data_9BBQ
# 
_entry.id   9BBQ 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.403 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   9BBQ         pdb_00009bbq 10.2210/pdb9bbq/pdb 
WWPDB D_1000282096 ?            ?                   
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
_pdbx_audit_revision_history.part_number 
1 'Structure model' 1 0 2025-04-16 ? 
2 'Structure model' 1 1 2025-05-14 ? 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_audit_revision_group.ordinal             1 
_pdbx_audit_revision_group.revision_ordinal    2 
_pdbx_audit_revision_group.data_content_type   'Structure model' 
_pdbx_audit_revision_group.group               'Derived calculations' 
# 
loop_
_pdbx_audit_revision_category.ordinal 
_pdbx_audit_revision_category.revision_ordinal 
_pdbx_audit_revision_category.data_content_type 
_pdbx_audit_revision_category.category 
1 2 'Structure model' pdbx_struct_assembly      
2 2 'Structure model' pdbx_struct_assembly_gen  
3 2 'Structure model' pdbx_struct_assembly_prop 
4 2 'Structure model' pdbx_struct_oper_list     
# 
loop_
_pdbx_audit_revision_item.ordinal 
_pdbx_audit_revision_item.revision_ordinal 
_pdbx_audit_revision_item.data_content_type 
_pdbx_audit_revision_item.item 
1 2 'Structure model' '_pdbx_struct_assembly.details'             
2 2 'Structure model' '_pdbx_struct_assembly.method_details'      
3 2 'Structure model' '_pdbx_struct_assembly.oligomeric_count'    
4 2 'Structure model' '_pdbx_struct_assembly.oligomeric_details'  
5 2 'Structure model' '_pdbx_struct_assembly_gen.oper_expression' 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9BBQ 
_pdbx_database_status.recvd_initial_deposition_date   2024-04-07 
_pdbx_database_status.SG_entry                        N 
_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_contact_author.id                 4 
_pdbx_contact_author.email              olsens@uthscsa.edu 
_pdbx_contact_author.name_first         Shaun 
_pdbx_contact_author.name_last          Olsen 
_pdbx_contact_author.name_mi            K 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-1265-7101 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Afsar, M.'   1 0000-0002-3062-9219 
'Bury, P.'    2 0000-0003-3445-2649 
'Olsen, S.K.' 3 0000-0002-1265-7101 
# 
_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                     'SARS-CoV-2 Mpro in complex with compound 6c inhibitor' 
_citation.year                      ? 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      ? 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Afsar, M.'   1 0000-0002-3062-9219 
primary 'Bury, P.'    2 0000-0003-3445-2649 
primary 'Olsen, S.K.' 3 0000-0002-1265-7101 
# 
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 '3C-like proteinase nsp5' 33825.547 1   3.4.22.69 ? 'UNP residues 3264-3569' ? 
2 non-polymer syn 
;N-[(2R)-1-({(2S)-1-amino-3-[(2S,3R)-2-hydroxypyrrolidin-3-yl]propan-2-yl}amino)-4-methyl-1-oxopentan-2-yl]-4'-ethoxy[1,1'-biphenyl]-4-carboxamide
;
496.642   1   ?         ? ?                        ? 
3 water       nat water 18.015    115 ?         ? ?                        ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        '3CL-PRO,3CLp,Main protease,Mpro,Non-structural protein 5,nsp5,SARS coronavirus main proteinase' 
# 
_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       
;SGFRKMAFPSGKVEGCMVQVTCGTTTLNGLWLDDVVYCPRHVICTSEDMLNPNYEDLLIRKSNHNFLVQAGNVQLRVIGH
SMQNCVLKLKVDTANPKTPKYKFVRIQPGQTFSVLACYNGSPSGVYQCAMRPNFTIKGSFLNGSCGSVGFNIDYDCVSFC
YMHHMELPTGVHAGTDLEGNFYGPFVDRQTAQAAGTDTTITVNVLAWLYAAVINGDRWFLNRFTTTLNDFNLVAMKYNYE
PLTQDHVDILGPLSAQTGIAVLDMCASLKELLQNGMNGRTILGSALLEDEFTPFDVVRQCSGVTFQ
;
_entity_poly.pdbx_seq_one_letter_code_can   
;SGFRKMAFPSGKVEGCMVQVTCGTTTLNGLWLDDVVYCPRHVICTSEDMLNPNYEDLLIRKSNHNFLVQAGNVQLRVIGH
SMQNCVLKLKVDTANPKTPKYKFVRIQPGQTFSVLACYNGSPSGVYQCAMRPNFTIKGSFLNGSCGSVGFNIDYDCVSFC
YMHHMELPTGVHAGTDLEGNFYGPFVDRQTAQAAGTDTTITVNVLAWLYAAVINGDRWFLNRFTTTLNDFNLVAMKYNYE
PLTQDHVDILGPLSAQTGIAVLDMCASLKELLQNGMNGRTILGSALLEDEFTPFDVVRQCSGVTFQ
;
_entity_poly.pdbx_strand_id                 A 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 
;N-[(2R)-1-({(2S)-1-amino-3-[(2S,3R)-2-hydroxypyrrolidin-3-yl]propan-2-yl}amino)-4-methyl-1-oxopentan-2-yl]-4'-ethoxy[1,1'-biphenyl]-4-carboxamide
;
A1ALF 
3 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   GLY n 
1 3   PHE n 
1 4   ARG n 
1 5   LYS n 
1 6   MET n 
1 7   ALA n 
1 8   PHE n 
1 9   PRO n 
1 10  SER n 
1 11  GLY n 
1 12  LYS n 
1 13  VAL n 
1 14  GLU n 
1 15  GLY n 
1 16  CYS n 
1 17  MET n 
1 18  VAL n 
1 19  GLN n 
1 20  VAL n 
1 21  THR n 
1 22  CYS n 
1 23  GLY n 
1 24  THR n 
1 25  THR n 
1 26  THR n 
1 27  LEU n 
1 28  ASN n 
1 29  GLY n 
1 30  LEU n 
1 31  TRP n 
1 32  LEU n 
1 33  ASP n 
1 34  ASP n 
1 35  VAL n 
1 36  VAL n 
1 37  TYR n 
1 38  CYS n 
1 39  PRO n 
1 40  ARG n 
1 41  HIS n 
1 42  VAL n 
1 43  ILE n 
1 44  CYS n 
1 45  THR n 
1 46  SER n 
1 47  GLU n 
1 48  ASP n 
1 49  MET n 
1 50  LEU n 
1 51  ASN n 
1 52  PRO n 
1 53  ASN n 
1 54  TYR n 
1 55  GLU n 
1 56  ASP n 
1 57  LEU n 
1 58  LEU n 
1 59  ILE n 
1 60  ARG n 
1 61  LYS n 
1 62  SER n 
1 63  ASN n 
1 64  HIS n 
1 65  ASN n 
1 66  PHE n 
1 67  LEU n 
1 68  VAL n 
1 69  GLN n 
1 70  ALA n 
1 71  GLY n 
1 72  ASN n 
1 73  VAL n 
1 74  GLN n 
1 75  LEU n 
1 76  ARG n 
1 77  VAL n 
1 78  ILE n 
1 79  GLY n 
1 80  HIS n 
1 81  SER n 
1 82  MET n 
1 83  GLN n 
1 84  ASN n 
1 85  CYS n 
1 86  VAL n 
1 87  LEU n 
1 88  LYS n 
1 89  LEU n 
1 90  LYS n 
1 91  VAL n 
1 92  ASP n 
1 93  THR n 
1 94  ALA n 
1 95  ASN n 
1 96  PRO n 
1 97  LYS n 
1 98  THR n 
1 99  PRO n 
1 100 LYS n 
1 101 TYR n 
1 102 LYS n 
1 103 PHE n 
1 104 VAL n 
1 105 ARG n 
1 106 ILE n 
1 107 GLN n 
1 108 PRO n 
1 109 GLY n 
1 110 GLN n 
1 111 THR n 
1 112 PHE n 
1 113 SER n 
1 114 VAL n 
1 115 LEU n 
1 116 ALA n 
1 117 CYS n 
1 118 TYR n 
1 119 ASN n 
1 120 GLY n 
1 121 SER n 
1 122 PRO n 
1 123 SER n 
1 124 GLY n 
1 125 VAL n 
1 126 TYR n 
1 127 GLN n 
1 128 CYS n 
1 129 ALA n 
1 130 MET n 
1 131 ARG n 
1 132 PRO n 
1 133 ASN n 
1 134 PHE n 
1 135 THR n 
1 136 ILE n 
1 137 LYS n 
1 138 GLY n 
1 139 SER n 
1 140 PHE n 
1 141 LEU n 
1 142 ASN n 
1 143 GLY n 
1 144 SER n 
1 145 CYS n 
1 146 GLY n 
1 147 SER n 
1 148 VAL n 
1 149 GLY n 
1 150 PHE n 
1 151 ASN n 
1 152 ILE n 
1 153 ASP n 
1 154 TYR n 
1 155 ASP n 
1 156 CYS n 
1 157 VAL n 
1 158 SER n 
1 159 PHE n 
1 160 CYS n 
1 161 TYR n 
1 162 MET n 
1 163 HIS n 
1 164 HIS n 
1 165 MET n 
1 166 GLU n 
1 167 LEU n 
1 168 PRO n 
1 169 THR n 
1 170 GLY n 
1 171 VAL n 
1 172 HIS n 
1 173 ALA n 
1 174 GLY n 
1 175 THR n 
1 176 ASP n 
1 177 LEU n 
1 178 GLU n 
1 179 GLY n 
1 180 ASN n 
1 181 PHE n 
1 182 TYR n 
1 183 GLY n 
1 184 PRO n 
1 185 PHE n 
1 186 VAL n 
1 187 ASP n 
1 188 ARG n 
1 189 GLN n 
1 190 THR n 
1 191 ALA n 
1 192 GLN n 
1 193 ALA n 
1 194 ALA n 
1 195 GLY n 
1 196 THR n 
1 197 ASP n 
1 198 THR n 
1 199 THR n 
1 200 ILE n 
1 201 THR n 
1 202 VAL n 
1 203 ASN n 
1 204 VAL n 
1 205 LEU n 
1 206 ALA n 
1 207 TRP n 
1 208 LEU n 
1 209 TYR n 
1 210 ALA n 
1 211 ALA n 
1 212 VAL n 
1 213 ILE n 
1 214 ASN n 
1 215 GLY n 
1 216 ASP n 
1 217 ARG n 
1 218 TRP n 
1 219 PHE n 
1 220 LEU n 
1 221 ASN n 
1 222 ARG n 
1 223 PHE n 
1 224 THR n 
1 225 THR n 
1 226 THR n 
1 227 LEU n 
1 228 ASN n 
1 229 ASP n 
1 230 PHE n 
1 231 ASN n 
1 232 LEU n 
1 233 VAL n 
1 234 ALA n 
1 235 MET n 
1 236 LYS n 
1 237 TYR n 
1 238 ASN n 
1 239 TYR n 
1 240 GLU n 
1 241 PRO n 
1 242 LEU n 
1 243 THR n 
1 244 GLN n 
1 245 ASP n 
1 246 HIS n 
1 247 VAL n 
1 248 ASP n 
1 249 ILE n 
1 250 LEU n 
1 251 GLY n 
1 252 PRO n 
1 253 LEU n 
1 254 SER n 
1 255 ALA n 
1 256 GLN n 
1 257 THR n 
1 258 GLY n 
1 259 ILE n 
1 260 ALA n 
1 261 VAL n 
1 262 LEU n 
1 263 ASP n 
1 264 MET n 
1 265 CYS n 
1 266 ALA n 
1 267 SER n 
1 268 LEU n 
1 269 LYS n 
1 270 GLU n 
1 271 LEU n 
1 272 LEU n 
1 273 GLN n 
1 274 ASN n 
1 275 GLY n 
1 276 MET n 
1 277 ASN n 
1 278 GLY n 
1 279 ARG n 
1 280 THR n 
1 281 ILE n 
1 282 LEU n 
1 283 GLY n 
1 284 SER n 
1 285 ALA n 
1 286 LEU n 
1 287 LEU n 
1 288 GLU n 
1 289 ASP n 
1 290 GLU n 
1 291 PHE n 
1 292 THR n 
1 293 PRO n 
1 294 PHE n 
1 295 ASP n 
1 296 VAL n 
1 297 VAL n 
1 298 ARG n 
1 299 GLN n 
1 300 CYS n 
1 301 SER n 
1 302 GLY n 
1 303 VAL n 
1 304 THR n 
1 305 PHE n 
1 306 GLN 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                   306 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'rep, 1a-1b' 
_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      'Severe acute respiratory syndrome coronavirus 2' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     2697049 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      
;Escherichia coli 'BL21-Gold(DE3)pLysS AG'
;
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     866768 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
A1ALF non-polymer         . 
;N-[(2R)-1-({(2S)-1-amino-3-[(2S,3R)-2-hydroxypyrrolidin-3-yl]propan-2-yl}amino)-4-methyl-1-oxopentan-2-yl]-4'-ethoxy[1,1'-biphenyl]-4-carboxamide
;
? 'C28 H40 N4 O4'  496.642 
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 
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   1   1   SER SER A . n 
A 1 2   GLY 2   2   2   GLY GLY A . n 
A 1 3   PHE 3   3   3   PHE PHE A . n 
A 1 4   ARG 4   4   4   ARG ARG A . n 
A 1 5   LYS 5   5   5   LYS LYS A . n 
A 1 6   MET 6   6   6   MET MET A . n 
A 1 7   ALA 7   7   7   ALA ALA A . n 
A 1 8   PHE 8   8   8   PHE PHE A . n 
A 1 9   PRO 9   9   9   PRO PRO A . n 
A 1 10  SER 10  10  10  SER SER A . n 
A 1 11  GLY 11  11  11  GLY GLY A . n 
A 1 12  LYS 12  12  12  LYS LYS A . n 
A 1 13  VAL 13  13  13  VAL VAL A . n 
A 1 14  GLU 14  14  14  GLU GLU A . n 
A 1 15  GLY 15  15  15  GLY GLY A . n 
A 1 16  CYS 16  16  16  CYS CYS A . n 
A 1 17  MET 17  17  17  MET MET A . n 
A 1 18  VAL 18  18  18  VAL VAL A . n 
A 1 19  GLN 19  19  19  GLN GLN A . n 
A 1 20  VAL 20  20  20  VAL VAL A . n 
A 1 21  THR 21  21  21  THR THR A . n 
A 1 22  CYS 22  22  22  CYS CYS A . n 
A 1 23  GLY 23  23  23  GLY GLY A . n 
A 1 24  THR 24  24  24  THR THR A . n 
A 1 25  THR 25  25  25  THR THR A . n 
A 1 26  THR 26  26  26  THR THR A . n 
A 1 27  LEU 27  27  27  LEU LEU A . n 
A 1 28  ASN 28  28  28  ASN ASN A . n 
A 1 29  GLY 29  29  29  GLY GLY A . n 
A 1 30  LEU 30  30  30  LEU LEU A . n 
A 1 31  TRP 31  31  31  TRP TRP A . n 
A 1 32  LEU 32  32  32  LEU LEU A . n 
A 1 33  ASP 33  33  33  ASP ASP A . n 
A 1 34  ASP 34  34  34  ASP ASP A . n 
A 1 35  VAL 35  35  35  VAL VAL A . n 
A 1 36  VAL 36  36  36  VAL VAL A . n 
A 1 37  TYR 37  37  37  TYR TYR A . n 
A 1 38  CYS 38  38  38  CYS CYS A . n 
A 1 39  PRO 39  39  39  PRO PRO A . n 
A 1 40  ARG 40  40  40  ARG ARG A . n 
A 1 41  HIS 41  41  41  HIS HIS A . n 
A 1 42  VAL 42  42  42  VAL VAL A . n 
A 1 43  ILE 43  43  43  ILE ILE A . n 
A 1 44  CYS 44  44  44  CYS CYS A . n 
A 1 45  THR 45  45  45  THR THR A . n 
A 1 46  SER 46  46  46  SER SER A . n 
A 1 47  GLU 47  47  47  GLU ALA A . n 
A 1 48  ASP 48  48  48  ASP ASP A . n 
A 1 49  MET 49  49  49  MET MET A . n 
A 1 50  LEU 50  50  50  LEU LEU A . n 
A 1 51  ASN 51  51  51  ASN ASN A . n 
A 1 52  PRO 52  52  52  PRO PRO A . n 
A 1 53  ASN 53  53  53  ASN ASN A . n 
A 1 54  TYR 54  54  54  TYR TYR A . n 
A 1 55  GLU 55  55  55  GLU GLU A . n 
A 1 56  ASP 56  56  56  ASP ASP A . n 
A 1 57  LEU 57  57  57  LEU LEU A . n 
A 1 58  LEU 58  58  58  LEU LEU A . n 
A 1 59  ILE 59  59  59  ILE ILE A . n 
A 1 60  ARG 60  60  60  ARG ARG A . n 
A 1 61  LYS 61  61  61  LYS LYS A . n 
A 1 62  SER 62  62  62  SER SER A . n 
A 1 63  ASN 63  63  63  ASN ASN A . n 
A 1 64  HIS 64  64  64  HIS HIS A . n 
A 1 65  ASN 65  65  65  ASN ASN A . n 
A 1 66  PHE 66  66  66  PHE PHE A . n 
A 1 67  LEU 67  67  67  LEU LEU A . n 
A 1 68  VAL 68  68  68  VAL VAL A . n 
A 1 69  GLN 69  69  69  GLN GLN A . n 
A 1 70  ALA 70  70  70  ALA ALA A . n 
A 1 71  GLY 71  71  71  GLY GLY A . n 
A 1 72  ASN 72  72  72  ASN ALA A . n 
A 1 73  VAL 73  73  73  VAL VAL A . n 
A 1 74  GLN 74  74  74  GLN GLN A . n 
A 1 75  LEU 75  75  75  LEU LEU A . n 
A 1 76  ARG 76  76  76  ARG ARG A . n 
A 1 77  VAL 77  77  77  VAL VAL A . n 
A 1 78  ILE 78  78  78  ILE ILE A . n 
A 1 79  GLY 79  79  79  GLY GLY A . n 
A 1 80  HIS 80  80  80  HIS HIS A . n 
A 1 81  SER 81  81  81  SER SER A . n 
A 1 82  MET 82  82  82  MET MET A . n 
A 1 83  GLN 83  83  83  GLN GLN A . n 
A 1 84  ASN 84  84  84  ASN ASN A . n 
A 1 85  CYS 85  85  85  CYS CYS A . n 
A 1 86  VAL 86  86  86  VAL VAL A . n 
A 1 87  LEU 87  87  87  LEU LEU A . n 
A 1 88  LYS 88  88  88  LYS LYS A . n 
A 1 89  LEU 89  89  89  LEU LEU A . n 
A 1 90  LYS 90  90  90  LYS LYS A . n 
A 1 91  VAL 91  91  91  VAL VAL A . n 
A 1 92  ASP 92  92  92  ASP ASP A . n 
A 1 93  THR 93  93  93  THR THR A . n 
A 1 94  ALA 94  94  94  ALA ALA A . n 
A 1 95  ASN 95  95  95  ASN ASN A . n 
A 1 96  PRO 96  96  96  PRO PRO A . n 
A 1 97  LYS 97  97  97  LYS LYS A . n 
A 1 98  THR 98  98  98  THR THR A . n 
A 1 99  PRO 99  99  99  PRO PRO A . n 
A 1 100 LYS 100 100 100 LYS LYS A . n 
A 1 101 TYR 101 101 101 TYR TYR A . n 
A 1 102 LYS 102 102 102 LYS LYS A . n 
A 1 103 PHE 103 103 103 PHE PHE A . n 
A 1 104 VAL 104 104 104 VAL VAL A . n 
A 1 105 ARG 105 105 105 ARG ARG A . n 
A 1 106 ILE 106 106 106 ILE ILE A . n 
A 1 107 GLN 107 107 107 GLN GLN A . n 
A 1 108 PRO 108 108 108 PRO PRO A . n 
A 1 109 GLY 109 109 109 GLY GLY A . n 
A 1 110 GLN 110 110 110 GLN GLN A . n 
A 1 111 THR 111 111 111 THR THR A . n 
A 1 112 PHE 112 112 112 PHE PHE A . n 
A 1 113 SER 113 113 113 SER SER A . n 
A 1 114 VAL 114 114 114 VAL VAL A . n 
A 1 115 LEU 115 115 115 LEU LEU A . n 
A 1 116 ALA 116 116 116 ALA ALA A . n 
A 1 117 CYS 117 117 117 CYS CYS A . n 
A 1 118 TYR 118 118 118 TYR TYR A . n 
A 1 119 ASN 119 119 119 ASN ASN A . n 
A 1 120 GLY 120 120 120 GLY GLY A . n 
A 1 121 SER 121 121 121 SER SER A . n 
A 1 122 PRO 122 122 122 PRO PRO A . n 
A 1 123 SER 123 123 123 SER SER A . n 
A 1 124 GLY 124 124 124 GLY GLY A . n 
A 1 125 VAL 125 125 125 VAL VAL A . n 
A 1 126 TYR 126 126 126 TYR TYR A . n 
A 1 127 GLN 127 127 127 GLN GLN A . n 
A 1 128 CYS 128 128 128 CYS CYS A . n 
A 1 129 ALA 129 129 129 ALA ALA A . n 
A 1 130 MET 130 130 130 MET MET A . n 
A 1 131 ARG 131 131 131 ARG ARG A . n 
A 1 132 PRO 132 132 132 PRO PRO A . n 
A 1 133 ASN 133 133 133 ASN ASN A . n 
A 1 134 PHE 134 134 134 PHE PHE A . n 
A 1 135 THR 135 135 135 THR THR A . n 
A 1 136 ILE 136 136 136 ILE ILE A . n 
A 1 137 LYS 137 137 137 LYS LYS A . n 
A 1 138 GLY 138 138 138 GLY GLY A . n 
A 1 139 SER 139 139 139 SER SER A . n 
A 1 140 PHE 140 140 140 PHE PHE A . n 
A 1 141 LEU 141 141 141 LEU LEU A . n 
A 1 142 ASN 142 142 142 ASN ASN A . n 
A 1 143 GLY 143 143 143 GLY GLY A . n 
A 1 144 SER 144 144 144 SER SER A . n 
A 1 145 CYS 145 145 145 CYS CYS A . n 
A 1 146 GLY 146 146 146 GLY GLY A . n 
A 1 147 SER 147 147 147 SER SER A . n 
A 1 148 VAL 148 148 148 VAL VAL A . n 
A 1 149 GLY 149 149 149 GLY GLY A . n 
A 1 150 PHE 150 150 150 PHE PHE A . n 
A 1 151 ASN 151 151 151 ASN ASN A . n 
A 1 152 ILE 152 152 152 ILE ILE A . n 
A 1 153 ASP 153 153 153 ASP ASP A . n 
A 1 154 TYR 154 154 154 TYR ALA A . n 
A 1 155 ASP 155 155 155 ASP ASP A . n 
A 1 156 CYS 156 156 156 CYS CYS A . n 
A 1 157 VAL 157 157 157 VAL VAL A . n 
A 1 158 SER 158 158 158 SER SER A . n 
A 1 159 PHE 159 159 159 PHE PHE A . n 
A 1 160 CYS 160 160 160 CYS CYS A . n 
A 1 161 TYR 161 161 161 TYR TYR A . n 
A 1 162 MET 162 162 162 MET MET A . n 
A 1 163 HIS 163 163 163 HIS HIS A . n 
A 1 164 HIS 164 164 164 HIS HIS A . n 
A 1 165 MET 165 165 165 MET MET A . n 
A 1 166 GLU 166 166 166 GLU GLU A . n 
A 1 167 LEU 167 167 167 LEU LEU A . n 
A 1 168 PRO 168 168 168 PRO PRO A . n 
A 1 169 THR 169 169 169 THR THR A . n 
A 1 170 GLY 170 170 170 GLY GLY A . n 
A 1 171 VAL 171 171 171 VAL VAL A . n 
A 1 172 HIS 172 172 172 HIS HIS A . n 
A 1 173 ALA 173 173 173 ALA ALA A . n 
A 1 174 GLY 174 174 174 GLY GLY A . n 
A 1 175 THR 175 175 175 THR THR A . n 
A 1 176 ASP 176 176 176 ASP ASP A . n 
A 1 177 LEU 177 177 177 LEU LEU A . n 
A 1 178 GLU 178 178 178 GLU GLU A . n 
A 1 179 GLY 179 179 179 GLY GLY A . n 
A 1 180 ASN 180 180 180 ASN ASN A . n 
A 1 181 PHE 181 181 181 PHE PHE A . n 
A 1 182 TYR 182 182 182 TYR TYR A . n 
A 1 183 GLY 183 183 183 GLY GLY A . n 
A 1 184 PRO 184 184 184 PRO PRO A . n 
A 1 185 PHE 185 185 185 PHE PHE A . n 
A 1 186 VAL 186 186 186 VAL VAL A . n 
A 1 187 ASP 187 187 187 ASP ASP A . n 
A 1 188 ARG 188 188 188 ARG ARG A . n 
A 1 189 GLN 189 189 189 GLN GLN A . n 
A 1 190 THR 190 190 190 THR THR A . n 
A 1 191 ALA 191 191 191 ALA ALA A . n 
A 1 192 GLN 192 192 192 GLN GLN A . n 
A 1 193 ALA 193 193 193 ALA ALA A . n 
A 1 194 ALA 194 194 194 ALA ALA A . n 
A 1 195 GLY 195 195 195 GLY GLY A . n 
A 1 196 THR 196 196 196 THR THR A . n 
A 1 197 ASP 197 197 197 ASP ASP A . n 
A 1 198 THR 198 198 198 THR THR A . n 
A 1 199 THR 199 199 199 THR THR A . n 
A 1 200 ILE 200 200 200 ILE ILE A . n 
A 1 201 THR 201 201 201 THR THR A . n 
A 1 202 VAL 202 202 202 VAL VAL A . n 
A 1 203 ASN 203 203 203 ASN ASN A . n 
A 1 204 VAL 204 204 204 VAL VAL A . n 
A 1 205 LEU 205 205 205 LEU LEU A . n 
A 1 206 ALA 206 206 206 ALA ALA A . n 
A 1 207 TRP 207 207 207 TRP TRP A . n 
A 1 208 LEU 208 208 208 LEU LEU A . n 
A 1 209 TYR 209 209 209 TYR TYR A . n 
A 1 210 ALA 210 210 210 ALA ALA A . n 
A 1 211 ALA 211 211 211 ALA ALA A . n 
A 1 212 VAL 212 212 212 VAL VAL A . n 
A 1 213 ILE 213 213 213 ILE ILE A . n 
A 1 214 ASN 214 214 214 ASN ASN A . n 
A 1 215 GLY 215 215 215 GLY GLY A . n 
A 1 216 ASP 216 216 216 ASP ASP A . n 
A 1 217 ARG 217 217 217 ARG ALA A . n 
A 1 218 TRP 218 218 218 TRP TRP A . n 
A 1 219 PHE 219 219 219 PHE PHE A . n 
A 1 220 LEU 220 220 220 LEU LEU A . n 
A 1 221 ASN 221 221 221 ASN ASN A . n 
A 1 222 ARG 222 222 222 ARG ALA A . n 
A 1 223 PHE 223 223 223 PHE PHE A . n 
A 1 224 THR 224 224 224 THR THR A . n 
A 1 225 THR 225 225 225 THR THR A . n 
A 1 226 THR 226 226 226 THR THR A . n 
A 1 227 LEU 227 227 227 LEU LEU A . n 
A 1 228 ASN 228 228 228 ASN ASN A . n 
A 1 229 ASP 229 229 229 ASP ASP A . n 
A 1 230 PHE 230 230 230 PHE PHE A . n 
A 1 231 ASN 231 231 231 ASN ASN A . n 
A 1 232 LEU 232 232 232 LEU LEU A . n 
A 1 233 VAL 233 233 233 VAL VAL A . n 
A 1 234 ALA 234 234 234 ALA ALA A . n 
A 1 235 MET 235 235 235 MET ALA A . n 
A 1 236 LYS 236 236 236 LYS LYS A . n 
A 1 237 TYR 237 237 237 TYR TYR A . n 
A 1 238 ASN 238 238 238 ASN ASN A . n 
A 1 239 TYR 239 239 239 TYR TYR A . n 
A 1 240 GLU 240 240 240 GLU GLU A . n 
A 1 241 PRO 241 241 241 PRO PRO A . n 
A 1 242 LEU 242 242 242 LEU LEU A . n 
A 1 243 THR 243 243 243 THR THR A . n 
A 1 244 GLN 244 244 244 GLN GLN A . n 
A 1 245 ASP 245 245 245 ASP ASP A . n 
A 1 246 HIS 246 246 246 HIS HIS A . n 
A 1 247 VAL 247 247 247 VAL VAL A . n 
A 1 248 ASP 248 248 248 ASP ASP A . n 
A 1 249 ILE 249 249 249 ILE ILE A . n 
A 1 250 LEU 250 250 250 LEU LEU A . n 
A 1 251 GLY 251 251 251 GLY GLY A . n 
A 1 252 PRO 252 252 252 PRO PRO A . n 
A 1 253 LEU 253 253 253 LEU LEU A . n 
A 1 254 SER 254 254 254 SER SER A . n 
A 1 255 ALA 255 255 255 ALA ALA A . n 
A 1 256 GLN 256 256 256 GLN GLN A . n 
A 1 257 THR 257 257 257 THR THR A . n 
A 1 258 GLY 258 258 258 GLY GLY A . n 
A 1 259 ILE 259 259 259 ILE ILE A . n 
A 1 260 ALA 260 260 260 ALA ALA A . n 
A 1 261 VAL 261 261 261 VAL VAL A . n 
A 1 262 LEU 262 262 262 LEU LEU A . n 
A 1 263 ASP 263 263 263 ASP ASP A . n 
A 1 264 MET 264 264 264 MET MET A . n 
A 1 265 CYS 265 265 265 CYS CYS A . n 
A 1 266 ALA 266 266 266 ALA ALA A . n 
A 1 267 SER 267 267 267 SER SER A . n 
A 1 268 LEU 268 268 268 LEU LEU A . n 
A 1 269 LYS 269 269 269 LYS LYS A . n 
A 1 270 GLU 270 270 270 GLU ALA A . n 
A 1 271 LEU 271 271 271 LEU LEU A . n 
A 1 272 LEU 272 272 272 LEU LEU A . n 
A 1 273 GLN 273 273 273 GLN GLN A . n 
A 1 274 ASN 274 274 274 ASN ASN A . n 
A 1 275 GLY 275 275 275 GLY GLY A . n 
A 1 276 MET 276 276 276 MET MET A . n 
A 1 277 ASN 277 277 277 ASN ASN A . n 
A 1 278 GLY 278 278 278 GLY GLY A . n 
A 1 279 ARG 279 279 279 ARG ALA A . n 
A 1 280 THR 280 280 280 THR THR A . n 
A 1 281 ILE 281 281 281 ILE ILE A . n 
A 1 282 LEU 282 282 282 LEU LEU A . n 
A 1 283 GLY 283 283 283 GLY GLY A . n 
A 1 284 SER 284 284 284 SER SER A . n 
A 1 285 ALA 285 285 285 ALA ALA A . n 
A 1 286 LEU 286 286 286 LEU LEU A . n 
A 1 287 LEU 287 287 287 LEU LEU A . n 
A 1 288 GLU 288 288 288 GLU GLU A . n 
A 1 289 ASP 289 289 289 ASP ASP A . n 
A 1 290 GLU 290 290 290 GLU GLU A . n 
A 1 291 PHE 291 291 291 PHE PHE A . n 
A 1 292 THR 292 292 292 THR THR A . n 
A 1 293 PRO 293 293 293 PRO PRO A . n 
A 1 294 PHE 294 294 294 PHE PHE A . n 
A 1 295 ASP 295 295 295 ASP ASP A . n 
A 1 296 VAL 296 296 296 VAL VAL A . n 
A 1 297 VAL 297 297 297 VAL VAL A . n 
A 1 298 ARG 298 298 298 ARG ALA A . n 
A 1 299 GLN 299 299 299 GLN GLN A . n 
A 1 300 CYS 300 300 300 CYS CYS A . n 
A 1 301 SER 301 301 301 SER SER A . n 
A 1 302 GLY 302 302 302 GLY GLY A . n 
A 1 303 VAL 303 303 303 VAL VAL A . n 
A 1 304 THR 304 304 304 THR THR A . n 
A 1 305 PHE 305 305 305 PHE PHE A . n 
A 1 306 GLN 306 306 ?   ?   ?   A . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1ALF 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1ALF 
_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 A1ALF 1   401 401 A1ALF LIG A . 
C 3 HOH   1   501 101 HOH   HOH A . 
C 3 HOH   2   502 7   HOH   HOH A . 
C 3 HOH   3   503 112 HOH   HOH A . 
C 3 HOH   4   504 83  HOH   HOH A . 
C 3 HOH   5   505 57  HOH   HOH A . 
C 3 HOH   6   506 85  HOH   HOH A . 
C 3 HOH   7   507 46  HOH   HOH A . 
C 3 HOH   8   508 98  HOH   HOH A . 
C 3 HOH   9   509 41  HOH   HOH A . 
C 3 HOH   10  510 39  HOH   HOH A . 
C 3 HOH   11  511 53  HOH   HOH A . 
C 3 HOH   12  512 99  HOH   HOH A . 
C 3 HOH   13  513 104 HOH   HOH A . 
C 3 HOH   14  514 62  HOH   HOH A . 
C 3 HOH   15  515 50  HOH   HOH A . 
C 3 HOH   16  516 63  HOH   HOH A . 
C 3 HOH   17  517 54  HOH   HOH A . 
C 3 HOH   18  518 65  HOH   HOH A . 
C 3 HOH   19  519 16  HOH   HOH A . 
C 3 HOH   20  520 24  HOH   HOH A . 
C 3 HOH   21  521 40  HOH   HOH A . 
C 3 HOH   22  522 15  HOH   HOH A . 
C 3 HOH   23  523 82  HOH   HOH A . 
C 3 HOH   24  524 78  HOH   HOH A . 
C 3 HOH   25  525 66  HOH   HOH A . 
C 3 HOH   26  526 1   HOH   HOH A . 
C 3 HOH   27  527 95  HOH   HOH A . 
C 3 HOH   28  528 20  HOH   HOH A . 
C 3 HOH   29  529 23  HOH   HOH A . 
C 3 HOH   30  530 34  HOH   HOH A . 
C 3 HOH   31  531 73  HOH   HOH A . 
C 3 HOH   32  532 3   HOH   HOH A . 
C 3 HOH   33  533 29  HOH   HOH A . 
C 3 HOH   34  534 51  HOH   HOH A . 
C 3 HOH   35  535 9   HOH   HOH A . 
C 3 HOH   36  536 25  HOH   HOH A . 
C 3 HOH   37  537 27  HOH   HOH A . 
C 3 HOH   38  538 64  HOH   HOH A . 
C 3 HOH   39  539 94  HOH   HOH A . 
C 3 HOH   40  540 5   HOH   HOH A . 
C 3 HOH   41  541 58  HOH   HOH A . 
C 3 HOH   42  542 84  HOH   HOH A . 
C 3 HOH   43  543 6   HOH   HOH A . 
C 3 HOH   44  544 8   HOH   HOH A . 
C 3 HOH   45  545 105 HOH   HOH A . 
C 3 HOH   46  546 2   HOH   HOH A . 
C 3 HOH   47  547 4   HOH   HOH A . 
C 3 HOH   48  548 12  HOH   HOH A . 
C 3 HOH   49  549 56  HOH   HOH A . 
C 3 HOH   50  550 11  HOH   HOH A . 
C 3 HOH   51  551 33  HOH   HOH A . 
C 3 HOH   52  552 32  HOH   HOH A . 
C 3 HOH   53  553 74  HOH   HOH A . 
C 3 HOH   54  554 43  HOH   HOH A . 
C 3 HOH   55  555 26  HOH   HOH A . 
C 3 HOH   56  556 14  HOH   HOH A . 
C 3 HOH   57  557 93  HOH   HOH A . 
C 3 HOH   58  558 68  HOH   HOH A . 
C 3 HOH   59  559 49  HOH   HOH A . 
C 3 HOH   60  560 45  HOH   HOH A . 
C 3 HOH   61  561 35  HOH   HOH A . 
C 3 HOH   62  562 67  HOH   HOH A . 
C 3 HOH   63  563 18  HOH   HOH A . 
C 3 HOH   64  564 48  HOH   HOH A . 
C 3 HOH   65  565 55  HOH   HOH A . 
C 3 HOH   66  566 103 HOH   HOH A . 
C 3 HOH   67  567 108 HOH   HOH A . 
C 3 HOH   68  568 110 HOH   HOH A . 
C 3 HOH   69  569 13  HOH   HOH A . 
C 3 HOH   70  570 100 HOH   HOH A . 
C 3 HOH   71  571 102 HOH   HOH A . 
C 3 HOH   72  572 96  HOH   HOH A . 
C 3 HOH   73  573 76  HOH   HOH A . 
C 3 HOH   74  574 19  HOH   HOH A . 
C 3 HOH   75  575 42  HOH   HOH A . 
C 3 HOH   76  576 17  HOH   HOH A . 
C 3 HOH   77  577 47  HOH   HOH A . 
C 3 HOH   78  578 59  HOH   HOH A . 
C 3 HOH   79  579 111 HOH   HOH A . 
C 3 HOH   80  580 31  HOH   HOH A . 
C 3 HOH   81  581 44  HOH   HOH A . 
C 3 HOH   82  582 28  HOH   HOH A . 
C 3 HOH   83  583 10  HOH   HOH A . 
C 3 HOH   84  584 60  HOH   HOH A . 
C 3 HOH   85  585 114 HOH   HOH A . 
C 3 HOH   86  586 37  HOH   HOH A . 
C 3 HOH   87  587 115 HOH   HOH A . 
C 3 HOH   88  588 22  HOH   HOH A . 
C 3 HOH   89  589 92  HOH   HOH A . 
C 3 HOH   90  590 109 HOH   HOH A . 
C 3 HOH   91  591 106 HOH   HOH A . 
C 3 HOH   92  592 75  HOH   HOH A . 
C 3 HOH   93  593 38  HOH   HOH A . 
C 3 HOH   94  594 107 HOH   HOH A . 
C 3 HOH   95  595 90  HOH   HOH A . 
C 3 HOH   96  596 21  HOH   HOH A . 
C 3 HOH   97  597 69  HOH   HOH A . 
C 3 HOH   98  598 72  HOH   HOH A . 
C 3 HOH   99  599 88  HOH   HOH A . 
C 3 HOH   100 600 91  HOH   HOH A . 
C 3 HOH   101 601 36  HOH   HOH A . 
C 3 HOH   102 602 79  HOH   HOH A . 
C 3 HOH   103 603 61  HOH   HOH A . 
C 3 HOH   104 604 30  HOH   HOH A . 
C 3 HOH   105 605 86  HOH   HOH A . 
C 3 HOH   106 606 97  HOH   HOH A . 
C 3 HOH   107 607 87  HOH   HOH A . 
C 3 HOH   108 608 52  HOH   HOH A . 
C 3 HOH   109 609 89  HOH   HOH A . 
C 3 HOH   110 610 80  HOH   HOH A . 
C 3 HOH   111 611 113 HOH   HOH A . 
C 3 HOH   112 612 77  HOH   HOH A . 
C 3 HOH   113 613 81  HOH   HOH A . 
C 3 HOH   114 614 71  HOH   HOH A . 
C 3 HOH   115 615 70  HOH   HOH A . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1  1 Y 1 A GLU 47  ? CG  ? A GLU 47  CG  
2  1 Y 1 A GLU 47  ? CD  ? A GLU 47  CD  
3  1 Y 1 A GLU 47  ? OE1 ? A GLU 47  OE1 
4  1 Y 1 A GLU 47  ? OE2 ? A GLU 47  OE2 
5  1 Y 1 A ASN 72  ? CG  ? A ASN 72  CG  
6  1 Y 1 A ASN 72  ? OD1 ? A ASN 72  OD1 
7  1 Y 1 A ASN 72  ? ND2 ? A ASN 72  ND2 
8  1 Y 1 A TYR 154 ? CG  ? A TYR 154 CG  
9  1 Y 1 A TYR 154 ? CD1 ? A TYR 154 CD1 
10 1 Y 1 A TYR 154 ? CD2 ? A TYR 154 CD2 
11 1 Y 1 A TYR 154 ? CE1 ? A TYR 154 CE1 
12 1 Y 1 A TYR 154 ? CE2 ? A TYR 154 CE2 
13 1 Y 1 A TYR 154 ? CZ  ? A TYR 154 CZ  
14 1 Y 1 A TYR 154 ? OH  ? A TYR 154 OH  
15 1 Y 1 A ARG 217 ? CG  ? A ARG 217 CG  
16 1 Y 1 A ARG 217 ? CD  ? A ARG 217 CD  
17 1 Y 1 A ARG 217 ? NE  ? A ARG 217 NE  
18 1 Y 1 A ARG 217 ? CZ  ? A ARG 217 CZ  
19 1 Y 1 A ARG 217 ? NH1 ? A ARG 217 NH1 
20 1 Y 1 A ARG 217 ? NH2 ? A ARG 217 NH2 
21 1 Y 1 A ARG 222 ? CG  ? A ARG 222 CG  
22 1 Y 1 A ARG 222 ? CD  ? A ARG 222 CD  
23 1 Y 1 A ARG 222 ? NE  ? A ARG 222 NE  
24 1 Y 1 A ARG 222 ? CZ  ? A ARG 222 CZ  
25 1 Y 1 A ARG 222 ? NH1 ? A ARG 222 NH1 
26 1 Y 1 A ARG 222 ? NH2 ? A ARG 222 NH2 
27 1 Y 1 A MET 235 ? CG  ? A MET 235 CG  
28 1 Y 1 A MET 235 ? SD  ? A MET 235 SD  
29 1 Y 1 A MET 235 ? CE  ? A MET 235 CE  
30 1 Y 1 A GLU 270 ? CG  ? A GLU 270 CG  
31 1 Y 1 A GLU 270 ? CD  ? A GLU 270 CD  
32 1 Y 1 A GLU 270 ? OE1 ? A GLU 270 OE1 
33 1 Y 1 A GLU 270 ? OE2 ? A GLU 270 OE2 
34 1 Y 1 A ARG 279 ? CG  ? A ARG 279 CG  
35 1 Y 1 A ARG 279 ? CD  ? A ARG 279 CD  
36 1 Y 1 A ARG 279 ? NE  ? A ARG 279 NE  
37 1 Y 1 A ARG 279 ? CZ  ? A ARG 279 CZ  
38 1 Y 1 A ARG 279 ? NH1 ? A ARG 279 NH1 
39 1 Y 1 A ARG 279 ? NH2 ? A ARG 279 NH2 
40 1 Y 1 A ARG 298 ? CG  ? A ARG 298 CG  
41 1 Y 1 A ARG 298 ? CD  ? A ARG 298 CD  
42 1 Y 1 A ARG 298 ? NE  ? A ARG 298 NE  
43 1 Y 1 A ARG 298 ? CZ  ? A ARG 298 CZ  
44 1 Y 1 A ARG 298 ? NH1 ? A ARG 298 NH1 
45 1 Y 1 A ARG 298 ? NH2 ? A ARG 298 NH2 
# 
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  ? ? ? 1.20.1_4487 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS     ? ? ? .           2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? Aimless ? ? ? .           3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER  ? ? ? .           4 
# 
_cell.angle_alpha                  90.000 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   101.880 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9BBQ 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     114.508 
_cell.length_a_esd                 ? 
_cell.length_b                     53.476 
_cell.length_b_esd                 ? 
_cell.length_c                     45.375 
_cell.length_c_esd                 ? 
_cell.volume                       271899.318 
_cell.volume_esd                   ? 
_cell.Z_PDB                        4 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         9BBQ 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                5 
_symmetry.space_group_name_Hall            'C 2y' 
_symmetry.space_group_name_H-M             'C 1 2 1' 
_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                   9BBQ 
_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             2.01 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          38.79 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              7.0 
_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    '0.2 M Potassium chloride, 20% w/v Polyethylene glycol 3,350' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            291.15 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS EIGER2 X 16M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2021-10-10 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.979 
_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                        'APS BEAMLINE 24-ID-E' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.979 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   24-ID-E 
_diffrn_source.pdbx_synchrotron_site       APS 
# 
_reflns.B_iso_Wilson_estimate                          27.01 
_reflns.entry_id                                       9BBQ 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.78 
_reflns.d_resolution_low                               56.01 
_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                                     25826 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           99.8 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                8.9 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          16.1 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                ? 
_reflns.pdbx_Rpim_I_all                                ? 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.999 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.067 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    1.78 
_reflns_shell.d_res_low                                     1.82 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           0.5 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             1497 
_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                               ? 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               ? 
_reflns_shell.pdbx_Rpim_I_all                               ? 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.311 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  3.336 
_reflns_shell.pdbx_Rsym_value                               1.6 
_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                               31.36 
_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                                 9BBQ 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            1.78 
_refine.ls_d_res_low                             48.26 
_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                     25578 
_refine.ls_number_reflns_R_free                  1999 
_refine.ls_number_reflns_R_work                  23579 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    98.88 
_refine.ls_percent_reflns_R_free                 7.82 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2000 
_refine.ls_R_factor_R_free                       0.2317 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1973 
_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                          1.40 
_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            ? 
_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                 22.8215 
_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                            0.2434 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       1.78 
_refine_hist.d_res_low                        48.26 
_refine_hist.number_atoms_solvent             115 
_refine_hist.number_atoms_total               2464 
_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        2313 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         36 
_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' ? 0.0055 ? 2403 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.8822 ? 3272 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 0.0554 ? 374  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.0073 ? 422  ? f_plane_restr      ? ? 
'X-RAY DIFFRACTION' ? 7.2123 ? 328  ? 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' 1.78 1.83  . . 139 1650 97.07 . . . . 0.3192 . . . . . . . . . . . 0.3187 
'X-RAY DIFFRACTION' 1.83 1.87  . . 142 1655 98.47 . . . . 0.2555 . . . . . . . . . . . 0.2780 
'X-RAY DIFFRACTION' 1.87 1.93  . . 140 1664 98.47 . . . . 0.2394 . . . . . . . . . . . 0.2687 
'X-RAY DIFFRACTION' 1.93 1.99  . . 143 1682 99.02 . . . . 0.2216 . . . . . . . . . . . 0.2718 
'X-RAY DIFFRACTION' 1.99 2.06  . . 145 1703 98.93 . . . . 0.2241 . . . . . . . . . . . 0.2415 
'X-RAY DIFFRACTION' 2.06 2.15  . . 138 1634 97.52 . . . . 0.2198 . . . . . . . . . . . 0.2602 
'X-RAY DIFFRACTION' 2.15 2.24  . . 143 1678 99.24 . . . . 0.2207 . . . . . . . . . . . 0.2533 
'X-RAY DIFFRACTION' 2.24 2.36  . . 143 1689 99.62 . . . . 0.2137 . . . . . . . . . . . 0.2584 
'X-RAY DIFFRACTION' 2.36 2.51  . . 144 1700 99.78 . . . . 0.2200 . . . . . . . . . . . 0.2437 
'X-RAY DIFFRACTION' 2.51 2.70  . . 144 1689 99.51 . . . . 0.2183 . . . . . . . . . . . 0.2834 
'X-RAY DIFFRACTION' 2.70 2.98  . . 142 1688 99.56 . . . . 0.2155 . . . . . . . . . . . 0.2691 
'X-RAY DIFFRACTION' 2.98 3.41  . . 144 1695 99.24 . . . . 0.2002 . . . . . . . . . . . 0.2302 
'X-RAY DIFFRACTION' 3.41 4.29  . . 144 1707 99.52 . . . . 0.1688 . . . . . . . . . . . 0.2021 
'X-RAY DIFFRACTION' 4.29 48.26 . . 148 1745 98.44 . . . . 0.1588 . . . . . . . . . . . 0.1794 
# 
_struct.entry_id                     9BBQ 
_struct.title                        'SARS-CoV-2 Mpro in complex with compound 6c inhibitor' 
_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        9BBQ 
_struct_keywords.text            'Protease, Inhibitor, VIRAL PROTEIN, Hydrolase' 
_struct_keywords.pdbx_keywords   'VIRAL PROTEIN, Hydrolase' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    R1AB_SARS2 
_struct_ref.pdbx_db_accession          P0DTD1 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;SGFRKMAFPSGKVEGCMVQVTCGTTTLNGLWLDDVVYCPRHVICTSEDMLNPNYEDLLIRKSNHNFLVQAGNVQLRVIGH
SMQNCVLKLKVDTANPKTPKYKFVRIQPGQTFSVLACYNGSPSGVYQCAMRPNFTIKGSFLNGSCGSVGFNIDYDCVSFC
YMHHMELPTGVHAGTDLEGNFYGPFVDRQTAQAAGTDTTITVNVLAWLYAAVINGDRWFLNRFTTTLNDFNLVAMKYNYE
PLTQDHVDILGPLSAQTGIAVLDMCASLKELLQNGMNGRTILGSALLEDEFTPFDVVRQCSGVTFQ
;
_struct_ref.pdbx_align_begin           3264 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              9BBQ 
_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                 306 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             P0DTD1 
_struct_ref_seq.db_align_beg                  3264 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  3569 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       1 
_struct_ref_seq.pdbx_auth_seq_align_end       306 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   dimeric 
_pdbx_struct_assembly.oligomeric_count     2 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 4920  ? 
1 MORE         -29   ? 
1 'SSA (A^2)'  24650 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1,2 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C 
# 
loop_
_pdbx_struct_oper_list.id 
_pdbx_struct_oper_list.type 
_pdbx_struct_oper_list.name 
_pdbx_struct_oper_list.symmetry_operation 
_pdbx_struct_oper_list.matrix[1][1] 
_pdbx_struct_oper_list.matrix[1][2] 
_pdbx_struct_oper_list.matrix[1][3] 
_pdbx_struct_oper_list.vector[1] 
_pdbx_struct_oper_list.matrix[2][1] 
_pdbx_struct_oper_list.matrix[2][2] 
_pdbx_struct_oper_list.matrix[2][3] 
_pdbx_struct_oper_list.vector[2] 
_pdbx_struct_oper_list.matrix[3][1] 
_pdbx_struct_oper_list.matrix[3][2] 
_pdbx_struct_oper_list.matrix[3][3] 
_pdbx_struct_oper_list.vector[3] 
1 'identity operation'         1_555 x,y,z     1.0000000000  0.0000000000 0.0000000000 0.0000000000   0.0000000000 1.0000000000 
0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000  0.0000000000 
2 'crystal symmetry operation' 2_755 -x+2,y,-z -1.0000000000 0.0000000000 0.0000000000 229.0160000000 0.0000000000 1.0000000000 
0.0000000000 0.0000000000 0.0000000000 0.0000000000 -1.0000000000 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 SER A 10  ? GLY A 15  ? SER A 10  GLY A 15  1 ? 6  
HELX_P HELX_P2  AA2 HIS A 41  ? CYS A 44  ? HIS A 41  CYS A 44  5 ? 4  
HELX_P HELX_P3  AA3 GLU A 47  ? ASN A 51  ? GLU A 47  ASN A 51  5 ? 5  
HELX_P HELX_P4  AA4 ASN A 53  ? ARG A 60  ? ASN A 53  ARG A 60  1 ? 8  
HELX_P HELX_P5  AA5 LYS A 61  ? HIS A 64  ? LYS A 61  HIS A 64  5 ? 4  
HELX_P HELX_P6  AA6 ILE A 200 ? ASN A 214 ? ILE A 200 ASN A 214 1 ? 15 
HELX_P HELX_P7  AA7 THR A 226 ? TYR A 237 ? THR A 226 TYR A 237 1 ? 12 
HELX_P HELX_P8  AA8 THR A 243 ? LEU A 250 ? THR A 243 LEU A 250 1 ? 8  
HELX_P HELX_P9  AA9 LEU A 250 ? GLY A 258 ? LEU A 250 GLY A 258 1 ? 9  
HELX_P HELX_P10 AB1 ALA A 260 ? GLY A 275 ? ALA A 260 GLY A 275 1 ? 16 
HELX_P HELX_P11 AB2 THR A 292 ? GLY A 302 ? THR A 292 GLY A 302 1 ? 11 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
_struct_conn.id                            covale1 
_struct_conn.conn_type_id                  covale 
_struct_conn.pdbx_leaving_atom_flag        none 
_struct_conn.pdbx_PDB_id                   ? 
_struct_conn.ptnr1_label_asym_id           A 
_struct_conn.ptnr1_label_comp_id           CYS 
_struct_conn.ptnr1_label_seq_id            145 
_struct_conn.ptnr1_label_atom_id           SG 
_struct_conn.pdbx_ptnr1_label_alt_id       ? 
_struct_conn.pdbx_ptnr1_PDB_ins_code       ? 
_struct_conn.pdbx_ptnr1_standard_comp_id   ? 
_struct_conn.ptnr1_symmetry                1_555 
_struct_conn.ptnr2_label_asym_id           B 
_struct_conn.ptnr2_label_comp_id           A1ALF 
_struct_conn.ptnr2_label_seq_id            . 
_struct_conn.ptnr2_label_atom_id           C09 
_struct_conn.pdbx_ptnr2_label_alt_id       ? 
_struct_conn.pdbx_ptnr2_PDB_ins_code       ? 
_struct_conn.ptnr1_auth_asym_id            A 
_struct_conn.ptnr1_auth_comp_id            CYS 
_struct_conn.ptnr1_auth_seq_id             145 
_struct_conn.ptnr2_auth_asym_id            A 
_struct_conn.ptnr2_auth_comp_id            A1ALF 
_struct_conn.ptnr2_auth_seq_id             401 
_struct_conn.ptnr2_symmetry                1_555 
_struct_conn.pdbx_ptnr3_label_atom_id      ? 
_struct_conn.pdbx_ptnr3_label_seq_id       ? 
_struct_conn.pdbx_ptnr3_label_comp_id      ? 
_struct_conn.pdbx_ptnr3_label_asym_id      ? 
_struct_conn.pdbx_ptnr3_label_alt_id       ? 
_struct_conn.pdbx_ptnr3_PDB_ins_code       ? 
_struct_conn.details                       ? 
_struct_conn.pdbx_dist_value               1.643 
_struct_conn.pdbx_value_order              ? 
_struct_conn.pdbx_role                     ? 
# 
_struct_conn_type.id          covale 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
_pdbx_modification_feature.ordinal                            1 
_pdbx_modification_feature.label_comp_id                      A1ALF 
_pdbx_modification_feature.label_asym_id                      B 
_pdbx_modification_feature.label_seq_id                       . 
_pdbx_modification_feature.label_alt_id                       ? 
_pdbx_modification_feature.modified_residue_label_comp_id     CYS 
_pdbx_modification_feature.modified_residue_label_asym_id     A 
_pdbx_modification_feature.modified_residue_label_seq_id      145 
_pdbx_modification_feature.modified_residue_label_alt_id      ? 
_pdbx_modification_feature.auth_comp_id                       A1ALF 
_pdbx_modification_feature.auth_asym_id                       A 
_pdbx_modification_feature.auth_seq_id                        401 
_pdbx_modification_feature.PDB_ins_code                       ? 
_pdbx_modification_feature.symmetry                           1_555 
_pdbx_modification_feature.modified_residue_auth_comp_id      CYS 
_pdbx_modification_feature.modified_residue_auth_asym_id      A 
_pdbx_modification_feature.modified_residue_auth_seq_id       145 
_pdbx_modification_feature.modified_residue_PDB_ins_code      ? 
_pdbx_modification_feature.modified_residue_symmetry          1_555 
_pdbx_modification_feature.comp_id_linking_atom               C09 
_pdbx_modification_feature.modified_residue_id_linking_atom   SG 
_pdbx_modification_feature.modified_residue_id                CYS 
_pdbx_modification_feature.ref_pcm_id                         1 
_pdbx_modification_feature.ref_comp_id                        A1ALF 
_pdbx_modification_feature.type                               None 
_pdbx_modification_feature.category                           'Covalent chemical modification' 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 7 ? 
AA2 ? 5 ? 
AA3 ? 3 ? 
# 
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 
AA1 6 7 ? anti-parallel 
AA2 1 2 ? parallel      
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA2 4 5 ? anti-parallel 
AA3 1 2 ? parallel      
AA3 2 3 ? 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 73  ? LEU A 75  ? VAL A 73  LEU A 75  
AA1 2 PHE A 66  ? ALA A 70  ? PHE A 66  ALA A 70  
AA1 3 MET A 17  ? CYS A 22  ? MET A 17  CYS A 22  
AA1 4 THR A 25  ? LEU A 32  ? THR A 25  LEU A 32  
AA1 5 VAL A 35  ? PRO A 39  ? VAL A 35  PRO A 39  
AA1 6 VAL A 86  ? VAL A 91  ? VAL A 86  VAL A 91  
AA1 7 VAL A 77  ? GLN A 83  ? VAL A 77  GLN A 83  
AA2 1 LYS A 100 ? PHE A 103 ? LYS A 100 PHE A 103 
AA2 2 CYS A 156 ? GLU A 166 ? CYS A 156 GLU A 166 
AA2 3 VAL A 148 ? ASP A 153 ? VAL A 148 ASP A 153 
AA2 4 THR A 111 ? TYR A 118 ? THR A 111 TYR A 118 
AA2 5 SER A 121 ? ALA A 129 ? SER A 121 ALA A 129 
AA3 1 LYS A 100 ? PHE A 103 ? LYS A 100 PHE A 103 
AA3 2 CYS A 156 ? GLU A 166 ? CYS A 156 GLU A 166 
AA3 3 HIS A 172 ? THR A 175 ? HIS A 172 THR A 175 
# 
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 O VAL A 73  ? O VAL A 73  N ALA A 70  ? N ALA A 70  
AA1 2 3 O LEU A 67  ? O LEU A 67  N THR A 21  ? N THR A 21  
AA1 3 4 N VAL A 20  ? N VAL A 20  O LEU A 27  ? O LEU A 27  
AA1 4 5 N LEU A 30  ? N LEU A 30  O TYR A 37  ? O TYR A 37  
AA1 5 6 N CYS A 38  ? N CYS A 38  O LEU A 87  ? O LEU A 87  
AA1 6 7 O LYS A 88  ? O LYS A 88  N SER A 81  ? N SER A 81  
AA2 1 2 N LYS A 100 ? N LYS A 100 O VAL A 157 ? O VAL A 157 
AA2 2 3 O CYS A 156 ? O CYS A 156 N ASP A 153 ? N ASP A 153 
AA2 3 4 O PHE A 150 ? O PHE A 150 N SER A 113 ? N SER A 113 
AA2 4 5 N ALA A 116 ? N ALA A 116 O SER A 123 ? O SER A 123 
AA3 1 2 N LYS A 100 ? N LYS A 100 O VAL A 157 ? O VAL A 157 
AA3 2 3 N MET A 165 ? N MET A 165 O ALA A 173 ? O ALA A 173 
# 
_pdbx_entry_details.entry_id                   9BBQ 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   Y 
# 
_pdbx_validate_close_contact.id               1 
_pdbx_validate_close_contact.PDB_model_num    1 
_pdbx_validate_close_contact.auth_atom_id_1   NH1 
_pdbx_validate_close_contact.auth_asym_id_1   A 
_pdbx_validate_close_contact.auth_comp_id_1   ARG 
_pdbx_validate_close_contact.auth_seq_id_1    60 
_pdbx_validate_close_contact.PDB_ins_code_1   ? 
_pdbx_validate_close_contact.label_alt_id_1   ? 
_pdbx_validate_close_contact.auth_atom_id_2   O 
_pdbx_validate_close_contact.auth_asym_id_2   A 
_pdbx_validate_close_contact.auth_comp_id_2   HOH 
_pdbx_validate_close_contact.auth_seq_id_2    501 
_pdbx_validate_close_contact.PDB_ins_code_2   ? 
_pdbx_validate_close_contact.label_alt_id_2   ? 
_pdbx_validate_close_contact.dist             2.15 
# 
_pdbx_validate_symm_contact.id                1 
_pdbx_validate_symm_contact.PDB_model_num     1 
_pdbx_validate_symm_contact.auth_atom_id_1    OG 
_pdbx_validate_symm_contact.auth_asym_id_1    A 
_pdbx_validate_symm_contact.auth_comp_id_1    SER 
_pdbx_validate_symm_contact.auth_seq_id_1     1 
_pdbx_validate_symm_contact.PDB_ins_code_1    ? 
_pdbx_validate_symm_contact.label_alt_id_1    ? 
_pdbx_validate_symm_contact.site_symmetry_1   1_555 
_pdbx_validate_symm_contact.auth_atom_id_2    O 
_pdbx_validate_symm_contact.auth_asym_id_2    A 
_pdbx_validate_symm_contact.auth_comp_id_2    PHE 
_pdbx_validate_symm_contact.auth_seq_id_2     140 
_pdbx_validate_symm_contact.PDB_ins_code_2    ? 
_pdbx_validate_symm_contact.label_alt_id_2    ? 
_pdbx_validate_symm_contact.site_symmetry_2   2_755 
_pdbx_validate_symm_contact.dist              2.15 
# 
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 ASP A 33  ? ? 54.14   -134.27 
2 1 ASN A 51  ? ? -157.40 65.33   
3 1 ASN A 84  ? ? 50.64   -120.35 
4 1 TYR A 154 ? ? 55.11   -95.84  
5 1 ASN A 277 ? ? 38.55   37.59   
# 
_pdbx_struct_special_symmetry.id              1 
_pdbx_struct_special_symmetry.PDB_model_num   1 
_pdbx_struct_special_symmetry.auth_asym_id    A 
_pdbx_struct_special_symmetry.auth_comp_id    HOH 
_pdbx_struct_special_symmetry.auth_seq_id     598 
_pdbx_struct_special_symmetry.PDB_ins_code    ? 
_pdbx_struct_special_symmetry.label_asym_id   C 
_pdbx_struct_special_symmetry.label_comp_id   HOH 
_pdbx_struct_special_symmetry.label_seq_id    . 
# 
loop_
_space_group_symop.id 
_space_group_symop.operation_xyz 
1 x,y,z           
2 -x,y,-z         
3 x+1/2,y+1/2,z   
4 -x+1/2,y+1/2,-z 
# 
_pdbx_refine_tls.id               1 
_pdbx_refine_tls.pdbx_refine_id   'X-RAY DIFFRACTION' 
_pdbx_refine_tls.details          ? 
_pdbx_refine_tls.method           refined 
_pdbx_refine_tls.origin_x         127.003955368 
_pdbx_refine_tls.origin_y         -27.1725194194 
_pdbx_refine_tls.origin_z         5.31255176497 
_pdbx_refine_tls.T[1][1]          0.126228971286 
_pdbx_refine_tls.T[1][1]_esd      ? 
_pdbx_refine_tls.T[1][2]          -0.00993222829304 
_pdbx_refine_tls.T[1][2]_esd      ? 
_pdbx_refine_tls.T[1][3]          0.0274613352295 
_pdbx_refine_tls.T[1][3]_esd      ? 
_pdbx_refine_tls.T[2][2]          0.16521073257 
_pdbx_refine_tls.T[2][2]_esd      ? 
_pdbx_refine_tls.T[2][3]          0.0135985552076 
_pdbx_refine_tls.T[2][3]_esd      ? 
_pdbx_refine_tls.T[3][3]          0.165408009097 
_pdbx_refine_tls.T[3][3]_esd      ? 
_pdbx_refine_tls.L[1][1]          1.58647026427 
_pdbx_refine_tls.L[1][1]_esd      ? 
_pdbx_refine_tls.L[1][2]          -0.129657906506 
_pdbx_refine_tls.L[1][2]_esd      ? 
_pdbx_refine_tls.L[1][3]          0.684643427397 
_pdbx_refine_tls.L[1][3]_esd      ? 
_pdbx_refine_tls.L[2][2]          1.46744360507 
_pdbx_refine_tls.L[2][2]_esd      ? 
_pdbx_refine_tls.L[2][3]          -0.480678058737 
_pdbx_refine_tls.L[2][3]_esd      ? 
_pdbx_refine_tls.L[3][3]          1.79191699214 
_pdbx_refine_tls.L[3][3]_esd      ? 
_pdbx_refine_tls.S[1][1]          -0.00663571640346 
_pdbx_refine_tls.S[1][1]_esd      ? 
_pdbx_refine_tls.S[1][2]          0.0576467485227 
_pdbx_refine_tls.S[1][2]_esd      ? 
_pdbx_refine_tls.S[1][3]          0.109279641493 
_pdbx_refine_tls.S[1][3]_esd      ? 
_pdbx_refine_tls.S[2][1]          -0.0222151552517 
_pdbx_refine_tls.S[2][1]_esd      ? 
_pdbx_refine_tls.S[2][2]          -0.00659388948205 
_pdbx_refine_tls.S[2][2]_esd      ? 
_pdbx_refine_tls.S[2][3]          0.0154702415064 
_pdbx_refine_tls.S[2][3]_esd      ? 
_pdbx_refine_tls.S[3][1]          0.0432106814504 
_pdbx_refine_tls.S[3][1]_esd      ? 
_pdbx_refine_tls.S[3][2]          -0.0209226448746 
_pdbx_refine_tls.S[3][2]_esd      ? 
_pdbx_refine_tls.S[3][3]          -0.0167024806217 
_pdbx_refine_tls.S[3][3]_esd      ? 
# 
_pdbx_refine_tls_group.id                  1 
_pdbx_refine_tls_group.pdbx_refine_id      'X-RAY DIFFRACTION' 
_pdbx_refine_tls_group.refine_tls_id       1 
_pdbx_refine_tls_group.beg_label_asym_id   A 
_pdbx_refine_tls_group.beg_label_seq_id    1 
_pdbx_refine_tls_group.beg_auth_asym_id    A 
_pdbx_refine_tls_group.beg_auth_seq_id     1 
_pdbx_refine_tls_group.beg_PDB_ins_code    ? 
_pdbx_refine_tls_group.end_label_asym_id   C 
_pdbx_refine_tls_group.end_label_seq_id    ? 
_pdbx_refine_tls_group.end_auth_asym_id    S 
_pdbx_refine_tls_group.end_auth_seq_id     115 
_pdbx_refine_tls_group.end_PDB_ins_code    ? 
_pdbx_refine_tls_group.selection           ? 
_pdbx_refine_tls_group.selection_details   all 
# 
_pdbx_distant_solvent_atoms.id                                1 
_pdbx_distant_solvent_atoms.PDB_model_num                     1 
_pdbx_distant_solvent_atoms.auth_atom_id                      O 
_pdbx_distant_solvent_atoms.label_alt_id                      ? 
_pdbx_distant_solvent_atoms.auth_asym_id                      A 
_pdbx_distant_solvent_atoms.auth_comp_id                      HOH 
_pdbx_distant_solvent_atoms.auth_seq_id                       615 
_pdbx_distant_solvent_atoms.PDB_ins_code                      ? 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance   6.16 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance          . 
# 
_pdbx_unobs_or_zero_occ_residues.id               1 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num    1 
_pdbx_unobs_or_zero_occ_residues.polymer_flag     Y 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag   1 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id     A 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id     GLN 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id      306 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code     ? 
_pdbx_unobs_or_zero_occ_residues.label_asym_id    A 
_pdbx_unobs_or_zero_occ_residues.label_comp_id    GLN 
_pdbx_unobs_or_zero_occ_residues.label_seq_id     306 
# 
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 
A1ALF C13  C N R 1   
A1ALF C15  C N N 2   
A1ALF C17  C N N 3   
A1ALF C20  C Y N 4   
A1ALF C21  C Y N 5   
A1ALF C22  C Y N 6   
A1ALF C24  C Y N 7   
A1ALF C26  C Y N 8   
A1ALF C02  C N S 9   
A1ALF C04  C N N 10  
A1ALF C05  C N N 11  
A1ALF C06  C N R 12  
A1ALF C07  C N N 13  
A1ALF C08  C N S 14  
A1ALF C09  C N N 15  
A1ALF C12  C N N 16  
A1ALF C14  C N N 17  
A1ALF C16  C N N 18  
A1ALF C19  C N N 19  
A1ALF C23  C Y N 20  
A1ALF C25  C Y N 21  
A1ALF C27  C Y N 22  
A1ALF C29  C N N 23  
A1ALF C30  C N N 24  
A1ALF C31  C Y N 25  
A1ALF C32  C Y N 26  
A1ALF C33  C Y N 27  
A1ALF C34  C Y N 28  
A1ALF N03  N N N 29  
A1ALF N10  N N N 30  
A1ALF N11  N N N 31  
A1ALF N18  N N N 32  
A1ALF O01  O N N 33  
A1ALF O28  O N N 34  
A1ALF O35  O N N 35  
A1ALF O36  O N N 36  
A1ALF H131 H N N 37  
A1ALF H151 H N N 38  
A1ALF H172 H N N 39  
A1ALF H171 H N N 40  
A1ALF H173 H N N 41  
A1ALF H211 H N N 42  
A1ALF H221 H N N 43  
A1ALF H261 H N N 44  
A1ALF H021 H N N 45  
A1ALF H042 H N N 46  
A1ALF H041 H N N 47  
A1ALF H051 H N N 48  
A1ALF H052 H N N 49  
A1ALF H061 H N N 50  
A1ALF H072 H N N 51  
A1ALF H071 H N N 52  
A1ALF H081 H N N 53  
A1ALF H092 H N N 54  
A1ALF H091 H N N 55  
A1ALF H142 H N N 56  
A1ALF H141 H N N 57  
A1ALF H162 H N N 58  
A1ALF H163 H N N 59  
A1ALF H161 H N N 60  
A1ALF H251 H N N 61  
A1ALF H292 H N N 62  
A1ALF H291 H N N 63  
A1ALF H303 H N N 64  
A1ALF H301 H N N 65  
A1ALF H302 H N N 66  
A1ALF H311 H N N 67  
A1ALF H321 H N N 68  
A1ALF H331 H N N 69  
A1ALF H341 H N N 70  
A1ALF H031 H N N 71  
A1ALF H2   H N N 72  
A1ALF H102 H N N 73  
A1ALF H111 H N N 74  
A1ALF H181 H N N 75  
A1ALF H011 H N N 76  
ALA   N    N N N 77  
ALA   CA   C N S 78  
ALA   C    C N N 79  
ALA   O    O N N 80  
ALA   CB   C N N 81  
ALA   OXT  O N N 82  
ALA   H    H N N 83  
ALA   H2   H N N 84  
ALA   HA   H N N 85  
ALA   HB1  H N N 86  
ALA   HB2  H N N 87  
ALA   HB3  H N N 88  
ALA   HXT  H N N 89  
ARG   N    N N N 90  
ARG   CA   C N S 91  
ARG   C    C N N 92  
ARG   O    O N N 93  
ARG   CB   C N N 94  
ARG   CG   C N N 95  
ARG   CD   C N N 96  
ARG   NE   N N N 97  
ARG   CZ   C N N 98  
ARG   NH1  N N N 99  
ARG   NH2  N N N 100 
ARG   OXT  O N N 101 
ARG   H    H N N 102 
ARG   H2   H N N 103 
ARG   HA   H N N 104 
ARG   HB2  H N N 105 
ARG   HB3  H N N 106 
ARG   HG2  H N N 107 
ARG   HG3  H N N 108 
ARG   HD2  H N N 109 
ARG   HD3  H N N 110 
ARG   HE   H N N 111 
ARG   HH11 H N N 112 
ARG   HH12 H N N 113 
ARG   HH21 H N N 114 
ARG   HH22 H N N 115 
ARG   HXT  H N N 116 
ASN   N    N N N 117 
ASN   CA   C N S 118 
ASN   C    C N N 119 
ASN   O    O N N 120 
ASN   CB   C N N 121 
ASN   CG   C N N 122 
ASN   OD1  O N N 123 
ASN   ND2  N N N 124 
ASN   OXT  O N N 125 
ASN   H    H N N 126 
ASN   H2   H N N 127 
ASN   HA   H N N 128 
ASN   HB2  H N N 129 
ASN   HB3  H N N 130 
ASN   HD21 H N N 131 
ASN   HD22 H N N 132 
ASN   HXT  H N N 133 
ASP   N    N N N 134 
ASP   CA   C N S 135 
ASP   C    C N N 136 
ASP   O    O N N 137 
ASP   CB   C N N 138 
ASP   CG   C N N 139 
ASP   OD1  O N N 140 
ASP   OD2  O N N 141 
ASP   OXT  O N N 142 
ASP   H    H N N 143 
ASP   H2   H N N 144 
ASP   HA   H N N 145 
ASP   HB2  H N N 146 
ASP   HB3  H N N 147 
ASP   HD2  H N N 148 
ASP   HXT  H N N 149 
CYS   N    N N N 150 
CYS   CA   C N R 151 
CYS   C    C N N 152 
CYS   O    O N N 153 
CYS   CB   C N N 154 
CYS   SG   S N N 155 
CYS   OXT  O N N 156 
CYS   H    H N N 157 
CYS   H2   H N N 158 
CYS   HA   H N N 159 
CYS   HB2  H N N 160 
CYS   HB3  H N N 161 
CYS   HG   H N N 162 
CYS   HXT  H N N 163 
GLN   N    N N N 164 
GLN   CA   C N S 165 
GLN   C    C N N 166 
GLN   O    O N N 167 
GLN   CB   C N N 168 
GLN   CG   C N N 169 
GLN   CD   C N N 170 
GLN   OE1  O N N 171 
GLN   NE2  N N N 172 
GLN   OXT  O N N 173 
GLN   H    H N N 174 
GLN   H2   H N N 175 
GLN   HA   H N N 176 
GLN   HB2  H N N 177 
GLN   HB3  H N N 178 
GLN   HG2  H N N 179 
GLN   HG3  H N N 180 
GLN   HE21 H N N 181 
GLN   HE22 H N N 182 
GLN   HXT  H N N 183 
GLU   N    N N N 184 
GLU   CA   C N S 185 
GLU   C    C N N 186 
GLU   O    O N N 187 
GLU   CB   C N N 188 
GLU   CG   C N N 189 
GLU   CD   C N N 190 
GLU   OE1  O N N 191 
GLU   OE2  O N N 192 
GLU   OXT  O N N 193 
GLU   H    H N N 194 
GLU   H2   H N N 195 
GLU   HA   H N N 196 
GLU   HB2  H N N 197 
GLU   HB3  H N N 198 
GLU   HG2  H N N 199 
GLU   HG3  H N N 200 
GLU   HE2  H N N 201 
GLU   HXT  H N N 202 
GLY   N    N N N 203 
GLY   CA   C N N 204 
GLY   C    C N N 205 
GLY   O    O N N 206 
GLY   OXT  O N N 207 
GLY   H    H N N 208 
GLY   H2   H N N 209 
GLY   HA2  H N N 210 
GLY   HA3  H N N 211 
GLY   HXT  H N N 212 
HIS   N    N N N 213 
HIS   CA   C N S 214 
HIS   C    C N N 215 
HIS   O    O N N 216 
HIS   CB   C N N 217 
HIS   CG   C Y N 218 
HIS   ND1  N Y N 219 
HIS   CD2  C Y N 220 
HIS   CE1  C Y N 221 
HIS   NE2  N Y N 222 
HIS   OXT  O N N 223 
HIS   H    H N N 224 
HIS   H2   H N N 225 
HIS   HA   H N N 226 
HIS   HB2  H N N 227 
HIS   HB3  H N N 228 
HIS   HD1  H N N 229 
HIS   HD2  H N N 230 
HIS   HE1  H N N 231 
HIS   HE2  H N N 232 
HIS   HXT  H N N 233 
HOH   O    O N N 234 
HOH   H1   H N N 235 
HOH   H2   H N N 236 
ILE   N    N N N 237 
ILE   CA   C N S 238 
ILE   C    C N N 239 
ILE   O    O N N 240 
ILE   CB   C N S 241 
ILE   CG1  C N N 242 
ILE   CG2  C N N 243 
ILE   CD1  C N N 244 
ILE   OXT  O N N 245 
ILE   H    H N N 246 
ILE   H2   H N N 247 
ILE   HA   H N N 248 
ILE   HB   H N N 249 
ILE   HG12 H N N 250 
ILE   HG13 H N N 251 
ILE   HG21 H N N 252 
ILE   HG22 H N N 253 
ILE   HG23 H N N 254 
ILE   HD11 H N N 255 
ILE   HD12 H N N 256 
ILE   HD13 H N N 257 
ILE   HXT  H N N 258 
LEU   N    N N N 259 
LEU   CA   C N S 260 
LEU   C    C N N 261 
LEU   O    O N N 262 
LEU   CB   C N N 263 
LEU   CG   C N N 264 
LEU   CD1  C N N 265 
LEU   CD2  C N N 266 
LEU   OXT  O N N 267 
LEU   H    H N N 268 
LEU   H2   H N N 269 
LEU   HA   H N N 270 
LEU   HB2  H N N 271 
LEU   HB3  H N N 272 
LEU   HG   H N N 273 
LEU   HD11 H N N 274 
LEU   HD12 H N N 275 
LEU   HD13 H N N 276 
LEU   HD21 H N N 277 
LEU   HD22 H N N 278 
LEU   HD23 H N N 279 
LEU   HXT  H N N 280 
LYS   N    N N N 281 
LYS   CA   C N S 282 
LYS   C    C N N 283 
LYS   O    O N N 284 
LYS   CB   C N N 285 
LYS   CG   C N N 286 
LYS   CD   C N N 287 
LYS   CE   C N N 288 
LYS   NZ   N N N 289 
LYS   OXT  O N N 290 
LYS   H    H N N 291 
LYS   H2   H N N 292 
LYS   HA   H N N 293 
LYS   HB2  H N N 294 
LYS   HB3  H N N 295 
LYS   HG2  H N N 296 
LYS   HG3  H N N 297 
LYS   HD2  H N N 298 
LYS   HD3  H N N 299 
LYS   HE2  H N N 300 
LYS   HE3  H N N 301 
LYS   HZ1  H N N 302 
LYS   HZ2  H N N 303 
LYS   HZ3  H N N 304 
LYS   HXT  H N N 305 
MET   N    N N N 306 
MET   CA   C N S 307 
MET   C    C N N 308 
MET   O    O N N 309 
MET   CB   C N N 310 
MET   CG   C N N 311 
MET   SD   S N N 312 
MET   CE   C N N 313 
MET   OXT  O N N 314 
MET   H    H N N 315 
MET   H2   H N N 316 
MET   HA   H N N 317 
MET   HB2  H N N 318 
MET   HB3  H N N 319 
MET   HG2  H N N 320 
MET   HG3  H N N 321 
MET   HE1  H N N 322 
MET   HE2  H N N 323 
MET   HE3  H N N 324 
MET   HXT  H N N 325 
PHE   N    N N N 326 
PHE   CA   C N S 327 
PHE   C    C N N 328 
PHE   O    O N N 329 
PHE   CB   C N N 330 
PHE   CG   C Y N 331 
PHE   CD1  C Y N 332 
PHE   CD2  C Y N 333 
PHE   CE1  C Y N 334 
PHE   CE2  C Y N 335 
PHE   CZ   C Y N 336 
PHE   OXT  O N N 337 
PHE   H    H N N 338 
PHE   H2   H N N 339 
PHE   HA   H N N 340 
PHE   HB2  H N N 341 
PHE   HB3  H N N 342 
PHE   HD1  H N N 343 
PHE   HD2  H N N 344 
PHE   HE1  H N N 345 
PHE   HE2  H N N 346 
PHE   HZ   H N N 347 
PHE   HXT  H N N 348 
PRO   N    N N N 349 
PRO   CA   C N S 350 
PRO   C    C N N 351 
PRO   O    O N N 352 
PRO   CB   C N N 353 
PRO   CG   C N N 354 
PRO   CD   C N N 355 
PRO   OXT  O N N 356 
PRO   H    H N N 357 
PRO   HA   H N N 358 
PRO   HB2  H N N 359 
PRO   HB3  H N N 360 
PRO   HG2  H N N 361 
PRO   HG3  H N N 362 
PRO   HD2  H N N 363 
PRO   HD3  H N N 364 
PRO   HXT  H N N 365 
SER   N    N N N 366 
SER   CA   C N S 367 
SER   C    C N N 368 
SER   O    O N N 369 
SER   CB   C N N 370 
SER   OG   O N N 371 
SER   OXT  O N N 372 
SER   H    H N N 373 
SER   H2   H N N 374 
SER   HA   H N N 375 
SER   HB2  H N N 376 
SER   HB3  H N N 377 
SER   HG   H N N 378 
SER   HXT  H N N 379 
THR   N    N N N 380 
THR   CA   C N S 381 
THR   C    C N N 382 
THR   O    O N N 383 
THR   CB   C N R 384 
THR   OG1  O N N 385 
THR   CG2  C N N 386 
THR   OXT  O N N 387 
THR   H    H N N 388 
THR   H2   H N N 389 
THR   HA   H N N 390 
THR   HB   H N N 391 
THR   HG1  H N N 392 
THR   HG21 H N N 393 
THR   HG22 H N N 394 
THR   HG23 H N N 395 
THR   HXT  H N N 396 
TRP   N    N N N 397 
TRP   CA   C N S 398 
TRP   C    C N N 399 
TRP   O    O N N 400 
TRP   CB   C N N 401 
TRP   CG   C Y N 402 
TRP   CD1  C Y N 403 
TRP   CD2  C Y N 404 
TRP   NE1  N Y N 405 
TRP   CE2  C Y N 406 
TRP   CE3  C Y N 407 
TRP   CZ2  C Y N 408 
TRP   CZ3  C Y N 409 
TRP   CH2  C Y N 410 
TRP   OXT  O N N 411 
TRP   H    H N N 412 
TRP   H2   H N N 413 
TRP   HA   H N N 414 
TRP   HB2  H N N 415 
TRP   HB3  H N N 416 
TRP   HD1  H N N 417 
TRP   HE1  H N N 418 
TRP   HE3  H N N 419 
TRP   HZ2  H N N 420 
TRP   HZ3  H N N 421 
TRP   HH2  H N N 422 
TRP   HXT  H N N 423 
TYR   N    N N N 424 
TYR   CA   C N S 425 
TYR   C    C N N 426 
TYR   O    O N N 427 
TYR   CB   C N N 428 
TYR   CG   C Y N 429 
TYR   CD1  C Y N 430 
TYR   CD2  C Y N 431 
TYR   CE1  C Y N 432 
TYR   CE2  C Y N 433 
TYR   CZ   C Y N 434 
TYR   OH   O N N 435 
TYR   OXT  O N N 436 
TYR   H    H N N 437 
TYR   H2   H N N 438 
TYR   HA   H N N 439 
TYR   HB2  H N N 440 
TYR   HB3  H N N 441 
TYR   HD1  H N N 442 
TYR   HD2  H N N 443 
TYR   HE1  H N N 444 
TYR   HE2  H N N 445 
TYR   HH   H N N 446 
TYR   HXT  H N N 447 
VAL   N    N N N 448 
VAL   CA   C N S 449 
VAL   C    C N N 450 
VAL   O    O N N 451 
VAL   CB   C N N 452 
VAL   CG1  C N N 453 
VAL   CG2  C N N 454 
VAL   OXT  O N N 455 
VAL   H    H N N 456 
VAL   H2   H N N 457 
VAL   HA   H N N 458 
VAL   HB   H N N 459 
VAL   HG11 H N N 460 
VAL   HG12 H N N 461 
VAL   HG13 H N N 462 
VAL   HG21 H N N 463 
VAL   HG22 H N N 464 
VAL   HG23 H N N 465 
VAL   HXT  H N N 466 
# 
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 
A1ALF C02 C06  sing N N 1   
A1ALF C02 N03  sing N N 2   
A1ALF C02 O01  sing N N 3   
A1ALF C04 C05  sing N N 4   
A1ALF C04 N03  sing N N 5   
A1ALF C05 C06  sing N N 6   
A1ALF C06 C07  sing N N 7   
A1ALF C07 C08  sing N N 8   
A1ALF C08 C09  sing N N 9   
A1ALF C08 N11  sing N N 10  
A1ALF C09 N10  sing N N 11  
A1ALF C12 C13  sing N N 12  
A1ALF C12 N11  sing N N 13  
A1ALF C12 O36  doub N N 14  
A1ALF C13 C14  sing N N 15  
A1ALF C13 N18  sing N N 16  
A1ALF C14 C15  sing N N 17  
A1ALF C15 C16  sing N N 18  
A1ALF C15 C17  sing N N 19  
A1ALF C19 C20  sing N N 20  
A1ALF C19 N18  sing N N 21  
A1ALF C19 O35  doub N N 22  
A1ALF C20 C21  doub Y N 23  
A1ALF C20 C34  sing Y N 24  
A1ALF C21 C22  sing Y N 25  
A1ALF C22 C23  doub Y N 26  
A1ALF C23 C24  sing N N 27  
A1ALF C23 C33  sing Y N 28  
A1ALF C24 C25  doub Y N 29  
A1ALF C24 C32  sing Y N 30  
A1ALF C25 C26  sing Y N 31  
A1ALF C26 C27  doub Y N 32  
A1ALF C27 C31  sing Y N 33  
A1ALF C27 O28  sing N N 34  
A1ALF C29 C30  sing N N 35  
A1ALF C29 O28  sing N N 36  
A1ALF C31 C32  doub Y N 37  
A1ALF C33 C34  doub Y N 38  
A1ALF C13 H131 sing N N 39  
A1ALF C15 H151 sing N N 40  
A1ALF C17 H172 sing N N 41  
A1ALF C17 H171 sing N N 42  
A1ALF C17 H173 sing N N 43  
A1ALF C21 H211 sing N N 44  
A1ALF C22 H221 sing N N 45  
A1ALF C26 H261 sing N N 46  
A1ALF C02 H021 sing N N 47  
A1ALF C04 H042 sing N N 48  
A1ALF C04 H041 sing N N 49  
A1ALF C05 H051 sing N N 50  
A1ALF C05 H052 sing N N 51  
A1ALF C06 H061 sing N N 52  
A1ALF C07 H072 sing N N 53  
A1ALF C07 H071 sing N N 54  
A1ALF C08 H081 sing N N 55  
A1ALF C09 H092 sing N N 56  
A1ALF C09 H091 sing N N 57  
A1ALF C14 H142 sing N N 58  
A1ALF C14 H141 sing N N 59  
A1ALF C16 H162 sing N N 60  
A1ALF C16 H163 sing N N 61  
A1ALF C16 H161 sing N N 62  
A1ALF C25 H251 sing N N 63  
A1ALF C29 H292 sing N N 64  
A1ALF C29 H291 sing N N 65  
A1ALF C30 H303 sing N N 66  
A1ALF C30 H301 sing N N 67  
A1ALF C30 H302 sing N N 68  
A1ALF C31 H311 sing N N 69  
A1ALF C32 H321 sing N N 70  
A1ALF C33 H331 sing N N 71  
A1ALF C34 H341 sing N N 72  
A1ALF N03 H031 sing N N 73  
A1ALF N10 H2   sing N N 74  
A1ALF N10 H102 sing N N 75  
A1ALF N11 H111 sing N N 76  
A1ALF N18 H181 sing N N 77  
A1ALF O01 H011 sing N N 78  
ALA   N   CA   sing N N 79  
ALA   N   H    sing N N 80  
ALA   N   H2   sing N N 81  
ALA   CA  C    sing N N 82  
ALA   CA  CB   sing N N 83  
ALA   CA  HA   sing N N 84  
ALA   C   O    doub N N 85  
ALA   C   OXT  sing N N 86  
ALA   CB  HB1  sing N N 87  
ALA   CB  HB2  sing N N 88  
ALA   CB  HB3  sing N N 89  
ALA   OXT HXT  sing N N 90  
ARG   N   CA   sing N N 91  
ARG   N   H    sing N N 92  
ARG   N   H2   sing N N 93  
ARG   CA  C    sing N N 94  
ARG   CA  CB   sing N N 95  
ARG   CA  HA   sing N N 96  
ARG   C   O    doub N N 97  
ARG   C   OXT  sing N N 98  
ARG   CB  CG   sing N N 99  
ARG   CB  HB2  sing N N 100 
ARG   CB  HB3  sing N N 101 
ARG   CG  CD   sing N N 102 
ARG   CG  HG2  sing N N 103 
ARG   CG  HG3  sing N N 104 
ARG   CD  NE   sing N N 105 
ARG   CD  HD2  sing N N 106 
ARG   CD  HD3  sing N N 107 
ARG   NE  CZ   sing N N 108 
ARG   NE  HE   sing N N 109 
ARG   CZ  NH1  sing N N 110 
ARG   CZ  NH2  doub N N 111 
ARG   NH1 HH11 sing N N 112 
ARG   NH1 HH12 sing N N 113 
ARG   NH2 HH21 sing N N 114 
ARG   NH2 HH22 sing N N 115 
ARG   OXT HXT  sing N N 116 
ASN   N   CA   sing N N 117 
ASN   N   H    sing N N 118 
ASN   N   H2   sing N N 119 
ASN   CA  C    sing N N 120 
ASN   CA  CB   sing N N 121 
ASN   CA  HA   sing N N 122 
ASN   C   O    doub N N 123 
ASN   C   OXT  sing N N 124 
ASN   CB  CG   sing N N 125 
ASN   CB  HB2  sing N N 126 
ASN   CB  HB3  sing N N 127 
ASN   CG  OD1  doub N N 128 
ASN   CG  ND2  sing N N 129 
ASN   ND2 HD21 sing N N 130 
ASN   ND2 HD22 sing N N 131 
ASN   OXT HXT  sing N N 132 
ASP   N   CA   sing N N 133 
ASP   N   H    sing N N 134 
ASP   N   H2   sing N N 135 
ASP   CA  C    sing N N 136 
ASP   CA  CB   sing N N 137 
ASP   CA  HA   sing N N 138 
ASP   C   O    doub N N 139 
ASP   C   OXT  sing N N 140 
ASP   CB  CG   sing N N 141 
ASP   CB  HB2  sing N N 142 
ASP   CB  HB3  sing N N 143 
ASP   CG  OD1  doub N N 144 
ASP   CG  OD2  sing N N 145 
ASP   OD2 HD2  sing N N 146 
ASP   OXT HXT  sing N N 147 
CYS   N   CA   sing N N 148 
CYS   N   H    sing N N 149 
CYS   N   H2   sing N N 150 
CYS   CA  C    sing N N 151 
CYS   CA  CB   sing N N 152 
CYS   CA  HA   sing N N 153 
CYS   C   O    doub N N 154 
CYS   C   OXT  sing N N 155 
CYS   CB  SG   sing N N 156 
CYS   CB  HB2  sing N N 157 
CYS   CB  HB3  sing N N 158 
CYS   SG  HG   sing N N 159 
CYS   OXT HXT  sing N N 160 
GLN   N   CA   sing N N 161 
GLN   N   H    sing N N 162 
GLN   N   H2   sing N N 163 
GLN   CA  C    sing N N 164 
GLN   CA  CB   sing N N 165 
GLN   CA  HA   sing N N 166 
GLN   C   O    doub N N 167 
GLN   C   OXT  sing N N 168 
GLN   CB  CG   sing N N 169 
GLN   CB  HB2  sing N N 170 
GLN   CB  HB3  sing N N 171 
GLN   CG  CD   sing N N 172 
GLN   CG  HG2  sing N N 173 
GLN   CG  HG3  sing N N 174 
GLN   CD  OE1  doub N N 175 
GLN   CD  NE2  sing N N 176 
GLN   NE2 HE21 sing N N 177 
GLN   NE2 HE22 sing N N 178 
GLN   OXT HXT  sing N N 179 
GLU   N   CA   sing N N 180 
GLU   N   H    sing N N 181 
GLU   N   H2   sing N N 182 
GLU   CA  C    sing N N 183 
GLU   CA  CB   sing N N 184 
GLU   CA  HA   sing N N 185 
GLU   C   O    doub N N 186 
GLU   C   OXT  sing N N 187 
GLU   CB  CG   sing N N 188 
GLU   CB  HB2  sing N N 189 
GLU   CB  HB3  sing N N 190 
GLU   CG  CD   sing N N 191 
GLU   CG  HG2  sing N N 192 
GLU   CG  HG3  sing N N 193 
GLU   CD  OE1  doub N N 194 
GLU   CD  OE2  sing N N 195 
GLU   OE2 HE2  sing N N 196 
GLU   OXT HXT  sing N N 197 
GLY   N   CA   sing N N 198 
GLY   N   H    sing N N 199 
GLY   N   H2   sing N N 200 
GLY   CA  C    sing N N 201 
GLY   CA  HA2  sing N N 202 
GLY   CA  HA3  sing N N 203 
GLY   C   O    doub N N 204 
GLY   C   OXT  sing N N 205 
GLY   OXT HXT  sing N N 206 
HIS   N   CA   sing N N 207 
HIS   N   H    sing N N 208 
HIS   N   H2   sing N N 209 
HIS   CA  C    sing N N 210 
HIS   CA  CB   sing N N 211 
HIS   CA  HA   sing N N 212 
HIS   C   O    doub N N 213 
HIS   C   OXT  sing N N 214 
HIS   CB  CG   sing N N 215 
HIS   CB  HB2  sing N N 216 
HIS   CB  HB3  sing N N 217 
HIS   CG  ND1  sing Y N 218 
HIS   CG  CD2  doub Y N 219 
HIS   ND1 CE1  doub Y N 220 
HIS   ND1 HD1  sing N N 221 
HIS   CD2 NE2  sing Y N 222 
HIS   CD2 HD2  sing N N 223 
HIS   CE1 NE2  sing Y N 224 
HIS   CE1 HE1  sing N N 225 
HIS   NE2 HE2  sing N N 226 
HIS   OXT HXT  sing N N 227 
HOH   O   H1   sing N N 228 
HOH   O   H2   sing N N 229 
ILE   N   CA   sing N N 230 
ILE   N   H    sing N N 231 
ILE   N   H2   sing N N 232 
ILE   CA  C    sing N N 233 
ILE   CA  CB   sing N N 234 
ILE   CA  HA   sing N N 235 
ILE   C   O    doub N N 236 
ILE   C   OXT  sing N N 237 
ILE   CB  CG1  sing N N 238 
ILE   CB  CG2  sing N N 239 
ILE   CB  HB   sing N N 240 
ILE   CG1 CD1  sing N N 241 
ILE   CG1 HG12 sing N N 242 
ILE   CG1 HG13 sing N N 243 
ILE   CG2 HG21 sing N N 244 
ILE   CG2 HG22 sing N N 245 
ILE   CG2 HG23 sing N N 246 
ILE   CD1 HD11 sing N N 247 
ILE   CD1 HD12 sing N N 248 
ILE   CD1 HD13 sing N N 249 
ILE   OXT HXT  sing N N 250 
LEU   N   CA   sing N N 251 
LEU   N   H    sing N N 252 
LEU   N   H2   sing N N 253 
LEU   CA  C    sing N N 254 
LEU   CA  CB   sing N N 255 
LEU   CA  HA   sing N N 256 
LEU   C   O    doub N N 257 
LEU   C   OXT  sing N N 258 
LEU   CB  CG   sing N N 259 
LEU   CB  HB2  sing N N 260 
LEU   CB  HB3  sing N N 261 
LEU   CG  CD1  sing N N 262 
LEU   CG  CD2  sing N N 263 
LEU   CG  HG   sing N N 264 
LEU   CD1 HD11 sing N N 265 
LEU   CD1 HD12 sing N N 266 
LEU   CD1 HD13 sing N N 267 
LEU   CD2 HD21 sing N N 268 
LEU   CD2 HD22 sing N N 269 
LEU   CD2 HD23 sing N N 270 
LEU   OXT HXT  sing N N 271 
LYS   N   CA   sing N N 272 
LYS   N   H    sing N N 273 
LYS   N   H2   sing N N 274 
LYS   CA  C    sing N N 275 
LYS   CA  CB   sing N N 276 
LYS   CA  HA   sing N N 277 
LYS   C   O    doub N N 278 
LYS   C   OXT  sing N N 279 
LYS   CB  CG   sing N N 280 
LYS   CB  HB2  sing N N 281 
LYS   CB  HB3  sing N N 282 
LYS   CG  CD   sing N N 283 
LYS   CG  HG2  sing N N 284 
LYS   CG  HG3  sing N N 285 
LYS   CD  CE   sing N N 286 
LYS   CD  HD2  sing N N 287 
LYS   CD  HD3  sing N N 288 
LYS   CE  NZ   sing N N 289 
LYS   CE  HE2  sing N N 290 
LYS   CE  HE3  sing N N 291 
LYS   NZ  HZ1  sing N N 292 
LYS   NZ  HZ2  sing N N 293 
LYS   NZ  HZ3  sing N N 294 
LYS   OXT HXT  sing N N 295 
MET   N   CA   sing N N 296 
MET   N   H    sing N N 297 
MET   N   H2   sing N N 298 
MET   CA  C    sing N N 299 
MET   CA  CB   sing N N 300 
MET   CA  HA   sing N N 301 
MET   C   O    doub N N 302 
MET   C   OXT  sing N N 303 
MET   CB  CG   sing N N 304 
MET   CB  HB2  sing N N 305 
MET   CB  HB3  sing N N 306 
MET   CG  SD   sing N N 307 
MET   CG  HG2  sing N N 308 
MET   CG  HG3  sing N N 309 
MET   SD  CE   sing N N 310 
MET   CE  HE1  sing N N 311 
MET   CE  HE2  sing N N 312 
MET   CE  HE3  sing N N 313 
MET   OXT HXT  sing N N 314 
PHE   N   CA   sing N N 315 
PHE   N   H    sing N N 316 
PHE   N   H2   sing N N 317 
PHE   CA  C    sing N N 318 
PHE   CA  CB   sing N N 319 
PHE   CA  HA   sing N N 320 
PHE   C   O    doub N N 321 
PHE   C   OXT  sing N N 322 
PHE   CB  CG   sing N N 323 
PHE   CB  HB2  sing N N 324 
PHE   CB  HB3  sing N N 325 
PHE   CG  CD1  doub Y N 326 
PHE   CG  CD2  sing Y N 327 
PHE   CD1 CE1  sing Y N 328 
PHE   CD1 HD1  sing N N 329 
PHE   CD2 CE2  doub Y N 330 
PHE   CD2 HD2  sing N N 331 
PHE   CE1 CZ   doub Y N 332 
PHE   CE1 HE1  sing N N 333 
PHE   CE2 CZ   sing Y N 334 
PHE   CE2 HE2  sing N N 335 
PHE   CZ  HZ   sing N N 336 
PHE   OXT HXT  sing N N 337 
PRO   N   CA   sing N N 338 
PRO   N   CD   sing N N 339 
PRO   N   H    sing N N 340 
PRO   CA  C    sing N N 341 
PRO   CA  CB   sing N N 342 
PRO   CA  HA   sing N N 343 
PRO   C   O    doub N N 344 
PRO   C   OXT  sing N N 345 
PRO   CB  CG   sing N N 346 
PRO   CB  HB2  sing N N 347 
PRO   CB  HB3  sing N N 348 
PRO   CG  CD   sing N N 349 
PRO   CG  HG2  sing N N 350 
PRO   CG  HG3  sing N N 351 
PRO   CD  HD2  sing N N 352 
PRO   CD  HD3  sing N N 353 
PRO   OXT HXT  sing N N 354 
SER   N   CA   sing N N 355 
SER   N   H    sing N N 356 
SER   N   H2   sing N N 357 
SER   CA  C    sing N N 358 
SER   CA  CB   sing N N 359 
SER   CA  HA   sing N N 360 
SER   C   O    doub N N 361 
SER   C   OXT  sing N N 362 
SER   CB  OG   sing N N 363 
SER   CB  HB2  sing N N 364 
SER   CB  HB3  sing N N 365 
SER   OG  HG   sing N N 366 
SER   OXT HXT  sing N N 367 
THR   N   CA   sing N N 368 
THR   N   H    sing N N 369 
THR   N   H2   sing N N 370 
THR   CA  C    sing N N 371 
THR   CA  CB   sing N N 372 
THR   CA  HA   sing N N 373 
THR   C   O    doub N N 374 
THR   C   OXT  sing N N 375 
THR   CB  OG1  sing N N 376 
THR   CB  CG2  sing N N 377 
THR   CB  HB   sing N N 378 
THR   OG1 HG1  sing N N 379 
THR   CG2 HG21 sing N N 380 
THR   CG2 HG22 sing N N 381 
THR   CG2 HG23 sing N N 382 
THR   OXT HXT  sing N N 383 
TRP   N   CA   sing N N 384 
TRP   N   H    sing N N 385 
TRP   N   H2   sing N N 386 
TRP   CA  C    sing N N 387 
TRP   CA  CB   sing N N 388 
TRP   CA  HA   sing N N 389 
TRP   C   O    doub N N 390 
TRP   C   OXT  sing N N 391 
TRP   CB  CG   sing N N 392 
TRP   CB  HB2  sing N N 393 
TRP   CB  HB3  sing N N 394 
TRP   CG  CD1  doub Y N 395 
TRP   CG  CD2  sing Y N 396 
TRP   CD1 NE1  sing Y N 397 
TRP   CD1 HD1  sing N N 398 
TRP   CD2 CE2  doub Y N 399 
TRP   CD2 CE3  sing Y N 400 
TRP   NE1 CE2  sing Y N 401 
TRP   NE1 HE1  sing N N 402 
TRP   CE2 CZ2  sing Y N 403 
TRP   CE3 CZ3  doub Y N 404 
TRP   CE3 HE3  sing N N 405 
TRP   CZ2 CH2  doub Y N 406 
TRP   CZ2 HZ2  sing N N 407 
TRP   CZ3 CH2  sing Y N 408 
TRP   CZ3 HZ3  sing N N 409 
TRP   CH2 HH2  sing N N 410 
TRP   OXT HXT  sing N N 411 
TYR   N   CA   sing N N 412 
TYR   N   H    sing N N 413 
TYR   N   H2   sing N N 414 
TYR   CA  C    sing N N 415 
TYR   CA  CB   sing N N 416 
TYR   CA  HA   sing N N 417 
TYR   C   O    doub N N 418 
TYR   C   OXT  sing N N 419 
TYR   CB  CG   sing N N 420 
TYR   CB  HB2  sing N N 421 
TYR   CB  HB3  sing N N 422 
TYR   CG  CD1  doub Y N 423 
TYR   CG  CD2  sing Y N 424 
TYR   CD1 CE1  sing Y N 425 
TYR   CD1 HD1  sing N N 426 
TYR   CD2 CE2  doub Y N 427 
TYR   CD2 HD2  sing N N 428 
TYR   CE1 CZ   doub Y N 429 
TYR   CE1 HE1  sing N N 430 
TYR   CE2 CZ   sing Y N 431 
TYR   CE2 HE2  sing N N 432 
TYR   CZ  OH   sing N N 433 
TYR   OH  HH   sing N N 434 
TYR   OXT HXT  sing N N 435 
VAL   N   CA   sing N N 436 
VAL   N   H    sing N N 437 
VAL   N   H2   sing N N 438 
VAL   CA  C    sing N N 439 
VAL   CA  CB   sing N N 440 
VAL   CA  HA   sing N N 441 
VAL   C   O    doub N N 442 
VAL   C   OXT  sing N N 443 
VAL   CB  CG1  sing N N 444 
VAL   CB  CG2  sing N N 445 
VAL   CB  HB   sing N N 446 
VAL   CG1 HG11 sing N N 447 
VAL   CG1 HG12 sing N N 448 
VAL   CG1 HG13 sing N N 449 
VAL   CG2 HG21 sing N N 450 
VAL   CG2 HG22 sing N N 451 
VAL   CG2 HG23 sing N N 452 
VAL   OXT HXT  sing N N 453 
# 
loop_
_pdbx_audit_support.funding_organization 
_pdbx_audit_support.country 
_pdbx_audit_support.grant_number 
_pdbx_audit_support.ordinal 
'National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)' 'United States' R01GM115568 1 
'National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)' 'United States' R01GM128731 2 
'Cancer Prevention and Research Institute of Texas (CPRIT)'                                'United States' RR200030    3 
# 
_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   ? 
_pdbx_initial_refinement_model.details          ? 
# 
_space_group.name_H-M_alt     'C 1 2 1' 
_space_group.name_Hall        'C 2y' 
_space_group.IT_number        5 
_space_group.crystal_system   monoclinic 
_space_group.id               1 
# 
_atom_sites.entry_id                    9BBQ 
_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]   0.008733 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.001837 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.018700 
_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]   0.022521 
_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.
;
? 
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.
;
? 
O1- ? ? 5.12366 3.84317 ? ? 3.49406  27.47979 ? ? 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   ? 112.99680 -20.05289 -16.67858 1.000 52.04532 ?  1   SER   A N   1 
ATOM   2    C CA  . SER   A 1 1   ? 111.94030 -21.02246 -16.39652 1.000 39.89870 ?  1   SER   A CA  1 
ATOM   3    C C   . SER   A 1 1   ? 111.81590 -21.27828 -14.89313 1.000 40.40223 ?  1   SER   A C   1 
ATOM   4    O O   . SER   A 1 1   ? 111.37932 -22.34859 -14.45066 1.000 34.28127 ?  1   SER   A O   1 
ATOM   5    C CB  . SER   A 1 1   ? 112.20844 -22.32804 -17.13859 1.000 40.42709 ?  1   SER   A CB  1 
ATOM   6    O OG  . SER   A 1 1   ? 111.31629 -23.33137 -16.71190 1.000 44.04350 ?  1   SER   A OG  1 
ATOM   7    N N   . GLY   A 1 2   ? 112.21016 -20.28178 -14.10822 1.000 40.85373 ?  2   GLY   A N   1 
ATOM   8    C CA  . GLY   A 1 2   ? 112.09171 -20.36867 -12.67098 1.000 34.32735 ?  2   GLY   A CA  1 
ATOM   9    C C   . GLY   A 1 2   ? 113.40278 -20.72278 -12.00960 1.000 34.96719 ?  2   GLY   A C   1 
ATOM   10   O O   . GLY   A 1 2   ? 114.18890 -21.51154 -12.54245 1.000 34.99863 ?  2   GLY   A O   1 
ATOM   11   N N   . PHE   A 1 3   ? 113.65207 -20.14534 -10.84181 1.000 34.30742 ?  3   PHE   A N   1 
ATOM   12   C CA  . PHE   A 1 3   ? 114.86254 -20.44591 -10.09022 1.000 31.85314 ?  3   PHE   A CA  1 
ATOM   13   C C   . PHE   A 1 3   ? 114.51851 -20.54262 -8.61728  1.000 32.20742 ?  3   PHE   A C   1 
ATOM   14   O O   . PHE   A 1 3   ? 113.98395 -19.59306 -8.03871  1.000 34.46320 ?  3   PHE   A O   1 
ATOM   15   C CB  . PHE   A 1 3   ? 115.94756 -19.39341 -10.33536 1.000 31.78791 ?  3   PHE   A CB  1 
ATOM   16   C CG  . PHE   A 1 3   ? 117.32967 -19.90423 -10.08045 1.000 32.76179 ?  3   PHE   A CG  1 
ATOM   17   C CD1 . PHE   A 1 3   ? 117.97096 -20.70656 -11.01342 1.000 34.04168 ?  3   PHE   A CD1 1 
ATOM   18   C CD2 . PHE   A 1 3   ? 117.98618 -19.58448 -8.90692  1.000 30.00949 ?  3   PHE   A CD2 1 
ATOM   19   C CE1 . PHE   A 1 3   ? 119.24590 -21.18905 -10.77776 1.000 31.66170 ?  3   PHE   A CE1 1 
ATOM   20   C CE2 . PHE   A 1 3   ? 119.25994 -20.05828 -8.66153  1.000 30.76906 ?  3   PHE   A CE2 1 
ATOM   21   C CZ  . PHE   A 1 3   ? 119.88956 -20.86541 -9.59804  1.000 31.88775 ?  3   PHE   A CZ  1 
ATOM   22   N N   . ARG   A 1 4   ? 114.82922 -21.69089 -8.01846  1.000 30.74112 ?  4   ARG   A N   1 
ATOM   23   C CA  . ARG   A 1 4   ? 114.49631 -21.98666 -6.63716  1.000 27.65577 ?  4   ARG   A CA  1 
ATOM   24   C C   . ARG   A 1 4   ? 115.71114 -22.52092 -5.89678  1.000 24.96694 ?  4   ARG   A C   1 
ATOM   25   O O   . ARG   A 1 4   ? 116.57204 -23.18719 -6.47658  1.000 24.94370 ?  4   ARG   A O   1 
ATOM   26   C CB  . ARG   A 1 4   ? 113.36314 -23.02039 -6.54011  1.000 28.01017 ?  4   ARG   A CB  1 
ATOM   27   C CG  . ARG   A 1 4   ? 112.17748 -22.68939 -7.38889  1.000 30.41603 ?  4   ARG   A CG  1 
ATOM   28   C CD  . ARG   A 1 4   ? 111.33563 -21.66439 -6.67341  1.000 35.80012 ?  4   ARG   A CD  1 
ATOM   29   N NE  . ARG   A 1 4   ? 111.53684 -21.76250 -5.23540  1.000 31.81249 ?  4   ARG   A NE  1 
ATOM   30   C CZ  . ARG   A 1 4   ? 110.62599 -22.23084 -4.39533  1.000 37.33921 ?  4   ARG   A CZ  1 
ATOM   31   N NH1 . ARG   A 1 4   ? 109.41528 -22.56258 -4.81133  1.000 34.84097 ?  4   ARG   A NH1 1 
ATOM   32   N NH2 . ARG   A 1 4   ? 110.94325 -22.38185 -3.10848  1.000 35.08055 ?  4   ARG   A NH2 1 
ATOM   33   N N   . LYS   A 1 5   ? 115.76389 -22.23253 -4.60262  1.000 23.75232 ?  5   LYS   A N   1 
ATOM   34   C CA  . LYS   A 1 5   ? 116.75222 -22.87421 -3.74517  1.000 26.66410 ?  5   LYS   A CA  1 
ATOM   35   C C   . LYS   A 1 5   ? 116.36355 -24.33906 -3.61734  1.000 25.88930 ?  5   LYS   A C   1 
ATOM   36   O O   . LYS   A 1 5   ? 115.30406 -24.66160 -3.07448  1.000 29.49192 ?  5   LYS   A O   1 
ATOM   37   C CB  . LYS   A 1 5   ? 116.80948 -22.19742 -2.38074  1.000 29.52528 ?  5   LYS   A CB  1 
ATOM   38   C CG  . LYS   A 1 5   ? 118.13034 -22.38543 -1.66548  1.000 30.30708 ?  5   LYS   A CG  1 
ATOM   39   C CD  . LYS   A 1 5   ? 118.27721 -21.44369 -0.47145  1.000 34.58592 ?  5   LYS   A CD  1 
ATOM   40   C CE  . LYS   A 1 5   ? 118.89899 -20.11760 -0.85480  1.000 37.55469 ?  5   LYS   A CE  1 
ATOM   41   N NZ  . LYS   A 1 5   ? 119.94464 -20.31321 -1.88570  1.000 40.21727 ?  5   LYS   A NZ  1 
ATOM   42   N N   . MET   A 1 6   ? 117.17970 -25.22815 -4.16400  1.000 22.75122 ?  6   MET   A N   1 
ATOM   43   C CA  . MET   A 1 6   ? 116.77459 -26.61454 -4.30837  1.000 23.34222 ?  6   MET   A CA  1 
ATOM   44   C C   . MET   A 1 6   ? 117.79795 -27.52666 -3.65439  1.000 24.28002 ?  6   MET   A C   1 
ATOM   45   O O   . MET   A 1 6   ? 119.00474 -27.35707 -3.84340  1.000 25.05957 ?  6   MET   A O   1 
ATOM   46   C CB  . MET   A 1 6   ? 116.55791 -26.92261 -5.79154  1.000 25.84514 ?  6   MET   A CB  1 
ATOM   47   C CG  . MET   A 1 6   ? 116.63228 -28.34799 -6.22257  1.000 26.37663 ?  6   MET   A CG  1 
ATOM   48   S SD  . MET   A 1 6   ? 116.21829 -28.41947 -7.99263  1.000 38.42095 ?  6   MET   A SD  1 
ATOM   49   C CE  . MET   A 1 6   ? 115.37535 -26.86324 -8.22778  1.000 33.04356 ?  6   MET   A CE  1 
ATOM   50   N N   . ALA   A 1 7   ? 117.30593 -28.46849 -2.86462  1.000 19.29276 ?  7   ALA   A N   1 
ATOM   51   C CA  . ALA   A 1 7   ? 118.13044 -29.43900 -2.16655  1.000 21.20857 ?  7   ALA   A CA  1 
ATOM   52   C C   . ALA   A 1 7   ? 118.20283 -30.73114 -2.96556  1.000 22.57564 ?  7   ALA   A C   1 
ATOM   53   O O   . ALA   A 1 7   ? 117.35403 -31.01225 -3.81027  1.000 22.63688 ?  7   ALA   A O   1 
ATOM   54   C CB  . ALA   A 1 7   ? 117.55879 -29.71315 -0.78198  1.000 20.43773 ?  7   ALA   A CB  1 
ATOM   55   N N   . PHE   A 1 8   ? 119.22650 -31.52684 -2.68663  1.000 19.62044 ?  8   PHE   A N   1 
ATOM   56   C CA  . PHE   A 1 8   ? 119.30242 -32.83311 -3.31484  1.000 24.03073 ?  8   PHE   A CA  1 
ATOM   57   C C   . PHE   A 1 8   ? 118.19316 -33.73288 -2.78571  1.000 22.69131 ?  8   PHE   A C   1 
ATOM   58   O O   . PHE   A 1 8   ? 117.75629 -33.58345 -1.64033  1.000 22.13930 ?  8   PHE   A O   1 
ATOM   59   C CB  . PHE   A 1 8   ? 120.65075 -33.48492 -3.04854  1.000 22.69612 ?  8   PHE   A CB  1 
ATOM   60   C CG  . PHE   A 1 8   ? 121.78553 -32.83452 -3.76574  1.000 24.70044 ?  8   PHE   A CG  1 
ATOM   61   C CD1 . PHE   A 1 8   ? 122.03426 -33.11308 -5.09797  1.000 31.47572 ?  8   PHE   A CD1 1 
ATOM   62   C CD2 . PHE   A 1 8   ? 122.62573 -31.96065 -3.10188  1.000 26.08867 ?  8   PHE   A CD2 1 
ATOM   63   C CE1 . PHE   A 1 8   ? 123.08729 -32.51675 -5.75025  1.000 30.94113 ?  8   PHE   A CE1 1 
ATOM   64   C CE2 . PHE   A 1 8   ? 123.68302 -31.36959 -3.75683  1.000 28.87034 ?  8   PHE   A CE2 1 
ATOM   65   C CZ  . PHE   A 1 8   ? 123.91120 -31.64773 -5.08174  1.000 30.15170 ?  8   PHE   A CZ  1 
ATOM   66   N N   . PRO   A 1 9   ? 117.71701 -34.67949 -3.59452  1.000 21.79536 ?  9   PRO   A N   1 
ATOM   67   C CA  . PRO   A 1 9   ? 116.79760 -35.68928 -3.06654  1.000 24.26426 ?  9   PRO   A CA  1 
ATOM   68   C C   . PRO   A 1 9   ? 117.47028 -36.40921 -1.90486  1.000 23.29370 ?  9   PRO   A C   1 
ATOM   69   O O   . PRO   A 1 9   ? 118.63776 -36.78760 -1.98609  1.000 25.28574 ?  9   PRO   A O   1 
ATOM   70   C CB  . PRO   A 1 9   ? 116.55442 -36.61730 -4.25994  1.000 24.79160 ?  9   PRO   A CB  1 
ATOM   71   C CG  . PRO   A 1 9   ? 116.94011 -35.79601 -5.47704  1.000 28.86562 ?  9   PRO   A CG  1 
ATOM   72   C CD  . PRO   A 1 9   ? 118.07461 -34.93143 -5.00049  1.000 24.76036 ?  9   PRO   A CD  1 
ATOM   73   N N   . SER   A 1 10  ? 116.72897 -36.58392 -0.81897  1.000 23.31373 ?  10  SER   A N   1 
ATOM   74   C CA  . SER   A 1 10  ? 117.31797 -37.00257 0.44539   1.000 25.70657 ?  10  SER   A CA  1 
ATOM   75   C C   . SER   A 1 10  ? 117.17802 -38.49648 0.71084   1.000 24.31385 ?  10  SER   A C   1 
ATOM   76   O O   . SER   A 1 10  ? 117.58652 -38.95959 1.77870   1.000 25.75462 ?  10  SER   A O   1 
ATOM   77   C CB  . SER   A 1 10  ? 116.69340 -36.20065 1.58975   1.000 21.97385 ?  10  SER   A CB  1 
ATOM   78   O OG  . SER   A 1 10  ? 115.31040 -36.48679 1.72045   1.000 25.14713 ?  10  SER   A OG  1 
ATOM   79   N N   . GLY   A 1 11  ? 116.62546 -39.26004 -0.23683  1.000 25.37883 ?  11  GLY   A N   1 
ATOM   80   C CA  . GLY   A 1 11  ? 116.30638 -40.65534 0.03591   1.000 26.06781 ?  11  GLY   A CA  1 
ATOM   81   C C   . GLY   A 1 11  ? 117.49880 -41.48707 0.48043   1.000 26.34863 ?  11  GLY   A C   1 
ATOM   82   O O   . GLY   A 1 11  ? 117.39757 -42.27540 1.42641   1.000 28.88928 ?  11  GLY   A O   1 
ATOM   83   N N   . LYS   A 1 12  ? 118.63415 -41.34962 -0.21070  1.000 24.71960 ?  12  LYS   A N   1 
ATOM   84   C CA  . LYS   A 1 12  ? 119.79806 -42.15986 0.13190   1.000 24.32740 ?  12  LYS   A CA  1 
ATOM   85   C C   . LYS   A 1 12  ? 120.30300 -41.85612 1.53639   1.000 25.87590 ?  12  LYS   A C   1 
ATOM   86   O O   . LYS   A 1 12  ? 120.82222 -42.75201 2.20710   1.000 27.72685 ?  12  LYS   A O   1 
ATOM   87   C CB  . LYS   A 1 12  ? 120.91875 -41.95514 -0.89001  1.000 26.75581 ?  12  LYS   A CB  1 
ATOM   88   C CG  . LYS   A 1 12  ? 120.52329 -42.30027 -2.33427  1.000 32.43909 ?  12  LYS   A CG  1 
ATOM   89   C CD  . LYS   A 1 12  ? 121.42678 -41.61226 -3.34306  1.000 35.66231 ?  12  LYS   A CD  1 
ATOM   90   C CE  . LYS   A 1 12  ? 121.16363 -42.10377 -4.75455  1.000 45.36328 ?  12  LYS   A CE  1 
ATOM   91   N NZ  . LYS   A 1 12  ? 121.96614 -43.31173 -5.07362  1.000 47.24429 ?  12  LYS   A NZ  1 
ATOM   92   N N   . VAL   A 1 13  ? 120.15434 -40.61144 1.99753   1.000 23.30688 ?  13  VAL   A N   1 
ATOM   93   C CA  . VAL   A 1 13  ? 120.61843 -40.24879 3.33138   1.000 22.16186 ?  13  VAL   A CA  1 
ATOM   94   C C   . VAL   A 1 13  ? 119.61139 -40.67736 4.38751   1.000 24.64941 ?  13  VAL   A C   1 
ATOM   95   O O   . VAL   A 1 13  ? 120.00334 -41.07249 5.49076   1.000 20.84363 ?  13  VAL   A O   1 
ATOM   96   C CB  . VAL   A 1 13  ? 120.90554 -38.74166 3.42825   1.000 20.57002 ?  13  VAL   A CB  1 
ATOM   97   C CG1 . VAL   A 1 13  ? 121.34149 -38.36585 4.86825   1.000 23.14633 ?  13  VAL   A CG1 1 
ATOM   98   C CG2 . VAL   A 1 13  ? 121.96863 -38.32838 2.42698   1.000 23.44345 ?  13  VAL   A CG2 1 
ATOM   99   N N   . GLU   A 1 14  ? 118.31099 -40.61586 4.07435   1.000 22.08182 ?  14  GLU   A N   1 
ATOM   100  C CA  . GLU   A 1 14  ? 117.28688 -41.05163 5.02394   1.000 22.34138 ?  14  GLU   A CA  1 
ATOM   101  C C   . GLU   A 1 14  ? 117.56681 -42.45940 5.52439   1.000 25.39157 ?  14  GLU   A C   1 
ATOM   102  O O   . GLU   A 1 14  ? 117.39853 -42.74858 6.71316   1.000 26.19446 ?  14  GLU   A O   1 
ATOM   103  C CB  . GLU   A 1 14  ? 115.89872 -40.99008 4.37570   1.000 25.41645 ?  14  GLU   A CB  1 
ATOM   104  C CG  . GLU   A 1 14  ? 115.46348 -39.57677 4.01226   1.000 25.31878 ?  14  GLU   A CG  1 
ATOM   105  C CD  . GLU   A 1 14  ? 114.15864 -39.52357 3.22400   1.000 24.66225 ?  14  GLU   A CD  1 
ATOM   106  O OE1 . GLU   A 1 14  ? 113.23729 -40.30194 3.49648   1.000 28.24764 ?  14  GLU   A OE1 1 
ATOM   107  O OE2 . GLU   A 1 14  ? 114.08124 -38.69634 2.30074   1.000 29.13708 -1 14  GLU   A OE2 1 
ATOM   108  N N   . GLY   A 1 15  ? 118.01388 -43.34358 4.63469   1.000 25.98010 ?  15  GLY   A N   1 
ATOM   109  C CA  . GLY   A 1 15  ? 118.27854 -44.72274 5.00790   1.000 26.83670 ?  15  GLY   A CA  1 
ATOM   110  C C   . GLY   A 1 15  ? 119.47478 -44.93834 5.91321   1.000 24.45886 ?  15  GLY   A C   1 
ATOM   111  O O   . GLY   A 1 15  ? 119.73714 -46.08496 6.28647   1.000 26.36250 ?  15  GLY   A O   1 
ATOM   112  N N   . CYS   A 1 16  ? 120.19670 -43.87942 6.26762   1.000 22.54893 ?  16  CYS   A N   1 
ATOM   113  C CA  . CYS   A 1 16  ? 121.39747 -43.96442 7.09461   1.000 23.51317 ?  16  CYS   A CA  1 
ATOM   114  C C   . CYS   A 1 16  ? 121.23159 -43.29324 8.44912   1.000 24.42798 ?  16  CYS   A C   1 
ATOM   115  O O   . CYS   A 1 16  ? 122.19153 -43.24086 9.22340   1.000 24.37154 ?  16  CYS   A O   1 
ATOM   116  C CB  . CYS   A 1 16  ? 122.57917 -43.31288 6.37560   1.000 22.69265 ?  16  CYS   A CB  1 
ATOM   117  S SG  . CYS   A 1 16  ? 122.94855 -43.97636 4.73477   1.000 26.94305 ?  16  CYS   A SG  1 
ATOM   118  N N   . MET   A 1 17  ? 120.06266 -42.74335 8.73660   1.000 23.92776 ?  17  MET   A N   1 
ATOM   119  C CA  . MET   A 1 17  ? 119.83315 -41.99430 9.96416   1.000 24.43387 ?  17  MET   A CA  1 
ATOM   120  C C   . MET   A 1 17  ? 119.40701 -42.96146 11.05648  1.000 26.28928 ?  17  MET   A C   1 
ATOM   121  O O   . MET   A 1 17  ? 118.47591 -43.74567 10.86143  1.000 26.62244 ?  17  MET   A O   1 
ATOM   122  C CB  . MET   A 1 17  ? 118.75563 -40.94024 9.71802   1.000 25.74529 ?  17  MET   A CB  1 
ATOM   123  C CG  . MET   A 1 17  ? 119.21505 -39.66755 8.98780   1.000 25.47426 ?  17  MET   A CG  1 
ATOM   124  S SD  . MET   A 1 17  ? 120.96284 -39.20283 8.99786   1.000 24.00535 ?  17  MET   A SD  1 
ATOM   125  C CE  . MET   A 1 17  ? 121.19964 -38.83748 10.74874  1.000 25.25660 ?  17  MET   A CE  1 
ATOM   126  N N   . VAL   A 1 18  ? 120.11182 -42.93005 12.18736  1.000 24.23583 ?  18  VAL   A N   1 
ATOM   127  C CA  . VAL   A 1 18  ? 119.77371 -43.73650 13.34953  1.000 25.91882 ?  18  VAL   A CA  1 
ATOM   128  C C   . VAL   A 1 18  ? 119.74635 -42.83569 14.57602  1.000 23.37728 ?  18  VAL   A C   1 
ATOM   129  O O   . VAL   A 1 18  ? 120.16502 -41.67895 14.54521  1.000 23.86196 ?  18  VAL   A O   1 
ATOM   130  C CB  . VAL   A 1 18  ? 120.74623 -44.91652 13.57495  1.000 29.01248 ?  18  VAL   A CB  1 
ATOM   131  C CG1 . VAL   A 1 18  ? 120.71142 -45.87697 12.40209  1.000 29.35552 ?  18  VAL   A CG1 1 
ATOM   132  C CG2 . VAL   A 1 18  ? 122.14732 -44.42232 13.83408  1.000 25.40271 ?  18  VAL   A CG2 1 
ATOM   133  N N   . GLN   A 1 19  ? 119.24017 -43.39298 15.66862  1.000 27.75629 ?  19  GLN   A N   1 
ATOM   134  C CA  . GLN   A 1 19  ? 119.17255 -42.70285 16.94397  1.000 28.66668 ?  19  GLN   A CA  1 
ATOM   135  C C   . GLN   A 1 19  ? 120.24348 -43.26678 17.86405  1.000 26.76458 ?  19  GLN   A C   1 
ATOM   136  O O   . GLN   A 1 19  ? 120.39597 -44.48637 17.96598  1.000 28.98968 ?  19  GLN   A O   1 
ATOM   137  C CB  . GLN   A 1 19  ? 117.78491 -42.86206 17.56105  1.000 31.44185 ?  19  GLN   A CB  1 
ATOM   138  C CG  . GLN   A 1 19  ? 117.67558 -42.35636 18.96789  1.000 33.27393 ?  19  GLN   A CG  1 
ATOM   139  C CD  . GLN   A 1 19  ? 116.40893 -42.82660 19.63830  1.000 38.84152 ?  19  GLN   A CD  1 
ATOM   140  O OE1 . GLN   A 1 19  ? 115.40998 -42.11005 19.65592  1.000 43.43664 ?  19  GLN   A OE1 1 
ATOM   141  N NE2 . GLN   A 1 19  ? 116.43677 -44.03839 20.19275  1.000 42.82242 ?  19  GLN   A NE2 1 
ATOM   142  N N   . VAL   A 1 20  ? 121.01008 -42.38355 18.49892  1.000 26.45843 ?  20  VAL   A N   1 
ATOM   143  C CA  . VAL   A 1 20  ? 122.04834 -42.78209 19.43865  1.000 26.55595 ?  20  VAL   A CA  1 
ATOM   144  C C   . VAL   A 1 20  ? 121.69784 -42.20847 20.79820  1.000 27.97925 ?  20  VAL   A C   1 
ATOM   145  O O   . VAL   A 1 20  ? 121.49716 -40.99697 20.93197  1.000 25.85410 ?  20  VAL   A O   1 
ATOM   146  C CB  . VAL   A 1 20  ? 123.44625 -42.30637 19.00623  1.000 24.21318 ?  20  VAL   A CB  1 
ATOM   147  C CG1 . VAL   A 1 20  ? 124.49889 -42.85698 19.97088  1.000 25.00480 ?  20  VAL   A CG1 1 
ATOM   148  C CG2 . VAL   A 1 20  ? 123.74585 -42.75601 17.58233  1.000 25.50946 ?  20  VAL   A CG2 1 
ATOM   149  N N   . THR   A 1 21  ? 121.63684 -43.07504 21.80151  1.000 26.11161 ?  21  THR   A N   1 
ATOM   150  C CA  . THR   A 1 21  ? 121.34973 -42.67476 23.16681  1.000 30.54436 ?  21  THR   A CA  1 
ATOM   151  C C   . THR   A 1 21  ? 122.51669 -43.09650 24.04526  1.000 30.52650 ?  21  THR   A C   1 
ATOM   152  O O   . THR   A 1 21  ? 122.96970 -44.24479 23.98045  1.000 33.18040 ?  21  THR   A O   1 
ATOM   153  C CB  . THR   A 1 21  ? 120.05284 -43.30783 23.67431  1.000 31.58945 ?  21  THR   A CB  1 
ATOM   154  O OG1 . THR   A 1 21  ? 118.96917 -42.92092 22.82382  1.000 33.21756 ?  21  THR   A OG1 1 
ATOM   155  C CG2 . THR   A 1 21  ? 119.75733 -42.82878 25.07866  1.000 32.81589 ?  21  THR   A CG2 1 
ATOM   156  N N   . CYS   A 1 22  ? 123.00917 -42.16389 24.84629  1.000 28.20273 ?  22  CYS   A N   1 
ATOM   157  C CA  . CYS   A 1 22  ? 123.98359 -42.45650 25.88376  1.000 32.24216 ?  22  CYS   A CA  1 
ATOM   158  C C   . CYS   A 1 22  ? 123.47465 -41.77448 27.14002  1.000 34.55254 ?  22  CYS   A C   1 
ATOM   159  O O   . CYS   A 1 22  ? 123.33245 -40.54710 27.16363  1.000 36.21048 ?  22  CYS   A O   1 
ATOM   160  C CB  . CYS   A 1 22  ? 125.38543 -41.96065 25.49677  1.000 28.43352 ?  22  CYS   A CB  1 
ATOM   161  S SG  . CYS   A 1 22  ? 126.71163 -42.42681 26.65660  1.000 35.64261 ?  22  CYS   A SG  1 
ATOM   162  N N   . GLY   A 1 23  ? 123.15157 -42.56729 28.15248  1.000 38.18645 ?  23  GLY   A N   1 
ATOM   163  C CA  . GLY   A 1 23  ? 122.55294 -42.01422 29.35512  1.000 39.72694 ?  23  GLY   A CA  1 
ATOM   164  C C   . GLY   A 1 23  ? 121.23242 -41.34931 29.02608  1.000 39.49746 ?  23  GLY   A C   1 
ATOM   165  O O   . GLY   A 1 23  ? 120.33381 -41.95284 28.42579  1.000 41.50185 ?  23  GLY   A O   1 
ATOM   166  N N   . THR   A 1 24  ? 121.10481 -40.08100 29.40473  1.000 39.84343 ?  24  THR   A N   1 
ATOM   167  C CA  . THR   A 1 24  ? 119.88377 -39.33670 29.13993  1.000 41.59562 ?  24  THR   A CA  1 
ATOM   168  C C   . THR   A 1 24  ? 119.91111 -38.60850 27.80391  1.000 40.74987 ?  24  THR   A C   1 
ATOM   169  O O   . THR   A 1 24  ? 118.85009 -38.21506 27.30768  1.000 43.41686 ?  24  THR   A O   1 
ATOM   170  C CB  . THR   A 1 24  ? 119.63214 -38.32941 30.26796  1.000 50.02016 ?  24  THR   A CB  1 
ATOM   171  O OG1 . THR   A 1 24  ? 118.37745 -37.67140 30.05632  1.000 62.17774 ?  24  THR   A OG1 1 
ATOM   172  C CG2 . THR   A 1 24  ? 120.74382 -37.29249 30.31816  1.000 51.80252 ?  24  THR   A CG2 1 
ATOM   173  N N   . THR   A 1 25  ? 121.08644 -38.43573 27.20555  1.000 40.61530 ?  25  THR   A N   1 
ATOM   174  C CA  . THR   A 1 25  ? 121.22734 -37.68367 25.96402  1.000 38.01576 ?  25  THR   A CA  1 
ATOM   175  C C   . THR   A 1 25  ? 120.96231 -38.57205 24.75549  1.000 34.34229 ?  25  THR   A C   1 
ATOM   176  O O   . THR   A 1 25  ? 121.52275 -39.66809 24.64103  1.000 33.80985 ?  25  THR   A O   1 
ATOM   177  C CB  . THR   A 1 25  ? 122.62083 -37.06349 25.87414  1.000 35.42429 ?  25  THR   A CB  1 
ATOM   178  O OG1 . THR   A 1 25  ? 123.02102 -36.60574 27.17313  1.000 38.42913 ?  25  THR   A OG1 1 
ATOM   179  C CG2 . THR   A 1 25  ? 122.63861 -35.90619 24.88856  1.000 36.79218 ?  25  THR   A CG2 1 
ATOM   180  N N   . THR   A 1 26  ? 120.09672 -38.09336 23.86661  1.000 33.83684 ?  26  THR   A N   1 
ATOM   181  C CA  . THR   A 1 26  ? 119.77934 -38.75496 22.61083  1.000 31.35465 ?  26  THR   A CA  1 
ATOM   182  C C   . THR   A 1 26  ? 120.06089 -37.77317 21.48366  1.000 29.26475 ?  26  THR   A C   1 
ATOM   183  O O   . THR   A 1 26  ? 119.72445 -36.58953 21.58829  1.000 30.66561 ?  26  THR   A O   1 
ATOM   184  C CB  . THR   A 1 26  ? 118.31261 -39.20949 22.57802  1.000 29.78422 ?  26  THR   A CB  1 
ATOM   185  O OG1 . THR   A 1 26  ? 118.14208 -40.34433 23.44316  1.000 35.30638 ?  26  THR   A OG1 1 
ATOM   186  C CG2 . THR   A 1 26  ? 117.89356 -39.60804 21.17192  1.000 34.15057 ?  26  THR   A CG2 1 
ATOM   187  N N   . LEU   A 1 27  ? 120.70444 -38.24662 20.42473  1.000 25.23371 ?  27  LEU   A N   1 
ATOM   188  C CA  . LEU   A 1 27  ? 120.82162 -37.43634 19.22219  1.000 25.90805 ?  27  LEU   A CA  1 
ATOM   189  C C   . LEU   A 1 27  ? 120.87319 -38.36583 18.01973  1.000 23.77989 ?  27  LEU   A C   1 
ATOM   190  O O   . LEU   A 1 27  ? 120.62482 -39.57349 18.13101  1.000 24.99991 ?  27  LEU   A O   1 
ATOM   191  C CB  . LEU   A 1 27  ? 122.02489 -36.48205 19.29081  1.000 22.32408 ?  27  LEU   A CB  1 
ATOM   192  C CG  . LEU   A 1 27  ? 123.34433 -36.92602 19.91178  1.000 24.47977 ?  27  LEU   A CG  1 
ATOM   193  C CD1 . LEU   A 1 27  ? 123.94726 -38.06280 19.12523  1.000 24.75337 ?  27  LEU   A CD1 1 
ATOM   194  C CD2 . LEU   A 1 27  ? 124.31604 -35.74850 20.03137  1.000 20.90064 ?  27  LEU   A CD2 1 
ATOM   195  N N   . ASN   A 1 28  ? 121.19699 -37.78761 16.86846  1.000 20.80186 ?  28  ASN   A N   1 
ATOM   196  C CA  . ASN   A 1 28  ? 121.18641 -38.50727 15.60589  1.000 22.97877 ?  28  ASN   A CA  1 
ATOM   197  C C   . ASN   A 1 28  ? 122.57459 -39.02437 15.27552  1.000 24.77107 ?  28  ASN   A C   1 
ATOM   198  O O   . ASN   A 1 28  ? 123.58943 -38.39462 15.58571  1.000 22.32687 ?  28  ASN   A O   1 
ATOM   199  C CB  . ASN   A 1 28  ? 120.68174 -37.61785 14.46998  1.000 23.34613 ?  28  ASN   A CB  1 
ATOM   200  C CG  . ASN   A 1 28  ? 119.37026 -36.93932 14.80136  1.000 25.61862 ?  28  ASN   A CG  1 
ATOM   201  O OD1 . ASN   A 1 28  ? 118.31854 -37.57655 14.80105  1.000 26.98664 ?  28  ASN   A OD1 1 
ATOM   202  N ND2 . ASN   A 1 28  ? 119.42051 -35.64354 15.08078  1.000 25.69635 ?  28  ASN   A ND2 1 
ATOM   203  N N   . GLY   A 1 29  ? 122.60513 -40.20008 14.65538  1.000 22.38068 ?  29  GLY   A N   1 
ATOM   204  C CA  . GLY   A 1 29  ? 123.83577 -40.75808 14.16443  1.000 21.60502 ?  29  GLY   A CA  1 
ATOM   205  C C   . GLY   A 1 29  ? 123.67299 -41.16068 12.70118  1.000 21.29510 ?  29  GLY   A C   1 
ATOM   206  O O   . GLY   A 1 29  ? 122.56384 -41.30420 12.20085  1.000 20.57459 ?  29  GLY   A O   1 
ATOM   207  N N   . LEU   A 1 30  ? 124.80901 -41.35178 12.05741  1.000 19.25791 ?  30  LEU   A N   1 
ATOM   208  C CA  . LEU   A 1 30  ? 124.86469 -41.72392 10.64556  1.000 20.18784 ?  30  LEU   A CA  1 
ATOM   209  C C   . LEU   A 1 30  ? 125.43013 -43.13326 10.54518  1.000 21.57080 ?  30  LEU   A C   1 
ATOM   210  O O   . LEU   A 1 30  ? 126.56864 -43.37141 10.95402  1.000 21.57080 ?  30  LEU   A O   1 
ATOM   211  C CB  . LEU   A 1 30  ? 125.72315 -40.72831 9.87241   1.000 19.64498 ?  30  LEU   A CB  1 
ATOM   212  C CG  . LEU   A 1 30  ? 125.88334 -40.95221 8.37632   1.000 21.59080 ?  30  LEU   A CG  1 
ATOM   213  C CD1 . LEU   A 1 30  ? 124.56761 -40.61676 7.69438   1.000 22.79257 ?  30  LEU   A CD1 1 
ATOM   214  C CD2 . LEU   A 1 30  ? 127.00697 -40.08270 7.84559   1.000 19.86235 ?  30  LEU   A CD2 1 
ATOM   215  N N   . TRP   A 1 31  ? 124.62908 -44.05907 10.01416  1.000 20.52610 ?  31  TRP   A N   1 
ATOM   216  C CA  . TRP   A 1 31  ? 124.95698 -45.48305 9.96158   1.000 20.18656 ?  31  TRP   A CA  1 
ATOM   217  C C   . TRP   A 1 31  ? 125.41372 -45.84545 8.55333   1.000 24.70328 ?  31  TRP   A C   1 
ATOM   218  O O   . TRP   A 1 31  ? 124.60856 -45.87635 7.61823   1.000 25.49945 ?  31  TRP   A O   1 
ATOM   219  C CB  . TRP   A 1 31  ? 123.74750 -46.31770 10.38049  1.000 25.16323 ?  31  TRP   A CB  1 
ATOM   220  C CG  . TRP   A 1 31  ? 123.95442 -47.81090 10.42734  1.000 25.31905 ?  31  TRP   A CG  1 
ATOM   221  C CD1 . TRP   A 1 31  ? 125.13303 -48.48580 10.53969  1.000 27.59102 ?  31  TRP   A CD1 1 
ATOM   222  C CD2 . TRP   A 1 31  ? 122.92826 -48.80448 10.35835  1.000 30.06975 ?  31  TRP   A CD2 1 
ATOM   223  N NE1 . TRP   A 1 31  ? 124.90312 -49.84924 10.54457  1.000 28.47552 ?  31  TRP   A NE1 1 
ATOM   224  C CE2 . TRP   A 1 31  ? 123.55482 -50.06623 10.43657  1.000 29.07432 ?  31  TRP   A CE2 1 
ATOM   225  C CE3 . TRP   A 1 31  ? 121.53769 -48.74868 10.23038  1.000 29.90811 ?  31  TRP   A CE3 1 
ATOM   226  C CZ2 . TRP   A 1 31  ? 122.83757 -51.25764 10.39353  1.000 29.69267 ?  31  TRP   A CZ2 1 
ATOM   227  C CZ3 . TRP   A 1 31  ? 120.82762 -49.93433 10.19418  1.000 32.20119 ?  31  TRP   A CZ3 1 
ATOM   228  C CH2 . TRP   A 1 31  ? 121.47901 -51.17123 10.27292  1.000 32.15009 ?  31  TRP   A CH2 1 
ATOM   229  N N   . LEU   A 1 32  ? 126.70664 -46.10656 8.40460   1.000 25.32561 ?  32  LEU   A N   1 
ATOM   230  C CA  . LEU   A 1 32  ? 127.30499 -46.47095 7.12865   1.000 27.50041 ?  32  LEU   A CA  1 
ATOM   231  C C   . LEU   A 1 32  ? 128.13566 -47.71688 7.35478   1.000 27.66978 ?  32  LEU   A C   1 
ATOM   232  O O   . LEU   A 1 32  ? 128.96927 -47.74086 8.26400   1.000 24.89705 ?  32  LEU   A O   1 
ATOM   233  C CB  . LEU   A 1 32  ? 128.18811 -45.35031 6.58966   1.000 24.77779 ?  32  LEU   A CB  1 
ATOM   234  C CG  . LEU   A 1 32  ? 127.46332 -44.02369 6.38774   1.000 24.70923 ?  32  LEU   A CG  1 
ATOM   235  C CD1 . LEU   A 1 32  ? 128.46405 -42.94540 6.13320   1.000 21.68238 ?  32  LEU   A CD1 1 
ATOM   236  C CD2 . LEU   A 1 32  ? 126.49274 -44.13179 5.21026   1.000 23.35893 ?  32  LEU   A CD2 1 
ATOM   237  N N   . ASP   A 1 33  ? 127.91882 -48.73822 6.53445   1.000 30.82700 ?  33  ASP   A N   1 
ATOM   238  C CA  . ASP   A 1 33  ? 128.60363 -50.01687 6.71062   1.000 30.89722 ?  33  ASP   A CA  1 
ATOM   239  C C   . ASP   A 1 33  ? 128.32900 -50.44916 8.15345   1.000 30.77627 ?  33  ASP   A C   1 
ATOM   240  O O   . ASP   A 1 33  ? 127.18427 -50.31843 8.61023   1.000 29.90276 ?  33  ASP   A O   1 
ATOM   241  C CB  . ASP   A 1 33  ? 130.06743 -49.84086 6.32954   1.000 32.81014 ?  33  ASP   A CB  1 
ATOM   242  C CG  . ASP   A 1 33  ? 130.25335 -49.54242 4.84607   1.000 39.49948 ?  33  ASP   A CG  1 
ATOM   243  O OD1 . ASP   A 1 33  ? 129.45549 -50.03667 4.02125   1.000 37.64648 -1 33  ASP   A OD1 1 
ATOM   244  O OD2 . ASP   A 1 33  ? 131.17907 -48.77063 4.51095   1.000 39.60219 ?  33  ASP   A OD2 1 
ATOM   245  N N   . ASP   A 1 34  ? 129.32700 -50.90793 8.91359   1.000 31.01744 ?  34  ASP   A N   1 
ATOM   246  C CA  . ASP   A 1 34  ? 129.10199 -51.34024 10.28774  1.000 30.88640 ?  34  ASP   A CA  1 
ATOM   247  C C   . ASP   A 1 34  ? 129.57277 -50.30603 11.30819  1.000 29.78496 ?  34  ASP   A C   1 
ATOM   248  O O   . ASP   A 1 34  ? 129.96987 -50.66659 12.42221  1.000 28.13861 ?  34  ASP   A O   1 
ATOM   249  C CB  . ASP   A 1 34  ? 129.76206 -52.70286 10.54063  1.000 31.53723 ?  34  ASP   A CB  1 
ATOM   250  C CG  . ASP   A 1 34  ? 131.29135 -52.67784 10.41561  1.000 36.28840 ?  34  ASP   A CG  1 
ATOM   251  O OD1 . ASP   A 1 34  ? 131.85650 -51.69421 9.89608   1.000 34.88336 ?  34  ASP   A OD1 1 
ATOM   252  O OD2 . ASP   A 1 34  ? 131.93081 -53.68347 10.81005  1.000 37.54438 -1 34  ASP   A OD2 1 
ATOM   253  N N   . VAL   A 1 35  ? 129.51109 -49.01941 10.96026  1.000 28.30687 ?  35  VAL   A N   1 
ATOM   254  C CA  . VAL   A 1 35  ? 129.94402 -47.94100 11.84103  1.000 27.69705 ?  35  VAL   A CA  1 
ATOM   255  C C   . VAL   A 1 35  ? 128.83632 -46.90218 11.92315  1.000 25.02942 ?  35  VAL   A C   1 
ATOM   256  O O   . VAL   A 1 35  ? 128.18574 -46.58929 10.91749  1.000 24.51473 ?  35  VAL   A O   1 
ATOM   257  C CB  . VAL   A 1 35  ? 131.26229 -47.29400 11.35415  1.000 27.69893 ?  35  VAL   A CB  1 
ATOM   258  C CG1 . VAL   A 1 35  ? 131.69531 -46.18226 12.30139  1.000 25.53706 ?  35  VAL   A CG1 1 
ATOM   259  C CG2 . VAL   A 1 35  ? 132.36807 -48.34752 11.23921  1.000 27.99198 ?  35  VAL   A CG2 1 
ATOM   260  N N   . VAL   A 1 36  ? 128.61949 -46.37038 13.12091  1.000 21.11894 ?  36  VAL   A N   1 
ATOM   261  C CA  . VAL   A 1 36  ? 127.67718 -45.28094 13.33531  1.000 21.72122 ?  36  VAL   A CA  1 
ATOM   262  C C   . VAL   A 1 36  ? 128.47372 -44.08172 13.82538  1.000 20.50899 ?  36  VAL   A C   1 
ATOM   263  O O   . VAL   A 1 36  ? 129.25974 -44.20392 14.77368  1.000 21.99957 ?  36  VAL   A O   1 
ATOM   264  C CB  . VAL   A 1 36  ? 126.57748 -45.65971 14.34383  1.000 22.05892 ?  36  VAL   A CB  1 
ATOM   265  C CG1 . VAL   A 1 36  ? 125.76436 -44.42704 14.72595  1.000 22.08487 ?  36  VAL   A CG1 1 
ATOM   266  C CG2 . VAL   A 1 36  ? 125.67610 -46.78919 13.79455  1.000 22.25758 ?  36  VAL   A CG2 1 
ATOM   267  N N   . TYR   A 1 37  ? 128.27564 -42.93360 13.17980  1.000 20.13906 ?  37  TYR   A N   1 
ATOM   268  C CA  . TYR   A 1 37  ? 128.99277 -41.69196 13.46799  1.000 19.27769 ?  37  TYR   A CA  1 
ATOM   269  C C   . TYR   A 1 37  ? 128.05285 -40.71008 14.15103  1.000 19.85308 ?  37  TYR   A C   1 
ATOM   270  O O   . TYR   A 1 37  ? 126.93933 -40.50067 13.67407  1.000 20.01139 ?  37  TYR   A O   1 
ATOM   271  C CB  . TYR   A 1 37  ? 129.51853 -41.06661 12.16913  1.000 21.30246 ?  37  TYR   A CB  1 
ATOM   272  C CG  . TYR   A 1 37  ? 130.37812 -41.99057 11.34191  1.000 21.14669 ?  37  TYR   A CG  1 
ATOM   273  C CD1 . TYR   A 1 37  ? 129.80839 -42.93401 10.49672  1.000 21.88902 ?  37  TYR   A CD1 1 
ATOM   274  C CD2 . TYR   A 1 37  ? 131.76555 -41.91251 11.39757  1.000 22.89024 ?  37  TYR   A CD2 1 
ATOM   275  C CE1 . TYR   A 1 37  ? 130.60137 -43.79043 9.74313   1.000 23.58713 ?  37  TYR   A CE1 1 
ATOM   276  C CE2 . TYR   A 1 37  ? 132.56646 -42.75897 10.63575  1.000 22.68718 ?  37  TYR   A CE2 1 
ATOM   277  C CZ  . TYR   A 1 37  ? 131.97729 -43.69459 9.81690   1.000 24.91455 ?  37  TYR   A CZ  1 
ATOM   278  O OH  . TYR   A 1 37  ? 132.76504 -44.54318 9.06797   1.000 23.71056 ?  37  TYR   A OH  1 
ATOM   279  N N   . CYS   A 1 38  ? 128.49667 -40.07793 15.23825  1.000 19.26231 ?  38  CYS   A N   1 
ATOM   280  C CA  . CYS   A 1 38  ? 127.65212 -39.09429 15.90402  1.000 17.68006 ?  38  CYS   A CA  1 
ATOM   281  C C   . CYS   A 1 38  ? 128.53816 -38.10146 16.65761  1.000 18.36320 ?  38  CYS   A C   1 
ATOM   282  O O   . CYS   A 1 38  ? 129.72766 -38.36071 16.85931  1.000 19.08772 ?  38  CYS   A O   1 
ATOM   283  C CB  . CYS   A 1 38  ? 126.65279 -39.78536 16.84982  1.000 20.39078 ?  38  CYS   A CB  1 
ATOM   284  S SG  . CYS   A 1 38  ? 127.34797 -40.35548 18.40376  1.000 24.09070 ?  38  CYS   A SG  1 
ATOM   285  N N   . PRO   A 1 39  ? 127.99979 -36.94653 17.05964  1.000 16.89794 ?  39  PRO   A N   1 
ATOM   286  C CA  . PRO   A 1 39  ? 128.79714 -36.00357 17.84817  1.000 18.07941 ?  39  PRO   A CA  1 
ATOM   287  C C   . PRO   A 1 39  ? 129.20542 -36.62018 19.17198  1.000 16.93764 ?  39  PRO   A C   1 
ATOM   288  O O   . PRO   A 1 39  ? 128.41471 -37.29300 19.83413  1.000 19.91581 ?  39  PRO   A O   1 
ATOM   289  C CB  . PRO   A 1 39  ? 127.84993 -34.81648 18.06004  1.000 17.77615 ?  39  PRO   A CB  1 
ATOM   290  C CG  . PRO   A 1 39  ? 126.84167 -34.95251 16.96103  1.000 20.36579 ?  39  PRO   A CG  1 
ATOM   291  C CD  . PRO   A 1 39  ? 126.63954 -36.42558 16.84210  1.000 18.50663 ?  39  PRO   A CD  1 
ATOM   292  N N   . ARG   A 1 40  ? 130.44984 -36.37691 19.55985  1.000 17.94622 ?  40  ARG   A N   1 
ATOM   293  C CA  . ARG   A 1 40  ? 130.91757 -36.94910 20.81478  1.000 18.19081 ?  40  ARG   A CA  1 
ATOM   294  C C   . ARG   A 1 40  ? 130.21106 -36.36187 22.03313  1.000 19.66791 ?  40  ARG   A C   1 
ATOM   295  O O   . ARG   A 1 40  ? 130.20641 -36.99785 23.09415  1.000 18.60281 ?  40  ARG   A O   1 
ATOM   296  C CB  . ARG   A 1 40  ? 132.43030 -36.76756 20.93353  1.000 18.50798 ?  40  ARG   A CB  1 
ATOM   297  C CG  . ARG   A 1 40  ? 132.87327 -35.33514 21.17280  1.000 16.91284 ?  40  ARG   A CG  1 
ATOM   298  C CD  . ARG   A 1 40  ? 134.38854 -35.29603 21.32128  1.000 18.00023 ?  40  ARG   A CD  1 
ATOM   299  N NE  . ARG   A 1 40  ? 134.91924 -33.94125 21.39300  1.000 18.30715 ?  40  ARG   A NE  1 
ATOM   300  C CZ  . ARG   A 1 40  ? 136.18163 -33.65167 21.66429  1.000 20.31116 ?  40  ARG   A CZ  1 
ATOM   301  N NH1 . ARG   A 1 40  ? 137.07565 -34.60662 21.87936  1.000 20.62085 ?  40  ARG   A NH1 1 
ATOM   302  N NH2 . ARG   A 1 40  ? 136.54754 -32.37446 21.77208  1.000 19.29929 ?  40  ARG   A NH2 1 
ATOM   303  N N   . HIS   A 1 41  ? 129.59844 -35.18133 21.91657  1.000 17.45646 ?  41  HIS   A N   1 
ATOM   304  C CA  . HIS   A 1 41  ? 128.92760 -34.67824 23.12226  1.000 20.61122 ?  41  HIS   A CA  1 
ATOM   305  C C   . HIS   A 1 41  ? 127.64996 -35.43774 23.47197  1.000 21.07574 ?  41  HIS   A C   1 
ATOM   306  O O   . HIS   A 1 41  ? 126.99293 -35.07982 24.46081  1.000 22.81615 ?  41  HIS   A O   1 
ATOM   307  C CB  . HIS   A 1 41  ? 128.70980 -33.16128 22.99652  1.000 20.74410 ?  41  HIS   A CB  1 
ATOM   308  C CG  . HIS   A 1 41  ? 127.63060 -32.73884 22.03919  1.000 23.27654 ?  41  HIS   A CG  1 
ATOM   309  N ND1 . HIS   A 1 41  ? 126.28332 -32.87831 22.29682  1.000 25.02971 ?  41  HIS   A ND1 1 
ATOM   310  C CD2 . HIS   A 1 41  ? 127.71791 -32.15377 20.82143  1.000 21.88444 ?  41  HIS   A CD2 1 
ATOM   311  C CE1 . HIS   A 1 41  ? 125.58809 -32.39768 21.28203  1.000 22.40140 ?  41  HIS   A CE1 1 
ATOM   312  N NE2 . HIS   A 1 41  ? 126.43592 -31.95508 20.36931  1.000 25.65333 ?  41  HIS   A NE2 1 
ATOM   313  N N   . VAL   A 1 42  ? 127.32971 -36.52138 22.76209  1.000 19.95009 ?  42  VAL   A N   1 
ATOM   314  C CA  . VAL   A 1 42  ? 126.26786 -37.41365 23.21610  1.000 22.62820 ?  42  VAL   A CA  1 
ATOM   315  C C   . VAL   A 1 42  ? 126.58766 -37.95737 24.60889  1.000 24.47906 ?  42  VAL   A C   1 
ATOM   316  O O   . VAL   A 1 42  ? 125.67863 -38.30803 25.37223  1.000 27.33280 ?  42  VAL   A O   1 
ATOM   317  C CB  . VAL   A 1 42  ? 126.06371 -38.55910 22.20722  1.000 20.43874 ?  42  VAL   A CB  1 
ATOM   318  C CG1 . VAL   A 1 42  ? 127.25948 -39.50885 22.22580  1.000 21.26120 ?  42  VAL   A CG1 1 
ATOM   319  C CG2 . VAL   A 1 42  ? 124.75156 -39.30812 22.48288  1.000 25.21445 ?  42  VAL   A CG2 1 
ATOM   320  N N   . ILE   A 1 43  ? 127.87419 -38.02806 24.97231  1.000 22.98298 ?  43  ILE   A N   1 
ATOM   321  C CA  . ILE   A 1 43  ? 128.25426 -38.56791 26.28242  1.000 25.62731 ?  43  ILE   A CA  1 
ATOM   322  C C   . ILE   A 1 43  ? 128.19435 -37.54965 27.40869  1.000 28.25463 ?  43  ILE   A C   1 
ATOM   323  O O   . ILE   A 1 43  ? 128.52053 -37.89270 28.55380  1.000 30.78897 ?  43  ILE   A O   1 
ATOM   324  C CB  . ILE   A 1 43  ? 129.67298 -39.17396 26.24098  1.000 26.30039 ?  43  ILE   A CB  1 
ATOM   325  C CG1 . ILE   A 1 43  ? 130.73358 -38.07537 26.17218  1.000 25.18459 ?  43  ILE   A CG1 1 
ATOM   326  C CG2 . ILE   A 1 43  ? 129.81437 -40.12612 25.06535  1.000 25.15979 ?  43  ILE   A CG2 1 
ATOM   327  C CD1 . ILE   A 1 43  ? 132.16710 -38.60847 26.16002  1.000 26.95734 ?  43  ILE   A CD1 1 
ATOM   328  N N   . CYS   A 1 44  ? 127.76531 -36.32324 27.14214  1.000 26.47538 ?  44  CYS   A N   1 
ATOM   329  C CA  . CYS   A 1 44  ? 127.82693 -35.25374 28.12748  1.000 27.95070 ?  44  CYS   A CA  1 
ATOM   330  C C   . CYS   A 1 44  ? 126.49216 -35.09901 28.84062  1.000 34.43473 ?  44  CYS   A C   1 
ATOM   331  O O   . CYS   A 1 44  ? 125.43414 -35.17544 28.21255  1.000 33.19952 ?  44  CYS   A O   1 
ATOM   332  C CB  . CYS   A 1 44  ? 128.18047 -33.93048 27.45959  1.000 30.77183 ?  44  CYS   A CB  1 
ATOM   333  S SG  . CYS   A 1 44  ? 129.87397 -33.80781 26.93752  1.000 27.41037 ?  44  CYS   A SG  1 
ATOM   334  N N   . THR   A 1 45  ? 126.54356 -34.86132 30.14962  1.000 34.54094 ?  45  THR   A N   1 
ATOM   335  C CA  . THR   A 1 45  ? 125.35641 -34.32991 30.79730  1.000 42.29927 ?  45  THR   A CA  1 
ATOM   336  C C   . THR   A 1 45  ? 125.25345 -32.83047 30.52706  1.000 42.66468 ?  45  THR   A C   1 
ATOM   337  O O   . THR   A 1 45  ? 126.17011 -32.19965 29.99045  1.000 40.04102 ?  45  THR   A O   1 
ATOM   338  C CB  . THR   A 1 45  ? 125.37488 -34.60195 32.29780  1.000 41.08976 ?  45  THR   A CB  1 
ATOM   339  O OG1 . THR   A 1 45  ? 126.41072 -33.82754 32.91584  1.000 42.05748 ?  45  THR   A OG1 1 
ATOM   340  C CG2 . THR   A 1 45  ? 125.61405 -36.08159 32.57442  1.000 43.37222 ?  45  THR   A CG2 1 
ATOM   341  N N   . SER   A 1 46  ? 124.11051 -32.25436 30.89687  1.000 45.01861 ?  46  SER   A N   1 
ATOM   342  C CA  . SER   A 1 46  ? 123.95208 -30.81294 30.74518  1.000 45.87804 ?  46  SER   A CA  1 
ATOM   343  C C   . SER   A 1 46  ? 125.02495 -30.05287 31.52008  1.000 44.40910 ?  46  SER   A C   1 
ATOM   344  O O   . SER   A 1 46  ? 125.49810 -29.00595 31.06044  1.000 41.15056 ?  46  SER   A O   1 
ATOM   345  C CB  . SER   A 1 46  ? 122.54944 -30.39830 31.18828  1.000 48.23561 ?  46  SER   A CB  1 
ATOM   346  O OG  . SER   A 1 46  ? 121.57204 -30.89121 30.28556  1.000 51.11270 ?  46  SER   A OG  1 
ATOM   347  N N   . GLU   A 1 47  ? 125.44852 -30.58446 32.67186  1.000 42.74270 ?  47  GLU   A N   1 
ATOM   348  C CA  . GLU   A 1 47  ? 126.52407 -29.97139 33.44626  1.000 42.81144 ?  47  GLU   A CA  1 
ATOM   349  C C   . GLU   A 1 47  ? 127.89264 -30.16984 32.79440  1.000 39.70227 ?  47  GLU   A C   1 
ATOM   350  O O   . GLU   A 1 47  ? 128.71349 -29.24422 32.78747  1.000 38.42897 ?  47  GLU   A O   1 
ATOM   351  C CB  . GLU   A 1 47  ? 126.52926 -30.53507 34.86627  1.000 42.67457 ?  47  GLU   A CB  1 
ATOM   352  N N   . ASP   A 1 48  ? 128.16212 -31.36978 32.26135  1.000 36.91156 ?  48  ASP   A N   1 
ATOM   353  C CA  . ASP   A 1 48  ? 129.42840 -31.63305 31.57374  1.000 35.14198 ?  48  ASP   A CA  1 
ATOM   354  C C   . ASP   A 1 48  ? 129.71174 -30.61570 30.47608  1.000 32.82131 ?  48  ASP   A C   1 
ATOM   355  O O   . ASP   A 1 48  ? 130.87247 -30.25276 30.25071  1.000 30.90613 ?  48  ASP   A O   1 
ATOM   356  C CB  . ASP   A 1 48  ? 129.41779 -33.03301 30.95493  1.000 33.73055 ?  48  ASP   A CB  1 
ATOM   357  C CG  . ASP   A 1 48  ? 129.44359 -34.14032 31.98710  1.000 36.67179 ?  48  ASP   A CG  1 
ATOM   358  O OD1 . ASP   A 1 48  ? 130.01517 -33.93647 33.08269  1.000 34.22026 ?  48  ASP   A OD1 1 
ATOM   359  O OD2 . ASP   A 1 48  ? 128.87892 -35.21851 31.69506  1.000 39.91159 -1 48  ASP   A OD2 1 
ATOM   360  N N   . MET   A 1 49  ? 128.66699 -30.14206 29.79349  1.000 33.20806 ?  49  MET   A N   1 
ATOM   361  C CA  . MET   A 1 49  ? 128.83229 -29.37068 28.56221  1.000 31.20827 ?  49  MET   A CA  1 
ATOM   362  C C   . MET   A 1 49  ? 129.49600 -28.01723 28.79798  1.000 26.48292 ?  49  MET   A C   1 
ATOM   363  O O   . MET   A 1 49  ? 130.02521 -27.42116 27.85065  1.000 22.13901 ?  49  MET   A O   1 
ATOM   364  C CB  . MET   A 1 49  ? 127.46999 -29.18363 27.89030  1.000 33.52424 ?  49  MET   A CB  1 
ATOM   365  C CG  . MET   A 1 49  ? 126.95388 -30.42137 27.15320  1.000 38.16209 ?  49  MET   A CG  1 
ATOM   366  S SD  . MET   A 1 49  ? 125.27312 -30.22528 26.51320  1.000 62.43226 ?  49  MET   A SD  1 
ATOM   367  C CE  . MET   A 1 49  ? 124.90780 -31.89162 25.93517  1.000 39.85199 ?  49  MET   A CE  1 
ATOM   368  N N   . LEU   A 1 50  ? 129.49201 -27.52419 30.03403  1.000 27.58992 ?  50  LEU   A N   1 
ATOM   369  C CA  . LEU   A 1 50  ? 130.12904 -26.24276 30.31026  1.000 29.61669 ?  50  LEU   A CA  1 
ATOM   370  C C   . LEU   A 1 50  ? 131.64397 -26.32212 30.12101  1.000 31.40956 ?  50  LEU   A C   1 
ATOM   371  O O   . LEU   A 1 50  ? 132.26483 -25.37219 29.62954  1.000 33.23610 ?  50  LEU   A O   1 
ATOM   372  C CB  . LEU   A 1 50  ? 129.77451 -25.78699 31.72654  1.000 30.89993 ?  50  LEU   A CB  1 
ATOM   373  C CG  . LEU   A 1 50  ? 128.26911 -25.74663 32.04271  1.000 35.29955 ?  50  LEU   A CG  1 
ATOM   374  C CD1 . LEU   A 1 50  ? 128.00190 -25.37508 33.50043  1.000 37.12870 ?  50  LEU   A CD1 1 
ATOM   375  C CD2 . LEU   A 1 50  ? 127.51377 -24.80376 31.11203  1.000 32.17093 ?  50  LEU   A CD2 1 
ATOM   376  N N   . ASN   A 1 51  ? 132.25314 -27.45294 30.47623  1.000 30.15027 ?  51  ASN   A N   1 
ATOM   377  C CA  . ASN   A 1 51  ? 133.70334 -27.60127 30.40438  1.000 29.74940 ?  51  ASN   A CA  1 
ATOM   378  C C   . ASN   A 1 51  ? 134.09451 -29.07512 30.31689  1.000 28.08449 ?  51  ASN   A C   1 
ATOM   379  O O   . ASN   A 1 51  ? 134.73111 -29.60058 31.24193  1.000 28.96298 ?  51  ASN   A O   1 
ATOM   380  C CB  . ASN   A 1 51  ? 134.34676 -26.95187 31.63107  1.000 31.67092 ?  51  ASN   A CB  1 
ATOM   381  C CG  . ASN   A 1 51  ? 135.85656 -26.84490 31.51864  1.000 37.27061 ?  51  ASN   A CG  1 
ATOM   382  O OD1 . ASN   A 1 51  ? 136.41590 -26.90573 30.42398  1.000 39.69757 ?  51  ASN   A OD1 1 
ATOM   383  N ND2 . ASN   A 1 51  ? 136.52524 -26.68550 32.66193  1.000 39.35073 ?  51  ASN   A ND2 1 
ATOM   384  N N   . PRO   A 1 52  ? 133.74214 -29.77161 29.23757  1.000 25.07793 ?  52  PRO   A N   1 
ATOM   385  C CA  . PRO   A 1 52  ? 133.93674 -31.22815 29.20060  1.000 25.58464 ?  52  PRO   A CA  1 
ATOM   386  C C   . PRO   A 1 52  ? 135.38409 -31.62998 28.96798  1.000 27.28063 ?  52  PRO   A C   1 
ATOM   387  O O   . PRO   A 1 52  ? 136.10059 -31.02944 28.16632  1.000 27.32089 ?  52  PRO   A O   1 
ATOM   388  C CB  . PRO   A 1 52  ? 133.04949 -31.66954 28.03019  1.000 23.24007 ?  52  PRO   A CB  1 
ATOM   389  C CG  . PRO   A 1 52  ? 132.99196 -30.47101 27.13604  1.000 23.71836 ?  52  PRO   A CG  1 
ATOM   390  C CD  . PRO   A 1 52  ? 133.15393 -29.25393 27.98913  1.000 25.80701 ?  52  PRO   A CD  1 
ATOM   391  N N   . ASN   A 1 53  ? 135.82337 -32.64732 29.70704  1.000 24.54736 ?  53  ASN   A N   1 
ATOM   392  C CA  . ASN   A 1 53  ? 137.04578 -33.37474 29.37545  1.000 23.69588 ?  53  ASN   A CA  1 
ATOM   393  C C   . ASN   A 1 53  ? 136.58261 -34.64545 28.67101  1.000 23.30987 ?  53  ASN   A C   1 
ATOM   394  O O   . ASN   A 1 53  ? 136.19521 -35.61459 29.32387  1.000 25.38566 ?  53  ASN   A O   1 
ATOM   395  C CB  . ASN   A 1 53  ? 137.85674 -33.69634 30.63076  1.000 27.79831 ?  53  ASN   A CB  1 
ATOM   396  C CG  . ASN   A 1 53  ? 139.19520 -34.34339 30.31176  1.000 29.08179 ?  53  ASN   A CG  1 
ATOM   397  O OD1 . ASN   A 1 53  ? 139.29175 -35.23303 29.47141  1.000 30.41202 ?  53  ASN   A OD1 1 
ATOM   398  N ND2 . ASN   A 1 53  ? 140.23878 -33.89078 30.99080  1.000 29.51209 ?  53  ASN   A ND2 1 
ATOM   399  N N   . TYR   A 1 54  ? 136.60269 -34.64369 27.33547  1.000 23.63428 ?  54  TYR   A N   1 
ATOM   400  C CA  . TYR   A 1 54  ? 135.95695 -35.73606 26.61665  1.000 24.72130 ?  54  TYR   A CA  1 
ATOM   401  C C   . TYR   A 1 54  ? 136.68919 -37.05910 26.81386  1.000 24.77515 ?  54  TYR   A C   1 
ATOM   402  O O   . TYR   A 1 54  ? 136.05482 -38.11194 26.92720  1.000 25.85219 ?  54  TYR   A O   1 
ATOM   403  C CB  . TYR   A 1 54  ? 135.84697 -35.38821 25.14025  1.000 20.51987 ?  54  TYR   A CB  1 
ATOM   404  C CG  . TYR   A 1 54  ? 134.71728 -34.42810 24.87199  1.000 19.59378 ?  54  TYR   A CG  1 
ATOM   405  C CD1 . TYR   A 1 54  ? 133.40076 -34.87151 24.83823  1.000 19.77133 ?  54  TYR   A CD1 1 
ATOM   406  C CD2 . TYR   A 1 54  ? 134.96721 -33.07930 24.63949  1.000 22.46032 ?  54  TYR   A CD2 1 
ATOM   407  C CE1 . TYR   A 1 54  ? 132.35756 -33.99116 24.57534  1.000 19.28434 ?  54  TYR   A CE1 1 
ATOM   408  C CE2 . TYR   A 1 54  ? 133.93278 -32.20065 24.37222  1.000 19.96504 ?  54  TYR   A CE2 1 
ATOM   409  C CZ  . TYR   A 1 54  ? 132.63057 -32.66328 24.34497  1.000 18.57348 ?  54  TYR   A CZ  1 
ATOM   410  O OH  . TYR   A 1 54  ? 131.59420 -31.78817 24.08363  1.000 18.30985 ?  54  TYR   A OH  1 
ATOM   411  N N   . GLU   A 1 55  ? 138.01787 -37.02903 26.88063  1.000 26.03399 ?  55  GLU   A N   1 
ATOM   412  C CA  . GLU   A 1 55  ? 138.75181 -38.26725 27.12741  1.000 27.41946 ?  55  GLU   A CA  1 
ATOM   413  C C   . GLU   A 1 55  ? 138.35874 -38.88837 28.46142  1.000 26.87563 ?  55  GLU   A C   1 
ATOM   414  O O   . GLU   A 1 55  ? 138.09908 -40.09532 28.54028  1.000 27.81799 ?  55  GLU   A O   1 
ATOM   415  C CB  . GLU   A 1 55  ? 140.25144 -37.99778 27.05428  1.000 30.87010 ?  55  GLU   A CB  1 
ATOM   416  C CG  . GLU   A 1 55  ? 140.70875 -37.71918 25.62784  1.000 35.36880 ?  55  GLU   A CG  1 
ATOM   417  C CD  . GLU   A 1 55  ? 140.54436 -36.25276 25.22113  1.000 44.92956 ?  55  GLU   A CD  1 
ATOM   418  O OE1 . GLU   A 1 55  ? 140.91642 -35.91984 24.07132  1.000 48.10191 ?  55  GLU   A OE1 1 
ATOM   419  O OE2 . GLU   A 1 55  ? 140.03796 -35.43922 26.03861  1.000 35.18131 -1 55  GLU   A OE2 1 
ATOM   420  N N   . ASP   A 1 56  ? 138.27008 -38.07743 29.51568  1.000 27.68098 ?  56  ASP   A N   1 
ATOM   421  C CA  . ASP   A 1 56  ? 137.88132 -38.60971 30.81886  1.000 30.44834 ?  56  ASP   A CA  1 
ATOM   422  C C   . ASP   A 1 56  ? 136.43011 -39.08344 30.82338  1.000 29.16675 ?  56  ASP   A C   1 
ATOM   423  O O   . ASP   A 1 56  ? 136.09846 -40.08770 31.46415  1.000 31.23804 ?  56  ASP   A O   1 
ATOM   424  C CB  . ASP   A 1 56  ? 138.08194 -37.55096 31.89744  1.000 30.91136 ?  56  ASP   A CB  1 
ATOM   425  C CG  . ASP   A 1 56  ? 139.54505 -37.32122 32.23879  1.000 34.83224 ?  56  ASP   A CG  1 
ATOM   426  O OD1 . ASP   A 1 56  ? 140.41876 -38.05912 31.72781  1.000 34.48149 ?  56  ASP   A OD1 1 
ATOM   427  O OD2 . ASP   A 1 56  ? 139.81515 -36.39268 33.02673  1.000 36.10485 -1 56  ASP   A OD2 1 
ATOM   428  N N   . LEU   A 1 57  ? 135.54033 -38.34426 30.16331  1.000 27.08910 ?  57  LEU   A N   1 
ATOM   429  C CA  . LEU   A 1 57  ? 134.13342 -38.72726 30.15777  1.000 28.59103 ?  57  LEU   A CA  1 
ATOM   430  C C   . LEU   A 1 57  ? 133.91800 -40.02529 29.39607  1.000 29.65899 ?  57  LEU   A C   1 
ATOM   431  O O   . LEU   A 1 57  ? 133.10870 -40.86475 29.80871  1.000 32.00862 ?  57  LEU   A O   1 
ATOM   432  C CB  . LEU   A 1 57  ? 133.28206 -37.60741 29.55899  1.000 25.21639 ?  57  LEU   A CB  1 
ATOM   433  C CG  . LEU   A 1 57  ? 133.25453 -36.26480 30.29429  1.000 28.45905 ?  57  LEU   A CG  1 
ATOM   434  C CD1 . LEU   A 1 57  ? 132.47625 -35.27070 29.46070  1.000 27.07459 ?  57  LEU   A CD1 1 
ATOM   435  C CD2 . LEU   A 1 57  ? 132.61029 -36.42026 31.67418  1.000 29.09987 ?  57  LEU   A CD2 1 
ATOM   436  N N   . LEU   A 1 58  ? 134.63452 -40.20631 28.28248  1.000 28.63072 ?  58  LEU   A N   1 
ATOM   437  C CA  . LEU   A 1 58  ? 134.46345 -41.40296 27.46526  1.000 28.91711 ?  58  LEU   A CA  1 
ATOM   438  C C   . LEU   A 1 58  ? 134.97584 -42.64851 28.17588  1.000 26.49599 ?  58  LEU   A C   1 
ATOM   439  O O   . LEU   A 1 58  ? 134.43816 -43.74020 27.97185  1.000 28.52008 ?  58  LEU   A O   1 
ATOM   440  C CB  . LEU   A 1 58  ? 135.17778 -41.22796 26.12328  1.000 24.94739 ?  58  LEU   A CB  1 
ATOM   441  C CG  . LEU   A 1 58  ? 134.90367 -42.30893 25.07388  1.000 26.14256 ?  58  LEU   A CG  1 
ATOM   442  C CD1 . LEU   A 1 58  ? 133.41341 -42.46517 24.81744  1.000 26.64919 ?  58  LEU   A CD1 1 
ATOM   443  C CD2 . LEU   A 1 58  ? 135.63052 -41.99413 23.77706  1.000 26.26717 ?  58  LEU   A CD2 1 
ATOM   444  N N   . ILE   A 1 59  ? 135.99895 -42.50309 29.01795  1.000 29.81332 ?  59  ILE   A N   1 
ATOM   445  C CA  . ILE   A 1 59  ? 136.57070 -43.65446 29.70761  1.000 30.90109 ?  59  ILE   A CA  1 
ATOM   446  C C   . ILE   A 1 59  ? 135.56786 -44.25845 30.68106  1.000 33.83261 ?  59  ILE   A C   1 
ATOM   447  O O   . ILE   A 1 59  ? 135.63637 -45.45189 31.00374  1.000 35.65830 ?  59  ILE   A O   1 
ATOM   448  C CB  . ILE   A 1 59  ? 137.87774 -43.23005 30.40419  1.000 30.69213 ?  59  ILE   A CB  1 
ATOM   449  C CG1 . ILE   A 1 59  ? 139.00293 -43.19330 29.37440  1.000 30.13223 ?  59  ILE   A CG1 1 
ATOM   450  C CG2 . ILE   A 1 59  ? 138.23149 -44.14845 31.56049  1.000 35.03398 ?  59  ILE   A CG2 1 
ATOM   451  C CD1 . ILE   A 1 59  ? 140.10397 -42.27137 29.72355  1.000 35.41918 ?  59  ILE   A CD1 1 
ATOM   452  N N   . ARG   A 1 60  ? 134.61528 -43.46436 31.15113  1.000 31.59306 ?  60  ARG   A N   1 
ATOM   453  C CA  . ARG   A 1 60  ? 133.56137 -44.00424 31.99707  1.000 34.22293 ?  60  ARG   A CA  1 
ATOM   454  C C   . ARG   A 1 60  ? 132.48373 -44.74317 31.20725  1.000 34.04461 ?  60  ARG   A C   1 
ATOM   455  O O   . ARG   A 1 60  ? 131.58096 -45.32290 31.82324  1.000 35.65033 ?  60  ARG   A O   1 
ATOM   456  C CB  . ARG   A 1 60  ? 132.91929 -42.88923 32.83762  1.000 37.67585 ?  60  ARG   A CB  1 
ATOM   457  C CG  . ARG   A 1 60  ? 133.85248 -42.04036 33.72685  1.000 42.63600 ?  60  ARG   A CG  1 
ATOM   458  C CD  . ARG   A 1 60  ? 135.16512 -42.74423 34.09147  1.000 48.84956 ?  60  ARG   A CD  1 
ATOM   459  N NE  . ARG   A 1 60  ? 135.59338 -42.46705 35.45924  1.000 55.76280 ?  60  ARG   A NE  1 
ATOM   460  C CZ  . ARG   A 1 60  ? 136.51067 -41.57091 35.80119  1.000 60.22112 ?  60  ARG   A CZ  1 
ATOM   461  N NH1 . ARG   A 1 60  ? 137.09453 -40.79844 34.89950  1.000 59.51369 ?  60  ARG   A NH1 1 
ATOM   462  N NH2 . ARG   A 1 60  ? 136.84011 -41.43616 37.08362  1.000 63.49797 ?  60  ARG   A NH2 1 
ATOM   463  N N   . LYS   A 1 61  ? 132.55883 -44.76013 29.87782  1.000 32.63484 ?  61  LYS   A N   1 
ATOM   464  C CA  . LYS   A 1 61  ? 131.54157 -45.39012 29.04950  1.000 34.79628 ?  61  LYS   A CA  1 
ATOM   465  C C   . LYS   A 1 61  ? 132.07730 -46.68594 28.44714  1.000 34.77958 ?  61  LYS   A C   1 
ATOM   466  O O   . LYS   A 1 61  ? 133.26159 -46.78499 28.10725  1.000 34.30733 ?  61  LYS   A O   1 
ATOM   467  C CB  . LYS   A 1 61  ? 131.08226 -44.44195 27.93748  1.000 33.00734 ?  61  LYS   A CB  1 
ATOM   468  C CG  . LYS   A 1 61  ? 130.49892 -43.14496 28.47366  1.000 32.98134 ?  61  LYS   A CG  1 
ATOM   469  C CD  . LYS   A 1 61  ? 129.20265 -43.34872 29.23113  1.000 34.99695 ?  61  LYS   A CD  1 
ATOM   470  C CE  . LYS   A 1 61  ? 128.61626 -42.00266 29.62540  1.000 35.13927 ?  61  LYS   A CE  1 
ATOM   471  N NZ  . LYS   A 1 61  ? 127.27571 -42.10892 30.26335  1.000 44.04071 ?  61  LYS   A NZ  1 
ATOM   472  N N   . SER   A 1 62  ? 131.19909 -47.67870 28.32795  1.000 31.93984 ?  62  SER   A N   1 
ATOM   473  C CA  . SER   A 1 62  ? 131.47770 -48.94742 27.66866  1.000 31.70755 ?  62  SER   A CA  1 
ATOM   474  C C   . SER   A 1 62  ? 130.51952 -49.10174 26.49342  1.000 31.35661 ?  62  SER   A C   1 
ATOM   475  O O   . SER   A 1 62  ? 129.56267 -48.33793 26.35267  1.000 32.45947 ?  62  SER   A O   1 
ATOM   476  C CB  . SER   A 1 62  ? 131.32354 -50.13014 28.63966  1.000 35.37502 ?  62  SER   A CB  1 
ATOM   477  O OG  . SER   A 1 62  ? 132.13735 -49.97369 29.79068  1.000 38.38389 ?  62  SER   A OG  1 
ATOM   478  N N   . ASN   A 1 63  ? 130.78459 -50.11033 25.65012  1.000 32.57758 ?  63  ASN   A N   1 
ATOM   479  C CA  . ASN   A 1 63  ? 129.94350 -50.36385 24.47623  1.000 30.24737 ?  63  ASN   A CA  1 
ATOM   480  C C   . ASN   A 1 63  ? 128.46090 -50.42934 24.83319  1.000 31.48933 ?  63  ASN   A C   1 
ATOM   481  O O   . ASN   A 1 63  ? 127.61883 -49.87323 24.11922  1.000 33.67879 ?  63  ASN   A O   1 
ATOM   482  C CB  . ASN   A 1 63  ? 130.36156 -51.67199 23.79400  1.000 31.11394 ?  63  ASN   A CB  1 
ATOM   483  C CG  . ASN   A 1 63  ? 131.73279 -51.59193 23.15540  1.000 32.94711 ?  63  ASN   A CG  1 
ATOM   484  O OD1 . ASN   A 1 63  ? 132.14461 -50.54006 22.66230  1.000 28.59155 ?  63  ASN   A OD1 1 
ATOM   485  N ND2 . ASN   A 1 63  ? 132.44648 -52.71135 23.15297  1.000 32.15707 ?  63  ASN   A ND2 1 
ATOM   486  N N   . HIS   A 1 64  ? 128.12105 -51.10187 25.93713  1.000 35.37388 ?  64  HIS   A N   1 
ATOM   487  C CA  . HIS   A 1 64  ? 126.71106 -51.30235 26.26037  1.000 35.78590 ?  64  HIS   A CA  1 
ATOM   488  C C   . HIS   A 1 64  ? 126.03413 -50.03731 26.78281  1.000 36.91509 ?  64  HIS   A C   1 
ATOM   489  O O   . HIS   A 1 64  ? 124.80622 -50.03217 26.92530  1.000 36.84174 ?  64  HIS   A O   1 
ATOM   490  C CB  . HIS   A 1 64  ? 126.55858 -52.46072 27.26206  1.000 36.39204 ?  64  HIS   A CB  1 
ATOM   491  C CG  . HIS   A 1 64  ? 127.15881 -52.19673 28.60953  1.000 37.80937 ?  64  HIS   A CG  1 
ATOM   492  N ND1 . HIS   A 1 64  ? 126.59863 -51.32250 29.51825  1.000 39.53304 ?  64  HIS   A ND1 1 
ATOM   493  C CD2 . HIS   A 1 64  ? 128.28812 -52.66635 29.18972  1.000 41.05192 ?  64  HIS   A CD2 1 
ATOM   494  C CE1 . HIS   A 1 64  ? 127.34471 -51.28299 30.60700  1.000 41.67439 ?  64  HIS   A CE1 1 
ATOM   495  N NE2 . HIS   A 1 64  ? 128.37749 -52.08844 30.43294  1.000 43.86012 ?  64  HIS   A NE2 1 
ATOM   496  N N   . ASN   A 1 65  ? 126.79336 -48.96811 27.05364  1.000 35.22166 ?  65  ASN   A N   1 
ATOM   497  C CA  . ASN   A 1 65  ? 126.21514 -47.68888 27.44992  1.000 35.31665 ?  65  ASN   A CA  1 
ATOM   498  C C   . ASN   A 1 65  ? 125.64172 -46.91166 26.27153  1.000 34.82908 ?  65  ASN   A C   1 
ATOM   499  O O   . ASN   A 1 65  ? 124.99399 -45.88284 26.48747  1.000 33.32931 ?  65  ASN   A O   1 
ATOM   500  C CB  . ASN   A 1 65  ? 127.26333 -46.81027 28.13810  1.000 35.49668 ?  65  ASN   A CB  1 
ATOM   501  C CG  . ASN   A 1 65  ? 127.65357 -47.31372 29.51544  1.000 37.59400 ?  65  ASN   A CG  1 
ATOM   502  O OD1 . ASN   A 1 65  ? 128.83528 -47.32458 29.86106  1.000 37.51692 ?  65  ASN   A OD1 1 
ATOM   503  N ND2 . ASN   A 1 65  ? 126.66883 -47.71998 30.31288  1.000 38.10271 ?  65  ASN   A ND2 1 
ATOM   504  N N   . PHE   A 1 66  ? 125.88807 -47.35996 25.04339  1.000 32.72710 ?  66  PHE   A N   1 
ATOM   505  C CA  . PHE   A 1 66  ? 125.41989 -46.69810 23.83045  1.000 32.86214 ?  66  PHE   A CA  1 
ATOM   506  C C   . PHE   A 1 66  ? 124.27306 -47.50627 23.24749  1.000 35.87377 ?  66  PHE   A C   1 
ATOM   507  O O   . PHE   A 1 66  ? 124.45600 -48.67539 22.89771  1.000 37.26857 ?  66  PHE   A O   1 
ATOM   508  C CB  . PHE   A 1 66  ? 126.55575 -46.56963 22.81426  1.000 30.02614 ?  66  PHE   A CB  1 
ATOM   509  C CG  . PHE   A 1 66  ? 127.65770 -45.67307 23.26098  1.000 29.97219 ?  66  PHE   A CG  1 
ATOM   510  C CD1 . PHE   A 1 66  ? 127.46636 -44.30281 23.31979  1.000 30.79433 ?  66  PHE   A CD1 1 
ATOM   511  C CD2 . PHE   A 1 66  ? 128.85756 -46.19955 23.70763  1.000 29.61249 ?  66  PHE   A CD2 1 
ATOM   512  C CE1 . PHE   A 1 66  ? 128.47778 -43.46371 23.74869  1.000 30.19904 ?  66  PHE   A CE1 1 
ATOM   513  C CE2 . PHE   A 1 66  ? 129.87196 -45.36175 24.14715  1.000 29.48038 ?  66  PHE   A CE2 1 
ATOM   514  C CZ  . PHE   A 1 66  ? 129.67604 -43.99387 24.16907  1.000 30.74732 ?  66  PHE   A CZ  1 
ATOM   515  N N   . LEU   A 1 67  ? 123.10053 -46.88842 23.14735  1.000 31.06637 ?  67  LEU   A N   1 
ATOM   516  C CA  . LEU   A 1 67  ? 121.93522 -47.51497 22.53816  1.000 32.20445 ?  67  LEU   A CA  1 
ATOM   517  C C   . LEU   A 1 67  ? 121.74737 -46.91817 21.15517  1.000 32.72582 ?  67  LEU   A C   1 
ATOM   518  O O   . LEU   A 1 67  ? 121.63016 -45.69656 21.01301  1.000 29.44659 ?  67  LEU   A O   1 
ATOM   519  C CB  . LEU   A 1 67  ? 120.67336 -47.31828 23.37911  1.000 37.46023 ?  67  LEU   A CB  1 
ATOM   520  C CG  . LEU   A 1 67  ? 120.47048 -48.19061 24.62575  1.000 44.42537 ?  67  LEU   A CG  1 
ATOM   521  C CD1 . LEU   A 1 67  ? 120.86820 -49.64309 24.35266  1.000 48.29620 ?  67  LEU   A CD1 1 
ATOM   522  C CD2 . LEU   A 1 67  ? 121.20739 -47.64597 25.83731  1.000 46.24723 ?  67  LEU   A CD2 1 
ATOM   523  N N   . VAL   A 1 68  ? 121.73915 -47.77017 20.14182  1.000 32.97825 ?  68  VAL   A N   1 
ATOM   524  C CA  . VAL   A 1 68  ? 121.57608 -47.32494 18.76935  1.000 31.67222 ?  68  VAL   A CA  1 
ATOM   525  C C   . VAL   A 1 68  ? 120.32575 -47.99482 18.22761  1.000 37.11870 ?  68  VAL   A C   1 
ATOM   526  O O   . VAL   A 1 68  ? 120.19003 -49.22110 18.31240  1.000 37.38868 ?  68  VAL   A O   1 
ATOM   527  C CB  . VAL   A 1 68  ? 122.81122 -47.64603 17.91480  1.000 33.77908 ?  68  VAL   A CB  1 
ATOM   528  C CG1 . VAL   A 1 68  ? 122.57929 -47.24910 16.46761  1.000 32.66743 ?  68  VAL   A CG1 1 
ATOM   529  C CG2 . VAL   A 1 68  ? 124.04012 -46.93647 18.49579  1.000 28.95230 ?  68  VAL   A CG2 1 
ATOM   530  N N   . GLN   A 1 69  ? 119.40324 -47.18637 17.70937  1.000 34.13727 ?  69  GLN   A N   1 
ATOM   531  C CA  . GLN   A 1 69  ? 118.13474 -47.65071 17.16241  1.000 39.62034 ?  69  GLN   A CA  1 
ATOM   532  C C   . GLN   A 1 69  ? 118.00519 -47.19341 15.71874  1.000 40.00119 ?  69  GLN   A C   1 
ATOM   533  O O   . GLN   A 1 69  ? 118.19412 -46.00990 15.42114  1.000 33.50268 ?  69  GLN   A O   1 
ATOM   534  C CB  . GLN   A 1 69  ? 116.93818 -47.11134 17.95307  1.000 42.93118 ?  69  GLN   A CB  1 
ATOM   535  C CG  . GLN   A 1 69  ? 115.93218 -48.15887 18.36558  1.000 50.18150 ?  69  GLN   A CG  1 
ATOM   536  C CD  . GLN   A 1 69  ? 114.91796 -47.62650 19.35687  1.000 54.57158 ?  69  GLN   A CD  1 
ATOM   537  O OE1 . GLN   A 1 69  ? 115.23121 -47.38747 20.52282  1.000 58.49648 ?  69  GLN   A OE1 1 
ATOM   538  N NE2 . GLN   A 1 69  ? 113.68902 -47.42969 18.88970  1.000 54.44752 ?  69  GLN   A NE2 1 
ATOM   539  N N   . ALA   A 1 70  ? 117.66130 -48.12047 14.83175  1.000 42.87131 ?  70  ALA   A N   1 
ATOM   540  C CA  . ALA   A 1 70  ? 117.32723 -47.79571 13.44946  1.000 42.37733 ?  70  ALA   A CA  1 
ATOM   541  C C   . ALA   A 1 70  ? 115.84087 -48.09846 13.28625  1.000 48.38900 ?  70  ALA   A C   1 
ATOM   542  O O   . ALA   A 1 70  ? 115.45100 -49.25343 13.09444  1.000 51.08967 ?  70  ALA   A O   1 
ATOM   543  C CB  . ALA   A 1 70  ? 118.19138 -48.58693 12.47491  1.000 42.46905 ?  70  ALA   A CB  1 
ATOM   544  N N   . GLY   A 1 71  ? 115.01104 -47.06355 13.38329  1.000 45.40908 ?  71  GLY   A N   1 
ATOM   545  C CA  . GLY   A 1 71  ? 113.57876 -47.27850 13.44685  1.000 49.10783 ?  71  GLY   A CA  1 
ATOM   546  C C   . GLY   A 1 71  ? 113.19830 -47.99287 14.72773  1.000 51.92462 ?  71  GLY   A C   1 
ATOM   547  O O   . GLY   A 1 71  ? 113.24899 -47.40199 15.81060  1.000 54.50036 ?  71  GLY   A O   1 
ATOM   548  N N   . ASN   A 1 72  ? 112.82014 -49.26700 14.62606  1.000 50.86339 ?  72  ASN   A N   1 
ATOM   549  C CA  . ASN   A 1 72  ? 112.57417 -50.08924 15.80194  1.000 53.30799 ?  72  ASN   A CA  1 
ATOM   550  C C   . ASN   A 1 72  ? 113.65345 -51.13531 16.02849  1.000 58.21401 ?  72  ASN   A C   1 
ATOM   551  O O   . ASN   A 1 72  ? 113.67865 -51.75484 17.09822  1.000 59.70102 ?  72  ASN   A O   1 
ATOM   552  C CB  . ASN   A 1 72  ? 111.20903 -50.78734 15.70049  1.000 51.57651 ?  72  ASN   A CB  1 
ATOM   553  N N   . VAL   A 1 73  ? 114.54107 -51.34363 15.05575  1.000 54.65248 ?  73  VAL   A N   1 
ATOM   554  C CA  . VAL   A 1 73  ? 115.60456 -52.32699 15.19589  1.000 54.72982 ?  73  VAL   A CA  1 
ATOM   555  C C   . VAL   A 1 73  ? 116.66063 -51.79350 16.15347  1.000 52.96065 ?  73  VAL   A C   1 
ATOM   556  O O   . VAL   A 1 73  ? 116.96998 -50.59389 16.16481  1.000 48.47109 ?  73  VAL   A O   1 
ATOM   557  C CB  . VAL   A 1 73  ? 116.20545 -52.65268 13.81669  1.000 55.52786 ?  73  VAL   A CB  1 
ATOM   558  C CG1 . VAL   A 1 73  ? 117.34330 -53.66025 13.93993  1.000 56.96836 ?  73  VAL   A CG1 1 
ATOM   559  C CG2 . VAL   A 1 73  ? 115.12188 -53.16134 12.86888  1.000 62.95622 ?  73  VAL   A CG2 1 
ATOM   560  N N   . GLN   A 1 74  ? 117.21180 -52.67991 16.97286  1.000 52.46095 ?  74  GLN   A N   1 
ATOM   561  C CA  . GLN   A 1 74  ? 118.25721 -52.32643 17.92042  1.000 48.43459 ?  74  GLN   A CA  1 
ATOM   562  C C   . GLN   A 1 74  ? 119.58548 -52.89115 17.44089  1.000 48.63586 ?  74  GLN   A C   1 
ATOM   563  O O   . GLN   A 1 74  ? 119.74872 -54.11177 17.34429  1.000 48.89024 ?  74  GLN   A O   1 
ATOM   564  C CB  . GLN   A 1 74  ? 117.91844 -52.83426 19.31868  1.000 50.76638 ?  74  GLN   A CB  1 
ATOM   565  C CG  . GLN   A 1 74  ? 118.30576 -51.85998 20.40741  1.000 51.07078 ?  74  GLN   A CG  1 
ATOM   566  C CD  . GLN   A 1 74  ? 117.17155 -50.92527 20.77436  1.000 59.27208 ?  74  GLN   A CD  1 
ATOM   567  O OE1 . GLN   A 1 74  ? 115.99619 -51.23775 20.56519  1.000 66.75164 ?  74  GLN   A OE1 1 
ATOM   568  N NE2 . GLN   A 1 74  ? 117.51899 -49.76821 21.33283  1.000 49.82479 ?  74  GLN   A NE2 1 
ATOM   569  N N   . LEU   A 1 75  ? 120.52890 -52.00377 17.14501  1.000 45.68853 ?  75  LEU   A N   1 
ATOM   570  C CA  . LEU   A 1 75  ? 121.85542 -52.43213 16.74196  1.000 41.87711 ?  75  LEU   A CA  1 
ATOM   571  C C   . LEU   A 1 75  ? 122.70197 -52.70275 17.97152  1.000 41.87427 ?  75  LEU   A C   1 
ATOM   572  O O   . LEU   A 1 75  ? 122.55335 -52.05061 19.00938  1.000 43.72387 ?  75  LEU   A O   1 
ATOM   573  C CB  . LEU   A 1 75  ? 122.54706 -51.37994 15.87892  1.000 39.73109 ?  75  LEU   A CB  1 
ATOM   574  C CG  . LEU   A 1 75  ? 121.95288 -50.90798 14.55606  1.000 38.55508 ?  75  LEU   A CG  1 
ATOM   575  C CD1 . LEU   A 1 75  ? 120.69857 -50.06586 14.75544  1.000 43.71831 ?  75  LEU   A CD1 1 
ATOM   576  C CD2 . LEU   A 1 75  ? 123.00566 -50.12561 13.81453  1.000 31.75152 ?  75  LEU   A CD2 1 
ATOM   577  N N   . ARG   A 1 76  ? 123.60265 -53.66785 17.84894  1.000 38.47218 ?  76  ARG   A N   1 
ATOM   578  C CA  . ARG   A 1 76  ? 124.46244 -54.04900 18.95700  1.000 41.52837 ?  76  ARG   A CA  1 
ATOM   579  C C   . ARG   A 1 76  ? 125.82706 -53.39906 18.76807  1.000 38.68623 ?  76  ARG   A C   1 
ATOM   580  O O   . ARG   A 1 76  ? 126.43906 -53.53205 17.70412  1.000 36.60653 ?  76  ARG   A O   1 
ATOM   581  C CB  . ARG   A 1 76  ? 124.58626 -55.56933 19.05262  1.000 41.63535 ?  76  ARG   A CB  1 
ATOM   582  C CG  . ARG   A 1 76  ? 125.33107 -56.05354 20.28625  1.000 42.07861 ?  76  ARG   A CG  1 
ATOM   583  C CD  . ARG   A 1 76  ? 125.51263 -57.55378 20.25727  1.000 42.67399 ?  76  ARG   A CD  1 
ATOM   584  N NE  . ARG   A 1 76  ? 124.22788 -58.24073 20.24721  1.000 45.72874 ?  76  ARG   A NE  1 
ATOM   585  C CZ  . ARG   A 1 76  ? 123.55805 -58.60633 21.33131  1.000 42.61117 ?  76  ARG   A CZ  1 
ATOM   586  N NH1 . ARG   A 1 76  ? 124.04025 -58.39621 22.54496  1.000 41.01284 ?  76  ARG   A NH1 1 
ATOM   587  N NH2 . ARG   A 1 76  ? 122.37306 -59.19670 21.19194  1.000 42.43584 ?  76  ARG   A NH2 1 
ATOM   588  N N   . VAL   A 1 77  ? 126.28866 -52.69027 19.79531  1.000 38.07702 ?  77  VAL   A N   1 
ATOM   589  C CA  . VAL   A 1 77  ? 127.53808 -51.94059 19.73852  1.000 34.92584 ?  77  VAL   A CA  1 
ATOM   590  C C   . VAL   A 1 77  ? 128.67508 -52.83789 20.21270  1.000 35.48185 ?  77  VAL   A C   1 
ATOM   591  O O   . VAL   A 1 77  ? 128.67377 -53.32290 21.35116  1.000 34.11545 ?  77  VAL   A O   1 
ATOM   592  C CB  . VAL   A 1 77  ? 127.44591 -50.65667 20.57675  1.000 34.62488 ?  77  VAL   A CB  1 
ATOM   593  C CG1 . VAL   A 1 77  ? 128.77135 -49.90709 20.57119  1.000 31.63958 ?  77  VAL   A CG1 1 
ATOM   594  C CG2 . VAL   A 1 77  ? 126.32496 -49.77593 20.04349  1.000 34.10418 ?  77  VAL   A CG2 1 
ATOM   595  N N   . ILE   A 1 78  ? 129.65050 -53.06395 19.33650  1.000 31.53726 ?  78  ILE   A N   1 
ATOM   596  C CA  . ILE   A 1 78  ? 130.75195 -53.97426 19.61528  1.000 34.72191 ?  78  ILE   A CA  1 
ATOM   597  C C   . ILE   A 1 78  ? 132.09985 -53.26251 19.64926  1.000 34.67961 ?  78  ILE   A C   1 
ATOM   598  O O   . ILE   A 1 78  ? 133.14081 -53.91579 19.71008  1.000 35.57471 ?  78  ILE   A O   1 
ATOM   599  C CB  . ILE   A 1 78  ? 130.75280 -55.15113 18.61809  1.000 35.56324 ?  78  ILE   A CB  1 
ATOM   600  C CG1 . ILE   A 1 78  ? 131.41210 -54.75286 17.29786  1.000 36.00752 ?  78  ILE   A CG1 1 
ATOM   601  C CG2 . ILE   A 1 78  ? 129.34108 -55.68491 18.40993  1.000 38.66052 ?  78  ILE   A CG2 1 
ATOM   602  C CD1 . ILE   A 1 78  ? 131.50546 -55.87576 16.27769  1.000 37.83771 ?  78  ILE   A CD1 1 
ATOM   603  N N   . GLY   A 1 79  ? 132.10067 -51.93319 19.64887  1.000 33.53985 ?  79  GLY   A N   1 
ATOM   604  C CA  . GLY   A 1 79  ? 133.32585 -51.16504 19.74534  1.000 31.60416 ?  79  GLY   A CA  1 
ATOM   605  C C   . GLY   A 1 79  ? 133.04393 -49.67679 19.69024  1.000 27.71098 ?  79  GLY   A C   1 
ATOM   606  O O   . GLY   A 1 79  ? 132.03103 -49.25596 19.12602  1.000 29.78227 ?  79  GLY   A O   1 
ATOM   607  N N   . HIS   A 1 80  ? 133.91183 -48.86320 20.28258  1.000 27.51609 ?  80  HIS   A N   1 
ATOM   608  C CA  . HIS   A 1 80  ? 133.69778 -47.42428 20.23912  1.000 27.92896 ?  80  HIS   A CA  1 
ATOM   609  C C   . HIS   A 1 80  ? 135.03962 -46.71213 20.22388  1.000 27.54644 ?  80  HIS   A C   1 
ATOM   610  O O   . HIS   A 1 80  ? 136.02563 -47.19774 20.79144  1.000 24.98861 ?  80  HIS   A O   1 
ATOM   611  C CB  . HIS   A 1 80  ? 132.85181 -46.94761 21.42568  1.000 25.61996 ?  80  HIS   A CB  1 
ATOM   612  C CG  . HIS   A 1 80  ? 133.52399 -47.11700 22.75267  1.000 28.28857 ?  80  HIS   A CG  1 
ATOM   613  N ND1 . HIS   A 1 80  ? 133.40669 -48.26767 23.50414  1.000 30.40102 ?  80  HIS   A ND1 1 
ATOM   614  C CD2 . HIS   A 1 80  ? 134.32269 -46.28509 23.46190  1.000 26.21740 ?  80  HIS   A CD2 1 
ATOM   615  C CE1 . HIS   A 1 80  ? 134.10135 -48.13498 24.62067  1.000 29.77461 ?  80  HIS   A CE1 1 
ATOM   616  N NE2 . HIS   A 1 80  ? 134.66558 -46.94103 24.62073  1.000 29.80729 ?  80  HIS   A NE2 1 
ATOM   617  N N   . SER   A 1 81  ? 135.06963 -45.55041 19.57353  1.000 24.93851 ?  81  SER   A N   1 
ATOM   618  C CA  . SER   A 1 81  ? 136.28316 -44.75180 19.58093  1.000 24.80263 ?  81  SER   A CA  1 
ATOM   619  C C   . SER   A 1 81  ? 135.94035 -43.30233 19.26731  1.000 25.28760 ?  81  SER   A C   1 
ATOM   620  O O   . SER   A 1 81  ? 134.93493 -43.00077 18.62403  1.000 26.76771 ?  81  SER   A O   1 
ATOM   621  C CB  . SER   A 1 81  ? 137.30902 -45.28341 18.57928  1.000 26.28773 ?  81  SER   A CB  1 
ATOM   622  O OG  . SER   A 1 81  ? 136.92537 -44.96933 17.26485  1.000 28.65002 ?  81  SER   A OG  1 
ATOM   623  N N   . MET   A 1 82  ? 136.79702 -42.41640 19.74829  1.000 23.34185 ?  82  MET   A N   1 
ATOM   624  C CA  . MET   A 1 82  ? 136.71907 -40.98639 19.48977  1.000 23.59016 ?  82  MET   A CA  1 
ATOM   625  C C   . MET   A 1 82  ? 137.68587 -40.61441 18.38712  1.000 22.89696 ?  82  MET   A C   1 
ATOM   626  O O   . MET   A 1 82  ? 138.88736 -40.86505 18.51719  1.000 26.07208 ?  82  MET   A O   1 
ATOM   627  C CB  . MET   A 1 82  ? 137.09419 -40.17988 20.72915  1.000 27.53738 ?  82  MET   A CB  1 
ATOM   628  C CG  . MET   A 1 82  ? 136.48788 -38.81396 20.72888  1.000 25.21738 ?  82  MET   A CG  1 
ATOM   629  S SD  . MET   A 1 82  ? 136.41677 -38.05226 22.33879  1.000 25.06949 ?  82  MET   A SD  1 
ATOM   630  C CE  . MET   A 1 82  ? 138.01658 -38.46830 23.04337  1.000 26.45757 ?  82  MET   A CE  1 
ATOM   631  N N   . GLN   A 1 83  ? 137.17368 -39.97566 17.33454  1.000 23.59592 ?  83  GLN   A N   1 
ATOM   632  C CA  . GLN   A 1 83  ? 138.01407 -39.38295 16.30393  1.000 22.38835 ?  83  GLN   A CA  1 
ATOM   633  C C   . GLN   A 1 83  ? 137.70263 -37.89489 16.28115  1.000 20.27461 ?  83  GLN   A C   1 
ATOM   634  O O   . GLN   A 1 83  ? 136.61716 -37.49978 15.84834  1.000 18.33427 ?  83  GLN   A O   1 
ATOM   635  C CB  . GLN   A 1 83  ? 137.77132 -40.02414 14.94049  1.000 21.51155 ?  83  GLN   A CB  1 
ATOM   636  C CG  . GLN   A 1 83  ? 138.51837 -39.30704 13.83682  1.000 25.33715 ?  83  GLN   A CG  1 
ATOM   637  C CD  . GLN   A 1 83  ? 138.30275 -39.91231 12.46658  1.000 25.61756 ?  83  GLN   A CD  1 
ATOM   638  O OE1 . GLN   A 1 83  ? 137.33348 -40.64087 12.22521  1.000 26.18618 ?  83  GLN   A OE1 1 
ATOM   639  N NE2 . GLN   A 1 83  ? 139.23515 -39.63919 11.56301  1.000 24.83155 ?  83  GLN   A NE2 1 
ATOM   640  N N   . ASN   A 1 84  ? 138.63227 -37.08211 16.78926  1.000 19.77318 ?  84  ASN   A N   1 
ATOM   641  C CA  . ASN   A 1 84  ? 138.40437 -35.65191 16.95448  1.000 18.88610 ?  84  ASN   A CA  1 
ATOM   642  C C   . ASN   A 1 84  ? 137.08082 -35.41958 17.69213  1.000 18.18397 ?  84  ASN   A C   1 
ATOM   643  O O   . ASN   A 1 84  ? 136.90549 -35.90378 18.81587  1.000 18.44565 ?  84  ASN   A O   1 
ATOM   644  C CB  . ASN   A 1 84  ? 138.44573 -34.96674 15.58848  1.000 19.27480 ?  84  ASN   A CB  1 
ATOM   645  C CG  . ASN   A 1 84  ? 139.76680 -35.20564 14.87654  1.000 20.68433 ?  84  ASN   A CG  1 
ATOM   646  O OD1 . ASN   A 1 84  ? 140.84103 -34.97606 15.44728  1.000 22.55597 ?  84  ASN   A OD1 1 
ATOM   647  N ND2 . ASN   A 1 84  ? 139.70005 -35.75100 13.67049  1.000 21.75947 ?  84  ASN   A ND2 1 
ATOM   648  N N   . CYS   A 1 85  ? 136.12256 -34.71630 17.09290  1.000 17.06440 ?  85  CYS   A N   1 
ATOM   649  C CA  . CYS   A 1 85  ? 134.87206 -34.44847 17.79410  1.000 17.14224 ?  85  CYS   A CA  1 
ATOM   650  C C   . CYS   A 1 85  ? 133.74675 -35.41140 17.44220  1.000 17.34217 ?  85  CYS   A C   1 
ATOM   651  O O   . CYS   A 1 85  ? 132.60119 -35.16352 17.83634  1.000 18.57941 ?  85  CYS   A O   1 
ATOM   652  C CB  . CYS   A 1 85  ? 134.40686 -33.01213 17.55763  1.000 16.53082 ?  85  CYS   A CB  1 
ATOM   653  S SG  . CYS   A 1 85  ? 135.60867 -31.82885 18.17450  1.000 19.79368 ?  85  CYS   A SG  1 
ATOM   654  N N   . VAL   A 1 86  ? 134.03197 -36.50887 16.74504  1.000 16.29848 ?  86  VAL   A N   1 
ATOM   655  C CA  . VAL   A 1 86  ? 132.98795 -37.47766 16.45187  1.000 15.82801 ?  86  VAL   A CA  1 
ATOM   656  C C   . VAL   A 1 86  ? 133.28637 -38.76611 17.19232  1.000 19.28384 ?  86  VAL   A C   1 
ATOM   657  O O   . VAL   A 1 86  ? 134.44129 -39.14551 17.43375  1.000 20.89612 ?  86  VAL   A O   1 
ATOM   658  C CB  . VAL   A 1 86  ? 132.78257 -37.76875 14.94732  1.000 18.82584 ?  86  VAL   A CB  1 
ATOM   659  C CG1 . VAL   A 1 86  ? 132.13810 -36.55889 14.25612  1.000 19.18716 ?  86  VAL   A CG1 1 
ATOM   660  C CG2 . VAL   A 1 86  ? 134.06842 -38.20982 14.29200  1.000 27.84238 ?  86  VAL   A CG2 1 
ATOM   661  N N   . LEU   A 1 87  ? 132.21324 -39.42148 17.58415  1.000 17.63456 ?  87  LEU   A N   1 
ATOM   662  C CA  . LEU   A 1 87  ? 132.26374 -40.75789 18.13655  1.000 22.64461 ?  87  LEU   A CA  1 
ATOM   663  C C   . LEU   A 1 87  ? 131.93387 -41.74578 17.02955  1.000 21.29521 ?  87  LEU   A C   1 
ATOM   664  O O   . LEU   A 1 87  ? 131.03317 -41.50357 16.22170  1.000 21.47821 ?  87  LEU   A O   1 
ATOM   665  C CB  . LEU   A 1 87  ? 131.27051 -40.87909 19.28770  1.000 22.76825 ?  87  LEU   A CB  1 
ATOM   666  C CG  . LEU   A 1 87  ? 131.43372 -41.99751 20.29792  1.000 30.33670 ?  87  LEU   A CG  1 
ATOM   667  C CD1 . LEU   A 1 87  ? 132.80080 -41.93269 20.93726  1.000 35.82281 ?  87  LEU   A CD1 1 
ATOM   668  C CD2 . LEU   A 1 87  ? 130.34668 -41.81577 21.32560  1.000 30.44008 ?  87  LEU   A CD2 1 
ATOM   669  N N   . LYS   A 1 88  ? 132.70424 -42.82451 16.96271  1.000 22.50872 ?  88  LYS   A N   1 
ATOM   670  C CA  . LYS   A 1 88  ? 132.49313 -43.89802 16.00096  1.000 21.90581 ?  88  LYS   A CA  1 
ATOM   671  C C   . LYS   A 1 88  ? 132.11465 -45.15056 16.78394  1.000 26.21211 ?  88  LYS   A C   1 
ATOM   672  O O   . LYS   A 1 88  ? 132.92207 -45.67700 17.55788  1.000 23.44847 ?  88  LYS   A O   1 
ATOM   673  C CB  . LYS   A 1 88  ? 133.73901 -44.13221 15.14722  1.000 25.58372 ?  88  LYS   A CB  1 
ATOM   674  C CG  . LYS   A 1 88  ? 134.05326 -42.95424 14.24174  1.000 27.13724 ?  88  LYS   A CG  1 
ATOM   675  C CD  . LYS   A 1 88  ? 135.11460 -43.28808 13.21858  1.000 29.86176 ?  88  LYS   A CD  1 
ATOM   676  C CE  . LYS   A 1 88  ? 136.46422 -43.50883 13.85211  1.000 30.62837 ?  88  LYS   A CE  1 
ATOM   677  N NZ  . LYS   A 1 88  ? 137.49498 -43.65498 12.79442  1.000 32.74984 ?  88  LYS   A NZ  1 
ATOM   678  N N   . LEU   A 1 89  ? 130.88841 -45.61411 16.59770  1.000 21.89787 ?  89  LEU   A N   1 
ATOM   679  C CA  . LEU   A 1 89  ? 130.39926 -46.81952 17.24971  1.000 24.73658 ?  89  LEU   A CA  1 
ATOM   680  C C   . LEU   A 1 89  ? 130.38938 -47.95282 16.24033  1.000 24.05668 ?  89  LEU   A C   1 
ATOM   681  O O   . LEU   A 1 89  ? 129.70227 -47.86962 15.21886  1.000 26.37577 ?  89  LEU   A O   1 
ATOM   682  C CB  . LEU   A 1 89  ? 129.00294 -46.60487 17.83268  1.000 23.53270 ?  89  LEU   A CB  1 
ATOM   683  C CG  . LEU   A 1 89  ? 128.90021 -45.35993 18.70577  1.000 25.55715 ?  89  LEU   A CG  1 
ATOM   684  C CD1 . LEU   A 1 89  ? 127.45557 -45.08064 19.07074  1.000 24.74615 ?  89  LEU   A CD1 1 
ATOM   685  C CD2 . LEU   A 1 89  ? 129.76212 -45.54984 19.95828  1.000 25.47600 ?  89  LEU   A CD2 1 
ATOM   686  N N   . LYS   A 1 90  ? 131.16674 -48.99328 16.51316  1.000 27.68368 ?  90  LYS   A N   1 
ATOM   687  C CA  . LYS   A 1 90  ? 131.15433 -50.17383 15.66793  1.000 27.07743 ?  90  LYS   A CA  1 
ATOM   688  C C   . LYS   A 1 90  ? 129.97112 -51.04736 16.05725  1.000 30.58751 ?  90  LYS   A C   1 
ATOM   689  O O   . LYS   A 1 90  ? 129.77957 -51.35132 17.23709  1.000 29.40259 ?  90  LYS   A O   1 
ATOM   690  C CB  . LYS   A 1 90  ? 132.46187 -50.95137 15.80675  1.000 31.12247 ?  90  LYS   A CB  1 
ATOM   691  C CG  . LYS   A 1 90  ? 132.49568 -52.25857 15.03358  1.000 33.82253 ?  90  LYS   A CG  1 
ATOM   692  C CD  . LYS   A 1 90  ? 133.60023 -52.27626 13.99440  1.000 40.64658 ?  90  LYS   A CD  1 
ATOM   693  C CE  . LYS   A 1 90  ? 133.60545 -53.58807 13.22422  1.000 41.54156 ?  90  LYS   A CE  1 
ATOM   694  N NZ  . LYS   A 1 90  ? 134.94694 -54.23235 13.22540  1.000 51.04887 ?  90  LYS   A NZ  1 
ATOM   695  N N   . VAL   A 1 91  ? 129.16672 -51.43900 15.06858  1.000 32.13926 ?  91  VAL   A N   1 
ATOM   696  C CA  . VAL   A 1 91  ? 127.99506 -52.26347 15.32597  1.000 33.20423 ?  91  VAL   A CA  1 
ATOM   697  C C   . VAL   A 1 91  ? 128.17661 -53.60987 14.63079  1.000 35.73609 ?  91  VAL   A C   1 
ATOM   698  O O   . VAL   A 1 91  ? 129.03729 -53.77913 13.76447  1.000 33.01779 ?  91  VAL   A O   1 
ATOM   699  C CB  . VAL   A 1 91  ? 126.69364 -51.56675 14.88659  1.000 32.72719 ?  91  VAL   A CB  1 
ATOM   700  C CG1 . VAL   A 1 91  ? 126.47840 -50.30242 15.72177  1.000 30.31035 ?  91  VAL   A CG1 1 
ATOM   701  C CG2 . VAL   A 1 91  ? 126.72801 -51.21229 13.40691  1.000 31.99499 ?  91  VAL   A CG2 1 
ATOM   702  N N   . ASP   A 1 92  ? 127.37526 -54.58667 15.05143  1.000 34.62614 ?  92  ASP   A N   1 
ATOM   703  C CA  . ASP   A 1 92  ? 127.48511 -55.94110 14.51519  1.000 38.79373 ?  92  ASP   A CA  1 
ATOM   704  C C   . ASP   A 1 92  ? 126.78121 -56.12746 13.17177  1.000 39.56233 ?  92  ASP   A C   1 
ATOM   705  O O   . ASP   A 1 92  ? 126.88704 -57.20838 12.58397  1.000 41.50089 ?  92  ASP   A O   1 
ATOM   706  C CB  . ASP   A 1 92  ? 126.93435 -56.95824 15.51888  1.000 44.11461 ?  92  ASP   A CB  1 
ATOM   707  C CG  . ASP   A 1 92  ? 125.47909 -56.70688 15.87723  1.000 44.24270 ?  92  ASP   A CG  1 
ATOM   708  O OD1 . ASP   A 1 92  ? 124.86086 -55.77670 15.31443  1.000 45.62410 ?  92  ASP   A OD1 1 
ATOM   709  O OD2 . ASP   A 1 92  ? 124.94971 -57.45737 16.72259  1.000 47.10020 -1 92  ASP   A OD2 1 
ATOM   710  N N   . THR   A 1 93  ? 126.07048 -55.11908 12.67500  1.000 36.34596 ?  93  THR   A N   1 
ATOM   711  C CA  . THR   A 1 93  ? 125.30514 -55.21882 11.43630  1.000 38.42084 ?  93  THR   A CA  1 
ATOM   712  C C   . THR   A 1 93  ? 125.70861 -54.08741 10.50221  1.000 35.75515 ?  93  THR   A C   1 
ATOM   713  O O   . THR   A 1 93  ? 125.73675 -52.92496 10.91724  1.000 34.46013 ?  93  THR   A O   1 
ATOM   714  C CB  . THR   A 1 93  ? 123.79759 -55.14596 11.71436  1.000 38.22299 ?  93  THR   A CB  1 
ATOM   715  O OG1 . THR   A 1 93  ? 123.40805 -56.24381 12.54744  1.000 45.91166 ?  93  THR   A OG1 1 
ATOM   716  C CG2 . THR   A 1 93  ? 123.00223 -55.19990 10.41208  1.000 35.29441 ?  93  THR   A CG2 1 
ATOM   717  N N   . ALA   A 1 94  ? 126.01567 -54.41939 9.24593   1.000 34.30837 ?  94  ALA   A N   1 
ATOM   718  C CA  . ALA   A 1 94  ? 126.26595 -53.39099 8.24428   1.000 32.58465 ?  94  ALA   A CA  1 
ATOM   719  C C   . ALA   A 1 94  ? 124.93988 -52.89420 7.68919   1.000 32.71610 ?  94  ALA   A C   1 
ATOM   720  O O   . ALA   A 1 94  ? 124.01640 -53.68019 7.46973   1.000 33.12284 ?  94  ALA   A O   1 
ATOM   721  C CB  . ALA   A 1 94  ? 127.14146 -53.93067 7.11341   1.000 36.62786 ?  94  ALA   A CB  1 
ATOM   722  N N   . ASN   A 1 95  ? 124.84009 -51.58676 7.48406   1.000 29.18697 ?  95  ASN   A N   1 
ATOM   723  C CA  . ASN   A 1 95  ? 123.58434 -50.98638 7.04977   1.000 32.68949 ?  95  ASN   A CA  1 
ATOM   724  C C   . ASN   A 1 95  ? 123.23620 -51.51056 5.66243   1.000 30.02637 ?  95  ASN   A C   1 
ATOM   725  O O   . ASN   A 1 95  ? 123.98312 -51.25521 4.71084   1.000 30.70303 ?  95  ASN   A O   1 
ATOM   726  C CB  . ASN   A 1 95  ? 123.70302 -49.45380 7.04068   1.000 26.08242 ?  95  ASN   A CB  1 
ATOM   727  C CG  . ASN   A 1 95  ? 122.40422 -48.75632 6.63811   1.000 30.65937 ?  95  ASN   A CG  1 
ATOM   728  O OD1 . ASN   A 1 95  ? 121.42706 -49.39775 6.26023   1.000 29.36259 ?  95  ASN   A OD1 1 
ATOM   729  N ND2 . ASN   A 1 95  ? 122.38665 -47.42855 6.75442   1.000 24.59990 ?  95  ASN   A ND2 1 
ATOM   730  N N   . PRO   A 1 96  ? 122.13340 -52.24492 5.49790   1.000 32.04378 ?  96  PRO   A N   1 
ATOM   731  C CA  . PRO   A 1 96  ? 121.79773 -52.76426 4.16273   1.000 33.04875 ?  96  PRO   A CA  1 
ATOM   732  C C   . PRO   A 1 96  ? 121.45605 -51.67158 3.17592   1.000 35.29037 ?  96  PRO   A C   1 
ATOM   733  O O   . PRO   A 1 96  ? 121.48382 -51.91782 1.96227   1.000 38.36823 ?  96  PRO   A O   1 
ATOM   734  C CB  . PRO   A 1 96  ? 120.58931 -53.67610 4.42718   1.000 36.61769 ?  96  PRO   A CB  1 
ATOM   735  C CG  . PRO   A 1 96  ? 120.00003 -53.18205 5.69134   1.000 36.89780 ?  96  PRO   A CG  1 
ATOM   736  C CD  . PRO   A 1 96  ? 121.14145 -52.63112 6.51470   1.000 31.93308 ?  96  PRO   A CD  1 
ATOM   737  N N   . LYS   A 1 97  ? 121.14309 -50.46899 3.65370   1.000 32.81007 ?  97  LYS   A N   1 
ATOM   738  C CA  . LYS   A 1 97  ? 120.79620 -49.35062 2.79384   1.000 33.21533 ?  97  LYS   A CA  1 
ATOM   739  C C   . LYS   A 1 97  ? 121.95236 -48.37347 2.61178   1.000 31.91600 ?  97  LYS   A C   1 
ATOM   740  O O   . LYS   A 1 97  ? 121.72163 -47.23308 2.19824   1.000 30.52824 ?  97  LYS   A O   1 
ATOM   741  C CB  . LYS   A 1 97  ? 119.57770 -48.61343 3.35256   1.000 34.42603 ?  97  LYS   A CB  1 
ATOM   742  C CG  . LYS   A 1 97  ? 118.39670 -49.49910 3.71361   1.000 39.54761 ?  97  LYS   A CG  1 
ATOM   743  C CD  . LYS   A 1 97  ? 117.36230 -48.71716 4.51579   1.000 42.01186 ?  97  LYS   A CD  1 
ATOM   744  C CE  . LYS   A 1 97  ? 116.01445 -49.41902 4.54004   1.000 55.18762 ?  97  LYS   A CE  1 
ATOM   745  N NZ  . LYS   A 1 97  ? 115.27136 -49.21237 3.26169   1.000 59.06082 ?  97  LYS   A NZ  1 
ATOM   746  N N   . THR   A 1 98  ? 123.18129 -48.78338 2.92849   1.000 32.95252 ?  98  THR   A N   1 
ATOM   747  C CA  . THR   A 1 98  ? 124.34430 -47.91623 2.74146   1.000 30.67564 ?  98  THR   A CA  1 
ATOM   748  C C   . THR   A 1 98  ? 124.48278 -47.54320 1.27273   1.000 30.81452 ?  98  THR   A C   1 
ATOM   749  O O   . THR   A 1 98  ? 124.57250 -48.44122 0.42757   1.000 29.04392 ?  98  THR   A O   1 
ATOM   750  C CB  . THR   A 1 98  ? 125.64253 -48.59306 3.19593   1.000 30.50067 ?  98  THR   A CB  1 
ATOM   751  O OG1 . THR   A 1 98  ? 125.53868 -48.99671 4.56320   1.000 30.92234 ?  98  THR   A OG1 1 
ATOM   752  C CG2 . THR   A 1 98  ? 126.82091 -47.65254 3.03695   1.000 29.00417 ?  98  THR   A CG2 1 
ATOM   753  N N   . PRO   A 1 99  ? 124.52469 -46.26138 0.92689   1.000 30.23352 ?  99  PRO   A N   1 
ATOM   754  C CA  . PRO   A 1 99  ? 124.75668 -45.87164 -0.46255  1.000 30.91309 ?  99  PRO   A CA  1 
ATOM   755  C C   . PRO   A 1 99  ? 126.25349 -45.83909 -0.74625  1.000 29.55516 ?  99  PRO   A C   1 
ATOM   756  O O   . PRO   A 1 99  ? 127.08425 -45.92689 0.15788   1.000 30.29117 ?  99  PRO   A O   1 
ATOM   757  C CB  . PRO   A 1 99  ? 124.15510 -44.46349 -0.52072  1.000 28.26752 ?  99  PRO   A CB  1 
ATOM   758  C CG  . PRO   A 1 99  ? 124.50200 -43.90335 0.83358   1.000 29.12180 ?  99  PRO   A CG  1 
ATOM   759  C CD  . PRO   A 1 99  ? 124.41419 -45.08165 1.80540   1.000 30.26257 ?  99  PRO   A CD  1 
ATOM   760  N N   . LYS   A 1 100 ? 126.58296 -45.73731 -2.02986  1.000 29.31050 ?  100 LYS   A N   1 
ATOM   761  C CA  . LYS   A 1 100 ? 127.93912 -45.34903 -2.38340  1.000 29.49094 ?  100 LYS   A CA  1 
ATOM   762  C C   . LYS   A 1 100 ? 128.20036 -43.98150 -1.77457  1.000 28.60755 ?  100 LYS   A C   1 
ATOM   763  O O   . LYS   A 1 100 ? 127.39746 -43.05837 -1.95231  1.000 29.30260 ?  100 LYS   A O   1 
ATOM   764  C CB  . LYS   A 1 100 ? 128.11800 -45.31707 -3.90332  1.000 34.03366 ?  100 LYS   A CB  1 
ATOM   765  C CG  . LYS   A 1 100 ? 129.33220 -44.52520 -4.36287  1.000 38.20763 ?  100 LYS   A CG  1 
ATOM   766  C CD  . LYS   A 1 100 ? 129.80867 -44.90790 -5.75878  1.000 49.75235 ?  100 LYS   A CD  1 
ATOM   767  C CE  . LYS   A 1 100 ? 131.27960 -45.29790 -5.73757  1.000 59.76445 ?  100 LYS   A CE  1 
ATOM   768  N NZ  . LYS   A 1 100 ? 132.15216 -44.08709 -5.65777  1.000 56.67111 ?  100 LYS   A NZ  1 
ATOM   769  N N   . TYR   A 1 101 ? 129.29222 -43.84857 -1.02393  1.000 29.44207 ?  101 TYR   A N   1 
ATOM   770  C CA  . TYR   A 1 101 ? 129.51526 -42.60916 -0.29488  1.000 27.79960 ?  101 TYR   A CA  1 
ATOM   771  C C   . TYR   A 1 101 ? 130.99527 -42.26827 -0.20559  1.000 27.68107 ?  101 TYR   A C   1 
ATOM   772  O O   . TYR   A 1 101 ? 131.87321 -43.12083 -0.36420  1.000 27.83265 ?  101 TYR   A O   1 
ATOM   773  C CB  . TYR   A 1 101 ? 128.91663 -42.66193 1.12362   1.000 24.17339 ?  101 TYR   A CB  1 
ATOM   774  C CG  . TYR   A 1 101 ? 129.68873 -43.52822 2.10406   1.000 26.20626 ?  101 TYR   A CG  1 
ATOM   775  C CD1 . TYR   A 1 101 ? 129.39757 -44.88187 2.23532   1.000 28.37308 ?  101 TYR   A CD1 1 
ATOM   776  C CD2 . TYR   A 1 101 ? 130.67862 -42.98867 2.92712   1.000 26.56064 ?  101 TYR   A CD2 1 
ATOM   777  C CE1 . TYR   A 1 101 ? 130.08780 -45.68521 3.12646   1.000 27.63715 ?  101 TYR   A CE1 1 
ATOM   778  C CE2 . TYR   A 1 101 ? 131.37027 -43.78815 3.82612   1.000 27.47154 ?  101 TYR   A CE2 1 
ATOM   779  C CZ  . TYR   A 1 101 ? 131.06395 -45.13466 3.92254   1.000 29.05768 ?  101 TYR   A CZ  1 
ATOM   780  O OH  . TYR   A 1 101 ? 131.74055 -45.94319 4.80779   1.000 34.03913 ?  101 TYR   A OH  1 
ATOM   781  N N   . LYS   A 1 102 ? 131.24363 -40.98791 0.07154   1.000 26.47023 ?  102 LYS   A N   1 
ATOM   782  C CA  . LYS   A 1 102 ? 132.55969 -40.45051 0.38077   1.000 27.15785 ?  102 LYS   A CA  1 
ATOM   783  C C   . LYS   A 1 102 ? 132.41406 -39.46805 1.53040   1.000 23.30634 ?  102 LYS   A C   1 
ATOM   784  O O   . LYS   A 1 102 ? 131.35375 -38.87026 1.71441   1.000 22.85952 ?  102 LYS   A O   1 
ATOM   785  C CB  . LYS   A 1 102 ? 133.19072 -39.72615 -0.82104  1.000 30.12726 ?  102 LYS   A CB  1 
ATOM   786  C CG  . LYS   A 1 102 ? 133.64541 -40.64315 -1.93076  1.000 41.50351 ?  102 LYS   A CG  1 
ATOM   787  C CD  . LYS   A 1 102 ? 134.63767 -39.95425 -2.85330  1.000 46.87323 ?  102 LYS   A CD  1 
ATOM   788  C CE  . LYS   A 1 102 ? 134.09917 -39.80495 -4.26298  1.000 50.40897 ?  102 LYS   A CE  1 
ATOM   789  N NZ  . LYS   A 1 102 ? 135.02281 -38.98153 -5.08764  1.000 50.87718 ?  102 LYS   A NZ  1 
ATOM   790  N N   . PHE   A 1 103 ? 133.48443 -39.29914 2.29936   1.000 21.63840 ?  103 PHE   A N   1 
ATOM   791  C CA  . PHE   A 1 103 ? 133.59415 -38.20267 3.24884   1.000 21.05710 ?  103 PHE   A CA  1 
ATOM   792  C C   . PHE   A 1 103 ? 134.42905 -37.11181 2.59319   1.000 22.43740 ?  103 PHE   A C   1 
ATOM   793  O O   . PHE   A 1 103 ? 135.55336 -37.37578 2.15085   1.000 26.00966 ?  103 PHE   A O   1 
ATOM   794  C CB  . PHE   A 1 103 ? 134.25725 -38.64384 4.55782   1.000 21.08161 ?  103 PHE   A CB  1 
ATOM   795  C CG  . PHE   A 1 103 ? 133.40348 -39.53188 5.42134   1.000 21.49775 ?  103 PHE   A CG  1 
ATOM   796  C CD1 . PHE   A 1 103 ? 132.06403 -39.71450 5.15131   1.000 21.57747 ?  103 PHE   A CD1 1 
ATOM   797  C CD2 . PHE   A 1 103 ? 133.95107 -40.15616 6.54218   1.000 21.47936 ?  103 PHE   A CD2 1 
ATOM   798  C CE1 . PHE   A 1 103 ? 131.27971 -40.52834 5.94586   1.000 20.92287 ?  103 PHE   A CE1 1 
ATOM   799  C CE2 . PHE   A 1 103 ? 133.17322 -40.96650 7.34861   1.000 23.93049 ?  103 PHE   A CE2 1 
ATOM   800  C CZ  . PHE   A 1 103 ? 131.83496 -41.15209 7.05275   1.000 22.65390 ?  103 PHE   A CZ  1 
ATOM   801  N N   . VAL   A 1 104 ? 133.89790 -35.89210 2.53431   1.000 19.94530 ?  104 VAL   A N   1 
ATOM   802  C CA  . VAL   A 1 104 ? 134.65213 -34.77176 1.98456   1.000 21.11941 ?  104 VAL   A CA  1 
ATOM   803  C C   . VAL   A 1 104 ? 134.62309 -33.60509 2.96204   1.000 20.78086 ?  104 VAL   A C   1 
ATOM   804  O O   . VAL   A 1 104 ? 133.66218 -33.41439 3.71401   1.000 22.02733 ?  104 VAL   A O   1 
ATOM   805  C CB  . VAL   A 1 104 ? 134.11661 -34.31291 0.60245   1.000 26.56510 ?  104 VAL   A CB  1 
ATOM   806  C CG1 . VAL   A 1 104 ? 134.09611 -35.47189 -0.39468  1.000 24.55946 ?  104 VAL   A CG1 1 
ATOM   807  C CG2 . VAL   A 1 104 ? 132.75716 -33.69825 0.74702   1.000 29.50477 ?  104 VAL   A CG2 1 
ATOM   808  N N   . ARG   A 1 105 ? 135.69787 -32.82389 2.95335   1.000 21.58704 ?  105 ARG   A N   1 
ATOM   809  C CA  . ARG   A 1 105 ? 135.75534 -31.54891 3.65906   1.000 19.84417 ?  105 ARG   A CA  1 
ATOM   810  C C   . ARG   A 1 105 ? 135.55138 -30.44954 2.62660   1.000 24.09037 ?  105 ARG   A C   1 
ATOM   811  O O   . ARG   A 1 105 ? 136.39975 -30.25380 1.75150   1.000 24.31853 ?  105 ARG   A O   1 
ATOM   812  C CB  . ARG   A 1 105 ? 137.08679 -31.36703 4.38792   1.000 24.78399 ?  105 ARG   A CB  1 
ATOM   813  C CG  . ARG   A 1 105 ? 137.03998 -30.27935 5.45650   1.000 21.97237 ?  105 ARG   A CG  1 
ATOM   814  C CD  . ARG   A 1 105 ? 138.33123 -30.17063 6.24455   1.000 27.03475 ?  105 ARG   A CD  1 
ATOM   815  N NE  . ARG   A 1 105 ? 138.35592 -28.93696 7.02326   1.000 25.09650 ?  105 ARG   A NE  1 
ATOM   816  C CZ  . ARG   A 1 105 ? 137.72651 -28.77457 8.17960   1.000 25.65690 ?  105 ARG   A CZ  1 
ATOM   817  N NH1 . ARG   A 1 105 ? 137.04371 -29.76083 8.73875   1.000 20.19971 ?  105 ARG   A NH1 1 
ATOM   818  N NH2 . ARG   A 1 105 ? 137.78699 -27.59608 8.79129   1.000 19.52840 ?  105 ARG   A NH2 1 
ATOM   819  N N   . ILE   A 1 106 ? 134.42852 -29.73844 2.71726   1.000 20.81484 ?  106 ILE   A N   1 
ATOM   820  C CA  . ILE   A 1 106 ? 134.12003 -28.74186 1.69931   1.000 24.62589 ?  106 ILE   A CA  1 
ATOM   821  C C   . ILE   A 1 106 ? 134.81984 -27.42781 2.01584   1.000 24.27182 ?  106 ILE   A C   1 
ATOM   822  O O   . ILE   A 1 106 ? 135.25092 -27.16179 3.14036   1.000 23.16984 ?  106 ILE   A O   1 
ATOM   823  C CB  . ILE   A 1 106 ? 132.60802 -28.52171 1.54536   1.000 23.90430 ?  106 ILE   A CB  1 
ATOM   824  C CG1 . ILE   A 1 106 ? 132.00684 -28.12877 2.88403   1.000 21.58187 ?  106 ILE   A CG1 1 
ATOM   825  C CG2 . ILE   A 1 106 ? 131.93372 -29.72654 0.89448   1.000 26.40933 ?  106 ILE   A CG2 1 
ATOM   826  C CD1 . ILE   A 1 106 ? 130.68935 -27.39874 2.76533   1.000 25.05928 ?  106 ILE   A CD1 1 
ATOM   827  N N   . GLN   A 1 107 ? 134.89257 -26.57603 0.99801   1.000 23.88298 ?  107 GLN   A N   1 
ATOM   828  C CA  . GLN   A 1 107 ? 135.51537 -25.26753 1.06450   1.000 24.16678 ?  107 GLN   A CA  1 
ATOM   829  C C   . GLN   A 1 107 ? 134.47495 -24.20585 1.39310   1.000 21.33106 ?  107 GLN   A C   1 
ATOM   830  O O   . GLN   A 1 107 ? 133.29253 -24.36958 1.08593   1.000 22.21982 ?  107 GLN   A O   1 
ATOM   831  C CB  . GLN   A 1 107 ? 136.19163 -24.94040 -0.26482  1.000 24.42422 ?  107 GLN   A CB  1 
ATOM   832  C CG  . GLN   A 1 107 ? 137.34144 -25.87236 -0.59752  1.000 29.80074 ?  107 GLN   A CG  1 
ATOM   833  C CD  . GLN   A 1 107 ? 138.54641 -25.62888 0.29409   1.000 34.07149 ?  107 GLN   A CD  1 
ATOM   834  O OE1 . GLN   A 1 107 ? 139.01254 -24.49488 0.42642   1.000 37.37661 ?  107 GLN   A OE1 1 
ATOM   835  N NE2 . GLN   A 1 107 ? 139.05721 -26.69091 0.91106   1.000 38.67989 ?  107 GLN   A NE2 1 
ATOM   836  N N   . PRO   A 1 108 ? 134.86981 -23.12235 2.05301   1.000 23.18207 ?  108 PRO   A N   1 
ATOM   837  C CA  . PRO   A 1 108 ? 133.92000 -22.03070 2.28074   1.000 22.86653 ?  108 PRO   A CA  1 
ATOM   838  C C   . PRO   A 1 108 ? 133.38837 -21.53662 0.94410   1.000 20.03617 ?  108 PRO   A C   1 
ATOM   839  O O   . PRO   A 1 108 ? 134.11151 -21.50299 -0.05459  1.000 25.26811 ?  108 PRO   A O   1 
ATOM   840  C CB  . PRO   A 1 108 ? 134.76347 -20.96234 2.98583   1.000 24.64186 ?  108 PRO   A CB  1 
ATOM   841  C CG  . PRO   A 1 108 ? 136.18720 -21.29703 2.61338   1.000 25.82339 ?  108 PRO   A CG  1 
ATOM   842  C CD  . PRO   A 1 108 ? 136.22378 -22.79168 2.52405   1.000 23.26541 ?  108 PRO   A CD  1 
ATOM   843  N N   . GLY   A 1 109 ? 132.10729 -21.20185 0.92229   1.000 21.12248 ?  109 GLY   A N   1 
ATOM   844  C CA  . GLY   A 1 109 ? 131.43877 -20.79306 -0.29173  1.000 21.73774 ?  109 GLY   A CA  1 
ATOM   845  C C   . GLY   A 1 109 ? 130.72074 -21.90840 -1.01378  1.000 25.14749 ?  109 GLY   A C   1 
ATOM   846  O O   . GLY   A 1 109 ? 129.84550 -21.62845 -1.83824  1.000 24.37924 ?  109 GLY   A O   1 
ATOM   847  N N   . GLN   A 1 110 ? 131.07925 -23.16035 -0.73766  1.000 23.14521 ?  110 GLN   A N   1 
ATOM   848  C CA  . GLN   A 1 110 ? 130.41642 -24.32111 -1.31140  1.000 23.05810 ?  110 GLN   A CA  1 
ATOM   849  C C   . GLN   A 1 110 ? 129.08634 -24.56409 -0.60382  1.000 23.75607 ?  110 GLN   A C   1 
ATOM   850  O O   . GLN   A 1 110 ? 128.86954 -24.14102 0.53875   1.000 21.54200 ?  110 GLN   A O   1 
ATOM   851  C CB  . GLN   A 1 110 ? 131.31058 -25.55656 -1.18806  1.000 24.06968 ?  110 GLN   A CB  1 
ATOM   852  C CG  . GLN   A 1 110 ? 132.44293 -25.62175 -2.21616  1.000 28.86153 ?  110 GLN   A CG  1 
ATOM   853  C CD  . GLN   A 1 110 ? 132.01119 -25.15583 -3.58862  1.000 38.86587 ?  110 GLN   A CD  1 
ATOM   854  O OE1 . GLN   A 1 110 ? 131.10426 -25.73541 -4.18897  1.000 39.24242 ?  110 GLN   A OE1 1 
ATOM   855  N NE2 . GLN   A 1 110 ? 132.63788 -24.09200 -4.08597  1.000 44.24773 ?  110 GLN   A NE2 1 
ATOM   856  N N   . THR   A 1 111 ? 128.18868 -25.25887 -1.29589  1.000 21.96114 ?  111 THR   A N   1 
ATOM   857  C CA  . THR   A 1 111 ? 126.84838 -25.50046 -0.78675  1.000 22.00718 ?  111 THR   A CA  1 
ATOM   858  C C   . THR   A 1 111 ? 126.61788 -26.98849 -0.57699  1.000 19.79899 ?  111 THR   A C   1 
ATOM   859  O O   . THR   A 1 111 ? 127.33911 -27.83587 -1.11921  1.000 20.98996 ?  111 THR   A O   1 
ATOM   860  C CB  . THR   A 1 111 ? 125.77214 -24.96849 -1.73994  1.000 22.04555 ?  111 THR   A CB  1 
ATOM   861  O OG1 . THR   A 1 111 ? 125.99741 -25.49994 -3.05007  1.000 22.71744 ?  111 THR   A OG1 1 
ATOM   862  C CG2 . THR   A 1 111 ? 125.79115 -23.45098 -1.78246  1.000 22.57760 ?  111 THR   A CG2 1 
ATOM   863  N N   . PHE   A 1 112 ? 125.57631 -27.29338 0.19977   1.000 16.48263 ?  112 PHE   A N   1 
ATOM   864  C CA  . PHE   A 1 112 ? 125.21395 -28.67280 0.48485   1.000 20.49737 ?  112 PHE   A CA  1 
ATOM   865  C C   . PHE   A 1 112 ? 123.79719 -28.71147 1.03914   1.000 18.83417 ?  112 PHE   A C   1 
ATOM   866  O O   . PHE   A 1 112 ? 123.26139 -27.70156 1.49286   1.000 21.46977 ?  112 PHE   A O   1 
ATOM   867  C CB  . PHE   A 1 112 ? 126.21233 -29.31863 1.46629   1.000 18.21314 ?  112 PHE   A CB  1 
ATOM   868  C CG  . PHE   A 1 112 ? 126.36257 -28.58380 2.77818   1.000 20.35813 ?  112 PHE   A CG  1 
ATOM   869  C CD1 . PHE   A 1 112 ? 127.27537 -27.54927 2.91536   1.000 22.46649 ?  112 PHE   A CD1 1 
ATOM   870  C CD2 . PHE   A 1 112 ? 125.64071 -28.96911 3.89864   1.000 17.66429 ?  112 PHE   A CD2 1 
ATOM   871  C CE1 . PHE   A 1 112 ? 127.42886 -26.88888 4.13705   1.000 23.08517 ?  112 PHE   A CE1 1 
ATOM   872  C CE2 . PHE   A 1 112 ? 125.79305 -28.30726 5.11639   1.000 18.83477 ?  112 PHE   A CE2 1 
ATOM   873  C CZ  . PHE   A 1 112 ? 126.69149 -27.27489 5.23244   1.000 19.29171 ?  112 PHE   A CZ  1 
ATOM   874  N N   . SER   A 1 113 ? 123.18762 -29.88939 0.96248   1.000 15.39802 ?  113 SER   A N   1 
ATOM   875  C CA  . SER   A 1 113 ? 121.85885 -30.11419 1.50155   1.000 15.72398 ?  113 SER   A CA  1 
ATOM   876  C C   . SER   A 1 113 ? 121.97825 -30.61245 2.93272   1.000 17.13597 ?  113 SER   A C   1 
ATOM   877  O O   . SER   A 1 113 ? 122.86996 -31.40209 3.24137   1.000 21.07004 ?  113 SER   A O   1 
ATOM   878  C CB  . SER   A 1 113 ? 121.11655 -31.15127 0.66850   1.000 21.22771 ?  113 SER   A CB  1 
ATOM   879  O OG  . SER   A 1 113 ? 120.89781 -30.67814 -0.64108  1.000 22.13504 ?  113 SER   A OG  1 
ATOM   880  N N   . VAL   A 1 114 ? 121.06014 -30.17026 3.78776   1.000 17.45360 ?  114 VAL   A N   1 
ATOM   881  C CA  . VAL   A 1 114 ? 120.98192 -30.61836 5.17612   1.000 17.31810 ?  114 VAL   A CA  1 
ATOM   882  C C   . VAL   A 1 114 ? 119.69398 -31.40161 5.35108   1.000 18.57045 ?  114 VAL   A C   1 
ATOM   883  O O   . VAL   A 1 114 ? 118.61074 -30.91250 5.00772   1.000 19.23494 ?  114 VAL   A O   1 
ATOM   884  C CB  . VAL   A 1 114 ? 121.03045 -29.43763 6.16082   1.000 19.02714 ?  114 VAL   A CB  1 
ATOM   885  C CG1 . VAL   A 1 114 ? 120.69914 -29.92177 7.57991   1.000 20.76031 ?  114 VAL   A CG1 1 
ATOM   886  C CG2 . VAL   A 1 114 ? 122.39250 -28.74874 6.10028   1.000 18.38405 ?  114 VAL   A CG2 1 
ATOM   887  N N   . LEU   A 1 115 ? 119.80692 -32.61512 5.88143   1.000 15.91185 ?  115 LEU   A N   1 
ATOM   888  C CA  . LEU   A 1 115 ? 118.65535 -33.40224 6.30822   1.000 18.75856 ?  115 LEU   A CA  1 
ATOM   889  C C   . LEU   A 1 115 ? 118.52055 -33.25030 7.81776   1.000 20.79412 ?  115 LEU   A C   1 
ATOM   890  O O   . LEU   A 1 115 ? 119.24224 -33.89673 8.58506   1.000 21.59553 ?  115 LEU   A O   1 
ATOM   891  C CB  . LEU   A 1 115 ? 118.81466 -34.86175 5.90538   1.000 19.21800 ?  115 LEU   A CB  1 
ATOM   892  C CG  . LEU   A 1 115 ? 117.64738 -35.76143 6.30921   1.000 19.76894 ?  115 LEU   A CG  1 
ATOM   893  C CD1 . LEU   A 1 115 ? 116.34787 -35.30918 5.64276   1.000 21.64845 ?  115 LEU   A CD1 1 
ATOM   894  C CD2 . LEU   A 1 115 ? 117.95839 -37.21120 5.97634   1.000 23.47986 ?  115 LEU   A CD2 1 
ATOM   895  N N   . ALA   A 1 116 ? 117.60426 -32.38042 8.23425   1.000 18.99615 ?  116 ALA   A N   1 
ATOM   896  C CA  . ALA   A 1 116 ? 117.36006 -32.11731 9.64715   1.000 18.86592 ?  116 ALA   A CA  1 
ATOM   897  C C   . ALA   A 1 116 ? 116.57697 -33.26177 10.26728  1.000 23.12006 ?  116 ALA   A C   1 
ATOM   898  O O   . ALA   A 1 116 ? 115.56569 -33.70509 9.71975   1.000 23.27093 ?  116 ALA   A O   1 
ATOM   899  C CB  . ALA   A 1 116 ? 116.58886 -30.80866 9.81624   1.000 21.54658 ?  116 ALA   A CB  1 
ATOM   900  N N   . CYS   A 1 117 ? 117.03979 -33.72711 11.42954  1.000 19.91038 ?  117 CYS   A N   1 
ATOM   901  C CA  . CYS   A 1 117 ? 116.56591 -34.97789 12.00274  1.000 22.02688 ?  117 CYS   A CA  1 
ATOM   902  C C   . CYS   A 1 117 ? 116.38725 -34.79683 13.50312  1.000 28.67214 ?  117 CYS   A C   1 
ATOM   903  O O   . CYS   A 1 117 ? 117.10352 -34.00906 14.12813  1.000 25.88298 ?  117 CYS   A O   1 
ATOM   904  C CB  . CYS   A 1 117 ? 117.59167 -36.08652 11.76212  1.000 26.97388 ?  117 CYS   A CB  1 
ATOM   905  S SG  . CYS   A 1 117 ? 117.53137 -36.81946 10.12931  1.000 30.26220 ?  117 CYS   A SG  1 
ATOM   906  N N   . TYR   A 1 118 ? 115.45593 -35.56031 14.08222  1.000 27.37364 ?  118 TYR   A N   1 
ATOM   907  C CA  . TYR   A 1 118 ? 115.23789 -35.60163 15.52861  1.000 29.81033 ?  118 TYR   A CA  1 
ATOM   908  C C   . TYR   A 1 118 ? 114.91118 -37.03390 15.92573  1.000 31.51137 ?  118 TYR   A C   1 
ATOM   909  O O   . TYR   A 1 118 ? 114.10579 -37.69398 15.26023  1.000 29.57737 ?  118 TYR   A O   1 
ATOM   910  C CB  . TYR   A 1 118 ? 114.11551 -34.62983 15.96103  1.000 29.46057 ?  118 TYR   A CB  1 
ATOM   911  C CG  . TYR   A 1 118 ? 114.44128 -33.19974 15.59078  1.000 30.87947 ?  118 TYR   A CG  1 
ATOM   912  C CD1 . TYR   A 1 118 ? 114.09951 -32.67611 14.34314  1.000 31.61199 ?  118 TYR   A CD1 1 
ATOM   913  C CD2 . TYR   A 1 118 ? 115.14863 -32.38882 16.47076  1.000 31.24330 ?  118 TYR   A CD2 1 
ATOM   914  C CE1 . TYR   A 1 118 ? 114.44085 -31.37666 13.99884  1.000 29.41175 ?  118 TYR   A CE1 1 
ATOM   915  C CE2 . TYR   A 1 118 ? 115.48563 -31.09584 16.14353  1.000 29.46121 ?  118 TYR   A CE2 1 
ATOM   916  C CZ  . TYR   A 1 118 ? 115.13858 -30.59347 14.90463  1.000 31.62084 ?  118 TYR   A CZ  1 
ATOM   917  O OH  . TYR   A 1 118 ? 115.48407 -29.30084 14.58405  1.000 30.77098 ?  118 TYR   A OH  1 
ATOM   918  N N   . ASN   A 1 119 ? 115.56253 -37.52015 16.98869  1.000 31.36294 ?  119 ASN   A N   1 
ATOM   919  C CA  . ASN   A 1 119 ? 115.37040 -38.88816 17.48283  1.000 30.91025 ?  119 ASN   A CA  1 
ATOM   920  C C   . ASN   A 1 119 ? 115.63847 -39.93875 16.40578  1.000 32.10607 ?  119 ASN   A C   1 
ATOM   921  O O   . ASN   A 1 119 ? 115.06405 -41.03178 16.43915  1.000 34.96494 ?  119 ASN   A O   1 
ATOM   922  C CB  . ASN   A 1 119 ? 113.96530 -39.06990 18.07142  1.000 33.83473 ?  119 ASN   A CB  1 
ATOM   923  C CG  . ASN   A 1 119 ? 113.84816 -38.51415 19.47964  1.000 40.34227 ?  119 ASN   A CG  1 
ATOM   924  O OD1 . ASN   A 1 119 ? 114.82007 -38.50469 20.23794  1.000 43.70231 ?  119 ASN   A OD1 1 
ATOM   925  N ND2 . ASN   A 1 119 ? 112.66485 -38.02834 19.82801  1.000 50.26373 ?  119 ASN   A ND2 1 
ATOM   926  N N   . GLY   A 1 120 ? 116.51632 -39.62507 15.45017  1.000 29.44521 ?  120 GLY   A N   1 
ATOM   927  C CA  . GLY   A 1 120 ? 116.82587 -40.54282 14.37179  1.000 28.14428 ?  120 GLY   A CA  1 
ATOM   928  C C   . GLY   A 1 120 ? 115.86392 -40.52806 13.20324  1.000 31.97527 ?  120 GLY   A C   1 
ATOM   929  O O   . GLY   A 1 120 ? 115.99373 -41.37098 12.30617  1.000 31.07458 ?  120 GLY   A O   1 
ATOM   930  N N   . SER   A 1 121 ? 114.90999 -39.59858 13.17299  1.000 30.48776 ?  121 SER   A N   1 
ATOM   931  C CA  . SER   A 1 121 ? 113.88845 -39.58299 12.13936  1.000 32.75745 ?  121 SER   A CA  1 
ATOM   932  C C   . SER   A 1 121 ? 113.96085 -38.29520 11.32856  1.000 32.79072 ?  121 SER   A C   1 
ATOM   933  O O   . SER   A 1 121 ? 113.92562 -37.19730 11.90347  1.000 27.84972 ?  121 SER   A O   1 
ATOM   934  C CB  . SER   A 1 121 ? 112.49334 -39.74029 12.74904  1.000 34.44896 ?  121 SER   A CB  1 
ATOM   935  O OG  . SER   A 1 121 ? 112.36502 -41.01449 13.35459  1.000 36.36955 ?  121 SER   A OG  1 
ATOM   936  N N   . PRO   A 1 122 ? 114.06815 -38.38592 10.00574  1.000 31.52938 ?  122 PRO   A N   1 
ATOM   937  C CA  . PRO   A 1 122 ? 114.17491 -37.17060 9.18785   1.000 30.13204 ?  122 PRO   A CA  1 
ATOM   938  C C   . PRO   A 1 122 ? 112.95477 -36.27550 9.32900   1.000 31.76075 ?  122 PRO   A C   1 
ATOM   939  O O   . PRO   A 1 122 ? 111.81115 -36.73763 9.34369   1.000 35.07632 ?  122 PRO   A O   1 
ATOM   940  C CB  . PRO   A 1 122 ? 114.31901 -37.70436 7.75815   1.000 32.79810 ?  122 PRO   A CB  1 
ATOM   941  C CG  . PRO   A 1 122 ? 114.59011 -39.15931 7.86752   1.000 33.71144 ?  122 PRO   A CG  1 
ATOM   942  C CD  . PRO   A 1 122 ? 114.35888 -39.62446 9.26246   1.000 34.15397 ?  122 PRO   A CD  1 
ATOM   943  N N   . SER   A 1 123 ? 113.21372 -34.97616 9.43547   1.000 29.11378 ?  123 SER   A N   1 
ATOM   944  C CA  . SER   A 1 123 ? 112.17076 -33.96991 9.55811   1.000 30.85872 ?  123 SER   A CA  1 
ATOM   945  C C   . SER   A 1 123 ? 112.01025 -33.10605 8.31255   1.000 29.30917 ?  123 SER   A C   1 
ATOM   946  O O   . SER   A 1 123 ? 110.88031 -32.82001 7.91014   1.000 30.65805 ?  123 SER   A O   1 
ATOM   947  C CB  . SER   A 1 123 ? 112.46252 -33.08216 10.77536  1.000 33.50691 ?  123 SER   A CB  1 
ATOM   948  O OG  . SER   A 1 123 ? 111.68539 -31.90528 10.76514  1.000 42.65225 ?  123 SER   A OG  1 
ATOM   949  N N   . GLY   A 1 124 ? 113.10200 -32.69500 7.67820   1.000 24.83377 ?  124 GLY   A N   1 
ATOM   950  C CA  . GLY   A 1 124 ? 113.01781 -31.83479 6.50731   1.000 22.08355 ?  124 GLY   A CA  1 
ATOM   951  C C   . GLY   A 1 124 ? 114.37806 -31.67933 5.86431   1.000 21.63593 ?  124 GLY   A C   1 
ATOM   952  O O   . GLY   A 1 124 ? 115.40327 -32.07951 6.42089   1.000 21.31902 ?  124 GLY   A O   1 
ATOM   953  N N   . VAL   A 1 125 ? 114.37961 -31.09817 4.66382   1.000 19.02351 ?  125 VAL   A N   1 
ATOM   954  C CA  . VAL   A 1 125 ? 115.61625 -30.91597 3.91889   1.000 20.03651 ?  125 VAL   A CA  1 
ATOM   955  C C   . VAL   A 1 125 ? 115.70218 -29.47766 3.42094   1.000 18.45587 ?  125 VAL   A C   1 
ATOM   956  O O   . VAL   A 1 125 ? 114.69791 -28.88420 3.01543   1.000 20.53515 ?  125 VAL   A O   1 
ATOM   957  C CB  . VAL   A 1 125 ? 115.72756 -31.92916 2.75794   1.000 23.33304 ?  125 VAL   A CB  1 
ATOM   958  C CG1 . VAL   A 1 125 ? 114.55985 -31.78219 1.79144   1.000 27.70268 ?  125 VAL   A CG1 1 
ATOM   959  C CG2 . VAL   A 1 125 ? 117.08307 -31.81776 2.06851   1.000 23.73009 ?  125 VAL   A CG2 1 
ATOM   960  N N   . TYR   A 1 126 ? 116.89422 -28.89582 3.50724   1.000 20.69877 ?  126 TYR   A N   1 
ATOM   961  C CA  . TYR   A 1 126 ? 117.10806 -27.57227 2.94201   1.000 22.03734 ?  126 TYR   A CA  1 
ATOM   962  C C   . TYR   A 1 126 ? 118.55307 -27.41975 2.49368   1.000 20.96598 ?  126 TYR   A C   1 
ATOM   963  O O   . TYR   A 1 126 ? 119.43757 -28.19199 2.86569   1.000 19.42865 ?  126 TYR   A O   1 
ATOM   964  C CB  . TYR   A 1 126 ? 116.74488 -26.46292 3.92672   1.000 22.60941 ?  126 TYR   A CB  1 
ATOM   965  C CG  . TYR   A 1 126 ? 117.40720 -26.59033 5.28054   1.000 23.77143 ?  126 TYR   A CG  1 
ATOM   966  C CD1 . TYR   A 1 126 ? 118.66143 -26.03269 5.51670   1.000 27.92064 ?  126 TYR   A CD1 1 
ATOM   967  C CD2 . TYR   A 1 126 ? 116.76272 -27.23105 6.32866   1.000 25.00579 ?  126 TYR   A CD2 1 
ATOM   968  C CE1 . TYR   A 1 126 ? 119.26131 -26.13929 6.75321   1.000 26.72012 ?  126 TYR   A CE1 1 
ATOM   969  C CE2 . TYR   A 1 126 ? 117.35890 -27.34158 7.57631   1.000 28.08556 ?  126 TYR   A CE2 1 
ATOM   970  C CZ  . TYR   A 1 126 ? 118.60265 -26.79434 7.77674   1.000 25.53378 ?  126 TYR   A CZ  1 
ATOM   971  O OH  . TYR   A 1 126 ? 119.19791 -26.89348 9.01738   1.000 32.36013 ?  126 TYR   A OH  1 
ATOM   972  N N   . GLN   A 1 127 ? 118.77795 -26.37342 1.71310   1.000 22.17859 ?  127 GLN   A N   1 
ATOM   973  C CA  . GLN   A 1 127 ? 120.05507 -26.08086 1.08303   1.000 22.76268 ?  127 GLN   A CA  1 
ATOM   974  C C   . GLN   A 1 127 ? 120.73802 -24.94504 1.82620   1.000 26.70199 ?  127 GLN   A C   1 
ATOM   975  O O   . GLN   A 1 127 ? 120.08473 -23.99096 2.24900   1.000 29.64401 ?  127 GLN   A O   1 
ATOM   976  C CB  . GLN   A 1 127 ? 119.81833 -25.68706 -0.37870  1.000 26.26372 ?  127 GLN   A CB  1 
ATOM   977  C CG  . GLN   A 1 127 ? 121.01129 -25.63034 -1.29463  1.000 28.78825 ?  127 GLN   A CG  1 
ATOM   978  C CD  . GLN   A 1 127 ? 121.59413 -26.98408 -1.60785  1.000 23.45435 ?  127 GLN   A CD  1 
ATOM   979  O OE1 . GLN   A 1 127 ? 121.04329 -28.01920 -1.23262  1.000 27.51362 ?  127 GLN   A OE1 1 
ATOM   980  N NE2 . GLN   A 1 127 ? 122.67260 -26.98610 -2.37439  1.000 26.38606 ?  127 GLN   A NE2 1 
ATOM   981  N N   . CYS   A 1 128 ? 122.05149 -25.03837 1.98069   1.000 24.72472 ?  128 CYS   A N   1 
ATOM   982  C CA  . CYS   A 1 128 ? 122.77087 -23.92896 2.58011   1.000 27.96624 ?  128 CYS   A CA  1 
ATOM   983  C C   . CYS   A 1 128 ? 124.20787 -23.92448 2.08838   1.000 23.15856 ?  128 CYS   A C   1 
ATOM   984  O O   . CYS   A 1 128 ? 124.69007 -24.88013 1.47797   1.000 22.77405 ?  128 CYS   A O   1 
ATOM   985  C CB  . CYS   A 1 128 ? 122.73844 -23.99733 4.09677   1.000 33.86588 ?  128 CYS   A CB  1 
ATOM   986  S SG  . CYS   A 1 128 ? 123.71477 -25.33720 4.64884   1.000 34.63740 ?  128 CYS   A SG  1 
ATOM   987  N N   . ALA   A 1 129 ? 124.88867 -22.82792 2.38194   1.000 23.63217 ?  129 ALA   A N   1 
ATOM   988  C CA  . ALA   A 1 129 ? 126.27554 -22.63602 2.00569   1.000 21.69039 ?  129 ALA   A CA  1 
ATOM   989  C C   . ALA   A 1 129 ? 127.12720 -22.61349 3.26576   1.000 21.83484 ?  129 ALA   A C   1 
ATOM   990  O O   . ALA   A 1 129 ? 126.68780 -22.13339 4.31010   1.000 21.89908 ?  129 ALA   A O   1 
ATOM   991  C CB  . ALA   A 1 129 ? 126.45528 -21.32874 1.22677   1.000 24.23929 ?  129 ALA   A CB  1 
ATOM   992  N N   . MET   A 1 130 ? 128.33525 -23.16067 3.16829   1.000 18.03552 ?  130 MET   A N   1 
ATOM   993  C CA  . MET   A 1 130 ? 129.33612 -22.97898 4.22289   1.000 19.66137 ?  130 MET   A CA  1 
ATOM   994  C C   . MET   A 1 130 ? 129.82755 -21.53563 4.10948   1.000 20.61768 ?  130 MET   A C   1 
ATOM   995  O O   . MET   A 1 130 ? 130.39168 -21.15642 3.07680   1.000 21.66400 ?  130 MET   A O   1 
ATOM   996  C CB  . MET   A 1 130 ? 130.47628 -23.98260 4.03491   1.000 21.50939 ?  130 MET   A CB  1 
ATOM   997  C CG  . MET   A 1 130 ? 131.68748 -23.83610 4.99004   1.000 19.38345 ?  130 MET   A CG  1 
ATOM   998  S SD  . MET   A 1 130 ? 131.18737 -24.14266 6.68257   1.000 23.83783 ?  130 MET   A SD  1 
ATOM   999  C CE  . MET   A 1 130 ? 130.35431 -25.71287 6.51146   1.000 22.74447 ?  130 MET   A CE  1 
ATOM   1000 N N   . ARG   A 1 131 ? 129.55752 -20.70556 5.12010   1.000 18.13811 ?  131 ARG   A N   1 
ATOM   1001 C CA  . ARG   A 1 131 ? 129.92335 -19.29720 5.04241   1.000 19.66791 ?  131 ARG   A CA  1 
ATOM   1002 C C   . ARG   A 1 131 ? 131.44136 -19.13339 4.99661   1.000 18.65650 ?  131 ARG   A C   1 
ATOM   1003 O O   . ARG   A 1 131 ? 132.19571 -20.01703 5.43155   1.000 18.24057 ?  131 ARG   A O   1 
ATOM   1004 C CB  . ARG   A 1 131 ? 129.37657 -18.50624 6.23896   1.000 18.96376 ?  131 ARG   A CB  1 
ATOM   1005 C CG  . ARG   A 1 131 ? 127.85241 -18.54177 6.50504   1.000 21.93112 ?  131 ARG   A CG  1 
ATOM   1006 C CD  . ARG   A 1 131 ? 126.97353 -18.04739 5.35767   1.000 21.59838 ?  131 ARG   A CD  1 
ATOM   1007 N NE  . ARG   A 1 131 ? 127.41622 -16.75740 4.84098   1.000 23.18614 ?  131 ARG   A NE  1 
ATOM   1008 C CZ  . ARG   A 1 131 ? 127.14264 -16.31987 3.62055   1.000 25.18021 ?  131 ARG   A CZ  1 
ATOM   1009 N NH1 . ARG   A 1 131 ? 126.29301 -16.96497 2.83248   1.000 21.54781 ?  131 ARG   A NH1 1 
ATOM   1010 N NH2 . ARG   A 1 131 ? 127.72082 -15.20230 3.18769   1.000 24.82959 ?  131 ARG   A NH2 1 
ATOM   1011 N N   . PRO   A 1 132 ? 131.92102 -18.00283 4.48582   1.000 19.39339 ?  132 PRO   A N   1 
ATOM   1012 C CA  . PRO   A 1 132 ? 133.36050 -17.72952 4.57499   1.000 20.12869 ?  132 PRO   A CA  1 
ATOM   1013 C C   . PRO   A 1 132 ? 133.89585 -17.79487 5.99490   1.000 20.01186 ?  132 PRO   A C   1 
ATOM   1014 O O   . PRO   A 1 132 ? 135.07849 -18.11801 6.17960   1.000 20.54799 ?  132 PRO   A O   1 
ATOM   1015 C CB  . PRO   A 1 132 ? 133.47770 -16.32427 3.97929   1.000 24.49865 ?  132 PRO   A CB  1 
ATOM   1016 C CG  . PRO   A 1 132 ? 132.36757 -16.29462 2.95562   1.000 22.39243 ?  132 PRO   A CG  1 
ATOM   1017 C CD  . PRO   A 1 132 ? 131.23194 -17.06476 3.57614   1.000 21.20698 ?  132 PRO   A CD  1 
ATOM   1018 N N   . ASN   A 1 133 ? 133.07354 -17.50418 7.00793   1.000 19.81872 ?  133 ASN   A N   1 
ATOM   1019 C CA  . ASN   A 1 133 ? 133.52617 -17.64259 8.39379   1.000 19.85434 ?  133 ASN   A CA  1 
ATOM   1020 C C   . ASN   A 1 133 ? 133.22727 -19.02340 8.97293   1.000 19.73159 ?  133 ASN   A C   1 
ATOM   1021 O O   . ASN   A 1 133 ? 133.26807 -19.19593 10.19815  1.000 19.18564 ?  133 ASN   A O   1 
ATOM   1022 C CB  . ASN   A 1 133 ? 132.91915 -16.55079 9.28251   1.000 20.69682 ?  133 ASN   A CB  1 
ATOM   1023 C CG  . ASN   A 1 133 ? 131.41757 -16.71029 9.51313   1.000 22.18253 ?  133 ASN   A CG  1 
ATOM   1024 O OD1 . ASN   A 1 133 ? 130.77132 -17.61220 8.98699   1.000 22.13548 ?  133 ASN   A OD1 1 
ATOM   1025 N ND2 . ASN   A 1 133 ? 130.86466 -15.83103 10.34113  1.000 20.17131 ?  133 ASN   A ND2 1 
ATOM   1026 N N   . PHE   A 1 134 ? 132.90099 -19.99605 8.11856   1.000 17.43865 ?  134 PHE   A N   1 
ATOM   1027 C CA  . PHE   A 1 134 ? 132.75025 -21.40768 8.49735   1.000 20.09415 ?  134 PHE   A CA  1 
ATOM   1028 C C   . PHE   A 1 134 ? 131.58243 -21.64232 9.45282   1.000 20.82358 ?  134 PHE   A C   1 
ATOM   1029 O O   . PHE   A 1 134 ? 131.61024 -22.57069 10.26440  1.000 22.56639 ?  134 PHE   A O   1 
ATOM   1030 C CB  . PHE   A 1 134 ? 134.04179 -21.97062 9.10167   1.000 19.36994 ?  134 PHE   A CB  1 
ATOM   1031 C CG  . PHE   A 1 134 ? 135.15206 -22.14386 8.10223   1.000 19.79499 ?  134 PHE   A CG  1 
ATOM   1032 C CD1 . PHE   A 1 134 ? 135.12109 -23.17751 7.17955   1.000 22.01901 ?  134 PHE   A CD1 1 
ATOM   1033 C CD2 . PHE   A 1 134 ? 136.21420 -21.26258 8.07573   1.000 20.77901 ?  134 PHE   A CD2 1 
ATOM   1034 C CE1 . PHE   A 1 134 ? 136.13776 -23.32535 6.24550   1.000 23.46209 ?  134 PHE   A CE1 1 
ATOM   1035 C CE2 . PHE   A 1 134 ? 137.23222 -21.40850 7.15799   1.000 25.22252 ?  134 PHE   A CE2 1 
ATOM   1036 C CZ  . PHE   A 1 134 ? 137.19381 -22.44226 6.23979   1.000 25.02373 ?  134 PHE   A CZ  1 
ATOM   1037 N N   . THR   A 1 135 ? 130.55340 -20.80815 9.38767   1.000 19.69604 ?  135 THR   A N   1 
ATOM   1038 C CA  . THR   A 1 135 ? 129.27252 -21.11569 10.00699  1.000 21.26508 ?  135 THR   A CA  1 
ATOM   1039 C C   . THR   A 1 135 ? 128.27398 -21.43280 8.91141   1.000 19.78555 ?  135 THR   A C   1 
ATOM   1040 O O   . THR   A 1 135 ? 128.53875 -21.23420 7.72409   1.000 21.29485 ?  135 THR   A O   1 
ATOM   1041 C CB  . THR   A 1 135 ? 128.75326 -19.95248 10.86053  1.000 20.16876 ?  135 THR   A CB  1 
ATOM   1042 O OG1 . THR   A 1 135 ? 128.52139 -18.82070 10.01960  1.000 20.32642 ?  135 THR   A OG1 1 
ATOM   1043 C CG2 . THR   A 1 135 ? 129.77049 -19.57122 11.94379  1.000 20.33459 ?  135 THR   A CG2 1 
ATOM   1044 N N   . ILE   A 1 136 ? 127.12199 -21.94050 9.31602   1.000 21.91791 ?  136 ILE   A N   1 
ATOM   1045 C CA  . ILE   A 1 136 ? 126.00228 -22.09162 8.39949   1.000 19.25285 ?  136 ILE   A CA  1 
ATOM   1046 C C   . ILE   A 1 136 ? 124.77718 -21.46359 9.04818   1.000 23.50341 ?  136 ILE   A C   1 
ATOM   1047 O O   . ILE   A 1 136 ? 124.66238 -21.39526 10.27374  1.000 21.14967 ?  136 ILE   A O   1 
ATOM   1048 C CB  . ILE   A 1 136 ? 125.74987 -23.56674 8.00725   1.000 24.06921 ?  136 ILE   A CB  1 
ATOM   1049 C CG1 . ILE   A 1 136 ? 125.18137 -24.36879 9.16682   1.000 21.13747 ?  136 ILE   A CG1 1 
ATOM   1050 C CG2 . ILE   A 1 136 ? 127.03630 -24.24369 7.49133   1.000 21.71936 ?  136 ILE   A CG2 1 
ATOM   1051 C CD1 . ILE   A 1 136 ? 124.84445 -25.81745 8.74117   1.000 20.83793 ?  136 ILE   A CD1 1 
ATOM   1052 N N   . LYS   A 1 137 ? 123.87522 -20.94816 8.21763   1.000 24.67123 ?  137 LYS   A N   1 
ATOM   1053 C CA  . LYS   A 1 137 ? 122.62307 -20.38929 8.71540   1.000 26.49386 ?  137 LYS   A CA  1 
ATOM   1054 C C   . LYS   A 1 137 ? 121.55991 -21.46123 8.52137   1.000 26.88252 ?  137 LYS   A C   1 
ATOM   1055 O O   . LYS   A 1 137 ? 120.93539 -21.56586 7.46426   1.000 26.50494 ?  137 LYS   A O   1 
ATOM   1056 C CB  . LYS   A 1 137 ? 122.25600 -19.09464 8.00597   1.000 28.44763 ?  137 LYS   A CB  1 
ATOM   1057 C CG  . LYS   A 1 137 ? 123.36226 -18.08121 7.86134   1.000 28.89399 ?  137 LYS   A CG  1 
ATOM   1058 C CD  . LYS   A 1 137 ? 123.01649 -17.15340 6.69618   1.000 38.04563 ?  137 LYS   A CD  1 
ATOM   1059 C CE  . LYS   A 1 137 ? 123.51164 -15.73073 6.89914   1.000 44.80031 ?  137 LYS   A CE  1 
ATOM   1060 N NZ  . LYS   A 1 137 ? 123.67547 -15.03171 5.58304   1.000 44.02529 ?  137 LYS   A NZ  1 
ATOM   1061 N N   . GLY   A 1 138 ? 121.36113 -22.27850 9.55333   1.000 25.19974 ?  138 GLY   A N   1 
ATOM   1062 C CA  . GLY   A 1 138 ? 120.48217 -23.41144 9.47395   1.000 25.11733 ?  138 GLY   A CA  1 
ATOM   1063 C C   . GLY   A 1 138 ? 119.18195 -23.21986 10.21110  1.000 27.39925 ?  138 GLY   A C   1 
ATOM   1064 O O   . GLY   A 1 138 ? 118.76307 -22.08668 10.52034  1.000 28.57620 ?  138 GLY   A O   1 
ATOM   1065 N N   . SER   A 1 139 ? 118.50206 -24.33579 10.46628  1.000 24.75130 ?  139 SER   A N   1 
ATOM   1066 C CA  . SER   A 1 139 ? 117.29169 -24.43254 11.27504  1.000 26.81380 ?  139 SER   A CA  1 
ATOM   1067 C C   . SER   A 1 139 ? 117.45204 -25.70768 12.09726  1.000 27.42245 ?  139 SER   A C   1 
ATOM   1068 O O   . SER   A 1 139 ? 117.25355 -26.81233 11.58274  1.000 26.86794 ?  139 SER   A O   1 
ATOM   1069 C CB  . SER   A 1 139 ? 116.03553 -24.48296 10.41316  1.000 29.94332 ?  139 SER   A CB  1 
ATOM   1070 O OG  . SER   A 1 139 ? 114.87238 -24.60025 11.21810  1.000 30.56792 ?  139 SER   A OG  1 
ATOM   1071 N N   . PHE   A 1 140 ? 117.82652 -25.55481 13.36449  1.000 26.66684 ?  140 PHE   A N   1 
ATOM   1072 C CA  . PHE   A 1 140 ? 118.23690 -26.67424 14.21092  1.000 28.11921 ?  140 PHE   A CA  1 
ATOM   1073 C C   . PHE   A 1 140 ? 117.69340 -26.44290 15.61146  1.000 30.68007 ?  140 PHE   A C   1 
ATOM   1074 O O   . PHE   A 1 140 ? 117.97727 -25.40341 16.21119  1.000 31.93346 ?  140 PHE   A O   1 
ATOM   1075 C CB  . PHE   A 1 140 ? 119.76697 -26.80505 14.28460  1.000 25.03850 ?  140 PHE   A CB  1 
ATOM   1076 C CG  . PHE   A 1 140 ? 120.44559 -27.26556 13.00171  1.000 23.88411 ?  140 PHE   A CG  1 
ATOM   1077 C CD1 . PHE   A 1 140 ? 120.24499 -28.53865 12.50600  1.000 22.32822 ?  140 PHE   A CD1 1 
ATOM   1078 C CD2 . PHE   A 1 140 ? 121.31727 -26.42735 12.32413  1.000 23.07942 ?  140 PHE   A CD2 1 
ATOM   1079 C CE1 . PHE   A 1 140 ? 120.90028 -28.95987 11.35318  1.000 22.11315 ?  140 PHE   A CE1 1 
ATOM   1080 C CE2 . PHE   A 1 140 ? 121.96125 -26.84152 11.16736  1.000 22.10693 ?  140 PHE   A CE2 1 
ATOM   1081 C CZ  . PHE   A 1 140 ? 121.75497 -28.11001 10.69046  1.000 20.41583 ?  140 PHE   A CZ  1 
ATOM   1082 N N   . LEU   A 1 141 ? 116.94161 -27.40102 16.13998  1.000 30.88789 ?  141 LEU   A N   1 
ATOM   1083 C CA  . LEU   A 1 141 ? 116.43671 -27.33292 17.50521  1.000 32.18382 ?  141 LEU   A CA  1 
ATOM   1084 C C   . LEU   A 1 141 ? 117.18973 -28.33514 18.37113  1.000 33.15894 ?  141 LEU   A C   1 
ATOM   1085 O O   . LEU   A 1 141 ? 118.08171 -29.04389 17.90918  1.000 27.38298 ?  141 LEU   A O   1 
ATOM   1086 C CB  . LEU   A 1 141 ? 114.93345 -27.60445 17.54746  1.000 33.00453 ?  141 LEU   A CB  1 
ATOM   1087 C CG  . LEU   A 1 141 ? 114.01952 -26.70544 16.71255  1.000 36.44911 ?  141 LEU   A CG  1 
ATOM   1088 C CD1 . LEU   A 1 141 ? 112.62450 -27.30618 16.67906  1.000 40.37261 ?  141 LEU   A CD1 1 
ATOM   1089 C CD2 . LEU   A 1 141 ? 113.99215 -25.28018 17.24264  1.000 39.21941 ?  141 LEU   A CD2 1 
ATOM   1090 N N   . ASN   A 1 142 ? 116.82039 -28.40203 19.64834  1.000 34.61526 ?  142 ASN   A N   1 
ATOM   1091 C CA  . ASN   A 1 142 ? 117.42751 -29.40015 20.51733  1.000 34.63422 ?  142 ASN   A CA  1 
ATOM   1092 C C   . ASN   A 1 142 ? 117.14724 -30.79178 19.96414  1.000 31.83937 ?  142 ASN   A C   1 
ATOM   1093 O O   . ASN   A 1 142 ? 116.06629 -31.05716 19.43157  1.000 32.18477 ?  142 ASN   A O   1 
ATOM   1094 C CB  . ASN   A 1 142 ? 116.88526 -29.26604 21.94128  1.000 37.93619 ?  142 ASN   A CB  1 
ATOM   1095 C CG  . ASN   A 1 142 ? 117.41464 -28.03539 22.64091  1.000 46.81638 ?  142 ASN   A CG  1 
ATOM   1096 O OD1 . ASN   A 1 142 ? 118.31759 -28.12011 23.47156  1.000 59.97823 ?  142 ASN   A OD1 1 
ATOM   1097 N ND2 . ASN   A 1 142 ? 116.85502 -26.87599 22.30369  1.000 52.24899 ?  142 ASN   A ND2 1 
ATOM   1098 N N   . GLY   A 1 143 ? 118.13958 -31.67522 20.06145  1.000 31.38640 ?  143 GLY   A N   1 
ATOM   1099 C CA  . GLY   A 1 143 ? 118.02222 -33.01120 19.51562  1.000 30.42462 ?  143 GLY   A CA  1 
ATOM   1100 C C   . GLY   A 1 143 ? 118.42586 -33.14099 18.05950  1.000 28.65649 ?  143 GLY   A C   1 
ATOM   1101 O O   . GLY   A 1 143 ? 118.52436 -34.26879 17.55460  1.000 26.28505 ?  143 GLY   A O   1 
ATOM   1102 N N   . SER   A 1 144 ? 118.68311 -32.02937 17.37605  1.000 26.52424 ?  144 SER   A N   1 
ATOM   1103 C CA  . SER   A 1 144 ? 119.05427 -32.06665 15.96456  1.000 27.13788 ?  144 SER   A CA  1 
ATOM   1104 C C   . SER   A 1 144 ? 120.51220 -32.43098 15.72910  1.000 25.17184 ?  144 SER   A C   1 
ATOM   1105 O O   . SER   A 1 144 ? 120.88531 -32.71874 14.58361  1.000 19.99227 ?  144 SER   A O   1 
ATOM   1106 C CB  . SER   A 1 144 ? 118.76212 -30.71163 15.32848  1.000 27.32025 ?  144 SER   A CB  1 
ATOM   1107 O OG  . SER   A 1 144 ? 119.75313 -29.77784 15.69805  1.000 28.49456 ?  144 SER   A OG  1 
ATOM   1108 N N   . CYS   A 1 145 ? 121.34452 -32.43314 16.77173  1.000 20.52945 ?  145 CYS   A N   1 
ATOM   1109 C CA  . CYS   A 1 145 ? 122.75604 -32.71581 16.57087  1.000 20.53888 ?  145 CYS   A CA  1 
ATOM   1110 C C   . CYS   A 1 145 ? 122.94995 -34.09804 15.96621  1.000 20.14430 ?  145 CYS   A C   1 
ATOM   1111 O O   . CYS   A 1 145 ? 122.21340 -35.03826 16.26817  1.000 22.98364 ?  145 CYS   A O   1 
ATOM   1112 C CB  . CYS   A 1 145 ? 123.52058 -32.59882 17.88567  1.000 22.29391 ?  145 CYS   A CB  1 
ATOM   1113 S SG  . CYS   A 1 145 ? 123.86414 -30.88524 18.24060  1.000 28.44029 ?  145 CYS   A SG  1 
ATOM   1114 N N   . GLY   A 1 146 ? 123.94356 -34.20189 15.08579  1.000 20.32784 ?  146 GLY   A N   1 
ATOM   1115 C CA  . GLY   A 1 146 ? 124.15611 -35.39520 14.31225  1.000 19.78058 ?  146 GLY   A CA  1 
ATOM   1116 C C   . GLY   A 1 146 ? 123.43102 -35.42468 12.98800  1.000 18.96638 ?  146 GLY   A C   1 
ATOM   1117 O O   . GLY   A 1 146 ? 123.65493 -36.35894 12.21513  1.000 22.17139 ?  146 GLY   A O   1 
ATOM   1118 N N   . SER   A 1 147 ? 122.54025 -34.46130 12.72184  1.000 20.98664 ?  147 SER   A N   1 
ATOM   1119 C CA  . SER   A 1 147 ? 122.02744 -34.27652 11.36756  1.000 20.62113 ?  147 SER   A CA  1 
ATOM   1120 C C   . SER   A 1 147 ? 123.18241 -33.89637 10.45668  1.000 18.79872 ?  147 SER   A C   1 
ATOM   1121 O O   . SER   A 1 147 ? 124.13942 -33.24382 10.88744  1.000 18.10316 ?  147 SER   A O   1 
ATOM   1122 C CB  . SER   A 1 147 ? 120.95389 -33.18364 11.31689  1.000 20.70179 ?  147 SER   A CB  1 
ATOM   1123 O OG  . SER   A 1 147 ? 119.90738 -33.39121 12.26436  1.000 22.64044 ?  147 SER   A OG  1 
ATOM   1124 N N   . VAL   A 1 148 ? 123.08574 -34.29149 9.17752   1.000 18.99895 ?  148 VAL   A N   1 
ATOM   1125 C CA  . VAL   A 1 148 ? 124.24142 -34.22607 8.29433   1.000 17.41287 ?  148 VAL   A CA  1 
ATOM   1126 C C   . VAL   A 1 148 ? 123.94817 -33.39533 7.05240   1.000 16.15554 ?  148 VAL   A C   1 
ATOM   1127 O O   . VAL   A 1 148 ? 122.79579 -33.22906 6.62179   1.000 16.81737 ?  148 VAL   A O   1 
ATOM   1128 C CB  . VAL   A 1 148 ? 124.74020 -35.62715 7.87762   1.000 17.70005 ?  148 VAL   A CB  1 
ATOM   1129 C CG1 . VAL   A 1 148 ? 125.22818 -36.39716 9.09864   1.000 18.77477 ?  148 VAL   A CG1 1 
ATOM   1130 C CG2 . VAL   A 1 148 ? 123.64777 -36.38288 7.15979   1.000 21.03353 ?  148 VAL   A CG2 1 
ATOM   1131 N N   . GLY   A 1 149 ? 125.03547 -32.86023 6.49277   1.000 16.90199 ?  149 GLY   A N   1 
ATOM   1132 C CA  . GLY   A 1 149 ? 125.01976 -32.16210 5.21950   1.000 18.89730 ?  149 GLY   A CA  1 
ATOM   1133 C C   . GLY   A 1 149 ? 125.73093 -33.00006 4.17422   1.000 15.87970 ?  149 GLY   A C   1 
ATOM   1134 O O   . GLY   A 1 149 ? 126.66466 -33.73662 4.48537   1.000 15.90962 ?  149 GLY   A O   1 
ATOM   1135 N N   . PHE   A 1 150 ? 125.28092 -32.89353 2.92319   1.000 16.14705 ?  150 PHE   A N   1 
ATOM   1136 C CA  . PHE   A 1 150 ? 125.76481 -33.78470 1.87978   1.000 17.48769 ?  150 PHE   A CA  1 
ATOM   1137 C C   . PHE   A 1 150 ? 125.53054 -33.15936 0.51122   1.000 20.73949 ?  150 PHE   A C   1 
ATOM   1138 O O   . PHE   A 1 150 ? 124.69010 -32.27101 0.34707   1.000 17.92585 ?  150 PHE   A O   1 
ATOM   1139 C CB  . PHE   A 1 150 ? 125.07495 -35.15461 1.94994   1.000 18.92051 ?  150 PHE   A CB  1 
ATOM   1140 C CG  . PHE   A 1 150 ? 123.58286 -35.09465 1.73228   1.000 19.35392 ?  150 PHE   A CG  1 
ATOM   1141 C CD1 . PHE   A 1 150 ? 122.73691 -34.72724 2.77559   1.000 20.28487 ?  150 PHE   A CD1 1 
ATOM   1142 C CD2 . PHE   A 1 150 ? 123.03278 -35.36180 0.49078   1.000 20.92511 ?  150 PHE   A CD2 1 
ATOM   1143 C CE1 . PHE   A 1 150 ? 121.37428 -34.64617 2.59234   1.000 20.92279 ?  150 PHE   A CE1 1 
ATOM   1144 C CE2 . PHE   A 1 150 ? 121.65880 -35.28728 0.29617   1.000 23.87073 ?  150 PHE   A CE2 1 
ATOM   1145 C CZ  . PHE   A 1 150 ? 120.82863 -34.92782 1.34857   1.000 23.28271 ?  150 PHE   A CZ  1 
ATOM   1146 N N   . ASN   A 1 151 ? 126.28132 -33.65768 -0.46554  1.000 19.83111 ?  151 ASN   A N   1 
ATOM   1147 C CA  . ASN   A 1 151 ? 126.02608 -33.42095 -1.88127  1.000 23.20566 ?  151 ASN   A CA  1 
ATOM   1148 C C   . ASN   A 1 151 ? 125.82629 -34.77513 -2.55327  1.000 26.32943 ?  151 ASN   A C   1 
ATOM   1149 O O   . ASN   A 1 151 ? 126.24000 -35.80598 -2.02767  1.000 23.39599 ?  151 ASN   A O   1 
ATOM   1150 C CB  . ASN   A 1 151 ? 127.19413 -32.66684 -2.52049  1.000 24.12879 ?  151 ASN   A CB  1 
ATOM   1151 C CG  . ASN   A 1 151 ? 127.19953 -31.18844 -2.16730  1.000 25.56406 ?  151 ASN   A CG  1 
ATOM   1152 O OD1 . ASN   A 1 151 ? 127.91229 -30.76784 -1.25377  1.000 24.49731 ?  151 ASN   A OD1 1 
ATOM   1153 N ND2 . ASN   A 1 151 ? 126.43203 -30.39354 -2.89372  1.000 24.94629 ?  151 ASN   A ND2 1 
ATOM   1154 N N   . ILE   A 1 152 ? 125.19681 -34.79194 -3.72896  1.000 23.42889 ?  152 ILE   A N   1 
ATOM   1155 C CA  . ILE   A 1 152 ? 124.97451 -36.03784 -4.45226  1.000 29.85313 ?  152 ILE   A CA  1 
ATOM   1156 C C   . ILE   A 1 152 ? 125.63390 -35.88509 -5.81661  1.000 36.22337 ?  152 ILE   A C   1 
ATOM   1157 O O   . ILE   A 1 152 ? 125.44222 -34.86316 -6.48329  1.000 33.82608 ?  152 ILE   A O   1 
ATOM   1158 C CB  . ILE   A 1 152 ? 123.47642 -36.34863 -4.61267  1.000 32.57459 ?  152 ILE   A CB  1 
ATOM   1159 C CG1 . ILE   A 1 152 ? 122.85440 -36.83461 -3.30367  1.000 31.06221 ?  152 ILE   A CG1 1 
ATOM   1160 C CG2 . ILE   A 1 152 ? 123.30135 -37.45450 -5.63175  1.000 38.63732 ?  152 ILE   A CG2 1 
ATOM   1161 C CD1 . ILE   A 1 152 ? 122.85893 -38.31560 -3.12963  1.000 42.24789 ?  152 ILE   A CD1 1 
ATOM   1162 N N   . ASP   A 1 153 ? 126.42585 -36.88044 -6.21680  1.000 38.37150 ?  153 ASP   A N   1 
ATOM   1163 C CA  . ASP   A 1 153 ? 127.05271 -36.92398 -7.54113  1.000 42.94096 ?  153 ASP   A CA  1 
ATOM   1164 C C   . ASP   A 1 153 ? 126.57413 -38.21707 -8.19825  1.000 41.25830 ?  153 ASP   A C   1 
ATOM   1165 O O   . ASP   A 1 153 ? 127.10966 -39.29384 -7.91761  1.000 44.08784 ?  153 ASP   A O   1 
ATOM   1166 C CB  . ASP   A 1 153 ? 128.58045 -36.85690 -7.42598  1.000 46.31239 ?  153 ASP   A CB  1 
ATOM   1167 C CG  . ASP   A 1 153 ? 129.30342 -37.01533 -8.77480  1.000 60.30649 ?  153 ASP   A CG  1 
ATOM   1168 O OD1 . ASP   A 1 153 ? 130.34424 -36.34913 -8.96281  1.000 70.94455 -1 153 ASP   A OD1 1 
ATOM   1169 O OD2 . ASP   A 1 153 ? 128.85943 -37.79366 -9.64635  1.000 62.56016 ?  153 ASP   A OD2 1 
ATOM   1170 N N   . TYR   A 1 154 ? 125.56991 -38.10791 -9.07068  1.000 42.47651 ?  154 TYR   A N   1 
ATOM   1171 C CA  . TYR   A 1 154 ? 124.94872 -39.26947 -9.69650  1.000 43.28931 ?  154 TYR   A CA  1 
ATOM   1172 C C   . TYR   A 1 154 ? 124.45685 -40.24959 -8.63868  1.000 41.95160 ?  154 TYR   A C   1 
ATOM   1173 O O   . TYR   A 1 154 ? 123.35797 -40.08893 -8.09823  1.000 42.01519 ?  154 TYR   A O   1 
ATOM   1174 C CB  . TYR   A 1 154 ? 125.91799 -39.95894 -10.66197 1.000 42.88028 ?  154 TYR   A CB  1 
ATOM   1175 N N   . ASP   A 1 155 ? 125.25905 -41.26207 -8.32054  1.000 41.51384 ?  155 ASP   A N   1 
ATOM   1176 C CA  . ASP   A 1 155 ? 124.86361 -42.25214 -7.32809  1.000 41.37401 ?  155 ASP   A CA  1 
ATOM   1177 C C   . ASP   A 1 155 ? 125.67812 -42.18464 -6.04452  1.000 39.88993 ?  155 ASP   A C   1 
ATOM   1178 O O   . ASP   A 1 155 ? 125.43091 -42.98582 -5.13948  1.000 37.18875 ?  155 ASP   A O   1 
ATOM   1179 C CB  . ASP   A 1 155 ? 124.95442 -43.67241 -7.90974  1.000 44.87179 ?  155 ASP   A CB  1 
ATOM   1180 C CG  . ASP   A 1 155 ? 126.33378 -43.99624 -8.47118  1.000 44.55927 ?  155 ASP   A CG  1 
ATOM   1181 O OD1 . ASP   A 1 155 ? 127.21372 -43.10892 -8.46074  1.000 40.42020 -1 155 ASP   A OD1 1 
ATOM   1182 O OD2 . ASP   A 1 155 ? 126.54307 -45.15206 -8.90651  1.000 52.25431 ?  155 ASP   A OD2 1 
ATOM   1183 N N   . CYS   A 1 156 ? 126.62448 -41.25448 -5.93234  1.000 37.01321 ?  156 CYS   A N   1 
ATOM   1184 C CA  . CYS   A 1 156 ? 127.55102 -41.19959 -4.80768  1.000 35.08520 ?  156 CYS   A CA  1 
ATOM   1185 C C   . CYS   A 1 156 ? 127.18696 -40.06133 -3.86436  1.000 30.89179 ?  156 CYS   A C   1 
ATOM   1186 O O   . CYS   A 1 156 ? 127.08979 -38.90769 -4.28955  1.000 31.47816 ?  156 CYS   A O   1 
ATOM   1187 C CB  . CYS   A 1 156 ? 128.98573 -41.01474 -5.29724  1.000 35.76046 ?  156 CYS   A CB  1 
ATOM   1188 S SG  . CYS   A 1 156 ? 130.19779 -40.99969 -3.96207  1.000 38.80434 ?  156 CYS   A SG  1 
ATOM   1189 N N   . VAL   A 1 157 ? 127.02330 -40.38091 -2.58375  1.000 29.45668 ?  157 VAL   A N   1 
ATOM   1190 C CA  . VAL   A 1 157 ? 126.72693 -39.37606 -1.56780  1.000 26.42589 ?  157 VAL   A CA  1 
ATOM   1191 C C   . VAL   A 1 157 ? 128.04045 -38.90241 -0.95873  1.000 25.98020 ?  157 VAL   A C   1 
ATOM   1192 O O   . VAL   A 1 157 ? 128.81145 -39.70625 -0.42897  1.000 23.57209 ?  157 VAL   A O   1 
ATOM   1193 C CB  . VAL   A 1 157 ? 125.80478 -39.93438 -0.47412  1.000 24.95574 ?  157 VAL   A CB  1 
ATOM   1194 C CG1 . VAL   A 1 157 ? 125.51636 -38.84728 0.57275   1.000 23.02167 ?  157 VAL   A CG1 1 
ATOM   1195 C CG2 . VAL   A 1 157 ? 124.53442 -40.49612 -1.06807  1.000 23.74876 ?  157 VAL   A CG2 1 
ATOM   1196 N N   . SER   A 1 158 ? 128.28525 -37.60016 -1.00860  1.000 24.43915 ?  158 SER   A N   1 
ATOM   1197 C CA  . SER   A 1 158 ? 129.46767 -36.99860 -0.40142  1.000 23.18064 ?  158 SER   A CA  1 
ATOM   1198 C C   . SER   A 1 158 ? 129.02339 -36.29831 0.87365   1.000 20.02799 ?  158 SER   A C   1 
ATOM   1199 O O   . SER   A 1 158 ? 128.45443 -35.20914 0.82435   1.000 20.59941 ?  158 SER   A O   1 
ATOM   1200 C CB  . SER   A 1 158 ? 130.13025 -36.02250 -1.36092  1.000 24.79426 ?  158 SER   A CB  1 
ATOM   1201 O OG  . SER   A 1 158 ? 130.80702 -36.72200 -2.37632  1.000 27.01697 ?  158 SER   A OG  1 
ATOM   1202 N N   . PHE   A 1 159 ? 129.28658 -36.92425 2.01818   1.000 20.65838 ?  159 PHE   A N   1 
ATOM   1203 C CA  . PHE   A 1 159 ? 128.94313 -36.32529 3.30165   1.000 19.97030 ?  159 PHE   A CA  1 
ATOM   1204 C C   . PHE   A 1 159 ? 129.99763 -35.29161 3.66975   1.000 18.42799 ?  159 PHE   A C   1 
ATOM   1205 O O   . PHE   A 1 159 ? 131.19542 -35.58421 3.65067   1.000 21.10056 ?  159 PHE   A O   1 
ATOM   1206 C CB  . PHE   A 1 159 ? 128.85944 -37.40437 4.38194   1.000 18.29450 ?  159 PHE   A CB  1 
ATOM   1207 C CG  . PHE   A 1 159 ? 127.71555 -38.36140 4.20073   1.000 18.59598 ?  159 PHE   A CG  1 
ATOM   1208 C CD1 . PHE   A 1 159 ? 126.41455 -37.98737 4.51555   1.000 16.98692 ?  159 PHE   A CD1 1 
ATOM   1209 C CD2 . PHE   A 1 159 ? 127.93732 -39.62555 3.69135   1.000 17.60681 ?  159 PHE   A CD2 1 
ATOM   1210 C CE1 . PHE   A 1 159 ? 125.36575 -38.86703 4.34248   1.000 19.52168 ?  159 PHE   A CE1 1 
ATOM   1211 C CE2 . PHE   A 1 159 ? 126.88039 -40.52367 3.52040   1.000 19.80844 ?  159 PHE   A CE2 1 
ATOM   1212 C CZ  . PHE   A 1 159 ? 125.60241 -40.14472 3.84566   1.000 20.24383 ?  159 PHE   A CZ  1 
ATOM   1213 N N   . CYS   A 1 160 ? 129.55843 -34.07952 4.00362   1.000 16.82326 ?  160 CYS   A N   1 
ATOM   1214 C CA  . CYS   A 1 160 ? 130.49751 -33.01156 4.28304   1.000 15.37867 ?  160 CYS   A CA  1 
ATOM   1215 C C   . CYS   A 1 160 ? 130.28582 -32.31829 5.62104   1.000 16.28047 ?  160 CYS   A C   1 
ATOM   1216 O O   . CYS   A 1 160 ? 131.16027 -31.54613 6.02950   1.000 18.06461 ?  160 CYS   A O   1 
ATOM   1217 C CB  . CYS   A 1 160 ? 130.44484 -31.94827 3.17739   1.000 19.02069 ?  160 CYS   A CB  1 
ATOM   1218 S SG  . CYS   A 1 160 ? 128.82553 -31.20721 2.91668   1.000 20.34788 ?  160 CYS   A SG  1 
ATOM   1219 N N   . TYR   A 1 161 ? 129.17718 -32.56316 6.31406   1.000 15.70333 ?  161 TYR   A N   1 
ATOM   1220 C CA  . TYR   A 1 161 ? 128.85992 -31.78380 7.50061   1.000 16.06396 ?  161 TYR   A CA  1 
ATOM   1221 C C   . TYR   A 1 161 ? 128.09022 -32.62421 8.50376   1.000 16.30424 ?  161 TYR   A C   1 
ATOM   1222 O O   . TYR   A 1 161 ? 127.21629 -33.40760 8.11924   1.000 14.95966 ?  161 TYR   A O   1 
ATOM   1223 C CB  . TYR   A 1 161 ? 128.02907 -30.54527 7.13722   1.000 14.67952 ?  161 TYR   A CB  1 
ATOM   1224 C CG  . TYR   A 1 161 ? 127.64680 -29.68379 8.32846   1.000 16.42200 ?  161 TYR   A CG  1 
ATOM   1225 C CD1 . TYR   A 1 161 ? 128.53968 -28.75060 8.84099   1.000 16.54158 ?  161 TYR   A CD1 1 
ATOM   1226 C CD2 . TYR   A 1 161 ? 126.39706 -29.79180 8.92334   1.000 16.83070 ?  161 TYR   A CD2 1 
ATOM   1227 C CE1 . TYR   A 1 161 ? 128.19999 -27.95176 9.91714   1.000 17.56037 ?  161 TYR   A CE1 1 
ATOM   1228 C CE2 . TYR   A 1 161 ? 126.04182 -28.99729 10.00527  1.000 16.85701 ?  161 TYR   A CE2 1 
ATOM   1229 C CZ  . TYR   A 1 161 ? 126.95510 -28.08332 10.50028  1.000 16.26807 ?  161 TYR   A CZ  1 
ATOM   1230 O OH  . TYR   A 1 161 ? 126.62580 -27.29251 11.56929  1.000 17.42376 ?  161 TYR   A OH  1 
ATOM   1231 N N   . MET   A 1 162 ? 128.39633 -32.43983 9.79207   1.000 15.87317 ?  162 MET   A N   1 
ATOM   1232 C CA  . MET   A 1 162 ? 127.49963 -32.97938 10.80425  1.000 13.20001 ?  162 MET   A CA  1 
ATOM   1233 C C   . MET   A 1 162 ? 127.31833 -31.91438 11.87777  1.000 14.47414 ?  162 MET   A C   1 
ATOM   1234 O O   . MET   A 1 162 ? 128.27516 -31.23086 12.25944  1.000 13.84898 ?  162 MET   A O   1 
ATOM   1235 C CB  . MET   A 1 162 ? 128.00020 -34.32551 11.37782  1.000 17.14160 ?  162 MET   A CB  1 
ATOM   1236 C CG  . MET   A 1 162 ? 127.41834 -34.68227 12.74828  1.000 17.60026 ?  162 MET   A CG  1 
ATOM   1237 S SD  . MET   A 1 162 ? 128.05227 -36.25805 13.35003  1.000 22.25008 ?  162 MET   A SD  1 
ATOM   1238 C CE  . MET   A 1 162 ? 127.12456 -37.40926 12.34866  1.000 20.37226 ?  162 MET   A CE  1 
ATOM   1239 N N   . HIS   A 1 163 ? 126.07030 -31.72396 12.30346  1.000 16.16930 ?  163 HIS   A N   1 
ATOM   1240 C CA  . HIS   A 1 163 ? 125.74247 -30.58106 13.13864  1.000 16.49023 ?  163 HIS   A CA  1 
ATOM   1241 C C   . HIS   A 1 163 ? 126.11129 -30.83840 14.59184  1.000 16.79565 ?  163 HIS   A C   1 
ATOM   1242 O O   . HIS   A 1 163 ? 125.84665 -31.92047 15.12154  1.000 17.27857 ?  163 HIS   A O   1 
ATOM   1243 C CB  . HIS   A 1 163 ? 124.25819 -30.23821 13.05601  1.000 18.53104 ?  163 HIS   A CB  1 
ATOM   1244 C CG  . HIS   A 1 163 ? 123.91124 -29.04218 13.86792  1.000 18.08432 ?  163 HIS   A CG  1 
ATOM   1245 N ND1 . HIS   A 1 163 ? 124.49660 -27.81795 13.63908  1.000 19.52761 ?  163 HIS   A ND1 1 
ATOM   1246 C CD2 . HIS   A 1 163 ? 123.05668 -28.86682 14.89937  1.000 19.08238 ?  163 HIS   A CD2 1 
ATOM   1247 C CE1 . HIS   A 1 163 ? 124.02376 -26.94049 14.50223  1.000 20.60056 ?  163 HIS   A CE1 1 
ATOM   1248 N NE2 . HIS   A 1 163 ? 123.14404 -27.54838 15.27290  1.000 21.34991 ?  163 HIS   A NE2 1 
ATOM   1249 N N   . HIS   A 1 164 ? 126.72683 -29.83023 15.23310  1.000 14.39763 ?  164 HIS   A N   1 
ATOM   1250 C CA  . HIS   A 1 164 ? 127.10164 -29.91984 16.64857  1.000 15.16401 ?  164 HIS   A CA  1 
ATOM   1251 C C   . HIS   A 1 164 ? 126.53069 -28.82571 17.53536  1.000 19.93510 ?  164 HIS   A C   1 
ATOM   1252 O O   . HIS   A 1 164 ? 126.23171 -29.09908 18.69403  1.000 21.83676 ?  164 HIS   A O   1 
ATOM   1253 C CB  . HIS   A 1 164 ? 128.63136 -29.90203 16.83343  1.000 16.24397 ?  164 HIS   A CB  1 
ATOM   1254 C CG  . HIS   A 1 164 ? 129.32063 -31.15117 16.38797  1.000 17.48907 ?  164 HIS   A CG  1 
ATOM   1255 N ND1 . HIS   A 1 164 ? 129.96192 -31.99289 17.27153  1.000 16.30202 ?  164 HIS   A ND1 1 
ATOM   1256 C CD2 . HIS   A 1 164 ? 129.48656 -31.69759 15.16094  1.000 15.29241 ?  164 HIS   A CD2 1 
ATOM   1257 C CE1 . HIS   A 1 164 ? 130.49762 -32.99942 16.60764  1.000 16.75257 ?  164 HIS   A CE1 1 
ATOM   1258 N NE2 . HIS   A 1 164 ? 130.21148 -32.85374 15.32526  1.000 15.25090 ?  164 HIS   A NE2 1 
ATOM   1259 N N   . MET   A 1 165 ? 126.43593 -27.57659 17.07730  1.000 17.73446 ?  165 MET   A N   1 
ATOM   1260 C CA  . MET   A 1 165 ? 126.11535 -26.54144 18.05113  1.000 23.42016 ?  165 MET   A CA  1 
ATOM   1261 C C   . MET   A 1 165 ? 125.55186 -25.29435 17.39596  1.000 20.71330 ?  165 MET   A C   1 
ATOM   1262 O O   . MET   A 1 165 ? 125.72095 -25.05679 16.19841  1.000 20.79889 ?  165 MET   A O   1 
ATOM   1263 C CB  . MET   A 1 165 ? 127.33597 -26.11374 18.85829  1.000 24.65774 ?  165 MET   A CB  1 
ATOM   1264 C CG  . MET   A 1 165 ? 128.53186 -25.84239 18.01598  1.000 25.42448 ?  165 MET   A CG  1 
ATOM   1265 S SD  . MET   A 1 165 ? 129.95689 -25.69330 19.10576  1.000 35.20238 ?  165 MET   A SD  1 
ATOM   1266 C CE  . MET   A 1 165 ? 129.20883 -24.79708 20.45470  1.000 23.97053 ?  165 MET   A CE  1 
ATOM   1267 N N   . GLU   A 1 166 ? 124.90295 -24.48479 18.23124  1.000 23.35536 ?  166 GLU   A N   1 
ATOM   1268 C CA  . GLU   A 1 166 ? 124.44253 -23.15100 17.87669  1.000 23.80207 ?  166 GLU   A CA  1 
ATOM   1269 C C   . GLU   A 1 166 ? 125.32632 -22.10394 18.53951  1.000 29.32765 ?  166 GLU   A C   1 
ATOM   1270 O O   . GLU   A 1 166 ? 125.65100 -22.22348 19.71922  1.000 29.06429 ?  166 GLU   A O   1 
ATOM   1271 C CB  . GLU   A 1 166 ? 123.00152 -22.92371 18.32966  1.000 29.89782 ?  166 GLU   A CB  1 
ATOM   1272 C CG  . GLU   A 1 166 ? 122.31391 -21.82286 17.56984  1.000 31.85143 ?  166 GLU   A CG  1 
ATOM   1273 C CD  . GLU   A 1 166 ? 120.82313 -21.81729 17.80286  1.000 34.70947 ?  166 GLU   A CD  1 
ATOM   1274 O OE1 . GLU   A 1 166 ? 120.38674 -21.33555 18.86764  1.000 40.17219 ?  166 GLU   A OE1 1 
ATOM   1275 O OE2 . GLU   A 1 166 ? 120.09070 -22.32775 16.93530  1.000 34.97208 -1 166 GLU   A OE2 1 
ATOM   1276 N N   . LEU   A 1 167 ? 125.68401 -21.06819 17.79104  1.000 29.79473 ?  167 LEU   A N   1 
ATOM   1277 C CA  . LEU   A 1 167 ? 126.52614 -19.98743 18.29529  1.000 30.43052 ?  167 LEU   A CA  1 
ATOM   1278 C C   . LEU   A 1 167 ? 125.66897 -18.87607 18.88504  1.000 39.30090 ?  167 LEU   A C   1 
ATOM   1279 O O   . LEU   A 1 167 ? 124.43729 -18.89616 18.77545  1.000 39.41023 ?  167 LEU   A O   1 
ATOM   1280 C CB  . LEU   A 1 167 ? 127.42510 -19.47336 17.17114  1.000 32.17719 ?  167 LEU   A CB  1 
ATOM   1281 C CG  . LEU   A 1 167 ? 128.43500 -20.50693 16.66581  1.000 28.54157 ?  167 LEU   A CG  1 
ATOM   1282 C CD1 . LEU   A 1 167 ? 129.17993 -19.98953 15.45434  1.000 26.15087 ?  167 LEU   A CD1 1 
ATOM   1283 C CD2 . LEU   A 1 167 ? 129.38953 -20.92587 17.77356  1.000 32.86647 ?  167 LEU   A CD2 1 
ATOM   1284 N N   . PRO   A 1 168 ? 126.28497 -17.88431 19.54856  1.000 35.57596 ?  168 PRO   A N   1 
ATOM   1285 C CA  . PRO   A 1 168 ? 125.46793 -16.82835 20.17327  1.000 36.94006 ?  168 PRO   A CA  1 
ATOM   1286 C C   . PRO   A 1 168 ? 124.71340 -15.97347 19.18093  1.000 38.39831 ?  168 PRO   A C   1 
ATOM   1287 O O   . PRO   A 1 168 ? 123.64386 -15.45328 19.52112  1.000 38.79512 ?  168 PRO   A O   1 
ATOM   1288 C CB  . PRO   A 1 168 ? 126.48453 -15.99296 20.97024  1.000 37.45473 ?  168 PRO   A CB  1 
ATOM   1289 C CG  . PRO   A 1 168 ? 127.76493 -16.73631 20.96169  1.000 36.93132 ?  168 PRO   A CG  1 
ATOM   1290 C CD  . PRO   A 1 168 ? 127.71968 -17.76375 19.88366  1.000 34.63641 ?  168 PRO   A CD  1 
ATOM   1291 N N   . THR   A 1 169 ? 125.23161 -15.80165 17.96633  1.000 37.68383 ?  169 THR   A N   1 
ATOM   1292 C CA  . THR   A 1 169 ? 124.51420 -15.02354 16.96724  1.000 39.88650 ?  169 THR   A CA  1 
ATOM   1293 C C   . THR   A 1 169 ? 123.38776 -15.81053 16.31398  1.000 38.91908 ?  169 THR   A C   1 
ATOM   1294 O O   . THR   A 1 169 ? 122.73007 -15.28284 15.41039  1.000 40.73074 ?  169 THR   A O   1 
ATOM   1295 C CB  . THR   A 1 169 ? 125.48056 -14.50698 15.89380  1.000 40.64976 ?  169 THR   A CB  1 
ATOM   1296 O OG1 . THR   A 1 169 ? 126.11129 -15.61530 15.24431  1.000 38.07189 ?  169 THR   A OG1 1 
ATOM   1297 C CG2 . THR   A 1 169 ? 126.55191 -13.60343 16.51560  1.000 39.14108 ?  169 THR   A CG2 1 
ATOM   1298 N N   . GLY   A 1 170 ? 123.14829 -17.04787 16.74483  1.000 37.60817 ?  170 GLY   A N   1 
ATOM   1299 C CA  . GLY   A 1 170 ? 122.08591 -17.86050 16.19292  1.000 36.54812 ?  170 GLY   A CA  1 
ATOM   1300 C C   . GLY   A 1 170 ? 122.45565 -18.67316 14.97222  1.000 35.06972 ?  170 GLY   A C   1 
ATOM   1301 O O   . GLY   A 1 170 ? 121.58829 -19.36926 14.42582  1.000 31.47831 ?  170 GLY   A O   1 
ATOM   1302 N N   . VAL   A 1 171 ? 123.69981 -18.58936 14.50587  1.000 33.18550 ?  171 VAL   A N   1 
ATOM   1303 C CA  . VAL   A 1 171 ? 124.15232 -19.42066 13.39972  1.000 28.10691 ?  171 VAL   A CA  1 
ATOM   1304 C C   . VAL   A 1 171 ? 124.67707 -20.73535 13.96415  1.000 23.70951 ?  171 VAL   A C   1 
ATOM   1305 O O   . VAL   A 1 171 ? 124.73117 -20.93138 15.18261  1.000 24.54696 ?  171 VAL   A O   1 
ATOM   1306 C CB  . VAL   A 1 171 ? 125.21449 -18.70458 12.54017  1.000 26.75053 ?  171 VAL   A CB  1 
ATOM   1307 C CG1 . VAL   A 1 171 ? 124.64580 -17.41895 11.94218  1.000 29.65764 ?  171 VAL   A CG1 1 
ATOM   1308 C CG2 . VAL   A 1 171 ? 126.44472 -18.38119 13.37685  1.000 26.15853 ?  171 VAL   A CG2 1 
ATOM   1309 N N   . HIS   A 1 172 ? 125.06129 -21.64914 13.08386  1.000 23.96960 ?  172 HIS   A N   1 
ATOM   1310 C CA  . HIS   A 1 172 ? 125.32224 -23.01607 13.49496  1.000 21.21222 ?  172 HIS   A CA  1 
ATOM   1311 C C   . HIS   A 1 172 ? 126.72756 -23.44138 13.09883  1.000 18.95057 ?  172 HIS   A C   1 
ATOM   1312 O O   . HIS   A 1 172 ? 127.30765 -22.93098 12.13350  1.000 19.04858 ?  172 HIS   A O   1 
ATOM   1313 C CB  . HIS   A 1 172 ? 124.26994 -23.95081 12.89702  1.000 21.56502 ?  172 HIS   A CB  1 
ATOM   1314 C CG  . HIS   A 1 172 ? 122.87173 -23.56213 13.26181  1.000 24.45877 ?  172 HIS   A CG  1 
ATOM   1315 N ND1 . HIS   A 1 172 ? 122.03512 -22.87877 12.40391  1.000 26.12967 ?  172 HIS   A ND1 1 
ATOM   1316 C CD2 . HIS   A 1 172 ? 122.18743 -23.70035 14.42188  1.000 26.29966 ?  172 HIS   A CD2 1 
ATOM   1317 C CE1 . HIS   A 1 172 ? 120.88286 -22.64856 13.00820  1.000 28.10550 ?  172 HIS   A CE1 1 
ATOM   1318 N NE2 . HIS   A 1 172 ? 120.95138 -23.13161 14.23663  1.000 27.94197 ?  172 HIS   A NE2 1 
ATOM   1319 N N   . ALA   A 1 173 ? 127.28056 -24.37054 13.88140  1.000 18.49768 ?  173 ALA   A N   1 
ATOM   1320 C CA  . ALA   A 1 173 ? 128.63915 -24.84085 13.67195  1.000 17.42926 ?  173 ALA   A CA  1 
ATOM   1321 C C   . ALA   A 1 173 ? 128.66828 -26.35248 13.78598  1.000 15.76141 ?  173 ALA   A C   1 
ATOM   1322 O O   . ALA   A 1 173 ? 127.87466 -26.95701 14.51514  1.000 16.79765 ?  173 ALA   A O   1 
ATOM   1323 C CB  . ALA   A 1 173 ? 129.62097 -24.23771 14.67463  1.000 20.65972 ?  173 ALA   A CB  1 
ATOM   1324 N N   . GLY   A 1 174 ? 129.60225 -26.94903 13.06520  1.000 16.33989 ?  174 GLY   A N   1 
ATOM   1325 C CA  . GLY   A 1 174 ? 129.70934 -28.39102 13.04302  1.000 16.32732 ?  174 GLY   A CA  1 
ATOM   1326 C C   . GLY   A 1 174 ? 131.02483 -28.82269 12.43917  1.000 13.85557 ?  174 GLY   A C   1 
ATOM   1327 O O   . GLY   A 1 174 ? 131.92425 -28.01514 12.21345  1.000 15.58635 ?  174 GLY   A O   1 
ATOM   1328 N N   . THR   A 1 175 ? 131.12424 -30.12396 12.19098  1.000 14.52713 ?  175 THR   A N   1 
ATOM   1329 C CA  . THR   A 1 175 ? 132.35638 -30.77211 11.78431  1.000 13.70870 ?  175 THR   A CA  1 
ATOM   1330 C C   . THR   A 1 175 ? 132.17942 -31.44087 10.43101  1.000 15.77558 ?  175 THR   A C   1 
ATOM   1331 O O   . THR   A 1 175 ? 131.05916 -31.58762 9.93756   1.000 14.82463 ?  175 THR   A O   1 
ATOM   1332 C CB  . THR   A 1 175 ? 132.77558 -31.83172 12.82072  1.000 15.78241 ?  175 THR   A CB  1 
ATOM   1333 O OG1 . THR   A 1 175 ? 131.83960 -32.91502 12.76282  1.000 16.45382 ?  175 THR   A OG1 1 
ATOM   1334 C CG2 . THR   A 1 175 ? 132.83978 -31.25200 14.23143  1.000 15.08792 ?  175 THR   A CG2 1 
ATOM   1335 N N   . ASP   A 1 176 ? 133.30760 -31.86358 9.84905   1.000 16.15672 ?  176 ASP   A N   1 
ATOM   1336 C CA  . ASP   A 1 176 ? 133.26845 -32.83917 8.76766   1.000 14.89552 ?  176 ASP   A CA  1 
ATOM   1337 C C   . ASP   A 1 176 ? 133.06364 -34.22387 9.38818   1.000 17.73382 ?  176 ASP   A C   1 
ATOM   1338 O O   . ASP   A 1 176 ? 132.91006 -34.37220 10.60916  1.000 16.39215 ?  176 ASP   A O   1 
ATOM   1339 C CB  . ASP   A 1 176 ? 134.52813 -32.74608 7.89336   1.000 18.42978 ?  176 ASP   A CB  1 
ATOM   1340 C CG  . ASP   A 1 176 ? 135.83723 -33.01078 8.65419   1.000 21.67177 ?  176 ASP   A CG  1 
ATOM   1341 O OD1 . ASP   A 1 176 ? 135.82736 -33.73709 9.67428   1.000 17.91737 ?  176 ASP   A OD1 1 
ATOM   1342 O OD2 . ASP   A 1 176 ? 136.90139 -32.51280 8.19398   1.000 21.72129 -1 176 ASP   A OD2 1 
ATOM   1343 N N   . LEU   A 1 177 ? 133.04715 -35.25791 8.56732   1.000 16.10567 ?  177 LEU   A N   1 
ATOM   1344 C CA  . LEU   A 1 177 ? 132.70867 -36.56447 9.12728   1.000 16.52744 ?  177 LEU   A CA  1 
ATOM   1345 C C   . LEU   A 1 177 ? 133.91896 -37.26386 9.73348   1.000 17.47289 ?  177 LEU   A C   1 
ATOM   1346 O O   . LEU   A 1 177 ? 133.77844 -38.37451 10.25951  1.000 22.24972 ?  177 LEU   A O   1 
ATOM   1347 C CB  . LEU   A 1 177 ? 132.03745 -37.42838 8.05832   1.000 17.48021 ?  177 LEU   A CB  1 
ATOM   1348 C CG  . LEU   A 1 177 ? 130.49271 -37.42541 8.06146   1.000 18.97954 ?  177 LEU   A CG  1 
ATOM   1349 C CD1 . LEU   A 1 177 ? 129.90438 -37.98134 9.34938   1.000 19.92260 ?  177 LEU   A CD1 1 
ATOM   1350 C CD2 . LEU   A 1 177 ? 129.96903 -35.99234 7.85461   1.000 19.54734 ?  177 LEU   A CD2 1 
ATOM   1351 N N   . GLU   A 1 178 ? 135.09215 -36.64761 9.65792   1.000 15.57578 ?  178 GLU   A N   1 
ATOM   1352 C CA  . GLU   A 1 178 ? 136.23670 -37.03811 10.47622  1.000 21.74460 ?  178 GLU   A CA  1 
ATOM   1353 C C   . GLU   A 1 178 ? 136.24814 -36.33223 11.82518  1.000 18.74249 ?  178 GLU   A C   1 
ATOM   1354 O O   . GLU   A 1 178 ? 137.18745 -36.53023 12.60829  1.000 20.22585 ?  178 GLU   A O   1 
ATOM   1355 C CB  . GLU   A 1 178 ? 137.53735 -36.73893 9.73489   1.000 21.17966 ?  178 GLU   A CB  1 
ATOM   1356 C CG  . GLU   A 1 178 ? 137.67840 -37.54272 8.46080   1.000 25.36784 ?  178 GLU   A CG  1 
ATOM   1357 C CD  . GLU   A 1 178 ? 139.08634 -37.53267 7.91452   1.000 33.70576 ?  178 GLU   A CD  1 
ATOM   1358 O OE1 . GLU   A 1 178 ? 139.73685 -36.46596 7.96267   1.000 34.88781 ?  178 GLU   A OE1 1 
ATOM   1359 O OE2 . GLU   A 1 178 ? 139.52810 -38.57943 7.40297   1.000 38.99641 -1 178 GLU   A OE2 1 
ATOM   1360 N N   . GLY   A 1 179 ? 135.25250 -35.49197 12.10453  1.000 17.70313 ?  179 GLY   A N   1 
ATOM   1361 C CA  . GLY   A 1 179 ? 135.14349 -34.86039 13.40550  1.000 16.21718 ?  179 GLY   A CA  1 
ATOM   1362 C C   . GLY   A 1 179 ? 135.88090 -33.55170 13.57614  1.000 18.32739 ?  179 GLY   A C   1 
ATOM   1363 O O   . GLY   A 1 179 ? 135.94563 -33.04442 14.70026  1.000 17.97258 ?  179 GLY   A O   1 
ATOM   1364 N N   . ASN   A 1 180 ? 136.44163 -32.98605 12.50977  1.000 18.08526 ?  180 ASN   A N   1 
ATOM   1365 C CA  . ASN   A 1 180 ? 137.17254 -31.73134 12.61284  1.000 16.55399 ?  180 ASN   A CA  1 
ATOM   1366 C C   . ASN   A 1 180 ? 136.21680 -30.58049 12.36092  1.000 16.10342 ?  180 ASN   A C   1 
ATOM   1367 O O   . ASN   A 1 180 ? 135.60031 -30.50907 11.29235  1.000 16.20056 ?  180 ASN   A O   1 
ATOM   1368 C CB  . ASN   A 1 180 ? 138.33804 -31.66880 11.62425  1.000 18.43747 ?  180 ASN   A CB  1 
ATOM   1369 C CG  . ASN   A 1 180 ? 139.36947 -32.74337 11.86675  1.000 23.07884 ?  180 ASN   A CG  1 
ATOM   1370 O OD1 . ASN   A 1 180 ? 139.56470 -33.62973 11.03947  1.000 30.26189 ?  180 ASN   A OD1 1 
ATOM   1371 N ND2 . ASN   A 1 180 ? 140.00805 -32.69337 13.02815  1.000 22.11587 ?  180 ASN   A ND2 1 
ATOM   1372 N N   . PHE   A 1 181 ? 136.09808 -29.68289 13.33582  1.000 14.87234 ?  181 PHE   A N   1 
ATOM   1373 C CA  . PHE   A 1 181 ? 135.21797 -28.53638 13.16495  1.000 14.80926 ?  181 PHE   A CA  1 
ATOM   1374 C C   . PHE   A 1 181 ? 135.62203 -27.73101 11.94388  1.000 14.58043 ?  181 PHE   A C   1 
ATOM   1375 O O   . PHE   A 1 181 ? 136.81148 -27.54990 11.65392  1.000 16.86034 ?  181 PHE   A O   1 
ATOM   1376 C CB  . PHE   A 1 181 ? 135.26130 -27.62366 14.38791  1.000 15.51052 ?  181 PHE   A CB  1 
ATOM   1377 C CG  . PHE   A 1 181 ? 134.15377 -27.87207 15.33967  1.000 16.76946 ?  181 PHE   A CG  1 
ATOM   1378 C CD1 . PHE   A 1 181 ? 132.91755 -27.25304 15.16394  1.000 18.35519 ?  181 PHE   A CD1 1 
ATOM   1379 C CD2 . PHE   A 1 181 ? 134.32701 -28.74747 16.39982  1.000 19.15448 ?  181 PHE   A CD2 1 
ATOM   1380 C CE1 . PHE   A 1 181 ? 131.86967 -27.50287 16.03943  1.000 18.30430 ?  181 PHE   A CE1 1 
ATOM   1381 C CE2 . PHE   A 1 181 ? 133.29498 -29.00076 17.27818  1.000 18.39427 ?  181 PHE   A CE2 1 
ATOM   1382 C CZ  . PHE   A 1 181 ? 132.05535 -28.37486 17.09977  1.000 18.33632 ?  181 PHE   A CZ  1 
ATOM   1383 N N   . TYR   A 1 182 ? 134.61351 -27.24990 11.22936  1.000 15.50417 ?  182 TYR   A N   1 
ATOM   1384 C CA  . TYR   A 1 182 ? 134.80244 -26.11256 10.36076  1.000 15.66548 ?  182 TYR   A CA  1 
ATOM   1385 C C   . TYR   A 1 182 ? 134.91594 -24.85016 11.20835  1.000 15.18528 ?  182 TYR   A C   1 
ATOM   1386 O O   . TYR   A 1 182 ? 134.07002 -24.58921 12.06191  1.000 20.10341 ?  182 TYR   A O   1 
ATOM   1387 C CB  . TYR   A 1 182 ? 133.63272 -26.00325 9.38739   1.000 14.79736 ?  182 TYR   A CB  1 
ATOM   1388 C CG  . TYR   A 1 182 ? 133.54797 -27.13273 8.37749   1.000 18.40945 ?  182 TYR   A CG  1 
ATOM   1389 C CD1 . TYR   A 1 182 ? 134.28788 -27.08258 7.20045   1.000 17.34410 ?  182 TYR   A CD1 1 
ATOM   1390 C CD2 . TYR   A 1 182 ? 132.67763 -28.19429 8.55969   1.000 15.58095 ?  182 TYR   A CD2 1 
ATOM   1391 C CE1 . TYR   A 1 182 ? 134.19574 -28.09686 6.24880   1.000 19.46312 ?  182 TYR   A CE1 1 
ATOM   1392 C CE2 . TYR   A 1 182 ? 132.57351 -29.21593 7.62492   1.000 15.36106 ?  182 TYR   A CE2 1 
ATOM   1393 C CZ  . TYR   A 1 182 ? 133.33776 -29.15695 6.46557   1.000 15.53323 ?  182 TYR   A CZ  1 
ATOM   1394 O OH  . TYR   A 1 182 ? 133.23942 -30.15774 5.51955   1.000 17.23682 ?  182 TYR   A OH  1 
ATOM   1395 N N   . GLY   A 1 183 ? 135.97438 -24.08197 10.99489  1.000 17.01062 ?  183 GLY   A N   1 
ATOM   1396 C CA  . GLY   A 1 183 ? 136.15872 -22.85273 11.73108  1.000 16.55718 ?  183 GLY   A CA  1 
ATOM   1397 C C   . GLY   A 1 183 ? 136.81007 -23.05660 13.07886  1.000 21.07874 ?  183 GLY   A C   1 
ATOM   1398 O O   . GLY   A 1 183 ? 137.29827 -24.14117 13.40241  1.000 20.26105 ?  183 GLY   A O   1 
ATOM   1399 N N   . PRO   A 1 184 ? 136.83409 -22.00025 13.88390  1.000 20.15018 ?  184 PRO   A N   1 
ATOM   1400 C CA  . PRO   A 1 184 ? 137.63622 -22.01054 15.11225  1.000 22.40014 ?  184 PRO   A CA  1 
ATOM   1401 C C   . PRO   A 1 184 ? 136.88356 -22.55697 16.31590  1.000 23.69030 ?  184 PRO   A C   1 
ATOM   1402 O O   . PRO   A 1 184 ? 137.26646 -22.29860 17.46207  1.000 29.22546 ?  184 PRO   A O   1 
ATOM   1403 C CB  . PRO   A 1 184 ? 137.96771 -20.52688 15.29334  1.000 23.33761 ?  184 PRO   A CB  1 
ATOM   1404 C CG  . PRO   A 1 184 ? 136.68579 -19.84796 14.80233  1.000 22.67430 ?  184 PRO   A CG  1 
ATOM   1405 C CD  . PRO   A 1 184 ? 136.22776 -20.68284 13.62925  1.000 22.57354 ?  184 PRO   A CD  1 
ATOM   1406 N N   . PHE   A 1 185 ? 135.82965 -23.32281 16.08412  1.000 22.88435 ?  185 PHE   A N   1 
ATOM   1407 C CA  . PHE   A 1 185 ? 134.90271 -23.65034 17.15891  1.000 19.08882 ?  185 PHE   A CA  1 
ATOM   1408 C C   . PHE   A 1 185 ? 135.29653 -24.93850 17.88668  1.000 18.39641 ?  185 PHE   A C   1 
ATOM   1409 O O   . PHE   A 1 185 ? 136.03468 -25.77919 17.36203  1.000 19.36844 ?  185 PHE   A O   1 
ATOM   1410 C CB  . PHE   A 1 185 ? 133.48407 -23.72819 16.60203  1.000 19.20567 ?  185 PHE   A CB  1 
ATOM   1411 C CG  . PHE   A 1 185 ? 133.15438 -22.55775 15.70383  1.000 18.89029 ?  185 PHE   A CG  1 
ATOM   1412 C CD1 . PHE   A 1 185 ? 133.02980 -21.29076 16.24646  1.000 23.34646 ?  185 PHE   A CD1 1 
ATOM   1413 C CD2 . PHE   A 1 185 ? 132.98456 -22.71756 14.33524  1.000 19.63592 ?  185 PHE   A CD2 1 
ATOM   1414 C CE1 . PHE   A 1 185 ? 132.75187 -20.19320 15.44536  1.000 24.37111 ?  185 PHE   A CE1 1 
ATOM   1415 C CE2 . PHE   A 1 185 ? 132.70491 -21.62753 13.53029  1.000 20.21302 ?  185 PHE   A CE2 1 
ATOM   1416 C CZ  . PHE   A 1 185 ? 132.58881 -20.36401 14.08296  1.000 21.60283 ?  185 PHE   A CZ  1 
ATOM   1417 N N   . VAL   A 1 186 ? 134.82251 -25.04462 19.13810  1.000 21.86909 ?  186 VAL   A N   1 
ATOM   1418 C CA  . VAL   A 1 186 ? 135.00999 -26.20686 20.00554  1.000 20.11593 ?  186 VAL   A CA  1 
ATOM   1419 C C   . VAL   A 1 186 ? 133.64494 -26.63776 20.53557  1.000 18.70988 ?  186 VAL   A C   1 
ATOM   1420 O O   . VAL   A 1 186 ? 132.71002 -25.83368 20.61139  1.000 21.12862 ?  186 VAL   A O   1 
ATOM   1421 C CB  . VAL   A 1 186 ? 135.96216 -25.90087 21.17581  1.000 18.75895 ?  186 VAL   A CB  1 
ATOM   1422 C CG1 . VAL   A 1 186 ? 137.36961 -25.60050 20.65854  1.000 24.49784 ?  186 VAL   A CG1 1 
ATOM   1423 C CG2 . VAL   A 1 186 ? 135.42884 -24.75159 21.98726  1.000 20.04290 ?  186 VAL   A CG2 1 
ATOM   1424 N N   . ASP   A 1 187 ? 133.51847 -27.92344 20.88487  1.000 17.52367 ?  187 ASP   A N   1 
ATOM   1425 C CA  . ASP   A 1 187 ? 132.23028 -28.44525 21.33255  1.000 16.54753 ?  187 ASP   A CA  1 
ATOM   1426 C C   . ASP   A 1 187 ? 132.15892 -28.29534 22.84739  1.000 19.68488 ?  187 ASP   A C   1 
ATOM   1427 O O   . ASP   A 1 187 ? 132.28657 -29.24413 23.61716  1.000 20.78158 ?  187 ASP   A O   1 
ATOM   1428 C CB  . ASP   A 1 187 ? 131.99218 -29.88288 20.86855  1.000 17.86511 ?  187 ASP   A CB  1 
ATOM   1429 C CG  . ASP   A 1 187 ? 133.19974 -30.79235 21.02153  1.000 20.61777 ?  187 ASP   A CG  1 
ATOM   1430 O OD1 . ASP   A 1 187 ? 134.32378 -30.32494 21.29808  1.000 21.47272 ?  187 ASP   A OD1 1 
ATOM   1431 O OD2 . ASP   A 1 187 ? 133.00416 -32.01214 20.83461  1.000 18.22814 -1 187 ASP   A OD2 1 
ATOM   1432 N N   . ARG   A 1 188 ? 131.89479 -27.06356 23.26180  1.000 19.19960 ?  188 ARG   A N   1 
ATOM   1433 C CA  . ARG   A 1 188 ? 131.76432 -26.70828 24.66263  1.000 20.43731 ?  188 ARG   A CA  1 
ATOM   1434 C C   . ARG   A 1 188 ? 130.76483 -25.56514 24.76691  1.000 24.57035 ?  188 ARG   A C   1 
ATOM   1435 O O   . ARG   A 1 188 ? 130.71782 -24.70389 23.88621  1.000 21.61496 ?  188 ARG   A O   1 
ATOM   1436 C CB  . ARG   A 1 188 ? 133.13662 -26.31515 25.23097  1.000 22.24156 ?  188 ARG   A CB  1 
ATOM   1437 C CG  . ARG   A 1 188 ? 133.07032 -25.39351 26.41195  1.000 27.14894 ?  188 ARG   A CG  1 
ATOM   1438 C CD  . ARG   A 1 188 ? 134.44750 -25.00901 26.91292  1.000 29.37454 ?  188 ARG   A CD  1 
ATOM   1439 N NE  . ARG   A 1 188 ? 134.37617 -24.52375 28.28167  1.000 33.19401 ?  188 ARG   A NE  1 
ATOM   1440 C CZ  . ARG   A 1 188 ? 135.37043 -23.90801 28.90297  1.000 34.98423 ?  188 ARG   A CZ  1 
ATOM   1441 N NH1 . ARG   A 1 188 ? 136.54534 -23.73460 28.31905  1.000 35.24323 ?  188 ARG   A NH1 1 
ATOM   1442 N NH2 . ARG   A 1 188 ? 135.17473 -23.43942 30.13141  1.000 35.70156 ?  188 ARG   A NH2 1 
ATOM   1443 N N   . GLN   A 1 189 ? 129.95957 -25.56275 25.83392  1.000 21.41268 ?  189 GLN   A N   1 
ATOM   1444 C CA  . GLN   A 1 189 ? 128.98989 -24.48674 26.05093  1.000 25.43479 ?  189 GLN   A CA  1 
ATOM   1445 C C   . GLN   A 1 189 ? 129.71279 -23.27728 26.63796  1.000 26.28200 ?  189 GLN   A C   1 
ATOM   1446 O O   . GLN   A 1 189 ? 129.72379 -23.02051 27.84721  1.000 26.29130 ?  189 GLN   A O   1 
ATOM   1447 C CB  . GLN   A 1 189 ? 127.83985 -24.95121 26.93700  1.000 24.21109 ?  189 GLN   A CB  1 
ATOM   1448 C CG  . GLN   A 1 189 ? 126.78083 -23.87186 27.18429  1.000 28.06946 ?  189 GLN   A CG  1 
ATOM   1449 C CD  . GLN   A 1 189 ? 125.60125 -24.40514 27.96436  1.000 30.07033 ?  189 GLN   A CD  1 
ATOM   1450 O OE1 . GLN   A 1 189 ? 125.23541 -25.56797 27.80387  1.000 32.64820 ?  189 GLN   A OE1 1 
ATOM   1451 N NE2 . GLN   A 1 189 ? 125.00635 -23.57076 28.82270  1.000 28.04430 ?  189 GLN   A NE2 1 
ATOM   1452 N N   . THR   A 1 190 ? 130.33177 -22.51267 25.74457  1.000 25.43060 ?  190 THR   A N   1 
ATOM   1453 C CA  . THR   A 1 190 ? 130.99934 -21.27539 26.11555  1.000 28.57331 ?  190 THR   A CA  1 
ATOM   1454 C C   . THR   A 1 190 ? 130.77252 -20.29173 24.97955  1.000 31.46117 ?  190 THR   A C   1 
ATOM   1455 O O   . THR   A 1 190 ? 130.42606 -20.68435 23.86342  1.000 31.97707 ?  190 THR   A O   1 
ATOM   1456 C CB  . THR   A 1 190 ? 132.49895 -21.50608 26.40253  1.000 30.90856 ?  190 THR   A CB  1 
ATOM   1457 O OG1 . THR   A 1 190 ? 133.06747 -20.34874 27.03213  1.000 33.08235 ?  190 THR   A OG1 1 
ATOM   1458 C CG2 . THR   A 1 190 ? 133.25436 -21.83175 25.12450  1.000 32.50365 ?  190 THR   A CG2 1 
ATOM   1459 N N   . ALA   A 1 191 ? 130.91361 -19.00443 25.28409  1.000 32.28274 ?  191 ALA   A N   1 
ATOM   1460 C CA  . ALA   A 1 191 ? 130.75253 -17.97970 24.26112  1.000 32.06296 ?  191 ALA   A CA  1 
ATOM   1461 C C   . ALA   A 1 191 ? 131.84777 -18.12080 23.21423  1.000 28.69959 ?  191 ALA   A C   1 
ATOM   1462 O O   . ALA   A 1 191 ? 133.03184 -18.21076 23.55409  1.000 31.04481 ?  191 ALA   A O   1 
ATOM   1463 C CB  . ALA   A 1 191 ? 130.79540 -16.59036 24.89329  1.000 34.39378 ?  191 ALA   A CB  1 
ATOM   1464 N N   . GLN   A 1 192 ? 131.45689 -18.15830 21.94158  1.000 28.83573 ?  192 GLN   A N   1 
ATOM   1465 C CA  . GLN   A 1 192 ? 132.39628 -18.38433 20.85140  1.000 27.81949 ?  192 GLN   A CA  1 
ATOM   1466 C C   . GLN   A 1 192 ? 132.12602 -17.41096 19.71715  1.000 30.80672 ?  192 GLN   A C   1 
ATOM   1467 O O   . GLN   A 1 192 ? 130.98517 -17.26643 19.26422  1.000 29.42221 ?  192 GLN   A O   1 
ATOM   1468 C CB  . GLN   A 1 192 ? 132.32563 -19.83030 20.35675  1.000 27.53226 ?  192 GLN   A CB  1 
ATOM   1469 C CG  . GLN   A 1 192 ? 132.87761 -20.79473 21.38642  1.000 24.74951 ?  192 GLN   A CG  1 
ATOM   1470 C CD  . GLN   A 1 192 ? 132.96251 -22.20978 20.89988  1.000 23.80495 ?  192 GLN   A CD  1 
ATOM   1471 O OE1 . GLN   A 1 192 ? 133.68775 -22.51889 19.95277  1.000 20.50953 ?  192 GLN   A OE1 1 
ATOM   1472 N NE2 . GLN   A 1 192 ? 132.24528 -23.09823 21.56951  1.000 25.40280 ?  192 GLN   A NE2 1 
ATOM   1473 N N   . ALA   A 1 193 ? 133.18537 -16.75378 19.26472  1.000 29.42627 ?  193 ALA   A N   1 
ATOM   1474 C CA  . ALA   A 1 193 ? 133.08666 -15.73603 18.23656  1.000 29.80674 ?  193 ALA   A CA  1 
ATOM   1475 C C   . ALA   A 1 193 ? 133.31195 -16.36272 16.86803  1.000 29.29201 ?  193 ALA   A C   1 
ATOM   1476 O O   . ALA   A 1 193 ? 134.30608 -17.05906 16.64728  1.000 26.92174 ?  193 ALA   A O   1 
ATOM   1477 C CB  . ALA   A 1 193 ? 134.11129 -14.62446 18.48806  1.000 31.18272 ?  193 ALA   A CB  1 
ATOM   1478 N N   . ALA   A 1 194 ? 132.37745 -16.13494 15.96437  1.000 27.03524 ?  194 ALA   A N   1 
ATOM   1479 C CA  . ALA   A 1 194 ? 132.66301 -16.29844 14.55611  1.000 30.40058 ?  194 ALA   A CA  1 
ATOM   1480 C C   . ALA   A 1 194 ? 133.24463 -14.98567 14.05402  1.000 31.74507 ?  194 ALA   A C   1 
ATOM   1481 O O   . ALA   A 1 194 ? 132.92919 -13.91260 14.57073  1.000 39.06731 ?  194 ALA   A O   1 
ATOM   1482 C CB  . ALA   A 1 194 ? 131.39599 -16.67293 13.78909  1.000 25.55532 ?  194 ALA   A CB  1 
ATOM   1483 N N   . GLY   A 1 195 ? 134.11527 -15.06803 13.06612  1.000 33.37916 ?  195 GLY   A N   1 
ATOM   1484 C CA  . GLY   A 1 195 ? 134.64519 -13.84743 12.48846  1.000 39.64295 ?  195 GLY   A CA  1 
ATOM   1485 C C   . GLY   A 1 195 ? 133.54905 -13.04473 11.81935  1.000 31.40040 ?  195 GLY   A C   1 
ATOM   1486 O O   . GLY   A 1 195 ? 132.40713 -13.48374 11.67628  1.000 27.42666 ?  195 GLY   A O   1 
ATOM   1487 N N   . THR   A 1 196 ? 133.89844 -11.83271 11.40334  1.000 28.32278 ?  196 THR   A N   1 
ATOM   1488 C CA  . THR   A 1 196 ? 132.99564 -11.12832 10.51037  1.000 28.27091 ?  196 THR   A CA  1 
ATOM   1489 C C   . THR   A 1 196 ? 132.76660 -12.00292 9.28408   1.000 29.46991 ?  196 THR   A C   1 
ATOM   1490 O O   . THR   A 1 196 ? 133.68863 -12.66717 8.79599   1.000 28.69553 ?  196 THR   A O   1 
ATOM   1491 C CB  . THR   A 1 196 ? 133.55746 -9.76696  10.09676  1.000 33.84496 ?  196 THR   A CB  1 
ATOM   1492 O OG1 . THR   A 1 196 ? 134.52737 -9.94846  9.06465   1.000 43.19552 ?  196 THR   A OG1 1 
ATOM   1493 C CG2 . THR   A 1 196 ? 134.21885 -9.06855  11.26726  1.000 28.58226 ?  196 THR   A CG2 1 
ATOM   1494 N N   . ASP   A 1 197 ? 131.53087 -12.05850 8.82268   1.000 29.38942 ?  197 ASP   A N   1 
ATOM   1495 C CA  . ASP   A 1 197 ? 131.26683 -12.84560 7.63223   1.000 30.74606 ?  197 ASP   A CA  1 
ATOM   1496 C C   . ASP   A 1 197 ? 131.38190 -11.94374 6.41712   1.000 32.83303 ?  197 ASP   A C   1 
ATOM   1497 O O   . ASP   A 1 197 ? 131.27728 -10.71764 6.51684   1.000 33.24431 ?  197 ASP   A O   1 
ATOM   1498 C CB  . ASP   A 1 197 ? 129.89300 -13.49389 7.67043   1.000 31.91284 ?  197 ASP   A CB  1 
ATOM   1499 C CG  . ASP   A 1 197 ? 129.78726 -14.69455 6.73429   1.000 27.90451 ?  197 ASP   A CG  1 
ATOM   1500 O OD1 . ASP   A 1 197 ? 130.82773 -15.22233 6.24261   1.000 24.28585 -1 197 ASP   A OD1 1 
ATOM   1501 O OD2 . ASP   A 1 197 ? 128.63983 -15.08633 6.47359   1.000 24.81041 ?  197 ASP   A OD2 1 
ATOM   1502 N N   . THR   A 1 198 ? 131.64564 -12.55939 5.27446   1.000 28.39787 ?  198 THR   A N   1 
ATOM   1503 C CA  . THR   A 1 198 ? 131.71644 -11.84733 4.01088   1.000 28.30124 ?  198 THR   A CA  1 
ATOM   1504 C C   . THR   A 1 198 ? 130.76797 -12.50624 3.01603   1.000 25.01861 ?  198 THR   A C   1 
ATOM   1505 O O   . THR   A 1 198 ? 130.32434 -13.63973 3.21247   1.000 24.52096 ?  198 THR   A O   1 
ATOM   1506 C CB  . THR   A 1 198 ? 133.15496 -11.81696 3.47056   1.000 31.06450 ?  198 THR   A CB  1 
ATOM   1507 O OG1 . THR   A 1 198 ? 133.63033 -13.15415 3.28237   1.000 33.06917 ?  198 THR   A OG1 1 
ATOM   1508 C CG2 . THR   A 1 198 ? 134.06929 -11.09136 4.44027   1.000 36.01941 ?  198 THR   A CG2 1 
ATOM   1509 N N   . THR   A 1 199 ? 130.41779 -11.76234 1.96904   1.000 24.61561 ?  199 THR   A N   1 
ATOM   1510 C CA  . THR   A 1 199 ? 129.53647 -12.28120 0.93227   1.000 20.90265 ?  199 THR   A CA  1 
ATOM   1511 C C   . THR   A 1 199 ? 130.34306 -13.03030 -0.11922  1.000 24.67191 ?  199 THR   A C   1 
ATOM   1512 O O   . THR   A 1 199 ? 131.41812 -12.58777 -0.52751  1.000 22.77036 ?  199 THR   A O   1 
ATOM   1513 C CB  . THR   A 1 199 ? 128.74022 -11.15333 0.27944   1.000 26.98877 ?  199 THR   A CB  1 
ATOM   1514 O OG1 . THR   A 1 199 ? 128.02351 -10.43883 1.28650   1.000 26.97256 ?  199 THR   A OG1 1 
ATOM   1515 C CG2 . THR   A 1 199 ? 127.75061 -11.70514 -0.73126  1.000 21.93765 ?  199 THR   A CG2 1 
ATOM   1516 N N   . ILE   A 1 200 ? 129.81077 -14.17171 -0.55553  1.000 21.79324 ?  200 ILE   A N   1 
ATOM   1517 C CA  . ILE   A 1 200 ? 130.49813 -15.03692 -1.51355  1.000 22.33200 ?  200 ILE   A CA  1 
ATOM   1518 C C   . ILE   A 1 200 ? 130.28310 -14.45005 -2.90457  1.000 21.99446 ?  200 ILE   A C   1 
ATOM   1519 O O   . ILE   A 1 200 ? 129.26111 -14.69488 -3.55017  1.000 20.12143 ?  200 ILE   A O   1 
ATOM   1520 C CB  . ILE   A 1 200 ? 130.01047 -16.48319 -1.42151  1.000 20.92125 ?  200 ILE   A CB  1 
ATOM   1521 C CG1 . ILE   A 1 200 ? 129.99031 -16.93389 0.04117   1.000 22.85373 ?  200 ILE   A CG1 1 
ATOM   1522 C CG2 . ILE   A 1 200 ? 130.88757 -17.39574 -2.27906  1.000 22.10651 ?  200 ILE   A CG2 1 
ATOM   1523 C CD1 . ILE   A 1 200 ? 129.03381 -18.09697 0.32603   1.000 19.56588 ?  200 ILE   A CD1 1 
ATOM   1524 N N   . THR   A 1 201 ? 131.26950 -13.68560 -3.37431  1.000 21.81995 ?  201 THR   A N   1 
ATOM   1525 C CA  . THR   A 1 201 ? 131.08496 -12.86254 -4.56944  1.000 21.32776 ?  201 THR   A CA  1 
ATOM   1526 C C   . THR   A 1 201 ? 130.83212 -13.71261 -5.80454  1.000 21.40289 ?  201 THR   A C   1 
ATOM   1527 O O   . THR   A 1 201 ? 129.98205 -13.37155 -6.63650  1.000 22.10971 ?  201 THR   A O   1 
ATOM   1528 C CB  . THR   A 1 201 ? 132.31389 -11.98321 -4.77222  1.000 25.11420 ?  201 THR   A CB  1 
ATOM   1529 O OG1 . THR   A 1 201 ? 132.59229 -11.26095 -3.56197  1.000 25.46459 ?  201 THR   A OG1 1 
ATOM   1530 C CG2 . THR   A 1 201 ? 132.12610 -11.01617 -5.94527  1.000 25.62033 ?  201 THR   A CG2 1 
ATOM   1531 N N   . VAL   A 1 202 ? 131.57312 -14.81190 -5.95772  1.000 20.86673 ?  202 VAL   A N   1 
ATOM   1532 C CA  . VAL   A 1 202 ? 131.41531 -15.59037 -7.17960  1.000 23.03818 ?  202 VAL   A CA  1 
ATOM   1533 C C   . VAL   A 1 202 ? 130.01741 -16.20801 -7.21519  1.000 22.56258 ?  202 VAL   A C   1 
ATOM   1534 O O   . VAL   A 1 202 ? 129.44342 -16.40585 -8.29299  1.000 20.92295 ?  202 VAL   A O   1 
ATOM   1535 C CB  . VAL   A 1 202 ? 132.51377 -16.66568 -7.28599  1.000 23.19754 ?  202 VAL   A CB  1 
ATOM   1536 C CG1 . VAL   A 1 202 ? 132.52233 -17.55962 -6.04003  1.000 24.71712 ?  202 VAL   A CG1 1 
ATOM   1537 C CG2 . VAL   A 1 202 ? 132.41285 -17.44677 -8.61103  1.000 22.98128 ?  202 VAL   A CG2 1 
ATOM   1538 N N   . ASN   A 1 203 ? 129.43787 -16.48892 -6.04360  1.000 20.77148 ?  203 ASN   A N   1 
ATOM   1539 C CA  . ASN   A 1 203 ? 128.07768 -17.03121 -5.97312  1.000 18.63921 ?  203 ASN   A CA  1 
ATOM   1540 C C   . ASN   A 1 203 ? 127.04113 -15.98424 -6.36733  1.000 21.76362 ?  203 ASN   A C   1 
ATOM   1541 O O   . ASN   A 1 203 ? 126.05754 -16.29940 -7.04984  1.000 20.01941 ?  203 ASN   A O   1 
ATOM   1542 C CB  . ASN   A 1 203 ? 127.79585 -17.54924 -4.55668  1.000 21.24586 ?  203 ASN   A CB  1 
ATOM   1543 C CG  . ASN   A 1 203 ? 128.49473 -18.84905 -4.26627  1.000 18.94218 ?  203 ASN   A CG  1 
ATOM   1544 O OD1 . ASN   A 1 203 ? 129.31747 -19.30773 -5.05095  1.000 20.98292 ?  203 ASN   A OD1 1 
ATOM   1545 N ND2 . ASN   A 1 203 ? 128.15161 -19.47225 -3.14113  1.000 18.06302 ?  203 ASN   A ND2 1 
ATOM   1546 N N   . VAL   A 1 204 ? 127.24334 -14.72739 -5.95814  1.000 23.22676 ?  204 VAL   A N   1 
ATOM   1547 C CA  . VAL   A 1 204 ? 126.29838 -13.67996 -6.33663  1.000 20.75875 ?  204 VAL   A CA  1 
ATOM   1548 C C   . VAL   A 1 204 ? 126.31148 -13.48199 -7.84731  1.000 23.17884 ?  204 VAL   A C   1 
ATOM   1549 O O   . VAL   A 1 204 ? 125.25965 -13.31420 -8.47305  1.000 25.28987 ?  204 VAL   A O   1 
ATOM   1550 C CB  . VAL   A 1 204 ? 126.61887 -12.37051 -5.59597  1.000 24.15849 ?  204 VAL   A CB  1 
ATOM   1551 C CG1 . VAL   A 1 204 ? 125.83320 -11.20363 -6.19197  1.000 23.86277 ?  204 VAL   A CG1 1 
ATOM   1552 C CG2 . VAL   A 1 204 ? 126.39064 -12.53505 -4.09749  1.000 21.38341 ?  204 VAL   A CG2 1 
ATOM   1553 N N   . LEU   A 1 205 ? 127.50064 -13.49291 -8.44945  1.000 22.19745 ?  205 LEU   A N   1 
ATOM   1554 C CA  . LEU   A 1 205 ? 127.60461 -13.38327 -9.89945  1.000 25.36829 ?  205 LEU   A CA  1 
ATOM   1555 C C   . LEU   A 1 205 ? 126.91989 -14.54846 -10.59501 1.000 22.90768 ?  205 LEU   A C   1 
ATOM   1556 O O   . LEU   A 1 205 ? 126.24526 -14.35443 -11.61041 1.000 23.71289 ?  205 LEU   A O   1 
ATOM   1557 C CB  . LEU   A 1 205 ? 129.07567 -13.29094 -10.31599 1.000 23.99857 ?  205 LEU   A CB  1 
ATOM   1558 C CG  . LEU   A 1 205 ? 129.80044 -12.05439 -9.79271  1.000 24.72912 ?  205 LEU   A CG  1 
ATOM   1559 C CD1 . LEU   A 1 205 ? 131.27937 -12.16506 -10.05062 1.000 25.90089 ?  205 LEU   A CD1 1 
ATOM   1560 C CD2 . LEU   A 1 205 ? 129.25392 -10.83959 -10.54596 1.000 27.83891 ?  205 LEU   A CD2 1 
ATOM   1561 N N   . ALA   A 1 206 ? 127.09331 -15.76857 -10.07930 1.000 21.82978 ?  206 ALA   A N   1 
ATOM   1562 C CA  . ALA   A 1 206 ? 126.40103 -16.90257 -10.68482 1.000 22.76506 ?  206 ALA   A CA  1 
ATOM   1563 C C   . ALA   A 1 206 ? 124.89714 -16.68004 -10.66279 1.000 24.65905 ?  206 ALA   A C   1 
ATOM   1564 O O   . ALA   A 1 206 ? 124.19845 -16.96483 -11.64188 1.000 22.85164 ?  206 ALA   A O   1 
ATOM   1565 C CB  . ALA   A 1 206 ? 126.76938 -18.19870 -9.96455  1.000 20.51848 ?  206 ALA   A CB  1 
ATOM   1566 N N   . TRP   A 1 207 ? 124.39092 -16.13733 -9.55747  1.000 22.32782 ?  207 TRP   A N   1 
ATOM   1567 C CA  . TRP   A 1 207 ? 122.96061 -15.90942 -9.40664  1.000 25.04311 ?  207 TRP   A CA  1 
ATOM   1568 C C   . TRP   A 1 207 ? 122.48855 -14.79256 -10.33124 1.000 24.42936 ?  207 TRP   A C   1 
ATOM   1569 O O   . TRP   A 1 207 ? 121.40416 -14.87890 -10.92038 1.000 26.15101 ?  207 TRP   A O   1 
ATOM   1570 C CB  . TRP   A 1 207 ? 122.69183 -15.59863 -7.93452  1.000 23.22542 ?  207 TRP   A CB  1 
ATOM   1571 C CG  . TRP   A 1 207 ? 121.31644 -15.22027 -7.51942  1.000 24.74371 ?  207 TRP   A CG  1 
ATOM   1572 C CD1 . TRP   A 1 207 ? 120.24917 -16.04897 -7.31889  1.000 25.53858 ?  207 TRP   A CD1 1 
ATOM   1573 C CD2 . TRP   A 1 207 ? 120.87447 -13.90461 -7.19238  1.000 25.26445 ?  207 TRP   A CD2 1 
ATOM   1574 N NE1 . TRP   A 1 207 ? 119.15818 -15.31434 -6.89992  1.000 27.03450 ?  207 TRP   A NE1 1 
ATOM   1575 C CE2 . TRP   A 1 207 ? 119.52141 -13.99677 -6.81632  1.000 27.57588 ?  207 TRP   A CE2 1 
ATOM   1576 C CE3 . TRP   A 1 207 ? 121.49505 -12.65070 -7.18724  1.000 27.09935 ?  207 TRP   A CE3 1 
ATOM   1577 C CZ2 . TRP   A 1 207 ? 118.78104 -12.88795 -6.44074  1.000 28.69066 ?  207 TRP   A CZ2 1 
ATOM   1578 C CZ3 . TRP   A 1 207 ? 120.75558 -11.54944 -6.81745  1.000 29.91243 ?  207 TRP   A CZ3 1 
ATOM   1579 C CH2 . TRP   A 1 207 ? 119.41490 -11.67497 -6.44847  1.000 28.39434 ?  207 TRP   A CH2 1 
ATOM   1580 N N   . LEU   A 1 208 ? 123.30377 -13.74749 -10.49774 1.000 23.68551 ?  208 LEU   A N   1 
ATOM   1581 C CA  . LEU   A 1 208 ? 123.00200 -12.73532 -11.50781 1.000 24.52834 ?  208 LEU   A CA  1 
ATOM   1582 C C   . LEU   A 1 208 ? 122.93085 -13.34971 -12.90159 1.000 26.47090 ?  208 LEU   A C   1 
ATOM   1583 O O   . LEU   A 1 208 ? 122.06805 -12.98049 -13.70556 1.000 28.11394 ?  208 LEU   A O   1 
ATOM   1584 C CB  . LEU   A 1 208 ? 124.05225 -11.62370 -11.46012 1.000 25.31175 ?  208 LEU   A CB  1 
ATOM   1585 C CG  . LEU   A 1 208 ? 123.93809 -10.68497 -10.25773 1.000 26.69900 ?  208 LEU   A CG  1 
ATOM   1586 C CD1 . LEU   A 1 208 ? 124.90495 -9.51803  -10.37672 1.000 28.86300 ?  208 LEU   A CD1 1 
ATOM   1587 C CD2 . LEU   A 1 208 ? 122.50427 -10.17323 -10.10773 1.000 29.03469 ?  208 LEU   A CD2 1 
ATOM   1588 N N   . TYR   A 1 209 ? 123.83150 -14.28685 -13.21081 1.000 25.94218 ?  209 TYR   A N   1 
ATOM   1589 C CA  . TYR   A 1 209 ? 123.73292 -14.98514 -14.48746 1.000 25.78459 ?  209 TYR   A CA  1 
ATOM   1590 C C   . TYR   A 1 209 ? 122.44383 -15.79320 -14.54908 1.000 26.99743 ?  209 TYR   A C   1 
ATOM   1591 O O   . TYR   A 1 209 ? 121.76821 -15.82330 -15.58443 1.000 29.47284 ?  209 TYR   A O   1 
ATOM   1592 C CB  . TYR   A 1 209 ? 124.94253 -15.89635 -14.69409 1.000 26.03282 ?  209 TYR   A CB  1 
ATOM   1593 C CG  . TYR   A 1 209 ? 126.13577 -15.19126 -15.28665 1.000 30.21795 ?  209 TYR   A CG  1 
ATOM   1594 C CD1 . TYR   A 1 209 ? 126.17023 -14.83708 -16.62668 1.000 31.53905 ?  209 TYR   A CD1 1 
ATOM   1595 C CD2 . TYR   A 1 209 ? 127.24079 -14.89100 -14.49559 1.000 27.92078 ?  209 TYR   A CD2 1 
ATOM   1596 C CE1 . TYR   A 1 209 ? 127.26360 -14.18373 -17.16467 1.000 31.99441 ?  209 TYR   A CE1 1 
ATOM   1597 C CE2 . TYR   A 1 209 ? 128.33088 -14.23769 -15.01898 1.000 29.02888 ?  209 TYR   A CE2 1 
ATOM   1598 C CZ  . TYR   A 1 209 ? 128.34334 -13.88842 -16.34831 1.000 33.65256 ?  209 TYR   A CZ  1 
ATOM   1599 O OH  . TYR   A 1 209 ? 129.44404 -13.24220 -16.85820 1.000 34.43943 ?  209 TYR   A OH  1 
ATOM   1600 N N   . ALA   A 1 210 ? 122.08511 -16.44586 -13.43966 1.000 28.00581 ?  210 ALA   A N   1 
ATOM   1601 C CA  . ALA   A 1 210 ? 120.81644 -17.16647 -13.37400 1.000 26.88057 ?  210 ALA   A CA  1 
ATOM   1602 C C   . ALA   A 1 210 ? 119.64711 -16.23515 -13.65891 1.000 27.71908 ?  210 ALA   A C   1 
ATOM   1603 O O   . ALA   A 1 210 ? 118.71347 -16.59752 -14.38588 1.000 30.54728 ?  210 ALA   A O   1 
ATOM   1604 C CB  . ALA   A 1 210 ? 120.65788 -17.82558 -12.00004 1.000 25.68580 ?  210 ALA   A CB  1 
ATOM   1605 N N   . ALA   A 1 211 ? 119.69167 -15.02236 -13.10695 1.000 25.90485 ?  211 ALA   A N   1 
ATOM   1606 C CA  . ALA   A 1 211 ? 118.61513 -14.06167 -13.32112 1.000 30.63606 ?  211 ALA   A CA  1 
ATOM   1607 C C   . ALA   A 1 211 ? 118.47313 -13.71564 -14.79488 1.000 32.30307 ?  211 ALA   A C   1 
ATOM   1608 O O   . ALA   A 1 211 ? 117.36298 -13.70993 -15.33494 1.000 32.85240 ?  211 ALA   A O   1 
ATOM   1609 C CB  . ALA   A 1 211 ? 118.86401 -12.79897 -12.49727 1.000 31.38477 ?  211 ALA   A CB  1 
ATOM   1610 N N   . VAL   A 1 212 ? 119.59277 -13.42196 -15.46193 1.000 29.92907 ?  212 VAL   A N   1 
ATOM   1611 C CA  . VAL   A 1 212 ? 119.54727 -13.08255 -16.88153 1.000 32.69964 ?  212 VAL   A CA  1 
ATOM   1612 C C   . VAL   A 1 212 ? 119.00032 -14.24839 -17.68687 1.000 32.41761 ?  212 VAL   A C   1 
ATOM   1613 O O   . VAL   A 1 212 ? 118.22573 -14.05890 -18.63247 1.000 37.08241 ?  212 VAL   A O   1 
ATOM   1614 C CB  . VAL   A 1 212 ? 120.93989 -12.65417 -17.38674 1.000 32.06017 ?  212 VAL   A CB  1 
ATOM   1615 C CG1 . VAL   A 1 212 ? 120.87726 -12.25798 -18.85357 1.000 35.04827 ?  212 VAL   A CG1 1 
ATOM   1616 C CG2 . VAL   A 1 212 ? 121.46179 -11.49009 -16.56741 1.000 33.79294 ?  212 VAL   A CG2 1 
ATOM   1617 N N   . ILE   A 1 213 ? 119.40067 -15.47126 -17.33474 1.000 31.87193 ?  213 ILE   A N   1 
ATOM   1618 C CA  . ILE   A 1 213 ? 118.89272 -16.64065 -18.04264 1.000 32.81487 ?  213 ILE   A CA  1 
ATOM   1619 C C   . ILE   A 1 213 ? 117.38261 -16.73676 -17.89064 1.000 34.94633 ?  213 ILE   A C   1 
ATOM   1620 O O   . ILE   A 1 213 ? 116.68401 -17.17491 -18.81307 1.000 39.19908 ?  213 ILE   A O   1 
ATOM   1621 C CB  . ILE   A 1 213 ? 119.60031 -17.91079 -17.53612 1.000 33.46952 ?  213 ILE   A CB  1 
ATOM   1622 C CG1 . ILE   A 1 213 ? 121.08323 -17.88655 -17.92207 1.000 33.23653 ?  213 ILE   A CG1 1 
ATOM   1623 C CG2 . ILE   A 1 213 ? 118.94579 -19.15038 -18.10841 1.000 39.27109 ?  213 ILE   A CG2 1 
ATOM   1624 C CD1 . ILE   A 1 213 ? 121.89130 -19.01877 -17.31272 1.000 33.50450 ?  213 ILE   A CD1 1 
ATOM   1625 N N   . ASN   A 1 214 ? 116.84734 -16.29592 -16.75070 1.000 32.69853 ?  214 ASN   A N   1 
ATOM   1626 C CA  . ASN   A 1 214 ? 115.43220 -16.45968 -16.44603 1.000 37.44666 ?  214 ASN   A CA  1 
ATOM   1627 C C   . ASN   A 1 214 ? 114.60796 -15.20136 -16.71027 1.000 43.61419 ?  214 ASN   A C   1 
ATOM   1628 O O   . ASN   A 1 214 ? 113.46946 -15.10714 -16.23961 1.000 52.20976 ?  214 ASN   A O   1 
ATOM   1629 C CB  . ASN   A 1 214 ? 115.25463 -16.91460 -14.99996 1.000 38.32682 ?  214 ASN   A CB  1 
ATOM   1630 C CG  . ASN   A 1 214 ? 115.45770 -18.39908 -14.84146 1.000 39.34830 ?  214 ASN   A CG  1 
ATOM   1631 O OD1 . ASN   A 1 214 ? 114.50625 -19.17524 -14.92044 1.000 45.17020 ?  214 ASN   A OD1 1 
ATOM   1632 N ND2 . ASN   A 1 214 ? 116.70319 -18.80751 -14.59707 1.000 38.35966 ?  214 ASN   A ND2 1 
ATOM   1633 N N   . GLY   A 1 215 ? 115.14833 -14.23592 -17.45047 1.000 38.80201 ?  215 GLY   A N   1 
ATOM   1634 C CA  . GLY   A 1 215 ? 114.37906 -13.10722 -17.92463 1.000 40.34902 ?  215 GLY   A CA  1 
ATOM   1635 C C   . GLY   A 1 215 ? 114.57822 -11.80881 -17.16583 1.000 43.38478 ?  215 GLY   A C   1 
ATOM   1636 O O   . GLY   A 1 215 ? 114.19657 -10.75042 -17.68226 1.000 40.29926 ?  215 GLY   A O   1 
ATOM   1637 N N   . ASP   A 1 216 ? 115.14158 -11.85507 -15.95644 1.000 37.71193 ?  216 ASP   A N   1 
ATOM   1638 C CA  . ASP   A 1 216 ? 115.45668 -10.63896 -15.20718 1.000 40.38960 ?  216 ASP   A CA  1 
ATOM   1639 C C   . ASP   A 1 216 ? 116.73002 -10.02195 -15.77167 1.000 42.03472 ?  216 ASP   A C   1 
ATOM   1640 O O   . ASP   A 1 216 ? 117.81081 -10.60876 -15.65972 1.000 48.21528 ?  216 ASP   A O   1 
ATOM   1641 C CB  . ASP   A 1 216 ? 115.63460 -10.93899 -13.72273 1.000 39.91100 ?  216 ASP   A CB  1 
ATOM   1642 C CG  . ASP   A 1 216 ? 114.36472 -10.74956 -12.92747 1.000 46.62801 ?  216 ASP   A CG  1 
ATOM   1643 O OD1 . ASP   A 1 216 ? 113.63393 -9.77192  -13.19587 1.000 56.00453 -1 216 ASP   A OD1 1 
ATOM   1644 O OD2 . ASP   A 1 216 ? 114.11380 -11.56068 -12.00948 1.000 48.55962 ?  216 ASP   A OD2 1 
ATOM   1645 N N   . ARG   A 1 217 ? 116.61877 -8.82933  -16.35420 1.000 40.82000 ?  217 ARG   A N   1 
ATOM   1646 C CA  . ARG   A 1 217 ? 117.78212 -8.19375  -16.95735 1.000 39.62634 ?  217 ARG   A CA  1 
ATOM   1647 C C   . ARG   A 1 217 ? 117.86788 -6.70118  -16.65528 1.000 41.56834 ?  217 ARG   A C   1 
ATOM   1648 O O   . ARG   A 1 217 ? 118.76074 -6.03085  -17.18797 1.000 38.54987 ?  217 ARG   A O   1 
ATOM   1649 C CB  . ARG   A 1 217 ? 117.78742 -8.42276  -18.47389 1.000 41.03878 ?  217 ARG   A CB  1 
ATOM   1650 N N   . TRP   A 1 218 ? 116.99186 -6.16665  -15.79814 1.000 42.94875 ?  218 TRP   A N   1 
ATOM   1651 C CA  . TRP   A 1 218 ? 116.95300 -4.72474  -15.56270 1.000 43.04047 ?  218 TRP   A CA  1 
ATOM   1652 C C   . TRP   A 1 218 ? 118.24242 -4.20152  -14.93871 1.000 42.92776 ?  218 TRP   A C   1 
ATOM   1653 O O   . TRP   A 1 218 ? 118.60622 -3.03867  -15.15730 1.000 44.02751 ?  218 TRP   A O   1 
ATOM   1654 C CB  . TRP   A 1 218 ? 115.74680 -4.37355  -14.68428 1.000 44.47642 ?  218 TRP   A CB  1 
ATOM   1655 C CG  . TRP   A 1 218 ? 115.75672 -5.01388  -13.31279 1.000 43.34652 ?  218 TRP   A CG  1 
ATOM   1656 C CD1 . TRP   A 1 218 ? 115.09063 -6.14213  -12.93436 1.000 42.90325 ?  218 TRP   A CD1 1 
ATOM   1657 C CD2 . TRP   A 1 218 ? 116.44626 -4.54746  -12.14500 1.000 43.45493 ?  218 TRP   A CD2 1 
ATOM   1658 N NE1 . TRP   A 1 218 ? 115.33136 -6.41447  -11.61025 1.000 42.94475 ?  218 TRP   A NE1 1 
ATOM   1659 C CE2 . TRP   A 1 218 ? 116.15958 -5.44950  -11.10236 1.000 42.90381 ?  218 TRP   A CE2 1 
ATOM   1660 C CE3 . TRP   A 1 218 ? 117.27816 -3.45521  -11.88070 1.000 44.91989 ?  218 TRP   A CE3 1 
ATOM   1661 C CZ2 . TRP   A 1 218 ? 116.67544 -5.29427  -9.81748  1.000 42.42794 ?  218 TRP   A CZ2 1 
ATOM   1662 C CZ3 . TRP   A 1 218 ? 117.79586 -3.30653  -10.60455 1.000 47.20086 ?  218 TRP   A CZ3 1 
ATOM   1663 C CH2 . TRP   A 1 218 ? 117.49200 -4.22163  -9.58894  1.000 45.57641 ?  218 TRP   A CH2 1 
ATOM   1664 N N   . PHE   A 1 219 ? 118.94577 -5.03283  -14.17278 1.000 42.51296 ?  219 PHE   A N   1 
ATOM   1665 C CA  . PHE   A 1 219 ? 120.14691 -4.60121  -13.46870 1.000 42.24267 ?  219 PHE   A CA  1 
ATOM   1666 C C   . PHE   A 1 219 ? 121.36308 -4.47871  -14.37995 1.000 41.55278 ?  219 PHE   A C   1 
ATOM   1667 O O   . PHE   A 1 219 ? 122.41276 -4.01558  -13.92209 1.000 42.34059 ?  219 PHE   A O   1 
ATOM   1668 C CB  . PHE   A 1 219 ? 120.46184 -5.57868  -12.33361 1.000 37.67719 ?  219 PHE   A CB  1 
ATOM   1669 C CG  . PHE   A 1 219 ? 120.48328 -7.00465  -12.76938 1.000 36.45945 ?  219 PHE   A CG  1 
ATOM   1670 C CD1 . PHE   A 1 219 ? 121.64751 -7.57278  -13.25469 1.000 36.86435 ?  219 PHE   A CD1 1 
ATOM   1671 C CD2 . PHE   A 1 219 ? 119.33915 -7.77789  -12.70929 1.000 36.84033 ?  219 PHE   A CD2 1 
ATOM   1672 C CE1 . PHE   A 1 219 ? 121.66764 -8.88335  -13.67602 1.000 35.25398 ?  219 PHE   A CE1 1 
ATOM   1673 C CE2 . PHE   A 1 219 ? 119.35313 -9.08240  -13.12578 1.000 34.48703 ?  219 PHE   A CE2 1 
ATOM   1674 C CZ  . PHE   A 1 219 ? 120.52199 -9.63750  -13.61300 1.000 32.32621 ?  219 PHE   A CZ  1 
ATOM   1675 N N   . LEU   A 1 220 ? 121.25739 -4.89900  -15.63714 1.000 41.29859 ?  220 LEU   A N   1 
ATOM   1676 C CA  . LEU   A 1 220 ? 122.37921 -4.79610  -16.55839 1.000 43.07714 ?  220 LEU   A CA  1 
ATOM   1677 C C   . LEU   A 1 220 ? 122.61447 -3.33331  -16.91513 1.000 45.41323 ?  220 LEU   A C   1 
ATOM   1678 O O   . LEU   A 1 220 ? 121.66768 -2.59780  -17.20417 1.000 43.90930 ?  220 LEU   A O   1 
ATOM   1679 C CB  . LEU   A 1 220 ? 122.10294 -5.61048  -17.82343 1.000 41.69954 ?  220 LEU   A CB  1 
ATOM   1680 C CG  . LEU   A 1 220 ? 121.88212 -7.11447  -17.62936 1.000 40.37762 ?  220 LEU   A CG  1 
ATOM   1681 C CD1 . LEU   A 1 220 ? 121.44612 -7.77550  -18.92974 1.000 37.77619 ?  220 LEU   A CD1 1 
ATOM   1682 C CD2 . LEU   A 1 220 ? 123.12599 -7.78296  -17.06836 1.000 42.23542 ?  220 LEU   A CD2 1 
ATOM   1683 N N   . ASN   A 1 221 ? 123.86915 -2.89980  -16.87759 1.000 47.32542 ?  221 ASN   A N   1 
ATOM   1684 C CA  . ASN   A 1 221 ? 124.17793 -1.52260  -17.22269 1.000 47.69623 ?  221 ASN   A CA  1 
ATOM   1685 C C   . ASN   A 1 221 ? 125.15781 -1.48590  -18.38837 1.000 50.24764 ?  221 ASN   A C   1 
ATOM   1686 O O   . ASN   A 1 221 ? 125.63057 -2.51725  -18.87431 1.000 49.95626 ?  221 ASN   A O   1 
ATOM   1687 C CB  . ASN   A 1 221 ? 124.72016 -0.75046  -16.01563 1.000 47.90107 ?  221 ASN   A CB  1 
ATOM   1688 C CG  . ASN   A 1 221 ? 126.05614 -1.27327  -15.51836 1.000 47.93737 ?  221 ASN   A CG  1 
ATOM   1689 O OD1 . ASN   A 1 221 ? 126.71699 -2.09331  -16.16279 1.000 48.96964 ?  221 ASN   A OD1 1 
ATOM   1690 N ND2 . ASN   A 1 221 ? 126.45904 -0.79499  -14.34720 1.000 47.52465 ?  221 ASN   A ND2 1 
ATOM   1691 N N   . ARG   A 1 222 ? 125.46253 -0.26679  -18.81890 1.000 47.99335 ?  222 ARG   A N   1 
ATOM   1692 C CA  . ARG   A 1 222 ? 126.34482 -0.00630  -19.94393 1.000 51.17966 ?  222 ARG   A CA  1 
ATOM   1693 C C   . ARG   A 1 222 ? 127.80364 0.13317   -19.53227 1.000 49.43541 ?  222 ARG   A C   1 
ATOM   1694 O O   . ARG   A 1 222 ? 128.63372 0.51549   -20.36543 1.000 48.14901 ?  222 ARG   A O   1 
ATOM   1695 C CB  . ARG   A 1 222 ? 125.88976 1.26014   -20.67401 1.000 50.80378 ?  222 ARG   A CB  1 
ATOM   1696 N N   . PHE   A 1 223 ? 128.13312 -0.16367  -18.27779 1.000 46.00741 ?  223 PHE   A N   1 
ATOM   1697 C CA  . PHE   A 1 223 ? 129.47565 0.02576   -17.75611 1.000 45.07013 ?  223 PHE   A CA  1 
ATOM   1698 C C   . PHE   A 1 223 ? 130.22692 -1.29474  -17.73425 1.000 43.87301 ?  223 PHE   A C   1 
ATOM   1699 O O   . PHE   A 1 223 ? 129.63398 -2.37482  -17.77034 1.000 41.40661 ?  223 PHE   A O   1 
ATOM   1700 C CB  . PHE   A 1 223 ? 129.45831 0.61444   -16.33765 1.000 45.60775 ?  223 PHE   A CB  1 
ATOM   1701 C CG  . PHE   A 1 223 ? 128.82082 1.97152   -16.23628 1.000 51.64032 ?  223 PHE   A CG  1 
ATOM   1702 C CD1 . PHE   A 1 223 ? 129.55582 3.04963   -15.76638 1.000 54.65288 ?  223 PHE   A CD1 1 
ATOM   1703 C CD2 . PHE   A 1 223 ? 127.48341 2.16597   -16.55580 1.000 52.78478 ?  223 PHE   A CD2 1 
ATOM   1704 C CE1 . PHE   A 1 223 ? 128.98861 4.30219   -15.65628 1.000 55.65807 ?  223 PHE   A CE1 1 
ATOM   1705 C CE2 . PHE   A 1 223 ? 126.90520 3.42233   -16.44771 1.000 56.19925 ?  223 PHE   A CE2 1 
ATOM   1706 C CZ  . PHE   A 1 223 ? 127.66142 4.49049   -15.99270 1.000 58.13066 ?  223 PHE   A CZ  1 
ATOM   1707 N N   . THR   A 1 224 ? 131.55157 -1.19318  -17.67778 1.000 43.68742 ?  224 THR   A N   1 
ATOM   1708 C CA  . THR   A 1 224 ? 132.38958 -2.32413  -17.31267 1.000 42.30960 ?  224 THR   A CA  1 
ATOM   1709 C C   . THR   A 1 224 ? 133.33577 -1.88221  -16.20319 1.000 42.26596 ?  224 THR   A C   1 
ATOM   1710 O O   . THR   A 1 224 ? 133.28058 -0.74369  -15.73453 1.000 43.26411 ?  224 THR   A O   1 
ATOM   1711 C CB  . THR   A 1 224 ? 133.16863 -2.87862  -18.50828 1.000 43.37470 ?  224 THR   A CB  1 
ATOM   1712 O OG1 . THR   A 1 224 ? 133.77766 -4.12199  -18.12274 1.000 41.85662 ?  224 THR   A OG1 1 
ATOM   1713 C CG2 . THR   A 1 224 ? 134.24529 -1.89861  -18.95096 1.000 45.76443 ?  224 THR   A CG2 1 
ATOM   1714 N N   . THR   A 1 225 ? 134.20025 -2.79612  -15.77326 1.000 41.21212 ?  225 THR   A N   1 
ATOM   1715 C CA  . THR   A 1 225 ? 135.15762 -2.51816  -14.70762 1.000 42.76137 ?  225 THR   A CA  1 
ATOM   1716 C C   . THR   A 1 225 ? 136.35345 -3.45300  -14.85424 1.000 42.23913 ?  225 THR   A C   1 
ATOM   1717 O O   . THR   A 1 225 ? 136.43877 -4.25074  -15.79287 1.000 41.01805 ?  225 THR   A O   1 
ATOM   1718 C CB  . THR   A 1 225 ? 134.51036 -2.65182  -13.32267 1.000 43.48217 ?  225 THR   A CB  1 
ATOM   1719 O OG1 . THR   A 1 225 ? 135.41044 -2.15658  -12.32212 1.000 45.25891 ?  225 THR   A OG1 1 
ATOM   1720 C CG2 . THR   A 1 225 ? 134.14398 -4.09943  -13.01646 1.000 39.18596 ?  225 THR   A CG2 1 
ATOM   1721 N N   . THR   A 1 226 ? 137.29243 -3.33203  -13.91897 1.000 42.03926 ?  226 THR   A N   1 
ATOM   1722 C CA  . THR   A 1 226 ? 138.46635 -4.18598  -13.87714 1.000 42.32226 ?  226 THR   A CA  1 
ATOM   1723 C C   . THR   A 1 226 ? 138.45220 -4.97975  -12.57955 1.000 41.62154 ?  226 THR   A C   1 
ATOM   1724 O O   . THR   A 1 226 ? 137.78958 -4.61125  -11.60437 1.000 39.74596 ?  226 THR   A O   1 
ATOM   1725 C CB  . THR   A 1 226 ? 139.77837 -3.38794  -13.95666 1.000 43.29985 ?  226 THR   A CB  1 
ATOM   1726 O OG1 . THR   A 1 226 ? 140.00158 -2.71469  -12.71345 1.000 43.98947 ?  226 THR   A OG1 1 
ATOM   1727 C CG2 . THR   A 1 226 ? 139.71683 -2.35495  -15.06257 1.000 45.27192 ?  226 THR   A CG2 1 
ATOM   1728 N N   . LEU   A 1 227 ? 139.21750 -6.06948  -12.57304 1.000 40.38428 ?  227 LEU   A N   1 
ATOM   1729 C CA  . LEU   A 1 227 ? 139.26323 -6.92424  -11.39663 1.000 41.71556 ?  227 LEU   A CA  1 
ATOM   1730 C C   . LEU   A 1 227 ? 139.71326 -6.13386  -10.17258 1.000 43.12425 ?  227 LEU   A C   1 
ATOM   1731 O O   . LEU   A 1 227 ? 139.10116 -6.22806  -9.10281  1.000 40.09236 ?  227 LEU   A O   1 
ATOM   1732 C CB  . LEU   A 1 227 ? 140.19057 -8.10676  -11.67439 1.000 44.39017 ?  227 LEU   A CB  1 
ATOM   1733 C CG  . LEU   A 1 227 ? 139.91326 -9.46499  -11.04541 1.000 43.56536 ?  227 LEU   A CG  1 
ATOM   1734 C CD1 . LEU   A 1 227 ? 138.42785 -9.78594  -11.08104 1.000 39.78786 ?  227 LEU   A CD1 1 
ATOM   1735 C CD2 . LEU   A 1 227 ? 140.70286 -10.52107 -11.80004 1.000 40.04228 ?  227 LEU   A CD2 1 
ATOM   1736 N N   . ASN   A 1 228 ? 140.75424 -5.30795  -10.32364 1.000 42.41515 ?  228 ASN   A N   1 
ATOM   1737 C CA  . ASN   A 1 228 ? 141.22612 -4.51295  -9.19405  1.000 43.22566 ?  228 ASN   A CA  1 
ATOM   1738 C C   . ASN   A 1 228 ? 140.22987 -3.41360  -8.82667  1.000 42.34404 ?  228 ASN   A C   1 
ATOM   1739 O O   . ASN   A 1 228 ? 140.04861 -3.10409  -7.64330  1.000 41.33326 ?  228 ASN   A O   1 
ATOM   1740 C CB  . ASN   A 1 228 ? 142.60292 -3.92848  -9.51207  1.000 46.85329 ?  228 ASN   A CB  1 
ATOM   1741 C CG  . ASN   A 1 228 ? 143.73458 -4.85899  -9.10396  1.000 44.39462 ?  228 ASN   A CG  1 
ATOM   1742 O OD1 . ASN   A 1 228 ? 143.56977 -6.07874  -9.06546  1.000 47.24529 ?  228 ASN   A OD1 1 
ATOM   1743 N ND2 . ASN   A 1 228 ? 144.88976 -4.28678  -8.80427  1.000 42.40814 ?  228 ASN   A ND2 1 
ATOM   1744 N N   . ASP   A 1 229 ? 139.56506 -2.82056  -9.81871  1.000 41.83280 ?  229 ASP   A N   1 
ATOM   1745 C CA  . ASP   A 1 229 ? 138.59628 -1.76624  -9.52224  1.000 42.94059 ?  229 ASP   A CA  1 
ATOM   1746 C C   . ASP   A 1 229 ? 137.37104 -2.33282  -8.81240  1.000 42.94312 ?  229 ASP   A C   1 
ATOM   1747 O O   . ASP   A 1 229 ? 136.86717 -1.74169  -7.84846  1.000 42.47083 ?  229 ASP   A O   1 
ATOM   1748 C CB  . ASP   A 1 229 ? 138.18943 -1.05569  -10.81385 1.000 46.14560 ?  229 ASP   A CB  1 
ATOM   1749 C CG  . ASP   A 1 229 ? 136.99812 -0.13154  -10.62854 1.000 52.42141 ?  229 ASP   A CG  1 
ATOM   1750 O OD1 . ASP   A 1 229 ? 136.19710 0.00324   -11.57956 1.000 57.56468 ?  229 ASP   A OD1 1 
ATOM   1751 O OD2 . ASP   A 1 229 ? 136.88229 0.48540   -9.54872  1.000 59.22957 -1 229 ASP   A OD2 1 
ATOM   1752 N N   . PHE   A 1 230 ? 136.87358 -3.47597  -9.28040  1.000 42.02524 ?  230 PHE   A N   1 
ATOM   1753 C CA  . PHE   A 1 230 ? 135.76257 -4.12345  -8.59693  1.000 39.77102 ?  230 PHE   A CA  1 
ATOM   1754 C C   . PHE   A 1 230 ? 136.14474 -4.52253  -7.17618  1.000 39.17605 ?  230 PHE   A C   1 
ATOM   1755 O O   . PHE   A 1 230 ? 135.36393 -4.32409  -6.23879  1.000 38.38379 ?  230 PHE   A O   1 
ATOM   1756 C CB  . PHE   A 1 230 ? 135.30525 -5.34541  -9.38660  1.000 37.70093 ?  230 PHE   A CB  1 
ATOM   1757 C CG  . PHE   A 1 230 ? 134.27313 -6.15531  -8.67981  1.000 35.55891 ?  230 PHE   A CG  1 
ATOM   1758 C CD1 . PHE   A 1 230 ? 132.94208 -5.76929  -8.70579  1.000 35.23658 ?  230 PHE   A CD1 1 
ATOM   1759 C CD2 . PHE   A 1 230 ? 134.63089 -7.27934  -7.95690  1.000 34.59025 ?  230 PHE   A CD2 1 
ATOM   1760 C CE1 . PHE   A 1 230 ? 131.98176 -6.50806  -8.04024  1.000 36.15501 ?  230 PHE   A CE1 1 
ATOM   1761 C CE2 . PHE   A 1 230 ? 133.67478 -8.01924  -7.29235  1.000 32.29822 ?  230 PHE   A CE2 1 
ATOM   1762 C CZ  . PHE   A 1 230 ? 132.35173 -7.63191  -7.32978  1.000 35.87663 ?  230 PHE   A CZ  1 
ATOM   1763 N N   . ASN   A 1 231 ? 137.34205 -5.09000  -6.99364  1.000 39.61718 ?  231 ASN   A N   1 
ATOM   1764 C CA  . ASN   A 1 231 ? 137.72530 -5.56633  -5.66721  1.000 39.12262 ?  231 ASN   A CA  1 
ATOM   1765 C C   . ASN   A 1 231 ? 137.84521 -4.42248  -4.67303  1.000 40.84647 ?  231 ASN   A C   1 
ATOM   1766 O O   . ASN   A 1 231 ? 137.68241 -4.63567  -3.46570  1.000 38.88554 ?  231 ASN   A O   1 
ATOM   1767 C CB  . ASN   A 1 231 ? 139.02898 -6.35751  -5.73947  1.000 39.68622 ?  231 ASN   A CB  1 
ATOM   1768 C CG  . ASN   A 1 231 ? 138.81127 -7.76579  -6.23753  1.000 38.90826 ?  231 ASN   A CG  1 
ATOM   1769 O OD1 . ASN   A 1 231 ? 137.68531 -8.25550  -6.23312  1.000 38.34685 ?  231 ASN   A OD1 1 
ATOM   1770 N ND2 . ASN   A 1 231 ? 139.88025 -8.42719  -6.66827  1.000 38.36748 ?  231 ASN   A ND2 1 
ATOM   1771 N N   . LEU   A 1 232 ? 138.12911 -3.20725  -5.15737  1.000 40.44013 ?  232 LEU   A N   1 
ATOM   1772 C CA  . LEU   A 1 232 ? 138.03500 -2.03164  -4.29949  1.000 42.28667 ?  232 LEU   A CA  1 
ATOM   1773 C C   . LEU   A 1 232 ? 136.62744 -1.88440  -3.74201  1.000 42.96319 ?  232 LEU   A C   1 
ATOM   1774 O O   . LEU   A 1 232 ? 136.44411 -1.60721  -2.55127  1.000 44.37597 ?  232 LEU   A O   1 
ATOM   1775 C CB  . LEU   A 1 232 ? 138.43717 -0.78162  -5.08056  1.000 42.76853 ?  232 LEU   A CB  1 
ATOM   1776 C CG  . LEU   A 1 232 ? 139.92890 -0.45489  -5.10187  1.000 44.26529 ?  232 LEU   A CG  1 
ATOM   1777 C CD1 . LEU   A 1 232 ? 140.12677 1.03528   -5.33677  1.000 44.78510 ?  232 LEU   A CD1 1 
ATOM   1778 C CD2 . LEU   A 1 232 ? 140.60117 -0.89203  -3.80900  1.000 46.68566 ?  232 LEU   A CD2 1 
ATOM   1779 N N   . VAL   A 1 233 ? 135.62107 -2.09200  -4.58749  1.000 41.03073 ?  233 VAL   A N   1 
ATOM   1780 C CA  . VAL   A 1 233 ? 134.23730 -2.01942  -4.14124  1.000 42.50403 ?  233 VAL   A CA  1 
ATOM   1781 C C   . VAL   A 1 233 ? 133.84735 -3.25432  -3.33478  1.000 40.42494 ?  233 VAL   A C   1 
ATOM   1782 O O   . VAL   A 1 233 ? 133.02498 -3.16559  -2.41529  1.000 40.69124 ?  233 VAL   A O   1 
ATOM   1783 C CB  . VAL   A 1 233 ? 133.33117 -1.81120  -5.36296  1.000 43.03487 ?  233 VAL   A CB  1 
ATOM   1784 C CG1 . VAL   A 1 233 ? 131.86461 -1.89946  -4.97888  1.000 47.58416 ?  233 VAL   A CG1 1 
ATOM   1785 C CG2 . VAL   A 1 233 ? 133.64961 -0.47236  -5.99678  1.000 44.89066 ?  233 VAL   A CG2 1 
ATOM   1786 N N   . ALA   A 1 234 ? 134.43399 -4.41469  -3.63767  1.000 38.66338 ?  234 ALA   A N   1 
ATOM   1787 C CA  . ALA   A 1 234 ? 134.14167 -5.60924  -2.85335  1.000 38.34443 ?  234 ALA   A CA  1 
ATOM   1788 C C   . ALA   A 1 234 ? 134.57653 -5.43481  -1.40244  1.000 38.72453 ?  234 ALA   A C   1 
ATOM   1789 O O   . ALA   A 1 234 ? 133.80248 -5.71060  -0.47914  1.000 37.02914 ?  234 ALA   A O   1 
ATOM   1790 C CB  . ALA   A 1 234 ? 134.81704 -6.83193  -3.47712  1.000 36.26109 ?  234 ALA   A CB  1 
ATOM   1791 N N   . MET   A 1 235 ? 135.81098 -4.96483  -1.18227  1.000 38.35145 ?  235 MET   A N   1 
ATOM   1792 C CA  . MET   A 1 235 ? 136.30546 -4.79232  0.18205   1.000 40.08176 ?  235 MET   A CA  1 
ATOM   1793 C C   . MET   A 1 235 ? 135.40170 -3.86634  0.98947   1.000 40.19827 ?  235 MET   A C   1 
ATOM   1794 O O   . MET   A 1 235 ? 135.10941 -4.14008  2.16055   1.000 40.09728 ?  235 MET   A O   1 
ATOM   1795 C CB  . MET   A 1 235 ? 137.73915 -4.26174  0.16302   1.000 43.31298 ?  235 MET   A CB  1 
ATOM   1796 N N   . LYS   A 1 236 ? 134.92691 -2.78161  0.37158   1.000 40.72642 ?  236 LYS   A N   1 
ATOM   1797 C CA  . LYS   A 1 236 ? 134.10178 -1.81476  1.09072   1.000 40.23170 ?  236 LYS   A CA  1 
ATOM   1798 C C   . LYS   A 1 236 ? 132.78566 -2.43052  1.54672   1.000 40.61679 ?  236 LYS   A C   1 
ATOM   1799 O O   . LYS   A 1 236 ? 132.27640 -2.09606  2.62212   1.000 43.68713 ?  236 LYS   A O   1 
ATOM   1800 C CB  . LYS   A 1 236 ? 133.84446 -0.58603  0.21614   1.000 45.57640 ?  236 LYS   A CB  1 
ATOM   1801 C CG  . LYS   A 1 236 ? 132.90940 0.43672   0.85240   1.000 50.44231 ?  236 LYS   A CG  1 
ATOM   1802 C CD  . LYS   A 1 236 ? 133.11983 1.83614   0.28553   1.000 58.10178 ?  236 LYS   A CD  1 
ATOM   1803 C CE  . LYS   A 1 236 ? 131.86405 2.68856   0.42299   1.000 57.80574 ?  236 LYS   A CE  1 
ATOM   1804 N NZ  . LYS   A 1 236 ? 131.27588 3.02058   -0.90298  1.000 61.24067 ?  236 LYS   A NZ  1 
ATOM   1805 N N   . TYR   A 1 237 ? 132.22416 -3.34148  0.75058   1.000 39.12888 ?  237 TYR   A N   1 
ATOM   1806 C CA  . TYR   A 1 237 ? 130.94731 -3.97312  1.05451   1.000 38.03768 ?  237 TYR   A CA  1 
ATOM   1807 C C   . TYR   A 1 237 ? 131.10095 -5.37586  1.63249   1.000 35.79197 ?  237 TYR   A C   1 
ATOM   1808 O O   . TYR   A 1 237 ? 130.14049 -6.14771  1.63610   1.000 35.40216 ?  237 TYR   A O   1 
ATOM   1809 C CB  . TYR   A 1 237 ? 130.06909 -3.98554  -0.19758  1.000 36.59835 ?  237 TYR   A CB  1 
ATOM   1810 C CG  . TYR   A 1 237 ? 129.63907 -2.59357  -0.59675  1.000 39.97430 ?  237 TYR   A CG  1 
ATOM   1811 C CD1 . TYR   A 1 237 ? 128.56806 -1.97409  0.03563   1.000 41.41070 ?  237 TYR   A CD1 1 
ATOM   1812 C CD2 . TYR   A 1 237 ? 130.34922 -1.86657  -1.54419  1.000 40.58999 ?  237 TYR   A CD2 1 
ATOM   1813 C CE1 . TYR   A 1 237 ? 128.17844 -0.69274  -0.30762  1.000 42.40876 ?  237 TYR   A CE1 1 
ATOM   1814 C CE2 . TYR   A 1 237 ? 129.96767 -0.57966  -1.89453  1.000 43.56523 ?  237 TYR   A CE2 1 
ATOM   1815 C CZ  . TYR   A 1 237 ? 128.88304 0.00038   -1.27068  1.000 44.10898 ?  237 TYR   A CZ  1 
ATOM   1816 O OH  . TYR   A 1 237 ? 128.50025 1.27714   -1.60634  1.000 47.29145 ?  237 TYR   A OH  1 
ATOM   1817 N N   . ASN   A 1 238 ? 132.27829 -5.70054  2.15567   1.000 35.68895 ?  238 ASN   A N   1 
ATOM   1818 C CA  . ASN   A 1 238 ? 132.52879 -6.99144  2.79064   1.000 33.36279 ?  238 ASN   A CA  1 
ATOM   1819 C C   . ASN   A 1 238 ? 132.21205 -8.14574  1.83845   1.000 31.89281 ?  238 ASN   A C   1 
ATOM   1820 O O   . ASN   A 1 238 ? 131.59548 -9.13846  2.22571   1.000 31.30044 ?  238 ASN   A O   1 
ATOM   1821 C CB  . ASN   A 1 238 ? 131.73567 -7.13303  4.09544   1.000 37.05881 ?  238 ASN   A CB  1 
ATOM   1822 C CG  . ASN   A 1 238 ? 132.43058 -6.47212  5.28265   1.000 44.07358 ?  238 ASN   A CG  1 
ATOM   1823 O OD1 . ASN   A 1 238 ? 133.65966 -6.40711  5.34798   1.000 44.88984 ?  238 ASN   A OD1 1 
ATOM   1824 N ND2 . ASN   A 1 238 ? 131.63802 -5.98721  6.23337   1.000 52.14179 ?  238 ASN   A ND2 1 
ATOM   1825 N N   . TYR   A 1 239 ? 132.61921 -8.00730  0.58203   1.000 32.27295 ?  239 TYR   A N   1 
ATOM   1826 C CA  . TYR   A 1 239 ? 132.52829 -9.08143  -0.39700  1.000 31.04345 ?  239 TYR   A CA  1 
ATOM   1827 C C   . TYR   A 1 239 ? 133.90074 -9.73096  -0.55432  1.000 31.26870 ?  239 TYR   A C   1 
ATOM   1828 O O   . TYR   A 1 239 ? 134.93179 -9.05997  -0.45914  1.000 30.63891 ?  239 TYR   A O   1 
ATOM   1829 C CB  . TYR   A 1 239 ? 132.05726 -8.55637  -1.75906  1.000 28.70642 ?  239 TYR   A CB  1 
ATOM   1830 C CG  . TYR   A 1 239 ? 130.55461 -8.54870  -1.97246  1.000 28.81099 ?  239 TYR   A CG  1 
ATOM   1831 C CD1 . TYR   A 1 239 ? 129.69889 -7.88819  -1.09047  1.000 27.77803 ?  239 TYR   A CD1 1 
ATOM   1832 C CD2 . TYR   A 1 239 ? 129.98895 -9.23316  -3.04337  1.000 28.67127 ?  239 TYR   A CD2 1 
ATOM   1833 C CE1 . TYR   A 1 239 ? 128.31283 -7.88985  -1.29116  1.000 28.57338 ?  239 TYR   A CE1 1 
ATOM   1834 C CE2 . TYR   A 1 239 ? 128.61028 -9.24290  -3.24804  1.000 27.62550 ?  239 TYR   A CE2 1 
ATOM   1835 C CZ  . TYR   A 1 239 ? 127.78029 -8.57436  -2.36879  1.000 27.52445 ?  239 TYR   A CZ  1 
ATOM   1836 O OH  . TYR   A 1 239 ? 126.41864 -8.59386  -2.58019  1.000 26.84639 ?  239 TYR   A OH  1 
ATOM   1837 N N   . GLU   A 1 240 ? 133.91081 -11.04025 -0.79290  1.000 27.52815 ?  240 GLU   A N   1 
ATOM   1838 C CA  . GLU   A 1 240 ? 135.17021 -11.73401 -1.04046  1.000 29.75140 ?  240 GLU   A CA  1 
ATOM   1839 C C   . GLU   A 1 240 ? 135.82609 -11.19293 -2.30629  1.000 27.90573 ?  240 GLU   A C   1 
ATOM   1840 O O   . GLU   A 1 240 ? 135.13592 -10.92802 -3.30042  1.000 30.12417 ?  240 GLU   A O   1 
ATOM   1841 C CB  . GLU   A 1 240 ? 134.94255 -13.23765 -1.19897  1.000 30.96403 ?  240 GLU   A CB  1 
ATOM   1842 C CG  . GLU   A 1 240 ? 134.30669 -13.93801 -0.02149  1.000 31.18344 ?  240 GLU   A CG  1 
ATOM   1843 C CD  . GLU   A 1 240 ? 134.29130 -15.44526 -0.21976  1.000 40.40542 ?  240 GLU   A CD  1 
ATOM   1844 O OE1 . GLU   A 1 240 ? 134.14277 -15.88412 -1.38801  1.000 35.51833 ?  240 GLU   A OE1 1 
ATOM   1845 O OE2 . GLU   A 1 240 ? 134.41796 -16.18829 0.78030   1.000 49.12321 -1 240 GLU   A OE2 1 
ATOM   1846 N N   . PRO   A 1 241 ? 137.14522 -11.01479 -2.31558  1.000 30.54762 ?  241 PRO   A N   1 
ATOM   1847 C CA  . PRO   A 1 241 ? 137.81096 -10.53327 -3.52970  1.000 32.70312 ?  241 PRO   A CA  1 
ATOM   1848 C C   . PRO   A 1 241 ? 137.67295 -11.54294 -4.66174  1.000 30.29281 ?  241 PRO   A C   1 
ATOM   1849 O O   . PRO   A 1 241 ? 137.73447 -12.75576 -4.45210  1.000 30.57788 ?  241 PRO   A O   1 
ATOM   1850 C CB  . PRO   A 1 241 ? 139.27300 -10.37224 -3.09497  1.000 34.50228 ?  241 PRO   A CB  1 
ATOM   1851 C CG  . PRO   A 1 241 ? 139.22989 -10.34723 -1.58763  1.000 34.55736 ?  241 PRO   A CG  1 
ATOM   1852 C CD  . PRO   A 1 241 ? 138.09082 -11.22831 -1.20833  1.000 32.43328 ?  241 PRO   A CD  1 
ATOM   1853 N N   . LEU   A 1 242 ? 137.48742 -11.03587 -5.86988  1.000 34.01780 ?  242 LEU   A N   1 
ATOM   1854 C CA  . LEU   A 1 242 ? 137.32238 -11.90278 -7.02440  1.000 34.05308 ?  242 LEU   A CA  1 
ATOM   1855 C C   . LEU   A 1 242 ? 138.67815 -12.14453 -7.68426  1.000 33.32042 ?  242 LEU   A C   1 
ATOM   1856 O O   . LEU   A 1 242 ? 139.46197 -11.20913 -7.87533  1.000 34.16055 ?  242 LEU   A O   1 
ATOM   1857 C CB  . LEU   A 1 242 ? 136.32489 -11.29188 -8.00668  1.000 32.47723 ?  242 LEU   A CB  1 
ATOM   1858 C CG  . LEU   A 1 242 ? 135.66531 -12.27876 -8.97192  1.000 33.11012 ?  242 LEU   A CG  1 
ATOM   1859 C CD1 . LEU   A 1 242 ? 134.44560 -12.90486 -8.31600  1.000 30.94260 ?  242 LEU   A CD1 1 
ATOM   1860 C CD2 . LEU   A 1 242 ? 135.27437 -11.57127 -10.25465 1.000 34.62513 ?  242 LEU   A CD2 1 
ATOM   1861 N N   . THR   A 1 243 ? 138.95509 -13.40581 -8.00167  1.000 32.15315 ?  243 THR   A N   1 
ATOM   1862 C CA  . THR   A 1 243 ? 140.20622 -13.85522 -8.59200  1.000 33.39139 ?  243 THR   A CA  1 
ATOM   1863 C C   . THR   A 1 243 ? 139.96242 -14.34882 -10.01328 1.000 33.13360 ?  243 THR   A C   1 
ATOM   1864 O O   . THR   A 1 243 ? 138.81937 -14.53572 -10.44441 1.000 32.73423 ?  243 THR   A O   1 
ATOM   1865 C CB  . THR   A 1 243 ? 140.81357 -14.98417 -7.76017  1.000 33.31124 ?  243 THR   A CB  1 
ATOM   1866 O OG1 . THR   A 1 243 ? 139.97112 -16.13485 -7.87176  1.000 33.01579 ?  243 THR   A OG1 1 
ATOM   1867 C CG2 . THR   A 1 243 ? 140.90397 -14.58585 -6.29684  1.000 33.81155 ?  243 THR   A CG2 1 
ATOM   1868 N N   . GLN   A 1 244 ? 141.05782 -14.59874 -10.73628 1.000 32.10310 ?  244 GLN   A N   1 
ATOM   1869 C CA  . GLN   A 1 244 ? 140.91494 -15.17626 -12.07094 1.000 33.38811 ?  244 GLN   A CA  1 
ATOM   1870 C C   . GLN   A 1 244 ? 140.38197 -16.60218 -12.00089 1.000 33.51073 ?  244 GLN   A C   1 
ATOM   1871 O O   . GLN   A 1 244 ? 139.69215 -17.05075 -12.92388 1.000 31.64581 ?  244 GLN   A O   1 
ATOM   1872 C CB  . GLN   A 1 244 ? 142.24612 -15.14309 -12.81799 1.000 35.39716 ?  244 GLN   A CB  1 
ATOM   1873 C CG  . GLN   A 1 244 ? 142.16333 -15.58078 -14.28041 1.000 37.05737 ?  244 GLN   A CG  1 
ATOM   1874 C CD  . GLN   A 1 244 ? 141.26787 -14.68648 -15.12479 1.000 39.23265 ?  244 GLN   A CD  1 
ATOM   1875 O OE1 . GLN   A 1 244 ? 141.38919 -13.46205 -15.10047 1.000 40.75379 ?  244 GLN   A OE1 1 
ATOM   1876 N NE2 . GLN   A 1 244 ? 140.37437 -15.30051 -15.89434 1.000 38.14557 ?  244 GLN   A NE2 1 
ATOM   1877 N N   . ASP   A 1 245 ? 140.68890 -17.32875 -10.92366 1.000 33.19890 ?  245 ASP   A N   1 
ATOM   1878 C CA  . ASP   A 1 245 ? 140.07056 -18.63621 -10.72778 1.000 32.38411 ?  245 ASP   A CA  1 
ATOM   1879 C C   . ASP   A 1 245 ? 138.55437 -18.51931 -10.69295 1.000 33.23375 ?  245 ASP   A C   1 
ATOM   1880 O O   . ASP   A 1 245 ? 137.84614 -19.35479 -11.26642 1.000 30.96133 ?  245 ASP   A O   1 
ATOM   1881 C CB  . ASP   A 1 245 ? 140.56817 -19.28419 -9.44139  1.000 36.70726 ?  245 ASP   A CB  1 
ATOM   1882 C CG  . ASP   A 1 245 ? 141.93684 -19.89143 -9.58653  1.000 45.74112 ?  245 ASP   A CG  1 
ATOM   1883 O OD1 . ASP   A 1 245 ? 142.37923 -20.09543 -10.73568 1.000 43.56525 ?  245 ASP   A OD1 1 
ATOM   1884 O OD2 . ASP   A 1 245 ? 142.54986 -20.20617 -8.54524  1.000 48.49220 -1 245 ASP   A OD2 1 
ATOM   1885 N N   . HIS   A 1 246 ? 138.03983 -17.49089 -10.01148 1.000 31.26825 ?  246 HIS   A N   1 
ATOM   1886 C CA  . HIS   A 1 246 ? 136.60104 -17.24666 -9.99112  1.000 31.22022 ?  246 HIS   A CA  1 
ATOM   1887 C C   . HIS   A 1 246 ? 136.08247 -16.90992 -11.38220 1.000 28.91484 ?  246 HIS   A C   1 
ATOM   1888 O O   . HIS   A 1 246 ? 135.02939 -17.41277 -11.79308 1.000 29.23503 ?  246 HIS   A O   1 
ATOM   1889 C CB  . HIS   A 1 246 ? 136.28039 -16.10498 -9.02772  1.000 29.99364 ?  246 HIS   A CB  1 
ATOM   1890 C CG  . HIS   A 1 246 ? 136.55751 -16.41988 -7.59277  1.000 31.38340 ?  246 HIS   A CG  1 
ATOM   1891 N ND1 . HIS   A 1 246 ? 136.93142 -15.45277 -6.68426  1.000 33.74826 ?  246 HIS   A ND1 1 
ATOM   1892 C CD2 . HIS   A 1 246 ? 136.44960 -17.57486 -6.89214  1.000 30.19448 ?  246 HIS   A CD2 1 
ATOM   1893 C CE1 . HIS   A 1 246 ? 137.08716 -16.00804 -5.49390  1.000 31.02860 ?  246 HIS   A CE1 1 
ATOM   1894 N NE2 . HIS   A 1 246 ? 136.79196 -17.29308 -5.59042  1.000 31.53308 ?  246 HIS   A NE2 1 
ATOM   1895 N N   . VAL   A 1 247 ? 136.77911 -16.01790 -12.09754 1.000 28.02760 ?  247 VAL   A N   1 
ATOM   1896 C CA  . VAL   A 1 247 ? 136.37191 -15.67812 -13.45981 1.000 31.25785 ?  247 VAL   A CA  1 
ATOM   1897 C C   . VAL   A 1 247 ? 136.29306 -16.93780 -14.30890 1.000 33.35450 ?  247 VAL   A C   1 
ATOM   1898 O O   . VAL   A 1 247 ? 135.31764 -17.15232 -15.03888 1.000 33.11375 ?  247 VAL   A O   1 
ATOM   1899 C CB  . VAL   A 1 247 ? 137.33598 -14.64497 -14.07233 1.000 34.03398 ?  247 VAL   A CB  1 
ATOM   1900 C CG1 . VAL   A 1 247 ? 136.89049 -14.26742 -15.49254 1.000 32.11980 ?  247 VAL   A CG1 1 
ATOM   1901 C CG2 . VAL   A 1 247 ? 137.43386 -13.41535 -13.18732 1.000 32.68479 ?  247 VAL   A CG2 1 
ATOM   1902 N N   . ASP   A 1 248 ? 137.30224 -17.80674 -14.19764 1.000 32.54632 ?  248 ASP   A N   1 
ATOM   1903 C CA  . ASP   A 1 248 ? 137.31898 -19.04182 -14.97822 1.000 33.46596 ?  248 ASP   A CA  1 
ATOM   1904 C C   . ASP   A 1 248 ? 136.12576 -19.92990 -14.63575 1.000 31.52559 ?  248 ASP   A C   1 
ATOM   1905 O O   . ASP   A 1 248 ? 135.51770 -20.54450 -15.52084 1.000 28.55378 ?  248 ASP   A O   1 
ATOM   1906 C CB  . ASP   A 1 248 ? 138.62146 -19.80347 -14.72408 1.000 33.09041 ?  248 ASP   A CB  1 
ATOM   1907 C CG  . ASP   A 1 248 ? 139.81867 -19.20232 -15.44699 1.000 34.25746 ?  248 ASP   A CG  1 
ATOM   1908 O OD1 . ASP   A 1 248 ? 139.64174 -18.40005 -16.39003 1.000 36.80322 ?  248 ASP   A OD1 1 
ATOM   1909 O OD2 . ASP   A 1 248 ? 140.95543 -19.56220 -15.07694 1.000 38.06856 -1 248 ASP   A OD2 1 
ATOM   1910 N N   . ILE   A 1 249 ? 135.78477 -20.02497 -13.35145 1.000 26.64321 ?  249 ILE   A N   1 
ATOM   1911 C CA  . ILE   A 1 249 ? 134.62789 -20.82312 -12.95021 1.000 28.35246 ?  249 ILE   A CA  1 
ATOM   1912 C C   . ILE   A 1 249 ? 133.34642 -20.26899 -13.56031 1.000 29.48548 ?  249 ILE   A C   1 
ATOM   1913 O O   . ILE   A 1 249 ? 132.41172 -21.02564 -13.85806 1.000 29.07466 ?  249 ILE   A O   1 
ATOM   1914 C CB  . ILE   A 1 249 ? 134.55080 -20.89264 -11.41107 1.000 24.64199 ?  249 ILE   A CB  1 
ATOM   1915 C CG1 . ILE   A 1 249 ? 135.71890 -21.70132 -10.85264 1.000 28.54661 ?  249 ILE   A CG1 1 
ATOM   1916 C CG2 . ILE   A 1 249 ? 133.24773 -21.48644 -10.94033 1.000 29.36589 ?  249 ILE   A CG2 1 
ATOM   1917 C CD1 . ILE   A 1 249 ? 135.87237 -21.54391 -9.36616  1.000 27.30416 ?  249 ILE   A CD1 1 
ATOM   1918 N N   . LEU   A 1 250 ? 133.27377 -18.95414 -13.75570 1.000 26.88346 ?  250 LEU   A N   1 
ATOM   1919 C CA  . LEU   A 1 250 ? 132.08162 -18.34375 -14.33189 1.000 29.11734 ?  250 LEU   A CA  1 
ATOM   1920 C C   . LEU   A 1 250 ? 132.05295 -18.42480 -15.84227 1.000 30.11857 ?  250 LEU   A C   1 
ATOM   1921 O O   . LEU   A 1 250 ? 131.06335 -18.00225 -16.44878 1.000 32.14639 ?  250 LEU   A O   1 
ATOM   1922 C CB  . LEU   A 1 250 ? 131.96547 -16.87925 -13.90700 1.000 27.44206 ?  250 LEU   A CB  1 
ATOM   1923 C CG  . LEU   A 1 250 ? 131.65639 -16.72752 -12.41026 1.000 24.59291 ?  250 LEU   A CG  1 
ATOM   1924 C CD1 . LEU   A 1 250 ? 131.92729 -15.30220 -11.96267 1.000 25.07852 ?  250 LEU   A CD1 1 
ATOM   1925 C CD2 . LEU   A 1 250 ? 130.21574 -17.12033 -12.09995 1.000 23.56596 ?  250 LEU   A CD2 1 
ATOM   1926 N N   . GLY   A 1 251 ? 133.10213 -18.96071 -16.44666 1.000 29.88290 ?  251 GLY   A N   1 
ATOM   1927 C CA  . GLY   A 1 251 ? 133.26472 -18.94728 -17.87847 1.000 35.04167 ?  251 GLY   A CA  1 
ATOM   1928 C C   . GLY   A 1 251 ? 132.11190 -19.53137 -18.66813 1.000 35.11602 ?  251 GLY   A C   1 
ATOM   1929 O O   . GLY   A 1 251 ? 131.57578 -18.89042 -19.57923 1.000 32.57848 ?  251 GLY   A O   1 
ATOM   1930 N N   . PRO   A 1 252 ? 131.74149 -20.77789 -18.37239 1.000 33.47941 ?  252 PRO   A N   1 
ATOM   1931 C CA  . PRO   A 1 252 ? 130.58635 -21.37657 -19.06767 1.000 33.75232 ?  252 PRO   A CA  1 
ATOM   1932 C C   . PRO   A 1 252 ? 129.32501 -20.52979 -19.01435 1.000 35.60394 ?  252 PRO   A C   1 
ATOM   1933 O O   . PRO   A 1 252 ? 128.61756 -20.42524 -20.02271 1.000 34.20457 ?  252 PRO   A O   1 
ATOM   1934 C CB  . PRO   A 1 252 ? 130.41443 -22.71474 -18.34012 1.000 36.53407 ?  252 PRO   A CB  1 
ATOM   1935 C CG  . PRO   A 1 252 ? 131.81004 -23.07909 -17.93135 1.000 34.56785 ?  252 PRO   A CG  1 
ATOM   1936 C CD  . PRO   A 1 252 ? 132.51136 -21.78189 -17.61779 1.000 33.59139 ?  252 PRO   A CD  1 
ATOM   1937 N N   . LEU   A 1 253 ? 129.03112 -19.91528 -17.86726 1.000 33.18276 ?  253 LEU   A N   1 
ATOM   1938 C CA  . LEU   A 1 253 ? 127.87078 -19.03386 -17.76285 1.000 34.56729 ?  253 LEU   A CA  1 
ATOM   1939 C C   . LEU   A 1 253 ? 128.05886 -17.76744 -18.58081 1.000 34.78010 ?  253 LEU   A C   1 
ATOM   1940 O O   . LEU   A 1 253 ? 127.09987 -17.25648 -19.17162 1.000 37.35119 ?  253 LEU   A O   1 
ATOM   1941 C CB  . LEU   A 1 253 ? 127.60772 -18.68430 -16.29563 1.000 31.19941 ?  253 LEU   A CB  1 
ATOM   1942 C CG  . LEU   A 1 253 ? 126.95470 -19.75401 -15.42965 1.000 31.16800 ?  253 LEU   A CG  1 
ATOM   1943 C CD1 . LEU   A 1 253 ? 126.84047 -19.29094 -13.96636 1.000 30.86764 ?  253 LEU   A CD1 1 
ATOM   1944 C CD2 . LEU   A 1 253 ? 125.58653 -20.10049 -15.98883 1.000 34.33325 ?  253 LEU   A CD2 1 
ATOM   1945 N N   . SER   A 1 254 ? 129.28004 -17.23268 -18.61366 1.000 33.75214 ?  254 SER   A N   1 
ATOM   1946 C CA  . SER   A 1 254 ? 129.56944 -16.11919 -19.51229 1.000 33.45881 ?  254 SER   A CA  1 
ATOM   1947 C C   . SER   A 1 254 ? 129.29413 -16.49856 -20.96183 1.000 37.63533 ?  254 SER   A C   1 
ATOM   1948 O O   . SER   A 1 254 ? 128.70105 -15.71886 -21.71752 1.000 38.60435 ?  254 SER   A O   1 
ATOM   1949 C CB  . SER   A 1 254 ? 131.02660 -15.67729 -19.34169 1.000 34.83327 ?  254 SER   A CB  1 
ATOM   1950 O OG  . SER   A 1 254 ? 131.26720 -14.44401 -19.99922 1.000 37.27647 ?  254 SER   A OG  1 
ATOM   1951 N N   . ALA   A 1 255 ? 129.71708 -17.69798 -21.36669 1.000 35.32176 ?  255 ALA   A N   1 
ATOM   1952 C CA  . ALA   A 1 255 ? 129.58033 -18.09762 -22.76088 1.000 40.55532 ?  255 ALA   A CA  1 
ATOM   1953 C C   . ALA   A 1 255 ? 128.12544 -18.30161 -23.14752 1.000 41.95398 ?  255 ALA   A C   1 
ATOM   1954 O O   . ALA   A 1 255 ? 127.74134 -18.00841 -24.28540 1.000 45.66377 ?  255 ALA   A O   1 
ATOM   1955 C CB  . ALA   A 1 255 ? 130.37547 -19.37460 -23.02646 1.000 41.55474 ?  255 ALA   A CB  1 
ATOM   1956 N N   . GLN   A 1 256 ? 127.30514 -18.79546 -22.22190 1.000 40.66205 ?  256 GLN   A N   1 
ATOM   1957 C CA  . GLN   A 1 256 ? 125.90907 -19.05359 -22.54892 1.000 41.77679 ?  256 GLN   A CA  1 
ATOM   1958 C C   . GLN   A 1 256 ? 125.12303 -17.75138 -22.64384 1.000 46.67047 ?  256 GLN   A C   1 
ATOM   1959 O O   . GLN   A 1 256 ? 124.34767 -17.55251 -23.58734 1.000 42.94306 ?  256 GLN   A O   1 
ATOM   1960 C CB  . GLN   A 1 256 ? 125.30014 -20.00117 -21.51437 1.000 43.48632 ?  256 GLN   A CB  1 
ATOM   1961 C CG  . GLN   A 1 256 ? 123.86650 -19.69998 -21.13096 1.000 47.62955 ?  256 GLN   A CG  1 
ATOM   1962 C CD  . GLN   A 1 256 ? 123.22073 -20.83780 -20.36485 1.000 55.47711 ?  256 GLN   A CD  1 
ATOM   1963 O OE1 . GLN   A 1 256 ? 123.90419 -21.67528 -19.77146 1.000 60.23319 ?  256 GLN   A OE1 1 
ATOM   1964 N NE2 . GLN   A 1 256 ? 121.89513 -20.88617 -20.39250 1.000 56.87988 ?  256 GLN   A NE2 1 
ATOM   1965 N N   . THR   A 1 257 ? 125.33837 -16.83611 -21.69961 1.000 43.86428 ?  257 THR   A N   1 
ATOM   1966 C CA  . THR   A 1 257 ? 124.61091 -15.57306 -21.69428 1.000 41.67011 ?  257 THR   A CA  1 
ATOM   1967 C C   . THR   A 1 257 ? 125.22493 -14.50661 -22.59379 1.000 41.04344 ?  257 THR   A C   1 
ATOM   1968 O O   . THR   A 1 257 ? 124.57829 -13.47861 -22.83220 1.000 39.84559 ?  257 THR   A O   1 
ATOM   1969 C CB  . THR   A 1 257 ? 124.49490 -15.05439 -20.25947 1.000 40.28787 ?  257 THR   A CB  1 
ATOM   1970 O OG1 . THR   A 1 257 ? 125.73418 -14.46133 -19.85595 1.000 36.76583 ?  257 THR   A OG1 1 
ATOM   1971 C CG2 . THR   A 1 257 ? 124.14064 -16.18390 -19.31841 1.000 38.91914 ?  257 THR   A CG2 1 
ATOM   1972 N N   . GLY   A 1 258 ? 126.43155 -14.72340 -23.11359 1.000 37.33376 ?  258 GLY   A N   1 
ATOM   1973 C CA  . GLY   A 1 258 ? 127.07394 -13.69949 -23.91153 1.000 37.80024 ?  258 GLY   A CA  1 
ATOM   1974 C C   . GLY   A 1 258 ? 127.38199 -12.43506 -23.14889 1.000 39.52898 ?  258 GLY   A C   1 
ATOM   1975 O O   . GLY   A 1 258 ? 127.49188 -11.36776 -23.75289 1.000 40.90903 ?  258 GLY   A O   1 
ATOM   1976 N N   . ILE   A 1 259 ? 127.51338 -12.52153 -21.82668 1.000 37.49902 ?  259 ILE   A N   1 
ATOM   1977 C CA  . ILE   A 1 259 ? 127.83811 -11.37531 -20.98620 1.000 37.88153 ?  259 ILE   A CA  1 
ATOM   1978 C C   . ILE   A 1 259 ? 129.19856 -11.62043 -20.34922 1.000 35.19062 ?  259 ILE   A C   1 
ATOM   1979 O O   . ILE   A 1 259 ? 129.37476 -12.58859 -19.59601 1.000 37.94353 ?  259 ILE   A O   1 
ATOM   1980 C CB  . ILE   A 1 259 ? 126.77539 -11.13169 -19.90602 1.000 38.86193 ?  259 ILE   A CB  1 
ATOM   1981 C CG1 . ILE   A 1 259 ? 125.41806 -10.85068 -20.55007 1.000 42.02480 ?  259 ILE   A CG1 1 
ATOM   1982 C CG2 . ILE   A 1 259 ? 127.19682 -9.96676  -19.01705 1.000 36.36101 ?  259 ILE   A CG2 1 
ATOM   1983 C CD1 . ILE   A 1 259 ? 124.50034 -10.01282 -19.69627 1.000 48.01916 ?  259 ILE   A CD1 1 
ATOM   1984 N N   . ALA   A 1 260 ? 130.15041 -10.73500 -20.63769 1.000 38.22489 ?  260 ALA   A N   1 
ATOM   1985 C CA  . ALA   A 1 260 ? 131.48055 -10.84517 -20.05545 1.000 36.69616 ?  260 ALA   A CA  1 
ATOM   1986 C C   . ALA   A 1 260 ? 131.41538 -10.73281 -18.53442 1.000 35.82323 ?  260 ALA   A C   1 
ATOM   1987 O O   . ALA   A 1 260 ? 130.62906 -9.95859  -17.98093 1.000 35.77776 ?  260 ALA   A O   1 
ATOM   1988 C CB  . ALA   A 1 260 ? 132.39528 -9.76350  -20.63047 1.000 38.50026 ?  260 ALA   A CB  1 
ATOM   1989 N N   . VAL   A 1 261 ? 132.25961 -11.51136 -17.85654 1.000 33.71798 ?  261 VAL   A N   1 
ATOM   1990 C CA  . VAL   A 1 261 ? 132.22853 -11.54900 -16.39552 1.000 33.80090 ?  261 VAL   A CA  1 
ATOM   1991 C C   . VAL   A 1 261 ? 132.47172 -10.15842 -15.81553 1.000 33.32454 ?  261 VAL   A C   1 
ATOM   1992 O O   . VAL   A 1 261 ? 131.81130 -9.74171  -14.85602 1.000 31.72252 ?  261 VAL   A O   1 
ATOM   1993 C CB  . VAL   A 1 261 ? 133.25451 -12.57157 -15.86838 1.000 34.17664 ?  261 VAL   A CB  1 
ATOM   1994 C CG1 . VAL   A 1 261 ? 133.41802 -12.43569 -14.37727 1.000 31.33688 ?  261 VAL   A CG1 1 
ATOM   1995 C CG2 . VAL   A 1 261 ? 132.83795 -13.99416 -16.23634 1.000 34.19235 ?  261 VAL   A CG2 1 
ATOM   1996 N N   . LEU   A 1 262 ? 133.40696 -9.40785  -16.39943 1.000 36.07158 ?  262 LEU   A N   1 
ATOM   1997 C CA  . LEU   A 1 262 ? 133.71131 -8.09113  -15.85426 1.000 35.22938 ?  262 LEU   A CA  1 
ATOM   1998 C C   . LEU   A 1 262 ? 132.59200 -7.08931  -16.10101 1.000 35.82670 ?  262 LEU   A C   1 
ATOM   1999 O O   . LEU   A 1 262 ? 132.47748 -6.11171  -15.35244 1.000 36.01467 ?  262 LEU   A O   1 
ATOM   2000 C CB  . LEU   A 1 262 ? 135.01832 -7.55813  -16.43693 1.000 37.17511 ?  262 LEU   A CB  1 
ATOM   2001 C CG  . LEU   A 1 262 ? 136.28008 -8.17229  -15.83570 1.000 36.81845 ?  262 LEU   A CG  1 
ATOM   2002 C CD1 . LEU   A 1 262 ? 137.50996 -7.70502  -16.60475 1.000 39.34647 ?  262 LEU   A CD1 1 
ATOM   2003 C CD2 . LEU   A 1 262 ? 136.39714 -7.88745  -14.33967 1.000 38.35703 ?  262 LEU   A CD2 1 
ATOM   2004 N N   . ASP   A 1 263 ? 131.76313 -7.30853  -17.12300 1.000 36.25347 ?  263 ASP   A N   1 
ATOM   2005 C CA  . ASP   A 1 263 ? 130.57730 -6.47510  -17.28002 1.000 36.68791 ?  263 ASP   A CA  1 
ATOM   2006 C C   . ASP   A 1 263 ? 129.56494 -6.77567  -16.18129 1.000 35.56353 ?  263 ASP   A C   1 
ATOM   2007 O O   . ASP   A 1 263 ? 128.92670 -5.86401  -15.63912 1.000 35.64461 ?  263 ASP   A O   1 
ATOM   2008 C CB  . ASP   A 1 263 ? 129.93986 -6.69596  -18.65261 1.000 38.08391 ?  263 ASP   A CB  1 
ATOM   2009 C CG  . ASP   A 1 263 ? 130.79902 -6.17383  -19.79695 1.000 39.91794 ?  263 ASP   A CG  1 
ATOM   2010 O OD1 . ASP   A 1 263 ? 131.73782 -5.39143  -19.53954 1.000 40.90195 ?  263 ASP   A OD1 1 
ATOM   2011 O OD2 . ASP   A 1 263 ? 130.50800 -6.51766  -20.96364 1.000 41.24514 -1 263 ASP   A OD2 1 
ATOM   2012 N N   . MET   A 1 264 ? 129.39329 -8.05375  -15.84838 1.000 33.20189 ?  264 MET   A N   1 
ATOM   2013 C CA  . MET   A 1 264 ? 128.51983 -8.39521  -14.73381 1.000 32.53329 ?  264 MET   A CA  1 
ATOM   2014 C C   . MET   A 1 264 ? 129.04227 -7.79293  -13.43508 1.000 34.90069 ?  264 MET   A C   1 
ATOM   2015 O O   . MET   A 1 264 ? 128.25940 -7.31092  -12.60791 1.000 33.20423 ?  264 MET   A O   1 
ATOM   2016 C CB  . MET   A 1 264 ? 128.37274 -9.91256  -14.61548 1.000 31.56685 ?  264 MET   A CB  1 
ATOM   2017 C CG  . MET   A 1 264 ? 127.15310 -10.36012 -13.82734 1.000 28.93619 ?  264 MET   A CG  1 
ATOM   2018 S SD  . MET   A 1 264 ? 125.54606 -9.79317  -14.42991 1.000 34.85902 ?  264 MET   A SD  1 
ATOM   2019 C CE  . MET   A 1 264 ? 125.04388 -11.20868 -15.40536 1.000 31.86438 ?  264 MET   A CE  1 
ATOM   2020 N N   . CYS   A 1 265 ? 130.36600 -7.78113  -13.25083 1.000 32.85701 ?  265 CYS   A N   1 
ATOM   2021 C CA  . CYS   A 1 265 ? 130.92676 -7.13706  -12.06667 1.000 34.92424 ?  265 CYS   A CA  1 
ATOM   2022 C C   . CYS   A 1 265 ? 130.52601 -5.67156  -11.98502 1.000 35.54814 ?  265 CYS   A C   1 
ATOM   2023 O O   . CYS   A 1 265 ? 130.25902 -5.15848  -10.89180 1.000 34.38305 ?  265 CYS   A O   1 
ATOM   2024 C CB  . CYS   A 1 265 ? 132.44831 -7.27841  -12.04420 1.000 33.38966 ?  265 CYS   A CB  1 
ATOM   2025 S SG  . CYS   A 1 265 ? 133.00432 -8.98000  -11.85999 1.000 32.52814 ?  265 CYS   A SG  1 
ATOM   2026 N N   . ALA   A 1 266 ? 130.47817 -4.97858  -13.12944 1.000 35.52154 ?  266 ALA   A N   1 
ATOM   2027 C CA  . ALA   A 1 266 ? 130.07529 -3.57476  -13.12308 1.000 36.24987 ?  266 ALA   A CA  1 
ATOM   2028 C C   . ALA   A 1 266 ? 128.60217 -3.42011  -12.77056 1.000 38.84502 ?  266 ALA   A C   1 
ATOM   2029 O O   . ALA   A 1 266 ? 128.22542 -2.48113  -12.05897 1.000 39.57679 ?  266 ALA   A O   1 
ATOM   2030 C CB  . ALA   A 1 266 ? 130.36316 -2.93151  -14.47861 1.000 38.86143 ?  266 ALA   A CB  1 
ATOM   2031 N N   . SER   A 1 267 ? 127.74853 -4.31500  -13.27734 1.000 37.78141 ?  267 SER   A N   1 
ATOM   2032 C CA  . SER   A 1 267 ? 126.35945 -4.34235  -12.82811 1.000 38.15915 ?  267 SER   A CA  1 
ATOM   2033 C C   . SER   A 1 267 ? 126.27665 -4.56881  -11.32242 1.000 35.28083 ?  267 SER   A C   1 
ATOM   2034 O O   . SER   A 1 267 ? 125.55266 -3.85898  -10.61406 1.000 33.81210 ?  267 SER   A O   1 
ATOM   2035 C CB  . SER   A 1 267 ? 125.58152 -5.42732  -13.57723 1.000 38.39956 ?  267 SER   A CB  1 
ATOM   2036 O OG  . SER   A 1 267 ? 125.38940 -5.07096  -14.93781 1.000 42.28238 ?  267 SER   A OG  1 
ATOM   2037 N N   . LEU   A 1 268 ? 127.01647 -5.55670  -10.81433 1.000 34.75785 ?  268 LEU   A N   1 
ATOM   2038 C CA  . LEU   A 1 268 ? 126.99181 -5.82243  -9.38035  1.000 33.64439 ?  268 LEU   A CA  1 
ATOM   2039 C C   . LEU   A 1 268 ? 127.54306 -4.63405  -8.60160  1.000 35.25798 ?  268 LEU   A C   1 
ATOM   2040 O O   . LEU   A 1 268 ? 127.01842 -4.28260  -7.53785  1.000 36.19763 ?  268 LEU   A O   1 
ATOM   2041 C CB  . LEU   A 1 268 ? 127.78325 -7.09290  -9.06534  1.000 31.96038 ?  268 LEU   A CB  1 
ATOM   2042 C CG  . LEU   A 1 268 ? 128.08601 -7.43626  -7.60440  1.000 31.17170 ?  268 LEU   A CG  1 
ATOM   2043 C CD1 . LEU   A 1 268 ? 126.79319 -7.53453  -6.80426  1.000 29.87013 ?  268 LEU   A CD1 1 
ATOM   2044 C CD2 . LEU   A 1 268 ? 128.85061 -8.74130  -7.50730  1.000 26.26669 ?  268 LEU   A CD2 1 
ATOM   2045 N N   . LYS   A 1 269 ? 128.59332 -3.99655  -9.12888  1.000 32.20690 ?  269 LYS   A N   1 
ATOM   2046 C CA  . LYS   A 1 269 ? 129.12335 -2.76767  -8.53964  1.000 36.98161 ?  269 LYS   A CA  1 
ATOM   2047 C C   . LYS   A 1 269 ? 128.02403 -1.73183  -8.31497  1.000 39.48384 ?  269 LYS   A C   1 
ATOM   2048 O O   . LYS   A 1 269 ? 127.90256 -1.15695  -7.22501  1.000 40.55909 ?  269 LYS   A O   1 
ATOM   2049 C CB  . LYS   A 1 269 ? 130.20932 -2.19782  -9.45297  1.000 40.51448 ?  269 LYS   A CB  1 
ATOM   2050 C CG  . LYS   A 1 269 ? 130.99878 -1.03532  -8.88717  1.000 43.43195 ?  269 LYS   A CG  1 
ATOM   2051 C CD  . LYS   A 1 269 ? 132.22702 -0.77161  -9.75167  1.000 45.19957 ?  269 LYS   A CD  1 
ATOM   2052 C CE  . LYS   A 1 269 ? 132.93590 0.51224   -9.36221  1.000 51.79537 ?  269 LYS   A CE  1 
ATOM   2053 N NZ  . LYS   A 1 269 ? 132.11746 1.71296   -9.66067  1.000 53.28446 ?  269 LYS   A NZ  1 
ATOM   2054 N N   . GLU   A 1 270 ? 127.21979 -1.47038  -9.34735  1.000 36.61711 ?  270 GLU   A N   1 
ATOM   2055 C CA  . GLU   A 1 270 ? 126.18357 -0.45083  -9.23327  1.000 38.07127 ?  270 GLU   A CA  1 
ATOM   2056 C C   . GLU   A 1 270 ? 125.06466 -0.89411  -8.30163  1.000 40.76834 ?  270 GLU   A C   1 
ATOM   2057 O O   . GLU   A 1 270 ? 124.45288 -0.05814  -7.62917  1.000 41.20885 ?  270 GLU   A O   1 
ATOM   2058 C CB  . GLU   A 1 270 ? 125.63240 -0.10311  -10.61514 1.000 40.11443 ?  270 GLU   A CB  1 
ATOM   2059 N N   . LEU   A 1 271 ? 124.78583 -2.19855  -8.24262  1.000 37.70398 ?  271 LEU   A N   1 
ATOM   2060 C CA  . LEU   A 1 271 ? 123.85156 -2.70686  -7.24500  1.000 38.04537 ?  271 LEU   A CA  1 
ATOM   2061 C C   . LEU   A 1 271 ? 124.36609 -2.45227  -5.83727  1.000 39.22797 ?  271 LEU   A C   1 
ATOM   2062 O O   . LEU   A 1 271 ? 123.60104 -2.05159  -4.95346  1.000 40.72956 ?  271 LEU   A O   1 
ATOM   2063 C CB  . LEU   A 1 271 ? 123.61564 -4.19799  -7.46873  1.000 35.13214 ?  271 LEU   A CB  1 
ATOM   2064 C CG  . LEU   A 1 271 ? 122.70614 -4.56869  -8.63930  1.000 33.84879 ?  271 LEU   A CG  1 
ATOM   2065 C CD1 . LEU   A 1 271 ? 122.58408 -6.07718  -8.76045  1.000 34.82713 ?  271 LEU   A CD1 1 
ATOM   2066 C CD2 . LEU   A 1 271 ? 121.33967 -3.93500  -8.45789  1.000 38.02754 ?  271 LEU   A CD2 1 
ATOM   2067 N N   . LEU   A 1 272 ? 125.66477 -2.66877  -5.61725  1.000 36.57909 ?  272 LEU   A N   1 
ATOM   2068 C CA  . LEU   A 1 272 ? 126.23915 -2.50916  -4.28746  1.000 40.23036 ?  272 LEU   A CA  1 
ATOM   2069 C C   . LEU   A 1 272 ? 126.27202 -1.04536  -3.86555  1.000 43.49699 ?  272 LEU   A C   1 
ATOM   2070 O O   . LEU   A 1 272 ? 126.10583 -0.74011  -2.67855  1.000 44.98560 ?  272 LEU   A O   1 
ATOM   2071 C CB  . LEU   A 1 272 ? 127.64956 -3.09604  -4.26238  1.000 38.49535 ?  272 LEU   A CB  1 
ATOM   2072 C CG  . LEU   A 1 272 ? 127.73521 -4.62053  -4.27425  1.000 34.79365 ?  272 LEU   A CG  1 
ATOM   2073 C CD1 . LEU   A 1 272 ? 129.17772 -5.08261  -4.32027  1.000 33.96038 ?  272 LEU   A CD1 1 
ATOM   2074 C CD2 . LEU   A 1 272 ? 127.01236 -5.21554  -3.08259  1.000 35.60570 ?  272 LEU   A CD2 1 
ATOM   2075 N N   . GLN   A 1 273 ? 126.48705 -0.13270  -4.81846  1.000 41.21460 ?  273 GLN   A N   1 
ATOM   2076 C CA  . GLN   A 1 273 ? 126.57870 1.28504   -4.49303  1.000 45.14435 ?  273 GLN   A CA  1 
ATOM   2077 C C   . GLN   A 1 273 ? 125.20814 1.94983   -4.42617  1.000 47.73379 ?  273 GLN   A C   1 
ATOM   2078 O O   . GLN   A 1 273 ? 125.00305 2.86006   -3.61595  1.000 49.34278 ?  273 GLN   A O   1 
ATOM   2079 C CB  . GLN   A 1 273 ? 127.46283 2.00251   -5.51466  1.000 43.88810 ?  273 GLN   A CB  1 
ATOM   2080 C CG  . GLN   A 1 273 ? 128.90838 1.53323   -5.51390  1.000 45.77594 ?  273 GLN   A CG  1 
ATOM   2081 C CD  . GLN   A 1 273 ? 129.67108 1.99985   -6.73626  1.000 47.25149 ?  273 GLN   A CD  1 
ATOM   2082 O OE1 . GLN   A 1 273 ? 130.87349 1.77209   -6.85393  1.000 51.91326 ?  273 GLN   A OE1 1 
ATOM   2083 N NE2 . GLN   A 1 273 ? 128.97086 2.63374   -7.66265  1.000 49.10397 ?  273 GLN   A NE2 1 
ATOM   2084 N N   . ASN   A 1 274 ? 124.26139 1.52664   -5.26580  1.000 45.16149 ?  274 ASN   A N   1 
ATOM   2085 C CA  . ASN   A 1 274 ? 122.97850 2.21148   -5.38641  1.000 47.58382 ?  274 ASN   A CA  1 
ATOM   2086 C C   . ASN   A 1 274 ? 121.81011 1.42143   -4.81390  1.000 48.56907 ?  274 ASN   A C   1 
ATOM   2087 O O   . ASN   A 1 274 ? 120.68178 1.93104   -4.80322  1.000 48.09333 ?  274 ASN   A O   1 
ATOM   2088 C CB  . ASN   A 1 274 ? 122.68128 2.55443   -6.85333  1.000 50.70950 ?  274 ASN   A CB  1 
ATOM   2089 C CG  . ASN   A 1 274 ? 123.82670 3.29033   -7.54174  1.000 54.58332 ?  274 ASN   A CG  1 
ATOM   2090 O OD1 . ASN   A 1 274 ? 123.85222 3.39774   -8.76561  1.000 60.11753 ?  274 ASN   A OD1 1 
ATOM   2091 N ND2 . ASN   A 1 274 ? 124.75594 3.82836   -6.75910  1.000 58.80042 ?  274 ASN   A ND2 1 
ATOM   2092 N N   . GLY   A 1 275 ? 122.03943 0.20095   -4.34790  1.000 47.04985 ?  275 GLY   A N   1 
ATOM   2093 C CA  . GLY   A 1 275 ? 120.96186 -0.58841  -3.79681  1.000 48.50724 ?  275 GLY   A CA  1 
ATOM   2094 C C   . GLY   A 1 275 ? 119.99355 -1.08853  -4.86073  1.000 50.48657 ?  275 GLY   A C   1 
ATOM   2095 O O   . GLY   A 1 275 ? 120.20343 -0.95731  -6.06685  1.000 47.32295 ?  275 GLY   A O   1 
ATOM   2096 N N   . MET   A 1 276 ? 118.90122 -1.67402  -4.37367  1.000 51.50768 ?  276 MET   A N   1 
ATOM   2097 C CA  . MET   A 1 276 ? 117.86368 -2.22869  -5.22907  1.000 53.49475 ?  276 MET   A CA  1 
ATOM   2098 C C   . MET   A 1 276 ? 116.72237 -1.24623  -5.45975  1.000 57.49161 ?  276 MET   A C   1 
ATOM   2099 O O   . MET   A 1 276 ? 115.91213 -1.45547  -6.37237  1.000 53.74835 ?  276 MET   A O   1 
ATOM   2100 C CB  . MET   A 1 276 ? 117.31636 -3.51629  -4.60269  1.000 52.57568 ?  276 MET   A CB  1 
ATOM   2101 C CG  . MET   A 1 276 ? 118.24530 -4.71692  -4.73175  1.000 49.23322 ?  276 MET   A CG  1 
ATOM   2102 S SD  . MET   A 1 276 ? 117.43201 -6.18970  -5.35761  1.000 50.38262 ?  276 MET   A SD  1 
ATOM   2103 C CE  . MET   A 1 276 ? 118.83633 -7.27481  -5.59757  1.000 34.01131 ?  276 MET   A CE  1 
ATOM   2104 N N   . ASN   A 1 277 ? 116.65566 -0.18682  -4.64865  1.000 56.30665 ?  277 ASN   A N   1 
ATOM   2105 C CA  . ASN   A 1 277 ? 115.64450 0.86495   -4.69095  1.000 57.36934 ?  277 ASN   A CA  1 
ATOM   2106 C C   . ASN   A 1 277 ? 114.25073 0.32051   -5.00190  1.000 54.79147 ?  277 ASN   A C   1 
ATOM   2107 O O   . ASN   A 1 277 ? 113.45138 0.96177   -5.69201  1.000 59.80922 ?  277 ASN   A O   1 
ATOM   2108 C CB  . ASN   A 1 277 ? 116.09726 1.97935   -5.65579  1.000 60.56851 ?  277 ASN   A CB  1 
ATOM   2109 C CG  . ASN   A 1 277 ? 115.78068 1.69326   -7.11069  1.000 58.85942 ?  277 ASN   A CG  1 
ATOM   2110 O OD1 . ASN   A 1 277 ? 116.33852 0.78243   -7.71660  1.000 59.99289 ?  277 ASN   A OD1 1 
ATOM   2111 N ND2 . ASN   A 1 277 ? 114.89841 2.49909   -7.68715  1.000 65.80534 ?  277 ASN   A ND2 1 
ATOM   2112 N N   . GLY   A 1 278 ? 113.94221 -0.85666  -4.45933  1.000 53.84835 ?  278 GLY   A N   1 
ATOM   2113 C CA  . GLY   A 1 278 ? 112.59150 -1.38087  -4.44773  1.000 54.35774 ?  278 GLY   A CA  1 
ATOM   2114 C C   . GLY   A 1 278 ? 112.31206 -2.48367  -5.44236  1.000 50.85161 ?  278 GLY   A C   1 
ATOM   2115 O O   . GLY   A 1 278 ? 111.22693 -3.07651  -5.38712  1.000 53.49899 ?  278 GLY   A O   1 
ATOM   2116 N N   . ARG   A 1 279 ? 113.23330 -2.77426  -6.35388  1.000 51.60429 ?  279 ARG   A N   1 
ATOM   2117 C CA  . ARG   A 1 279 ? 113.00521 -3.84331  -7.30867  1.000 46.34141 ?  279 ARG   A CA  1 
ATOM   2118 C C   . ARG   A 1 279 ? 113.41329 -5.18547  -6.70668  1.000 43.71514 ?  279 ARG   A C   1 
ATOM   2119 O O   . ARG   A 1 279 ? 113.97465 -5.26497  -5.60932  1.000 43.96812 ?  279 ARG   A O   1 
ATOM   2120 C CB  . ARG   A 1 279 ? 113.76687 -3.57749  -8.60655  1.000 46.77741 ?  279 ARG   A CB  1 
ATOM   2121 N N   . THR   A 1 280 ? 113.12069 -6.25485  -7.44351  1.000 39.35281 ?  280 THR   A N   1 
ATOM   2122 C CA  . THR   A 1 280 ? 113.44852 -7.61002  -7.02657  1.000 38.96973 ?  280 THR   A CA  1 
ATOM   2123 C C   . THR   A 1 280 ? 114.18677 -8.33352  -8.14605  1.000 38.94912 ?  280 THR   A C   1 
ATOM   2124 O O   . THR   A 1 280 ? 114.02321 -8.01712  -9.32973  1.000 41.83663 ?  280 THR   A O   1 
ATOM   2125 C CB  . THR   A 1 280 ? 112.18896 -8.40534  -6.63992  1.000 40.55265 ?  280 THR   A CB  1 
ATOM   2126 O OG1 . THR   A 1 280 ? 111.33684 -8.54099  -7.78388  1.000 42.85094 ?  280 THR   A OG1 1 
ATOM   2127 C CG2 . THR   A 1 280 ? 111.42662 -7.69195  -5.53631  1.000 42.81744 ?  280 THR   A CG2 1 
ATOM   2128 N N   . ILE   A 1 281 ? 115.01343 -9.30187  -7.75401  1.000 36.37389 ?  281 ILE   A N   1 
ATOM   2129 C CA  . ILE   A 1 281 ? 115.75913 -10.15278 -8.67636  1.000 34.97641 ?  281 ILE   A CA  1 
ATOM   2130 C C   . ILE   A 1 281 ? 115.47149 -11.59948 -8.31776  1.000 33.02690 ?  281 ILE   A C   1 
ATOM   2131 O O   . ILE   A 1 281 ? 115.76244 -12.02909 -7.19680  1.000 30.36041 ?  281 ILE   A O   1 
ATOM   2132 C CB  . ILE   A 1 281 ? 117.27020 -9.88692  -8.62076  1.000 33.90512 ?  281 ILE   A CB  1 
ATOM   2133 C CG1 . ILE   A 1 281 ? 117.56341 -8.40779  -8.86674  1.000 35.68004 ?  281 ILE   A CG1 1 
ATOM   2134 C CG2 . ILE   A 1 281 ? 118.00686 -10.80247 -9.58820  1.000 32.52090 ?  281 ILE   A CG2 1 
ATOM   2135 C CD1 . ILE   A 1 281 ? 118.96592 -8.12629  -9.30829  1.000 36.61431 ?  281 ILE   A CD1 1 
ATOM   2136 N N   . LEU   A 1 282 ? 114.91679 -12.35214 -9.26915  1.000 34.66751 ?  282 LEU   A N   1 
ATOM   2137 C CA  . LEU   A 1 282 ? 114.53949 -13.74585 -9.03834  1.000 32.16580 ?  282 LEU   A CA  1 
ATOM   2138 C C   . LEU   A 1 282 ? 113.72664 -13.90426 -7.75689  1.000 31.66683 ?  282 LEU   A C   1 
ATOM   2139 O O   . LEU   A 1 282 ? 113.89141 -14.86875 -7.00775  1.000 32.97682 ?  282 LEU   A O   1 
ATOM   2140 C CB  . LEU   A 1 282 ? 115.76757 -14.65357 -9.01088  1.000 29.42697 ?  282 LEU   A CB  1 
ATOM   2141 C CG  . LEU   A 1 282 ? 116.49817 -14.80881 -10.33968 1.000 29.37598 ?  282 LEU   A CG  1 
ATOM   2142 C CD1 . LEU   A 1 282 ? 117.76033 -15.62961 -10.13687 1.000 28.55859 ?  282 LEU   A CD1 1 
ATOM   2143 C CD2 . LEU   A 1 282 ? 115.59200 -15.46247 -11.36986 1.000 32.75956 ?  282 LEU   A CD2 1 
ATOM   2144 N N   . GLY   A 1 283 ? 112.84753 -12.93668 -7.49870  1.000 32.20330 ?  283 GLY   A N   1 
ATOM   2145 C CA  . GLY   A 1 283 ? 111.96457 -12.98294 -6.35461  1.000 35.76774 ?  283 GLY   A CA  1 
ATOM   2146 C C   . GLY   A 1 283 ? 112.56427 -12.54380 -5.03831  1.000 36.05301 ?  283 GLY   A C   1 
ATOM   2147 O O   . GLY   A 1 283 ? 111.87375 -12.61398 -4.01339  1.000 38.89639 ?  283 GLY   A O   1 
ATOM   2148 N N   . SER   A 1 284 ? 113.82091 -12.10177 -5.01794  1.000 31.75623 ?  284 SER   A N   1 
ATOM   2149 C CA  . SER   A 1 284 ? 114.46067 -11.64998 -3.79095  1.000 32.93053 ?  284 SER   A CA  1 
ATOM   2150 C C   . SER   A 1 284 ? 114.76797 -10.16106 -3.88733  1.000 34.67821 ?  284 SER   A C   1 
ATOM   2151 O O   . SER   A 1 284 ? 115.07830 -9.63919  -4.96098  1.000 32.41723 ?  284 SER   A O   1 
ATOM   2152 C CB  . SER   A 1 284 ? 115.74743 -12.43251 -3.50300  1.000 33.36252 ?  284 SER   A CB  1 
ATOM   2153 O OG  . SER   A 1 284 ? 116.60486 -11.70989 -2.63045  1.000 34.38683 ?  284 SER   A OG  1 
ATOM   2154 N N   . ALA   A 1 285 ? 114.65978 -9.47720  -2.75480  1.000 30.13859 ?  285 ALA   A N   1 
ATOM   2155 C CA  . ALA   A 1 285 ? 115.03358 -8.07636  -2.65641  1.000 34.53176 ?  285 ALA   A CA  1 
ATOM   2156 C C   . ALA   A 1 285 ? 116.46058 -7.89127  -2.15939  1.000 34.51114 ?  285 ALA   A C   1 
ATOM   2157 O O   . ALA   A 1 285 ? 116.90471 -6.75132  -1.99561  1.000 37.74920 ?  285 ALA   A O   1 
ATOM   2158 C CB  . ALA   A 1 285 ? 114.05625 -7.33714  -1.74222  1.000 33.66427 ?  285 ALA   A CB  1 
ATOM   2159 N N   . LEU   A 1 286 ? 117.18125 -8.98856  -1.92897  1.000 31.66709 ?  286 LEU   A N   1 
ATOM   2160 C CA  . LEU   A 1 286 ? 118.56001 -9.02518  -1.46914  1.000 32.52115 ?  286 LEU   A CA  1 
ATOM   2161 C C   . LEU   A 1 286 ? 119.41923 -9.67430  -2.54575  1.000 30.49296 ?  286 LEU   A C   1 
ATOM   2162 O O   . LEU   A 1 286 ? 118.92009 -10.40517 -3.40590  1.000 31.62653 ?  286 LEU   A O   1 
ATOM   2163 C CB  . LEU   A 1 286 ? 118.67709 -9.83816  -0.16683  1.000 33.05377 ?  286 LEU   A CB  1 
ATOM   2164 C CG  . LEU   A 1 286 ? 118.21116 -9.20794  1.13989   1.000 34.76681 ?  286 LEU   A CG  1 
ATOM   2165 C CD1 . LEU   A 1 286 ? 118.98155 -9.77709  2.30428   1.000 37.98740 ?  286 LEU   A CD1 1 
ATOM   2166 C CD2 . LEU   A 1 286 ? 118.41273 -7.70011  1.07061   1.000 35.63886 ?  286 LEU   A CD2 1 
ATOM   2167 N N   . LEU   A 1 287 ? 120.72223 -9.42440  -2.49238  1.000 27.12660 ?  287 LEU   A N   1 
ATOM   2168 C CA  . LEU   A 1 287 ? 121.63910 -10.14466 -3.36421  1.000 27.87795 ?  287 LEU   A CA  1 
ATOM   2169 C C   . LEU   A 1 287 ? 121.96279 -11.50451 -2.74202  1.000 27.13269 ?  287 LEU   A C   1 
ATOM   2170 O O   . LEU   A 1 287 ? 122.54485 -11.57093 -1.65630  1.000 28.67211 ?  287 LEU   A O   1 
ATOM   2171 C CB  . LEU   A 1 287 ? 122.89804 -9.31761  -3.60638  1.000 29.22628 ?  287 LEU   A CB  1 
ATOM   2172 C CG  . LEU   A 1 287 ? 122.65122 -7.97246  -4.29469  1.000 29.50947 ?  287 LEU   A CG  1 
ATOM   2173 C CD1 . LEU   A 1 287 ? 123.83911 -7.05230  -4.10646  1.000 31.89061 ?  287 LEU   A CD1 1 
ATOM   2174 C CD2 . LEU   A 1 287 ? 122.34286 -8.15983  -5.77396  1.000 30.75557 ?  287 LEU   A CD2 1 
ATOM   2175 N N   . GLU   A 1 288 ? 121.60228 -12.58788 -3.43707  1.000 25.98903 ?  288 GLU   A N   1 
ATOM   2176 C CA  . GLU   A 1 288 ? 121.71671 -13.95218 -2.92218  1.000 27.01441 ?  288 GLU   A CA  1 
ATOM   2177 C C   . GLU   A 1 288 ? 123.08352 -14.56415 -3.20841  1.000 25.60804 ?  288 GLU   A C   1 
ATOM   2178 O O   . GLU   A 1 288 ? 123.54854 -14.55134 -4.35246  1.000 21.26199 ?  288 GLU   A O   1 
ATOM   2179 C CB  . GLU   A 1 288 ? 120.62568 -14.83221 -3.53948  1.000 28.29520 ?  288 GLU   A CB  1 
ATOM   2180 C CG  . GLU   A 1 288 ? 119.43714 -15.17711 -2.63639  1.000 40.72443 ?  288 GLU   A CG  1 
ATOM   2181 C CD  . GLU   A 1 288 ? 119.84114 -15.85646 -1.32104  1.000 39.69711 ?  288 GLU   A CD  1 
ATOM   2182 O OE1 . GLU   A 1 288 ? 119.28056 -15.47703 -0.26895  1.000 46.09104 ?  288 GLU   A OE1 1 
ATOM   2183 O OE2 . GLU   A 1 288 ? 120.70116 -16.78110 -1.33797  1.000 37.02503 -1 288 GLU   A OE2 1 
ATOM   2184 N N   . ASP   A 1 289 ? 123.70959 -15.15561 -2.18270  1.000 22.03360 ?  289 ASP   A N   1 
ATOM   2185 C CA  . ASP   A 1 289 ? 125.05667 -15.68553 -2.37459  1.000 23.47770 ?  289 ASP   A CA  1 
ATOM   2186 C C   . ASP   A 1 289 ? 125.17945 -17.15967 -2.01183  1.000 22.14949 ?  289 ASP   A C   1 
ATOM   2187 O O   . ASP   A 1 289 ? 126.29724 -17.65380 -1.84799  1.000 21.17520 ?  289 ASP   A O   1 
ATOM   2188 C CB  . ASP   A 1 289 ? 126.09191 -14.85149 -1.60491  1.000 24.85771 ?  289 ASP   A CB  1 
ATOM   2189 C CG  . ASP   A 1 289 ? 126.17737 -15.18826 -0.12354  1.000 22.92899 ?  289 ASP   A CG  1 
ATOM   2190 O OD1 . ASP   A 1 289 ? 125.21538 -15.72386 0.46833   1.000 23.46360 ?  289 ASP   A OD1 1 
ATOM   2191 O OD2 . ASP   A 1 289 ? 127.21684 -14.82365 0.46917   1.000 23.34079 -1 289 ASP   A OD2 1 
ATOM   2192 N N   . GLU   A 1 290 ? 124.07211 -17.89266 -1.89788  1.000 23.25955 ?  290 GLU   A N   1 
ATOM   2193 C CA  . GLU   A 1 290 ? 124.17886 -19.30744 -1.57561  1.000 23.97019 ?  290 GLU   A CA  1 
ATOM   2194 C C   . GLU   A 1 290 ? 123.84899 -20.20818 -2.77122  1.000 26.79126 ?  290 GLU   A C   1 
ATOM   2195 O O   . GLU   A 1 290 ? 123.41003 -21.34473 -2.58980  1.000 24.58968 ?  290 GLU   A O   1 
ATOM   2196 C CB  . GLU   A 1 290 ? 123.32363 -19.64499 -0.34773  1.000 26.31946 ?  290 GLU   A CB  1 
ATOM   2197 C CG  . GLU   A 1 290 ? 123.64878 -18.76049 0.88422   1.000 26.85828 ?  290 GLU   A CG  1 
ATOM   2198 C CD  . GLU   A 1 290 ? 123.57706 -19.48824 2.24220   1.000 28.71989 ?  290 GLU   A CD  1 
ATOM   2199 O OE1 . GLU   A 1 290 ? 122.84092 -20.48533 2.37033   1.000 26.75059 ?  290 GLU   A OE1 1 
ATOM   2200 O OE2 . GLU   A 1 290 ? 124.21818 -19.01877 3.21714   1.000 27.56598 -1 290 GLU   A OE2 1 
ATOM   2201 N N   . PHE   A 1 291 ? 124.10177 -19.73683 -4.00019  1.000 22.43501 ?  291 PHE   A N   1 
ATOM   2202 C CA  . PHE   A 1 291 ? 124.08698 -20.58468 -5.19194  1.000 23.11878 ?  291 PHE   A CA  1 
ATOM   2203 C C   . PHE   A 1 291 ? 125.48365 -20.56104 -5.79323  1.000 20.09472 ?  291 PHE   A C   1 
ATOM   2204 O O   . PHE   A 1 291 ? 125.96251 -19.49053 -6.17148  1.000 21.51365 ?  291 PHE   A O   1 
ATOM   2205 C CB  . PHE   A 1 291 ? 123.08625 -20.08747 -6.24315  1.000 24.30679 ?  291 PHE   A CB  1 
ATOM   2206 C CG  . PHE   A 1 291 ? 121.65081 -20.17539 -5.82269  1.000 26.14035 ?  291 PHE   A CG  1 
ATOM   2207 C CD1 . PHE   A 1 291 ? 120.94377 -21.35568 -5.95228  1.000 27.77493 ?  291 PHE   A CD1 1 
ATOM   2208 C CD2 . PHE   A 1 291 ? 121.00141 -19.05956 -5.32271  1.000 27.13757 ?  291 PHE   A CD2 1 
ATOM   2209 C CE1 . PHE   A 1 291 ? 119.60799 -21.42313 -5.57478  1.000 29.55020 ?  291 PHE   A CE1 1 
ATOM   2210 C CE2 . PHE   A 1 291 ? 119.66708 -19.11453 -4.95351  1.000 32.67686 ?  291 PHE   A CE2 1 
ATOM   2211 C CZ  . PHE   A 1 291 ? 118.97162 -20.29905 -5.07369  1.000 31.39301 ?  291 PHE   A CZ  1 
ATOM   2212 N N   . THR   A 1 292 ? 126.13546 -21.73224 -5.90129  1.000 20.92830 ?  292 THR   A N   1 
ATOM   2213 C CA  . THR   A 1 292 ? 127.42894 -21.77438 -6.57577  1.000 21.16490 ?  292 THR   A CA  1 
ATOM   2214 C C   . THR   A 1 292 ? 127.23500 -21.72473 -8.08734  1.000 23.57379 ?  292 THR   A C   1 
ATOM   2215 O O   . THR   A 1 292 ? 126.13606 -21.97480 -8.58984  1.000 23.73779 ?  292 THR   A O   1 
ATOM   2216 C CB  . THR   A 1 292 ? 128.19788 -23.04751 -6.24998  1.000 23.87805 ?  292 THR   A CB  1 
ATOM   2217 O OG1 . THR   A 1 292 ? 127.49920 -24.17382 -6.80329  1.000 24.50247 ?  292 THR   A OG1 1 
ATOM   2218 C CG2 . THR   A 1 292 ? 128.37683 -23.21572 -4.75200  1.000 24.88536 ?  292 THR   A CG2 1 
ATOM   2219 N N   . PRO   A 1 293 ? 128.29003 -21.42249 -8.83848  1.000 24.85107 ?  293 PRO   A N   1 
ATOM   2220 C CA  . PRO   A 1 293 ? 128.17848 -21.54011 -10.30211 1.000 23.96867 ?  293 PRO   A CA  1 
ATOM   2221 C C   . PRO   A 1 293 ? 127.72448 -22.92500 -10.74175 1.000 28.49819 ?  293 PRO   A C   1 
ATOM   2222 O O   . PRO   A 1 293 ? 126.91529 -23.05499 -11.66796 1.000 26.41597 ?  293 PRO   A O   1 
ATOM   2223 C CB  . PRO   A 1 293 ? 129.59684 -21.21491 -10.77580 1.000 26.64704 ?  293 PRO   A CB  1 
ATOM   2224 C CG  . PRO   A 1 293 ? 130.11310 -20.27873 -9.73790  1.000 25.07414 ?  293 PRO   A CG  1 
ATOM   2225 C CD  . PRO   A 1 293 ? 129.55809 -20.78205 -8.43497  1.000 24.29230 ?  293 PRO   A CD  1 
ATOM   2226 N N   . PHE   A 1 294 ? 128.21920 -23.96721 -10.07342 1.000 24.42704 ?  294 PHE   A N   1 
ATOM   2227 C CA  . PHE   A 1 294 ? 127.77957 -25.32742 -10.36730 1.000 30.24015 ?  294 PHE   A CA  1 
ATOM   2228 C C   . PHE   A 1 294 ? 126.28607 -25.48886 -10.09930 1.000 28.75121 ?  294 PHE   A C   1 
ATOM   2229 O O   . PHE   A 1 294 ? 125.57041 -26.11119 -10.89638 1.000 28.30445 ?  294 PHE   A O   1 
ATOM   2230 C CB  . PHE   A 1 294 ? 128.58974 -26.31510 -9.52602  1.000 35.19276 ?  294 PHE   A CB  1 
ATOM   2231 C CG  . PHE   A 1 294 ? 129.90569 -26.71494 -10.14500 1.000 49.34742 ?  294 PHE   A CG  1 
ATOM   2232 C CD1 . PHE   A 1 294 ? 130.69027 -25.78372 -10.81649 1.000 49.68246 ?  294 PHE   A CD1 1 
ATOM   2233 C CD2 . PHE   A 1 294 ? 130.38554 -28.00778 -10.00768 1.000 64.78381 ?  294 PHE   A CD2 1 
ATOM   2234 C CE1 . PHE   A 1 294 ? 131.90651 -26.14138 -11.36981 1.000 53.81741 ?  294 PHE   A CE1 1 
ATOM   2235 C CE2 . PHE   A 1 294 ? 131.60533 -28.37041 -10.55256 1.000 60.24533 ?  294 PHE   A CE2 1 
ATOM   2236 C CZ  . PHE   A 1 294 ? 132.36542 -27.43584 -11.23817 1.000 58.21353 ?  294 PHE   A CZ  1 
ATOM   2237 N N   . ASP   A 1 295 ? 125.79961 -24.92965 -8.97973  1.000 27.71479 ?  295 ASP   A N   1 
ATOM   2238 C CA  . ASP   A 1 295 ? 124.37257 -24.97609 -8.65742  1.000 27.85370 ?  295 ASP   A CA  1 
ATOM   2239 C C   . ASP   A 1 295 ? 123.52599 -24.37334 -9.76318  1.000 30.80467 ?  295 ASP   A C   1 
ATOM   2240 O O   . ASP   A 1 295 ? 122.46134 -24.90738 -10.09874 1.000 33.09016 ?  295 ASP   A O   1 
ATOM   2241 C CB  . ASP   A 1 295 ? 124.07680 -24.23394 -7.35211  1.000 24.42310 ?  295 ASP   A CB  1 
ATOM   2242 C CG  . ASP   A 1 295 ? 124.72687 -24.86333 -6.14937  1.000 28.57414 ?  295 ASP   A CG  1 
ATOM   2243 O OD1 . ASP   A 1 295 ? 125.23832 -25.99473 -6.26373  1.000 30.04710 ?  295 ASP   A OD1 1 
ATOM   2244 O OD2 . ASP   A 1 295 ? 124.75034 -24.19906 -5.09125  1.000 24.21401 -1 295 ASP   A OD2 1 
ATOM   2245 N N   . VAL   A 1 296 ? 123.96144 -23.23620 -10.30994 1.000 28.89367 ?  296 VAL   A N   1 
ATOM   2246 C CA  . VAL   A 1 296 ? 123.19716 -22.55777 -11.34911 1.000 27.97713 ?  296 VAL   A CA  1 
ATOM   2247 C C   . VAL   A 1 296 ? 123.17808 -23.39337 -12.61962 1.000 32.15881 ?  296 VAL   A C   1 
ATOM   2248 O O   . VAL   A 1 296 ? 122.12631 -23.57442 -13.24686 1.000 32.55655 ?  296 VAL   A O   1 
ATOM   2249 C CB  . VAL   A 1 296 ? 123.78601 -21.15563 -11.59602 1.000 27.50416 ?  296 VAL   A CB  1 
ATOM   2250 C CG1 . VAL   A 1 296 ? 123.12994 -20.50469 -12.79612 1.000 28.71619 ?  296 VAL   A CG1 1 
ATOM   2251 C CG2 . VAL   A 1 296 ? 123.63317 -20.30115 -10.35229 1.000 26.21123 ?  296 VAL   A CG2 1 
ATOM   2252 N N   . VAL   A 1 297 ? 124.33930 -23.92245 -13.01358 1.000 31.95196 ?  297 VAL   A N   1 
ATOM   2253 C CA  . VAL   A 1 297 ? 124.42196 -24.74227 -14.22073 1.000 33.44573 ?  297 VAL   A CA  1 
ATOM   2254 C C   . VAL   A 1 297 ? 123.56277 -25.98892 -14.06767 1.000 36.08243 ?  297 VAL   A C   1 
ATOM   2255 O O   . VAL   A 1 297 ? 122.84921 -26.39202 -14.99645 1.000 40.73582 ?  297 VAL   A O   1 
ATOM   2256 C CB  . VAL   A 1 297 ? 125.89122 -25.10044 -14.51844 1.000 31.82489 ?  297 VAL   A CB  1 
ATOM   2257 C CG1 . VAL   A 1 297 ? 125.97419 -26.26187 -15.50752 1.000 35.65121 ?  297 VAL   A CG1 1 
ATOM   2258 C CG2 . VAL   A 1 297 ? 126.64878 -23.88375 -15.03779 1.000 33.51628 ?  297 VAL   A CG2 1 
ATOM   2259 N N   . ARG   A 1 298 ? 123.60743 -26.60870 -12.88456 1.000 34.37439 ?  298 ARG   A N   1 
ATOM   2260 C CA  . ARG   A 1 298 ? 122.82138 -27.81198 -12.63497 1.000 37.49700 ?  298 ARG   A CA  1 
ATOM   2261 C C   . ARG   A 1 298 ? 121.33171 -27.53191 -12.77019 1.000 39.46920 ?  298 ARG   A C   1 
ATOM   2262 O O   . ARG   A 1 298 ? 120.61100 -28.26409 -13.45760 1.000 43.29293 ?  298 ARG   A O   1 
ATOM   2263 C CB  . ARG   A 1 298 ? 123.13627 -28.36570 -11.24462 1.000 36.53719 ?  298 ARG   A CB  1 
ATOM   2264 N N   . GLN   A 1 299 ? 120.85002 -26.47302 -12.11497 1.000 36.86325 ?  299 GLN   A N   1 
ATOM   2265 C CA  . GLN   A 1 299 ? 119.42024 -26.18787 -12.14099 1.000 38.69494 ?  299 GLN   A CA  1 
ATOM   2266 C C   . GLN   A 1 299 ? 118.96546 -25.75393 -13.52160 1.000 42.71247 ?  299 GLN   A C   1 
ATOM   2267 O O   . GLN   A 1 299 ? 117.84922 -26.08253 -13.93967 1.000 47.32946 ?  299 GLN   A O   1 
ATOM   2268 C CB  . GLN   A 1 299 ? 119.05887 -25.11825 -11.10853 1.000 36.28194 ?  299 GLN   A CB  1 
ATOM   2269 C CG  . GLN   A 1 299 ? 117.56723 -24.79351 -11.08477 1.000 35.69019 ?  299 GLN   A CG  1 
ATOM   2270 C CD  . GLN   A 1 299 ? 117.09116 -24.14096 -9.79813  1.000 32.22868 ?  299 GLN   A CD  1 
ATOM   2271 O OE1 . GLN   A 1 299 ? 115.95950 -23.66127 -9.72782  1.000 31.83970 ?  299 GLN   A OE1 1 
ATOM   2272 N NE2 . GLN   A 1 299 ? 117.94120 -24.12513 -8.77770  1.000 29.89200 ?  299 GLN   A NE2 1 
ATOM   2273 N N   . CYS   A 1 300 ? 119.81057 -25.02941 -14.24656 1.000 42.76243 ?  300 CYS   A N   1 
ATOM   2274 C CA  . CYS   A 1 300 ? 119.43151 -24.58406 -15.57629 1.000 43.25428 ?  300 CYS   A CA  1 
ATOM   2275 C C   . CYS   A 1 300 ? 119.62758 -25.66269 -16.63728 1.000 48.04249 ?  300 CYS   A C   1 
ATOM   2276 O O   . CYS   A 1 300 ? 119.05803 -25.54687 -17.72589 1.000 43.47527 ?  300 CYS   A O   1 
ATOM   2277 C CB  . CYS   A 1 300 ? 120.21049 -23.31525 -15.93237 1.000 43.86303 ?  300 CYS   A CB  1 
ATOM   2278 S SG  . CYS   A 1 300 ? 119.78089 -21.91910 -14.84592 1.000 44.49574 ?  300 CYS   A SG  1 
ATOM   2279 N N   . SER   A 1 301 ? 120.38907 -26.72012 -16.34206 1.000 42.36886 ?  301 SER   A N   1 
ATOM   2280 C CA  . SER   A 1 301 ? 120.57060 -27.82245 -17.27856 1.000 46.19842 ?  301 SER   A CA  1 
ATOM   2281 C C   . SER   A 1 301 ? 119.81298 -29.08967 -16.89413 1.000 47.51696 ?  301 SER   A C   1 
ATOM   2282 O O   . SER   A 1 301 ? 119.81291 -30.04943 -17.67473 1.000 50.29538 ?  301 SER   A O   1 
ATOM   2283 C CB  . SER   A 1 301 ? 122.06325 -28.15385 -17.42897 1.000 49.42360 ?  301 SER   A CB  1 
ATOM   2284 O OG  . SER   A 1 301 ? 122.24596 -29.37650 -18.12112 1.000 63.12572 ?  301 SER   A OG  1 
ATOM   2285 N N   . GLY   A 1 302 ? 119.17786 -29.12633 -15.72272 1.000 47.67326 ?  302 GLY   A N   1 
ATOM   2286 C CA  . GLY   A 1 302 ? 118.35634 -30.25736 -15.32982 1.000 43.02399 ?  302 GLY   A CA  1 
ATOM   2287 C C   . GLY   A 1 302 ? 119.11980 -31.54123 -15.07447 1.000 43.87907 ?  302 GLY   A C   1 
ATOM   2288 O O   . GLY   A 1 302 ? 118.72558 -32.60820 -15.55473 1.000 42.45301 ?  302 GLY   A O   1 
ATOM   2289 N N   . VAL   A 1 303 ? 120.21113 -31.45173 -14.31300 1.000 43.34192 ?  303 VAL   A N   1 
ATOM   2290 C CA  . VAL   A 1 303 ? 121.00701 -32.63015 -13.98491 1.000 43.65252 ?  303 VAL   A CA  1 
ATOM   2291 C C   . VAL   A 1 303 ? 120.23172 -33.51154 -13.01249 1.000 43.62589 ?  303 VAL   A C   1 
ATOM   2292 O O   . VAL   A 1 303 ? 119.65703 -33.02100 -12.03168 1.000 42.51887 ?  303 VAL   A O   1 
ATOM   2293 C CB  . VAL   A 1 303 ? 122.36454 -32.20351 -13.40204 1.000 44.41256 ?  303 VAL   A CB  1 
ATOM   2294 C CG1 . VAL   A 1 303 ? 123.12974 -33.40434 -12.84019 1.000 45.93848 ?  303 VAL   A CG1 1 
ATOM   2295 C CG2 . VAL   A 1 303 ? 123.19120 -31.47594 -14.45918 1.000 45.96323 ?  303 VAL   A CG2 1 
ATOM   2296 N N   . THR   A 1 304 ? 120.20363 -34.81705 -13.28052 1.000 40.76684 ?  304 THR   A N   1 
ATOM   2297 C CA  . THR   A 1 304 ? 119.54426 -35.78355 -12.41083 1.000 42.22158 ?  304 THR   A CA  1 
ATOM   2298 C C   . THR   A 1 304 ? 120.57583 -36.69566 -11.74460 1.000 50.56504 ?  304 THR   A C   1 
ATOM   2299 O O   . THR   A 1 304 ? 121.75451 -36.72354 -12.11286 1.000 47.73270 ?  304 THR   A O   1 
ATOM   2300 C CB  . THR   A 1 304 ? 118.50981 -36.60880 -13.19057 1.000 40.50439 ?  304 THR   A CB  1 
ATOM   2301 O OG1 . THR   A 1 304 ? 119.15970 -37.36444 -14.21968 1.000 44.96298 ?  304 THR   A OG1 1 
ATOM   2302 C CG2 . THR   A 1 304 ? 117.47971 -35.68932 -13.84256 1.000 35.84800 ?  304 THR   A CG2 1 
ATOM   2303 N N   . PHE   A 1 305 ? 120.11975 -37.44094 -10.73782 1.000 42.97141 ?  305 PHE   A N   1 
ATOM   2304 C CA  . PHE   A 1 305 ? 121.00413 -38.32733 -9.97414  1.000 45.51874 ?  305 PHE   A CA  1 
ATOM   2305 C C   . PHE   A 1 305 ? 120.44863 -39.74557 -9.87410  1.000 45.62975 ?  305 PHE   A C   1 
ATOM   2306 O O   . PHE   A 1 305 ? 119.25244 -39.96903 -10.06654 1.000 45.95994 ?  305 PHE   A O   1 
ATOM   2307 C CB  . PHE   A 1 305 ? 121.24423 -37.75524 -8.57200  1.000 43.10217 ?  305 PHE   A CB  1 
ATOM   2308 C CG  . PHE   A 1 305 ? 121.63490 -36.31415 -8.58277  1.000 41.78656 ?  305 PHE   A CG  1 
ATOM   2309 C CD1 . PHE   A 1 305 ? 122.92731 -35.93695 -8.91713  1.000 44.42206 ?  305 PHE   A CD1 1 
ATOM   2310 C CD2 . PHE   A 1 305 ? 120.69791 -35.32995 -8.31946  1.000 40.03907 ?  305 PHE   A CD2 1 
ATOM   2311 C CE1 . PHE   A 1 305 ? 123.28775 -34.60301 -8.95783  1.000 44.16260 ?  305 PHE   A CE1 1 
ATOM   2312 C CE2 . PHE   A 1 305 ? 121.04896 -33.99299 -8.36219  1.000 40.14974 ?  305 PHE   A CE2 1 
ATOM   2313 C CZ  . PHE   A 1 305 ? 122.34479 -33.62978 -8.68483  1.000 44.76403 ?  305 PHE   A CZ  1 
HETATM 2314 C C13 . A1ALF B 2 .   ? 125.63515 -27.82662 21.86259  1.000 29.19463 ?  401 A1ALF A C13 1 
HETATM 2315 C C15 . A1ALF B 2 .   ? 127.82795 -28.47766 22.96116  1.000 28.80365 ?  401 A1ALF A C15 1 
HETATM 2316 C C17 . A1ALF B 2 .   ? 128.48580 -29.37887 23.97600  1.000 30.48558 ?  401 A1ALF A C17 1 
HETATM 2317 C C20 . A1ALF B 2 .   ? 125.30528 -23.88198 22.44980  1.000 32.41013 ?  401 A1ALF A C20 1 
HETATM 2318 C C21 . A1ALF B 2 .   ? 124.27821 -22.89695 22.49869  1.000 33.57739 ?  401 A1ALF A C21 1 
HETATM 2319 C C22 . A1ALF B 2 .   ? 124.54140 -21.65477 23.03991  1.000 35.07444 ?  401 A1ALF A C22 1 
HETATM 2320 C C24 . A1ALF B 2 .   ? 126.18839 -19.95247 24.17038  1.000 37.78356 ?  401 A1ALF A C24 1 
HETATM 2321 C C26 . A1ALF B 2 .   ? 127.32204 -18.52949 25.81400  1.000 37.79780 ?  401 A1ALF A C26 1 
HETATM 2322 C C02 . A1ALF B 2 .   ? 121.37024 -25.73816 18.42201  1.000 32.43648 ?  401 A1ALF A C02 1 
HETATM 2323 C C04 . A1ALF B 2 .   ? 119.48200 -25.74482 19.99642  1.000 43.05025 ?  401 A1ALF A C04 1 
HETATM 2324 C C05 . A1ALF B 2 .   ? 120.34234 -26.74021 20.34027  1.000 35.32517 ?  401 A1ALF A C05 1 
HETATM 2325 C C06 . A1ALF B 2 .   ? 121.63556 -26.64921 19.36861  1.000 35.28184 ?  401 A1ALF A C06 1 
HETATM 2326 C C07 . A1ALF B 2 .   ? 121.98832 -28.08822 18.73119  1.000 29.11577 ?  401 A1ALF A C07 1 
HETATM 2327 C C08 . A1ALF B 2 .   ? 122.54076 -29.12154 19.81878  1.000 30.20879 ?  401 A1ALF A C08 1 
HETATM 2328 C C09 . A1ALF B 2 .   ? 122.59448 -30.54696 19.22713  1.000 25.17427 ?  401 A1ALF A C09 1 
HETATM 2329 C C12 . A1ALF B 2 .   ? 124.16268 -28.23075 21.57496  1.000 31.62394 ?  401 A1ALF A C12 1 
HETATM 2330 C C14 . A1ALF B 2 .   ? 126.26537 -28.80210 22.81626  1.000 31.23250 ?  401 A1ALF A C14 1 
HETATM 2331 C C16 . A1ALF B 2 .   ? 128.54180 -28.46586 21.57049  1.000 27.70913 ?  401 A1ALF A C16 1 
HETATM 2332 C C19 . A1ALF B 2 .   ? 125.08049 -25.29946 21.82359  1.000 32.26444 ?  401 A1ALF A C19 1 
HETATM 2333 C C23 . A1ALF B 2 .   ? 125.87133 -21.34626 23.56838  1.000 36.69242 ?  401 A1ALF A C23 1 
HETATM 2334 C C25 . A1ALF B 2 .   ? 127.03972 -19.82425 25.28656  1.000 33.73467 ?  401 A1ALF A C25 1 
HETATM 2335 C C27 . A1ALF B 2 .   ? 126.77243 -17.39855 25.23655  1.000 40.94235 ?  401 A1ALF A C27 1 
HETATM 2336 C C29 . A1ALF B 2 .   ? 127.03676 -14.97854 24.88682  1.000 44.25140 ?  401 A1ALF A C29 1 
HETATM 2337 C C30 . A1ALF B 2 .   ? 125.85586 -14.08943 25.27931  1.000 42.80088 ?  401 A1ALF A C30 1 
HETATM 2338 C C31 . A1ALF B 2 .   ? 125.92846 -17.52316 24.11925  1.000 38.17341 ?  401 A1ALF A C31 1 
HETATM 2339 C C32 . A1ALF B 2 .   ? 125.64269 -18.80848 23.57916  1.000 37.54238 ?  401 A1ALF A C32 1 
HETATM 2340 C C33 . A1ALF B 2 .   ? 126.89805 -22.32810 23.50393  1.000 36.08615 ?  401 A1ALF A C33 1 
HETATM 2341 C C34 . A1ALF B 2 .   ? 126.62876 -23.57073 22.95508  1.000 30.13696 ?  401 A1ALF A C34 1 
HETATM 2342 N N03 . A1ALF B 2 .   ? 119.84708 -25.36818 18.54073  1.000 33.82080 ?  401 A1ALF A N03 1 
HETATM 2343 N N10 . A1ALF B 2 .   ? 121.48025 -31.35047 19.69168  1.000 28.66874 ?  401 A1ALF A N10 1 
HETATM 2344 N N11 . A1ALF B 2 .   ? 123.84510 -28.73368 20.19909  1.000 28.85169 ?  401 A1ALF A N11 1 
HETATM 2345 N N18 . A1ALF B 2 .   ? 125.76501 -26.46571 22.42370  1.000 31.23634 ?  401 A1ALF A N18 1 
HETATM 2346 O O01 . A1ALF B 2 .   ? 121.71341 -26.23747 17.09026  1.000 28.28760 ?  401 A1ALF A O01 1 
HETATM 2347 O O28 . A1ALF B 2 .   ? 127.07884 -16.11143 25.80353  1.000 51.19800 ?  401 A1ALF A O28 1 
HETATM 2348 O O35 . A1ALF B 2 .   ? 124.41325 -25.44251 20.85971  1.000 29.66160 ?  401 A1ALF A O35 1 
HETATM 2349 O O36 . A1ALF B 2 .   ? 123.31298 -28.14099 22.43232  1.000 33.67241 ?  401 A1ALF A O36 1 
HETATM 2350 O O   . HOH   C 3 .   ? 138.01090 -41.19477 32.99691  1.000 49.82529 ?  501 HOH   A O   1 
HETATM 2351 O O   . HOH   C 3 .   ? 121.08248 -21.33371 1.33456   1.000 31.03958 ?  502 HOH   A O   1 
HETATM 2352 O O   . HOH   C 3 .   ? 124.89745 -52.74620 3.27437   1.000 38.31087 ?  503 HOH   A O   1 
HETATM 2353 O O   . HOH   C 3 .   ? 134.65123 -17.46288 -2.97398  1.000 37.52603 ?  504 HOH   A O   1 
HETATM 2354 O O   . HOH   C 3 .   ? 107.82149 -20.89645 -4.77601  1.000 31.74317 ?  505 HOH   A O   1 
HETATM 2355 O O   . HOH   C 3 .   ? 139.84361 -31.46926 15.02946  1.000 32.49018 ?  506 HOH   A O   1 
HETATM 2356 O O   . HOH   C 3 .   ? 130.65381 -55.31601 11.94579  1.000 40.47630 ?  507 HOH   A O   1 
HETATM 2357 O O   . HOH   C 3 .   ? 128.31834 -52.10044 3.76944   1.000 40.52749 ?  508 HOH   A O   1 
HETATM 2358 O O   . HOH   C 3 .   ? 112.97783 -22.99695 -2.01818  1.000 35.37455 ?  509 HOH   A O   1 
HETATM 2359 O O   . HOH   C 3 .   ? 121.90297 -50.60967 20.87520  1.000 38.52895 ?  510 HOH   A O   1 
HETATM 2360 O O   . HOH   C 3 .   ? 139.21608 -33.39420 8.24914   1.000 30.35297 ?  511 HOH   A O   1 
HETATM 2361 O O   . HOH   C 3 .   ? 132.07620 -48.79421 31.98412  1.000 50.80460 ?  512 HOH   A O   1 
HETATM 2362 O O   . HOH   C 3 .   ? 140.20160 -34.69689 22.01481  1.000 37.42721 ?  513 HOH   A O   1 
HETATM 2363 O O   . HOH   C 3 .   ? 116.04094 -44.77885 13.43604  1.000 40.93487 ?  514 HOH   A O   1 
HETATM 2364 O O   . HOH   C 3 .   ? 125.08913 -2.28122  -0.95352  1.000 48.08845 ?  515 HOH   A O   1 
HETATM 2365 O O   . HOH   C 3 .   ? 114.96250 -28.54417 12.21874  1.000 34.04278 ?  516 HOH   A O   1 
HETATM 2366 O O   . HOH   C 3 .   ? 120.81192 -35.89757 8.66235   1.000 26.26423 ?  517 HOH   A O   1 
HETATM 2367 O O   . HOH   C 3 .   ? 129.19828 -38.17987 31.00228  1.000 38.64410 ?  518 HOH   A O   1 
HETATM 2368 O O   . HOH   C 3 .   ? 119.97716 -45.38254 1.86976   1.000 29.93571 ?  519 HOH   A O   1 
HETATM 2369 O O   . HOH   C 3 .   ? 131.24127 -40.23408 31.47193  1.000 37.27188 ?  520 HOH   A O   1 
HETATM 2370 O O   . HOH   C 3 .   ? 130.14725 -21.09415 -15.10575 1.000 32.84984 ?  521 HOH   A O   1 
HETATM 2371 O O   . HOH   C 3 .   ? 125.07532 -28.21986 -3.35656  1.000 26.58010 ?  522 HOH   A O   1 
HETATM 2372 O O   . HOH   C 3 .   ? 143.69472 -12.41164 -14.49236 1.000 38.48714 ?  523 HOH   A O   1 
HETATM 2373 O O   . HOH   C 3 .   ? 126.18353 -17.33420 -26.26734 1.000 44.78263 ?  524 HOH   A O   1 
HETATM 2374 O O   . HOH   C 3 .   ? 136.93178 -18.06020 4.34272   1.000 29.54909 ?  525 HOH   A O   1 
HETATM 2375 O O   . HOH   C 3 .   ? 124.10154 -16.98337 -5.16728  1.000 22.01829 ?  526 HOH   A O   1 
HETATM 2376 O O   . HOH   C 3 .   ? 139.19627 -14.13182 -2.75878  1.000 39.27163 ?  527 HOH   A O   1 
HETATM 2377 O O   . HOH   C 3 .   ? 124.83528 -7.50669  -0.78592  1.000 31.47958 ?  528 HOH   A O   1 
HETATM 2378 O O   . HOH   C 3 .   ? 125.42375 -26.60157 25.38952  1.000 31.31655 ?  529 HOH   A O   1 
HETATM 2379 O O   . HOH   C 3 .   ? 135.37411 -40.58200 10.44933  1.000 26.34810 ?  530 HOH   A O   1 
HETATM 2380 O O   . HOH   C 3 .   ? 135.54506 -17.26096 20.36592  1.000 35.27510 ?  531 HOH   A O   1 
HETATM 2381 O O   . HOH   C 3 .   ? 122.51534 -23.95090 -3.65668  1.000 27.65202 ?  532 HOH   A O   1 
HETATM 2382 O O   . HOH   C 3 .   ? 138.05761 -25.50576 15.63597  1.000 27.23249 ?  533 HOH   A O   1 
HETATM 2383 O O   . HOH   C 3 .   ? 131.52524 -46.51114 7.73775   1.000 29.39101 ?  534 HOH   A O   1 
HETATM 2384 O O   . HOH   C 3 .   ? 136.47960 -29.11867 20.25693  1.000 20.70640 ?  535 HOH   A O   1 
HETATM 2385 O O   . HOH   C 3 .   ? 136.15424 -18.34033 18.11433  1.000 28.91737 ?  536 HOH   A O   1 
HETATM 2386 O O   . HOH   C 3 .   ? 140.37748 -39.09847 19.89000  1.000 32.78242 ?  537 HOH   A O   1 
HETATM 2387 O O   . HOH   C 3 .   ? 128.98901 -27.26118 -3.53049  1.000 31.50573 ?  538 HOH   A O   1 
HETATM 2388 O O   . HOH   C 3 .   ? 122.80665 -51.72923 26.31625  1.000 42.28815 ?  539 HOH   A O   1 
HETATM 2389 O O   . HOH   C 3 .   ? 131.43554 -20.93348 -4.66940  1.000 23.87575 ?  540 HOH   A O   1 
HETATM 2390 O O   . HOH   C 3 .   ? 135.90904 -21.02753 19.42518  1.000 29.61335 ?  541 HOH   A O   1 
HETATM 2391 O O   . HOH   C 3 .   ? 129.31100 -8.73595  -22.26430 1.000 39.98997 ?  542 HOH   A O   1 
HETATM 2392 O O   . HOH   C 3 .   ? 124.50821 -20.89058 5.36654   1.000 23.30284 ?  543 HOH   A O   1 
HETATM 2393 O O   . HOH   C 3 .   ? 137.50497 -28.05180 17.81552  1.000 23.83932 ?  544 HOH   A O   1 
HETATM 2394 O O   . HOH   C 3 .   ? 127.23269 -34.17664 35.53031  1.000 41.84606 ?  545 HOH   A O   1 
HETATM 2395 O O   . HOH   C 3 .   ? 133.53592 -35.17960 5.83612   1.000 23.09516 ?  546 HOH   A O   1 
HETATM 2396 O O   . HOH   C 3 .   ? 131.33266 -24.87164 11.79816  1.000 18.71499 ?  547 HOH   A O   1 
HETATM 2397 O O   . HOH   C 3 .   ? 135.26252 -18.10929 11.80477  1.000 24.05433 ?  548 HOH   A O   1 
HETATM 2398 O O   . HOH   C 3 .   ? 127.83032 -26.94897 -5.86111  1.000 33.98518 ?  549 HOH   A O   1 
HETATM 2399 O O   . HOH   C 3 .   ? 136.03415 -45.89658 26.83090  1.000 26.38019 ?  550 HOH   A O   1 
HETATM 2400 O O   . HOH   C 3 .   ? 123.98713 -14.17462 2.45518   1.000 37.99646 ?  551 HOH   A O   1 
HETATM 2401 O O   . HOH   C 3 .   ? 127.97841 -16.14109 10.66463  1.000 28.69805 ?  552 HOH   A O   1 
HETATM 2402 O O   . HOH   C 3 .   ? 116.44160 -25.39061 0.49837   1.000 31.37807 ?  553 HOH   A O   1 
HETATM 2403 O O   . HOH   C 3 .   ? 122.06614 -7.64934  -0.74831  1.000 31.25542 ?  554 HOH   A O   1 
HETATM 2404 O O   . HOH   C 3 .   ? 138.10636 -24.57479 9.19889   1.000 28.98146 ?  555 HOH   A O   1 
HETATM 2405 O O   . HOH   C 3 .   ? 118.27164 -39.65102 -2.50766  1.000 31.63789 ?  556 HOH   A O   1 
HETATM 2406 O O   . HOH   C 3 .   ? 134.69254 -33.36754 32.20430  1.000 29.24431 ?  557 HOH   A O   1 
HETATM 2407 O O   . HOH   C 3 .   ? 138.71192 -43.32995 21.62783  1.000 28.32752 ?  558 HOH   A O   1 
HETATM 2408 O O   . HOH   C 3 .   ? 138.14249 -34.82292 34.71723  1.000 38.31155 ?  559 HOH   A O   1 
HETATM 2409 O O   . HOH   C 3 .   ? 129.19426 -15.62040 17.77753  1.000 38.72174 ?  560 HOH   A O   1 
HETATM 2410 O O   . HOH   C 3 .   ? 139.37352 -36.32001 20.19077  1.000 26.19148 ?  561 HOH   A O   1 
HETATM 2411 O O   . HOH   C 3 .   ? 135.46047 -48.59263 27.87241  1.000 40.19719 ?  562 HOH   A O   1 
HETATM 2412 O O   . HOH   C 3 .   ? 138.96629 -25.97800 6.74735   1.000 31.97898 ?  563 HOH   A O   1 
HETATM 2413 O O   . HOH   C 3 .   ? 138.61239 -41.57289 26.13788  1.000 30.42498 ?  564 HOH   A O   1 
HETATM 2414 O O   . HOH   C 3 .   ? 130.56970 -23.98192 -8.42870  1.000 32.05172 ?  565 HOH   A O   1 
HETATM 2415 O O   . HOH   C 3 .   ? 116.58395 -15.89553 -5.76028  1.000 31.49984 ?  566 HOH   A O   1 
HETATM 2416 O O   . HOH   C 3 .   ? 133.45777 -56.18749 21.44743  1.000 44.85126 ?  567 HOH   A O   1 
HETATM 2417 O O   . HOH   C 3 .   ? 126.04766 -44.69871 30.52861  1.000 48.18701 ?  568 HOH   A O   1 
HETATM 2418 O O   . HOH   C 3 .   ? 129.72193 -32.71294 -0.04713  1.000 25.53236 ?  569 HOH   A O   1 
HETATM 2419 O O   . HOH   C 3 .   ? 132.28534 0.55093   -13.30726 1.000 44.09300 ?  570 HOH   A O   1 
HETATM 2420 O O   . HOH   C 3 .   ? 124.14638 -45.38303 -4.03345  1.000 34.38535 ?  571 HOH   A O   1 
HETATM 2421 O O   . HOH   C 3 .   ? 113.17758 -30.69159 19.04936  1.000 43.84343 ?  572 HOH   A O   1 
HETATM 2422 O O   . HOH   C 3 .   ? 131.77484 -22.54441 30.25691  1.000 35.13853 ?  573 HOH   A O   1 
HETATM 2423 O O   . HOH   C 3 .   ? 141.35098 -38.08550 17.34362  1.000 29.50380 ?  574 HOH   A O   1 
HETATM 2424 O O   . HOH   C 3 .   ? 120.50384 -25.27497 -7.85143  1.000 29.28814 ?  575 HOH   A O   1 
HETATM 2425 O O   . HOH   C 3 .   ? 137.83493 -29.77710 15.74262  1.000 21.42440 ?  576 HOH   A O   1 
HETATM 2426 O O   . HOH   C 3 .   ? 138.01434 -33.84456 1.37353   1.000 33.89662 ?  577 HOH   A O   1 
HETATM 2427 O O   . HOH   C 3 .   ? 120.01143 -24.82506 -5.06517  1.000 27.46775 ?  578 HOH   A O   1 
HETATM 2428 O O   . HOH   C 3 .   ? 135.20518 -18.37095 25.60074  1.000 41.00455 ?  579 HOH   A O   1 
HETATM 2429 O O   . HOH   C 3 .   ? 137.68930 -26.02188 4.44681   1.000 32.38592 ?  580 HOH   A O   1 
HETATM 2430 O O   . HOH   C 3 .   ? 135.93047 -40.97914 1.91333   1.000 31.84871 ?  581 HOH   A O   1 
HETATM 2431 O O   . HOH   C 3 .   ? 139.37485 -13.61048 -18.20226 1.000 43.14355 ?  582 HOH   A O   1 
HETATM 2432 O O   . HOH   C 3 .   ? 133.48268 -51.43285 26.06159  1.000 33.58169 ?  583 HOH   A O   1 
HETATM 2433 O O   . HOH   C 3 .   ? 134.94353 -14.05966 6.40532   1.000 34.93098 ?  584 HOH   A O   1 
HETATM 2434 O O   . HOH   C 3 .   ? 122.25967 -25.95311 24.30000  1.000 37.04525 ?  585 HOH   A O   1 
HETATM 2435 O O   . HOH   C 3 .   ? 139.52445 -11.02047 -15.38145 1.000 38.74138 ?  586 HOH   A O   1 
HETATM 2436 O O   . HOH   C 3 .   ? 111.91229 -17.70467 -10.10826 1.000 42.01930 ?  587 HOH   A O   1 
HETATM 2437 O O   . HOH   C 3 .   ? 138.27245 -32.46742 25.92196  1.000 27.78556 ?  588 HOH   A O   1 
HETATM 2438 O O   . HOH   C 3 .   ? 136.35899 -50.43270 21.38751  1.000 35.26301 ?  589 HOH   A O   1 
HETATM 2439 O O   . HOH   C 3 .   ? 138.89698 -31.26598 23.52943  1.000 37.77373 ?  590 HOH   A O   1 
HETATM 2440 O O   . HOH   C 3 .   ? 131.33758 -55.62501 23.60606  1.000 41.71329 ?  591 HOH   A O   1 
HETATM 2441 O O   . HOH   C 3 .   ? 132.50763 -22.28475 -6.75347  1.000 34.18386 ?  592 HOH   A O   1 
HETATM 2442 O O   . HOH   C 3 .   ? 135.83172 -28.99623 23.85891  1.000 28.25012 ?  593 HOH   A O   1 
HETATM 2443 O O   . HOH   C 3 .   ? 131.71815 -52.83391 6.75847   1.000 43.61436 ?  594 HOH   A O   1 
HETATM 2444 O O   . HOH   C 3 .   ? 137.02639 -49.28499 25.63636  1.000 34.96921 ?  595 HOH   A O   1 
HETATM 2445 O O   . HOH   C 3 .   ? 137.32668 -44.98261 23.44227  1.000 28.21681 ?  596 HOH   A O   1 
HETATM 2446 O O   . HOH   C 3 .   ? 131.03450 -32.31680 -2.37949  1.000 32.03703 ?  597 HOH   A O   1 
HETATM 2447 O O   . HOH   C 3 .   ? 114.50800 -26.62307 0.00000   0.50  32.24877 ?  598 HOH   A O   1 
HETATM 2448 O O   . HOH   C 3 .   ? 137.01362 -14.98303 5.54305   1.000 43.31372 ?  599 HOH   A O   1 
HETATM 2449 O O   . HOH   C 3 .   ? 133.46609 -48.73808 7.49909   1.000 41.74266 ?  600 HOH   A O   1 
HETATM 2450 O O   . HOH   C 3 .   ? 137.86901 -28.84713 22.52525  1.000 31.64373 ?  601 HOH   A O   1 
HETATM 2451 O O   . HOH   C 3 .   ? 133.86781 -19.69202 -3.52143  1.000 34.78527 ?  602 HOH   A O   1 
HETATM 2452 O O   . HOH   C 3 .   ? 141.92076 -13.58448 -19.15441 1.000 42.69211 ?  603 HOH   A O   1 
HETATM 2453 O O   . HOH   C 3 .   ? 138.06943 -44.40055 26.10255  1.000 26.88938 ?  604 HOH   A O   1 
HETATM 2454 O O   . HOH   C 3 .   ? 145.26393 -14.57383 -15.55139 1.000 41.21249 ?  605 HOH   A O   1 
HETATM 2455 O O   . HOH   C 3 .   ? 136.58438 -42.10294 8.50009   1.000 36.26315 ?  606 HOH   A O   1 
HETATM 2456 O O   . HOH   C 3 .   ? 141.49750 -39.82068 22.54118  1.000 35.13621 ?  607 HOH   A O   1 
HETATM 2457 O O   . HOH   C 3 .   ? 137.46645 -18.56989 10.12499  1.000 28.92048 ?  608 HOH   A O   1 
HETATM 2458 O O   . HOH   C 3 .   ? 140.91741 -9.20398  -15.63826 1.000 45.14482 ?  609 HOH   A O   1 
HETATM 2459 O O   . HOH   C 3 .   ? 140.04323 -27.30488 18.25278  1.000 31.08743 ?  610 HOH   A O   1 
HETATM 2460 O O   . HOH   C 3 .   ? 144.46502 -11.81000 -12.10527 1.000 37.27177 ?  611 HOH   A O   1 
HETATM 2461 O O   . HOH   C 3 .   ? 125.35812 -4.87061  0.15799   1.000 39.34543 ?  612 HOH   A O   1 
HETATM 2462 O O   . HOH   C 3 .   ? 139.90076 -41.68230 23.47488  1.000 35.44337 ?  613 HOH   A O   1 
HETATM 2463 O O   . HOH   C 3 .   ? 141.11285 -45.36581 21.49812  1.000 40.76960 ?  614 HOH   A O   1 
HETATM 2464 O O   . HOH   C 3 .   ? 139.37864 -27.18134 23.48321  1.000 40.83953 ?  615 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   ? 0.63403 0.73551 0.60794 -0.02213 -0.11385 0.12929  1   SER   A N   
2    C CA  . SER   A 1   ? 0.47449 0.58360 0.45788 -0.02561 -0.12160 0.12149  1   SER   A CA  
3    C C   . SER   A 1   ? 0.47106 0.58364 0.48039 -0.02403 -0.11254 0.11335  1   SER   A C   
4    O O   . SER   A 1   ? 0.39119 0.50714 0.40420 -0.02850 -0.11369 0.10464  1   SER   A O   
5    C CB  . SER   A 1   ? 0.49338 0.59649 0.44618 -0.03163 -0.12461 0.11272  1   SER   A CB  
6    O OG  . SER   A 1   ? 0.53406 0.64206 0.49734 -0.03656 -0.13126 0.10475  1   SER   A OG  
7    N N   . GLY   A 2   ? 0.47177 0.58254 0.49795 -0.01802 -0.10403 0.11656  2   GLY   A N   
8    C CA  . GLY   A 2   ? 0.38028 0.49447 0.42954 -0.01534 -0.09538 0.10952  2   GLY   A CA  
9    C C   . GLY   A 2   ? 0.39525 0.49892 0.43442 -0.01591 -0.08146 0.10190  2   GLY   A C   
10   O O   . GLY   A 2   ? 0.40593 0.50277 0.42109 -0.01994 -0.07864 0.09764  2   GLY   A O   
11   N N   . PHE   A 3   ? 0.38136 0.48376 0.43840 -0.01118 -0.07301 0.09974  3   PHE   A N   
12   C CA  . PHE   A 3   ? 0.35534 0.44909 0.40584 -0.01168 -0.06072 0.09278  3   PHE   A CA  
13   C C   . PHE   A 3   ? 0.35155 0.44952 0.42266 -0.00882 -0.05458 0.08584  3   PHE   A C   
14   O O   . PHE   A 3   ? 0.37257 0.47377 0.46311 -0.00264 -0.05506 0.08846  3   PHE   A O   
15   C CB  . PHE   A 3   ? 0.35964 0.44384 0.40432 -0.00954 -0.05630 0.09940  3   PHE   A CB  
16   C CG  . PHE   A 3   ? 0.37876 0.45630 0.40974 -0.01198 -0.04584 0.09415  3   PHE   A CG  
17   C CD1 . PHE   A 3   ? 0.40343 0.47974 0.41026 -0.01560 -0.04461 0.09307  3   PHE   A CD1 
18   C CD2 . PHE   A 3   ? 0.34175 0.41475 0.38372 -0.00991 -0.03755 0.08995  3   PHE   A CD2 
19   C CE1 . PHE   A 3   ? 0.37813 0.45053 0.37434 -0.01640 -0.03463 0.08835  3   PHE   A CE1 
20   C CE2 . PHE   A 3   ? 0.35625 0.42507 0.38776 -0.01198 -0.02872 0.08579  3   PHE   A CE2 
21   C CZ  . PHE   A 3   ? 0.37747 0.44687 0.38725 -0.01488 -0.02694 0.08523  3   PHE   A CZ  
22   N N   . ARG   A 4   ? 0.33503 0.43231 0.40069 -0.01268 -0.04892 0.07702  4   ARG   A N   
23   C CA  . ARG   A 4   ? 0.28889 0.39130 0.37060 -0.01124 -0.04289 0.07070  4   ARG   A CA  
24   C C   . ARG   A 4   ? 0.26125 0.35418 0.33320 -0.01253 -0.03290 0.06367  4   ARG   A C   
25   O O   . ARG   A 4   ? 0.26981 0.35524 0.32270 -0.01598 -0.03149 0.06160  4   ARG   A O   
26   C CB  . ARG   A 4   ? 0.28716 0.40125 0.37585 -0.01618 -0.04810 0.06849  4   ARG   A CB  
27   C CG  . ARG   A 4   ? 0.31096 0.43624 0.40847 -0.01628 -0.05966 0.07561  4   ARG   A CG  
28   C CD  . ARG   A 4   ? 0.36641 0.50362 0.49021 -0.00823 -0.05879 0.07902  4   ARG   A CD  
29   N NE  . ARG   A 4   ? 0.31211 0.45089 0.44573 -0.00535 -0.04779 0.07252  4   ARG   A NE  
30   C CZ  . ARG   A 4   ? 0.37113 0.52576 0.52183 -0.00587 -0.04564 0.07072  4   ARG   A CZ  
31   N NH1 . ARG   A 4   ? 0.32945 0.50113 0.49322 -0.00902 -0.05400 0.07537  4   ARG   A NH1 
32   N NH2 . ARG   A 4   ? 0.34119 0.49579 0.49592 -0.00372 -0.03508 0.06480  4   ARG   A NH2 
33   N N   . LYS   A 5   ? 0.24123 0.33520 0.32605 -0.00895 -0.02613 0.05978  5   LYS   A N   
34   C CA  . LYS   A 5   ? 0.28280 0.36988 0.36044 -0.01052 -0.01782 0.05300  5   LYS   A CA  
35   C C   . LYS   A 5   ? 0.27365 0.36381 0.34622 -0.01651 -0.01879 0.04856  5   LYS   A C   
36   O O   . LYS   A 5   ? 0.31142 0.41217 0.39697 -0.01779 -0.02026 0.04829  5   LYS   A O   
37   C CB  . LYS   A 5   ? 0.31456 0.40186 0.40541 -0.00525 -0.01158 0.04979  5   LYS   A CB  
38   C CG  . LYS   A 5   ? 0.33052 0.40803 0.41299 -0.00580 -0.00444 0.04502  5   LYS   A CG  
39   C CD  . LYS   A 5   ? 0.38225 0.45692 0.47494 -0.00012 -0.00025 0.04212  5   LYS   A CD  
40   C CE  . LYS   A 5   ? 0.42266 0.48779 0.51646 0.00285  -0.00243 0.04640  5   LYS   A CE  
41   N NZ  . LYS   A 5   ? 0.46243 0.52248 0.54316 -0.00202 -0.00308 0.05084  5   LYS   A NZ  
42   N N   . MET   A 6   ? 0.24302 0.32427 0.29716 -0.02014 -0.01846 0.04561  6   MET   A N   
43   C CA  . MET   A 6   ? 0.25339 0.33341 0.30010 -0.02621 -0.02231 0.04181  6   MET   A CA  
44   C C   . MET   A 6   ? 0.27198 0.34199 0.30856 -0.02704 -0.01594 0.03545  6   MET   A C   
45   O O   . MET   A 6   ? 0.28774 0.35051 0.31390 -0.02391 -0.01108 0.03408  6   MET   A O   
46   C CB  . MET   A 6   ? 0.29101 0.36817 0.32282 -0.02900 -0.03105 0.04361  6   MET   A CB  
47   C CG  . MET   A 6   ? 0.30638 0.37434 0.32147 -0.03428 -0.03536 0.03784  6   MET   A CG  
48   S SD  . MET   A 6   ? 0.46567 0.53146 0.46269 -0.03643 -0.04698 0.04014  6   MET   A SD  
49   C CE  . MET   A 6   ? 0.38628 0.46692 0.40231 -0.03332 -0.05052 0.05057  6   MET   A CE  
50   N N   . ALA   A 7   ? 0.20701 0.27790 0.24813 -0.03135 -0.01612 0.03267  7   ALA   A N   
51   C CA  . ALA   A 7   ? 0.23746 0.29831 0.27006 -0.03241 -0.01156 0.02742  7   ALA   A CA  
52   C C   . ALA   A 7   ? 0.26435 0.31346 0.27996 -0.03679 -0.01791 0.02352  7   ALA   A C   
53   O O   . ALA   A 7   ? 0.26557 0.31591 0.27862 -0.04114 -0.02665 0.02475  7   ALA   A O   
54   C CB  . ALA   A 7   ? 0.22091 0.28847 0.26717 -0.03482 -0.00817 0.02771  7   ALA   A CB  
55   N N   . PHE   A 8   ? 0.23498 0.27181 0.23870 -0.03520 -0.01430 0.01841  8   PHE   A N   
56   C CA  . PHE   A 8   ? 0.30128 0.32359 0.28818 -0.03821 -0.02059 0.01325  8   PHE   A CA  
57   C C   . PHE   A 8   ? 0.28208 0.30356 0.27652 -0.04731 -0.02730 0.01432  8   PHE   A C   
58   O O   . PHE   A 8   ? 0.26669 0.29748 0.27702 -0.04982 -0.02353 0.01802  8   PHE   A O   
59   C CB  . PHE   A 8   ? 0.29272 0.30237 0.26726 -0.03294 -0.01508 0.00767  8   PHE   A CB  
60   C CG  . PHE   A 8   ? 0.32069 0.33171 0.28611 -0.02503 -0.00927 0.00685  8   PHE   A CG  
61   C CD1 . PHE   A 8   ? 0.41473 0.41971 0.36150 -0.02237 -0.01247 0.00360  8   PHE   A CD1 
62   C CD2 . PHE   A 8   ? 0.33255 0.35127 0.30743 -0.02063 -0.00076 0.00957  8   PHE   A CD2 
63   C CE1 . PHE   A 8   ? 0.40912 0.41842 0.34809 -0.01545 -0.00592 0.00429  8   PHE   A CE1 
64   C CE2 . PHE   A 8   ? 0.36879 0.39076 0.33740 -0.01481 0.00450  0.01046  8   PHE   A CE2 
65   C CZ  . PHE   A 8   ? 0.39198 0.41050 0.34315 -0.01220 0.00260  0.00839  8   PHE   A CZ  
66   N N   . PRO   A 9   ? 0.27825 0.28881 0.26106 -0.05277 -0.03752 0.01141  9   PRO   A N   
67   C CA  . PRO   A 9   ? 0.30842 0.31562 0.29789 -0.06306 -0.04471 0.01300  9   PRO   A CA  
68   C C   . PRO   A 9   ? 0.29947 0.29712 0.28847 -0.06268 -0.03906 0.01151  9   PRO   A C   
69   O O   . PRO   A 9   ? 0.33437 0.31764 0.30872 -0.05587 -0.03555 0.00565  9   PRO   A O   
70   C CB  . PRO   A 9   ? 0.32700 0.31725 0.29772 -0.06731 -0.05724 0.00767  9   PRO   A CB  
71   C CG  . PRO   A 9   ? 0.38173 0.37477 0.34026 -0.05995 -0.05679 0.00569  9   PRO   A CG  
72   C CD  . PRO   A 9   ? 0.32683 0.32606 0.28790 -0.04992 -0.04312 0.00619  9   PRO   A CD  
73   N N   . SER   A 10  ? 0.29101 0.29834 0.29647 -0.06961 -0.03799 0.01752  10  SER   A N   
74   C CA  . SER   A 10  ? 0.32224 0.32514 0.32936 -0.06879 -0.03126 0.01825  10  SER   A CA  
75   C C   . SER   A 10  ? 0.31329 0.29741 0.31312 -0.07713 -0.03897 0.01796  10  SER   A C   
76   O O   . SER   A 10  ? 0.33281 0.31221 0.33353 -0.07763 -0.03481 0.01991  10  SER   A O   
77   C CB  . SER   A 10  ? 0.26056 0.28625 0.28810 -0.06988 -0.02353 0.02527  10  SER   A CB  
78   O OG  . SER   A 10  ? 0.29176 0.33010 0.33362 -0.08027 -0.02895 0.03194  10  SER   A OG  
79   N N   . GLY   A 11  ? 0.33365 0.30534 0.32529 -0.08388 -0.05110 0.01567  11  GLY   A N   
80   C CA  . GLY   A 11  ? 0.35021 0.30306 0.33719 -0.09399 -0.06051 0.01662  11  GLY   A CA  
81   C C   . GLY   A 11  ? 0.36664 0.29585 0.33863 -0.08798 -0.05849 0.01149  11  GLY   A C   
82   O O   . GLY   A 11  ? 0.40017 0.32185 0.37563 -0.09452 -0.05990 0.01642  11  GLY   A O   
83   N N   . LYS   A 12  ? 0.35526 0.27322 0.31075 -0.07543 -0.05541 0.00231  12  LYS   A N   
84   C CA  . LYS   A 12  ? 0.36189 0.25833 0.30411 -0.06801 -0.05395 -0.00296 12  LYS   A CA  
85   C C   . LYS   A 12  ? 0.37426 0.28120 0.32771 -0.06564 -0.04394 0.00301  12  LYS   A C   
86   O O   . LYS   A 12  ? 0.40497 0.29535 0.35317 -0.06520 -0.04559 0.00325  12  LYS   A O   
87   C CB  . LYS   A 12  ? 0.40105 0.28959 0.32596 -0.05391 -0.05069 -0.01317 12  LYS   A CB  
88   C CG  . LYS   A 12  ? 0.48273 0.35867 0.39114 -0.05468 -0.06067 -0.02054 12  LYS   A CG  
89   C CD  . LYS   A 12  ? 0.52605 0.40717 0.42179 -0.04142 -0.05382 -0.02731 12  LYS   A CD  
90   C CE  . LYS   A 12  ? 0.66148 0.52672 0.53539 -0.04065 -0.06383 -0.03603 12  LYS   A CE  
91   N NZ  . LYS   A 12  ? 0.70238 0.53821 0.55447 -0.03246 -0.06794 -0.04697 12  LYS   A NZ  
92   N N   . VAL   A 13  ? 0.32836 0.26108 0.29611 -0.06385 -0.03448 0.00767  13  VAL   A N   
93   C CA  . VAL   A 13  ? 0.30774 0.25031 0.28400 -0.06140 -0.02558 0.01238  13  VAL   A CA  
94   C C   . VAL   A 13  ? 0.33339 0.28235 0.32082 -0.07330 -0.02718 0.02173  13  VAL   A C   
95   O O   . VAL   A 13  ? 0.28640 0.23184 0.27372 -0.07374 -0.02427 0.02557  13  VAL   A O   
96   C CB  . VAL   A 13  ? 0.27726 0.24177 0.26254 -0.05426 -0.01564 0.01261  13  VAL   A CB  
97   C CG1 . VAL   A 13  ? 0.30460 0.27799 0.29686 -0.05221 -0.00770 0.01664  13  VAL   A CG1 
98   C CG2 . VAL   A 13  ? 0.31850 0.27863 0.29362 -0.04355 -0.01335 0.00543  13  VAL   A CG2 
99   N N   . GLU   A 14  ? 0.29388 0.25376 0.29137 -0.08323 -0.03185 0.02639  14  GLU   A N   
100  C CA  . GLU   A 14  ? 0.28980 0.25935 0.29972 -0.09552 -0.03290 0.03673  14  GLU   A CA  
101  C C   . GLU   A 14  ? 0.33960 0.28499 0.34018 -0.10176 -0.03968 0.03932  14  GLU   A C   
102  O O   . GLU   A 14  ? 0.34619 0.29696 0.35212 -0.10703 -0.03611 0.04772  14  GLU   A O   
103  C CB  . GLU   A 14  ? 0.32043 0.30284 0.34244 -0.10590 -0.03976 0.04103  14  GLU   A CB  
104  C CG  . GLU   A 14  ? 0.30660 0.31469 0.34071 -0.10007 -0.03346 0.04057  14  GLU   A CG  
105  C CD  . GLU   A 14  ? 0.29018 0.31071 0.33617 -0.10911 -0.04186 0.04443  14  GLU   A CD  
106  O OE1 . GLU   A 14  ? 0.33156 0.35510 0.38663 -0.12233 -0.04835 0.05203  14  GLU   A OE1 
107  O OE2 . GLU   A 14  ? 0.34445 0.37181 0.39081 -0.10328 -0.04264 0.04048  14  GLU   A OE2 
108  N N   . GLY   A 15  ? 0.36141 0.27904 0.34667 -0.10056 -0.04958 0.03213  15  GLY   A N   
109  C CA  . GLY   A 15  ? 0.38472 0.27474 0.36021 -0.10578 -0.05798 0.03390  15  GLY   A CA  
110  C C   . GLY   A 15  ? 0.36015 0.24077 0.32841 -0.09666 -0.05210 0.03351  15  GLY   A C   
111  O O   . GLY   A 15  ? 0.39497 0.25149 0.35520 -0.10010 -0.05936 0.03577  15  GLY   A O   
112  N N   . CYS   A 16  ? 0.32922 0.22715 0.30038 -0.08558 -0.04046 0.03108  16  CYS   A N   
113  C CA  . CYS   A 16  ? 0.34539 0.23722 0.31078 -0.07633 -0.03535 0.03046  16  CYS   A CA  
114  C C   . CYS   A 16  ? 0.34626 0.26032 0.32157 -0.07847 -0.02607 0.03884  16  CYS   A C   
115  O O   . CYS   A 16  ? 0.34764 0.25958 0.31879 -0.07138 -0.02205 0.03894  16  CYS   A O   
116  C CB  . CYS   A 16  ? 0.33702 0.22909 0.29611 -0.06099 -0.03038 0.02004  16  CYS   A CB  
117  S SG  . CYS   A 16  ? 0.40394 0.27229 0.34749 -0.05463 -0.03874 0.00823  16  CYS   A SG  
118  N N   . MET   A 17  ? 0.32831 0.26455 0.31628 -0.08702 -0.02257 0.04530  17  MET   A N   
119  C CA  . MET   A 17  ? 0.32444 0.28359 0.32035 -0.08740 -0.01267 0.05166  17  MET   A CA  
120  C C   . MET   A 17  ? 0.34957 0.30456 0.34474 -0.09812 -0.01493 0.06315  17  MET   A C   
121  O O   . MET   A 17  ? 0.35370 0.30461 0.35322 -0.11059 -0.02179 0.06983  17  MET   A O   
122  C CB  . MET   A 17  ? 0.32725 0.31333 0.33762 -0.08973 -0.00729 0.05288  17  MET   A CB  
123  C CG  . MET   A 17  ? 0.32023 0.31528 0.33240 -0.07834 -0.00244 0.04383  17  MET   A CG  
124  S SD  . MET   A 17  ? 0.30885 0.29322 0.31002 -0.06400 0.00116  0.03518  17  MET   A SD  
125  C CE  . MET   A 17  ? 0.32071 0.31653 0.32240 -0.06296 0.00904  0.04043  17  MET   A CE  
126  N N   . VAL   A 18  ? 0.32543 0.28077 0.31465 -0.09395 -0.01012 0.06608  18  VAL   A N   
127  C CA  . VAL   A 18  ? 0.34807 0.30174 0.33498 -0.10350 -0.01095 0.07836  18  VAL   A CA  
128  C C   . VAL   A 18  ? 0.30745 0.28513 0.29566 -0.10020 0.00055  0.08186  18  VAL   A C   
129  O O   . VAL   A 18  ? 0.30905 0.29904 0.29856 -0.08985 0.00743  0.07379  18  VAL   A O   
130  C CB  . VAL   A 18  ? 0.40193 0.32498 0.37543 -0.10204 -0.01960 0.07961  18  VAL   A CB  
131  C CG1 . VAL   A 18  ? 0.41630 0.31280 0.38628 -0.10489 -0.03160 0.07527  18  VAL   A CG1 
132  C CG2 . VAL   A 18  ? 0.36003 0.27940 0.32575 -0.08735 -0.01616 0.07191  18  VAL   A CG2 
133  N N   . GLN   A 19  ? 0.36153 0.34481 0.34827 -0.10947 0.00214  0.09428  19  GLN   A N   
134  C CA  . GLN   A 19  ? 0.36686 0.37137 0.35097 -0.10688 0.01269  0.09832  19  GLN   A CA  
135  C C   . GLN   A 19  ? 0.35352 0.34146 0.32196 -0.10377 0.00977  0.10149  19  GLN   A C   
136  O O   . GLN   A 19  ? 0.39054 0.35762 0.35332 -0.11080 0.00108  0.10919  19  GLN   A O   
137  C CB  . GLN   A 19  ? 0.39118 0.41892 0.38455 -0.11918 0.01818  0.11120  19  GLN   A CB  
138  C CG  . GLN   A 19  ? 0.40966 0.45793 0.39667 -0.11704 0.02910  0.11656  19  GLN   A CG  
139  C CD  . GLN   A 19  ? 0.47118 0.53876 0.46586 -0.12764 0.03336  0.12926  19  GLN   A CD  
140  O OE1 . GLN   A 19  ? 0.51634 0.61038 0.52367 -0.12562 0.04154  0.12776  19  GLN   A OE1 
141  N NE2 . GLN   A 19  ? 0.52876 0.58162 0.51668 -0.13545 0.02699  0.13901  19  GLN   A NE2 
142  N N   . VAL   A 20  ? 0.34947 0.34490 0.31093 -0.09316 0.01562  0.09540  20  VAL   A N   
143  C CA  . VAL   A 20  ? 0.35969 0.34269 0.30663 -0.08944 0.01262  0.09829  20  VAL   A CA  
144  C C   . VAL   A 20  ? 0.37306 0.37721 0.31281 -0.09002 0.02189  0.10363  20  VAL   A C   
145  O O   . VAL   A 20  ? 0.33895 0.36197 0.28142 -0.08348 0.03031  0.09606  20  VAL   A O   
146  C CB  . VAL   A 20  ? 0.33496 0.30647 0.27856 -0.07620 0.00934  0.08618  20  VAL   A CB  
147  C CG1 . VAL   A 20  ? 0.35375 0.31236 0.28396 -0.07307 0.00432  0.09066  20  VAL   A CG1 
148  C CG2 . VAL   A 20  ? 0.35515 0.30919 0.30491 -0.07386 0.00225  0.07952  20  VAL   A CG2 
149  N N   . THR   A 21  ? 0.35437 0.35413 0.28363 -0.09735 0.02002  0.11653  21  THR   A N   
150  C CA  . THR   A 21  ? 0.40787 0.42651 0.32617 -0.09804 0.02857  0.12270  21  THR   A CA  
151  C C   . THR   A 21  ? 0.41881 0.42160 0.31945 -0.09417 0.02231  0.12562  21  THR   A C   
152  O O   . THR   A 21  ? 0.46115 0.44141 0.35814 -0.09847 0.01224  0.13316  21  THR   A O   
153  C CB  . THR   A 21  ? 0.41509 0.44858 0.33659 -0.11206 0.03335  0.13862  21  THR   A CB  
154  O OG1 . THR   A 21  ? 0.42399 0.47377 0.36435 -0.11544 0.03803  0.13606  21  THR   A OG1 
155  C CG2 . THR   A 21  ? 0.42767 0.48214 0.33705 -0.10943 0.04350  0.14207  21  THR   A CG2 
156  N N   . CYS   A 22  ? 0.38953 0.40283 0.27921 -0.08567 0.02719  0.11930  22  CYS   A N   
157  C CA  . CYS   A 22  ? 0.45005 0.45354 0.32147 -0.08273 0.02186  0.12330  22  CYS   A CA  
158  C C   . CYS   A 22  ? 0.47673 0.50243 0.33368 -0.08241 0.03206  0.12570  22  CYS   A C   
159  O O   . CYS   A 22  ? 0.49251 0.53305 0.35028 -0.07472 0.03948  0.11381  22  CYS   A O   
160  C CB  . CYS   A 22  ? 0.40597 0.39674 0.27764 -0.07098 0.01469  0.11058  22  CYS   A CB  
161  S SG  . CYS   A 22  ? 0.50825 0.48554 0.36047 -0.06714 0.00487  0.11598  22  CYS   A SG  
162  N N   . GLY   A 23  ? 0.52666 0.55430 0.36995 -0.09066 0.03258  0.14116  23  GLY   A N   
163  C CA  . GLY   A 23  ? 0.54352 0.59351 0.37241 -0.08975 0.04348  0.14338  23  GLY   A CA  
164  C C   . GLY   A 23  ? 0.52747 0.60156 0.37169 -0.08952 0.05625  0.13861  23  GLY   A C   
165  O O   . GLY   A 23  ? 0.54592 0.62275 0.40821 -0.09712 0.05706  0.14442  23  GLY   A O   
166  N N   . THR   A 24  ? 0.52849 0.61949 0.36589 -0.08014 0.06532  0.12729  24  THR   A N   
167  C CA  . THR   A 24  ? 0.53816 0.65205 0.39023 -0.07724 0.07728  0.12159  24  THR   A CA  
168  C C   . THR   A 24  ? 0.52118 0.63631 0.39082 -0.07390 0.07698  0.11146  24  THR   A C   
169  O O   . THR   A 24  ? 0.54364 0.67493 0.43107 -0.07319 0.08418  0.10884  24  THR   A O   
170  C CB  . THR   A 24  ? 0.64508 0.77497 0.48049 -0.06727 0.08746  0.11360  24  THR   A CB  
171  O OG1 . THR   A 24  ? 0.78662 0.93839 0.63746 -0.06366 0.09892  0.10895  24  THR   A OG1 
172  C CG2 . THR   A 24  ? 0.67506 0.79773 0.49547 -0.05727 0.08394  0.09980  24  THR   A CG2 
173  N N   . THR   A 25  ? 0.52671 0.61944 0.39705 -0.06840 0.06642  0.10177  25  THR   A N   
174  C CA  . THR   A 25  ? 0.48928 0.57778 0.37737 -0.06221 0.06441  0.08880  25  THR   A CA  
175  C C   . THR   A 25  ? 0.43990 0.51866 0.34629 -0.07032 0.05840  0.09441  25  THR   A C   
176  O O   . THR   A 25  ? 0.44045 0.50031 0.34386 -0.07610 0.04919  0.10185  25  THR   A O   
177  C CB  . THR   A 25  ? 0.46442 0.53582 0.34572 -0.05302 0.05631  0.07661  25  THR   A CB  
178  O OG1 . THR   A 25  ? 0.50869 0.58343 0.36802 -0.04826 0.05810  0.07429  25  THR   A OG1 
179  C CG2 . THR   A 25  ? 0.47634 0.54950 0.37209 -0.04522 0.05754  0.06270  25  THR   A CG2 
180  N N   . THR   A 26  ? 0.42346 0.51428 0.34790 -0.07019 0.06295  0.09053  26  THR   A N   
181  C CA  . THR   A 26  ? 0.38924 0.47155 0.33054 -0.07694 0.05689  0.09331  26  THR   A CA  
182  C C   . THR   A 26  ? 0.35990 0.43945 0.31258 -0.06819 0.05556  0.07937  26  THR   A C   
183  O O   . THR   A 26  ? 0.37171 0.46610 0.32734 -0.06042 0.06278  0.07137  26  THR   A O   
184  C CB  . THR   A 26  ? 0.35856 0.46078 0.31232 -0.08757 0.06268  0.10479  26  THR   A CB  
185  O OG1 . THR   A 26  ? 0.43230 0.53250 0.37668 -0.09842 0.06147  0.12030  26  THR   A OG1 
186  C CG2 . THR   A 26  ? 0.41012 0.50542 0.38202 -0.09321 0.05606  0.10448  26  THR   A CG2 
187  N N   . LEU   A 27  ? 0.31367 0.37358 0.27152 -0.06874 0.04631  0.07645  27  LEU   A N   
188  C CA  . LEU   A 27  ? 0.31868 0.37754 0.28817 -0.06251 0.04520  0.06582  27  LEU   A CA  
189  C C   . LEU   A 27  ? 0.29464 0.33763 0.27126 -0.06797 0.03666  0.06761  27  LEU   A C   
190  O O   . LEU   A 27  ? 0.31381 0.34778 0.28829 -0.07713 0.03192  0.07697  27  LEU   A O   
191  C CB  . LEU   A 27  ? 0.27775 0.32948 0.24099 -0.05161 0.04392  0.05478  27  LEU   A CB  
192  C CG  . LEU   A 27  ? 0.31477 0.35075 0.26460 -0.04918 0.03781  0.05500  27  LEU   A CG  
193  C CD1 . LEU   A 27  ? 0.32405 0.34070 0.27577 -0.05203 0.02899  0.05791  27  LEU   A CD1 
194  C CD2 . LEU   A 27  ? 0.27075 0.30567 0.21771 -0.03964 0.03732  0.04440  27  LEU   A CD2 
195  N N   . ASN   A 28  ? 0.25597 0.29454 0.23986 -0.06231 0.03433  0.05859  28  ASN   A N   
196  C CA  . ASN   A 28  ? 0.28643 0.31116 0.27550 -0.06582 0.02684  0.05801  28  ASN   A CA  
197  C C   . ASN   A 28  ? 0.31933 0.32197 0.29988 -0.06049 0.01995  0.05377  28  ASN   A C   
198  O O   . ASN   A 28  ? 0.29015 0.29183 0.26634 -0.05225 0.02116  0.04833  28  ASN   A O   
199  C CB  . ASN   A 28  ? 0.28406 0.31804 0.28494 -0.06271 0.02834  0.05157  28  ASN   A CB  
200  C CG  . ASN   A 28  ? 0.30114 0.35958 0.31267 -0.06511 0.03568  0.05476  28  ASN   A CG  
201  O OD1 . ASN   A 28  ? 0.31341 0.37995 0.33201 -0.07456 0.03519  0.06288  28  ASN   A OD1 
202  N ND2 . ASN   A 28  ? 0.29741 0.36789 0.31104 -0.05644 0.04211  0.04855  28  ASN   A ND2 
203  N N   . GLY   A 29  ? 0.29562 0.28048 0.27426 -0.06520 0.01219  0.05638  29  GLY   A N   
204  C CA  . GLY   A 29  ? 0.29486 0.25920 0.26683 -0.05865 0.00582  0.05162  29  GLY   A CA  
205  C C   . GLY   A 29  ? 0.29389 0.24683 0.26840 -0.05878 0.00047  0.04654  29  GLY   A C   
206  O O   . GLY   A 29  ? 0.28145 0.23858 0.26171 -0.06664 -0.00082 0.04893  29  GLY   A O   
207  N N   . LEU   A 30  ? 0.27411 0.21368 0.24393 -0.04973 -0.00274 0.03971  30  LEU   A N   
208  C CA  . LEU   A 30  ? 0.29044 0.21788 0.25872 -0.04724 -0.00744 0.03316  30  LEU   A CA  
209  C C   . LEU   A 30  ? 0.32011 0.22088 0.27860 -0.04579 -0.01603 0.03330  30  LEU   A C   
210  O O   . LEU   A 30  ? 0.32386 0.21756 0.27818 -0.03746 -0.01662 0.03215  30  LEU   A O   
211  C CB  . LEU   A 30  ? 0.28001 0.21573 0.25068 -0.03654 -0.00292 0.02478  30  LEU   A CB  
212  C CG  . LEU   A 30  ? 0.30902 0.23543 0.27590 -0.03217 -0.00603 0.01745  30  LEU   A CG  
213  C CD1 . LEU   A 30  ? 0.32011 0.25423 0.29166 -0.04016 -0.00681 0.01809  30  LEU   A CD1 
214  C CD2 . LEU   A 30  ? 0.28359 0.21880 0.25229 -0.02119 -0.00084 0.01157  30  LEU   A CD2 
215  N N   . TRP   A 31  ? 0.31297 0.19853 0.26840 -0.05383 -0.02355 0.03482  31  TRP   A N   
216  C CA  . TRP   A 31  ? 0.32180 0.17786 0.26734 -0.05412 -0.03352 0.03555  31  TRP   A CA  
217  C C   . TRP   A 31  ? 0.38717 0.22644 0.32500 -0.04561 -0.03818 0.02409  31  TRP   A C   
218  O O   . TRP   A 31  ? 0.39824 0.23521 0.33541 -0.05100 -0.04171 0.02080  31  TRP   A O   
219  C CB  . TRP   A 31  ? 0.38710 0.23526 0.33372 -0.07021 -0.04016 0.04564  31  TRP   A CB  
220  C CG  . TRP   A 31  ? 0.40356 0.21826 0.34019 -0.07282 -0.05209 0.04814  31  TRP   A CG  
221  C CD1 . TRP   A 31  ? 0.44249 0.23587 0.36998 -0.06161 -0.05627 0.04459  31  TRP   A CD1 
222  C CD2 . TRP   A 31  ? 0.46949 0.26769 0.40533 -0.08777 -0.06225 0.05518  31  TRP   A CD2 
223  N NE1 . TRP   A 31  ? 0.46678 0.22866 0.38651 -0.06785 -0.06870 0.04843  31  TRP   A NE1 
224  C CE2 . TRP   A 31  ? 0.47215 0.23586 0.39668 -0.08483 -0.07289 0.05520  31  TRP   A CE2 
225  C CE3 . TRP   A 31  ? 0.46059 0.27030 0.40549 -0.10355 -0.06400 0.06193  31  TRP   A CE3 
226  C CZ2 . TRP   A 31  ? 0.48983 0.22768 0.41068 -0.09804 -0.08581 0.06168  31  TRP   A CZ2 
227  C CZ3 . TRP   A 31  ? 0.49787 0.28499 0.44063 -0.11745 -0.07649 0.06904  31  TRP   A CZ3 
228  C CH2 . TRP   A 31  ? 0.51373 0.26389 0.44394 -0.11508 -0.08760 0.06881  31  TRP   A CH2 
229  N N   . LEU   A 32  ? 0.40044 0.22950 0.33232 -0.03184 -0.03812 0.01806  32  LEU   A N   
230  C CA  . LEU   A 32  ? 0.43593 0.25026 0.35870 -0.02084 -0.04092 0.00654  32  LEU   A CA  
231  C C   . LEU   A 32  ? 0.45045 0.23688 0.36399 -0.01281 -0.04842 0.00495  32  LEU   A C   
232  O O   . LEU   A 32  ? 0.41313 0.20286 0.32999 -0.00706 -0.04636 0.00920  32  LEU   A O   
233  C CB  . LEU   A 32  ? 0.39287 0.22862 0.31996 -0.00893 -0.03095 0.00016  32  LEU   A CB  
234  C CG  . LEU   A 32  ? 0.38004 0.24219 0.31661 -0.01532 -0.02382 0.00191  32  LEU   A CG  
235  C CD1 . LEU   A 32  ? 0.33331 0.21510 0.27543 -0.00487 -0.01482 -0.00161 32  LEU   A CD1 
236  C CD2 . LEU   A 32  ? 0.36654 0.22306 0.29793 -0.02089 -0.02823 -0.00244 32  LEU   A CD2 
237  N N   . ASP   A 33  ? 0.50384 0.26201 0.40544 -0.01195 -0.05794 -0.00141 33  ASP   A N   
238  C CA  . ASP   A 33  ? 0.51847 0.24513 0.41035 -0.00403 -0.06684 -0.00340 33  ASP   A CA  
239  C C   . ASP   A 33  ? 0.51657 0.23926 0.41353 -0.01462 -0.07074 0.01085  33  ASP   A C   
240  O O   . ASP   A 33  ? 0.50138 0.23133 0.40346 -0.03154 -0.07192 0.02008  33  ASP   A O   
241  C CB  . ASP   A 33  ? 0.54157 0.27299 0.43207 0.01678  -0.06070 -0.01218 33  ASP   A CB  
242  C CG  . ASP   A 33  ? 0.62822 0.36186 0.51072 0.02643  -0.05710 -0.02549 33  ASP   A CG  
243  O OD1 . ASP   A 33  ? 0.61471 0.32967 0.48601 0.02085  -0.06458 -0.03105 33  ASP   A OD1 
244  O OD2 . ASP   A 33  ? 0.62055 0.37614 0.50801 0.03868  -0.04692 -0.02965 33  ASP   A OD2 
245  N N   . ASP   A 34  ? 0.52255 0.23702 0.41896 -0.00529 -0.07222 0.01392  34  ASP   A N   
246  C CA  . ASP   A 34  ? 0.52151 0.23170 0.42033 -0.01512 -0.07631 0.02828  34  ASP   A CA  
247  C C   . ASP   A 34  ? 0.49377 0.23555 0.40238 -0.01376 -0.06622 0.03477  34  ASP   A C   
248  O O   . ASP   A 34  ? 0.47428 0.21233 0.38252 -0.01416 -0.06907 0.04407  34  ASP   A O   
249  C CB  . ASP   A 34  ? 0.54469 0.21912 0.43446 -0.00760 -0.08800 0.02926  34  ASP   A CB  
250  C CG  . ASP   A 34  ? 0.60415 0.28010 0.49455 0.01436  -0.08495 0.02161  34  ASP   A CG  
251  O OD1 . ASP   A 34  ? 0.57567 0.27747 0.47227 0.02386  -0.07440 0.01393  34  ASP   A OD1 
252  O OD2 . ASP   A 34  ? 0.63015 0.28083 0.51553 0.02224  -0.09376 0.02382  34  ASP   A OD2 
253  N N   . VAL   A 35  ? 0.46254 0.23404 0.37895 -0.01266 -0.05544 0.03028  35  VAL   A N   
254  C CA  . VAL   A 35  ? 0.44253 0.24249 0.36734 -0.01137 -0.04668 0.03457  35  VAL   A CA  
255  C C   . VAL   A 35  ? 0.39866 0.22245 0.32990 -0.02326 -0.03935 0.03728  35  VAL   A C   
256  O O   . VAL   A 35  ? 0.39058 0.21770 0.32316 -0.02603 -0.03776 0.03153  35  VAL   A O   
257  C CB  . VAL   A 35  ? 0.43652 0.24966 0.36626 0.00503  -0.04087 0.02582  35  VAL   A CB  
258  C CG1 . VAL   A 35  ? 0.39739 0.23739 0.33552 0.00477  -0.03396 0.03030  35  VAL   A CG1 
259  C CG2 . VAL   A 35  ? 0.44900 0.24052 0.37405 0.01894  -0.04765 0.02276  35  VAL   A CG2 
260  N N   . VAL   A 36  ? 0.34256 0.18284 0.27703 -0.02949 -0.03519 0.04581  36  VAL   A N   
261  C CA  . VAL   A 36  ? 0.33968 0.20481 0.28082 -0.03792 -0.02711 0.04783  36  VAL   A CA  
262  C C   . VAL   A 36  ? 0.31562 0.20216 0.26147 -0.03042 -0.01971 0.04506  36  VAL   A C   
263  O O   . VAL   A 36  ? 0.33569 0.22161 0.27859 -0.02667 -0.02125 0.04896  36  VAL   A O   
264  C CB  . VAL   A 36  ? 0.34371 0.21095 0.28347 -0.05234 -0.02797 0.06014  36  VAL   A CB  
265  C CG1 . VAL   A 36  ? 0.33198 0.22817 0.27898 -0.05750 -0.01809 0.06150  36  VAL   A CG1 
266  C CG2 . VAL   A 36  ? 0.35383 0.20065 0.29121 -0.06252 -0.03642 0.06377  36  VAL   A CG2 
267  N N   . TYR   A 37  ? 0.30268 0.20690 0.25561 -0.02866 -0.01290 0.03876  37  TYR   A N   
268  C CA  . TYR   A 37  ? 0.28371 0.20666 0.24209 -0.02241 -0.00684 0.03526  37  TYR   A CA  
269  C C   . TYR   A 37  ? 0.28382 0.22526 0.24525 -0.02955 -0.00061 0.03814  37  TYR   A C   
270  O O   . TYR   A 37  ? 0.28274 0.22976 0.24783 -0.03571 0.00178  0.03828  37  TYR   A O   
271  C CB  . TYR   A 37  ? 0.30572 0.23391 0.26977 -0.01457 -0.00398 0.02641  37  TYR   A CB  
272  C CG  . TYR   A 37  ? 0.31031 0.22238 0.27078 -0.00568 -0.00850 0.02197  37  TYR   A CG  
273  C CD1 . TYR   A 37  ? 0.32774 0.22202 0.28192 -0.00755 -0.01320 0.01967  37  TYR   A CD1 
274  C CD2 . TYR   A 37  ? 0.33037 0.24542 0.29394 0.00511  -0.00838 0.01969  37  TYR   A CD2 
275  C CE1 . TYR   A 37  ? 0.35655 0.23431 0.30534 0.00243  -0.01724 0.01405  37  TYR   A CE1 
276  C CE2 . TYR   A 37  ? 0.33306 0.23514 0.29381 0.01538  -0.01147 0.01506  37  TYR   A CE2 
277  C CZ  . TYR   A 37  ? 0.37062 0.25316 0.32286 0.01464  -0.01564 0.01167  37  TYR   A CZ  
278  O OH  . TYR   A 37  ? 0.36187 0.22980 0.30923 0.02648  -0.01864 0.00561  37  TYR   A OH  
279  N N   . CYS   A 38  ? 0.27354 0.22490 0.23344 -0.02799 0.00172  0.03983  38  CYS   A N   
280  C CA  . CYS   A 38  ? 0.24747 0.21573 0.20857 -0.03248 0.00811  0.04083  38  CYS   A CA  
281  C C   . CYS   A 38  ? 0.25352 0.23067 0.21352 -0.02693 0.00957  0.03758  38  CYS   A C   
282  O O   . CYS   A 38  ? 0.26524 0.23635 0.22366 -0.02160 0.00491  0.03718  38  CYS   A O   
283  C CB  . CYS   A 38  ? 0.28390 0.25221 0.23864 -0.04171 0.00855  0.05021  38  CYS   A CB  
284  S SG  . CYS   A 38  ? 0.33696 0.29969 0.27868 -0.04188 0.00492  0.05778  38  CYS   A SG  
285  N N   . PRO   A 39  ? 0.22985 0.22098 0.19121 -0.02764 0.01522  0.03484  39  PRO   A N   
286  C CA  . PRO   A 39  ? 0.24392 0.24069 0.20232 -0.02332 0.01498  0.03120  39  PRO   A CA  
287  C C   . PRO   A 39  ? 0.23507 0.22755 0.18093 -0.02455 0.01130  0.03687  39  PRO   A C   
288  O O   . PRO   A 39  ? 0.27558 0.26762 0.21351 -0.03008 0.01281  0.04374  39  PRO   A O   
289  C CB  . PRO   A 39  ? 0.23532 0.24481 0.19529 -0.02403 0.02167  0.02731  39  PRO   A CB  
290  C CG  . PRO   A 39  ? 0.26418 0.27636 0.23327 -0.02684 0.02486  0.02764  39  PRO   A CG  
291  C CD  . PRO   A 39  ? 0.24504 0.24723 0.21090 -0.03180 0.02138  0.03462  39  PRO   A CD  
292  N N   . ARG   A 40  ? 0.24895 0.23943 0.19349 -0.01989 0.00604  0.03492  40  ARG   A N   
293  C CA  . ARG   A 40  ? 0.25771 0.24389 0.18956 -0.02065 0.00109  0.04066  40  ARG   A CA  
294  C C   . ARG   A 40  ? 0.27813 0.27252 0.19664 -0.02362 0.00521  0.04107  40  ARG   A C   
295  O O   . ARG   A 40  ? 0.27013 0.26174 0.17495 -0.02620 0.00283  0.04803  40  ARG   A O   
296  C CB  . ARG   A 40  ? 0.26113 0.24556 0.19652 -0.01494 -0.00644 0.03857  40  ARG   A CB  
297  C CG  . ARG   A 40  ? 0.23714 0.23055 0.17492 -0.01302 -0.00653 0.03111  40  ARG   A CG  
298  C CD  . ARG   A 40  ? 0.24906 0.24241 0.19246 -0.00888 -0.01522 0.03110  40  ARG   A CD  
299  N NE  . ARG   A 40  ? 0.24887 0.24932 0.19740 -0.00830 -0.01709 0.02443  40  ARG   A NE  
300  C CZ  . ARG   A 40  ? 0.27134 0.27481 0.22559 -0.00642 -0.02527 0.02427  40  ARG   A CZ  
301  N NH1 . ARG   A 40  ? 0.27519 0.27674 0.23156 -0.00345 -0.03187 0.03017  40  ARG   A NH1 
302  N NH2 . ARG   A 40  ? 0.25566 0.26379 0.21383 -0.00768 -0.02780 0.01843  40  ARG   A NH2 
303  N N   . HIS   A 41  ? 0.24603 0.25013 0.16711 -0.02270 0.01139  0.03398  41  HIS   A N   
304  C CA  . HIS   A 41  ? 0.28831 0.30016 0.19466 -0.02370 0.01595  0.03352  41  HIS   A CA  
305  C C   . HIS   A 41  ? 0.29410 0.31164 0.19505 -0.02953 0.02270  0.04189  41  HIS   A C   
306  O O   . HIS   A 41  ? 0.31715 0.34413 0.20563 -0.02993 0.02839  0.04232  41  HIS   A O   
307  C CB  . HIS   A 41  ? 0.28667 0.30528 0.19623 -0.01940 0.01969  0.02272  41  HIS   A CB  
308  C CG  . HIS   A 41  ? 0.31209 0.33787 0.23444 -0.01948 0.02719  0.02022  41  HIS   A CG  
309  N ND1 . HIS   A 41  ? 0.33145 0.36780 0.25177 -0.02182 0.03565  0.02346  41  HIS   A ND1 
310  C CD2 . HIS   A 41  ? 0.28949 0.31472 0.22730 -0.01749 0.02710  0.01548  41  HIS   A CD2 
311  C CE1 . HIS   A 41  ? 0.29158 0.33327 0.22630 -0.02095 0.03966  0.02045  41  HIS   A CE1 
312  N NE2 . HIS   A 41  ? 0.33207 0.36619 0.27645 -0.01839 0.03446  0.01562  41  HIS   A NE2 
313  N N   . VAL   A 42  ? 0.27913 0.29098 0.18790 -0.03425 0.02166  0.04902  42  VAL   A N   
314  C CA  . VAL   A 42  ? 0.31345 0.32924 0.21708 -0.04198 0.02572  0.05967  42  VAL   A CA  
315  C C   . VAL   A 42  ? 0.34398 0.35753 0.22859 -0.04414 0.02314  0.06765  42  VAL   A C   
316  O O   . VAL   A 42  ? 0.37997 0.40268 0.25588 -0.04984 0.02891  0.07601  42  VAL   A O   
317  C CB  . VAL   A 42  ? 0.28597 0.29059 0.20002 -0.04715 0.02170  0.06555  42  VAL   A CB  
318  C CG1 . VAL   A 42  ? 0.30398 0.28989 0.21396 -0.04536 0.01144  0.06903  42  VAL   A CG1 
319  C CG2 . VAL   A 42  ? 0.34439 0.35570 0.25795 -0.05712 0.02623  0.07653  42  VAL   A CG2 
320  N N   . ILE   A 43  ? 0.33067 0.33379 0.20879 -0.03982 0.01446  0.06608  43  ILE   A N   
321  C CA  . ILE   A 43  ? 0.37162 0.37152 0.23058 -0.04167 0.01028  0.07427  43  ILE   A CA  
322  C C   . ILE   A 43  ? 0.40676 0.41777 0.24902 -0.03845 0.01414  0.06883  43  ILE   A C   
323  O O   . ILE   A 43  ? 0.44571 0.45504 0.26909 -0.03960 0.01054  0.07497  43  ILE   A O   
324  C CB  . ILE   A 43  ? 0.38512 0.36957 0.24461 -0.03806 -0.00209 0.07607  43  ILE   A CB  
325  C CG1 . ILE   A 43  ? 0.36909 0.35574 0.23206 -0.03053 -0.00631 0.06453  43  ILE   A CG1 
326  C CG2 . ILE   A 43  ? 0.36988 0.34149 0.24459 -0.03874 -0.00600 0.07889  43  ILE   A CG2 
327  C CD1 . ILE   A 43  ? 0.39398 0.37000 0.26027 -0.02629 -0.01827 0.06667  43  ILE   A CD1 
328  N N   . CYS   A 44  ? 0.37931 0.40039 0.22625 -0.03415 0.02084  0.05753  44  CYS   A N   
329  C CA  . CYS   A 44  ? 0.40128 0.42901 0.23170 -0.02926 0.02299  0.04931  44  CYS   A CA  
330  C C   . CYS   A 44  ? 0.48178 0.52563 0.30095 -0.03068 0.03542  0.05206  44  CYS   A C   
331  O O   . CYS   A 44  ? 0.45837 0.51217 0.29089 -0.03312 0.04392  0.05429  44  CYS   A O   
332  C CB  . CYS   A 44  ? 0.43354 0.46065 0.27500 -0.02281 0.02214  0.03481  44  CYS   A CB  
333  S SG  . CYS   A 44  ? 0.39210 0.40578 0.24358 -0.02032 0.00824  0.03080  44  CYS   A SG  
334  N N   . THR   A 45  ? 0.48996 0.53787 0.28457 -0.02879 0.03646  0.05184  45  THR   A N   
335  C CA  . THR   A 45  ? 0.58585 0.65171 0.36962 -0.02645 0.04975  0.04989  45  THR   A CA  
336  C C   . THR   A 45  ? 0.58860 0.65658 0.37589 -0.01689 0.05279  0.03241  45  THR   A C   
337  O O   . THR   A 45  ? 0.55705 0.61211 0.35222 -0.01347 0.04376  0.02293  45  THR   A O   
338  C CB  . THR   A 45  ? 0.57918 0.64954 0.33250 -0.02707 0.05098  0.05563  45  THR   A CB  
339  O OG1 . THR   A 45  ? 0.60070 0.66021 0.33708 -0.02076 0.04175  0.04435  45  THR   A OG1 
340  C CG2 . THR   A 45  ? 0.61136 0.67581 0.36078 -0.03672 0.04554  0.07389  45  THR   A CG2 
341  N N   . SER   A 46  ? 0.61442 0.69936 0.39672 -0.01240 0.06570  0.02874  46  SER   A N   
342  C CA  . SER   A 46  ? 0.62491 0.70997 0.40828 -0.00201 0.06837  0.01186  46  SER   A CA  
343  C C   . SER   A 46  ? 0.61847 0.68839 0.38048 0.00341  0.05837  0.00032  46  SER   A C   
344  O O   . SER   A 46  ? 0.57864 0.63755 0.34734 0.00879  0.05256  -0.01262 46  SER   A O   
345  C CB  . SER   A 46  ? 0.64881 0.75613 0.42779 0.00362  0.08439  0.01025  46  SER   A CB  
346  O OG  . SER   A 46  ? 0.67221 0.79361 0.47623 -0.00127 0.09185  0.01912  46  SER   A OG  
347  N N   . GLU   A 47  ? 0.60637 0.67470 0.34296 0.00110  0.05493  0.00570  47  GLU   A N   
348  C CA  . GLU   A 47  ? 0.61925 0.67281 0.33458 0.00479  0.04316  -0.00414 47  GLU   A CA  
349  C C   . GLU   A 47  ? 0.58056 0.61723 0.31071 0.00019  0.02712  -0.00312 47  GLU   A C   
350  O O   . GLU   A 47  ? 0.56909 0.59342 0.29762 0.00362  0.01714  -0.01496 47  GLU   A O   
351  C CB  . GLU   A 47  ? 0.62684 0.68512 0.30949 0.00346  0.04403  0.00263  47  GLU   A CB  
352  N N   . ASP   A 48  ? 0.54058 0.57661 0.28529 -0.00739 0.02420  0.01099  48  ASP   A N   
353  C CA  . ASP   A 48  ? 0.51703 0.54013 0.27807 -0.01032 0.01064  0.01256  48  ASP   A CA  
354  C C   . ASP   A 48  ? 0.48197 0.50010 0.26499 -0.00708 0.00836  0.00139  48  ASP   A C   
355  O O   . ASP   A 48  ? 0.45872 0.46718 0.24840 -0.00720 -0.00356 -0.00271 48  ASP   A O   
356  C CB  . ASP   A 48  ? 0.49416 0.51729 0.27015 -0.01695 0.01053  0.02771  48  ASP   A CB  
357  C CG  . ASP   A 48  ? 0.53791 0.56144 0.29401 -0.02153 0.00864  0.04113  48  ASP   A CG  
358  O OD1 . ASP   A 48  ? 0.51566 0.53596 0.24860 -0.01995 0.00195  0.03942  48  ASP   A OD1 
359  O OD2 . ASP   A 48  ? 0.57570 0.60190 0.33886 -0.02723 0.01308  0.05383  48  ASP   A OD2 
360  N N   . MET   A 49  ? 0.48029 0.50603 0.27543 -0.00450 0.01930  -0.00261 49  MET   A N   
361  C CA  . MET   A 49  ? 0.44848 0.47008 0.26721 -0.00268 0.01781  -0.00965 49  MET   A CA  
362  C C   . MET   A 49  ? 0.39387 0.40511 0.20724 0.00188  0.00984  -0.02344 49  MET   A C   
363  O O   . MET   A 49  ? 0.33459 0.33972 0.16688 0.00161  0.00468  -0.02739 49  MET   A O   
364  C CB  . MET   A 49  ? 0.46995 0.50294 0.30088 -0.00066 0.03082  -0.00996 49  MET   A CB  
365  C CG  . MET   A 49  ? 0.52145 0.56133 0.36720 -0.00703 0.03553  0.00302  49  MET   A CG  
366  S SD  . MET   A 49  ? 0.81870 0.87522 0.67822 -0.00559 0.04981  0.00376  49  MET   A SD  
367  C CE  . MET   A 49  ? 0.52773 0.58781 0.39865 -0.01579 0.05093  0.02024  49  MET   A CE  
368  N N   . LEU   A 50  ? 0.41756 0.42598 0.20474 0.00563  0.00817  -0.03055 50  LEU   A N   
369  C CA  . LEU   A 50  ? 0.44992 0.44523 0.23015 0.00929  -0.00134 -0.04434 50  LEU   A CA  
370  C C   . LEU   A 50  ? 0.47290 0.45858 0.26194 0.00360  -0.01735 -0.04202 50  LEU   A C   
371  O O   . LEU   A 50  ? 0.49530 0.47167 0.29585 0.00329  -0.02553 -0.04933 50  LEU   A O   
372  C CB  . LEU   A 50  ? 0.47797 0.47155 0.22453 0.01506  0.00007  -0.05308 50  LEU   A CB  
373  C CG  . LEU   A 50  ? 0.53223 0.53978 0.26922 0.02179  0.01736  -0.05466 50  LEU   A CG  
374  C CD1 . LEU   A 50  ? 0.56772 0.57484 0.26816 0.02835  0.01932  -0.06309 50  LEU   A CD1 
375  C CD2 . LEU   A 50  ? 0.48610 0.49420 0.24205 0.02779  0.02416  -0.06281 50  LEU   A CD2 
376  N N   . ASN   A 51  ? 0.45716 0.44569 0.24273 -0.00106 -0.02218 -0.03094 51  ASN   A N   
377  C CA  . ASN   A 51  ? 0.45113 0.43380 0.24541 -0.00544 -0.03735 -0.02784 51  ASN   A CA  
378  C C   . ASN   A 51  ? 0.42624 0.41436 0.22648 -0.00909 -0.03853 -0.01302 51  ASN   A C   
379  O O   . ASN   A 51  ? 0.44310 0.42933 0.22803 -0.01064 -0.04726 -0.00828 51  ASN   A O   
380  C CB  . ASN   A 51  ? 0.48668 0.46029 0.25638 -0.00491 -0.04952 -0.03604 51  ASN   A CB  
381  C CG  . ASN   A 51  ? 0.55499 0.52392 0.33720 -0.00975 -0.06663 -0.03422 51  ASN   A CG  
382  O OD1 . ASN   A 51  ? 0.57510 0.54719 0.38604 -0.01239 -0.06850 -0.02985 51  ASN   A OD1 
383  N ND2 . ASN   A 51  ? 0.59060 0.55349 0.35105 -0.01089 -0.07929 -0.03726 51  ASN   A ND2 
384  N N   . PRO   A 52  ? 0.37946 0.37283 0.20055 -0.01019 -0.03102 -0.00564 52  PRO   A N   
385  C CA  . PRO   A 52  ? 0.38424 0.37973 0.20813 -0.01274 -0.03151 0.00781  52  PRO   A CA  
386  C C   . PRO   A 52  ? 0.40216 0.39501 0.23937 -0.01375 -0.04448 0.01252  52  PRO   A C   
387  O O   . PRO   A 52  ? 0.39588 0.38922 0.25297 -0.01351 -0.04892 0.00846  52  PRO   A O   
388  C CB  . PRO   A 52  ? 0.34711 0.34705 0.18885 -0.01319 -0.02010 0.01147  52  PRO   A CB  
389  C CG  . PRO   A 52  ? 0.34793 0.34805 0.20521 -0.01116 -0.01813 0.00149  52  PRO   A CG  
390  C CD  . PRO   A 52  ? 0.38091 0.37679 0.22285 -0.00900 -0.02281 -0.00945 52  PRO   A CD  
391  N N   . ASN   A 53  ? 0.37172 0.36288 0.19809 -0.01476 -0.05071 0.02198  53  ASN   A N   
392  C CA  . ASN   A 53  ? 0.35594 0.34643 0.19797 -0.01425 -0.06102 0.02929  53  ASN   A CA  
393  C C   . ASN   A 53  ? 0.34841 0.33741 0.19984 -0.01396 -0.05421 0.03887  53  ASN   A C   
394  O O   . ASN   A 53  ? 0.38085 0.36612 0.21757 -0.01553 -0.05371 0.04792  53  ASN   A O   
395  C CB  . ASN   A 53  ? 0.41460 0.40256 0.23905 -0.01483 -0.07404 0.03395  53  ASN   A CB  
396  C CG  . ASN   A 53  ? 0.42409 0.41353 0.26735 -0.01295 -0.08565 0.04105  53  ASN   A CG  
397  O OD1 . ASN   A 53  ? 0.43537 0.42466 0.29548 -0.01055 -0.08251 0.04750  53  ASN   A OD1 
398  N ND2 . ASN   A 53  ? 0.42995 0.42102 0.27036 -0.01355 -0.09964 0.03949  53  ASN   A ND2 
399  N N   . TYR   A 54  ? 0.34413 0.33502 0.21885 -0.01237 -0.04942 0.03710  54  TYR   A N   
400  C CA  . TYR   A 54  ? 0.35702 0.34425 0.23803 -0.01249 -0.04247 0.04383  54  TYR   A CA  
401  C C   . TYR   A 54  ? 0.35970 0.34010 0.24154 -0.01052 -0.05061 0.05426  54  TYR   A C   
402  O O   . TYR   A 54  ? 0.37821 0.35132 0.25274 -0.01255 -0.04797 0.06239  54  TYR   A O   
403  C CB  . TYR   A 54  ? 0.29546 0.28573 0.19847 -0.01071 -0.03629 0.03867  54  TYR   A CB  
404  C CG  . TYR   A 54  ? 0.28301 0.27747 0.18400 -0.01278 -0.02637 0.03133  54  TYR   A CG  
405  C CD1 . TYR   A 54  ? 0.28759 0.28187 0.18177 -0.01560 -0.01716 0.03426  54  TYR   A CD1 
406  C CD2 . TYR   A 54  ? 0.31579 0.31449 0.22312 -0.01199 -0.02686 0.02212  54  TYR   A CD2 
407  C CE1 . TYR   A 54  ? 0.27935 0.27948 0.17389 -0.01628 -0.00816 0.02784  54  TYR   A CE1 
408  C CE2 . TYR   A 54  ? 0.28367 0.28499 0.18993 -0.01249 -0.01838 0.01545  54  TYR   A CE2 
409  C CZ  . TYR   A 54  ? 0.26753 0.27047 0.16771 -0.01398 -0.00882 0.01819  54  TYR   A CZ  
410  O OH  . TYR   A 54  ? 0.26240 0.26993 0.16336 -0.01335 -0.00053 0.01187  54  TYR   A OH  
411  N N   . GLU   A 55  ? 0.37173 0.35434 0.26310 -0.00670 -0.06118 0.05483  55  GLU   A N   
412  C CA  . GLU   A 55  ? 0.39107 0.36714 0.28361 -0.00317 -0.06983 0.06476  55  GLU   A CA  
413  C C   . GLU   A 55  ? 0.39501 0.36407 0.26207 -0.00690 -0.07376 0.07341  55  GLU   A C   
414  O O   . GLU   A 55  ? 0.41197 0.37063 0.27436 -0.00703 -0.07466 0.08314  55  GLU   A O   
415  C CB  . GLU   A 55  ? 0.42680 0.41065 0.33547 0.00181  -0.08067 0.06398  55  GLU   A CB  
416  C CG  . GLU   A 55  ? 0.47243 0.46376 0.40766 0.00631  -0.07611 0.05889  55  GLU   A CG  
417  C CD  . GLU   A 55  ? 0.58819 0.58891 0.53002 0.00257  -0.07132 0.04910  55  GLU   A CD  
418  O OE1 . GLU   A 55  ? 0.61895 0.62722 0.58148 0.00527  -0.06736 0.04578  55  GLU   A OE1 
419  O OE2 . GLU   A 55  ? 0.47045 0.47031 0.39597 -0.00261 -0.07149 0.04480  55  GLU   A OE2 
420  N N   . ASP   A 56  ? 0.40979 0.38333 0.25863 -0.01017 -0.07613 0.07011  56  ASP   A N   
421  C CA  . ASP   A 56  ? 0.45549 0.42421 0.27719 -0.01375 -0.07903 0.07861  56  ASP   A CA  
422  C C   . ASP   A 56  ? 0.44393 0.40984 0.25443 -0.01875 -0.06650 0.08316  56  ASP   A C   
423  O O   . ASP   A 56  ? 0.47718 0.43629 0.27343 -0.02191 -0.06804 0.09532  56  ASP   A O   
424  C CB  . ASP   A 56  ? 0.46596 0.44009 0.26844 -0.01534 -0.08385 0.07198  56  ASP   A CB  
425  C CG  . ASP   A 56  ? 0.51272 0.48902 0.32172 -0.01249 -0.09989 0.07158  56  ASP   A CG  
426  O OD1 . ASP   A 56  ? 0.50218 0.47752 0.33044 -0.00836 -0.10681 0.07778  56  ASP   A OD1 
427  O OD2 . ASP   A 56  ? 0.53258 0.51179 0.32746 -0.01408 -0.10594 0.06476  56  ASP   A OD2 
428  N N   . LEU   A 57  ? 0.41346 0.38548 0.23031 -0.02007 -0.05457 0.07448  57  LEU   A N   
429  C CA  . LEU   A 57  ? 0.43473 0.40778 0.24382 -0.02522 -0.04268 0.07905  57  LEU   A CA  
430  C C   . LEU   A 57  ? 0.44764 0.41054 0.26873 -0.02692 -0.04255 0.08861  57  LEU   A C   
431  O O   . LEU   A 57  ? 0.48223 0.44142 0.29254 -0.03283 -0.03927 0.09942  57  LEU   A O   
432  C CB  . LEU   A 57  ? 0.38649 0.36915 0.20247 -0.02507 -0.03111 0.06739  57  LEU   A CB  
433  C CG  . LEU   A 57  ? 0.42972 0.41974 0.23185 -0.02308 -0.02997 0.05644  57  LEU   A CG  
434  C CD1 . LEU   A 57  ? 0.40591 0.40266 0.22014 -0.02166 -0.01962 0.04572  57  LEU   A CD1 
435  C CD2 . LEU   A 57  ? 0.44640 0.44015 0.21912 -0.02580 -0.02672 0.06172  57  LEU   A CD2 
436  N N   . LEU   A 58  ? 0.42896 0.38705 0.27182 -0.02190 -0.04625 0.08486  58  LEU   A N   
437  C CA  . LEU   A 58  ? 0.43323 0.37892 0.28657 -0.02210 -0.04684 0.09144  58  LEU   A CA  
438  C C   . LEU   A 58  ? 0.41028 0.34232 0.25413 -0.02205 -0.05729 0.10455  58  LEU   A C   
439  O O   . LEU   A 58  ? 0.44057 0.35973 0.28333 -0.02581 -0.05748 0.11346  58  LEU   A O   
440  C CB  . LEU   A 58  ? 0.37540 0.32051 0.25198 -0.01498 -0.04774 0.08305  58  LEU   A CB  
441  C CG  . LEU   A 58  ? 0.39163 0.32322 0.27845 -0.01403 -0.04713 0.08600  58  LEU   A CG  
442  C CD1 . LEU   A 58  ? 0.39965 0.33053 0.28237 -0.02265 -0.03801 0.08801  58  LEU   A CD1 
443  C CD2 . LEU   A 58  ? 0.38556 0.31982 0.29266 -0.00597 -0.04656 0.07665  58  LEU   A CD2 
444  N N   . ILE   A 59  ? 0.45406 0.38776 0.29095 -0.01828 -0.06712 0.10637  59  ILE   A N   
445  C CA  . ILE   A 59  ? 0.47504 0.39565 0.30341 -0.01717 -0.07854 0.11941  59  ILE   A CA  
446  C C   . ILE   A 59  ? 0.52136 0.43727 0.32685 -0.02661 -0.07590 0.13210  59  ILE   A C   
447  O O   . ILE   A 59  ? 0.55157 0.45215 0.35113 -0.02829 -0.08309 0.14539  59  ILE   A O   
448  C CB  . ILE   A 59  ? 0.47093 0.39753 0.29770 -0.01138 -0.09024 0.11818  59  ILE   A CB  
449  C CG1 . ILE   A 59  ? 0.45446 0.38270 0.30773 -0.00159 -0.09505 0.11162  59  ILE   A CG1 
450  C CG2 . ILE   A 59  ? 0.53516 0.45192 0.34405 -0.01248 -0.10154 0.13274  59  ILE   A CG2 
451  C CD1 . ILE   A 59  ? 0.51496 0.45680 0.37401 0.00226  -0.10261 0.10575  59  ILE   A CD1 
452  N N   . ARG   A 60  ? 0.49286 0.42195 0.28558 -0.03266 -0.06545 0.12885  60  ARG   A N   
453  C CA  . ARG   A 60  ? 0.53286 0.46185 0.30560 -0.04204 -0.06036 0.14146  60  ARG   A CA  
454  C C   . ARG   A 60  ? 0.52936 0.45205 0.31213 -0.04882 -0.05308 0.14702  60  ARG   A C   
455  O O   . ARG   A 60  ? 0.55403 0.47690 0.32362 -0.05810 -0.04909 0.15984  60  ARG   A O   
456  C CB  . ARG   A 60  ? 0.57652 0.52394 0.33105 -0.04458 -0.05096 0.13570  60  ARG   A CB  
457  C CG  . ARG   A 60  ? 0.64218 0.59535 0.38245 -0.03931 -0.05855 0.12892  60  ARG   A CG  
458  C CD  . ARG   A 60  ? 0.72502 0.66626 0.46479 -0.03521 -0.07546 0.13641  60  ARG   A CD  
459  N NE  . ARG   A 60  ? 0.82019 0.76510 0.53344 -0.03549 -0.08285 0.13969  60  ARG   A NE  
460  C CZ  . ARG   A 60  ? 0.87576 0.82591 0.58646 -0.03056 -0.09105 0.12964  60  ARG   A CZ  
461  N NH1 . ARG   A 60  ? 0.85778 0.81175 0.59171 -0.02544 -0.09203 0.11622  60  ARG   A NH1 
462  N NH2 . ARG   A 60  ? 0.92581 0.87751 0.60932 -0.03152 -0.09888 0.13362  60  ARG   A NH2 
463  N N   . LYS   A 61  ? 0.50579 0.42329 0.31089 -0.04507 -0.05179 0.13852  61  LYS   A N   
464  C CA  . LYS   A 61  ? 0.53207 0.44312 0.34691 -0.05173 -0.04623 0.14207  61  LYS   A CA  
465  C C   . LYS   A 61  ? 0.53735 0.42344 0.36068 -0.04937 -0.05711 0.14825  61  LYS   A C   
466  O O   . LYS   A 61  ? 0.53125 0.40956 0.36272 -0.03897 -0.06551 0.14311  61  LYS   A O   
467  C CB  . LYS   A 61  ? 0.49999 0.42274 0.33140 -0.04948 -0.03656 0.12741  61  LYS   A CB  
468  C CG  . LYS   A 61  ? 0.49472 0.43984 0.31858 -0.05046 -0.02600 0.12029  61  LYS   A CG  
469  C CD  . LYS   A 61  ? 0.52114 0.47646 0.33213 -0.06055 -0.01721 0.13066  61  LYS   A CD  
470  C CE  . LYS   A 61  ? 0.51755 0.49495 0.32263 -0.05865 -0.00586 0.12096  61  LYS   A CE  
471  N NZ  . LYS   A 61  ? 0.62844 0.62098 0.42392 -0.06708 0.00524  0.13007  61  LYS   A NZ  
472  N N   . SER   A 62  ? 0.50601 0.37975 0.32780 -0.05893 -0.05721 0.15943  62  SER   A N   
473  C CA  . SER   A 62  ? 0.50984 0.35614 0.33876 -0.05775 -0.06732 0.16452  62  SER   A CA  
474  C C   . SER   A 62  ? 0.50233 0.34495 0.34413 -0.06325 -0.06180 0.15961  62  SER   A C   
475  O O   . SER   A 62  ? 0.50883 0.37105 0.35342 -0.06943 -0.05050 0.15581  62  SER   A O   
476  C CB  . SER   A 62  ? 0.56643 0.39656 0.38110 -0.06550 -0.07549 0.18356  62  SER   A CB  
477  O OG  . SER   A 62  ? 0.60685 0.44274 0.40882 -0.06066 -0.08028 0.18771  62  SER   A OG  
478  N N   . ASN   A 63  ? 0.52401 0.34063 0.37316 -0.06032 -0.07061 0.15945  63  ASN   A N   
479  C CA  . ASN   A 63  ? 0.49340 0.30266 0.35321 -0.06539 -0.06800 0.15433  63  ASN   A CA  
480  C C   . ASN   A 63  ? 0.50672 0.32624 0.36349 -0.08261 -0.06126 0.16499  63  ASN   A C   
481  O O   . ASN   A 63  ? 0.52678 0.35975 0.39311 -0.08689 -0.05309 0.15811  63  ASN   A O   
482  C CB  . ASN   A 63  ? 0.51522 0.28956 0.37740 -0.06146 -0.08074 0.15572  63  ASN   A CB  
483  C CG  . ASN   A 63  ? 0.53841 0.30570 0.40773 -0.04289 -0.08538 0.14306  63  ASN   A CG  
484  O OD1 . ASN   A 63  ? 0.47374 0.26107 0.35154 -0.03473 -0.07791 0.13000  63  ASN   A OD1 
485  N ND2 . ASN   A 63  ? 0.53869 0.27772 0.40541 -0.03594 -0.09784 0.14746  63  ASN   A ND2 
486  N N   . HIS   A 64  ? 0.55914 0.37817 0.40673 -0.09054 -0.06297 0.17878  64  HIS   A N   
487  C CA  . HIS   A 64  ? 0.55838 0.39225 0.40907 -0.10442 -0.05524 0.18586  64  HIS   A CA  
488  C C   . HIS   A 64  ? 0.56213 0.43033 0.41015 -0.10744 -0.04072 0.18447  64  HIS   A C   
489  O O   . HIS   A 64  ? 0.55366 0.43870 0.40746 -0.11717 -0.03265 0.18857  64  HIS   A O   
490  C CB  . HIS   A 64  ? 0.57145 0.39600 0.41528 -0.11056 -0.06073 0.19933  64  HIS   A CB  
491  C CG  . HIS   A 64  ? 0.59127 0.42567 0.41964 -0.10672 -0.05967 0.20564  64  HIS   A CG  
492  N ND1 . HIS   A 64  ? 0.60618 0.46966 0.42624 -0.11010 -0.04769 0.20801  64  HIS   A ND1 
493  C CD2 . HIS   A 64  ? 0.64039 0.45969 0.45971 -0.09882 -0.06944 0.20912  64  HIS   A CD2 
494  C CE1 . HIS   A 64  ? 0.63802 0.50262 0.44280 -0.10521 -0.05057 0.21264  64  HIS   A CE1 
495  N NE2 . HIS   A 64  ? 0.67429 0.51303 0.47916 -0.09870 -0.06399 0.21392  64  HIS   A NE2 
496  N N   . ASN   A 65  ? 0.53964 0.41888 0.37974 -0.09875 -0.03761 0.17820  65  ASN   A N   
497  C CA  . ASN   A 65  ? 0.53167 0.44163 0.36857 -0.09952 -0.02412 0.17391  65  ASN   A CA  
498  C C   . ASN   A 65  ? 0.51576 0.43736 0.37022 -0.09758 -0.01666 0.16023  65  ASN   A C   
499  O O   . ASN   A 65  ? 0.48787 0.43506 0.34343 -0.09748 -0.00496 0.15527  65  ASN   A O   
500  C CB  . ASN   A 65  ? 0.53482 0.45299 0.36090 -0.08788 -0.02409 0.16573  65  ASN   A CB  
501  C CG  . ASN   A 65  ? 0.56913 0.48398 0.37529 -0.08983 -0.02897 0.17863  65  ASN   A CG  
502  O OD1 . ASN   A 65  ? 0.57395 0.47896 0.37256 -0.08170 -0.03806 0.17723  65  ASN   A OD1 
503  N ND2 . ASN   A 65  ? 0.57318 0.49905 0.37550 -0.09785 -0.02223 0.18741  65  ASN   A ND2 
504  N N   . PHE   A 66  ? 0.49110 0.39421 0.35817 -0.09490 -0.02336 0.15351  66  PHE   A N   
505  C CA  . PHE   A 66  ? 0.48475 0.39635 0.36751 -0.09270 -0.01803 0.14080  66  PHE   A CA  
506  C C   . PHE   A 66  ? 0.52215 0.42755 0.41334 -0.10590 -0.01977 0.14884  66  PHE   A C   
507  O O   . PHE   A 66  ? 0.54902 0.42747 0.43955 -0.10969 -0.03081 0.15443  66  PHE   A O   
508  C CB  . PHE   A 66  ? 0.45149 0.34842 0.34095 -0.07964 -0.02409 0.12676  66  PHE   A CB  
509  C CG  . PHE   A 66  ? 0.44922 0.35505 0.33454 -0.06783 -0.02277 0.11853  66  PHE   A CG  
510  C CD1 . PHE   A 66  ? 0.45092 0.38001 0.33912 -0.06425 -0.01314 0.10930  66  PHE   A CD1 
511  C CD2 . PHE   A 66  ? 0.45189 0.34287 0.33038 -0.06084 -0.03201 0.12096  66  PHE   A CD2 
512  C CE1 . PHE   A 66  ? 0.44240 0.37819 0.32684 -0.05484 -0.01346 0.10194  66  PHE   A CE1 
513  C CE2 . PHE   A 66  ? 0.44780 0.34851 0.32382 -0.05127 -0.03201 0.11412  66  PHE   A CE2 
514  C CZ  . PHE   A 66  ? 0.45567 0.37822 0.33437 -0.04900 -0.02300 0.10460  66  PHE   A CZ  
515  N N   . LEU   A 67  ? 0.45038 0.38010 0.34990 -0.11265 -0.00973 0.14936  67  LEU   A N   
516  C CA  . LEU   A 67  ? 0.46118 0.39014 0.37231 -0.12540 -0.01125 0.15582  67  LEU   A CA  
517  C C   . LEU   A 67  ? 0.46251 0.39366 0.38727 -0.12089 -0.01038 0.14186  67  LEU   A C   
518  O O   . LEU   A 67  ? 0.41187 0.36517 0.34180 -0.11364 -0.00090 0.13203  67  LEU   A O   
519  C CB  . LEU   A 67  ? 0.51614 0.47496 0.43221 -0.13233 -0.00070 0.16280  67  LEU   A CB  
520  C CG  . LEU   A 67  ? 0.60749 0.56565 0.51482 -0.13792 -0.00181 0.17566  67  LEU   A CG  
521  C CD1 . LEU   A 67  ? 0.66819 0.59302 0.57383 -0.14255 -0.01660 0.18147  67  LEU   A CD1 
522  C CD2 . LEU   A 67  ? 0.63381 0.59993 0.52345 -0.13058 0.00320  0.17687  67  LEU   A CD2 
523  N N   . VAL   A 68  ? 0.47221 0.37916 0.40165 -0.12419 -0.02083 0.14014  68  VAL   A N   
524  C CA  . VAL   A 68  ? 0.45217 0.35892 0.39231 -0.11979 -0.02138 0.12685  68  VAL   A CA  
525  C C   . VAL   A 68  ? 0.51849 0.42342 0.46843 -0.13533 -0.02603 0.13460  68  VAL   A C   
526  O O   . VAL   A 68  ? 0.52964 0.41397 0.47698 -0.14207 -0.03580 0.14121  68  VAL   A O   
527  C CB  . VAL   A 68  ? 0.48951 0.36923 0.42471 -0.10722 -0.02984 0.11476  68  VAL   A CB  
528  C CG1 . VAL   A 68  ? 0.47262 0.35211 0.41648 -0.10365 -0.03044 0.10216  68  VAL   A CG1 
529  C CG2 . VAL   A 68  ? 0.42867 0.31418 0.35720 -0.09310 -0.02556 0.10851  68  VAL   A CG2 
530  N N   . GLN   A 69  ? 0.46818 0.39761 0.43127 -0.13788 -0.01909 0.13100  69  GLN   A N   
531  C CA  . GLN   A 69  ? 0.53117 0.46678 0.50744 -0.14927 -0.02273 0.13484  69  GLN   A CA  
532  C C   . GLN   A 69  ? 0.53482 0.46673 0.51831 -0.14780 -0.02616 0.12428  69  GLN   A C   
533  O O   . GLN   A 69  ? 0.44533 0.39511 0.43251 -0.13667 -0.01767 0.11383  69  GLN   A O   
534  C CB  . GLN   A 69  ? 0.55680 0.53002 0.54437 -0.15370 -0.01117 0.14182  69  GLN   A CB  
535  C CG  . GLN   A 69  ? 0.64581 0.62130 0.63955 -0.16553 -0.01558 0.15302  69  GLN   A CG  
536  C CD  . GLN   A 69  ? 0.68645 0.69855 0.68846 -0.16774 -0.00282 0.16047  69  GLN   A CD  
537  O OE1 . GLN   A 69  ? 0.73618 0.75774 0.72868 -0.16391 0.00516  0.16471  69  GLN   A OE1 
538  N NE2 . GLN   A 69  ? 0.67224 0.70509 0.69143 -0.17323 -0.00113 0.16177  69  GLN   A NE2 
539  N N   . ALA   A 70  ? 0.57758 0.48856 0.56277 -0.15379 -0.03836 0.12250  70  ALA   A N   
540  C CA  . ALA   A 70  ? 0.57006 0.47854 0.56155 -0.15413 -0.04295 0.11322  70  ALA   A CA  
541  C C   . ALA   A 70  ? 0.63512 0.56174 0.64171 -0.16539 -0.04513 0.11938  70  ALA   A C   
542  O O   . ALA   A 70  ? 0.67569 0.58442 0.68107 -0.17337 -0.05630 0.12301  70  ALA   A O   
543  C CB  . ALA   A 70  ? 0.58859 0.45803 0.56701 -0.14812 -0.05560 0.10269  70  ALA   A CB  
544  N N   . GLY   A 71  ? 0.58072 0.54286 0.60176 -0.16541 -0.03479 0.12071  71  GLY   A N   
545  C CA  . GLY   A 71  ? 0.61500 0.59905 0.65183 -0.17499 -0.03512 0.12840  71  GLY   A CA  
546  C C   . GLY   A 71  ? 0.64861 0.63915 0.68515 -0.18134 -0.03243 0.14109  71  GLY   A C   
547  O O   . GLY   A 71  ? 0.67442 0.68585 0.71050 -0.17687 -0.01998 0.14519  71  GLY   A O   
548  N N   . ASN   A 72  ? 0.64158 0.61376 0.67723 -0.19171 -0.04435 0.14726  72  ASN   A N   
549  C CA  . ASN   A 72  ? 0.67280 0.64630 0.70636 -0.19869 -0.04372 0.16007  72  ASN   A CA  
550  C C   . ASN   A 72  ? 0.75338 0.68909 0.76940 -0.19779 -0.05330 0.16033  72  ASN   A C   
551  O O   . ASN   A 72  ? 0.77402 0.70881 0.78554 -0.20189 -0.05233 0.17084  72  ASN   A O   
552  C CB  . ASN   A 72  ? 0.64241 0.62699 0.69027 -0.21252 -0.04978 0.16989  72  ASN   A CB  
553  N N   . VAL   A 73  ? 0.72199 0.62677 0.72779 -0.19176 -0.06248 0.14901  73  VAL   A N   
554  C CA  . VAL   A 73  ? 0.74079 0.60837 0.73032 -0.18834 -0.07199 0.14779  73  VAL   A CA  
555  C C   . VAL   A 73  ? 0.72075 0.59126 0.70025 -0.17828 -0.06255 0.14843  73  VAL   A C   
556  O O   . VAL   A 73  ? 0.65732 0.54629 0.63807 -0.17042 -0.05185 0.14305  73  VAL   A O   
557  C CB  . VAL   A 73  ? 0.76458 0.59949 0.74574 -0.18279 -0.08381 0.13391  73  VAL   A CB  
558  C CG1 . VAL   A 73  ? 0.80122 0.59742 0.76589 -0.17635 -0.09334 0.13125  73  VAL   A CG1 
559  C CG2 . VAL   A 73  ? 0.85671 0.68914 0.84620 -0.19307 -0.09406 0.13314  73  VAL   A CG2 
560  N N   . GLN   A 74  ? 0.72385 0.57621 0.69321 -0.17861 -0.06714 0.15541  74  GLN   A N   
561  C CA  . GLN   A 74  ? 0.67666 0.52878 0.63485 -0.16941 -0.06068 0.15699  74  GLN   A CA  
562  C C   . GLN   A 74  ? 0.69634 0.51047 0.64113 -0.15904 -0.07088 0.14877  74  GLN   A C   
563  O O   . GLN   A 74  ? 0.71063 0.49676 0.65022 -0.16142 -0.08293 0.15078  74  GLN   A O   
564  C CB  . GLN   A 74  ? 0.70327 0.56615 0.65948 -0.17624 -0.05750 0.17180  74  GLN   A CB  
565  C CG  . GLN   A 74  ? 0.70100 0.58778 0.65168 -0.16963 -0.04393 0.17447  74  GLN   A CG  
566  C CD  . GLN   A 74  ? 0.78741 0.71477 0.74990 -0.17361 -0.03028 0.17754  74  GLN   A CD  
567  O OE1 . GLN   A 74  ? 0.87372 0.81353 0.84901 -0.18370 -0.03106 0.18272  74  GLN   A OE1 
568  N NE2 . GLN   A 74  ? 0.66224 0.61045 0.62042 -0.16497 -0.01807 0.17409  74  GLN   A NE2 
569  N N   . LEU   A 75  ? 0.66095 0.47446 0.60055 -0.14695 -0.06611 0.13952  75  LEU   A N   
570  C CA  . LEU   A 75  ? 0.62751 0.40833 0.55529 -0.13449 -0.07429 0.13144  75  LEU   A CA  
571  C C   . LEU   A 75  ? 0.63198 0.40865 0.55040 -0.12939 -0.07377 0.13936  75  LEU   A C   
572  O O   . LEU   A 75  ? 0.64691 0.44917 0.56523 -0.13152 -0.06392 0.14705  75  LEU   A O   
573  C CB  . LEU   A 75  ? 0.60024 0.38247 0.52689 -0.12306 -0.06988 0.11843  75  LEU   A CB  
574  C CG  . LEU   A 75  ? 0.58061 0.36928 0.51502 -0.12339 -0.06928 0.10695  75  LEU   A CG  
575  C CD1 . LEU   A 75  ? 0.62962 0.45399 0.57749 -0.13468 -0.05978 0.11312  75  LEU   A CD1 
576  C CD2 . LEU   A 75  ? 0.49418 0.28604 0.42619 -0.10428 -0.06425 0.09004  75  LEU   A CD2 
577  N N   . ARG   A 76  ? 0.60241 0.34702 0.51234 -0.12156 -0.08462 0.13675  76  ARG   A N   
578  C CA  . ARG   A 76  ? 0.64618 0.38419 0.54751 -0.11597 -0.08641 0.14428  76  ARG   A CA  
579  C C   . ARG   A 76  ? 0.61409 0.34616 0.50965 -0.09902 -0.08532 0.13560  76  ARG   A C   
580  O O   . ARG   A 76  ? 0.59475 0.30680 0.48933 -0.08834 -0.09056 0.12337  76  ARG   A O   
581  C CB  . ARG   A 76  ? 0.65891 0.36701 0.55604 -0.11762 -0.09945 0.14830  76  ARG   A CB  
582  C CG  . ARG   A 76  ? 0.66899 0.37170 0.55811 -0.11384 -0.10198 0.15829  76  ARG   A CG  
583  C CD  . ARG   A 76  ? 0.68850 0.35905 0.57387 -0.11429 -0.11563 0.16112  76  ARG   A CD  
584  N NE  . ARG   A 76  ? 0.72522 0.39641 0.61586 -0.13137 -0.11897 0.16895  76  ARG   A NE  
585  C CZ  . ARG   A 76  ? 0.68152 0.36490 0.57261 -0.14395 -0.11734 0.18449  76  ARG   A CZ  
586  N NH1 . ARG   A 76  ? 0.65972 0.35425 0.54433 -0.14157 -0.11267 0.19375  76  ARG   A NH1 
587  N NH2 . ARG   A 76  ? 0.67650 0.36150 0.57437 -0.15922 -0.12079 0.19102  76  ARG   A NH2 
588  N N   . VAL   A 77  ? 0.60163 0.35212 0.49301 -0.09612 -0.07860 0.14159  77  VAL   A N   
589  C CA  . VAL   A 77  ? 0.55961 0.31727 0.45015 -0.07877 -0.07518 0.13100  77  VAL   A CA  
590  C C   . VAL   A 77  ? 0.57777 0.31001 0.46037 -0.06925 -0.08609 0.13523  77  VAL   A C   
591  O O   . VAL   A 77  ? 0.56317 0.29407 0.43900 -0.07472 -0.08907 0.14845  77  VAL   A O   
592  C CB  . VAL   A 77  ? 0.54340 0.33744 0.43475 -0.07904 -0.06246 0.13184  77  VAL   A CB  
593  C CG1 . VAL   A 77  ? 0.50228 0.30517 0.39471 -0.06206 -0.06011 0.12089  77  VAL   A CG1 
594  C CG2 . VAL   A 77  ? 0.52571 0.34379 0.42631 -0.08647 -0.05217 0.12710  77  VAL   A CG2 
595  N N   . ILE   A 78  ? 0.53225 0.24879 0.41724 -0.05337 -0.09077 0.12246  78  ILE   A N   
596  C CA  . ILE   A 78  ? 0.58283 0.27384 0.46261 -0.04177 -0.10186 0.12489  78  ILE   A CA  
597  C C   . ILE   A 78  ? 0.57517 0.28249 0.46001 -0.02362 -0.09802 0.11572  78  ILE   A C   
598  O O   . ILE   A 78  ? 0.59262 0.28256 0.47650 -0.01053 -0.10642 0.11523  78  ILE   A O   
599  C CB  . ILE   A 78  ? 0.60455 0.26275 0.48394 -0.03741 -0.11149 0.11755  78  ILE   A CB  
600  C CG1 . ILE   A 78  ? 0.61002 0.26473 0.49337 -0.02131 -0.10943 0.09967  78  ILE   A CG1 
601  C CG2 . ILE   A 78  ? 0.64472 0.29931 0.52490 -0.05557 -0.11248 0.12174  78  ILE   A CG2 
602  C CD1 . ILE   A 78  ? 0.64489 0.26764 0.52513 -0.01437 -0.11841 0.08993  78  ILE   A CD1 
603  N N   . GLY   A 79  ? 0.54754 0.28818 0.43864 -0.02285 -0.08613 0.10925  79  GLY   A N   
604  C CA  . GLY   A 79  ? 0.51486 0.27369 0.41226 -0.00847 -0.08282 0.10208  79  GLY   A CA  
605  C C   . GLY   A 79  ? 0.45235 0.24469 0.35585 -0.01142 -0.07027 0.09555  79  GLY   A C   
606  O O   . GLY   A 79  ? 0.47537 0.27517 0.38105 -0.01985 -0.06365 0.09200  79  GLY   A O   
607  N N   . HIS   A 80  ? 0.44230 0.25432 0.34887 -0.00485 -0.06788 0.09419  80  HIS   A N   
608  C CA  . HIS   A 80  ? 0.43622 0.27682 0.34814 -0.00715 -0.05730 0.08750  80  HIS   A CA  
609  C C   . HIS   A 80  ? 0.42343 0.27888 0.34433 0.00518  -0.05731 0.08106  80  HIS   A C   
610  O O   . HIS   A 80  ? 0.39309 0.24288 0.31349 0.01255  -0.06528 0.08557  80  HIS   A O   
611  C CB  . HIS   A 80  ? 0.40589 0.25948 0.30808 -0.01960 -0.05322 0.09615  80  HIS   A CB  
612  C CG  . HIS   A 80  ? 0.44266 0.29676 0.33542 -0.01848 -0.05940 0.10523  80  HIS   A CG  
613  N ND1 . HIS   A 80  ? 0.47935 0.31460 0.36115 -0.02309 -0.06777 0.11858  80  HIS   A ND1 
614  C CD2 . HIS   A 80  ? 0.41129 0.28162 0.30323 -0.01381 -0.05955 0.10335  80  HIS   A CD2 
615  C CE1 . HIS   A 80  ? 0.47220 0.31302 0.34608 -0.02076 -0.07244 0.12467  80  HIS   A CE1 
616  N NE2 . HIS   A 80  ? 0.46360 0.32561 0.34334 -0.01523 -0.06788 0.11516  80  HIS   A NE2 
617  N N   . SER   A 81  ? 0.38080 0.25583 0.31093 0.00689  -0.04899 0.07143  81  SER   A N   
618  C CA  . SER   A 81  ? 0.37002 0.26198 0.31039 0.01604  -0.04884 0.06648  81  SER   A CA  
619  C C   . SER   A 81  ? 0.36706 0.28047 0.31328 0.01210  -0.03972 0.05933  81  SER   A C   
620  O O   . SER   A 81  ? 0.38552 0.30004 0.33150 0.00640  -0.03312 0.05571  81  SER   A O   
621  C CB  . SER   A 81  ? 0.38702 0.27339 0.33840 0.02993  -0.05138 0.06098  81  SER   A CB  
622  O OG  . SER   A 81  ? 0.41419 0.30316 0.37122 0.03136  -0.04410 0.05203  81  SER   A OG  
623  N N   . MET   A 82  ? 0.33520 0.26472 0.28697 0.01502  -0.04067 0.05779  82  MET   A N   
624  C CA  . MET   A 82  ? 0.32990 0.27797 0.28845 0.01254  -0.03413 0.05106  82  MET   A CA  
625  C C   . MET   A 82  ? 0.31226 0.27006 0.28766 0.02125  -0.03235 0.04501  82  MET   A C   
626  O O   . MET   A 82  ? 0.34836 0.31024 0.33202 0.02906  -0.03790 0.04667  82  MET   A O   
627  C CB  . MET   A 82  ? 0.37807 0.33667 0.33155 0.00937  -0.03764 0.05290  82  MET   A CB  
628  C CG  . MET   A 82  ? 0.34468 0.31542 0.29805 0.00380  -0.03103 0.04686  82  MET   A CG  
629  S SD  . MET   A 82  ? 0.34602 0.32232 0.28418 -0.00154 -0.03453 0.04824  82  MET   A SD  
630  C CE  . MET   A 82  ? 0.36225 0.33938 0.30363 0.00422  -0.04733 0.05312  82  MET   A CE  
631  N N   . GLN   A 83  ? 0.31728 0.28095 0.29830 0.01985  -0.02460 0.03885  83  GLN   A N   
632  C CA  . GLN   A 83  ? 0.29248 0.26940 0.28878 0.02637  -0.02127 0.03395  83  GLN   A CA  
633  C C   . GLN   A 83  ? 0.25964 0.25065 0.26005 0.01989  -0.01670 0.03063  83  GLN   A C   
634  O O   . GLN   A 83  ? 0.23706 0.22628 0.23328 0.01461  -0.01107 0.02785  83  GLN   A O   
635  C CB  . GLN   A 83  ? 0.28342 0.25273 0.28120 0.03171  -0.01695 0.02985  83  GLN   A CB  
636  C CG  . GLN   A 83  ? 0.32173 0.30744 0.33353 0.03752  -0.01161 0.02550  83  GLN   A CG  
637  C CD  . GLN   A 83  ? 0.32820 0.30679 0.33836 0.04369  -0.00711 0.02057  83  GLN   A CD  
638  O OE1 . GLN   A 83  ? 0.34514 0.30615 0.34367 0.04090  -0.00770 0.01922  83  GLN   A OE1 
639  N NE2 . GLN   A 83  ? 0.30976 0.30245 0.33128 0.05207  -0.00297 0.01811  83  GLN   A NE2 
640  N N   . ASN   A 84  ? 0.24622 0.25019 0.25489 0.02007  -0.02027 0.03122  84  ASN   A N   
641  C CA  . ASN   A 84  ? 0.23092 0.24455 0.24212 0.01368  -0.01830 0.02814  84  ASN   A CA  
642  C C   . ASN   A 84  ? 0.22997 0.23557 0.22537 0.00652  -0.01618 0.02712  84  ASN   A C   
643  O O   . ASN   A 84  ? 0.23954 0.23869 0.22261 0.00458  -0.02038 0.03051  84  ASN   A O   
644  C CB  . ASN   A 84  ? 0.22875 0.25145 0.25216 0.01479  -0.01163 0.02475  84  ASN   A CB  
645  C CG  . ASN   A 84  ? 0.23746 0.27176 0.27669 0.02245  -0.01220 0.02647  84  ASN   A CG  
646  O OD1 . ASN   A 84  ? 0.25476 0.29899 0.30328 0.02363  -0.01818 0.02940  84  ASN   A OD1 
647  N ND2 . ASN   A 84  ? 0.25049 0.28401 0.29225 0.02824  -0.00639 0.02477  84  ASN   A ND2 
648  N N   . CYS   A 85  ? 0.21534 0.22229 0.21074 0.00297  -0.00951 0.02323  85  CYS   A N   
649  C CA  . CYS   A 85  ? 0.22188 0.22488 0.20456 -0.00256 -0.00657 0.02233  85  CYS   A CA  
650  C C   . CYS   A 85  ? 0.22926 0.22414 0.20553 -0.00453 -0.00243 0.02464  85  CYS   A C   
651  O O   . CYS   A 85  ? 0.24719 0.24254 0.21620 -0.00915 0.00163  0.02446  85  CYS   A O   
652  C CB  . CYS   A 85  ? 0.21072 0.22021 0.19717 -0.00514 -0.00282 0.01691  85  CYS   A CB  
653  S SG  . CYS   A 85  ? 0.24815 0.26388 0.24004 -0.00543 -0.00988 0.01442  85  CYS   A SG  
654  N N   . VAL   A 86  ? 0.21765 0.20514 0.19648 -0.00108 -0.00376 0.02679  86  VAL   A N   
655  C CA  . VAL   A 86  ? 0.21728 0.19446 0.18965 -0.00431 -0.00202 0.02928  86  VAL   A CA  
656  C C   . VAL   A 86  ? 0.26799 0.23270 0.23200 -0.00374 -0.00816 0.03565  86  VAL   A C   
657  O O   . VAL   A 86  ? 0.28830 0.25097 0.25468 0.00226  -0.01365 0.03711  86  VAL   A O   
658  C CB  . VAL   A 86  ? 0.25429 0.22813 0.23288 -0.00179 0.00067  0.02582  86  VAL   A CB  
659  C CG1 . VAL   A 86  ? 0.25324 0.23788 0.23791 -0.00425 0.00659  0.02144  86  VAL   A CG1 
660  C CG2 . VAL   A 86  ? 0.36683 0.33913 0.35192 0.00716  -0.00198 0.02425  86  VAL   A CG2 
661  N N   . LEU   A 87  ? 0.25256 0.20982 0.20765 -0.01040 -0.00755 0.04045  87  LEU   A N   
662  C CA  . LEU   A 87  ? 0.32392 0.26591 0.27056 -0.01163 -0.01363 0.04797  87  LEU   A CA  
663  C C   . LEU   A 87  ? 0.31114 0.23828 0.25970 -0.01096 -0.01526 0.04711  87  LEU   A C   
664  O O   . LEU   A 87  ? 0.31167 0.24112 0.26328 -0.01494 -0.01091 0.04392  87  LEU   A O   
665  C CB  . LEU   A 87  ? 0.32873 0.27233 0.26403 -0.02075 -0.01206 0.05531  87  LEU   A CB  
666  C CG  . LEU   A 87  ? 0.43252 0.36362 0.35652 -0.02333 -0.01875 0.06555  87  LEU   A CG  
667  C CD1 . LEU   A 87  ? 0.50243 0.43362 0.42506 -0.01595 -0.02524 0.06590  87  LEU   A CD1 
668  C CD2 . LEU   A 87  ? 0.43455 0.37389 0.34815 -0.03264 -0.01406 0.07211  87  LEU   A CD2 
669  N N   . LYS   A 88  ? 0.33237 0.24380 0.27906 -0.00503 -0.02227 0.04925  88  LYS   A N   
670  C CA  . LYS   A 88  ? 0.33152 0.22382 0.27699 -0.00314 -0.02579 0.04762  88  LYS   A CA  
671  C C   . LYS   A 88  ? 0.39602 0.26851 0.33140 -0.00888 -0.03324 0.05741  88  LYS   A C   
672  O O   . LYS   A 88  ? 0.36456 0.22994 0.29644 -0.00439 -0.03934 0.06260  88  LYS   A O   
673  C CB  . LYS   A 88  ? 0.37717 0.26597 0.32893 0.01065  -0.02767 0.04092  88  LYS   A CB  
674  C CG  . LYS   A 88  ? 0.38709 0.29515 0.34885 0.01490  -0.02015 0.03282  88  LYS   A CG  
675  C CD  . LYS   A 88  ? 0.42044 0.32639 0.38779 0.02816  -0.02033 0.02652  88  LYS   A CD  
676  C CE  . LYS   A 88  ? 0.42693 0.33678 0.40002 0.03756  -0.02453 0.02925  88  LYS   A CE  
677  N NZ  . LYS   A 88  ? 0.44958 0.36397 0.43079 0.05135  -0.02229 0.02292  88  LYS   A NZ  
678  N N   . LEU   A 89  ? 0.34543 0.20967 0.27692 -0.01942 -0.03341 0.06098  89  LEU   A N   
679  C CA  . LEU   A 89  ? 0.39084 0.23547 0.31357 -0.02734 -0.04078 0.07175  89  LEU   A CA  
680  C C   . LEU   A 89  ? 0.39186 0.20945 0.31273 -0.02462 -0.04840 0.06831  89  LEU   A C   
681  O O   . LEU   A 89  ? 0.42086 0.23700 0.34430 -0.02776 -0.04665 0.06226  89  LEU   A O   
682  C CB  . LEU   A 89  ? 0.37274 0.22802 0.29338 -0.04252 -0.03629 0.07993  89  LEU   A CB  
683  C CG  . LEU   A 89  ? 0.38925 0.27150 0.31031 -0.04374 -0.02755 0.08046  89  LEU   A CG  
684  C CD1 . LEU   A 89  ? 0.37431 0.27042 0.29551 -0.05652 -0.02119 0.08666  89  LEU   A CD1 
685  C CD2 . LEU   A 89  ? 0.39162 0.27231 0.30404 -0.04046 -0.03158 0.08715  89  LEU   A CD2 
686  N N   . LYS   A 90  ? 0.44691 0.24231 0.36264 -0.01801 -0.05753 0.07159  90  LYS   A N   
687  C CA  . LYS   A 90  ? 0.45088 0.21566 0.36228 -0.01482 -0.06632 0.06816  90  LYS   A CA  
688  C C   . LYS   A 90  ? 0.50333 0.25052 0.40834 -0.03135 -0.07283 0.07934  90  LYS   A C   
689  O O   . LYS   A 90  ? 0.48997 0.23658 0.39062 -0.03939 -0.07536 0.09265  90  LYS   A O   
690  C CB  . LYS   A 90  ? 0.50875 0.25569 0.41807 0.00027  -0.07401 0.06717  90  LYS   A CB  
691  C CG  . LYS   A 90  ? 0.55729 0.26792 0.45989 0.00531  -0.08439 0.06314  90  LYS   A CG  
692  C CD  . LYS   A 90  ? 0.64354 0.35153 0.54932 0.02541  -0.08311 0.04897  90  LYS   A CD  
693  C CE  . LYS   A 90  ? 0.67096 0.34008 0.56736 0.03183  -0.09377 0.04316  90  LYS   A CE  
694  N NZ  . LYS   A 90  ? 0.79548 0.45156 0.69258 0.05212  -0.09882 0.03944  90  LYS   A NZ  
695  N N   . VAL   A 91  ? 0.52767 0.26151 0.43196 -0.03721 -0.07586 0.07464  91  VAL   A N   
696  C CA  . VAL   A 91  ? 0.54764 0.26564 0.44833 -0.05466 -0.08292 0.08558  91  VAL   A CA  
697  C C   . VAL   A 91  ? 0.59610 0.27280 0.48891 -0.05132 -0.09678 0.08199  91  VAL   A C   
698  O O   . VAL   A 91  ? 0.56676 0.23079 0.45697 -0.03517 -0.09876 0.06873  91  VAL   A O   
699  C CB  . VAL   A 91  ? 0.53233 0.27109 0.44007 -0.06785 -0.07628 0.08526  91  VAL   A CB  
700  C CG1 . VAL   A 91  ? 0.48704 0.26349 0.40113 -0.07053 -0.06331 0.08944  91  VAL   A CG1 
701  C CG2 . VAL   A 91  ? 0.52271 0.26051 0.43244 -0.06020 -0.07494 0.06940  91  VAL   A CG2 
702  N N   . ASP   A 92  ? 0.58945 0.24733 0.47885 -0.06609 -0.10586 0.09363  92  ASP   A N   
703  C CA  . ASP   A 92  ? 0.65419 0.28127 0.53853 -0.06251 -0.11756 0.08829  92  ASP   A CA  
704  C C   . ASP   A 92  ? 0.66765 0.28444 0.55110 -0.06588 -0.12136 0.07690  92  ASP   A C   
705  O O   . ASP   A 92  ? 0.70314 0.29327 0.58044 -0.06179 -0.13137 0.07026  92  ASP   A O   
706  C CB  . ASP   A 92  ? 0.72350 0.34487 0.60779 -0.07542 -0.12377 0.10293  92  ASP   A CB  
707  C CG  . ASP   A 92  ? 0.71541 0.35862 0.60699 -0.09633 -0.11967 0.11365  92  ASP   A CG  
708  O OD1 . ASP   A 92  ? 0.72465 0.38688 0.62197 -0.10103 -0.11260 0.10947  92  ASP   A OD1 
709  O OD2 . ASP   A 92  ? 0.75167 0.39398 0.64395 -0.10763 -0.12347 0.12651  92  ASP   A OD2 
710  N N   . THR   A 93  ? 0.61841 0.25543 0.50714 -0.07306 -0.11424 0.07445  93  THR   A N   
711  C CA  . THR   A 93  ? 0.64705 0.27771 0.53506 -0.07784 -0.11822 0.06477  93  THR   A CA  
712  C C   . THR   A 93  ? 0.60926 0.25235 0.49693 -0.06685 -0.10997 0.05146  93  THR   A C   
713  O O   . THR   A 93  ? 0.57760 0.25698 0.47475 -0.06592 -0.09680 0.05363  93  THR   A O   
714  C CB  . THR   A 93  ? 0.63473 0.28478 0.53279 -0.09940 -0.11762 0.07590  93  THR   A CB  
715  O OG1 . THR   A 93  ? 0.73481 0.37605 0.63356 -0.10900 -0.12466 0.08792  93  THR   A OG1 
716  C CG2 . THR   A 93  ? 0.59933 0.24452 0.49718 -0.10436 -0.12285 0.06624  93  THR   A CG2 
717  N N   . ALA   A 94  ? 0.60088 0.22349 0.47919 -0.05649 -0.11521 0.03605  94  ALA   A N   
718  C CA  . ALA   A 94  ? 0.57107 0.21622 0.45078 -0.04600 -0.10513 0.02272  94  ALA   A CA  
719  C C   . ALA   A 94  ? 0.56589 0.22599 0.45118 -0.06167 -0.10493 0.02390  94  ALA   A C   
720  O O   . ALA   A 94  ? 0.57892 0.21837 0.46123 -0.07589 -0.11692 0.02749  94  ALA   A O   
721  C CB  . ALA   A 94  ? 0.63548 0.25509 0.50112 -0.02755 -0.10971 0.00580  94  ALA   A CB  
722  N N   . ASN   A 95  ? 0.50620 0.20211 0.40066 -0.05950 -0.09218 0.02165  95  ASN   A N   
723  C CA  . ASN   A 95  ? 0.54152 0.25646 0.44407 -0.07330 -0.09104 0.02407  95  ASN   A CA  
724  C C   . ASN   A 95  ? 0.51930 0.21136 0.41020 -0.07329 -0.10150 0.01251  95  ASN   A C   
725  O O   . ASN   A 95  ? 0.53209 0.22111 0.41337 -0.05795 -0.09852 -0.00110 95  ASN   A O   
726  C CB  . ASN   A 95  ? 0.44113 0.19550 0.35438 -0.06778 -0.07586 0.02251  95  ASN   A CB  
727  C CG  . ASN   A 95  ? 0.48833 0.26472 0.41187 -0.08048 -0.07432 0.02563  95  ASN   A CG  
728  O OD1 . ASN   A 95  ? 0.47612 0.24023 0.39929 -0.09349 -0.08471 0.02829  95  ASN   A OD1 
729  N ND2 . ASN   A 95  ? 0.39725 0.20635 0.33109 -0.07690 -0.06205 0.02588  95  ASN   A ND2 
730  N N   . PRO   A 96  ? 0.55024 0.22629 0.44099 -0.09025 -0.11408 0.01756  96  PRO   A N   
731  C CA  . PRO   A 96  ? 0.57551 0.22735 0.45284 -0.09062 -0.12593 0.00554  96  PRO   A CA  
732  C C   . PRO   A 96  ? 0.59447 0.27226 0.47414 -0.08789 -0.11922 -0.00181 96  PRO   A C   
733  O O   . PRO   A 96  ? 0.64418 0.30482 0.50882 -0.08267 -0.12625 -0.01466 96  PRO   A O   
734  C CB  . PRO   A 96  ? 0.61993 0.26697 0.50440 -0.10919 -0.13703 0.01617  96  PRO   A CB  
735  C CG  . PRO   A 96  ? 0.60743 0.28341 0.51111 -0.12197 -0.12912 0.03360  96  PRO   A CG  
736  C CD  . PRO   A 96  ? 0.54345 0.22375 0.44612 -0.11041 -0.11833 0.03489  96  PRO   A CD  
737  N N   . LYS   A 97  ? 0.54418 0.26159 0.44086 -0.09064 -0.10623 0.00574  97  LYS   A N   
738  C CA  . LYS   A 97  ? 0.53943 0.28251 0.44009 -0.08825 -0.09987 0.00068  97  LYS   A CA  
739  C C   . LYS   A 97  ? 0.51786 0.27828 0.41653 -0.06971 -0.08566 -0.00647 97  LYS   A C   
740  O O   . LYS   A 97  ? 0.48896 0.27615 0.39482 -0.06808 -0.07774 -0.00713 97  LYS   A O   
741  C CB  . LYS   A 97  ? 0.53688 0.31230 0.45886 -0.10349 -0.09587 0.01359  97  LYS   A CB  
742  C CG  . LYS   A 97  ? 0.60252 0.36834 0.53177 -0.12394 -0.10823 0.02434  97  LYS   A CG  
743  C CD  . LYS   A 97  ? 0.61330 0.41698 0.56599 -0.13598 -0.10036 0.03844  97  LYS   A CD  
744  C CE  . LYS   A 97  ? 0.77737 0.57901 0.74050 -0.15743 -0.11278 0.04892  97  LYS   A CE  
745  N NZ  . LYS   A 97  ? 0.82545 0.63007 0.78853 -0.16113 -0.12123 0.04244  97  LYS   A NZ  
746  N N   . THR   A 98  ? 0.53833 0.28482 0.42889 -0.05617 -0.08278 -0.01081 98  THR   A N   
747  C CA  . THR   A 98  ? 0.50392 0.26748 0.39414 -0.03925 -0.07005 -0.01679 98  THR   A CA  
748  C C   . THR   A 98  ? 0.50933 0.27363 0.38784 -0.03099 -0.06941 -0.02859 98  THR   A C   
749  O O   . THR   A 98  ? 0.50207 0.23858 0.36289 -0.02689 -0.07875 -0.03835 98  THR   A O   
750  C CB  . THR   A 98  ? 0.50966 0.25618 0.39305 -0.02549 -0.06925 -0.02006 98  THR   A CB  
751  O OG1 . THR   A 98  ? 0.51301 0.25703 0.40487 -0.03319 -0.07089 -0.00840 98  THR   A OG1 
752  C CG2 . THR   A 98  ? 0.48232 0.25079 0.36892 -0.00973 -0.05617 -0.02448 98  THR   A CG2 
753  N N   . PRO   A 99  ? 0.48971 0.28324 0.37579 -0.02798 -0.05916 -0.02822 99  PRO   A N   
754  C CA  . PRO   A 99  ? 0.50180 0.29742 0.37534 -0.01946 -0.05763 -0.03817 99  PRO   A CA  
755  C C   . PRO   A 99  ? 0.48737 0.28267 0.35292 -0.00059 -0.04921 -0.04572 99  PRO   A C   
756  O O   . PRO   A 99  ? 0.49336 0.29121 0.36636 0.00537  -0.04416 -0.04243 99  PRO   A O   
757  C CB  . PRO   A 99  ? 0.45254 0.28074 0.34076 -0.02534 -0.05020 -0.03160 99  PRO   A CB  
758  C CG  . PRO   A 99  ? 0.45166 0.29750 0.35733 -0.02600 -0.04139 -0.02257 99  PRO   A CG  
759  C CD  . PRO   A 99  ? 0.47319 0.29824 0.37841 -0.03149 -0.04850 -0.01868 99  PRO   A CD  
760  N N   . LYS   A 100 ? 0.49019 0.28328 0.34020 0.00880  -0.04804 -0.05556 100 LYS   A N   
761  C CA  . LYS   A 100 ? 0.48964 0.29436 0.33652 0.02598  -0.03667 -0.06042 100 LYS   A CA  
762  C C   . LYS   A 100 ? 0.46027 0.29882 0.32787 0.02387  -0.02506 -0.05060 100 LYS   A C   
763  O O   . LYS   A 100 ? 0.46095 0.31631 0.33611 0.01454  -0.02384 -0.04533 100 LYS   A O   
764  C CB  . LYS   A 100 ? 0.55510 0.35666 0.38137 0.03504  -0.03602 -0.07113 100 LYS   A CB  
765  C CG  . LYS   A 100 ? 0.59967 0.42496 0.42709 0.04954  -0.02168 -0.07248 100 LYS   A CG  
766  C CD  . LYS   A 100 ? 0.75724 0.57361 0.55952 0.06319  -0.02048 -0.08505 100 LYS   A CD  
767  C CE  . LYS   A 100 ? 0.88413 0.70245 0.68420 0.08248  -0.01154 -0.09049 100 LYS   A CE  
768  N NZ  . LYS   A 100 ? 0.82710 0.68226 0.64389 0.08702  0.00336  -0.08244 100 LYS   A NZ  
769  N N   . TYR   A 101 ? 0.46458 0.31220 0.34188 0.03227  -0.01768 -0.04799 101 TYR   A N   
770  C CA  . TYR   A 101 ? 0.42789 0.30373 0.32464 0.02884  -0.00887 -0.03881 101 TYR   A CA  
771  C C   . TYR   A 101 ? 0.41965 0.30997 0.32213 0.04225  0.00060  -0.03930 101 TYR   A C   
772  O O   . TYR   A 101 ? 0.42798 0.30666 0.32287 0.05450  0.00045  -0.04532 101 TYR   A O   
773  C CB  . TYR   A 101 ? 0.37773 0.25314 0.28761 0.01742  -0.01224 -0.03002 101 TYR   A CB  
774  C CG  . TYR   A 101 ? 0.40722 0.27005 0.31844 0.02270  -0.01428 -0.02893 101 TYR   A CG  
775  C CD1 . TYR   A 101 ? 0.44790 0.28162 0.34853 0.02136  -0.02436 -0.03157 101 TYR   A CD1 
776  C CD2 . TYR   A 101 ? 0.40227 0.28130 0.32562 0.02816  -0.00751 -0.02452 101 TYR   A CD2 
777  C CE1 . TYR   A 101 ? 0.44258 0.26334 0.34416 0.02641  -0.02722 -0.02960 101 TYR   A CE1 
778  C CE2 . TYR   A 101 ? 0.41715 0.28498 0.34167 0.03308  -0.01052 -0.02279 101 TYR   A CE2 
779  C CZ  . TYR   A 101 ? 0.45063 0.28927 0.36417 0.03249  -0.02019 -0.02506 101 TYR   A CZ  
780  O OH  . TYR   A 101 ? 0.51765 0.34364 0.43204 0.03765  -0.02410 -0.02243 101 TYR   A OH  
781  N N   . LYS   A 102 ? 0.39075 0.30697 0.30802 0.03963  0.00832  -0.03254 102 LYS   A N   
782  C CA  . LYS   A 102 ? 0.38952 0.32426 0.31809 0.04830  0.01658  -0.02986 102 LYS   A CA  
783  C C   . LYS   A 102 ? 0.32975 0.27980 0.27598 0.03922  0.01832  -0.02094 102 LYS   A C   
784  O O   . LYS   A 102 ? 0.32203 0.27495 0.27157 0.02843  0.01648  -0.01737 102 LYS   A O   
785  C CB  . LYS   A 102 ? 0.42202 0.37465 0.34803 0.05564  0.02498  -0.03150 102 LYS   A CB  
786  C CG  . LYS   A 102 ? 0.57607 0.51726 0.48361 0.06845  0.02566  -0.04129 102 LYS   A CG  
787  C CD  . LYS   A 102 ? 0.63594 0.60065 0.54437 0.07794  0.03660  -0.04084 102 LYS   A CD  
788  C CE  . LYS   A 102 ? 0.68747 0.65067 0.57717 0.07852  0.03744  -0.04549 102 LYS   A CE  
789  N NZ  . LYS   A 102 ? 0.68369 0.67358 0.57583 0.08558  0.04907  -0.04206 102 LYS   A NZ  
790  N N   . PHE   A 103 ? 0.30155 0.26166 0.25895 0.04426  0.02149  -0.01774 103 PHE   A N   
791  C CA  . PHE   A 103 ? 0.28358 0.26012 0.25637 0.03759  0.02373  -0.01055 103 PHE   A CA  
792  C C   . PHE   A 103 ? 0.29069 0.28957 0.27226 0.04121  0.03121  -0.00823 103 PHE   A C   
793  O O   . PHE   A 103 ? 0.33286 0.33938 0.31601 0.05148  0.03533  -0.00969 103 PHE   A O   
794  C CB  . PHE   A 103 ? 0.28250 0.25647 0.26203 0.03940  0.02089  -0.00761 103 PHE   A CB  
795  C CG  . PHE   A 103 ? 0.29643 0.25104 0.26934 0.03317  0.01372  -0.00671 103 PHE   A CG  
796  C CD1 . PHE   A 103 ? 0.30329 0.24772 0.26884 0.02449  0.01050  -0.00739 103 PHE   A CD1 
797  C CD2 . PHE   A 103 ? 0.29755 0.24585 0.27272 0.03528  0.00985  -0.00377 103 PHE   A CD2 
798  C CE1 . PHE   A 103 ? 0.30167 0.23057 0.26273 0.01744  0.00420  -0.00482 103 PHE   A CE1 
799  C CE2 . PHE   A 103 ? 0.33643 0.26763 0.30519 0.02860  0.00346  -0.00113 103 PHE   A CE2 
800  C CZ  . PHE   A 103 ? 0.32553 0.24754 0.28768 0.01929  0.00099  -0.00136 103 PHE   A CZ  
801  N N   . VAL   A 104 ? 0.25330 0.26315 0.24138 0.03305  0.03296  -0.00402 104 VAL   A N   
802  C CA  . VAL   A 104 ? 0.25826 0.28833 0.25586 0.03422  0.03901  0.00017  104 VAL   A CA  
803  C C   . VAL   A 104 ? 0.24634 0.28531 0.25793 0.02621  0.03797  0.00592  104 VAL   A C   
804  O O   . VAL   A 104 ? 0.26485 0.29608 0.27601 0.01923  0.03410  0.00609  104 VAL   A O   
805  C CB  . VAL   A 104 ? 0.32882 0.36238 0.31815 0.03334  0.04187  -0.00026 104 VAL   A CB  
806  C CG1 . VAL   A 104 ? 0.31297 0.33536 0.28481 0.04160  0.04202  -0.00762 104 VAL   A CG1 
807  C CG2 . VAL   A 104 ? 0.36791 0.39630 0.35683 0.02340  0.03790  0.00139  104 VAL   A CG2 
808  N N   . ARG   A 105 ? 0.24681 0.30251 0.27089 0.02738  0.04133  0.01061  105 ARG   A N   
809  C CA  . ARG   A 105 ? 0.21801 0.28141 0.25456 0.01971  0.03972  0.01568  105 ARG   A CA  
810  C C   . ARG   A 105 ? 0.26797 0.34037 0.30698 0.01609  0.04296  0.01989  105 ARG   A C   
811  O O   . ARG   A 105 ? 0.26509 0.35117 0.30773 0.01952  0.04799  0.02345  105 ARG   A O   
812  C CB  . ARG   A 105 ? 0.27213 0.34724 0.32231 0.02143  0.03911  0.01919  105 ARG   A CB  
813  C CG  . ARG   A 105 ? 0.23314 0.30916 0.29255 0.01322  0.03439  0.02207  105 ARG   A CG  
814  C CD  . ARG   A 105 ? 0.28941 0.37602 0.36177 0.01396  0.03163  0.02536  105 ARG   A CD  
815  N NE  . ARG   A 105 ? 0.26191 0.34935 0.34229 0.00556  0.02666  0.02787  105 ARG   A NE  
816  C CZ  . ARG   A 105 ? 0.27495 0.35031 0.34958 0.00181  0.02137  0.02449  105 ARG   A CZ  
817  N NH1 . ARG   A 105 ? 0.21379 0.27734 0.27636 0.00446  0.02056  0.02020  105 ARG   A NH1 
818  N NH2 . ARG   A 105 ? 0.19560 0.27036 0.27603 -0.00478 0.01665  0.02557  105 ARG   A NH2 
819  N N   . ILE   A 106 ? 0.22929 0.29502 0.26656 0.00960  0.04030  0.02018  106 ILE   A N   
820  C CA  . ILE   A 106 ? 0.27522 0.34694 0.31351 0.00642  0.04218  0.02473  106 ILE   A CA  
821  C C   . ILE   A 106 ? 0.26265 0.34383 0.31574 0.00133  0.04145  0.03147  106 ILE   A C   
822  O O   . ILE   A 106 ? 0.24617 0.32661 0.30757 -0.00095 0.03806  0.03130  106 ILE   A O   
823  C CB  . ILE   A 106 ? 0.27174 0.33323 0.30328 0.00264  0.03905  0.02276  106 ILE   A CB  
824  C CG1 . ILE   A 106 ? 0.24281 0.29746 0.27975 -0.00140 0.03493  0.02102  106 ILE   A CG1 
825  C CG2 . ILE   A 106 ? 0.31111 0.36429 0.32803 0.00604  0.03884  0.01750  106 ILE   A CG2 
826  C CD1 . ILE   A 106 ? 0.28824 0.33871 0.32519 -0.00503 0.03257  0.02141  106 ILE   A CD1 
827  N N   . GLN   A 107 ? 0.25441 0.34327 0.30976 -0.00115 0.04370  0.03784  107 GLN   A N   
828  C CA  . GLN   A 107 ? 0.25083 0.34739 0.32000 -0.00735 0.04231  0.04589  107 GLN   A CA  
829  C C   . GLN   A 107 ? 0.21840 0.30309 0.28899 -0.01285 0.03674  0.04621  107 GLN   A C   
830  O O   . GLN   A 107 ? 0.23547 0.31182 0.29696 -0.01166 0.03592  0.04290  107 GLN   A O   
831  C CB  . GLN   A 107 ? 0.24847 0.36051 0.31903 -0.00725 0.04810  0.05434  107 GLN   A CB  
832  C CG  . GLN   A 107 ? 0.31130 0.43841 0.38259 -0.00028 0.05472  0.05433  107 GLN   A CG  
833  C CD  . GLN   A 107 ? 0.35587 0.49372 0.44497 -0.00253 0.05314  0.05797  107 GLN   A CD  
834  O OE1 . GLN   A 107 ? 0.39100 0.53527 0.49387 -0.01065 0.05041  0.06623  107 GLN   A OE1 
835  N NE2 . GLN   A 107 ? 0.41384 0.55281 0.50301 0.00425  0.05368  0.05225  107 GLN   A NE2 
836  N N   . PRO   A 108 ? 0.23848 0.32162 0.32071 -0.01849 0.03212  0.04971  108 PRO   A N   
837  C CA  . PRO   A 108 ? 0.23820 0.30896 0.32166 -0.02207 0.02681  0.04973  108 PRO   A CA  
838  C C   . PRO   A 108 ? 0.20284 0.27551 0.28294 -0.02300 0.02835  0.05628  108 PRO   A C   
839  O O   . PRO   A 108 ? 0.26468 0.34956 0.34583 -0.02412 0.03245  0.06401  108 PRO   A O   
840  C CB  . PRO   A 108 ? 0.25686 0.32619 0.35322 -0.02827 0.02123  0.05353  108 PRO   A CB  
841  C CG  . PRO   A 108 ? 0.26322 0.35014 0.36781 -0.02971 0.02486  0.06008  108 PRO   A CG  
842  C CD  . PRO   A 108 ? 0.23191 0.32472 0.32735 -0.02190 0.03082  0.05430  108 PRO   A CD  
843  N N   . GLY   A 109 ? 0.22157 0.28374 0.29725 -0.02196 0.02534  0.05347  109 GLY   A N   
844  C CA  . GLY   A 109 ? 0.23061 0.29341 0.30192 -0.02228 0.02535  0.05928  109 GLY   A CA  
845  C C   . GLY   A 109 ? 0.27730 0.34276 0.33543 -0.01781 0.02855  0.05537  109 GLY   A C   
846  O O   . GLY   A 109 ? 0.26978 0.33346 0.32307 -0.01764 0.02664  0.05823  109 GLY   A O   
847  N N   . GLN   A 110 ? 0.25293 0.32146 0.30502 -0.01433 0.03225  0.04913  110 GLN   A N   
848  C CA  . GLN   A 110 ? 0.25663 0.32408 0.29539 -0.01053 0.03374  0.04404  110 GLN   A CA  
849  C C   . GLN   A 110 ? 0.26872 0.32701 0.30689 -0.01041 0.02967  0.03794  110 GLN   A C   
850  O O   . GLN   A 110 ? 0.23955 0.29331 0.28564 -0.01132 0.02765  0.03543  110 GLN   A O   
851  C CB  . GLN   A 110 ? 0.26999 0.34129 0.30327 -0.00632 0.03818  0.03946  110 GLN   A CB  
852  C CG  . GLN   A 110 ? 0.32736 0.41141 0.35784 -0.00407 0.04403  0.04475  110 GLN   A CG  
853  C CD  . GLN   A 110 ? 0.45576 0.54332 0.47765 -0.00503 0.04461  0.05055  110 GLN   A CD  
854  O OE1 . GLN   A 110 ? 0.46694 0.54842 0.47568 -0.00312 0.04265  0.04641  110 GLN   A OE1 
855  N NE2 . GLN   A 110 ? 0.51832 0.61537 0.54752 -0.00883 0.04633  0.06092  110 GLN   A NE2 
856  N N   . THR   A 111 ? 0.24986 0.30635 0.27822 -0.00935 0.02838  0.03564  111 THR   A N   
857  C CA  . THR   A 111 ? 0.25166 0.30325 0.28127 -0.01010 0.02461  0.03170  111 THR   A CA  
858  C C   . THR   A 111 ? 0.22803 0.27554 0.24870 -0.00931 0.02469  0.02532  111 THR   A C   
859  O O   . THR   A 111 ? 0.24671 0.29337 0.25745 -0.00697 0.02682  0.02331  111 THR   A O   
860  C CB  . THR   A 111 ? 0.25207 0.30491 0.28066 -0.01113 0.02043  0.03567  111 THR   A CB  
861  O OG1 . THR   A 111 ? 0.26444 0.31917 0.27956 -0.01056 0.02069  0.03711  111 THR   A OG1 
862  C CG2 . THR   A 111 ? 0.25519 0.30866 0.29400 -0.01181 0.01875  0.04215  111 THR   A CG2 
863  N N   . PHE   A 112 ? 0.18562 0.23062 0.21002 -0.01106 0.02225  0.02248  112 PHE   A N   
864  C CA  . PHE   A 112 ? 0.24060 0.28023 0.25798 -0.01213 0.02097  0.01787  112 PHE   A CA  
865  C C   . PHE   A 112 ? 0.21661 0.25824 0.24076 -0.01552 0.01800  0.01791  112 PHE   A C   
866  O O   . PHE   A 112 ? 0.24465 0.29175 0.27935 -0.01513 0.01834  0.01998  112 PHE   A O   
867  C CB  . PHE   A 112 ? 0.21332 0.24908 0.22962 -0.01038 0.02396  0.01484  112 PHE   A CB  
868  C CG  . PHE   A 112 ? 0.23639 0.27449 0.26265 -0.01067 0.02560  0.01525  112 PHE   A CG  
869  C CD1 . PHE   A 112 ? 0.25997 0.30133 0.29232 -0.00930 0.02729  0.01746  112 PHE   A CD1 
870  C CD2 . PHE   A 112 ? 0.20198 0.23877 0.23042 -0.01263 0.02518  0.01350  112 PHE   A CD2 
871  C CE1 . PHE   A 112 ? 0.26568 0.30665 0.30480 -0.00952 0.02741  0.01651  112 PHE   A CE1 
872  C CE2 . PHE   A 112 ? 0.21435 0.25269 0.24860 -0.01200 0.02675  0.01280  112 PHE   A CE2 
873  C CZ  . PHE   A 112 ? 0.21834 0.25753 0.25712 -0.01022 0.02734  0.01356  112 PHE   A CZ  
874  N N   . SER   A 113 ? 0.17648 0.21375 0.19483 -0.01868 0.01480  0.01577  113 SER   A N   
875  C CA  . SER   A 113 ? 0.17653 0.21833 0.20258 -0.02311 0.01223  0.01697  113 SER   A CA  
876  C C   . SER   A 113 ? 0.19394 0.23449 0.22266 -0.02424 0.01539  0.01581  113 SER   A C   
877  O O   . SER   A 113 ? 0.24936 0.28113 0.27007 -0.02340 0.01630  0.01344  113 SER   A O   
878  C CB  . SER   A 113 ? 0.25014 0.28740 0.26902 -0.02791 0.00562  0.01637  113 SER   A CB  
879  O OG  . SER   A 113 ? 0.26234 0.30151 0.27717 -0.02708 0.00193  0.01772  113 SER   A OG  
880  N N   . VAL   A 114 ? 0.19121 0.24124 0.23071 -0.02552 0.01707  0.01776  114 VAL   A N   
881  C CA  . VAL   A 114 ? 0.18863 0.23981 0.22957 -0.02708 0.02038  0.01769  114 VAL   A CA  
882  C C   . VAL   A 114 ? 0.20074 0.25821 0.24664 -0.03386 0.01798  0.02110  114 VAL   A C   
883  O O   . VAL   A 114 ? 0.20176 0.27103 0.25805 -0.03490 0.01672  0.02372  114 VAL   A O   
884  C CB  . VAL   A 114 ? 0.20558 0.26384 0.25353 -0.02228 0.02545  0.01681  114 VAL   A CB  
885  C CG1 . VAL   A 114 ? 0.22624 0.28842 0.27414 -0.02415 0.02910  0.01734  114 VAL   A CG1 
886  C CG2 . VAL   A 114 ? 0.20115 0.25230 0.24505 -0.01766 0.02652  0.01429  114 VAL   A CG2 
887  N N   . LEU   A 115 ? 0.17161 0.22167 0.21130 -0.03876 0.01675  0.02196  115 LEU   A N   
888  C CA  . LEU   A 115 ? 0.20353 0.26017 0.24904 -0.04693 0.01490  0.02692  115 LEU   A CA  
889  C C   . LEU   A 115 ? 0.22519 0.29077 0.27412 -0.04651 0.02180  0.02926  115 LEU   A C   
890  O O   . LEU   A 115 ? 0.24148 0.29757 0.28148 -0.04717 0.02282  0.02925  115 LEU   A O   
891  C CB  . LEU   A 115 ? 0.21810 0.25844 0.25366 -0.05351 0.00791  0.02725  115 LEU   A CB  
892  C CG  . LEU   A 115 ? 0.22111 0.26669 0.26333 -0.06437 0.00444  0.03390  115 LEU   A CG  
893  C CD1 . LEU   A 115 ? 0.23476 0.29694 0.29084 -0.06831 0.00142  0.03724  115 LEU   A CD1 
894  C CD2 . LEU   A 115 ? 0.27935 0.30310 0.30968 -0.07048 -0.00375 0.03348  115 LEU   A CD2 
895  N N   . ALA   A 116 ? 0.19221 0.27624 0.25332 -0.04446 0.02646  0.03112  116 ALA   A N   
896  C CA  . ALA   A 116 ? 0.18623 0.28125 0.24934 -0.04265 0.03406  0.03259  116 ALA   A CA  
897  C C   . ALA   A 116 ? 0.23713 0.33880 0.30253 -0.05243 0.03412  0.04020  116 ALA   A C   
898  O O   . ALA   A 116 ? 0.23280 0.34312 0.30827 -0.05958 0.03031  0.04531  116 ALA   A O   
899  C CB  . ALA   A 116 ? 0.21024 0.32287 0.28556 -0.03553 0.03921  0.03129  116 ALA   A CB  
900  N N   . CYS   A 117 ? 0.20072 0.29879 0.25700 -0.05345 0.03783  0.04183  117 CYS   A N   
901  C CA  . CYS   A 117 ? 0.22768 0.32650 0.28275 -0.06402 0.03657  0.05031  117 CYS   A CA  
902  C C   . CYS   A 117 ? 0.30847 0.42036 0.36059 -0.06254 0.04556  0.05363  117 CYS   A C   
903  O O   . CYS   A 117 ? 0.27649 0.38635 0.32060 -0.05355 0.05011  0.04752  117 CYS   A O   
904  C CB  . CYS   A 117 ? 0.30350 0.37658 0.34481 -0.06754 0.02919  0.04972  117 CYS   A CB  
905  S SG  . CYS   A 117 ? 0.35045 0.40750 0.39187 -0.07257 0.01788  0.04788  117 CYS   A SG  
906  N N   . TYR   A 118 ? 0.28587 0.41075 0.34346 -0.07204 0.04758  0.06371  118 TYR   A N   
907  C CA  . TYR   A 118 ? 0.31403 0.45218 0.36645 -0.07225 0.05637  0.06888  118 TYR   A CA  
908  C C   . TYR   A 118 ? 0.33734 0.47216 0.38779 -0.08633 0.05282  0.08118  118 TYR   A C   
909  O O   . TYR   A 118 ? 0.30767 0.44604 0.37010 -0.09670 0.04732  0.08789  118 TYR   A O   
910  C CB  . TYR   A 118 ? 0.29494 0.46385 0.36058 -0.06682 0.06674  0.06949  118 TYR   A CB  
911  C CG  . TYR   A 118 ? 0.31258 0.48109 0.37961 -0.05277 0.06896  0.05752  118 TYR   A CG  
912  C CD1 . TYR   A 118 ? 0.31719 0.48661 0.39730 -0.05052 0.06414  0.05419  118 TYR   A CD1 
913  C CD2 . TYR   A 118 ? 0.32289 0.48746 0.37675 -0.04238 0.07439  0.04980  118 TYR   A CD2 
914  C CE1 . TYR   A 118 ? 0.29003 0.45655 0.37093 -0.03842 0.06520  0.04454  118 TYR   A CE1 
915  C CE2 . TYR   A 118 ? 0.30124 0.46207 0.35607 -0.03067 0.07490  0.03932  118 TYR   A CE2 
916  C CZ  . TYR   A 118 ? 0.32375 0.48525 0.39245 -0.02882 0.07042  0.03719  118 TYR   A CZ  
917  O OH  . TYR   A 118 ? 0.31448 0.47061 0.38407 -0.01785 0.07022  0.02809  118 TYR   A OH  
918  N N   . ASN   A 119 ? 0.34345 0.46980 0.37839 -0.08721 0.05459  0.08448  119 ASN   A N   
919  C CA  . ASN   A 119 ? 0.34127 0.46116 0.37202 -0.10053 0.05064  0.09731  119 ASN   A CA  
920  C C   . ASN   A 119 ? 0.36469 0.45907 0.39612 -0.10857 0.03719  0.09826  119 ASN   A C   
921  O O   . ASN   A 119 ? 0.40079 0.49185 0.43587 -0.12213 0.03183  0.10946  119 ASN   A O   
922  C CB  . ASN   A 119 ? 0.36556 0.51162 0.40839 -0.10696 0.05696  0.10717  119 ASN   A CB  
923  C CG  . ASN   A 119 ? 0.44541 0.60808 0.47933 -0.09952 0.06877  0.10737  119 ASN   A CG  
924  O OD1 . ASN   A 119 ? 0.49743 0.64987 0.51319 -0.09607 0.07029  0.10624  119 ASN   A OD1 
925  N ND2 . ASN   A 119 ? 0.55862 0.74676 0.60441 -0.09656 0.07679  0.10844  119 ASN   A ND2 
926  N N   . GLY   A 120 ? 0.33860 0.41436 0.36583 -0.10037 0.03150  0.08665  120 GLY   A N   
927  C CA  . GLY   A 120 ? 0.33108 0.38200 0.35627 -0.10528 0.01939  0.08507  120 GLY   A CA  
928  C C   . GLY   A 120 ? 0.37274 0.43012 0.41206 -0.11107 0.01437  0.08486  120 GLY   A C   
929  O O   . GLY   A 120 ? 0.36951 0.40557 0.40562 -0.11625 0.00341  0.08355  120 GLY   A O   
930  N N   . SER   A 121 ? 0.33959 0.42499 0.39382 -0.10963 0.02135  0.08564  121 SER   A N   
931  C CA  . SER   A 121 ? 0.35999 0.45506 0.42958 -0.11592 0.01594  0.08717  121 SER   A CA  
932  C C   . SER   A 121 ? 0.35592 0.45918 0.43079 -0.10405 0.01856  0.07702  121 SER   A C   
933  O O   . SER   A 121 ? 0.28636 0.40700 0.36480 -0.09446 0.02863  0.07414  121 SER   A O   
934  C CB  . SER   A 121 ? 0.36578 0.49022 0.45290 -0.12643 0.02047  0.09998  121 SER   A CB  
935  O OG  . SER   A 121 ? 0.39630 0.50839 0.47718 -0.13621 0.01575  0.10828  121 SER   A OG  
936  N N   . PRO   A 122 ? 0.34465 0.43460 0.41872 -0.10417 0.00935  0.07147  122 PRO   A N   
937  C CA  . PRO   A 122 ? 0.32351 0.41989 0.40148 -0.09348 0.01113  0.06325  122 PRO   A CA  
938  C C   . PRO   A 122 ? 0.32694 0.45482 0.42501 -0.09238 0.01691  0.06739  122 PRO   A C   
939  O O   . PRO   A 122 ? 0.35868 0.50282 0.47124 -0.10264 0.01452  0.07619  122 PRO   A O   
940  C CB  . PRO   A 122 ? 0.36553 0.44285 0.43780 -0.09686 -0.00095 0.05904  122 PRO   A CB  
941  C CG  . PRO   A 122 ? 0.38806 0.44299 0.44982 -0.10638 -0.00887 0.06202  122 PRO   A CG  
942  C CD  . PRO   A 122 ? 0.39009 0.45309 0.45452 -0.11229 -0.00318 0.07115  122 PRO   A CD  
943  N N   . SER   A 123 ? 0.28996 0.42646 0.38977 -0.07963 0.02416  0.06120  123 SER   A N   
944  C CA  . SER   A 123 ? 0.29660 0.46117 0.41472 -0.07472 0.03010  0.06321  123 SER   A CA  
945  C C   . SER   A 123 ? 0.27467 0.43974 0.39920 -0.06874 0.02496  0.05857  123 SER   A C   
946  O O   . SER   A 123 ? 0.27894 0.46447 0.42146 -0.07052 0.02319  0.06318  123 SER   A O   
947  C CB  . SER   A 123 ? 0.32803 0.50199 0.44308 -0.06388 0.04226  0.05982  123 SER   A CB  
948  O OG  . SER   A 123 ? 0.43166 0.62729 0.56164 -0.05476 0.04770  0.05839  123 SER   A OG  
949  N N   . GLY   A 124 ? 0.22937 0.37384 0.34036 -0.06203 0.02224  0.05064  124 GLY   A N   
950  C CA  . GLY   A 124 ? 0.19325 0.33750 0.30832 -0.05643 0.01759  0.04738  124 GLY   A CA  
951  C C   . GLY   A 124 ? 0.20142 0.32172 0.29893 -0.05165 0.01492  0.04033  124 GLY   A C   
952  O O   . GLY   A 124 ? 0.20655 0.31255 0.29093 -0.05075 0.01757  0.03725  124 GLY   A O   
953  N N   . VAL   A 125 ? 0.16914 0.28666 0.26700 -0.04859 0.00952  0.03864  125 VAL   A N   
954  C CA  . VAL   A 125 ? 0.19349 0.29193 0.27588 -0.04432 0.00750  0.03328  125 VAL   A CA  
955  C C   . VAL   A 125 ? 0.17030 0.27315 0.25779 -0.03560 0.00872  0.03216  125 VAL   A C   
956  O O   . VAL   A 125 ? 0.18770 0.30424 0.28830 -0.03445 0.00618  0.03555  125 VAL   A O   
957  C CB  . VAL   A 125 ? 0.24349 0.32841 0.31464 -0.05088 -0.00188 0.03258  125 VAL   A CB  
958  C CG1 . VAL   A 125 ? 0.29200 0.38782 0.37276 -0.05486 -0.00977 0.03643  125 VAL   A CG1 
959  C CG2 . VAL   A 125 ? 0.25982 0.32754 0.31428 -0.04542 -0.00188 0.02715  125 VAL   A CG2 
960  N N   . TYR   A 126 ? 0.20537 0.29714 0.28395 -0.02959 0.01220  0.02818  126 TYR   A N   
961  C CA  . TYR   A 126 ? 0.22114 0.31319 0.30299 -0.02272 0.01199  0.02807  126 TYR   A CA  
962  C C   . TYR   A 126 ? 0.21689 0.29426 0.28546 -0.02057 0.01251  0.02542  126 TYR   A C   
963  O O   . TYR   A 126 ? 0.20370 0.27214 0.26237 -0.02218 0.01450  0.02268  126 TYR   A O   
964  C CB  . TYR   A 126 ? 0.22163 0.32250 0.31493 -0.01565 0.01751  0.02721  126 TYR   A CB  
965  C CG  . TYR   A 126 ? 0.23940 0.33627 0.32754 -0.01396 0.02414  0.02324  126 TYR   A CG  
966  C CD1 . TYR   A 126 ? 0.29876 0.38323 0.37886 -0.01032 0.02576  0.01963  126 TYR   A CD1 
967  C CD2 . TYR   A 126 ? 0.25056 0.35732 0.34223 -0.01645 0.02835  0.02398  126 TYR   A CD2 
968  C CE1 . TYR   A 126 ? 0.28656 0.36741 0.36127 -0.00900 0.03037  0.01604  126 TYR   A CE1 
969  C CE2 . TYR   A 126 ? 0.29307 0.39621 0.37784 -0.01484 0.03392  0.02078  126 TYR   A CE2 
970  C CZ  . TYR   A 126 ? 0.26818 0.35786 0.34413 -0.01093 0.03439  0.01641  126 TYR   A CZ  
971  O OH  . TYR   A 126 ? 0.35839 0.44439 0.42676 -0.00953 0.03853  0.01322  126 TYR   A OH  
972  N N   . GLN   A 127 ? 0.23222 0.30842 0.30205 -0.01668 0.01073  0.02718  127 GLN   A N   
973  C CA  . GLN   A 127 ? 0.24626 0.31264 0.30598 -0.01520 0.01115  0.02692  127 GLN   A CA  
974  C C   . GLN   A 127 ? 0.29543 0.35899 0.36013 -0.01057 0.01487  0.02605  127 GLN   A C   
975  O O   . GLN   A 127 ? 0.32786 0.39545 0.40303 -0.00674 0.01487  0.02654  127 GLN   A O   
976  C CB  . GLN   A 127 ? 0.29139 0.35847 0.34804 -0.01546 0.00578  0.03127  127 GLN   A CB  
977  C CG  . GLN   A 127 ? 0.32982 0.39003 0.37397 -0.01505 0.00638  0.03237  127 GLN   A CG  
978  C CD  . GLN   A 127 ? 0.26907 0.32331 0.29878 -0.01725 0.00689  0.02834  127 GLN   A CD  
979  O OE1 . GLN   A 127 ? 0.32143 0.37425 0.34971 -0.02036 0.00513  0.02520  127 GLN   A OE1 
980  N NE2 . GLN   A 127 ? 0.31095 0.36178 0.32982 -0.01554 0.00893  0.02890  127 GLN   A NE2 
981  N N   . CYS   A 128 ? 0.27513 0.33157 0.33272 -0.01058 0.01740  0.02456  128 CYS   A N   
982  C CA  . CYS   A 128 ? 0.31601 0.36843 0.37815 -0.00769 0.01895  0.02420  128 CYS   A CA  
983  C C   . CYS   A 128 ? 0.25860 0.30670 0.31462 -0.00899 0.01989  0.02600  128 CYS   A C   
984  O O   . CYS   A 128 ? 0.25656 0.30489 0.30386 -0.01050 0.02080  0.02599  128 CYS   A O   
985  C CB  . CYS   A 128 ? 0.39019 0.44203 0.45453 -0.00610 0.02209  0.01914  128 CYS   A CB  
986  S SG  . CYS   A 128 ? 0.40435 0.45285 0.45887 -0.00900 0.02462  0.01640  128 CYS   A SG  
987  N N   . ALA   A 129 ? 0.26415 0.30845 0.32531 -0.00815 0.01948  0.02747  129 ALA   A N   
988  C CA  . ALA   A 129 ? 0.24050 0.28379 0.29985 -0.01007 0.02042  0.03076  129 ALA   A CA  
989  C C   . ALA   A 129 ? 0.24276 0.28271 0.30416 -0.01023 0.02144  0.02677  129 ALA   A C   
990  O O   . ALA   A 129 ? 0.24389 0.27952 0.30865 -0.00852 0.02032  0.02258  129 ALA   A O   
991  C CB  . ALA   A 129 ? 0.27162 0.31306 0.33631 -0.01111 0.01741  0.03791  129 ALA   A CB  
992  N N   . MET   A 130 ? 0.19456 0.23733 0.25338 -0.01157 0.02348  0.02783  130 MET   A N   
993  C CA  . MET   A 130 ? 0.21466 0.25542 0.27696 -0.01252 0.02283  0.02585  130 MET   A CA  
994  C C   . MET   A 130 ? 0.22504 0.26241 0.29593 -0.01529 0.01911  0.03044  130 MET   A C   
995  O O   . MET   A 130 ? 0.23573 0.27786 0.30955 -0.01781 0.01947  0.03782  130 MET   A O   
996  C CB  . MET   A 130 ? 0.23697 0.28394 0.29635 -0.01233 0.02576  0.02667  130 MET   A CB  
997  C CG  . MET   A 130 ? 0.20796 0.25580 0.27273 -0.01371 0.02414  0.02624  130 MET   A CG  
998  S SD  . MET   A 130 ? 0.26854 0.30835 0.32884 -0.01249 0.02191  0.01845  130 MET   A SD  
999  C CE  . MET   A 130 ? 0.25797 0.29806 0.30816 -0.00971 0.02555  0.01560  130 MET   A CE  
1000 N N   . ARG   A 131 ? 0.19558 0.22399 0.26960 -0.01485 0.01529  0.02638  131 ARG   A N   
1001 C CA  . ARG   A 131 ? 0.21494 0.23576 0.29659 -0.01773 0.00993  0.03015  131 ARG   A CA  
1002 C C   . ARG   A 131 ? 0.19873 0.22379 0.28634 -0.02344 0.00833  0.03543  131 ARG   A C   
1003 O O   . ARG   A 131 ? 0.19163 0.22372 0.27771 -0.02359 0.01060  0.03363  131 ARG   A O   
1004 C CB  . ARG   A 131 ? 0.21036 0.21837 0.29181 -0.01481 0.00565  0.02252  131 ARG   A CB  
1005 C CG  . ARG   A 131 ? 0.24962 0.25587 0.32779 -0.00808 0.00765  0.01692  131 ARG   A CG  
1006 C CD  . ARG   A 131 ? 0.24368 0.25082 0.32613 -0.00639 0.00696  0.02243  131 ARG   A CD  
1007 N NE  . ARG   A 131 ? 0.26486 0.26225 0.35386 -0.00915 0.00091  0.02842  131 ARG   A NE  
1008 C CZ  . ARG   A 131 ? 0.28856 0.28720 0.38097 -0.01037 -0.00066 0.03699  131 ARG   A CZ  
1009 N NH1 . ARG   A 131 ? 0.24023 0.24849 0.33000 -0.00808 0.00252  0.03908  131 ARG   A NH1 
1010 N NH2 . ARG   A 131 ? 0.28524 0.27470 0.38347 -0.01461 -0.00644 0.04416  131 ARG   A NH2 
1011 N N   . PRO   A 132 ? 0.20655 0.22804 0.30227 -0.02845 0.00394  0.04287  132 PRO   A N   
1012 C CA  . PRO   A 132 ? 0.21115 0.23804 0.31561 -0.03520 0.00144  0.04869  132 PRO   A CA  
1013 C C   . PRO   A 132 ? 0.21145 0.23281 0.31610 -0.03592 -0.00309 0.04127  132 PRO   A C   
1014 O O   . PRO   A 132 ? 0.21286 0.24417 0.32370 -0.03980 -0.00356 0.04457  132 PRO   A O   
1015 C CB  . PRO   A 132 ? 0.26643 0.28523 0.37918 -0.04111 -0.00455 0.05741  132 PRO   A CB  
1016 C CG  . PRO   A 132 ? 0.24163 0.26011 0.34907 -0.03704 -0.00142 0.06016  132 PRO   A CG  
1017 C CD  . PRO   A 132 ? 0.23069 0.24628 0.32880 -0.02885 0.00154  0.04884  132 PRO   A CD  
1018 N N   . ASN   A 133 ? 0.21601 0.22315 0.31386 -0.03183 -0.00641 0.03150  133 ASN   A N   
1019 C CA  . ASN   A 133 ? 0.21947 0.22126 0.31364 -0.03190 -0.01067 0.02377  133 ASN   A CA  
1020 C C   . ASN   A 133 ? 0.21863 0.22797 0.30310 -0.02653 -0.00460 0.01790  133 ASN   A C   
1021 O O   . ASN   A 133 ? 0.21591 0.21968 0.29338 -0.02498 -0.00736 0.01060  133 ASN   A O   
1022 C CB  . ASN   A 133 ? 0.23831 0.22002 0.32806 -0.02991 -0.01775 0.01568  133 ASN   A CB  
1023 C CG  . ASN   A 133 ? 0.26169 0.23896 0.34218 -0.02084 -0.01293 0.00815  133 ASN   A CG  
1024 O OD1 . ASN   A 133 ? 0.25821 0.24660 0.33624 -0.01742 -0.00531 0.00958  133 ASN   A OD1 
1025 N ND2 . ASN   A 133 ? 0.24330 0.20439 0.31873 -0.01673 -0.01778 -0.00026 133 ASN   A ND2 
1026 N N   . PHE   A 134 ? 0.18653 0.20691 0.26915 -0.02387 0.00289  0.02104  134 PHE   A N   
1027 C CA  . PHE   A 134 ? 0.22070 0.24748 0.29531 -0.02002 0.00786  0.01746  134 PHE   A CA  
1028 C C   . PHE   A 134 ? 0.23571 0.25533 0.30016 -0.01560 0.00897  0.00939  134 PHE   A C   
1029 O O   . PHE   A 134 ? 0.25968 0.28084 0.31690 -0.01396 0.01037  0.00599  134 PHE   A O   
1030 C CB  . PHE   A 134 ? 0.20864 0.24153 0.28580 -0.02193 0.00571  0.01835  134 PHE   A CB  
1031 C CG  . PHE   A 134 ? 0.20612 0.25242 0.29358 -0.02441 0.00764  0.02675  134 PHE   A CG  
1032 C CD1 . PHE   A 134 ? 0.23207 0.28771 0.31685 -0.02058 0.01458  0.02907  134 PHE   A CD1 
1033 C CD2 . PHE   A 134 ? 0.21333 0.26320 0.31298 -0.03056 0.00245  0.03234  134 PHE   A CD2 
1034 C CE1 . PHE   A 134 ? 0.24282 0.31266 0.33597 -0.02128 0.01774  0.03632  134 PHE   A CE1 
1035 C CE2 . PHE   A 134 ? 0.26061 0.32664 0.37109 -0.03270 0.00551  0.04114  134 PHE   A CE2 
1036 C CZ  . PHE   A 134 ? 0.25575 0.33255 0.36248 -0.02726 0.01390  0.04288  134 PHE   A CZ  
1037 N N   . THR   A 135 ? 0.22384 0.23653 0.28800 -0.01331 0.00849  0.00691  135 THR   A N   
1038 C CA  . THR   A 135 ? 0.24659 0.25806 0.30333 -0.00827 0.01196  0.00098  135 THR   A CA  
1039 C C   . THR   A 135 ? 0.22495 0.24262 0.28418 -0.00670 0.01614  0.00454  135 THR   A C   
1040 O O   . THR   A 135 ? 0.24139 0.26173 0.30599 -0.00891 0.01574  0.01068  135 THR   A O   
1041 C CB  . THR   A 135 ? 0.23715 0.23744 0.29173 -0.00472 0.00849  -0.00577 135 THR   A CB  
1042 O OG1 . THR   A 135 ? 0.23848 0.23263 0.30120 -0.00462 0.00528  -0.00275 135 THR   A OG1 
1043 C CG2 . THR   A 135 ? 0.24341 0.23546 0.29375 -0.00698 0.00237  -0.01002 135 THR   A CG2 
1044 N N   . ILE   A 136 ? 0.25217 0.27332 0.30728 -0.00333 0.01994  0.00126  136 ILE   A N   
1045 C CA  . ILE   A 136 ? 0.21524 0.24230 0.27398 -0.00195 0.02227  0.00410  136 ILE   A CA  
1046 C C   . ILE   A 136 ? 0.26847 0.29572 0.32883 0.00363  0.02357  -0.00046 136 ILE   A C   
1047 O O   . ILE   A 136 ? 0.24109 0.26648 0.29603 0.00645  0.02497  -0.00627 136 ILE   A O   
1048 C CB  . ILE   A 136 ? 0.27512 0.30971 0.32970 -0.00428 0.02553  0.00638  136 ILE   A CB  
1049 C CG1 . ILE   A 136 ? 0.23889 0.27649 0.28775 -0.00362 0.02865  0.00291  136 ILE   A CG1 
1050 C CG2 . ILE   A 136 ? 0.24635 0.28062 0.29827 -0.00738 0.02496  0.00933  136 ILE   A CG2 
1051 C CD1 . ILE   A 136 ? 0.23478 0.27684 0.28012 -0.00695 0.03025  0.00580  136 ILE   A CD1 
1052 N N   . LYS   A 137 ? 0.27991 0.30997 0.34751 0.00605  0.02299  0.00223  137 LYS   A N   
1053 C CA  . LYS   A 137 ? 0.30050 0.33394 0.37221 0.01292  0.02484  -0.00154 137 LYS   A CA  
1054 C C   . LYS   A 137 ? 0.29978 0.34805 0.37357 0.01181  0.02907  0.00103  137 LYS   A C   
1055 O O   . LYS   A 137 ? 0.29089 0.34512 0.37106 0.01072  0.02753  0.00602  137 LYS   A O   
1056 C CB  . LYS   A 137 ? 0.32450 0.35171 0.40467 0.01707  0.02041  0.00024  137 LYS   A CB  
1057 C CG  . LYS   A 137 ? 0.33541 0.34706 0.41537 0.01516  0.01443  0.00083  137 LYS   A CG  
1058 C CD  . LYS   A 137 ? 0.44986 0.45735 0.53835 0.01630  0.00965  0.00718  137 LYS   A CD  
1059 C CE  . LYS   A 137 ? 0.54075 0.52986 0.63161 0.01812  0.00288  0.00577  137 LYS   A CE  
1060 N NZ  . LYS   A 137 ? 0.53034 0.51473 0.62769 0.01487  -0.00252 0.01579  137 LYS   A NZ  
1061 N N   . GLY   A 138 ? 0.27846 0.33256 0.34646 0.01122  0.03365  -0.00170 138 GLY   A N   
1062 C CA  . GLY   A 138 ? 0.27247 0.33960 0.34228 0.00784  0.03691  0.00181  138 GLY   A CA  
1063 C C   . GLY   A 138 ? 0.29487 0.37552 0.37065 0.01309  0.04201  0.00019  138 GLY   A C   
1064 O O   . GLY   A 138 ? 0.30839 0.38870 0.38868 0.02147  0.04279  -0.00397 138 GLY   A O   
1065 N N   . SER   A 139 ? 0.25690 0.35002 0.33352 0.00837  0.04543  0.00390  139 SER   A N   
1066 C CA  . SER   A 139 ? 0.27512 0.38601 0.35767 0.01156  0.05193  0.00428  139 SER   A CA  
1067 C C   . SER   A 139 ? 0.28476 0.39896 0.35821 0.00442  0.05526  0.00703  139 SER   A C   
1068 O O   . SER   A 139 ? 0.27623 0.39321 0.35143 -0.00426 0.05298  0.01314  139 SER   A O   
1069 C CB  . SER   A 139 ? 0.30409 0.43081 0.40281 0.01096  0.05093  0.00982  139 SER   A CB  
1070 O OG  . SER   A 139 ? 0.30224 0.45008 0.40912 0.01393  0.05807  0.01126  139 SER   A OG  
1071 N N   . PHE   A 140 ? 0.27955 0.39162 0.34205 0.00794  0.05966  0.00255  140 PHE   A N   
1072 C CA  . PHE   A 140 ? 0.30219 0.41325 0.35296 0.00150  0.06158  0.00538  140 PHE   A CA  
1073 C C   . PHE   A 140 ? 0.33275 0.45556 0.37739 0.00682  0.06983  0.00290  140 PHE   A C   
1074 O O   . PHE   A 140 ? 0.35265 0.46988 0.39080 0.01575  0.07119  -0.00536 140 PHE   A O   
1075 C CB  . PHE   A 140 ? 0.27394 0.36522 0.31219 -0.00042 0.05621  0.00244  140 PHE   A CB  
1076 C CG  . PHE   A 140 ? 0.26175 0.34274 0.30300 -0.00567 0.04951  0.00533  140 PHE   A CG  
1077 C CD1 . PHE   A 140 ? 0.24151 0.32343 0.28343 -0.01345 0.04764  0.01145  140 PHE   A CD1 
1078 C CD2 . PHE   A 140 ? 0.25495 0.32477 0.29719 -0.00276 0.04501  0.00191  140 PHE   A CD2 
1079 C CE1 . PHE   A 140 ? 0.24222 0.31395 0.28403 -0.01655 0.04199  0.01257  140 PHE   A CE1 
1080 C CE2 . PHE   A 140 ? 0.24456 0.30730 0.28810 -0.00662 0.04031  0.00462  140 PHE   A CE2 
1081 C CZ  . PHE   A 140 ? 0.22324 0.28684 0.26563 -0.01269 0.03912  0.00919  140 PHE   A CZ  
1082 N N   . LEU   A 141 ? 0.32993 0.46818 0.37548 0.00122  0.07501  0.01004  141 LEU   A N   
1083 C CA  . LEU   A 141 ? 0.34439 0.49641 0.38204 0.00545  0.08413  0.00926  141 LEU   A CA  
1084 C C   . LEU   A 141 ? 0.36507 0.50924 0.38558 -0.00164 0.08352  0.01301  141 LEU   A C   
1085 O O   . LEU   A 141 ? 0.29860 0.42677 0.31506 -0.00864 0.07605  0.01557  141 LEU   A O   
1086 C CB  . LEU   A 141 ? 0.34032 0.52033 0.39337 0.00440  0.09166  0.01646  141 LEU   A CB  
1087 C CG  . LEU   A 141 ? 0.37343 0.56530 0.44617 0.01168  0.09214  0.01453  141 LEU   A CG  
1088 C CD1 . LEU   A 141 ? 0.40743 0.62881 0.49774 0.00685  0.09784  0.02468  141 LEU   A CD1 
1089 C CD2 . LEU   A 141 ? 0.41034 0.60068 0.47914 0.02745  0.09634  0.00312  141 LEU   A CD2 
1090 N N   . ASN   A 142 ? 0.38310 0.53922 0.39290 0.00093  0.09162  0.01358  142 ASN   A N   
1091 C CA  . ASN   A 142 ? 0.39084 0.54104 0.38407 -0.00621 0.09089  0.01904  142 ASN   A CA  
1092 C C   . ASN   A 142 ? 0.35204 0.50407 0.35364 -0.01958 0.08755  0.03160  142 ASN   A C   
1093 O O   . ASN   A 142 ? 0.34542 0.51384 0.36362 -0.02374 0.09021  0.03796  142 ASN   A O   
1094 C CB  . ASN   A 142 ? 0.43157 0.59812 0.41172 -0.00158 0.10133  0.01915  142 ASN   A CB  
1095 C CG  . ASN   A 142 ? 0.55204 0.70966 0.51711 0.01109  0.10222  0.00534  142 ASN   A CG  
1096 O OD1 . ASN   A 142 ? 0.72970 0.87462 0.67457 0.01122  0.09912  0.00232  142 ASN   A OD1 
1097 N ND2 . ASN   A 142 ? 0.61587 0.77879 0.59056 0.02188  0.10532  -0.00319 142 ASN   A ND2 
1098 N N   . GLY   A 143 ? 0.35592 0.49004 0.34658 -0.02615 0.08056  0.03496  143 GLY   A N   
1099 C CA  . GLY   A 143 ? 0.34348 0.47289 0.33963 -0.03810 0.07535  0.04539  143 GLY   A CA  
1100 C C   . GLY   A 143 ? 0.32252 0.43750 0.32880 -0.03996 0.06660  0.04285  143 GLY   A C   
1101 O O   . GLY   A 143 ? 0.29526 0.40052 0.30293 -0.04875 0.06046  0.04934  143 GLY   A O   
1102 N N   . SER   A 144 ? 0.29461 0.40664 0.30655 -0.03181 0.06552  0.03367  144 SER   A N   
1103 C CA  . SER   A 144 ? 0.30357 0.40392 0.32362 -0.03294 0.05817  0.03151  144 SER   A CA  
1104 C C   . SER   A 144 ? 0.28910 0.36810 0.29922 -0.03261 0.05121  0.02863  144 SER   A C   
1105 O O   . SER   A 144 ? 0.22541 0.29451 0.23969 -0.03411 0.04552  0.02787  144 SER   A O   
1106 C CB  . SER   A 144 ? 0.30070 0.40667 0.33068 -0.02470 0.05961  0.02450  144 SER   A CB  
1107 O OG  . SER   A 144 ? 0.32179 0.41753 0.34335 -0.01701 0.05891  0.01635  144 SER   A OG  
1108 N N   . CYS   A 145 ? 0.23672 0.30957 0.23373 -0.03025 0.05142  0.02708  145 CYS   A N   
1109 C CA  . CYS   A 145 ? 0.24479 0.30049 0.23511 -0.02901 0.04476  0.02468  145 CYS   A CA  
1110 C C   . CYS   A 145 ? 0.24345 0.28830 0.23365 -0.03542 0.03927  0.03053  145 CYS   A C   
1111 O O   . CYS   A 145 ? 0.27888 0.32618 0.26822 -0.04252 0.03973  0.03807  145 CYS   A O   
1112 C CB  . CYS   A 145 ? 0.27281 0.32513 0.24913 -0.02642 0.04475  0.02337  145 CYS   A CB  
1113 S SG  . CYS   A 145 ? 0.35035 0.40494 0.32530 -0.01748 0.04648  0.01279  145 CYS   A SG  
1114 N N   . GLY   A 146 ? 0.24948 0.28220 0.24069 -0.03272 0.03398  0.02707  146 GLY   A N   
1115 C CA  . GLY   A 146 ? 0.24686 0.26721 0.23750 -0.03634 0.02849  0.03002  146 GLY   A CA  
1116 C C   . GLY   A 146 ? 0.23331 0.25489 0.23244 -0.03860 0.02725  0.02913  146 GLY   A C   
1117 O O   . GLY   A 146 ? 0.27884 0.28787 0.27571 -0.04056 0.02194  0.02965  146 GLY   A O   
1118 N N   . SER   A 147 ? 0.25129 0.28685 0.25925 -0.03797 0.03133  0.02770  147 SER   A N   
1119 C CA  . SER   A 147 ? 0.24366 0.28053 0.25932 -0.03868 0.02910  0.02616  147 SER   A CA  
1120 C C   . SER   A 147 ? 0.22431 0.25217 0.23779 -0.03258 0.02666  0.02069  147 SER   A C   
1121 O O   . SER   A 147 ? 0.21642 0.24350 0.22791 -0.02729 0.02820  0.01768  147 SER   A O   
1122 C CB  . SER   A 147 ? 0.23528 0.28948 0.26182 -0.03732 0.03362  0.02583  147 SER   A CB  
1123 O OG  . SER   A 147 ? 0.25425 0.32180 0.28418 -0.04152 0.03798  0.03105  147 SER   A OG  
1124 N N   . VAL   A 148 ? 0.22875 0.25071 0.24242 -0.03364 0.02266  0.01967  148 VAL   A N   
1125 C CA  . VAL   A 148 ? 0.21285 0.22645 0.22231 -0.02805 0.02092  0.01553  148 VAL   A CA  
1126 C C   . VAL   A 148 ? 0.19353 0.21266 0.20765 -0.02625 0.02085  0.01374  148 VAL   A C   
1127 O O   . VAL   A 148 ? 0.19798 0.22361 0.21740 -0.03001 0.01968  0.01551  148 VAL   A O   
1128 C CB  . VAL   A 148 ? 0.22496 0.22247 0.22509 -0.02858 0.01595  0.01487  148 VAL   A CB  
1129 C CG1 . VAL   A 148 ? 0.24256 0.23307 0.23773 -0.02931 0.01523  0.01750  148 VAL   A CG1 
1130 C CG2 . VAL   A 148 ? 0.26912 0.26191 0.26814 -0.03520 0.01108  0.01621  148 VAL   A CG2 
1131 N N   . GLY   A 149 ? 0.20385 0.22168 0.21667 -0.02061 0.02191  0.01118  149 GLY   A N   
1132 C CA  . GLY   A 149 ? 0.22739 0.24876 0.24186 -0.01858 0.02165  0.01048  149 GLY   A CA  
1133 C C   . GLY   A 149 ? 0.19545 0.20783 0.20008 -0.01585 0.01960  0.00799  149 GLY   A C   
1134 O O   . GLY   A 149 ? 0.19995 0.20517 0.19937 -0.01268 0.01973  0.00630  149 GLY   A O   
1135 N N   . PHE   A 150 ? 0.19980 0.21261 0.20111 -0.01623 0.01748  0.00753  150 PHE   A N   
1136 C CA  . PHE   A 150 ? 0.22421 0.22735 0.21289 -0.01318 0.01523  0.00386  150 PHE   A CA  
1137 C C   . PHE   A 150 ? 0.26496 0.27301 0.25004 -0.01218 0.01461  0.00421  150 PHE   A C   
1138 O O   . PHE   A 150 ? 0.22395 0.24050 0.21665 -0.01541 0.01371  0.00769  150 PHE   A O   
1139 C CB  . PHE   A 150 ? 0.24939 0.23900 0.23050 -0.01761 0.00907  0.00184  150 PHE   A CB  
1140 C CG  . PHE   A 150 ? 0.25224 0.24538 0.23773 -0.02557 0.00426  0.00445  150 PHE   A CG  
1141 C CD1 . PHE   A 150 ? 0.25669 0.25942 0.25462 -0.03084 0.00552  0.00906  150 PHE   A CD1 
1142 C CD2 . PHE   A 150 ? 0.27627 0.26506 0.25373 -0.02732 -0.00141 0.00243  150 PHE   A CD2 
1143 C CE1 . PHE   A 150 ? 0.26000 0.26992 0.26506 -0.03759 0.00168  0.01231  150 PHE   A CE1 
1144 C CE2 . PHE   A 150 ? 0.30959 0.30390 0.29348 -0.03505 -0.00683 0.00565  150 PHE   A CE2 
1145 C CZ  . PHE   A 150 ? 0.29313 0.29917 0.29233 -0.04012 -0.00503 0.01097  150 PHE   A CZ  
1146 N N   . ASN   A 151 ? 0.25938 0.26208 0.23203 -0.00689 0.01507  0.00062  151 ASN   A N   
1147 C CA  . ASN   A 151 ? 0.30484 0.30900 0.26788 -0.00590 0.01335  0.00011  151 ASN   A CA  
1148 C C   . ASN   A 151 ? 0.35548 0.34365 0.30127 -0.00493 0.00765  -0.00665 151 ASN   A C   
1149 O O   . ASN   A 151 ? 0.32375 0.30003 0.26516 -0.00274 0.00666  -0.01074 151 ASN   A O   
1150 C CB  . ASN   A 151 ? 0.31366 0.32769 0.27543 0.00039  0.02015  0.00212  151 ASN   A CB  
1151 C CG  . ASN   A 151 ? 0.32240 0.34949 0.29943 -0.00214 0.02313  0.00927  151 ASN   A CG  
1152 O OD1 . ASN   A 151 ? 0.30389 0.33544 0.29146 -0.00128 0.02680  0.01109  151 ASN   A OD1 
1153 N ND2 . ASN   A 151 ? 0.31271 0.34466 0.29048 -0.00507 0.02057  0.01328  151 ASN   A ND2 
1154 N N   . ILE   A 152 ? 0.32312 0.30918 0.25790 -0.00640 0.00281  -0.00804 152 ILE   A N   
1155 C CA  . ILE   A 152 ? 0.41668 0.38504 0.33256 -0.00561 -0.00419 -0.01566 152 ILE   A CA  
1156 C C   . ILE   A 152 ? 0.50274 0.47267 0.40092 0.00221  -0.00128 -0.01911 152 ILE   A C   
1157 O O   . ILE   A 152 ? 0.46759 0.45054 0.36710 0.00123  0.00043  -0.01389 152 ILE   A O   
1158 C CB  . ILE   A 152 ? 0.45263 0.41575 0.36931 -0.01586 -0.01495 -0.01475 152 ILE   A CB  
1159 C CG1 . ILE   A 152 ? 0.42984 0.38978 0.36061 -0.02342 -0.01773 -0.01189 152 ILE   A CG1 
1160 C CG2 . ILE   A 152 ? 0.54336 0.48734 0.43735 -0.01500 -0.02355 -0.02319 152 ILE   A CG2 
1161 C CD1 . ILE   A 152 ? 0.58261 0.52030 0.50232 -0.02504 -0.02458 -0.01764 152 ILE   A CD1 
1162 N N   . ASP   A 153 ? 0.53985 0.49687 0.42122 0.01063  -0.00039 -0.02751 153 ASP   A N   
1163 C CA  . ASP   A 153 ? 0.60435 0.56213 0.46508 0.01955  0.00296  -0.03233 153 ASP   A CA  
1164 C C   . ASP   A 153 ? 0.59886 0.53223 0.43654 0.02059  -0.00715 -0.04322 153 ASP   A C   
1165 O O   . ASP   A 153 ? 0.64284 0.55960 0.47269 0.02697  -0.00803 -0.05104 153 ASP   A O   
1166 C CB  . ASP   A 153 ? 0.64337 0.61065 0.50564 0.03112  0.01477  -0.03295 153 ASP   A CB  
1167 C CG  . ASP   A 153 ? 0.82719 0.79717 0.66701 0.04205  0.02007  -0.03832 153 ASP   A CG  
1168 O OD1 . ASP   A 153 ? 0.95363 0.94302 0.79892 0.04831  0.03115  -0.03343 153 ASP   A OD1 
1169 O OD2 . ASP   A 153 ? 0.86901 0.82258 0.68542 0.04437  0.01332  -0.04721 153 ASP   A OD2 
1170 N N   . TYR   A 154 ? 0.61906 0.54907 0.44579 0.01438  -0.01585 -0.04372 154 TYR   A N   
1171 C CA  . TYR   A 154 ? 0.64478 0.55014 0.44987 0.01276  -0.02831 -0.05382 154 TYR   A CA  
1172 C C   . TYR   A 154 ? 0.63069 0.51807 0.44521 0.00571  -0.03639 -0.05551 154 TYR   A C   
1173 O O   . TYR   A 154 ? 0.62532 0.51566 0.45541 -0.00704 -0.04348 -0.04895 154 TYR   A O   
1174 C CB  . TYR   A 154 ? 0.65286 0.54671 0.42968 0.02713  -0.02479 -0.06550 154 TYR   A CB  
1175 N N   . ASP   A 155 ? 0.63383 0.50357 0.43993 0.01409  -0.03523 -0.06337 155 ASP   A N   
1176 C CA  . ASP   A 155 ? 0.63605 0.48655 0.44943 0.00742  -0.04333 -0.06399 155 ASP   A CA  
1177 C C   . ASP   A 155 ? 0.60867 0.46644 0.44052 0.01116  -0.03429 -0.05888 155 ASP   A C   
1178 O O   . ASP   A 155 ? 0.57743 0.42020 0.41537 0.00590  -0.04016 -0.05789 155 ASP   A O   
1179 C CB  . ASP   A 155 ? 0.70016 0.51693 0.48783 0.01246  -0.05364 -0.07733 155 ASP   A CB  
1180 C CG  . ASP   A 155 ? 0.70373 0.51575 0.47357 0.03177  -0.04465 -0.08728 155 ASP   A CG  
1181 O OD1 . ASP   A 155 ? 0.64014 0.47716 0.41848 0.03991  -0.03051 -0.08275 155 ASP   A OD1 
1182 O OD2 . ASP   A 155 ? 0.81809 0.60127 0.56606 0.03896  -0.05198 -0.09958 155 ASP   A OD2 
1183 N N   . CYS   A 156 ? 0.56175 0.44194 0.40264 0.01911  -0.02114 -0.05481 156 CYS   A N   
1184 C CA  . CYS   A 156 ? 0.52990 0.41705 0.38613 0.02400  -0.01324 -0.05096 156 CYS   A CA  
1185 C C   . CYS   A 156 ? 0.46134 0.37056 0.34185 0.01502  -0.00870 -0.03938 156 CYS   A C   
1186 O O   . CYS   A 156 ? 0.46037 0.38898 0.34668 0.01365  -0.00368 -0.03450 156 CYS   A O   
1187 C CB  . CYS   A 156 ? 0.53703 0.43421 0.38750 0.03963  -0.00218 -0.05470 156 CYS   A CB  
1188 S SG  . CYS   A 156 ? 0.56608 0.47247 0.43584 0.04601  0.00576  -0.05004 156 CYS   A SG  
1189 N N   . VAL   A 157 ? 0.44016 0.34552 0.33354 0.00963  -0.01048 -0.03507 157 VAL   A N   
1190 C CA  . VAL   A 157 ? 0.38848 0.31285 0.30274 0.00265  -0.00600 -0.02559 157 VAL   A CA  
1191 C C   . VAL   A 157 ? 0.37589 0.31225 0.29899 0.01104  0.00332  -0.02355 157 VAL   A C   
1192 O O   . VAL   A 157 ? 0.34941 0.27575 0.27047 0.01705  0.00331  -0.02605 157 VAL   A O   
1193 C CB  . VAL   A 157 ? 0.36980 0.28614 0.29227 -0.00815 -0.01237 -0.02118 157 VAL   A CB  
1194 C CG1 . VAL   A 157 ? 0.33206 0.26886 0.27380 -0.01341 -0.00665 -0.01270 157 VAL   A CG1 
1195 C CG2 . VAL   A 157 ? 0.36052 0.26554 0.27629 -0.01759 -0.02284 -0.02244 157 VAL   A CG2 
1196 N N   . SER   A 158 ? 0.34586 0.30306 0.27965 0.01103  0.01016  -0.01847 158 SER   A N   
1197 C CA  . SER   A 158 ? 0.32176 0.29241 0.26659 0.01661  0.01776  -0.01527 158 SER   A CA  
1198 C C   . SER   A 158 ? 0.27394 0.25253 0.23450 0.00885  0.01795  -0.00889 158 SER   A C   
1199 O O   . SER   A 158 ? 0.27467 0.26480 0.24322 0.00386  0.01932  -0.00472 158 SER   A O   
1200 C CB  . SER   A 158 ? 0.33652 0.32373 0.28181 0.02142  0.02465  -0.01355 158 SER   A CB  
1201 O OG  . SER   A 158 ? 0.37132 0.35359 0.30161 0.03120  0.02664  -0.01981 158 SER   A OG  
1202 N N   . PHE   A 159 ? 0.28311 0.25485 0.24696 0.00861  0.01636  -0.00825 159 PHE   A N   
1203 C CA  . PHE   A 159 ? 0.26804 0.24700 0.24374 0.00244  0.01699  -0.00300 159 PHE   A CA  
1204 C C   . PHE   A 159 ? 0.24018 0.23391 0.22609 0.00624  0.02248  -0.00041 159 PHE   A C   
1205 O O   . PHE   A 159 ? 0.27346 0.26863 0.25963 0.01345  0.02452  -0.00151 159 PHE   A O   
1206 C CB  . PHE   A 159 ? 0.25192 0.21796 0.22522 0.00037  0.01282  -0.00227 159 PHE   A CB  
1207 C CG  . PHE   A 159 ? 0.26300 0.21463 0.22894 -0.00638 0.00624  -0.00286 159 PHE   A CG  
1208 C CD1 . PHE   A 159 ? 0.23862 0.19635 0.21046 -0.01605 0.00489  0.00123  159 PHE   A CD1 
1209 C CD2 . PHE   A 159 ? 0.26100 0.19316 0.21481 -0.00290 0.00094  -0.00751 159 PHE   A CD2 
1210 C CE1 . PHE   A 159 ? 0.27589 0.22249 0.24336 -0.02373 -0.00187 0.00196  159 PHE   A CE1 
1211 C CE2 . PHE   A 159 ? 0.29614 0.21302 0.24347 -0.01072 -0.00690 -0.00768 159 PHE   A CE2 
1212 C CZ  . PHE   A 159 ? 0.29635 0.22147 0.25135 -0.02190 -0.00841 -0.00234 159 PHE   A CZ  
1213 N N   . CYS   A 160 ? 0.21314 0.21779 0.20828 0.00154  0.02426  0.00307  160 CYS   A N   
1214 C CA  . CYS   A 160 ? 0.18757 0.20429 0.19246 0.00353  0.02781  0.00567  160 CYS   A CA  
1215 C C   . CYS   A 160 ? 0.19539 0.21530 0.20789 -0.00059 0.02716  0.00775  160 CYS   A C   
1216 O O   . CYS   A 160 ? 0.21308 0.24022 0.23307 0.00046  0.02825  0.00940  160 CYS   A O   
1217 C CB  . CYS   A 160 ? 0.22958 0.25575 0.23737 0.00327  0.03041  0.00773  160 CYS   A CB  
1218 S SG  . CYS   A 160 ? 0.24571 0.27236 0.25506 -0.00314 0.02817  0.00919  160 CYS   A SG  
1219 N N   . TYR   A 161 ? 0.19021 0.20566 0.20079 -0.00527 0.02534  0.00779  161 TYR   A N   
1220 C CA  . TYR   A 161 ? 0.19167 0.21134 0.20735 -0.00805 0.02577  0.00886  161 TYR   A CA  
1221 C C   . TYR   A 161 ? 0.19808 0.21254 0.20887 -0.01160 0.02444  0.00961  161 TYR   A C   
1222 O O   . TYR   A 161 ? 0.18378 0.19370 0.19092 -0.01475 0.02297  0.01021  161 TYR   A O   
1223 C CB  . TYR   A 161 ? 0.16982 0.19622 0.19171 -0.00993 0.02706  0.00941  161 TYR   A CB  
1224 C CG  . TYR   A 161 ? 0.18961 0.21913 0.21523 -0.01099 0.02775  0.00885  161 TYR   A CG  
1225 C CD1 . TYR   A 161 ? 0.18939 0.22026 0.21885 -0.00949 0.02719  0.00813  161 TYR   A CD1 
1226 C CD2 . TYR   A 161 ? 0.19423 0.22585 0.21940 -0.01335 0.02880  0.00891  161 TYR   A CD2 
1227 C CE1 . TYR   A 161 ? 0.20198 0.23319 0.23204 -0.00952 0.02713  0.00598  161 TYR   A CE1 
1228 C CE2 . TYR   A 161 ? 0.19295 0.22796 0.21958 -0.01253 0.03039  0.00730  161 TYR   A CE2 
1229 C CZ  . TYR   A 161 ? 0.18573 0.21897 0.21341 -0.01021 0.02928  0.00507  161 TYR   A CZ  
1230 O OH  . TYR   A 161 ? 0.20053 0.23457 0.22692 -0.00855 0.03012  0.00190  161 TYR   A OH  
1231 N N   . MET   A 162 ? 0.19244 0.20787 0.20280 -0.01184 0.02447  0.01015  162 MET   A N   
1232 C CA  . MET   A 162 ? 0.16052 0.17461 0.16641 -0.01596 0.02458  0.01219  162 MET   A CA  
1233 C C   . MET   A 162 ? 0.17388 0.19496 0.18111 -0.01570 0.02684  0.01108  162 MET   A C   
1234 O O   . MET   A 162 ? 0.16547 0.18702 0.17371 -0.01290 0.02572  0.00914  162 MET   A O   
1235 C CB  . MET   A 162 ? 0.21633 0.22043 0.21454 -0.01638 0.02135  0.01457  162 MET   A CB  
1236 C CG  . MET   A 162 ? 0.22384 0.22837 0.21652 -0.02057 0.02176  0.01824  162 MET   A CG  
1237 S SD  . MET   A 162 ? 0.29050 0.28083 0.27407 -0.02117 0.01648  0.02262  162 MET   A SD  
1238 C CE  . MET   A 162 ? 0.27052 0.25061 0.25292 -0.02609 0.01375  0.02444  162 MET   A CE  
1239 N N   . HIS   A 163 ? 0.19315 0.22028 0.20093 -0.01836 0.02980  0.01201  163 HIS   A N   
1240 C CA  . HIS   A 163 ? 0.19475 0.22851 0.20329 -0.01617 0.03268  0.00922  163 HIS   A CA  
1241 C C   . HIS   A 163 ? 0.20243 0.23470 0.20102 -0.01620 0.03266  0.00947  163 HIS   A C   
1242 O O   . HIS   A 163 ? 0.21110 0.24192 0.20349 -0.01978 0.03272  0.01401  163 HIS   A O   
1243 C CB  . HIS   A 163 ? 0.21546 0.25923 0.22941 -0.01718 0.03680  0.00997  163 HIS   A CB  
1244 C CG  . HIS   A 163 ? 0.20786 0.25739 0.22187 -0.01267 0.04010  0.00571  163 HIS   A CG  
1245 N ND1 . HIS   A 163 ? 0.22646 0.27200 0.24351 -0.00826 0.03818  0.00088  163 HIS   A ND1 
1246 C CD2 . HIS   A 163 ? 0.21869 0.27695 0.22940 -0.01139 0.04509  0.00526  163 HIS   A CD2 
1247 C CE1 . HIS   A 163 ? 0.23974 0.28856 0.25443 -0.00392 0.04095  -0.00352 163 HIS   A CE1 
1248 N NE2 . HIS   A 163 ? 0.24767 0.30537 0.25817 -0.00500 0.04588  -0.00130 163 HIS   A NE2 
1249 N N   . HIS   A 164 ? 0.17309 0.20462 0.16934 -0.01272 0.03164  0.00492  164 HIS   A N   
1250 C CA  . HIS   A 164 ? 0.18724 0.21719 0.17173 -0.01229 0.03071  0.00420  164 HIS   A CA  
1251 C C   . HIS   A 164 ? 0.24804 0.28213 0.22728 -0.00878 0.03385  -0.00135 164 HIS   A C   
1252 O O   . HIS   A 164 ? 0.27519 0.31193 0.24257 -0.00881 0.03609  -0.00086 164 HIS   A O   
1253 C CB  . HIS   A 164 ? 0.20375 0.22675 0.18670 -0.01133 0.02411  0.00336  164 HIS   A CB  
1254 C CG  . HIS   A 164 ? 0.22063 0.23916 0.20472 -0.01270 0.02105  0.00842  164 HIS   A CG  
1255 N ND1 . HIS   A 164 ? 0.20992 0.22408 0.18540 -0.01322 0.01721  0.01173  164 HIS   A ND1 
1256 C CD2 . HIS   A 164 ? 0.19088 0.20760 0.18255 -0.01262 0.02086  0.01025  164 HIS   A CD2 
1257 C CE1 . HIS   A 164 ? 0.21609 0.22533 0.19510 -0.01277 0.01475  0.01519  164 HIS   A CE1 
1258 N NE2 . HIS   A 164 ? 0.19364 0.20422 0.18160 -0.01224 0.01721  0.01382  164 HIS   A NE2 
1259 N N   . MET   A 165 ? 0.21806 0.25158 0.20419 -0.00517 0.03367  -0.00679 165 MET   A N   
1260 C CA  . MET   A 165 ? 0.29276 0.32605 0.27105 -0.00031 0.03508  -0.01381 165 MET   A CA  
1261 C C   . MET   A 165 ? 0.25532 0.28844 0.24325 0.00423  0.03612  -0.01860 165 MET   A C   
1262 O O   . MET   A 165 ? 0.25289 0.28437 0.25299 0.00289  0.03397  -0.01638 165 MET   A O   
1263 C CB  . MET   A 165 ? 0.31478 0.33839 0.28371 0.00010  0.02802  -0.01808 165 MET   A CB  
1264 C CG  . MET   A 165 ? 0.32315 0.34042 0.30244 -0.00234 0.02101  -0.01693 165 MET   A CG  
1265 S SD  . MET   A 165 ? 0.45293 0.46243 0.42217 -0.00373 0.01171  -0.01948 165 MET   A SD  
1266 C CE  . MET   A 165 ? 0.31784 0.32350 0.26943 0.00142  0.01329  -0.02903 165 MET   A CE  
1267 N N   . GLU   A 166 ? 0.29073 0.32499 0.27167 0.01036  0.03928  -0.02530 166 GLU   A N   
1268 C CA  . GLU   A 166 ? 0.29548 0.32596 0.28293 0.01672  0.03899  -0.03154 166 GLU   A CA  
1269 C C   . GLU   A 166 ? 0.37363 0.38860 0.35209 0.01945  0.03178  -0.03999 166 GLU   A C   
1270 O O   . GLU   A 166 ? 0.37659 0.38861 0.33911 0.02044  0.03088  -0.04418 166 GLU   A O   
1271 C CB  . GLU   A 166 ? 0.36880 0.41158 0.35560 0.02375  0.04778  -0.03421 166 GLU   A CB  
1272 C CG  . GLU   A 166 ? 0.38963 0.43156 0.38902 0.03022  0.04791  -0.03745 166 GLU   A CG  
1273 C CD  . GLU   A 166 ? 0.41839 0.47798 0.42244 0.03685  0.05731  -0.03756 166 GLU   A CD  
1274 O OE1 . GLU   A 166 ? 0.49029 0.55236 0.48371 0.04519  0.06205  -0.04501 166 GLU   A OE1 
1275 O OE2 . GLU   A 166 ? 0.41284 0.48501 0.43093 0.03376  0.05994  -0.03011 166 GLU   A OE2 
1276 N N   . LEU   A 167 ? 0.37985 0.38439 0.36781 0.02016  0.02596  -0.04210 167 LEU   A N   
1277 C CA  . LEU   A 167 ? 0.39570 0.38314 0.37739 0.02123  0.01711  -0.04962 167 LEU   A CA  
1278 C C   . LEU   A 167 ? 0.51268 0.49302 0.48756 0.03156  0.01865  -0.06015 167 LEU   A C   
1279 O O   . LEU   A 167 ? 0.50926 0.50051 0.48765 0.03822  0.02710  -0.06059 167 LEU   A O   
1280 C CB  . LEU   A 167 ? 0.41560 0.39524 0.41175 0.01530  0.00948  -0.04475 167 LEU   A CB  
1281 C CG  . LEU   A 167 ? 0.36537 0.35192 0.36717 0.00688  0.00786  -0.03578 167 LEU   A CG  
1282 C CD1 . LEU   A 167 ? 0.33113 0.31443 0.34805 0.00183  0.00276  -0.02989 167 LEU   A CD1 
1283 C CD2 . LEU   A 167 ? 0.42514 0.40863 0.41501 0.00404  0.00290  -0.03791 167 LEU   A CD2 
1284 N N   . PRO   A 168 ? 0.47490 0.43689 0.43993 0.03365  0.01014  -0.06927 168 PRO   A N   
1285 C CA  . PRO   A 168 ? 0.49829 0.45101 0.45425 0.04549  0.01143  -0.08122 168 PRO   A CA  
1286 C C   . PRO   A 168 ? 0.51254 0.46208 0.48434 0.05108  0.01210  -0.08076 168 PRO   A C   
1287 O O   . PRO   A 168 ? 0.51804 0.46924 0.48676 0.06301  0.01782  -0.08802 168 PRO   A O   
1288 C CB  . PRO   A 168 ? 0.51707 0.44687 0.45917 0.04432  -0.00088 -0.09064 168 PRO   A CB  
1289 C CG  . PRO   A 168 ? 0.50941 0.44117 0.45264 0.03212  -0.00729 -0.08314 168 PRO   A CG  
1290 C CD  . PRO   A 168 ? 0.46863 0.41842 0.42897 0.02583  -0.00111 -0.06967 168 PRO   A CD  
1291 N N   . THR   A 169 ? 0.49913 0.44507 0.48761 0.04351  0.00658  -0.07210 169 THR   A N   
1292 C CA  . THR   A 169 ? 0.52307 0.46617 0.52627 0.04829  0.00646  -0.06995 169 THR   A CA  
1293 C C   . THR   A 169 ? 0.49953 0.46573 0.51349 0.05060  0.01703  -0.06269 169 THR   A C   
1294 O O   . THR   A 169 ? 0.51784 0.48473 0.54501 0.05432  0.01692  -0.05942 169 THR   A O   
1295 C CB  . THR   A 169 ? 0.53245 0.46380 0.54825 0.03882  -0.00338 -0.06218 169 THR   A CB  
1296 O OG1 . THR   A 169 ? 0.49274 0.43871 0.51510 0.02839  -0.00113 -0.05118 169 THR   A OG1 
1297 C CG2 . THR   A 169 ? 0.52390 0.43158 0.53170 0.03544  -0.01563 -0.06879 169 THR   A CG2 
1298 N N   . GLY   A 170 ? 0.47859 0.46291 0.48744 0.04793  0.02501  -0.05951 170 GLY   A N   
1299 C CA  . GLY   A 170 ? 0.45456 0.46053 0.47357 0.04841  0.03380  -0.05235 170 GLY   A CA  
1300 C C   . GLY   A 170 ? 0.42983 0.44254 0.46012 0.03809  0.03235  -0.04082 170 GLY   A C   
1301 O O   . GLY   A 170 ? 0.37611 0.40509 0.41483 0.03724  0.03786  -0.03474 170 GLY   A O   
1302 N N   . VAL   A 171 ? 0.40954 0.41089 0.44047 0.03044  0.02494  -0.03769 171 VAL   A N   
1303 C CA  . VAL   A 171 ? 0.34037 0.34840 0.37916 0.02185  0.02439  -0.02782 171 VAL   A CA  
1304 C C   . VAL   A 171 ? 0.28525 0.30008 0.31553 0.01636  0.02701  -0.02568 171 VAL   A C   
1305 O O   . VAL   A 171 ? 0.29999 0.31425 0.31844 0.01836  0.02863  -0.03082 171 VAL   A O   
1306 C CB  . VAL   A 171 ? 0.32500 0.32110 0.37030 0.01681  0.01641  -0.02404 171 VAL   A CB  
1307 C CG1 . VAL   A 171 ? 0.36190 0.34941 0.41555 0.02192  0.01292  -0.02466 171 VAL   A CG1 
1308 C CG2 . VAL   A 171 ? 0.32405 0.30819 0.36166 0.01356  0.01019  -0.02819 171 VAL   A CG2 
1309 N N   . HIS   A 172 ? 0.28509 0.30554 0.32011 0.01003  0.02715  -0.01817 172 HIS   A N   
1310 C CA  . HIS   A 172 ? 0.25033 0.27701 0.27863 0.00589  0.02981  -0.01534 172 HIS   A CA  
1311 C C   . HIS   A 172 ? 0.22304 0.24525 0.25174 0.00056  0.02523  -0.01175 172 HIS   A C   
1312 O O   . HIS   A 172 ? 0.22261 0.24191 0.25924 -0.00128 0.02194  -0.00882 172 HIS   A O   
1313 C CB  . HIS   A 172 ? 0.24937 0.28782 0.28218 0.00440  0.03476  -0.01030 172 HIS   A CB  
1314 C CG  . HIS   A 172 ? 0.28205 0.32945 0.31782 0.00971  0.03977  -0.01254 172 HIS   A CG  
1315 N ND1 . HIS   A 172 ? 0.29815 0.34949 0.34517 0.01303  0.03979  -0.01148 172 HIS   A ND1 
1316 C CD2 . HIS   A 172 ? 0.30513 0.35973 0.33440 0.01314  0.04515  -0.01559 172 HIS   A CD2 
1317 C CE1 . HIS   A 172 ? 0.31903 0.38067 0.36818 0.01872  0.04507  -0.01390 172 HIS   A CE1 
1318 N NE2 . HIS   A 172 ? 0.31971 0.38411 0.35785 0.01891  0.04902  -0.01648 172 HIS   A NE2 
1319 N N   . ALA   A 173 ? 0.21989 0.24270 0.24023 -0.00156 0.02515  -0.01135 173 ALA   A N   
1320 C CA  . ALA   A 173 ? 0.20675 0.22733 0.22815 -0.00510 0.02097  -0.00821 173 ALA   A CA  
1321 C C   . ALA   A 173 ? 0.18604 0.21039 0.20243 -0.00690 0.02319  -0.00439 173 ALA   A C   
1322 O O   . ALA   A 173 ? 0.20083 0.22766 0.20974 -0.00671 0.02651  -0.00456 173 ALA   A O   
1323 C CB  . ALA   A 173 ? 0.25152 0.26539 0.26807 -0.00547 0.01503  -0.01204 173 ALA   A CB  
1324 N N   . GLY   A 174 ? 0.19181 0.21657 0.21247 -0.00842 0.02132  -0.00059 174 GLY   A N   
1325 C CA  . GLY   A 174 ? 0.19306 0.21805 0.20925 -0.00920 0.02222  0.00267  174 GLY   A CA  
1326 C C   . GLY   A 174 ? 0.16000 0.18542 0.18103 -0.00852 0.01958  0.00527  174 GLY   A C   
1327 O O   . GLY   A 174 ? 0.17876 0.20644 0.20701 -0.00856 0.01704  0.00544  174 GLY   A O   
1328 N N   . THR   A 175 ? 0.17038 0.19375 0.18784 -0.00777 0.02004  0.00758  175 THR   A N   
1329 C CA  . THR   A 175 ? 0.15868 0.18278 0.17940 -0.00496 0.01809  0.00955  175 THR   A CA  
1330 C C   . THR   A 175 ? 0.18486 0.20827 0.20627 -0.00293 0.02079  0.01016  175 THR   A C   
1331 O O   . THR   A 175 ? 0.17472 0.19563 0.19293 -0.00487 0.02279  0.00954  175 THR   A O   
1332 C CB  . THR   A 175 ? 0.18904 0.20804 0.20258 -0.00401 0.01476  0.01105  175 THR   A CB  
1333 O OG1 . THR   A 175 ? 0.20254 0.21439 0.20823 -0.00522 0.01611  0.01217  175 THR   A OG1 
1334 C CG2 . THR   A 175 ? 0.18192 0.20080 0.19055 -0.00609 0.01173  0.01005  175 THR   A CG2 
1335 N N   . ASP   A 176 ? 0.18735 0.21377 0.21276 0.00144  0.02055  0.01121  176 ASP   A N   
1336 C CA  . ASP   A 176 ? 0.17397 0.19659 0.19541 0.00532  0.02239  0.01042  176 ASP   A CA  
1337 C C   . ASP   A 176 ? 0.21695 0.22745 0.22940 0.00644  0.01934  0.01021  176 ASP   A C   
1338 O O   . ASP   A 176 ? 0.20210 0.20924 0.21149 0.00368  0.01662  0.01173  176 ASP   A O   
1339 C CB  . ASP   A 176 ? 0.21311 0.24530 0.24184 0.01102  0.02456  0.01140  176 ASP   A CB  
1340 C CG  . ASP   A 176 ? 0.25024 0.28763 0.28556 0.01480  0.02183  0.01334  176 ASP   A CG  
1341 O OD1 . ASP   A 176 ? 0.20709 0.23633 0.23736 0.01509  0.01776  0.01336  176 ASP   A OD1 
1342 O OD2 . ASP   A 176 ? 0.24270 0.29365 0.28896 0.01738  0.02358  0.01578  176 ASP   A OD2 
1343 N N   . LEU   A 177 ? 0.20090 0.20339 0.20765 0.01040  0.01925  0.00844  177 LEU   A N   
1344 C CA  . LEU   A 177 ? 0.21421 0.20170 0.21206 0.01011  0.01510  0.00889  177 LEU   A CA  
1345 C C   . LEU   A 177 ? 0.22671 0.21149 0.22569 0.01668  0.01191  0.01021  177 LEU   A C   
1346 O O   . LEU   A 177 ? 0.29433 0.26504 0.28602 0.01702  0.00746  0.01159  177 LEU   A O   
1347 C CB  . LEU   A 177 ? 0.23301 0.20862 0.22255 0.01070  0.01427  0.00579  177 LEU   A CB  
1348 C CG  . LEU   A 177 ? 0.25467 0.22603 0.24043 0.00150  0.01325  0.00681  177 LEU   A CG  
1349 C CD1 . LEU   A 177 ? 0.26981 0.23468 0.25248 -0.00475 0.01014  0.01135  177 LEU   A CD1 
1350 C CD2 . LEU   A 177 ? 0.25436 0.24072 0.24763 -0.00216 0.01748  0.00727  177 LEU   A CD2 
1351 N N   . GLU   A 178 ? 0.19489 0.19309 0.20383 0.02156  0.01347  0.01068  178 GLU   A N   
1352 C CA  . GLU   A 178 ? 0.27077 0.27115 0.28427 0.02660  0.00960  0.01324  178 GLU   A CA  
1353 C C   . GLU   A 178 ? 0.23059 0.23570 0.24584 0.02034  0.00632  0.01646  178 GLU   A C   
1354 O O   . GLU   A 178 ? 0.24709 0.25524 0.26616 0.02334  0.00180  0.01916  178 GLU   A O   
1355 C CB  . GLU   A 178 ? 0.25450 0.27017 0.28006 0.03465  0.01257  0.01302  178 GLU   A CB  
1356 C CG  . GLU   A 178 ? 0.31052 0.32157 0.33177 0.04342  0.01609  0.00890  178 GLU   A CG  
1357 C CD  . GLU   A 178 ? 0.40673 0.43416 0.43977 0.05377  0.01940  0.00945  178 GLU   A CD  
1358 O OE1 . GLU   A 178 ? 0.41059 0.45772 0.45727 0.05107  0.02154  0.01323  178 GLU   A OE1 
1359 O OE2 . GLU   A 178 ? 0.47726 0.49812 0.50630 0.06470  0.01986  0.00613  178 GLU   A OE2 
1360 N N   . GLY   A 179 ? 0.21804 0.22426 0.23034 0.01255  0.00818  0.01587  179 GLY   A N   
1361 C CA  . GLY   A 179 ? 0.19922 0.20768 0.20928 0.00753  0.00532  0.01736  179 GLY   A CA  
1362 C C   . GLY   A 179 ? 0.21854 0.23932 0.23850 0.00631  0.00444  0.01680  179 GLY   A C   
1363 O O   . GLY   A 179 ? 0.21506 0.23619 0.23162 0.00303  0.00065  0.01696  179 GLY   A O   
1364 N N   . ASN   A 180 ? 0.20853 0.23892 0.23971 0.00839  0.00735  0.01642  180 ASN   A N   
1365 C CA  . ASN   A 180 ? 0.18175 0.22321 0.22401 0.00568  0.00554  0.01723  180 ASN   A CA  
1366 C C   . ASN   A 180 ? 0.17688 0.21701 0.21797 0.00036  0.00822  0.01484  180 ASN   A C   
1367 O O   . ASN   A 180 ? 0.17799 0.21822 0.21933 0.00072  0.01325  0.01426  180 ASN   A O   
1368 C CB  . ASN   A 180 ? 0.19626 0.25137 0.25291 0.00998  0.00751  0.02003  180 ASN   A CB  
1369 C CG  . ASN   A 180 ? 0.25270 0.31111 0.31309 0.01718  0.00478  0.02224  180 ASN   A CG  
1370 O OD1 . ASN   A 180 ? 0.34377 0.40213 0.40391 0.02451  0.00860  0.02174  180 ASN   A OD1 
1371 N ND2 . ASN   A 180 ? 0.23920 0.29927 0.30183 0.01583  -0.00251 0.02424  180 ASN   A ND2 
1372 N N   . PHE   A 181 ? 0.16264 0.20077 0.20166 -0.00386 0.00423  0.01312  181 PHE   A N   
1373 C CA  . PHE   A 181 ? 0.16296 0.19846 0.20127 -0.00736 0.00608  0.01026  181 PHE   A CA  
1374 C C   . PHE   A 181 ? 0.15340 0.19626 0.20433 -0.00841 0.00803  0.01277  181 PHE   A C   
1375 O O   . PHE   A 181 ? 0.17545 0.22750 0.23766 -0.00867 0.00591  0.01653  181 PHE   A O   
1376 C CB  . PHE   A 181 ? 0.17478 0.20586 0.20869 -0.01040 0.00044  0.00692  181 PHE   A CB  
1377 C CG  . PHE   A 181 ? 0.19817 0.22191 0.21708 -0.01005 0.00204  0.00324  181 PHE   A CG  
1378 C CD1 . PHE   A 181 ? 0.22029 0.24119 0.23593 -0.01010 0.00650  -0.00012 181 PHE   A CD1 
1379 C CD2 . PHE   A 181 ? 0.23270 0.25387 0.24121 -0.00936 -0.00059 0.00408  181 PHE   A CD2 
1380 C CE1 . PHE   A 181 ? 0.22478 0.24275 0.22795 -0.00933 0.00938  -0.00273 181 PHE   A CE1 
1381 C CE2 . PHE   A 181 ? 0.22926 0.24607 0.22357 -0.00950 0.00197  0.00211  181 PHE   A CE2 
1382 C CZ  . PHE   A 181 ? 0.22941 0.24580 0.22148 -0.00942 0.00755  -0.00138 181 PHE   A CZ  
1383 N N   . TYR   A 182 ? 0.16643 0.20665 0.21600 -0.00920 0.01201  0.01167  182 TYR   A N   
1384 C CA  . TYR   A 182 ? 0.16391 0.20807 0.22324 -0.01181 0.01223  0.01422  182 TYR   A CA  
1385 C C   . TYR   A 182 ? 0.15905 0.19748 0.22044 -0.01574 0.00611  0.01197  182 TYR   A C   
1386 O O   . TYR   A 182 ? 0.22733 0.25696 0.27955 -0.01517 0.00506  0.00658  182 TYR   A O   
1387 C CB  . TYR   A 182 ? 0.15462 0.19666 0.21095 -0.01104 0.01704  0.01398  182 TYR   A CB  
1388 C CG  . TYR   A 182 ? 0.20018 0.24596 0.25334 -0.00766 0.02180  0.01553  182 TYR   A CG  
1389 C CD1 . TYR   A 182 ? 0.18164 0.23640 0.24095 -0.00660 0.02451  0.01989  182 TYR   A CD1 
1390 C CD2 . TYR   A 182 ? 0.16958 0.20953 0.21290 -0.00583 0.02342  0.01272  182 TYR   A CD2 
1391 C CE1 . TYR   A 182 ? 0.20986 0.26628 0.26337 -0.00235 0.02864  0.01971  182 TYR   A CE1 
1392 C CE2 . TYR   A 182 ? 0.16834 0.20817 0.20713 -0.00292 0.02618  0.01300  182 TYR   A CE2 
1393 C CZ  . TYR   A 182 ? 0.16666 0.21402 0.20952 -0.00051 0.02876  0.01566  182 TYR   A CZ  
1394 O OH  . TYR   A 182 ? 0.19122 0.23689 0.22681 0.00352  0.03128  0.01442  182 TYR   A OH  
1395 N N   . GLY   A 183 ? 0.17654 0.22008 0.24971 -0.01969 0.00187  0.01604  183 GLY   A N   
1396 C CA  . GLY   A 183 ? 0.17290 0.20820 0.24799 -0.02423 -0.00580 0.01367  183 GLY   A CA  
1397 C C   . GLY   A 183 ? 0.23252 0.26525 0.30313 -0.02516 -0.01282 0.01036  183 GLY   A C   
1398 O O   . GLY   A 183 ? 0.22055 0.25987 0.28941 -0.02258 -0.01209 0.01166  183 GLY   A O   
1399 N N   . PRO   A 184 ? 0.22539 0.24707 0.29315 -0.02857 -0.02065 0.00586  184 PRO   A N   
1400 C CA  . PRO   A 184 ? 0.25596 0.27521 0.31993 -0.03089 -0.02973 0.00322  184 PRO   A CA  
1401 C C   . PRO   A 184 ? 0.28178 0.29272 0.32563 -0.02622 -0.02906 -0.00436 184 PRO   A C   
1402 O O   . PRO   A 184 ? 0.35696 0.36130 0.39218 -0.02778 -0.03732 -0.00881 184 PRO   A O   
1403 C CB  . PRO   A 184 ? 0.26963 0.27833 0.33877 -0.03726 -0.03931 0.00146  184 PRO   A CB  
1404 C CG  . PRO   A 184 ? 0.26667 0.26436 0.33050 -0.03406 -0.03415 -0.00249 184 PRO   A CG  
1405 C CD  . PRO   A 184 ? 0.25973 0.26964 0.32832 -0.03052 -0.02294 0.00329  184 PRO   A CD  
1406 N N   . PHE   A 185 ? 0.27394 0.28580 0.30976 -0.02110 -0.01974 -0.00532 185 PHE   A N   
1407 C CA  . PHE   A 185 ? 0.23436 0.23936 0.25157 -0.01732 -0.01763 -0.01164 185 PHE   A CA  
1408 C C   . PHE   A 185 ? 0.22669 0.23626 0.23602 -0.01613 -0.01818 -0.00903 185 PHE   A C   
1409 O O   . PHE   A 185 ? 0.23311 0.25111 0.25169 -0.01617 -0.01782 -0.00270 185 PHE   A O   
1410 C CB  . PHE   A 185 ? 0.23696 0.24161 0.25116 -0.01353 -0.00815 -0.01310 185 PHE   A CB  
1411 C CG  . PHE   A 185 ? 0.23097 0.23181 0.25496 -0.01419 -0.00801 -0.01369 185 PHE   A CG  
1412 C CD1 . PHE   A 185 ? 0.29262 0.28151 0.31293 -0.01409 -0.01369 -0.02023 185 PHE   A CD1 
1413 C CD2 . PHE   A 185 ? 0.23440 0.24193 0.26975 -0.01463 -0.00308 -0.00782 185 PHE   A CD2 
1414 C CE1 . PHE   A 185 ? 0.30456 0.28750 0.33393 -0.01466 -0.01485 -0.01999 185 PHE   A CE1 
1415 C CE2 . PHE   A 185 ? 0.24030 0.24384 0.28386 -0.01555 -0.00381 -0.00704 185 PHE   A CE2 
1416 C CZ  . PHE   A 185 ? 0.26284 0.25376 0.30422 -0.01566 -0.00985 -0.01264 185 PHE   A CZ  
1417 N N   . VAL   A 186 ? 0.27871 0.28221 0.27001 -0.01447 -0.01937 -0.01399 186 VAL   A N   
1418 C CA  . VAL   A 186 ? 0.25962 0.26513 0.23956 -0.01349 -0.02027 -0.01119 186 VAL   A CA  
1419 C C   . VAL   A 186 ? 0.24759 0.25147 0.21184 -0.01061 -0.01213 -0.01333 186 VAL   A C   
1420 O O   . VAL   A 186 ? 0.28083 0.28162 0.24034 -0.00857 -0.00798 -0.01925 186 VAL   A O   
1421 C CB  . VAL   A 186 ? 0.24649 0.24809 0.21818 -0.01558 -0.03155 -0.01351 186 VAL   A CB  
1422 C CG1 . VAL   A 186 ? 0.31097 0.31819 0.30164 -0.01938 -0.03988 -0.00931 186 VAL   A CG1 
1423 C CG2 . VAL   A 186 ? 0.27106 0.26212 0.22836 -0.01498 -0.03421 -0.02326 186 VAL   A CG2 
1424 N N   . ASP   A 187 ? 0.23397 0.24056 0.19129 -0.01033 -0.00983 -0.00777 187 ASP   A N   
1425 C CA  . ASP   A 187 ? 0.22536 0.23317 0.17020 -0.00919 -0.00173 -0.00727 187 ASP   A CA  
1426 C C   . ASP   A 187 ? 0.27313 0.27799 0.19681 -0.00848 -0.00446 -0.01056 187 ASP   A C   
1427 O O   . ASP   A 187 ? 0.29076 0.29593 0.20292 -0.00955 -0.00585 -0.00526 187 ASP   A O   
1428 C CB  . ASP   A 187 ? 0.24019 0.25053 0.18808 -0.01037 0.00196  0.00106  187 ASP   A CB  
1429 C CG  . ASP   A 187 ? 0.27512 0.28349 0.22477 -0.01069 -0.00535 0.00672  187 ASP   A CG  
1430 O OD1 . ASP   A 187 ? 0.28495 0.29309 0.23782 -0.01051 -0.01330 0.00524  187 ASP   A OD1 
1431 O OD2 . ASP   A 187 ? 0.24563 0.25248 0.19447 -0.01110 -0.00364 0.01304  187 ASP   A OD2 
1432 N N   . ARG   A 188 ? 0.27047 0.27138 0.18765 -0.00620 -0.00523 -0.01963 188 ARG   A N   
1433 C CA  . ARG   A 188 ? 0.29503 0.29208 0.18941 -0.00419 -0.00753 -0.02539 188 ARG   A CA  
1434 C C   . ARG   A 188 ? 0.34984 0.34479 0.23893 0.00096  -0.00175 -0.03526 188 ARG   A C   
1435 O O   . ARG   A 188 ? 0.30872 0.30025 0.21230 0.00187  -0.00220 -0.03901 188 ARG   A O   
1436 C CB  . ARG   A 188 ? 0.32155 0.31127 0.21226 -0.00650 -0.02128 -0.02788 188 ARG   A CB  
1437 C CG  . ARG   A 188 ? 0.39381 0.37507 0.26266 -0.00391 -0.02604 -0.03831 188 ARG   A CG  
1438 C CD  . ARG   A 188 ? 0.42508 0.39902 0.29200 -0.00767 -0.04162 -0.04031 188 ARG   A CD  
1439 N NE  . ARG   A 188 ? 0.48555 0.45126 0.32441 -0.00532 -0.04682 -0.04905 188 ARG   A NE  
1440 C CZ  . ARG   A 188 ? 0.51371 0.47002 0.34551 -0.00818 -0.06155 -0.05428 188 ARG   A CZ  
1441 N NH1 . ARG   A 188 ? 0.50989 0.46635 0.36284 -0.01411 -0.07234 -0.05024 188 ARG   A NH1 
1442 N NH2 . ARG   A 188 ? 0.53544 0.48284 0.33822 -0.00508 -0.06564 -0.06380 188 ARG   A NH2 
1443 N N   . GLN   A 189 ? 0.31593 0.31345 0.18420 0.00494  0.00394  -0.03899 189 GLN   A N   
1444 C CA  . GLN   A 189 ? 0.36950 0.36575 0.23116 0.01222  0.01000  -0.04942 189 GLN   A CA  
1445 C C   . GLN   A 189 ? 0.38925 0.36955 0.23979 0.01462  -0.00089 -0.06137 189 GLN   A C   
1446 O O   . GLN   A 189 ? 0.39916 0.37462 0.22517 0.01808  -0.00318 -0.06846 189 GLN   A O   
1447 C CB  . GLN   A 189 ? 0.35584 0.36385 0.20022 0.01635  0.02158  -0.04856 189 GLN   A CB  
1448 C CG  . GLN   A 189 ? 0.40633 0.41572 0.24446 0.02619  0.02930  -0.05971 189 GLN   A CG  
1449 C CD  . GLN   A 189 ? 0.43046 0.45702 0.25506 0.03015  0.04277  -0.05687 189 GLN   A CD  
1450 O OE1 . GLN   A 189 ? 0.45683 0.49638 0.28727 0.02422  0.04853  -0.04430 189 GLN   A OE1 
1451 N NE2 . GLN   A 189 ? 0.41088 0.43760 0.21707 0.04019  0.04778  -0.06829 189 GLN   A NE2 
1452 N N   . THR   A 190 ? 0.37550 0.34690 0.24385 0.01222  -0.00830 -0.06337 190 THR   A N   
1453 C CA  . THR   A 190 ? 0.42320 0.37726 0.28519 0.01290  -0.02012 -0.07408 190 THR   A CA  
1454 C C   . THR   A 190 ? 0.45526 0.40293 0.33719 0.01393  -0.02030 -0.07652 190 THR   A C   
1455 O O   . THR   A 190 ? 0.45199 0.40948 0.35352 0.01231  -0.01361 -0.06840 190 THR   A O   
1456 C CB  . THR   A 190 ? 0.45412 0.40330 0.31697 0.00482  -0.03446 -0.07044 190 THR   A CB  
1457 O OG1 . THR   A 190 ? 0.49133 0.42273 0.34291 0.00482  -0.04718 -0.08168 190 THR   A OG1 
1458 C CG2 . THR   A 190 ? 0.46274 0.41805 0.35420 -0.00204 -0.03699 -0.06000 190 THR   A CG2 
1459 N N   . ALA   A 191 ? 0.47389 0.40368 0.34903 0.01692  -0.02840 -0.08794 191 ALA   A N   
1460 C CA  . ALA   A 191 ? 0.46822 0.38882 0.36121 0.01756  -0.03046 -0.08974 191 ALA   A CA  
1461 C C   . ALA   A 191 ? 0.41689 0.33993 0.33363 0.00686  -0.03763 -0.07892 191 ALA   A C   
1462 O O   . ALA   A 191 ? 0.44769 0.36755 0.36433 -0.00045 -0.04865 -0.07685 191 ALA   A O   
1463 C CB  . ALA   A 191 ? 0.51024 0.40717 0.38940 0.02239  -0.04005 -0.10438 191 ALA   A CB  
1464 N N   . GLN   A 192 ? 0.40935 0.33983 0.34645 0.00616  -0.03129 -0.07160 192 GLN   A N   
1465 C CA  . GLN   A 192 ? 0.38711 0.32372 0.34619 -0.00276 -0.03519 -0.06049 192 GLN   A CA  
1466 C C   . GLN   A 192 ? 0.42172 0.35175 0.39705 -0.00307 -0.03578 -0.05888 192 GLN   A C   
1467 O O   . GLN   A 192 ? 0.40283 0.33509 0.37998 0.00355  -0.02719 -0.06011 192 GLN   A O   
1468 C CB  . GLN   A 192 ? 0.37471 0.33077 0.34062 -0.00430 -0.02607 -0.05011 192 GLN   A CB  
1469 C CG  . GLN   A 192 ? 0.34220 0.30323 0.29494 -0.00585 -0.02835 -0.04902 192 GLN   A CG  
1470 C CD  . GLN   A 192 ? 0.32281 0.29900 0.28268 -0.00763 -0.02178 -0.03876 192 GLN   A CD  
1471 O OE1 . GLN   A 192 ? 0.27323 0.25581 0.25023 -0.01181 -0.02311 -0.03109 192 GLN   A OE1 
1472 N NE2 . GLN   A 192 ? 0.34579 0.32757 0.29183 -0.00436 -0.01482 -0.03839 192 GLN   A NE2 
1473 N N   . ALA   A 193 ? 0.40237 0.32542 0.39028 -0.01123 -0.04635 -0.05502 193 ALA   A N   
1474 C CA  . ALA   A 193 ? 0.40508 0.31967 0.40777 -0.01322 -0.04910 -0.05205 193 ALA   A CA  
1475 C C   . ALA   A 193 ? 0.38631 0.31849 0.40817 -0.01779 -0.04259 -0.03858 193 ALA   A C   
1476 O O   . ALA   A 193 ? 0.34935 0.29408 0.37948 -0.02417 -0.04382 -0.03078 193 ALA   A O   
1477 C CB  . ALA   A 193 ? 0.42727 0.32414 0.43338 -0.02104 -0.06486 -0.05405 193 ALA   A CB  
1478 N N   . ALA   A 194 ? 0.35517 0.28877 0.38328 -0.01360 -0.03573 -0.03623 194 ALA   A N   
1479 C CA  . ALA   A 194 ? 0.38839 0.33299 0.43371 -0.01860 -0.03264 -0.02425 194 ALA   A CA  
1480 C C   . ALA   A 194 ? 0.40631 0.33732 0.46254 -0.02504 -0.04269 -0.02073 194 ALA   A C   
1481 O O   . ALA   A 194 ? 0.50778 0.41845 0.55815 -0.02255 -0.04988 -0.02864 194 ALA   A O   
1482 C CB  . ALA   A 194 ? 0.32401 0.27651 0.37047 -0.01200 -0.02209 -0.02252 194 ALA   A CB  
1483 N N   . GLY   A 195 ? 0.41827 0.36005 0.48993 -0.03325 -0.04340 -0.00873 195 GLY   A N   
1484 C CA  . GLY   A 195 ? 0.49737 0.42794 0.58093 -0.04093 -0.05249 -0.00263 195 GLY   A CA  
1485 C C   . GLY   A 195 ? 0.39677 0.31552 0.48078 -0.03570 -0.05098 -0.00288 195 GLY   A C   
1486 O O   . GLY   A 195 ? 0.34713 0.27021 0.42474 -0.02649 -0.04219 -0.00665 195 GLY   A O   
1487 N N   . THR   A 196 ? 0.35995 0.26347 0.45271 -0.04205 -0.06056 0.00201  196 THR   A N   
1488 C CA  . THR   A 196 ? 0.36091 0.25594 0.45732 -0.03813 -0.05935 0.00567  196 THR   A CA  
1489 C C   . THR   A 196 ? 0.36618 0.28482 0.46873 -0.03792 -0.04789 0.01635  196 THR   A C   
1490 O O   . THR   A 196 ? 0.34781 0.28495 0.45754 -0.04491 -0.04452 0.02529  196 THR   A O   
1491 C CB  . THR   A 196 ? 0.43445 0.31042 0.54108 -0.04721 -0.07193 0.01285  196 THR   A CB  
1492 O OG1 . THR   A 196 ? 0.54206 0.43566 0.66352 -0.05880 -0.07060 0.02934  196 THR   A OG1 
1493 C CG2 . THR   A 196 ? 0.37637 0.23133 0.47829 -0.05158 -0.08535 0.00402  196 THR   A CG2 
1494 N N   . ASP   A 197 ? 0.36621 0.28512 0.46534 -0.02912 -0.04193 0.01468  197 ASP   A N   
1495 C CA  . ASP   A 197 ? 0.37549 0.31432 0.47840 -0.02913 -0.03271 0.02401  197 ASP   A CA  
1496 C C   . ASP   A 197 ? 0.40019 0.33455 0.51277 -0.03461 -0.03678 0.03672  197 ASP   A C   
1497 O O   . ASP   A 197 ? 0.41132 0.32478 0.52703 -0.03565 -0.04611 0.03689  197 ASP   A O   
1498 C CB  . ASP   A 197 ? 0.39071 0.33564 0.48619 -0.01838 -0.02465 0.01747  197 ASP   A CB  
1499 C CG  . ASP   A 197 ? 0.33273 0.29921 0.42830 -0.01903 -0.01543 0.02405  197 ASP   A CG  
1500 O OD1 . ASP   A 197 ? 0.28178 0.26017 0.38080 -0.02580 -0.01345 0.03133  197 ASP   A OD1 
1501 O OD2 . ASP   A 197 ? 0.29293 0.26439 0.38537 -0.01237 -0.01054 0.02177  197 ASP   A OD2 
1502 N N   . THR   A 198 ? 0.33655 0.28967 0.45277 -0.03821 -0.03018 0.04756  198 THR   A N   
1503 C CA  . THR   A 198 ? 0.33315 0.28580 0.45637 -0.04340 -0.03240 0.06133  198 THR   A CA  
1504 C C   . THR   A 198 ? 0.28908 0.25426 0.40725 -0.03742 -0.02453 0.06424  198 THR   A C   
1505 O O   . THR   A 198 ? 0.28117 0.25818 0.39233 -0.03175 -0.01704 0.05736  198 THR   A O   
1506 C CB  . THR   A 198 ? 0.36092 0.32592 0.49347 -0.05535 -0.03280 0.07404  198 THR   A CB  
1507 O OG1 . THR   A 198 ? 0.37936 0.36795 0.50916 -0.05432 -0.02283 0.07395  198 THR   A OG1 
1508 C CG2 . THR   A 198 ? 0.42582 0.37777 0.56498 -0.06274 -0.04287 0.07191  198 THR   A CG2 
1509 N N   . THR   A 199 ? 0.28435 0.24521 0.40572 -0.03908 -0.02755 0.07469  199 THR   A N   
1510 C CA  . THR   A 199 ? 0.23538 0.20727 0.35155 -0.03439 -0.02214 0.07858  199 THR   A CA  
1511 C C   . THR   A 199 ? 0.27695 0.26958 0.39089 -0.04023 -0.01510 0.08866  199 THR   A C   
1512 O O   . THR   A 199 ? 0.24955 0.24599 0.36963 -0.04907 -0.01636 0.09940  199 THR   A O   
1513 C CB  . THR   A 199 ? 0.31607 0.27392 0.43545 -0.03249 -0.02928 0.08547  199 THR   A CB  
1514 O OG1 . THR   A 199 ? 0.32176 0.25997 0.44311 -0.02518 -0.03543 0.07490  199 THR   A OG1 
1515 C CG2 . THR   A 199 ? 0.25011 0.21965 0.36377 -0.02742 -0.02512 0.08879  199 THR   A CG2 
1516 N N   . ILE   A 200 ? 0.23888 0.24518 0.34397 -0.03513 -0.00776 0.08512  200 ILE   A N   
1517 C CA  . ILE   A 200 ? 0.24118 0.26653 0.34080 -0.03796 -0.00022 0.09164  200 ILE   A CA  
1518 C C   . ILE   A 200 ? 0.23692 0.26468 0.33408 -0.04078 -0.00159 0.10507  200 ILE   A C   
1519 O O   . ILE   A 200 ? 0.21550 0.24399 0.30504 -0.03608 -0.00167 0.10469  200 ILE   A O   
1520 C CB  . ILE   A 200 ? 0.22349 0.25846 0.31296 -0.03157 0.00646  0.08185  200 ILE   A CB  
1521 C CG1 . ILE   A 200 ? 0.24911 0.27890 0.34032 -0.02849 0.00647  0.06937  200 ILE   A CG1 
1522 C CG2 . ILE   A 200 ? 0.23484 0.28730 0.31781 -0.03305 0.01414  0.08642  200 ILE   A CG2 
1523 C CD1 . ILE   A 200 ? 0.20920 0.24222 0.29200 -0.02212 0.01019  0.05966  200 ILE   A CD1 
1524 N N   . THR   A 201 ? 0.23172 0.26182 0.33552 -0.04923 -0.00307 0.11796  201 THR   A N   
1525 C CA  . THR   A 201 ? 0.22633 0.25522 0.32881 -0.05324 -0.00623 0.13281  201 THR   A CA  
1526 C C   . THR   A 201 ? 0.22661 0.27200 0.31460 -0.05036 0.00088  0.13656  201 THR   A C   
1527 O O   . THR   A 201 ? 0.23898 0.28057 0.32051 -0.04863 -0.00272 0.14228  201 THR   A O   
1528 C CB  . THR   A 201 ? 0.27004 0.30087 0.38332 -0.06450 -0.00841 0.14704  201 THR   A CB  
1529 O OG1 . THR   A 201 ? 0.27622 0.28984 0.40148 -0.06753 -0.01636 0.14178  201 THR   A OG1 
1530 C CG2 . THR   A 201 ? 0.27798 0.30527 0.39021 -0.06983 -0.01279 0.16438  201 THR   A CG2 
1531 N N   . VAL   A 202 ? 0.21591 0.27901 0.29792 -0.04931 0.01029  0.13330  202 VAL   A N   
1532 C CA  . VAL   A 202 ? 0.24418 0.32127 0.30989 -0.04622 0.01667  0.13621  202 VAL   A CA  
1533 C C   . VAL   A 202 ? 0.24402 0.31383 0.29943 -0.03862 0.01384  0.12566  202 VAL   A C   
1534 O O   . VAL   A 202 ? 0.22634 0.30004 0.26860 -0.03689 0.01360  0.12968  202 VAL   A O   
1535 C CB  . VAL   A 202 ? 0.24127 0.33745 0.30268 -0.04472 0.02731  0.13334  202 VAL   A CB  
1536 C CG1 . VAL   A 202 ? 0.26059 0.35303 0.32552 -0.03972 0.02848  0.11757  202 VAL   A CG1 
1537 C CG2 . VAL   A 202 ? 0.24076 0.35012 0.28230 -0.04058 0.03401  0.13548  202 VAL   A CG2 
1538 N N   . ASN   A 203 ? 0.22261 0.28264 0.28398 -0.03456 0.01117  0.11286  203 ASN   A N   
1539 C CA  . ASN   A 203 ? 0.19924 0.25437 0.25459 -0.02844 0.00821  0.10393  203 ASN   A CA  
1540 C C   . ASN   A 203 ? 0.24081 0.28615 0.29995 -0.02786 -0.00037 0.11040  203 ASN   A C   
1541 O O   . ASN   A 203 ? 0.22070 0.26804 0.27191 -0.02478 -0.00308 0.11027  203 ASN   A O   
1542 C CB  . ASN   A 203 ? 0.23201 0.28154 0.29370 -0.02480 0.00858  0.09027  203 ASN   A CB  
1543 C CG  . ASN   A 203 ? 0.20206 0.26038 0.25728 -0.02346 0.01583  0.08277  203 ASN   A CG  
1544 O OD1 . ASN   A 203 ? 0.22693 0.29582 0.27450 -0.02450 0.02121  0.08699  203 ASN   A OD1 
1545 N ND2 . ASN   A 203 ? 0.19145 0.24572 0.24914 -0.02042 0.01620  0.07174  203 ASN   A ND2 
1546 N N   . VAL   A 204 ? 0.25909 0.29291 0.33051 -0.03068 -0.00580 0.11622  204 VAL   A N   
1547 C CA  . VAL   A 204 ? 0.23009 0.25277 0.30588 -0.02897 -0.01468 0.12287  204 VAL   A CA  
1548 C C   . VAL   A 204 ? 0.26193 0.29153 0.32723 -0.03236 -0.01577 0.13703  204 VAL   A C   
1549 O O   . VAL   A 204 ? 0.29048 0.31832 0.35210 -0.02886 -0.02146 0.14001  204 VAL   A O   
1550 C CB  . VAL   A 204 ? 0.27426 0.27968 0.36398 -0.03130 -0.02113 0.12586  204 VAL   A CB  
1551 C CG1 . VAL   A 204 ? 0.27343 0.26611 0.36713 -0.02985 -0.03085 0.13576  204 VAL   A CG1 
1552 C CG2 . VAL   A 204 ? 0.23933 0.23687 0.33627 -0.02623 -0.02090 0.11058  204 VAL   A CG2 
1553 N N   . LEU   A 205 ? 0.24794 0.28705 0.30840 -0.03906 -0.01034 0.14648  205 LEU   A N   
1554 C CA  . LEU   A 205 ? 0.28944 0.33763 0.33680 -0.04225 -0.00969 0.16021  205 LEU   A CA  
1555 C C   . LEU   A 205 ? 0.26082 0.31902 0.29055 -0.03690 -0.00699 0.15339  205 LEU   A C   
1556 O O   . LEU   A 205 ? 0.27420 0.33318 0.29361 -0.03634 -0.01186 0.16089  205 LEU   A O   
1557 C CB  . LEU   A 205 ? 0.26825 0.32903 0.31456 -0.04987 -0.00213 0.17084  205 LEU   A CB  
1558 C CG  . LEU   A 205 ? 0.27502 0.32572 0.33886 -0.05782 -0.00673 0.18058  205 LEU   A CG  
1559 C CD1 . LEU   A 205 ? 0.28337 0.35138 0.34937 -0.06541 0.00187  0.18955  205 LEU   A CD1 
1560 C CD2 . LEU   A 205 ? 0.31822 0.35681 0.38273 -0.06120 -0.01645 0.19605  205 LEU   A CD2 
1561 N N   . ALA   A 206 ? 0.24645 0.31119 0.27179 -0.03332 -0.00034 0.13955  206 ALA   A N   
1562 C CA  . ALA   A 206 ? 0.26191 0.33260 0.27046 -0.02884 0.00043  0.13201  206 ALA   A CA  
1563 C C   . ALA   A 206 ? 0.28735 0.35009 0.29949 -0.02544 -0.00945 0.12961  206 ALA   A C   
1564 O O   . ALA   A 206 ? 0.26779 0.33387 0.26660 -0.02441 -0.01371 0.13217  206 ALA   A O   
1565 C CB  . ALA   A 206 ? 0.23299 0.30776 0.23886 -0.02559 0.00746  0.11736  206 ALA   A CB  
1566 N N   . TRP   A 207 ? 0.25505 0.30809 0.28521 -0.02332 -0.01346 0.12491  207 TRP   A N   
1567 C CA  . TRP   A 207 ? 0.28859 0.33697 0.32596 -0.01875 -0.02183 0.12227  207 TRP   A CA  
1568 C C   . TRP   A 207 ? 0.28217 0.32606 0.31998 -0.01938 -0.03051 0.13646  207 TRP   A C   
1569 O O   . TRP   A 207 ? 0.30413 0.35053 0.33896 -0.01662 -0.03755 0.13808  207 TRP   A O   
1570 C CB  . TRP   A 207 ? 0.26225 0.30268 0.31753 -0.01513 -0.02191 0.11317  207 TRP   A CB  
1571 C CG  . TRP   A 207 ? 0.27854 0.31569 0.34592 -0.00893 -0.02876 0.10993  207 TRP   A CG  
1572 C CD1 . TRP   A 207 ? 0.28551 0.33054 0.35430 -0.00545 -0.02982 0.10209  207 TRP   A CD1 
1573 C CD2 . TRP   A 207 ? 0.28428 0.30992 0.36574 -0.00498 -0.03541 0.11437  207 TRP   A CD2 
1574 N NE1 . TRP   A 207 ? 0.30021 0.34260 0.38438 0.00091  -0.03580 0.10192  207 TRP   A NE1 
1575 C CE2 . TRP   A 207 ? 0.30900 0.33840 0.40036 0.00223  -0.03931 0.10868  207 TRP   A CE2 
1576 C CE3 . TRP   A 207 ? 0.31020 0.32213 0.39732 -0.00689 -0.03896 0.12291  207 TRP   A CE3 
1577 C CZ2 . TRP   A 207 ? 0.32117 0.34163 0.42731 0.00948  -0.04578 0.11026  207 TRP   A CZ2 
1578 C CZ3 . TRP   A 207 ? 0.34554 0.34495 0.44604 -0.00047 -0.04666 0.12424  207 TRP   A CZ3 
1579 C CH2 . TRP   A 207 ? 0.32176 0.32571 0.43138 0.00857  -0.04960 0.11746  207 TRP   A CH2 
1580 N N   . LEU   A 208 ? 0.27361 0.31101 0.31532 -0.02368 -0.03098 0.14789  208 LEU   A N   
1581 C CA  . LEU   A 208 ? 0.28663 0.31937 0.32597 -0.02548 -0.03915 0.16381  208 LEU   A CA  
1582 C C   . LEU   A 208 ? 0.31453 0.35944 0.33181 -0.02751 -0.03865 0.17027  208 LEU   A C   
1583 O O   . LEU   A 208 ? 0.33719 0.38106 0.34995 -0.02600 -0.04756 0.17813  208 LEU   A O   
1584 C CB  . LEU   A 208 ? 0.29713 0.32118 0.34342 -0.03197 -0.03913 0.17599  208 LEU   A CB  
1585 C CG  . LEU   A 208 ? 0.31392 0.32007 0.38045 -0.02960 -0.04414 0.17183  208 LEU   A CG  
1586 C CD1 . LEU   A 208 ? 0.34293 0.33806 0.41567 -0.03772 -0.04707 0.18603  208 LEU   A CD1 
1587 C CD2 . LEU   A 208 ? 0.34364 0.34038 0.41917 -0.02081 -0.05407 0.16951  208 LEU   A CD2 
1588 N N   . TYR   A 209 ? 0.30894 0.36528 0.31146 -0.03015 -0.02872 0.16677  209 TYR   A N   
1589 C CA  . TYR   A 209 ? 0.31153 0.37841 0.28976 -0.03053 -0.02794 0.16981  209 TYR   A CA  
1590 C C   . TYR   A 209 ? 0.32820 0.39562 0.30195 -0.02572 -0.03458 0.15922  209 TYR   A C   
1591 O O   . TYR   A 209 ? 0.36327 0.43334 0.32323 -0.02555 -0.04185 0.16498  209 TYR   A O   
1592 C CB  . TYR   A 209 ? 0.31552 0.39405 0.27957 -0.03197 -0.01529 0.16556  209 TYR   A CB  
1593 C CG  . TYR   A 209 ? 0.36738 0.45280 0.32796 -0.03788 -0.00925 0.18115  209 TYR   A CG  
1594 C CD1 . TYR   A 209 ? 0.38809 0.47982 0.33044 -0.04057 -0.01078 0.19559  209 TYR   A CD1 
1595 C CD2 . TYR   A 209 ? 0.33273 0.41968 0.30846 -0.04142 -0.00223 0.18218  209 TYR   A CD2 
1596 C CE1 . TYR   A 209 ? 0.39166 0.49085 0.33314 -0.04621 -0.00455 0.20830  209 TYR   A CE1 
1597 C CE2 . TYR   A 209 ? 0.34398 0.43954 0.31944 -0.04816 0.00304  0.19784  209 TYR   A CE2 
1598 C CZ  . TYR   A 209 ? 0.40592 0.50718 0.36554 -0.04993 0.00225  0.20822  209 TYR   A CZ  
1599 O OH  . TYR   A 209 ? 0.41221 0.52135 0.37499 -0.05534 0.00759  0.21703  209 TYR   A OH  
1600 N N   . ALA   A 210 ? 0.33767 0.40320 0.32322 -0.02251 -0.03279 0.14456  210 ALA   A N   
1601 C CA  . ALA   A 210 ? 0.32276 0.38990 0.30868 -0.01930 -0.03957 0.13565  210 ALA   A CA  
1602 C C   . ALA   A 210 ? 0.33072 0.39488 0.32761 -0.01707 -0.05167 0.14415  210 ALA   A C   
1603 O O   . ALA   A 210 ? 0.36762 0.43640 0.35664 -0.01651 -0.06000 0.14494  210 ALA   A O   
1604 C CB  . ALA   A 210 ? 0.30330 0.36915 0.30349 -0.01694 -0.03517 0.12122  210 ALA   A CB  
1605 N N   . ALA   A 211 ? 0.30451 0.36020 0.31955 -0.01552 -0.05371 0.15056  211 ALA   A N   
1606 C CA  . ALA   A 211 ? 0.36173 0.41318 0.38912 -0.01157 -0.06534 0.15868  211 ALA   A CA  
1607 C C   . ALA   A 211 ? 0.38777 0.44137 0.39823 -0.01438 -0.07289 0.17324  211 ALA   A C   
1608 O O   . ALA   A 211 ? 0.39331 0.45081 0.40413 -0.01174 -0.08332 0.17620  211 ALA   A O   
1609 C CB  . ALA   A 211 ? 0.36918 0.40721 0.41608 -0.00906 -0.06614 0.16250  211 ALA   A CB  
1610 N N   . VAL   A 212 ? 0.36294 0.41562 0.35861 -0.01996 -0.06784 0.18325  212 VAL   A N   
1611 C CA  . VAL   A 212 ? 0.40347 0.45899 0.37998 -0.02307 -0.07395 0.19834  212 VAL   A CA  
1612 C C   . VAL   A 212 ? 0.40355 0.46956 0.35861 -0.02286 -0.07657 0.19189  212 VAL   A C   
1613 O O   . VAL   A 212 ? 0.46517 0.53322 0.41057 -0.02257 -0.08752 0.20015  212 VAL   A O   
1614 C CB  . VAL   A 212 ? 0.39912 0.45530 0.36373 -0.02970 -0.06564 0.21025  212 VAL   A CB  
1615 C CG1 . VAL   A 212 ? 0.44272 0.50215 0.38680 -0.03275 -0.07082 0.22495  212 VAL   A CG1 
1616 C CG2 . VAL   A 212 ? 0.41794 0.46146 0.40458 -0.03137 -0.06525 0.21660  212 VAL   A CG2 
1617 N N   . ILE   A 213 ? 0.39767 0.46906 0.34426 -0.02307 -0.06769 0.17711  213 ILE   A N   
1618 C CA  . ILE   A 213 ? 0.41452 0.49235 0.33995 -0.02308 -0.07123 0.16914  213 ILE   A CA  
1619 C C   . ILE   A 213 ? 0.43672 0.51556 0.37553 -0.02051 -0.08439 0.16584  213 ILE   A C   
1620 O O   . ILE   A 213 ? 0.49452 0.57742 0.41744 -0.02153 -0.09403 0.16691  213 ILE   A O   
1621 C CB  . ILE   A 213 ? 0.42485 0.50491 0.34193 -0.02301 -0.05990 0.15325  213 ILE   A CB  
1622 C CG1 . ILE   A 213 ? 0.42592 0.50941 0.32750 -0.02483 -0.04723 0.15771  213 ILE   A CG1 
1623 C CG2 . ILE   A 213 ? 0.50397 0.58641 0.40175 -0.02297 -0.06567 0.14292  213 ILE   A CG2 
1624 C CD1 . ILE   A 213 ? 0.43016 0.51547 0.32739 -0.02327 -0.03564 0.14290  213 ILE   A CD1 
1625 N N   . ASN   A 214 ? 0.39933 0.47562 0.36744 -0.01697 -0.08539 0.16229  214 ASN   A N   
1626 C CA  . ASN   A 214 ? 0.45212 0.53347 0.43721 -0.01388 -0.09574 0.15833  214 ASN   A CA  
1627 C C   . ASN   A 214 ? 0.52544 0.60534 0.52636 -0.00972 -0.10722 0.17153  214 ASN   A C   
1628 O O   . ASN   A 214 ? 0.62526 0.71083 0.64765 -0.00521 -0.11436 0.16907  214 ASN   A O   
1629 C CB  . ASN   A 214 ? 0.45573 0.53823 0.46229 -0.01138 -0.08889 0.14494  214 ASN   A CB  
1630 C CG  . ASN   A 214 ? 0.47194 0.55771 0.46541 -0.01506 -0.08376 0.13152  214 ASN   A CG  
1631 O OD1 . ASN   A 214 ? 0.54295 0.63525 0.53807 -0.01650 -0.09097 0.12615  214 ASN   A OD1 
1632 N ND2 . ASN   A 214 ? 0.46492 0.54599 0.44658 -0.01673 -0.07188 0.12638  214 ASN   A ND2 
1633 N N   . GLY   A 215 ? 0.46984 0.54297 0.46149 -0.01091 -0.10922 0.18617  215 GLY   A N   
1634 C CA  . GLY   A 215 ? 0.48698 0.55708 0.48901 -0.00720 -0.12207 0.20037  215 GLY   A CA  
1635 C C   . GLY   A 215 ? 0.52211 0.57953 0.54678 -0.00247 -0.12124 0.20629  215 GLY   A C   
1636 O O   . GLY   A 215 ? 0.48373 0.53413 0.51332 0.00012  -0.13034 0.21851  215 GLY   A O   
1637 N N   . ASP   A 216 ? 0.44761 0.49998 0.48529 -0.00114 -0.11043 0.19566  216 ASP   A N   
1638 C CA  . ASP   A 216 ? 0.48049 0.51758 0.53655 0.00277  -0.10986 0.19968  216 ASP   A CA  
1639 C C   . ASP   A 216 ? 0.50942 0.53657 0.55113 -0.00483 -0.10625 0.21242  216 ASP   A C   
1640 O O   . ASP   A 216 ? 0.59066 0.62090 0.62040 -0.01102 -0.09489 0.20796  216 ASP   A O   
1641 C CB  . ASP   A 216 ? 0.46962 0.50500 0.54182 0.00633  -0.10019 0.18353  216 ASP   A CB  
1642 C CG  . ASP   A 216 ? 0.54536 0.58451 0.64178 0.01673  -0.10514 0.17630  216 ASP   A CG  
1643 O OD1 . ASP   A 216 ? 0.66193 0.69563 0.77036 0.02344  -0.11573 0.18530  216 ASP   A OD1 
1644 O OD2 . ASP   A 216 ? 0.56436 0.61232 0.66836 0.01864  -0.09812 0.16211  216 ASP   A OD2 
1645 N N   . ARG   A 217 ? 0.49705 0.51287 0.54105 -0.00450 -0.11435 0.22590  217 ARG   A N   
1646 C CA  . ARG   A 217 ? 0.48863 0.49688 0.52011 -0.01304 -0.10945 0.23571  217 ARG   A CA  
1647 C C   . ARG   A 217 ? 0.51475 0.50269 0.56197 -0.01147 -0.11457 0.24163  217 ARG   A C   
1648 O O   . ARG   A 217 ? 0.48119 0.46274 0.52080 -0.01920 -0.11228 0.25118  217 ARG   A O   
1649 C CB  . ARG   A 217 ? 0.51174 0.52935 0.51820 -0.01807 -0.11120 0.24416  217 ARG   A CB  
1650 N N   . TRP   A 218 ? 0.52830 0.50633 0.59722 -0.00147 -0.12113 0.23559  218 TRP   A N   
1651 C CA  . TRP   A 218 ? 0.53241 0.48878 0.61415 0.00151  -0.12751 0.23991  218 TRP   A CA  
1652 C C   . TRP   A 218 ? 0.53472 0.47720 0.61914 -0.00575 -0.12148 0.24018  218 TRP   A C   
1653 O O   . TRP   A 218 ? 0.55338 0.47924 0.64022 -0.00900 -0.12609 0.24796  218 TRP   A O   
1654 C CB  . TRP   A 218 ? 0.54531 0.49574 0.64886 0.01582  -0.13398 0.23045  218 TRP   A CB  
1655 C CG  . TRP   A 218 ? 0.52573 0.47903 0.64221 0.02129  -0.12743 0.21596  218 TRP   A CG  
1656 C CD1 . TRP   A 218 ? 0.51218 0.48465 0.63329 0.02616  -0.12477 0.20722  218 TRP   A CD1 
1657 C CD2 . TRP   A 218 ? 0.52944 0.46592 0.65572 0.02222  -0.12335 0.20854  218 TRP   A CD2 
1658 N NE1 . TRP   A 218 ? 0.50981 0.47958 0.64231 0.03022  -0.11764 0.19410  218 TRP   A NE1 
1659 C CE2 . TRP   A 218 ? 0.51584 0.46265 0.65167 0.02844  -0.11761 0.19554  218 TRP   A CE2 
1660 C CE3 . TRP   A 218 ? 0.55512 0.46884 0.68279 0.01783  -0.12466 0.21142  218 TRP   A CE3 
1661 C CZ2 . TRP   A 218 ? 0.51095 0.44620 0.65492 0.03073  -0.11173 0.18319  218 TRP   A CZ2 
1662 C CZ3 . TRP   A 218 ? 0.58520 0.48622 0.72200 0.01977  -0.12076 0.20050  218 TRP   A CZ3 
1663 C CH2 . TRP   A 218 ? 0.55865 0.46966 0.70338 0.02672  -0.11476 0.18723  218 TRP   A CH2 
1664 N N   . PHE   A 219 ? 0.52729 0.47638 0.61163 -0.00883 -0.11195 0.23212  219 PHE   A N   
1665 C CA  . PHE   A 219 ? 0.52623 0.46365 0.61514 -0.01569 -0.10675 0.23092  219 PHE   A CA  
1666 C C   . PHE   A 219 ? 0.52014 0.46392 0.59475 -0.02910 -0.10129 0.24265  219 PHE   A C   
1667 O O   . PHE   A 219 ? 0.53106 0.46706 0.61063 -0.03628 -0.09804 0.24351  219 PHE   A O   
1668 C CB  . PHE   A 219 ? 0.46465 0.40829 0.55863 -0.01398 -0.09845 0.21841  219 PHE   A CB  
1669 C CG  . PHE   A 219 ? 0.44609 0.41328 0.52593 -0.01612 -0.09082 0.21650  219 PHE   A CG  
1670 C CD1 . PHE   A 219 ? 0.45225 0.43123 0.51721 -0.02636 -0.08125 0.22112  219 PHE   A CD1 
1671 C CD2 . PHE   A 219 ? 0.44655 0.42593 0.52728 -0.00779 -0.09172 0.20589  219 PHE   A CD2 
1672 C CE1 . PHE   A 219 ? 0.43026 0.42968 0.47956 -0.02704 -0.07312 0.21401  219 PHE   A CE1 
1673 C CE2 . PHE   A 219 ? 0.41515 0.41429 0.48091 -0.01035 -0.08462 0.19965  219 PHE   A CE2 
1674 C CZ  . PHE   A 219 ? 0.39053 0.39820 0.43951 -0.01942 -0.07545 0.20307  219 PHE   A CZ  
1675 N N   . LEU   A 220 ? 0.51766 0.47662 0.57488 -0.03235 -0.10013 0.25097  220 LEU   A N   
1676 C CA  . LEU   A 220 ? 0.54188 0.50966 0.58520 -0.04355 -0.09384 0.26179  220 LEU   A CA  
1677 C C   . LEU   A 220 ? 0.57502 0.52590 0.62458 -0.04804 -0.10154 0.27341  220 LEU   A C   
1678 O O   . LEU   A 220 ? 0.55870 0.49740 0.61226 -0.04229 -0.11229 0.27728  220 LEU   A O   
1679 C CB  . LEU   A 220 ? 0.52563 0.51232 0.54644 -0.04412 -0.09122 0.26620  220 LEU   A CB  
1680 C CG  . LEU   A 220 ? 0.50660 0.50999 0.51757 -0.04048 -0.08443 0.25511  220 LEU   A CG  
1681 C CD1 . LEU   A 220 ? 0.47684 0.49438 0.46411 -0.04017 -0.08510 0.25852  220 LEU   A CD1 
1682 C CD2 . LEU   A 220 ? 0.52750 0.54007 0.53719 -0.04575 -0.07130 0.24972  220 LEU   A CD2 
1683 N N   . ASN   A 221 ? 0.59873 0.54919 0.65023 -0.05820 -0.09660 0.27906  221 ASN   A N   
1684 C CA  . ASN   A 221 ? 0.60674 0.54140 0.66410 -0.06402 -0.10429 0.29098  221 ASN   A CA  
1685 C C   . ASN   A 221 ? 0.63819 0.58902 0.68198 -0.07494 -0.09782 0.30497  221 ASN   A C   
1686 O O   . ASN   A 221 ? 0.63161 0.60512 0.66138 -0.07696 -0.08681 0.30392  221 ASN   A O   
1687 C CB  . ASN   A 221 ? 0.60968 0.52481 0.68553 -0.06635 -0.10768 0.28559  221 ASN   A CB  
1688 C CG  . ASN   A 221 ? 0.60518 0.53305 0.68318 -0.07499 -0.09702 0.28243  221 ASN   A CG  
1689 O OD1 . ASN   A 221 ? 0.61427 0.56592 0.68043 -0.07985 -0.08633 0.28596  221 ASN   A OD1 
1690 N ND2 . ASN   A 221 ? 0.60033 0.51218 0.69321 -0.07611 -0.10014 0.27490  221 ASN   A ND2 
1691 N N   . ARG   A 222 ? 0.61233 0.55077 0.66043 -0.08144 -0.10479 0.31788  222 ARG   A N   
1692 C CA  . ARG   A 222 ? 0.65178 0.60369 0.68913 -0.09191 -0.10014 0.33340  222 ARG   A CA  
1693 C C   . ARG   A 222 ? 0.62415 0.58362 0.67055 -0.10264 -0.09289 0.33575  222 ARG   A C   
1694 O O   . ARG   A 222 ? 0.60592 0.57604 0.64748 -0.11211 -0.08956 0.34972  222 ARG   A O   
1695 C CB  . ARG   A 222 ? 0.65258 0.58757 0.69017 -0.09391 -0.11229 0.34791  222 ARG   A CB  
1696 N N   . PHE   A 223 ? 0.57774 0.53294 0.63739 -0.10136 -0.09065 0.32286  223 PHE   A N   
1697 C CA  . PHE   A 223 ? 0.56023 0.52113 0.63110 -0.11116 -0.08587 0.32419  223 PHE   A CA  
1698 C C   . PHE   A 223 ? 0.53803 0.52706 0.60188 -0.11128 -0.07054 0.31756  223 PHE   A C   
1699 O O   . PHE   A 223 ? 0.50731 0.50584 0.56011 -0.10289 -0.06482 0.30806  223 PHE   A O   
1700 C CB  . PHE   A 223 ? 0.56886 0.50553 0.65850 -0.11008 -0.09417 0.31397  223 PHE   A CB  
1701 C CG  . PHE   A 223 ? 0.65271 0.55911 0.75027 -0.10915 -0.10947 0.31870  223 PHE   A CG  
1702 C CD1 . PHE   A 223 ? 0.69185 0.58199 0.80272 -0.11798 -0.11714 0.32332  223 PHE   A CD1 
1703 C CD2 . PHE   A 223 ? 0.67321 0.56682 0.76555 -0.09887 -0.11687 0.31773  223 PHE   A CD2 
1704 C CE1 . PHE   A 223 ? 0.71237 0.57272 0.82966 -0.11654 -0.13153 0.32684  223 PHE   A CE1 
1705 C CE2 . PHE   A 223 ? 0.72335 0.58865 0.82332 -0.09663 -0.13081 0.32144  223 PHE   A CE2 
1706 C CZ  . PHE   A 223 ? 0.74972 0.59741 0.86156 -0.10532 -0.13802 0.32567  223 PHE   A CZ  
1707 N N   . THR   A 224 ? 0.52885 0.53132 0.59975 -0.12073 -0.06439 0.32279  224 THR   A N   
1708 C CA  . THR   A 224 ? 0.50395 0.52943 0.57418 -0.12023 -0.05115 0.31425  224 THR   A CA  
1709 C C   . THR   A 224 ? 0.49855 0.51832 0.58905 -0.12702 -0.05365 0.31123  224 THR   A C   
1710 O O   . THR   A 224 ? 0.51463 0.51153 0.61767 -0.13170 -0.06574 0.31475  224 THR   A O   
1711 C CB  . THR   A 224 ? 0.51225 0.56739 0.56840 -0.12338 -0.03859 0.32325  224 THR   A CB  
1712 O OG1 . THR   A 224 ? 0.48693 0.56265 0.54078 -0.11944 -0.02584 0.31201  224 THR   A OG1 
1713 C CG2 . THR   A 224 ? 0.53743 0.59843 0.60297 -0.13568 -0.03979 0.33959  224 THR   A CG2 
1714 N N   . THR   A 225 ? 0.47766 0.51747 0.57074 -0.12709 -0.04284 0.30411  225 THR   A N   
1715 C CA  . THR   A 225 ? 0.49195 0.52939 0.60340 -0.13327 -0.04488 0.30053  225 THR   A CA  
1716 C C   . THR   A 225 ? 0.47474 0.54398 0.58618 -0.13490 -0.03077 0.29998  225 THR   A C   
1717 O O   . THR   A 225 ? 0.45687 0.54810 0.55353 -0.13100 -0.01955 0.30207  225 THR   A O   
1718 C CB  . THR   A 225 ? 0.50595 0.52131 0.62487 -0.12701 -0.05129 0.28431  225 THR   A CB  
1719 O OG1 . THR   A 225 ? 0.52503 0.53378 0.66083 -0.13412 -0.05622 0.28204  225 THR   A OG1 
1720 C CG2 . THR   A 225 ? 0.45030 0.47855 0.56004 -0.11718 -0.04090 0.27065  225 THR   A CG2 
1721 N N   . THR   A 226 ? 0.46616 0.53718 0.59396 -0.14021 -0.03196 0.29682  226 THR   A N   
1722 C CA  . THR   A 226 ? 0.45890 0.55895 0.59020 -0.14090 -0.01983 0.29528  226 THR   A CA  
1723 C C   . THR   A 226 ? 0.44947 0.54548 0.58649 -0.13509 -0.01851 0.27822  226 THR   A C   
1724 O O   . THR   A 226 ? 0.43252 0.50277 0.57487 -0.13365 -0.02844 0.26967  226 THR   A O   
1725 C CB  . THR   A 226 ? 0.46237 0.57320 0.60962 -0.15325 -0.02211 0.30860  226 THR   A CB  
1726 O OG1 . THR   A 226 ? 0.47238 0.56268 0.63634 -0.15866 -0.03403 0.30388  226 THR   A OG1 
1727 C CG2 . THR   A 226 ? 0.48918 0.59755 0.63340 -0.16087 -0.02678 0.32652  226 THR   A CG2 
1728 N N   . LEU   A 227 ? 0.42566 0.54736 0.56140 -0.13134 -0.00609 0.27328  227 LEU   A N   
1729 C CA  . LEU   A 227 ? 0.44145 0.56179 0.58176 -0.12568 -0.00390 0.25772  227 LEU   A CA  
1730 C C   . LEU   A 227 ? 0.45872 0.56228 0.61753 -0.13308 -0.01541 0.25565  227 LEU   A C   
1731 O O   . LEU   A 227 ? 0.42628 0.50990 0.58715 -0.12948 -0.02136 0.24347  227 LEU   A O   
1732 C CB  . LEU   A 227 ? 0.46583 0.61738 0.60342 -0.12097 0.01064  0.25473  227 LEU   A CB  
1733 C CG  . LEU   A 227 ? 0.45605 0.61204 0.58720 -0.11036 0.01806  0.23844  227 LEU   A CG  
1734 C CD1 . LEU   A 227 ? 0.41909 0.55722 0.53544 -0.10309 0.01584  0.23064  227 LEU   A CD1 
1735 C CD2 . LEU   A 227 ? 0.40389 0.59022 0.52732 -0.10437 0.03277  0.23817  227 LEU   A CD2 
1736 N N   . ASN   A 228 ? 0.44313 0.55355 0.61490 -0.14371 -0.01938 0.26774  228 ASN   A N   
1737 C CA  . ASN   A 228 ? 0.45357 0.54709 0.64171 -0.15150 -0.03170 0.26599  228 ASN   A CA  
1738 C C   . ASN   A 228 ? 0.45469 0.51184 0.64236 -0.15325 -0.04649 0.26462  228 ASN   A C   
1739 O O   . ASN   A 228 ? 0.44720 0.48218 0.64110 -0.15344 -0.05605 0.25445  228 ASN   A O   
1740 C CB  . ASN   A 228 ? 0.48875 0.60033 0.69113 -0.16295 -0.03253 0.28046  228 ASN   A CB  
1741 C CG  . ASN   A 228 ? 0.44575 0.58459 0.65645 -0.16160 -0.02344 0.27677  228 ASN   A CG  
1742 O OD1 . ASN   A 228 ? 0.48032 0.63231 0.68248 -0.15126 -0.01238 0.26658  228 ASN   A OD1 
1743 N ND2 . ASN   A 228 ? 0.41214 0.55935 0.63983 -0.17196 -0.02863 0.28535  228 ASN   A ND2 
1744 N N   . ASP   A 229 ? 0.45331 0.50327 0.63288 -0.15372 -0.04874 0.27415  229 ASP   A N   
1745 C CA  . ASP   A 229 ? 0.47908 0.49414 0.65833 -0.15385 -0.06289 0.27285  229 ASP   A CA  
1746 C C   . ASP   A 229 ? 0.48771 0.48513 0.65880 -0.14196 -0.06347 0.25640  229 ASP   A C   
1747 O O   . ASP   A 229 ? 0.48983 0.45871 0.66515 -0.14034 -0.07460 0.24749  229 ASP   A O   
1748 C CB  . ASP   A 229 ? 0.52248 0.53601 0.69483 -0.15670 -0.06484 0.28785  229 ASP   A CB  
1749 C CG  . ASP   A 229 ? 0.61454 0.59302 0.78421 -0.15339 -0.07804 0.28543  229 ASP   A CG  
1750 O OD1 . ASP   A 229 ? 0.68392 0.66038 0.84289 -0.14974 -0.07751 0.29190  229 ASP   A OD1 
1751 O OD2 . ASP   A 229 ? 0.70662 0.65940 0.88444 -0.15405 -0.08930 0.27703  229 ASP   A OD2 
1752 N N   . PHE   A 230 ? 0.47468 0.48851 0.63358 -0.13325 -0.05173 0.25203  230 PHE   A N   
1753 C CA  . PHE   A 230 ? 0.45271 0.45330 0.60510 -0.12248 -0.05147 0.23730  230 PHE   A CA  
1754 C C   . PHE   A 230 ? 0.44414 0.43940 0.60498 -0.12162 -0.05265 0.22369  230 PHE   A C   
1755 O O   . PHE   A 230 ? 0.44191 0.41286 0.60365 -0.11649 -0.05997 0.21251  230 PHE   A O   
1756 C CB  . PHE   A 230 ? 0.42439 0.44601 0.56207 -0.11461 -0.03869 0.23586  230 PHE   A CB  
1757 C CG  . PHE   A 230 ? 0.40213 0.41460 0.53435 -0.10443 -0.03732 0.22172  230 PHE   A CG  
1758 C CD1 . PHE   A 230 ? 0.40663 0.39792 0.53428 -0.09808 -0.04474 0.21957  230 PHE   A CD1 
1759 C CD2 . PHE   A 230 ? 0.38548 0.41045 0.51835 -0.10098 -0.02916 0.21093  230 PHE   A CD2 
1760 C CE1 . PHE   A 230 ? 0.42178 0.40591 0.54603 -0.08870 -0.04360 0.20746  230 PHE   A CE1 
1761 C CE2 . PHE   A 230 ? 0.36062 0.37739 0.48918 -0.09240 -0.02800 0.19892  230 PHE   A CE2 
1762 C CZ  . PHE   A 230 ? 0.41394 0.41067 0.53855 -0.08645 -0.03511 0.19747  230 PHE   A CZ  
1763 N N   . ASN   A 231 ? 0.44012 0.45814 0.60701 -0.12590 -0.04561 0.22424  231 ASN   A N   
1764 C CA  . ASN   A 231 ? 0.43253 0.44753 0.60642 -0.12490 -0.04653 0.21150  231 ASN   A CA  
1765 C C   . ASN   A 231 ? 0.46047 0.44746 0.64405 -0.13054 -0.06172 0.20812  231 ASN   A C   
1766 O O   . ASN   A 231 ? 0.43952 0.41294 0.62501 -0.12747 -0.06573 0.19472  231 ASN   A O   
1767 C CB  . ASN   A 231 ? 0.42751 0.47352 0.60687 -0.12782 -0.03667 0.21391  231 ASN   A CB  
1768 C CG  . ASN   A 231 ? 0.41390 0.48236 0.58207 -0.11870 -0.02200 0.20939  231 ASN   A CG  
1769 O OD1 . ASN   A 231 ? 0.41329 0.47281 0.57090 -0.11076 -0.02004 0.20218  231 ASN   A OD1 
1770 N ND2 . ASN   A 231 ? 0.39669 0.49401 0.56708 -0.11928 -0.01199 0.21339  231 ASN   A ND2 
1771 N N   . LEU   A 232 ? 0.45685 0.43416 0.64553 -0.13867 -0.07064 0.21975  232 LEU   A N   
1772 C CA  . LEU   A 232 ? 0.48883 0.43427 0.68360 -0.14255 -0.08647 0.21561  232 LEU   A CA  
1773 C C   . LEU   A 232 ? 0.50973 0.42616 0.69651 -0.13178 -0.09193 0.20274  232 LEU   A C   
1774 O O   . LEU   A 232 ? 0.53469 0.42860 0.72280 -0.12924 -0.10020 0.18965  232 LEU   A O   
1775 C CB  . LEU   A 232 ? 0.49503 0.43468 0.69530 -0.15250 -0.09477 0.23153  232 LEU   A CB  
1776 C CG  . LEU   A 232 ? 0.50411 0.46044 0.71733 -0.16531 -0.09658 0.24208  232 LEU   A CG  
1777 C CD1 . LEU   A 232 ? 0.51535 0.45117 0.73511 -0.17517 -0.11093 0.25300  232 LEU   A CD1 
1778 C CD2 . LEU   A 232 ? 0.53232 0.48937 0.75215 -0.16626 -0.09861 0.23032  232 LEU   A CD2 
1779 N N   . VAL   A 233 ? 0.48787 0.40534 0.66577 -0.12465 -0.08732 0.20594  233 VAL   A N   
1780 C CA  . VAL   A 233 ? 0.51668 0.41008 0.68819 -0.11298 -0.09156 0.19467  233 VAL   A CA  
1781 C C   . VAL   A 233 ? 0.48947 0.38929 0.65721 -0.10453 -0.08361 0.18039  233 VAL   A C   
1782 O O   . VAL   A 233 ? 0.50082 0.37850 0.66677 -0.09592 -0.08870 0.16688  233 VAL   A O   
1783 C CB  . VAL   A 233 ? 0.52554 0.41973 0.68986 -0.10872 -0.09033 0.20443  233 VAL   A CB  
1784 C CG1 . VAL   A 233 ? 0.59140 0.46627 0.75031 -0.09500 -0.09321 0.19341  233 VAL   A CG1 
1785 C CG2 . VAL   A 233 ? 0.55151 0.43407 0.72006 -0.11699 -0.10022 0.21755  233 VAL   A CG2 
1786 N N   . ALA   A 234 ? 0.45765 0.38740 0.62398 -0.10616 -0.07106 0.18259  234 ALA   A N   
1787 C CA  . ALA   A 234 ? 0.45242 0.38861 0.61588 -0.09925 -0.06376 0.16979  234 ALA   A CA  
1788 C C   . ALA   A 234 ? 0.46027 0.38139 0.62970 -0.10076 -0.07069 0.15730  234 ALA   A C   
1789 O O   . ALA   A 234 ? 0.44507 0.35033 0.61154 -0.09267 -0.07260 0.14367  234 ALA   A O   
1790 C CB  . ALA   A 234 ? 0.41539 0.38638 0.57599 -0.10061 -0.04947 0.17441  234 ALA   A CB  
1791 N N   . MET   A 235 ? 0.45123 0.37721 0.62874 -0.11087 -0.07499 0.16177  235 MET   A N   
1792 C CA  . MET   A 235 ? 0.47623 0.38870 0.65799 -0.11307 -0.08273 0.15020  235 MET   A CA  
1793 C C   . MET   A 235 ? 0.49158 0.36664 0.66913 -0.10701 -0.09506 0.13866  235 MET   A C   
1794 O O   . MET   A 235 ? 0.49603 0.35751 0.66998 -0.10141 -0.09779 0.12319  235 MET   A O   
1795 C CB  . MET   A 235 ? 0.51036 0.43299 0.70234 -0.12541 -0.08740 0.15920  235 MET   A CB  
1796 N N   . LYS   A 236 ? 0.50409 0.36233 0.68100 -0.10688 -0.10232 0.14534  236 LYS   A N   
1797 C CA  . LYS   A 236 ? 0.51117 0.33368 0.68378 -0.09950 -0.11410 0.13398  236 LYS   A CA  
1798 C C   . LYS   A 236 ? 0.52156 0.33520 0.68649 -0.08423 -0.10966 0.12041  236 LYS   A C   
1799 O O   . LYS   A 236 ? 0.57006 0.35980 0.73005 -0.07579 -0.11604 0.10443  236 LYS   A O   
1800 C CB  . LYS   A 236 ? 0.58298 0.39157 0.75714 -0.10196 -0.12209 0.14531  236 LYS   A CB  
1801 C CG  . LYS   A 236 ? 0.65845 0.43044 0.82768 -0.09209 -0.13359 0.13354  236 LYS   A CG  
1802 C CD  . LYS   A 236 ? 0.75992 0.51481 0.93287 -0.09878 -0.14518 0.14430  236 LYS   A CD  
1803 C CE  . LYS   A 236 ? 0.76806 0.49279 0.93551 -0.08550 -0.15279 0.13622  236 LYS   A CE  
1804 N NZ  . LYS   A 236 ? 0.80965 0.53898 0.97824 -0.08462 -0.15171 0.15106  236 LYS   A NZ  
1805 N N   . TYR   A 237 ? 0.49669 0.33013 0.65991 -0.07992 -0.09866 0.12620  237 TYR   A N   
1806 C CA  . TYR   A 237 ? 0.48623 0.31469 0.64434 -0.06560 -0.09418 0.11577  237 TYR   A CA  
1807 C C   . TYR   A 237 ? 0.45134 0.30486 0.60373 -0.06162 -0.08175 0.10441  237 TYR   A C   
1808 O O   . TYR   A 237 ? 0.44502 0.30999 0.59011 -0.04979 -0.07324 0.09585  237 TYR   A O   
1809 C CB  . TYR   A 237 ? 0.46600 0.30206 0.62251 -0.06084 -0.09072 0.12692  237 TYR   A CB  
1810 C CG  . TYR   A 237 ? 0.51587 0.33001 0.67296 -0.05890 -0.10162 0.13114  237 TYR   A CG  
1811 C CD1 . TYR   A 237 ? 0.54302 0.33212 0.69827 -0.04508 -0.10840 0.11867  237 TYR   A CD1 
1812 C CD2 . TYR   A 237 ? 0.52130 0.33989 0.68105 -0.07039 -0.10513 0.14688  237 TYR   A CD2 
1813 C CE1 . TYR   A 237 ? 0.56235 0.33083 0.71816 -0.04268 -0.11842 0.12212  237 TYR   A CE1 
1814 C CE2 . TYR   A 237 ? 0.56586 0.36297 0.72645 -0.06918 -0.11573 0.15123  237 TYR   A CE2 
1815 C CZ  . TYR   A 237 ? 0.58198 0.35343 0.74053 -0.05535 -0.12253 0.13875  237 TYR   A CZ  
1816 O OH  . TYR   A 237 ? 0.62931 0.37888 0.78867 -0.05338 -0.13306 0.14272  237 TYR   A OH  
1817 N N   . ASN   A 238 ? 0.44594 0.30804 0.60204 -0.07124 -0.08141 0.10416  238 ASN   A N   
1818 C CA  . ASN   A 238 ? 0.41105 0.29485 0.56174 -0.06758 -0.07110 0.09349  238 ASN   A CA  
1819 C C   . ASN   A 238 ? 0.38429 0.29700 0.53050 -0.06381 -0.05737 0.09847  238 ASN   A C   
1820 O O   . ASN   A 238 ? 0.37604 0.29923 0.51400 -0.05424 -0.04926 0.08704  238 ASN   A O   
1821 C CB  . ASN   A 238 ? 0.46567 0.33554 0.60686 -0.05499 -0.07208 0.07279  238 ASN   A CB  
1822 C CG  . ASN   A 238 ? 0.56136 0.41006 0.70317 -0.05970 -0.08334 0.06441  238 ASN   A CG  
1823 O OD1 . ASN   A 238 ? 0.56735 0.42124 0.71701 -0.07265 -0.08745 0.07167  238 ASN   A OD1 
1824 N ND2 . ASN   A 238 ? 0.67404 0.49973 0.80738 -0.04881 -0.08849 0.04878  238 ASN   A ND2 
1825 N N   . TYR   A 239 ? 0.38359 0.30839 0.53424 -0.07158 -0.05519 0.11577  239 TYR   A N   
1826 C CA  . TYR   A 239 ? 0.36094 0.31283 0.50574 -0.06935 -0.04292 0.12108  239 TYR   A CA  
1827 C C   . TYR   A 239 ? 0.35417 0.32968 0.50422 -0.07808 -0.03642 0.12782  239 TYR   A C   
1828 O O   . TYR   A 239 ? 0.34296 0.31675 0.50442 -0.08951 -0.04217 0.13705  239 TYR   A O   
1829 C CB  . TYR   A 239 ? 0.33171 0.28387 0.47513 -0.07093 -0.04382 0.13595  239 TYR   A CB  
1830 C CG  . TYR   A 239 ? 0.33843 0.28192 0.47434 -0.05897 -0.04468 0.12969  239 TYR   A CG  
1831 C CD1 . TYR   A 239 ? 0.33276 0.25260 0.47008 -0.05084 -0.05249 0.11840  239 TYR   A CD1 
1832 C CD2 . TYR   A 239 ? 0.33394 0.29416 0.46127 -0.05522 -0.03775 0.13452  239 TYR   A CD2 
1833 C CE1 . TYR   A 239 ? 0.34555 0.26128 0.47883 -0.03925 -0.05285 0.11344  239 TYR   A CE1 
1834 C CE2 . TYR   A 239 ? 0.32411 0.27882 0.44672 -0.04500 -0.03950 0.12962  239 TYR   A CE2 
1835 C CZ  . TYR   A 239 ? 0.32828 0.26223 0.45530 -0.03703 -0.04670 0.11960  239 TYR   A CZ  
1836 O OH  . TYR   A 239 ? 0.32091 0.25316 0.44597 -0.02646 -0.04801 0.11561  239 TYR   A OH  
1837 N N   . GLU   A 240 ? 0.30192 0.29951 0.44452 -0.07255 -0.02495 0.12335  240 GLU   A N   
1838 C CA  . GLU   A 240 ? 0.32019 0.34248 0.46775 -0.07822 -0.01754 0.12958  240 GLU   A CA  
1839 C C   . GLU   A 240 ? 0.29070 0.32566 0.44392 -0.08766 -0.01576 0.14955  240 GLU   A C   
1840 O O   . GLU   A 240 ? 0.32186 0.35499 0.46773 -0.08597 -0.01489 0.15680  240 GLU   A O   
1841 C CB  . GLU   A 240 ? 0.33326 0.37359 0.46965 -0.06893 -0.00605 0.12098  240 GLU   A CB  
1842 C CG  . GLU   A 240 ? 0.34105 0.37271 0.47106 -0.06025 -0.00622 0.10323  240 GLU   A CG  
1843 C CD  . GLU   A 240 ? 0.45520 0.50424 0.57578 -0.05323 0.00412  0.09702  240 GLU   A CD  
1844 O OE1 . GLU   A 240 ? 0.39166 0.45274 0.50513 -0.05142 0.01050  0.10292  240 GLU   A OE1 
1845 O OE2 . GLU   A 240 ? 0.56608 0.61531 0.68506 -0.04944 0.00520  0.08628  240 GLU   A OE2 
1846 N N   . PRO   A 241 ? 0.31633 0.36527 0.47907 -0.09504 -0.01546 0.15598  241 PRO   A N   
1847 C CA  . PRO   A 241 ? 0.33881 0.40218 0.50158 -0.09966 -0.01289 0.16972  241 PRO   A CA  
1848 C C   . PRO   A 241 ? 0.30497 0.39081 0.45521 -0.09300 0.00024  0.17225  241 PRO   A C   
1849 O O   . PRO   A 241 ? 0.30569 0.40484 0.45129 -0.08635 0.00890  0.16423  241 PRO   A O   
1850 C CB  . PRO   A 241 ? 0.35295 0.42918 0.52880 -0.10655 -0.01444 0.17264  241 PRO   A CB  
1851 C CG  . PRO   A 241 ? 0.35712 0.41651 0.53939 -0.10735 -0.02259 0.16095  241 PRO   A CG  
1852 C CD  . PRO   A 241 ? 0.33562 0.38823 0.50846 -0.09830 -0.01813 0.14982  241 PRO   A CD  
1853 N N   . LEU   A 242 ? 0.35330 0.44228 0.49694 -0.09455 0.00108  0.18304  242 LEU   A N   
1854 C CA  . LEU   A 242 ? 0.35239 0.46030 0.48117 -0.08825 0.01230  0.18513  242 LEU   A CA  
1855 C C   . LEU   A 242 ? 0.33332 0.46772 0.46498 -0.09023 0.02039  0.19193  242 LEU   A C   
1856 O O   . LEU   A 242 ? 0.33957 0.47657 0.48180 -0.09870 0.01599  0.20231  242 LEU   A O   
1857 C CB  . LEU   A 242 ? 0.33947 0.43697 0.45755 -0.08806 0.00867  0.19280  242 LEU   A CB  
1858 C CG  . LEU   A 242 ? 0.35021 0.45901 0.44881 -0.07988 0.01746  0.19088  242 LEU   A CG  
1859 C CD1 . LEU   A 242 ? 0.32900 0.42448 0.42219 -0.07325 0.01580  0.18020  242 LEU   A CD1 
1860 C CD2 . LEU   A 242 ? 0.37293 0.48077 0.46190 -0.08212 0.01506  0.20294  242 LEU   A CD2 
1861 N N   . THR   A 243 ? 0.31516 0.46865 0.43786 -0.08205 0.03189  0.18586  243 THR   A N   
1862 C CA  . THR   A 243 ? 0.32143 0.50128 0.44601 -0.08084 0.04116  0.19001  243 THR   A CA  
1863 C C   . THR   A 243 ? 0.32029 0.51295 0.42569 -0.07484 0.05034  0.19318  243 THR   A C   
1864 O O   . THR   A 243 ? 0.32400 0.50587 0.41388 -0.07091 0.04964  0.19044  243 THR   A O   
1865 C CB  . THR   A 243 ? 0.31523 0.50582 0.44462 -0.07440 0.04675  0.17886  243 THR   A CB  
1866 O OG1 . THR   A 243 ? 0.31763 0.50627 0.43056 -0.06399 0.05280  0.16782  243 THR   A OG1 
1867 C CG2 . THR   A 243 ? 0.32117 0.49717 0.46635 -0.07970 0.03705  0.17407  243 THR   A CG2 
1868 N N   . GLN   A 244 ? 0.29909 0.51554 0.40514 -0.07373 0.05892  0.19869  244 GLN   A N   
1869 C CA  . GLN   A 244 ? 0.31782 0.54715 0.40363 -0.06683 0.06846  0.19994  244 GLN   A CA  
1870 C C   . GLN   A 244 ? 0.32487 0.55401 0.39437 -0.05436 0.07514  0.18479  244 GLN   A C   
1871 O O   . GLN   A 244 ? 0.30868 0.53699 0.35673 -0.04862 0.07889  0.18259  244 GLN   A O   
1872 C CB  . GLN   A 244 ? 0.33278 0.58855 0.42360 -0.06769 0.07683  0.20888  244 GLN   A CB  
1873 C CG  . GLN   A 244 ? 0.35668 0.62567 0.42566 -0.06134 0.08648  0.21142  244 GLN   A CG  
1874 C CD  . GLN   A 244 ? 0.39212 0.64901 0.44953 -0.06712 0.08078  0.22114  244 GLN   A CD  
1875 O OE1 . GLN   A 244 ? 0.40907 0.66035 0.47903 -0.07811 0.07301  0.23368  244 GLN   A OE1 
1876 N NE2 . GLN   A 244 ? 0.38810 0.64031 0.42095 -0.05966 0.08389  0.21547  244 GLN   A NE2 
1877 N N   . ASP   A 245 ? 0.31792 0.54706 0.39642 -0.05022 0.07594  0.17435  245 ASP   A N   
1878 C CA  . ASP   A 245 ? 0.31388 0.53886 0.37771 -0.03916 0.08039  0.15986  245 ASP   A CA  
1879 C C   . ASP   A 245 ? 0.33563 0.53980 0.38730 -0.03965 0.07405  0.15679  245 ASP   A C   
1880 O O   . ASP   A 245 ? 0.31441 0.51653 0.34545 -0.03190 0.07772  0.14984  245 ASP   A O   
1881 C CB  . ASP   A 245 ? 0.36384 0.58943 0.44144 -0.03614 0.08017  0.15054  245 ASP   A CB  
1882 C CG  . ASP   A 245 ? 0.46860 0.71653 0.55283 -0.03070 0.08839  0.15001  245 ASP   A CG  
1883 O OD1 . ASP   A 245 ? 0.43949 0.70237 0.51343 -0.02643 0.09633  0.15372  245 ASP   A OD1 
1884 O OD2 . ASP   A 245 ? 0.49753 0.74822 0.59672 -0.03004 0.08689  0.14559  245 ASP   A OD2 
1885 N N   . HIS   A 246 ? 0.31198 0.49996 0.37611 -0.04839 0.06386  0.16167  246 HIS   A N   
1886 C CA  . HIS   A 246 ? 0.32067 0.48963 0.37593 -0.04901 0.05710  0.16064  246 HIS   A CA  
1887 C C   . HIS   A 246 ? 0.29686 0.46698 0.33479 -0.04909 0.05731  0.16871  246 HIS   A C   
1888 O O   . HIS   A 246 ? 0.30892 0.47240 0.32948 -0.04427 0.05656  0.16448  246 HIS   A O   
1889 C CB  . HIS   A 246 ? 0.30521 0.45607 0.37834 -0.05763 0.04593  0.16464  246 HIS   A CB  
1890 C CG  . HIS   A 246 ? 0.31960 0.46575 0.40708 -0.05765 0.04405  0.15568  246 HIS   A CG  
1891 N ND1 . HIS   A 246 ? 0.34694 0.48269 0.45265 -0.06560 0.03556  0.15859  246 HIS   A ND1 
1892 C CD2 . HIS   A 246 ? 0.30490 0.45276 0.38960 -0.05046 0.04817  0.14293  246 HIS   A CD2 
1893 C CE1 . HIS   A 246 ? 0.31063 0.44402 0.42429 -0.06371 0.03518  0.14880  246 HIS   A CE1 
1894 N NE2 . HIS   A 246 ? 0.31924 0.45885 0.42003 -0.05388 0.04233  0.13819  246 HIS   A NE2 
1895 N N   . VAL   A 247 ? 0.28142 0.45952 0.32398 -0.05520 0.05723  0.18103  247 VAL   A N   
1896 C CA  . VAL   A 247 ? 0.32721 0.50763 0.35281 -0.05555 0.05760  0.18954  247 VAL   A CA  
1897 C C   . VAL   A 247 ? 0.35797 0.54972 0.35963 -0.04529 0.06706  0.18130  247 VAL   A C   
1898 O O   . VAL   A 247 ? 0.36378 0.54894 0.34545 -0.04218 0.06488  0.18040  247 VAL   A O   
1899 C CB  . VAL   A 247 ? 0.35570 0.54663 0.39081 -0.06363 0.05788  0.20414  247 VAL   A CB  
1900 C CG1 . VAL   A 247 ? 0.33692 0.52989 0.35360 -0.06426 0.05806  0.21360  247 VAL   A CG1 
1901 C CG2 . VAL   A 247 ? 0.33583 0.51257 0.39347 -0.07366 0.04711  0.21085  247 VAL   A CG2 
1902 N N   . ASP   A 248 ? 0.34202 0.54963 0.34497 -0.03934 0.07667  0.17446  248 ASP   A N   
1903 C CA  . ASP   A 248 ? 0.35853 0.57487 0.33816 -0.02830 0.08551  0.16491  248 ASP   A CA  
1904 C C   . ASP   A 248 ? 0.34390 0.54530 0.30863 -0.02207 0.08213  0.15239  248 ASP   A C   
1905 O O   . ASP   A 248 ? 0.31538 0.51463 0.25490 -0.01614 0.08335  0.14758  248 ASP   A O   
1906 C CB  . ASP   A 248 ? 0.34531 0.57918 0.33280 -0.02210 0.09520  0.15911  248 ASP   A CB  
1907 C CG  . ASP   A 248 ? 0.35080 0.60490 0.34593 -0.02575 0.10108  0.17106  248 ASP   A CG  
1908 O OD1 . ASP   A 248 ? 0.38487 0.64063 0.37286 -0.03125 0.09974  0.18255  248 ASP   A OD1 
1909 O OD2 . ASP   A 248 ? 0.38954 0.65890 0.39798 -0.02289 0.10707  0.16938  248 ASP   A OD2 
1910 N N   . ILE   A 249 ? 0.28067 0.47168 0.25997 -0.02352 0.07747  0.14690  249 ILE   A N   
1911 C CA  . ILE   A 249 ? 0.31071 0.48862 0.27793 -0.01872 0.07390  0.13639  249 ILE   A CA  
1912 C C   . ILE   A 249 ? 0.33334 0.49838 0.28860 -0.02212 0.06473  0.14145  249 ILE   A C   
1913 O O   . ILE   A 249 ? 0.33753 0.49196 0.27521 -0.01665 0.06050  0.13047  249 ILE   A O   
1914 C CB  . ILE   A 249 ? 0.26051 0.42723 0.24854 -0.02021 0.06910  0.12839  249 ILE   A CB  
1915 C CG1 . ILE   A 249 ? 0.30284 0.48296 0.29884 -0.01490 0.07782  0.12232  249 ILE   A CG1 
1916 C CG2 . ILE   A 249 ? 0.32980 0.47550 0.31046 -0.01652 0.06059  0.11426  249 ILE   A CG2 
1917 C CD1 . ILE   A 249 ? 0.28279 0.45388 0.30076 -0.01811 0.07252  0.11732  249 ILE   A CD1 
1918 N N   . LEU   A 250 ? 0.29766 0.46011 0.26367 -0.03082 0.05924  0.15582  250 LEU   A N   
1919 C CA  . LEU   A 250 ? 0.33295 0.48375 0.28962 -0.03369 0.04968  0.16259  250 LEU   A CA  
1920 C C   . LEU   A 250 ? 0.35116 0.50917 0.28404 -0.03147 0.05186  0.16679  250 LEU   A C   
1921 O O   . LEU   A 250 ? 0.38313 0.53259 0.30569 -0.03313 0.04339  0.17228  250 LEU   A O   
1922 C CB  . LEU   A 250 ? 0.30808 0.44858 0.28601 -0.04269 0.04112  0.17467  250 LEU   A CB  
1923 C CG  . LEU   A 250 ? 0.26996 0.39548 0.26898 -0.04328 0.03516  0.16554  250 LEU   A CG  
1924 C CD1 . LEU   A 250 ? 0.27198 0.38931 0.29158 -0.05232 0.02876  0.17839  250 LEU   A CD1 
1925 C CD2 . LEU   A 250 ? 0.26400 0.37339 0.25801 -0.03782 0.02663  0.15307  250 LEU   A CD2 
1926 N N   . GLY   A 251 ? 0.34595 0.51917 0.27029 -0.02725 0.06251  0.16405  251 GLY   A N   
1927 C CA  . GLY   A 251 ? 0.41581 0.59698 0.31864 -0.02543 0.06595  0.16865  251 GLY   A CA  
1928 C C   . GLY   A 251 ? 0.42912 0.60159 0.30354 -0.02081 0.06040  0.16310  251 GLY   A C   
1929 O O   . GLY   A 251 ? 0.40177 0.57091 0.26515 -0.02413 0.05456  0.17227  251 GLY   A O   
1930 N N   . PRO   A 252 ? 0.41416 0.58257 0.27533 -0.01310 0.06139  0.14786  252 PRO   A N   
1931 C CA  . PRO   A 252 ? 0.42994 0.58865 0.26384 -0.00949 0.05356  0.14148  252 PRO   A CA  
1932 C C   . PRO   A 252 ? 0.45543 0.60276 0.29459 -0.01614 0.03938  0.15067  252 PRO   A C   
1933 O O   . PRO   A 252 ? 0.44557 0.58896 0.26509 -0.01627 0.03236  0.15353  252 PRO   A O   
1934 C CB  . PRO   A 252 ? 0.46889 0.62167 0.29757 -0.00213 0.05470  0.12339  252 PRO   A CB  
1935 C CG  . PRO   A 252 ? 0.43618 0.60169 0.27556 0.00220  0.06812  0.12002  252 PRO   A CG  
1936 C CD  . PRO   A 252 ? 0.41197 0.58572 0.27863 -0.00640 0.07013  0.13532  252 PRO   A CD  
1937 N N   . LEU   A 253 ? 0.41810 0.55706 0.28563 -0.02078 0.03398  0.15263  253 LEU   A N   
1938 C CA  . LEU   A 253 ? 0.43649 0.56256 0.31435 -0.02538 0.02026  0.15923  253 LEU   A CA  
1939 C C   . LEU   A 253 ? 0.43792 0.56820 0.31537 -0.03152 0.01826  0.17943  253 LEU   A C   
1940 O O   . LEU   A 253 ? 0.47496 0.59791 0.34631 -0.03303 0.00737  0.18592  253 LEU   A O   
1941 C CB  . LEU   A 253 ? 0.38736 0.50238 0.29569 -0.02709 0.01622  0.15384  253 LEU   A CB  
1942 C CG  . LEU   A 253 ? 0.38877 0.49483 0.30065 -0.02232 0.01347  0.13485  253 LEU   A CG  
1943 C CD1 . LEU   A 253 ? 0.37819 0.47579 0.31884 -0.02396 0.01129  0.13128  253 LEU   A CD1 
1944 C CD2 . LEU   A 253 ? 0.43546 0.53426 0.33479 -0.02088 0.00220  0.13066  253 LEU   A CD2 
1945 N N   . SER   A 254 ? 0.41841 0.55733 0.30668 -0.03468 0.02721  0.18569  254 SER   A N   
1946 C CA  . SER   A 254 ? 0.41404 0.55488 0.30236 -0.04010 0.02564  0.20039  254 SER   A CA  
1947 C C   . SER   A 254 ? 0.47575 0.62101 0.33320 -0.03677 0.02594  0.20091  254 SER   A C   
1948 O O   . SER   A 254 ? 0.49185 0.63148 0.34345 -0.03995 0.01767  0.21137  254 SER   A O   
1949 C CB  . SER   A 254 ? 0.42233 0.57518 0.32600 -0.04408 0.03573  0.20592  254 SER   A CB  
1950 O OG  . SER   A 254 ? 0.45160 0.60439 0.36035 -0.05117 0.03245  0.22168  254 SER   A OG  
1951 N N   . ALA   A 255 ? 0.45050 0.60440 0.28716 -0.02979 0.03492  0.18910  255 ALA   A N   
1952 C CA  . ALA   A 255 ? 0.52631 0.68341 0.33119 -0.02606 0.03603  0.18817  255 ALA   A CA  
1953 C C   . ALA   A 255 ? 0.55380 0.69797 0.34229 -0.02489 0.02186  0.18535  255 ALA   A C   
1954 O O   . ALA   A 255 ? 0.60784 0.75043 0.37674 -0.02547 0.01715  0.19150  255 ALA   A O   
1955 C CB  . ALA   A 255 ? 0.54190 0.70836 0.32863 -0.01754 0.04837  0.17405  255 ALA   A CB  
1956 N N   . GLN   A 256 ? 0.53752 0.67323 0.33422 -0.02353 0.01441  0.17662  256 GLN   A N   
1957 C CA  . GLN   A 256 ? 0.55928 0.68491 0.34314 -0.02281 -0.00031 0.17350  256 GLN   A CA  
1958 C C   . GLN   A 256 ? 0.61842 0.73706 0.41779 -0.02839 -0.01238 0.18843  256 GLN   A C   
1959 O O   . GLN   A 256 ? 0.57778 0.69233 0.36153 -0.02853 -0.02211 0.19252  256 GLN   A O   
1960 C CB  . GLN   A 256 ? 0.58065 0.70146 0.37017 -0.02030 -0.00469 0.16015  256 GLN   A CB  
1961 C CG  . GLN   A 256 ? 0.63215 0.74091 0.43664 -0.02253 -0.02098 0.15924  256 GLN   A CG  
1962 C CD  . GLN   A 256 ? 0.73265 0.83264 0.54258 -0.01952 -0.02499 0.13951  256 GLN   A CD  
1963 O OE1 . GLN   A 256 ? 0.79256 0.89263 0.60340 -0.01627 -0.01554 0.12732  256 GLN   A OE1 
1964 N NE2 . GLN   A 256 ? 0.75131 0.84447 0.56539 -0.02081 -0.03950 0.13721  256 GLN   A NE2 
1965 N N   . THR   A 257 ? 0.57369 0.68965 0.40330 -0.03250 -0.01230 0.19631  257 THR   A N   
1966 C CA  . THR   A 257 ? 0.54350 0.65005 0.38973 -0.03640 -0.02402 0.20915  257 THR   A CA  
1967 C C   . THR   A 257 ? 0.53569 0.64430 0.37948 -0.04084 -0.02155 0.22382  257 THR   A C   
1968 O O   . THR   A 257 ? 0.52058 0.62032 0.37306 -0.04335 -0.03214 0.23463  257 THR   A O   
1969 C CB  . THR   A 257 ? 0.51781 0.61680 0.39614 -0.03797 -0.02650 0.20964  257 THR   A CB  
1970 O OG1 . THR   A 257 ? 0.46729 0.56948 0.36016 -0.04207 -0.01655 0.21489  257 THR   A OG1 
1971 C CG2 . THR   A 257 ? 0.49948 0.59799 0.38128 -0.03373 -0.02552 0.19330  257 THR   A CG2 
1972 N N   . GLY   A 258 ? 0.48845 0.60890 0.32117 -0.04152 -0.00825 0.22466  258 GLY   A N   
1973 C CA  . GLY   A 258 ? 0.49321 0.61742 0.32560 -0.04679 -0.00559 0.23969  258 GLY   A CA  
1974 C C   . GLY   A 258 ? 0.50710 0.62450 0.37032 -0.05344 -0.00869 0.25050  258 GLY   A C   
1975 O O   . GLY   A 258 ? 0.52467 0.63928 0.39041 -0.05860 -0.01243 0.26470  258 GLY   A O   
1976 N N   . ILE   A 259 ? 0.47527 0.58840 0.36112 -0.05350 -0.00793 0.24388  259 ILE   A N   
1977 C CA  . ILE   A 259 ? 0.47367 0.57758 0.38808 -0.05940 -0.01156 0.25160  259 ILE   A CA  
1978 C C   . ILE   A 259 ? 0.43188 0.54707 0.35813 -0.06204 0.00066  0.24827  259 ILE   A C   
1979 O O   . ILE   A 259 ? 0.46470 0.58431 0.39267 -0.05784 0.00656  0.23564  259 ILE   A O   
1980 C CB  . ILE   A 259 ? 0.48574 0.57264 0.41820 -0.05686 -0.02284 0.24681  259 ILE   A CB  
1981 C CG1 . ILE   A 259 ? 0.53173 0.60944 0.45558 -0.05362 -0.03590 0.25054  259 ILE   A CG1 
1982 C CG2 . ILE   A 259 ? 0.44900 0.52390 0.40865 -0.06223 -0.02647 0.25275  259 ILE   A CG2 
1983 C CD1 . ILE   A 259 ? 0.60602 0.66562 0.55286 -0.05194 -0.04836 0.25177  259 ILE   A CD1 
1984 N N   . ALA   A 260 ? 0.46565 0.58574 0.40099 -0.06917 0.00364  0.25997  260 ALA   A N   
1985 C CA  . ALA   A 260 ? 0.43752 0.56966 0.38711 -0.07243 0.01359  0.25840  260 ALA   A CA  
1986 C C   . ALA   A 260 ? 0.42253 0.54273 0.39586 -0.07306 0.00942  0.25089  260 ALA   A C   
1987 O O   . ALA   A 260 ? 0.42438 0.52511 0.40990 -0.07448 -0.00217 0.25301  260 ALA   A O   
1988 C CB  . ALA   A 260 ? 0.45572 0.59407 0.41305 -0.08133 0.01466  0.27430  260 ALA   A CB  
1989 N N   . VAL   A 261 ? 0.38999 0.52160 0.36954 -0.07127 0.01887  0.24171  261 VAL   A N   
1990 C CA  . VAL   A 261 ? 0.38790 0.50908 0.38730 -0.07132 0.01579  0.23331  261 VAL   A CA  
1991 C C   . VAL   A 261 ? 0.37925 0.48606 0.40087 -0.07964 0.00660  0.24210  261 VAL   A C   
1992 O O   . VAL   A 261 ? 0.36128 0.44867 0.39536 -0.07926 -0.00238 0.23807  261 VAL   A O   
1993 C CB  . VAL   A 261 ? 0.38618 0.52387 0.38850 -0.06836 0.02762  0.22341  261 VAL   A CB  
1994 C CG1 . VAL   A 261 ? 0.34635 0.47391 0.37040 -0.07022 0.02412  0.21686  261 VAL   A CG1 
1995 C CG2 . VAL   A 261 ? 0.39097 0.53682 0.37136 -0.05884 0.03462  0.21173  261 VAL   A CG2 
1996 N N   . LEU   A 262 ? 0.40964 0.52497 0.43594 -0.08703 0.00826  0.25413  262 LEU   A N   
1997 C CA  . LEU   A 262 ? 0.39707 0.49781 0.44367 -0.09559 -0.00132 0.26218  262 LEU   A CA  
1998 C C   . LEU   A 262 ? 0.41244 0.49027 0.45854 -0.09624 -0.01450 0.26876  262 LEU   A C   
1999 O O   . LEU   A 262 ? 0.41609 0.47390 0.47841 -0.10013 -0.02477 0.27024  262 LEU   A O   
2000 C CB  . LEU   A 262 ? 0.41427 0.53150 0.46672 -0.10408 0.00341  0.27456  262 LEU   A CB  
2001 C CG  . LEU   A 262 ? 0.40004 0.53576 0.46313 -0.10502 0.01267  0.26920  262 LEU   A CG  
2002 C CD1 . LEU   A 262 ? 0.42388 0.57975 0.49136 -0.11264 0.01802  0.28304  262 LEU   A CD1 
2003 C CD2 . LEU   A 262 ? 0.41806 0.53822 0.50111 -0.10739 0.00546  0.26138  262 LEU   A CD2 
2004 N N   . ASP   A 263 ? 0.42353 0.50296 0.45097 -0.09189 -0.01511 0.27205  263 ASP   A N   
2005 C CA  . ASP   A 263 ? 0.43619 0.49393 0.46386 -0.09034 -0.02825 0.27660  263 ASP   A CA  
2006 C C   . ASP   A 263 ? 0.42498 0.46626 0.46002 -0.08290 -0.03442 0.26386  263 ASP   A C   
2007 O O   . ASP   A 263 ? 0.42936 0.44830 0.47667 -0.08216 -0.04590 0.26448  263 ASP   A O   
2008 C CB  . ASP   A 263 ? 0.45900 0.52382 0.46419 -0.08732 -0.02803 0.28302  263 ASP   A CB  
2009 C CG  . ASP   A 263 ? 0.48033 0.55817 0.47820 -0.09471 -0.02367 0.29785  263 ASP   A CG  
2010 O OD1 . ASP   A 263 ? 0.48765 0.56559 0.50086 -0.10308 -0.02390 0.30549  263 ASP   A OD1 
2011 O OD2 . ASP   A 263 ? 0.50108 0.58857 0.47748 -0.09235 -0.02078 0.30224  263 ASP   A OD2 
2012 N N   . MET   A 264 ? 0.39409 0.44592 0.42150 -0.07672 -0.02695 0.25205  264 MET   A N   
2013 C CA  . MET   A 264 ? 0.38729 0.42580 0.42303 -0.07015 -0.03171 0.24047  264 MET   A CA  
2014 C C   . MET   A 264 ? 0.41471 0.43959 0.47177 -0.07349 -0.03479 0.23627  264 MET   A C   
2015 O O   . MET   A 264 ? 0.39636 0.40084 0.46440 -0.06939 -0.04384 0.23134  264 MET   A O   
2016 C CB  . MET   A 264 ? 0.37422 0.42758 0.39759 -0.06422 -0.02266 0.22938  264 MET   A CB  
2017 C CG  . MET   A 264 ? 0.34333 0.38576 0.37036 -0.05654 -0.02856 0.22004  264 MET   A CG  
2018 S SD  . MET   A 264 ? 0.42364 0.45344 0.44740 -0.05067 -0.04262 0.22494  264 MET   A SD  
2019 C CE  . MET   A 264 ? 0.38823 0.43682 0.38566 -0.04649 -0.03808 0.22076  264 MET   A CE  
2020 N N   . CYS   A 265 ? 0.38314 0.41899 0.44628 -0.08038 -0.02800 0.23782  265 CYS   A N   
2021 C CA  . CYS   A 265 ? 0.40745 0.42985 0.48967 -0.08468 -0.03260 0.23421  265 CYS   A CA  
2022 C C   . CYS   A 265 ? 0.42036 0.41807 0.51224 -0.08751 -0.04620 0.24081  265 CYS   A C   
2023 O O   . CYS   A 265 ? 0.40856 0.38521 0.51262 -0.08583 -0.05395 0.23348  265 CYS   A O   
2024 C CB  . CYS   A 265 ? 0.38009 0.42074 0.46782 -0.09219 -0.02454 0.23703  265 CYS   A CB  
2025 S SG  . CYS   A 265 ? 0.36332 0.42963 0.44297 -0.08701 -0.00923 0.22613  265 CYS   A SG  
2026 N N   . ALA   A 266 ? 0.42169 0.42062 0.50735 -0.09126 -0.04939 0.25410  266 ALA   A N   
2027 C CA  . ALA   A 266 ? 0.43625 0.41083 0.53025 -0.09351 -0.06271 0.26081  266 ALA   A CA  
2028 C C   . ALA   A 266 ? 0.47571 0.43027 0.56995 -0.08275 -0.07147 0.25382  266 ALA   A C   
2029 O O   . ALA   A 266 ? 0.48957 0.41915 0.59501 -0.08066 -0.08198 0.25050  266 ALA   A O   
2030 C CB  . ALA   A 266 ? 0.46937 0.45131 0.55587 -0.10014 -0.06360 0.27763  266 ALA   A CB  
2031 N N   . SER   A 267 ? 0.46276 0.42812 0.54464 -0.07521 -0.06778 0.25122  267 SER   A N   
2032 C CA  . SER   A 267 ? 0.47144 0.42236 0.55608 -0.06388 -0.07521 0.24331  267 SER   A CA  
2033 C C   . SER   A 267 ? 0.43466 0.37396 0.53189 -0.05896 -0.07554 0.22877  267 SER   A C   
2034 O O   . SER   A 267 ? 0.41998 0.33730 0.52743 -0.05201 -0.08470 0.22281  267 SER   A O   
2035 C CB  . SER   A 267 ? 0.47384 0.44198 0.54319 -0.05790 -0.07095 0.24246  267 SER   A CB  
2036 O OG  . SER   A 267 ? 0.52523 0.49909 0.58221 -0.06042 -0.07352 0.25486  267 SER   A OG  
2037 N N   . LEU   A 268 ? 0.42358 0.37741 0.51964 -0.06164 -0.06536 0.22230  268 LEU   A N   
2038 C CA  . LEU   A 268 ? 0.40940 0.35279 0.51615 -0.05752 -0.06528 0.20870  268 LEU   A CA  
2039 C C   . LEU   A 268 ? 0.43292 0.35443 0.55229 -0.06186 -0.07320 0.20699  268 LEU   A C   
2040 O O   . LEU   A 268 ? 0.44875 0.35008 0.57652 -0.05481 -0.07931 0.19602  268 LEU   A O   
2041 C CB  . LEU   A 268 ? 0.38256 0.34668 0.48511 -0.06057 -0.05280 0.20335  268 LEU   A CB  
2042 C CG  . LEU   A 268 ? 0.37145 0.32994 0.48299 -0.05811 -0.05050 0.18684  268 LEU   A CG  
2043 C CD1 . LEU   A 268 ? 0.35790 0.30510 0.47194 -0.04487 -0.05427 0.17043  268 LEU   A CD1 
2044 C CD2 . LEU   A 268 ? 0.30341 0.28616 0.40844 -0.05972 -0.03759 0.17995  268 LEU   A CD2 
2045 N N   . LYS   A 269 ? 0.39266 0.31811 0.51294 -0.07297 -0.07352 0.21739  269 LYS   A N   
2046 C CA  . LYS   A 269 ? 0.45662 0.36076 0.58775 -0.07846 -0.08300 0.21770  269 LYS   A CA  
2047 C C   . LYS   A 269 ? 0.49654 0.37221 0.63146 -0.07005 -0.09545 0.21476  269 LYS   A C   
2048 O O   . LYS   A 269 ? 0.51521 0.36818 0.65767 -0.06625 -0.10250 0.20403  269 LYS   A O   
2049 C CB  . LYS   A 269 ? 0.49772 0.41290 0.62875 -0.09115 -0.08233 0.23303  269 LYS   A CB  
2050 C CG  . LYS   A 269 ? 0.53675 0.43423 0.67923 -0.09957 -0.09168 0.23495  269 LYS   A CG  
2051 C CD  . LYS   A 269 ? 0.55236 0.46888 0.69613 -0.11261 -0.08813 0.25035  269 LYS   A CD  
2052 C CE  . LYS   A 269 ? 0.63820 0.53634 0.79345 -0.12211 -0.09956 0.25524  269 LYS   A CE  
2053 N NZ  . LYS   A 269 ? 0.66612 0.53706 0.82139 -0.11981 -0.11221 0.26003  269 LYS   A NZ  
2054 N N   . GLU   A 270 ? 0.46191 0.33854 0.59084 -0.06632 -0.09843 0.22362  270 GLU   A N   
2055 C CA  . GLU   A 270 ? 0.48735 0.33870 0.62049 -0.05744 -0.11017 0.22172  270 GLU   A CA  
2056 C C   . GLU   A 270 ? 0.52301 0.36626 0.65974 -0.04215 -0.11084 0.20586  270 GLU   A C   
2057 O O   . GLU   A 270 ? 0.53441 0.35370 0.67764 -0.03337 -0.11941 0.19770  270 GLU   A O   
2058 C CB  . GLU   A 270 ? 0.51389 0.37054 0.63973 -0.05753 -0.11329 0.23596  270 GLU   A CB  
2059 N N   . LEU   A 271 ? 0.47887 0.34230 0.61141 -0.03820 -0.10173 0.20106  271 LEU   A N   
2060 C CA  . LEU   A 271 ? 0.48293 0.34177 0.62085 -0.02445 -0.10124 0.18585  271 LEU   A CA  
2061 C C   . LEU   A 271 ? 0.50124 0.34322 0.64603 -0.02376 -0.10228 0.17227  271 LEU   A C   
2062 O O   . LEU   A 271 ? 0.52399 0.34895 0.67459 -0.01139 -0.10701 0.15951  271 LEU   A O   
2063 C CB  . LEU   A 271 ? 0.43945 0.32402 0.57139 -0.02270 -0.09138 0.18479  271 LEU   A CB  
2064 C CG  . LEU   A 271 ? 0.42062 0.32024 0.54524 -0.01874 -0.09216 0.19317  271 LEU   A CG  
2065 C CD1 . LEU   A 271 ? 0.42701 0.35438 0.54188 -0.01788 -0.08060 0.18456  271 LEU   A CD1 
2066 C CD2 . LEU   A 271 ? 0.47469 0.36209 0.60809 -0.00464 -0.10118 0.18825  271 LEU   A CD2 
2067 N N   . LEU   A 272 ? 0.46609 0.31391 0.60984 -0.03638 -0.09783 0.17423  272 LEU   A N   
2068 C CA  . LEU   A 272 ? 0.51543 0.34899 0.66415 -0.03708 -0.09930 0.16130  272 LEU   A CA  
2069 C C   . LEU   A 272 ? 0.56527 0.36951 0.71791 -0.03636 -0.11136 0.15822  272 LEU   A C   
2070 O O   . LEU   A 272 ? 0.58966 0.37513 0.74446 -0.02927 -0.11526 0.14300  272 LEU   A O   
2071 C CB  . LEU   A 272 ? 0.48807 0.33872 0.63585 -0.05119 -0.09211 0.16563  272 LEU   A CB  
2072 C CG  . LEU   A 272 ? 0.43403 0.31060 0.57737 -0.05059 -0.07947 0.16310  272 LEU   A CG  
2073 C CD1 . LEU   A 272 ? 0.41745 0.31173 0.56116 -0.06370 -0.07267 0.16825  272 LEU   A CD1 
2074 C CD2 . LEU   A 272 ? 0.44504 0.32092 0.58690 -0.03766 -0.07568 0.14083  272 LEU   A CD2 
2075 N N   . GLN   A 273 ? 0.53799 0.33762 0.69037 -0.04337 -0.11739 0.17216  273 GLN   A N   
2076 C CA  . GLN   A 273 ? 0.59617 0.36711 0.75200 -0.04391 -0.12955 0.17083  273 GLN   A CA  
2077 C C   . GLN   A 273 ? 0.63505 0.38698 0.79164 -0.02779 -0.13641 0.16470  273 GLN   A C   
2078 O O   . GLN   A 273 ? 0.66368 0.38908 0.82204 -0.02139 -0.14466 0.15426  273 GLN   A O   
2079 C CB  . GLN   A 273 ? 0.57894 0.35318 0.73543 -0.05904 -0.13337 0.18924  273 GLN   A CB  
2080 C CG  . GLN   A 273 ? 0.59595 0.38921 0.75411 -0.07432 -0.12736 0.19503  273 GLN   A CG  
2081 C CD  . GLN   A 273 ? 0.61046 0.41596 0.76892 -0.08769 -0.12783 0.21491  273 GLN   A CD  
2082 O OE1 . GLN   A 273 ? 0.66288 0.48531 0.82428 -0.09983 -0.12345 0.22149  273 GLN   A OE1 
2083 N NE2 . GLN   A 273 ? 0.63715 0.43577 0.79280 -0.08494 -0.13285 0.22474  273 GLN   A NE2 
2084 N N   . ASN   A 274 ? 0.59844 0.36409 0.75340 -0.02055 -0.13340 0.17070  274 ASN   A N   
2085 C CA  . ASN   A 274 ? 0.63307 0.38453 0.79037 -0.00566 -0.14020 0.16771  274 ASN   A CA  
2086 C C   . ASN   A 274 ? 0.64163 0.40222 0.80155 0.01149  -0.13493 0.15427  274 ASN   A C   
2087 O O   . ASN   A 274 ? 0.63716 0.38934 0.80083 0.02595  -0.13951 0.15005  274 ASN   A O   
2088 C CB  . ASN   A 274 ? 0.67102 0.42998 0.82573 -0.00976 -0.14349 0.18601  274 ASN   A CB  
2089 C CG  . ASN   A 274 ? 0.72222 0.47669 0.87501 -0.02708 -0.14767 0.20129  274 ASN   A CG  
2090 O OD1 . ASN   A 274 ? 0.79012 0.55531 0.93876 -0.03344 -0.14812 0.21725  274 ASN   A OD1 
2091 N ND2 . ASN   A 274 ? 0.77974 0.51886 0.93555 -0.03455 -0.15126 0.19649  274 ASN   A ND2 
2092 N N   . GLY   A 275 ? 0.61655 0.39546 0.77567 0.01058  -0.12540 0.14794  275 GLY   A N   
2093 C CA  . GLY   A 275 ? 0.62984 0.42013 0.79309 0.02607  -0.12017 0.13592  275 GLY   A CA  
2094 C C   . GLY   A 275 ? 0.64757 0.45879 0.81190 0.03091  -0.11900 0.14542  275 GLY   A C   
2095 O O   . GLY   A 275 ? 0.60695 0.42502 0.76609 0.02175  -0.12121 0.16128  275 GLY   A O   
2096 N N   . MET   A 276 ? 0.65430 0.47733 0.82543 0.04572  -0.11548 0.13491  276 MET   A N   
2097 C CA  . MET   A 276 ? 0.67104 0.51641 0.84510 0.05140  -0.11504 0.14159  276 MET   A CA  
2098 C C   . MET   A 276 ? 0.72245 0.55881 0.90316 0.06472  -0.12284 0.14120  276 MET   A C   
2099 O O   . MET   A 276 ? 0.66922 0.52134 0.85163 0.06750  -0.12529 0.14963  276 MET   A O   
2100 C CB  . MET   A 276 ? 0.64982 0.52178 0.82604 0.05739  -0.10400 0.12847  276 MET   A CB  
2101 C CG  . MET   A 276 ? 0.60517 0.49649 0.76898 0.04308  -0.09322 0.12806  276 MET   A CG  
2102 S SD  . MET   A 276 ? 0.60891 0.53651 0.76889 0.04298  -0.08563 0.12744  276 MET   A SD  
2103 C CE  . MET   A 276 ? 0.40306 0.34254 0.54668 0.02626  -0.07558 0.12887  276 MET   A CE  
2104 N N   . ASN   A 277 ? 0.71489 0.52613 0.89838 0.07303  -0.12704 0.13137  277 ASN   A N   
2105 C CA  . ASN   A 277 ? 0.73053 0.52922 0.92002 0.08744  -0.13406 0.12925  277 ASN   A CA  
2106 C C   . ASN   A 277 ? 0.68605 0.51043 0.88535 0.10049  -0.13217 0.12866  277 ASN   A C   
2107 O O   . ASN   A 277 ? 0.74880 0.57178 0.95191 0.10726  -0.13901 0.13569  277 ASN   A O   
2108 C CB  . ASN   A 277 ? 0.77958 0.55833 0.96341 0.07812  -0.14407 0.14430  277 ASN   A CB  
2109 C CG  . ASN   A 277 ? 0.75292 0.54932 0.93415 0.07174  -0.14683 0.16180  277 ASN   A CG  
2110 O OD1 . ASN   A 277 ? 0.76339 0.57819 0.93788 0.05919  -0.14205 0.17008  277 ASN   A OD1 
2111 N ND2 . ASN   A 277 ? 0.84165 0.63178 1.02687 0.08065  -0.15475 0.16741  277 ASN   A ND2 
2112 N N   . GLY   A 278 ? 0.66427 0.51297 0.86875 0.10399  -0.12317 0.12023  278 GLY   A N   
2113 C CA  . GLY   A 278 ? 0.65780 0.53292 0.87462 0.11723  -0.12031 0.11633  278 GLY   A CA  
2114 C C   . GLY   A 278 ? 0.60349 0.50798 0.82066 0.10881  -0.11941 0.12739  278 GLY   A C   
2115 O O   . GLY   A 278 ? 0.62465 0.55487 0.85320 0.11749  -0.11673 0.12395  278 GLY   A O   
2116 N N   . ARG   A 279 ? 0.61784 0.52062 0.82227 0.09210  -0.12137 0.14044  279 ARG   A N   
2117 C CA  . ARG   A 279 ? 0.54364 0.47285 0.74428 0.08413  -0.12064 0.14991  279 ARG   A CA  
2118 C C   . ARG   A 279 ? 0.50562 0.45399 0.70137 0.07762  -0.10833 0.13993  279 ARG   A C   
2119 O O   . ARG   A 279 ? 0.51180 0.45258 0.70621 0.07801  -0.10059 0.12730  279 ARG   A O   
2120 C CB  . ARG   A 279 ? 0.55712 0.47879 0.74142 0.06951  -0.12588 0.16666  279 ARG   A CB  
2121 N N   . THR   A 280 ? 0.44429 0.41728 0.63366 0.07059  -0.10597 0.14378  280 THR   A N   
2122 C CA  . THR   A 280 ? 0.43608 0.42758 0.61701 0.06291  -0.09413 0.13377  280 THR   A CA  
2123 C C   . THR   A 280 ? 0.44010 0.43832 0.60147 0.04809  -0.09343 0.14320  280 THR   A C   
2124 O O   . THR   A 280 ? 0.47867 0.47645 0.63448 0.04513  -0.10217 0.15716  280 THR   A O   
2125 C CB  . THR   A 280 ? 0.44321 0.46066 0.63695 0.07044  -0.09106 0.12571  280 THR   A CB  
2126 O OG1 . THR   A 280 ? 0.46681 0.49813 0.66320 0.07022  -0.10035 0.13678  280 THR   A OG1 
2127 C CG2 . THR   A 280 ? 0.46661 0.48075 0.67951 0.08689  -0.09017 0.11620  280 THR   A CG2 
2128 N N   . ILE   A 281 ? 0.40925 0.41348 0.55931 0.03961  -0.08295 0.13537  281 ILE   A N   
2129 C CA  . ILE   A 281 ? 0.39538 0.40766 0.52590 0.02730  -0.07988 0.14096  281 ILE   A CA  
2130 C C   . ILE   A 281 ? 0.36555 0.39685 0.49248 0.02513  -0.07225 0.12966  281 ILE   A C   
2131 O O   . ILE   A 281 ? 0.33046 0.36226 0.46083 0.02612  -0.06380 0.11780  281 ILE   A O   
2132 C CB  . ILE   A 281 ? 0.38982 0.38884 0.50958 0.01845  -0.07486 0.14402  281 ILE   A CB  
2133 C CG1 . ILE   A 281 ? 0.41771 0.39524 0.54273 0.01934  -0.08336 0.15566  281 ILE   A CG1 
2134 C CG2 . ILE   A 281 ? 0.37531 0.38545 0.47489 0.00791  -0.07034 0.14910  281 ILE   A CG2 
2135 C CD1 . ILE   A 281 ? 0.43611 0.40531 0.54975 0.00767  -0.08098 0.16533  281 ILE   A CD1 
2136 N N   . LEU   A 282 ? 0.38425 0.42978 0.50318 0.02166  -0.07613 0.13365  282 LEU   A N   
2137 C CA  . LEU   A 282 ? 0.34827 0.41004 0.46384 0.01867  -0.07134 0.12407  282 LEU   A CA  
2138 C C   . LEU   A 282 ? 0.33283 0.40241 0.46796 0.02622  -0.06746 0.11330  282 LEU   A C   
2139 O O   . LEU   A 282 ? 0.34784 0.42392 0.48121 0.02345  -0.05939 0.10334  282 LEU   A O   
2140 C CB  . LEU   A 282 ? 0.32034 0.38031 0.41744 0.01008  -0.06205 0.11908  282 LEU   A CB  
2141 C CG  . LEU   A 282 ? 0.32751 0.38594 0.40270 0.00279  -0.06385 0.12836  282 LEU   A CG  
2142 C CD1 . LEU   A 282 ? 0.32234 0.37982 0.38293 -0.00313 -0.05325 0.12228  282 LEU   A CD1 
2143 C CD2 . LEU   A 282 ? 0.36945 0.43919 0.43607 0.00104  -0.07194 0.13134  282 LEU   A CD2 
2144 N N   . GLY   A 283 ? 0.33359 0.40271 0.48728 0.03648  -0.07305 0.11575  283 GLY   A N   
2145 C CA  . GLY   A 283 ? 0.36879 0.44837 0.54185 0.04554  -0.06908 0.10661  283 GLY   A CA  
2146 C C   . GLY   A 283 ? 0.37539 0.44267 0.55178 0.05058  -0.06054 0.09681  283 GLY   A C   
2147 O O   . GLY   A 283 ? 0.40363 0.48047 0.59379 0.05866  -0.05563 0.08842  283 GLY   A O   
2148 N N   . SER   A 284 ? 0.33158 0.37925 0.49576 0.04587  -0.05867 0.09778  284 SER   A N   
2149 C CA  . SER   A 284 ? 0.35052 0.38445 0.51624 0.04963  -0.05245 0.08845  284 SER   A CA  
2150 C C   . SER   A 284 ? 0.37913 0.38979 0.54870 0.05489  -0.05968 0.09373  284 SER   A C   
2151 O O   . SER   A 284 ? 0.35506 0.35721 0.51943 0.05027  -0.06716 0.10614  284 SER   A O   
2152 C CB  . SER   A 284 ? 0.36237 0.39276 0.51250 0.03896  -0.04464 0.08417  284 SER   A CB  
2153 O OG  . SER   A 284 ? 0.38171 0.39375 0.53109 0.04042  -0.04247 0.07910  284 SER   A OG  
2154 N N   . ALA   A 285 ? 0.32261 0.32216 0.50036 0.06466  -0.05784 0.08433  285 ALA   A N   
2155 C CA  . ALA   A 285 ? 0.38632 0.35895 0.56678 0.06959  -0.06516 0.08695  285 ALA   A CA  
2156 C C   . ALA   A 285 ? 0.39595 0.35006 0.56526 0.06074  -0.06262 0.08399  285 ALA   A C   
2157 O O   . ALA   A 285 ? 0.44483 0.37393 0.61553 0.06266  -0.06938 0.08572  285 ALA   A O   
2158 C CB  . ALA   A 285 ? 0.37184 0.34036 0.56689 0.08713  -0.06609 0.07753  285 ALA   A CB  
2159 N N   . LEU   A 286 ? 0.35953 0.32504 0.51864 0.05099  -0.05401 0.08001  286 LEU   A N   
2160 C CA  . LEU   A 286 ? 0.37735 0.33124 0.52707 0.04173  -0.05092 0.07757  286 LEU   A CA  
2161 C C   . LEU   A 286 ? 0.35233 0.31488 0.49139 0.02821  -0.04930 0.08841  286 LEU   A C   
2162 O O   . LEU   A 286 ? 0.36218 0.34152 0.49796 0.02627  -0.04836 0.09346  286 LEU   A O   
2163 C CB  . LEU   A 286 ? 0.38244 0.34413 0.52932 0.04360  -0.04143 0.06276  286 LEU   A CB  
2164 C CG  . LEU   A 286 ? 0.40588 0.35686 0.55825 0.05590  -0.04092 0.04974  286 LEU   A CG  
2165 C CD1 . LEU   A 286 ? 0.44972 0.40006 0.59358 0.05245  -0.03389 0.03872  286 LEU   A CD1 
2166 C CD2 . LEU   A 286 ? 0.42497 0.34780 0.58134 0.06016  -0.05138 0.05271  286 LEU   A CD2 
2167 N N   . LEU   A 287 ? 0.31511 0.26702 0.44855 0.01900  -0.04905 0.09170  287 LEU   A N   
2168 C CA  . LEU   A 287 ? 0.32426 0.28760 0.44737 0.00744  -0.04493 0.10015  287 LEU   A CA  
2169 C C   . LEU   A 287 ? 0.31188 0.29039 0.42865 0.00539  -0.03490 0.08961  287 LEU   A C   
2170 O O   . LEU   A 287 ? 0.33296 0.30598 0.45048 0.00506  -0.03173 0.08076  287 LEU   A O   
2171 C CB  . LEU   A 287 ? 0.34623 0.29561 0.46862 -0.00193 -0.04856 0.10984  287 LEU   A CB  
2172 C CG  . LEU   A 287 ? 0.35378 0.28583 0.48162 -0.00154 -0.05953 0.12257  287 LEU   A CG  
2173 C CD1 . LEU   A 287 ? 0.38900 0.30307 0.51963 -0.01060 -0.06423 0.12931  287 LEU   A CD1 
2174 C CD2 . LEU   A 287 ? 0.36782 0.31176 0.48899 -0.00481 -0.06112 0.13678  287 LEU   A CD2 
2175 N N   . GLU   A 288 ? 0.29396 0.28995 0.40356 0.00381  -0.03097 0.09074  288 GLU   A N   
2176 C CA  . GLU   A 288 ? 0.30460 0.31360 0.40822 0.00266  -0.02277 0.08118  288 GLU   A CA  
2177 C C   . GLU   A 288 ? 0.28866 0.30184 0.38249 -0.00574 -0.01734 0.08372  288 GLU   A C   
2178 O O   . GLU   A 288 ? 0.23467 0.25191 0.32129 -0.01077 -0.01781 0.09382  288 GLU   A O   
2179 C CB  . GLU   A 288 ? 0.31689 0.34046 0.41774 0.00477  -0.02284 0.08079  288 GLU   A CB  
2180 C CG  . GLU   A 288 ? 0.46901 0.49928 0.57906 0.01208  -0.02162 0.07137  288 GLU   A CG  
2181 C CD  . GLU   A 288 ? 0.45600 0.48735 0.56496 0.01216  -0.01414 0.06017  288 GLU   A CD  
2182 O OE1 . GLU   A 288 ? 0.53483 0.56416 0.65226 0.01912  -0.01309 0.05308  288 GLU   A OE1 
2183 O OE2 . GLU   A 288 ? 0.42439 0.45897 0.52342 0.00605  -0.00932 0.05846  288 GLU   A OE2 
2184 N N   . ASP   A 289 ? 0.24337 0.25737 0.33643 -0.00661 -0.01181 0.07473  289 ASP   A N   
2185 C CA  . ASP   A 289 ? 0.26216 0.28120 0.34869 -0.01328 -0.00680 0.07712  289 ASP   A CA  
2186 C C   . ASP   A 289 ? 0.24437 0.27379 0.32342 -0.01282 -0.00001 0.06860  289 ASP   A C   
2187 O O   . ASP   A 289 ? 0.23186 0.26510 0.30760 -0.01625 0.00447  0.06800  289 ASP   A O   
2188 C CB  . ASP   A 289 ? 0.28087 0.28931 0.37431 -0.01680 -0.00850 0.07759  289 ASP   A CB  
2189 C CG  . ASP   A 289 ? 0.25699 0.26162 0.35259 -0.01385 -0.00642 0.06508  289 ASP   A CG  
2190 O OD1 . ASP   A 289 ? 0.26320 0.27042 0.35789 -0.00783 -0.00453 0.05640  289 ASP   A OD1 
2191 O OD2 . ASP   A 289 ? 0.26302 0.26205 0.36178 -0.01810 -0.00741 0.06483  289 ASP   A OD2 
2192 N N   . GLU   A 290 ? 0.25738 0.29177 0.33461 -0.00891 0.00038  0.06276  290 GLU   A N   
2193 C CA  . GLU   A 290 ? 0.26648 0.30797 0.33631 -0.00934 0.00557  0.05562  290 GLU   A CA  
2194 C C   . GLU   A 290 ? 0.30345 0.35241 0.36209 -0.01068 0.00557  0.05801  290 GLU   A C   
2195 O O   . GLU   A 290 ? 0.27604 0.32863 0.32962 -0.01038 0.00702  0.05195  290 GLU   A O   
2196 C CB  . GLU   A 290 ? 0.29442 0.33586 0.36974 -0.00551 0.00651  0.04667  290 GLU   A CB  
2197 C CG  . GLU   A 290 ? 0.30170 0.33424 0.38455 -0.00316 0.00625  0.04252  290 GLU   A CG  
2198 C CD  . GLU   A 290 ? 0.32520 0.35911 0.40692 -0.00143 0.01041  0.03321  290 GLU   A CD  
2199 O OE1 . GLU   A 290 ? 0.29842 0.34018 0.37780 -0.00099 0.01279  0.03025  290 GLU   A OE1 
2200 O OE2 . GLU   A 290 ? 0.31260 0.33918 0.39561 -0.00090 0.01051  0.02926  290 GLU   A OE2 
2201 N N   . PHE   A 291 ? 0.24960 0.30001 0.30282 -0.01261 0.00353  0.06697  291 PHE   A N   
2202 C CA  . PHE   A 291 ? 0.26125 0.31773 0.29943 -0.01381 0.00401  0.06872  291 PHE   A CA  
2203 C C   . PHE   A 291 ? 0.22431 0.28444 0.25476 -0.01610 0.00929  0.07397  291 PHE   A C   
2204 O O   . PHE   A 291 ? 0.24104 0.30058 0.27581 -0.01849 0.00830  0.08352  291 PHE   A O   
2205 C CB  . PHE   A 291 ? 0.27665 0.33439 0.31251 -0.01359 -0.00304 0.07565  291 PHE   A CB  
2206 C CG  . PHE   A 291 ? 0.29659 0.35518 0.34145 -0.01106 -0.00834 0.07171  291 PHE   A CG  
2207 C CD1 . PHE   A 291 ? 0.31789 0.38089 0.35654 -0.01179 -0.00977 0.06584  291 PHE   A CD1 
2208 C CD2 . PHE   A 291 ? 0.30522 0.36046 0.36543 -0.00780 -0.01228 0.07426  291 PHE   A CD2 
2209 C CE1 . PHE   A 291 ? 0.33523 0.40261 0.38493 -0.01037 -0.01453 0.06380  291 PHE   A CE1 
2210 C CE2 . PHE   A 291 ? 0.37043 0.43019 0.44095 -0.00438 -0.01624 0.07130  291 PHE   A CE2 
2211 C CZ  . PHE   A 291 ? 0.35301 0.42052 0.41927 -0.00619 -0.01708 0.06668  291 PHE   A CZ  
2212 N N   . THR   A 292 ? 0.23706 0.30137 0.25674 -0.01521 0.01479  0.06838  292 THR   A N   
2213 C CA  . THR   A 292 ? 0.23997 0.31171 0.25249 -0.01596 0.02092  0.07357  292 THR   A CA  
2214 C C   . THR   A 292 ? 0.27401 0.35063 0.27106 -0.01614 0.01994  0.08039  292 THR   A C   
2215 O O   . THR   A 292 ? 0.27963 0.35308 0.26922 -0.01544 0.01406  0.07866  292 THR   A O   
2216 C CB  . THR   A 292 ? 0.27562 0.35032 0.28132 -0.01287 0.02716  0.06505  292 THR   A CB  
2217 O OG1 . THR   A 292 ? 0.28967 0.36148 0.27983 -0.01018 0.02537  0.05804  292 THR   A OG1 
2218 C CG2 . THR   A 292 ? 0.28573 0.35570 0.30410 -0.01271 0.02759  0.05845  292 THR   A CG2 
2219 N N   . PRO   A 293 ? 0.28893 0.37468 0.28062 -0.01731 0.02552  0.08864  293 PRO   A N   
2220 C CA  . PRO   A 293 ? 0.28225 0.37386 0.25459 -0.01664 0.02583  0.09426  293 PRO   A CA  
2221 C C   . PRO   A 293 ? 0.34682 0.43611 0.29987 -0.01187 0.02559  0.08287  293 PRO   A C   
2222 O O   . PRO   A 293 ? 0.32597 0.41328 0.26444 -0.01172 0.02002  0.08375  293 PRO   A O   
2223 C CB  . PRO   A 293 ? 0.31199 0.41711 0.28337 -0.01790 0.03483  0.10335  293 PRO   A CB  
2224 C CG  . PRO   A 293 ? 0.28495 0.38812 0.27964 -0.02262 0.03418  0.10819  293 PRO   A CG  
2225 C CD  . PRO   A 293 ? 0.27556 0.36782 0.27961 -0.02031 0.03078  0.09533  293 PRO   A CD  
2226 N N   . PHE   A 294 ? 0.29584 0.38383 0.24845 -0.00818 0.03026  0.07219  294 PHE   A N   
2227 C CA  . PHE   A 294 ? 0.37743 0.45896 0.31260 -0.00401 0.02855  0.06048  294 PHE   A CA  
2228 C C   . PHE   A 294 ? 0.36101 0.43244 0.29896 -0.00686 0.01810  0.05637  294 PHE   A C   
2229 O O   . PHE   A 294 ? 0.36234 0.42940 0.28370 -0.00642 0.01244  0.05247  294 PHE   A O   
2230 C CB  . PHE   A 294 ? 0.43978 0.51974 0.37764 0.00031  0.03444  0.05104  294 PHE   A CB  
2231 C CG  . PHE   A 294 ? 0.61907 0.70966 0.54625 0.00622  0.04435  0.05124  294 PHE   A CG  
2232 C CD1 . PHE   A 294 ? 0.61784 0.72333 0.54654 0.00486  0.05036  0.06326  294 PHE   A CD1 
2233 C CD2 . PHE   A 294 ? 0.81928 0.90572 0.73649 0.01337  0.04785  0.04010  294 PHE   A CD2 
2234 C CE1 . PHE   A 294 ? 0.66822 0.78759 0.58901 0.01075  0.06078  0.06427  294 PHE   A CE1 
2235 C CE2 . PHE   A 294 ? 0.76065 0.85887 0.66953 0.02069  0.05777  0.03989  294 PHE   A CE2 
2236 C CZ  . PHE   A 294 ? 0.72811 0.84457 0.63917 0.01949  0.06485  0.05207  294 PHE   A CZ  
2237 N N   . ASP   A 295 ? 0.34186 0.41044 0.30074 -0.00970 0.01528  0.05716  295 ASP   A N   
2238 C CA  . ASP   A 295 ? 0.34313 0.40650 0.30868 -0.01204 0.00653  0.05473  295 ASP   A CA  
2239 C C   . ASP   A 295 ? 0.38194 0.44738 0.34112 -0.01373 -0.00091 0.06203  295 ASP   A C   
2240 O O   . ASP   A 295 ? 0.41351 0.47638 0.36739 -0.01508 -0.00873 0.05868  295 ASP   A O   
2241 C CB  . ASP   A 295 ? 0.29238 0.35481 0.28077 -0.01324 0.00625  0.05568  295 ASP   A CB  
2242 C CG  . ASP   A 295 ? 0.34381 0.40366 0.33822 -0.01210 0.01172  0.04842  295 ASP   A CG  
2243 O OD1 . ASP   A 295 ? 0.36712 0.42476 0.34978 -0.01025 0.01466  0.04206  295 ASP   A OD1 
2244 O OD2 . ASP   A 295 ? 0.28362 0.34275 0.29364 -0.01251 0.01263  0.04902  295 ASP   A OD2 
2245 N N   . VAL   A 296 ? 0.35565 0.42574 0.31644 -0.01441 0.00040  0.07300  296 VAL   A N   
2246 C CA  . VAL   A 296 ? 0.34540 0.41714 0.30046 -0.01590 -0.00730 0.08181  296 VAL   A CA  
2247 C C   . VAL   A 296 ? 0.40703 0.47977 0.33509 -0.01504 -0.00903 0.07945  296 VAL   A C   
2248 O O   . VAL   A 296 ? 0.41509 0.48622 0.33569 -0.01631 -0.01865 0.07945  296 VAL   A O   
2249 C CB  . VAL   A 296 ? 0.33590 0.41057 0.29856 -0.01750 -0.00546 0.09528  296 VAL   A CB  
2250 C CG1 . VAL   A 296 ? 0.35384 0.43002 0.30722 -0.01883 -0.01332 0.10590  296 VAL   A CG1 
2251 C CG2 . VAL   A 296 ? 0.31278 0.38279 0.30034 -0.01782 -0.00627 0.09599  296 VAL   A CG2 
2252 N N   . VAL   A 297 ? 0.40844 0.48430 0.32129 -0.01235 -0.00006 0.07699  297 VAL   A N   
2253 C CA  . VAL   A 297 ? 0.43705 0.51286 0.32087 -0.00980 -0.00064 0.07302  297 VAL   A CA  
2254 C C   . VAL   A 297 ? 0.47649 0.54196 0.35251 -0.00960 -0.00812 0.05990  297 VAL   A C   
2255 O O   . VAL   A 297 ? 0.54282 0.60462 0.40034 -0.01040 -0.01665 0.05786  297 VAL   A O   
2256 C CB  . VAL   A 297 ? 0.41819 0.50105 0.28996 -0.00504 0.01216  0.07181  297 VAL   A CB  
2257 C CG1 . VAL   A 297 ? 0.47823 0.55754 0.31880 0.00015  0.01225  0.06214  297 VAL   A CG1 
2258 C CG2 . VAL   A 297 ? 0.43449 0.52963 0.30935 -0.00704 0.01802  0.08743  297 VAL   A CG2 
2259 N N   . ARG   A 298 ? 0.45201 0.51218 0.34188 -0.00937 -0.00597 0.05150  298 ARG   A N   
2260 C CA  . ARG   A 298 ? 0.49678 0.54638 0.38155 -0.01067 -0.01327 0.04035  298 ARG   A CA  
2261 C C   . ARG   A 298 ? 0.51909 0.56870 0.41186 -0.01622 -0.02593 0.04371  298 ARG   A C   
2262 O O   . ARG   A 298 ? 0.57460 0.61820 0.45213 -0.01836 -0.03543 0.03889  298 ARG   A O   
2263 C CB  . ARG   A 298 ? 0.48074 0.52606 0.38145 -0.01024 -0.00847 0.03372  298 ARG   A CB  
2264 N N   . GLN   A 299 ? 0.47574 0.53208 0.39282 -0.01823 -0.02680 0.05172  299 GLN   A N   
2265 C CA  . GLN   A 299 ? 0.49400 0.55333 0.42290 -0.02216 -0.03813 0.05520  299 GLN   A CA  
2266 C C   . GLN   A 299 ? 0.54910 0.61110 0.46268 -0.02300 -0.04660 0.06218  299 GLN   A C   
2267 O O   . GLN   A 299 ? 0.60798 0.67028 0.52004 -0.02655 -0.05841 0.06162  299 GLN   A O   
2268 C CB  . GLN   A 299 ? 0.45176 0.51735 0.40944 -0.02177 -0.03624 0.06122  299 GLN   A CB  
2269 C CG  . GLN   A 299 ? 0.43701 0.50890 0.41015 -0.02411 -0.04697 0.06510  299 GLN   A CG  
2270 C CD  . GLN   A 299 ? 0.38198 0.45930 0.38326 -0.02238 -0.04418 0.06638  299 GLN   A CD  
2271 O OE1 . GLN   A 299 ? 0.36913 0.45430 0.38633 -0.02222 -0.05116 0.07073  299 GLN   A OE1 
2272 N NE2 . GLN   A 299 ? 0.35157 0.42547 0.35872 -0.02040 -0.03419 0.06238  299 GLN   A NE2 
2273 N N   . CYS   A 300 ? 0.55257 0.61743 0.45477 -0.02041 -0.04129 0.06963  300 CYS   A N   
2274 C CA  . CYS   A 300 ? 0.56353 0.63110 0.44883 -0.02122 -0.04911 0.07761  300 CYS   A CA  
2275 C C   . CYS   A 300 ? 0.63723 0.69912 0.48905 -0.02047 -0.05176 0.06970  300 CYS   A C   
2276 O O   . CYS   A 300 ? 0.58475 0.64736 0.41975 -0.02195 -0.06141 0.07385  300 CYS   A O   
2277 C CB  . CYS   A 300 ? 0.56885 0.64212 0.45563 -0.01976 -0.04279 0.09084  300 CYS   A CB  
2278 S SG  . CYS   A 300 ? 0.56391 0.63945 0.48728 -0.02012 -0.04371 0.09999  300 CYS   A SG  
2279 N N   . SER   A 301 ? 0.57124 0.62641 0.41217 -0.01763 -0.04436 0.05793  301 SER   A N   
2280 C CA  . SER   A 301 ? 0.63357 0.68015 0.44161 -0.01538 -0.04715 0.04790  301 SER   A CA  
2281 C C   . SER   A 301 ? 0.65496 0.68879 0.46167 -0.01862 -0.05651 0.03510  301 SER   A C   
2282 O O   . SER   A 301 ? 0.70318 0.72606 0.48176 -0.01726 -0.06180 0.02546  301 SER   A O   
2283 C CB  . SER   A 301 ? 0.67933 0.72671 0.47183 -0.00805 -0.03227 0.04364  301 SER   A CB  
2284 O OG  . SER   A 301 ? 0.86683 0.90293 0.62873 -0.00393 -0.03438 0.03057  301 SER   A OG  
2285 N N   . GLY   A 302 ? 0.64723 0.68169 0.48244 -0.02297 -0.05882 0.03484  302 GLY   A N   
2286 C CA  . GLY   A 302 ? 0.59111 0.61526 0.42835 -0.02818 -0.06860 0.02556  302 GLY   A CA  
2287 C C   . GLY   A 302 ? 0.61219 0.62101 0.43400 -0.02483 -0.06398 0.01225  302 GLY   A C   
2288 O O   . GLY   A 302 ? 0.60519 0.59963 0.40820 -0.02718 -0.07395 0.00285  302 GLY   A O   
2289 N N   . VAL   A 303 ? 0.60207 0.61279 0.43193 -0.01929 -0.04997 0.01134  303 VAL   A N   
2290 C CA  . VAL   A 303 ? 0.61465 0.61141 0.43254 -0.01460 -0.04508 -0.00054 303 VAL   A CA  
2291 C C   . VAL   A 303 ? 0.61298 0.59950 0.44511 -0.02148 -0.05264 -0.00554 303 VAL   A C   
2292 O O   . VAL   A 303 ? 0.58664 0.58246 0.44642 -0.02670 -0.05243 0.00106  303 VAL   A O   
2293 C CB  . VAL   A 303 ? 0.61885 0.62363 0.44500 -0.00727 -0.02887 0.00171  303 VAL   A CB  
2294 C CG1 . VAL   A 303 ? 0.64478 0.63612 0.46456 -0.00201 -0.02432 -0.00960 303 VAL   A CG1 
2295 C CG2 . VAL   A 303 ? 0.64035 0.65572 0.45032 -0.00120 -0.02119 0.00711  303 VAL   A CG2 
2296 N N   . THR   A 304 ? 0.58977 0.55670 0.40248 -0.02146 -0.05948 -0.01705 304 THR   A N   
2297 C CA  . THR   A 304 ? 0.60853 0.56334 0.43236 -0.02890 -0.06723 -0.02127 304 THR   A CA  
2298 C C   . THR   A 304 ? 0.72060 0.66130 0.53934 -0.02237 -0.05964 -0.02969 304 THR   A C   
2299 O O   . THR   A 304 ? 0.69018 0.62951 0.49394 -0.01145 -0.04980 -0.03414 304 THR   A O   
2300 C CB  . THR   A 304 ? 0.59687 0.53721 0.40490 -0.03663 -0.08501 -0.02685 304 THR   A CB  
2301 O OG1 . THR   A 304 ? 0.67129 0.59330 0.44379 -0.02907 -0.08704 -0.03869 304 THR   A OG1 
2302 C CG2 . THR   A 304 ? 0.53039 0.48652 0.34515 -0.04271 -0.09345 -0.01758 304 THR   A CG2 
2303 N N   . PHE   A 305 ? 0.62283 0.55451 0.45538 -0.02910 -0.06422 -0.03083 305 PHE   A N   
2304 C CA  . PHE   A 305 ? 0.66055 0.57801 0.49094 -0.02371 -0.05861 -0.03734 305 PHE   A CA  
2305 C C   . PHE   A 305 ? 0.67374 0.56541 0.49457 -0.03011 -0.07190 -0.04508 305 PHE   A C   
2306 O O   . PHE   A 305 ? 0.67762 0.56662 0.50203 -0.04168 -0.08500 -0.04296 305 PHE   A O   
2307 C CB  . PHE   A 305 ? 0.61570 0.54767 0.47432 -0.02487 -0.04868 -0.02916 305 PHE   A CB  
2308 C CG  . PHE   A 305 ? 0.58731 0.54241 0.45798 -0.02093 -0.03818 -0.02083 305 PHE   A CG  
2309 C CD1 . PHE   A 305 ? 0.62188 0.58198 0.48398 -0.01021 -0.02703 -0.02217 305 PHE   A CD1 
2310 C CD2 . PHE   A 305 ? 0.55294 0.52479 0.44358 -0.02781 -0.04007 -0.01138 305 PHE   A CD2 
2311 C CE1 . PHE   A 305 ? 0.60828 0.58803 0.48167 -0.00814 -0.01871 -0.01350 305 PHE   A CE1 
2312 C CE2 . PHE   A 305 ? 0.54512 0.53454 0.44585 -0.02418 -0.03191 -0.00387 305 PHE   A CE2 
2313 C CZ  . PHE   A 305 ? 0.60549 0.59797 0.49738 -0.01520 -0.02171 -0.00462 305 PHE   A CZ  
2314 C C13 . A1ALF B .   ? 0.37884 0.42070 0.30972 0.00020  0.04196  -0.01251 401 A1ALF A C13 
2315 C C15 . A1ALF B .   ? 0.38510 0.41110 0.29820 -0.00382 0.02721  -0.01066 401 A1ALF A C15 
2316 C C17 . A1ALF B .   ? 0.41242 0.43560 0.31030 -0.00670 0.02257  -0.00526 401 A1ALF A C17 
2317 C C20 . A1ALF B .   ? 0.42741 0.45334 0.35069 0.02067  0.03963  -0.04321 401 A1ALF A C20 
2318 C C21 . A1ALF B .   ? 0.44079 0.46976 0.36523 0.02980  0.04549  -0.05082 401 A1ALF A C21 
2319 C C22 . A1ALF B .   ? 0.46787 0.48270 0.38210 0.03686  0.04067  -0.06301 401 A1ALF A C22 
2320 C C24 . A1ALF B .   ? 0.52224 0.50072 0.41264 0.04001  0.02122  -0.08171 401 A1ALF A C24 
2321 C C26 . A1ALF B .   ? 0.54436 0.49070 0.40109 0.04458  0.00423  -0.10200 401 A1ALF A C26 
2322 C C02 . A1ALF B .   ? 0.38818 0.46496 0.37930 0.01229  0.06134  -0.01512 401 A1ALF A C02 
2323 C C04 . A1ALF B .   ? 0.51523 0.62122 0.49926 0.01985  0.07771  -0.01530 401 A1ALF A C04 
2324 C C05 . A1ALF B .   ? 0.42355 0.52162 0.39702 0.01172  0.07366  -0.01022 401 A1ALF A C05 
2325 C C06 . A1ALF B .   ? 0.42808 0.50645 0.40602 0.00814  0.06279  -0.01148 401 A1ALF A C06 
2326 C C07 . A1ALF B .   ? 0.34935 0.42549 0.33143 -0.00214 0.05918  -0.00141 401 A1ALF A C07 
2327 C C08 . A1ALF B .   ? 0.36956 0.44264 0.33560 -0.00685 0.05832  0.00338  401 A1ALF A C08 
2328 C C09 . A1ALF B .   ? 0.30503 0.37570 0.27578 -0.01576 0.05541  0.01320  401 A1ALF A C09 
2329 C C12 . A1ALF B .   ? 0.40208 0.45912 0.34037 -0.00047 0.05178  -0.00752 401 A1ALF A C12 
2330 C C14 . A1ALF B .   ? 0.41051 0.44963 0.32656 -0.00368 0.03864  -0.00706 401 A1ALF A C14 
2331 C C16 . A1ALF B .   ? 0.36615 0.38764 0.29902 -0.00575 0.02249  -0.00907 401 A1ALF A C16 
2332 C C19 . A1ALF B .   ? 0.41857 0.45554 0.35179 0.01315  0.04329  -0.03057 401 A1ALF A C19 
2333 C C23 . A1ALF B .   ? 0.49788 0.49563 0.40064 0.03333  0.02886  -0.06752 401 A1ALF A C23 
2334 C C25 . A1ALF B .   ? 0.48188 0.44892 0.35096 0.03891  0.01290  -0.08800 401 A1ALF A C25 
2335 C C27 . A1ALF B .   ? 0.58434 0.52077 0.45051 0.05168  0.00414  -0.10904 401 A1ALF A C27 
2336 C C29 . A1ALF B .   ? 0.63895 0.53465 0.50775 0.05916  -0.01225 -0.12675 401 A1ALF A C29 
2337 C C30 . A1ALF B .   ? 0.62589 0.51555 0.48479 0.07578  -0.00570 -0.13999 401 A1ALF A C30 
2338 C C31 . A1ALF B .   ? 0.53770 0.48669 0.42603 0.05324  0.01275  -0.10183 401 A1ALF A C31 
2339 C C32 . A1ALF B .   ? 0.51854 0.48910 0.41880 0.04701  0.02112  -0.08825 401 A1ALF A C32 
2340 C C33 . A1ALF B .   ? 0.48972 0.48778 0.39361 0.02378  0.02321  -0.05888 401 A1ALF A C33 
2341 C C34 . A1ALF B .   ? 0.40671 0.41801 0.32034 0.01837  0.02877  -0.04727 401 A1ALF A C34 
2342 N N03 . A1ALF B .   ? 0.39669 0.49229 0.39606 0.01814  0.07022  -0.01528 401 A1ALF A N03 
2343 N N10 . A1ALF B .   ? 0.34480 0.42907 0.31541 -0.02094 0.06151  0.02151  401 A1ALF A N10 
2344 N N11 . A1ALF B .   ? 0.36019 0.41929 0.31675 -0.00477 0.05151  -0.00188 401 A1ALF A N11 
2345 N N18 . A1ALF B .   ? 0.40917 0.44545 0.33222 0.00707  0.04038  -0.02372 401 A1ALF A N18 
2346 O O01 . A1ALF B .   ? 0.33318 0.40546 0.33616 0.00603  0.05623  -0.00955 401 A1ALF A O01 
2347 O O28 . A1ALF B .   ? 0.72711 0.63881 0.57937 0.05735  -0.00609 -0.12375 401 A1ALF A O28 
2348 O O35 . A1ALF B .   ? 0.37822 0.42219 0.32660 0.01226  0.04703  -0.02657 401 A1ALF A O35 
2349 O O36 . A1ALF B .   ? 0.42738 0.49519 0.35683 0.00236  0.05917  -0.00806 401 A1ALF A O36 
2350 O O   . HOH   C .   ? 0.72120 0.66993 0.50201 -0.01779 -0.09522 0.11161  501 HOH   A O   
2351 O O   . HOH   C .   ? 0.34778 0.40289 0.42869 -0.00106 0.01041  0.03323  502 HOH   A O   
2352 O O   . HOH   C .   ? 0.65728 0.29028 0.50808 -0.03986 -0.11330 -0.02245 503 HOH   A O   
2353 O O   . HOH   C .   ? 0.41177 0.50300 0.51105 -0.04595 0.02579  0.10725  504 HOH   A O   
2354 O O   . HOH   C .   ? 0.26987 0.46567 0.47055 0.00608  -0.05947 0.08424  505 HOH   A O   
2355 O O   . HOH   C .   ? 0.37491 0.42954 0.43002 0.00506  -0.01334 0.02307  506 HOH   A O   
2356 O O   . HOH   C .   ? 0.68511 0.29187 0.56093 -0.00212 -0.11317 0.04368  507 HOH   A O   
2357 O O   . HOH   C .   ? 0.67819 0.33194 0.52974 0.00825  -0.08921 -0.03317 508 HOH   A O   
2358 O O   . HOH   C .   ? 0.36104 0.49153 0.49150 -0.00634 -0.02122 0.05425  509 HOH   A O   
2359 O O   . HOH   C .   ? 0.56246 0.42060 0.48087 -0.13599 -0.04249 0.15905  510 HOH   A O   
2360 O O   . HOH   C .   ? 0.34126 0.40928 0.40274 0.02976  0.02289  0.01937  511 HOH   A O   
2361 O O   . HOH   C .   ? 0.76282 0.63272 0.53480 -0.06386 -0.07272 0.19219  512 HOH   A O   
2362 O O   . HOH   C .   ? 0.47402 0.49050 0.45755 0.00402  -0.05114 0.03556  513 HOH   A O   
2363 O O   . HOH   C .   ? 0.51583 0.50404 0.53547 -0.14416 -0.01594 0.10709  514 HOH   A O   
2364 O O   . HOH   C .   ? 0.62683 0.41841 0.78190 -0.00901 -0.10504 0.11543  515 HOH   A O   
2365 O O   . HOH   C .   ? 0.34927 0.50374 0.44046 -0.01644 0.05987  0.02742  516 HOH   A O   
2366 O O   . HOH   C .   ? 0.31862 0.34181 0.33748 -0.04989 0.01563  0.02811  517 HOH   A O   
2367 O O   . HOH   C .   ? 0.55993 0.56865 0.33972 -0.04026 0.00330  0.08438  518 HOH   A O   
2368 O O   . HOH   C .   ? 0.45582 0.29465 0.38696 -0.08173 -0.07106 0.00208  519 HOH   A O   
2369 O O   . HOH   C .   ? 0.55407 0.53322 0.32887 -0.04174 -0.02283 0.10386  520 HOH   A O   
2370 O O   . HOH   C .   ? 0.40199 0.53656 0.30959 -0.01581 0.04415  0.12769  521 HOH   A O   
2371 O O   . HOH   C .   ? 0.32415 0.36820 0.31757 -0.01046 0.01638  0.02433  522 HOH   A O   
2372 O O   . HOH   C .   ? 0.35836 0.63541 0.46856 -0.09245 0.07215  0.25045  523 HOH   A O   
2373 O O   . HOH   C .   ? 0.61212 0.74350 0.34591 -0.02727 -0.00224 0.20363  524 HOH   A O   
2374 O O   . HOH   C .   ? 0.31040 0.37219 0.44014 -0.04889 0.00198  0.06600  525 HOH   A O   
2375 O O   . HOH   C .   ? 0.24423 0.28416 0.30820 -0.01465 -0.00673 0.08830  526 HOH   A O   
2376 O O   . HOH   C .   ? 0.40487 0.52286 0.56442 -0.08366 0.01355  0.15022  527 HOH   A O   
2377 O O   . HOH   C .   ? 0.38752 0.28771 0.52085 -0.00659 -0.05743 0.09350  528 HOH   A O   
2378 O O   . HOH   C .   ? 0.42397 0.46581 0.30010 0.01255  0.04586  -0.02878 529 HOH   A O   
2379 O O   . HOH   C .   ? 0.35490 0.30447 0.34174 0.03313  -0.00082 0.01165  530 HOH   A O   
2380 O O   . HOH   C .   ? 0.47566 0.40182 0.46282 -0.02483 -0.06485 -0.05103 531 HOH   A O   
2381 O O   . HOH   C .   ? 0.32034 0.37847 0.35185 -0.01300 0.00528  0.04470  532 HOH   A O   
2382 O O   . HOH   C .   ? 0.31478 0.35184 0.36809 -0.01995 -0.02101 0.00832  533 HOH   A O   
2383 O O   . HOH   C .   ? 0.45707 0.27697 0.38268 0.02299  -0.03167 -0.00193 534 HOH   A O   
2384 O O   . HOH   C .   ? 0.26307 0.27820 0.24548 -0.01140 -0.02440 0.00418  535 HOH   A O   
2385 O O   . HOH   C .   ? 0.37270 0.32958 0.39644 -0.03101 -0.05353 -0.02892 536 HOH   A O   
2386 O O   . HOH   C .   ? 0.42032 0.41080 0.41446 0.02646  -0.04587 0.04766  537 HOH   A O   
2387 O O   . HOH   C .   ? 0.37978 0.44018 0.37711 -0.00256 0.03371  0.03192  538 HOH   A O   
2388 O O   . HOH   C .   ? 0.61838 0.49595 0.49242 -0.13878 -0.03637 0.20034  539 HOH   A O   
2389 O O   . HOH   C .   ? 0.25847 0.34575 0.30295 -0.02199 0.03439  0.08093  540 HOH   A O   
2390 O O   . HOH   C .   ? 0.38260 0.35897 0.38360 -0.02328 -0.04290 -0.02790 541 HOH   A O   
2391 O O   . HOH   C .   ? 0.49560 0.60038 0.42346 -0.07682 -0.01289 0.28683  542 HOH   A O   
2392 O O   . HOH   C .   ? 0.26013 0.29216 0.33311 -0.00087 0.01844  0.01644  543 HOH   A O   
2393 O O   . HOH   C .   ? 0.28566 0.31408 0.30604 -0.01263 -0.02185 0.00685  544 HOH   A O   
2394 O O   . HOH   C .   ? 0.61926 0.67559 0.29510 -0.02051 0.03341  0.05068  545 HOH   A O   
2395 O O   . HOH   C .   ? 0.28748 0.29707 0.29295 0.01926  0.02584  0.00403  546 HOH   A O   
2396 O O   . HOH   C .   ? 0.21575 0.23980 0.25553 -0.01060 0.01439  0.00154  547 HOH   A O   
2397 O O   . HOH   C .   ? 0.27928 0.27220 0.36247 -0.03516 -0.02511 0.00824  548 HOH   A O   
2398 O O   . HOH   C .   ? 0.41760 0.47959 0.39410 -0.00357 0.02888  0.03713  549 HOH   A O   
2399 O O   . HOH   C .   ? 0.41815 0.30255 0.28163 -0.01184 -0.07604 0.12056  550 HOH   A O   
2400 O O   . HOH   C .   ? 0.45121 0.43586 0.55662 0.00526  -0.01087 0.04184  551 HOH   A O   
2401 O O   . HOH   C .   ? 0.35378 0.31774 0.41887 0.00165  -0.00616 -0.01153 552 HOH   A O   
2402 O O   . HOH   C .   ? 0.33487 0.43151 0.42584 -0.01530 0.00115  0.03547  553 HOH   A O   
2403 O O   . HOH   C .   ? 0.38018 0.28847 0.51891 0.01848  -0.05694 0.08256  554 HOH   A O   
2404 O O   . HOH   C .   ? 0.31024 0.38342 0.40751 -0.01997 0.00660  0.03012  555 HOH   A O   
2405 O O   . HOH   C .   ? 0.43855 0.37655 0.38700 -0.06779 -0.05652 -0.00303 556 HOH   A O   
2406 O O   . HOH   C .   ? 0.45054 0.44138 0.21923 -0.01683 -0.04702 0.02980  557 HOH   A O   
2407 O O   . HOH   C .   ? 0.40108 0.32646 0.34878 0.02383  -0.05971 0.07074  558 HOH   A O   
2408 O O   . HOH   C .   ? 0.57888 0.55821 0.31857 -0.01851 -0.09488 0.04984  559 HOH   A O   
2409 O O   . HOH   C .   ? 0.51890 0.44014 0.51222 0.01431  -0.02176 -0.06248 560 HOH   A O   
2410 O O   . HOH   C .   ? 0.33266 0.33937 0.32313 0.01124  -0.03833 0.03761  561 HOH   A O   
2411 O O   . HOH   C .   ? 0.61490 0.45647 0.45594 -0.02110 -0.09110 0.15063  562 HOH   A O   
2412 O O   . HOH   C .   ? 0.33709 0.43711 0.44086 -0.01035 0.02194  0.03863  563 HOH   A O   
2413 O O   . HOH   C .   ? 0.43650 0.38260 0.33692 0.00401  -0.07241 0.08365  564 HOH   A O   
2414 O O   . HOH   C .   ? 0.38006 0.47975 0.35802 -0.00681 0.04387  0.07161  565 HOH   A O   
2415 O O   . HOH   C .   ? 0.34251 0.40254 0.45181 0.01237  -0.03944 0.08964  566 HOH   A O   
2416 O O   . HOH   C .   ? 0.72606 0.38000 0.59808 -0.01515 -0.12541 0.13832  567 HOH   A O   
2417 O O   . HOH   C .   ? 0.68645 0.66386 0.48058 -0.08943 0.00174  0.16528  568 HOH   A O   
2418 O O   . HOH   C .   ? 0.32214 0.34311 0.30486 0.00777  0.03013  0.00335  569 HOH   A O   
2419 O O   . HOH   C .   ? 0.53728 0.47359 0.66446 -0.12571 -0.08946 0.29447  570 HOH   A O   
2420 O O   . HOH   C .   ? 0.56035 0.35113 0.39501 -0.01211 -0.06530 -0.05914 571 HOH   A O   
2421 O O   . HOH   C .   ? 0.46145 0.68605 0.51835 -0.02301 0.10413  0.04808  572 HOH   A O   
2422 O O   . HOH   C .   ? 0.53481 0.48628 0.31402 0.01455  -0.03102 -0.08022 573 HOH   A O   
2423 O O   . HOH   C .   ? 0.35873 0.37494 0.38734 0.03544  -0.03383 0.03875  574 HOH   A O   
2424 O O   . HOH   C .   ? 0.35361 0.41548 0.34373 -0.01831 -0.01548 0.05067  575 HOH   A O   
2425 O O   . HOH   C .   ? 0.24600 0.28536 0.28267 -0.00522 -0.01133 0.01479  576 HOH   A O   
2426 O O   . HOH   C .   ? 0.39457 0.47315 0.42020 0.04848  0.05280  0.00965  577 HOH   A O   
2427 O O   . HOH   C .   ? 0.31737 0.38229 0.34398 -0.01685 -0.00909 0.04598  578 HOH   A O   
2428 O O   . HOH   C .   ? 0.58573 0.49456 0.47770 -0.01078 -0.07509 -0.08137 579 HOH   A O   
2429 O O   . HOH   C .   ? 0.34667 0.44643 0.43742 -0.00699 0.03307  0.04023  580 HOH   A O   
2430 O O   . HOH   C .   ? 0.43407 0.38869 0.38735 0.07372  0.02479  -0.02624 581 HOH   A O   
2431 O O   . HOH   C .   ? 0.46193 0.70754 0.46979 -0.07003 0.07757  0.24115  582 HOH   A O   
2432 O O   . HOH   C .   ? 0.54942 0.33001 0.39653 -0.03576 -0.09595 0.16318  583 HOH   A O   
2433 O O   . HOH   C .   ? 0.40546 0.38985 0.53191 -0.05422 -0.02926 0.05113  584 HOH   A O   
2434 O O   . HOH   C .   ? 0.47563 0.55177 0.38016 0.02236  0.07022  -0.02857 585 HOH   A O   
2435 O O   . HOH   C .   ? 0.39842 0.60480 0.46877 -0.09444 0.04832  0.25186  586 HOH   A O   
2436 O O   . HOH   C .   ? 0.45878 0.57184 0.56592 0.00499  -0.08187 0.11223  587 HOH   A O   
2437 O O   . HOH   C .   ? 0.38023 0.38200 0.29350 -0.01077 -0.05738 0.02257  588 HOH   A O   
2438 O O   . HOH   C .   ? 0.54974 0.33551 0.45458 0.01762  -0.08993 0.10496  589 HOH   A O   
2439 O O   . HOH   C .   ? 0.48838 0.50154 0.44531 -0.01004 -0.05186 0.01689  590 HOH   A O   
2440 O O   . HOH   C .   ? 0.67795 0.36907 0.53790 -0.05293 -0.11375 0.16582  591 HOH   A O   
2441 O O   . HOH   C .   ? 0.38953 0.50053 0.40876 -0.01552 0.04774  0.08460  592 HOH   A O   
2442 O O   . HOH   C .   ? 0.38104 0.38270 0.30963 -0.01258 -0.03366 -0.00262 593 HOH   A O   
2443 O O   . HOH   C .   ? 0.71035 0.36618 0.58061 0.04163  -0.08263 -0.01766 594 HOH   A O   
2444 O O   . HOH   C .   ? 0.54345 0.36618 0.41904 0.00330  -0.09833 0.13368  595 HOH   A O   
2445 O O   . HOH   C .   ? 0.42092 0.31651 0.33467 0.00995  -0.06760 0.09058  596 HOH   A O   
2446 O O   . HOH   C .   ? 0.40399 0.43969 0.37358 0.01767  0.03854  0.00464  597 HOH   A O   
2447 O O   . HOH   C .   ? 0.33611 0.45088 0.43832 0.00000  -0.00763 -0.00000 598 HOH   A O   
2448 O O   . HOH   C .   ? 0.49368 0.51525 0.63679 -0.06428 -0.02282 0.06755  599 HOH   A O   
2449 O O   . HOH   C .   ? 0.63239 0.40844 0.54520 0.05142  -0.04301 -0.01075 600 HOH   A O   
2450 O O   . HOH   C .   ? 0.40870 0.42001 0.37360 -0.01410 -0.04348 0.00288  601 HOH   A O   
2451 O O   . HOH   C .   ? 0.38278 0.48160 0.45730 -0.03188 0.03567  0.09229  602 HOH   A O   
2452 O O   . HOH   C .   ? 0.43551 0.73061 0.45599 -0.07235 0.09597  0.25585  603 HOH   A O   
2453 O O   . HOH   C .   ? 0.40755 0.31618 0.29795 0.00488  -0.07934 0.10262  604 HOH   A O   
2454 O O   . HOH   C .   ? 0.38033 0.70839 0.47717 -0.07221 0.09992  0.24148  605 HOH   A O   
2455 O O   . HOH   C .   ? 0.48672 0.42223 0.46889 0.05593  -0.00010 0.00121  606 HOH   A O   
2456 O O   . HOH   C .   ? 0.45711 0.44288 0.43503 0.02617  -0.06742 0.06100  607 HOH   A O   
2457 O O   . HOH   C .   ? 0.32048 0.34591 0.43246 -0.04585 -0.02292 0.02950  608 HOH   A O   
2458 O O   . HOH   C .   ? 0.46818 0.68303 0.56409 -0.11276 0.04173  0.27620  609 HOH   A O   
2459 O O   . HOH   C .   ? 0.36532 0.40756 0.40830 -0.01764 -0.03905 0.01199  610 HOH   A O   
2460 O O   . HOH   C .   ? 0.33520 0.59747 0.48349 -0.10279 0.05699  0.24566  611 HOH   A O   
2461 O O   . HOH   C .   ? 0.50331 0.34458 0.64706 -0.00717 -0.07991 0.09326  612 HOH   A O   
2462 O O   . HOH   C .   ? 0.48300 0.43551 0.42817 0.02042  -0.06841 0.07225  613 HOH   A O   
2463 O O   . HOH   C .   ? 0.55833 0.46801 0.52272 0.04969  -0.07828 0.07821  614 HOH   A O   
2464 O O   . HOH   C .   ? 0.52500 0.53427 0.49244 -0.02045 -0.06332 -0.00319 615 HOH   A O   
# 
