 0.63533 0.01189  0.02037  0.10048  308 MET A CG  
2209 S SD  . MET A 272 ? 1.10318 1.35259 0.86241 0.02176  -0.00628 0.09907  308 MET A SD  
2210 C CE  . MET A 272 ? 0.99613 1.26431 0.73097 0.03440  -0.02419 0.06064  308 MET A CE  
2211 N N   . LEU A 273 ? 0.64341 0.82819 0.53568 -0.03937 0.04170  0.12518  309 LEU A N   
2212 C CA  . LEU A 273 ? 0.69271 0.85497 0.61329 -0.05256 0.04758  0.13942  309 LEU A CA  
2213 C C   . LEU A 273 ? 0.66702 0.80391 0.60511 -0.05310 0.03447  0.12982  309 LEU A C   
2214 O O   . LEU A 273 ? 0.69000 0.80539 0.63858 -0.05528 0.03378  0.14495  309 LEU A O   
2215 C CB  . LEU A 273 ? 0.58133 0.74987 0.52463 -0.06509 0.05865  0.13335  309 LEU A CB  
2216 C CG  . LEU A 273 ? 0.68109 0.82756 0.65653 -0.08058 0.06268  0.14245  309 LEU A CG  
2217 C CD1 . LEU A 273 ? 0.70474 0.84501 0.68097 -0.08546 0.07340  0.17370  309 LEU A CD1 
2218 C CD2 . LEU A 273 ? 0.60670 0.76452 0.60553 -0.09124 0.06814  0.13009  309 LEU A CD2 
2219 N N   . LEU A 274 ? 0.67558 0.81415 0.61815 -0.05034 0.02526  0.10562  310 LEU A N   
2220 C CA  . LEU A 274 ? 0.63863 0.75766 0.59843 -0.04994 0.01577  0.09723  310 LEU A CA  
2221 C C   . LEU A 274 ? 0.61401 0.73311 0.56507 -0.03874 0.00428  0.10344  310 LEU A C   
2222 O O   . LEU A 274 ? 0.62530 0.72702 0.59179 -0.03722 0.00009  0.10752  310 LEU A O   
2223 C CB  . LEU A 274 ? 0.61315 0.73469 0.58242 -0.05105 0.01193  0.07335  310 LEU A CB  
2224 C CG  . LEU A 274 ? 0.57346 0.69485 0.55376 -0.06015 0.02052  0.06687  310 LEU A CG  
2225 C CD1 . LEU A 274 ? 0.44465 0.56440 0.43319 -0.05918 0.01648  0.04733  310 LEU A CD1 
2226 C CD2 . LEU A 274 ? 0.47388 0.57666 0.47052 -0.06935 0.02532  0.07666  310 LEU A CD2 
2227 N N   . LEU A 275 ? 0.64309 0.78293 0.56962 -0.02938 -0.00173 0.10311  311 LEU A N   
2228 C CA  . LEU A 275 ? 0.66587 0.81016 0.58347 -0.01763 -0.01543 0.10955  311 LEU A CA  
2229 C C   . LEU A 275 ? 0.71918 0.84976 0.63420 -0.01459 -0.01156 0.13828  311 LEU A C   
2230 O O   . LEU A 275 ? 0.68426 0.80779 0.60752 -0.00652 -0.02181 0.14472  311 LEU A O   
2231 C CB  . LEU A 275 ? 0.74206 0.91244 0.62888 -0.00741 -0.02405 0.10175  311 LEU A CB  
2232 C CG  . LEU A 275 ? 0.74918 0.92987 0.64247 -0.00617 -0.03683 0.07225  311 LEU A CG  
2233 C CD1 . LEU A 275 ? 0.78299 0.98738 0.64228 0.00497  -0.04645 0.06245  311 LEU A CD1 
2234 C CD2 . LEU A 275 ? 0.77442 0.94913 0.69536 -0.00508 -0.05030 0.06667  311 LEU A CD2 
2235 N N   . SER A 276 ? 0.66560 0.79227 0.57291 -0.02080 0.00352  0.15674  312 SER A N   
2236 C CA  . SER A 276 ? 0.75408 0.86257 0.66252 -0.01952 0.00882  0.18654  312 SER A CA  
2237 C C   . SER A 276 ? 0.73546 0.81273 0.67606 -0.02354 0.00669  0.18580  312 SER A C   
2238 O O   . SER A 276 ? 0.72461 0.78307 0.66902 -0.01795 0.00593  0.20724  312 SER A O   
2239 C CB  . SER A 276 ? 0.68521 0.79441 0.58936 -0.02973 0.02780  0.20553  312 SER A CB  
2240 O OG  . SER A 276 ? 0.69425 0.79183 0.62698 -0.04589 0.03592  0.19327  312 SER A OG  
2241 N N   . VAL A 277 ? 0.69991 0.77047 0.66194 -0.03145 0.00630  0.16214  313 VAL A N   
2242 C CA  . VAL A 277 ? 0.70587 0.74930 0.69397 -0.03221 0.00436  0.15770  313 VAL A CA  
2243 C C   . VAL A 277 ? 0.70072 0.74513 0.69164 -0.01662 -0.00828 0.16068  313 VAL A C   
2244 O O   . VAL A 277 ? 0.71963 0.74093 0.72437 -0.01095 -0.00900 0.17186  313 VAL A O   
2245 C CB  . VAL A 277 ? 0.70840 0.75026 0.71174 -0.04045 0.00600  0.13170  313 VAL A CB  
2246 C CG1 . VAL A 277 ? 0.65453 0.67127 0.67945 -0.03799 0.00469  0.12528  313 VAL A CG1 
2247 C CG2 . VAL A 277 ? 0.64251 0.68532 0.64713 -0.05471 0.01640  0.12920  313 VAL A CG2 
2248 N N   . LEU A 278 ? 0.69738 0.76888 0.67822 -0.00906 -0.01931 0.14974  314 LEU A N   
2249 C CA  . LEU A 278 ? 0.73922 0.81844 0.72819 0.00523  -0.03348 0.15086  314 LEU A CA  
2250 C C   . LEU A 278 ? 0.80914 0.88688 0.78173 0.01778  -0.03860 0.17845  314 LEU A C   
2251 O O   . LEU A 278 ? 0.79519 0.86903 0.78097 0.03062  -0.04786 0.18625  314 LEU A O   
2252 C CB  . LEU A 278 ? 0.70152 0.81070 0.68784 0.00767  -0.04576 0.13046  314 LEU A CB  
2253 C CG  . LEU A 278 ? 0.67755 0.78719 0.68136 -0.00312 -0.04084 0.10615  314 LEU A CG  
2254 C CD1 . LEU A 278 ? 0.75364 0.88894 0.75963 -0.00148 -0.05376 0.08752  314 LEU A CD1 
2255 C CD2 . LEU A 278 ? 0.69453 0.78567 0.72756 -0.00333 -0.03539 0.10272  314 LEU A CD2 
2256 N N   . ASP A 279 ? 0.84040 0.92244 0.78478 0.01564  -0.03176 0.19513  315 ASP A N   
2257 C CA  . ASP A 279 ? 0.86124 0.93926 0.78697 0.02792  -0.03388 0.22650  315 ASP A CA  
2258 C C   . ASP A 279 ? 0.85959 0.89837 0.80656 0.02557  -0.02421 0.24657  315 ASP A C   
2259 O O   . ASP A 279 ? 0.82158 0.84877 0.77125 0.03999  -0.03109 0.26640  315 ASP A O   
2260 C CB  . ASP A 279 ? 0.88409 0.97966 0.77228 0.02677  -0.02586 0.24036  315 ASP A CB  
2261 C CG  . ASP A 279 ? 1.01018 1.14300 0.87075 0.03560  -0.03960 0.22271  315 ASP A CG  
2262 O OD1 . ASP A 279 ? 1.21559 1.36098 1.08442 0.04546  -0.05877 0.20901  315 ASP A OD1 
2263 O OD2 . ASP A 279 ? 1.02173 1.17195 0.85449 0.03294  -0.03143 0.22142  315 ASP A OD2 
2264 N N   . ASP A 280 ? 0.82758 0.84497 0.79141 0.00821  -0.00977 0.24037  316 ASP A N   
2265 C CA  . ASP A 280 ? 0.87673 0.85318 0.86365 0.00401  -0.00182 0.25440  316 ASP A CA  
2266 C C   . ASP A 280 ? 0.87646 0.83556 0.88898 0.01484  -0.01051 0.24275  316 ASP A C   
2267 O O   . ASP A 280 ? 0.87393 0.80063 0.90079 0.02128  -0.00921 0.25890  316 ASP A O   
2268 C CB  . ASP A 280 ? 0.89716 0.85920 0.89874 -0.01766 0.01192  0.24413  316 ASP A CB  
2269 C CG  . ASP A 280 ? 0.88078 0.86189 0.86348 -0.02829 0.02343  0.25720  316 ASP A CG  
2270 O OD1 . ASP A 280 ? 0.87542 0.87804 0.82899 -0.01804 0.02238  0.27556  316 ASP A OD1 
2271 O OD2 . ASP A 280 ? 0.83291 0.80989 0.82983 -0.04585 0.03346  0.24858  316 ASP A OD2 
2272 N N   . LEU A 281 ? 0.80761 0.78717 0.82800 0.01745  -0.01802 0.21576  317 LEU A N   
2273 C CA  . LEU A 281 ? 0.90023 0.87013 0.94666 0.02786  -0.02327 0.20298  317 LEU A CA  
2274 C C   . LEU A 281 ? 0.80852 0.80293 0.85652 0.04739  -0.03880 0.20825  317 LEU A C   
2275 O O   . LEU A 281 ? 0.80963 0.80370 0.88270 0.05775  -0.04292 0.19824  317 LEU A O   
2276 C CB  . LEU A 281 ? 0.86085 0.83840 0.91940 0.01810  -0.01933 0.17211  317 LEU A CB  
2277 C CG  . LEU A 281 ? 0.76557 0.72494 0.82384 -0.00027 -0.00732 0.16237  317 LEU A CG  
2278 C CD1 . LEU A 281 ? 0.80173 0.77451 0.86556 -0.00653 -0.00532 0.13490  317 LEU A CD1 
2279 C CD2 . LEU A 281 ? 0.94589 0.86306 1.02001 -0.00115 -0.00140 0.16816  317 LEU A CD2 
2280 N N   . GLY A 282 ? 0.79422 0.81251 0.81646 0.05351  -0.04776 0.22285  318 GLY A N   
2281 C CA  . GLY A 282 ? 0.79717 0.84193 0.82064 0.07240  -0.06616 0.22717  318 GLY A CA  
2282 C C   . GLY A 282 ? 0.86384 0.94077 0.90518 0.07174  -0.07614 0.19903  318 GLY A C   
2283 O O   . GLY A 282 ? 0.82795 0.92295 0.88937 0.08627  -0.08994 0.19782  318 GLY A O   
2284 N N   . GLN A 283 ? 0.71685 0.80191 0.75478 0.05527  -0.06946 0.17751  319 GLN A N   
2285 C CA  . GLN A 283 ? 0.77893 0.89029 0.83620 0.05173  -0.07646 0.15215  319 GLN A CA  
2286 C C   . GLN A 283 ? 0.81076 0.95226 0.84408 0.04913  -0.08863 0.14341  319 GLN A C   
2287 O O   . GLN A 283 ? 0.81811 0.95876 0.81669 0.04671  -0.08570 0.15264  319 GLN A O   
2288 C CB  . GLN A 283 ? 0.80149 0.89793 0.87308 0.03697  -0.06060 0.13386  319 GLN A CB  
2289 C CG  . GLN A 283 ? 0.78809 0.85112 0.87548 0.03902  -0.04794 0.13889  319 GLN A CG  
2290 C CD  . GLN A 283 ? 0.82633 0.89242 0.94288 0.05602  -0.05368 0.14227  319 GLN A CD  
2291 O OE1 . GLN A 283 ? 0.79686 0.89252 0.93420 0.06098  -0.06259 0.13258  319 GLN A OE1 
2292 N NE2 . GLN A 283 ? 0.84744 0.88309 0.96934 0.06513  -0.04856 0.15584  319 GLN A NE2 
2293 N N   . ALA A 284 ? 0.81410 0.98283 0.86805 0.04989  -0.10194 0.12482  320 ALA A N   
2294 C CA  . ALA A 284 ? 0.68159 0.87764 0.71779 0.04768  -0.11640 0.11038  320 ALA A CA  
2295 C C   . ALA A 284 ? 0.74645 0.94259 0.79435 0.03129  -0.10865 0.08612  320 ALA A C   
2296 O O   . ALA A 284 ? 0.71190 0.89822 0.79041 0.02444  -0.09791 0.07902  320 ALA A O   
2297 C CB  . ALA A 284 ? 0.72631 0.95451 0.77991 0.05989  -0.14146 0.10584  320 ALA A CB  
2298 N N   . CYS A 285 ? 0.76072 0.96748 0.78196 0.02681  -0.11350 0.07414  321 CYS A N   
2299 C CA  . CYS A 285 ? 0.66680 0.87276 0.69737 0.01326  -0.10820 0.05154  321 CYS A CA  
2300 C C   . CYS A 285 ? 0.72930 0.95992 0.78399 0.01265  -0.12843 0.03091  321 CYS A C   
2301 O O   . CYS A 285 ? 0.75593 0.99967 0.79299 0.01231  -0.14100 0.01471  321 CYS A O   
2302 C CB  . CYS A 285 ? 0.76627 0.96749 0.75786 0.00957  -0.10015 0.04891  321 CYS A CB  
2303 S SG  . CYS A 285 ? 0.71931 0.91294 0.72095 -0.00478 -0.09056 0.02505  321 CYS A SG  
2304 N N   . ASP A 286 ? 0.72057 0.95807 0.81888 0.01272  -0.13138 0.03086  322 ASP A N   
2305 C CA  . ASP A 286 ? 0.66908 0.93297 0.80196 0.01079  -0.15105 0.01372  322 ASP A CA  
2306 C C   . ASP A 286 ? 0.69810 0.95704 0.86476 -0.00510 -0.14236 -0.00304 322 ASP A C   
2307 O O   . ASP A 286 ? 0.73624 1.01479 0.93564 -0.01058 -0.15783 -0.01914 322 ASP A O   
2308 C CB  . ASP A 286 ? 0.73238 1.01403 0.89944 0.02151  -0.16042 0.02493  322 ASP A CB  
2309 C CG  . ASP A 286 ? 0.64359 0.90643 0.83218 0.02235  -0.13794 0.03933  322 ASP A CG  
2310 O OD1 . ASP A 286 ? 0.59595 0.83631 0.78191 0.01189  -0.11730 0.03672  322 ASP A OD1 
2311 O OD2 . ASP A 286 ? 0.77840 1.04927 0.98553 0.03520  -0.14177 0.05243  322 ASP A OD2 
2312 N N   . GLY A 287 ? 0.62996 0.86356 0.79073 -0.01258 -0.11901 0.00096  323 GLY A N   
2313 C CA  . GLY A 287 ? 0.64692 0.87322 0.83567 -0.02579 -0.10862 -0.01027 323 GLY A CA  
2314 C C   . GLY A 287 ? 0.66235 0.88976 0.89286 -0.02777 -0.09507 -0.00230 323 GLY A C   
2315 O O   . GLY A 287 ? 0.58323 0.80987 0.84330 -0.03832 -0.08768 -0.00932 323 GLY A O   
2316 N N   . ASP A 288 ? 0.61995 0.84824 0.85359 -0.01696 -0.09028 0.01280  324 ASP A N   
2317 C CA  . ASP A 288 ? 0.60161 0.83286 0.87214 -0.01525 -0.07569 0.01973  324 ASP A CA  
2318 C C   . ASP A 288 ? 0.63699 0.83945 0.88736 -0.01741 -0.05153 0.02508  324 ASP A C   
2319 O O   . ASP A 288 ? 0.56873 0.75167 0.78587 -0.01191 -0.04671 0.03256  324 ASP A O   
2320 C CB  . ASP A 288 ? 0.54794 0.79277 0.83199 0.00021  -0.08276 0.03134  324 ASP A CB  
2321 C CG  . ASP A 288 ? 0.63330 0.88784 0.96048 0.00452  -0.06823 0.03636  324 ASP A CG  
2322 O OD1 . ASP A 288 ? 0.55508 0.83240 0.92581 -0.00315 -0.06871 0.02993  324 ASP A OD1 
2323 O OD2 . ASP A 288 ? 0.69947 0.93905 1.01858 0.01588  -0.05580 0.04652  324 ASP A OD2 
2324 N N   . MET A 289 ? 0.56571 0.76609 0.83694 -0.02548 -0.03699 0.02180  325 MET A N   
2325 C CA  . MET A 289 ? 0.56218 0.73836 0.81269 -0.02703 -0.01625 0.02497  325 MET A CA  
2326 C C   . MET A 289 ? 0.48589 0.66469 0.75806 -0.01937 0.00106  0.03211  325 MET A C   
2327 O O   . MET A 289 ? 0.52488 0.72719 0.83701 -0.01589 0.00022  0.03445  325 MET A O   
2328 C CB  . MET A 289 ? 0.41732 0.58621 0.66677 -0.03928 -0.01103 0.01790  325 MET A CB  
2329 C CG  . MET A 289 ? 0.41783 0.58642 0.65097 -0.04542 -0.02753 0.00735  325 MET A CG  
2330 S SD  . MET A 289 ? 0.52741 0.67665 0.70658 -0.04193 -0.02798 0.00843  325 MET A SD  
2331 C CE  . MET A 289 ? 0.57040 0.73727 0.74067 -0.03940 -0.05209 0.00112  325 MET A CE  
2332 N N   . ASP A 290 ? 0.41374 0.57003 0.65947 -0.01600 0.01672  0.03435  326 ASP A N   
2333 C CA  . ASP A 290 ? 0.47210 0.62829 0.72947 -0.00588 0.03437  0.03865  326 ASP A CA  
2334 C C   . ASP A 290 ? 0.43444 0.60922 0.72613 -0.01017 0.04783  0.04104  326 ASP A C   
2335 O O   . ASP A 290 ? 0.39190 0.58490 0.71489 -0.00181 0.05741  0.04560  326 ASP A O   
2336 C CB  . ASP A 290 ? 0.48704 0.61509 0.70580 -0.00225 0.04577  0.03679  326 ASP A CB  
2337 C CG  . ASP A 290 ? 0.56156 0.67058 0.75447 0.00125  0.03545  0.03671  326 ASP A CG  
2338 O OD1 . ASP A 290 ? 0.49831 0.61560 0.69862 0.00252  0.02075  0.04048  326 ASP A OD1 
2339 O OD2 . ASP A 290 ? 0.55819 0.64441 0.72386 0.00250  0.04161  0.03342  326 ASP A OD2 
2340 N N   . TRP A 291 ? 0.41647 0.58723 0.70546 -0.02260 0.04999  0.03938  327 TRP A N   
2341 C CA  . TRP A 291 ? 0.47779 0.66210 0.79913 -0.02767 0.06586  0.04540  327 TRP A CA  
2342 C C   . TRP A 291 ? 0.39660 0.61210 0.77410 -0.03331 0.05765  0.04614  327 TRP A C   
2343 O O   . TRP A 291 ? 0.36685 0.59876 0.78159 -0.03713 0.07307  0.05373  327 TRP A O   
2344 C CB  . TRP A 291 ? 0.47776 0.64562 0.78291 -0.03874 0.06956  0.04515  327 TRP A CB  
2345 C CG  . TRP A 291 ? 0.47680 0.64077 0.78050 -0.04961 0.04858  0.03564  327 TRP A CG  
2346 C CD1 . TRP A 291 ? 0.47198 0.65097 0.81419 -0.06042 0.03650  0.03085  327 TRP A CD1 
2347 C CD2 . TRP A 291 ? 0.42199 0.56699 0.68436 -0.05015 0.03750  0.02816  327 TRP A CD2 
2348 N NE1 . TRP A 291 ? 0.53032 0.69902 0.85282 -0.06586 0.01834  0.01913  327 TRP A NE1 
2349 C CE2 . TRP A 291 ? 0.43852 0.58786 0.71251 -0.05934 0.02007  0.01861  327 TRP A CE2 
2350 C CE3 . TRP A 291 ? 0.45980 0.58620 0.67902 -0.04398 0.04053  0.02772  327 TRP A CE3 
2351 C CZ2 . TRP A 291 ? 0.43578 0.57287 0.67720 -0.06050 0.00832  0.00984  327 TRP A CZ2 
2352 C CZ3 . TRP A 291 ? 0.47960 0.59569 0.67202 -0.04730 0.02859  0.02068  327 TRP A CZ3 
2353 C CH2 . TRP A 291 ? 0.52357 0.64565 0.72580 -0.05450 0.01394  0.01242  327 TRP A CH2 
2354 N N   . MET A 292 ? 0.33049 0.55659 0.71590 -0.03363 0.03390  0.03926  328 MET A N   
2355 C CA  . MET A 292 ? 0.47057 0.73000 0.91069 -0.03801 0.02166  0.03765  328 MET A CA  
2356 C C   . MET A 292 ? 0.47495 0.75909 0.94888 -0.02473 0.03189  0.04574  328 MET A C   
2357 O O   . MET A 292 ? 0.43408 0.75159 0.96411 -0.02872 0.02760  0.04676  328 MET A O   
2358 C CB  . MET A 292 ? 0.39438 0.65907 0.82548 -0.03917 -0.00865 0.02732  328 MET A CB  
2359 C CG  . MET A 292 ? 0.44951 0.68639 0.83135 -0.04493 -0.01667 0.01947  328 MET A CG  
2360 S SD  . MET A 292 ? 0.51118 0.75868 0.89445 -0.05315 -0.04846 0.00301  328 MET A SD  
2361 C CE  . MET A 292 ? 0.56421 0.84305 0.96693 -0.04037 -0.06911 0.00502  328 MET A CE  
2362 N N   . HIS A 293 ? 0.42198 0.69124 0.86627 -0.00886 0.04475  0.05015  329 HIS A N   
2363 C CA  . HIS A 293 ? 0.47172 0.76115 0.94470 0.00723  0.05700  0.05643  329 HIS A CA  
2364 C C   . HIS A 293 ? 0.48066 0.77266 0.96106 0.01074  0.08901  0.06369  329 HIS A C   
2365 O O   . HIS A 293 ? 0.39591 0.70498 0.89790 0.02621  0.10372  0.06816  329 HIS A O   
2366 C CB  . HIS A 293 ? 0.44067 0.71029 0.87937 0.02486  0.05122  0.05556  329 HIS A CB  
2367 C CG  . HIS A 293 ? 0.44613 0.71543 0.87557 0.02473  0.02239  0.05298  329 HIS A CG  
2368 N ND1 . HIS A 293 ? 0.34166 0.64241 0.81015 0.03145  0.00515  0.05492  329 HIS A ND1 
2369 C CD2 . HIS A 293 ? 0.40118 0.64526 0.78597 0.01987  0.00838  0.04976  329 HIS A CD2 
2370 C CE1 . HIS A 293 ? 0.46747 0.76074 0.91087 0.03164  -0.01859 0.05344  329 HIS A CE1 
2371 N NE2 . HIS A 293 ? 0.40505 0.66426 0.79809 0.02445  -0.01562 0.05083  329 HIS A NE2 
2372 N N   . LEU A 294 ? 0.47557 0.75191 0.93749 -0.00120 0.10075  0.06572  330 LEU A N   
2373 C CA  . LEU A 294 ? 0.48287 0.76201 0.94561 0.00339  0.13194  0.07522  330 LEU A CA  
2374 C C   . LEU A 294 ? 0.49503 0.81599 1.02566 0.00145  0.14563  0.08524  330 LEU A C   
2375 O O   . LEU A 294 ? 0.44054 0.78510 1.02048 -0.01165 0.12961  0.08422  330 LEU A O   
2376 C CB  . LEU A 294 ? 0.49601 0.75195 0.92962 -0.00931 0.13906  0.07831  330 LEU A CB  
2377 C CG  . LEU A 294 ? 0.54759 0.76604 0.91603 -0.00649 0.13074  0.06988  330 LEU A CG  
2378 C CD1 . LEU A 294 ? 0.51012 0.71110 0.85953 -0.01864 0.13520  0.07391  330 LEU A CD1 
2379 C CD2 . LEU A 294 ? 0.53720 0.74342 0.86936 0.01278  0.14538  0.06770  330 LEU A CD2 
2380 N N   . ASN A 295 ? 0.57113 0.90303 1.10463 0.01512  0.17557  0.09408  331 ASN A N   
2381 C CA  . ASN A 295 ? 0.53930 0.91322 1.13680 0.01412  0.19674  0.10715  331 ASN A CA  
2382 C C   . ASN A 295 ? 0.54609 0.95743 1.20559 0.01506  0.17847  0.10360  331 ASN A C   
2383 O O   . ASN A 295 ? 0.45489 0.89362 1.17299 -0.00249 0.16907  0.10659  331 ASN A O   
2384 C CB  . ASN A 295 ? 0.54361 0.92013 1.16521 -0.00808 0.20695  0.11930  331 ASN A CB  
2385 C CG  . ASN A 295 ? 0.63751 0.98320 1.20184 -0.00528 0.22841  0.12717  331 ASN A CG  
2386 O OD1 . ASN A 295 ? 0.68788 1.03273 1.22179 0.01369  0.25274  0.13160  331 ASN A OD1 
2387 N ND2 . ASN A 295 ? 0.63179 0.95251 1.18034 -0.02255 0.21856  0.12800  331 ASN A ND2 
2388 N N   . GLY A 296 ? 0.54942 0.96056 1.19604 0.03632  0.17185  0.09655  332 GLY A N   
2389 C CA  . GLY A 296 ? 0.48018 0.92758 1.18159 0.04292  0.15485  0.09462  332 GLY A CA  
2390 C C   . GLY A 296 ? 0.47785 0.93028 1.19729 0.02623  0.11746  0.08694  332 GLY A C   
2391 O O   . GLY A 296 ? 0.50248 0.99131 1.27399 0.02895  0.10011  0.08571  332 GLY A O   
2392 N N   . GLY A 297 ? 0.47324 0.89143 1.14951 0.01059  0.10402  0.08079  333 GLY A N   
2393 C CA  . GLY A 297 ? 0.48479 0.90578 1.17125 -0.00486 0.07021  0.07127  333 GLY A CA  
2394 C C   . GLY A 297 ? 0.50300 0.92607 1.21559 -0.03058 0.06912  0.07050  333 GLY A C   
2395 O O   . GLY A 297 ? 0.54695 0.96210 1.25331 -0.04329 0.04171  0.05886  333 GLY A O   
2396 N N   . ARG A 298 ? 0.48189 0.91405 1.22271 -0.03782 0.09854  0.08284  334 ARG A N   
2397 C CA  . ARG A 298 ? 0.53779 0.96466 1.30320 -0.06258 0.09933  0.08442  334 ARG A CA  
2398 C C   . ARG A 298 ? 0.61417 0.99285 1.31395 -0.06900 0.09123  0.07715  334 ARG A C   
2399 O O   . ARG A 298 ? 0.60662 0.97538 1.31770 -0.08729 0.07458  0.06890  334 ARG A O   
2400 C CB  . ARG A 298 ? 0.55542 0.99147 1.34511 -0.06585 0.13562  0.10291  334 ARG A CB  
2401 C CG  . ARG A 298 ? 0.62601 1.10007 1.46912 -0.06518 0.13978  0.10717  334 ARG A CG  
2402 C CD  . ARG A 298 ? 0.68721 1.17355 1.52081 -0.04432 0.17354  0.12050  334 ARG A CD  
2403 N NE  . ARG A 298 ? 0.83235 1.36090 1.71585 -0.03652 0.17035  0.11983  334 ARG A NE  
2404 C CZ  . ARG A 298 ? 0.74260 1.29088 1.62986 -0.01670 0.19514  0.12780  334 ARG A CZ  
2405 N NH1 . ARG A 298 ? 0.84456 1.37387 1.68506 -0.00155 0.22493  0.13590  334 ARG A NH1 
2406 N NH2 . ARG A 298 ? 0.63379 1.22254 1.57145 -0.01089 0.18909  0.12620  334 ARG A NH2 
2407 N N   . GLY A 299 ? 0.53303 0.88216 1.16676 -0.05387 0.10238  0.07876  335 GLY A N   
2408 C CA  . GLY A 299 ? 0.52733 0.83499 1.10295 -0.05850 0.10125  0.07533  335 GLY A CA  
2409 C C   . GLY A 299 ? 0.70263 0.99680 1.26257 -0.05784 0.13324  0.09077  335 GLY A C   
2410 O O   . GLY A 299 ? 0.58739 0.90222 1.17102 -0.05070 0.15925  0.10434  335 GLY A O   
2411 N N   . TRP A 300 ? 0.68286 0.94333 1.20071 -0.06373 0.13152  0.08929  336 TRP A N   
2412 C CA  . TRP A 300 ? 0.74983 0.99457 1.24436 -0.06146 0.15880  0.10481  336 TRP A CA  
2413 C C   . TRP A 300 ? 0.79286 1.05398 1.34593 -0.07589 0.17643  0.12161  336 TRP A C   
2414 O O   . TRP A 300 ? 0.65154 0.91962 1.25269 -0.09398 0.16089  0.11661  336 TRP A O   
2415 C CB  . TRP A 300 ? 0.73235 0.93968 1.17372 -0.06398 0.14930  0.09912  336 TRP A CB  
2416 C CG  . TRP A 300 ? 0.71481 0.91304 1.17932 -0.08178 0.12828  0.09016  336 TRP A CG  
2417 C CD1 . TRP A 300 ? 0.74983 0.95067 1.21922 -0.08669 0.09931  0.07149  336 TRP A CD1 
2418 C CD2 . TRP A 300 ? 0.76147 0.94526 1.24682 -0.09577 0.13456  0.09882  336 TRP A CD2 
2419 N NE1 . TRP A 300 ? 0.74233 0.93185 1.23269 -0.10232 0.08639  0.06464  336 TRP A NE1 
2420 C CE2 . TRP A 300 ? 0.76801 0.94496 1.27086 -0.10870 0.10737  0.08106  336 TRP A CE2 
2421 C CE3 . TRP A 300 ? 0.77583 0.95020 1.26481 -0.09743 0.16074  0.12061  336 TRP A CE3 
2422 C CZ2 . TRP A 300 ? 0.82329 0.98175 1.35053 -0.12367 0.10482  0.08190  336 TRP A CZ2 
2423 C CZ3 . TRP A 300 ? 0.78557 0.94127 1.30003 -0.11286 0.15902  0.12533  336 TRP A CZ3 
2424 C CH2 . TRP A 300 ? 0.80741 0.95394 1.34222 -0.12604 0.13084  0.10481  336 TRP A CH2 
2425 N N   . ASP A 301 ? 0.94161 1.20873 1.49056 -0.06784 0.20925  0.14155  337 ASP A N   
2426 C CA  . ASP A 301 ? 0.93697 1.21475 1.53198 -0.08003 0.22933  0.16141  337 ASP A CA  
2427 C C   . ASP A 301 ? 1.06983 1.32314 1.61608 -0.07209 0.25393  0.17996  337 ASP A C   
2428 O O   . ASP A 301 ? 1.13969 1.37774 1.62698 -0.05670 0.25934  0.17814  337 ASP A O   
2429 C CB  . ASP A 301 ? 0.93215 1.24653 1.56772 -0.07466 0.24027  0.16619  337 ASP A CB  
2430 C CG  . ASP A 301 ? 1.02573 1.34719 1.71100 -0.09182 0.24375  0.17666  337 ASP A CG  
2431 O OD1 . ASP A 301 ? 1.10442 1.40518 1.77509 -0.09575 0.26037  0.19356  337 ASP A OD1 
2432 O OD2 . ASP A 301 ? 1.03307 1.38073 1.77262 -0.10105 0.22902  0.16827  337 ASP A OD2 
2433 N N   . ALA A 302 ? 1.14210 1.38981 1.70871 -0.08142 0.26574  0.19657  338 ALA A N   
2434 C CA  . ALA A 302 ? 1.24243 1.46366 1.76568 -0.07564 0.28413  0.21557  338 ALA A CA  
2435 C C   . ALA A 302 ? 1.31155 1.54518 1.79642 -0.05382 0.31297  0.22976  338 ALA A C   
2436 O O   . ALA A 302 ? 1.37546 1.59211 1.79889 -0.03862 0.32212  0.23445  338 ALA A O   
2437 C CB  . ALA A 302 ? 1.28304 1.49043 1.84422 -0.09350 0.28510  0.22890  338 ALA A CB  
2438 N N   . THR A 303 ? 1.28925 1.55344 1.80831 -0.05108 0.32663  0.23532  339 THR A N   
2439 C CA  . THR A 303 ? 1.34965 1.62522 1.83567 -0.03135 0.35597  0.25032  339 THR A CA  
2440 C C   . THR A 303 ? 1.43209 1.70963 1.86160 -0.00740 0.35959  0.23690  339 THR A C   
2441 O O   . THR A 303 ? 1.45971 1.72862 1.83172 0.01068  0.37670  0.24479  339 THR A O   
2442 C CB  . THR A 303 ? 1.30149 1.61205 1.84268 -0.03445 0.36970  0.25824  339 THR A CB  
2443 O OG1 . THR A 303 ? 1.31224 1.62118 1.91267 -0.05891 0.36178  0.26596  339 THR A OG1 
2444 C CG2 . THR A 303 ? 1.26529 1.58542 1.77438 -0.01639 0.40222  0.27747  339 THR A CG2 
2445 N N   . ILE A 304 ? 1.33998 1.62791 1.78391 -0.00606 0.34267  0.21595  340 ILE A N   
2446 C CA  . ILE A 304 ? 1.30131 1.59296 1.70151 0.01751  0.34739  0.20190  340 ILE A CA  
2447 C C   . ILE A 304 ? 1.29531 1.55772 1.64058 0.02223  0.33535  0.19121  340 ILE A C   
2448 O O   . ILE A 304 ? 1.34154 1.59385 1.62606 0.04249  0.34524  0.18683  340 ILE A O   
2449 C CB  . ILE A 304 ? 1.20456 1.52353 1.65102 0.01984  0.33728  0.18687  340 ILE A CB  
2450 C CG1 . ILE A 304 ? 1.20029 1.55172 1.70114 0.01635  0.34997  0.19752  340 ILE A CG1 
2451 C CG2 . ILE A 304 ? 1.17288 1.49079 1.57668 0.04555  0.34188  0.17109  340 ILE A CG2 
2452 C CD1 . ILE A 304 ? 1.22413 1.58469 1.69463 0.03492  0.38086  0.20978  340 ILE A CD1 
2453 N N   . ASN A 305 ? 1.30315 1.54784 1.66188 0.00406  0.30775  0.18221  341 ASN A N   
2454 C CA  . ASN A 305 ? 1.18411 1.39662 1.48600 0.00770  0.28155  0.16208  341 ASN A CA  
2455 C C   . ASN A 305 ? 1.28259 1.47075 1.52819 0.01374  0.28912  0.17195  341 ASN A C   
2456 O O   . ASN A 305 ? 1.33125 1.50828 1.51793 0.03131  0.28983  0.16281  341 ASN A O   
2457 C CB  . ASN A 305 ? 1.02863 1.23145 1.35885 -0.01166 0.24958  0.14871  341 ASN A CB  
2458 C CG  . ASN A 305 ? 0.91529 1.13845 1.28252 -0.01225 0.23488  0.13443  341 ASN A CG  
2459 O OD1 . ASN A 305 ? 0.81931 1.05903 1.24321 -0.02737 0.22511  0.13488  341 ASN A OD1 
2460 N ND2 . ASN A 305 ? 0.89820 1.11952 1.23418 0.00490  0.23204  0.12131  341 ASN A ND2 
2461 N N   . LYS A 306 ? 1.51728 1.69605 1.78104 -0.00009 0.29314  0.18985  342 LYS A N   
2462 C CA  . LYS A 306 ? 1.56866 1.72360 1.78116 0.00646  0.29757  0.20109  342 LYS A CA  
2463 C C   . LYS A 306 ? 1.64362 1.81051 1.82692 0.02460  0.33183  0.22313  342 LYS A C   
2464 O O   . LYS A 306 ? 1.71953 1.87494 1.83790 0.04235  0.33345  0.22092  342 LYS A O   
2465 C CB  . LYS A 306 ? 1.44085 1.57826 1.68384 -0.01245 0.29121  0.21405  342 LYS A CB  
2466 C CG  . LYS A 306 ? 1.49643 1.60339 1.68853 -0.00768 0.27727  0.21234  342 LYS A CG  
2467 C CD  . LYS A 306 ? 1.41659 1.50968 1.60638 -0.01610 0.24294  0.18455  342 LYS A CD  
2468 C CE  . LYS A 306 ? 1.36288 1.43291 1.49863 -0.00722 0.22920  0.17935  342 LYS A CE  
2469 N NZ  . LYS A 306 ? 1.44796 1.52212 1.52745 0.01151  0.22867  0.16842  342 LYS A NZ  
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