data_9M18
# 
_entry.id   9M18 
# 
_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   9M18         pdb_00009m18 10.2210/pdb9m18/pdb 
WWPDB D_1300056763 ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2025-06-11 
_pdbx_audit_revision_history.part_number         ? 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9M18 
_pdbx_database_status.recvd_initial_deposition_date   2025-02-25 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBJ 
_pdbx_database_status.process_site                    PDBJ 
_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                 2 
_pdbx_contact_author.email              ito.str@tmd.ac.jp 
_pdbx_contact_author.name_first         Nobutoshi 
_pdbx_contact_author.name_last          Ito 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0003-0839-0384 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Thilakarathne, N.M.H.N.' 1 ? 
'Hanazono, Y.'            2 ? 
'Ito, N.'                 3 ? 
'Kagechika, H.'           4 ? 
'Fujii, S.'               5 ? 
# 
_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                   UK 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            Bioorg.Med.Chem. 
_citation.journal_id_ASTM           BMECEP 
_citation.journal_id_CSD            1200 
_citation.journal_id_ISSN           1464-3391 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                118261 
_citation.page_last                 ? 
_citation.title                     
;Structure-activity relationship and crystallographic analyses of non-secosteroidal vitamin D receptor ligands bearing diphenylsilane core as a hydrophobic pharmacophore
;
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1016/j.bmc.2025.118261 
_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 'Mudiyanselage, H.N.T.N.' 1 ? 
primary 'Misawa, T.'              2 ? 
primary 'Ochiai, K.'              3 ? 
primary 'Demizu, Y.'              4 ? 
primary 'Hanazono, Y.'            5 ? 
primary 'Ito, N.'                 6 ? 
primary 'Fujii, S.'               7 ? 
# 
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 'Vitamin D3 receptor' 30595.037 1  ? ? ? ? 
2 polymer     syn 'Mediator of RNA polymerase II transcription subunit 1' 1570.898  1  ? ? ? ? 
3 non-polymer nat 
'(4~{S})-5-[4-[[4-(2-ethyl-2-oxidanyl-butoxy)-3-methyl-phenyl]-bis(prop-2-enyl)silyl]-2-methyl-phenoxy]-4-oxidanyl-pentanoic acid' 
540.763   1  ? ? ? ? 
4 water       nat water 18.015    83 ? ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'VDR,1,25-dihydroxyvitamin D3 receptor,Nuclear receptor subfamily 1 group I member 1' 
# 
loop_
_entity_poly.entity_id 
_entity_poly.type 
_entity_poly.nstd_linkage 
_entity_poly.nstd_monomer 
_entity_poly.pdbx_seq_one_letter_code 
_entity_poly.pdbx_seq_one_letter_code_can 
_entity_poly.pdbx_strand_id 
_entity_poly.pdbx_target_identifier 
1 'polypeptide(L)' no no 
;GSHMGSPNSPLKDSLRPKLSEEQQHIIAILLDAHHKTYDPTYADFRDFRPPVRMDGSTGSVTLDLSPLSMLPHLADLVSY
SIQKVIGFAKMIPGFRDLTSDDQIVLLKSSAIEVIMLRSNQSFTMDDMSWDCGSQDYKYDVTDVSKAGHTLELIEPLIKF
QVGLKKLNLHEEEHVLLMAICIVSPDRPGVQDAKLVEAIQDRLSNTLQTYIRCRHPPPGSHQLYAKMIQKLADLRSLNEE
HSKQYRSLSFQPENSMKLTPLVLEVFGNEIS
;
;GSHMGSPNSPLKDSLRPKLSEEQQHIIAILLDAHHKTYDPTYADFRDFRPPVRMDGSTGSVTLDLSPLSMLPHLADLVSY
SIQKVIGFAKMIPGFRDLTSDDQIVLLKSSAIEVIMLRSNQSFTMDDMSWDCGSQDYKYDVTDVSKAGHTLELIEPLIKF
QVGLKKLNLHEEEHVLLMAICIVSPDRPGVQDAKLVEAIQDRLSNTLQTYIRCRHPPPGSHQLYAKMIQKLADLRSLNEE
HSKQYRSLSFQPENSMKLTPLVLEVFGNEIS
;
A ? 
2 'polypeptide(L)' no no KNHPMLMNLLKDN KNHPMLMNLLKDN C ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
3 
'(4~{S})-5-[4-[[4-(2-ethyl-2-oxidanyl-butoxy)-3-methyl-phenyl]-bis(prop-2-enyl)silyl]-2-methyl-phenoxy]-4-oxidanyl-pentanoic acid' 
A1L76 
4 water HOH   
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   GLY n 
1 2   SER n 
1 3   HIS n 
1 4   MET n 
1 5   GLY n 
1 6   SER n 
1 7   PRO n 
1 8   ASN n 
1 9   SER n 
1 10  PRO n 
1 11  LEU n 
1 12  LYS n 
1 13  ASP n 
1 14  SER n 
1 15  LEU n 
1 16  ARG n 
1 17  PRO n 
1 18  LYS n 
1 19  LEU n 
1 20  SER n 
1 21  GLU n 
1 22  GLU n 
1 23  GLN n 
1 24  GLN n 
1 25  HIS n 
1 26  ILE n 
1 27  ILE n 
1 28  ALA n 
1 29  ILE n 
1 30  LEU n 
1 31  LEU n 
1 32  ASP n 
1 33  ALA n 
1 34  HIS n 
1 35  HIS n 
1 36  LYS n 
1 37  THR n 
1 38  TYR n 
1 39  ASP n 
1 40  PRO n 
1 41  THR n 
1 42  TYR n 
1 43  ALA n 
1 44  ASP n 
1 45  PHE n 
1 46  ARG n 
1 47  ASP n 
1 48  PHE n 
1 49  ARG n 
1 50  PRO n 
1 51  PRO n 
1 52  VAL n 
1 53  ARG n 
1 54  MET n 
1 55  ASP n 
1 56  GLY n 
1 57  SER n 
1 58  THR n 
1 59  GLY n 
1 60  SER n 
1 61  VAL n 
1 62  THR n 
1 63  LEU n 
1 64  ASP n 
1 65  LEU n 
1 66  SER n 
1 67  PRO n 
1 68  LEU n 
1 69  SER n 
1 70  MET n 
1 71  LEU n 
1 72  PRO n 
1 73  HIS n 
1 74  LEU n 
1 75  ALA n 
1 76  ASP n 
1 77  LEU n 
1 78  VAL n 
1 79  SER n 
1 80  TYR n 
1 81  SER n 
1 82  ILE n 
1 83  GLN n 
1 84  LYS n 
1 85  VAL n 
1 86  ILE n 
1 87  GLY n 
1 88  PHE n 
1 89  ALA n 
1 90  LYS n 
1 91  MET n 
1 92  ILE n 
1 93  PRO n 
1 94  GLY n 
1 95  PHE n 
1 96  ARG n 
1 97  ASP n 
1 98  LEU n 
1 99  THR n 
1 100 SER n 
1 101 ASP n 
1 102 ASP n 
1 103 GLN n 
1 104 ILE n 
1 105 VAL n 
1 106 LEU n 
1 107 LEU n 
1 108 LYS n 
1 109 SER n 
1 110 SER n 
1 111 ALA n 
1 112 ILE n 
1 113 GLU n 
1 114 VAL n 
1 115 ILE n 
1 116 MET n 
1 117 LEU n 
1 118 ARG n 
1 119 SER n 
1 120 ASN n 
1 121 GLN n 
1 122 SER n 
1 123 PHE n 
1 124 THR n 
1 125 MET n 
1 126 ASP n 
1 127 ASP n 
1 128 MET n 
1 129 SER n 
1 130 TRP n 
1 131 ASP n 
1 132 CYS n 
1 133 GLY n 
1 134 SER n 
1 135 GLN n 
1 136 ASP n 
1 137 TYR n 
1 138 LYS n 
1 139 TYR n 
1 140 ASP n 
1 141 VAL n 
1 142 THR n 
1 143 ASP n 
1 144 VAL n 
1 145 SER n 
1 146 LYS n 
1 147 ALA n 
1 148 GLY n 
1 149 HIS n 
1 150 THR n 
1 151 LEU n 
1 152 GLU n 
1 153 LEU n 
1 154 ILE n 
1 155 GLU n 
1 156 PRO n 
1 157 LEU n 
1 158 ILE n 
1 159 LYS n 
1 160 PHE n 
1 161 GLN n 
1 162 VAL n 
1 163 GLY n 
1 164 LEU n 
1 165 LYS n 
1 166 LYS n 
1 167 LEU n 
1 168 ASN n 
1 169 LEU n 
1 170 HIS n 
1 171 GLU n 
1 172 GLU n 
1 173 GLU n 
1 174 HIS n 
1 175 VAL n 
1 176 LEU n 
1 177 LEU n 
1 178 MET n 
1 179 ALA n 
1 180 ILE n 
1 181 CYS n 
1 182 ILE n 
1 183 VAL n 
1 184 SER n 
1 185 PRO n 
1 186 ASP n 
1 187 ARG n 
1 188 PRO n 
1 189 GLY n 
1 190 VAL n 
1 191 GLN n 
1 192 ASP n 
1 193 ALA n 
1 194 LYS n 
1 195 LEU n 
1 196 VAL n 
1 197 GLU n 
1 198 ALA n 
1 199 ILE n 
1 200 GLN n 
1 201 ASP n 
1 202 ARG n 
1 203 LEU n 
1 204 SER n 
1 205 ASN n 
1 206 THR n 
1 207 LEU n 
1 208 GLN n 
1 209 THR n 
1 210 TYR n 
1 211 ILE n 
1 212 ARG n 
1 213 CYS n 
1 214 ARG n 
1 215 HIS n 
1 216 PRO n 
1 217 PRO n 
1 218 PRO n 
1 219 GLY n 
1 220 SER n 
1 221 HIS n 
1 222 GLN n 
1 223 LEU n 
1 224 TYR n 
1 225 ALA n 
1 226 LYS n 
1 227 MET n 
1 228 ILE n 
1 229 GLN n 
1 230 LYS n 
1 231 LEU n 
1 232 ALA n 
1 233 ASP n 
1 234 LEU n 
1 235 ARG n 
1 236 SER n 
1 237 LEU n 
1 238 ASN n 
1 239 GLU n 
1 240 GLU n 
1 241 HIS n 
1 242 SER n 
1 243 LYS n 
1 244 GLN n 
1 245 TYR n 
1 246 ARG n 
1 247 SER n 
1 248 LEU n 
1 249 SER n 
1 250 PHE n 
1 251 GLN n 
1 252 PRO n 
1 253 GLU n 
1 254 ASN n 
1 255 SER n 
1 256 MET n 
1 257 LYS n 
1 258 LEU n 
1 259 THR n 
1 260 PRO n 
1 261 LEU n 
1 262 VAL n 
1 263 LEU n 
1 264 GLU n 
1 265 VAL n 
1 266 PHE n 
1 267 GLY n 
1 268 ASN n 
1 269 GLU n 
1 270 ILE n 
1 271 SER n 
2 1   LYS n 
2 2   ASN n 
2 3   HIS n 
2 4   PRO n 
2 5   MET n 
2 6   LEU n 
2 7   MET n 
2 8   ASN n 
2 9   LEU n 
2 10  LEU n 
2 11  LYS n 
2 12  ASP n 
2 13  ASN n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   271 
_entity_src_gen.gene_src_common_name               'Norway rat' 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'Vdr, Nr1i1' 
_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      'Rattus norvegicus' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     10116 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     562 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_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                   ? 
# 
_pdbx_entity_src_syn.entity_id              2 
_pdbx_entity_src_syn.pdbx_src_id            1 
_pdbx_entity_src_syn.pdbx_alt_source_flag   sample 
_pdbx_entity_src_syn.pdbx_beg_seq_num       1 
_pdbx_entity_src_syn.pdbx_end_seq_num       13 
_pdbx_entity_src_syn.organism_scientific    'Homo sapiens' 
_pdbx_entity_src_syn.organism_common_name   human 
_pdbx_entity_src_syn.ncbi_taxonomy_id       9606 
_pdbx_entity_src_syn.details                ? 
# 
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 
A1L76 non-polymer         . 
'(4~{S})-5-[4-[[4-(2-ethyl-2-oxidanyl-butoxy)-3-methyl-phenyl]-bis(prop-2-enyl)silyl]-2-methyl-phenoxy]-4-oxidanyl-pentanoic acid' 
? 'C31 H44 O6 Si'  540.763 
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   GLY 1   106 ?   ?   ?   A . n 
A 1 2   SER 2   107 ?   ?   ?   A . n 
A 1 3   HIS 3   108 ?   ?   ?   A . n 
A 1 4   MET 4   109 ?   ?   ?   A . n 
A 1 5   GLY 5   110 ?   ?   ?   A . n 
A 1 6   SER 6   111 ?   ?   ?   A . n 
A 1 7   PRO 7   112 ?   ?   ?   A . n 
A 1 8   ASN 8   113 ?   ?   ?   A . n 
A 1 9   SER 9   114 ?   ?   ?   A . n 
A 1 10  PRO 10  115 ?   ?   ?   A . n 
A 1 11  LEU 11  116 ?   ?   ?   A . n 
A 1 12  LYS 12  117 ?   ?   ?   A . n 
A 1 13  ASP 13  118 ?   ?   ?   A . n 
A 1 14  SER 14  119 ?   ?   ?   A . n 
A 1 15  LEU 15  120 ?   ?   ?   A . n 
A 1 16  ARG 16  121 ?   ?   ?   A . n 
A 1 17  PRO 17  122 ?   ?   ?   A . n 
A 1 18  LYS 18  123 123 LYS LYS A . n 
A 1 19  LEU 19  124 124 LEU LEU A . n 
A 1 20  SER 20  125 125 SER SER A . n 
A 1 21  GLU 21  126 126 GLU GLU A . n 
A 1 22  GLU 22  127 127 GLU GLU A . n 
A 1 23  GLN 23  128 128 GLN GLN A . n 
A 1 24  GLN 24  129 129 GLN GLN A . n 
A 1 25  HIS 25  130 130 HIS HIS A . n 
A 1 26  ILE 26  131 131 ILE ILE A . n 
A 1 27  ILE 27  132 132 ILE ILE A . n 
A 1 28  ALA 28  133 133 ALA ALA A . n 
A 1 29  ILE 29  134 134 ILE ILE A . n 
A 1 30  LEU 30  135 135 LEU LEU A . n 
A 1 31  LEU 31  136 136 LEU LEU A . n 
A 1 32  ASP 32  137 137 ASP ASP A . n 
A 1 33  ALA 33  138 138 ALA ALA A . n 
A 1 34  HIS 34  139 139 HIS HIS A . n 
A 1 35  HIS 35  140 140 HIS HIS A . n 
A 1 36  LYS 36  141 141 LYS LYS A . n 
A 1 37  THR 37  142 142 THR THR A . n 
A 1 38  TYR 38  143 143 TYR TYR A . n 
A 1 39  ASP 39  144 144 ASP ASP A . n 
A 1 40  PRO 40  145 145 PRO PRO A . n 
A 1 41  THR 41  146 146 THR THR A . n 
A 1 42  TYR 42  147 147 TYR TYR A . n 
A 1 43  ALA 43  148 148 ALA ALA A . n 
A 1 44  ASP 44  149 149 ASP ASP A . n 
A 1 45  PHE 45  150 150 PHE PHE A . n 
A 1 46  ARG 46  151 151 ARG ARG A . n 
A 1 47  ASP 47  152 152 ASP ASP A . n 
A 1 48  PHE 48  153 153 PHE PHE A . n 
A 1 49  ARG 49  154 154 ARG ARG A . n 
A 1 50  PRO 50  155 155 PRO PRO A . n 
A 1 51  PRO 51  156 156 PRO PRO A . n 
A 1 52  VAL 52  157 157 VAL VAL A . n 
A 1 53  ARG 53  158 158 ARG ARG A . n 
A 1 54  MET 54  159 159 MET MET A . n 
A 1 55  ASP 55  207 ?   ?   ?   A . n 
A 1 56  GLY 56  208 ?   ?   ?   A . n 
A 1 57  SER 57  209 ?   ?   ?   A . n 
A 1 58  THR 58  210 ?   ?   ?   A . n 
A 1 59  GLY 59  211 ?   ?   ?   A . n 
A 1 60  SER 60  212 ?   ?   ?   A . n 
A 1 61  VAL 61  213 ?   ?   ?   A . n 
A 1 62  THR 62  214 ?   ?   ?   A . n 
A 1 63  LEU 63  215 ?   ?   ?   A . n 
A 1 64  ASP 64  216 ?   ?   ?   A . n 
A 1 65  LEU 65  217 ?   ?   ?   A . n 
A 1 66  SER 66  218 218 SER SER A . n 
A 1 67  PRO 67  219 219 PRO PRO A . n 
A 1 68  LEU 68  220 220 LEU LEU A . n 
A 1 69  SER 69  221 221 SER SER A . n 
A 1 70  MET 70  222 222 MET MET A . n 
A 1 71  LEU 71  223 223 LEU LEU A . n 
A 1 72  PRO 72  224 224 PRO PRO A . n 
A 1 73  HIS 73  225 225 HIS HIS A . n 
A 1 74  LEU 74  226 226 LEU LEU A . n 
A 1 75  ALA 75  227 227 ALA ALA A . n 
A 1 76  ASP 76  228 228 ASP ASP A . n 
A 1 77  LEU 77  229 229 LEU LEU A . n 
A 1 78  VAL 78  230 230 VAL VAL A . n 
A 1 79  SER 79  231 231 SER SER A . n 
A 1 80  TYR 80  232 232 TYR TYR A . n 
A 1 81  SER 81  233 233 SER SER A . n 
A 1 82  ILE 82  234 234 ILE ILE A . n 
A 1 83  GLN 83  235 235 GLN GLN A . n 
A 1 84  LYS 84  236 236 LYS LYS A . n 
A 1 85  VAL 85  237 237 VAL VAL A . n 
A 1 86  ILE 86  238 238 ILE ILE A . n 
A 1 87  GLY 87  239 239 GLY GLY A . n 
A 1 88  PHE 88  240 240 PHE PHE A . n 
A 1 89  ALA 89  241 241 ALA ALA A . n 
A 1 90  LYS 90  242 242 LYS LYS A . n 
A 1 91  MET 91  243 243 MET MET A . n 
A 1 92  ILE 92  244 244 ILE ILE A . n 
A 1 93  PRO 93  245 245 PRO PRO A . n 
A 1 94  GLY 94  246 246 GLY GLY A . n 
A 1 95  PHE 95  247 247 PHE PHE A . n 
A 1 96  ARG 96  248 248 ARG ARG A . n 
A 1 97  ASP 97  249 249 ASP ASP A . n 
A 1 98  LEU 98  250 250 LEU LEU A . n 
A 1 99  THR 99  251 251 THR THR A . n 
A 1 100 SER 100 252 252 SER SER A . n 
A 1 101 ASP 101 253 253 ASP ASP A . n 
A 1 102 ASP 102 254 254 ASP ASP A . n 
A 1 103 GLN 103 255 255 GLN GLN A . n 
A 1 104 ILE 104 256 256 ILE ILE A . n 
A 1 105 VAL 105 257 257 VAL VAL A . n 
A 1 106 LEU 106 258 258 LEU LEU A . n 
A 1 107 LEU 107 259 259 LEU LEU A . n 
A 1 108 LYS 108 260 260 LYS LYS A . n 
A 1 109 SER 109 261 261 SER SER A . n 
A 1 110 SER 110 262 262 SER SER A . n 
A 1 111 ALA 111 263 263 ALA ALA A . n 
A 1 112 ILE 112 264 264 ILE ILE A . n 
A 1 113 GLU 113 265 265 GLU GLU A . n 
A 1 114 VAL 114 266 266 VAL VAL A . n 
A 1 115 ILE 115 267 267 ILE ILE A . n 
A 1 116 MET 116 268 268 MET MET A . n 
A 1 117 LEU 117 269 269 LEU LEU A . n 
A 1 118 ARG 118 270 270 ARG ARG A . n 
A 1 119 SER 119 271 271 SER SER A . n 
A 1 120 ASN 120 272 272 ASN ASN A . n 
A 1 121 GLN 121 273 273 GLN GLN A . n 
A 1 122 SER 122 274 274 SER SER A . n 
A 1 123 PHE 123 275 275 PHE PHE A . n 
A 1 124 THR 124 276 276 THR THR A . n 
A 1 125 MET 125 277 277 MET MET A . n 
A 1 126 ASP 126 278 278 ASP ASP A . n 
A 1 127 ASP 127 279 279 ASP ASP A . n 
A 1 128 MET 128 280 280 MET MET A . n 
A 1 129 SER 129 281 281 SER SER A . n 
A 1 130 TRP 130 282 282 TRP TRP A . n 
A 1 131 ASP 131 283 283 ASP ASP A . n 
A 1 132 CYS 132 284 284 CYS CYS A . n 
A 1 133 GLY 133 285 285 GLY GLY A . n 
A 1 134 SER 134 286 286 SER SER A . n 
A 1 135 GLN 135 287 287 GLN GLN A . n 
A 1 136 ASP 136 288 288 ASP ASP A . n 
A 1 137 TYR 137 289 289 TYR TYR A . n 
A 1 138 LYS 138 290 290 LYS LYS A . n 
A 1 139 TYR 139 291 291 TYR TYR A . n 
A 1 140 ASP 140 292 292 ASP ASP A . n 
A 1 141 VAL 141 293 293 VAL VAL A . n 
A 1 142 THR 142 294 294 THR THR A . n 
A 1 143 ASP 143 295 295 ASP ASP A . n 
A 1 144 VAL 144 296 296 VAL VAL A . n 
A 1 145 SER 145 297 297 SER SER A . n 
A 1 146 LYS 146 298 298 LYS LYS A . n 
A 1 147 ALA 147 299 299 ALA ALA A . n 
A 1 148 GLY 148 300 300 GLY GLY A . n 
A 1 149 HIS 149 301 301 HIS HIS A . n 
A 1 150 THR 150 302 302 THR THR A . n 
A 1 151 LEU 151 303 303 LEU LEU A . n 
A 1 152 GLU 152 304 304 GLU GLU A . n 
A 1 153 LEU 153 305 305 LEU LEU A . n 
A 1 154 ILE 154 306 306 ILE ILE A . n 
A 1 155 GLU 155 307 307 GLU GLU A . n 
A 1 156 PRO 156 308 308 PRO PRO A . n 
A 1 157 LEU 157 309 309 LEU LEU A . n 
A 1 158 ILE 158 310 310 ILE ILE A . n 
A 1 159 LYS 159 311 311 LYS LYS A . n 
A 1 160 PHE 160 312 312 PHE PHE A . n 
A 1 161 GLN 161 313 313 GLN GLN A . n 
A 1 162 VAL 162 314 314 VAL VAL A . n 
A 1 163 GLY 163 315 315 GLY GLY A . n 
A 1 164 LEU 164 316 316 LEU LEU A . n 
A 1 165 LYS 165 317 317 LYS LYS A . n 
A 1 166 LYS 166 318 318 LYS LYS A . n 
A 1 167 LEU 167 319 319 LEU LEU A . n 
A 1 168 ASN 168 320 320 ASN ASN A . n 
A 1 169 LEU 169 321 321 LEU LEU A . n 
A 1 170 HIS 170 322 322 HIS HIS A . n 
A 1 171 GLU 171 323 323 GLU GLU A . n 
A 1 172 GLU 172 324 324 GLU GLU A . n 
A 1 173 GLU 173 325 325 GLU GLU A . n 
A 1 174 HIS 174 326 326 HIS HIS A . n 
A 1 175 VAL 175 327 327 VAL VAL A . n 
A 1 176 LEU 176 328 328 LEU LEU A . n 
A 1 177 LEU 177 329 329 LEU LEU A . n 
A 1 178 MET 178 330 330 MET MET A . n 
A 1 179 ALA 179 331 331 ALA ALA A . n 
A 1 180 ILE 180 332 332 ILE ILE A . n 
A 1 181 CYS 181 333 333 CYS CYS A . n 
A 1 182 ILE 182 334 334 ILE ILE A . n 
A 1 183 VAL 183 335 335 VAL VAL A . n 
A 1 184 SER 184 336 336 SER SER A . n 
A 1 185 PRO 185 337 337 PRO PRO A . n 
A 1 186 ASP 186 338 338 ASP ASP A . n 
A 1 187 ARG 187 339 339 ARG ARG A . n 
A 1 188 PRO 188 340 340 PRO PRO A . n 
A 1 189 GLY 189 341 341 GLY GLY A . n 
A 1 190 VAL 190 342 342 VAL VAL A . n 
A 1 191 GLN 191 343 343 GLN GLN A . n 
A 1 192 ASP 192 344 344 ASP ASP A . n 
A 1 193 ALA 193 345 345 ALA ALA A . n 
A 1 194 LYS 194 346 346 LYS LYS A . n 
A 1 195 LEU 195 347 347 LEU LEU A . n 
A 1 196 VAL 196 348 348 VAL VAL A . n 
A 1 197 GLU 197 349 349 GLU GLU A . n 
A 1 198 ALA 198 350 350 ALA ALA A . n 
A 1 199 ILE 199 351 351 ILE ILE A . n 
A 1 200 GLN 200 352 352 GLN GLN A . n 
A 1 201 ASP 201 353 353 ASP ASP A . n 
A 1 202 ARG 202 354 354 ARG ARG A . n 
A 1 203 LEU 203 355 355 LEU LEU A . n 
A 1 204 SER 204 356 356 SER SER A . n 
A 1 205 ASN 205 357 357 ASN ASN A . n 
A 1 206 THR 206 358 358 THR THR A . n 
A 1 207 LEU 207 359 359 LEU LEU A . n 
A 1 208 GLN 208 360 360 GLN GLN A . n 
A 1 209 THR 209 361 361 THR THR A . n 
A 1 210 TYR 210 362 362 TYR TYR A . n 
A 1 211 ILE 211 363 363 ILE ILE A . n 
A 1 212 ARG 212 364 364 ARG ARG A . n 
A 1 213 CYS 213 365 365 CYS CYS A . n 
A 1 214 ARG 214 366 366 ARG ARG A . n 
A 1 215 HIS 215 367 367 HIS HIS A . n 
A 1 216 PRO 216 368 368 PRO PRO A . n 
A 1 217 PRO 217 369 369 PRO PRO A . n 
A 1 218 PRO 218 370 370 PRO PRO A . n 
A 1 219 GLY 219 371 371 GLY GLY A . n 
A 1 220 SER 220 372 372 SER SER A . n 
A 1 221 HIS 221 373 373 HIS HIS A . n 
A 1 222 GLN 222 374 374 GLN GLN A . n 
A 1 223 LEU 223 375 375 LEU LEU A . n 
A 1 224 TYR 224 376 376 TYR TYR A . n 
A 1 225 ALA 225 377 377 ALA ALA A . n 
A 1 226 LYS 226 378 378 LYS LYS A . n 
A 1 227 MET 227 379 379 MET MET A . n 
A 1 228 ILE 228 380 380 ILE ILE A . n 
A 1 229 GLN 229 381 381 GLN GLN A . n 
A 1 230 LYS 230 382 382 LYS LYS A . n 
A 1 231 LEU 231 383 383 LEU LEU A . n 
A 1 232 ALA 232 384 384 ALA ALA A . n 
A 1 233 ASP 233 385 385 ASP ASP A . n 
A 1 234 LEU 234 386 386 LEU LEU A . n 
A 1 235 ARG 235 387 387 ARG ARG A . n 
A 1 236 SER 236 388 388 SER SER A . n 
A 1 237 LEU 237 389 389 LEU LEU A . n 
A 1 238 ASN 238 390 390 ASN ASN A . n 
A 1 239 GLU 239 391 391 GLU GLU A . n 
A 1 240 GLU 240 392 392 GLU GLU A . n 
A 1 241 HIS 241 393 393 HIS HIS A . n 
A 1 242 SER 242 394 394 SER SER A . n 
A 1 243 LYS 243 395 395 LYS LYS A . n 
A 1 244 GLN 244 396 396 GLN GLN A . n 
A 1 245 TYR 245 397 397 TYR TYR A . n 
A 1 246 ARG 246 398 398 ARG ARG A . n 
A 1 247 SER 247 399 399 SER SER A . n 
A 1 248 LEU 248 400 400 LEU LEU A . n 
A 1 249 SER 249 401 401 SER SER A . n 
A 1 250 PHE 250 402 402 PHE PHE A . n 
A 1 251 GLN 251 403 403 GLN GLN A . n 
A 1 252 PRO 252 404 404 PRO PRO A . n 
A 1 253 GLU 253 405 405 GLU GLU A . n 
A 1 254 ASN 254 406 406 ASN ASN A . n 
A 1 255 SER 255 407 407 SER SER A . n 
A 1 256 MET 256 408 408 MET MET A . n 
A 1 257 LYS 257 409 409 LYS LYS A . n 
A 1 258 LEU 258 410 410 LEU LEU A . n 
A 1 259 THR 259 411 411 THR THR A . n 
A 1 260 PRO 260 412 412 PRO PRO A . n 
A 1 261 LEU 261 413 413 LEU LEU A . n 
A 1 262 VAL 262 414 414 VAL VAL A . n 
A 1 263 LEU 263 415 415 LEU LEU A . n 
A 1 264 GLU 264 416 416 GLU GLU A . n 
A 1 265 VAL 265 417 417 VAL VAL A . n 
A 1 266 PHE 266 418 418 PHE PHE A . n 
A 1 267 GLY 267 419 419 GLY GLY A . n 
A 1 268 ASN 268 420 420 ASN ASN A . n 
A 1 269 GLU 269 421 ?   ?   ?   A . n 
A 1 270 ILE 270 422 ?   ?   ?   A . n 
A 1 271 SER 271 423 ?   ?   ?   A . n 
B 2 1   LYS 1   625 625 LYS LYS C . n 
B 2 2   ASN 2   626 626 ASN ASN C . n 
B 2 3   HIS 3   627 627 HIS HIS C . n 
B 2 4   PRO 4   628 628 PRO PRO C . n 
B 2 5   MET 5   629 629 MET MET C . n 
B 2 6   LEU 6   630 630 LEU LEU C . n 
B 2 7   MET 7   631 631 MET MET C . n 
B 2 8   ASN 8   632 632 ASN ASN C . n 
B 2 9   LEU 9   633 633 LEU LEU C . n 
B 2 10  LEU 10  634 634 LEU LEU C . n 
B 2 11  LYS 11  635 635 LYS LYS C . n 
B 2 12  ASP 12  636 ?   ?   ?   C . n 
B 2 13  ASN 13  637 ?   ?   ?   C . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1L76 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1L76 
_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 
C 3 A1L76 1  501 501 A1L76 LIG A . 
D 4 HOH   1  601 8   HOH   HOH A . 
D 4 HOH   2  602 165 HOH   HOH A . 
D 4 HOH   3  603 58  HOH   HOH A . 
D 4 HOH   4  604 234 HOH   HOH A . 
D 4 HOH   5  605 245 HOH   HOH A . 
D 4 HOH   6  606 210 HOH   HOH A . 
D 4 HOH   7  607 251 HOH   HOH A . 
D 4 HOH   8  608 140 HOH   HOH A . 
D 4 HOH   9  609 20  HOH   HOH A . 
D 4 HOH   10 610 67  HOH   HOH A . 
D 4 HOH   11 611 227 HOH   HOH A . 
D 4 HOH   12 612 11  HOH   HOH A . 
D 4 HOH   13 613 236 HOH   HOH A . 
D 4 HOH   14 614 7   HOH   HOH A . 
D 4 HOH   15 615 5   HOH   HOH A . 
D 4 HOH   16 616 28  HOH   HOH A . 
D 4 HOH   17 617 64  HOH   HOH A . 
D 4 HOH   18 618 44  HOH   HOH A . 
D 4 HOH   19 619 242 HOH   HOH A . 
D 4 HOH   20 620 1   HOH   HOH A . 
D 4 HOH   21 621 4   HOH   HOH A . 
D 4 HOH   22 622 52  HOH   HOH A . 
D 4 HOH   23 623 2   HOH   HOH A . 
D 4 HOH   24 624 29  HOH   HOH A . 
D 4 HOH   25 625 88  HOH   HOH A . 
D 4 HOH   26 626 3   HOH   HOH A . 
D 4 HOH   27 627 10  HOH   HOH A . 
D 4 HOH   28 628 235 HOH   HOH A . 
D 4 HOH   29 629 132 HOH   HOH A . 
D 4 HOH   30 630 26  HOH   HOH A . 
D 4 HOH   31 631 13  HOH   HOH A . 
D 4 HOH   32 632 69  HOH   HOH A . 
D 4 HOH   33 633 24  HOH   HOH A . 
D 4 HOH   34 634 21  HOH   HOH A . 
D 4 HOH   35 635 12  HOH   HOH A . 
D 4 HOH   36 636 248 HOH   HOH A . 
D 4 HOH   37 637 139 HOH   HOH A . 
D 4 HOH   38 638 19  HOH   HOH A . 
D 4 HOH   39 639 114 HOH   HOH A . 
D 4 HOH   40 640 229 HOH   HOH A . 
D 4 HOH   41 641 105 HOH   HOH A . 
D 4 HOH   42 642 171 HOH   HOH A . 
D 4 HOH   43 643 25  HOH   HOH A . 
D 4 HOH   44 644 15  HOH   HOH A . 
D 4 HOH   45 645 6   HOH   HOH A . 
D 4 HOH   46 646 230 HOH   HOH A . 
D 4 HOH   47 647 45  HOH   HOH A . 
D 4 HOH   48 648 241 HOH   HOH A . 
D 4 HOH   49 649 65  HOH   HOH A . 
D 4 HOH   50 650 208 HOH   HOH A . 
D 4 HOH   51 651 226 HOH   HOH A . 
D 4 HOH   52 652 22  HOH   HOH A . 
D 4 HOH   53 653 61  HOH   HOH A . 
D 4 HOH   54 654 113 HOH   HOH A . 
D 4 HOH   55 655 246 HOH   HOH A . 
D 4 HOH   56 656 68  HOH   HOH A . 
D 4 HOH   57 657 253 HOH   HOH A . 
D 4 HOH   58 658 18  HOH   HOH A . 
D 4 HOH   59 659 233 HOH   HOH A . 
D 4 HOH   60 660 237 HOH   HOH A . 
D 4 HOH   61 661 228 HOH   HOH A . 
D 4 HOH   62 662 250 HOH   HOH A . 
D 4 HOH   63 663 185 HOH   HOH A . 
D 4 HOH   64 664 244 HOH   HOH A . 
D 4 HOH   65 665 177 HOH   HOH A . 
D 4 HOH   66 666 231 HOH   HOH A . 
D 4 HOH   67 667 238 HOH   HOH A . 
D 4 HOH   68 668 247 HOH   HOH A . 
D 4 HOH   69 669 252 HOH   HOH A . 
D 4 HOH   70 670 27  HOH   HOH A . 
D 4 HOH   71 671 39  HOH   HOH A . 
D 4 HOH   72 672 78  HOH   HOH A . 
D 4 HOH   73 673 83  HOH   HOH A . 
D 4 HOH   74 674 148 HOH   HOH A . 
D 4 HOH   75 675 217 HOH   HOH A . 
D 4 HOH   76 676 243 HOH   HOH A . 
D 4 HOH   77 677 254 HOH   HOH A . 
D 4 HOH   78 678 166 HOH   HOH A . 
D 4 HOH   79 679 232 HOH   HOH A . 
D 4 HOH   80 680 240 HOH   HOH A . 
D 4 HOH   81 681 131 HOH   HOH A . 
E 4 HOH   1  701 239 HOH   HOH C . 
E 4 HOH   2  702 17  HOH   HOH C . 
# 
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 ? ? ? 1.14_3260 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS    ? ? ? .         2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? XDS    ? ? ? .         3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHENIX ? ? ? .         4 
# 
_cell.angle_alpha                  90.000 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   95.380 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9M18 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     154.333 
_cell.length_a_esd                 ? 
_cell.length_b                     41.498 
_cell.length_b_esd                 ? 
_cell.length_c                     41.990 
_cell.length_c_esd                 ? 
_cell.volume                       267740.727 
_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                         9M18 
_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                   9M18 
_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             2.08 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          40.89 
_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              ? 
_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    'PEG 3350, Sodium phosphate dibasic dihydrate, pH 9.1' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            293 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS EIGER X 4M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2023-07-21 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   1.0 
_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                        'SPRING-8 BEAMLINE BL26B1' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        1.0 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   BL26B1 
_diffrn_source.pdbx_synchrotron_site       SPring-8 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9M18 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.96 
_reflns.d_resolution_low                               41.81 
_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                                     19186 
_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                           99.42 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                3.3 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          10.3 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                ? 
_reflns.pdbx_Rpim_I_all                                ? 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.995 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.066 
_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                                    1.96 
_reflns_shell.d_res_low                                     2.03 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           0.8 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             1881 
_reflns_shell.percent_possible_obs                          98.22 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               3.36 
_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                                  0.644 
_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                                  1.25 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               53.64 
_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                                 9M18 
_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                            1.96 
_refine.ls_d_res_low                             41.81 
_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                     19124 
_refine.ls_number_reflns_R_free                  959 
_refine.ls_number_reflns_R_work                  18165 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.10 
_refine.ls_percent_reflns_R_free                 5.01 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2074 
_refine.ls_R_factor_R_free                       0.2357 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2060 
_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.correlation_coeff_I_to_Fcsqd_work        ? 
_refine.correlation_coeff_I_to_Fcsqd_free        ? 
_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                          1.34 
_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                      2ZLC 
_refine.pdbx_stereochemistry_target_values       '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             1.1100 
_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                 31.9952 
_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                            0.3001 
_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                       1.96 
_refine_hist.d_res_low                        41.81 
_refine_hist.number_atoms_solvent             83 
_refine_hist.number_atoms_total               2136 
_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        2015 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         38 
_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' ? 0.0053  ? 2203 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.7654  ? 2986 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 0.0389  ? 324  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.0037  ? 379  ? f_plane_restr      ? ? 
'X-RAY DIFFRACTION' ? 21.6004 ? 854  ? 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.correlation_coeff_Fo_to_Fc 
_refine_ls_shell.correlation_coeff_Fo_to_Fc_free 
_refine_ls_shell.correlation_coeff_I_to_Fcsqd_work 
_refine_ls_shell.correlation_coeff_I_to_Fcsqd_free 
_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' 1.96 2.06  . . 134 2543 98.09 . . . . 0.3887 . . . . . . . . . . . . . . . 0.4258 
'X-RAY DIFFRACTION' 2.06 2.19  . . 137 2587 99.34 . . . . 0.3157 . . . . . . . . . . . . . . . 0.3461 
'X-RAY DIFFRACTION' 2.19 2.36  . . 136 2577 99.49 . . . . 0.2792 . . . . . . . . . . . . . . . 0.3187 
'X-RAY DIFFRACTION' 2.36 2.60  . . 137 2603 99.38 . . . . 0.2372 . . . . . . . . . . . . . . . 0.2598 
'X-RAY DIFFRACTION' 2.60 2.98  . . 137 2587 99.27 . . . . 0.2200 . . . . . . . . . . . . . . . 0.2696 
'X-RAY DIFFRACTION' 2.98 3.75  . . 138 2605 99.35 . . . . 0.1953 . . . . . . . . . . . . . . . 0.2087 
'X-RAY DIFFRACTION' 3.75 41.81 . . 140 2663 98.84 . . . . 0.1562 . . . . . . . . . . . . . . . 0.1845 
# 
_struct.entry_id                     9M18 
_struct.title                        'Vitamin D receptor complex with a diallyldiphenylsilane derivative' 
_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        9M18 
_struct_keywords.text            'Vitamin D receptor, TRANSCRIPTION' 
_struct_keywords.pdbx_keywords   TRANSCRIPTION 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
D N N 4 ? 
E N N 4 ? 
# 
loop_
_struct_ref.id 
_struct_ref.db_name 
_struct_ref.db_code 
_struct_ref.pdbx_db_accession 
_struct_ref.pdbx_db_isoform 
_struct_ref.entity_id 
_struct_ref.pdbx_seq_one_letter_code 
_struct_ref.pdbx_align_begin 
1 UNP VDR_RAT    P13053 ? 1 
;LKDSLRPKLSEEQQHIIAILLDAHHKTYDPTYADFRDFRPPVRMDGSTGSYSPRPTLSFSGNSSSSSSDLYTTSLDMMEP
SGFSNLDLNGEDSDDPSVTLDLSPLSMLPHLADLVSYSIQKVIGFAKMIPGFRDLTSDDQIVLLKSSAIEVIMLRSNQSF
TMDDMSWDCGSQDYKYDVTDVSKAGHTLELIEPLIKFQVGLKKLNLHEEEHVLLMAICIVSPDRPGVQDAKLVEAIQDRL
SNTLQTYIRCRHPPPGSHQLYAKMIQKLADLRSLNEEHSKQYRSLSFQPENSMKLTPLVLEVFGNEIS
;
116 
2 UNP MED1_HUMAN Q15648 ? 2 KNHPMLMNLLKDN 640 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 9M18 A 11 ? 271 ? P13053 116 ? 423 ? 116 423 
2 2 9M18 C 1  ? 13  ? Q15648 640 ? 652 ? 625 637 
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
1 9M18 GLY A 1  ? UNP P13053 ?   ?   'expression tag' 106 1  
1 9M18 SER A 2  ? UNP P13053 ?   ?   'expression tag' 107 2  
1 9M18 HIS A 3  ? UNP P13053 ?   ?   'expression tag' 108 3  
1 9M18 MET A 4  ? UNP P13053 ?   ?   'expression tag' 109 4  
1 9M18 GLY A 5  ? UNP P13053 ?   ?   'expression tag' 110 5  
1 9M18 SER A 6  ? UNP P13053 ?   ?   'expression tag' 111 6  
1 9M18 PRO A 7  ? UNP P13053 ?   ?   'expression tag' 112 7  
1 9M18 ASN A 8  ? UNP P13053 ?   ?   'expression tag' 113 8  
1 9M18 SER A 9  ? UNP P13053 ?   ?   'expression tag' 114 9  
1 9M18 PRO A 10 ? UNP P13053 ?   ?   'expression tag' 115 10 
1 9M18 ?   A ?  ? UNP P13053 TYR 166 deletion         ?   11 
1 9M18 ?   A ?  ? UNP P13053 SER 167 deletion         ?   12 
1 9M18 ?   A ?  ? UNP P13053 PRO 168 deletion         ?   13 
1 9M18 ?   A ?  ? UNP P13053 ARG 169 deletion         ?   14 
1 9M18 ?   A ?  ? UNP P13053 PRO 170 deletion         ?   15 
1 9M18 ?   A ?  ? UNP P13053 THR 171 deletion         ?   16 
1 9M18 ?   A ?  ? UNP P13053 LEU 172 deletion         ?   17 
1 9M18 ?   A ?  ? UNP P13053 SER 173 deletion         ?   18 
1 9M18 ?   A ?  ? UNP P13053 PHE 174 deletion         ?   19 
1 9M18 ?   A ?  ? UNP P13053 SER 175 deletion         ?   20 
1 9M18 ?   A ?  ? UNP P13053 GLY 176 deletion         ?   21 
1 9M18 ?   A ?  ? UNP P13053 ASN 177 deletion         ?   22 
1 9M18 ?   A ?  ? UNP P13053 SER 178 deletion         ?   23 
1 9M18 ?   A ?  ? UNP P13053 SER 179 deletion         ?   24 
1 9M18 ?   A ?  ? UNP P13053 SER 180 deletion         ?   25 
1 9M18 ?   A ?  ? UNP P13053 SER 181 deletion         ?   26 
1 9M18 ?   A ?  ? UNP P13053 SER 182 deletion         ?   27 
1 9M18 ?   A ?  ? UNP P13053 SER 183 deletion         ?   28 
1 9M18 ?   A ?  ? UNP P13053 ASP 184 deletion         ?   29 
1 9M18 ?   A ?  ? UNP P13053 LEU 185 deletion         ?   30 
1 9M18 ?   A ?  ? UNP P13053 TYR 186 deletion         ?   31 
1 9M18 ?   A ?  ? UNP P13053 THR 187 deletion         ?   32 
1 9M18 ?   A ?  ? UNP P13053 THR 188 deletion         ?   33 
1 9M18 ?   A ?  ? UNP P13053 SER 189 deletion         ?   34 
1 9M18 ?   A ?  ? UNP P13053 LEU 190 deletion         ?   35 
1 9M18 ?   A ?  ? UNP P13053 ASP 191 deletion         ?   36 
1 9M18 ?   A ?  ? UNP P13053 MET 192 deletion         ?   37 
1 9M18 ?   A ?  ? UNP P13053 MET 193 deletion         ?   38 
1 9M18 ?   A ?  ? UNP P13053 GLU 194 deletion         ?   39 
1 9M18 ?   A ?  ? UNP P13053 PRO 195 deletion         ?   40 
1 9M18 ?   A ?  ? UNP P13053 SER 196 deletion         ?   41 
1 9M18 ?   A ?  ? UNP P13053 GLY 197 deletion         ?   42 
1 9M18 ?   A ?  ? UNP P13053 PHE 198 deletion         ?   43 
1 9M18 ?   A ?  ? UNP P13053 SER 199 deletion         ?   44 
1 9M18 ?   A ?  ? UNP P13053 ASN 200 deletion         ?   45 
1 9M18 ?   A ?  ? UNP P13053 LEU 201 deletion         ?   46 
1 9M18 ?   A ?  ? UNP P13053 ASP 202 deletion         ?   47 
1 9M18 ?   A ?  ? UNP P13053 LEU 203 deletion         ?   48 
1 9M18 ?   A ?  ? UNP P13053 ASN 204 deletion         ?   49 
1 9M18 ?   A ?  ? UNP P13053 GLY 205 deletion         ?   50 
1 9M18 ?   A ?  ? UNP P13053 GLU 206 deletion         ?   51 
1 9M18 ?   A ?  ? UNP P13053 ASP 207 deletion         ?   52 
1 9M18 ?   A ?  ? UNP P13053 SER 208 deletion         ?   53 
1 9M18 ?   A ?  ? UNP P13053 ASP 209 deletion         ?   54 
1 9M18 ?   A ?  ? UNP P13053 ASP 210 deletion         ?   55 
1 9M18 ?   A ?  ? UNP P13053 PRO 211 deletion         ?   56 
1 9M18 ?   A ?  ? UNP P13053 SER 212 deletion         ?   57 
# 
_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)' 1030  ? 
1 MORE         -9    ? 
1 'SSA (A^2)'  11940 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'gel filtration' 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 SER A 20  ? TYR A 38  ? SER A 125 TYR A 143 1 ? 19 
HELX_P HELX_P2  AA2 TYR A 42  ? PHE A 48  ? TYR A 147 PHE A 153 5 ? 7  
HELX_P HELX_P3  AA3 MET A 70  ? MET A 91  ? MET A 222 MET A 243 1 ? 22 
HELX_P HELX_P4  AA4 GLY A 94  ? LEU A 98  ? GLY A 246 LEU A 250 5 ? 5  
HELX_P HELX_P5  AA5 THR A 99  ? ASN A 120 ? THR A 251 ASN A 272 1 ? 22 
HELX_P HELX_P6  AA6 ASP A 140 ? LYS A 146 ? ASP A 292 LYS A 298 1 ? 7  
HELX_P HELX_P7  AA7 THR A 150 ? ASN A 168 ? THR A 302 ASN A 320 1 ? 19 
HELX_P HELX_P8  AA8 HIS A 170 ? VAL A 183 ? HIS A 322 VAL A 335 1 ? 14 
HELX_P HELX_P9  AA9 ASP A 192 ? HIS A 215 ? ASP A 344 HIS A 367 1 ? 24 
HELX_P HELX_P10 AB1 GLN A 222 ? GLN A 251 ? GLN A 374 GLN A 403 1 ? 30 
HELX_P HELX_P11 AB2 GLN A 251 ? MET A 256 ? GLN A 403 MET A 408 1 ? 6  
HELX_P HELX_P12 AB3 THR A 259 ? GLY A 267 ? THR A 411 GLY A 419 1 ? 9  
HELX_P HELX_P13 AB4 HIS B 3   ? LEU B 10  ? HIS C 627 LEU C 634 1 ? 8  
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
_struct_mon_prot_cis.pdbx_id                1 
_struct_mon_prot_cis.label_comp_id          PRO 
_struct_mon_prot_cis.label_seq_id           217 
_struct_mon_prot_cis.label_asym_id          A 
_struct_mon_prot_cis.label_alt_id           . 
_struct_mon_prot_cis.pdbx_PDB_ins_code      ? 
_struct_mon_prot_cis.auth_comp_id           PRO 
_struct_mon_prot_cis.auth_seq_id            369 
_struct_mon_prot_cis.auth_asym_id           A 
_struct_mon_prot_cis.pdbx_label_comp_id_2   PRO 
_struct_mon_prot_cis.pdbx_label_seq_id_2    218 
_struct_mon_prot_cis.pdbx_label_asym_id_2   A 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2    ? 
_struct_mon_prot_cis.pdbx_auth_comp_id_2    PRO 
_struct_mon_prot_cis.pdbx_auth_seq_id_2     370 
_struct_mon_prot_cis.pdbx_auth_asym_id_2    A 
_struct_mon_prot_cis.pdbx_PDB_model_num     1 
_struct_mon_prot_cis.pdbx_omega_angle       2.54 
# 
_struct_sheet.id               AA1 
_struct_sheet.type             ? 
_struct_sheet.number_strands   3 
_struct_sheet.details          ? 
# 
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 
# 
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 PHE A 123 ? THR A 124 ? PHE A 275 THR A 276 
AA1 2 SER A 129 ? ASP A 131 ? SER A 281 ASP A 283 
AA1 3 LYS A 138 ? TYR A 139 ? LYS A 290 TYR A 291 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N THR A 124 ? N THR A 276 O SER A 129 ? O SER A 281 
AA1 2 3 N TRP A 130 ? N TRP A 282 O TYR A 139 ? O TYR A 291 
# 
_pdbx_entry_details.entry_id                   9M18 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 CYS A 284 ? ? -107.93 43.06 
2 1 TYR A 289 ? ? -108.25 40.07 
3 1 HIS C 627 ? ? -117.73 69.40 
# 
loop_
_pdbx_refine_tls.id 
_pdbx_refine_tls.pdbx_refine_id 
_pdbx_refine_tls.details 
_pdbx_refine_tls.method 
_pdbx_refine_tls.origin_x 
_pdbx_refine_tls.origin_y 
_pdbx_refine_tls.origin_z 
_pdbx_refine_tls.T[1][1] 
_pdbx_refine_tls.T[1][1]_esd 
_pdbx_refine_tls.T[1][2] 
_pdbx_refine_tls.T[1][2]_esd 
_pdbx_refine_tls.T[1][3] 
_pdbx_refine_tls.T[1][3]_esd 
_pdbx_refine_tls.T[2][2] 
_pdbx_refine_tls.T[2][2]_esd 
_pdbx_refine_tls.T[2][3] 
_pdbx_refine_tls.T[2][3]_esd 
_pdbx_refine_tls.T[3][3] 
_pdbx_refine_tls.T[3][3]_esd 
_pdbx_refine_tls.L[1][1] 
_pdbx_refine_tls.L[1][1]_esd 
_pdbx_refine_tls.L[1][2] 
_pdbx_refine_tls.L[1][2]_esd 
_pdbx_refine_tls.L[1][3] 
_pdbx_refine_tls.L[1][3]_esd 
_pdbx_refine_tls.L[2][2] 
_pdbx_refine_tls.L[2][2]_esd 
_pdbx_refine_tls.L[2][3] 
_pdbx_refine_tls.L[2][3]_esd 
_pdbx_refine_tls.L[3][3] 
_pdbx_refine_tls.L[3][3]_esd 
_pdbx_refine_tls.S[1][1] 
_pdbx_refine_tls.S[1][1]_esd 
_pdbx_refine_tls.S[1][2] 
_pdbx_refine_tls.S[1][2]_esd 
_pdbx_refine_tls.S[1][3] 
_pdbx_refine_tls.S[1][3]_esd 
_pdbx_refine_tls.S[2][1] 
_pdbx_refine_tls.S[2][1]_esd 
_pdbx_refine_tls.S[2][2] 
_pdbx_refine_tls.S[2][2]_esd 
_pdbx_refine_tls.S[2][3] 
_pdbx_refine_tls.S[2][3]_esd 
_pdbx_refine_tls.S[3][1] 
_pdbx_refine_tls.S[3][1]_esd 
_pdbx_refine_tls.S[3][2] 
_pdbx_refine_tls.S[3][2]_esd 
_pdbx_refine_tls.S[3][3] 
_pdbx_refine_tls.S[3][3]_esd 
1 'X-RAY DIFFRACTION' ? refined 19.0708299475 0.449372311614 19.219892277  0.29250656773 ? -0.0555721596672 ? -0.0352849719382 ? 
0.377895569099 ? 0.0353922087293  ? 0.265837244995 ? 3.509230992   ? 0.430742373455 ? 0.46394743417 ? 1.44639798703 ? 
0.0118052355491 ? 2.40275707724 ? -0.0666406128838 ? -0.174797392469  ? -0.00041676166088 ? 0.0648912686812 ? -0.0142914094157 ? 
-0.0430795718744 ? -0.218460971628 ? -0.00298134314863 ? 0.0835154684355 ? 
2 'X-RAY DIFFRACTION' ? refined 5.63723062378 -10.6569781566 10.4508767253 0.48750481998 ? -0.110846874395  ? -0.0451329384713 ? 
0.995492091484 ? -0.0606444956913 ? 0.664849669345 ? 7.86496289135 ? -2.21964012857 ? 2.10097788609 ? 3.17094730524 ? 
0.659886375097  ? 7.07532916461 ? 0.00107526969318 ? -0.0540612763657 ? -1.02205684352    ? -0.322734418675 ? -0.0133225107916 ? 
0.290609063693   ? 0.812006618692  ? -0.707413011461   ? 0.0279256348395 ? 
# 
loop_
_pdbx_refine_tls_group.id 
_pdbx_refine_tls_group.pdbx_refine_id 
_pdbx_refine_tls_group.refine_tls_id 
_pdbx_refine_tls_group.beg_label_asym_id 
_pdbx_refine_tls_group.beg_label_seq_id 
_pdbx_refine_tls_group.beg_auth_asym_id 
_pdbx_refine_tls_group.beg_auth_seq_id 
_pdbx_refine_tls_group.beg_PDB_ins_code 
_pdbx_refine_tls_group.end_label_asym_id 
_pdbx_refine_tls_group.end_label_seq_id 
_pdbx_refine_tls_group.end_auth_asym_id 
_pdbx_refine_tls_group.end_auth_seq_id 
_pdbx_refine_tls_group.end_PDB_ins_code 
_pdbx_refine_tls_group.selection 
_pdbx_refine_tls_group.selection_details 
1 'X-RAY DIFFRACTION' 1 ? ? ? ? ? ? ? ? ? ? ? 'Chain A' 
2 'X-RAY DIFFRACTION' 2 ? ? ? ? ? ? ? ? ? ? ? 'Chain C' 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A GLY 106 ? A GLY 1   
2  1 Y 1 A SER 107 ? A SER 2   
3  1 Y 1 A HIS 108 ? A HIS 3   
4  1 Y 1 A MET 109 ? A MET 4   
5  1 Y 1 A GLY 110 ? A GLY 5   
6  1 Y 1 A SER 111 ? A SER 6   
7  1 Y 1 A PRO 112 ? A PRO 7   
8  1 Y 1 A ASN 113 ? A ASN 8   
9  1 Y 1 A SER 114 ? A SER 9   
10 1 Y 1 A PRO 115 ? A PRO 10  
11 1 Y 1 A LEU 116 ? A LEU 11  
12 1 Y 1 A LYS 117 ? A LYS 12  
13 1 Y 1 A ASP 118 ? A ASP 13  
14 1 Y 1 A SER 119 ? A SER 14  
15 1 Y 1 A LEU 120 ? A LEU 15  
16 1 Y 1 A ARG 121 ? A ARG 16  
17 1 Y 1 A PRO 122 ? A PRO 17  
18 1 Y 1 A ASP 207 ? A ASP 55  
19 1 Y 1 A GLY 208 ? A GLY 56  
20 1 Y 1 A SER 209 ? A SER 57  
21 1 Y 1 A THR 210 ? A THR 58  
22 1 Y 1 A GLY 211 ? A GLY 59  
23 1 Y 1 A SER 212 ? A SER 60  
24 1 Y 1 A VAL 213 ? A VAL 61  
25 1 Y 1 A THR 214 ? A THR 62  
26 1 Y 1 A LEU 215 ? A LEU 63  
27 1 Y 1 A ASP 216 ? A ASP 64  
28 1 Y 1 A LEU 217 ? A LEU 65  
29 1 Y 1 A GLU 421 ? A GLU 269 
30 1 Y 1 A ILE 422 ? A ILE 270 
31 1 Y 1 A SER 423 ? A SER 271 
32 1 Y 1 C ASP 636 ? B ASP 12  
33 1 Y 1 C ASN 637 ? B ASN 13  
# 
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 
A1L76 C10  C  N N 1   
A1L76 C13  C  Y N 2   
A1L76 C15  C  Y N 3   
A1L76 C20  C  N N 4   
A1L76 C21  C  N N 5   
A1L76 C22  C  N N 6   
A1L76 C26  C  N S 7   
A1L76 C28  C  N N 8   
A1L76 C01  C  Y N 9   
A1L76 C02  C  Y N 10  
A1L76 C03  C  Y N 11  
A1L76 C04  C  Y N 12  
A1L76 C05  C  Y N 13  
A1L76 C06  C  Y N 14  
A1L76 C09  C  Y N 15  
A1L76 C11  C  N N 16  
A1L76 C12  C  Y N 17  
A1L76 C14  C  Y N 18  
A1L76 C16  C  Y N 19  
A1L76 C18  C  N N 20  
A1L76 C19  C  N N 21  
A1L76 C23  C  N N 22  
A1L76 C25  C  N N 23  
A1L76 C29  C  N N 24  
A1L76 C30  C  N N 25  
A1L76 C33  C  N N 26  
A1L76 C34  C  N N 27  
A1L76 C35  C  N N 28  
A1L76 C36  C  N N 29  
A1L76 C37  C  N N 30  
A1L76 C38  C  N N 31  
A1L76 O07  O  N N 32  
A1L76 O17  O  N N 33  
A1L76 O24  O  N N 34  
A1L76 O27  O  N N 35  
A1L76 O31  O  N N 36  
A1L76 O32  O  N N 37  
A1L76 SI08 SI N N 38  
A1L76 H102 H  N N 39  
A1L76 H101 H  N N 40  
A1L76 H151 H  N N 41  
A1L76 H202 H  N N 42  
A1L76 H201 H  N N 43  
A1L76 H213 H  N N 44  
A1L76 H211 H  N N 45  
A1L76 H212 H  N N 46  
A1L76 H221 H  N N 47  
A1L76 H222 H  N N 48  
A1L76 H261 H  N N 49  
A1L76 H282 H  N N 50  
A1L76 H281 H  N N 51  
A1L76 H011 H  N N 52  
A1L76 H041 H  N N 53  
A1L76 H061 H  N N 54  
A1L76 H111 H  N N 55  
A1L76 H112 H  N N 56  
A1L76 H121 H  N N 57  
A1L76 H161 H  N N 58  
A1L76 H181 H  N N 59  
A1L76 H182 H  N N 60  
A1L76 H231 H  N N 61  
A1L76 H232 H  N N 62  
A1L76 H233 H  N N 63  
A1L76 H251 H  N N 64  
A1L76 H252 H  N N 65  
A1L76 H292 H  N N 66  
A1L76 H291 H  N N 67  
A1L76 H331 H  N N 68  
A1L76 H332 H  N N 69  
A1L76 H333 H  N N 70  
A1L76 H342 H  N N 71  
A1L76 H341 H  N N 72  
A1L76 H343 H  N N 73  
A1L76 H351 H  N N 74  
A1L76 H361 H  N N 75  
A1L76 H362 H  N N 76  
A1L76 H371 H  N N 77  
A1L76 H382 H  N N 78  
A1L76 H381 H  N N 79  
A1L76 H241 H  N N 80  
A1L76 H271 H  N N 81  
A1L76 H1   H  N N 82  
ALA   N    N  N N 83  
ALA   CA   C  N S 84  
ALA   C    C  N N 85  
ALA   O    O  N N 86  
ALA   CB   C  N N 87  
ALA   OXT  O  N N 88  
ALA   H    H  N N 89  
ALA   H2   H  N N 90  
ALA   HA   H  N N 91  
ALA   HB1  H  N N 92  
ALA   HB2  H  N N 93  
ALA   HB3  H  N N 94  
ALA   HXT  H  N N 95  
ARG   N    N  N N 96  
ARG   CA   C  N S 97  
ARG   C    C  N N 98  
ARG   O    O  N N 99  
ARG   CB   C  N N 100 
ARG   CG   C  N N 101 
ARG   CD   C  N N 102 
ARG   NE   N  N N 103 
ARG   CZ   C  N N 104 
ARG   NH1  N  N N 105 
ARG   NH2  N  N N 106 
ARG   OXT  O  N N 107 
ARG   H    H  N N 108 
ARG   H2   H  N N 109 
ARG   HA   H  N N 110 
ARG   HB2  H  N N 111 
ARG   HB3  H  N N 112 
ARG   HG2  H  N N 113 
ARG   HG3  H  N N 114 
ARG   HD2  H  N N 115 
ARG   HD3  H  N N 116 
ARG   HE   H  N N 117 
ARG   HH11 H  N N 118 
ARG   HH12 H  N N 119 
ARG   HH21 H  N N 120 
ARG   HH22 H  N N 121 
ARG   HXT  H  N N 122 
ASN   N    N  N N 123 
ASN   CA   C  N S 124 
ASN   C    C  N N 125 
ASN   O    O  N N 126 
ASN   CB   C  N N 127 
ASN   CG   C  N N 128 
ASN   OD1  O  N N 129 
ASN   ND2  N  N N 130 
ASN   OXT  O  N N 131 
ASN   H    H  N N 132 
ASN   H2   H  N N 133 
ASN   HA   H  N N 134 
ASN   HB2  H  N N 135 
ASN   HB3  H  N N 136 
ASN   HD21 H  N N 137 
ASN   HD22 H  N N 138 
ASN   HXT  H  N N 139 
ASP   N    N  N N 140 
ASP   CA   C  N S 141 
ASP   C    C  N N 142 
ASP   O    O  N N 143 
ASP   CB   C  N N 144 
ASP   CG   C  N N 145 
ASP   OD1  O  N N 146 
ASP   OD2  O  N N 147 
ASP   OXT  O  N N 148 
ASP   H    H  N N 149 
ASP   H2   H  N N 150 
ASP   HA   H  N N 151 
ASP   HB2  H  N N 152 
ASP   HB3  H  N N 153 
ASP   HD2  H  N N 154 
ASP   HXT  H  N N 155 
CYS   N    N  N N 156 
CYS   CA   C  N R 157 
CYS   C    C  N N 158 
CYS   O    O  N N 159 
CYS   CB   C  N N 160 
CYS   SG   S  N N 161 
CYS   OXT  O  N N 162 
CYS   H    H  N N 163 
CYS   H2   H  N N 164 
CYS   HA   H  N N 165 
CYS   HB2  H  N N 166 
CYS   HB3  H  N N 167 
CYS   HG   H  N N 168 
CYS   HXT  H  N N 169 
GLN   N    N  N N 170 
GLN   CA   C  N S 171 
GLN   C    C  N N 172 
GLN   O    O  N N 173 
GLN   CB   C  N N 174 
GLN   CG   C  N N 175 
GLN   CD   C  N N 176 
GLN   OE1  O  N N 177 
GLN   NE2  N  N N 178 
GLN   OXT  O  N N 179 
GLN   H    H  N N 180 
GLN   H2   H  N N 181 
GLN   HA   H  N N 182 
GLN   HB2  H  N N 183 
GLN   HB3  H  N N 184 
GLN   HG2  H  N N 185 
GLN   HG3  H  N N 186 
GLN   HE21 H  N N 187 
GLN   HE22 H  N N 188 
GLN   HXT  H  N N 189 
GLU   N    N  N N 190 
GLU   CA   C  N S 191 
GLU   C    C  N N 192 
GLU   O    O  N N 193 
GLU   CB   C  N N 194 
GLU   CG   C  N N 195 
GLU   CD   C  N N 196 
GLU   OE1  O  N N 197 
GLU   OE2  O  N N 198 
GLU   OXT  O  N N 199 
GLU   H    H  N N 200 
GLU   H2   H  N N 201 
GLU   HA   H  N N 202 
GLU   HB2  H  N N 203 
GLU   HB3  H  N N 204 
GLU   HG2  H  N N 205 
GLU   HG3  H  N N 206 
GLU   HE2  H  N N 207 
GLU   HXT  H  N N 208 
GLY   N    N  N N 209 
GLY   CA   C  N N 210 
GLY   C    C  N N 211 
GLY   O    O  N N 212 
GLY   OXT  O  N N 213 
GLY   H    H  N N 214 
GLY   H2   H  N N 215 
GLY   HA2  H  N N 216 
GLY   HA3  H  N N 217 
GLY   HXT  H  N N 218 
HIS   N    N  N N 219 
HIS   CA   C  N S 220 
HIS   C    C  N N 221 
HIS   O    O  N N 222 
HIS   CB   C  N N 223 
HIS   CG   C  Y N 224 
HIS   ND1  N  Y N 225 
HIS   CD2  C  Y N 226 
HIS   CE1  C  Y N 227 
HIS   NE2  N  Y N 228 
HIS   OXT  O  N N 229 
HIS   H    H  N N 230 
HIS   H2   H  N N 231 
HIS   HA   H  N N 232 
HIS   HB2  H  N N 233 
HIS   HB3  H  N N 234 
HIS   HD1  H  N N 235 
HIS   HD2  H  N N 236 
HIS   HE1  H  N N 237 
HIS   HE2  H  N N 238 
HIS   HXT  H  N N 239 
HOH   O    O  N N 240 
HOH   H1   H  N N 241 
HOH   H2   H  N N 242 
ILE   N    N  N N 243 
ILE   CA   C  N S 244 
ILE   C    C  N N 245 
ILE   O    O  N N 246 
ILE   CB   C  N S 247 
ILE   CG1  C  N N 248 
ILE   CG2  C  N N 249 
ILE   CD1  C  N N 250 
ILE   OXT  O  N N 251 
ILE   H    H  N N 252 
ILE   H2   H  N N 253 
ILE   HA   H  N N 254 
ILE   HB   H  N N 255 
ILE   HG12 H  N N 256 
ILE   HG13 H  N N 257 
ILE   HG21 H  N N 258 
ILE   HG22 H  N N 259 
ILE   HG23 H  N N 260 
ILE   HD11 H  N N 261 
ILE   HD12 H  N N 262 
ILE   HD13 H  N N 263 
ILE   HXT  H  N N 264 
LEU   N    N  N N 265 
LEU   CA   C  N S 266 
LEU   C    C  N N 267 
LEU   O    O  N N 268 
LEU   CB   C  N N 269 
LEU   CG   C  N N 270 
LEU   CD1  C  N N 271 
LEU   CD2  C  N N 272 
LEU   OXT  O  N N 273 
LEU   H    H  N N 274 
LEU   H2   H  N N 275 
LEU   HA   H  N N 276 
LEU   HB2  H  N N 277 
LEU   HB3  H  N N 278 
LEU   HG   H  N N 279 
LEU   HD11 H  N N 280 
LEU   HD12 H  N N 281 
LEU   HD13 H  N N 282 
LEU   HD21 H  N N 283 
LEU   HD22 H  N N 284 
LEU   HD23 H  N N 285 
LEU   HXT  H  N N 286 
LYS   N    N  N N 287 
LYS   CA   C  N S 288 
LYS   C    C  N N 289 
LYS   O    O  N N 290 
LYS   CB   C  N N 291 
LYS   CG   C  N N 292 
LYS   CD   C  N N 293 
LYS   CE   C  N N 294 
LYS   NZ   N  N N 295 
LYS   OXT  O  N N 296 
LYS   H    H  N N 297 
LYS   H2   H  N N 298 
LYS   HA   H  N N 299 
LYS   HB2  H  N N 300 
LYS   HB3  H  N N 301 
LYS   HG2  H  N N 302 
LYS   HG3  H  N N 303 
LYS   HD2  H  N N 304 
LYS   HD3  H  N N 305 
LYS   HE2  H  N N 306 
LYS   HE3  H  N N 307 
LYS   HZ1  H  N N 308 
LYS   HZ2  H  N N 309 
LYS   HZ3  H  N N 310 
LYS   HXT  H  N N 311 
MET   N    N  N N 312 
MET   CA   C  N S 313 
MET   C    C  N N 314 
MET   O    O  N N 315 
MET   CB   C  N N 316 
MET   CG   C  N N 317 
MET   SD   S  N N 318 
MET   CE   C  N N 319 
MET   OXT  O  N N 320 
MET   H    H  N N 321 
MET   H2   H  N N 322 
MET   HA   H  N N 323 
MET   HB2  H  N N 324 
MET   HB3  H  N N 325 
MET   HG2  H  N N 326 
MET   HG3  H  N N 327 
MET   HE1  H  N N 328 
MET   HE2  H  N N 329 
MET   HE3  H  N N 330 
MET   HXT  H  N N 331 
PHE   N    N  N N 332 
PHE   CA   C  N S 333 
PHE   C    C  N N 334 
PHE   O    O  N N 335 
PHE   CB   C  N N 336 
PHE   CG   C  Y N 337 
PHE   CD1  C  Y N 338 
PHE   CD2  C  Y N 339 
PHE   CE1  C  Y N 340 
PHE   CE2  C  Y N 341 
PHE   CZ   C  Y N 342 
PHE   OXT  O  N N 343 
PHE   H    H  N N 344 
PHE   H2   H  N N 345 
PHE   HA   H  N N 346 
PHE   HB2  H  N N 347 
PHE   HB3  H  N N 348 
PHE   HD1  H  N N 349 
PHE   HD2  H  N N 350 
PHE   HE1  H  N N 351 
PHE   HE2  H  N N 352 
PHE   HZ   H  N N 353 
PHE   HXT  H  N N 354 
PRO   N    N  N N 355 
PRO   CA   C  N S 356 
PRO   C    C  N N 357 
PRO   O    O  N N 358 
PRO   CB   C  N N 359 
PRO   CG   C  N N 360 
PRO   CD   C  N N 361 
PRO   OXT  O  N N 362 
PRO   H    H  N N 363 
PRO   HA   H  N N 364 
PRO   HB2  H  N N 365 
PRO   HB3  H  N N 366 
PRO   HG2  H  N N 367 
PRO   HG3  H  N N 368 
PRO   HD2  H  N N 369 
PRO   HD3  H  N N 370 
PRO   HXT  H  N N 371 
SER   N    N  N N 372 
SER   CA   C  N S 373 
SER   C    C  N N 374 
SER   O    O  N N 375 
SER   CB   C  N N 376 
SER   OG   O  N N 377 
SER   OXT  O  N N 378 
SER   H    H  N N 379 
SER   H2   H  N N 380 
SER   HA   H  N N 381 
SER   HB2  H  N N 382 
SER   HB3  H  N N 383 
SER   HG   H  N N 384 
SER   HXT  H  N N 385 
THR   N    N  N N 386 
THR   CA   C  N S 387 
THR   C    C  N N 388 
THR   O    O  N N 389 
THR   CB   C  N R 390 
THR   OG1  O  N N 391 
THR   CG2  C  N N 392 
THR   OXT  O  N N 393 
THR   H    H  N N 394 
THR   H2   H  N N 395 
THR   HA   H  N N 396 
THR   HB   H  N N 397 
THR   HG1  H  N N 398 
THR   HG21 H  N N 399 
THR   HG22 H  N N 400 
THR   HG23 H  N N 401 
THR   HXT  H  N N 402 
TRP   N    N  N N 403 
TRP   CA   C  N S 404 
TRP   C    C  N N 405 
TRP   O    O  N N 406 
TRP   CB   C  N N 407 
TRP   CG   C  Y N 408 
TRP   CD1  C  Y N 409 
TRP   CD2  C  Y N 410 
TRP   NE1  N  Y N 411 
TRP   CE2  C  Y N 412 
TRP   CE3  C  Y N 413 
TRP   CZ2  C  Y N 414 
TRP   CZ3  C  Y N 415 
TRP   CH2  C  Y N 416 
TRP   OXT  O  N N 417 
TRP   H    H  N N 418 
TRP   H2   H  N N 419 
TRP   HA   H  N N 420 
TRP   HB2  H  N N 421 
TRP   HB3  H  N N 422 
TRP   HD1  H  N N 423 
TRP   HE1  H  N N 424 
TRP   HE3  H  N N 425 
TRP   HZ2  H  N N 426 
TRP   HZ3  H  N N 427 
TRP   HH2  H  N N 428 
TRP   HXT  H  N N 429 
TYR   N    N  N N 430 
TYR   CA   C  N S 431 
TYR   C    C  N N 432 
TYR   O    O  N N 433 
TYR   CB   C  N N 434 
TYR   CG   C  Y N 435 
TYR   CD1  C  Y N 436 
TYR   CD2  C  Y N 437 
TYR   CE1  C  Y N 438 
TYR   CE2  C  Y N 439 
TYR   CZ   C  Y N 440 
TYR   OH   O  N N 441 
TYR   OXT  O  N N 442 
TYR   H    H  N N 443 
TYR   H2   H  N N 444 
TYR   HA   H  N N 445 
TYR   HB2  H  N N 446 
TYR   HB3  H  N N 447 
TYR   HD1  H  N N 448 
TYR   HD2  H  N N 449 
TYR   HE1  H  N N 450 
TYR   HE2  H  N N 451 
TYR   HH   H  N N 452 
TYR   HXT  H  N N 453 
VAL   N    N  N N 454 
VAL   CA   C  N S 455 
VAL   C    C  N N 456 
VAL   O    O  N N 457 
VAL   CB   C  N N 458 
VAL   CG1  C  N N 459 
VAL   CG2  C  N N 460 
VAL   OXT  O  N N 461 
VAL   H    H  N N 462 
VAL   H2   H  N N 463 
VAL   HA   H  N N 464 
VAL   HB   H  N N 465 
VAL   HG11 H  N N 466 
VAL   HG12 H  N N 467 
VAL   HG13 H  N N 468 
VAL   HG21 H  N N 469 
VAL   HG22 H  N N 470 
VAL   HG23 H  N N 471 
VAL   HXT  H  N N 472 
# 
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 
A1L76 C01  C02  doub Y N 1   
A1L76 C01  C06  sing Y N 2   
A1L76 C02  C03  sing Y N 3   
A1L76 C02  O07  sing N N 4   
A1L76 C03  C04  doub Y N 5   
A1L76 C03  C33  sing N N 6   
A1L76 C04  C05  sing Y N 7   
A1L76 C05  C06  doub Y N 8   
A1L76 C05  SI08 sing N N 9   
A1L76 O07  C25  sing N N 10  
A1L76 SI08 C09  sing N N 11  
A1L76 SI08 C10  sing N N 12  
A1L76 SI08 C11  sing N N 13  
A1L76 C09  C12  doub Y N 14  
A1L76 C09  C16  sing Y N 15  
A1L76 C10  C37  sing N N 16  
A1L76 C11  C35  sing N N 17  
A1L76 C12  C13  sing Y N 18  
A1L76 C13  C14  doub Y N 19  
A1L76 C13  C34  sing N N 20  
A1L76 C14  C15  sing Y N 21  
A1L76 C14  O17  sing N N 22  
A1L76 C15  C16  doub Y N 23  
A1L76 O17  C18  sing N N 24  
A1L76 C18  C19  sing N N 25  
A1L76 C19  C20  sing N N 26  
A1L76 C19  C22  sing N N 27  
A1L76 C19  O24  sing N N 28  
A1L76 C20  C21  sing N N 29  
A1L76 C22  C23  sing N N 30  
A1L76 C25  C26  sing N N 31  
A1L76 C26  O27  sing N N 32  
A1L76 C26  C28  sing N N 33  
A1L76 C28  C29  sing N N 34  
A1L76 C29  C30  sing N N 35  
A1L76 C30  O31  doub N N 36  
A1L76 C30  O32  sing N N 37  
A1L76 C35  C36  doub N N 38  
A1L76 C37  C38  doub N N 39  
A1L76 C10  H102 sing N N 40  
A1L76 C10  H101 sing N N 41  
A1L76 C15  H151 sing N N 42  
A1L76 C20  H202 sing N N 43  
A1L76 C20  H201 sing N N 44  
A1L76 C21  H213 sing N N 45  
A1L76 C21  H211 sing N N 46  
A1L76 C21  H212 sing N N 47  
A1L76 C22  H221 sing N N 48  
A1L76 C22  H222 sing N N 49  
A1L76 C26  H261 sing N N 50  
A1L76 C28  H282 sing N N 51  
A1L76 C28  H281 sing N N 52  
A1L76 C01  H011 sing N N 53  
A1L76 C04  H041 sing N N 54  
A1L76 C06  H061 sing N N 55  
A1L76 C11  H111 sing N N 56  
A1L76 C11  H112 sing N N 57  
A1L76 C12  H121 sing N N 58  
A1L76 C16  H161 sing N N 59  
A1L76 C18  H181 sing N N 60  
A1L76 C18  H182 sing N N 61  
A1L76 C23  H231 sing N N 62  
A1L76 C23  H232 sing N N 63  
A1L76 C23  H233 sing N N 64  
A1L76 C25  H251 sing N N 65  
A1L76 C25  H252 sing N N 66  
A1L76 C29  H292 sing N N 67  
A1L76 C29  H291 sing N N 68  
A1L76 C33  H331 sing N N 69  
A1L76 C33  H332 sing N N 70  
A1L76 C33  H333 sing N N 71  
A1L76 C34  H342 sing N N 72  
A1L76 C34  H341 sing N N 73  
A1L76 C34  H343 sing N N 74  
A1L76 C35  H351 sing N N 75  
A1L76 C36  H361 sing N N 76  
A1L76 C36  H362 sing N N 77  
A1L76 C37  H371 sing N N 78  
A1L76 C38  H382 sing N N 79  
A1L76 C38  H381 sing N N 80  
A1L76 O24  H241 sing N N 81  
A1L76 O27  H271 sing N N 82  
A1L76 O32  H1   sing N N 83  
ALA   N    CA   sing N N 84  
ALA   N    H    sing N N 85  
ALA   N    H2   sing N N 86  
ALA   CA   C    sing N N 87  
ALA   CA   CB   sing N N 88  
ALA   CA   HA   sing N N 89  
ALA   C    O    doub N N 90  
ALA   C    OXT  sing N N 91  
ALA   CB   HB1  sing N N 92  
ALA   CB   HB2  sing N N 93  
ALA   CB   HB3  sing N N 94  
ALA   OXT  HXT  sing N N 95  
ARG   N    CA   sing N N 96  
ARG   N    H    sing N N 97  
ARG   N    H2   sing N N 98  
ARG   CA   C    sing N N 99  
ARG   CA   CB   sing N N 100 
ARG   CA   HA   sing N N 101 
ARG   C    O    doub N N 102 
ARG   C    OXT  sing N N 103 
ARG   CB   CG   sing N N 104 
ARG   CB   HB2  sing N N 105 
ARG   CB   HB3  sing N N 106 
ARG   CG   CD   sing N N 107 
ARG   CG   HG2  sing N N 108 
ARG   CG   HG3  sing N N 109 
ARG   CD   NE   sing N N 110 
ARG   CD   HD2  sing N N 111 
ARG   CD   HD3  sing N N 112 
ARG   NE   CZ   sing N N 113 
ARG   NE   HE   sing N N 114 
ARG   CZ   NH1  sing N N 115 
ARG   CZ   NH2  doub N N 116 
ARG   NH1  HH11 sing N N 117 
ARG   NH1  HH12 sing N N 118 
ARG   NH2  HH21 sing N N 119 
ARG   NH2  HH22 sing N N 120 
ARG   OXT  HXT  sing N N 121 
ASN   N    CA   sing N N 122 
ASN   N    H    sing N N 123 
ASN   N    H2   sing N N 124 
ASN   CA   C    sing N N 125 
ASN   CA   CB   sing N N 126 
ASN   CA   HA   sing N N 127 
ASN   C    O    doub N N 128 
ASN   C    OXT  sing N N 129 
ASN   CB   CG   sing N N 130 
ASN   CB   HB2  sing N N 131 
ASN   CB   HB3  sing N N 132 
ASN   CG   OD1  doub N N 133 
ASN   CG   ND2  sing N N 134 
ASN   ND2  HD21 sing N N 135 
ASN   ND2  HD22 sing N N 136 
ASN   OXT  HXT  sing N N 137 
ASP   N    CA   sing N N 138 
ASP   N    H    sing N N 139 
ASP   N    H2   sing N N 140 
ASP   CA   C    sing N N 141 
ASP   CA   CB   sing N N 142 
ASP   CA   HA   sing N N 143 
ASP   C    O    doub N N 144 
ASP   C    OXT  sing N N 145 
ASP   CB   CG   sing N N 146 
ASP   CB   HB2  sing N N 147 
ASP   CB   HB3  sing N N 148 
ASP   CG   OD1  doub N N 149 
ASP   CG   OD2  sing N N 150 
ASP   OD2  HD2  sing N N 151 
ASP   OXT  HXT  sing N N 152 
CYS   N    CA   sing N N 153 
CYS   N    H    sing N N 154 
CYS   N    H2   sing N N 155 
CYS   CA   C    sing N N 156 
CYS   CA   CB   sing N N 157 
CYS   CA   HA   sing N N 158 
CYS   C    O    doub N N 159 
CYS   C    OXT  sing N N 160 
CYS   CB   SG   sing N N 161 
CYS   CB   HB2  sing N N 162 
CYS   CB   HB3  sing N N 163 
CYS   SG   HG   sing N N 164 
CYS   OXT  HXT  sing N N 165 
GLN   N    CA   sing N N 166 
GLN   N    H    sing N N 167 
GLN   N    H2   sing N N 168 
GLN   CA   C    sing N N 169 
GLN   CA   CB   sing N N 170 
GLN   CA   HA   sing N N 171 
GLN   C    O    doub N N 172 
GLN   C    OXT  sing N N 173 
GLN   CB   CG   sing N N 174 
GLN   CB   HB2  sing N N 175 
GLN   CB   HB3  sing N N 176 
GLN   CG   CD   sing N N 177 
GLN   CG   HG2  sing N N 178 
GLN   CG   HG3  sing N N 179 
GLN   CD   OE1  doub N N 180 
GLN   CD   NE2  sing N N 181 
GLN   NE2  HE21 sing N N 182 
GLN   NE2  HE22 sing N N 183 
GLN   OXT  HXT  sing N N 184 
GLU   N    CA   sing N N 185 
GLU   N    H    sing N N 186 
GLU   N    H2   sing N N 187 
GLU   CA   C    sing N N 188 
GLU   CA   CB   sing N N 189 
GLU   CA   HA   sing N N 190 
GLU   C    O    doub N N 191 
GLU   C    OXT  sing N N 192 
GLU   CB   CG   sing N N 193 
GLU   CB   HB2  sing N N 194 
GLU   CB   HB3  sing N N 195 
GLU   CG   CD   sing N N 196 
GLU   CG   HG2  sing N N 197 
GLU   CG   HG3  sing N N 198 
GLU   CD   OE1  doub N N 199 
GLU   CD   OE2  sing N N 200 
GLU   OE2  HE2  sing N N 201 
GLU   OXT  HXT  sing N N 202 
GLY   N    CA   sing N N 203 
GLY   N    H    sing N N 204 
GLY   N    H2   sing N N 205 
GLY   CA   C    sing N N 206 
GLY   CA   HA2  sing N N 207 
GLY   CA   HA3  sing N N 208 
GLY   C    O    doub N N 209 
GLY   C    OXT  sing N N 210 
GLY   OXT  HXT  sing N N 211 
HIS   N    CA   sing N N 212 
HIS   N    H    sing N N 213 
HIS   N    H2   sing N N 214 
HIS   CA   C    sing N N 215 
HIS   CA   CB   sing N N 216 
HIS   CA   HA   sing N N 217 
HIS   C    O    doub N N 218 
HIS   C    OXT  sing N N 219 
HIS   CB   CG   sing N N 220 
HIS   CB   HB2  sing N N 221 
HIS   CB   HB3  sing N N 222 
HIS   CG   ND1  sing Y N 223 
HIS   CG   CD2  doub Y N 224 
HIS   ND1  CE1  doub Y N 225 
HIS   ND1  HD1  sing N N 226 
HIS   CD2  NE2  sing Y N 227 
HIS   CD2  HD2  sing N N 228 
HIS   CE1  NE2  sing Y N 229 
HIS   CE1  HE1  sing N N 230 
HIS   NE2  HE2  sing N N 231 
HIS   OXT  HXT  sing N N 232 
HOH   O    H1   sing N N 233 
HOH   O    H2   sing N N 234 
ILE   N    CA   sing N N 235 
ILE   N    H    sing N N 236 
ILE   N    H2   sing N N 237 
ILE   CA   C    sing N N 238 
ILE   CA   CB   sing N N 239 
ILE   CA   HA   sing N N 240 
ILE   C    O    doub N N 241 
ILE   C    OXT  sing N N 242 
ILE   CB   CG1  sing N N 243 
ILE   CB   CG2  sing N N 244 
ILE   CB   HB   sing N N 245 
ILE   CG1  CD1  sing N N 246 
ILE   CG1  HG12 sing N N 247 
ILE   CG1  HG13 sing N N 248 
ILE   CG2  HG21 sing N N 249 
ILE   CG2  HG22 sing N N 250 
ILE   CG2  HG23 sing N N 251 
ILE   CD1  HD11 sing N N 252 
ILE   CD1  HD12 sing N N 253 
ILE   CD1  HD13 sing N N 254 
ILE   OXT  HXT  sing N N 255 
LEU   N    CA   sing N N 256 
LEU   N    H    sing N N 257 
LEU   N    H2   sing N N 258 
LEU   CA   C    sing N N 259 
LEU   CA   CB   sing N N 260 
LEU   CA   HA   sing N N 261 
LEU   C    O    doub N N 262 
LEU   C    OXT  sing N N 263 
LEU   CB   CG   sing N N 264 
LEU   CB   HB2  sing N N 265 
LEU   CB   HB3  sing N N 266 
LEU   CG   CD1  sing N N 267 
LEU   CG   CD2  sing N N 268 
LEU   CG   HG   sing N N 269 
LEU   CD1  HD11 sing N N 270 
LEU   CD1  HD12 sing N N 271 
LEU   CD1  HD13 sing N N 272 
LEU   CD2  HD21 sing N N 273 
LEU   CD2  HD22 sing N N 274 
LEU   CD2  HD23 sing N N 275 
LEU   OXT  HXT  sing N N 276 
LYS   N    CA   sing N N 277 
LYS   N    H    sing N N 278 
LYS   N    H2   sing N N 279 
LYS   CA   C    sing N N 280 
LYS   CA   CB   sing N N 281 
LYS   CA   HA   sing N N 282 
LYS   C    O    doub N N 283 
LYS   C    OXT  sing N N 284 
LYS   CB   CG   sing N N 285 
LYS   CB   HB2  sing N N 286 
LYS   CB   HB3  sing N N 287 
LYS   CG   CD   sing N N 288 
LYS   CG   HG2  sing N N 289 
LYS   CG   HG3  sing N N 290 
LYS   CD   CE   sing N N 291 
LYS   CD   HD2  sing N N 292 
LYS   CD   HD3  sing N N 293 
LYS   CE   NZ   sing N N 294 
LYS   CE   HE2  sing N N 295 
LYS   CE   HE3  sing N N 296 
LYS   NZ   HZ1  sing N N 297 
LYS   NZ   HZ2  sing N N 298 
LYS   NZ   HZ3  sing N N 299 
LYS   OXT  HXT  sing N N 300 
MET   N    CA   sing N N 301 
MET   N    H    sing N N 302 
MET   N    H2   sing N N 303 
MET   CA   C    sing N N 304 
MET   CA   CB   sing N N 305 
MET   CA   HA   sing N N 306 
MET   C    O    doub N N 307 
MET   C    OXT  sing N N 308 
MET   CB   CG   sing N N 309 
MET   CB   HB2  sing N N 310 
MET   CB   HB3  sing N N 311 
MET   CG   SD   sing N N 312 
MET   CG   HG2  sing N N 313 
MET   CG   HG3  sing N N 314 
MET   SD   CE   sing N N 315 
MET   CE   HE1  sing N N 316 
MET   CE   HE2  sing N N 317 
MET   CE   HE3  sing N N 318 
MET   OXT  HXT  sing N N 319 
PHE   N    CA   sing N N 320 
PHE   N    H    sing N N 321 
PHE   N    H2   sing N N 322 
PHE   CA   C    sing N N 323 
PHE   CA   CB   sing N N 324 
PHE   CA   HA   sing N N 325 
PHE   C    O    doub N N 326 
PHE   C    OXT  sing N N 327 
PHE   CB   CG   sing N N 328 
PHE   CB   HB2  sing N N 329 
PHE   CB   HB3  sing N N 330 
PHE   CG   CD1  doub Y N 331 
PHE   CG   CD2  sing Y N 332 
PHE   CD1  CE1  sing Y N 333 
PHE   CD1  HD1  sing N N 334 
PHE   CD2  CE2  doub Y N 335 
PHE   CD2  HD2  sing N N 336 
PHE   CE1  CZ   doub Y N 337 
PHE   CE1  HE1  sing N N 338 
PHE   CE2  CZ   sing Y N 339 
PHE   CE2  HE2  sing N N 340 
PHE   CZ   HZ   sing N N 341 
PHE   OXT  HXT  sing N N 342 
PRO   N    CA   sing N N 343 
PRO   N    CD   sing N N 344 
PRO   N    H    sing N N 345 
PRO   CA   C    sing N N 346 
PRO   CA   CB   sing N N 347 
PRO   CA   HA   sing N N 348 
PRO   C    O    doub N N 349 
PRO   C    OXT  sing N N 350 
PRO   CB   CG   sing N N 351 
PRO   CB   HB2  sing N N 352 
PRO   CB   HB3  sing N N 353 
PRO   CG   CD   sing N N 354 
PRO   CG   HG2  sing N N 355 
PRO   CG   HG3  sing N N 356 
PRO   CD   HD2  sing N N 357 
PRO   CD   HD3  sing N N 358 
PRO   OXT  HXT  sing N N 359 
SER   N    CA   sing N N 360 
SER   N    H    sing N N 361 
SER   N    H2   sing N N 362 
SER   CA   C    sing N N 363 
SER   CA   CB   sing N N 364 
SER   CA   HA   sing N N 365 
SER   C    O    doub N N 366 
SER   C    OXT  sing N N 367 
SER   CB   OG   sing N N 368 
SER   CB   HB2  sing N N 369 
SER   CB   HB3  sing N N 370 
SER   OG   HG   sing N N 371 
SER   OXT  HXT  sing N N 372 
THR   N    CA   sing N N 373 
THR   N    H    sing N N 374 
THR   N    H2   sing N N 375 
THR   CA   C    sing N N 376 
THR   CA   CB   sing N N 377 
THR   CA   HA   sing N N 378 
THR   C    O    doub N N 379 
THR   C    OXT  sing N N 380 
THR   CB   OG1  sing N N 381 
THR   CB   CG2  sing N N 382 
THR   CB   HB   sing N N 383 
THR   OG1  HG1  sing N N 384 
THR   CG2  HG21 sing N N 385 
THR   CG2  HG22 sing N N 386 
THR   CG2  HG23 sing N N 387 
THR   OXT  HXT  sing N N 388 
TRP   N    CA   sing N N 389 
TRP   N    H    sing N N 390 
TRP   N    H2   sing N N 391 
TRP   CA   C    sing N N 392 
TRP   CA   CB   sing N N 393 
TRP   CA   HA   sing N N 394 
TRP   C    O    doub N N 395 
TRP   C    OXT  sing N N 396 
TRP   CB   CG   sing N N 397 
TRP   CB   HB2  sing N N 398 
TRP   CB   HB3  sing N N 399 
TRP   CG   CD1  doub Y N 400 
TRP   CG   CD2  sing Y N 401 
TRP   CD1  NE1  sing Y N 402 
TRP   CD1  HD1  sing N N 403 
TRP   CD2  CE2  doub Y N 404 
TRP   CD2  CE3  sing Y N 405 
TRP   NE1  CE2  sing Y N 406 
TRP   NE1  HE1  sing N N 407 
TRP   CE2  CZ2  sing Y N 408 
TRP   CE3  CZ3  doub Y N 409 
TRP   CE3  HE3  sing N N 410 
TRP   CZ2  CH2  doub Y N 411 
TRP   CZ2  HZ2  sing N N 412 
TRP   CZ3  CH2  sing Y N 413 
TRP   CZ3  HZ3  sing N N 414 
TRP   CH2  HH2  sing N N 415 
TRP   OXT  HXT  sing N N 416 
TYR   N    CA   sing N N 417 
TYR   N    H    sing N N 418 
TYR   N    H2   sing N N 419 
TYR   CA   C    sing N N 420 
TYR   CA   CB   sing N N 421 
TYR   CA   HA   sing N N 422 
TYR   C    O    doub N N 423 
TYR   C    OXT  sing N N 424 
TYR   CB   CG   sing N N 425 
TYR   CB   HB2  sing N N 426 
TYR   CB   HB3  sing N N 427 
TYR   CG   CD1  doub Y N 428 
TYR   CG   CD2  sing Y N 429 
TYR   CD1  CE1  sing Y N 430 
TYR   CD1  HD1  sing N N 431 
TYR   CD2  CE2  doub Y N 432 
TYR   CD2  HD2  sing N N 433 
TYR   CE1  CZ   doub Y N 434 
TYR   CE1  HE1  sing N N 435 
TYR   CE2  CZ   sing Y N 436 
TYR   CE2  HE2  sing N N 437 
TYR   CZ   OH   sing N N 438 
TYR   OH   HH   sing N N 439 
TYR   OXT  HXT  sing N N 440 
VAL   N    CA   sing N N 441 
VAL   N    H    sing N N 442 
VAL   N    H2   sing N N 443 
VAL   CA   C    sing N N 444 
VAL   CA   CB   sing N N 445 
VAL   CA   HA   sing N N 446 
VAL   C    O    doub N N 447 
VAL   C    OXT  sing N N 448 
VAL   CB   CG1  sing N N 449 
VAL   CB   CG2  sing N N 450 
VAL   CB   HB   sing N N 451 
VAL   CG1  HG11 sing N N 452 
VAL   CG1  HG12 sing N N 453 
VAL   CG1  HG13 sing N N 454 
VAL   CG2  HG21 sing N N 455 
VAL   CG2  HG22 sing N N 456 
VAL   CG2  HG23 sing N N 457 
VAL   OXT  HXT  sing N N 458 
# 
_pdbx_audit_support.funding_organization   'Not funded' 
_pdbx_audit_support.country                ? 
_pdbx_audit_support.grant_number           ? 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   2ZLC 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    9M18 
_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]   0.006479 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000610 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.024098 
_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]   0.023921 
_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 
C  
N  
O  
S  
SI 
# 
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    . LYS   A 1 18  ? 43.56600 -2.45200  3.43400  1.000 73.70055  ?  123 LYS   A N    1 
ATOM   2    C  CA   . LYS   A 1 18  ? 42.85700 -1.26800  2.95500  1.000 74.95294  ?  123 LYS   A CA   1 
ATOM   3    C  C    . LYS   A 1 18  ? 41.38000 -1.55300  2.65800  1.000 70.69644  ?  123 LYS   A C    1 
ATOM   4    O  O    . LYS   A 1 18  ? 40.97800 -2.70400  2.48400  1.000 69.37772  ?  123 LYS   A O    1 
ATOM   5    C  CB   . LYS   A 1 18  ? 43.54900 -0.70700  1.71000  1.000 82.65845  ?  123 LYS   A CB   1 
ATOM   6    C  CG   . LYS   A 1 18  ? 43.70700 0.80600   1.72200  1.000 89.10332  ?  123 LYS   A CG   1 
ATOM   7    C  CD   . LYS   A 1 18  ? 43.87000 1.35800   0.31200  1.000 93.98682  ?  123 LYS   A CD   1 
ATOM   8    C  CE   . LYS   A 1 18  ? 42.52500 1.49100   -0.39100 1.000 92.49286  ?  123 LYS   A CE   1 
ATOM   9    N  NZ   . LYS   A 1 18  ? 41.53300 2.26200   0.40800  1.000 89.35179  ?  123 LYS   A NZ   1 
ATOM   10   N  N    . LEU   A 1 19  ? 40.58300 -0.48900  2.60100  1.000 64.80474  ?  124 LEU   A N    1 
ATOM   11   C  CA   . LEU   A 1 19  ? 39.13400 -0.60200  2.45800  1.000 66.05115  ?  124 LEU   A CA   1 
ATOM   12   C  C    . LEU   A 1 19  ? 38.79800 -1.05400  1.03900  1.000 64.56368  ?  124 LEU   A C    1 
ATOM   13   O  O    . LEU   A 1 19  ? 38.94500 -0.28300  0.08500  1.000 63.70078  ?  124 LEU   A O    1 
ATOM   14   C  CB   . LEU   A 1 19  ? 38.48300 0.73700   2.78900  1.000 66.62844  ?  124 LEU   A CB   1 
ATOM   15   C  CG   . LEU   A 1 19  ? 37.08600 0.75800   3.40200  1.000 65.52950  ?  124 LEU   A CG   1 
ATOM   16   C  CD1  . LEU   A 1 19  ? 37.04300 -0.05400  4.68800  1.000 59.65086  ?  124 LEU   A CD1  1 
ATOM   17   C  CD2  . LEU   A 1 19  ? 36.68900 2.20100   3.67100  1.000 67.62239  ?  124 LEU   A CD2  1 
ATOM   18   N  N    . SER   A 1 20  ? 38.35000 -2.30100  0.89800  1.000 61.66225  ?  125 SER   A N    1 
ATOM   19   C  CA   . SER   A 1 20  ? 38.00400 -2.83600  -0.41300 1.000 61.11650  ?  125 SER   A CA   1 
ATOM   20   C  C    . SER   A 1 20  ? 36.80500 -2.09500  -1.00100 1.000 64.91619  ?  125 SER   A C    1 
ATOM   21   O  O    . SER   A 1 20  ? 36.07300 -1.38800  -0.30300 1.000 65.32994  ?  125 SER   A O    1 
ATOM   22   C  CB   . SER   A 1 20  ? 37.69100 -4.33000  -0.31700 1.000 57.02597  ?  125 SER   A CB   1 
ATOM   23   O  OG   . SER   A 1 20  ? 36.37400 -4.54900  0.17200  1.000 55.59378  ?  125 SER   A OG   1 
ATOM   24   N  N    . GLU   A 1 21  ? 36.60500 -2.27200  -2.31100 1.000 66.87515  ?  126 GLU   A N    1 
ATOM   25   C  CA   . GLU   A 1 21  ? 35.47300 -1.63200  -2.97600 1.000 68.85754  ?  126 GLU   A CA   1 
ATOM   26   C  C    . GLU   A 1 21  ? 34.15200 -2.13100  -2.40700 1.000 62.54742  ?  126 GLU   A C    1 
ATOM   27   O  O    . GLU   A 1 21  ? 33.19800 -1.35900  -2.25400 1.000 55.36713  ?  126 GLU   A O    1 
ATOM   28   C  CB   . GLU   A 1 21  ? 35.53800 -1.87700  -4.48400 1.000 78.51144  ?  126 GLU   A CB   1 
ATOM   29   C  CG   . GLU   A 1 21  ? 34.95500 -0.74600  -5.32200 1.000 86.81179  ?  126 GLU   A CG   1 
ATOM   30   C  CD   . GLU   A 1 21  ? 35.75100 0.54400   -5.20300 1.000 92.73556  ?  126 GLU   A CD   1 
ATOM   31   O  OE1  . GLU   A 1 21  ? 35.17300 1.56500   -4.76900 1.000 93.10260  ?  126 GLU   A OE1  1 
ATOM   32   O  OE2  . GLU   A 1 21  ? 36.95400 0.53900   -5.54800 1.000 96.00191  ?  126 GLU   A OE2  1 
ATOM   33   N  N    . GLU   A 1 22  ? 34.08300 -3.42100  -2.07800 1.000 62.35649  ?  127 GLU   A N    1 
ATOM   34   C  CA   . GLU   A 1 22  ? 32.88300 -3.96900  -1.46300 1.000 59.64199  ?  127 GLU   A CA   1 
ATOM   35   C  C    . GLU   A 1 22  ? 32.66000 -3.40700  -0.06200 1.000 52.34460  ?  127 GLU   A C    1 
ATOM   36   O  O    . GLU   A 1 22  ? 31.51000 -3.23500  0.36000  1.000 43.61249  ?  127 GLU   A O    1 
ATOM   37   C  CB   . GLU   A 1 22  ? 32.97600 -5.49700  -1.43700 1.000 70.75940  ?  127 GLU   A CB   1 
ATOM   38   C  CG   . GLU   A 1 22  ? 32.05300 -6.18800  -0.43900 1.000 79.68674  ?  127 GLU   A CG   1 
ATOM   39   C  CD   . GLU   A 1 22  ? 31.86400 -7.66600  -0.74300 1.000 88.61087  ?  127 GLU   A CD   1 
ATOM   40   O  OE1  . GLU   A 1 22  ? 31.36600 -7.98800  -1.84300 1.000 93.16509  ?  127 GLU   A OE1  1 
ATOM   41   O  OE2  . GLU   A 1 22  ? 32.21200 -8.50400  0.11700  1.000 90.56596  ?  127 GLU   A OE2  1 
ATOM   42   N  N    . GLN   A 1 23  ? 33.73300 -3.09100  0.66300  1.000 57.47956  ?  128 GLN   A N    1 
ATOM   43   C  CA   . GLN   A 1 23  ? 33.56700 -2.59400  2.02400  1.000 52.04434  ?  128 GLN   A CA   1 
ATOM   44   C  C    . GLN   A 1 23  ? 33.04400 -1.16100  2.03800  1.000 51.43712  ?  128 GLN   A C    1 
ATOM   45   O  O    . GLN   A 1 23  ? 32.15100 -0.83300  2.82700  1.000 47.60494  ?  128 GLN   A O    1 
ATOM   46   C  CB   . GLN   A 1 23  ? 34.88100 -2.71300  2.78900  1.000 49.66196  ?  128 GLN   A CB   1 
ATOM   47   C  CG   . GLN   A 1 23  ? 35.23500 -4.15100  3.13900  1.000 50.12208  ?  128 GLN   A CG   1 
ATOM   48   C  CD   . GLN   A 1 23  ? 36.56700 -4.26600  3.85600  1.000 54.20199  ?  128 GLN   A CD   1 
ATOM   49   O  OE1  . GLN   A 1 23  ? 37.45300 -3.43400  3.67300  1.000 55.94515  ?  128 GLN   A OE1  1 
ATOM   50   N  NE2  . GLN   A 1 23  ? 36.71300 -5.30000  4.67800  1.000 50.56943  ?  128 GLN   A NE2  1 
ATOM   51   N  N    . GLN   A 1 24  ? 33.57000 -0.29400  1.16700  1.000 52.74420  ?  129 GLN   A N    1 
ATOM   52   C  CA   . GLN   A 1 24  ? 33.00200 1.04700   1.06900  1.000 55.42454  ?  129 GLN   A CA   1 
ATOM   53   C  C    . GLN   A 1 24  ? 31.60100 1.02800   0.47900  1.000 51.94242  ?  129 GLN   A C    1 
ATOM   54   O  O    . GLN   A 1 24  ? 30.82200 1.95000   0.73800  1.000 51.94914  ?  129 GLN   A O    1 
ATOM   55   C  CB   . GLN   A 1 24  ? 33.90600 1.96900   0.24800  1.000 64.93054  ?  129 GLN   A CB   1 
ATOM   56   C  CG   . GLN   A 1 24  ? 34.56400 1.31600   -0.94500 1.000 74.43869  ?  129 GLN   A CG   1 
ATOM   57   C  CD   . GLN   A 1 24  ? 35.78400 2.08400   -1.42900 1.000 79.55828  ?  129 GLN   A CD   1 
ATOM   58   O  OE1  . GLN   A 1 24  ? 36.82900 1.49600   -1.70600 1.000 79.22884  ?  129 GLN   A OE1  1 
ATOM   59   N  NE2  . GLN   A 1 24  ? 35.65500 3.40200   -1.53400 1.000 81.51517  ?  129 GLN   A NE2  1 
ATOM   60   N  N    . HIS   A 1 25  ? 31.26300 0.00300   -0.30600 1.000 50.81203  ?  130 HIS   A N    1 
ATOM   61   C  CA   . HIS   A 1 25  ? 29.88100 -0.16500  -0.74700 1.000 49.54160  ?  130 HIS   A CA   1 
ATOM   62   C  C    . HIS   A 1 25  ? 28.97400 -0.47700  0.43500  1.000 49.67983  ?  130 HIS   A C    1 
ATOM   63   O  O    . HIS   A 1 25  ? 27.88600 0.09800   0.56900  1.000 53.28308  ?  130 HIS   A O    1 
ATOM   64   C  CB   . HIS   A 1 25  ? 29.79200 -1.27600  -1.79500 1.000 54.18561  ?  130 HIS   A CB   1 
ATOM   65   C  CG   . HIS   A 1 25  ? 28.39000 -1.61000  -2.20200 1.000 60.02805  ?  130 HIS   A CG   1 
ATOM   66   N  ND1  . HIS   A 1 25  ? 27.53500 -0.68600  -2.76500 1.000 61.24210  ?  130 HIS   A ND1  1 
ATOM   67   C  CD2  . HIS   A 1 25  ? 27.68600 -2.76300  -2.10600 1.000 61.03954  ?  130 HIS   A CD2  1 
ATOM   68   C  CE1  . HIS   A 1 25  ? 26.37100 -1.26100  -3.01300 1.000 61.27665  ?  130 HIS   A CE1  1 
ATOM   69   N  NE2  . HIS   A 1 25  ? 26.43600 -2.52100  -2.62100 1.000 59.90381  ?  130 HIS   A NE2  1 
ATOM   70   N  N    . ILE   A 1 26  ? 29.41100 -1.39700  1.29800  1.000 47.86428  ?  131 ILE   A N    1 
ATOM   71   C  CA   . ILE   A 1 26  ? 28.65600 -1.74000  2.49800  1.000 44.51608  ?  131 ILE   A CA   1 
ATOM   72   C  C    . ILE   A 1 26  ? 28.43100 -0.50200  3.35600  1.000 45.10212  ?  131 ILE   A C    1 
ATOM   73   O  O    . ILE   A 1 26  ? 27.32400 -0.25800  3.84900  1.000 44.08347  ?  131 ILE   A O    1 
ATOM   74   C  CB   . ILE   A 1 26  ? 29.38700 -2.84300  3.28400  1.000 47.76955  ?  131 ILE   A CB   1 
ATOM   75   C  CG1  . ILE   A 1 26  ? 29.26800 -4.18200  2.55500  1.000 47.52367  ?  131 ILE   A CG1  1 
ATOM   76   C  CG2  . ILE   A 1 26  ? 28.84700 -2.94200  4.70700  1.000 46.86228  ?  131 ILE   A CG2  1 
ATOM   77   C  CD1  . ILE   A 1 26  ? 30.18100 -5.25300  3.09600  1.000 48.02966  ?  131 ILE   A CD1  1 
ATOM   78   N  N    . ILE   A 1 27  ? 29.48200 0.29400   3.55400  1.000 47.56767  ?  132 ILE   A N    1 
ATOM   79   C  CA   . ILE   A 1 27  ? 29.35200 1.49200   4.37900  1.000 45.97163  ?  132 ILE   A CA   1 
ATOM   80   C  C    . ILE   A 1 27  ? 28.36200 2.46600   3.75500  1.000 43.93794  ?  132 ILE   A C    1 
ATOM   81   O  O    . ILE   A 1 27  ? 27.51100 3.03800   4.44800  1.000 42.59722  ?  132 ILE   A O    1 
ATOM   82   C  CB   . ILE   A 1 27  ? 30.72900 2.14000   4.60000  1.000 44.27778  ?  132 ILE   A CB   1 
ATOM   83   C  CG1  . ILE   A 1 27  ? 31.54900 1.30000   5.58500  1.000 44.60404  ?  132 ILE   A CG1  1 
ATOM   84   C  CG2  . ILE   A 1 27  ? 30.56700 3.55900   5.10800  1.000 39.52374  ?  132 ILE   A CG2  1 
ATOM   85   C  CD1  . ILE   A 1 27  ? 33.03200 1.55800   5.52600  1.000 43.91845  ?  132 ILE   A CD1  1 
ATOM   86   N  N    . ALA   A 1 28  ? 28.45600 2.67000   2.43900  1.000 43.75507  ?  133 ALA   A N    1 
ATOM   87   C  CA   . ALA   A 1 28  ? 27.50700 3.53700   1.74900  1.000 44.33157  ?  133 ALA   A CA   1 
ATOM   88   C  C    . ALA   A 1 28  ? 26.07500 3.04500   1.92500  1.000 44.67801  ?  133 ALA   A C    1 
ATOM   89   O  O    . ALA   A 1 28  ? 25.16500 3.84300   2.18100  1.000 41.92586  ?  133 ALA   A O    1 
ATOM   90   C  CB   . ALA   A 1 28  ? 27.85900 3.62600   0.26300  1.000 44.51606  ?  133 ALA   A CB   1 
ATOM   91   N  N    . ILE   A 1 29  ? 25.85700 1.73300   1.79200  1.000 44.89169  ?  134 ILE   A N    1 
ATOM   92   C  CA   . ILE   A 1 29  ? 24.51000 1.18300   1.93300  1.000 46.31844  ?  134 ILE   A CA   1 
ATOM   93   C  C    . ILE   A 1 29  ? 23.98200 1.44000   3.33700  1.000 46.75230  ?  134 ILE   A C    1 
ATOM   94   O  O    . ILE   A 1 29  ? 22.83600 1.86700   3.52200  1.000 45.28596  ?  134 ILE   A O    1 
ATOM   95   C  CB   . ILE   A 1 29  ? 24.50400 -0.32200  1.60000  1.000 44.51473  ?  134 ILE   A CB   1 
ATOM   96   C  CG1  . ILE   A 1 29  ? 24.74800 -0.55700  0.10700  1.000 48.21684  ?  134 ILE   A CG1  1 
ATOM   97   C  CG2  . ILE   A 1 29  ? 23.20700 -0.97500  2.06200  1.000 37.16388  ?  134 ILE   A CG2  1 
ATOM   98   C  CD1  . ILE   A 1 29  ? 24.23100 0.54000   -0.77900 1.000 55.21238  ?  134 ILE   A CD1  1 
ATOM   99   N  N    . LEU   A 1 30  ? 24.82200 1.19200   4.34700  1.000 42.38542  ?  135 LEU   A N    1 
ATOM   100  C  CA   . LEU   A 1 30  ? 24.39300 1.34900   5.73300  1.000 39.13498  ?  135 LEU   A CA   1 
ATOM   101  C  C    . LEU   A 1 30  ? 24.16500 2.81400   6.08400  1.000 36.97426  ?  135 LEU   A C    1 
ATOM   102  O  O    . LEU   A 1 30  ? 23.20500 3.14500   6.78900  1.000 38.03399  ?  135 LEU   A O    1 
ATOM   103  C  CB   . LEU   A 1 30  ? 25.42600 0.72200   6.67300  1.000 37.36038  ?  135 LEU   A CB   1 
ATOM   104  C  CG   . LEU   A 1 30  ? 25.55600 -0.79500  6.51700  1.000 36.85425  ?  135 LEU   A CG   1 
ATOM   105  C  CD1  . LEU   A 1 30  ? 26.55800 -1.36700  7.50500  1.000 40.44830  ?  135 LEU   A CD1  1 
ATOM   106  C  CD2  . LEU   A 1 30  ? 24.20200 -1.45300  6.68800  1.000 30.91413  ?  135 LEU   A CD2  1 
ATOM   107  N  N    . LEU   A 1 31  ? 25.03900 3.70500   5.61100  1.000 35.17530  ?  136 LEU   A N    1 
ATOM   108  C  CA   . LEU   A 1 31  ? 24.82000 5.13300   5.82500  1.000 40.30306  ?  136 LEU   A CA   1 
ATOM   109  C  C    . LEU   A 1 31  ? 23.47500 5.56800   5.25900  1.000 45.42455  ?  136 LEU   A C    1 
ATOM   110  O  O    . LEU   A 1 31  ? 22.70000 6.26300   5.92600  1.000 45.77312  ?  136 LEU   A O    1 
ATOM   111  C  CB   . LEU   A 1 31  ? 25.94700 5.93700   5.18400  1.000 42.53085  ?  136 LEU   A CB   1 
ATOM   112  C  CG   . LEU   A 1 31  ? 27.27900 5.98200   5.92400  1.000 39.43454  ?  136 LEU   A CG   1 
ATOM   113  C  CD1  . LEU   A 1 31  ? 28.33700 6.57400   5.01900  1.000 42.45631  ?  136 LEU   A CD1  1 
ATOM   114  C  CD2  . LEU   A 1 31  ? 27.14700 6.78500   7.21000  1.000 40.52951  ?  136 LEU   A CD2  1 
ATOM   115  N  N    . ASP   A 1 32  ? 23.18200 5.15500   4.02300  1.000 43.40826  ?  137 ASP   A N    1 
ATOM   116  C  CA   . ASP   A 1 32  ? 21.92200 5.51500   3.37800  1.000 44.08531  ?  137 ASP   A CA   1 
ATOM   117  C  C    . ASP   A 1 32  ? 20.73100 4.90800   4.10900  1.000 42.48726  ?  137 ASP   A C    1 
ATOM   118  O  O    . ASP   A 1 32  ? 19.71600 5.58400   4.32600  1.000 41.40150  ?  137 ASP   A O    1 
ATOM   119  C  CB   . ASP   A 1 32  ? 21.96000 5.06600   1.91600  1.000 45.94068  ?  137 ASP   A CB   1 
ATOM   120  C  CG   . ASP   A 1 32  ? 20.65000 5.30600   1.18400  1.000 51.51569  ?  137 ASP   A CG   1 
ATOM   121  O  OD1  . ASP   A 1 32  ? 20.29400 6.48300   0.94500  1.000 52.49009  ?  137 ASP   A OD1  1 
ATOM   122  O  OD2  . ASP   A 1 32  ? 19.98400 4.30700   0.83800  1.000 52.45150  ?  137 ASP   A OD2  1 
ATOM   123  N  N    . ALA   A 1 33  ? 20.83800 3.63400   4.49900  1.000 41.19833  ?  138 ALA   A N    1 
ATOM   124  C  CA   . ALA   A 1 33  ? 19.75100 2.98000   5.22100  1.000 38.84233  ?  138 ALA   A CA   1 
ATOM   125  C  C    . ALA   A 1 33  ? 19.41200 3.72700   6.50000  1.000 36.68623  ?  138 ALA   A C    1 
ATOM   126  O  O    . ALA   A 1 33  ? 18.23400 3.87100   6.85300  1.000 34.89563  ?  138 ALA   A O    1 
ATOM   127  C  CB   . ALA   A 1 33  ? 20.12800 1.53400   5.53500  1.000 42.52674  ?  138 ALA   A CB   1 
ATOM   128  N  N    . HIS   A 1 34  ? 20.43500 4.20200   7.21500  1.000 37.53802  ?  139 HIS   A N    1 
ATOM   129  C  CA   . HIS   A 1 34  ? 20.20400 4.96400   8.43600  1.000 36.03345  ?  139 HIS   A CA   1 
ATOM   130  C  C    . HIS   A 1 34  ? 19.45200 6.25600   8.14000  1.000 40.16883  ?  139 HIS   A C    1 
ATOM   131  O  O    . HIS   A 1 34  ? 18.46700 6.58500   8.81200  1.000 40.14743  ?  139 HIS   A O    1 
ATOM   132  C  CB   . HIS   A 1 34  ? 21.54000 5.26300   9.12300  1.000 37.11579  ?  139 HIS   A CB   1 
ATOM   133  C  CG   . HIS   A 1 34  ? 21.40200 6.03100   10.39900 1.000 37.28936  ?  139 HIS   A CG   1 
ATOM   134  N  ND1  . HIS   A 1 34  ? 20.64000 5.58200   11.45600 1.000 37.72502  ?  139 HIS   A ND1  1 
ATOM   135  C  CD2  . HIS   A 1 34  ? 21.90800 7.22700   10.78100 1.000 40.77551  ?  139 HIS   A CD2  1 
ATOM   136  C  CE1  . HIS   A 1 34  ? 20.69200 6.46300   12.43900 1.000 38.43536  ?  139 HIS   A CE1  1 
ATOM   137  N  NE2  . HIS   A 1 34  ? 21.45400 7.47100   12.05500 1.000 39.77712  ?  139 HIS   A NE2  1 
ATOM   138  N  N    . HIS   A 1 35  ? 19.89800 6.99700   7.12200  1.000 40.28974  ?  140 HIS   A N    1 
ATOM   139  C  CA   . HIS   A 1 35  ? 19.26700 8.27400   6.80300  1.000 44.56832  ?  140 HIS   A CA   1 
ATOM   140  C  C    . HIS   A 1 35  ? 17.82500 8.09300   6.35300  1.000 41.85620  ?  140 HIS   A C    1 
ATOM   141  O  O    . HIS   A 1 35  ? 17.01500 9.01300   6.49700  1.000 40.48966  ?  140 HIS   A O    1 
ATOM   142  C  CB   . HIS   A 1 35  ? 20.07100 9.00500   5.72800  1.000 47.95983  ?  140 HIS   A CB   1 
ATOM   143  C  CG   . HIS   A 1 35  ? 21.46200 9.35000   6.15600  1.000 58.06382  ?  140 HIS   A CG   1 
ATOM   144  N  ND1  . HIS   A 1 35  ? 22.52000 9.41700   5.27400  1.000 61.10965  ?  140 HIS   A ND1  1 
ATOM   145  C  CD2  . HIS   A 1 35  ? 21.97100 9.63600   7.37800  1.000 57.98028  ?  140 HIS   A CD2  1 
ATOM   146  C  CE1  . HIS   A 1 35  ? 23.61900 9.73400   5.93500  1.000 60.23548  ?  140 HIS   A CE1  1 
ATOM   147  N  NE2  . HIS   A 1 35  ? 23.31400 9.87300   7.21200  1.000 58.27855  ?  140 HIS   A NE2  1 
ATOM   148  N  N    . LYS   A 1 36  ? 17.48900 6.92100   5.81300  1.000 41.23985  ?  141 LYS   A N    1 
ATOM   149  C  CA   . LYS   A 1 36  ? 16.12300 6.63600   5.39400  1.000 42.03080  ?  141 LYS   A CA   1 
ATOM   150  C  C    . LYS   A 1 36  ? 15.25300 6.11900   6.53100  1.000 43.19646  ?  141 LYS   A C    1 
ATOM   151  O  O    . LYS   A 1 36  ? 14.02600 6.19300   6.43400  1.000 43.00435  ?  141 LYS   A O    1 
ATOM   152  C  CB   . LYS   A 1 36  ? 16.12600 5.61600   4.25400  1.000 41.59996  ?  141 LYS   A CB   1 
ATOM   153  C  CG   . LYS   A 1 36  ? 16.74300 6.13600   2.96600  1.000 43.14287  ?  141 LYS   A CG   1 
ATOM   154  C  CD   . LYS   A 1 36  ? 16.67600 5.10000   1.85800  1.000 50.77003  ?  141 LYS   A CD   1 
ATOM   155  C  CE   . LYS   A 1 36  ? 17.03500 5.72500   0.51700  1.000 56.93953  ?  141 LYS   A CE   1 
ATOM   156  N  NZ   . LYS   A 1 36  ? 16.89000 7.20900   0.55700  1.000 59.69907  ?  141 LYS   A NZ   1 
ATOM   157  N  N    . THR   A 1 37  ? 15.85300 5.59900   7.60100  1.000 43.14776  ?  142 THR   A N    1 
ATOM   158  C  CA   . THR   A 1 37  ? 15.10100 5.05000   8.71700  1.000 40.12990  ?  142 THR   A CA   1 
ATOM   159  C  C    . THR   A 1 37  ? 15.22600 5.86600   9.99500  1.000 41.73659  ?  142 THR   A C    1 
ATOM   160  O  O    . THR   A 1 37  ? 14.53300 5.56000   10.97100 1.000 47.21310  ?  142 THR   A O    1 
ATOM   161  C  CB   . THR   A 1 37  ? 15.54200 3.60600   9.00000  1.000 42.23965  ?  142 THR   A CB   1 
ATOM   162  O  OG1  . THR   A 1 37  ? 16.97200 3.55100   9.11100  1.000 43.38938  ?  142 THR   A OG1  1 
ATOM   163  C  CG2  . THR   A 1 37  ? 15.09000 2.68900   7.88000  1.000 41.36151  ?  142 THR   A CG2  1 
ATOM   164  N  N    . TYR   A 1 38  ? 16.08800 6.87800   10.02500 1.000 38.35001  ?  143 TYR   A N    1 
ATOM   165  C  CA   . TYR   A 1 38  ? 16.20100 7.77500   11.16600 1.000 40.31178  ?  143 TYR   A CA   1 
ATOM   166  C  C    . TYR   A 1 38  ? 15.85400 9.18300   10.71600 1.000 42.00005  ?  143 TYR   A C    1 
ATOM   167  O  O    . TYR   A 1 38  ? 16.46600 9.71300   9.78400  1.000 43.57354  ?  143 TYR   A O    1 
ATOM   168  C  CB   . TYR   A 1 38  ? 17.60600 7.75100   11.77900 1.000 41.18198  ?  143 TYR   A CB   1 
ATOM   169  C  CG   . TYR   A 1 38  ? 17.69200 8.44200   13.12600 1.000 40.83653  ?  143 TYR   A CG   1 
ATOM   170  C  CD1  . TYR   A 1 38  ? 17.80700 9.82400   13.21300 1.000 43.03423  ?  143 TYR   A CD1  1 
ATOM   171  C  CD2  . TYR   A 1 38  ? 17.66100 7.71400   14.31000 1.000 34.64561  ?  143 TYR   A CD2  1 
ATOM   172  C  CE1  . TYR   A 1 38  ? 17.88300 10.46100  14.43400 1.000 42.15402  ?  143 TYR   A CE1  1 
ATOM   173  C  CE2  . TYR   A 1 38  ? 17.74100 8.34500   15.54100 1.000 34.71288  ?  143 TYR   A CE2  1 
ATOM   174  C  CZ   . TYR   A 1 38  ? 17.85100 9.72000   15.59600 1.000 39.42893  ?  143 TYR   A CZ   1 
ATOM   175  O  OH   . TYR   A 1 38  ? 17.93300 10.36800  16.81000 1.000 42.52421  ?  143 TYR   A OH   1 
ATOM   176  N  N    . ASP   A 1 39  ? 14.88700 9.79100   11.39100 1.000 47.41728  ?  144 ASP   A N    1 
ATOM   177  C  CA   . ASP   A 1 39  ? 14.41100 11.12100  11.03400 1.000 48.28812  ?  144 ASP   A CA   1 
ATOM   178  C  C    . ASP   A 1 39  ? 14.82100 12.12400  12.10300 1.000 49.59028  ?  144 ASP   A C    1 
ATOM   179  O  O    . ASP   A 1 39  ? 14.17200 12.20400  13.15800 1.000 44.12117  ?  144 ASP   A O    1 
ATOM   180  C  CB   . ASP   A 1 39  ? 12.89200 11.10500  10.86400 1.000 51.53284  ?  144 ASP   A CB   1 
ATOM   181  C  CG   . ASP   A 1 39  ? 12.34800 12.43700  10.43600 1.000 56.67947  ?  144 ASP   A CG   1 
ATOM   182  O  OD1  . ASP   A 1 39  ? 13.14800 13.30800  10.03300 1.000 56.94667  ?  144 ASP   A OD1  1 
ATOM   183  O  OD2  . ASP   A 1 39  ? 11.11600 12.61900  10.50100 1.000 61.82648  ?  144 ASP   A OD2  1 
ATOM   184  N  N    . PRO   A 1 40  ? 15.87600 12.91800  11.88300 1.000 55.08607  ?  145 PRO   A N    1 
ATOM   185  C  CA   . PRO   A 1 40  ? 16.31600 13.86300  12.92200 1.000 55.18704  ?  145 PRO   A CA   1 
ATOM   186  C  C    . PRO   A 1 40  ? 15.37200 15.03700  13.12200 1.000 58.09658  ?  145 PRO   A C    1 
ATOM   187  O  O    . PRO   A 1 40  ? 15.59900 15.83700  14.03900 1.000 58.21754  ?  145 PRO   A O    1 
ATOM   188  C  CB   . PRO   A 1 40  ? 17.69000 14.32700  12.41600 1.000 54.60599  ?  145 PRO   A CB   1 
ATOM   189  C  CG   . PRO   A 1 40  ? 17.60500 14.18000  10.93300 1.000 57.14326  ?  145 PRO   A CG   1 
ATOM   190  C  CD   . PRO   A 1 40  ? 16.73100 12.97000  10.68300 1.000 57.61645  ?  145 PRO   A CD   1 
ATOM   191  N  N    . THR   A 1 41  ? 14.32700 15.17000  12.30000 1.000 57.63219  ?  146 THR   A N    1 
ATOM   192  C  CA   . THR   A 1 41  ? 13.31100 16.18300  12.55900 1.000 59.05223  ?  146 THR   A CA   1 
ATOM   193  C  C    . THR   A 1 41  ? 12.39200 15.78000  13.70200 1.000 56.47521  ?  146 THR   A C    1 
ATOM   194  O  O    . THR   A 1 41  ? 11.81500 16.65300  14.36000 1.000 58.57268  ?  146 THR   A O    1 
ATOM   195  C  CB   . THR   A 1 41  ? 12.46400 16.43900  11.31000 1.000 64.11511  ?  146 THR   A CB   1 
ATOM   196  O  OG1  . THR   A 1 41  ? 11.79300 15.23100  10.93700 1.000 64.84308  ?  146 THR   A OG1  1 
ATOM   197  C  CG2  . THR   A 1 41  ? 13.33000 16.91200  10.15300 1.000 65.93652  ?  146 THR   A CG2  1 
ATOM   198  N  N    . TYR   A 1 42  ? 12.23800 14.47400  13.94100 1.000 54.08213  ?  147 TYR   A N    1 
ATOM   199  C  CA   . TYR   A 1 42  ? 11.32200 13.95200  14.95700 1.000 53.43111  ?  147 TYR   A CA   1 
ATOM   200  C  C    . TYR   A 1 42  ? 9.89100  14.41800  14.70300 1.000 56.05259  ?  147 TYR   A C    1 
ATOM   201  O  O    . TYR   A 1 42  ? 9.12200  14.65100  15.63900 1.000 55.14977  ?  147 TYR   A O    1 
ATOM   202  C  CB   . TYR   A 1 42  ? 11.78700 14.33500  16.36800 1.000 56.66694  ?  147 TYR   A CB   1 
ATOM   203  C  CG   . TYR   A 1 42  ? 13.23700 13.97200  16.63300 1.000 58.34425  ?  147 TYR   A CG   1 
ATOM   204  C  CD1  . TYR   A 1 42  ? 13.62600 12.64500  16.76800 1.000 55.92149  ?  147 TYR   A CD1  1 
ATOM   205  C  CD2  . TYR   A 1 42  ? 14.21600 14.95300  16.72600 1.000 61.55310  ?  147 TYR   A CD2  1 
ATOM   206  C  CE1  . TYR   A 1 42  ? 14.94600 12.30600  17.00000 1.000 58.72177  ?  147 TYR   A CE1  1 
ATOM   207  C  CE2  . TYR   A 1 42  ? 15.54400 14.62200  16.95900 1.000 61.55621  ?  147 TYR   A CE2  1 
ATOM   208  C  CZ   . TYR   A 1 42  ? 15.90300 13.29600  17.09500 1.000 60.44671  ?  147 TYR   A CZ   1 
ATOM   209  O  OH   . TYR   A 1 42  ? 17.21900 12.95500  17.32600 1.000 59.00073  ?  147 TYR   A OH   1 
ATOM   210  N  N    . ALA   A 1 43  ? 9.52900  14.54800  13.42300 1.000 57.66620  ?  148 ALA   A N    1 
ATOM   211  C  CA   . ALA   A 1 43  ? 8.23300  15.11400  13.06400 1.000 58.49941  ?  148 ALA   A CA   1 
ATOM   212  C  C    . ALA   A 1 43  ? 7.08800  14.16200  13.37200 1.000 62.42417  ?  148 ALA   A C    1 
ATOM   213  O  O    . ALA   A 1 43  ? 5.95500  14.60900  13.57600 1.000 63.97373  ?  148 ALA   A O    1 
ATOM   214  C  CB   . ALA   A 1 43  ? 8.21600  15.49000  11.58400 1.000 56.70932  ?  148 ALA   A CB   1 
ATOM   215  N  N    . ASP   A 1 44  ? 7.35200  12.85700  13.40500 1.000 62.85810  ?  149 ASP   A N    1 
ATOM   216  C  CA   . ASP   A 1 44  ? 6.29300  11.88700  13.64900 1.000 63.09573  ?  149 ASP   A CA   1 
ATOM   217  C  C    . ASP   A 1 44  ? 5.89700  11.79200  15.11600 1.000 57.99377  ?  149 ASP   A C    1 
ATOM   218  O  O    . ASP   A 1 44  ? 4.89700  11.13400  15.42600 1.000 47.10653  ?  149 ASP   A O    1 
ATOM   219  C  CB   . ASP   A 1 44  ? 6.71800  10.50900  13.14100 1.000 64.18104  ?  149 ASP   A CB   1 
ATOM   220  C  CG   . ASP   A 1 44  ? 6.86600  10.46700  11.63200 1.000 69.21315  ?  149 ASP   A CG   1 
ATOM   221  O  OD1  . ASP   A 1 44  ? 6.14900  11.22500  10.94300 1.000 71.44426  ?  149 ASP   A OD1  1 
ATOM   222  O  OD2  . ASP   A 1 44  ? 7.70400  9.68300   11.13800 1.000 70.46651  ?  149 ASP   A OD2  1 
ATOM   223  N  N    . PHE   A 1 45  ? 6.64600  12.43600  16.01700 1.000 60.12059  ?  150 PHE   A N    1 
ATOM   224  C  CA   . PHE   A 1 45  ? 6.34100  12.36600  17.44200 1.000 62.21813  ?  150 PHE   A CA   1 
ATOM   225  C  C    . PHE   A 1 45  ? 4.98700  12.98400  17.78000 1.000 66.29983  ?  150 PHE   A C    1 
ATOM   226  O  O    . PHE   A 1 45  ? 4.42000  12.65700  18.82900 1.000 64.24609  ?  150 PHE   A O    1 
ATOM   227  C  CB   . PHE   A 1 45  ? 7.44500  13.05200  18.25400 1.000 61.88380  ?  150 PHE   A CB   1 
ATOM   228  C  CG   . PHE   A 1 45  ? 8.69400  12.21800  18.43300 1.000 60.42563  ?  150 PHE   A CG   1 
ATOM   229  C  CD1  . PHE   A 1 45  ? 9.29900  11.59800  17.35200 1.000 59.49826  ?  150 PHE   A CD1  1 
ATOM   230  C  CD2  . PHE   A 1 45  ? 9.26800  12.07000  19.68700 1.000 60.98494  ?  150 PHE   A CD2  1 
ATOM   231  C  CE1  . PHE   A 1 45  ? 10.44700 10.84100  17.51800 1.000 60.91004  ?  150 PHE   A CE1  1 
ATOM   232  C  CE2  . PHE   A 1 45  ? 10.42000 11.31300  19.86200 1.000 60.17398  ?  150 PHE   A CE2  1 
ATOM   233  C  CZ   . PHE   A 1 45  ? 11.01000 10.69900  18.77600 1.000 60.58902  ?  150 PHE   A CZ   1 
ATOM   234  N  N    A ARG   A 1 46  ? 4.46800  13.86400  16.92100 0.580 72.78218  ?  151 ARG   A N    1 
ATOM   235  N  N    B ARG   A 1 46  ? 4.46300  13.88000  16.93000 0.420 72.97864  ?  151 ARG   A N    1 
ATOM   236  C  CA   A ARG   A 1 46  ? 3.13700  14.42500  17.11800 0.580 78.01589  ?  151 ARG   A CA   1 
ATOM   237  C  CA   B ARG   A 1 46  ? 3.12800  14.43100  17.15500 0.420 77.99364  ?  151 ARG   A CA   1 
ATOM   238  C  C    A ARG   A 1 46  ? 2.05200  13.36200  17.05900 0.580 78.31058  ?  151 ARG   A C    1 
ATOM   239  C  C    B ARG   A 1 46  ? 2.04000  13.36600  17.05600 0.420 78.26245  ?  151 ARG   A C    1 
ATOM   240  O  O    A ARG   A 1 46  ? 0.96900  13.56200  17.61900 0.580 80.95387  ?  151 ARG   A O    1 
ATOM   241  O  O    B ARG   A 1 46  ? 0.94200  13.56700  17.58900 0.420 80.76041  ?  151 ARG   A O    1 
ATOM   242  C  CB   A ARG   A 1 46  ? 2.86000  15.49700  16.06000 0.580 82.14898  ?  151 ARG   A CB   1 
ATOM   243  C  CB   B ARG   A 1 46  ? 2.81000  15.55200  16.15200 0.420 82.27554  ?  151 ARG   A CB   1 
ATOM   244  C  CG   A ARG   A 1 46  ? 3.13700  15.02600  14.64100 0.580 83.37015  ?  151 ARG   A CG   1 
ATOM   245  C  CG   B ARG   A 1 46  ? 2.99200  17.01000  16.60900 0.420 86.87691  ?  151 ARG   A CG   1 
ATOM   246  C  CD   A ARG   A 1 46  ? 2.04800  15.41700  13.65800 0.580 85.93443  ?  151 ARG   A CD   1 
ATOM   247  C  CD   B ARG   A 1 46  ? 1.90000  17.51800  17.56500 0.420 89.60337  ?  151 ARG   A CD   1 
ATOM   248  N  NE   A ARG   A 1 46  ? 2.33800  14.91300  12.31800 0.580 87.43959  ?  151 ARG   A NE   1 
ATOM   249  N  NE   B ARG   A 1 46  ? 0.57900  17.21800  17.14600 0.420 91.10607  ?  151 ARG   A NE   1 
ATOM   250  C  CZ   A ARG   A 1 46  ? 3.10300  15.54100  11.43100 0.580 89.87574  ?  151 ARG   A CZ   1 
ATOM   251  C  CZ   B ARG   A 1 46  ? -0.21100 17.89400  16.31100 0.420 93.28954  ?  151 ARG   A CZ   1 
ATOM   252  N  NH1  A ARG   A 1 46  ? 3.65800  16.70500  11.73900 0.580 91.91167  ?  151 ARG   A NH1  1 
ATOM   253  N  NH1  B ARG   A 1 46  ? 0.16000  19.03600  15.74400 0.420 94.80643  ?  151 ARG   A NH1  1 
ATOM   254  N  NH2  A ARG   A 1 46  ? 3.31300  15.00700  10.23500 0.580 89.67221  ?  151 ARG   A NH2  1 
ATOM   255  N  NH2  B ARG   A 1 46  ? -1.44800 17.46000  16.07200 0.420 94.19583  ?  151 ARG   A NH2  1 
ATOM   256  N  N    . ASP   A 1 47  ? 2.31500  12.24000  16.39100 1.000 71.81537  ?  152 ASP   A N    1 
ATOM   257  C  CA   . ASP   A 1 47  ? 1.31800  11.18900  16.24900 1.000 64.70749  ?  152 ASP   A CA   1 
ATOM   258  C  C    . ASP   A 1 47  ? 1.22300  10.29700  17.47700 1.000 58.67042  ?  152 ASP   A C    1 
ATOM   259  O  O    . ASP   A 1 47  ? 0.21900  9.59500   17.63700 1.000 57.06917  ?  152 ASP   A O    1 
ATOM   260  C  CB   . ASP   A 1 47  ? 1.62600  10.34000  15.01400 1.000 64.02593  ?  152 ASP   A CB   1 
ATOM   261  C  CG   . ASP   A 1 47  ? 1.64700  11.15700  13.73700 1.000 68.28374  ?  152 ASP   A CG   1 
ATOM   262  O  OD1  . ASP   A 1 47  ? 2.35700  10.76500  12.78500 1.000 67.56306  ?  152 ASP   A OD1  1 
ATOM   263  O  OD2  . ASP   A 1 47  ? 0.95100  12.19400  13.68900 1.000 72.16185  ?  152 ASP   A OD2  1 
ATOM   264  N  N    . PHE   A 1 48  ? 2.23300  10.31000  18.34400 1.000 52.47460  ?  153 PHE   A N    1 
ATOM   265  C  CA   . PHE   A 1 48  ? 2.20400  9.47400   19.53400 1.000 50.10497  ?  153 PHE   A CA   1 
ATOM   266  C  C    . PHE   A 1 48  ? 1.16100  9.98500   20.52200 1.000 52.19383  ?  153 PHE   A C    1 
ATOM   267  O  O    . PHE   A 1 48  ? 0.72200  11.13600  20.46600 1.000 62.35284  ?  153 PHE   A O    1 
ATOM   268  C  CB   . PHE   A 1 48  ? 3.57300  9.44200   20.22600 1.000 49.50267  ?  153 PHE   A CB   1 
ATOM   269  C  CG   . PHE   A 1 48  ? 4.71800  9.05700   19.32600 1.000 48.12973  ?  153 PHE   A CG   1 
ATOM   270  C  CD1  . PHE   A 1 48  ? 4.50400  8.33700   18.16100 1.000 49.88562  ?  153 PHE   A CD1  1 
ATOM   271  C  CD2  . PHE   A 1 48  ? 6.01600  9.41100   19.66000 1.000 48.36834  ?  153 PHE   A CD2  1 
ATOM   272  C  CE1  . PHE   A 1 48  ? 5.55500  7.98600   17.34300 1.000 50.09556  ?  153 PHE   A CE1  1 
ATOM   273  C  CE2  . PHE   A 1 48  ? 7.07800  9.06000   18.84600 1.000 50.65105  ?  153 PHE   A CE2  1 
ATOM   274  C  CZ   . PHE   A 1 48  ? 6.84700  8.34700   17.68400 1.000 52.91009  ?  153 PHE   A CZ   1 
ATOM   275  N  N    . ARG   A 1 49  ? 0.76500  9.10500   21.43800 1.000 48.17235  ?  154 ARG   A N    1 
ATOM   276  C  CA   . ARG   A 1 49  ? -0.07300 9.52900   22.54600 1.000 53.29285  ?  154 ARG   A CA   1 
ATOM   277  C  C    . ARG   A 1 49  ? 0.68400  10.55300  23.39300 1.000 59.02462  ?  154 ARG   A C    1 
ATOM   278  O  O    . ARG   A 1 49  ? 1.90700  10.46600  23.53700 1.000 58.03433  ?  154 ARG   A O    1 
ATOM   279  C  CB   . ARG   A 1 49  ? -0.49000 8.32800   23.39300 1.000 54.63034  ?  154 ARG   A CB   1 
ATOM   280  C  CG   . ARG   A 1 49  ? -1.68600 7.57400   22.82000 1.000 55.45187  ?  154 ARG   A CG   1 
ATOM   281  C  CD   . ARG   A 1 49  ? -1.86800 6.22300   23.48700 1.000 52.77081  ?  154 ARG   A CD   1 
ATOM   282  N  NE   . ARG   A 1 49  ? -0.82400 5.27500   23.10900 1.000 51.63785  ?  154 ARG   A NE   1 
ATOM   283  C  CZ   . ARG   A 1 49  ? -0.56400 4.15400   23.77400 1.000 48.97303  ?  154 ARG   A CZ   1 
ATOM   284  N  NH1  . ARG   A 1 49  ? -1.27300 3.84300   24.85200 1.000 51.50901  ?  154 ARG   A NH1  1 
ATOM   285  N  NH2  . ARG   A 1 49  ? 0.39800  3.34400   23.36200 1.000 44.60437  ?  154 ARG   A NH2  1 
ATOM   286  N  N    . PRO   A 1 50  ? -0.01600 11.53600  23.95300 1.000 66.18806  ?  155 PRO   A N    1 
ATOM   287  C  CA   . PRO   A 1 50  ? 0.66400  12.69700  24.54500 1.000 68.25009  ?  155 PRO   A CA   1 
ATOM   288  C  C    . PRO   A 1 50  ? 1.47600  12.31200  25.76800 1.000 67.76488  ?  155 PRO   A C    1 
ATOM   289  O  O    . PRO   A 1 50  ? 1.05300  11.46600  26.57000 1.000 67.88272  ?  155 PRO   A O    1 
ATOM   290  C  CB   . PRO   A 1 50  ? -0.49700 13.63400  24.91600 1.000 75.16383  ?  155 PRO   A CB   1 
ATOM   291  C  CG   . PRO   A 1 50  ? -1.69100 12.73700  25.03900 1.000 74.59973  ?  155 PRO   A CG   1 
ATOM   292  C  CD   . PRO   A 1 50  ? -1.48500 11.65400  24.02400 1.000 68.29248  ?  155 PRO   A CD   1 
ATOM   293  N  N    . PRO   A 1 51  ? 2.65400  12.91200  25.94400 1.000 66.43927  ?  156 PRO   A N    1 
ATOM   294  C  CA   . PRO   A 1 51  ? 3.43800  12.64600  27.15500 1.000 66.04013  ?  156 PRO   A CA   1 
ATOM   295  C  C    . PRO   A 1 51  ? 2.76200  13.24700  28.37500 1.000 71.28377  ?  156 PRO   A C    1 
ATOM   296  O  O    . PRO   A 1 51  ? 2.27800  14.38100  28.34400 1.000 76.30689  ?  156 PRO   A O    1 
ATOM   297  C  CB   . PRO   A 1 51  ? 4.78900  13.32300  26.87600 1.000 62.05709  ?  156 PRO   A CB   1 
ATOM   298  C  CG   . PRO   A 1 51  ? 4.75100  13.76700  25.44900 1.000 64.37578  ?  156 PRO   A CG   1 
ATOM   299  C  CD   . PRO   A 1 51  ? 3.30900  13.88900  25.06100 1.000 66.70107  ?  156 PRO   A CD   1 
ATOM   300  N  N    . VAL   A 1 52  ? 2.72400  12.47000  29.45300 1.000 71.55026  ?  157 VAL   A N    1 
ATOM   301  C  CA   . VAL   A 1 52  ? 2.13800  12.89800  30.71800 1.000 74.79970  ?  157 VAL   A CA   1 
ATOM   302  C  C    . VAL   A 1 52  ? 3.22200  12.80200  31.78100 1.000 77.74589  ?  157 VAL   A C    1 
ATOM   303  O  O    . VAL   A 1 52  ? 3.65700  11.69900  32.13700 1.000 77.88583  ?  157 VAL   A O    1 
ATOM   304  C  CB   . VAL   A 1 52  ? 0.91200  12.05700  31.10200 1.000 72.63007  ?  157 VAL   A CB   1 
ATOM   305  C  CG1  . VAL   A 1 52  ? 0.05600  12.80300  32.11500 1.000 72.95150  ?  157 VAL   A CG1  1 
ATOM   306  C  CG2  . VAL   A 1 52  ? 0.09600  11.70400  29.86700 1.000 70.16422  ?  157 VAL   A CG2  1 
ATOM   307  N  N    . ARG   A 1 53  ? 3.66800  13.95000  32.28100 1.000 81.37335  ?  158 ARG   A N    1 
ATOM   308  C  CA   . ARG   A 1 53  ? 4.64000  14.01700  33.36200 1.000 82.86311  ?  158 ARG   A CA   1 
ATOM   309  C  C    . ARG   A 1 53  ? 3.98500  14.63500  34.58900 1.000 91.28193  ?  158 ARG   A C    1 
ATOM   310  O  O    . ARG   A 1 53  ? 3.24000  15.61300  34.47800 1.000 94.88718  ?  158 ARG   A O    1 
ATOM   311  C  CB   . ARG   A 1 53  ? 5.87400  14.83200  32.95500 1.000 79.23476  ?  158 ARG   A CB   1 
ATOM   312  C  CG   . ARG   A 1 53  ? 6.68600  14.22600  31.81400 1.000 74.09807  ?  158 ARG   A CG   1 
ATOM   313  C  CD   . ARG   A 1 53  ? 7.53600  15.28100  31.11800 1.000 73.59103  ?  158 ARG   A CD   1 
ATOM   314  N  NE   . ARG   A 1 53  ? 8.44200  14.70600  30.12500 1.000 70.29633  ?  158 ARG   A NE   1 
ATOM   315  C  CZ   . ARG   A 1 53  ? 8.26800  14.80300  28.81000 1.000 70.92715  ?  158 ARG   A CZ   1 
ATOM   316  N  NH1  . ARG   A 1 53  ? 7.21600  15.44800  28.32300 1.000 70.39046  ?  158 ARG   A NH1  1 
ATOM   317  N  NH2  . ARG   A 1 53  ? 9.14200  14.24900  27.98000 1.000 69.11008  ?  158 ARG   A NH2  1 
ATOM   318  N  N    . MET   A 1 54  ? 4.26100  14.05700  35.75500 1.000 95.66753  ?  159 MET   A N    1 
ATOM   319  C  CA   . MET   A 1 54  ? 3.66300  14.52000  37.00600 1.000 102.31274 ?  159 MET   A CA   1 
ATOM   320  C  C    . MET   A 1 54  ? 3.99700  15.98300  37.29000 1.000 104.10623 ?  159 MET   A C    1 
ATOM   321  O  O    . MET   A 1 54  ? 3.13900  16.85900  37.17900 1.000 105.45138 ?  159 MET   A O    1 
ATOM   322  C  CB   . MET   A 1 54  ? 4.12600  13.65200  38.17600 1.000 105.61308 ?  159 MET   A CB   1 
ATOM   323  C  CG   . MET   A 1 54  ? 3.53400  14.06500  39.51200 1.000 112.46912 ?  159 MET   A CG   1 
ATOM   324  S  SD   . MET   A 1 54  ? 4.43300  13.38100  40.91600 1.000 115.24350 ?  159 MET   A SD   1 
ATOM   325  C  CE   . MET   A 1 54  ? 4.22200  14.68900  42.12200 1.000 119.95325 ?  159 MET   A CE   1 
ATOM   326  N  N    . SER   A 1 66  ? 4.07100  7.56300   41.49700 1.000 116.90005 ?  218 SER   A N    1 
ATOM   327  C  CA   . SER   A 1 66  ? 2.70700  7.06800   41.64000 1.000 117.25836 ?  218 SER   A CA   1 
ATOM   328  C  C    . SER   A 1 66  ? 2.24500  6.41700   40.29700 1.000 111.96069 ?  218 SER   A C    1 
ATOM   329  O  O    . SER   A 1 66  ? 2.50000  5.22400   40.11800 1.000 110.16247 ?  218 SER   A O    1 
ATOM   330  C  CB   . SER   A 1 66  ? 1.79500  8.19200   42.16800 1.000 121.05695 ?  218 SER   A CB   1 
ATOM   331  O  OG   . SER   A 1 66  ? 0.48700  7.73400   42.46000 1.000 123.55188 ?  218 SER   A OG   1 
ATOM   332  N  N    . PRO   A 1 67  ? 1.62700  7.12800   39.34100 1.000 106.98032 ?  219 PRO   A N    1 
ATOM   333  C  CA   . PRO   A 1 67  ? 1.19000  6.41200   38.14200 1.000 99.14744  ?  219 PRO   A CA   1 
ATOM   334  C  C    . PRO   A 1 67  ? 2.29300  6.33600   37.09700 1.000 90.53818  ?  219 PRO   A C    1 
ATOM   335  O  O    . PRO   A 1 67  ? 3.20100  7.16900   37.03600 1.000 90.04830  ?  219 PRO   A O    1 
ATOM   336  C  CB   . PRO   A 1 67  ? 0.01600  7.26800   37.65300 1.000 99.84738  ?  219 PRO   A CB   1 
ATOM   337  C  CG   . PRO   A 1 67  ? 0.50100  8.63600   37.89600 1.000 103.06334 ?  219 PRO   A CG   1 
ATOM   338  C  CD   . PRO   A 1 67  ? 1.36800  8.57500   39.15200 1.000 107.42019 ?  219 PRO   A CD   1 
ATOM   339  N  N    . LEU   A 1 68  ? 2.20700  5.29500   36.26500 1.000 79.62614  ?  220 LEU   A N    1 
ATOM   340  C  CA   . LEU   A 1 68  ? 3.12800  5.12100   35.14200 1.000 68.03279  ?  220 LEU   A CA   1 
ATOM   341  C  C    . LEU   A 1 68  ? 2.64300  5.98100   33.97400 1.000 61.14315  ?  220 LEU   A C    1 
ATOM   342  O  O    . LEU   A 1 68  ? 2.20800  5.49900   32.92700 1.000 59.96740  ?  220 LEU   A O    1 
ATOM   343  C  CB   . LEU   A 1 68  ? 3.23800  3.65200   34.76100 1.000 64.52285  ?  220 LEU   A CB   1 
ATOM   344  C  CG   . LEU   A 1 68  ? 3.77000  2.71000   35.84100 1.000 66.56633  ?  220 LEU   A CG   1 
ATOM   345  C  CD1  . LEU   A 1 68  ? 4.09600  1.35800   35.23500 1.000 66.08220  ?  220 LEU   A CD1  1 
ATOM   346  C  CD2  . LEU   A 1 68  ? 4.99300  3.30400   36.53600 1.000 64.55924  ?  220 LEU   A CD2  1 
ATOM   347  N  N    . SER   A 1 69  ? 2.74000  7.29500   34.17700 1.000 61.55659  ?  221 SER   A N    1 
ATOM   348  C  CA   . SER   A 1 69  ? 2.10300  8.26000   33.29100 1.000 63.20699  ?  221 SER   A CA   1 
ATOM   349  C  C    . SER   A 1 69  ? 2.78200  8.37600   31.93400 1.000 60.79786  ?  221 SER   A C    1 
ATOM   350  O  O    . SER   A 1 69  ? 2.14100  8.81900   30.97500 1.000 60.83074  ?  221 SER   A O    1 
ATOM   351  C  CB   . SER   A 1 69  ? 2.07000  9.63400   33.96000 1.000 68.12315  ?  221 SER   A CB   1 
ATOM   352  O  OG   . SER   A 1 69  ? 3.36200  10.01400  34.40000 1.000 69.81203  ?  221 SER   A OG   1 
ATOM   353  N  N    . MET   A 1 70  ? 4.05500  8.01200   31.83000 1.000 55.91139  ?  222 MET   A N    1 
ATOM   354  C  CA   . MET   A 1 70  ? 4.76800  8.10100   30.56300 1.000 55.05304  ?  222 MET   A CA   1 
ATOM   355  C  C    . MET   A 1 70  ? 4.61700  6.85100   29.70800 1.000 48.31571  ?  222 MET   A C    1 
ATOM   356  O  O    . MET   A 1 70  ? 5.12900  6.82200   28.58600 1.000 50.51081  ?  222 MET   A O    1 
ATOM   357  C  CB   . MET   A 1 70  ? 6.26000  8.37300   30.80800 1.000 56.89527  ?  222 MET   A CB   1 
ATOM   358  C  CG   . MET   A 1 70  ? 6.61500  9.83700   31.02900 1.000 58.03833  ?  222 MET   A CG   1 
ATOM   359  S  SD   . MET   A 1 70  ? 5.92500  10.91800  29.76100 1.000 59.33865  ?  222 MET   A SD   1 
ATOM   360  C  CE   . MET   A 1 70  ? 7.40600  11.58100  29.01900 1.000 59.53594  ?  222 MET   A CE   1 
ATOM   361  N  N    . LEU   A 1 71  ? 3.93300  5.82300   30.20700 1.000 46.83818  ?  223 LEU   A N    1 
ATOM   362  C  CA   . LEU   A 1 71  ? 3.87100  4.55700   29.47900 1.000 45.41645  ?  223 LEU   A CA   1 
ATOM   363  C  C    . LEU   A 1 71  ? 3.14500  4.67100   28.14200 1.000 43.92426  ?  223 LEU   A C    1 
ATOM   364  O  O    . LEU   A 1 71  ? 3.65400  4.12600   27.14700 1.000 42.08193  ?  223 LEU   A O    1 
ATOM   365  C  CB   . LEU   A 1 71  ? 3.24200  3.47900   30.36800 1.000 49.04449  ?  223 LEU   A CB   1 
ATOM   366  C  CG   . LEU   A 1 71  ? 3.18200  2.07600   29.76000 1.000 48.10389  ?  223 LEU   A CG   1 
ATOM   367  C  CD1  . LEU   A 1 71  ? 4.51900  1.69500   29.14800 1.000 46.90349  ?  223 LEU   A CD1  1 
ATOM   368  C  CD2  . LEU   A 1 71  ? 2.75600  1.05000   30.79800 1.000 49.21702  ?  223 LEU   A CD2  1 
ATOM   369  N  N    . PRO   A 1 72  ? 1.98600  5.33200   28.02900 1.000 45.81453  ?  224 PRO   A N    1 
ATOM   370  C  CA   . PRO   A 1 72  ? 1.37600  5.45200   26.68900 1.000 47.68813  ?  224 PRO   A CA   1 
ATOM   371  C  C    . PRO   A 1 72  ? 2.29800  6.11400   25.67600 1.000 45.74371  ?  224 PRO   A C    1 
ATOM   372  O  O    . PRO   A 1 72  ? 2.52200  5.56200   24.59100 1.000 43.60700  ?  224 PRO   A O    1 
ATOM   373  C  CB   . PRO   A 1 72  ? 0.10600  6.27300   26.95700 1.000 50.21866  ?  224 PRO   A CB   1 
ATOM   374  C  CG   . PRO   A 1 72  ? -0.21500 6.00700   28.38300 1.000 49.83837  ?  224 PRO   A CG   1 
ATOM   375  C  CD   . PRO   A 1 72  ? 1.11100  5.89700   29.07200 1.000 44.43878  ?  224 PRO   A CD   1 
ATOM   376  N  N    . HIS   A 1 73  ? 2.88000  7.26600   26.02100 1.000 48.10208  ?  225 HIS   A N    1 
ATOM   377  C  CA   . HIS   A 1 73  ? 3.72300  7.97400   25.06400 1.000 48.91319  ?  225 HIS   A CA   1 
ATOM   378  C  C    . HIS   A 1 73  ? 4.98100  7.18100   24.72400 1.000 47.59091  ?  225 HIS   A C    1 
ATOM   379  O  O    . HIS   A 1 73  ? 5.40200  7.14300   23.56100 1.000 47.30138  ?  225 HIS   A O    1 
ATOM   380  C  CB   . HIS   A 1 73  ? 4.10100  9.34900   25.60500 1.000 48.55920  ?  225 HIS   A CB   1 
ATOM   381  C  CG   . HIS   A 1 73  ? 5.11600  10.05900  24.76500 1.000 50.23173  ?  225 HIS   A CG   1 
ATOM   382  N  ND1  . HIS   A 1 73  ? 4.77700  10.77200  23.63500 1.000 51.38139  ?  225 HIS   A ND1  1 
ATOM   383  C  CD2  . HIS   A 1 73  ? 6.46200  10.15400  24.88100 1.000 49.16879  ?  225 HIS   A CD2  1 
ATOM   384  C  CE1  . HIS   A 1 73  ? 5.87100  11.28200  23.09500 1.000 50.93210  ?  225 HIS   A CE1  1 
ATOM   385  N  NE2  . HIS   A 1 73  ? 6.90600  10.92000  23.83000 1.000 47.98134  ?  225 HIS   A NE2  1 
ATOM   386  N  N    . LEU   A 1 74  ? 5.60300  6.55000   25.71800 1.000 45.58353  ?  226 LEU   A N    1 
ATOM   387  C  CA   . LEU   A 1 74  ? 6.84600  5.84200   25.44700 1.000 44.17067  ?  226 LEU   A CA   1 
ATOM   388  C  C    . LEU   A 1 74  ? 6.59900  4.51800   24.74100 1.000 44.34225  ?  226 LEU   A C    1 
ATOM   389  O  O    . LEU   A 1 74  ? 7.44600  4.07500   23.95600 1.000 40.21743  ?  226 LEU   A O    1 
ATOM   390  C  CB   . LEU   A 1 74  ? 7.62400  5.63700   26.74600 1.000 47.18749  ?  226 LEU   A CB   1 
ATOM   391  C  CG   . LEU   A 1 74  ? 8.10800  6.95600   27.36000 1.000 51.59889  ?  226 LEU   A CG   1 
ATOM   392  C  CD1  . LEU   A 1 74  ? 8.82300  6.72300   28.68100 1.000 50.53220  ?  226 LEU   A CD1  1 
ATOM   393  C  CD2  . LEU   A 1 74  ? 8.99800  7.72600   26.38000 1.000 47.53689  ?  226 LEU   A CD2  1 
ATOM   394  N  N    . ALA   A 1 75  ? 5.44700  3.88700   24.98900 1.000 46.22475  ?  227 ALA   A N    1 
ATOM   395  C  CA   . ALA   A 1 75  ? 5.06800  2.70800   24.21500 1.000 43.10707  ?  227 ALA   A CA   1 
ATOM   396  C  C    . ALA   A 1 75  ? 4.99700  3.03700   22.73000 1.000 44.59400  ?  227 ALA   A C    1 
ATOM   397  O  O    . ALA   A 1 75  ? 5.55100  2.31200   21.89300 1.000 41.42273  ?  227 ALA   A O    1 
ATOM   398  C  CB   . ALA   A 1 75  ? 3.72900  2.15600   24.70800 1.000 39.12966  ?  227 ALA   A CB   1 
ATOM   399  N  N    . ASP   A 1 76  ? 4.32600  4.14300   22.38800 1.000 44.29196  ?  228 ASP   A N    1 
ATOM   400  C  CA   . ASP   A 1 76  ? 4.27100  4.58000   20.99600 1.000 44.25841  ?  228 ASP   A CA   1 
ATOM   401  C  C    . ASP   A 1 76  ? 5.66000  4.93200   20.46900 1.000 44.90670  ?  228 ASP   A C    1 
ATOM   402  O  O    . ASP   A 1 76  ? 5.98800  4.63000   19.31500 1.000 43.30579  ?  228 ASP   A O    1 
ATOM   403  C  CB   . ASP   A 1 76  ? 3.32700  5.77400   20.85800 1.000 44.11704  ?  228 ASP   A CB   1 
ATOM   404  C  CG   . ASP   A 1 76  ? 1.86800  5.39100   21.04300 1.000 48.20361  ?  228 ASP   A CG   1 
ATOM   405  O  OD1  . ASP   A 1 76  ? 1.53200  4.19700   20.88900 1.000 46.92796  ?  228 ASP   A OD1  1 
ATOM   406  O  OD2  . ASP   A 1 76  ? 1.05600  6.29100   21.34100 1.000 51.50061  ?  228 ASP   A OD2  1 
ATOM   407  N  N    . LEU   A 1 77  ? 6.48700  5.57900   21.29700 1.000 45.61107  ?  229 LEU   A N    1 
ATOM   408  C  CA   . LEU   A 1 77  ? 7.86100  5.87600   20.89100 1.000 42.35433  ?  229 LEU   A CA   1 
ATOM   409  C  C    . LEU   A 1 77  ? 8.61500  4.59600   20.55600 1.000 38.70840  ?  229 LEU   A C    1 
ATOM   410  O  O    . LEU   A 1 77  ? 9.19900  4.47000   19.47400 1.000 38.94712  ?  229 LEU   A O    1 
ATOM   411  C  CB   . LEU   A 1 77  ? 8.58000  6.65600   21.99200 1.000 39.24503  ?  229 LEU   A CB   1 
ATOM   412  C  CG   . LEU   A 1 77  ? 10.09400 6.86500   21.85100 1.000 42.73844  ?  229 LEU   A CG   1 
ATOM   413  C  CD1  . LEU   A 1 77  ? 10.44900 7.54300   20.52800 1.000 43.60904  ?  229 LEU   A CD1  1 
ATOM   414  C  CD2  . LEU   A 1 77  ? 10.62300 7.67500   23.02000 1.000 44.36256  ?  229 LEU   A CD2  1 
ATOM   415  N  N    . VAL   A 1 78  ? 8.59200  3.62500   21.47000 1.000 38.20436  ?  230 VAL   A N    1 
ATOM   416  C  CA   . VAL   A 1 78  ? 9.26500  2.35000   21.23700 1.000 35.39360  ?  230 VAL   A CA   1 
ATOM   417  C  C    . VAL   A 1 78  ? 8.72300  1.67200   19.98400 1.000 39.72872  ?  230 VAL   A C    1 
ATOM   418  O  O    . VAL   A 1 78  ? 9.48800  1.23000   19.11800 1.000 38.88194  ?  230 VAL   A O    1 
ATOM   419  C  CB   . VAL   A 1 78  ? 9.12500  1.44600   22.47100 1.000 37.15654  ?  230 VAL   A CB   1 
ATOM   420  C  CG1  . VAL   A 1 78  ? 9.60900  0.04500   22.15400 1.000 38.43053  ?  230 VAL   A CG1  1 
ATOM   421  C  CG2  . VAL   A 1 78  ? 9.91400  2.03700   23.62500 1.000 40.73343  ?  230 VAL   A CG2  1 
ATOM   422  N  N    . SER   A 1 79  ? 7.39200  1.58100   19.87100 1.000 43.57604  ?  231 SER   A N    1 
ATOM   423  C  CA   . SER   A 1 79  ? 6.77600  0.93300   18.71400 1.000 40.16337  ?  231 SER   A CA   1 
ATOM   424  C  C    . SER   A 1 79  ? 7.23600  1.56700   17.40800 1.000 39.61489  ?  231 SER   A C    1 
ATOM   425  O  O    . SER   A 1 79  ? 7.51700  0.86400   16.43100 1.000 42.78277  ?  231 SER   A O    1 
ATOM   426  C  CB   . SER   A 1 79  ? 5.25500  1.00100   18.83000 1.000 38.92215  ?  231 SER   A CB   1 
ATOM   427  O  OG   . SER   A 1 79  ? 4.63700  -0.06400  18.12800 1.000 41.59651  ?  231 SER   A OG   1 
ATOM   428  N  N    . TYR   A 1 80  ? 7.31600  2.89800   17.37800 1.000 38.04396  ?  232 TYR   A N    1 
ATOM   429  C  CA   . TYR   A 1 80  ? 7.78400  3.61500   16.19600 1.000 36.99500  ?  232 TYR   A CA   1 
ATOM   430  C  C    . TYR   A 1 80  ? 9.21400  3.21900   15.83300 1.000 38.29016  ?  232 TYR   A C    1 
ATOM   431  O  O    . TYR   A 1 80  ? 9.51600  2.93300   14.66700 1.000 34.09648  ?  232 TYR   A O    1 
ATOM   432  C  CB   . TYR   A 1 80  ? 7.67200  5.11700   16.46000 1.000 40.66766  ?  232 TYR   A CB   1 
ATOM   433  C  CG   . TYR   A 1 80  ? 8.20800  6.02700   15.37900 1.000 48.05087  ?  232 TYR   A CG   1 
ATOM   434  C  CD1  . TYR   A 1 80  ? 7.47500  6.28700   14.22800 1.000 46.89917  ?  232 TYR   A CD1  1 
ATOM   435  C  CD2  . TYR   A 1 80  ? 9.44200  6.64700   15.52400 1.000 49.19897  ?  232 TYR   A CD2  1 
ATOM   436  C  CE1  . TYR   A 1 80  ? 7.96700  7.13400   13.24700 1.000 50.53974  ?  232 TYR   A CE1  1 
ATOM   437  C  CE2  . TYR   A 1 80  ? 9.94000  7.49200   14.55300 1.000 50.02097  ?  232 TYR   A CE2  1 
ATOM   438  C  CZ   . TYR   A 1 80  ? 9.20200  7.73300   13.41700 1.000 53.33403  ?  232 TYR   A CZ   1 
ATOM   439  O  OH   . TYR   A 1 80  ? 9.70900  8.57700   12.45600 1.000 56.76945  ?  232 TYR   A OH   1 
ATOM   440  N  N    . SER   A 1 81  ? 10.11300 3.18400   16.82300 1.000 37.75345  ?  233 SER   A N    1 
ATOM   441  C  CA   . SER   A 1 81  ? 11.50900 2.86600   16.52200 1.000 41.33916  ?  233 SER   A CA   1 
ATOM   442  C  C    . SER   A 1 81  ? 11.71000 1.40200   16.16700 1.000 38.66914  ?  233 SER   A C    1 
ATOM   443  O  O    . SER   A 1 81  ? 12.59900 1.09000   15.36900 1.000 37.92324  ?  233 SER   A O    1 
ATOM   444  C  CB   . SER   A 1 81  ? 12.41900 3.24600   17.68500 1.000 51.50787  ?  233 SER   A CB   1 
ATOM   445  O  OG   . SER   A 1 81  ? 12.35300 4.64200   17.89600 1.000 61.23406  ?  233 SER   A OG   1 
ATOM   446  N  N    . ILE   A 1 82  ? 10.91600 0.49200   16.73500 1.000 35.05242  ?  234 ILE   A N    1 
ATOM   447  C  CA   . ILE   A 1 82  ? 10.97100 -0.88800  16.26300 1.000 35.79405  ?  234 ILE   A CA   1 
ATOM   448  C  C    . ILE   A 1 82  ? 10.72500 -0.93500  14.75700 1.000 40.95791  ?  234 ILE   A C    1 
ATOM   449  O  O    . ILE   A 1 82  ? 11.45000 -1.61500  14.02000 1.000 44.41363  ?  234 ILE   A O    1 
ATOM   450  C  CB   . ILE   A 1 82  ? 9.97900  -1.77000  17.04500 1.000 38.48049  ?  234 ILE   A CB   1 
ATOM   451  C  CG1  . ILE   A 1 82  ? 10.34400 -1.80200  18.53600 1.000 38.48819  ?  234 ILE   A CG1  1 
ATOM   452  C  CG2  . ILE   A 1 82  ? 9.95200  -3.18300  16.48000 1.000 40.23582  ?  234 ILE   A CG2  1 
ATOM   453  C  CD1  . ILE   A 1 82  ? 9.38700  -2.62000  19.39900 1.000 37.83256  ?  234 ILE   A CD1  1 
ATOM   454  N  N    . GLN   A 1 83  ? 9.73600  -0.17400  14.27200 1.000 36.32182  ?  235 GLN   A N    1 
ATOM   455  C  CA   . GLN   A 1 83  ? 9.48800  -0.10000  12.83300 1.000 38.16588  ?  235 GLN   A CA   1 
ATOM   456  C  C    . GLN   A 1 83  ? 10.71200 0.42000   12.09500 1.000 37.40622  ?  235 GLN   A C    1 
ATOM   457  O  O    . GLN   A 1 83  ? 11.12300 -0.13900  11.07100 1.000 30.51645  ?  235 GLN   A O    1 
ATOM   458  C  CB   . GLN   A 1 83  ? 8.28200  0.79800   12.55200 1.000 40.49250  ?  235 GLN   A CB   1 
ATOM   459  C  CG   . GLN   A 1 83  ? 6.97200  0.25200   13.06300 1.000 39.88868  ?  235 GLN   A CG   1 
ATOM   460  C  CD   . GLN   A 1 83  ? 5.78600  1.01900   12.52100 1.000 48.67195  ?  235 GLN   A CD   1 
ATOM   461  O  OE1  . GLN   A 1 83  ? 5.43700  0.89000   11.34900 1.000 46.74737  ?  235 GLN   A OE1  1 
ATOM   462  N  NE2  . GLN   A 1 83  ? 5.15800  1.82500   13.37300 1.000 52.64782  ?  235 GLN   A NE2  1 
ATOM   463  N  N    . LYS   A 1 84  ? 11.31300 1.49300   12.61200 1.000 41.94484  ?  236 LYS   A N    1 
ATOM   464  C  CA   . LYS   A 1 84  ? 12.52300 2.03400   12.00700 1.000 37.07428  ?  236 LYS   A CA   1 
ATOM   465  C  C    . LYS   A 1 84  ? 13.65600 1.01800   12.03700 1.000 35.54838  ?  236 LYS   A C    1 
ATOM   466  O  O    . LYS   A 1 84  ? 14.41900 0.89900   11.07000 1.000 35.80785  ?  236 LYS   A O    1 
ATOM   467  C  CB   . LYS   A 1 84  ? 12.92800 3.31800   12.72600 1.000 36.96036  ?  236 LYS   A CB   1 
ATOM   468  C  CG   . LYS   A 1 84  ? 11.90000 4.43300   12.61800 1.000 39.69233  ?  236 LYS   A CG   1 
ATOM   469  C  CD   . LYS   A 1 84  ? 11.48100 4.64800   11.17400 1.000 40.32223  ?  236 LYS   A CD   1 
ATOM   470  C  CE   . LYS   A 1 84  ? 10.84700 6.01200   10.97600 1.000 46.78286  ?  236 LYS   A CE   1 
ATOM   471  N  NZ   . LYS   A 1 84  ? 11.74900 7.13200   11.35100 1.000 50.00989  ?  236 LYS   A NZ   1 
ATOM   472  N  N    . VAL   A 1 85  ? 13.78400 0.27600   13.13900 1.000 35.93177  ?  237 VAL   A N    1 
ATOM   473  C  CA   . VAL   A 1 85  ? 14.85900 -0.70500  13.24600 1.000 37.60259  ?  237 VAL   A CA   1 
ATOM   474  C  C    . VAL   A 1 85  ? 14.67500 -1.81300  12.21800 1.000 36.59035  ?  237 VAL   A C    1 
ATOM   475  O  O    . VAL   A 1 85  ? 15.63300 -2.22200  11.55000 1.000 35.14571  ?  237 VAL   A O    1 
ATOM   476  C  CB   . VAL   A 1 85  ? 14.93500 -1.26100  14.67900 1.000 32.18646  ?  237 VAL   A CB   1 
ATOM   477  C  CG1  . VAL   A 1 85  ? 15.80500 -2.50500  14.71800 1.000 34.23614  ?  237 VAL   A CG1  1 
ATOM   478  C  CG2  . VAL   A 1 85  ? 15.48100 -0.20600  15.61200 1.000 32.40294  ?  237 VAL   A CG2  1 
ATOM   479  N  N    . ILE   A 1 86  ? 13.44300 -2.30600  12.06900 1.000 33.81007  ?  238 ILE   A N    1 
ATOM   480  C  CA   . ILE   A 1 86  ? 13.14000 -3.29900  11.03900 1.000 34.27974  ?  238 ILE   A CA   1 
ATOM   481  C  C    . ILE   A 1 86  ? 13.51800 -2.77400  9.66200  1.000 33.08979  ?  238 ILE   A C    1 
ATOM   482  O  O    . ILE   A 1 86  ? 14.11300 -3.49200  8.84900  1.000 38.26033  ?  238 ILE   A O    1 
ATOM   483  C  CB   . ILE   A 1 86  ? 11.64900 -3.68900  11.09600 1.000 37.68203  ?  238 ILE   A CB   1 
ATOM   484  C  CG1  . ILE   A 1 86  ? 11.30600 -4.31900  12.44900 1.000 37.31837  ?  238 ILE   A CG1  1 
ATOM   485  C  CG2  . ILE   A 1 86  ? 11.28600 -4.63400  9.93800  1.000 38.40420  ?  238 ILE   A CG2  1 
ATOM   486  C  CD1  . ILE   A 1 86  ? 9.81300  -4.33400  12.75500 1.000 37.35161  ?  238 ILE   A CD1  1 
ATOM   487  N  N    . GLY   A 1 87  ? 13.17200 -1.51700  9.37400  1.000 31.65966  ?  239 GLY   A N    1 
ATOM   488  C  CA   . GLY   A 1 87  ? 13.48400 -0.95700  8.07100  1.000 32.28118  ?  239 GLY   A CA   1 
ATOM   489  C  C    . GLY   A 1 87  ? 14.97600 -0.89400  7.81900  1.000 36.13227  ?  239 GLY   A C    1 
ATOM   490  O  O    . GLY   A 1 87  ? 15.44700 -1.20500  6.72000  1.000 37.28925  ?  239 GLY   A O    1 
ATOM   491  N  N    . PHE   A 1 88  ? 15.73900 -0.49800  8.83800  1.000 33.51746  ?  240 PHE   A N    1 
ATOM   492  C  CA   . PHE   A 1 88  ? 17.19500 -0.50900  8.73400  1.000 33.74617  ?  240 PHE   A CA   1 
ATOM   493  C  C    . PHE   A 1 88  ? 17.70800 -1.91700  8.47100  1.000 35.35523  ?  240 PHE   A C    1 
ATOM   494  O  O    . PHE   A 1 88  ? 18.47900 -2.14200  7.53000  1.000 34.41657  ?  240 PHE   A O    1 
ATOM   495  C  CB   . PHE   A 1 88  ? 17.80100 0.05500   10.01600 1.000 31.36638  ?  240 PHE   A CB   1 
ATOM   496  C  CG   . PHE   A 1 88  ? 19.30100 -0.00300  10.06300 1.000 35.90359  ?  240 PHE   A CG   1 
ATOM   497  C  CD1  . PHE   A 1 88  ? 20.06000 0.97600   9.44500  1.000 37.44717  ?  240 PHE   A CD1  1 
ATOM   498  C  CD2  . PHE   A 1 88  ? 19.95100 -1.01600  10.75300 1.000 35.07259  ?  240 PHE   A CD2  1 
ATOM   499  C  CE1  . PHE   A 1 88  ? 21.44700 0.93800   9.49900  1.000 40.54368  ?  240 PHE   A CE1  1 
ATOM   500  C  CE2  . PHE   A 1 88  ? 21.33500 -1.06100  10.81100 1.000 37.75292  ?  240 PHE   A CE2  1 
ATOM   501  C  CZ   . PHE   A 1 88  ? 22.08300 -0.08100  10.18600 1.000 40.01656  ?  240 PHE   A CZ   1 
ATOM   502  N  N    . ALA   A 1 89  ? 17.27000 -2.88200  9.28800  1.000 35.62120  ?  241 ALA   A N    1 
ATOM   503  C  CA   . ALA   A 1 89  ? 17.76300 -4.25100  9.16900  1.000 35.04559  ?  241 ALA   A CA   1 
ATOM   504  C  C    . ALA   A 1 89  ? 17.56400 -4.79900  7.76300  1.000 37.57680  ?  241 ALA   A C    1 
ATOM   505  O  O    . ALA   A 1 89  ? 18.45800 -5.45400  7.21600  1.000 36.59245  ?  241 ALA   A O    1 
ATOM   506  C  CB   . ALA   A 1 89  ? 17.07100 -5.14900  10.19300 1.000 35.78953  ?  241 ALA   A CB   1 
ATOM   507  N  N    . LYS   A 1 90  ? 16.40300 -4.53400  7.15600  1.000 39.26854  ?  242 LYS   A N    1 
ATOM   508  C  CA   . LYS   A 1 90  ? 16.12100 -5.06800  5.82800  1.000 37.95517  ?  242 LYS   A CA   1 
ATOM   509  C  C    . LYS   A 1 90  ? 17.12600 -4.60100  4.78100  1.000 39.71600  ?  242 LYS   A C    1 
ATOM   510  O  O    . LYS   A 1 90  ? 17.27100 -5.25600  3.74200  1.000 42.87668  ?  242 LYS   A O    1 
ATOM   511  C  CB   . LYS   A 1 90  ? 14.70800 -4.68000  5.40900  1.000 37.97278  ?  242 LYS   A CB   1 
ATOM   512  C  CG   . LYS   A 1 90  ? 13.62600 -5.44000  6.14800  1.000 42.16639  ?  242 LYS   A CG   1 
ATOM   513  C  CD   . LYS   A 1 90  ? 12.26000 -4.82500  5.88100  1.000 47.16369  ?  242 LYS   A CD   1 
ATOM   514  C  CE   . LYS   A 1 90  ? 11.93000 -4.83900  4.40000  1.000 46.80758  ?  242 LYS   A CE   1 
ATOM   515  N  NZ   . LYS   A 1 90  ? 10.46800 -4.63600  4.17500  1.000 52.78478  ?  242 LYS   A NZ   1 
ATOM   516  N  N    . MET   A 1 91  ? 17.83000 -3.49900  5.03400  1.000 37.32306  ?  243 MET   A N    1 
ATOM   517  C  CA   . MET   A 1 91  ? 18.80100 -2.95100  4.09800  1.000 42.87012  ?  243 MET   A CA   1 
ATOM   518  C  C    . MET   A 1 91  ? 20.23900 -3.35200  4.40600  1.000 41.76408  ?  243 MET   A C    1 
ATOM   519  O  O    . MET   A 1 91  ? 21.13800 -2.99500  3.64000  1.000 40.54164  ?  243 MET   A O    1 
ATOM   520  C  CB   . MET   A 1 91  ? 18.68600 -1.42500  4.06800  1.000 47.74208  ?  243 MET   A CB   1 
ATOM   521  C  CG   . MET   A 1 91  ? 17.30700 -0.93900  3.66400  1.000 51.34519  ?  243 MET   A CG   1 
ATOM   522  S  SD   . MET   A 1 91  ? 17.28800 0.81900   3.30100  1.000 56.63810  ?  243 MET   A SD   1 
ATOM   523  C  CE   . MET   A 1 91  ? 16.46400 1.45700   4.75200  1.000 50.63396  ?  243 MET   A CE   1 
ATOM   524  N  N    . ILE   A 1 92  ? 20.48200 -4.06900  5.49900  1.000 39.40252  ?  244 ILE   A N    1 
ATOM   525  C  CA   . ILE   A 1 92  ? 21.83300 -4.57100  5.77800  1.000 42.44266  ?  244 ILE   A CA   1 
ATOM   526  C  C    . ILE   A 1 92  ? 22.22400 -5.57500  4.70000  1.000 44.07854  ?  244 ILE   A C    1 
ATOM   527  O  O    . ILE   A 1 92  ? 21.45700 -6.51700  4.43400  1.000 39.71264  ?  244 ILE   A O    1 
ATOM   528  C  CB   . ILE   A 1 92  ? 21.88900 -5.21700  7.16200  1.000 40.20642  ?  244 ILE   A CB   1 
ATOM   529  C  CG1  . ILE   A 1 92  ? 21.62000 -4.18200  8.26000  1.000 35.00786  ?  244 ILE   A CG1  1 
ATOM   530  C  CG2  . ILE   A 1 92  ? 23.24000 -5.90400  7.35500  1.000 39.86612  ?  244 ILE   A CG2  1 
ATOM   531  C  CD1  . ILE   A 1 92  ? 21.35000 -4.79600  9.64000  1.000 31.81364  ?  244 ILE   A CD1  1 
ATOM   532  N  N    . PRO   A 1 93  ? 23.38900 -5.43200  4.06500  1.000 47.98175  ?  245 PRO   A N    1 
ATOM   533  C  CA   . PRO   A 1 93  ? 23.77400 -6.37400  3.00100  1.000 48.45810  ?  245 PRO   A CA   1 
ATOM   534  C  C    . PRO   A 1 93  ? 23.81100 -7.80500  3.51400  1.000 51.19251  ?  245 PRO   A C    1 
ATOM   535  O  O    . PRO   A 1 93  ? 24.48100 -8.11500  4.50300  1.000 55.80760  ?  245 PRO   A O    1 
ATOM   536  C  CB   . PRO   A 1 93  ? 25.16400 -5.88200  2.58100  1.000 48.13208  ?  245 PRO   A CB   1 
ATOM   537  C  CG   . PRO   A 1 93  ? 25.17700 -4.43100  2.95000  1.000 50.31915  ?  245 PRO   A CG   1 
ATOM   538  C  CD   . PRO   A 1 93  ? 24.36100 -4.33600  4.21500  1.000 46.81838  ?  245 PRO   A CD   1 
ATOM   539  N  N    . GLY   A 1 94  ? 23.06200 -8.67700  2.84100  1.000 51.98219  ?  246 GLY   A N    1 
ATOM   540  C  CA   . GLY   A 1 94  ? 22.98600 -10.07500 3.18900  1.000 53.02622  ?  246 GLY   A CA   1 
ATOM   541  C  C    . GLY   A 1 94  ? 21.83400 -10.44900 4.10200  1.000 51.77241  ?  246 GLY   A C    1 
ATOM   542  O  O    . GLY   A 1 94  ? 21.48400 -11.63300 4.17000  1.000 51.94915  ?  246 GLY   A O    1 
ATOM   543  N  N    . PHE   A 1 95  ? 21.23100 -9.47700  4.79500  1.000 49.35745  ?  247 PHE   A N    1 
ATOM   544  C  CA   . PHE   A 1 95  ? 20.18800 -9.79100  5.77200  1.000 49.77004  ?  247 PHE   A CA   1 
ATOM   545  C  C    . PHE   A 1 95  ? 19.05200 -10.58600 5.13700  1.000 54.63037  ?  247 PHE   A C    1 
ATOM   546  O  O    . PHE   A 1 95  ? 18.59900 -11.59500 5.69200  1.000 54.86598  ?  247 PHE   A O    1 
ATOM   547  C  CB   . PHE   A 1 95  ? 19.65200 -8.50700  6.40800  1.000 46.46399  ?  247 PHE   A CB   1 
ATOM   548  C  CG   . PHE   A 1 95  ? 18.65700 -8.74500  7.51900  1.000 46.72125  ?  247 PHE   A CG   1 
ATOM   549  C  CD1  . PHE   A 1 95  ? 19.08600 -9.11000  8.78800  1.000 45.57477  ?  247 PHE   A CD1  1 
ATOM   550  C  CD2  . PHE   A 1 95  ? 17.29400 -8.61000  7.29300  1.000 44.05563  ?  247 PHE   A CD2  1 
ATOM   551  C  CE1  . PHE   A 1 95  ? 18.17500 -9.33100  9.81300  1.000 45.70254  ?  247 PHE   A CE1  1 
ATOM   552  C  CE2  . PHE   A 1 95  ? 16.37700 -8.83000  8.31100  1.000 41.67618  ?  247 PHE   A CE2  1 
ATOM   553  C  CZ   . PHE   A 1 95  ? 16.81700 -9.18900  9.57300  1.000 42.99159  ?  247 PHE   A CZ   1 
ATOM   554  N  N    . ARG   A 1 96  ? 18.59100 -10.15600 3.96200  1.000 59.03422  ?  248 ARG   A N    1 
ATOM   555  C  CA   . ARG   A 1 96  ? 17.47500 -10.82200 3.29800  1.000 63.56514  ?  248 ARG   A CA   1 
ATOM   556  C  C    . ARG   A 1 96  ? 17.84000 -12.17200 2.71400  1.000 61.72029  ?  248 ARG   A C    1 
ATOM   557  O  O    . ARG   A 1 96  ? 16.94300 -12.87700 2.24600  1.000 62.61799  ?  248 ARG   A O    1 
ATOM   558  C  CB   . ARG   A 1 96  ? 16.90000 -9.93900  2.19400  1.000 72.30855  ?  248 ARG   A CB   1 
ATOM   559  C  CG   . ARG   A 1 96  ? 15.69200 -9.17800  2.65500  1.000 81.06294  ?  248 ARG   A CG   1 
ATOM   560  C  CD   . ARG   A 1 96  ? 14.55100 -10.12500 3.14300  1.000 92.44404  ?  248 ARG   A CD   1 
ATOM   561  N  NE   . ARG   A 1 96  ? 13.89200 -10.87900 2.06700  1.000 99.41528  ?  248 ARG   A NE   1 
ATOM   562  C  CZ   . ARG   A 1 96  ? 13.79300 -12.20700 1.99400  1.000 104.23961 ?  248 ARG   A CZ   1 
ATOM   563  N  NH1  . ARG   A 1 96  ? 13.17100 -12.76900 0.96700  1.000 110.88695 ?  248 ARG   A NH1  1 
ATOM   564  N  NH2  . ARG   A 1 96  ? 14.30400 -12.98000 2.93400  1.000 102.57587 ?  248 ARG   A NH2  1 
ATOM   565  N  N    . ASP   A 1 97  ? 19.11800 -12.53600 2.68700  1.000 58.14207  ?  249 ASP   A N    1 
ATOM   566  C  CA   . ASP   A 1 97  ? 19.48700 -13.88700 2.30200  1.000 59.67577  ?  249 ASP   A CA   1 
ATOM   567  C  C    . ASP   A 1 97  ? 19.17000 -14.90200 3.39100  1.000 58.56300  ?  249 ASP   A C    1 
ATOM   568  O  O    . ASP   A 1 97  ? 19.28500 -16.10700 3.14500  1.000 61.87593  ?  249 ASP   A O    1 
ATOM   569  C  CB   . ASP   A 1 97  ? 20.97600 -13.94400 1.94800  1.000 65.93284  ?  249 ASP   A CB   1 
ATOM   570  C  CG   . ASP   A 1 97  ? 21.30600 -13.17900 0.67700  1.000 69.75149  ?  249 ASP   A CG   1 
ATOM   571  O  OD1  . ASP   A 1 97  ? 20.36600 -12.73800 -0.02100 1.000 72.51945  ?  249 ASP   A OD1  1 
ATOM   572  O  OD2  . ASP   A 1 97  ? 22.50800 -13.02200 0.37400  1.000 70.79275  ?  249 ASP   A OD2  1 
ATOM   573  N  N    . LEU   A 1 98  ? 18.78300 -14.44500 4.58000  1.000 54.66641  ?  250 LEU   A N    1 
ATOM   574  C  CA   . LEU   A 1 98  ? 18.39000 -15.32800 5.66400  1.000 54.69923  ?  250 LEU   A CA   1 
ATOM   575  C  C    . LEU   A 1 98  ? 16.93100 -15.73600 5.51100  1.000 55.80880  ?  250 LEU   A C    1 
ATOM   576  O  O    . LEU   A 1 98  ? 16.14400 -15.07800 4.82400  1.000 56.54741  ?  250 LEU   A O    1 
ATOM   577  C  CB   . LEU   A 1 98  ? 18.58200 -14.64400 7.02000  1.000 53.19041  ?  250 LEU   A CB   1 
ATOM   578  C  CG   . LEU   A 1 98  ? 19.97000 -14.13800 7.41600  1.000 51.05890  ?  250 LEU   A CG   1 
ATOM   579  C  CD1  . LEU   A 1 98  ? 19.84700 -13.16300 8.56600  1.000 47.85468  ?  250 LEU   A CD1  1 
ATOM   580  C  CD2  . LEU   A 1 98  ? 20.87600 -15.28900 7.79600  1.000 51.42631  ?  250 LEU   A CD2  1 
ATOM   581  N  N    . THR   A 1 99  ? 16.56900 -16.83300 6.17200  1.000 57.40996  ?  251 THR   A N    1 
ATOM   582  C  CA   . THR   A 1 99  ? 15.16800 -17.21500 6.22200  1.000 55.08488  ?  251 THR   A CA   1 
ATOM   583  C  C    . THR   A 1 99  ? 14.38500 -16.19700 7.03900  1.000 51.95315  ?  251 THR   A C    1 
ATOM   584  O  O    . THR   A 1 99  ? 14.93200 -15.48800 7.89100  1.000 48.40717  ?  251 THR   A O    1 
ATOM   585  C  CB   . THR   A 1 99  ? 14.97900 -18.60600 6.83800  1.000 58.00038  ?  251 THR   A CB   1 
ATOM   586  O  OG1  . THR   A 1 99  ? 15.33700 -18.58100 8.22800  1.000 58.23303  ?  251 THR   A OG1  1 
ATOM   587  C  CG2  . THR   A 1 99  ? 15.82100 -19.64300 6.10800  1.000 61.11684  ?  251 THR   A CG2  1 
ATOM   588  N  N    A SER   A 1 100 ? 13.07900 -16.12800 6.76400  0.460 50.09475  ?  252 SER   A N    1 
ATOM   589  N  N    B SER   A 1 100 ? 13.08000 -16.12600 6.76300  0.540 50.06990  ?  252 SER   A N    1 
ATOM   590  C  CA   A SER   A 1 100 ? 12.21500 -15.21700 7.50600  0.460 47.94924  ?  252 SER   A CA   1 
ATOM   591  C  CA   B SER   A 1 100 ? 12.21900 -15.21500 7.50700  0.540 47.87326  ?  252 SER   A CA   1 
ATOM   592  C  C    A SER   A 1 100 ? 12.21500 -15.53600 8.99500  0.460 48.74727  ?  252 SER   A C    1 
ATOM   593  C  C    B SER   A 1 100 ? 12.22000 -15.53400 8.99500  0.540 48.73071  ?  252 SER   A C    1 
ATOM   594  O  O    A SER   A 1 100 ? 12.06200 -14.62900 9.82200  0.460 46.90168  ?  252 SER   A O    1 
ATOM   595  O  O    B SER   A 1 100 ? 12.07700 -14.62700 9.82300  0.540 46.88264  ?  252 SER   A O    1 
ATOM   596  C  CB   A SER   A 1 100 ? 10.79100 -15.27300 6.95100  0.460 48.29732  ?  252 SER   A CB   1 
ATOM   597  C  CB   B SER   A 1 100 ? 10.79700 -15.26900 6.94800  0.540 48.30484  ?  252 SER   A CB   1 
ATOM   598  O  OG   A SER   A 1 100 ? 9.99300  -16.18400 7.68600  0.460 45.50964  ?  252 SER   A OG   1 
ATOM   599  O  OG   B SER   A 1 100 ? 10.78300 -14.90700 5.57800  0.540 51.43195  ?  252 SER   A OG   1 
ATOM   600  N  N    . ASP   A 1 101 ? 12.38200 -16.81100 9.35500  1.000 54.08433  ?  253 ASP   A N    1 
ATOM   601  C  CA   . ASP   A 1 101 ? 12.46300 -17.17600 10.76600 1.000 57.95821  ?  253 ASP   A CA   1 
ATOM   602  C  C    . ASP   A 1 101 ? 13.70400 -16.57700 11.41100 1.000 55.22472  ?  253 ASP   A C    1 
ATOM   603  O  O    . ASP   A 1 101 ? 13.64300 -16.05300 12.53000 1.000 53.59687  ?  253 ASP   A O    1 
ATOM   604  C  CB   . ASP   A 1 101 ? 12.46600 -18.69900 10.92300 1.000 63.48730  ?  253 ASP   A CB   1 
ATOM   605  C  CG   . ASP   A 1 101 ? 11.26000 -19.35900 10.27300 1.000 71.82290  ?  253 ASP   A CG   1 
ATOM   606  O  OD1  . ASP   A 1 101 ? 10.11500 -18.98500 10.61000 1.000 71.85010  ?  253 ASP   A OD1  1 
ATOM   607  O  OD2  . ASP   A 1 101 ? 11.46300 -20.25100 9.41900  1.000 75.30395  ?  253 ASP   A OD2  1 
ATOM   608  N  N    . ASP   A 1 102 ? 14.84000 -16.63400 10.71200 1.000 54.69335  ?  254 ASP   A N    1 
ATOM   609  C  CA   . ASP   A 1 102 ? 16.07100 -16.08500 11.26700 1.000 49.64149  ?  254 ASP   A CA   1 
ATOM   610  C  C    . ASP   A 1 102 ? 16.01000 -14.56600 11.34400 1.000 45.89577  ?  254 ASP   A C    1 
ATOM   611  O  O    . ASP   A 1 102 ? 16.48100 -13.97100 12.32000 1.000 48.67898  ?  254 ASP   A O    1 
ATOM   612  C  CB   . ASP   A 1 102 ? 17.27000 -16.53600 10.43600 1.000 53.72396  ?  254 ASP   A CB   1 
ATOM   613  C  CG   . ASP   A 1 102 ? 17.77500 -17.90000 10.84900 1.000 55.42335  ?  254 ASP   A CG   1 
ATOM   614  O  OD1  . ASP   A 1 102 ? 17.32100 -18.40700 11.89600 1.000 55.65780  ?  254 ASP   A OD1  1 
ATOM   615  O  OD2  . ASP   A 1 102 ? 18.61700 -18.46800 10.12800 1.000 56.47096  ?  254 ASP   A OD2  1 
ATOM   616  N  N    . GLN   A 1 103 ? 15.43500 -13.92000 10.32800 1.000 46.24188  ?  255 GLN   A N    1 
ATOM   617  C  CA   . GLN   A 1 103 ? 15.26100 -12.47300 10.39500 1.000 44.00230  ?  255 GLN   A CA   1 
ATOM   618  C  C    . GLN   A 1 103 ? 14.38600 -12.08700 11.57900 1.000 41.21771  ?  255 GLN   A C    1 
ATOM   619  O  O    . GLN   A 1 103 ? 14.63100 -11.07000 12.23900 1.000 40.76784  ?  255 GLN   A O    1 
ATOM   620  C  CB   . GLN   A 1 103 ? 14.66500 -11.95800 9.09000  1.000 45.68292  ?  255 GLN   A CB   1 
ATOM   621  C  CG   . GLN   A 1 103 ? 15.48100 -12.33700 7.87800  1.000 49.81585  ?  255 GLN   A CG   1 
ATOM   622  C  CD   . GLN   A 1 103 ? 14.82100 -11.93500 6.58000  1.000 55.72984  ?  255 GLN   A CD   1 
ATOM   623  O  OE1  . GLN   A 1 103 ? 13.89300 -11.13100 6.56100  1.000 51.07880  ?  255 GLN   A OE1  1 
ATOM   624  N  NE2  . GLN   A 1 103 ? 15.29400 -12.50300 5.48400  1.000 60.50032  ?  255 GLN   A NE2  1 
ATOM   625  N  N    . ILE   A 1 104 ? 13.37500 -12.90300 11.87400 1.000 41.44386  ?  256 ILE   A N    1 
ATOM   626  C  CA   . ILE   A 1 104 ? 12.50800 -12.63600 13.01600 1.000 42.94012  ?  256 ILE   A CA   1 
ATOM   627  C  C    . ILE   A 1 104 ? 13.27300 -12.83200 14.31800 1.000 41.90919  ?  256 ILE   A C    1 
ATOM   628  O  O    . ILE   A 1 104 ? 13.22800 -11.98500 15.21900 1.000 44.46346  ?  256 ILE   A O    1 
ATOM   629  C  CB   . ILE   A 1 104 ? 11.25300 -13.52600 12.95400 1.000 42.78856  ?  256 ILE   A CB   1 
ATOM   630  C  CG1  . ILE   A 1 104 ? 10.25600 -12.97200 11.92800 1.000 43.00662  ?  256 ILE   A CG1  1 
ATOM   631  C  CG2  . ILE   A 1 104 ? 10.61900 -13.65300 14.33400 1.000 43.87676  ?  256 ILE   A CG2  1 
ATOM   632  C  CD1  . ILE   A 1 104 ? 9.19500  -13.97200 11.47700 1.000 47.72956  ?  256 ILE   A CD1  1 
ATOM   633  N  N    . VAL   A 1 105 ? 13.99300 -13.94800 14.43300 1.000 43.76575  ?  257 VAL   A N    1 
ATOM   634  C  CA   . VAL   A 1 105 ? 14.77900 -14.21100 15.63600 1.000 46.22573  ?  257 VAL   A CA   1 
ATOM   635  C  C    . VAL   A 1 105 ? 15.76700 -13.07700 15.88400 1.000 44.35664  ?  257 VAL   A C    1 
ATOM   636  O  O    . VAL   A 1 105 ? 15.89300 -12.57400 17.00800 1.000 46.71501  ?  257 VAL   A O    1 
ATOM   637  C  CB   . VAL   A 1 105 ? 15.49500 -15.56900 15.52200 1.000 49.05513  ?  257 VAL   A CB   1 
ATOM   638  C  CG1  . VAL   A 1 105 ? 16.58400 -15.68400 16.56800 1.000 54.20285  ?  257 VAL   A CG1  1 
ATOM   639  C  CG2  . VAL   A 1 105 ? 14.49100 -16.70700 15.65900 1.000 50.75987  ?  257 VAL   A CG2  1 
ATOM   640  N  N    . LEU   A 1 106 ? 16.46700 -12.64000 14.83300 1.000 40.00204  ?  258 LEU   A N    1 
ATOM   641  C  CA   . LEU   A 1 106 ? 17.50200 -11.62400 15.00900 1.000 37.22314  ?  258 LEU   A CA   1 
ATOM   642  C  C    . LEU   A 1 106 ? 16.90900 -10.29100 15.44300 1.000 35.42313  ?  258 LEU   A C    1 
ATOM   643  O  O    . LEU   A 1 106 ? 17.50700 -9.57500  16.25400 1.000 32.59648  ?  258 LEU   A O    1 
ATOM   644  C  CB   . LEU   A 1 106 ? 18.30000 -11.44800 13.71800 1.000 37.54848  ?  258 LEU   A CB   1 
ATOM   645  C  CG   . LEU   A 1 106 ? 19.19800 -12.61000 13.30000 1.000 40.55072  ?  258 LEU   A CG   1 
ATOM   646  C  CD1  . LEU   A 1 106 ? 19.97600 -12.25000 12.04700 1.000 42.97613  ?  258 LEU   A CD1  1 
ATOM   647  C  CD2  . LEU   A 1 106 ? 20.13100 -12.99100 14.43400 1.000 41.67149  ?  258 LEU   A CD2  1 
ATOM   648  N  N    . LEU   A 1 107 ? 15.73700 -9.93700  14.91400 1.000 35.87845  ?  259 LEU   A N    1 
ATOM   649  C  CA   . LEU   A 1 107 ? 15.16200 -8.63400  15.22100 1.000 35.89864  ?  259 LEU   A CA   1 
ATOM   650  C  C    . LEU   A 1 107 ? 14.46400 -8.62000  16.57600 1.000 35.48368  ?  259 LEU   A C    1 
ATOM   651  O  O    . LEU   A 1 107 ? 14.50500 -7.60600  17.28500 1.000 35.92744  ?  259 LEU   A O    1 
ATOM   652  C  CB   . LEU   A 1 107 ? 14.18900 -8.22000  14.12000 1.000 39.57250  ?  259 LEU   A CB   1 
ATOM   653  C  CG   . LEU   A 1 107 ? 14.86400 -7.47300  12.97600 1.000 42.77931  ?  259 LEU   A CG   1 
ATOM   654  C  CD1  . LEU   A 1 107 ? 14.02500 -7.57300  11.71200 1.000 46.13210  ?  259 LEU   A CD1  1 
ATOM   655  C  CD2  . LEU   A 1 107 ? 15.08600 -6.02800  13.38100 1.000 40.52227  ?  259 LEU   A CD2  1 
ATOM   656  N  N    . LYS   A 1 108 ? 13.80800 -9.72400  16.94700 1.000 29.92948  ?  260 LYS   A N    1 
ATOM   657  C  CA   . LYS   A 1 108 ? 13.16400 -9.78500  18.25700 1.000 38.03250  ?  260 LYS   A CA   1 
ATOM   658  C  C    . LYS   A 1 108 ? 14.18500 -9.64400  19.37500 1.000 39.37559  ?  260 LYS   A C    1 
ATOM   659  O  O    . LYS   A 1 108 ? 13.92400 -8.99400  20.39600 1.000 42.01618  ?  260 LYS   A O    1 
ATOM   660  C  CB   . LYS   A 1 108 ? 12.40100 -11.09800 18.41200 1.000 39.19661  ?  260 LYS   A CB   1 
ATOM   661  C  CG   . LYS   A 1 108 ? 10.92600 -11.00100 18.08400 1.000 49.18744  ?  260 LYS   A CG   1 
ATOM   662  C  CD   . LYS   A 1 108 ? 10.31400 -12.38200 17.92100 1.000 53.90068  ?  260 LYS   A CD   1 
ATOM   663  C  CE   . LYS   A 1 108 ? 10.15700 -13.08000 19.26200 1.000 57.91287  ?  260 LYS   A CE   1 
ATOM   664  N  NZ   . LYS   A 1 108 ? 9.21000  -12.34900 20.14300 1.000 58.37929  ?  260 LYS   A NZ   1 
ATOM   665  N  N    . SER   A 1 109 ? 15.34900 -10.25900 19.20500 1.000 35.92887  ?  261 SER   A N    1 
ATOM   666  C  CA   . SER   A 1 109 ? 16.37000 -10.24700 20.24300 1.000 39.60449  ?  261 SER   A CA   1 
ATOM   667  C  C    . SER   A 1 109 ? 17.21400 -8.98200  20.23200 1.000 35.06617  ?  261 SER   A C    1 
ATOM   668  O  O    . SER   A 1 109 ? 17.76700 -8.62100  21.27200 1.000 38.26655  ?  261 SER   A O    1 
ATOM   669  C  CB   . SER   A 1 109 ? 17.26900 -11.46400 20.08200 1.000 42.56015  ?  261 SER   A CB   1 
ATOM   670  O  OG   . SER   A 1 109 ? 17.90900 -11.40600 18.82300 1.000 46.90452  ?  261 SER   A OG   1 
ATOM   671  N  N    . SER   A 1 110 ? 17.30400 -8.28500  19.09700 1.000 35.53078  ?  262 SER   A N    1 
ATOM   672  C  CA   . SER   A 1 110 ? 18.18900 -7.13700  18.97800 1.000 35.65336  ?  262 SER   A CA   1 
ATOM   673  C  C    . SER   A 1 110 ? 17.49200 -5.78600  18.98800 1.000 34.92087  ?  262 SER   A C    1 
ATOM   674  O  O    . SER   A 1 110 ? 18.16300 -4.77600  19.22300 1.000 38.71846  ?  262 SER   A O    1 
ATOM   675  C  CB   . SER   A 1 110 ? 19.01900 -7.24500  17.69300 1.000 38.34064  ?  262 SER   A CB   1 
ATOM   676  O  OG   . SER   A 1 110 ? 18.20500 -6.98100  16.56200 1.000 35.50109  ?  262 SER   A OG   1 
ATOM   677  N  N    . ALA   A 1 111 ? 16.17800 -5.73400  18.75000 1.000 36.40822  ?  263 ALA   A N    1 
ATOM   678  C  CA   . ALA   A 1 111 ? 15.50600 -4.44500  18.59400 1.000 34.41836  ?  263 ALA   A CA   1 
ATOM   679  C  C    . ALA   A 1 111 ? 15.72000 -3.55500  19.81100 1.000 29.55405  ?  263 ALA   A C    1 
ATOM   680  O  O    . ALA   A 1 111 ? 15.99500 -2.35700  19.67200 1.000 33.45094  ?  263 ALA   A O    1 
ATOM   681  C  CB   . ALA   A 1 111 ? 14.00700 -4.64900  18.33600 1.000 33.70618  ?  263 ALA   A CB   1 
ATOM   682  N  N    . ILE   A 1 112 ? 15.59400 -4.12300  21.01200 1.000 29.65419  ?  264 ILE   A N    1 
ATOM   683  C  CA   . ILE   A 1 112 ? 15.81500 -3.34800  22.23000 1.000 36.24430  ?  264 ILE   A CA   1 
ATOM   684  C  C    . ILE   A 1 112 ? 17.23100 -2.77300  22.24700 1.000 36.89754  ?  264 ILE   A C    1 
ATOM   685  O  O    . ILE   A 1 112 ? 17.44300 -1.61900  22.64000 1.000 38.96161  ?  264 ILE   A O    1 
ATOM   686  C  CB   . ILE   A 1 112 ? 15.51700 -4.21600  23.47300 1.000 40.92002  ?  264 ILE   A CB   1 
ATOM   687  C  CG1  . ILE   A 1 112 ? 15.65100 -3.39700  24.75600 1.000 41.48202  ?  264 ILE   A CG1  1 
ATOM   688  C  CG2  . ILE   A 1 112 ? 16.41700 -5.44700  23.53700 1.000 43.13480  ?  264 ILE   A CG2  1 
ATOM   689  C  CD1  . ILE   A 1 112 ? 14.93000 -2.08700  24.70700 1.000 33.37467  ?  264 ILE   A CD1  1 
ATOM   690  N  N    . GLU   A 1 113 ? 18.21000 -3.54400  21.76900 1.000 36.67875  ?  265 GLU   A N    1 
ATOM   691  C  CA   . GLU   A 1 113 ? 19.59600 -3.08400  21.79800 1.000 37.77386  ?  265 GLU   A CA   1 
ATOM   692  C  C    . GLU   A 1 113 ? 19.85100 -2.01500  20.74300 1.000 38.97398  ?  265 GLU   A C    1 
ATOM   693  O  O    . GLU   A 1 113 ? 20.58700 -1.05100  20.99600 1.000 38.58692  ?  265 GLU   A O    1 
ATOM   694  C  CB   . GLU   A 1 113 ? 20.54600 -4.26100  21.60200 1.000 36.20884  ?  265 GLU   A CB   1 
ATOM   695  C  CG   . GLU   A 1 113 ? 20.42400 -5.34800  22.65700 1.000 33.23425  ?  265 GLU   A CG   1 
ATOM   696  C  CD   . GLU   A 1 113 ? 21.29200 -6.55000  22.34000 1.000 38.20703  ?  265 GLU   A CD   1 
ATOM   697  O  OE1  . GLU   A 1 113 ? 22.25800 -6.39700  21.55800 1.000 39.95998  ?  265 GLU   A OE1  1 
ATOM   698  O  OE2  . GLU   A 1 113 ? 20.99700 -7.65400  22.84500 1.000 39.48496  ?  265 GLU   A OE2  1 
ATOM   699  N  N    . VAL   A 1 114 ? 19.25800 -2.16700  19.55400 1.000 33.46108  ?  266 VAL   A N    1 
ATOM   700  C  CA   . VAL   A 1 114 ? 19.43800 -1.16600  18.50900 1.000 29.98866  ?  266 VAL   A CA   1 
ATOM   701  C  C    . VAL   A 1 114 ? 18.76900 0.13800   18.91100 1.000 31.14157  ?  266 VAL   A C    1 
ATOM   702  O  O    . VAL   A 1 114 ? 19.26200 1.22800   18.59800 1.000 35.09279  ?  266 VAL   A O    1 
ATOM   703  C  CB   . VAL   A 1 114 ? 18.90300 -1.69300  17.16500 1.000 31.29732  ?  266 VAL   A CB   1 
ATOM   704  C  CG1  . VAL   A 1 114 ? 19.12700 -0.67800  16.05600 1.000 24.17958  ?  266 VAL   A CG1  1 
ATOM   705  C  CG2  . VAL   A 1 114 ? 19.56800 -3.01300  16.82300 1.000 31.75647  ?  266 VAL   A CG2  1 
ATOM   706  N  N    . ILE   A 1 115 ? 17.63500 0.04800   19.61000 1.000 31.65628  ?  267 ILE   A N    1 
ATOM   707  C  CA   . ILE   A 1 115 ? 16.98500 1.24600   20.13000 1.000 33.36268  ?  267 ILE   A CA   1 
ATOM   708  C  C    . ILE   A 1 115 ? 17.92300 1.97600   21.08700 1.000 34.23799  ?  267 ILE   A C    1 
ATOM   709  O  O    . ILE   A 1 115 ? 18.11900 3.19400   20.98700 1.000 35.94273  ?  267 ILE   A O    1 
ATOM   710  C  CB   . ILE   A 1 115 ? 15.64500 0.87500   20.79600 1.000 34.14449  ?  267 ILE   A CB   1 
ATOM   711  C  CG1  . ILE   A 1 115 ? 14.58200 0.60500   19.72600 1.000 35.97313  ?  267 ILE   A CG1  1 
ATOM   712  C  CG2  . ILE   A 1 115 ? 15.19000 1.96400   21.74500 1.000 34.75047  ?  267 ILE   A CG2  1 
ATOM   713  C  CD1  . ILE   A 1 115 ? 13.30200 -0.02500  20.25700 1.000 34.59357  ?  267 ILE   A CD1  1 
ATOM   714  N  N    . MET   A 1 116 ? 18.54400 1.23300   22.00700 1.000 33.41816  ?  268 MET   A N    1 
ATOM   715  C  CA   . MET   A 1 116 ? 19.53900 1.82800   22.89800 1.000 36.84111  ?  268 MET   A CA   1 
ATOM   716  C  C    . MET   A 1 116 ? 20.66800 2.48600   22.11100 1.000 36.68783  ?  268 MET   A C    1 
ATOM   717  O  O    . MET   A 1 116 ? 21.08000 3.60800   22.42600 1.000 38.85271  ?  268 MET   A O    1 
ATOM   718  C  CB   . MET   A 1 116 ? 20.09300 0.76500   23.84700 1.000 35.65238  ?  268 MET   A CB   1 
ATOM   719  C  CG   . MET   A 1 116 ? 19.15500 0.43100   25.00300 1.000 38.72088  ?  268 MET   A CG   1 
ATOM   720  S  SD   . MET   A 1 116 ? 19.47700 -1.18000  25.74700 1.000 41.52237  ?  268 MET   A SD   1 
ATOM   721  C  CE   . MET   A 1 116 ? 18.21100 -1.24000  27.00900 1.000 37.29607  ?  268 MET   A CE   1 
ATOM   722  N  N    . LEU   A 1 117 ? 21.16800 1.81200   21.07200 1.000 33.91169  ?  269 LEU   A N    1 
ATOM   723  C  CA   . LEU   A 1 117 ? 22.23500 2.38200   20.25300 1.000 32.12413  ?  269 LEU   A CA   1 
ATOM   724  C  C    . LEU   A 1 117 ? 21.76900 3.63100   19.51400 1.000 34.25334  ?  269 LEU   A C    1 
ATOM   725  O  O    . LEU   A 1 117 ? 22.38700 4.69700   19.62500 1.000 32.94123  ?  269 LEU   A O    1 
ATOM   726  C  CB   . LEU   A 1 117 ? 22.74800 1.34400   19.25400 1.000 37.47118  ?  269 LEU   A CB   1 
ATOM   727  C  CG   . LEU   A 1 117 ? 23.62600 0.21900   19.79000 1.000 38.18158  ?  269 LEU   A CG   1 
ATOM   728  C  CD1  . LEU   A 1 117 ? 23.83800 -0.82500  18.71300 1.000 38.58631  ?  269 LEU   A CD1  1 
ATOM   729  C  CD2  . LEU   A 1 117 ? 24.96700 0.76200   20.29900 1.000 37.57657  ?  269 LEU   A CD2  1 
ATOM   730  N  N    . ARG   A 1 118 ? 20.67900 3.51600   18.74000 1.000 36.09830  ?  270 ARG   A N    1 
ATOM   731  C  CA   . ARG   A 1 118 ? 20.22600 4.63300   17.91500 1.000 38.14397  ?  270 ARG   A CA   1 
ATOM   732  C  C    . ARG   A 1 118 ? 19.73700 5.81100   18.74900 1.000 38.92485  ?  270 ARG   A C    1 
ATOM   733  O  O    . ARG   A 1 118 ? 19.77000 6.95000   18.26700 1.000 38.72410  ?  270 ARG   A O    1 
ATOM   734  C  CB   . ARG   A 1 118 ? 19.12100 4.17600   16.94800 1.000 38.74901  ?  270 ARG   A CB   1 
ATOM   735  C  CG   . ARG   A 1 118 ? 17.76900 3.90600   17.59400 1.000 39.66666  ?  270 ARG   A CG   1 
ATOM   736  C  CD   . ARG   A 1 118 ? 16.87400 3.04400   16.70000 1.000 42.13786  ?  270 ARG   A CD   1 
ATOM   737  N  NE   . ARG   A 1 118 ? 16.21200 3.82500   15.65400 1.000 40.30538  ?  270 ARG   A NE   1 
ATOM   738  C  CZ   . ARG   A 1 118 ? 16.61700 3.86000   14.38900 1.000 44.20643  ?  270 ARG   A CZ   1 
ATOM   739  N  NH1  . ARG   A 1 118 ? 17.68500 3.16500   14.01600 1.000 52.06816  ?  270 ARG   A NH1  1 
ATOM   740  N  NH2  . ARG   A 1 118 ? 15.96700 4.59800   13.50200 1.000 41.21411  ?  270 ARG   A NH2  1 
ATOM   741  N  N    . SER   A 1 119 ? 19.29100 5.56700   19.98500 1.000 34.21894  ?  271 SER   A N    1 
ATOM   742  C  CA   . SER   A 1 119 ? 18.91200 6.66700   20.86400 1.000 42.53282  ?  271 SER   A CA   1 
ATOM   743  C  C    . SER   A 1 119 ? 20.10700 7.52100   21.27500 1.000 42.69724  ?  271 SER   A C    1 
ATOM   744  O  O    . SER   A 1 119 ? 19.91000 8.66500   21.69600 1.000 44.65421  ?  271 SER   A O    1 
ATOM   745  C  CB   . SER   A 1 119 ? 18.19800 6.13600   22.11500 1.000 44.50384  ?  271 SER   A CB   1 
ATOM   746  O  OG   . SER   A 1 119 ? 19.10800 5.55200   23.03600 1.000 43.96799  ?  271 SER   A OG   1 
ATOM   747  N  N    . ASN   A 1 120 ? 21.33600 7.00100   21.15400 1.000 42.11145  ?  272 ASN   A N    1 
ATOM   748  C  CA   . ASN   A 1 120 ? 22.52300 7.77400   21.52200 1.000 40.08639  ?  272 ASN   A CA   1 
ATOM   749  C  C    . ASN   A 1 120 ? 22.68700 9.02400   20.66800 1.000 41.12847  ?  272 ASN   A C    1 
ATOM   750  O  O    . ASN   A 1 120 ? 23.37000 9.96300   21.09000 1.000 43.70314  ?  272 ASN   A O    1 
ATOM   751  C  CB   . ASN   A 1 120 ? 23.78000 6.90300   21.40700 1.000 40.53208  ?  272 ASN   A CB   1 
ATOM   752  C  CG   . ASN   A 1 120 ? 24.99900 7.50900   22.11300 1.000 41.80679  ?  272 ASN   A CG   1 
ATOM   753  O  OD1  . ASN   A 1 120 ? 26.04600 7.71000   21.49200 1.000 44.11638  ?  272 ASN   A OD1  1 
ATOM   754  N  ND2  . ASN   A 1 120 ? 24.87900 7.76400   23.41700 1.000 34.03858  ?  272 ASN   A ND2  1 
ATOM   755  N  N    . GLN   A 1 121 ? 22.08500 9.05300   19.47400 1.000 39.77138  ?  273 GLN   A N    1 
ATOM   756  C  CA   . GLN   A 1 121 ? 22.17500 10.23400  18.62200 1.000 41.16221  ?  273 GLN   A CA   1 
ATOM   757  C  C    . GLN   A 1 121 ? 21.50900 11.43700  19.27800 1.000 44.00512  ?  273 GLN   A C    1 
ATOM   758  O  O    . GLN   A 1 121 ? 22.05600 12.54600  19.25900 1.000 48.18814  ?  273 GLN   A O    1 
ATOM   759  C  CB   . GLN   A 1 121 ? 21.53700 9.94300   17.26100 1.000 48.27459  ?  273 GLN   A CB   1 
ATOM   760  C  CG   . GLN   A 1 121 ? 21.59000 11.10500  16.27400 1.000 50.20398  ?  273 GLN   A CG   1 
ATOM   761  C  CD   . GLN   A 1 121 ? 21.33700 10.67700  14.83700 1.000 47.79985  ?  273 GLN   A CD   1 
ATOM   762  O  OE1  . GLN   A 1 121 ? 21.01400 11.50100  13.98300 1.000 50.69583  ?  273 GLN   A OE1  1 
ATOM   763  N  NE2  . GLN   A 1 121 ? 21.47800 9.38300   14.56600 1.000 41.43626  ?  273 GLN   A NE2  1 
ATOM   764  N  N    . SER   A 1 122 ? 20.32600 11.23700  19.86400 1.000 46.64566  ?  274 SER   A N    1 
ATOM   765  C  CA   . SER   A 1 122 ? 19.61200 12.29600  20.56700 1.000 49.04055  ?  274 SER   A CA   1 
ATOM   766  C  C    . SER   A 1 122 ? 20.10300 12.49400  21.99400 1.000 47.70718  ?  274 SER   A C    1 
ATOM   767  O  O    . SER   A 1 122 ? 19.78900 13.52300  22.60500 1.000 46.13886  ?  274 SER   A O    1 
ATOM   768  C  CB   . SER   A 1 122 ? 18.11300 11.99400  20.59600 1.000 52.47839  ?  274 SER   A CB   1 
ATOM   769  O  OG   . SER   A 1 122 ? 17.84800 10.86400  21.40900 1.000 51.51275  ?  274 SER   A OG   1 
ATOM   770  N  N    . PHE   A 1 123 ? 20.84500 11.53600  22.54000 1.000 45.88913  ?  275 PHE   A N    1 
ATOM   771  C  CA   . PHE   A 1 123 ? 21.33000 11.65400  23.90600 1.000 45.07231  ?  275 PHE   A CA   1 
ATOM   772  C  C    . PHE   A 1 123 ? 22.35500 12.77700  24.00900 1.000 51.54336  ?  275 PHE   A C    1 
ATOM   773  O  O    . PHE   A 1 123 ? 23.22800 12.92100  23.14800 1.000 53.35069  ?  275 PHE   A O    1 
ATOM   774  C  CB   . PHE   A 1 123 ? 21.94300 10.33400  24.36100 1.000 44.15432  ?  275 PHE   A CB   1 
ATOM   775  C  CG   . PHE   A 1 123 ? 22.31800 10.31400  25.81100 1.000 46.98313  ?  275 PHE   A CG   1 
ATOM   776  C  CD1  . PHE   A 1 123 ? 21.36200 10.05800  26.78200 1.000 46.86822  ?  275 PHE   A CD1  1 
ATOM   777  C  CD2  . PHE   A 1 123 ? 23.62400 10.56100  26.20500 1.000 48.06975  ?  275 PHE   A CD2  1 
ATOM   778  C  CE1  . PHE   A 1 123 ? 21.70500 10.04400  28.12500 1.000 46.22014  ?  275 PHE   A CE1  1 
ATOM   779  C  CE2  . PHE   A 1 123 ? 23.97600 10.54500  27.54400 1.000 50.55490  ?  275 PHE   A CE2  1 
ATOM   780  C  CZ   . PHE   A 1 123 ? 23.01500 10.28700  28.50500 1.000 51.06837  ?  275 PHE   A CZ   1 
ATOM   781  N  N    . THR   A 1 124 ? 22.24000 13.58100  25.06600 1.000 54.88211  ?  276 THR   A N    1 
ATOM   782  C  CA   . THR   A 1 124 ? 23.17600 14.66800  25.32200 1.000 57.74654  ?  276 THR   A CA   1 
ATOM   783  C  C    . THR   A 1 124 ? 23.72800 14.54700  26.73400 1.000 60.99273  ?  276 THR   A C    1 
ATOM   784  O  O    . THR   A 1 124 ? 22.98700 14.27100  27.68300 1.000 62.21884  ?  276 THR   A O    1 
ATOM   785  C  CB   . THR   A 1 124 ? 22.52100 16.05400  25.12200 1.000 60.63318  ?  276 THR   A CB   1 
ATOM   786  O  OG1  . THR   A 1 124 ? 23.46900 17.08300  25.43100 1.000 63.15082  ?  276 THR   A OG1  1 
ATOM   787  C  CG2  . THR   A 1 124 ? 21.28700 16.22000  26.00400 1.000 60.74104  ?  276 THR   A CG2  1 
ATOM   788  N  N    . MET   A 1 125 ? 25.03500 14.74800  26.86800 1.000 61.54275  ?  277 MET   A N    1 
ATOM   789  C  CA   . MET   A 1 125 ? 25.68900 14.63200  28.16100 1.000 63.69756  ?  277 MET   A CA   1 
ATOM   790  C  C    . MET   A 1 125 ? 25.64900 15.92400  28.96000 1.000 69.08865  ?  277 MET   A C    1 
ATOM   791  O  O    . MET   A 1 125 ? 26.15100 15.95500  30.08900 1.000 71.16000  ?  277 MET   A O    1 
ATOM   792  C  CB   . MET   A 1 125 ? 27.13200 14.17200  27.97200 1.000 61.68943  ?  277 MET   A CB   1 
ATOM   793  C  CG   . MET   A 1 125 ? 27.24300 12.70800  27.61400 1.000 61.37883  ?  277 MET   A CG   1 
ATOM   794  S  SD   . MET   A 1 125 ? 28.94900 12.22400  27.38600 1.000 65.04807  ?  277 MET   A SD   1 
ATOM   795  C  CE   . MET   A 1 125 ? 29.41700 13.31500  26.04300 1.000 68.60629  ?  277 MET   A CE   1 
ATOM   796  N  N    . ASP   A 1 126 ? 25.06300 16.98600  28.40600 1.000 70.70449  ?  278 ASP   A N    1 
ATOM   797  C  CA   . ASP   A 1 126 ? 24.88800 18.21900  29.16500 1.000 79.40713  ?  278 ASP   A CA   1 
ATOM   798  C  C    . ASP   A 1 126 ? 23.99800 17.98800  30.38000 1.000 76.88180  ?  278 ASP   A C    1 
ATOM   799  O  O    . ASP   A 1 126 ? 24.32300 18.41400  31.49500 1.000 80.78795  ?  278 ASP   A O    1 
ATOM   800  C  CB   . ASP   A 1 126 ? 24.30100 19.30400  28.26100 1.000 88.64934  ?  278 ASP   A CB   1 
ATOM   801  C  CG   . ASP   A 1 126 ? 25.16700 19.57900  27.04600 1.000 95.82293  ?  278 ASP   A CG   1 
ATOM   802  O  OD1  . ASP   A 1 126 ? 24.69100 20.26200  26.11400 1.000 97.80498  ?  278 ASP   A OD1  1 
ATOM   803  O  OD2  . ASP   A 1 126 ? 26.32900 19.11500  27.02700 1.000 97.85170  ?  278 ASP   A OD2  1 
ATOM   804  N  N    . ASP   A 1 127 ? 22.86900 17.30100  30.18300 1.000 70.62581  ?  279 ASP   A N    1 
ATOM   805  C  CA   . ASP   A 1 127 ? 21.95300 16.99200  31.27300 1.000 69.95902  ?  279 ASP   A CA   1 
ATOM   806  C  C    . ASP   A 1 127 ? 21.53300 15.52600  31.29300 1.000 66.97553  ?  279 ASP   A C    1 
ATOM   807  O  O    . ASP   A 1 127 ? 20.55700 15.18600  31.97400 1.000 68.20185  ?  279 ASP   A O    1 
ATOM   808  C  CB   . ASP   A 1 127 ? 20.71300 17.89100  31.20300 1.000 72.63455  ?  279 ASP   A CB   1 
ATOM   809  C  CG   . ASP   A 1 127 ? 20.08500 17.91400  29.82500 1.000 72.73971  ?  279 ASP   A CG   1 
ATOM   810  O  OD1  . ASP   A 1 127 ? 20.36700 17.00700  29.01300 1.000 70.16538  ?  279 ASP   A OD1  1 
ATOM   811  O  OD2  . ASP   A 1 127 ? 19.31800 18.85700  29.54500 1.000 74.49496  ?  279 ASP   A OD2  1 
ATOM   812  N  N    . MET   A 1 128 ? 22.23800 14.65600  30.56600 1.000 63.00756  ?  280 MET   A N    1 
ATOM   813  C  CA   . MET   A 1 128 ? 21.96000 13.21900  30.54700 1.000 58.16129  ?  280 MET   A CA   1 
ATOM   814  C  C    . MET   A 1 128 ? 20.51500 12.94000  30.13300 1.000 55.21408  ?  280 MET   A C    1 
ATOM   815  O  O    . MET   A 1 128 ? 19.78400 12.19500  30.78800 1.000 53.58884  ?  280 MET   A O    1 
ATOM   816  C  CB   . MET   A 1 128 ? 22.27800 12.58100  31.90200 1.000 59.62893  ?  280 MET   A CB   1 
ATOM   817  C  CG   . MET   A 1 128 ? 23.69200 12.85400  32.38200 1.000 60.60633  ?  280 MET   A CG   1 
ATOM   818  S  SD   . MET   A 1 128 ? 24.91400 12.30100  31.18200 1.000 60.95316  ?  280 MET   A SD   1 
ATOM   819  C  CE   . MET   A 1 128 ? 26.43300 12.88300  31.93400 1.000 59.70014  ?  280 MET   A CE   1 
ATOM   820  N  N    . SER   A 1 129 ? 20.10600 13.54600  29.02300 1.000 54.00584  ?  281 SER   A N    1 
ATOM   821  C  CA   . SER   A 1 129 ? 18.74600 13.41200  28.53000 1.000 55.33895  ?  281 SER   A CA   1 
ATOM   822  C  C    . SER   A 1 129 ? 18.76200 13.07700  27.04700 1.000 57.10619  ?  281 SER   A C    1 
ATOM   823  O  O    . SER   A 1 129 ? 19.73400 13.34300  26.33600 1.000 58.52098  ?  281 SER   A O    1 
ATOM   824  C  CB   . SER   A 1 129 ? 17.93600 14.69300  28.77500 1.000 56.64314  ?  281 SER   A CB   1 
ATOM   825  O  OG   . SER   A 1 129 ? 18.14500 15.63200  27.73400 1.000 59.08657  ?  281 SER   A OG   1 
ATOM   826  N  N    . TRP   A 1 130 ? 17.66800 12.47300  26.59100 1.000 58.24760  ?  282 TRP   A N    1 
ATOM   827  C  CA   . TRP   A 1 130 ? 17.44600 12.22400  25.16800 1.000 55.49338  ?  282 TRP   A CA   1 
ATOM   828  C  C    . TRP   A 1 130 ? 16.64400 13.40000  24.62700 1.000 55.07409  ?  282 TRP   A C    1 
ATOM   829  O  O    . TRP   A 1 130 ? 15.43100 13.48400  24.82900 1.000 57.06407  ?  282 TRP   A O    1 
ATOM   830  C  CB   . TRP   A 1 130 ? 16.72100 10.90000  24.95200 1.000 53.11282  ?  282 TRP   A CB   1 
ATOM   831  C  CG   . TRP   A 1 130 ? 17.54600 9.67200   25.25200 1.000 50.39205  ?  282 TRP   A CG   1 
ATOM   832  C  CD1  . TRP   A 1 130 ? 18.31700 8.96600   24.37200 1.000 46.01407  ?  282 TRP   A CD1  1 
ATOM   833  C  CD2  . TRP   A 1 130 ? 17.66200 8.99700   26.51400 1.000 50.36033  ?  282 TRP   A CD2  1 
ATOM   834  N  NE1  . TRP   A 1 130 ? 18.90500 7.89600   25.00700 1.000 43.98864  ?  282 TRP   A NE1  1 
ATOM   835  C  CE2  . TRP   A 1 130 ? 18.52200 7.89600   26.32300 1.000 45.23407  ?  282 TRP   A CE2  1 
ATOM   836  C  CE3  . TRP   A 1 130 ? 17.12300 9.21800   27.78600 1.000 50.63447  ?  282 TRP   A CE3  1 
ATOM   837  C  CZ2  . TRP   A 1 130 ? 18.85500 7.02200   27.35400 1.000 45.43574  ?  282 TRP   A CZ2  1 
ATOM   838  C  CZ3  . TRP   A 1 130 ? 17.45500 8.34600   28.80900 1.000 48.96881  ?  282 TRP   A CZ3  1 
ATOM   839  C  CH2  . TRP   A 1 130 ? 18.31100 7.26200   28.58700 1.000 48.07138  ?  282 TRP   A CH2  1 
ATOM   840  N  N    . ASP   A 1 131 ? 17.32500 14.32000  23.95100 1.000 56.82726  ?  283 ASP   A N    1 
ATOM   841  C  CA   . ASP   A 1 131 ? 16.69800 15.53200  23.43300 1.000 61.33442  ?  283 ASP   A CA   1 
ATOM   842  C  C    . ASP   A 1 131 ? 16.27600 15.28000  21.99000 1.000 58.25089  ?  283 ASP   A C    1 
ATOM   843  O  O    . ASP   A 1 131 ? 17.11900 15.21000  21.09100 1.000 56.28090  ?  283 ASP   A O    1 
ATOM   844  C  CB   . ASP   A 1 131 ? 17.65900 16.71600  23.53800 1.000 64.03169  ?  283 ASP   A CB   1 
ATOM   845  C  CG   . ASP   A 1 131 ? 17.00800 18.04100  23.18000 1.000 69.63842  ?  283 ASP   A CG   1 
ATOM   846  O  OD1  . ASP   A 1 131 ? 15.87000 18.04100  22.66400 1.000 70.96987  ?  283 ASP   A OD1  1 
ATOM   847  O  OD2  . ASP   A 1 131 ? 17.63700 19.09300  23.42500 1.000 72.84955  ?  283 ASP   A OD2  1 
ATOM   848  N  N    . CYS   A 1 132 ? 14.97000 15.14900  21.76700 1.000 61.68660  ?  284 CYS   A N    1 
ATOM   849  C  CA   . CYS   A 1 132 ? 14.41600 14.90800  20.43800 1.000 58.13303  ?  284 CYS   A CA   1 
ATOM   850  C  C    . CYS   A 1 132 ? 13.69500 16.13300  19.87700 1.000 61.64016  ?  284 CYS   A C    1 
ATOM   851  O  O    . CYS   A 1 132 ? 12.61400 16.02500  19.29000 1.000 55.13018  ?  284 CYS   A O    1 
ATOM   852  C  CB   . CYS   A 1 132 ? 13.48600 13.69700  20.44400 1.000 53.52471  ?  284 CYS   A CB   1 
ATOM   853  S  SG   . CYS   A 1 132 ? 14.27100 12.10000  20.78000 1.000 48.71136  ?  284 CYS   A SG   1 
ATOM   854  N  N    . GLY   A 1 133 ? 14.29100 17.31700  20.04300 1.000 66.25305  ?  285 GLY   A N    1 
ATOM   855  C  CA   . GLY   A 1 133 ? 13.87000 18.51300  19.35500 1.000 68.36378  ?  285 GLY   A CA   1 
ATOM   856  C  C    . GLY   A 1 133 ? 13.02900 19.47100  20.17800 1.000 71.67779  ?  285 GLY   A C    1 
ATOM   857  O  O    . GLY   A 1 133 ? 13.01400 20.67200  19.88000 1.000 72.22648  ?  285 GLY   A O    1 
ATOM   858  N  N    . SER   A 1 134 ? 12.32900 18.97900  21.19700 1.000 73.19389  ?  286 SER   A N    1 
ATOM   859  C  CA   . SER   A 1 134 ? 11.43500 19.83300  21.96500 1.000 77.02337  ?  286 SER   A CA   1 
ATOM   860  C  C    . SER   A 1 134 ? 11.40000 19.36500  23.41200 1.000 77.42058  ?  286 SER   A C    1 
ATOM   861  O  O    . SER   A 1 134 ? 11.72500 18.21600  23.72400 1.000 74.12851  ?  286 SER   A O    1 
ATOM   862  C  CB   . SER   A 1 134 ? 10.01900 19.84300  21.37300 1.000 79.06056  ?  286 SER   A CB   1 
ATOM   863  O  OG   . SER   A 1 134 ? 9.16100  18.96500  22.08000 1.000 80.04896  ?  286 SER   A OG   1 
ATOM   864  N  N    . GLN   A 1 135 ? 10.99300 20.28100  24.29500 1.000 82.14189  ?  287 GLN   A N    1 
ATOM   865  C  CA   . GLN   A 1 135 ? 10.89000 19.95600  25.71400 1.000 86.98464  ?  287 GLN   A CA   1 
ATOM   866  C  C    . GLN   A 1 135 ? 9.90100  18.82300  25.95100 1.000 86.82737  ?  287 GLN   A C    1 
ATOM   867  O  O    . GLN   A 1 135 ? 10.15100 17.93200  26.77200 1.000 85.31575  ?  287 GLN   A O    1 
ATOM   868  C  CB   . GLN   A 1 135 ? 10.47900 21.19700  26.50700 1.000 93.72658  ?  287 GLN   A CB   1 
ATOM   869  C  CG   . GLN   A 1 135 ? 10.83000 21.12800  27.98200 1.000 96.46535  ?  287 GLN   A CG   1 
ATOM   870  C  CD   . GLN   A 1 135 ? 12.32200 21.20400  28.22400 1.000 97.74415  ?  287 GLN   A CD   1 
ATOM   871  O  OE1  . GLN   A 1 135 ? 12.86500 20.47100  29.05000 1.000 97.41160  ?  287 GLN   A OE1  1 
ATOM   872  N  NE2  . GLN   A 1 135 ? 12.99600 22.09200  27.50100 1.000 99.58141  ?  287 GLN   A NE2  1 
ATOM   873  N  N    . ASP   A 1 136 ? 8.76800  18.84600  25.24600 1.000 89.17855  ?  288 ASP   A N    1 
ATOM   874  C  CA   . ASP   A 1 136 ? 7.80700  17.75300  25.34700 1.000 89.28903  ?  288 ASP   A CA   1 
ATOM   875  C  C    . ASP   A 1 136 ? 8.45700  16.42100  25.00100 1.000 81.91005  ?  288 ASP   A C    1 
ATOM   876  O  O    . ASP   A 1 136 ? 8.16100  15.39200  25.62200 1.000 79.77950  ?  288 ASP   A O    1 
ATOM   877  C  CB   . ASP   A 1 136 ? 6.61500  18.02300  24.42700 1.000 94.98265  ?  288 ASP   A CB   1 
ATOM   878  C  CG   . ASP   A 1 136 ? 5.36900  18.42900  25.18900 1.000 103.75940 ?  288 ASP   A CG   1 
ATOM   879  O  OD1  . ASP   A 1 136 ? 4.33900  18.71400  24.54000 1.000 107.37086 ?  288 ASP   A OD1  1 
ATOM   880  O  OD2  . ASP   A 1 136 ? 5.41800  18.46300  26.43600 1.000 107.51103 ?  288 ASP   A OD2  1 
ATOM   881  N  N    . TYR   A 1 137 ? 9.35800  16.42400  24.02300 1.000 75.86474  ?  289 TYR   A N    1 
ATOM   882  C  CA   . TYR   A 1 137 ? 10.03000 15.22200  23.54500 1.000 69.60418  ?  289 TYR   A CA   1 
ATOM   883  C  C    . TYR   A 1 137 ? 11.49300 15.20900  23.97900 1.000 66.55119  ?  289 TYR   A C    1 
ATOM   884  O  O    . TYR   A 1 137 ? 12.39000 14.84400  23.21700 1.000 62.98386  ?  289 TYR   A O    1 
ATOM   885  C  CB   . TYR   A 1 137 ? 9.89700  15.11000  22.02900 1.000 68.11860  ?  289 TYR   A CB   1 
ATOM   886  C  CG   . TYR   A 1 137 ? 8.46900  15.27500  21.55200 1.000 68.91175  ?  289 TYR   A CG   1 
ATOM   887  C  CD1  . TYR   A 1 137 ? 7.40600  14.78200  22.30100 1.000 68.92841  ?  289 TYR   A CD1  1 
ATOM   888  C  CD2  . TYR   A 1 137 ? 8.18100  15.94700  20.37200 1.000 70.95400  ?  289 TYR   A CD2  1 
ATOM   889  C  CE1  . TYR   A 1 137 ? 6.10200  14.93900  21.88200 1.000 73.04808  ?  289 TYR   A CE1  1 
ATOM   890  C  CE2  . TYR   A 1 137 ? 6.87500  16.11000  19.94300 1.000 74.32246  ?  289 TYR   A CE2  1 
ATOM   891  C  CZ   . TYR   A 1 137 ? 5.83900  15.60200  20.70300 1.000 75.03468  ?  289 TYR   A CZ   1 
ATOM   892  O  OH   . TYR   A 1 137 ? 4.53700  15.75700  20.28600 1.000 76.90486  ?  289 TYR   A OH   1 
ATOM   893  N  N    . LYS   A 1 138 ? 11.72500 15.64400  25.21500 1.000 65.96281  ?  290 LYS   A N    1 
ATOM   894  C  CA   . LYS   A 1 138 ? 13.06800 15.63200  25.84100 1.000 66.08979  ?  290 LYS   A CA   1 
ATOM   895  C  C    . LYS   A 1 138 ? 12.95800 14.69000  27.03300 1.000 62.84663  ?  290 LYS   A C    1 
ATOM   896  O  O    . LYS   A 1 138 ? 12.31300 15.05700  27.96900 1.000 65.63817  ?  290 LYS   A O    1 
ATOM   897  C  CB   . LYS   A 1 138 ? 13.47200 17.05600  26.21000 1.000 71.07255  ?  290 LYS   A CB   1 
ATOM   898  C  CG   . LYS   A 1 138 ? 14.96600 17.29600  26.31500 1.000 75.03914  ?  290 LYS   A CG   1 
ATOM   899  C  CD   . LYS   A 1 138 ? 15.31900 18.06700  27.56000 1.000 81.75980  ?  290 LYS   A CD   1 
ATOM   900  C  CE   . LYS   A 1 138 ? 16.80600 18.22700  27.78900 1.000 83.51360  ?  290 LYS   A CE   1 
ATOM   901  N  NZ   . LYS   A 1 138 ? 17.30600 19.43100  27.10300 1.000 85.50676  ?  290 LYS   A NZ   1 
ATOM   902  N  N    . TYR   A 1 139 ? 13.60000 13.52900  26.97600 1.000 56.30698  ?  291 TYR   A N    1 
ATOM   903  C  CA   . TYR   A 1 139 ? 13.40900 12.47100  27.95800 1.000 55.98777  ?  291 TYR   A CA   1 
ATOM   904  C  C    . TYR   A 1 139 ? 14.63100 12.34100  28.85700 1.000 58.76663  ?  291 TYR   A C    1 
ATOM   905  O  O    . TYR   A 1 139 ? 15.76600 12.30800  28.36900 1.000 56.34747  ?  291 TYR   A O    1 
ATOM   906  C  CB   . TYR   A 1 139 ? 13.12100 11.13900  27.26500 1.000 53.65774  ?  291 TYR   A CB   1 
ATOM   907  C  CG   . TYR   A 1 139 ? 12.11900 11.24400  26.13500 1.000 52.13223  ?  291 TYR   A CG   1 
ATOM   908  C  CD1  . TYR   A 1 139 ? 10.74900 11.24300  26.38700 1.000 55.41494  ?  291 TYR   A CD1  1 
ATOM   909  C  CD2  . TYR   A 1 139 ? 12.54200 11.35000  24.81900 1.000 53.44217  ?  291 TYR   A CD2  1 
ATOM   910  C  CE1  . TYR   A 1 139 ? 9.82500  11.33900  25.35200 1.000 51.26811  ?  291 TYR   A CE1  1 
ATOM   911  C  CE2  . TYR   A 1 139 ? 11.63000 11.44900  23.77700 1.000 53.43965  ?  291 TYR   A CE2  1 
ATOM   912  C  CZ   . TYR   A 1 139 ? 10.27500 11.44300  24.05100 1.000 54.29725  ?  291 TYR   A CZ   1 
ATOM   913  O  OH   . TYR   A 1 139 ? 9.37700  11.54000  23.01000 1.000 54.15212  ?  291 TYR   A OH   1 
ATOM   914  N  N    . ASP   A 1 140 ? 14.39400 12.25800  30.16300 1.000 60.74361  ?  292 ASP   A N    1 
ATOM   915  C  CA   . ASP   A 1 140 ? 15.43500 12.01400  31.15600 1.000 63.02994  ?  292 ASP   A CA   1 
ATOM   916  C  C    . ASP   A 1 140 ? 15.09300 10.75600  31.95900 1.000 57.67730  ?  292 ASP   A C    1 
ATOM   917  O  O    . ASP   A 1 140 ? 14.15400 10.02000  31.63800 1.000 55.06564  ?  292 ASP   A O    1 
ATOM   918  C  CB   . ASP   A 1 140 ? 15.62000 13.23900  32.05700 1.000 69.64709  ?  292 ASP   A CB   1 
ATOM   919  C  CG   . ASP   A 1 140 ? 14.34100 13.65400  32.75400 1.000 74.11201  ?  292 ASP   A CG   1 
ATOM   920  O  OD1  . ASP   A 1 140 ? 14.03400 14.86300  32.75600 1.000 78.83775  ?  292 ASP   A OD1  1 
ATOM   921  O  OD2  . ASP   A 1 140 ? 13.63900 12.77900  33.29600 1.000 74.09525  ?  292 ASP   A OD2  1 
ATOM   922  N  N    . VAL   A 1 141 ? 15.86100 10.51900  33.02600 1.000 58.47601  ?  293 VAL   A N    1 
ATOM   923  C  CA   . VAL   A 1 141 ? 15.67000 9.30200   33.80500 1.000 56.07043  ?  293 VAL   A CA   1 
ATOM   924  C  C    . VAL   A 1 141 ? 14.33700 9.30300   34.54300 1.000 58.37813  ?  293 VAL   A C    1 
ATOM   925  O  O    . VAL   A 1 141 ? 13.81300 8.22800   34.85800 1.000 57.14449  ?  293 VAL   A O    1 
ATOM   926  C  CB   . VAL   A 1 141 ? 16.84900 9.09300   34.77400 1.000 53.34213  ?  293 VAL   A CB   1 
ATOM   927  C  CG1  . VAL   A 1 141 ? 18.15900 9.15900   34.01900 1.000 54.69422  ?  293 VAL   A CG1  1 
ATOM   928  C  CG2  . VAL   A 1 141 ? 16.82600 10.13000  35.88100 1.000 53.11140  ?  293 VAL   A CG2  1 
ATOM   929  N  N    . THR   A 1 142 ? 13.76400 10.48000  34.81600 1.000 61.64473  ?  294 THR   A N    1 
ATOM   930  C  CA   . THR   A 1 142 ? 12.43300 10.52900  35.41200 1.000 62.76215  ?  294 THR   A CA   1 
ATOM   931  C  C    . THR   A 1 142 ? 11.38900 9.96400   34.45800 1.000 59.58063  ?  294 THR   A C    1 
ATOM   932  O  O    . THR   A 1 142 ? 10.46600 9.26000   34.88100 1.000 58.18633  ?  294 THR   A O    1 
ATOM   933  C  CB   . THR   A 1 142 ? 12.08000 11.96500  35.80400 1.000 66.14963  ?  294 THR   A CB   1 
ATOM   934  O  OG1  . THR   A 1 142 ? 12.95700 12.40900  36.84600 1.000 68.89561  ?  294 THR   A OG1  1 
ATOM   935  C  CG2  . THR   A 1 142 ? 10.63700 12.06100  36.27800 1.000 70.28055  ?  294 THR   A CG2  1 
ATOM   936  N  N    . ASP   A 1 143 ? 11.52800 10.25100  33.16200 1.000 55.83641  ?  295 ASP   A N    1 
ATOM   937  C  CA   . ASP   A 1 143 ? 10.57400 9.72900   32.19000 1.000 55.79742  ?  295 ASP   A CA   1 
ATOM   938  C  C    . ASP   A 1 143 ? 10.70300 8.21700   32.04300 1.000 54.12204  ?  295 ASP   A C    1 
ATOM   939  O  O    . ASP   A 1 143 ? 9.69400  7.52000   31.88700 1.000 50.19841  ?  295 ASP   A O    1 
ATOM   940  C  CB   . ASP   A 1 143 ? 10.76000 10.43400  30.84800 1.000 54.58135  ?  295 ASP   A CB   1 
ATOM   941  C  CG   . ASP   A 1 143 ? 10.55200 11.93200  30.95200 1.000 61.33317  ?  295 ASP   A CG   1 
ATOM   942  O  OD1  . ASP   A 1 143 ? 9.77800  12.35800  31.83400 1.000 67.06874  ?  295 ASP   A OD1  1 
ATOM   943  O  OD2  . ASP   A 1 143 ? 11.16200 12.68400  30.16600 1.000 62.09162  ?  295 ASP   A OD2  1 
ATOM   944  N  N    . VAL   A 1 144 ? 11.92900 7.68900   32.10400 1.000 49.87291  ?  296 VAL   A N    1 
ATOM   945  C  CA   . VAL   A 1 144 ? 12.10100 6.23800   32.11700 1.000 47.76419  ?  296 VAL   A CA   1 
ATOM   946  C  C    . VAL   A 1 144 ? 11.40700 5.64000   33.32800 1.000 53.65497  ?  296 VAL   A C    1 
ATOM   947  O  O    . VAL   A 1 144 ? 10.77400 4.58100   33.24200 1.000 51.79076  ?  296 VAL   A O    1 
ATOM   948  C  CB   . VAL   A 1 144 ? 13.59200 5.85800   32.10300 1.000 48.69255  ?  296 VAL   A CB   1 
ATOM   949  C  CG1  . VAL   A 1 144 ? 13.75000 4.41800   31.63600 1.000 47.57935  ?  296 VAL   A CG1  1 
ATOM   950  C  CG2  . VAL   A 1 144 ? 14.39600 6.81200   31.24400 1.000 44.18186  ?  296 VAL   A CG2  1 
ATOM   951  N  N    . SER   A 1 145 ? 11.53900 6.29700   34.48400 1.000 56.66590  ?  297 SER   A N    1 
ATOM   952  C  CA   . SER   A 1 145 ? 10.88200 5.81800   35.69400 1.000 59.89429  ?  297 SER   A CA   1 
ATOM   953  C  C    . SER   A 1 145 ? 9.37000  5.80900   35.53000 1.000 58.31715  ?  297 SER   A C    1 
ATOM   954  O  O    . SER   A 1 145 ? 8.69600  4.87200   35.97300 1.000 53.19414  ?  297 SER   A O    1 
ATOM   955  C  CB   . SER   A 1 145 ? 11.27800 6.68700   36.88600 1.000 63.00544  ?  297 SER   A CB   1 
ATOM   956  O  OG   . SER   A 1 145 ? 12.39000 6.13800   37.56700 1.000 69.46211  ?  297 SER   A OG   1 
ATOM   957  N  N    . LYS   A 1 146 ? 8.82100  6.83900   34.88800 1.000 59.49730  ?  298 LYS   A N    1 
ATOM   958  C  CA   . LYS   A 1 146 ? 7.38200  6.95700   34.68700 1.000 60.96759  ?  298 LYS   A CA   1 
ATOM   959  C  C    . LYS   A 1 146 ? 6.86200  6.03800   33.58700 1.000 60.27304  ?  298 LYS   A C    1 
ATOM   960  O  O    . LYS   A 1 146 ? 5.70800  6.18200   33.17500 1.000 59.12847  ?  298 LYS   A O    1 
ATOM   961  C  CB   . LYS   A 1 146 ? 7.00800  8.41100   34.38200 1.000 62.52092  ?  298 LYS   A CB   1 
ATOM   962  C  CG   . LYS   A 1 146 ? 7.23300  9.38100   35.54100 1.000 66.03131  ?  298 LYS   A CG   1 
ATOM   963  C  CD   . LYS   A 1 146 ? 7.12200  8.67400   36.89100 1.000 73.29641  ?  298 LYS   A CD   1 
ATOM   964  C  CE   . LYS   A 1 146 ? 6.37400  9.50600   37.92700 1.000 80.46185  ?  298 LYS   A CE   1 
ATOM   965  N  NZ   . LYS   A 1 146 ? 6.90500  9.27100   39.30400 1.000 82.05292  ?  298 LYS   A NZ   1 
ATOM   966  N  N    . ALA   A 1 147 ? 7.69400  5.11600   33.10100 1.000 58.10278  ?  299 ALA   A N    1 
ATOM   967  C  CA   . ALA   A 1 147 ? 7.26100  4.01500   32.25500 1.000 54.46189  ?  299 ALA   A CA   1 
ATOM   968  C  C    . ALA   A 1 147 ? 7.35900  2.67000   32.96200 1.000 53.17881  ?  299 ALA   A C    1 
ATOM   969  O  O    . ALA   A 1 147 ? 7.12800  1.63500   32.32800 1.000 45.39006  ?  299 ALA   A O    1 
ATOM   970  C  CB   . ALA   A 1 147 ? 8.08300  3.98000   30.96000 1.000 53.89114  ?  299 ALA   A CB   1 
ATOM   971  N  N    . GLY   A 1 148 ? 7.72400  2.65600   34.24700 1.000 56.26016  ?  300 GLY   A N    1 
ATOM   972  C  CA   . GLY   A 1 148 ? 7.75100  1.44200   35.04200 1.000 55.30488  ?  300 GLY   A CA   1 
ATOM   973  C  C    . GLY   A 1 148 ? 9.12600  0.87800   35.33900 1.000 50.75094  ?  300 GLY   A C    1 
ATOM   974  O  O    . GLY   A 1 148 ? 9.21800  -0.12200  36.06100 1.000 47.62857  ?  300 GLY   A O    1 
ATOM   975  N  N    . HIS   A 1 149 ? 10.19300 1.46900   34.81900 1.000 47.92905  ?  301 HIS   A N    1 
ATOM   976  C  CA   . HIS   A 1 149 ? 11.52100 0.89400   34.95600 1.000 48.31678  ?  301 HIS   A CA   1 
ATOM   977  C  C    . HIS   A 1 149 ? 12.26000 1.49000   36.14800 1.000 50.27740  ?  301 HIS   A C    1 
ATOM   978  O  O    . HIS   A 1 149 ? 12.02100 2.63400   36.54300 1.000 48.88073  ?  301 HIS   A O    1 
ATOM   979  C  CB   . HIS   A 1 149 ? 12.32300 1.09600   33.67300 1.000 46.87207  ?  301 HIS   A CB   1 
ATOM   980  C  CG   . HIS   A 1 149 ? 11.86300 0.22600   32.54800 1.000 45.21160  ?  301 HIS   A CG   1 
ATOM   981  N  ND1  . HIS   A 1 149 ? 11.92200 -1.15000  32.60200 1.000 44.87093  ?  301 HIS   A ND1  1 
ATOM   982  C  CD2  . HIS   A 1 149 ? 11.31100 0.53400   31.35000 1.000 41.60376  ?  301 HIS   A CD2  1 
ATOM   983  C  CE1  . HIS   A 1 149 ? 11.43400 -1.65300  31.48200 1.000 41.80685  ?  301 HIS   A CE1  1 
ATOM   984  N  NE2  . HIS   A 1 149 ? 11.06600 -0.65200  30.70100 1.000 42.15884  ?  301 HIS   A NE2  1 
ATOM   985  N  N    . THR   A 1 150 ? 13.16700 0.69600   36.71300 1.000 55.14783  ?  302 THR   A N    1 
ATOM   986  C  CA   . THR   A 1 150 ? 13.88300 1.01800   37.93900 1.000 52.81476  ?  302 THR   A CA   1 
ATOM   987  C  C    . THR   A 1 150 ? 15.36000 1.25700   37.65200 1.000 54.01245  ?  302 THR   A C    1 
ATOM   988  O  O    . THR   A 1 150 ? 15.87300 0.90100   36.58700 1.000 54.28732  ?  302 THR   A O    1 
ATOM   989  C  CB   . THR   A 1 150 ? 13.74500 -0.11400  38.96000 1.000 55.55610  ?  302 THR   A CB   1 
ATOM   990  O  OG1  . THR   A 1 150 ? 14.56300 -1.21800  38.55000 1.000 56.96711  ?  302 THR   A OG1  1 
ATOM   991  C  CG2  . THR   A 1 150 ? 12.29700 -0.57500  39.04900 1.000 55.35224  ?  302 THR   A CG2  1 
ATOM   992  N  N    . LEU   A 1 151 ? 16.05000 1.84000   38.64000 1.000 53.58994  ?  303 LEU   A N    1 
ATOM   993  C  CA   . LEU   A 1 151 ? 17.46000 2.18600   38.47200 1.000 51.43453  ?  303 LEU   A CA   1 
ATOM   994  C  C    . LEU   A 1 151 ? 18.31600 0.97700   38.11300 1.000 48.99676  ?  303 LEU   A C    1 
ATOM   995  O  O    . LEU   A 1 151 ? 19.38400 1.14800   37.51000 1.000 47.82046  ?  303 LEU   A O    1 
ATOM   996  C  CB   . LEU   A 1 151 ? 17.99600 2.85300   39.74000 1.000 54.48845  ?  303 LEU   A CB   1 
ATOM   997  C  CG   . LEU   A 1 151 ? 19.00600 3.98300   39.51200 1.000 60.06893  ?  303 LEU   A CG   1 
ATOM   998  C  CD1  . LEU   A 1 151 ? 18.29000 5.24800   39.03800 1.000 63.23845  ?  303 LEU   A CD1  1 
ATOM   999  C  CD2  . LEU   A 1 151 ? 19.86100 4.25600   40.75700 1.000 59.99425  ?  303 LEU   A CD2  1 
ATOM   1000 N  N    . GLU   A 1 152 ? 17.86500 -0.23700  38.45500 1.000 47.09075  ?  304 GLU   A N    1 
ATOM   1001 C  CA   . GLU   A 1 152 ? 18.52900 -1.45300  37.99000 1.000 49.84355  ?  304 GLU   A CA   1 
ATOM   1002 C  C    . GLU   A 1 152 ? 18.82800 -1.39100  36.49600 1.000 52.05711  ?  304 GLU   A C    1 
ATOM   1003 O  O    . GLU   A 1 152 ? 19.86700 -1.88100  36.03700 1.000 46.47700  ?  304 GLU   A O    1 
ATOM   1004 C  CB   . GLU   A 1 152 ? 17.65800 -2.67100  38.29900 1.000 54.64210  ?  304 GLU   A CB   1 
ATOM   1005 C  CG   . GLU   A 1 152 ? 17.69100 -3.12700  39.74100 1.000 64.98679  ?  304 GLU   A CG   1 
ATOM   1006 C  CD   . GLU   A 1 152 ? 18.81300 -4.11000  40.01800 1.000 75.91322  ?  304 GLU   A CD   1 
ATOM   1007 O  OE1  . GLU   A 1 152 ? 19.94900 -3.87100  39.55200 1.000 77.94693  ?  304 GLU   A OE1  1 
ATOM   1008 O  OE2  . GLU   A 1 152 ? 18.55700 -5.12400  40.70200 1.000 81.03831  ?  304 GLU   A OE2  1 
ATOM   1009 N  N    . LEU   A 1 153 ? 17.92500 -0.79100  35.72000 1.000 48.53903  ?  305 LEU   A N    1 
ATOM   1010 C  CA   . LEU   A 1 153 ? 18.13500 -0.57800  34.29600 1.000 41.27562  ?  305 LEU   A CA   1 
ATOM   1011 C  C    . LEU   A 1 153 ? 18.68900 0.80900   33.98800 1.000 42.89212  ?  305 LEU   A C    1 
ATOM   1012 O  O    . LEU   A 1 153 ? 19.64500 0.93300   33.21300 1.000 41.54467  ?  305 LEU   A O    1 
ATOM   1013 C  CB   . LEU   A 1 153 ? 16.82000 -0.80400  33.54300 1.000 38.35292  ?  305 LEU   A CB   1 
ATOM   1014 C  CG   . LEU   A 1 153 ? 16.79900 -0.57700  32.03200 1.000 38.35329  ?  305 LEU   A CG   1 
ATOM   1015 C  CD1  . LEU   A 1 153 ? 17.59000 -1.65600  31.31700 1.000 37.62983  ?  305 LEU   A CD1  1 
ATOM   1016 C  CD2  . LEU   A 1 153 ? 15.35700 -0.54100  31.53600 1.000 38.50637  ?  305 LEU   A CD2  1 
ATOM   1017 N  N    . ILE   A 1 154 ? 18.12200 1.85800   34.59700 1.000 43.75373  ?  306 ILE   A N    1 
ATOM   1018 C  CA   . ILE   A 1 154 ? 18.47300 3.22500   34.20800 1.000 49.22773  ?  306 ILE   A CA   1 
ATOM   1019 C  C    . ILE   A 1 154 ? 19.94900 3.50600   34.45900 1.000 46.88485  ?  306 ILE   A C    1 
ATOM   1020 O  O    . ILE   A 1 154 ? 20.62600 4.11500   33.62000 1.000 43.46769  ?  306 ILE   A O    1 
ATOM   1021 C  CB   . ILE   A 1 154 ? 17.57500 4.25200   34.92500 1.000 53.50045  ?  306 ILE   A CB   1 
ATOM   1022 C  CG1  . ILE   A 1 154 ? 16.13100 4.14300   34.43700 1.000 56.62104  ?  306 ILE   A CG1  1 
ATOM   1023 C  CG2  . ILE   A 1 154 ? 18.07500 5.66000   34.68100 1.000 51.15877  ?  306 ILE   A CG2  1 
ATOM   1024 C  CD1  . ILE   A 1 154 ? 15.25800 3.23300   35.24500 1.000 60.60494  ?  306 ILE   A CD1  1 
ATOM   1025 N  N    . GLU   A 1 155 ? 20.47500 3.07300   35.61200 1.000 47.01809  ?  307 GLU   A N    1 
ATOM   1026 C  CA   . GLU   A 1 155 ? 21.86900 3.37300   35.93500 1.000 49.56734  ?  307 GLU   A CA   1 
ATOM   1027 C  C    . GLU   A 1 155 ? 22.82700 2.79800   34.89900 1.000 48.98793  ?  307 GLU   A C    1 
ATOM   1028 O  O    . GLU   A 1 155 ? 23.60000 3.57200   34.30700 1.000 55.89398  ?  307 GLU   A O    1 
ATOM   1029 C  CB   . GLU   A 1 155 ? 22.18300 2.90900   37.36400 1.000 52.38895  ?  307 GLU   A CB   1 
ATOM   1030 C  CG   . GLU   A 1 155 ? 23.53400 3.38600   37.89800 1.000 58.70592  ?  307 GLU   A CG   1 
ATOM   1031 C  CD   . GLU   A 1 155 ? 24.63500 2.33200   37.80700 1.000 60.12763  ?  307 GLU   A CD   1 
ATOM   1032 O  OE1  . GLU   A 1 155 ? 24.37800 1.21600   37.31400 1.000 58.13220  ?  307 GLU   A OE1  1 
ATOM   1033 O  OE2  . GLU   A 1 155 ? 25.77200 2.62800   38.23200 1.000 62.64257  ?  307 GLU   A OE2  1 
ATOM   1034 N  N    . PRO   A 1 156 ? 22.82500 1.49000   34.60300 1.000 45.97219  ?  308 PRO   A N    1 
ATOM   1035 C  CA   . PRO   A 1 156 ? 23.71700 1.00200   33.53500 1.000 47.07645  ?  308 PRO   A CA   1 
ATOM   1036 C  C    . PRO   A 1 156 ? 23.36800 1.53100   32.15400 1.000 45.44352  ?  308 PRO   A C    1 
ATOM   1037 O  O    . PRO   A 1 156 ? 24.25100 1.56600   31.28600 1.000 46.77214  ?  308 PRO   A O    1 
ATOM   1038 C  CB   . PRO   A 1 156 ? 23.56800 -0.52500  33.60700 1.000 49.02111  ?  308 PRO   A CB   1 
ATOM   1039 C  CG   . PRO   A 1 156 ? 22.31000 -0.76700  34.32400 1.000 49.77198  ?  308 PRO   A CG   1 
ATOM   1040 C  CD   . PRO   A 1 156 ? 22.09400 0.38400   35.25000 1.000 44.36944  ?  308 PRO   A CD   1 
ATOM   1041 N  N    . LEU   A 1 157 ? 22.12300 1.95700   31.92600 1.000 44.19658  ?  309 LEU   A N    1 
ATOM   1042 C  CA   . LEU   A 1 157 ? 21.74500 2.50900   30.63000 1.000 39.05404  ?  309 LEU   A CA   1 
ATOM   1043 C  C    . LEU   A 1 157 ? 22.39600 3.86800   30.39700 1.000 40.05560  ?  309 LEU   A C    1 
ATOM   1044 O  O    . LEU   A 1 157 ? 22.94000 4.13400   29.31500 1.000 36.38295  ?  309 LEU   A O    1 
ATOM   1045 C  CB   . LEU   A 1 157 ? 20.22100 2.62100   30.54500 1.000 38.78099  ?  309 LEU   A CB   1 
ATOM   1046 C  CG   . LEU   A 1 157 ? 19.66300 3.32000   29.30600 1.000 39.43607  ?  309 LEU   A CG   1 
ATOM   1047 C  CD1  . LEU   A 1 157 ? 20.11800 2.59100   28.05000 1.000 38.97334  ?  309 LEU   A CD1  1 
ATOM   1048 C  CD2  . LEU   A 1 157 ? 18.14300 3.40700   29.36700 1.000 39.13626  ?  309 LEU   A CD2  1 
ATOM   1049 N  N    . ILE   A 1 158 ? 22.33000 4.75100   31.39700 1.000 41.91234  ?  310 ILE   A N    1 
ATOM   1050 C  CA   . ILE   A 1 158 ? 22.98700 6.05200   31.29500 1.000 50.25542  ?  310 ILE   A CA   1 
ATOM   1051 C  C    . ILE   A 1 158 ? 24.49700 5.87900   31.18400 1.000 49.38291  ?  310 ILE   A C    1 
ATOM   1052 O  O    . ILE   A 1 158 ? 25.16100 6.57500   30.40400 1.000 52.52970  ?  310 ILE   A O    1 
ATOM   1053 C  CB   . ILE   A 1 158 ? 22.60700 6.94000   32.49500 1.000 55.19771  ?  310 ILE   A CB   1 
ATOM   1054 C  CG1  . ILE   A 1 158 ? 21.12100 7.29700   32.44200 1.000 53.54596  ?  310 ILE   A CG1  1 
ATOM   1055 C  CG2  . ILE   A 1 158 ? 23.45700 8.20800   32.52400 1.000 55.18174  ?  310 ILE   A CG2  1 
ATOM   1056 C  CD1  . ILE   A 1 158 ? 20.79700 8.34200   31.40300 1.000 50.77755  ?  310 ILE   A CD1  1 
ATOM   1057 N  N    . LYS   A 1 159 ? 25.06700 4.95500   31.95900 1.000 44.54625  ?  311 LYS   A N    1 
ATOM   1058 C  CA   . LYS   A 1 159 ? 26.50100 4.70500   31.83800 1.000 48.13527  ?  311 LYS   A CA   1 
ATOM   1059 C  C    . LYS   A 1 159 ? 26.84300 4.20400   30.44300 1.000 46.34242  ?  311 LYS   A C    1 
ATOM   1060 O  O    . LYS   A 1 159 ? 27.90800 4.52200   29.90200 1.000 46.83767  ?  311 LYS   A O    1 
ATOM   1061 C  CB   . LYS   A 1 159 ? 26.96700 3.70700   32.89700 1.000 43.45860  ?  311 LYS   A CB   1 
ATOM   1062 C  CG   . LYS   A 1 159 ? 27.56300 4.35600   34.13000 1.000 54.97407  ?  311 LYS   A CG   1 
ATOM   1063 C  CD   . LYS   A 1 159 ? 27.22400 3.56300   35.37600 1.000 64.86688  ?  311 LYS   A CD   1 
ATOM   1064 C  CE   . LYS   A 1 159 ? 28.48600 3.10800   36.09600 1.000 70.00569  ?  311 LYS   A CE   1 
ATOM   1065 N  NZ   . LYS   A 1 159 ? 28.26100 2.89500   37.55700 1.000 71.43204  ?  311 LYS   A NZ   1 
ATOM   1066 N  N    . PHE   A 1 160 ? 25.94500 3.42300   29.84200 1.000 40.30447  ?  312 PHE   A N    1 
ATOM   1067 C  CA   . PHE   A 1 160 ? 26.15100 2.98900   28.46700 1.000 43.61959  ?  312 PHE   A CA   1 
ATOM   1068 C  C    . PHE   A 1 160 ? 26.09800 4.17300   27.50700 1.000 46.61266  ?  312 PHE   A C    1 
ATOM   1069 O  O    . PHE   A 1 160 ? 26.98400 4.33500   26.65800 1.000 45.58682  ?  312 PHE   A O    1 
ATOM   1070 C  CB   . PHE   A 1 160 ? 25.10400 1.94000   28.09100 1.000 42.52301  ?  312 PHE   A CB   1 
ATOM   1071 C  CG   . PHE   A 1 160 ? 25.03300 1.65500   26.62200 1.000 39.86292  ?  312 PHE   A CG   1 
ATOM   1072 C  CD1  . PHE   A 1 160 ? 25.92400 0.77200   26.03200 1.000 41.13339  ?  312 PHE   A CD1  1 
ATOM   1073 C  CD2  . PHE   A 1 160 ? 24.07700 2.27000   25.82700 1.000 41.30199  ?  312 PHE   A CD2  1 
ATOM   1074 C  CE1  . PHE   A 1 160 ? 25.86000 0.50900   24.67100 1.000 45.77196  ?  312 PHE   A CE1  1 
ATOM   1075 C  CE2  . PHE   A 1 160 ? 24.00900 2.01100   24.47200 1.000 46.52565  ?  312 PHE   A CE2  1 
ATOM   1076 C  CZ   . PHE   A 1 160 ? 24.90500 1.13200   23.89400 1.000 46.99405  ?  312 PHE   A CZ   1 
ATOM   1077 N  N    . GLN   A 1 161 ? 25.05700 5.00700   27.62200 1.000 47.06282  ?  313 GLN   A N    1 
ATOM   1078 C  CA   . GLN   A 1 161 ? 24.92700 6.17200   26.74800 1.000 43.59351  ?  313 GLN   A CA   1 
ATOM   1079 C  C    . GLN   A 1 161 ? 26.13800 7.08700   26.86600 1.000 46.59048  ?  313 GLN   A C    1 
ATOM   1080 O  O    . GLN   A 1 161 ? 26.65700 7.58100   25.85700 1.000 47.14611  ?  313 GLN   A O    1 
ATOM   1081 C  CB   . GLN   A 1 161 ? 23.64400 6.93700   27.08000 1.000 44.23060  ?  313 GLN   A CB   1 
ATOM   1082 C  CG   . GLN   A 1 161 ? 22.35100 6.15600   26.84500 1.000 40.03578  ?  313 GLN   A CG   1 
ATOM   1083 C  CD   . GLN   A 1 161 ? 22.15300 5.80400   25.38700 1.000 41.12694  ?  313 GLN   A CD   1 
ATOM   1084 O  OE1  . GLN   A 1 161 ? 22.53400 6.56700   24.50000 1.000 43.38567  ?  313 GLN   A OE1  1 
ATOM   1085 N  NE2  . GLN   A 1 161 ? 21.54600 4.64900   25.12800 1.000 38.93976  ?  313 GLN   A NE2  1 
ATOM   1086 N  N    . VAL   A 1 162 ? 26.60700 7.31400   28.09300 1.000 46.84535  ?  314 VAL   A N    1 
ATOM   1087 C  CA   . VAL   A 1 162 ? 27.79900 8.12800   28.31200 1.000 46.79821  ?  314 VAL   A CA   1 
ATOM   1088 C  C    . VAL   A 1 162 ? 29.01500 7.48800   27.65100 1.000 45.65645  ?  314 VAL   A C    1 
ATOM   1089 O  O    . VAL   A 1 162 ? 29.77100 8.14800   26.92800 1.000 41.13019  ?  314 VAL   A O    1 
ATOM   1090 C  CB   . VAL   A 1 162 ? 28.02500 8.33600   29.81900 1.000 51.67959  ?  314 VAL   A CB   1 
ATOM   1091 C  CG1  . VAL   A 1 162 ? 29.43700 8.81100   30.08000 1.000 49.11297  ?  314 VAL   A CG1  1 
ATOM   1092 C  CG2  . VAL   A 1 162 ? 27.00100 9.31900   30.37900 1.000 54.41046  ?  314 VAL   A CG2  1 
ATOM   1093 N  N    . GLY   A 1 163 ? 29.22600 6.19300   27.89500 1.000 46.75819  ?  315 GLY   A N    1 
ATOM   1094 C  CA   . GLY   A 1 163 ? 30.39300 5.53000   27.33300 1.000 42.00633  ?  315 GLY   A CA   1 
ATOM   1095 C  C    . GLY   A 1 163 ? 30.35200 5.46100   25.81900 1.000 43.41404  ?  315 GLY   A C    1 
ATOM   1096 O  O    . GLY   A 1 163 ? 31.38200 5.59300   25.15400 1.000 39.17222  ?  315 GLY   A O    1 
ATOM   1097 N  N    . LEU   A 1 164 ? 29.15800 5.26000   25.25100 1.000 41.23241  ?  316 LEU   A N    1 
ATOM   1098 C  CA   . LEU   A 1 164 ? 29.02200 5.26800   23.79900 1.000 41.47914  ?  316 LEU   A CA   1 
ATOM   1099 C  C    . LEU   A 1 164 ? 29.32100 6.64700   23.22900 1.000 45.25829  ?  316 LEU   A C    1 
ATOM   1100 O  O    . LEU   A 1 164 ? 30.05500 6.77600   22.24200 1.000 47.93338  ?  316 LEU   A O    1 
ATOM   1101 C  CB   . LEU   A 1 164 ? 27.61900 4.81800   23.40500 1.000 38.06778  ?  316 LEU   A CB   1 
ATOM   1102 C  CG   . LEU   A 1 164 ? 27.38300 4.61800   21.91000 1.000 40.54461  ?  316 LEU   A CG   1 
ATOM   1103 C  CD1  . LEU   A 1 164 ? 28.44700 3.70000   21.31900 1.000 38.47259  ?  316 LEU   A CD1  1 
ATOM   1104 C  CD2  . LEU   A 1 164 ? 25.98900 4.05700   21.69200 1.000 38.51308  ?  316 LEU   A CD2  1 
ATOM   1105 N  N    . LYS   A 1 165 ? 28.75700 7.69400   23.83800 1.000 46.91378  ?  317 LYS   A N    1 
ATOM   1106 C  CA   . LYS   A 1 165 ? 29.07300 9.05200   23.40500 1.000 51.16924  ?  317 LYS   A CA   1 
ATOM   1107 C  C    . LYS   A 1 165 ? 30.56900 9.34500   23.50600 1.000 54.71005  ?  317 LYS   A C    1 
ATOM   1108 O  O    . LYS   A 1 165 ? 31.11200 10.08200  22.67400 1.000 53.83123  ?  317 LYS   A O    1 
ATOM   1109 C  CB   . LYS   A 1 165 ? 28.26500 10.05700  24.22700 1.000 52.83988  ?  317 LYS   A CB   1 
ATOM   1110 C  CG   . LYS   A 1 165 ? 27.89300 11.31400  23.47300 1.000 55.85604  ?  317 LYS   A CG   1 
ATOM   1111 C  CD   . LYS   A 1 165 ? 26.62300 11.13200  22.67100 1.000 58.91070  ?  317 LYS   A CD   1 
ATOM   1112 C  CE   . LYS   A 1 165 ? 26.13700 12.46100  22.12200 1.000 59.84513  ?  317 LYS   A CE   1 
ATOM   1113 N  NZ   . LYS   A 1 165 ? 24.91600 12.29200  21.28400 1.000 55.53279  ?  317 LYS   A NZ   1 
ATOM   1114 N  N    . LYS   A 1 166 ? 31.24900 8.76300   24.50500 1.000 55.19241  ?  318 LYS   A N    1 
ATOM   1115 C  CA   . LYS   A 1 166 ? 32.69000 8.96500   24.67100 1.000 58.73845  ?  318 LYS   A CA   1 
ATOM   1116 C  C    . LYS   A 1 166 ? 33.47900 8.44700   23.47800 1.000 58.12564  ?  318 LYS   A C    1 
ATOM   1117 O  O    . LYS   A 1 166 ? 34.53200 8.99800   23.13700 1.000 51.86782  ?  318 LYS   A O    1 
ATOM   1118 C  CB   . LYS   A 1 166 ? 33.18900 8.27200   25.94000 1.000 58.63844  ?  318 LYS   A CB   1 
ATOM   1119 C  CG   . LYS   A 1 166 ? 34.61900 8.66500   26.33400 1.000 72.70248  ?  318 LYS   A CG   1 
ATOM   1120 C  CD   . LYS   A 1 166 ? 35.55800 7.45500   26.26000 1.000 75.18456  ?  318 LYS   A CD   1 
ATOM   1121 C  CE   . LYS   A 1 166 ? 36.69400 7.53700   27.27300 1.000 78.44872  ?  318 LYS   A CE   1 
ATOM   1122 N  NZ   . LYS   A 1 166 ? 37.35800 6.21500   27.49200 1.000 79.41998  ?  318 LYS   A NZ   1 
ATOM   1123 N  N    . LEU   A 1 167 ? 33.00600 7.36700   22.85100 1.000 58.11079  ?  319 LEU   A N    1 
ATOM   1124 C  CA   . LEU   A 1 167 ? 33.71300 6.82100   21.70200 1.000 55.51726  ?  319 LEU   A CA   1 
ATOM   1125 C  C    . LEU   A 1 167 ? 33.74300 7.80100   20.53900 1.000 54.49034  ?  319 LEU   A C    1 
ATOM   1126 O  O    . LEU   A 1 167 ? 34.63900 7.70800   19.69200 1.000 53.23508  ?  319 LEU   A O    1 
ATOM   1127 C  CB   . LEU   A 1 167 ? 33.07700 5.49500   21.28000 1.000 50.09130  ?  319 LEU   A CB   1 
ATOM   1128 C  CG   . LEU   A 1 167 ? 33.07600 4.40900   22.36100 1.000 47.61148  ?  319 LEU   A CG   1 
ATOM   1129 C  CD1  . LEU   A 1 167 ? 32.34700 3.16100   21.90100 1.000 45.45250  ?  319 LEU   A CD1  1 
ATOM   1130 C  CD2  . LEU   A 1 167 ? 34.50800 4.07700   22.79300 1.000 49.37447  ?  319 LEU   A CD2  1 
ATOM   1131 N  N    . ASN   A 1 168 ? 32.81000 8.75300   20.50200 1.000 56.19805  ?  320 ASN   A N    1 
ATOM   1132 C  CA   . ASN   A 1 168 ? 32.73900 9.75600   19.44100 1.000 61.48528  ?  320 ASN   A CA   1 
ATOM   1133 C  C    . ASN   A 1 168 ? 32.79600 9.08900   18.06900 1.000 56.66593  ?  320 ASN   A C    1 
ATOM   1134 O  O    . ASN   A 1 168 ? 33.59800 9.45000   17.20300 1.000 59.94109  ?  320 ASN   A O    1 
ATOM   1135 C  CB   . ASN   A 1 168 ? 33.85200 10.79300  19.60000 1.000 69.71895  ?  320 ASN   A CB   1 
ATOM   1136 C  CG   . ASN   A 1 168 ? 33.35300 12.21200  19.42500 1.000 78.51549  ?  320 ASN   A CG   1 
ATOM   1137 O  OD1  . ASN   A 1 168 ? 33.06700 12.65000  18.31000 1.000 81.10116  ?  320 ASN   A OD1  1 
ATOM   1138 N  ND2  . ASN   A 1 168 ? 33.24200 12.94000  20.53200 1.000 82.28648  ?  320 ASN   A ND2  1 
ATOM   1139 N  N    . LEU   A 1 169 ? 31.94500 8.08100   17.89200 1.000 48.99550  ?  321 LEU   A N    1 
ATOM   1140 C  CA   . LEU   A 1 169 ? 31.99500 7.26000   16.69100 1.000 48.20444  ?  321 LEU   A CA   1 
ATOM   1141 C  C    . LEU   A 1 169 ? 31.76000 8.10300   15.44700 1.000 43.93611  ?  321 LEU   A C    1 
ATOM   1142 O  O    . LEU   A 1 169 ? 31.00000 9.07400   15.46800 1.000 42.08083  ?  321 LEU   A O    1 
ATOM   1143 C  CB   . LEU   A 1 169 ? 30.95000 6.14600   16.76300 1.000 45.62565  ?  321 LEU   A CB   1 
ATOM   1144 C  CG   . LEU   A 1 169 ? 31.07700 5.14300   17.90900 1.000 43.83278  ?  321 LEU   A CG   1 
ATOM   1145 C  CD1  . LEU   A 1 169 ? 29.97300 4.10400   17.83700 1.000 39.75780  ?  321 LEU   A CD1  1 
ATOM   1146 C  CD2  . LEU   A 1 169 ? 32.44000 4.48000   17.87300 1.000 45.63722  ?  321 LEU   A CD2  1 
ATOM   1147 N  N    . HIS   A 1 170 ? 32.45200 7.74800   14.36700 1.000 49.17280  ?  322 HIS   A N    1 
ATOM   1148 C  CA   . HIS   A 1 170 ? 32.01900 8.19300   13.05300 1.000 47.38150  ?  322 HIS   A CA   1 
ATOM   1149 C  C    . HIS   A 1 170 ? 30.64500 7.60200   12.76700 1.000 45.41478  ?  322 HIS   A C    1 
ATOM   1150 O  O    . HIS   A 1 170 ? 30.32100 6.50000   13.21500 1.000 50.18623  ?  322 HIS   A O    1 
ATOM   1151 C  CB   . HIS   A 1 170 ? 33.00600 7.75200   11.97100 1.000 44.47744  ?  322 HIS   A CB   1 
ATOM   1152 C  CG   . HIS   A 1 170 ? 34.37000 8.35300   12.10200 1.000 45.71325  ?  322 HIS   A CG   1 
ATOM   1153 N  ND1  . HIS   A 1 170 ? 35.41000 8.01500   11.26300 1.000 48.35217  ?  322 HIS   A ND1  1 
ATOM   1154 C  CD2  . HIS   A 1 170 ? 34.86700 9.26900   12.96700 1.000 47.98800  ?  322 HIS   A CD2  1 
ATOM   1155 C  CE1  . HIS   A 1 170 ? 36.49000 8.69500   11.60700 1.000 51.31079  ?  322 HIS   A CE1  1 
ATOM   1156 N  NE2  . HIS   A 1 170 ? 36.18700 9.46300   12.63800 1.000 48.44453  ?  322 HIS   A NE2  1 
ATOM   1157 N  N    . GLU   A 1 171 ? 29.82100 8.34700   12.02600 1.000 40.46588  ?  323 GLU   A N    1 
ATOM   1158 C  CA   . GLU   A 1 171 ? 28.52800 7.79800   11.62900 1.000 40.07605  ?  323 GLU   A CA   1 
ATOM   1159 C  C    . GLU   A 1 171 ? 28.70500 6.45100   10.94000 1.000 35.88898  ?  323 GLU   A C    1 
ATOM   1160 O  O    . GLU   A 1 171 ? 27.92900 5.51900   11.17200 1.000 39.03839  ?  323 GLU   A O    1 
ATOM   1161 C  CB   . GLU   A 1 171 ? 27.78900 8.77900   10.72200 1.000 44.97829  ?  323 GLU   A CB   1 
ATOM   1162 C  CG   . GLU   A 1 171 ? 26.36500 8.34000   10.38500 1.000 50.31628  ?  323 GLU   A CG   1 
ATOM   1163 C  CD   . GLU   A 1 171 ? 25.55300 9.44800   9.75200  1.000 54.04820  ?  323 GLU   A CD   1 
ATOM   1164 O  OE1  . GLU   A 1 171 ? 26.06100 10.08300  8.80700  1.000 58.36145  ?  323 GLU   A OE1  1 
ATOM   1165 O  OE2  . GLU   A 1 171 ? 24.41100 9.68800   10.19900 1.000 56.86948  ?  323 GLU   A OE2  1 
ATOM   1166 N  N    . GLU   A 1 172 ? 29.75600 6.32400   10.12300 1.000 38.05038  ?  324 GLU   A N    1 
ATOM   1167 C  CA   . GLU   A 1 172 ? 30.09300 5.04100   9.51400  1.000 38.59741  ?  324 GLU   A CA   1 
ATOM   1168 C  C    . GLU   A 1 172 ? 30.21800 3.93800   10.55900 1.000 39.67982  ?  324 GLU   A C    1 
ATOM   1169 O  O    . GLU   A 1 172 ? 29.71300 2.82400   10.36600 1.000 43.69712  ?  324 GLU   A O    1 
ATOM   1170 C  CB   . GLU   A 1 172 ? 31.39700 5.17500   8.72400  1.000 38.14275  ?  324 GLU   A CB   1 
ATOM   1171 C  CG   . GLU   A 1 172 ? 31.28800 6.00300   7.44200  1.000 41.93884  ?  324 GLU   A CG   1 
ATOM   1172 C  CD   . GLU   A 1 172 ? 31.40700 7.50100   7.66800  1.000 43.57471  ?  324 GLU   A CD   1 
ATOM   1173 O  OE1  . GLU   A 1 172 ? 31.39600 7.94500   8.83400  1.000 44.77323  ?  324 GLU   A OE1  1 
ATOM   1174 O  OE2  . GLU   A 1 172 ? 31.51500 8.24000   6.66700  1.000 44.66994  ?  324 GLU   A OE2  1 
ATOM   1175 N  N    . GLU   A 1 173 ? 30.88700 4.23200   11.67900 1.000 34.51278  ?  325 GLU   A N    1 
ATOM   1176 C  CA   . GLU   A 1 173 ? 31.02900 3.24600   12.74300 1.000 36.96199  ?  325 GLU   A CA   1 
ATOM   1177 C  C    . GLU   A 1 173 ? 29.72300 3.05800   13.50000 1.000 34.51859  ?  325 GLU   A C    1 
ATOM   1178 O  O    . GLU   A 1 173 ? 29.44800 1.96300   14.00300 1.000 37.16567  ?  325 GLU   A O    1 
ATOM   1179 C  CB   . GLU   A 1 173 ? 32.15300 3.66600   13.70600 1.000 37.16000  ?  325 GLU   A CB   1 
ATOM   1180 C  CG   . GLU   A 1 173 ? 33.54300 3.68700   13.06200 1.000 39.63154  ?  325 GLU   A CG   1 
ATOM   1181 C  CD   . GLU   A 1 173 ? 34.48600 4.72000   13.66600 1.000 44.79388  ?  325 GLU   A CD   1 
ATOM   1182 O  OE1  . GLU   A 1 173 ? 34.03300 5.56300   14.46700 1.000 44.80596  ?  325 GLU   A OE1  1 
ATOM   1183 O  OE2  . GLU   A 1 173 ? 35.69400 4.69700   13.32400 1.000 48.74386  ?  325 GLU   A OE2  1 
ATOM   1184 N  N    . HIS   A 1 174 ? 28.91700 4.11400   13.59800 1.000 33.31435  ?  326 HIS   A N    1 
ATOM   1185 C  CA   . HIS   A 1 174 ? 27.63500 4.01500   14.28500 1.000 38.50883  ?  326 HIS   A CA   1 
ATOM   1186 C  C    . HIS   A 1 174 ? 26.69300 3.06900   13.54900 1.000 37.44430  ?  326 HIS   A C    1 
ATOM   1187 O  O    . HIS   A 1 174 ? 26.07900 2.18300   14.16000 1.000 32.45913  ?  326 HIS   A O    1 
ATOM   1188 C  CB   . HIS   A 1 174 ? 27.01900 5.40700   14.42200 1.000 42.77665  ?  326 HIS   A CB   1 
ATOM   1189 C  CG   . HIS   A 1 174 ? 25.73400 5.43100   15.18800 1.000 47.33810  ?  326 HIS   A CG   1 
ATOM   1190 N  ND1  . HIS   A 1 174 ? 25.67000 5.19600   16.54500 1.000 46.94331  ?  326 HIS   A ND1  1 
ATOM   1191 C  CD2  . HIS   A 1 174 ? 24.46200 5.66200   14.78500 1.000 46.23446  ?  326 HIS   A CD2  1 
ATOM   1192 C  CE1  . HIS   A 1 174 ? 24.41400 5.28500   16.94600 1.000 48.02571  ?  326 HIS   A CE1  1 
ATOM   1193 N  NE2  . HIS   A 1 174 ? 23.66000 5.56400   15.89700 1.000 48.42681  ?  326 HIS   A NE2  1 
ATOM   1194 N  N    . VAL   A 1 175 ? 26.57400 3.23000   12.22800 1.000 37.33177  ?  327 VAL   A N    1 
ATOM   1195 C  CA   . VAL   A 1 175 ? 25.67100 2.35800   11.48200 1.000 31.96769  ?  327 VAL   A CA   1 
ATOM   1196 C  C    . VAL   A 1 175 ? 26.23500 0.94400   11.40100 1.000 34.41717  ?  327 VAL   A C    1 
ATOM   1197 O  O    . VAL   A 1 175 ? 25.47900 -0.03400  11.44600 1.000 34.25564  ?  327 VAL   A O    1 
ATOM   1198 C  CB   . VAL   A 1 175 ? 25.37000 2.95100   10.08900 1.000 36.62537  ?  327 VAL   A CB   1 
ATOM   1199 C  CG1  . VAL   A 1 175 ? 24.74200 4.32100   10.23700 1.000 37.66671  ?  327 VAL   A CG1  1 
ATOM   1200 C  CG2  . VAL   A 1 175 ? 26.62500 3.03900   9.22500  1.000 35.70439  ?  327 VAL   A CG2  1 
ATOM   1201 N  N    . LEU   A 1 176 ? 27.56500 0.80500   11.31900 1.000 36.82937  ?  328 LEU   A N    1 
ATOM   1202 C  CA   . LEU   A 1 176 ? 28.17200 -0.52300  11.28400 1.000 38.10098  ?  328 LEU   A CA   1 
ATOM   1203 C  C    . LEU   A 1 176 ? 27.92300 -1.28100  12.58400 1.000 37.35575  ?  328 LEU   A C    1 
ATOM   1204 O  O    . LEU   A 1 176 ? 27.72600 -2.50200  12.57200 1.000 38.04488  ?  328 LEU   A O    1 
ATOM   1205 C  CB   . LEU   A 1 176 ? 29.67400 -0.40700  11.01500 1.000 35.37631  ?  328 LEU   A CB   1 
ATOM   1206 C  CG   . LEU   A 1 176 ? 30.08500 -0.27500  9.54700  1.000 38.03467  ?  328 LEU   A CG   1 
ATOM   1207 C  CD1  . LEU   A 1 176 ? 31.54500 0.12000   9.43100  1.000 38.79712  ?  328 LEU   A CD1  1 
ATOM   1208 C  CD2  . LEU   A 1 176 ? 29.83100 -1.57500  8.80700  1.000 38.81697  ?  328 LEU   A CD2  1 
ATOM   1209 N  N    . LEU   A 1 177 ? 27.92000 -0.57700  13.71300 1.000 36.52082  ?  329 LEU   A N    1 
ATOM   1210 C  CA   . LEU   A 1 177 ? 27.70400 -1.24600  14.99200 1.000 35.39066  ?  329 LEU   A CA   1 
ATOM   1211 C  C    . LEU   A 1 177 ? 26.24800 -1.66200  15.15000 1.000 34.93114  ?  329 LEU   A C    1 
ATOM   1212 O  O    . LEU   A 1 177 ? 25.95300 -2.73800  15.69100 1.000 29.49488  ?  329 LEU   A O    1 
ATOM   1213 C  CB   . LEU   A 1 177 ? 28.13900 -0.33000  16.13200 1.000 34.24154  ?  329 LEU   A CB   1 
ATOM   1214 C  CG   . LEU   A 1 177 ? 28.13600 -0.90600  17.54800 1.000 32.67680  ?  329 LEU   A CG   1 
ATOM   1215 C  CD1  . LEU   A 1 177 ? 29.04000 -2.12300  17.64200 1.000 31.35528  ?  329 LEU   A CD1  1 
ATOM   1216 C  CD2  . LEU   A 1 177 ? 28.55600 0.17100   18.52100 1.000 32.33630  ?  329 LEU   A CD2  1 
ATOM   1217 N  N    . MET   A 1 178 ? 25.32200 -0.82900  14.67600 1.000 31.91101  ?  330 MET   A N    1 
ATOM   1218 C  CA   . MET   A 1 178 ? 23.92000 -1.23100  14.69300 1.000 36.40251  ?  330 MET   A CA   1 
ATOM   1219 C  C    . MET   A 1 178 ? 23.70800 -2.48300  13.85600 1.000 36.30720  ?  330 MET   A C    1 
ATOM   1220 O  O    . MET   A 1 178 ? 22.98900 -3.40000  14.27000 1.000 33.44199  ?  330 MET   A O    1 
ATOM   1221 C  CB   . MET   A 1 178 ? 23.03300 -0.09200  14.19500 1.000 37.06523  ?  330 MET   A CB   1 
ATOM   1222 C  CG   . MET   A 1 178 ? 22.81500 0.98300   15.23900 1.000 43.00655  ?  330 MET   A CG   1 
ATOM   1223 S  SD   . MET   A 1 178 ? 21.61200 2.22000   14.73500 1.000 42.96887  ?  330 MET   A SD   1 
ATOM   1224 C  CE   . MET   A 1 178 ? 22.46200 2.98600   13.35000 1.000 34.18203  ?  330 MET   A CE   1 
ATOM   1225 N  N    . ALA   A 1 179 ? 24.35300 -2.55400  12.68800 1.000 35.80096  ?  331 ALA   A N    1 
ATOM   1226 C  CA   . ALA   A 1 179 ? 24.14800 -3.70100  11.80700 1.000 33.52103  ?  331 ALA   A CA   1 
ATOM   1227 C  C    . ALA   A 1 179 ? 24.79200 -4.95600  12.37900 1.000 35.58047  ?  331 ALA   A C    1 
ATOM   1228 O  O    . ALA   A 1 179 ? 24.21000 -6.04500  12.30500 1.000 35.27449  ?  331 ALA   A O    1 
ATOM   1229 C  CB   . ALA   A 1 179 ? 24.69600 -3.39500  10.41300 1.000 34.04570  ?  331 ALA   A CB   1 
ATOM   1230 N  N    . ILE   A 1 180 ? 25.99900 -4.82500  12.94300 1.000 35.65224  ?  332 ILE   A N    1 
ATOM   1231 C  CA   . ILE   A 1 180 ? 26.64700 -5.95700  13.60100 1.000 34.54397  ?  332 ILE   A CA   1 
ATOM   1232 C  C    . ILE   A 1 180 ? 25.78400 -6.46200  14.74900 1.000 35.40557  ?  332 ILE   A C    1 
ATOM   1233 O  O    . ILE   A 1 180 ? 25.60100 -7.67400  14.92500 1.000 42.15306  ?  332 ILE   A O    1 
ATOM   1234 C  CB   . ILE   A 1 180 ? 28.05900 -5.55800  14.07900 1.000 31.63898  ?  332 ILE   A CB   1 
ATOM   1235 C  CG1  . ILE   A 1 180 ? 29.00400 -5.40100  12.88300 1.000 30.48882  ?  332 ILE   A CG1  1 
ATOM   1236 C  CG2  . ILE   A 1 180 ? 28.59900 -6.57900  15.06800 1.000 32.38945  ?  332 ILE   A CG2  1 
ATOM   1237 C  CD1  . ILE   A 1 180 ? 30.29000 -4.62900  13.19800 1.000 33.17691  ?  332 ILE   A CD1  1 
ATOM   1238 N  N    . CYS   A 1 181 ? 25.24700 -5.53800  15.54800 1.000 36.58068  ?  333 CYS   A N    1 
ATOM   1239 C  CA   . CYS   A 1 181 ? 24.31700 -5.89900  16.61800 1.000 38.99447  ?  333 CYS   A CA   1 
ATOM   1240 C  C    . CYS   A 1 181 ? 23.18900 -6.79000  16.10900 1.000 37.08907  ?  333 CYS   A C    1 
ATOM   1241 O  O    . CYS   A 1 181 ? 22.88000 -7.82500  16.71100 1.000 38.40070  ?  333 CYS   A O    1 
ATOM   1242 C  CB   . CYS   A 1 181 ? 23.73800 -4.62900  17.24300 1.000 33.46109  ?  333 CYS   A CB   1 
ATOM   1243 S  SG   . CYS   A 1 181 ? 22.64100 -4.92000  18.64300 1.000 36.31725  ?  333 CYS   A SG   1 
ATOM   1244 N  N    . ILE   A 1 182 ? 22.57900 -6.41400  14.98300 1.000 35.89898  ?  334 ILE   A N    1 
ATOM   1245 C  CA   . ILE   A 1 182 ? 21.39600 -7.11700  14.49300 1.000 34.65296  ?  334 ILE   A CA   1 
ATOM   1246 C  C    . ILE   A 1 182 ? 21.76000 -8.52100  14.02100 1.000 39.02298  ?  334 ILE   A C    1 
ATOM   1247 O  O    . ILE   A 1 182 ? 21.12300 -9.50800  14.40700 1.000 38.32328  ?  334 ILE   A O    1 
ATOM   1248 C  CB   . ILE   A 1 182 ? 20.72600 -6.29800  13.37400 1.000 37.28829  ?  334 ILE   A CB   1 
ATOM   1249 C  CG1  . ILE   A 1 182 ? 20.13500 -4.99900  13.93400 1.000 35.31298  ?  334 ILE   A CG1  1 
ATOM   1250 C  CG2  . ILE   A 1 182 ? 19.65800 -7.11400  12.66600 1.000 35.54810  ?  334 ILE   A CG2  1 
ATOM   1251 C  CD1  . ILE   A 1 182 ? 19.76800 -3.97800  12.86800 1.000 35.12902  ?  334 ILE   A CD1  1 
ATOM   1252 N  N    . VAL   A 1 183 ? 22.80600 -8.63800  13.20400 1.000 43.66708  ?  335 VAL   A N    1 
ATOM   1253 C  CA   . VAL   A 1 183 ? 23.18000 -9.92900  12.63600 1.000 44.82447  ?  335 VAL   A CA   1 
ATOM   1254 C  C    . VAL   A 1 183 ? 24.17800 -10.63600 13.55100 1.000 43.17429  ?  335 VAL   A C    1 
ATOM   1255 O  O    . VAL   A 1 183 ? 25.34200 -10.81800 13.18600 1.000 43.76151  ?  335 VAL   A O    1 
ATOM   1256 C  CB   . VAL   A 1 183 ? 23.75200 -9.76100  11.21200 1.000 46.56347  ?  335 VAL   A CB   1 
ATOM   1257 C  CG1  . VAL   A 1 183 ? 23.78000 -11.09400 10.48200 1.000 46.79579  ?  335 VAL   A CG1  1 
ATOM   1258 C  CG2  . VAL   A 1 183 ? 22.93600 -8.74500  10.42100 1.000 44.49319  ?  335 VAL   A CG2  1 
ATOM   1259 N  N    . SER   A 1 184 ? 23.72800 -11.05500 14.74000 1.000 45.27030  ?  336 SER   A N    1 
ATOM   1260 C  CA   . SER   A 1 184 ? 24.59000 -11.74600 15.70000 1.000 44.43814  ?  336 SER   A CA   1 
ATOM   1261 C  C    . SER   A 1 184 ? 24.28300 -13.23700 15.70500 1.000 44.34652  ?  336 SER   A C    1 
ATOM   1262 O  O    . SER   A 1 184 ? 23.13100 -13.62000 15.97300 1.000 43.68174  ?  336 SER   A O    1 
ATOM   1263 C  CB   . SER   A 1 184 ? 24.40600 -11.16800 17.10000 1.000 48.23361  ?  336 SER   A CB   1 
ATOM   1264 O  OG   . SER   A 1 184 ? 24.41400 -9.74800  17.08700 1.000 49.71756  ?  336 SER   A OG   1 
ATOM   1265 N  N    . PRO   A 1 185 ? 25.26200 -14.10900 15.44700 1.000 46.01042  ?  337 PRO   A N    1 
ATOM   1266 C  CA   . PRO   A 1 185 ? 24.97100 -15.54300 15.29500 1.000 44.56805  ?  337 PRO   A CA   1 
ATOM   1267 C  C    . PRO   A 1 185 ? 24.68400 -16.29000 16.59100 1.000 47.82478  ?  337 PRO   A C    1 
ATOM   1268 O  O    . PRO   A 1 185 ? 24.32400 -17.47100 16.52900 1.000 56.40274  ?  337 PRO   A O    1 
ATOM   1269 C  CB   . PRO   A 1 185 ? 26.25100 -16.07600 14.62800 1.000 51.29578  ?  337 PRO   A CB   1 
ATOM   1270 C  CG   . PRO   A 1 185 ? 27.33400 -15.15900 15.12000 1.000 48.87476  ?  337 PRO   A CG   1 
ATOM   1271 C  CD   . PRO   A 1 185 ? 26.68500 -13.79800 15.19800 1.000 48.57242  ?  337 PRO   A CD   1 
ATOM   1272 N  N    . ASP   A 1 186 ? 24.81400 -15.66300 17.75800 1.000 45.69956  ?  338 ASP   A N    1 
ATOM   1273 C  CA   . ASP   A 1 186 ? 24.57800 -16.35000 19.02100 1.000 49.09593  ?  338 ASP   A CA   1 
ATOM   1274 C  C    . ASP   A 1 186 ? 23.22200 -16.02600 19.63700 1.000 50.20077  ?  338 ASP   A C    1 
ATOM   1275 O  O    . ASP   A 1 186 ? 22.96200 -16.42300 20.77700 1.000 54.34114  ?  338 ASP   A O    1 
ATOM   1276 C  CB   . ASP   A 1 186 ? 25.68900 -16.02500 20.02000 1.000 43.69421  ?  338 ASP   A CB   1 
ATOM   1277 C  CG   . ASP   A 1 186 ? 25.67600 -14.58000 20.45300 1.000 44.26508  ?  338 ASP   A CG   1 
ATOM   1278 O  OD1  . ASP   A 1 186 ? 25.36800 -13.70600 19.61400 1.000 42.72975  ?  338 ASP   A OD1  1 
ATOM   1279 O  OD2  . ASP   A 1 186 ? 25.98200 -14.31700 21.63400 1.000 48.40824  ?  338 ASP   A OD2  1 
ATOM   1280 N  N    . ARG   A 1 187 ? 22.36000 -15.31600 18.92500 1.000 49.04643  ?  339 ARG   A N    1 
ATOM   1281 C  CA   . ARG   A 1 187 ? 21.03500 -15.04200 19.45500 1.000 46.81059  ?  339 ARG   A CA   1 
ATOM   1282 C  C    . ARG   A 1 187 ? 20.26100 -16.35000 19.61000 1.000 51.11371  ?  339 ARG   A C    1 
ATOM   1283 O  O    . ARG   A 1 187 ? 20.40500 -17.25900 18.78600 1.000 49.52876  ?  339 ARG   A O    1 
ATOM   1284 C  CB   . ARG   A 1 187 ? 20.27800 -14.08500 18.53900 1.000 44.68036  ?  339 ARG   A CB   1 
ATOM   1285 C  CG   . ARG   A 1 187 ? 21.00000 -12.77000 18.28200 1.000 42.47383  ?  339 ARG   A CG   1 
ATOM   1286 C  CD   . ARG   A 1 187 ? 20.98300 -11.86200 19.50400 1.000 40.07489  ?  339 ARG   A CD   1 
ATOM   1287 N  NE   . ARG   A 1 187 ? 21.25900 -10.47500 19.13900 1.000 37.83301  ?  339 ARG   A NE   1 
ATOM   1288 C  CZ   . ARG   A 1 187 ? 21.37500 -9.47900  20.01000 1.000 40.78575  ?  339 ARG   A CZ   1 
ATOM   1289 N  NH1  . ARG   A 1 187 ? 21.23800 -9.70700  21.31100 1.000 41.27484  ?  339 ARG   A NH1  1 
ATOM   1290 N  NH2  . ARG   A 1 187 ? 21.63300 -8.25200  19.58000 1.000 43.28199  ?  339 ARG   A NH2  1 
ATOM   1291 N  N    . PRO   A 1 188 ? 19.44900 -16.48200 20.65700 1.000 58.35957  ?  340 PRO   A N    1 
ATOM   1292 C  CA   . PRO   A 1 188 ? 18.72900 -17.74300 20.87900 1.000 61.02275  ?  340 PRO   A CA   1 
ATOM   1293 C  C    . PRO   A 1 188 ? 17.69200 -17.98600 19.78900 1.000 57.38651  ?  340 PRO   A C    1 
ATOM   1294 O  O    . PRO   A 1 188 ? 16.91500 -17.09500 19.44000 1.000 54.12241  ?  340 PRO   A O    1 
ATOM   1295 C  CB   . PRO   A 1 188 ? 18.07300 -17.54000 22.25000 1.000 63.78887  ?  340 PRO   A CB   1 
ATOM   1296 C  CG   . PRO   A 1 188 ? 17.95400 -16.05600 22.39300 1.000 62.44686  ?  340 PRO   A CG   1 
ATOM   1297 C  CD   . PRO   A 1 188 ? 19.16400 -15.48800 21.70600 1.000 61.35104  ?  340 PRO   A CD   1 
ATOM   1298 N  N    . GLY   A 1 189 ? 17.69200 -19.20300 19.25100 1.000 58.98424  ?  341 GLY   A N    1 
ATOM   1299 C  CA   . GLY   A 1 189 ? 16.74700 -19.59700 18.23000 1.000 61.16964  ?  341 GLY   A CA   1 
ATOM   1300 C  C    . GLY   A 1 189 ? 17.23300 -19.46600 16.80400 1.000 60.56105  ?  341 GLY   A C    1 
ATOM   1301 O  O    . GLY   A 1 189 ? 16.48800 -19.82500 15.88300 1.000 60.95768  ?  341 GLY   A O    1 
ATOM   1302 N  N    . VAL   A 1 190 ? 18.44800 -18.95900 16.58800 1.000 57.10982  ?  342 VAL   A N    1 
ATOM   1303 C  CA   . VAL   A 1 190 ? 18.97000 -18.81200 15.23400 1.000 55.18038  ?  342 VAL   A CA   1 
ATOM   1304 C  C    . VAL   A 1 190 ? 19.16600 -20.19000 14.62100 1.000 56.95269  ?  342 VAL   A C    1 
ATOM   1305 O  O    . VAL   A 1 190 ? 19.74300 -21.09100 15.24600 1.000 59.86209  ?  342 VAL   A O    1 
ATOM   1306 C  CB   . VAL   A 1 190 ? 20.27900 -18.00200 15.24200 1.000 52.58769  ?  342 VAL   A CB   1 
ATOM   1307 C  CG1  . VAL   A 1 190 ? 20.91900 -17.99600 13.86300 1.000 52.89834  ?  342 VAL   A CG1  1 
ATOM   1308 C  CG2  . VAL   A 1 190 ? 20.02100 -16.57400 15.69900 1.000 48.53953  ?  342 VAL   A CG2  1 
ATOM   1309 N  N    A GLN   A 1 191 ? 18.68900 -20.36300 13.38800 0.520 56.68669  ?  343 GLN   A N    1 
ATOM   1310 N  N    B GLN   A 1 191 ? 18.67000 -20.36800 13.39700 0.480 56.66609  ?  343 GLN   A N    1 
ATOM   1311 C  CA   A GLN   A 1 191 ? 18.79500 -21.64600 12.69900 0.520 58.15750  ?  343 GLN   A CA   1 
ATOM   1312 C  CA   B GLN   A 1 191 ? 18.79500 -21.64800 12.68900 0.480 58.16082  ?  343 GLN   A CA   1 
ATOM   1313 C  C    A GLN   A 1 191 ? 20.08100 -21.74400 11.88200 0.520 59.13084  ?  343 GLN   A C    1 
ATOM   1314 C  C    B GLN   A 1 191 ? 20.11500 -21.70000 11.92700 0.480 59.06733  ?  343 GLN   A C    1 
ATOM   1315 O  O    A GLN   A 1 191 ? 20.89900 -22.64100 12.10500 0.520 62.18487  ?  343 GLN   A O    1 
ATOM   1316 O  O    B GLN   A 1 191 ? 20.99000 -22.51500 12.23400 0.480 62.08751  ?  343 GLN   A O    1 
ATOM   1317 C  CB   A GLN   A 1 191 ? 17.57000 -21.86500 11.80200 0.520 57.20094  ?  343 GLN   A CB   1 
ATOM   1318 C  CB   B GLN   A 1 191 ? 17.60800 -21.85300 11.74400 0.480 57.20877  ?  343 GLN   A CB   1 
ATOM   1319 C  CG   A GLN   A 1 191 ? 17.54400 -23.21700 11.11600 0.520 58.82230  ?  343 GLN   A CG   1 
ATOM   1320 C  CG   B GLN   A 1 191 ? 16.39000 -22.48600 12.38800 0.480 57.11994  ?  343 GLN   A CG   1 
ATOM   1321 C  CD   A GLN   A 1 191 ? 17.94700 -23.14100 9.65600  0.520 60.22534  ?  343 GLN   A CD   1 
ATOM   1322 C  CD   B GLN   A 1 191 ? 15.09500 -22.00300 11.76600 0.480 56.67912  ?  343 GLN   A CD   1 
ATOM   1323 O  OE1  A GLN   A 1 191 ? 19.10200 -23.38700 9.30300  0.520 48.48350  ?  343 GLN   A OE1  1 
ATOM   1324 O  OE1  B GLN   A 1 191 ? 14.05300 -21.96100 12.42300 0.480 56.48042  ?  343 GLN   A OE1  1 
ATOM   1325 N  NE2  A GLN   A 1 191 ? 16.99000 -22.80500 8.79500  0.520 58.09985  ?  343 GLN   A NE2  1 
ATOM   1326 N  NE2  B GLN   A 1 191 ? 15.15300 -21.63100 10.48900 0.480 55.10446  ?  343 GLN   A NE2  1 
ATOM   1327 N  N    . ASP   A 1 192 ? 20.26600 -20.83000 10.93000 1.000 57.59974  ?  344 ASP   A N    1 
ATOM   1328 C  CA   . ASP   A 1 192 ? 21.44900 -20.82700 10.07000 1.000 60.56937  ?  344 ASP   A CA   1 
ATOM   1329 C  C    . ASP   A 1 192 ? 22.52100 -19.91400 10.66800 1.000 63.58188  ?  344 ASP   A C    1 
ATOM   1330 O  O    . ASP   A 1 192 ? 22.85200 -18.84800 10.14500 1.000 63.09948  ?  344 ASP   A O    1 
ATOM   1331 C  CB   . ASP   A 1 192 ? 21.07200 -20.40700 8.65600  1.000 58.90483  ?  344 ASP   A CB   1 
ATOM   1332 C  CG   . ASP   A 1 192 ? 22.05400 -20.90700 7.62000  1.000 67.59052  ?  344 ASP   A CG   1 
ATOM   1333 O  OD1  . ASP   A 1 192 ? 23.08900 -21.49300 8.01000  1.000 73.55215  ?  344 ASP   A OD1  1 
ATOM   1334 O  OD2  . ASP   A 1 192 ? 21.79300 -20.71500 6.41500  1.000 69.26450  ?  344 ASP   A OD2  1 
ATOM   1335 N  N    . ALA   A 1 193 ? 23.07500 -20.37100 11.79600 1.000 64.61141  ?  345 ALA   A N    1 
ATOM   1336 C  CA   . ALA   A 1 193 ? 24.12300 -19.60700 12.46600 1.000 63.29275  ?  345 ALA   A CA   1 
ATOM   1337 C  C    . ALA   A 1 193 ? 25.37000 -19.47900 11.59900 1.000 61.49064  ?  345 ALA   A C    1 
ATOM   1338 O  O    . ALA   A 1 193 ? 26.13700 -18.52200 11.75600 1.000 58.31247  ?  345 ALA   A O    1 
ATOM   1339 C  CB   . ALA   A 1 193 ? 24.46800 -20.25400 13.80700 1.000 64.37446  ?  345 ALA   A CB   1 
ATOM   1340 N  N    . LYS   A 1 194 ? 25.59300 -20.43100 10.68800 1.000 64.35597  ?  346 LYS   A N    1 
ATOM   1341 C  CA   . LYS   A 1 194 ? 26.69600 -20.30900 9.73700  1.000 68.32818  ?  346 LYS   A CA   1 
ATOM   1342 C  C    . LYS   A 1 194 ? 26.54500 -19.05600 8.88600  1.000 63.76965  ?  346 LYS   A C    1 
ATOM   1343 O  O    . LYS   A 1 194 ? 27.49200 -18.27500 8.73100  1.000 58.30623  ?  346 LYS   A O    1 
ATOM   1344 C  CB   . LYS   A 1 194 ? 26.76200 -21.54700 8.84000  1.000 75.88327  ?  346 LYS   A CB   1 
ATOM   1345 C  CG   . LYS   A 1 194 ? 28.03700 -22.36600 8.96100  1.000 83.26423  ?  346 LYS   A CG   1 
ATOM   1346 C  CD   . LYS   A 1 194 ? 28.29200 -22.78400 10.39500 1.000 87.72316  ?  346 LYS   A CD   1 
ATOM   1347 C  CE   . LYS   A 1 194 ? 27.47900 -24.02000 10.75000 1.000 93.17787  ?  346 LYS   A CE   1 
ATOM   1348 N  NZ   . LYS   A 1 194 ? 27.83600 -24.56300 12.09100 1.000 95.83844  ?  346 LYS   A NZ   1 
ATOM   1349 N  N    . LEU   A 1 195 ? 25.35000 -18.84900 8.32400  1.000 58.86587  ?  347 LEU   A N    1 
ATOM   1350 C  CA   . LEU   A 1 195 ? 25.12500 -17.70900 7.44500  1.000 54.00783  ?  347 LEU   A CA   1 
ATOM   1351 C  C    . LEU   A 1 195 ? 25.10700 -16.40200 8.22600  1.000 49.30254  ?  347 LEU   A C    1 
ATOM   1352 O  O    . LEU   A 1 195 ? 25.61500 -15.38200 7.74900  1.000 52.06300  ?  347 LEU   A O    1 
ATOM   1353 C  CB   . LEU   A 1 195 ? 23.81900 -17.90000 6.67800  1.000 54.86514  ?  347 LEU   A CB   1 
ATOM   1354 C  CG   . LEU   A 1 195 ? 23.53700 -16.93000 5.53300  1.000 55.31053  ?  347 LEU   A CG   1 
ATOM   1355 C  CD1  . LEU   A 1 195 ? 24.58500 -17.07400 4.44800  1.000 59.42928  ?  347 LEU   A CD1  1 
ATOM   1356 C  CD2  . LEU   A 1 195 ? 22.14100 -17.17200 4.97500  1.000 50.97940  ?  347 LEU   A CD2  1 
ATOM   1357 N  N    . VAL   A 1 196 ? 24.52700 -16.41000 9.42600  1.000 50.80914  ?  348 VAL   A N    1 
ATOM   1358 C  CA   . VAL   A 1 196 ? 24.49000 -15.19500 10.23500 1.000 49.63516  ?  348 VAL   A CA   1 
ATOM   1359 C  C    . VAL   A 1 196 ? 25.90300 -14.75300 10.59200 1.000 48.59309  ?  348 VAL   A C    1 
ATOM   1360 O  O    . VAL   A 1 196 ? 26.21700 -13.55600 10.57000 1.000 48.51401  ?  348 VAL   A O    1 
ATOM   1361 C  CB   . VAL   A 1 196 ? 23.62200 -15.41500 11.48800 1.000 46.83517  ?  348 VAL   A CB   1 
ATOM   1362 C  CG1  . VAL   A 1 196 ? 23.52900 -14.14500 12.30500 1.000 42.02757  ?  348 VAL   A CG1  1 
ATOM   1363 C  CG2  . VAL   A 1 196 ? 22.23500 -15.87700 11.08800 1.000 47.20433  ?  348 VAL   A CG2  1 
ATOM   1364 N  N    . GLU   A 1 197 ? 26.78500 -15.71100 10.90400 1.000 47.99639  ?  349 GLU   A N    1 
ATOM   1365 C  CA   . GLU   A 1 197 ? 28.16800 -15.36000 11.22100 1.000 53.75750  ?  349 GLU   A CA   1 
ATOM   1366 C  C    . GLU   A 1 197 ? 28.90600 -14.84700 9.99000  1.000 51.31165  ?  349 GLU   A C    1 
ATOM   1367 O  O    . GLU   A 1 197 ? 29.67600 -13.88500 10.08200 1.000 50.88118  ?  349 GLU   A O    1 
ATOM   1368 C  CB   . GLU   A 1 197 ? 28.90200 -16.55800 11.82900 1.000 60.29733  ?  349 GLU   A CB   1 
ATOM   1369 C  CG   . GLU   A 1 197 ? 29.98400 -16.16500 12.84300 1.000 64.98240  ?  349 GLU   A CG   1 
ATOM   1370 C  CD   . GLU   A 1 197 ? 30.95500 -17.29100 13.15800 1.000 69.83807  ?  349 GLU   A CD   1 
ATOM   1371 O  OE1  . GLU   A 1 197 ? 30.49500 -18.41300 13.45500 1.000 72.82690  ?  349 GLU   A OE1  1 
ATOM   1372 O  OE2  . GLU   A 1 197 ? 32.18100 -17.04700 13.12900 1.000 73.73017  ?  349 GLU   A OE2  1 
ATOM   1373 N  N    . ALA   A 1 198 ? 28.68200 -15.46800 8.82900  1.000 51.97282  ?  350 ALA   A N    1 
ATOM   1374 C  CA   . ALA   A 1 198 ? 29.35100 -15.01100 7.61300  1.000 52.24577  ?  350 ALA   A CA   1 
ATOM   1375 C  C    . ALA   A 1 198 ? 28.92000 -13.59600 7.24300  1.000 52.74263  ?  350 ALA   A C    1 
ATOM   1376 O  O    . ALA   A 1 198 ? 29.73200 -12.79400 6.77100  1.000 55.88562  ?  350 ALA   A O    1 
ATOM   1377 C  CB   . ALA   A 1 198 ? 29.07300 -15.97700 6.46200  1.000 54.17803  ?  350 ALA   A CB   1 
ATOM   1378 N  N    . ILE   A 1 199 ? 27.64600 -13.26800 7.45400  1.000 47.83741  ?  351 ILE   A N    1 
ATOM   1379 C  CA   . ILE   A 1 199 ? 27.18400 -11.90600 7.20700  1.000 47.50626  ?  351 ILE   A CA   1 
ATOM   1380 C  C    . ILE   A 1 199 ? 27.82100 -10.93800 8.19800  1.000 47.20988  ?  351 ILE   A C    1 
ATOM   1381 O  O    . ILE   A 1 199 ? 28.30500 -9.86400  7.82100  1.000 45.42635  ?  351 ILE   A O    1 
ATOM   1382 C  CB   . ILE   A 1 199 ? 25.65300 -11.85100 7.27700  1.000 43.92529  ?  351 ILE   A CB   1 
ATOM   1383 C  CG1  . ILE   A 1 199 ? 25.06200 -12.77800 6.22300  1.000 45.71273  ?  351 ILE   A CG1  1 
ATOM   1384 C  CG2  . ILE   A 1 199 ? 25.17300 -10.41600 7.09900  1.000 42.82865  ?  351 ILE   A CG2  1 
ATOM   1385 C  CD1  . ILE   A 1 199 ? 23.58300 -12.65700 6.09500  1.000 46.30228  ?  351 ILE   A CD1  1 
ATOM   1386 N  N    . GLN   A 1 200 ? 27.82000 -11.29900 9.48300  1.000 49.32515  ?  352 GLN   A N    1 
ATOM   1387 C  CA   . GLN   A 1 200 ? 28.39300 -10.41500 10.49200 1.000 46.85165  ?  352 GLN   A CA   1 
ATOM   1388 C  C    . GLN   A 1 200 ? 29.89600 -10.25700 10.32300 1.000 46.10683  ?  352 GLN   A C    1 
ATOM   1389 O  O    . GLN   A 1 200 ? 30.44700 -9.20800  10.67200 1.000 49.24611  ?  352 GLN   A O    1 
ATOM   1390 C  CB   . GLN   A 1 200 ? 28.08200 -10.93400 11.88900 1.000 45.84421  ?  352 GLN   A CB   1 
ATOM   1391 C  CG   . GLN   A 1 200 ? 28.34300 -9.91500  12.98700 1.000 46.83140  ?  352 GLN   A CG   1 
ATOM   1392 C  CD   . GLN   A 1 200 ? 28.40900 -10.55000 14.35700 1.000 46.11768  ?  352 GLN   A CD   1 
ATOM   1393 O  OE1  . GLN   A 1 200 ? 29.13800 -11.51900 14.57000 1.000 50.60448  ?  352 GLN   A OE1  1 
ATOM   1394 N  NE2  . GLN   A 1 200 ? 27.64600 -10.00900 15.29500 1.000 43.41582  ?  352 GLN   A NE2  1 
ATOM   1395 N  N    . ASP   A 1 201 ? 30.57600 -11.27900 9.79900  1.000 48.08924  ?  353 ASP   A N    1 
ATOM   1396 C  CA   . ASP   A 1 201 ? 32.02100 -11.17700 9.61600  1.000 55.37294  ?  353 ASP   A CA   1 
ATOM   1397 C  C    . ASP   A 1 201 ? 32.37100 -10.12100 8.57600  1.000 55.28979  ?  353 ASP   A C    1 
ATOM   1398 O  O    . ASP   A 1 201 ? 33.30700 -9.33600  8.77200  1.000 53.10077  ?  353 ASP   A O    1 
ATOM   1399 C  CB   . ASP   A 1 201 ? 32.60600 -12.53400 9.22300  1.000 60.22730  ?  353 ASP   A CB   1 
ATOM   1400 C  CG   . ASP   A 1 201 ? 32.75300 -13.46900 10.40700 1.000 60.49834  ?  353 ASP   A CG   1 
ATOM   1401 O  OD1  . ASP   A 1 201 ? 32.71200 -12.98400 11.55800 1.000 59.30631  ?  353 ASP   A OD1  1 
ATOM   1402 O  OD2  . ASP   A 1 201 ? 32.91300 -14.68900 10.18500 1.000 61.63473  ?  353 ASP   A OD2  1 
ATOM   1403 N  N    . ARG   A 1 202 ? 31.63200 -10.08900 7.46200  1.000 51.27886  ?  354 ARG   A N    1 
ATOM   1404 C  CA   . ARG   A 1 202 ? 31.86600 -9.05600  6.45900  1.000 50.36552  ?  354 ARG   A CA   1 
ATOM   1405 C  C    . ARG   A 1 202 ? 31.63100 -7.66800  7.03900  1.000 47.21400  ?  354 ARG   A C    1 
ATOM   1406 O  O    . ARG   A 1 202 ? 32.35100 -6.72000  6.71200  1.000 44.86035  ?  354 ARG   A O    1 
ATOM   1407 C  CB   . ARG   A 1 202 ? 30.97300 -9.29100  5.23800  1.000 51.60163  ?  354 ARG   A CB   1 
ATOM   1408 C  CG   . ARG   A 1 202 ? 31.19000 -10.64500 4.57600  1.000 61.09393  ?  354 ARG   A CG   1 
ATOM   1409 C  CD   . ARG   A 1 202 ? 30.83400 -10.60600 3.10000  1.000 68.18638  ?  354 ARG   A CD   1 
ATOM   1410 N  NE   . ARG   A 1 202 ? 29.49700 -10.06400 2.88600  1.000 73.30584  ?  354 ARG   A NE   1 
ATOM   1411 C  CZ   . ARG   A 1 202 ? 28.38700 -10.79700 2.86200  1.000 78.29239  ?  354 ARG   A CZ   1 
ATOM   1412 N  NH1  . ARG   A 1 202 ? 28.45500 -12.11300 3.03000  1.000 80.96189  ?  354 ARG   A NH1  1 
ATOM   1413 N  NH2  . ARG   A 1 202 ? 27.20900 -10.21600 2.66700  1.000 76.28008  ?  354 ARG   A NH2  1 
ATOM   1414 N  N    . LEU   A 1 203 ? 30.62700 -7.52800  7.90700  1.000 43.27014  ?  355 LEU   A N    1 
ATOM   1415 C  CA   . LEU   A 1 203 ? 30.42900 -6.25300  8.58600  1.000 41.25251  ?  355 LEU   A CA   1 
ATOM   1416 C  C    . LEU   A 1 203 ? 31.54200 -5.98700  9.59100  1.000 42.35884  ?  355 LEU   A C    1 
ATOM   1417 O  O    . LEU   A 1 203 ? 32.00600 -4.84800  9.72200  1.000 42.12526  ?  355 LEU   A O    1 
ATOM   1418 C  CB   . LEU   A 1 203 ? 29.07400 -6.23600  9.28300  1.000 40.22471  ?  355 LEU   A CB   1 
ATOM   1419 C  CG   . LEU   A 1 203 ? 27.87700 -6.63200  8.42800  1.000 42.13448  ?  355 LEU   A CG   1 
ATOM   1420 C  CD1  . LEU   A 1 203 ? 26.72100 -7.00200  9.34000  1.000 41.43956  ?  355 LEU   A CD1  1 
ATOM   1421 C  CD2  . LEU   A 1 203 ? 27.50100 -5.49300  7.49200  1.000 41.56808  ?  355 LEU   A CD2  1 
ATOM   1422 N  N    . SER   A 1 204 ? 31.97300 -7.02400  10.31700 1.000 42.47060  ?  356 SER   A N    1 
ATOM   1423 C  CA   . SER   A 1 204 ? 33.02300 -6.84900  11.31600 1.000 45.88983  ?  356 SER   A CA   1 
ATOM   1424 C  C    . SER   A 1 204 ? 34.34300 -6.46700  10.65900 1.000 47.76449  ?  356 SER   A C    1 
ATOM   1425 O  O    . SER   A 1 204 ? 35.01500 -5.52700  11.10000 1.000 45.60121  ?  356 SER   A O    1 
ATOM   1426 C  CB   . SER   A 1 204 ? 33.18100 -8.12200  12.15100 1.000 48.30937  ?  356 SER   A CB   1 
ATOM   1427 O  OG   . SER   A 1 204 ? 32.09500 -8.27600  13.05000 1.000 50.46361  ?  356 SER   A OG   1 
ATOM   1428 N  N    A ASN   A 1 205 ? 34.73100 -7.18800  9.60600  0.730 49.34358  ?  357 ASN   A N    1 
ATOM   1429 N  N    B ASN   A 1 205 ? 34.73200 -7.17800  9.59600  0.270 49.58080  ?  357 ASN   A N    1 
ATOM   1430 C  CA   A ASN   A 1 205 ? 35.95500 -6.84600  8.89100  0.730 51.96705  ?  357 ASN   A CA   1 
ATOM   1431 C  CA   B ASN   A 1 205 ? 35.97100 -6.82700  8.90900  0.270 51.54705  ?  357 ASN   A CA   1 
ATOM   1432 C  C    A ASN   A 1 205 ? 35.85400 -5.46900  8.24700  0.730 50.70322  ?  357 ASN   A C    1 
ATOM   1433 C  C    B ASN   A 1 205 ? 35.86300 -5.46800  8.22900  0.270 50.73634  ?  357 ASN   A C    1 
ATOM   1434 O  O    A ASN   A 1 205 ? 36.85500 -4.75200  8.15700  0.730 51.94719  ?  357 ASN   A O    1 
ATOM   1435 O  O    B ASN   A 1 205 ? 36.87000 -4.76600  8.08900  0.270 51.99077  ?  357 ASN   A O    1 
ATOM   1436 C  CB   A ASN   A 1 205 ? 36.26300 -7.91500  7.84200  0.730 53.05184  ?  357 ASN   A CB   1 
ATOM   1437 C  CB   B ASN   A 1 205 ? 36.36900 -7.92600  7.91100  0.270 53.30187  ?  357 ASN   A CB   1 
ATOM   1438 C  CG   A ASN   A 1 205 ? 36.68300 -9.23400  8.46300  0.730 54.07000  ?  357 ASN   A CG   1 
ATOM   1439 C  CG   B ASN   A 1 205 ? 35.41500 -8.05300  6.72100  0.270 53.94023  ?  357 ASN   A CG   1 
ATOM   1440 O  OD1  A ASN   A 1 205 ? 37.27800 -9.26700  9.54100  0.730 55.79167  ?  357 ASN   A OD1  1 
ATOM   1441 O  OD1  B ASN   A 1 205 ? 34.90100 -7.06800  6.19500  0.270 53.98640  ?  357 ASN   A OD1  1 
ATOM   1442 N  ND2  A ASN   A 1 205 ? 36.37700 -10.33100 7.78200  0.730 56.54394  ?  357 ASN   A ND2  1 
ATOM   1443 N  ND2  B ASN   A 1 205 ? 35.19900 -9.28700  6.27900  0.270 54.94657  ?  357 ASN   A ND2  1 
ATOM   1444 N  N    . THR   A 1 206 ? 34.65700 -5.08000  7.80600  1.000 47.84986  ?  358 THR   A N    1 
ATOM   1445 C  CA   . THR   A 1 206 ? 34.46600 -3.73500  7.27200  1.000 50.29296  ?  358 THR   A CA   1 
ATOM   1446 C  C    . THR   A 1 206 ? 34.71300 -2.68400  8.34700  1.000 47.57614  ?  358 THR   A C    1 
ATOM   1447 O  O    . THR   A 1 206 ? 35.37300 -1.67000  8.09400  1.000 48.42426  ?  358 THR   A O    1 
ATOM   1448 C  CB   . THR   A 1 206 ? 33.05100 -3.58100  6.70200  1.000 48.75797  ?  358 THR   A CB   1 
ATOM   1449 O  OG1  . THR   A 1 206 ? 32.81900 -4.56800  5.68900  1.000 51.73482  ?  358 THR   A OG1  1 
ATOM   1450 C  CG2  . THR   A 1 206 ? 32.87000 -2.20100  6.09300  1.000 50.00980  ?  358 THR   A CG2  1 
ATOM   1451 N  N    . LEU   A 1 207 ? 34.18700 -2.91000  9.55500  1.000 43.60017  ?  359 LEU   A N    1 
ATOM   1452 C  CA   . LEU   A 1 207 ? 34.35600 -1.93700  10.62800 1.000 41.53826  ?  359 LEU   A CA   1 
ATOM   1453 C  C    . LEU   A 1 207 ? 35.81000 -1.85300  11.07300 1.000 41.68222  ?  359 LEU   A C    1 
ATOM   1454 O  O    . LEU   A 1 207 ? 36.33700 -0.75300  11.27700 1.000 36.22381  ?  359 LEU   A O    1 
ATOM   1455 C  CB   . LEU   A 1 207 ? 33.45600 -2.29500  11.81000 1.000 42.77828  ?  359 LEU   A CB   1 
ATOM   1456 C  CG   . LEU   A 1 207 ? 33.67900 -1.49000  13.09300 1.000 41.42342  ?  359 LEU   A CG   1 
ATOM   1457 C  CD1  . LEU   A 1 207 ? 33.44000 -0.00600  12.85700 1.000 42.02414  ?  359 LEU   A CD1  1 
ATOM   1458 C  CD2  . LEU   A 1 207 ? 32.77500 -2.01900  14.19500 1.000 32.37299  ?  359 LEU   A CD2  1 
ATOM   1459 N  N    . GLN   A 1 208 ? 36.46800 -3.00600  11.23800 1.000 43.76789  ?  360 GLN   A N    1 
ATOM   1460 C  CA   . GLN   A 1 208 ? 37.87200 -3.01900  11.64100 1.000 49.85130  ?  360 GLN   A CA   1 
ATOM   1461 C  C    . GLN   A 1 208 ? 38.73900 -2.30300  10.61700 1.000 50.52246  ?  360 GLN   A C    1 
ATOM   1462 O  O    . GLN   A 1 208 ? 39.58800 -1.47700  10.97200 1.000 51.55454  ?  360 GLN   A O    1 
ATOM   1463 C  CB   . GLN   A 1 208 ? 38.35600 -4.45800  11.82300 1.000 54.58090  ?  360 GLN   A CB   1 
ATOM   1464 C  CG   . GLN   A 1 208 ? 37.66800 -5.21900  12.93800 1.000 57.96870  ?  360 GLN   A CG   1 
ATOM   1465 C  CD   . GLN   A 1 208 ? 38.32800 -6.55300  13.20700 1.000 64.86258  ?  360 GLN   A CD   1 
ATOM   1466 O  OE1  . GLN   A 1 208 ? 39.47100 -6.61200  13.66700 1.000 67.68002  ?  360 GLN   A OE1  1 
ATOM   1467 N  NE2  . GLN   A 1 208 ? 37.61600 -7.63500  12.91300 1.000 66.08179  ?  360 GLN   A NE2  1 
ATOM   1468 N  N    . THR   A 1 209 ? 38.54300 -2.61800  9.33300  1.000 50.44887  ?  361 THR   A N    1 
ATOM   1469 C  CA   . THR   A 1 209 ? 39.33200 -1.98000  8.28600  1.000 52.76337  ?  361 THR   A CA   1 
ATOM   1470 C  C    . THR   A 1 209 ? 39.04000 -0.48600  8.22200  1.000 53.52827  ?  361 THR   A C    1 
ATOM   1471 O  O    . THR   A 1 209 ? 39.95000 0.32000   7.99800  1.000 55.78445  ?  361 THR   A O    1 
ATOM   1472 C  CB   . THR   A 1 209 ? 39.05900 -2.64600  6.93300  1.000 55.97409  ?  361 THR   A CB   1 
ATOM   1473 O  OG1  . THR   A 1 209 ? 39.36000 -4.04700  7.01200  1.000 57.77008  ?  361 THR   A OG1  1 
ATOM   1474 C  CG2  . THR   A 1 209 ? 39.91500 -2.02200  5.84000  1.000 55.31484  ?  361 THR   A CG2  1 
ATOM   1475 N  N    . TYR   A 1 210 ? 37.77700 -0.09400  8.43600  1.000 51.87372  ?  362 TYR   A N    1 
ATOM   1476 C  CA   . TYR   A 1 210 ? 37.44300 1.32900   8.44700  1.000 49.13434  ?  362 TYR   A CA   1 
ATOM   1477 C  C    . TYR   A 1 210 ? 38.18200 2.05800   9.56100  1.000 51.31516  ?  362 TYR   A C    1 
ATOM   1478 O  O    . TYR   A 1 210 ? 38.69500 3.16400   9.35500  1.000 54.93762  ?  362 TYR   A O    1 
ATOM   1479 C  CB   . TYR   A 1 210 ? 35.93200 1.54800   8.60100  1.000 47.07653  ?  362 TYR   A CB   1 
ATOM   1480 C  CG   . TYR   A 1 210 ? 35.57900 3.02600   8.66700  1.000 47.33169  ?  362 TYR   A CG   1 
ATOM   1481 C  CD1  . TYR   A 1 210 ? 35.31100 3.74400   7.50800  1.000 47.08247  ?  362 TYR   A CD1  1 
ATOM   1482 C  CD2  . TYR   A 1 210 ? 35.55400 3.71400   9.88100  1.000 42.64901  ?  362 TYR   A CD2  1 
ATOM   1483 C  CE1  . TYR   A 1 210 ? 35.01000 5.09400   7.55000  1.000 45.09505  ?  362 TYR   A CE1  1 
ATOM   1484 C  CE2  . TYR   A 1 210 ? 35.26200 5.07400   9.92800  1.000 42.70523  ?  362 TYR   A CE2  1 
ATOM   1485 C  CZ   . TYR   A 1 210 ? 34.98900 5.75500   8.75600  1.000 43.98722  ?  362 TYR   A CZ   1 
ATOM   1486 O  OH   . TYR   A 1 210 ? 34.69500 7.09900   8.77700  1.000 43.75610  ?  362 TYR   A OH   1 
ATOM   1487 N  N    . ILE   A 1 211 ? 38.22600 1.46800   10.75600 1.000 49.22027  ?  363 ILE   A N    1 
ATOM   1488 C  CA   . ILE   A 1 211 ? 38.88400 2.13100   11.87700 1.000 47.42603  ?  363 ILE   A CA   1 
ATOM   1489 C  C    . ILE   A 1 211 ? 40.36100 2.34300   11.56800 1.000 50.83471  ?  363 ILE   A C    1 
ATOM   1490 O  O    . ILE   A 1 211 ? 40.90900 3.43000   11.79400 1.000 48.70969  ?  363 ILE   A O    1 
ATOM   1491 C  CB   . ILE   A 1 211 ? 38.66600 1.32700   13.17200 1.000 44.20204  ?  363 ILE   A CB   1 
ATOM   1492 C  CG1  . ILE   A 1 211 ? 37.18700 1.38000   13.57100 1.000 42.62494  ?  363 ILE   A CG1  1 
ATOM   1493 C  CG2  . ILE   A 1 211 ? 39.52900 1.87300   14.30000 1.000 44.08043  ?  363 ILE   A CG2  1 
ATOM   1494 C  CD1  . ILE   A 1 211 ? 36.78300 0.32200   14.57100 1.000 47.83951  ?  363 ILE   A CD1  1 
ATOM   1495 N  N    . ARG   A 1 212 ? 41.00900 1.33200   10.98600 1.000 57.72909  ?  364 ARG   A N    1 
ATOM   1496 C  CA   . ARG   A 1 212 ? 42.42700 1.43900   10.65300 1.000 64.17055  ?  364 ARG   A CA   1 
ATOM   1497 C  C    . ARG   A 1 212 ? 42.68400 2.56400   9.65400  1.000 64.90740  ?  364 ARG   A C    1 
ATOM   1498 O  O    . ARG   A 1 212 ? 43.57300 3.40000   9.86000  1.000 65.09904  ?  364 ARG   A O    1 
ATOM   1499 C  CB   . ARG   A 1 212 ? 42.93900 0.10600   10.10300 1.000 70.01518  ?  364 ARG   A CB   1 
ATOM   1500 C  CG   . ARG   A 1 212 ? 43.59200 -0.79600  11.14100 1.000 77.59430  ?  364 ARG   A CG   1 
ATOM   1501 C  CD   . ARG   A 1 212 ? 42.59800 -1.21500  12.21100 1.000 83.11882  ?  364 ARG   A CD   1 
ATOM   1502 N  NE   . ARG   A 1 212 ? 43.23900 -1.57300  13.47500 1.000 90.16062  ?  364 ARG   A NE   1 
ATOM   1503 C  CZ   . ARG   A 1 212 ? 43.71100 -2.78200  13.76600 1.000 94.27229  ?  364 ARG   A CZ   1 
ATOM   1504 N  NH1  . ARG   A 1 212 ? 43.61900 -3.76300  12.87800 1.000 96.13108  ?  364 ARG   A NH1  1 
ATOM   1505 N  NH2  . ARG   A 1 212 ? 44.27300 -3.01200  14.94600 1.000 94.38951  ?  364 ARG   A NH2  1 
ATOM   1506 N  N    . CYS   A 1 213 ? 41.91100 2.60900   8.56600  1.000 61.40409  ?  365 CYS   A N    1 
ATOM   1507 C  CA   . CYS   A 1 213 ? 42.22000 3.51100   7.46100  1.000 67.26337  ?  365 CYS   A CA   1 
ATOM   1508 C  C    . CYS   A 1 213 ? 41.57000 4.88400   7.56200  1.000 63.28424  ?  365 CYS   A C    1 
ATOM   1509 O  O    . CYS   A 1 213 ? 42.07600 5.83200   6.95200  1.000 65.28549  ?  365 CYS   A O    1 
ATOM   1510 C  CB   . CYS   A 1 213 ? 41.80900 2.89200   6.11900  1.000 73.33502  ?  365 CYS   A CB   1 
ATOM   1511 S  SG   . CYS   A 1 213 ? 42.33500 1.18700   5.83900  1.000 78.46603  ?  365 CYS   A SG   1 
ATOM   1512 N  N    A ARG   A 1 214 ? 40.47900 5.02300   8.31400  0.450 59.24539  ?  366 ARG   A N    1 
ATOM   1513 N  N    D ARG   A 1 214 ? 40.47500 5.02500   8.30800  0.550 59.22948  ?  366 ARG   A N    1 
ATOM   1514 C  CA   A ARG   A 1 214 ? 39.72400 6.26600   8.32200  0.450 58.09773  ?  366 ARG   A CA   1 
ATOM   1515 C  CA   D ARG   A 1 214 ? 39.73300 6.27700   8.31900  0.550 58.09258  ?  366 ARG   A CA   1 
ATOM   1516 C  C    A ARG   A 1 214 ? 39.53900 6.89100   9.69700  0.450 56.90779  ?  366 ARG   A C    1 
ATOM   1517 C  C    D ARG   A 1 214 ? 39.55900 6.90300   9.69500  0.550 56.95815  ?  366 ARG   A C    1 
ATOM   1518 O  O    A ARG   A 1 214 ? 39.07300 8.03400   9.77000  0.450 57.54978  ?  366 ARG   A O    1 
ATOM   1519 O  O    D ARG   A 1 214 ? 39.12000 8.05700   9.76900  0.550 57.58664  ?  366 ARG   A O    1 
ATOM   1520 C  CB   A ARG   A 1 214 ? 38.34200 6.05200   7.68400  0.450 56.78918  ?  366 ARG   A CB   1 
ATOM   1521 C  CB   D ARG   A 1 214 ? 38.34700 6.08200   7.68400  0.550 56.81759  ?  366 ARG   A CB   1 
ATOM   1522 C  CG   A ARG   A 1 214 ? 38.37800 5.25300   6.39000  0.450 57.92548  ?  366 ARG   A CG   1 
ATOM   1523 C  CG   D ARG   A 1 214 ? 38.39100 5.51000   6.27500  0.550 58.19235  ?  366 ARG   A CG   1 
ATOM   1524 C  CD   A ARG   A 1 214 ? 38.20700 6.15500   5.17700  0.450 60.45952  ?  366 ARG   A CD   1 
ATOM   1525 C  CD   D ARG   A 1 214 ? 38.66900 6.59100   5.23800  0.550 61.01153  ?  366 ARG   A CD   1 
ATOM   1526 N  NE   A ARG   A 1 214 ? 39.38900 6.97800   4.93300  0.450 62.80379  ?  366 ARG   A NE   1 
ATOM   1527 N  NE   D ARG   A 1 214 ? 38.41400 6.12400   3.87600  0.550 62.78042  ?  366 ARG   A NE   1 
ATOM   1528 C  CZ   A ARG   A 1 214 ? 39.36200 8.29700   4.77400  0.450 63.70227  ?  366 ARG   A CZ   1 
ATOM   1529 C  CZ   D ARG   A 1 214 ? 39.21900 5.31200   3.19600  0.550 64.31060  ?  366 ARG   A CZ   1 
ATOM   1530 N  NH1  A ARG   A 1 214 ? 38.21000 8.95100   4.83300  0.450 62.32725  ?  366 ARG   A NH1  1 
ATOM   1531 N  NH1  D ARG   A 1 214 ? 38.90000 4.93900   1.96400  0.550 65.12738  ?  366 ARG   A NH1  1 
ATOM   1532 N  NH2  A ARG   A 1 214 ? 40.48800 8.96400   4.55700  0.450 66.01568  ?  366 ARG   A NH2  1 
ATOM   1533 N  NH2  D ARG   A 1 214 ? 40.34500 4.87500   3.74200  0.550 64.35177  ?  366 ARG   A NH2  1 
ATOM   1534 N  N    . HIS   A 1 215 ? 39.87800 6.19400   10.78100 1.000 53.66633  ?  367 HIS   A N    1 
ATOM   1535 C  CA   . HIS   A 1 215 ? 39.77000 6.77800   12.11300 1.000 54.12042  ?  367 HIS   A CA   1 
ATOM   1536 C  C    . HIS   A 1 215 ? 41.16300 7.10300   12.62200 1.000 52.79888  ?  367 HIS   A C    1 
ATOM   1537 O  O    . HIS   A 1 215 ? 41.91400 6.18500   12.98600 1.000 54.38481  ?  367 HIS   A O    1 
ATOM   1538 C  CB   . HIS   A 1 215 ? 39.04900 5.84900   13.09100 1.000 52.35073  ?  367 HIS   A CB   1 
ATOM   1539 C  CG   . HIS   A 1 215 ? 38.32600 6.58000   14.18300 1.000 52.70688  ?  367 HIS   A CG   1 
ATOM   1540 N  ND1  . HIS   A 1 215 ? 36.96400 6.48200   14.37800 1.000 49.68403  ?  367 HIS   A ND1  1 
ATOM   1541 C  CD2  . HIS   A 1 215 ? 38.77600 7.45000   15.11800 1.000 53.57275  ?  367 HIS   A CD2  1 
ATOM   1542 C  CE1  . HIS   A 1 215 ? 36.61000 7.24600   15.39600 1.000 47.28209  ?  367 HIS   A CE1  1 
ATOM   1543 N  NE2  . HIS   A 1 215 ? 37.69000 7.84400   15.86300 1.000 51.26471  ?  367 HIS   A NE2  1 
ATOM   1544 N  N    . PRO   A 1 216 ? 41.55200 8.37800   12.66200 1.000 51.93273  ?  368 PRO   A N    1 
ATOM   1545 C  CA   . PRO   A 1 216 ? 42.93700 8.70400   13.00200 1.000 54.90264  ?  368 PRO   A CA   1 
ATOM   1546 C  C    . PRO   A 1 216 ? 43.19900 8.50400   14.47500 1.000 50.56021  ?  368 PRO   A C    1 
ATOM   1547 O  O    . PRO   A 1 216 ? 42.28600 8.61900   15.31400 1.000 49.33692  ?  368 PRO   A O    1 
ATOM   1548 C  CB   . PRO   A 1 216 ? 43.05400 10.18900  12.60100 1.000 56.74399  ?  368 PRO   A CB   1 
ATOM   1549 C  CG   . PRO   A 1 216 ? 41.84900 10.46300  11.72700 1.000 60.44310  ?  368 PRO   A CG   1 
ATOM   1550 C  CD   . PRO   A 1 216 ? 40.78400 9.55700   12.24100 1.000 54.84119  ?  368 PRO   A CD   1 
ATOM   1551 N  N    . PRO   A 1 217 ? 44.44000 8.18200   14.85800 1.000 49.08963  ?  369 PRO   A N    1 
ATOM   1552 C  CA   . PRO   A 1 217 ? 44.77000 8.10700   16.27500 1.000 49.18617  ?  369 PRO   A CA   1 
ATOM   1553 C  C    . PRO   A 1 217 ? 44.79200 9.51200   16.89400 1.000 53.65840  ?  369 PRO   A C    1 
ATOM   1554 O  O    . PRO   A 1 217 ? 45.00400 10.49800  16.18300 1.000 53.60676  ?  369 PRO   A O    1 
ATOM   1555 C  CB   . PRO   A 1 217 ? 46.17300 7.47400   16.28100 1.000 51.02999  ?  369 PRO   A CB   1 
ATOM   1556 C  CG   . PRO   A 1 217 ? 46.75100 7.83500   14.95800 1.000 54.95629  ?  369 PRO   A CG   1 
ATOM   1557 C  CD   . PRO   A 1 217 ? 45.58700 7.85200   13.99400 1.000 51.01220  ?  369 PRO   A CD   1 
ATOM   1558 N  N    . PRO   A 1 218 ? 44.58700 9.60700   18.21100 1.000 53.48231  ?  370 PRO   A N    1 
ATOM   1559 C  CA   . PRO   A 1 218 ? 44.38900 8.52100   19.17100 1.000 53.96565  ?  370 PRO   A CA   1 
ATOM   1560 C  C    . PRO   A 1 218 ? 42.93800 8.04500   19.31500 1.000 56.36161  ?  370 PRO   A C    1 
ATOM   1561 O  O    . PRO   A 1 218 ? 42.66900 7.14500   20.11400 1.000 56.55472  ?  370 PRO   A O    1 
ATOM   1562 C  CB   . PRO   A 1 218 ? 44.88800 9.13500   20.47600 1.000 60.52742  ?  370 PRO   A CB   1 
ATOM   1563 C  CG   . PRO   A 1 218 ? 44.54600 10.58500  20.34200 1.000 60.83971  ?  370 PRO   A CG   1 
ATOM   1564 C  CD   . PRO   A 1 218 ? 44.63500 10.92700  18.87300 1.000 56.04343  ?  370 PRO   A CD   1 
ATOM   1565 N  N    . GLY   A 1 219 ? 42.02100 8.62900   18.53900 1.000 52.39681  ?  371 GLY   A N    1 
ATOM   1566 C  CA   . GLY   A 1 219 ? 40.62700 8.22700   18.62400 1.000 47.36087  ?  371 GLY   A CA   1 
ATOM   1567 C  C    . GLY   A 1 219 ? 40.38900 6.76900   18.27600 1.000 45.38526  ?  371 GLY   A C    1 
ATOM   1568 O  O    . GLY   A 1 219 ? 39.44100 6.15600   18.77100 1.000 50.06695  ?  371 GLY   A O    1 
ATOM   1569 N  N    . SER   A 1 220 ? 41.24100 6.19100   17.43400 1.000 46.54253  ?  372 SER   A N    1 
ATOM   1570 C  CA   . SER   A 1 220 ? 41.09000 4.80000   17.03000 1.000 49.05229  ?  372 SER   A CA   1 
ATOM   1571 C  C    . SER   A 1 220 ? 41.69200 3.80500   18.01600 1.000 52.51506  ?  372 SER   A C    1 
ATOM   1572 O  O    . SER   A 1 220 ? 41.52200 2.59500   17.82300 1.000 49.98781  ?  372 SER   A O    1 
ATOM   1573 C  CB   . SER   A 1 220 ? 41.72600 4.58500   15.65600 1.000 52.68669  ?  372 SER   A CB   1 
ATOM   1574 O  OG   . SER   A 1 220 ? 43.11700 4.84600   15.70600 1.000 59.54758  ?  372 SER   A OG   1 
ATOM   1575 N  N    . HIS   A 1 221 ? 42.39600 4.27700   19.04900 1.000 52.74182  ?  373 HIS   A N    1 
ATOM   1576 C  CA   . HIS   A 1 221 ? 43.05900 3.38100   19.99100 1.000 52.23475  ?  373 HIS   A CA   1 
ATOM   1577 C  C    . HIS   A 1 221 ? 42.04900 2.45500   20.66000 1.000 53.56765  ?  373 HIS   A C    1 
ATOM   1578 O  O    . HIS   A 1 221 ? 41.15500 2.91200   21.38100 1.000 52.85804  ?  373 HIS   A O    1 
ATOM   1579 C  CB   . HIS   A 1 221 ? 43.81300 4.18900   21.04500 1.000 58.78140  ?  373 HIS   A CB   1 
ATOM   1580 C  CG   . HIS   A 1 221 ? 44.46300 3.34400   22.09900 1.000 61.96548  ?  373 HIS   A CG   1 
ATOM   1581 N  ND1  . HIS   A 1 221 ? 45.22800 2.23600   21.79900 1.000 61.04837  ?  373 HIS   A ND1  1 
ATOM   1582 C  CD2  . HIS   A 1 221 ? 44.43900 3.42900   23.45000 1.000 58.30289  ?  373 HIS   A CD2  1 
ATOM   1583 C  CE1  . HIS   A 1 221 ? 45.65500 1.68200   22.91900 1.000 62.04866  ?  373 HIS   A CE1  1 
ATOM   1584 N  NE2  . HIS   A 1 221 ? 45.18600 2.38400   23.93500 1.000 62.81980  ?  373 HIS   A NE2  1 
ATOM   1585 N  N    . GLN   A 1 222 ? 42.19500 1.15100   20.41100 1.000 49.59174  ?  374 GLN   A N    1 
ATOM   1586 C  CA   . GLN   A 1 222 ? 41.33700 0.11300   20.98000 1.000 51.35471  ?  374 GLN   A CA   1 
ATOM   1587 C  C    . GLN   A 1 222 ? 39.87000 0.30600   20.61000 1.000 51.24363  ?  374 GLN   A C    1 
ATOM   1588 O  O    . GLN   A 1 222 ? 38.98400 -0.21700  21.29600 1.000 50.42641  ?  374 GLN   A O    1 
ATOM   1589 C  CB   . GLN   A 1 222 ? 41.48300 0.04000   22.50500 1.000 50.63360  ?  374 GLN   A CB   1 
ATOM   1590 C  CG   . GLN   A 1 222 ? 42.79200 -0.57200  22.97900 1.000 62.70859  ?  374 GLN   A CG   1 
ATOM   1591 C  CD   . GLN   A 1 222 ? 43.01300 -0.39300  24.47100 1.000 68.30422  ?  374 GLN   A CD   1 
ATOM   1592 O  OE1  . GLN   A 1 222 ? 42.34100 0.41300   25.12000 1.000 67.79607  ?  374 GLN   A OE1  1 
ATOM   1593 N  NE2  . GLN   A 1 222 ? 43.96300 -1.14400  25.02300 1.000 72.51144  ?  374 GLN   A NE2  1 
ATOM   1594 N  N    . LEU   A 1 223 ? 39.59500 1.04000   19.53000 1.000 51.04177  ?  375 LEU   A N    1 
ATOM   1595 C  CA   . LEU   A 1 223 ? 38.21800 1.41600   19.22000 1.000 49.57654  ?  375 LEU   A CA   1 
ATOM   1596 C  C    . LEU   A 1 223 ? 37.35200 0.19200   18.94700 1.000 51.92335  ?  375 LEU   A C    1 
ATOM   1597 O  O    . LEU   A 1 223 ? 36.23000 0.08800   19.45800 1.000 52.42932  ?  375 LEU   A O    1 
ATOM   1598 C  CB   . LEU   A 1 223 ? 38.18400 2.37400   18.03100 1.000 50.03067  ?  375 LEU   A CB   1 
ATOM   1599 C  CG   . LEU   A 1 223 ? 36.81500 3.01100   17.75400 1.000 48.37993  ?  375 LEU   A CG   1 
ATOM   1600 C  CD1  . LEU   A 1 223 ? 36.05300 3.31000   19.04200 1.000 42.59574  ?  375 LEU   A CD1  1 
ATOM   1601 C  CD2  . LEU   A 1 223 ? 36.94800 4.26100   16.90400 1.000 51.16482  ?  375 LEU   A CD2  1 
ATOM   1602 N  N    . TYR   A 1 224 ? 37.85100 -0.74400  18.13200 1.000 51.46889  ?  376 TYR   A N    1 
ATOM   1603 C  CA   . TYR   A 1 224 ? 37.06500 -1.93600  17.82200 1.000 53.21573  ?  376 TYR   A CA   1 
ATOM   1604 C  C    . TYR   A 1 224 ? 36.75300 -2.73200  19.08000 1.000 54.24845  ?  376 TYR   A C    1 
ATOM   1605 O  O    . TYR   A 1 224 ? 35.61700 -3.18300  19.27600 1.000 51.10023  ?  376 TYR   A O    1 
ATOM   1606 C  CB   . TYR   A 1 224 ? 37.79900 -2.81800  16.81500 1.000 54.53236  ?  376 TYR   A CB   1 
ATOM   1607 C  CG   . TYR   A 1 224 ? 36.98900 -4.02500  16.39600 1.000 58.19645  ?  376 TYR   A CG   1 
ATOM   1608 C  CD1  . TYR   A 1 224 ? 35.81200 -3.87400  15.67400 1.000 59.29715  ?  376 TYR   A CD1  1 
ATOM   1609 C  CD2  . TYR   A 1 224 ? 37.39400 -5.31100  16.72900 1.000 58.42171  ?  376 TYR   A CD2  1 
ATOM   1610 C  CE1  . TYR   A 1 224 ? 35.06400 -4.96700  15.29000 1.000 59.43078  ?  376 TYR   A CE1  1 
ATOM   1611 C  CE2  . TYR   A 1 224 ? 36.65100 -6.41400  16.34700 1.000 60.19123  ?  376 TYR   A CE2  1 
ATOM   1612 C  CZ   . TYR   A 1 224 ? 35.48700 -6.23500  15.62700 1.000 61.33228  ?  376 TYR   A CZ   1 
ATOM   1613 O  OH   . TYR   A 1 224 ? 34.73900 -7.32500  15.24100 1.000 63.78599  ?  376 TYR   A OH   1 
ATOM   1614 N  N    . ALA   A 1 225 ? 37.75700 -2.91900  19.94000 1.000 55.87274  ?  377 ALA   A N    1 
ATOM   1615 C  CA   . ALA   A 1 225 ? 37.54800 -3.64200  21.18800 1.000 51.07074  ?  377 ALA   A CA   1 
ATOM   1616 C  C    . ALA   A 1 225 ? 36.54300 -2.92200  22.07400 1.000 45.78944  ?  377 ALA   A C    1 
ATOM   1617 O  O    . ALA   A 1 225 ? 35.71100 -3.56300  22.72600 1.000 48.46224  ?  377 ALA   A O    1 
ATOM   1618 C  CB   . ALA   A 1 225 ? 38.88100 -3.82400  21.91700 1.000 52.40072  ?  377 ALA   A CB   1 
ATOM   1619 N  N    A LYS   A 1 226 ? 36.60500 -1.58900  22.11200 0.580 43.69601  ?  378 LYS   A N    1 
ATOM   1620 N  N    B LYS   A 1 226 ? 36.59600 -1.58800  22.10300 0.420 44.11785  ?  378 LYS   A N    1 
ATOM   1621 C  CA   A LYS   A 1 226 ? 35.63700 -0.83100  22.89800 0.580 45.84237  ?  378 LYS   A CA   1 
ATOM   1622 C  CA   B LYS   A 1 226 ? 35.63500 -0.83500  22.90200 0.420 45.83001  ?  378 LYS   A CA   1 
ATOM   1623 C  C    A LYS   A 1 226 ? 34.23600 -0.92500  22.30400 0.580 44.38740  ?  378 LYS   A C    1 
ATOM   1624 C  C    B LYS   A 1 226 ? 34.23400 -0.89300  22.30300 0.420 44.35562  ?  378 LYS   A C    1 
ATOM   1625 O  O    A LYS   A 1 226 ? 33.24700 -0.93000  23.04700 0.580 44.61077  ?  378 LYS   A O    1 
ATOM   1626 O  O    B LYS   A 1 226 ? 33.24300 -0.83700  23.04100 0.420 44.60615  ?  378 LYS   A O    1 
ATOM   1627 C  CB   A LYS   A 1 226 ? 36.07500 0.63000   23.00600 0.580 48.97799  ?  378 LYS   A CB   1 
ATOM   1628 C  CB   B LYS   A 1 226 ? 36.09800 0.61400   23.05200 0.420 48.97297  ?  378 LYS   A CB   1 
ATOM   1629 C  CG   A LYS   A 1 226 ? 37.35600 0.83700   23.80800 0.580 52.39246  ?  378 LYS   A CG   1 
ATOM   1630 C  CG   B LYS   A 1 226 ? 37.31600 0.78000   23.95200 0.420 52.47108  ?  378 LYS   A CG   1 
ATOM   1631 C  CD   A LYS   A 1 226 ? 37.36000 2.18200   24.52200 0.580 55.18653  ?  378 LYS   A CD   1 
ATOM   1632 C  CD   B LYS   A 1 226 ? 38.00200 2.12100   23.73300 0.420 54.84853  ?  378 LYS   A CD   1 
ATOM   1633 C  CE   A LYS   A 1 226 ? 38.30000 3.17100   23.84500 0.580 57.34790  ?  378 LYS   A CE   1 
ATOM   1634 C  CE   B LYS   A 1 226 ? 37.48400 3.17800   24.70000 0.420 57.00096  ?  378 LYS   A CE   1 
ATOM   1635 N  NZ   A LYS   A 1 226 ? 39.73500 2.89900   24.14600 0.580 55.86630  ?  378 LYS   A NZ   1 
ATOM   1636 N  NZ   B LYS   A 1 226 ? 38.15800 4.49500   24.51000 0.420 58.96194  ?  378 LYS   A NZ   1 
ATOM   1637 N  N    . MET   A 1 227 ? 34.12700 -1.00700  20.97800 1.000 41.12786  ?  379 MET   A N    1 
ATOM   1638 C  CA   . MET   A 1 227 ? 32.80900 -1.12400  20.35700 1.000 40.86044  ?  379 MET   A CA   1 
ATOM   1639 C  C    . MET   A 1 227 ? 32.20300 -2.49600  20.62300 1.000 42.21409  ?  379 MET   A C    1 
ATOM   1640 O  O    . MET   A 1 227 ? 31.01300 -2.60500  20.95200 1.000 37.35680  ?  379 MET   A O    1 
ATOM   1641 C  CB   . MET   A 1 227 ? 32.91300 -0.85300  18.85700 1.000 35.34441  ?  379 MET   A CB   1 
ATOM   1642 C  CG   . MET   A 1 227 ? 33.12900 0.61200   18.51500 1.000 37.04816  ?  379 MET   A CG   1 
ATOM   1643 S  SD   . MET   A 1 227 ? 33.43700 0.88000   16.75900 1.000 41.12193  ?  379 MET   A SD   1 
ATOM   1644 C  CE   . MET   A 1 227 ? 31.74200 0.86300   16.15600 1.000 35.83617  ?  379 MET   A CE   1 
ATOM   1645 N  N    . ILE   A 1 228 ? 33.01500 -3.55200  20.50500 1.000 50.57471  ?  380 ILE   A N    1 
ATOM   1646 C  CA   . ILE   A 1 228 ? 32.56600 -4.89900  20.84500 1.000 51.76923  ?  380 ILE   A CA   1 
ATOM   1647 C  C    . ILE   A 1 228 ? 32.15100 -4.96900  22.31000 1.000 49.55736  ?  380 ILE   A C    1 
ATOM   1648 O  O    . ILE   A 1 228 ? 31.16600 -5.63100  22.65900 1.000 48.35134  ?  380 ILE   A O    1 
ATOM   1649 C  CB   . ILE   A 1 228 ? 33.66900 -5.92300  20.51500 1.000 55.04687  ?  380 ILE   A CB   1 
ATOM   1650 C  CG1  . ILE   A 1 228 ? 33.94400 -5.95000  19.00900 1.000 55.65931  ?  380 ILE   A CG1  1 
ATOM   1651 C  CG2  . ILE   A 1 228 ? 33.29000 -7.30800  21.01200 1.000 56.58027  ?  380 ILE   A CG2  1 
ATOM   1652 C  CD1  . ILE   A 1 228 ? 32.78000 -6.46800  18.18600 1.000 57.90864  ?  380 ILE   A CD1  1 
ATOM   1653 N  N    . GLN   A 1 229 ? 32.88500 -4.27900  23.18900 1.000 43.41129  ?  381 GLN   A N    1 
ATOM   1654 C  CA   . GLN   A 1 229 ? 32.48500 -4.23500  24.59300 1.000 45.05450  ?  381 GLN   A CA   1 
ATOM   1655 C  C    . GLN   A 1 229 ? 31.08000 -3.66400  24.74500 1.000 43.96444  ?  381 GLN   A C    1 
ATOM   1656 O  O    . GLN   A 1 229 ? 30.28600 -4.15500  25.55500 1.000 44.06666  ?  381 GLN   A O    1 
ATOM   1657 C  CB   . GLN   A 1 229 ? 33.48900 -3.42100  25.40900 1.000 51.04289  ?  381 GLN   A CB   1 
ATOM   1658 C  CG   . GLN   A 1 229 ? 33.09700 -3.23400  26.87000 1.000 52.37482  ?  381 GLN   A CG   1 
ATOM   1659 C  CD   . GLN   A 1 229 ? 32.87400 -4.55700  27.59000 1.000 55.38487  ?  381 GLN   A CD   1 
ATOM   1660 O  OE1  . GLN   A 1 229 ? 31.99800 -4.66900  28.44600 1.000 54.03957  ?  381 GLN   A OE1  1 
ATOM   1661 N  NE2  . GLN   A 1 229 ? 33.66800 -5.56300  27.24400 1.000 56.77531  ?  381 GLN   A NE2  1 
ATOM   1662 N  N    . LYS   A 1 230 ? 30.75300 -2.63300  23.96300 1.000 42.23852  ?  382 LYS   A N    1 
ATOM   1663 C  CA   . LYS   A 1 230 ? 29.41800 -2.05300  24.01800 1.000 43.02855  ?  382 LYS   A CA   1 
ATOM   1664 C  C    . LYS   A 1 230 ? 28.35500 -3.04700  23.56600 1.000 38.93786  ?  382 LYS   A C    1 
ATOM   1665 O  O    . LYS   A 1 230 ? 27.21400 -2.99100  24.03800 1.000 37.31847  ?  382 LYS   A O    1 
ATOM   1666 C  CB   . LYS   A 1 230 ? 29.37500 -0.77900  23.17800 1.000 43.62746  ?  382 LYS   A CB   1 
ATOM   1667 C  CG   . LYS   A 1 230 ? 30.10100 0.38900   23.82800 1.000 45.03829  ?  382 LYS   A CG   1 
ATOM   1668 C  CD   . LYS   A 1 230 ? 29.47200 0.75800   25.16600 1.000 46.18015  ?  382 LYS   A CD   1 
ATOM   1669 C  CE   . LYS   A 1 230 ? 30.46500 1.46100   26.09600 1.000 53.90020  ?  382 LYS   A CE   1 
ATOM   1670 N  NZ   . LYS   A 1 230 ? 31.80200 0.78000   26.20700 1.000 56.77317  ?  382 LYS   A NZ   1 
ATOM   1671 N  N    . LEU   A 1 231 ? 28.70700 -3.97100  22.67100 1.000 37.01476  ?  383 LEU   A N    1 
ATOM   1672 C  CA   . LEU   A 1 231 ? 27.78700 -5.05600  22.34800 1.000 38.51458  ?  383 LEU   A CA   1 
ATOM   1673 C  C    . LEU   A 1 231 ? 27.54600 -5.94100  23.56300 1.000 38.27519  ?  383 LEU   A C    1 
ATOM   1674 O  O    . LEU   A 1 231 ? 26.42400 -6.41200  23.78800 1.000 35.05831  ?  383 LEU   A O    1 
ATOM   1675 C  CB   . LEU   A 1 231 ? 28.33200 -5.88400  21.18700 1.000 36.05314  ?  383 LEU   A CB   1 
ATOM   1676 C  CG   . LEU   A 1 231 ? 28.33200 -5.20900  19.81900 1.000 34.80952  ?  383 LEU   A CG   1 
ATOM   1677 C  CD1  . LEU   A 1 231 ? 29.14500 -6.03700  18.83800 1.000 35.38526  ?  383 LEU   A CD1  1 
ATOM   1678 C  CD2  . LEU   A 1 231 ? 26.90900 -5.02000  19.33500 1.000 34.05909  ?  383 LEU   A CD2  1 
ATOM   1679 N  N    . ALA   A 1 232 ? 28.59800 -6.18800  24.35300 1.000 39.66463  ?  384 ALA   A N    1 
ATOM   1680 C  CA   . ALA   A 1 232 ? 28.44500 -6.94900  25.59000 1.000 40.20286  ?  384 ALA   A CA   1 
ATOM   1681 C  C    . ALA   A 1 232 ? 27.60800 -6.18400  26.60600 1.000 40.55619  ?  384 ALA   A C    1 
ATOM   1682 O  O    . ALA   A 1 232 ? 26.74500 -6.76900  27.27200 1.000 40.41286  ?  384 ALA   A O    1 
ATOM   1683 C  CB   . ALA   A 1 232 ? 29.81800 -7.28400  26.17800 1.000 41.24836  ?  384 ALA   A CB   1 
ATOM   1684 N  N    . ASP   A 1 233 ? 27.86700 -4.87800  26.75300 1.000 36.48785  ?  385 ASP   A N    1 
ATOM   1685 C  CA   . ASP   A 1 233 ? 27.01700 -4.04300  27.59400 1.000 37.75998  ?  385 ASP   A CA   1 
ATOM   1686 C  C    . ASP   A 1 233 ? 25.55800 -4.14800  27.16500 1.000 38.49714  ?  385 ASP   A C    1 
ATOM   1687 O  O    . ASP   A 1 233 ? 24.65400 -4.15800  28.00700 1.000 38.65390  ?  385 ASP   A O    1 
ATOM   1688 C  CB   . ASP   A 1 233 ? 27.46700 -2.58400  27.52400 1.000 37.38661  ?  385 ASP   A CB   1 
ATOM   1689 C  CG   . ASP   A 1 233 ? 28.86600 -2.36400  28.07500 1.000 47.61280  ?  385 ASP   A CG   1 
ATOM   1690 O  OD1  . ASP   A 1 233 ? 29.30600 -1.19600  28.07100 1.000 49.99553  ?  385 ASP   A OD1  1 
ATOM   1691 O  OD2  . ASP   A 1 233 ? 29.52200 -3.33700  28.51000 1.000 48.13089  ?  385 ASP   A OD2  1 
ATOM   1692 N  N    . LEU   A 1 234 ? 25.31500 -4.22900  25.85200 1.000 35.39190  ?  386 LEU   A N    1 
ATOM   1693 C  CA   . LEU   A 1 234 ? 23.95000 -4.29000  25.34600 1.000 39.06258  ?  386 LEU   A CA   1 
ATOM   1694 C  C    . LEU   A 1 234 ? 23.26800 -5.59700  25.72400 1.000 42.36699  ?  386 LEU   A C    1 
ATOM   1695 O  O    . LEU   A 1 234 ? 22.06300 -5.61100  26.00800 1.000 41.84037  ?  386 LEU   A O    1 
ATOM   1696 C  CB   . LEU   A 1 234 ? 23.94900 -4.10600  23.83200 1.000 38.43053  ?  386 LEU   A CB   1 
ATOM   1697 C  CG   . LEU   A 1 234 ? 24.16600 -2.66300  23.39300 1.000 41.09143  ?  386 LEU   A CG   1 
ATOM   1698 C  CD1  . LEU   A 1 234 ? 24.35100 -2.60700  21.89300 1.000 45.52590  ?  386 LEU   A CD1  1 
ATOM   1699 C  CD2  . LEU   A 1 234 ? 22.99200 -1.80100  23.83600 1.000 44.26358  ?  386 LEU   A CD2  1 
ATOM   1700 N  N    . ARG   A 1 235 ? 24.00900 -6.70900  25.71200 1.000 37.27962  ?  387 ARG   A N    1 
ATOM   1701 C  CA   . ARG   A 1 235 ? 23.41400 -7.97900  26.12000 1.000 38.38979  ?  387 ARG   A CA   1 
ATOM   1702 C  C    . ARG   A 1 235 ? 22.93200 -7.91200  27.56000 1.000 42.91016  ?  387 ARG   A C    1 
ATOM   1703 O  O    . ARG   A 1 235 ? 21.87400 -8.45500  27.89800 1.000 39.95140  ?  387 ARG   A O    1 
ATOM   1704 C  CB   . ARG   A 1 235 ? 24.41700 -9.11700  25.95400 1.000 38.79330  ?  387 ARG   A CB   1 
ATOM   1705 C  CG   . ARG   A 1 235 ? 24.94100 -9.28800  24.55400 1.000 41.75116  ?  387 ARG   A CG   1 
ATOM   1706 C  CD   . ARG   A 1 235 ? 23.80700 -9.55600  23.56600 1.000 40.84551  ?  387 ARG   A CD   1 
ATOM   1707 N  NE   . ARG   A 1 235 ? 24.34000 -9.91700  22.25700 1.000 37.33269  ?  387 ARG   A NE   1 
ATOM   1708 C  CZ   . ARG   A 1 235 ? 24.52100 -11.16900 21.85200 1.000 39.18577  ?  387 ARG   A CZ   1 
ATOM   1709 N  NH1  . ARG   A 1 235 ? 24.20200 -12.17700 22.65200 1.000 34.12208  ?  387 ARG   A NH1  1 
ATOM   1710 N  NH2  . ARG   A 1 235 ? 25.01600 -11.41100 20.64700 1.000 44.61900  ?  387 ARG   A NH2  1 
ATOM   1711 N  N    . SER   A 1 236 ? 23.70200 -7.24600  28.42500 1.000 46.71959  ?  388 SER   A N    1 
ATOM   1712 C  CA   . SER   A 1 236 ? 23.30000 -7.10400  29.81800 1.000 46.40012  ?  388 SER   A CA   1 
ATOM   1713 C  C    . SER   A 1 236 ? 22.12400 -6.14400  29.95200 1.000 39.98854  ?  388 SER   A C    1 
ATOM   1714 O  O    . SER   A 1 236 ? 21.19200 -6.40000  30.72400 1.000 39.31138  ?  388 SER   A O    1 
ATOM   1715 C  CB   . SER   A 1 236 ? 24.49900 -6.64100  30.65400 1.000 51.36474  ?  388 SER   A CB   1 
ATOM   1716 O  OG   . SER   A 1 236 ? 24.09600 -5.81800  31.73300 1.000 58.02334  ?  388 SER   A OG   1 
ATOM   1717 N  N    . LEU   A 1 237 ? 22.14500 -5.04100  29.20000 1.000 41.27462  ?  389 LEU   A N    1 
ATOM   1718 C  CA   . LEU   A 1 237 ? 21.00300 -4.13200  29.17200 1.000 41.97056  ?  389 LEU   A CA   1 
ATOM   1719 C  C    . LEU   A 1 237 ? 19.76100 -4.82400  28.61800 1.000 42.28978  ?  389 LEU   A C    1 
ATOM   1720 O  O    . LEU   A 1 237 ? 18.64900 -4.61600  29.11700 1.000 36.44712  ?  389 LEU   A O    1 
ATOM   1721 C  CB   . LEU   A 1 237 ? 21.35500 -2.88900  28.34800 1.000 38.70060  ?  389 LEU   A CB   1 
ATOM   1722 C  CG   . LEU   A 1 237 ? 22.35800 -1.94300  29.01900 1.000 42.59613  ?  389 LEU   A CG   1 
ATOM   1723 C  CD1  . LEU   A 1 237 ? 22.80500 -0.82000  28.08700 1.000 38.51263  ?  389 LEU   A CD1  1 
ATOM   1724 C  CD2  . LEU   A 1 237 ? 21.75100 -1.36000  30.29000 1.000 45.21151  ?  389 LEU   A CD2  1 
ATOM   1725 N  N    . ASN   A 1 238 ? 19.93700 -5.64800  27.58100 1.000 42.42957  ?  390 ASN   A N    1 
ATOM   1726 C  CA   . ASN   A 1 238 ? 18.84800 -6.46700  27.05200 1.000 40.10909  ?  390 ASN   A CA   1 
ATOM   1727 C  C    . ASN   A 1 238 ? 18.25700 -7.35300  28.14000 1.000 41.29718  ?  390 ASN   A C    1 
ATOM   1728 O  O    . ASN   A 1 238 ? 17.03400 -7.41000  28.32200 1.000 35.73864  ?  390 ASN   A O    1 
ATOM   1729 C  CB   . ASN   A 1 238 ? 19.37700 -7.31200  25.88800 1.000 38.49104  ?  390 ASN   A CB   1 
ATOM   1730 C  CG   . ASN   A 1 238 ? 18.28000 -8.00700  25.09500 1.000 40.52534  ?  390 ASN   A CG   1 
ATOM   1731 O  OD1  . ASN   A 1 238 ? 17.20600 -8.31400  25.60800 1.000 40.68108  ?  390 ASN   A OD1  1 
ATOM   1732 N  ND2  . ASN   A 1 238 ? 18.56400 -8.26900  23.82600 1.000 34.64354  ?  390 ASN   A ND2  1 
ATOM   1733 N  N    . GLU   A 1 239 ? 19.12100 -8.05600  28.87300 1.000 38.22631  ?  391 GLU   A N    1 
ATOM   1734 C  CA   . GLU   A 1 239 ? 18.67300 -8.93500  29.94800 1.000 46.90588  ?  391 GLU   A CA   1 
ATOM   1735 C  C    . GLU   A 1 239 ? 17.82600 -8.18200  30.96700 1.000 48.60654  ?  391 GLU   A C    1 
ATOM   1736 O  O    . GLU   A 1 239 ? 16.74400 -8.64000  31.35500 1.000 46.39819  ?  391 GLU   A O    1 
ATOM   1737 C  CB   . GLU   A 1 239 ? 19.88800 -9.56200  30.63200 1.000 55.85435  ?  391 GLU   A CB   1 
ATOM   1738 C  CG   . GLU   A 1 239 ? 20.04000 -11.05200 30.42400 1.000 61.50958  ?  391 GLU   A CG   1 
ATOM   1739 C  CD   . GLU   A 1 239 ? 20.77700 -11.71000 31.57400 1.000 68.86465  ?  391 GLU   A CD   1 
ATOM   1740 O  OE1  . GLU   A 1 239 ? 21.92300 -11.30100 31.86200 1.000 69.04693  ?  391 GLU   A OE1  1 
ATOM   1741 O  OE2  . GLU   A 1 239 ? 20.20500 -12.63200 32.19500 1.000 72.36282  ?  391 GLU   A OE2  1 
ATOM   1742 N  N    . GLU   A 1 240 ? 18.30900 -7.02200  31.41900 1.000 48.84624  ?  392 GLU   A N    1 
ATOM   1743 C  CA   . GLU   A 1 240 ? 17.60800 -6.30200  32.47400 1.000 49.03154  ?  392 GLU   A CA   1 
ATOM   1744 C  C    . GLU   A 1 240 ? 16.29600 -5.71700  31.97300 1.000 45.45737  ?  392 GLU   A C    1 
ATOM   1745 O  O    . GLU   A 1 240 ? 15.28200 -5.78700  32.67500 1.000 47.30868  ?  392 GLU   A O    1 
ATOM   1746 C  CB   . GLU   A 1 240 ? 18.49800 -5.20200  33.05300 1.000 49.21042  ?  392 GLU   A CB   1 
ATOM   1747 C  CG   . GLU   A 1 240 ? 17.93400 -4.55900  34.30800 1.000 45.36524  ?  392 GLU   A CG   1 
ATOM   1748 C  CD   . GLU   A 1 240 ? 17.64500 -5.57200  35.40600 1.000 45.89109  ?  392 GLU   A CD   1 
ATOM   1749 O  OE1  . GLU   A 1 240 ? 18.40200 -6.56000  35.52900 1.000 45.75242  ?  392 GLU   A OE1  1 
ATOM   1750 O  OE2  . GLU   A 1 240 ? 16.65300 -5.38800  36.14000 1.000 48.61957  ?  392 GLU   A OE2  1 
ATOM   1751 N  N    . HIS   A 1 241 ? 16.29600 -5.12400  30.77200 1.000 42.11807  ?  393 HIS   A N    1 
ATOM   1752 C  CA   . HIS   A 1 241 ? 15.04900 -4.60500  30.21300 1.000 43.46897  ?  393 HIS   A CA   1 
ATOM   1753 C  C    . HIS   A 1 241 ? 14.02600 -5.72000  30.03900 1.000 39.71849  ?  393 HIS   A C    1 
ATOM   1754 O  O    . HIS   A 1 241 ? 12.86300 -5.57100  30.42500 1.000 39.18391  ?  393 HIS   A O    1 
ATOM   1755 C  CB   . HIS   A 1 241 ? 15.28800 -3.90200  28.87300 1.000 42.43375  ?  393 HIS   A CB   1 
ATOM   1756 C  CG   . HIS   A 1 241 ? 14.02100 -3.45300  28.20300 1.000 43.23260  ?  393 HIS   A CG   1 
ATOM   1757 N  ND1  . HIS   A 1 241 ? 13.30000 -4.26000  27.34800 1.000 41.55079  ?  393 HIS   A ND1  1 
ATOM   1758 C  CD2  . HIS   A 1 241 ? 13.33100 -2.29000  28.28900 1.000 42.78237  ?  393 HIS   A CD2  1 
ATOM   1759 C  CE1  . HIS   A 1 241 ? 12.22800 -3.61100  26.92900 1.000 43.26947  ?  393 HIS   A CE1  1 
ATOM   1760 N  NE2  . HIS   A 1 241 ? 12.22300 -2.41300  27.48500 1.000 42.97844  ?  393 HIS   A NE2  1 
ATOM   1761 N  N    . SER   A 1 242 ? 14.45300 -6.85300  29.47400 1.000 40.89587  ?  394 SER   A N    1 
ATOM   1762 C  CA   . SER   A 1 242 ? 13.54000 -7.96900  29.23900 1.000 44.33796  ?  394 SER   A CA   1 
ATOM   1763 C  C    . SER   A 1 242 ? 12.88400 -8.43500  30.53200 1.000 47.16393  ?  394 SER   A C    1 
ATOM   1764 O  O    . SER   A 1 242 ? 11.69200 -8.76900  30.55100 1.000 48.68405  ?  394 SER   A O    1 
ATOM   1765 C  CB   . SER   A 1 242 ? 14.29100 -9.12600  28.57600 1.000 42.81371  ?  394 SER   A CB   1 
ATOM   1766 O  OG   . SER   A 1 242 ? 14.80800 -8.74200  27.31000 1.000 43.31268  ?  394 SER   A OG   1 
ATOM   1767 N  N    . LYS   A 1 243 ? 13.64800 -8.46800  31.62400 1.000 46.86000  ?  395 LYS   A N    1 
ATOM   1768 C  CA   . LYS   A 1 243 ? 13.10000 -8.92600  32.89500 1.000 46.04156  ?  395 LYS   A CA   1 
ATOM   1769 C  C    . LYS   A 1 243 ? 12.13600 -7.89800  33.47600 1.000 45.43585  ?  395 LYS   A C    1 
ATOM   1770 O  O    . LYS   A 1 243 ? 11.08600 -8.25900  34.01900 1.000 48.56563  ?  395 LYS   A O    1 
ATOM   1771 C  CB   . LYS   A 1 243 ? 14.24500 -9.23300  33.86100 1.000 49.32717  ?  395 LYS   A CB   1 
ATOM   1772 C  CG   . LYS   A 1 243 ? 13.96100 -9.00400  35.33700 1.000 53.59252  ?  395 LYS   A CG   1 
ATOM   1773 C  CD   . LYS   A 1 243 ? 15.24500 -9.20300  36.16200 1.000 49.17596  ?  395 LYS   A CD   1 
ATOM   1774 C  CE   . LYS   A 1 243 ? 14.99800 -10.05300 37.40300 1.000 55.28241  ?  395 LYS   A CE   1 
ATOM   1775 N  NZ   . LYS   A 1 243 ? 16.23100 -10.19400 38.25100 1.000 60.41556  ?  395 LYS   A NZ   1 
ATOM   1776 N  N    . GLN   A 1 244 ? 12.46400 -6.61100  33.35600 1.000 43.11454  ?  396 GLN   A N    1 
ATOM   1777 C  CA   . GLN   A 1 244 ? 11.54500 -5.58000  33.82400 1.000 40.23186  ?  396 GLN   A CA   1 
ATOM   1778 C  C    . GLN   A 1 244 ? 10.34100 -5.44800  32.90000 1.000 46.63776  ?  396 GLN   A C    1 
ATOM   1779 O  O    . GLN   A 1 244 ? 9.22900  -5.16100  33.36500 1.000 45.58139  ?  396 GLN   A O    1 
ATOM   1780 C  CB   . GLN   A 1 244 ? 12.27700 -4.24500  33.94300 1.000 39.12859  ?  396 GLN   A CB   1 
ATOM   1781 C  CG   . GLN   A 1 244 ? 13.35900 -4.25900  35.00600 1.000 40.75912  ?  396 GLN   A CG   1 
ATOM   1782 C  CD   . GLN   A 1 244 ? 13.91500 -2.88100  35.30600 1.000 46.86207  ?  396 GLN   A CD   1 
ATOM   1783 O  OE1  . GLN   A 1 244 ? 13.33600 -1.86400  34.91800 1.000 46.27862  ?  396 GLN   A OE1  1 
ATOM   1784 N  NE2  . GLN   A 1 244 ? 15.05000 -2.84200  36.00100 1.000 46.46762  ?  396 GLN   A NE2  1 
ATOM   1785 N  N    . TYR   A 1 245 ? 10.53700 -5.65300  31.59800 1.000 45.47663  ?  397 TYR   A N    1 
ATOM   1786 C  CA   . TYR   A 1 245 ? 9.40000  -5.63000  30.68700 1.000 47.16236  ?  397 TYR   A CA   1 
ATOM   1787 C  C    . TYR   A 1 245 ? 8.45400  -6.79100  30.96700 1.000 46.37537  ?  397 TYR   A C    1 
ATOM   1788 O  O    . TYR   A 1 245 ? 7.23000  -6.62800  30.90500 1.000 46.77018  ?  397 TYR   A O    1 
ATOM   1789 C  CB   . TYR   A 1 245 ? 9.87500  -5.66200  29.23400 1.000 41.40503  ?  397 TYR   A CB   1 
ATOM   1790 C  CG   . TYR   A 1 245 ? 8.72800  -5.81700  28.25000 1.000 38.57584  ?  397 TYR   A CG   1 
ATOM   1791 C  CD1  . TYR   A 1 245 ? 8.04500  -4.70800  27.77300 1.000 38.31115  ?  397 TYR   A CD1  1 
ATOM   1792 C  CD2  . TYR   A 1 245 ? 8.31600  -7.07500  27.82100 1.000 38.01702  ?  397 TYR   A CD2  1 
ATOM   1793 C  CE1  . TYR   A 1 245 ? 6.98600  -4.84900  26.88300 1.000 36.20492  ?  397 TYR   A CE1  1 
ATOM   1794 C  CE2  . TYR   A 1 245 ? 7.25800  -7.22200  26.94100 1.000 37.17302  ?  397 TYR   A CE2  1 
ATOM   1795 C  CZ   . TYR   A 1 245 ? 6.60400  -6.10800  26.47400 1.000 36.49802  ?  397 TYR   A CZ   1 
ATOM   1796 O  OH   . TYR   A 1 245 ? 5.56000  -6.25700  25.59000 1.000 44.30034  ?  397 TYR   A OH   1 
ATOM   1797 N  N    . ARG   A 1 246 ? 9.00300  -7.97200  31.26100 1.000 43.55150  ?  398 ARG   A N    1 
ATOM   1798 C  CA   . ARG   A 1 246 ? 8.16300  -9.12400  31.57000 1.000 50.56596  ?  398 ARG   A CA   1 
ATOM   1799 C  C    . ARG   A 1 246 ? 7.34500  -8.88100  32.83200 1.000 56.45319  ?  398 ARG   A C    1 
ATOM   1800 O  O    . ARG   A 1 246 ? 6.16200  -9.23900  32.89500 1.000 55.81785  ?  398 ARG   A O    1 
ATOM   1801 C  CB   . ARG   A 1 246 ? 9.02800  -10.37600 31.71500 1.000 55.37041  ?  398 ARG   A CB   1 
ATOM   1802 C  CG   . ARG   A 1 246 ? 8.24800  -11.65400 31.98600 1.000 65.77758  ?  398 ARG   A CG   1 
ATOM   1803 C  CD   . ARG   A 1 246 ? 8.74000  -12.35400 33.25200 1.000 75.07519  ?  398 ARG   A CD   1 
ATOM   1804 N  NE   . ARG   A 1 246 ? 8.37800  -13.77000 33.27900 1.000 81.40876  ?  398 ARG   A NE   1 
ATOM   1805 C  CZ   . ARG   A 1 246 ? 8.30700  -14.50800 34.38500 1.000 86.54206  ?  398 ARG   A CZ   1 
ATOM   1806 N  NH1  . ARG   A 1 246 ? 8.57100  -13.96800 35.56900 1.000 87.25228  ?  398 ARG   A NH1  1 
ATOM   1807 N  NH2  . ARG   A 1 246 ? 7.96700  -15.78800 34.30700 1.000 89.42704  ?  398 ARG   A NH2  1 
ATOM   1808 N  N    . SER   A 1 247 ? 7.95600  -8.26600  33.84600 1.000 55.16885  ?  399 SER   A N    1 
ATOM   1809 C  CA   . SER   A 1 247 ? 7.21400  -7.93600  35.05800 1.000 57.35612  ?  399 SER   A CA   1 
ATOM   1810 C  C    . SER   A 1 247 ? 6.15300  -6.87700  34.78100 1.000 54.60964  ?  399 SER   A C    1 
ATOM   1811 O  O    . SER   A 1 247 ? 5.01400  -6.99300  35.25000 1.000 56.14895  ?  399 SER   A O    1 
ATOM   1812 C  CB   . SER   A 1 247 ? 8.18100  -7.46700  36.14700 1.000 55.68872  ?  399 SER   A CB   1 
ATOM   1813 O  OG   . SER   A 1 247 ? 7.59000  -6.48000  36.97500 1.000 57.29884  ?  399 SER   A OG   1 
ATOM   1814 N  N    . LEU   A 1 248 ? 6.50600  -5.84300  34.01300 1.000 50.48955  ?  400 LEU   A N    1 
ATOM   1815 C  CA   . LEU   A 1 248 ? 5.55800  -4.77500  33.71600 1.000 53.06139  ?  400 LEU   A CA   1 
ATOM   1816 C  C    . LEU   A 1 248 ? 4.40600  -5.28600  32.85900 1.000 54.90667  ?  400 LEU   A C    1 
ATOM   1817 O  O    . LEU   A 1 248 ? 3.23500  -5.01700  33.14900 1.000 56.03271  ?  400 LEU   A O    1 
ATOM   1818 C  CB   . LEU   A 1 248 ? 6.27500  -3.61700  33.01800 1.000 49.23296  ?  400 LEU   A CB   1 
ATOM   1819 C  CG   . LEU   A 1 248 ? 7.12700  -2.70000  33.90000 1.000 49.01105  ?  400 LEU   A CG   1 
ATOM   1820 C  CD1  . LEU   A 1 248 ? 8.00200  -1.78800  33.04800 1.000 47.67528  ?  400 LEU   A CD1  1 
ATOM   1821 C  CD2  . LEU   A 1 248 ? 6.25400  -1.88700  34.84800 1.000 47.11658  ?  400 LEU   A CD2  1 
ATOM   1822 N  N    . SER   A 1 249 ? 4.72000  -6.03700  31.80100 1.000 54.94788  ?  401 SER   A N    1 
ATOM   1823 C  CA   . SER   A 1 249 ? 3.69300  -6.50100  30.87800 1.000 54.77187  ?  401 SER   A CA   1 
ATOM   1824 C  C    . SER   A 1 249 ? 2.81800  -7.59300  31.47300 1.000 58.98039  ?  401 SER   A C    1 
ATOM   1825 O  O    . SER   A 1 249 ? 1.76200  -7.89000  30.90500 1.000 60.72622  ?  401 SER   A O    1 
ATOM   1826 C  CB   . SER   A 1 249 ? 4.33200  -6.99500  29.57300 1.000 51.06942  ?  401 SER   A CB   1 
ATOM   1827 O  OG   . SER   A 1 249 ? 4.95700  -8.25900  29.73200 1.000 51.62004  ?  401 SER   A OG   1 
ATOM   1828 N  N    . PHE   A 1 250 ? 3.22000  -8.19500  32.59500 1.000 60.82400  ?  402 PHE   A N    1 
ATOM   1829 C  CA   . PHE   A 1 250 ? 2.36500  -9.19100  33.23400 1.000 63.76298  ?  402 PHE   A CA   1 
ATOM   1830 C  C    . PHE   A 1 250 ? 1.07900  -8.55900  33.74900 1.000 64.27923  ?  402 PHE   A C    1 
ATOM   1831 O  O    . PHE   A 1 250 ? 0.01700  -9.19100  33.71700 1.000 67.68683  ?  402 PHE   A O    1 
ATOM   1832 C  CB   . PHE   A 1 250 ? 3.11000  -9.88800  34.37200 1.000 68.75858  ?  402 PHE   A CB   1 
ATOM   1833 C  CG   . PHE   A 1 250 ? 2.39800  -11.10300 34.90800 1.000 75.88768  ?  402 PHE   A CG   1 
ATOM   1834 C  CD1  . PHE   A 1 250 ? 2.30400  -12.26000 34.14800 1.000 77.35007  ?  402 PHE   A CD1  1 
ATOM   1835 C  CD2  . PHE   A 1 250 ? 1.81900  -11.08700 36.16900 1.000 79.31315  ?  402 PHE   A CD2  1 
ATOM   1836 C  CE1  . PHE   A 1 250 ? 1.65000  -13.37900 34.63700 1.000 79.45095  ?  402 PHE   A CE1  1 
ATOM   1837 C  CE2  . PHE   A 1 250 ? 1.16400  -12.20300 36.66200 1.000 82.43361  ?  402 PHE   A CE2  1 
ATOM   1838 C  CZ   . PHE   A 1 250 ? 1.07900  -13.35000 35.89500 1.000 82.06952  ?  402 PHE   A CZ   1 
ATOM   1839 N  N    . GLN   A 1 251 ? 1.15600  -7.32500  34.23000 1.000 62.04647  ?  403 GLN   A N    1 
ATOM   1840 C  CA   . GLN   A 1 251 ? -0.03200 -6.61000  34.66800 1.000 61.90586  ?  403 GLN   A CA   1 
ATOM   1841 C  C    . GLN   A 1 251 ? -0.85600 -6.24400  33.44100 1.000 56.33483  ?  403 GLN   A C    1 
ATOM   1842 O  O    . GLN   A 1 251 ? -0.36900 -5.49700  32.58200 1.000 51.96843  ?  403 GLN   A O    1 
ATOM   1843 C  CB   . GLN   A 1 251 ? 0.34300  -5.35600  35.45000 1.000 66.30285  ?  403 GLN   A CB   1 
ATOM   1844 C  CG   . GLN   A 1 251 ? 1.58400  -5.49800  36.32400 1.000 75.41366  ?  403 GLN   A CG   1 
ATOM   1845 C  CD   . GLN   A 1 251 ? 1.37200  -6.43500  37.49500 1.000 84.42805  ?  403 GLN   A CD   1 
ATOM   1846 O  OE1  . GLN   A 1 251 ? 1.94700  -7.52300  37.54800 1.000 86.38480  ?  403 GLN   A OE1  1 
ATOM   1847 N  NE2  . GLN   A 1 251 ? 0.53200  -6.02000  38.43900 1.000 89.23787  ?  403 GLN   A NE2  1 
ATOM   1848 N  N    . PRO   A 1 252 ? -2.08400 -6.75500  33.30300 1.000 53.77086  ?  404 PRO   A N    1 
ATOM   1849 C  CA   . PRO   A 1 252 ? -2.85700 -6.46300  32.08400 1.000 52.38873  ?  404 PRO   A CA   1 
ATOM   1850 C  C    . PRO   A 1 252 ? -3.11700 -4.98200  31.87900 1.000 53.69228  ?  404 PRO   A C    1 
ATOM   1851 O  O    . PRO   A 1 252 ? -3.09200 -4.50700  30.73600 1.000 58.18153  ?  404 PRO   A O    1 
ATOM   1852 C  CB   . PRO   A 1 252 ? -4.15500 -7.25300  32.30000 1.000 56.74409  ?  404 PRO   A CB   1 
ATOM   1853 C  CG   . PRO   A 1 252 ? -3.79100 -8.33200  33.25900 1.000 58.93539  ?  404 PRO   A CG   1 
ATOM   1854 C  CD   . PRO   A 1 252 ? -2.76300 -7.72900  34.17400 1.000 56.90047  ?  404 PRO   A CD   1 
ATOM   1855 N  N    . GLU   A 1 253 ? -3.35100 -4.23500  32.96200 1.000 55.85355  ?  405 GLU   A N    1 
ATOM   1856 C  CA   . GLU   A 1 253 ? -3.55000 -2.79300  32.85000 1.000 59.36219  ?  405 GLU   A CA   1 
ATOM   1857 C  C    . GLU   A 1 253 ? -2.36500 -2.11100  32.17800 1.000 57.39453  ?  405 GLU   A C    1 
ATOM   1858 O  O    . GLU   A 1 253 ? -2.55100 -1.14100  31.43400 1.000 55.73620  ?  405 GLU   A O    1 
ATOM   1859 C  CB   . GLU   A 1 253 ? -3.79700 -2.18500  34.23300 1.000 67.71368  ?  405 GLU   A CB   1 
ATOM   1860 C  CG   . GLU   A 1 253 ? -2.70700 -2.47400  35.27800 1.000 76.46892  ?  405 GLU   A CG   1 
ATOM   1861 C  CD   . GLU   A 1 253 ? -2.81600 -3.85200  35.92400 1.000 83.39941  ?  405 GLU   A CD   1 
ATOM   1862 O  OE1  . GLU   A 1 253 ? -3.32400 -4.79000  35.27300 1.000 85.96139  ?  405 GLU   A OE1  1 
ATOM   1863 O  OE2  . GLU   A 1 253 ? -2.38200 -3.99500  37.08900 1.000 85.79956  ?  405 GLU   A OE2  1 
ATOM   1864 N  N    . ASN   A 1 254 ? -1.14400 -2.59900  32.42800 1.000 52.82107  ?  406 ASN   A N    1 
ATOM   1865 C  CA   . ASN   A 1 254 ? 0.02300  -2.06100  31.73500 1.000 51.23887  ?  406 ASN   A CA   1 
ATOM   1866 C  C    . ASN   A 1 254 ? 0.05500  -2.51300  30.28100 1.000 46.47020  ?  406 ASN   A C    1 
ATOM   1867 O  O    . ASN   A 1 254 ? 0.32300  -1.70800  29.38300 1.000 42.06910  ?  406 ASN   A O    1 
ATOM   1868 C  CB   . ASN   A 1 254 ? 1.30700  -2.48000  32.45700 1.000 54.02132  ?  406 ASN   A CB   1 
ATOM   1869 C  CG   . ASN   A 1 254 ? 1.58100  -1.64500  33.70000 1.000 60.25803  ?  406 ASN   A CG   1 
ATOM   1870 O  OD1  . ASN   A 1 254 ? 1.08500  -0.52400  33.83200 1.000 61.44120  ?  406 ASN   A OD1  1 
ATOM   1871 N  ND2  . ASN   A 1 254 ? 2.37200  -2.19200  34.62000 1.000 60.46892  ?  406 ASN   A ND2  1 
ATOM   1872 N  N    . SER   A 1 255 ? -0.21800 -3.80000  30.03300 1.000 51.79881  ?  407 SER   A N    1 
ATOM   1873 C  CA   . SER   A 1 255 ? -0.28400 -4.31200  28.66500 1.000 56.21011  ?  407 SER   A CA   1 
ATOM   1874 C  C    . SER   A 1 255 ? -1.24500 -3.51300  27.79400 1.000 52.09971  ?  407 SER   A C    1 
ATOM   1875 O  O    . SER   A 1 255 ? -1.03600 -3.40800  26.58200 1.000 50.58089  ?  407 SER   A O    1 
ATOM   1876 C  CB   . SER   A 1 255 ? -0.70900 -5.78200  28.66600 1.000 61.48988  ?  407 SER   A CB   1 
ATOM   1877 O  OG   . SER   A 1 255 ? 0.40200  -6.64500  28.80200 1.000 64.96945  ?  407 SER   A OG   1 
ATOM   1878 N  N    A MET   A 1 256 ? -2.29600 -2.94400  28.38800 0.260 52.07821  ?  408 MET   A N    1 
ATOM   1879 N  N    C MET   A 1 256 ? -2.29800 -2.94800  28.38800 0.740 51.34145  ?  408 MET   A N    1 
ATOM   1880 C  CA   A MET   A 1 256 ? -3.29800 -2.22900  27.60300 0.260 53.21445  ?  408 MET   A CA   1 
ATOM   1881 C  CA   C MET   A 1 256 ? -3.29400 -2.23100  27.60100 0.740 53.61172  ?  408 MET   A CA   1 
ATOM   1882 C  C    A MET   A 1 256 ? -2.72700 -0.97900  26.94700 0.260 52.23147  ?  408 MET   A C    1 
ATOM   1883 C  C    C MET   A 1 256 ? -2.71800 -0.98800  26.94000 0.740 52.75542  ?  408 MET   A C    1 
ATOM   1884 O  O    A MET   A 1 256 ? -3.20200 -0.57000  25.88100 0.260 51.91315  ?  408 MET   A O    1 
ATOM   1885 O  O    C MET   A 1 256 ? -3.18600 -0.58700  25.86900 0.740 51.82360  ?  408 MET   A O    1 
ATOM   1886 C  CB   A MET   A 1 256 ? -4.48300 -1.85400  28.48600 0.260 55.63724  ?  408 MET   A CB   1 
ATOM   1887 C  CB   C MET   A 1 256 ? -4.47200 -1.84200  28.48400 0.740 55.19918  ?  408 MET   A CB   1 
ATOM   1888 C  CG   A MET   A 1 256 ? -5.61000 -2.86100  28.47600 0.260 57.67504  ?  408 MET   A CG   1 
ATOM   1889 C  CG   C MET   A 1 256 ? -5.63900 -2.78100  28.39700 0.740 57.64094  ?  408 MET   A CG   1 
ATOM   1890 S  SD   A MET   A 1 256 ? -6.88400 -2.42500  29.67000 0.260 61.71696  ?  408 MET   A SD   1 
ATOM   1891 S  SD   C MET   A 1 256 ? -6.96500 -2.20100  29.46100 0.740 61.85344  ?  408 MET   A SD   1 
ATOM   1892 C  CE   A MET   A 1 256 ? -6.69200 -0.64500  29.73500 0.260 61.53441  ?  408 MET   A CE   1 
ATOM   1893 C  CE   C MET   A 1 256 ? -6.61500 -3.12400  30.96000 0.740 60.93086  ?  408 MET   A CE   1 
ATOM   1894 N  N    . LYS   A 1 257 ? -1.72600 -0.35500  27.56500 1.000 49.54181  ?  409 LYS   A N    1 
ATOM   1895 C  CA   . LYS   A 1 257 ? -1.14800 0.86600   27.02300 1.000 49.66637  ?  409 LYS   A CA   1 
ATOM   1896 C  C    . LYS   A 1 257 ? -0.00500 0.59600   26.06000 1.000 43.52092  ?  409 LYS   A C    1 
ATOM   1897 O  O    . LYS   A 1 257 ? 0.51100  1.54100   25.45300 1.000 43.45734  ?  409 LYS   A O    1 
ATOM   1898 C  CB   . LYS   A 1 257 ? -0.68300 1.79300   28.15600 1.000 53.76253  ?  409 LYS   A CB   1 
ATOM   1899 C  CG   . LYS   A 1 257 ? -1.71000 1.95200   29.27300 1.000 62.17045  ?  409 LYS   A CG   1 
ATOM   1900 C  CD   . LYS   A 1 257 ? -2.97200 2.68100   28.77300 1.000 71.35759  ?  409 LYS   A CD   1 
ATOM   1901 C  CE   . LYS   A 1 257 ? -3.11800 4.09900   29.33600 1.000 78.17313  ?  409 LYS   A CE   1 
ATOM   1902 N  NZ   . LYS   A 1 257 ? -3.69300 5.06200   28.33700 1.000 80.00042  ?  409 LYS   A NZ   1 
ATOM   1903 N  N    . LEU   A 1 258 ? 0.39000  -0.66400  25.89500 1.000 38.58314  ?  410 LEU   A N    1 
ATOM   1904 C  CA   . LEU   A 1 258 ? 1.40100  -1.01600  24.91500 1.000 43.89188  ?  410 LEU   A CA   1 
ATOM   1905 C  C    . LEU   A 1 258 ? 0.77800  -1.07000  23.52400 1.000 43.60085  ?  410 LEU   A C    1 
ATOM   1906 O  O    . LEU   A 1 258 ? -0.44100 -0.98400  23.35500 1.000 40.68926  ?  410 LEU   A O    1 
ATOM   1907 C  CB   . LEU   A 1 258 ? 2.04600  -2.35700  25.26800 1.000 44.06292  ?  410 LEU   A CB   1 
ATOM   1908 C  CG   . LEU   A 1 258 ? 2.75300  -2.44000  26.62400 1.000 41.51816  ?  410 LEU   A CG   1 
ATOM   1909 C  CD1  . LEU   A 1 258 ? 3.44500  -3.78500  26.78600 1.000 41.18878  ?  410 LEU   A CD1  1 
ATOM   1910 C  CD2  . LEU   A 1 258 ? 3.74500  -1.30500  26.76600 1.000 38.41875  ?  410 LEU   A CD2  1 
ATOM   1911 N  N    . THR   A 1 259 ? 1.62700  -1.21100  22.51600 1.000 43.69559  ?  411 THR   A N    1 
ATOM   1912 C  CA   . THR   A 1 259 ? 1.10200  -1.36300  21.17100 1.000 42.32937  ?  411 THR   A CA   1 
ATOM   1913 C  C    . THR   A 1 259 ? 1.12800  -2.82800  20.75600 1.000 41.51997  ?  411 THR   A C    1 
ATOM   1914 O  O    . THR   A 1 259 ? 1.80600  -3.65000  21.37800 1.000 42.10321  ?  411 THR   A O    1 
ATOM   1915 C  CB   . THR   A 1 259 ? 1.90400  -0.51300  20.17900 1.000 43.60335  ?  411 THR   A CB   1 
ATOM   1916 O  OG1  . THR   A 1 259 ? 3.16700  -1.13400  19.92300 1.000 45.97850  ?  411 THR   A OG1  1 
ATOM   1917 C  CG2  . THR   A 1 259 ? 2.12200  0.89200   20.73200 1.000 43.90906  ?  411 THR   A CG2  1 
ATOM   1918 N  N    . PRO   A 1 260 ? 0.35600  -3.20900  19.73100 1.000 42.71726  ?  412 PRO   A N    1 
ATOM   1919 C  CA   . PRO   A 1 260 ? 0.42400  -4.60400  19.25800 1.000 41.17447  ?  412 PRO   A CA   1 
ATOM   1920 C  C    . PRO   A 1 260 ? 1.80800  -5.01400  18.77300 1.000 39.53000  ?  412 PRO   A C    1 
ATOM   1921 O  O    . PRO   A 1 260 ? 2.21500  -6.16600  18.98100 1.000 41.66487  ?  412 PRO   A O    1 
ATOM   1922 C  CB   . PRO   A 1 260 ? -0.61600 -4.63800  18.12600 1.000 44.06877  ?  412 PRO   A CB   1 
ATOM   1923 C  CG   . PRO   A 1 260 ? -1.56700 -3.53700  18.46400 1.000 48.27583  ?  412 PRO   A CG   1 
ATOM   1924 C  CD   . PRO   A 1 260 ? -0.73600 -2.45600  19.08700 1.000 43.22506  ?  412 PRO   A CD   1 
ATOM   1925 N  N    . LEU   A 1 261 ? 2.54700  -4.10900  18.12900 1.000 36.13573  ?  413 LEU   A N    1 
ATOM   1926 C  CA   . LEU   A 1 261 ? 3.88900  -4.45600  17.66600 1.000 38.92932  ?  413 LEU   A CA   1 
ATOM   1927 C  C    . LEU   A 1 261 ? 4.82800  -4.70200  18.84300 1.000 38.51841  ?  413 LEU   A C    1 
ATOM   1928 O  O    . LEU   A 1 261 ? 5.55000  -5.70500  18.87500 1.000 39.24828  ?  413 LEU   A O    1 
ATOM   1929 C  CB   . LEU   A 1 261 ? 4.43800  -3.35600  16.75600 1.000 41.38240  ?  413 LEU   A CB   1 
ATOM   1930 C  CG   . LEU   A 1 261 ? 5.81700  -3.63200  16.14100 1.000 42.41661  ?  413 LEU   A CG   1 
ATOM   1931 C  CD1  . LEU   A 1 261 ? 5.77600  -4.87000  15.24800 1.000 43.99448  ?  413 LEU   A CD1  1 
ATOM   1932 C  CD2  . LEU   A 1 261 ? 6.32900  -2.42700  15.36500 1.000 35.65912  ?  413 LEU   A CD2  1 
ATOM   1933 N  N    . VAL   A 1 262 ? 4.81700  -3.80100  19.82900 1.000 39.43687  ?  414 VAL   A N    1 
ATOM   1934 C  CA   . VAL   A 1 262 ? 5.64600  -3.98100  21.02100 1.000 38.02322  ?  414 VAL   A CA   1 
ATOM   1935 C  C    . VAL   A 1 262 ? 5.35200  -5.32300  21.67900 1.000 39.96764  ?  414 VAL   A C    1 
ATOM   1936 O  O    . VAL   A 1 262 ? 6.26800  -6.06300  22.05500 1.000 39.93208  ?  414 VAL   A O    1 
ATOM   1937 C  CB   . VAL   A 1 262 ? 5.43100  -2.81200  22.00100 1.000 40.26224  ?  414 VAL   A CB   1 
ATOM   1938 C  CG1  . VAL   A 1 262 ? 6.09600  -3.10600  23.34200 1.000 37.61789  ?  414 VAL   A CG1  1 
ATOM   1939 C  CG2  . VAL   A 1 262 ? 5.95200  -1.50800  21.40600 1.000 38.60106  ?  414 VAL   A CG2  1 
ATOM   1940 N  N    . LEU   A 1 263 ? 4.07000  -5.66700  21.81700 1.000 40.60890  ?  415 LEU   A N    1 
ATOM   1941 C  CA   . LEU   A 1 263 ? 3.70700  -6.95000  22.40900 1.000 43.16472  ?  415 LEU   A CA   1 
ATOM   1942 C  C    . LEU   A 1 263 ? 4.18500  -8.11700  21.56000 1.000 43.49089  ?  415 LEU   A C    1 
ATOM   1943 O  O    . LEU   A 1 263 ? 4.50400  -9.18500  22.09500 1.000 43.29169  ?  415 LEU   A O    1 
ATOM   1944 C  CB   . LEU   A 1 263 ? 2.19100  -7.03300  22.59400 1.000 47.17421  ?  415 LEU   A CB   1 
ATOM   1945 C  CG   . LEU   A 1 263 ? 1.59600  -6.23500  23.75100 1.000 47.75662  ?  415 LEU   A CG   1 
ATOM   1946 C  CD1  . LEU   A 1 263 ? 0.08100  -6.18500  23.62500 1.000 47.11598  ?  415 LEU   A CD1  1 
ATOM   1947 C  CD2  . LEU   A 1 263 ? 2.01300  -6.85200  25.07500 1.000 47.02077  ?  415 LEU   A CD2  1 
ATOM   1948 N  N    . GLU   A 1 264 ? 4.21800  -7.94400  20.23900 1.000 47.95452  ?  416 GLU   A N    1 
ATOM   1949 C  CA   . GLU   A 1 264 ? 4.66700  -9.02100  19.36600 1.000 47.42377  ?  416 GLU   A CA   1 
ATOM   1950 C  C    . GLU   A 1 264 ? 6.17900  -9.19000  19.42300 1.000 46.63892  ?  416 GLU   A C    1 
ATOM   1951 O  O    . GLU   A 1 264 ? 6.68400  -10.31900 19.43400 1.000 45.96449  ?  416 GLU   A O    1 
ATOM   1952 C  CB   . GLU   A 1 264 ? 4.22000  -8.74900  17.92900 1.000 46.46054  ?  416 GLU   A CB   1 
ATOM   1953 C  CG   . GLU   A 1 264 ? 4.36900  -9.94400  17.00900 1.000 48.22236  ?  416 GLU   A CG   1 
ATOM   1954 C  CD   . GLU   A 1 264 ? 4.18400  -9.58400  15.54800 1.000 51.94527  ?  416 GLU   A CD   1 
ATOM   1955 O  OE1  . GLU   A 1 264 ? 5.19900  -9.32200  14.86800 1.000 50.70923  ?  416 GLU   A OE1  1 
ATOM   1956 O  OE2  . GLU   A 1 264 ? 3.02900  -9.57600  15.07400 1.000 51.11422  ?  416 GLU   A OE2  1 
ATOM   1957 N  N    . VAL   A 1 265 ? 6.91700  -8.08500  19.46100 1.000 44.01786  ?  417 VAL   A N    1 
ATOM   1958 C  CA   . VAL   A 1 265 ? 8.37000  -8.17100  19.38600 1.000 42.26012  ?  417 VAL   A CA   1 
ATOM   1959 C  C    . VAL   A 1 265 ? 8.97100  -8.42300  20.76200 1.000 45.04564  ?  417 VAL   A C    1 
ATOM   1960 O  O    . VAL   A 1 265 ? 9.76400  -9.35100  20.94700 1.000 47.61163  ?  417 VAL   A O    1 
ATOM   1961 C  CB   . VAL   A 1 265 ? 8.94300  -6.89900  18.74200 1.000 40.79834  ?  417 VAL   A CB   1 
ATOM   1962 C  CG1  . VAL   A 1 265 ? 10.47400 -6.92600  18.77200 1.000 44.33301  ?  417 VAL   A CG1  1 
ATOM   1963 C  CG2  . VAL   A 1 265 ? 8.43700  -6.77200  17.31900 1.000 33.94433  ?  417 VAL   A CG2  1 
ATOM   1964 N  N    . PHE   A 1 266 ? 8.59400  -7.61300  21.75200 1.000 43.96724  ?  418 PHE   A N    1 
ATOM   1965 C  CA   . PHE   A 1 266 ? 9.16500  -7.74600  23.09000 1.000 45.65004  ?  418 PHE   A CA   1 
ATOM   1966 C  C    . PHE   A 1 266 ? 8.57100  -8.91800  23.86100 1.000 47.35451  ?  418 PHE   A C    1 
ATOM   1967 O  O    . PHE   A 1 266 ? 9.22600  -9.45000  24.76500 1.000 44.66497  ?  418 PHE   A O    1 
ATOM   1968 C  CB   . PHE   A 1 266 ? 8.97000  -6.45100  23.88800 1.000 40.37936  ?  418 PHE   A CB   1 
ATOM   1969 C  CG   . PHE   A 1 266 ? 9.84300  -5.31300  23.43300 1.000 37.34123  ?  418 PHE   A CG   1 
ATOM   1970 C  CD1  . PHE   A 1 266 ? 10.78100 -5.49300  22.42800 1.000 34.13369  ?  418 PHE   A CD1  1 
ATOM   1971 C  CD2  . PHE   A 1 266 ? 9.74000  -4.06800  24.02800 1.000 35.61804  ?  418 PHE   A CD2  1 
ATOM   1972 C  CE1  . PHE   A 1 266 ? 11.58800 -4.44700  22.01600 1.000 37.43544  ?  418 PHE   A CE1  1 
ATOM   1973 C  CE2  . PHE   A 1 266 ? 10.54300 -3.01900  23.62100 1.000 35.44844  ?  418 PHE   A CE2  1 
ATOM   1974 C  CZ   . PHE   A 1 266 ? 11.47500 -3.21000  22.61600 1.000 36.33951  ?  418 PHE   A CZ   1 
ATOM   1975 N  N    . GLY   A 1 267 ? 7.34500  -9.32900  23.53500 1.000 47.50104  ?  419 GLY   A N    1 
ATOM   1976 C  CA   . GLY   A 1 267 ? 6.73000  -10.46500 24.19300 1.000 52.70535  ?  419 GLY   A CA   1 
ATOM   1977 C  C    . GLY   A 1 267 ? 5.38200  -10.15200 24.81300 1.000 65.00502  ?  419 GLY   A C    1 
ATOM   1978 O  O    . GLY   A 1 267 ? 5.03800  -8.98100  25.00600 1.000 60.81223  ?  419 GLY   A O    1 
ATOM   1979 N  N    . ASN   A 1 268 ? 4.61700  -11.19600 25.13500 1.000 77.64908  ?  420 ASN   A N    1 
ATOM   1980 C  CA   . ASN   A 1 268 ? 3.26000  -11.05800 25.66900 1.000 83.26119  ?  420 ASN   A CA   1 
ATOM   1981 C  C    . ASN   A 1 268 ? 3.21300  -10.21500 26.94100 1.000 89.64512  ?  420 ASN   A C    1 
ATOM   1982 O  O    . ASN   A 1 268 ? 2.13700  -9.95600  27.48400 1.000 95.23702  ?  420 ASN   A O    1 
ATOM   1983 C  CB   . ASN   A 1 268 ? 2.65300  -12.43900 25.94900 1.000 84.89369  ?  420 ASN   A CB   1 
ATOM   1984 C  CG   . ASN   A 1 268 ? 3.14000  -13.04000 27.25900 1.000 87.34672  ?  420 ASN   A CG   1 
ATOM   1985 O  OD1  . ASN   A 1 268 ? 4.21600  -13.63300 27.32000 1.000 91.75093  ?  420 ASN   A OD1  1 
ATOM   1986 N  ND2  . ASN   A 1 268 ? 2.34100  -12.89800 28.31200 1.000 86.69492  ?  420 ASN   A ND2  1 
ATOM   1987 N  N    . LYS   B 2 1   ? 2.99400  -17.27800 10.86700 1.000 141.98700 ?  625 LYS   C N    1 
ATOM   1988 C  CA   . LYS   B 2 1   ? 2.81800  -18.02100 12.10200 1.000 143.44005 ?  625 LYS   C CA   1 
ATOM   1989 C  C    . LYS   B 2 1   ? 2.40200  -17.15300 13.29000 1.000 137.12704 ?  625 LYS   C C    1 
ATOM   1990 O  O    . LYS   B 2 1   ? 1.23200  -16.80100 13.42700 1.000 140.00905 ?  625 LYS   C O    1 
ATOM   1991 C  CB   . LYS   B 2 1   ? 4.11200  -18.73700 12.44000 1.000 146.50905 ?  625 LYS   C CB   1 
ATOM   1992 C  CG   . LYS   B 2 1   ? 4.04400  -19.53800 13.69900 1.000 151.83322 ?  625 LYS   C CG   1 
ATOM   1993 C  CD   . LYS   B 2 1   ? 3.79500  -20.94300 13.28600 1.000 158.80272 ?  625 LYS   C CD   1 
ATOM   1994 C  CE   . LYS   B 2 1   ? 3.68600  -21.88300 14.45200 1.000 163.95836 ?  625 LYS   C CE   1 
ATOM   1995 N  NZ   . LYS   B 2 1   ? 2.62800  -22.86600 14.20600 1.000 170.33966 ?  625 LYS   C NZ   1 
ATOM   1996 N  N    . ASN   B 2 2   ? 3.36700  -16.79400 14.13900 1.000 125.73281 ?  626 ASN   C N    1 
ATOM   1997 C  CA   . ASN   B 2 2   ? 3.06900  -16.09900 15.38400 1.000 116.22167 ?  626 ASN   C CA   1 
ATOM   1998 C  C    . ASN   B 2 2   ? 3.49300  -14.63800 15.37600 1.000 101.72112 ?  626 ASN   C C    1 
ATOM   1999 O  O    . ASN   B 2 2   ? 3.04500  -13.87400 16.23100 1.000 102.21455 ?  626 ASN   C O    1 
ATOM   2000 C  CB   . ASN   B 2 2   ? 3.73100  -16.80600 16.57900 1.000 119.56885 ?  626 ASN   C CB   1 
ATOM   2001 C  CG   . ASN   B 2 2   ? 5.15300  -17.23400 16.30200 1.000 120.27793 ?  626 ASN   C CG   1 
ATOM   2002 O  OD1  . ASN   B 2 2   ? 5.56200  -17.36600 15.15200 1.000 120.12267 ?  626 ASN   C OD1  1 
ATOM   2003 N  ND2  . ASN   B 2 2   ? 5.91800  -17.45800 17.36600 1.000 121.47180 ?  626 ASN   C ND2  1 
ATOM   2004 N  N    . HIS   B 2 3   ? 4.32600  -14.21000 14.43200 1.000 88.25286  ?  627 HIS   C N    1 
ATOM   2005 C  CA   . HIS   B 2 3   ? 4.75800  -12.81600 14.32200 1.000 75.81487  ?  627 HIS   C CA   1 
ATOM   2006 C  C    . HIS   B 2 3   ? 4.28700  -12.24600 12.98500 1.000 68.92090  ?  627 HIS   C C    1 
ATOM   2007 O  O    . HIS   B 2 3   ? 5.10100  -11.95700 12.09300 1.000 66.45384  ?  627 HIS   C O    1 
ATOM   2008 C  CB   . HIS   B 2 3   ? 6.27500  -12.68400 14.46000 1.000 70.47303  ?  627 HIS   C CB   1 
ATOM   2009 C  CG   . HIS   B 2 3   ? 6.84000  -13.39300 15.64900 1.000 68.41744  ?  627 HIS   C CG   1 
ATOM   2010 N  ND1  . HIS   B 2 3   ? 7.28300  -14.69700 15.59600 1.000 70.79175  ?  627 HIS   C ND1  1 
ATOM   2011 C  CD2  . HIS   B 2 3   ? 7.01600  -12.98600 16.92800 1.000 67.35741  ?  627 HIS   C CD2  1 
ATOM   2012 C  CE1  . HIS   B 2 3   ? 7.71700  -15.06000 16.79000 1.000 66.23457  ?  627 HIS   C CE1  1 
ATOM   2013 N  NE2  . HIS   B 2 3   ? 7.56200  -14.04200 17.61600 1.000 70.18337  ?  627 HIS   C NE2  1 
ATOM   2014 N  N    . PRO   B 2 4   ? 2.97300  -12.05000 12.82200 1.000 68.99404  ?  628 PRO   C N    1 
ATOM   2015 C  CA   . PRO   B 2 4   ? 2.46700  -11.60300 11.51400 1.000 67.08823  ?  628 PRO   C CA   1 
ATOM   2016 C  C    . PRO   B 2 4   ? 2.80700  -10.16100 11.18900 1.000 61.96803  ?  628 PRO   C C    1 
ATOM   2017 O  O    . PRO   B 2 4   ? 2.95200  -9.82300  10.00800 1.000 59.81975  ?  628 PRO   C O    1 
ATOM   2018 C  CB   . PRO   B 2 4   ? 0.95100  -11.80600 11.64200 1.000 70.03403  ?  628 PRO   C CB   1 
ATOM   2019 C  CG   . PRO   B 2 4   ? 0.68900  -11.62300 13.09600 1.000 70.42381  ?  628 PRO   C CG   1 
ATOM   2020 C  CD   . PRO   B 2 4   ? 1.88300  -12.19400 13.80700 1.000 70.81082  ?  628 PRO   C CD   1 
ATOM   2021 N  N    . MET   B 2 5   ? 2.92900  -9.29200  12.19300 1.000 62.76603  ?  629 MET   C N    1 
ATOM   2022 C  CA   . MET   B 2 5   ? 3.25200  -7.89900  11.91400 1.000 57.92247  ?  629 MET   C CA   1 
ATOM   2023 C  C    . MET   B 2 5   ? 4.74200  -7.70000  11.68400 1.000 58.66675  ?  629 MET   C C    1 
ATOM   2024 O  O    . MET   B 2 5   ? 5.13000  -6.84700  10.87600 1.000 54.14689  ?  629 MET   C O    1 
ATOM   2025 C  CB   . MET   B 2 5   ? 2.76500  -7.01000  13.05300 1.000 56.76413  ?  629 MET   C CB   1 
ATOM   2026 C  CG   . MET   B 2 5   ? 1.27600  -7.14700  13.31700 1.000 65.26072  ?  629 MET   C CG   1 
ATOM   2027 S  SD   . MET   B 2 5   ? 0.75800  -6.09800  14.67900 1.000 73.06518  ?  629 MET   C SD   1 
ATOM   2028 C  CE   . MET   B 2 5   ? 1.48000  -6.98800  16.04600 1.000 68.56340  ?  629 MET   C CE   1 
ATOM   2029 N  N    . LEU   B 2 6   ? 5.58500  -8.46200  12.38800 1.000 53.26408  ?  630 LEU   C N    1 
ATOM   2030 C  CA   . LEU   B 2 6   ? 7.00800  -8.47700  12.07000 1.000 52.14923  ?  630 LEU   C CA   1 
ATOM   2031 C  C    . LEU   B 2 6   ? 7.23800  -9.01300  10.66200 1.000 58.49079  ?  630 LEU   C C    1 
ATOM   2032 O  O    . LEU   B 2 6   ? 7.96000  -8.40600  9.86300  1.000 59.18294  ?  630 LEU   C O    1 
ATOM   2033 C  CB   . LEU   B 2 6   ? 7.76600  -9.31800  13.09900 1.000 52.74901  ?  630 LEU   C CB   1 
ATOM   2034 C  CG   . LEU   B 2 6   ? 8.84800  -8.62700  13.93000 1.000 60.61243  ?  630 LEU   C CG   1 
ATOM   2035 C  CD1  . LEU   B 2 6   ? 9.62200  -9.64700  14.74900 1.000 58.11725  ?  630 LEU   C CD1  1 
ATOM   2036 C  CD2  . LEU   B 2 6   ? 9.79100  -7.84700  13.02700 1.000 55.08781  ?  630 LEU   C CD2  1 
ATOM   2037 N  N    . MET   B 2 7   ? 6.61200  -10.14900 10.33600 1.000 61.52209  ?  631 MET   C N    1 
ATOM   2038 C  CA   . MET   B 2 7   ? 6.77900  -10.74000 9.01200  1.000 65.01850  ?  631 MET   C CA   1 
ATOM   2039 C  C    . MET   B 2 7   ? 6.30400  -9.79700  7.91400  1.000 61.86660  ?  631 MET   C C    1 
ATOM   2040 O  O    . MET   B 2 7   ? 6.93400  -9.70100  6.85500  1.000 67.53763  ?  631 MET   C O    1 
ATOM   2041 C  CB   . MET   B 2 7   ? 6.02800  -12.06800 8.93400  1.000 71.45261  ?  631 MET   C CB   1 
ATOM   2042 C  CG   . MET   B 2 7   ? 6.86600  -13.22800 8.43000  1.000 79.12638  ?  631 MET   C CG   1 
ATOM   2043 S  SD   . MET   B 2 7   ? 5.92300  -14.76300 8.40000  1.000 91.90674  ?  631 MET   C SD   1 
ATOM   2044 C  CE   . MET   B 2 7   ? 5.81500  -15.13200 10.15000 1.000 91.67751  ?  631 MET   C CE   1 
ATOM   2045 N  N    . ASN   B 2 8   ? 5.19700  -9.09000  8.14700  1.000 56.29163  ?  632 ASN   C N    1 
ATOM   2046 C  CA   . ASN   B 2 8   ? 4.68500  -8.16900  7.13600  1.000 59.56689  ?  632 ASN   C CA   1 
ATOM   2047 C  C    . ASN   B 2 8   ? 5.60800  -6.96800  6.95900  1.000 61.31693  ?  632 ASN   C C    1 
ATOM   2048 O  O    . ASN   B 2 8   ? 5.78200  -6.46900  5.83900  1.000 54.71101  ?  632 ASN   C O    1 
ATOM   2049 C  CB   . ASN   B 2 8   ? 3.27300  -7.71400  7.50700  1.000 61.47078  ?  632 ASN   C CB   1 
ATOM   2050 C  CG   . ASN   B 2 8   ? 2.75300  -6.63300  6.58700  1.000 61.55057  ?  632 ASN   C CG   1 
ATOM   2051 O  OD1  . ASN   B 2 8   ? 2.75400  -5.45000  6.93500  1.000 61.22552  ?  632 ASN   C OD1  1 
ATOM   2052 N  ND2  . ASN   B 2 8   ? 2.31800  -7.03100  5.39700  1.000 62.96605  ?  632 ASN   C ND2  1 
ATOM   2053 N  N    . LEU   B 2 9   ? 6.20300  -6.48700  8.05300  1.000 52.42931  ?  633 LEU   C N    1 
ATOM   2054 C  CA   . LEU   B 2 9   ? 7.16400  -5.39400  7.96400  1.000 59.32285  ?  633 LEU   C CA   1 
ATOM   2055 C  C    . LEU   B 2 9   ? 8.47500  -5.82800  7.32100  1.000 59.88676  ?  633 LEU   C C    1 
ATOM   2056 O  O    . LEU   B 2 9   ? 9.20100  -4.97700  6.79400  1.000 52.06370  ?  633 LEU   C O    1 
ATOM   2057 C  CB   . LEU   B 2 9   ? 7.42900  -4.81500  9.35400  1.000 55.02381  ?  633 LEU   C CB   1 
ATOM   2058 C  CG   . LEU   B 2 9   ? 6.28700  -3.97000  9.91600  1.000 56.22029  ?  633 LEU   C CG   1 
ATOM   2059 C  CD1  . LEU   B 2 9   ? 6.61300  -3.46500  11.32000 1.000 55.24196  ?  633 LEU   C CD1  1 
ATOM   2060 C  CD2  . LEU   B 2 9   ? 5.97700  -2.81600  8.97200  1.000 57.47765  ?  633 LEU   C CD2  1 
ATOM   2061 N  N    . LEU   B 2 10  ? 8.79200  -7.12100  7.35500  1.000 59.52603  ?  634 LEU   C N    1 
ATOM   2062 C  CA   . LEU   B 2 10  ? 9.94500  -7.66400  6.64800  1.000 64.14043  ?  634 LEU   C CA   1 
ATOM   2063 C  C    . LEU   B 2 10  ? 9.64800  -7.96300  5.18100  1.000 72.67507  ?  634 LEU   C C    1 
ATOM   2064 O  O    . LEU   B 2 10  ? 10.50400 -8.54300  4.50100  1.000 77.84076  ?  634 LEU   C O    1 
ATOM   2065 C  CB   . LEU   B 2 10  ? 10.44000 -8.93500  7.34400  1.000 58.30645  ?  634 LEU   C CB   1 
ATOM   2066 C  CG   . LEU   B 2 10  ? 11.13700 -8.74700  8.69000  1.000 56.17280  ?  634 LEU   C CG   1 
ATOM   2067 C  CD1  . LEU   B 2 10  ? 11.40200 -10.09800 9.33600  1.000 57.57221  ?  634 LEU   C CD1  1 
ATOM   2068 C  CD2  . LEU   B 2 10  ? 12.42900 -7.95700  8.51900  1.000 59.36492  ?  634 LEU   C CD2  1 
ATOM   2069 N  N    . LYS   B 2 11  ? 8.46700  -7.58700  4.69300  1.000 69.23866  ?  635 LYS   C N    1 
ATOM   2070 C  CA   . LYS   B 2 11  ? 8.08000  -7.78100  3.29900  1.000 74.10553  ?  635 LYS   C CA   1 
ATOM   2071 C  C    . LYS   B 2 11  ? 8.14900  -9.25200  2.90400  1.000 81.37417  ?  635 LYS   C C    1 
ATOM   2072 O  O    . LYS   B 2 11  ? 7.76600  -10.12800 3.67900  1.000 84.03709  ?  635 LYS   C O    1 
ATOM   2073 C  CB   . LYS   B 2 11  ? 8.96100  -6.94200  2.36800  1.000 76.07295  ?  635 LYS   C CB   1 
ATOM   2074 C  CG   . LYS   B 2 11  ? 8.54500  -7.00900  0.90500  1.000 86.67799  ?  635 LYS   C CG   1 
ATOM   2075 C  CD   . LYS   B 2 11  ? 8.68800  -5.66000  0.21900  1.000 88.94310  ?  635 LYS   C CD   1 
ATOM   2076 C  CE   . LYS   B 2 11  ? 7.78900  -5.56900  -1.00400 1.000 91.97314  ?  635 LYS   C CE   1 
ATOM   2077 N  NZ   . LYS   B 2 11  ? 6.64100  -6.51800  -0.92000 1.000 94.09391  ?  635 LYS   C NZ   1 
HETATM 2078 C  C10  A A1L76 C 3 .   ? 15.92200 5.50300   26.31100 0.520 47.21779  ?  501 A1L76 A C10  1 
HETATM 2079 C  C10  B A1L76 C 3 .   ? 15.93400 5.49600   26.36300 0.460 47.02567  ?  501 A1L76 A C10  1 
HETATM 2080 C  C13  A A1L76 C 3 .   ? 12.53400 2.12800   25.88800 0.520 39.40126  ?  501 A1L76 A C13  1 
HETATM 2081 C  C13  B A1L76 C 3 .   ? 12.53500 2.12800   25.89500 0.460 39.63348  ?  501 A1L76 A C13  1 
HETATM 2082 C  C15  A A1L76 C 3 .   ? 11.17300 3.49700   27.23800 0.520 43.33643  ?  501 A1L76 A C15  1 
HETATM 2083 C  C15  B A1L76 C 3 .   ? 11.15600 3.47900   27.25500 0.460 43.19484  ?  501 A1L76 A C15  1 
HETATM 2084 C  C20  A A1L76 C 3 .   ? 8.51700  -0.56800  26.58100 0.520 39.18678  ?  501 A1L76 A C20  1 
HETATM 2085 C  C20  B A1L76 C 3 .   ? 8.51200  -0.56800  26.57700 0.460 38.93106  ?  501 A1L76 A C20  1 
HETATM 2086 C  C21  A A1L76 C 3 .   ? 7.48500  0.33300   25.94000 0.520 39.09531  ?  501 A1L76 A C21  1 
HETATM 2087 C  C21  B A1L76 C 3 .   ? 7.48000  0.34100   25.94400 0.460 39.55834  ?  501 A1L76 A C21  1 
HETATM 2088 C  C22  A A1L76 C 3 .   ? 7.72200  0.03900   28.84900 0.520 41.38565  ?  501 A1L76 A C22  1 
HETATM 2089 C  C22  B A1L76 C 3 .   ? 7.71800  0.03400   28.85100 0.460 41.13169  ?  501 A1L76 A C22  1 
HETATM 2090 C  C26  A A1L76 C 3 .   ? 14.81000 6.94800   17.40900 0.520 50.44976  ?  501 A1L76 A C26  1 
HETATM 2091 C  C26  B A1L76 C 3 .   ? 15.06200 8.03800   18.09000 0.460 50.89249  ?  501 A1L76 A C26  1 
HETATM 2092 C  C28  A A1L76 C 3 .   ? 13.64800 7.81500   16.99900 0.520 50.30728  ?  501 A1L76 A C28  1 
HETATM 2093 C  C28  B A1L76 C 3 .   ? 13.72300 7.84000   17.41300 0.460 50.05887  ?  501 A1L76 A C28  1 
HETATM 2094 C  C01  A A1L76 C 3 .   ? 14.70500 7.85900   22.11400 0.520 50.09295  ?  501 A1L76 A C01  1 
HETATM 2095 C  C01  B A1L76 C 3 .   ? 14.66800 7.73000   22.16600 0.460 49.79864  ?  501 A1L76 A C01  1 
HETATM 2096 C  C02  A A1L76 C 3 .   ? 14.24300 7.02300   21.13600 0.520 49.29543  ?  501 A1L76 A C02  1 
HETATM 2097 C  C02  B A1L76 C 3 .   ? 14.17600 6.80900   21.28700 0.460 49.28543  ?  501 A1L76 A C02  1 
HETATM 2098 C  C03  A A1L76 C 3 .   ? 13.74200 5.80600   21.54600 0.520 48.84450  ?  501 A1L76 A C03  1 
HETATM 2099 C  C03  B A1L76 C 3 .   ? 13.68800 5.62200   21.73200 0.460 48.83043  ?  501 A1L76 A C03  1 
HETATM 2100 C  C04  A A1L76 C 3 .   ? 13.71600 5.44000   22.87100 0.520 48.86270  ?  501 A1L76 A C04  1 
HETATM 2101 C  C04  B A1L76 C 3 .   ? 13.68500 5.32600   23.06000 0.460 48.85047  ?  501 A1L76 A C04  1 
HETATM 2102 C  C05  A A1L76 C 3 .   ? 14.19400 6.28100   23.83600 0.520 48.71015  ?  501 A1L76 A C05  1 
HETATM 2103 C  C05  B A1L76 C 3 .   ? 14.18100 6.23700   23.94500 0.460 48.81997  ?  501 A1L76 A C05  1 
HETATM 2104 C  C06  A A1L76 C 3 .   ? 14.67600 7.48800   23.43600 0.520 49.74334  ?  501 A1L76 A C06  1 
HETATM 2105 C  C06  B A1L76 C 3 .   ? 14.66300 7.43200   23.50000 0.460 49.52508  ?  501 A1L76 A C06  1 
HETATM 2106 C  C09  A A1L76 C 3 .   ? 13.06300 4.43000   26.11000 0.520 46.02849  ?  501 A1L76 A C09  1 
HETATM 2107 C  C09  B A1L76 C 3 .   ? 13.05900 4.42700   26.16600 0.460 46.12706  ?  501 A1L76 A C09  1 
HETATM 2108 C  C11  A A1L76 C 3 .   ? 13.62300 7.46500   26.46700 0.520 51.63454  ?  501 A1L76 A C11  1 
HETATM 2109 C  C11  B A1L76 C 3 .   ? 13.62500 7.48000   26.55900 0.460 51.51914  ?  501 A1L76 A C11  1 
HETATM 2110 C  C12  A A1L76 C 3 .   ? 13.33800 3.19300   25.59300 0.520 42.12547  ?  501 A1L76 A C12  1 
HETATM 2111 C  C12  B A1L76 C 3 .   ? 13.34300 3.20000   25.62600 0.460 41.94671  ?  501 A1L76 A C12  1 
HETATM 2112 C  C14  A A1L76 C 3 .   ? 11.45100 2.27100   26.70800 0.520 40.56444  ?  501 A1L76 A C14  1 
HETATM 2113 C  C14  B A1L76 C 3 .   ? 11.44300 2.26100   26.70700 0.460 40.65069  ?  501 A1L76 A C14  1 
HETATM 2114 C  C16  A A1L76 C 3 .   ? 11.97400 4.57700   26.94200 0.520 45.71907  ?  501 A1L76 A C16  1 
HETATM 2115 C  C16  B A1L76 C 3 .   ? 11.96000 4.56300   26.98600 0.460 45.48929  ?  501 A1L76 A C16  1 
HETATM 2116 C  C18  A A1L76 C 3 .   ? 9.63700  1.26900   27.86200 0.520 39.63702  ?  501 A1L76 A C18  1 
HETATM 2117 C  C18  B A1L76 C 3 .   ? 9.63700  1.26000   27.86400 0.460 39.47640  ?  501 A1L76 A C18  1 
HETATM 2118 C  C19  A A1L76 C 3 .   ? 8.93700  -0.06900  27.94800 0.520 39.44900  ?  501 A1L76 A C19  1 
HETATM 2119 C  C19  B A1L76 C 3 .   ? 8.93400  -0.07700  27.94800 0.460 39.48765  ?  501 A1L76 A C19  1 
HETATM 2120 C  C23  A A1L76 C 3 .   ? 7.16800  -1.33800  29.15300 0.520 39.96439  ?  501 A1L76 A C23  1 
HETATM 2121 C  C23  B A1L76 C 3 .   ? 7.16600  -1.34500  29.15500 0.460 40.53259  ?  501 A1L76 A C23  1 
HETATM 2122 C  C25  A A1L76 C 3 .   ? 14.76500 6.52000   18.88600 0.520 49.74323  ?  501 A1L76 A C25  1 
HETATM 2123 C  C25  B A1L76 C 3 .   ? 14.83500 8.18500   19.57300 0.460 50.59415  ?  501 A1L76 A C25  1 
HETATM 2124 C  C29  A A1L76 C 3 .   ? 14.05400 8.49400   15.70500 0.520 50.92535  ?  501 A1L76 A C29  1 
HETATM 2125 C  C29  B A1L76 C 3 .   ? 13.87700 8.15100   15.94100 0.460 50.73305  ?  501 A1L76 A C29  1 
HETATM 2126 C  C30  A A1L76 C 3 .   ? 13.61500 7.75600   14.44700 0.520 50.62085  ?  501 A1L76 A C30  1 
HETATM 2127 C  C30  B A1L76 C 3 .   ? 14.09300 6.82200   15.25200 0.460 50.28047  ?  501 A1L76 A C30  1 
HETATM 2128 C  C33  A A1L76 C 3 .   ? 13.20300 4.81000   20.55300 0.520 49.03631  ?  501 A1L76 A C33  1 
HETATM 2129 C  C33  B A1L76 C 3 .   ? 13.15100 4.62800   20.73400 0.460 49.22644  ?  501 A1L76 A C33  1 
HETATM 2130 C  C34  A A1L76 C 3 .   ? 12.84100 0.77700   25.30100 0.520 37.29544  ?  501 A1L76 A C34  1 
HETATM 2131 C  C34  B A1L76 C 3 .   ? 12.84700 0.78300   25.29100 0.460 38.28268  ?  501 A1L76 A C34  1 
HETATM 2132 C  C35  A A1L76 C 3 .   ? 13.22500 7.25200   27.90200 0.520 53.25098  ?  501 A1L76 A C35  1 
HETATM 2133 C  C35  B A1L76 C 3 .   ? 13.12200 7.24400   27.95900 0.460 53.13582  ?  501 A1L76 A C35  1 
HETATM 2134 C  C36  A A1L76 C 3 .   ? 12.29800 8.01600   28.38800 0.520 53.70687  ?  501 A1L76 A C36  1 
HETATM 2135 C  C36  B A1L76 C 3 .   ? 12.26400 8.08800   28.44100 0.460 54.33747  ?  501 A1L76 A C36  1 
HETATM 2136 C  C37  A A1L76 C 3 .   ? 16.61300 4.50000   25.41000 0.520 45.42286  ?  501 A1L76 A C37  1 
HETATM 2137 C  C37  B A1L76 C 3 .   ? 16.59600 4.51000   25.42000 0.460 45.21582  ?  501 A1L76 A C37  1 
HETATM 2138 C  C38  A A1L76 C 3 .   ? 16.70100 3.24700   25.73600 0.520 44.00584  ?  501 A1L76 A C38  1 
HETATM 2139 C  C38  B A1L76 C 3 .   ? 16.71000 3.25300   25.73200 0.460 44.71332  ?  501 A1L76 A C38  1 
HETATM 2140 O  O07  A A1L76 C 3 .   ? 14.29500 7.45300   19.80400 0.520 50.67727  ?  501 A1L76 A O07  1 
HETATM 2141 O  O07  B A1L76 C 3 .   ? 14.16100 7.05100   19.93800 0.460 50.14818  ?  501 A1L76 A O07  1 
HETATM 2142 O  O17  A A1L76 C 3 .   ? 10.68100 1.15300   26.97200 0.520 40.28523  ?  501 A1L76 A O17  1 
HETATM 2143 O  O17  B A1L76 C 3 .   ? 10.66300 1.14400   26.95000 0.460 40.04029  ?  501 A1L76 A O17  1 
HETATM 2144 O  O24  A A1L76 C 3 .   ? 9.79100  -1.02200  28.42000 0.520 39.25119  ?  501 A1L76 A O24  1 
HETATM 2145 O  O24  B A1L76 C 3 .   ? 9.79200  -1.03000  28.42500 0.460 39.64406  ?  501 A1L76 A O24  1 
HETATM 2146 O  O27  A A1L76 C 3 .   ? 14.74400 5.84400   16.53900 0.520 49.36579  ?  501 A1L76 A O27  1 
HETATM 2147 O  O27  B A1L76 C 3 .   ? 15.80300 6.89200   17.87800 0.460 49.90223  ?  501 A1L76 A O27  1 
HETATM 2148 O  O31  A A1L76 C 3 .   ? 13.06000 8.39900   13.53500 0.520 48.11656  ?  501 A1L76 A O31  1 
HETATM 2149 O  O31  B A1L76 C 3 .   ? 13.76500 6.71800   14.04900 0.460 49.49885  ?  501 A1L76 A O31  1 
HETATM 2150 O  O32  A A1L76 C 3 .   ? 13.82400 6.53600   14.29700 0.520 49.99711  -1 501 A1L76 A O32  1 
HETATM 2151 O  O32  B A1L76 C 3 .   ? 14.59500 5.86000   15.90500 0.460 49.27166  -1 501 A1L76 A O32  1 
HETATM 2152 SI SI08 A A1L76 C 3 .   ? 14.18900 5.87000   25.68100 0.520 48.81329  ?  501 A1L76 A SI08 1 
HETATM 2153 SI SI08 B A1L76 C 3 .   ? 14.18700 5.87600   25.78100 0.460 48.85384  ?  501 A1L76 A SI08 1 
HETATM 2154 O  O    . HOH   D 4 .   ? 20.23300 -10.01800 16.43700 1.000 42.50804  ?  601 HOH   A O    1 
HETATM 2155 O  O    . HOH   D 4 .   ? 24.56100 -23.05700 7.18400  1.000 66.41496  ?  602 HOH   A O    1 
HETATM 2156 O  O    . HOH   D 4 .   ? 23.19000 -3.87500  32.66100 1.000 57.29013  ?  603 HOH   A O    1 
HETATM 2157 O  O    . HOH   D 4 .   ? 19.60400 -20.03900 5.82200  1.000 57.35480  ?  604 HOH   A O    1 
HETATM 2158 O  O    . HOH   D 4 .   ? 28.562   0.566     38.003   1.000 58.67761  ?  605 HOH   A O    1 
HETATM 2159 O  O    . HOH   D 4 .   ? 40.94300 -5.07900  14.79600 1.000 61.72537  ?  606 HOH   A O    1 
HETATM 2160 O  O    A HOH   D 4 .   ? 15.85900 -14.97500 1.55500  0.420 84.92288  ?  607 HOH   A O    1 
HETATM 2161 O  O    B HOH   D 4 .   ? 11.21300 -10.83400 1.46900  0.580 77.79367  ?  607 HOH   A O    1 
HETATM 2162 O  O    . HOH   D 4 .   ? 20.59300 15.69300  21.75100 1.000 57.17957  ?  608 HOH   A O    1 
HETATM 2163 O  O    . HOH   D 4 .   ? 26.19600 -16.09200 23.33700 1.000 40.44100  ?  609 HOH   A O    1 
HETATM 2164 O  O    . HOH   D 4 .   ? 28.61800 0.71000   29.48400 1.000 50.43688  ?  610 HOH   A O    1 
HETATM 2165 O  O    . HOH   D 4 .   ? 18.47800 12.05400  32.90600 1.000 56.56177  ?  611 HOH   A O    1 
HETATM 2166 O  O    . HOH   D 4 .   ? 26.18700 -0.00500  31.05800 1.000 39.72427  ?  612 HOH   A O    1 
HETATM 2167 O  O    . HOH   D 4 .   ? 10.43800 17.07900  29.11200 1.000 70.74362  ?  613 HOH   A O    1 
HETATM 2168 O  O    . HOH   D 4 .   ? 18.46400 -18.25600 7.61800  1.000 49.02394  ?  614 HOH   A O    1 
HETATM 2169 O  O    . HOH   D 4 .   ? 13.27000 -6.51000  26.19500 1.000 40.86619  ?  615 HOH   A O    1 
HETATM 2170 O  O    . HOH   D 4 .   ? 11.96000 10.64200  13.94200 1.000 68.76657  ?  616 HOH   A O    1 
HETATM 2171 O  O    . HOH   D 4 .   ? 15.98000 -11.06500 31.22800 1.000 48.22742  ?  617 HOH   A O    1 
HETATM 2172 O  O    . HOH   D 4 .   ? 13.80300 -1.11500  4.70000  1.000 50.51576  ?  618 HOH   A O    1 
HETATM 2173 O  O    . HOH   D 4 .   ? 19.52800 -7.33000  2.87000  1.000 51.65207  ?  619 HOH   A O    1 
HETATM 2174 O  O    . HOH   D 4 .   ? 24.81800 -7.41100  21.61500 1.000 35.39470  ?  620 HOH   A O    1 
HETATM 2175 O  O    . HOH   D 4 .   ? 18.49300 3.67300   11.55400 1.000 37.69441  ?  621 HOH   A O    1 
HETATM 2176 O  O    . HOH   D 4 .   ? 20.60800 -3.20100  1.05400  1.000 44.12747  ?  622 HOH   A O    1 
HETATM 2177 O  O    . HOH   D 4 .   ? 13.94000 -6.47500  21.23200 1.000 34.67817  ?  623 HOH   A O    1 
HETATM 2178 O  O    . HOH   D 4 .   ? 15.49000 -9.30000  23.83600 1.000 47.49184  ?  624 HOH   A O    1 
HETATM 2179 O  O    . HOH   D 4 .   ? 10.66300 -10.14400 28.50900 1.000 51.79965  ?  625 HOH   A O    1 
HETATM 2180 O  O    . HOH   D 4 .   ? 21.04800 6.94000   15.55900 1.000 37.17034  ?  626 HOH   A O    1 
HETATM 2181 O  O    . HOH   D 4 .   ? 18.62400 3.00000   -1.06000 1.000 42.63775  ?  627 HOH   A O    1 
HETATM 2182 O  O    . HOH   D 4 .   ? 3.95800  1.38900   15.73900 1.000 57.95611  ?  628 HOH   A O    1 
HETATM 2183 O  O    . HOH   D 4 .   ? 25.33400 6.46300   1.55000  1.000 44.65164  ?  629 HOH   A O    1 
HETATM 2184 O  O    . HOH   D 4 .   ? 31.53500 -10.91500 13.42300 1.000 47.03666  ?  630 HOH   A O    1 
HETATM 2185 O  O    . HOH   D 4 .   ? 20.98700 1.85800   1.51000  1.000 38.72808  ?  631 HOH   A O    1 
HETATM 2186 O  O    . HOH   D 4 .   ? 23.65100 -12.77200 25.26600 1.000 50.44830  ?  632 HOH   A O    1 
HETATM 2187 O  O    . HOH   D 4 .   ? 29.61300 7.93800   19.80300 1.000 40.36005  ?  633 HOH   A O    1 
HETATM 2188 O  O    . HOH   D 4 .   ? 11.46000 -8.99800  26.29300 1.000 49.93043  ?  634 HOH   A O    1 
HETATM 2189 O  O    . HOH   D 4 .   ? 27.16600 -9.34100  28.14000 1.000 41.93633  ?  635 HOH   A O    1 
HETATM 2190 O  O    . HOH   D 4 .   ? 35.93300 -6.05500  23.88800 1.000 47.12895  ?  636 HOH   A O    1 
HETATM 2191 O  O    . HOH   D 4 .   ? 7.20400  0.92800   9.20700  1.000 49.28121  ?  637 HOH   A O    1 
HETATM 2192 O  O    . HOH   D 4 .   ? 12.09600 -9.93500  22.38600 1.000 44.46902  ?  638 HOH   A O    1 
HETATM 2193 O  O    . HOH   D 4 .   ? -0.96100 3.21100   20.05500 1.000 41.56179  ?  639 HOH   A O    1 
HETATM 2194 O  O    . HOH   D 4 .   ? 30.14800 5.27000   31.42800 1.000 56.53884  ?  640 HOH   A O    1 
HETATM 2195 O  O    . HOH   D 4 .   ? 9.25600  -1.10000  9.19600  1.000 44.66225  ?  641 HOH   A O    1 
HETATM 2196 O  O    . HOH   D 4 .   ? 14.33000 13.74600  7.50800  1.000 51.56985  ?  642 HOH   A O    1 
HETATM 2197 O  O    . HOH   D 4 .   ? 27.99900 -10.21700 18.09700 1.000 39.30762  ?  643 HOH   A O    1 
HETATM 2198 O  O    . HOH   D 4 .   ? 19.12700 10.70800  9.59700  1.000 51.80852  ?  644 HOH   A O    1 
HETATM 2199 O  O    . HOH   D 4 .   ? 1.75600  -1.61400  16.98600 1.000 29.39398  ?  645 HOH   A O    1 
HETATM 2200 O  O    . HOH   D 4 .   ? 43.63700 1.13700   14.31500 1.000 66.34141  ?  646 HOH   A O    1 
HETATM 2201 O  O    . HOH   D 4 .   ? 3.89500  4.30200   17.32500 1.000 44.34671  ?  647 HOH   A O    1 
HETATM 2202 O  O    . HOH   D 4 .   ? 20.65400 -25.51800 12.44400 1.000 66.23553  ?  648 HOH   A O    1 
HETATM 2203 O  O    . HOH   D 4 .   ? 0.76100  -8.70700  19.06100 1.000 49.68661  ?  649 HOH   A O    1 
HETATM 2204 O  O    . HOH   D 4 .   ? 40.53500 -2.65200  19.04400 1.000 47.37165  ?  650 HOH   A O    1 
HETATM 2205 O  O    . HOH   D 4 .   ? 44.16100 -0.16200  18.67800 1.000 55.07057  ?  651 HOH   A O    1 
HETATM 2206 O  O    . HOH   D 4 .   ? 25.76200 -8.78100  19.52400 1.000 45.92358  ?  652 HOH   A O    1 
HETATM 2207 O  O    . HOH   D 4 .   ? 27.09100 6.77300   18.63300 1.000 46.46266  ?  653 HOH   A O    1 
HETATM 2208 O  O    . HOH   D 4 .   ? 13.21200 -10.58200 25.58200 1.000 45.09247  ?  654 HOH   A O    1 
HETATM 2209 O  O    . HOH   D 4 .   ? 12.21900 -17.54500 4.26500  1.000 66.68825  ?  655 HOH   A O    1 
HETATM 2210 O  O    . HOH   D 4 .   ? 9.76400  -3.05500  36.37700 1.000 46.60075  ?  656 HOH   A O    1 
HETATM 2211 O  O    . HOH   D 4 .   ? 38.84800 10.35800  7.85100  1.000 64.86425  ?  657 HOH   A O    1 
HETATM 2212 O  O    . HOH   D 4 .   ? 27.60200 -12.52100 17.98300 1.000 42.52232  ?  658 HOH   A O    1 
HETATM 2213 O  O    . HOH   D 4 .   ? 31.83200 2.05000   28.93900 1.000 57.69458  ?  659 HOH   A O    1 
HETATM 2214 O  O    . HOH   D 4 .   ? 21.56400 -8.21500  33.11800 1.000 56.16261  ?  660 HOH   A O    1 
HETATM 2215 O  O    . HOH   D 4 .   ? -2.80200 0.89900   23.05900 1.000 53.59973  ?  661 HOH   A O    1 
HETATM 2216 O  O    . HOH   D 4 .   ? 46.26700 -3.32700  4.52400  1.000 62.02331  ?  662 HOH   A O    1 
HETATM 2217 O  O    . HOH   D 4 .   ? 32.90800 -16.57000 7.76400  1.000 55.34287  ?  663 HOH   A O    1 
HETATM 2218 O  O    . HOH   D 4 .   ? 12.67500 -11.69600 30.90300 1.000 73.34720  ?  664 HOH   A O    1 
HETATM 2219 O  O    A HOH   D 4 .   ? -0.70400 -12.68200 28.89800 0.480 39.10070  ?  665 HOH   A O    1 
HETATM 2220 O  O    B HOH   D 4 .   ? -1.34100 -13.62000 27.06000 0.520 39.10445  ?  665 HOH   A O    1 
HETATM 2221 O  O    . HOH   D 4 .   ? 27.29800 -14.99800 3.04800  1.000 59.60675  ?  666 HOH   A O    1 
HETATM 2222 O  O    . HOH   D 4 .   ? 24.49200 6.23700   35.69300 1.000 60.35201  ?  667 HOH   A O    1 
HETATM 2223 O  O    . HOH   D 4 .   ? 1.37500  -11.20400 17.20400 1.000 56.21984  ?  668 HOH   A O    1 
HETATM 2224 O  O    . HOH   D 4 .   ? 33.91400 3.92900   26.13100 1.000 44.77309  ?  669 HOH   A O    1 
HETATM 2225 O  O    . HOH   D 4 .   ? 26.17500 10.22300  19.19900 1.000 52.26643  ?  670 HOH   A O    1 
HETATM 2226 O  O    . HOH   D 4 .   ? 13.34300 -7.67900  23.80400 1.000 47.42355  ?  671 HOH   A O    1 
HETATM 2227 O  O    . HOH   D 4 .   ? 29.28900 10.40400  19.46400 1.000 49.39101  ?  672 HOH   A O    1 
HETATM 2228 O  O    . HOH   D 4 .   ? 33.63000 -10.87100 15.63000 1.000 57.90992  ?  673 HOH   A O    1 
HETATM 2229 O  O    . HOH   D 4 .   ? -0.45300 -11.51700 30.79300 1.000 61.70291  ?  674 HOH   A O    1 
HETATM 2230 O  O    A HOH   D 4 .   ? 30.21300 6.31700   2.14700  0.680 43.61555  ?  675 HOH   A O    1 
HETATM 2231 O  O    B HOH   D 4 .   ? 28.11100 7.53900   1.23800  0.320 35.92035  ?  675 HOH   A O    1 
HETATM 2232 O  O    . HOH   D 4 .   ? 33.71000 5.27800   29.09100 1.000 51.89067  ?  676 HOH   A O    1 
HETATM 2233 O  O    . HOH   D 4 .   ? 0.57100  -10.81200 23.76200 1.000 64.65286  ?  677 HOH   A O    1 
HETATM 2234 O  O    . HOH   D 4 .   ? 30.92700 -9.36600  17.73500 1.000 60.16611  ?  678 HOH   A O    1 
HETATM 2235 O  O    . HOH   D 4 .   ? 30.13600 11.78200  29.45400 1.000 169.77440 ?  679 HOH   A O    1 
HETATM 2236 O  O    . HOH   D 4 .   ? 30.27500 7.31700   32.80100 1.000 86.96223  ?  680 HOH   A O    1 
HETATM 2237 O  O    . HOH   D 4 .   ? 40.888   -12.072   6.293    1.000 51.64839  ?  681 HOH   A O    1 
HETATM 2238 O  O    . HOH   E 4 .   ? 12.87500 -8.82800  5.41600  1.000 100.56315 ?  701 HOH   C O    1 
HETATM 2239 O  O    . HOH   E 4 .   ? 9.72300  -2.35800  6.94600  1.000 47.06091  ?  702 HOH   C 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    . LYS   A 18  ? 0.60722 1.34403 0.84903 -0.13789 0.12986  -0.02689 123 LYS   A N    
2    C  CA   . LYS   A 18  ? 0.64505 1.35738 0.84544 -0.16146 0.12602  -0.00842 123 LYS   A CA   
3    C  C    . LYS   A 18  ? 0.61384 1.28702 0.78528 -0.15581 0.12348  -0.01358 123 LYS   A C    
4    O  O    . LYS   A 18  ? 0.59697 1.26392 0.77515 -0.13461 0.12742  -0.03471 123 LYS   A O    
5    C  CB   . LYS   A 18  ? 0.73836 1.48006 0.92223 -0.17518 0.13626  -0.00495 123 LYS   A CB   
6    C  CG   . LYS   A 18  ? 0.83200 1.55876 0.99476 -0.20218 0.12763  0.02213  123 LYS   A CG   
7    C  CD   . LYS   A 18  ? 0.89649 1.64258 1.03201 -0.21643 0.13630  0.02772  123 LYS   A CD   
8    C  CE   . LYS   A 18  ? 0.89885 1.61824 0.99722 -0.21942 0.13503  0.03026  123 LYS   A CE   
9    N  NZ   . LYS   A 18  ? 0.88109 1.54953 0.96434 -0.22815 0.11978  0.04827  123 LYS   A NZ   
10   N  N    . LEU   A 19  ? 0.56152 1.20085 0.69992 -0.17337 0.11463  0.00579  124 LEU   A N    
11   C  CA   . LEU   A 19  ? 0.60266 1.19522 0.71176 -0.16758 0.10755  0.00443  124 LEU   A CA   
12   C  C    . LEU   A 19  ? 0.58179 1.19930 0.67203 -0.16657 0.12110  -0.00924 124 LEU   A C    
13   O  O    . LEU   A 19  ? 0.56984 1.21170 0.63880 -0.18565 0.12775  0.00216  124 LEU   A O    
14   C  CB   . LEU   A 19  ? 0.63159 1.18525 0.71474 -0.18591 0.09426  0.02929  124 LEU   A CB   
15   C  CG   . LEU   A 19  ? 0.64299 1.13867 0.70817 -0.17731 0.08033  0.03172  124 LEU   A CG   
16   C  CD1  . LEU   A 19  ? 0.56772 1.04212 0.65662 -0.15839 0.07255  0.02216  124 LEU   A CD1  
17   C  CD2  . LEU   A 19  ? 0.68669 1.15133 0.73133 -0.19601 0.06874  0.05563  124 LEU   A CD2  
18   N  N    . SER   A 20  ? 0.54455 1.15627 0.64207 -0.14535 0.12472  -0.03336 125 SER   A N    
19   C  CA   . SER   A 20  ? 0.53563 1.17098 0.61554 -0.14314 0.13699  -0.05106 125 SER   A CA   
20   C  C    . SER   A 20  ? 0.60633 1.21581 0.64438 -0.15644 0.13006  -0.03708 125 SER   A C    
21   O  O    . SER   A 20  ? 0.63021 1.19563 0.65640 -0.16160 0.11524  -0.01824 125 SER   A O    
22   C  CB   . SER   A 20  ? 0.48099 1.10633 0.57941 -0.11773 0.13961  -0.08059 125 SER   A CB   
23   O  OG   . SER   A 20  ? 0.48549 1.05680 0.57003 -0.11124 0.12618  -0.07906 125 SER   A OG   
24   N  N    . GLU   A 21  ? 0.62843 1.26818 0.64434 -0.16122 0.14086  -0.04734 126 GLU   A N    
25   C  CA   . GLU   A 21  ? 0.67298 1.29392 0.64937 -0.17293 0.13392  -0.03411 126 GLU   A CA   
26   C  C    . GLU   A 21  ? 0.61207 1.18068 0.58377 -0.15914 0.12049  -0.04060 126 GLU   A C    
27   O  O    . GLU   A 21  ? 0.53968 1.07447 0.48955 -0.16656 0.10772  -0.02141 126 GLU   A O    
28   C  CB   . GLU   A 21  ? 0.78955 1.44959 0.74394 -0.17729 0.14472  -0.04668 126 GLU   A CB   
29   C  CG   . GLU   A 21  ? 0.90986 1.56202 0.82657 -0.19564 0.13584  -0.02127 126 GLU   A CG   
30   C  CD   . GLU   A 21  ? 0.98447 1.63760 0.90145 -0.21328 0.13125  0.00872  126 GLU   A CD   
31   O  OE1  . GLU   A 21  ? 1.00493 1.62331 0.90924 -0.22390 0.11842  0.03507  126 GLU   A OE1  
32   O  OE2  . GLU   A 21  ? 1.00973 1.69753 0.94038 -0.21633 0.14015  0.00516  126 GLU   A OE2  
33   N  N    . GLU   A 22  ? 0.60453 1.16615 0.59858 -0.13896 0.12306  -0.06710 127 GLU   A N    
34   C  CA   . GLU   A 22  ? 0.58625 1.10010 0.57978 -0.12694 0.11088  -0.07281 127 GLU   A CA   
35   C  C    . GLU   A 22  ? 0.50440 0.97630 0.50816 -0.12606 0.09667  -0.05234 127 GLU   A C    
36   O  O    . GLU   A 22  ? 0.41071 0.84419 0.40218 -0.12457 0.08470  -0.04493 127 GLU   A O    
37   C  CB   . GLU   A 22  ? 0.71817 1.23405 0.73632 -0.10692 0.11719  -0.10488 127 GLU   A CB   
38   C  CG   . GLU   A 22  ? 0.84366 1.30993 0.87414 -0.09350 0.10492  -0.10868 127 GLU   A CG   
39   C  CD   . GLU   A 22  ? 0.95172 1.41644 0.99865 -0.07734 0.11024  -0.14068 127 GLU   A CD   
40   O  OE1  . GLU   A 22  ? 1.01093 1.49037 1.03855 -0.08023 0.11535  -0.15774 127 GLU   A OE1  
41   O  OE2  . GLU   A 22  ? 0.97122 1.41945 1.05042 -0.06209 0.10855  -0.14861 127 GLU   A OE2  
42   N  N    . GLN   A 23  ? 0.55886 1.04047 0.58464 -0.12750 0.09772  -0.04361 128 GLN   A N    
43   C  CA   . GLN   A 23  ? 0.49932 0.94410 0.53403 -0.12672 0.08429  -0.02700 128 GLN   A CA   
44   C  C    . GLN   A 23  ? 0.50700 0.93188 0.51550 -0.14385 0.07492  -0.00156 128 GLN   A C    
45   O  O    . GLN   A 23  ? 0.47406 0.85862 0.47608 -0.14127 0.06247  0.00733  128 GLN   A O    
46   C  CB   . GLN   A 23  ? 0.45217 0.91607 0.51870 -0.12345 0.08699  -0.02640 128 GLN   A CB   
47   C  CG   . GLN   A 23  ? 0.44583 0.91517 0.54341 -0.10212 0.09132  -0.04846 128 GLN   A CG   
48   C  CD   . GLN   A 23  ? 0.47841 0.97160 0.60942 -0.09788 0.09310  -0.04673 128 GLN   A CD   
49   O  OE1  . GLN   A 23  ? 0.49012 1.01294 0.62261 -0.11203 0.09704  -0.03566 128 GLN   A OE1  
50   N  NE2  . GLN   A 23  ? 0.42705 0.90826 0.58610 -0.07904 0.08945  -0.05634 128 GLN   A NE2  
51   N  N    . GLN   A 24  ? 0.51919 0.97182 0.51304 -0.16131 0.08075  0.01066  129 GLN   A N    
52   C  CA   . GLN   A 24  ? 0.56896 0.99891 0.53800 -0.17701 0.07101  0.03549  129 GLN   A CA   
53   C  C    . GLN   A 24  ? 0.54046 0.94990 0.48322 -0.17421 0.06514  0.03556  129 GLN   A C    
54   O  O    . GLN   A 24  ? 0.55636 0.93343 0.48404 -0.17961 0.05323  0.05336  129 GLN   A O    
55   C  CB   . GLN   A 24  ? 0.68088 1.14526 0.64092 -0.19821 0.07824  0.05156  129 GLN   A CB   
56   C  CG   . GLN   A 24  ? 0.78360 1.30224 0.74249 -0.19980 0.09540  0.03707  129 GLN   A CG   
57   C  CD   . GLN   A 24  ? 0.83391 1.39359 0.79535 -0.22003 0.10445  0.05169  129 GLN   A CD   
58   O  OE1  . GLN   A 24  ? 0.80996 1.40984 0.79053 -0.21588 0.11645  0.03708  129 GLN   A OE1  
59   N  NE2  . GLN   A 24  ? 0.87126 1.41066 0.81529 -0.23779 0.09477  0.07908  129 GLN   A NE2  
60   N  N    . HIS   A 25  ? 0.52135 0.94955 0.45973 -0.16559 0.07272  0.01502  130 HIS   A N    
61   C  CA   . HIS   A 25  ? 0.51861 0.92783 0.43591 -0.16156 0.06570  0.01229  130 HIS   A CA   
62   C  C    . HIS   A 25  ? 0.53142 0.89637 0.45982 -0.14834 0.05410  0.00988  130 HIS   A C    
63   O  O    . HIS   A 25  ? 0.59121 0.92870 0.50460 -0.14928 0.04293  0.02168  130 HIS   A O    
64   C  CB   . HIS   A 25  ? 0.56873 1.00893 0.48115 -0.15583 0.07636  -0.01303 130 HIS   A CB   
65   C  CG   . HIS   A 25  ? 0.65428 1.07778 0.54874 -0.15143 0.06865  -0.01937 130 HIS   A CG   
66   N  ND1  . HIS   A 25  ? 0.68128 1.09809 0.54756 -0.16152 0.05963  0.00005  130 HIS   A ND1  
67   C  CD2  . HIS   A 25  ? 0.66813 1.08028 0.57082 -0.13847 0.06765  -0.04216 130 HIS   A CD2  
68   C  CE1  . HIS   A 25  ? 0.68809 1.09409 0.54606 -0.15474 0.05361  -0.01132 130 HIS   A CE1  
69   N  NE2  . HIS   A 25  ? 0.66473 1.06714 0.54421 -0.14175 0.05851  -0.03721 130 HIS   A NE2  
70   N  N    . ILE   A 26  ? 0.50107 0.86092 0.45664 -0.13563 0.05668  -0.00469 131 ILE   A N    
71   C  CA   . ILE   A 26  ? 0.46748 0.78943 0.43450 -0.12424 0.04674  -0.00558 131 ILE   A CA   
72   C  C    . ILE   A 26  ? 0.48604 0.78053 0.44711 -0.13071 0.03574  0.01655  131 ILE   A C    
73   O  O    . ILE   A 26  ? 0.48549 0.75033 0.43915 -0.12677 0.02598  0.02182  131 ILE   A O    
74   C  CB   . ILE   A 26  ? 0.49744 0.82211 0.49548 -0.11128 0.05116  -0.02037 131 ILE   A CB   
75   C  CG1  . ILE   A 26  ? 0.48701 0.82623 0.49244 -0.10150 0.05942  -0.04550 131 ILE   A CG1  
76   C  CG2  . ILE   A 26  ? 0.49420 0.78310 0.50326 -0.10321 0.04052  -0.01438 131 ILE   A CG2  
77   C  CD1  . ILE   A 26  ? 0.47988 0.82694 0.51809 -0.08835 0.06511  -0.06005 131 ILE   A CD1  
78   N  N    . ILE   A 27  ? 0.51219 0.81723 0.47793 -0.14085 0.03727  0.02843  132 ILE   A N    
79   C  CA   . ILE   A 27  ? 0.50263 0.78005 0.46404 -0.14776 0.02663  0.04685  132 ILE   A CA   
80   C  C    . ILE   A 27  ? 0.49101 0.75160 0.42683 -0.15504 0.01933  0.06139  132 ILE   A C    
81   O  O    . ILE   A 27  ? 0.48663 0.71404 0.41783 -0.15159 0.00864  0.06876  132 ILE   A O    
82   C  CB   . ILE   A 27  ? 0.47169 0.76658 0.44408 -0.15987 0.02967  0.05586  132 ILE   A CB   
83   C  CG1  . ILE   A 27  ? 0.46355 0.76711 0.46410 -0.14998 0.03202  0.04445  132 ILE   A CG1  
84   C  CG2  . ILE   A 27  ? 0.42406 0.69073 0.38693 -0.17122 0.01878  0.07511  132 ILE   A CG2  
85   C  CD1  . ILE   A 27  ? 0.43862 0.77509 0.45499 -0.16002 0.03847  0.04774  132 ILE   A CD1  
86   N  N    . ALA   A 28  ? 0.48606 0.77122 0.40521 -0.16461 0.02486  0.06589  133 ALA   A N    
87   C  CA   . ALA   A 28  ? 0.50580 0.77793 0.40067 -0.17081 0.01695  0.08162  133 ALA   A CA   
88   C  C    . ALA   A 28  ? 0.51866 0.77003 0.40887 -0.15728 0.00970  0.07347  133 ALA   A C    
89   O  O    . ALA   A 28  ? 0.49591 0.71953 0.37755 -0.15598 -0.00151 0.08602  133 ALA   A O    
90   C  CB   . ALA   A 28  ? 0.50191 0.81104 0.37846 -0.18293 0.02501  0.08635  133 ALA   A CB   
91   N  N    . ILE   A 29  ? 0.51441 0.77907 0.41219 -0.14712 0.01580  0.05209  134 ILE   A N    
92   C  CA   . ILE   A 29  ? 0.53866 0.78710 0.43413 -0.13633 0.00936  0.04375  134 ILE   A CA   
93   C  C    . ILE   A 29  ? 0.55168 0.76546 0.45923 -0.12792 0.00073  0.04760  134 ILE   A C    
94   O  O    . ILE   A 29  ? 0.54196 0.73622 0.44247 -0.12380 -0.00854 0.05395  134 ILE   A O    
95   C  CB   . ILE   A 29  ? 0.50664 0.77316 0.41156 -0.12852 0.01766  0.01886  134 ILE   A CB   
96   C  CG1  . ILE   A 29  ? 0.54720 0.84955 0.43528 -0.13616 0.02542  0.01204  134 ILE   A CG1  
97   C  CG2  . ILE   A 29  ? 0.41876 0.66501 0.32829 -0.11821 0.01077  0.01016  134 ILE   A CG2  
98   C  CD1  . ILE   A 29  ? 0.64311 0.95051 0.50419 -0.14696 0.01891  0.03191  134 ILE   A CD1  
99   N  N    . LEU   A 30  ? 0.49180 0.70077 0.41789 -0.12507 0.00365  0.04364  135 LEU   A N    
100  C  CA   . LEU   A 30  ? 0.45660 0.63747 0.39288 -0.11748 -0.00355 0.04552  135 LEU   A CA   
101  C  C    . LEU   A 30  ? 0.43994 0.59839 0.36653 -0.12296 -0.01261 0.06258  135 LEU   A C    
102  O  O    . LEU   A 30  ? 0.46133 0.59662 0.38717 -0.11591 -0.02030 0.06454  135 LEU   A O    
103  C  CB   . LEU   A 30  ? 0.42562 0.61108 0.38283 -0.11395 0.00093  0.03832  135 LEU   A CB   
104  C  CG   . LEU   A 30  ? 0.40961 0.60952 0.38116 -0.10530 0.00825  0.02088  135 LEU   A CG   
105  C  CD1  . LEU   A 30  ? 0.44649 0.64980 0.44056 -0.10028 0.01064  0.01691  135 LEU   A CD1  
106  C  CD2  . LEU   A 30  ? 0.33978 0.52472 0.31010 -0.09701 0.00414  0.01424  135 LEU   A CD2  
107  N  N    . LEU   A 31  ? 0.41698 0.58204 0.33749 -0.13567 -0.01165 0.07460  136 LEU   A N    
108  C  CA   . LEU   A 31  ? 0.49318 0.63306 0.40510 -0.14188 -0.02109 0.09121  136 LEU   A CA   
109  C  C    . LEU   A 31  ? 0.56723 0.69393 0.46477 -0.13725 -0.02887 0.09843  136 LEU   A C    
110  O  O    . LEU   A 31  ? 0.58091 0.67962 0.47863 -0.13098 -0.03796 0.10281  136 LEU   A O    
111  C  CB   . LEU   A 31  ? 0.51888 0.67095 0.42615 -0.15903 -0.01836 0.10481  136 LEU   A CB   
112  C  CG   . LEU   A 31  ? 0.47183 0.63148 0.39502 -0.16595 -0.01456 0.10255  136 LEU   A CG   
113  C  CD1  . LEU   A 31  ? 0.50416 0.68608 0.42290 -0.18432 -0.00941 0.11542  136 LEU   A CD1  
114  C  CD2  . LEU   A 31  ? 0.49497 0.62099 0.42398 -0.16449 -0.02446 0.10501  136 LEU   A CD2  
115  N  N    . ASP   A 32  ? 0.53819 0.68739 0.42374 -0.13968 -0.02555 0.09868  137 ASP   A N    
116  C  CA   . ASP   A 32  ? 0.55340 0.69615 0.42549 -0.13566 -0.03385 0.10643  137 ASP   A CA   
117  C  C    . ASP   A 32  ? 0.53422 0.66502 0.41509 -0.12047 -0.03786 0.09420  137 ASP   A C    
118  O  O    . ASP   A 32  ? 0.52759 0.63918 0.40631 -0.11375 -0.04756 0.10165  137 ASP   A O    
119  C  CB   . ASP   A 32  ? 0.57112 0.74684 0.42758 -0.14268 -0.02886 0.10667  137 ASP   A CB   
120  C  CG   . ASP   A 32  ? 0.64648 0.82186 0.48902 -0.13860 -0.03827 0.11404  137 ASP   A CG   
121  O  OD1  . ASP   A 32  ? 0.66730 0.82627 0.50082 -0.14151 -0.04821 0.13486  137 ASP   A OD1  
122  O  OD2  . ASP   A 32  ? 0.65311 0.84475 0.49506 -0.13264 -0.03643 0.09910  137 ASP   A OD2  
123  N  N    . ALA   A 33  ? 0.51012 0.65261 0.40262 -0.11487 -0.03052 0.07599  138 ALA   A N    
124  C  CA   . ALA   A 33  ? 0.48008 0.61363 0.38212 -0.10284 -0.03340 0.06556  138 ALA   A CA   
125  C  C    . ALA   A 33  ? 0.45938 0.56575 0.36878 -0.09628 -0.03962 0.07002  138 ALA   A C    
126  O  O    . ALA   A 33  ? 0.43929 0.53604 0.35055 -0.08742 -0.04563 0.06966  138 ALA   A O    
127  C  CB   . ALA   A 33  ? 0.51803 0.66416 0.43363 -0.09961 -0.02472 0.04787  138 ALA   A CB   
128  N  N    . HIS   A 34  ? 0.47183 0.56832 0.38613 -0.10063 -0.03814 0.07285  139 HIS   A N    
129  C  CA   . HIS   A 34  ? 0.45932 0.53099 0.37879 -0.09544 -0.04395 0.07458  139 HIS   A CA   
130  C  C    . HIS   A 34  ? 0.52115 0.57301 0.43208 -0.09368 -0.05368 0.08676  139 HIS   A C    
131  O  O    . HIS   A 34  ? 0.52446 0.56174 0.43922 -0.08296 -0.05906 0.08416  139 HIS   A O    
132  C  CB   . HIS   A 34  ? 0.47234 0.54029 0.39759 -0.10300 -0.04151 0.07508  139 HIS   A CB   
133  C  CG   . HIS   A 34  ? 0.48118 0.52545 0.41020 -0.09899 -0.04743 0.07393  139 HIS   A CG   
134  N  ND1  . HIS   A 34  ? 0.48615 0.52601 0.42122 -0.08786 -0.04800 0.06441  139 HIS   A ND1  
135  C  CD2  . HIS   A 34  ? 0.53258 0.55699 0.45971 -0.10534 -0.05299 0.08006  139 HIS   A CD2  
136  C  CE1  . HIS   A 34  ? 0.50148 0.52199 0.43690 -0.08661 -0.05309 0.06321  139 HIS   A CE1  
137  N  NE2  . HIS   A 34  ? 0.52373 0.53264 0.45498 -0.09699 -0.05667 0.07176  139 HIS   A NE2  
138  N  N    . HIS   A 35  ? 0.52610 0.57841 0.42632 -0.10384 -0.05601 0.10083  140 HIS   A N    
139  C  CA   . HIS   A 35  ? 0.58988 0.62004 0.48347 -0.10235 -0.06665 0.11551  140 HIS   A CA   
140  C  C    . HIS   A 35  ? 0.55463 0.58966 0.44605 -0.09078 -0.07215 0.11579  140 HIS   A C    
141  O  O    . HIS   A 35  ? 0.54375 0.55820 0.43648 -0.08257 -0.08170 0.12315  140 HIS   A O    
142  C  CB   . HIS   A 35  ? 0.63586 0.66867 0.51772 -0.11778 -0.06782 0.13368  140 HIS   A CB   
143  C  CG   . HIS   A 35  ? 0.76382 0.79240 0.64994 -0.13068 -0.06371 0.13530  140 HIS   A CG   
144  N  ND1  . HIS   A 35  ? 0.79825 0.84615 0.67748 -0.14700 -0.05827 0.14537  140 HIS   A ND1  
145  C  CD2  . HIS   A 35  ? 0.76501 0.77604 0.66193 -0.13037 -0.06430 0.12762  140 HIS   A CD2  
146  C  CE1  . HIS   A 35  ? 0.78621 0.82849 0.67397 -0.15628 -0.05595 0.14435  140 HIS   A CE1  
147  N  NE2  . HIS   A 35  ? 0.76566 0.78505 0.66360 -0.14659 -0.06014 0.13347  140 HIS   A NE2  
148  N  N    . LYS   A 36  ? 0.53823 0.60050 0.42819 -0.08973 -0.06677 0.10700  141 LYS   A N    
149  C  CA   . LYS   A 36  ? 0.54518 0.61699 0.43481 -0.08032 -0.07214 0.10569  141 LYS   A CA   
150  C  C    . LYS   A 36  ? 0.55627 0.62424 0.46076 -0.06759 -0.07143 0.09181  141 LYS   A C    
151  O  O    . LYS   A 36  ? 0.55142 0.62293 0.45962 -0.05811 -0.07757 0.09217  141 LYS   A O    
152  C  CB   . LYS   A 36  ? 0.53210 0.63552 0.41300 -0.08677 -0.06740 0.10088  141 LYS   A CB   
153  C  CG   . LYS   A 36  ? 0.55383 0.66868 0.41672 -0.09915 -0.06849 0.11594  141 LYS   A CG   
154  C  CD   . LYS   A 36  ? 0.64238 0.79140 0.49525 -0.10472 -0.06351 0.10727  141 LYS   A CD   
155  C  CE   . LYS   A 36  ? 0.72244 0.88705 0.55396 -0.11647 -0.06620 0.12472  141 LYS   A CE   
156  N  NZ   . LYS   A 36  ? 0.76722 0.90618 0.59489 -0.11655 -0.07719 0.14911  141 LYS   A NZ   
157  N  N    . THR   A 37  ? 0.55404 0.61792 0.46745 -0.06756 -0.06430 0.08074  142 THR   A N    
158  C  CA   . THR   A 37  ? 0.51173 0.57538 0.43765 -0.05758 -0.06251 0.06917  142 THR   A CA   
159  C  C    . THR   A 37  ? 0.53773 0.57926 0.46881 -0.05192 -0.06435 0.06748  142 THR   A C    
160  O  O    . THR   A 37  ? 0.60366 0.64673 0.54349 -0.04332 -0.06291 0.05882  142 THR   A O    
161  C  CB   . THR   A 37  ? 0.53095 0.61045 0.46352 -0.06127 -0.05331 0.05742  142 THR   A CB   
162  O  OG1  . THR   A 37  ? 0.54674 0.62409 0.47776 -0.06964 -0.04814 0.05773  142 THR   A OG1  
163  C  CG2  . THR   A 37  ? 0.51348 0.61449 0.44357 -0.06441 -0.05198 0.05362  142 THR   A CG2  
164  N  N    . TYR   A 38  ? 0.50292 0.52553 0.42868 -0.05758 -0.06730 0.07480  143 TYR   A N    
165  C  CA   . TYR   A 38  ? 0.53422 0.53370 0.46374 -0.05299 -0.07043 0.07132  143 TYR   A CA   
166  C  C    . TYR   A 38  ? 0.56471 0.54013 0.49098 -0.04995 -0.08042 0.08231  143 TYR   A C    
167  O  O    . TYR   A 38  ? 0.58928 0.55863 0.50768 -0.06007 -0.08361 0.09596  143 TYR   A O    
168  C  CB   . TYR   A 38  ? 0.54680 0.54199 0.47594 -0.06348 -0.06634 0.06862  143 TYR   A CB   
169  C  CG   . TYR   A 38  ? 0.54754 0.52399 0.48008 -0.05913 -0.06889 0.06028  143 TYR   A CG   
170  C  CD1  . TYR   A 38  ? 0.58554 0.53349 0.51608 -0.05975 -0.07668 0.06416  143 TYR   A CD1  
171  C  CD2  . TYR   A 38  ? 0.46400 0.45107 0.40130 -0.05499 -0.06393 0.04843  143 TYR   A CD2  
172  C  CE1  . TYR   A 38  ? 0.57925 0.51017 0.51224 -0.05595 -0.07913 0.05312  143 TYR   A CE1  
173  C  CE2  . TYR   A 38  ? 0.46915 0.44293 0.40686 -0.05163 -0.06616 0.03927  143 TYR   A CE2  
174  C  CZ   . TYR   A 38  ? 0.53894 0.48480 0.47438 -0.05193 -0.07360 0.03995  143 TYR   A CZ   
175  O  OH   . TYR   A 38  ? 0.58273 0.51500 0.51799 -0.04879 -0.07602 0.02754  143 TYR   A OH   
176  N  N    . ASP   A 39  ? 0.63539 0.59761 0.56864 -0.03594 -0.08522 0.07677  144 ASP   A N    
177  C  CA   . ASP   A 39  ? 0.65474 0.59107 0.58892 -0.02933 -0.09588 0.08631  144 ASP   A CA   
178  C  C    . ASP   A 39  ? 0.68023 0.58587 0.61810 -0.02723 -0.09886 0.07837  144 ASP   A C    
179  O  O    . ASP   A 39  ? 0.60911 0.51274 0.55455 -0.01446 -0.09762 0.06319  144 ASP   A O    
180  C  CB   . ASP   A 39  ? 0.68977 0.63596 0.63229 -0.01246 -0.10016 0.08507  144 ASP   A CB   
181  C  CG   . ASP   A 39  ? 0.76246 0.68237 0.70873 -0.00315 -0.11238 0.09634  144 ASP   A CG   
182  O  OD1  . ASP   A 39  ? 0.77647 0.67064 0.71660 -0.01254 -0.11790 0.10878  144 ASP   A OD1  
183  O  OD2  . ASP   A 39  ? 0.82225 0.74754 0.77934 0.01356  -0.11682 0.09360  144 ASP   A OD2  
184  N  N    . PRO   A 40  ? 0.75915 0.64186 0.69201 -0.04020 -0.10271 0.08719  145 PRO   A N    
185  C  CA   . PRO   A 40  ? 0.76926 0.62176 0.70583 -0.04016 -0.10627 0.07718  145 PRO   A CA   
186  C  C    . PRO   A 40  ? 0.81355 0.63530 0.75856 -0.02416 -0.11596 0.07507  145 PRO   A C    
187  O  O    . PRO   A 40  ? 0.82257 0.61783 0.77159 -0.02189 -0.11913 0.06263  145 PRO   A O    
188  C  CB   . PRO   A 40  ? 0.76821 0.60801 0.69856 -0.06116 -0.10816 0.09016  145 PRO   A CB   
189  C  CG   . PRO   A 40  ? 0.79866 0.65018 0.72234 -0.06716 -0.10976 0.11138  145 PRO   A CG   
190  C  CD   . PRO   A 40  ? 0.79319 0.67924 0.71674 -0.05695 -0.10355 0.10596  145 PRO   A CD   
191  N  N    . THR   A 41  ? 0.80530 0.63032 0.75415 -0.01249 -0.12133 0.08580  146 THR   A N    
192  C  CA   . THR   A 41  ? 0.82760 0.62743 0.78868 0.00696  -0.13024 0.08191  146 THR   A CA   
193  C  C    . THR   A 41  ? 0.78623 0.60297 0.75660 0.02477  -0.12398 0.05811  146 THR   A C    
194  O  O    . THR   A 41  ? 0.81656 0.61117 0.79776 0.04045  -0.12855 0.04587  146 THR   A O    
195  C  CB   . THR   A 41  ? 0.89001 0.69226 0.85381 0.01465  -0.13917 0.10254  146 THR   A CB   
196  O  OG1  . THR   A 41  ? 0.88525 0.73093 0.84756 0.01803  -0.13278 0.10154  146 THR   A OG1  
197  C  CG2  . THR   A 41  ? 0.92172 0.70901 0.87455 -0.00363 -0.14553 0.12848  146 THR   A CG2  
198  N  N    . TYR   A 42  ? 0.74397 0.59987 0.71104 0.02254  -0.11345 0.05137  147 TYR   A N    
199  C  CA   . TYR   A 42  ? 0.72533 0.60437 0.70044 0.03696  -0.10633 0.03215  147 TYR   A CA   
200  C  C    . TYR   A 42  ? 0.75253 0.63454 0.74267 0.05844  -0.11206 0.03195  147 TYR   A C    
201  O  O    . TYR   A 42  ? 0.73599 0.62283 0.73662 0.07450  -0.10928 0.01422  147 TYR   A O    
202  C  CB   . TYR   A 42  ? 0.77111 0.63709 0.74489 0.03775  -0.10262 0.01148  147 TYR   A CB   
203  C  CG   . TYR   A 42  ? 0.79729 0.66100 0.75852 0.01698  -0.09893 0.01253  147 TYR   A CG   
204  C  CD1  . TYR   A 42  ? 0.75777 0.65395 0.71304 0.00722  -0.08975 0.01334  147 TYR   A CD1  
205  C  CD2  . TYR   A 42  ? 0.85062 0.67986 0.80825 0.00707  -0.10533 0.01328  147 TYR   A CD2  
206  C  CE1  . TYR   A 42  ? 0.79582 0.69259 0.74275 -0.00979 -0.08701 0.01471  147 TYR   A CE1  
207  C  CE2  . TYR   A 42  ? 0.85278 0.68461 0.80147 -0.01204 -0.10238 0.01447  147 TYR   A CE2  
208  C  CZ   . TYR   A 42  ? 0.82868 0.69557 0.77245 -0.01941 -0.09321 0.01520  147 TYR   A CZ   
209  O  OH   . TYR   A 42  ? 0.81061 0.68270 0.74845 -0.03645 -0.09081 0.01664  147 TYR   A OH   
210  N  N    . ALA   A 43  ? 0.77232 0.65500 0.76374 0.05895  -0.12010 0.05176  148 ALA   A N    
211  C  CA   . ALA   A 43  ? 0.77708 0.66102 0.78461 0.07973  -0.12836 0.05497  148 ALA   A CA   
212  C  C    . ALA   A 43  ? 0.80857 0.73678 0.82648 0.09019  -0.12120 0.04478  148 ALA   A C    
213  O  O    . ALA   A 43  ? 0.82007 0.75487 0.85577 0.11074  -0.12476 0.03863  148 ALA   A O    
214  C  CB   . ALA   A 43  ? 0.75841 0.63399 0.76229 0.07553  -0.14014 0.08156  148 ALA   A CB   
215  N  N    . ASP   A 44  ? 0.80671 0.76569 0.81592 0.07648  -0.11137 0.04304  149 ASP   A N    
216  C  CA   . ASP   A 44  ? 0.79232 0.79312 0.81192 0.08280  -0.10482 0.03543  149 ASP   A CA   
217  C  C    . ASP   A 44  ? 0.72124 0.73358 0.74868 0.09227  -0.09514 0.01398  149 ASP   A C    
218  O  O    . ASP   A 44  ? 0.56763 0.61550 0.60671 0.09898  -0.08959 0.00747  149 ASP   A O    
219  C  CB   . ASP   A 44  ? 0.80129 0.82711 0.81019 0.06423  -0.09849 0.04124  149 ASP   A CB   
220  C  CG   . ASP   A 44  ? 0.86745 0.89364 0.86870 0.05607  -0.10696 0.06008  149 ASP   A CG   
221  O  OD1  . ASP   A 44  ? 0.89454 0.91675 0.90327 0.06740  -0.11792 0.07008  149 ASP   A OD1  
222  O  OD2  . ASP   A 44  ? 0.88589 0.91774 0.87378 0.03890  -0.10281 0.06480  149 ASP   A OD2  
223  N  N    . PHE   A 45  ? 0.75917 0.74491 0.78023 0.09188  -0.09309 0.00281  150 PHE   A N    
224  C  CA   . PHE   A 45  ? 0.78006 0.77919 0.80476 0.09966  -0.08359 -0.01854 150 PHE   A CA   
225  C  C    . PHE   A 45  ? 0.82081 0.83218 0.86609 0.12392  -0.08468 -0.02997 150 PHE   A C    
226  O  O    . PHE   A 45  ? 0.78390 0.82270 0.83446 0.13080  -0.07469 -0.04640 150 PHE   A O    
227  C  CB   . PHE   A 45  ? 0.79058 0.75737 0.80336 0.09396  -0.08337 -0.02909 150 PHE   A CB   
228  C  CG   . PHE   A 45  ? 0.77710 0.74626 0.77253 0.07191  -0.07808 -0.02444 150 PHE   A CG   
229  C  CD1  . PHE   A 45  ? 0.76736 0.73739 0.75592 0.05696  -0.08026 -0.00596 150 PHE   A CD1  
230  C  CD2  . PHE   A 45  ? 0.78605 0.75861 0.77249 0.06694  -0.07123 -0.03920 150 PHE   A CD2  
231  C  CE1  . PHE   A 45  ? 0.78825 0.76170 0.76435 0.03906  -0.07537 -0.00276 150 PHE   A CE1  
232  C  CE2  . PHE   A 45  ? 0.77900 0.75519 0.75215 0.04826  -0.06761 -0.03386 150 PHE   A CE2  
233  C  CZ   . PHE   A 45  ? 0.78550 0.76161 0.75500 0.03511  -0.06954 -0.01585 150 PHE   A CZ   
234  N  N    A ARG   A 46  ? 0.90469 0.89846 0.96224 0.13715  -0.09654 -0.02090 151 ARG   A N    
235  N  N    B ARG   A 46  ? 0.90722 0.90070 0.96493 0.13742  -0.09658 -0.02111 151 ARG   A N    
236  C  CA   A ARG   A 46  ? 0.95818 0.96656 1.03951 0.16237  -0.09867 -0.03033 151 ARG   A CA   
237  C  CA   B ARG   A 46  ? 0.95776 0.96639 1.03926 0.16269  -0.09841 -0.03101 151 ARG   A CA   
238  C  C    A ARG   A 46  ? 0.93985 1.00255 1.03305 0.16444  -0.09186 -0.02975 151 ARG   A C    
239  C  C    B ARG   A 46  ? 0.93911 1.00197 1.03254 0.16464  -0.09191 -0.02975 151 ARG   A C    
240  O  O    A ARG   A 46  ? 0.95820 1.04659 1.07109 0.18320  -0.08803 -0.04319 151 ARG   A O    
241  O  O    B ARG   A 46  ? 0.95545 1.04420 1.06887 0.18353  -0.08832 -0.04281 151 ARG   A O    
242  C  CB   A ARG   A 46  ? 1.01683 0.99510 1.10935 0.17483  -0.11499 -0.01535 151 ARG   A CB   
243  C  CB   B ARG   A 46  ? 1.01803 0.99624 1.11182 0.17655  -0.11464 -0.01731 151 ARG   A CB   
244  C  CG   A ARG   A 46  ? 1.03463 1.01534 1.11772 0.15983  -0.12311 0.01159  151 ARG   A CG   
245  C  CG   B ARG   A 46  ? 1.08938 1.02073 1.19082 0.19225  -0.12165 -0.02871 151 ARG   A CG   
246  C  CD   A ARG   A 46  ? 1.05715 1.04903 1.15894 0.17603  -0.13559 0.02576  151 ARG   A CD   
247  C  CD   B ARG   A 46  ? 1.11112 1.05783 1.23557 0.21954  -0.11701 -0.05379 151 ARG   A CD   
248  N  NE   A ARG   A 46  ? 1.07820 1.07694 1.16717 0.15987  -0.14282 0.05006  151 ARG   A NE   
249  N  NE   B ARG   A 46  ? 1.10909 1.09666 1.25586 0.23553  -0.11829 -0.04936 151 ARG   A NE   
250  C  CZ   A ARG   A 46  ? 1.12477 1.08890 1.20120 0.15123  -0.15349 0.06976  151 ARG   A CZ   
251  C  CZ   B ARG   A 46  ? 1.13156 1.11325 1.29976 0.25431  -0.13178 -0.03716 151 ARG   A CZ   
252  N  NH1  A ARG   A 46  ? 1.16629 1.08279 1.24314 0.15647  -0.15908 0.06899  151 ARG   A NH1  
253  N  NH1  B ARG   A 46  ? 1.16709 1.09682 1.33830 0.26111  -0.14665 -0.02604 151 ARG   A NH1  
254  N  NH2  A ARG   A 46  ? 1.12197 1.09991 1.18525 0.13639  -0.15850 0.08981  151 ARG   A NH2  
255  N  NH2  B ARG   A 46  ? 1.11994 1.14962 1.30945 0.26751  -0.13113 -0.03575 151 ARG   A NH2  
256  N  N    . ASP   A 47  ? 0.85469 0.93619 0.93778 0.14535  -0.09017 -0.01550 152 ASP   A N    
257  C  CA   . ASP   A 47  ? 0.74434 0.87495 0.83930 0.14403  -0.08502 -0.01395 152 ASP   A CA   
258  C  C    . ASP   A 47  ? 0.65856 0.81919 0.75146 0.13733  -0.06942 -0.02788 152 ASP   A C    
259  O  O    . ASP   A 47  ? 0.61913 0.82260 0.72664 0.13926  -0.06379 -0.03011 152 ASP   A O    
260  C  CB   . ASP   A 47  ? 0.73684 0.87371 0.82214 0.12596  -0.09007 0.00481  152 ASP   A CB   
261  C  CG   . ASP   A 47  ? 0.79826 0.91252 0.88369 0.13107  -0.10568 0.02156  152 ASP   A CG   
262  O  OD1  . ASP   A 47  ? 0.79739 0.90288 0.86682 0.11458  -0.10984 0.03580  152 ASP   A OD1  
263  O  OD2  . ASP   A 47  ? 0.84454 0.95081 0.94647 0.15200  -0.11379 0.02074  152 ASP   A OD2  
264  N  N    . PHE   A 48  ? 0.59237 0.73355 0.66788 0.12859  -0.06292 -0.03600 153 PHE   A N    
265  C  CA   . PHE   A 48  ? 0.55434 0.72406 0.62536 0.12127  -0.04901 -0.04643 153 PHE   A CA   
266  C  C    . PHE   A 48  ? 0.56697 0.76247 0.65370 0.14085  -0.04210 -0.06508 153 PHE   A C    
267  O  O    . PHE   A 48  ? 0.69640 0.87735 0.79537 0.16120  -0.04799 -0.07385 153 PHE   A O    
268  C  CB   . PHE   A 48  ? 0.56285 0.70686 0.61117 0.10800  -0.04552 -0.05007 153 PHE   A CB   
269  C  CG   . PHE   A 48  ? 0.55872 0.67737 0.59262 0.09024  -0.05140 -0.03410 153 PHE   A CG   
270  C  CD1  . PHE   A 48  ? 0.57635 0.70510 0.61397 0.08224  -0.05540 -0.01894 153 PHE   A CD1  
271  C  CD2  . PHE   A 48  ? 0.57764 0.66547 0.59467 0.08121  -0.05263 -0.03576 153 PHE   A CD2  
272  C  CE1  . PHE   A 48  ? 0.58994 0.69914 0.61433 0.06683  -0.05940 -0.00668 153 PHE   A CE1  
273  C  CE2  . PHE   A 48  ? 0.61648 0.68582 0.62221 0.06539  -0.05685 -0.02189 153 PHE   A CE2  
274  C  CZ   . PHE   A 48  ? 0.64028 0.72063 0.64943 0.05875  -0.05965 -0.00778 153 PHE   A CZ   
275  N  N    . ARG   A 49  ? 0.50277 0.73770 0.58986 0.13460  -0.02926 -0.07087 154 ARG   A N    
276  C  CA   . ARG   A 49  ? 0.55435 0.81832 0.65221 0.15074  -0.01975 -0.09062 154 ARG   A CA   
277  C  C    . ARG   A 49  ? 0.64232 0.87425 0.72610 0.15824  -0.01938 -0.10857 154 ARG   A C    
278  O  O    . ARG   A 49  ? 0.64683 0.84934 0.70887 0.14357  -0.02137 -0.10497 154 ARG   A O    
279  C  CB   . ARG   A 49  ? 0.55557 0.86779 0.65235 0.13810  -0.00561 -0.09014 154 ARG   A CB   
280  C  CG   . ARG   A 49  ? 0.54416 0.89884 0.66391 0.13713  -0.00425 -0.08049 154 ARG   A CG   
281  C  CD   . ARG   A 49  ? 0.49847 0.89176 0.61482 0.11772  0.00780  -0.07371 154 ARG   A CD   
282  N  NE   . ARG   A 49  ? 0.49787 0.86762 0.59651 0.09475  0.00481  -0.05757 154 ARG   A NE   
283  C  CZ   . ARG   A 49  ? 0.46127 0.84848 0.55101 0.07623  0.01340  -0.04994 154 ARG   A CZ   
284  N  NH1  . ARG   A 49  ? 0.47745 0.90764 0.57202 0.07598  0.02590  -0.05544 154 ARG   A NH1  
285  N  NH2  . ARG   A 49  ? 0.41830 0.78125 0.49521 0.05829  0.00957  -0.03630 154 ARG   A NH2  
286  N  N    . PRO   A 50  ? 0.72667 0.96433 0.82385 0.18114  -0.01722 -0.12928 155 PRO   A N    
287  C  CA   . PRO   A 50  ? 0.76923 0.96775 0.85622 0.19026  -0.02025 -0.14818 155 PRO   A CA   
288  C  C    . PRO   A 50  ? 0.76918 0.97472 0.83086 0.17582  -0.01052 -0.15876 155 PRO   A C    
289  O  O    . PRO   A 50  ? 0.75627 1.00847 0.81450 0.16958  0.00233  -0.16126 155 PRO   A O    
290  C  CB   . PRO   A 50  ? 0.84339 1.05758 0.95491 0.21972  -0.01790 -0.17006 155 PRO   A CB   
291  C  CG   . PRO   A 50  ? 0.80965 1.08675 0.93805 0.22150  -0.00744 -0.16645 155 PRO   A CG   
292  C  CD   . PRO   A 50  ? 0.72968 1.01037 0.85475 0.20058  -0.01247 -0.13749 155 PRO   A CD   
293  N  N    . PRO   A 51  ? 0.77302 0.93468 0.81669 0.16908  -0.01690 -0.16381 156 PRO   A N    
294  C  CA   . PRO   A 51  ? 0.77333 0.94310 0.79280 0.15644  -0.00931 -0.17530 156 PRO   A CA   
295  C  C    . PRO   A 51  ? 0.83065 1.02579 0.85202 0.17343  0.00060  -0.20598 156 PRO   A C    
296  O  O    . PRO   A 51  ? 0.89542 1.07220 0.93169 0.19524  -0.00309 -0.22502 156 PRO   A O    
297  C  CB   . PRO   A 51  ? 0.74612 0.86063 0.75113 0.14696  -0.02100 -0.17399 156 PRO   A CB   
298  C  CG   . PRO   A 51  ? 0.78223 0.86192 0.80184 0.15131  -0.03362 -0.15706 156 PRO   A CG   
299  C  CD   . PRO   A 51  ? 0.79485 0.89946 0.84003 0.17189  -0.03186 -0.15859 156 PRO   A CD   
300  N  N    . VAL   A 52  ? 0.82454 1.06302 0.83102 0.16360  0.01329  -0.21055 157 VAL   A N    
301  C  CA   . VAL   A 52  ? 0.85559 1.12749 0.85896 0.17661  0.02509  -0.24002 157 VAL   A CA   
302  C  C    . VAL   A 52  ? 0.90417 1.17390 0.87592 0.16078  0.02721  -0.24910 157 VAL   A C    
303  O  O    . VAL   A 52  ? 0.90327 1.19746 0.85858 0.14043  0.03177  -0.23127 157 VAL   A O    
304  C  CB   . VAL   A 52  ? 0.80221 1.13998 0.81743 0.17959  0.03981  -0.23683 157 VAL   A CB   
305  C  CG1  . VAL   A 52  ? 0.79330 1.16381 0.81471 0.20110  0.05126  -0.27076 157 VAL   A CG1  
306  C  CG2  . VAL   A 52  ? 0.76018 1.10258 0.80316 0.18473  0.03528  -0.21648 157 VAL   A CG2  
307  N  N    . ARG   A 53  ? 0.96267 1.20239 0.92675 0.16981  0.02284  -0.27643 158 ARG   A N    
308  C  CA   . ARG   A 53  ? 0.99131 1.23142 0.92569 0.15652  0.02386  -0.29019 158 ARG   A CA   
309  C  C    . ARG   A 53  ? 1.08884 1.36141 1.01805 0.17235  0.03526  -0.32739 158 ARG   A C    
310  O  O    . ARG   A 53  ? 1.13162 1.39293 1.08073 0.19650  0.03554  -0.35092 158 ARG   A O    
311  C  CB   . ARG   A 53  ? 0.96882 1.14586 0.89587 0.14948  0.00816  -0.29273 158 ARG   A CB   
312  C  CG   . ARG   A 53  ? 0.91283 1.06112 0.84144 0.13190  -0.00216 -0.25773 158 ARG   A CG   
313  C  CD   . ARG   A 53  ? 0.92644 1.01097 0.85871 0.13114  -0.01745 -0.26024 158 ARG   A CD   
314  N  NE   . ARG   A 53  ? 0.89277 0.95491 0.82326 0.11252  -0.02597 -0.22891 158 ARG   A NE   
315  C  CZ   . ARG   A 53  ? 0.90355 0.94009 0.85127 0.11563  -0.03320 -0.20936 158 ARG   A CZ   
316  N  NH1  . ARG   A 53  ? 0.89214 0.92108 0.86130 0.13690  -0.03430 -0.21575 158 ARG   A NH1  
317  N  NH2  . ARG   A 53  ? 0.88695 0.90820 0.83071 0.09799  -0.03939 -0.18350 158 ARG   A NH2  
318  N  N    . MET   A 54  ? 1.13932 1.45356 1.04205 0.15926  0.04453  -0.33254 159 MET   A N    
319  C  CA   . MET   A 54  ? 1.21319 1.56802 1.10620 0.17171  0.05737  -0.36799 159 MET   A CA   
320  C  C    . MET   A 54  ? 1.25058 1.56230 1.14267 0.18645  0.05009  -0.40662 159 MET   A C    
321  O  O    . MET   A 54  ? 1.26233 1.56749 1.17686 0.21209  0.05273  -0.43145 159 MET   A O    
322  C  CB   . MET   A 54  ? 1.25027 1.65282 1.10973 0.15104  0.06570  -0.36298 159 MET   A CB   
323  C  CG   . MET   A 54  ? 1.32584 1.77523 1.17225 0.16054  0.07942  -0.39661 159 MET   A CG   
324  S  SD   . MET   A 54  ? 1.36342 1.84554 1.16977 0.13217  0.08084  -0.38612 159 MET   A SD   
325  C  CE   . MET   A 54  ? 1.42527 1.90664 1.22576 0.14405  0.08346  -0.42850 159 MET   A CE   
326  N  N    . SER   A 66  ? 1.34045 1.97721 1.12401 0.05452  0.10220  -0.23266 218 SER   A N    
327  C  CA   . SER   A 66  ? 1.32360 2.00500 1.12668 0.05750  0.11559  -0.22433 218 SER   A CA   
328  C  C    . SER   A 66  ? 1.25072 1.92415 1.07913 0.05856  0.11642  -0.20293 218 SER   A C    
329  O  O    . SER   A 66  ? 1.22628 1.90667 1.05272 0.03972  0.11504  -0.16845 218 SER   A O    
330  C  CB   . SER   A 66  ? 1.36330 2.06046 1.17585 0.07831  0.12360  -0.26125 218 SER   A CB   
331  O  OG   . SER   A 66  ? 1.37290 2.11875 1.20276 0.07981  0.13629  -0.25417 218 SER   A OG   
332  N  N    . PRO   A 67  ? 1.18476 1.84215 1.03786 0.07943  0.11744  -0.22079 219 PRO   A N    
333  C  CA   . PRO   A 67  ? 1.08048 1.72428 0.96239 0.07599  0.11385  -0.19360 219 PRO   A CA   
334  C  C    . PRO   A 67  ? 0.99266 1.57052 0.87686 0.06919  0.09582  -0.17714 219 PRO   A C    
335  O  O    . PRO   A 67  ? 1.00427 1.53994 0.87722 0.07387  0.08550  -0.19240 219 PRO   A O    
336  C  CB   . PRO   A 67  ? 1.07682 1.72833 0.98859 0.10129  0.11908  -0.21706 219 PRO   A CB   
337  C  CG   . PRO   A 67  ? 1.13179 1.74997 1.03418 0.11859  0.11347  -0.25198 219 PRO   A CG   
338  C  CD   . PRO   A 67  ? 1.19482 1.82815 1.05851 0.10533  0.11572  -0.25956 219 PRO   A CD   
339  N  N    . LEU   A 68  ? 0.85163 1.42259 0.75121 0.05688  0.09239  -0.14587 220 LEU   A N    
340  C  CA   . LEU   A 68  ? 0.72182 1.23597 0.62714 0.05085  0.07702  -0.12950 220 LEU   A CA   
341  C  C    . LEU   A 68  ? 0.63665 1.11918 0.56733 0.06944  0.07083  -0.14154 220 LEU   A C    
342  O  O    . LEU   A 68  ? 0.61721 1.09179 0.56949 0.06813  0.06751  -0.12531 220 LEU   A O    
343  C  CB   . LEU   A 68  ? 0.67356 1.19345 0.58457 0.03073  0.07603  -0.09414 220 LEU   A CB   
344  C  CG   . LEU   A 68  ? 0.69815 1.24502 0.58605 0.01154  0.07986  -0.07608 220 LEU   A CG   
345  C  CD1  . LEU   A 68  ? 0.69314 1.22719 0.59049 -0.00630 0.07470  -0.04190 220 LEU   A CD1  
346  C  CD2  . LEU   A 68  ? 0.68823 1.21651 0.54821 0.01025  0.07288  -0.08781 220 LEU   A CD2  
347  N  N    . SER   A 69  ? 0.64932 1.11284 0.57671 0.08678  0.06836  -0.17079 221 SER   A N    
348  C  CA   . SER   A 69  ? 0.66974 1.11008 0.62175 0.10808  0.06375  -0.18511 221 SER   A CA   
349  C  C    . SER   A 69  ? 0.65488 1.03934 0.61582 0.10535  0.04831  -0.16988 221 SER   A C    
350  O  O    . SER   A 69  ? 0.65212 1.02285 0.63632 0.11892  0.04368  -0.17053 221 SER   A O    
351  C  CB   . SER   A 69  ? 0.73679 1.16859 0.68299 0.12721  0.06492  -0.22148 221 SER   A CB   
352  O  OG   . SER   A 69  ? 0.77752 1.17675 0.69827 0.11809  0.05711  -0.22840 221 SER   A OG   
353  N  N    . MET   A 70  ? 0.60866 0.96361 0.55211 0.08864  0.04021  -0.15619 222 MET   A N    
354  C  CA   . MET   A 70  ? 0.61177 0.91803 0.56196 0.08463  0.02688  -0.14191 222 MET   A CA   
355  C  C    . MET   A 70  ? 0.52034 0.83402 0.48142 0.07169  0.02619  -0.11357 222 MET   A C    
356  O  O    . MET   A 70  ? 0.55771 0.83689 0.52459 0.06796  0.01636  -0.10134 222 MET   A O    
357  C  CB   . MET   A 70  ? 0.65365 0.92558 0.58253 0.07339  0.01832  -0.14256 222 MET   A CB   
358  C  CG   . MET   A 70  ? 0.68050 0.91996 0.60473 0.08562  0.01224  -0.16875 222 MET   A CG   
359  S  SD   . MET   A 70  ? 0.70015 0.90357 0.65088 0.10597  0.00427  -0.17453 222 MET   A SD   
360  C  CE   . MET   A 70  ? 0.72588 0.86752 0.66869 0.09588  -0.01142 -0.16833 222 MET   A CE   
361  N  N    . LEU   A 71  ? 0.48591 0.84392 0.44981 0.06391  0.03641  -0.10334 223 LEU   A N    
362  C  CA   . LEU   A 71  ? 0.46323 0.82550 0.43688 0.04925  0.03526  -0.07749 223 LEU   A CA   
363  C  C    . LEU   A 71  ? 0.43976 0.79189 0.43727 0.05710  0.02996  -0.07321 223 LEU   A C    
364  O  O    . LEU   A 71  ? 0.42349 0.75117 0.42427 0.04757  0.02230  -0.05745 223 LEU   A O    
365  C  CB   . LEU   A 71  ? 0.49307 0.90465 0.46575 0.03806  0.04717  -0.06701 223 LEU   A CB   
366  C  CG   . LEU   A 71  ? 0.47644 0.89163 0.45966 0.02089  0.04617  -0.04076 223 LEU   A CG   
367  C  CD1  . LEU   A 71  ? 0.47841 0.85062 0.45309 0.01061  0.03552  -0.02802 223 LEU   A CD1  
368  C  CD2  . LEU   A 71  ? 0.47731 0.93647 0.45625 0.00713  0.05699  -0.02803 223 LEU   A CD2  
369  N  N    . PRO   A 72  ? 0.45139 0.82293 0.46643 0.07428  0.03315  -0.08640 224 PRO   A N    
370  C  CA   . PRO   A 72  ? 0.47126 0.83253 0.50815 0.08126  0.02553  -0.08014 224 PRO   A CA   
371  C  C    . PRO   A 72  ? 0.46602 0.77421 0.49782 0.08343  0.01190  -0.07746 224 PRO   A C    
372  O  O    . PRO   A 72  ? 0.44233 0.73582 0.47871 0.07440  0.00502  -0.06163 224 PRO   A O    
373  C  CB   . PRO   A 72  ? 0.48733 0.87780 0.54295 0.10293  0.03075  -0.09816 224 PRO   A CB   
374  C  CG   . PRO   A 72  ? 0.47129 0.90416 0.51819 0.10062  0.04515  -0.10766 224 PRO   A CG   
375  C  CD   . PRO   A 72  ? 0.42047 0.82974 0.43827 0.08801  0.04407  -0.10658 224 PRO   A CD   
376  N  N    . HIS   A 73  ? 0.50884 0.78841 0.53041 0.09360  0.00802  -0.09281 225 HIS   A N    
377  C  CA   . HIS   A 73  ? 0.53680 0.76692 0.55476 0.09462  -0.00481 -0.08897 225 HIS   A CA   
378  C  C    . HIS   A 73  ? 0.53181 0.74181 0.53461 0.07393  -0.00852 -0.07242 225 HIS   A C    
379  O  O    . HIS   A 73  ? 0.53563 0.72083 0.54077 0.06925  -0.01701 -0.06016 225 HIS   A O    
380  C  CB   . HIS   A 73  ? 0.54372 0.74639 0.55492 0.10765  -0.00816 -0.10951 225 HIS   A CB   
381  C  CG   . HIS   A 73  ? 0.58397 0.73532 0.58929 0.10457  -0.02085 -0.10384 225 HIS   A CG   
382  N  ND1  . HIS   A 73  ? 0.60194 0.72901 0.62131 0.11515  -0.03081 -0.09841 225 HIS   A ND1  
383  C  CD2  . HIS   A 73  ? 0.58602 0.70857 0.57360 0.09104  -0.02535 -0.10109 225 HIS   A CD2  
384  C  CE1  . HIS   A 73  ? 0.61362 0.69848 0.62309 0.10730  -0.04020 -0.09198 225 HIS   A CE1  
385  N  NE2  . HIS   A 73  ? 0.58327 0.66538 0.57442 0.09263  -0.03685 -0.09423 225 HIS   A NE2  
386  N  N    . LEU   A 74  ? 0.50741 0.72969 0.49487 0.06192  -0.00243 -0.07168 226 LEU   A N    
387  C  CA   . LEU   A 74  ? 0.49963 0.70328 0.47537 0.04464  -0.00641 -0.05707 226 LEU   A CA   
388  C  C    . LEU   A 74  ? 0.49410 0.71145 0.47925 0.03330  -0.00503 -0.03849 226 LEU   A C    
389  O  O    . LEU   A 74  ? 0.44973 0.64592 0.43243 0.02340  -0.01052 -0.02698 226 LEU   A O    
390  C  CB   . LEU   A 74  ? 0.54115 0.75347 0.49829 0.03646  -0.00228 -0.06131 226 LEU   A CB   
391  C  CG   . LEU   A 74  ? 0.60745 0.79981 0.55327 0.04468  -0.00572 -0.08146 226 LEU   A CG   
392  C  CD1  . LEU   A 74  ? 0.59566 0.80271 0.52162 0.03582  -0.00224 -0.08634 226 LEU   A CD1  
393  C  CD2  . LEU   A 74  ? 0.57111 0.71801 0.51706 0.04378  -0.01714 -0.07938 226 LEU   A CD2  
394  N  N    . ALA   A 75  ? 0.50203 0.75523 0.49907 0.03426  0.00235  -0.03649 227 ALA   A N    
395  C  CA   . ALA   A 75  ? 0.45486 0.71895 0.46406 0.02372  0.00246  -0.02115 227 ALA   A CA   
396  C  C    . ALA   A 75  ? 0.47792 0.72035 0.49609 0.02758  -0.00677 -0.01792 227 ALA   A C    
397  O  O    . ALA   A 75  ? 0.44238 0.67121 0.46029 0.01658  -0.01078 -0.00702 227 ALA   A O    
398  C  CB   . ALA   A 75  ? 0.38521 0.69318 0.40836 0.02426  0.01139  -0.02088 227 ALA   A CB   
399  N  N    . ASP   A 76  ? 0.47238 0.71203 0.49848 0.04377  -0.01049 -0.02748 228 ASP   A N    
400  C  CA   . ASP   A 76  ? 0.47654 0.69608 0.50900 0.04797  -0.02058 -0.02251 228 ASP   A CA   
401  C  C    . ASP   A 76  ? 0.50298 0.68306 0.52021 0.04146  -0.02752 -0.01789 228 ASP   A C    
402  O  O    . ASP   A 76  ? 0.48673 0.65481 0.50389 0.03470  -0.03337 -0.00804 228 ASP   A O    
403  C  CB   . ASP   A 76  ? 0.46964 0.69206 0.51455 0.06838  -0.02420 -0.03245 228 ASP   A CB   
404  C  CG   . ASP   A 76  ? 0.50006 0.76630 0.56516 0.07489  -0.01866 -0.03508 228 ASP   A CG   
405  O  OD1  . ASP   A 76  ? 0.47407 0.76404 0.54494 0.06154  -0.01483 -0.02610 228 ASP   A OD1  
406  O  OD2  . ASP   A 76  ? 0.53421 0.81134 0.61123 0.09341  -0.01826 -0.04665 228 ASP   A OD2  
407  N  N    . LEU   A 77  ? 0.52213 0.68449 0.52639 0.04266  -0.02684 -0.02567 229 LEU   A N    
408  C  CA   . LEU   A 77  ? 0.49628 0.62540 0.48760 0.03435  -0.03276 -0.02098 229 LEU   A CA   
409  C  C    . LEU   A 77  ? 0.45024 0.58277 0.43774 0.01796  -0.03083 -0.00890 229 LEU   A C    
410  O  O    . LEU   A 77  ? 0.45895 0.57594 0.44492 0.01169  -0.03584 -0.00066 229 LEU   A O    
411  C  CB   . LEU   A 77  ? 0.46555 0.58087 0.44471 0.03626  -0.03208 -0.03276 229 LEU   A CB   
412  C  CG   . LEU   A 77  ? 0.52332 0.61081 0.48974 0.02494  -0.03702 -0.02865 229 LEU   A CG   
413  C  CD1  . LEU   A 77  ? 0.54318 0.60230 0.51146 0.02468  -0.04592 -0.02088 229 LEU   A CD1  
414  C  CD2  . LEU   A 77  ? 0.55058 0.62870 0.50629 0.02703  -0.03704 -0.04311 229 LEU   A CD2  
415  N  N    . VAL   A 78  ? 0.43709 0.59087 0.42363 0.01122  -0.02351 -0.00752 230 VAL   A N    
416  C  CA   . VAL   A 78  ? 0.40101 0.55657 0.38721 -0.00266 -0.02195 0.00364  230 VAL   A CA   
417  C  C    . VAL   A 78  ? 0.45070 0.61066 0.44815 -0.00607 -0.02394 0.01026  230 VAL   A C    
418  O  O    . VAL   A 78  ? 0.44500 0.59153 0.44081 -0.01362 -0.02692 0.01591  230 VAL   A O    
419  C  CB   . VAL   A 78  ? 0.41591 0.59468 0.40119 -0.00842 -0.01454 0.00638  230 VAL   A CB   
420  C  CG1  . VAL   A 78  ? 0.43019 0.60956 0.42043 -0.02103 -0.01367 0.01877  230 VAL   A CG1  
421  C  CG2  . VAL   A 78  ? 0.46761 0.64191 0.43817 -0.00761 -0.01403 0.00024  230 VAL   A CG2  
422  N  N    . SER   A 79  ? 0.48815 0.66993 0.49761 -0.00069 -0.02224 0.00839  231 SER   A N    
423  C  CA   . SER   A 79  ? 0.43857 0.62847 0.45899 -0.00482 -0.02505 0.01317  231 SER   A CA   
424  C  C    . SER   A 79  ? 0.44040 0.60914 0.45564 -0.00300 -0.03334 0.01491  231 SER   A C    
425  O  O    . SER   A 79  ? 0.48122 0.64730 0.49702 -0.01161 -0.03556 0.01921  231 SER   A O    
426  C  CB   . SER   A 79  ? 0.40811 0.62729 0.44347 0.00233  -0.02324 0.00992  231 SER   A CB   
427  O  OG   . SER   A 79  ? 0.43261 0.66782 0.48005 -0.00701 -0.02368 0.01473  231 SER   A OG   
428  N  N    . TYR   A 80  ? 0.42728 0.58088 0.43733 0.00775  -0.03798 0.01147  232 TYR   A N    
429  C  CA   . TYR   A 80  ? 0.42303 0.55578 0.42683 0.00859  -0.04622 0.01616  232 TYR   A CA   
430  C  C    . TYR   A 80  ? 0.44896 0.56447 0.44142 -0.00367 -0.04583 0.02074  232 TYR   A C    
431  O  O    . TYR   A 80  ? 0.39765 0.51059 0.38727 -0.00996 -0.04904 0.02602  232 TYR   A O    
432  C  CB   . TYR   A 80  ? 0.47598 0.59133 0.47787 0.02185  -0.05114 0.01210  232 TYR   A CB   
433  C  CG   . TYR   A 80  ? 0.58025 0.67042 0.57505 0.02216  -0.06027 0.01968  232 TYR   A CG   
434  C  CD1  . TYR   A 80  ? 0.56219 0.65768 0.56209 0.02675  -0.06782 0.02697  232 TYR   A CD1  
435  C  CD2  . TYR   A 80  ? 0.60771 0.67077 0.59086 0.01686  -0.06189 0.02084  232 TYR   A CD2  
436  C  CE1  . TYR   A 80  ? 0.61825 0.69183 0.61020 0.02590  -0.07648 0.03695  232 TYR   A CE1  
437  C  CE2  . TYR   A 80  ? 0.62762 0.66847 0.60448 0.01506  -0.06990 0.03004  232 TYR   A CE2  
438  C  CZ   . TYR   A 80  ? 0.66674 0.71247 0.64724 0.01956  -0.07704 0.03891  232 TYR   A CZ   
439  O  OH   . TYR   A 80  ? 0.71984 0.74453 0.69261 0.01651  -0.08525 0.05099  232 TYR   A OH   
440  N  N    . SER   A 81  ? 0.44710 0.55413 0.43323 -0.00714 -0.04185 0.01822  233 SER   A N    
441  C  CA   . SER   A 81  ? 0.49955 0.59329 0.47786 -0.01751 -0.04165 0.02229  233 SER   A CA   
442  C  C    . SER   A 81  ? 0.45994 0.56559 0.44373 -0.02667 -0.03754 0.02510  233 SER   A C    
443  O  O    . SER   A 81  ? 0.45378 0.55280 0.43434 -0.03355 -0.03809 0.02782  233 SER   A O    
444  C  CB   . SER   A 81  ? 0.63386 0.71795 0.60525 -0.01873 -0.04003 0.01893  233 SER   A CB   
445  O  OG   . SER   A 81  ? 0.76409 0.83184 0.73068 -0.01132 -0.04471 0.01438  233 SER   A OG   
446  N  N    . ILE   A 82  ? 0.40520 0.52840 0.39824 -0.02724 -0.03323 0.02417  234 ILE   A N    
447  C  CA   . ILE   A 82  ? 0.40952 0.54007 0.41043 -0.03589 -0.03069 0.02620  234 ILE   A CA   
448  C  C    . ILE   A 82  ? 0.47462 0.60593 0.47566 -0.03796 -0.03474 0.02538  234 ILE   A C    
449  O  O    . ILE   A 82  ? 0.51993 0.64717 0.52042 -0.04478 -0.03402 0.02473  234 ILE   A O    
450  C  CB   . ILE   A 82  ? 0.43353 0.58276 0.44580 -0.03765 -0.02634 0.02703  234 ILE   A CB   
451  C  CG1  . ILE   A 82  ? 0.43400 0.58550 0.44287 -0.03724 -0.02216 0.02939  234 ILE   A CG1  
452  C  CG2  . ILE   A 82  ? 0.45120 0.60365 0.47393 -0.04723 -0.02499 0.02832  234 ILE   A CG2  
453  C  CD1  . ILE   A 82  ? 0.41541 0.58815 0.43390 -0.04049 -0.01708 0.03289  234 ILE   A CD1  
454  N  N    . GLN   A 83  ? 0.41353 0.55151 0.41503 -0.03140 -0.03937 0.02502  235 GLN   A N    
455  C  CA   . GLN   A 83  ? 0.43663 0.57805 0.43545 -0.03339 -0.04474 0.02579  235 GLN   A CA   
456  C  C    . GLN   A 83  ? 0.43681 0.56216 0.42229 -0.03681 -0.04660 0.02891  235 GLN   A C    
457  O  O    . GLN   A 83  ? 0.34959 0.47847 0.33142 -0.04397 -0.04658 0.02773  235 GLN   A O    
458  C  CB   . GLN   A 83  ? 0.46177 0.61274 0.46402 -0.02366 -0.05098 0.02732  235 GLN   A CB   
459  C  CG   . GLN   A 83  ? 0.44113 0.61555 0.45891 -0.02136 -0.04910 0.02413  235 GLN   A CG   
460  C  CD   . GLN   A 83  ? 0.54547 0.73415 0.56970 -0.01158 -0.05645 0.02558  235 GLN   A CD   
461  O  OE1  . GLN   A 83  ? 0.51831 0.71605 0.54183 -0.01459 -0.06285 0.02760  235 GLN   A OE1  
462  N  NE2  . GLN   A 83  ? 0.59226 0.78489 0.62323 0.00088  -0.05591 0.02390  235 GLN   A NE2  
463  N  N    . LYS   A 84  ? 0.50210 0.61114 0.48048 -0.03257 -0.04789 0.03200  236 LYS   A N    
464  C  CA   . LYS   A 84  ? 0.44879 0.54391 0.41596 -0.03779 -0.04923 0.03642  236 LYS   A CA   
465  C  C    . LYS   A 84  ? 0.42860 0.52528 0.39679 -0.04641 -0.04295 0.03353  236 LYS   A C    
466  O  O    . LYS   A 84  ? 0.43348 0.53135 0.39570 -0.05282 -0.04227 0.03475  236 LYS   A O    
467  C  CB   . LYS   A 84  ? 0.45540 0.53133 0.41760 -0.03306 -0.05208 0.03891  236 LYS   A CB   
468  C  CG   . LYS   A 84  ? 0.49156 0.56183 0.45474 -0.02241 -0.05911 0.04138  236 LYS   A CG   
469  C  CD   . LYS   A 84  ? 0.49912 0.57485 0.45810 -0.02349 -0.06540 0.04932  236 LYS   A CD   
470  C  CE   . LYS   A 84  ? 0.58539 0.64766 0.54449 -0.01313 -0.07453 0.05590  236 LYS   A CE   
471  N  NZ   . LYS   A 84  ? 0.63780 0.67160 0.59074 -0.01403 -0.07706 0.05944  236 LYS   A NZ   
472  N  N    . VAL   A 85  ? 0.43015 0.52867 0.40643 -0.04624 -0.03831 0.03021  237 VAL   A N    
473  C  CA   . VAL   A 85  ? 0.44966 0.54874 0.43032 -0.05221 -0.03340 0.02842  237 VAL   A CA   
474  C  C    . VAL   A 85  ? 0.43180 0.54066 0.41781 -0.05669 -0.03139 0.02338  237 VAL   A C    
475  O  O    . VAL   A 85  ? 0.41341 0.52319 0.39878 -0.06106 -0.02865 0.02059  237 VAL   A O    
476  C  CB   . VAL   A 85  ? 0.37844 0.47796 0.36654 -0.05076 -0.03042 0.02880  237 VAL   A CB   
477  C  CG1  . VAL   A 85  ? 0.40076 0.50184 0.39822 -0.05518 -0.02652 0.02798  237 VAL   A CG1  
478  C  CG2  . VAL   A 85  ? 0.38666 0.47724 0.36726 -0.04826 -0.03227 0.03086  237 VAL   A CG2  
479  N  N    . ILE   A 86  ? 0.39146 0.50954 0.38363 -0.05592 -0.03260 0.02069  238 ILE   A N    
480  C  CA   . ILE   A 86  ? 0.39284 0.52007 0.38956 -0.06117 -0.03202 0.01351  238 ILE   A CA   
481  C  C    . ILE   A 86  ? 0.38072 0.51219 0.36434 -0.06384 -0.03425 0.01238  238 ILE   A C    
482  O  O    . ILE   A 86  ? 0.44475 0.58089 0.42807 -0.06880 -0.03114 0.00483  238 ILE   A O    
483  C  CB   . ILE   A 86  ? 0.42914 0.56814 0.43447 -0.06108 -0.03458 0.01174  238 ILE   A CB   
484  C  CG1  . ILE   A 86  ? 0.42057 0.55882 0.43854 -0.06076 -0.03113 0.01439  238 ILE   A CG1  
485  C  CG2  . ILE   A 86  ? 0.43381 0.58266 0.44271 -0.06798 -0.03555 0.00231  238 ILE   A CG2  
486  C  CD1  . ILE   A 86  ? 0.41312 0.56670 0.43938 -0.05974 -0.03301 0.01530  238 ILE   A CD1  
487  N  N    . GLY   A 87  ? 0.36654 0.49704 0.33934 -0.06044 -0.03969 0.01995  239 GLY   A N    
488  C  CA   . GLY   A 87  ? 0.37732 0.51326 0.33596 -0.06415 -0.04259 0.02273  239 GLY   A CA   
489  C  C    . GLY   A 87  ? 0.42945 0.56131 0.38210 -0.06919 -0.03741 0.02307  239 GLY   A C    
490  O  O    . GLY   A 87  ? 0.44266 0.58622 0.38794 -0.07507 -0.03513 0.01896  239 GLY   A O    
491  N  N    . PHE   A 88  ? 0.39962 0.51824 0.35564 -0.06734 -0.03533 0.02710  240 PHE   A N    
492  C  CA   . PHE   A 88  ? 0.40314 0.52132 0.35774 -0.07230 -0.03028 0.02720  240 PHE   A CA   
493  C  C    . PHE   A 88  ? 0.41675 0.54499 0.38159 -0.07419 -0.02346 0.01545  240 PHE   A C    
494  O  O    . PHE   A 88  ? 0.40236 0.54220 0.36311 -0.07888 -0.01917 0.01097  240 PHE   A O    
495  C  CB   . PHE   A 88  ? 0.37631 0.48055 0.33492 -0.07009 -0.03060 0.03214  240 PHE   A CB   
496  C  CG   . PHE   A 88  ? 0.43207 0.53896 0.39315 -0.07519 -0.02605 0.03237  240 PHE   A CG   
497  C  CD1  . PHE   A 88  ? 0.45487 0.56189 0.40606 -0.08193 -0.02686 0.03966  240 PHE   A CD1  
498  C  CD2  . PHE   A 88  ? 0.41581 0.52604 0.39075 -0.07348 -0.02154 0.02684  240 PHE   A CD2  
499  C  CE1  . PHE   A 88  ? 0.49025 0.60420 0.44603 -0.08749 -0.02240 0.03997  240 PHE   A CE1  
500  C  CE2  . PHE   A 88  ? 0.44595 0.56235 0.42614 -0.07702 -0.01792 0.02713  240 PHE   A CE2  
501  C  CZ   . PHE   A 88  ? 0.47653 0.59643 0.44749 -0.08430 -0.01797 0.03300  240 PHE   A CZ   
502  N  N    . ALA   A 89  ? 0.41673 0.54103 0.39568 -0.07055 -0.02228 0.01030  241 ALA   A N    
503  C  CA   . ALA   A 89  ? 0.40371 0.53170 0.39617 -0.07104 -0.01683 -0.00043 241 ALA   A CA   
504  C  C    . ALA   A 89  ? 0.43289 0.57404 0.42082 -0.07502 -0.01503 -0.01209 241 ALA   A C    
505  O  O    . ALA   A 89  ? 0.41650 0.56466 0.40919 -0.07602 -0.00922 -0.02198 241 ALA   A O    
506  C  CB   . ALA   A 89  ? 0.41078 0.53089 0.41817 -0.06817 -0.01753 -0.00100 241 ALA   A CB   
507  N  N    . LYS   A 90  ? 0.45526 0.60246 0.43430 -0.07690 -0.02011 -0.01212 242 LYS   A N    
508  C  CA   . LYS   A 90  ? 0.43562 0.59816 0.40834 -0.08171 -0.01962 -0.02431 242 LYS   A CA   
509  C  C    . LYS   A 90  ? 0.45819 0.63459 0.41624 -0.08575 -0.01559 -0.02543 242 LYS   A C    
510  O  O    . LYS   A 90  ? 0.49450 0.68605 0.44856 -0.08952 -0.01216 -0.03961 242 LYS   A O    
511  C  CB   . LYS   A 90  ? 0.43591 0.60589 0.40100 -0.08300 -0.02764 -0.02104 242 LYS   A CB   
512  C  CG   . LYS   A 90  ? 0.48531 0.65015 0.46667 -0.08182 -0.03017 -0.02432 242 LYS   A CG   
513  C  CD   . LYS   A 90  ? 0.54685 0.72221 0.52295 -0.08143 -0.03856 -0.01831 242 LYS   A CD   
514  C  CE   . LYS   A 90  ? 0.54034 0.73545 0.50268 -0.08716 -0.04259 -0.02519 242 LYS   A CE   
515  N  NZ   . LYS   A 90  ? 0.61094 0.81972 0.57493 -0.08722 -0.05162 -0.02239 242 LYS   A NZ   
516  N  N    . MET   A 91  ? 0.43172 0.60452 0.38187 -0.08602 -0.01564 -0.01161 243 MET   A N    
517  C  CA   . MET   A 91  ? 0.50152 0.68936 0.43799 -0.09193 -0.01153 -0.00909 243 MET   A CA   
518  C  C    . MET   A 91  ? 0.48259 0.67363 0.43063 -0.09141 -0.00272 -0.01428 243 MET   A C    
519  O  O    . MET   A 91  ? 0.46434 0.67247 0.40358 -0.09704 0.00249  -0.01339 243 MET   A O    
520  C  CB   . MET   A 91  ? 0.57018 0.75212 0.49168 -0.09466 -0.01797 0.01087  243 MET   A CB   
521  C  CG   . MET   A 91  ? 0.61921 0.80102 0.53065 -0.09352 -0.02753 0.01743  243 MET   A CG   
522  S  SD   . MET   A 91  ? 0.69437 0.86945 0.58817 -0.09680 -0.03555 0.04109  243 MET   A SD   
523  C  CE   . MET   A 91  ? 0.62340 0.77087 0.52958 -0.08627 -0.04273 0.04802  243 MET   A CE   
524  N  N    . ILE   A 92  ? 0.45045 0.62824 0.41843 -0.08507 -0.00117 -0.01830 244 ILE   A N    
525  C  CA   . ILE   A 92  ? 0.48217 0.66564 0.46483 -0.08280 0.00623  -0.02380 244 ILE   A CA   
526  C  C    . ILE   A 92  ? 0.49547 0.69752 0.48179 -0.08274 0.01403  -0.04333 244 ILE   A C    
527  O  O    . ILE   A 92  ? 0.43978 0.63806 0.43106 -0.08063 0.01321  -0.05660 244 ILE   A O    
528  C  CB   . ILE   A 92  ? 0.45291 0.61873 0.45603 -0.07548 0.00453  -0.02251 244 ILE   A CB   
529  C  CG1  . ILE   A 92  ? 0.39365 0.54484 0.39165 -0.07559 -0.00211 -0.00594 244 ILE   A CG1  
530  C  CG2  . ILE   A 92  ? 0.43964 0.61369 0.46139 -0.07125 0.01116  -0.02926 244 ILE   A CG2  
531  C  CD1  . ILE   A 92  ? 0.35312 0.48938 0.36628 -0.06956 -0.00487 -0.00318 244 ILE   A CD1  
532  N  N    . PRO   A 93  ? 0.53819 0.76163 0.52327 -0.08538 0.02192  -0.04712 245 PRO   A N    
533  C  CA   . PRO   A 93  ? 0.53623 0.78070 0.52426 -0.08434 0.03059  -0.06902 245 PRO   A CA   
534  C  C    . PRO   A 93  ? 0.56649 0.79763 0.58097 -0.07410 0.03246  -0.08562 245 PRO   A C    
535  O  O    . PRO   A 93  ? 0.62134 0.84226 0.65683 -0.06707 0.03280  -0.08143 245 PRO   A O    
536  C  CB   . PRO   A 93  ? 0.52369 0.79410 0.51101 -0.08790 0.03932  -0.06679 245 PRO   A CB   
537  C  CG   . PRO   A 93  ? 0.55821 0.82261 0.53108 -0.09603 0.03332  -0.04195 245 PRO   A CG   
538  C  CD   . PRO   A 93  ? 0.52237 0.75429 0.50222 -0.09085 0.02340  -0.03218 245 PRO   A CD   
539  N  N    . GLY   A 94  ? 0.57695 0.80750 0.59064 -0.07388 0.03253  -0.10382 246 GLY   A N    
540  C  CA   . GLY   A 94  ? 0.58720 0.80153 0.62603 -0.06564 0.03343  -0.12058 246 GLY   A CA   
541  C  C    . GLY   A 94  ? 0.57829 0.76376 0.62507 -0.06530 0.02415  -0.11277 246 GLY   A C    
542  O  O    . GLY   A 94  ? 0.57956 0.75041 0.64386 -0.06196 0.02354  -0.12713 246 GLY   A O    
543  N  N    . PHE   A 95  ? 0.55421 0.73161 0.58954 -0.06899 0.01720  -0.09104 247 PHE   A N    
544  C  CA   . PHE   A 95  ? 0.56410 0.71891 0.60802 -0.06860 0.00976  -0.08241 247 PHE   A CA   
545  C  C    . PHE   A 95  ? 0.62647 0.77852 0.67071 -0.07315 0.00681  -0.09714 247 PHE   A C    
546  O  O    . PHE   A 95  ? 0.62920 0.76293 0.69253 -0.07188 0.00453  -0.10128 247 PHE   A O    
547  C  CB   . PHE   A 95  ? 0.52821 0.68029 0.55692 -0.07150 0.00374  -0.06079 247 PHE   A CB   
548  C  CG   . PHE   A 95  ? 0.53446 0.66880 0.57194 -0.07069 -0.00229 -0.05116 247 PHE   A CG   
549  C  CD1  . PHE   A 95  ? 0.51916 0.63968 0.57279 -0.06574 -0.00260 -0.04214 247 PHE   A CD1  
550  C  CD2  . PHE   A 95  ? 0.50293 0.63824 0.53275 -0.07527 -0.00767 -0.05047 247 PHE   A CD2  
551  C  CE1  . PHE   A 95  ? 0.52269 0.63112 0.58267 -0.06625 -0.00714 -0.03233 247 PHE   A CE1  
552  C  CE2  . PHE   A 95  ? 0.47353 0.59760 0.51237 -0.07525 -0.01188 -0.04170 247 PHE   A CE2  
553  C  CZ   . PHE   A 95  ? 0.48990 0.60074 0.54285 -0.07119 -0.01108 -0.03251 247 PHE   A CZ   
554  N  N    . ARG   A 96  ? 0.68285 0.85386 0.70632 -0.07961 0.00618  -0.10446 248 ARG   A N    
555  C  CA   . ARG   A 96  ? 0.74018 0.91289 0.76211 -0.08560 0.00199  -0.11896 248 ARG   A CA   
556  C  C    . ARG   A 96  ? 0.71271 0.88262 0.74975 -0.08422 0.00695  -0.14611 248 ARG   A C    
557  O  O    . ARG   A 96  ? 0.72393 0.89184 0.76343 -0.09012 0.00298  -0.16068 248 ARG   A O    
558  C  CB   . ARG   A 96  ? 0.85212 1.04907 0.84620 -0.09280 -0.00152 -0.11770 248 ARG   A CB   
559  C  CG   . ARG   A 96  ? 0.96628 1.16015 0.95359 -0.09540 -0.01092 -0.09955 248 ARG   A CG   
560  C  CD   . ARG   A 96  ? 1.10873 1.28976 1.11396 -0.09819 -0.01618 -0.10549 248 ARG   A CD   
561  N  NE   . ARG   A 96  ? 1.19385 1.38723 1.19624 -0.10585 -0.01891 -0.12665 248 ARG   A NE   
562  C  CZ   . ARG   A 96  ? 1.25271 1.43455 1.27338 -0.10853 -0.01761 -0.14668 248 ARG   A CZ   
563  N  NH1  . ARG   A 96  ? 1.33423 1.52925 1.34973 -0.11675 -0.02104 -0.16711 248 ARG   A NH1  
564  N  NH2  . ARG   A 96  ? 1.23210 1.38884 1.27647 -0.10344 -0.01382 -0.14632 248 ARG   A NH2  
565  N  N    . ASP   A 97  ? 0.66329 0.83438 0.71146 -0.07661 0.01522  -0.15472 249 ASP   A N    
566  C  CA   . ASP   A 97  ? 0.67867 0.84171 0.74703 -0.07230 0.01975  -0.18134 249 ASP   A CA   
567  C  C    . ASP   A 97  ? 0.66615 0.79502 0.76396 -0.06864 0.01531  -0.17790 249 ASP   A C    
568  O  O    . ASP   A 97  ? 0.70614 0.82076 0.82411 -0.06565 0.01689  -0.19931 249 ASP   A O    
569  C  CB   . ASP   A 97  ? 0.75088 0.92913 0.82514 -0.06342 0.03036  -0.19161 249 ASP   A CB   
570  C  CG   . ASP   A 97  ? 0.79635 1.01160 0.84229 -0.06900 0.03629  -0.19935 249 ASP   A CG   
571  O  OD1  . ASP   A 97  ? 0.83527 1.06271 0.85743 -0.07908 0.03131  -0.19929 249 ASP   A OD1  
572  O  OD2  . ASP   A 97  ? 0.80241 1.03700 0.85039 -0.06366 0.04573  -0.20441 249 ASP   A OD2  
573  N  N    . LEU   A 98  ? 0.62027 0.73585 0.72095 -0.06905 0.00983  -0.15169 250 LEU   A N    
574  C  CA   . LEU   A 98  ? 0.62220 0.70851 0.74761 -0.06790 0.00517  -0.14361 250 LEU   A CA   
575  C  C    . LEU   A 98  ? 0.63873 0.71818 0.76357 -0.07933 -0.00158 -0.14735 250 LEU   A C    
576  O  O    . LEU   A 98  ? 0.64879 0.74739 0.75237 -0.08709 -0.00430 -0.14923 250 LEU   A O    
577  C  CB   . LEU   A 98  ? 0.60480 0.68514 0.73105 -0.06452 0.00268  -0.11448 250 LEU   A CB   
578  C  CG   . LEU   A 98  ? 0.57463 0.66251 0.70287 -0.05493 0.00729  -0.10601 250 LEU   A CG   
579  C  CD1  . LEU   A 98  ? 0.53711 0.62488 0.65627 -0.05567 0.00335  -0.07947 250 LEU   A CD1  
580  C  CD2  . LEU   A 98  ? 0.57467 0.64628 0.73301 -0.04471 0.00936  -0.11260 250 LEU   A CD2  
581  N  N    . THR   A 99  ? 0.65958 0.71230 0.80944 -0.08085 -0.00498 -0.14682 251 THR   A N    
582  C  CA   . THR   A 99  ? 0.63108 0.67795 0.78395 -0.09348 -0.01167 -0.14639 251 THR   A CA   
583  C  C    . THR   A 99  ? 0.59211 0.65001 0.73186 -0.09740 -0.01537 -0.12002 251 THR   A C    
584  O  O    . THR   A 99  ? 0.54830 0.60752 0.68343 -0.09041 -0.01366 -0.10054 251 THR   A O    
585  C  CB   . THR   A 99  ? 0.66855 0.68238 0.85282 -0.09593 -0.01466 -0.14797 251 THR   A CB   
586  O  OG1  . THR   A 99  ? 0.67235 0.67204 0.86820 -0.09052 -0.01534 -0.12107 251 THR   A OG1  
587  C  CG2  . THR   A 99  ? 0.70733 0.70611 0.90872 -0.08917 -0.01102 -0.17565 251 THR   A CG2  
588  N  N    A SER   A 100 ? 0.56701 0.63467 0.70170 -0.10858 -0.02071 -0.12111 252 SER   A N    
589  N  N    B SER   A 100 ? 0.56669 0.63439 0.70134 -0.10857 -0.02070 -0.12111 252 SER   A N    
590  C  CA   A SER   A 100 ? 0.53875 0.61899 0.66411 -0.11134 -0.02397 -0.09892 252 SER   A CA   
591  C  CA   B SER   A 100 ? 0.53780 0.61803 0.66313 -0.11130 -0.02395 -0.09889 252 SER   A CA   
592  C  C    A SER   A 100 ? 0.54916 0.61236 0.69066 -0.11019 -0.02382 -0.07751 252 SER   A C    
593  C  C    B SER   A 100 ? 0.54896 0.61216 0.69043 -0.11014 -0.02380 -0.07751 252 SER   A C    
594  O  O    A SER   A 100 ? 0.52588 0.59837 0.65780 -0.10690 -0.02362 -0.05840 252 SER   A O    
595  O  O    B SER   A 100 ? 0.52568 0.59808 0.65757 -0.10678 -0.02358 -0.05840 252 SER   A O    
596  C  CB   A SER   A 100 ? 0.53876 0.63435 0.66198 -0.12343 -0.03010 -0.10521 252 SER   A CB   
597  C  CB   B SER   A 100 ? 0.53887 0.63450 0.66199 -0.12338 -0.03008 -0.10524 252 SER   A CB   
598  O  OG   A SER   A 100 ? 0.50048 0.58260 0.64607 -0.13285 -0.03301 -0.09933 252 SER   A OG   
599  O  OG   B SER   A 100 ? 0.57801 0.69320 0.68297 -0.12479 -0.03129 -0.12300 252 SER   A OG   
600  N  N    . ASP   A 101 ? 0.61700 0.65528 0.78267 -0.11295 -0.02426 -0.08034 253 ASP   A N    
601  C  CA   . ASP   A 101 ? 0.66638 0.68921 0.84655 -0.11238 -0.02459 -0.05753 253 ASP   A CA   
602  C  C    . ASP   A 101 ? 0.63420 0.65635 0.80774 -0.09907 -0.02114 -0.04546 253 ASP   A C    
603  O  O    . ASP   A 101 ? 0.61356 0.64058 0.78230 -0.09755 -0.02128 -0.02403 253 ASP   A O    
604  C  CB   . ASP   A 101 ? 0.73686 0.72960 0.94578 -0.11792 -0.02691 -0.06215 253 ASP   A CB   
605  C  CG   . ASP   A 101 ? 0.83967 0.83189 1.05739 -0.13344 -0.03113 -0.07585 253 ASP   A CG   
606  O  OD1  . ASP   A 101 ? 0.83563 0.84537 1.04898 -0.14350 -0.03338 -0.06471 253 ASP   A OD1  
607  O  OD2  . ASP   A 101 ? 0.88510 0.86101 1.11509 -0.13553 -0.03221 -0.09921 253 ASP   A OD2  
608  N  N    . ASP   A 102 ? 0.62853 0.64784 0.80173 -0.08983 -0.01787 -0.06008 254 ASP   A N    
609  C  CA   . ASP   A 102 ? 0.56503 0.58675 0.73437 -0.07819 -0.01504 -0.04967 254 ASP   A CA   
610  C  C    . ASP   A 102 ? 0.51870 0.56355 0.66157 -0.07686 -0.01403 -0.04073 254 ASP   A C    
611  O  O    . ASP   A 102 ? 0.55464 0.60208 0.69286 -0.07221 -0.01409 -0.02373 254 ASP   A O    
612  C  CB   . ASP   A 102 ? 0.61518 0.63288 0.79320 -0.06898 -0.01095 -0.06895 254 ASP   A CB   
613  C  CG   . ASP   A 102 ? 0.63563 0.62583 0.84438 -0.06409 -0.01239 -0.07026 254 ASP   A CG   
614  O  OD1  . ASP   A 102 ? 0.63972 0.61406 0.86097 -0.06820 -0.01689 -0.05134 254 ASP   A OD1  
615  O  OD2  . ASP   A 102 ? 0.64651 0.63156 0.86756 -0.05594 -0.00901 -0.08982 254 ASP   A OD2  
616  N  N    . GLN   A 103 ? 0.52339 0.58463 0.64897 -0.08102 -0.01394 -0.05188 255 GLN   A N    
617  C  CA   . GLN   A 103 ? 0.49672 0.57585 0.59931 -0.07980 -0.01432 -0.04217 255 GLN   A CA   
618  C  C    . GLN   A 103 ? 0.46135 0.54181 0.56292 -0.08232 -0.01715 -0.02368 255 GLN   A C    
619  O  O    . GLN   A 103 ? 0.45759 0.54424 0.54716 -0.07797 -0.01701 -0.01163 255 GLN   A O    
620  C  CB   . GLN   A 103 ? 0.51787 0.61377 0.60410 -0.08423 -0.01545 -0.05499 255 GLN   A CB   
621  C  CG   . GLN   A 103 ? 0.56949 0.66938 0.65391 -0.08275 -0.01161 -0.07489 255 GLN   A CG   
622  C  CD   . GLN   A 103 ? 0.64388 0.76296 0.71064 -0.08873 -0.01369 -0.08689 255 GLN   A CD   
623  O  OE1  . GLN   A 103 ? 0.58533 0.71569 0.63975 -0.09196 -0.01846 -0.07770 255 GLN   A OE1  
624  N  NE2  . GLN   A 103 ? 0.70273 0.82741 0.76860 -0.08963 -0.01037 -0.10798 255 GLN   A NE2  
625  N  N    . ILE   A 104 ? 0.46141 0.53708 0.57619 -0.08999 -0.01941 -0.02212 256 ILE   A N    
626  C  CA   . ILE   A 104 ? 0.47825 0.55976 0.59352 -0.09318 -0.02066 -0.00509 256 ILE   A CA   
627  C  C    . ILE   A 104 ? 0.46658 0.53807 0.58771 -0.08885 -0.01946 0.01114  256 ILE   A C    
628  O  O    . ILE   A 104 ? 0.49944 0.58054 0.60944 -0.08576 -0.01899 0.02362  256 ILE   A O    
629  C  CB   . ILE   A 104 ? 0.47128 0.55325 0.60124 -0.10478 -0.02303 -0.00697 256 ILE   A CB   
630  C  CG1  . ILE   A 104 ? 0.47070 0.57235 0.59101 -0.10883 -0.02576 -0.01811 256 ILE   A CG1  
631  C  CG2  . ILE   A 104 ? 0.48162 0.56723 0.61826 -0.10903 -0.02255 0.01268  256 ILE   A CG2  
632  C  CD1  . ILE   A 104 ? 0.52484 0.62755 0.66112 -0.12179 -0.02905 -0.02663 256 ILE   A CD1  
633  N  N    . VAL   A 105 ? 0.49047 0.54299 0.62944 -0.08802 -0.01955 0.01060  257 VAL   A N    
634  C  CA   . VAL   A 105 ? 0.52215 0.56630 0.66792 -0.08350 -0.02000 0.02764  257 VAL   A CA   
635  C  C    . VAL   A 105 ? 0.50052 0.55488 0.62995 -0.07448 -0.01883 0.03063  257 VAL   A C    
636  O  O    . VAL   A 105 ? 0.53066 0.59176 0.65254 -0.07299 -0.01962 0.04577  257 VAL   A O    
637  C  CB   . VAL   A 105 ? 0.55770 0.57827 0.72790 -0.08145 -0.02131 0.02476  257 VAL   A CB   
638  C  CG1  . VAL   A 105 ? 0.62269 0.63808 0.79869 -0.07357 -0.02285 0.04124  257 VAL   A CG1  
639  C  CG2  . VAL   A 105 ? 0.57787 0.58462 0.76615 -0.09274 -0.02372 0.02796  257 VAL   A CG2  
640  N  N    . LEU   A 106 ? 0.44644 0.50393 0.56953 -0.06965 -0.01691 0.01587  258 LEU   A N    
641  C  CA   . LEU   A 106 ? 0.41251 0.47873 0.52306 -0.06305 -0.01602 0.01878  258 LEU   A CA   
642  C  C    . LEU   A 106 ? 0.39247 0.47143 0.48202 -0.06444 -0.01683 0.02551  258 LEU   A C    
643  O  O    . LEU   A 106 ? 0.35792 0.44121 0.43938 -0.06125 -0.01775 0.03439  258 LEU   A O    
644  C  CB   . LEU   A 106 ? 0.41608 0.48629 0.52431 -0.05970 -0.01288 0.00225  258 LEU   A CB   
645  C  CG   . LEU   A 106 ? 0.45026 0.51048 0.58001 -0.05460 -0.01097 -0.00757 258 LEU   A CG   
646  C  CD1  . LEU   A 106 ? 0.47907 0.55107 0.60276 -0.05173 -0.00623 -0.02427 258 LEU   A CD1  
647  C  CD2  . LEU   A 106 ? 0.46169 0.51600 0.60564 -0.04819 -0.01318 0.00668  258 LEU   A CD2  
648  N  N    . LEU   A 107 ? 0.39865 0.48416 0.48040 -0.06874 -0.01710 0.02044  259 LEU   A N    
649  C  CA   . LEU   A 107 ? 0.40108 0.49748 0.46543 -0.06769 -0.01811 0.02476  259 LEU   A CA   
650  C  C    . LEU   A 107 ? 0.39400 0.49534 0.45888 -0.06896 -0.01841 0.03718  259 LEU   A C    
651  O  O    . LEU   A 107 ? 0.40174 0.50934 0.45400 -0.06553 -0.01880 0.04199  259 LEU   A O    
652  C  CB   . LEU   A 107 ? 0.44724 0.55174 0.50460 -0.07012 -0.01923 0.01559  259 LEU   A CB   
653  C  CG   . LEU   A 107 ? 0.49121 0.59794 0.53627 -0.06807 -0.01925 0.00774  259 LEU   A CG   
654  C  CD1  . LEU   A 107 ? 0.53197 0.64694 0.57390 -0.07199 -0.02100 -0.00236 259 LEU   A CD1  
655  C  CD2  . LEU   A 107 ? 0.46705 0.57588 0.49672 -0.06399 -0.02082 0.01470  259 LEU   A CD2  
656  N  N    . LYS   A 108 ? 0.31954 0.41889 0.39876 -0.07467 -0.01808 0.04198  260 LYS   A N    
657  C  CA   . LYS   A 108 ? 0.41916 0.52744 0.49846 -0.07742 -0.01731 0.05542  260 LYS   A CA   
658  C  C    . LYS   A 108 ? 0.43829 0.54488 0.51293 -0.07365 -0.01796 0.06652  260 LYS   A C    
659  O  O    . LYS   A 108 ? 0.47133 0.59040 0.53469 -0.07271 -0.01724 0.07351  260 LYS   A O    
660  C  CB   . LYS   A 108 ? 0.42895 0.53391 0.52642 -0.08660 -0.01710 0.06099  260 LYS   A CB   
661  C  CG   . LYS   A 108 ? 0.54974 0.66981 0.64935 -0.09271 -0.01628 0.05703  260 LYS   A CG   
662  C  CD   . LYS   A 108 ? 0.60497 0.71772 0.72528 -0.10410 -0.01703 0.05926  260 LYS   A CD   
663  C  CE   . LYS   A 108 ? 0.65275 0.76668 0.78100 -0.11060 -0.01572 0.07917  260 LYS   A CE   
664  N  NZ   . LYS   A 108 ? 0.65254 0.79440 0.77121 -0.11198 -0.01208 0.08698  260 LYS   A NZ   
665  N  N    . SER   A 109 ? 0.39589 0.48947 0.47977 -0.07110 -0.01954 0.06730  261 SER   A N    
666  C  CA   . SER   A 109 ? 0.44278 0.53690 0.52511 -0.06773 -0.02173 0.07894  261 SER   A CA   
667  C  C    . SER   A 109 ? 0.38859 0.48850 0.45527 -0.06237 -0.02258 0.07351  261 SER   A C    
668  O  O    . SER   A 109 ? 0.42923 0.53609 0.48864 -0.06105 -0.02484 0.08212  261 SER   A O    
669  C  CB   . SER   A 109 ? 0.47837 0.55743 0.58129 -0.06580 -0.02385 0.08255  261 SER   A CB   
670  O  OG   . SER   A 109 ? 0.53409 0.60660 0.64147 -0.06156 -0.02254 0.06660  261 SER   A OG   
671  N  N    . SER   A 110 ? 0.39706 0.49517 0.45778 -0.06055 -0.02138 0.06015  262 SER   A N    
672  C  CA   . SER   A 110 ? 0.40178 0.50262 0.45027 -0.05747 -0.02253 0.05608  262 SER   A CA   
673  C  C    . SER   A 110 ? 0.39686 0.50238 0.42759 -0.05710 -0.02269 0.05167  262 SER   A C    
674  O  O    . SER   A 110 ? 0.44832 0.55428 0.46852 -0.05585 -0.02464 0.05051  262 SER   A O    
675  C  CB   . SER   A 110 ? 0.43532 0.53173 0.48972 -0.05611 -0.02112 0.04628  262 SER   A CB   
676  O  OG   . SER   A 110 ? 0.40126 0.49727 0.45035 -0.05792 -0.01937 0.03670  262 SER   A OG   
677  N  N    . ALA   A 111 ? 0.41510 0.52406 0.44419 -0.05800 -0.02129 0.04902  263 ALA   A N    
678  C  CA   . ALA   A 111 ? 0.39331 0.50540 0.40904 -0.05519 -0.02207 0.04383  263 ALA   A CA   
679  C  C    . ALA   A 111 ? 0.33431 0.45009 0.33852 -0.05267 -0.02328 0.04617  263 ALA   A C    
680  O  O    . ALA   A 111 ? 0.38896 0.49948 0.38254 -0.05011 -0.02555 0.04120  263 ALA   A O    
681  C  CB   . ALA   A 111 ? 0.38021 0.50062 0.39985 -0.05568 -0.02072 0.04185  263 ALA   A CB   
682  N  N    . ILE   A 112 ? 0.33209 0.45685 0.33779 -0.05415 -0.02215 0.05372  264 ILE   A N    
683  C  CA   . ILE   A 112 ? 0.41749 0.54931 0.41033 -0.05249 -0.02326 0.05423  264 ILE   A CA   
684  C  C    . ILE   A 112 ? 0.43013 0.55403 0.41778 -0.05290 -0.02745 0.05271  264 ILE   A C    
685  O  O    . ILE   A 112 ? 0.46092 0.58306 0.43638 -0.05137 -0.02975 0.04632  264 ILE   A O    
686  C  CB   . ILE   A 112 ? 0.47129 0.61775 0.46573 -0.05575 -0.02140 0.06528  264 ILE   A CB   
687  C  CG1  . ILE   A 112 ? 0.47985 0.63836 0.45792 -0.05440 -0.02216 0.06358  264 ILE   A CG1  
688  C  CG2  . ILE   A 112 ? 0.49678 0.63844 0.50371 -0.05935 -0.02349 0.07690  264 ILE   A CG2  
689  C  CD1  . ILE   A 112 ? 0.38038 0.53967 0.34803 -0.04859 -0.02087 0.04961  264 ILE   A CD1  
690  N  N    . GLU   A 113 ? 0.42526 0.54447 0.42390 -0.05498 -0.02855 0.05724  265 GLU   A N    
691  C  CA   . GLU   A 113 ? 0.44039 0.55735 0.43749 -0.05620 -0.03228 0.05672  265 GLU   A CA   
692  C  C    . GLU   A 113 ? 0.46071 0.56775 0.45237 -0.05671 -0.03285 0.04811  265 GLU   A C    
693  O  O    . GLU   A 113 ? 0.45913 0.56385 0.44314 -0.05892 -0.03634 0.04537  265 GLU   A O    
694  C  CB   . GLU   A 113 ? 0.41460 0.53274 0.42842 -0.05650 -0.03280 0.06370  265 GLU   A CB   
695  C  CG   . GLU   A 113 ? 0.37223 0.49758 0.39295 -0.05650 -0.03391 0.07615  265 GLU   A CG   
696  C  CD   . GLU   A 113 ? 0.42934 0.55160 0.47075 -0.05451 -0.03502 0.08250  265 GLU   A CD   
697  O  OE1  . GLU   A 113 ? 0.44970 0.57028 0.49831 -0.05293 -0.03511 0.07656  265 GLU   A OE1  
698  O  OE2  . GLU   A 113 ? 0.44228 0.56390 0.49407 -0.05445 -0.03559 0.09344  265 GLU   A OE2  
699  N  N    . VAL   A 114 ? 0.39149 0.49315 0.38673 -0.05590 -0.03012 0.04456  266 VAL   A N    
700  C  CA   . VAL   A 114 ? 0.35240 0.44593 0.34111 -0.05718 -0.03111 0.03958  266 VAL   A CA   
701  C  C    . VAL   A 114 ? 0.37355 0.46019 0.34951 -0.05479 -0.03395 0.03576  266 VAL   A C    
702  O  O    . VAL   A 114 ? 0.42913 0.50603 0.39821 -0.05706 -0.03714 0.03385  266 VAL   A O    
703  C  CB   . VAL   A 114 ? 0.36744 0.46055 0.36117 -0.05712 -0.02825 0.03702  266 VAL   A CB   
704  C  CG1  . VAL   A 114 ? 0.28206 0.36934 0.26732 -0.05950 -0.02970 0.03506  266 VAL   A CG1  
705  C  CG2  . VAL   A 114 ? 0.36685 0.46481 0.37494 -0.05816 -0.02521 0.03749  266 VAL   A CG2  
706  N  N    . ILE   A 115 ? 0.37899 0.47073 0.35308 -0.05023 -0.03271 0.03440  267 ILE   A N    
707  C  CA   . ILE   A 115 ? 0.40552 0.49233 0.36978 -0.04554 -0.03482 0.02823  267 ILE   A CA   
708  C  C    . ILE   A 115 ? 0.42059 0.50369 0.37661 -0.04819 -0.03834 0.02526  267 ILE   A C    
709  O  O    . ILE   A 115 ? 0.44916 0.51812 0.39837 -0.04800 -0.04230 0.01967  267 ILE   A O    
710  C  CB   . ILE   A 115 ? 0.41045 0.51055 0.37633 -0.04023 -0.03125 0.02674  267 ILE   A CB   
711  C  CG1  . ILE   A 115 ? 0.43049 0.53263 0.40369 -0.03751 -0.02998 0.02691  267 ILE   A CG1  
712  C  CG2  . ILE   A 115 ? 0.42130 0.52138 0.37768 -0.03442 -0.03222 0.01808  267 ILE   A CG2  
713  C  CD1  . ILE   A 115 ? 0.40493 0.52507 0.38440 -0.03489 -0.02576 0.02727  267 ILE   A CD1  
714  N  N    . MET   A 116 ? 0.40575 0.50097 0.36302 -0.05139 -0.03796 0.02956  268 MET   A N    
715  C  CA   . MET   A 116 ? 0.45141 0.54717 0.40122 -0.05545 -0.04249 0.02689  268 MET   A CA   
716  C  C    . MET   A 116 ? 0.45290 0.53651 0.40456 -0.06154 -0.04635 0.02662  268 MET   A C    
717  O  O    . MET   A 116 ? 0.48616 0.55992 0.43014 -0.06468 -0.05100 0.02002  268 MET   A O    
718  C  CB   . MET   A 116 ? 0.42941 0.54285 0.38237 -0.05805 -0.04264 0.03526  268 MET   A CB   
719  C  CG   . MET   A 116 ? 0.46562 0.59421 0.41139 -0.05501 -0.03991 0.03581  268 MET   A CG   
720  S  SD   . MET   A 116 ? 0.49228 0.63921 0.44617 -0.05784 -0.03940 0.05271  268 MET   A SD   
721  C  CE   . MET   A 116 ? 0.43636 0.60298 0.37774 -0.05617 -0.03499 0.05256  268 MET   A CE   
722  N  N    . LEU   A 117 ? 0.41382 0.49864 0.37602 -0.06398 -0.04419 0.03293  269 LEU   A N    
723  C  CA   . LEU   A 117 ? 0.39245 0.47109 0.35704 -0.07091 -0.04631 0.03389  269 LEU   A CA   
724  C  C    . LEU   A 117 ? 0.42833 0.48806 0.38508 -0.07159 -0.04838 0.03046  269 LEU   A C    
725  O  O    . LEU   A 117 ? 0.41690 0.46569 0.36902 -0.07771 -0.05315 0.02824  269 LEU   A O    
726  C  CB   . LEU   A 117 ? 0.45294 0.54054 0.43026 -0.07192 -0.04193 0.03917  269 LEU   A CB   
727  C  CG   . LEU   A 117 ? 0.45244 0.55591 0.44238 -0.07172 -0.04145 0.04393  269 LEU   A CG   
728  C  CD1  . LEU   A 117 ? 0.45124 0.56020 0.45467 -0.06978 -0.03612 0.04525  269 LEU   A CD1  
729  C  CD2  . LEU   A 117 ? 0.44173 0.55257 0.43345 -0.07848 -0.04635 0.04486  269 LEU   A CD2  
730  N  N    . ARG   A 118 ? 0.45330 0.50866 0.40961 -0.06583 -0.04581 0.03087  270 ARG   A N    
731  C  CA   . ARG   A 118 ? 0.48694 0.52492 0.43743 -0.06549 -0.04890 0.03086  270 ARG   A CA   
732  C  C    . ARG   A 118 ? 0.50453 0.52665 0.44779 -0.06126 -0.05374 0.02330  270 ARG   A C    
733  O  O    . ARG   A 118 ? 0.50980 0.51204 0.44950 -0.06309 -0.05858 0.02389  270 ARG   A O    
734  C  CB   . ARG   A 118 ? 0.49287 0.53417 0.44525 -0.05966 -0.04625 0.03315  270 ARG   A CB   
735  C  CG   . ARG   A 118 ? 0.50244 0.54888 0.45583 -0.04975 -0.04487 0.02831  270 ARG   A CG   
736  C  CD   . ARG   A 118 ? 0.52831 0.58546 0.48727 -0.04693 -0.04185 0.03070  270 ARG   A CD   
737  N  NE   . ARG   A 118 ? 0.50896 0.55789 0.46457 -0.04402 -0.04578 0.03313  270 ARG   A NE   
738  C  CZ   . ARG   A 118 ? 0.55952 0.60771 0.51241 -0.04967 -0.04672 0.03884  270 ARG   A CZ   
739  N  NH1  . ARG   A 118 ? 0.65601 0.71176 0.61058 -0.05767 -0.04288 0.04028  270 ARG   A NH1  
740  N  NH2  . ARG   A 118 ? 0.52508 0.56703 0.47384 -0.04690 -0.05157 0.04337  270 ARG   A NH2  
741  N  N    . SER   A 119 ? 0.44284 0.47333 0.38399 -0.05579 -0.05255 0.01615  271 SER   A N    
742  C  CA   . SER   A 119 ? 0.55471 0.57258 0.48876 -0.05133 -0.05637 0.00507  271 SER   A CA   
743  C  C    . SER   A 119 ? 0.56229 0.56787 0.49214 -0.06113 -0.06229 0.00133  271 SER   A C    
744  O  O    . SER   A 119 ? 0.59502 0.58170 0.51993 -0.05905 -0.06702 -0.00876 271 SER   A O    
745  C  CB   . SER   A 119 ? 0.57459 0.61080 0.50556 -0.04445 -0.05243 -0.00202 271 SER   A CB   
746  O  OG   . SER   A 119 ? 0.56369 0.61500 0.49190 -0.05126 -0.05253 -0.00086 271 SER   A OG   
747  N  N    . ASN   A 120 ? 0.55010 0.56626 0.48368 -0.07165 -0.06246 0.00829  272 ASN   A N    
748  C  CA   . ASN   A 120 ? 0.52753 0.53620 0.45936 -0.08304 -0.06857 0.00535  272 ASN   A CA   
749  C  C    . ASN   A 120 ? 0.55009 0.53096 0.48164 -0.08879 -0.07351 0.00700  272 ASN   A C    
750  O  O    . ASN   A 120 ? 0.58808 0.55498 0.51746 -0.09761 -0.07992 0.00128  272 ASN   A O    
751  C  CB   . ASN   A 120 ? 0.52335 0.55337 0.46332 -0.09203 -0.06735 0.01402  272 ASN   A CB   
752  C  CG   . ASN   A 120 ? 0.53904 0.57088 0.47855 -0.10395 -0.07413 0.00993  272 ASN   A CG   
753  O  OD1  . ASN   A 120 ? 0.56511 0.59904 0.51207 -0.11507 -0.07568 0.01628  272 ASN   A OD1  
754  N  ND2  . ASN   A 120 ? 0.44246 0.47750 0.37334 -0.10248 -0.07798 -0.00098 272 ASN   A ND2  
755  N  N    . GLN   A 121 ? 0.53490 0.50765 0.46858 -0.08506 -0.07147 0.01555  273 GLN   A N    
756  C  CA   . GLN   A 121 ? 0.56173 0.50757 0.49467 -0.09056 -0.07692 0.02096  273 GLN   A CA   
757  C  C    . GLN   A 121 ? 0.60842 0.52595 0.53762 -0.08376 -0.08333 0.00902  273 GLN   A C    
758  O  O    . GLN   A 121 ? 0.66982 0.56220 0.59891 -0.09265 -0.09039 0.00803  273 GLN   A O    
759  C  CB   . GLN   A 121 ? 0.65094 0.59829 0.58498 -0.08656 -0.07402 0.03305  273 GLN   A CB   
760  C  CG   . GLN   A 121 ? 0.68458 0.60601 0.61693 -0.09256 -0.08017 0.04340  273 GLN   A CG   
761  C  CD   . GLN   A 121 ? 0.65097 0.58307 0.58214 -0.09354 -0.07710 0.05780  273 GLN   A CD   
762  O  OE1  . GLN   A 121 ? 0.69465 0.60853 0.62303 -0.09472 -0.08231 0.06842  273 GLN   A OE1  
763  N  NE2  . GLN   A 121 ? 0.55991 0.52137 0.49311 -0.09304 -0.06924 0.05810  273 GLN   A NE2  
764  N  N    . SER   A 122 ? 0.64108 0.56260 0.56865 -0.06819 -0.08082 -0.00084 274 SER   A N    
765  C  CA   . SER   A 122 ? 0.67966 0.57836 0.60530 -0.05846 -0.08546 -0.01590 274 SER   A CA   
766  C  C    . SER   A 122 ? 0.66340 0.56634 0.58292 -0.06172 -0.08690 -0.03321 274 SER   A C    
767  O  O    . SER   A 122 ? 0.65162 0.53233 0.56912 -0.05665 -0.09170 -0.04894 274 SER   A O    
768  C  CB   . SER   A 122 ? 0.71944 0.62697 0.64752 -0.03998 -0.08118 -0.02013 274 SER   A CB   
769  O  OG   . SER   A 122 ? 0.69718 0.63731 0.62275 -0.03646 -0.07357 -0.02492 274 SER   A OG   
770  N  N    . PHE   A 123 ? 0.63183 0.56309 0.54866 -0.06935 -0.08341 -0.03126 275 PHE   A N    
771  C  CA   . PHE   A 123 ? 0.62090 0.56162 0.53003 -0.07327 -0.08565 -0.04618 275 PHE   A CA   
772  C  C    . PHE   A 123 ? 0.71101 0.62748 0.61992 -0.08732 -0.09487 -0.05209 275 PHE   A C    
773  O  O    . PHE   A 123 ? 0.73418 0.64334 0.64957 -0.10017 -0.09763 -0.03868 275 PHE   A O    
774  C  CB   . PHE   A 123 ? 0.59753 0.57429 0.50585 -0.07832 -0.08141 -0.03836 275 PHE   A CB   
775  C  CG   . PHE   A 123 ? 0.63118 0.62450 0.52946 -0.08130 -0.08386 -0.05146 275 PHE   A CG   
776  C  CD1  . PHE   A 123 ? 0.62762 0.63633 0.51683 -0.07018 -0.07938 -0.06237 275 PHE   A CD1  
777  C  CD2  . PHE   A 123 ? 0.64390 0.64102 0.54152 -0.09603 -0.09077 -0.05274 275 PHE   A CD2  
778  C  CE1  . PHE   A 123 ? 0.61719 0.64482 0.49414 -0.07372 -0.08172 -0.07415 275 PHE   A CE1  
779  C  CE2  . PHE   A 123 ? 0.67289 0.68833 0.55964 -0.09946 -0.09429 -0.06476 275 PHE   A CE2  
780  C  CZ   . PHE   A 123 ? 0.67824 0.70885 0.55327 -0.08829 -0.08976 -0.07541 275 PHE   A CZ   
781  N  N    . THR   A 124 ? 0.75945 0.66473 0.66109 -0.08566 -0.09940 -0.07315 276 THR   A N    
782  C  CA   . THR   A 124 ? 0.80378 0.68503 0.70530 -0.10017 -0.10916 -0.08239 276 THR   A CA   
783  C  C    . THR   A 124 ? 0.84122 0.74421 0.73202 -0.10610 -0.11189 -0.09927 276 THR   A C    
784  O  O    . THR   A 124 ? 0.85448 0.77441 0.73515 -0.09442 -0.10774 -0.11330 276 THR   A O    
785  C  CB   . THR   A 124 ? 0.85447 0.69042 0.75890 -0.09341 -0.11493 -0.09465 276 THR   A CB   
786  O  OG1  . THR   A 124 ? 0.89450 0.70533 0.79961 -0.10971 -0.12510 -0.10458 276 THR   A OG1  
787  C  CG2  . THR   A 124 ? 0.85728 0.69520 0.75540 -0.07345 -0.11113 -0.11646 276 THR   A CG2  
788  N  N    . MET   A 125 ? 0.84643 0.75254 0.73937 -0.12505 -0.11895 -0.09725 277 MET   A N    
789  C  CA   . MET   A 125 ? 0.86910 0.79920 0.75192 -0.13295 -0.12356 -0.11149 277 MET   A CA   
790  C  C    . MET   A 125 ? 0.94891 0.85196 0.82418 -0.13637 -0.13185 -0.13930 277 MET   A C    
791  O  O    . MET   A 125 ? 0.97229 0.89481 0.83665 -0.14359 -0.13679 -0.15479 277 MET   A O    
792  C  CB   . MET   A 125 ? 0.83356 0.78583 0.72453 -0.15139 -0.12788 -0.09674 277 MET   A CB   
793  C  CG   . MET   A 125 ? 0.81597 0.80375 0.71240 -0.14620 -0.12003 -0.07544 277 MET   A CG   
794  S  SD   . MET   A 125 ? 0.84855 0.86419 0.75879 -0.16516 -0.12504 -0.06017 277 MET   A SD   
795  C  CE   . MET   A 125 ? 0.90131 0.88082 0.82459 -0.17899 -0.12777 -0.05276 277 MET   A CE   
796  N  N    . ASP   A 126 ? 0.98226 0.84085 0.86334 -0.13110 -0.13418 -0.14632 278 ASP   A N    
797  C  CA   . ASP   A 126 ? 1.10442 0.93258 0.98011 -0.13119 -0.14167 -0.17591 278 ASP   A CA   
798  C  C    . ASP   A 126 ? 1.07026 0.92096 0.92995 -0.11498 -0.13614 -0.19974 278 ASP   A C    
799  O  O    . ASP   A 126 ? 1.12169 0.97866 0.96923 -0.12088 -0.14147 -0.22463 278 ASP   A O    
800  C  CB   . ASP   A 126 ? 1.23520 1.01000 1.12307 -0.12491 -0.14492 -0.17555 278 ASP   A CB   
801  C  CG   . ASP   A 126 ? 1.32823 1.08256 1.23004 -0.14273 -0.15002 -0.15021 278 ASP   A CG   
802  O  OD1  . ASP   A 126 ? 1.36281 1.07869 1.27465 -0.13796 -0.15209 -0.14097 278 ASP   A OD1  
803  O  OD2  . ASP   A 126 ? 1.34519 1.12432 1.24842 -0.16150 -0.15205 -0.13882 278 ASP   A OD2  
804  N  N    . ASP   A 127 ? 0.98600 0.85234 0.84511 -0.09552 -0.12524 -0.19266 279 ASP   A N    
805  C  CA   . ASP   A 127 ? 0.97316 0.86703 0.81794 -0.08034 -0.11787 -0.21207 279 ASP   A CA   
806  C  C    . ASP   A 127 ? 0.92153 0.86058 0.76266 -0.07361 -0.10719 -0.19188 279 ASP   A C    
807  O  O    . ASP   A 127 ? 0.93217 0.89483 0.76436 -0.05956 -0.09882 -0.20235 279 ASP   A O    
808  C  CB   . ASP   A 127 ? 1.01542 0.87910 0.86526 -0.06017 -0.11521 -0.23180 279 ASP   A CB   
809  C  CG   . ASP   A 127 ? 1.01891 0.85817 0.88670 -0.05035 -0.11287 -0.21020 279 ASP   A CG   
810  O  OD1  . ASP   A 127 ? 0.97933 0.83430 0.85234 -0.05604 -0.10975 -0.18154 279 ASP   A OD1  
811  O  OD2  . ASP   A 127 ? 1.04969 0.85397 0.92680 -0.03657 -0.11480 -0.22247 279 ASP   A OD2  
812  N  N    . MET   A 128 ? 0.86444 0.81620 0.71336 -0.08346 -0.10704 -0.16387 280 MET   A N    
813  C  CA   . MET   A 128 ? 0.79053 0.78087 0.63846 -0.07885 -0.09832 -0.14382 280 MET   A CA   
814  C  C    . MET   A 128 ? 0.75157 0.74212 0.60420 -0.05997 -0.08834 -0.14134 280 MET   A C    
815  O  O    . MET   A 128 ? 0.72296 0.74522 0.56796 -0.05157 -0.08032 -0.14215 280 MET   A O    
816  C  CB   . MET   A 128 ? 0.80101 0.83269 0.63192 -0.08327 -0.09809 -0.14986 280 MET   A CB   
817  C  CG   . MET   A 128 ? 0.81311 0.84977 0.63988 -0.10192 -0.10928 -0.15320 280 MET   A CG   
818  S  SD   . MET   A 128 ? 0.81188 0.84553 0.65853 -0.11548 -0.11322 -0.12368 280 MET   A SD   
819  C  CE   . MET   A 128 ? 0.79483 0.83619 0.63732 -0.13691 -0.12723 -0.13417 280 MET   A CE   
820  N  N    . SER   A 129 ? 0.74311 0.69982 0.60904 -0.05423 -0.08938 -0.13677 281 SER   A N    
821  C  CA   . SER   A 129 ? 0.75796 0.71353 0.63114 -0.03640 -0.08190 -0.13463 281 SER   A CA   
822  C  C    . SER   A 129 ? 0.78006 0.72247 0.66725 -0.03781 -0.08186 -0.11011 281 SER   A C    
823  O  O    . SER   A 129 ? 0.80247 0.72656 0.69450 -0.05085 -0.08810 -0.09904 281 SER   A O    
824  C  CB   . SER   A 129 ? 0.78322 0.71063 0.65832 -0.02273 -0.08397 -0.15908 281 SER   A CB   
825  O  OG   . SER   A 129 ? 0.82488 0.70787 0.71228 -0.02446 -0.09194 -0.15361 281 SER   A OG   
826  N  N    . TRP   A 130 ? 0.78810 0.74356 0.68148 -0.02516 -0.07451 -0.10206 282 TRP   A N    
827  C  CA   . TRP   A 130 ? 0.75290 0.69741 0.65818 -0.02411 -0.07446 -0.08204 282 TRP   A CA   
828  C  C    . TRP   A 130 ? 0.75577 0.66754 0.66925 -0.01169 -0.07880 -0.08915 282 TRP   A C    
829  O  O    . TRP   A 130 ? 0.77703 0.69633 0.69481 0.00497  -0.07455 -0.09797 282 TRP   A O    
830  C  CB   . TRP   A 130 ? 0.71084 0.68776 0.61945 -0.01875 -0.06558 -0.06965 282 TRP   A CB   
831  C  CG   . TRP   A 130 ? 0.66878 0.67245 0.57344 -0.03042 -0.06257 -0.05791 282 TRP   A CG   
832  C  CD1  . TRP   A 130 ? 0.61072 0.61643 0.52118 -0.04014 -0.06305 -0.04013 282 TRP   A CD1  
833  C  CD2  . TRP   A 130 ? 0.66177 0.69487 0.55682 -0.03248 -0.05885 -0.06268 282 TRP   A CD2  
834  N  NE1  . TRP   A 130 ? 0.57728 0.60916 0.48493 -0.04667 -0.06039 -0.03393 282 TRP   A NE1  
835  C  CE2  . TRP   A 130 ? 0.59080 0.63953 0.48836 -0.04277 -0.05838 -0.04582 282 TRP   A CE2  
836  C  CE3  . TRP   A 130 ? 0.66338 0.71283 0.54766 -0.02643 -0.05582 -0.07944 282 TRP   A CE3  
837  C  CZ2  . TRP   A 130 ? 0.58614 0.66351 0.47669 -0.04707 -0.05641 -0.04254 282 TRP   A CZ2  
838  C  CZ3  . TRP   A 130 ? 0.63503 0.71613 0.50943 -0.03232 -0.05310 -0.07610 282 TRP   A CZ3  
839  C  CH2  . TRP   A 130 ? 0.61834 0.71185 0.49631 -0.04249 -0.05408 -0.05647 282 TRP   A CH2  
840  N  N    . ASP   A 131 ? 0.78859 0.66482 0.70576 -0.01984 -0.08762 -0.08446 283 ASP   A N    
841  C  CA   . ASP   A 131 ? 0.85514 0.69398 0.78131 -0.00908 -0.09415 -0.08885 283 ASP   A CA   
842  C  C    . ASP   A 131 ? 0.81437 0.64962 0.74928 -0.00650 -0.09483 -0.06530 283 ASP   A C    
843  O  O    . ASP   A 131 ? 0.79225 0.61921 0.72696 -0.02113 -0.09816 -0.04696 283 ASP   A O    
844  C  CB   . ASP   A 131 ? 0.90253 0.70232 0.82806 -0.02113 -0.10440 -0.09569 283 ASP   A CB   
845  C  CG   . ASP   A 131 ? 0.98462 0.74055 0.92077 -0.00885 -0.11236 -0.10236 283 ASP   A CG   
846  O  OD1  . ASP   A 131 ? 0.99821 0.75500 0.94333 0.00887  -0.11069 -0.09778 283 ASP   A OD1  
847  O  OD2  . ASP   A 131 ? 1.03697 0.75695 0.97403 -0.01699 -0.12112 -0.11222 283 ASP   A OD2  
848  N  N    . CYS   A 132 ? 0.85210 0.69705 0.79466 0.01168  -0.09166 -0.06622 284 CYS   A N    
849  C  CA   . CYS   A 132 ? 0.80425 0.65005 0.75449 0.01558  -0.09315 -0.04561 284 CYS   A CA   
850  C  C    . CYS   A 132 ? 0.85638 0.66771 0.81796 0.02944  -0.10224 -0.04488 284 CYS   A C    
851  O  O    . CYS   A 132 ? 0.76769 0.58833 0.73868 0.04368  -0.10245 -0.03845 284 CYS   A O    
852  C  CB   . CYS   A 132 ? 0.73132 0.61834 0.68404 0.02375  -0.08393 -0.04310 284 CYS   A CB   
853  S  SG   . CYS   A 132 ? 0.66110 0.58542 0.60430 0.00791  -0.07473 -0.03652 284 CYS   A SG   
854  N  N    . GLY   A 133 ? 0.92815 0.69868 0.89048 0.02515  -0.11088 -0.05084 285 GLY   A N    
855  C  CA   . GLY   A 133 ? 0.96462 0.69452 0.93837 0.03442  -0.12184 -0.04443 285 GLY   A CA   
856  C  C    . GLY   A 133 ? 1.00996 0.71884 0.99463 0.05588  -0.12476 -0.06929 285 GLY   A C    
857  O  O    . GLY   A 133 ? 1.02888 0.69225 1.02315 0.06064  -0.13573 -0.06860 285 GLY   A O    
858  N  N    . SER   A 134 ? 1.01866 0.75949 1.00288 0.06896  -0.11515 -0.09106 286 SER   A N    
859  C  CA   . SER   A 134 ? 1.06772 0.79534 1.06348 0.09185  -0.11604 -0.11717 286 SER   A CA   
860  C  C    . SER   A 134 ? 1.06550 0.82542 1.05071 0.09348  -0.10498 -0.14474 286 SER   A C    
861  O  O    . SER   A 134 ? 1.01502 0.81411 0.98741 0.08153  -0.09611 -0.13951 286 SER   A O    
862  C  CB   . SER   A 134 ? 1.08332 0.82343 1.09719 0.11563  -0.11632 -0.11110 286 SER   A CB   
863  O  OG   . SER   A 134 ? 1.07886 0.86954 1.09309 0.12640  -0.10358 -0.12416 286 SER   A OG   
864  N  N    . GLN   A 135 ? 1.12909 0.87195 1.11998 0.10884  -0.10592 -0.17434 287 GLN   A N    
865  C  CA   . GLN   A 135 ? 1.18349 0.95881 1.16272 0.11155  -0.09546 -0.20285 287 GLN   A CA   
866  C  C    . GLN   A 135 ? 1.16195 0.99526 1.14184 0.12113  -0.08218 -0.20027 287 GLN   A C    
867  O  O    . GLN   A 135 ? 1.13508 1.00740 1.09913 0.11132  -0.07264 -0.20501 287 GLN   A O    
868  C  CB   . GLN   A 135 ? 1.27552 1.02266 1.26299 0.12957  -0.09852 -0.23742 287 GLN   A CB   
869  C  CG   . GLN   A 135 ? 1.30901 1.07787 1.27836 0.12493  -0.09126 -0.26881 287 GLN   A CG   
870  C  CD   . GLN   A 135 ? 1.33736 1.08725 1.28921 0.09754  -0.09795 -0.26678 287 GLN   A CD   
871  O  OE1  . GLN   A 135 ? 1.32789 1.11312 1.26018 0.08397  -0.09161 -0.27202 287 GLN   A OE1  
872  N  NE2  . GLN   A 135 ? 1.37611 1.07163 1.33590 0.08866  -0.11136 -0.25757 287 GLN   A NE2  
873  N  N    . ASP   A 136 ? 1.18298 1.02342 1.18198 0.13958  -0.08214 -0.19163 288 ASP   A N    
874  C  CA   . ASP   A 136 ? 1.16480 1.06048 1.16729 0.14634  -0.07040 -0.18646 288 ASP   A CA   
875  C  C    . ASP   A 136 ? 1.06743 0.98906 1.05572 0.12353  -0.06626 -0.16205 288 ASP   A C    
876  O  O    . ASP   A 136 ? 1.02763 0.99464 1.00899 0.11986  -0.05504 -0.16317 288 ASP   A O    
877  C  CB   . ASP   A 136 ? 1.22852 1.12472 1.25567 0.16695  -0.07421 -0.17671 288 ASP   A CB   
878  C  CG   . ASP   A 136 ? 1.32649 1.24618 1.36972 0.19357  -0.06702 -0.20314 288 ASP   A CG   
879  O  OD1  . ASP   A 136 ? 1.36325 1.28662 1.42973 0.21309  -0.07048 -0.19774 288 ASP   A OD1  
880  O  OD2  . ASP   A 136 ? 1.37151 1.30906 1.40436 0.19521  -0.05792 -0.22951 288 ASP   A OD2  
881  N  N    . TYR   A 137 ? 1.00151 0.89502 0.98598 0.10789  -0.07504 -0.13986 289 TYR   A N    
882  C  CA   . TYR   A 137 ? 0.91903 0.83267 0.89294 0.08781  -0.07206 -0.11727 289 TYR   A CA   
883  C  C    . TYR   A 137 ? 0.89075 0.79015 0.84774 0.06713  -0.07438 -0.11803 289 TYR   A C    
884  O  O    . TYR   A 137 ? 0.85002 0.74068 0.80239 0.05063  -0.07811 -0.09836 289 TYR   A O    
885  C  CB   . TYR   A 137 ? 0.90108 0.80323 0.88388 0.08587  -0.07887 -0.09128 289 TYR   A CB   
886  C  CG   . TYR   A 137 ? 0.90079 0.81522 0.90233 0.10688  -0.07941 -0.09026 289 TYR   A CG   
887  C  CD1  . TYR   A 137 ? 0.88522 0.84002 0.89372 0.11970  -0.06931 -0.10374 289 TYR   A CD1  
888  C  CD2  . TYR   A 137 ? 0.93156 0.81984 0.94453 0.11364  -0.09041 -0.07499 289 TYR   A CD2  
889  C  CE1  . TYR   A 137 ? 0.92556 0.89594 0.95399 0.13900  -0.06999 -0.10327 289 TYR   A CE1  
890  C  CE2  . TYR   A 137 ? 0.96326 0.86553 0.99513 0.13370  -0.09233 -0.07344 289 TYR   A CE2  
891  C  CZ   . TYR   A 137 ? 0.95541 0.89951 0.99605 0.14659  -0.08202 -0.08838 289 TYR   A CZ   
892  O  OH   . TYR   A 137 ? 0.96577 0.92834 1.02792 0.16655  -0.08400 -0.08714 289 TYR   A OH   
893  N  N    . LYS   A 138 ? 0.88616 0.78565 0.83448 0.06840  -0.07228 -0.14225 290 LYS   A N    
894  C  CA   . LYS   A 138 ? 0.89537 0.78817 0.82757 0.04917  -0.07477 -0.14654 290 LYS   A CA   
895  C  C    . LYS   A 138 ? 0.84323 0.78222 0.76244 0.04687  -0.06425 -0.15580 290 LYS   A C    
896  O  O    . LYS   A 138 ? 0.87528 0.82652 0.79216 0.05901  -0.05953 -0.17883 290 LYS   A O    
897  C  CB   . LYS   A 138 ? 0.97264 0.82249 0.90531 0.05093  -0.08381 -0.16700 290 LYS   A CB   
898  C  CG   . LYS   A 138 ? 1.03299 0.86289 0.95527 0.02823  -0.09120 -0.16420 290 LYS   A CG   
899  C  CD   . LYS   A 138 ? 1.12452 0.94469 1.03729 0.02717  -0.09372 -0.19510 290 LYS   A CD   
900  C  CE   . LYS   A 138 ? 1.15409 0.96218 1.05687 0.00311  -0.10122 -0.19365 290 LYS   A CE   
901  N  NZ   . LYS   A 138 ? 1.19403 0.94772 1.10712 -0.00319 -0.11338 -0.19192 290 LYS   A NZ   
902  N  N    . TYR   A 139 ? 0.75492 0.71811 0.66638 0.03172  -0.06104 -0.13778 291 TYR   A N    
903  C  CA   . TYR   A 139 ? 0.73935 0.74759 0.64034 0.02909  -0.05149 -0.13915 291 TYR   A CA   
904  C  C    . TYR   A 139 ? 0.77815 0.79249 0.66222 0.01328  -0.05442 -0.14385 291 TYR   A C    
905  O  O    . TYR   A 139 ? 0.75337 0.75077 0.63680 -0.00107 -0.06142 -0.13174 291 TYR   A O    
906  C  CB   . TYR   A 139 ? 0.69964 0.73209 0.60703 0.02506  -0.04613 -0.11438 291 TYR   A CB   
907  C  CG   . TYR   A 139 ? 0.67725 0.70183 0.60171 0.03684  -0.04618 -0.10592 291 TYR   A CG   
908  C  CD1  . TYR   A 139 ? 0.70852 0.75508 0.64192 0.05299  -0.03941 -0.11478 291 TYR   A CD1  
909  C  CD2  . TYR   A 139 ? 0.69992 0.69904 0.63160 0.03147  -0.05311 -0.08892 291 TYR   A CD2  
910  C  CE1  . TYR   A 139 ? 0.65164 0.69438 0.60194 0.06384  -0.04085 -0.10651 291 TYR   A CE1  
911  C  CE2  . TYR   A 139 ? 0.69670 0.69143 0.64234 0.04168  -0.05449 -0.08030 291 TYR   A CE2  
912  C  CZ   . TYR   A 139 ? 0.69712 0.71335 0.65258 0.05802  -0.04901 -0.08902 291 TYR   A CZ   
913  O  OH   . TYR   A 139 ? 0.69074 0.70557 0.66122 0.06804  -0.05179 -0.07981 291 TYR   A OH   
914  N  N    . ASP   A 140 ? 0.79833 0.84073 0.66892 0.01566  -0.04903 -0.16106 292 ASP   A N    
915  C  CA   . ASP   A 140 ? 0.82809 0.88604 0.68072 0.00123  -0.05175 -0.16509 292 ASP   A CA   
916  C  C    . ASP   A 140 ? 0.74720 0.85435 0.58992 -0.00114 -0.04251 -0.15542 292 ASP   A C    
917  O  O    . ASP   A 140 ? 0.70485 0.83108 0.55632 0.00580  -0.03432 -0.14368 292 ASP   A O    
918  C  CB   . ASP   A 140 ? 0.92023 0.96394 0.76211 0.00370  -0.05619 -0.19687 292 ASP   A CB   
919  C  CG   . ASP   A 140 ? 0.97177 1.03211 0.81204 0.02222  -0.04733 -0.22100 292 ASP   A CG   
920  O  OD1  . ASP   A 140 ? 1.03978 1.07002 0.88567 0.03317  -0.05086 -0.24471 292 ASP   A OD1  
921  O  OD2  . ASP   A 140 ? 0.95894 1.06257 0.79378 0.02591  -0.03674 -0.21628 292 ASP   A OD2  
922  N  N    . VAL   A 141 ? 0.75626 0.88479 0.58077 -0.01206 -0.04465 -0.15959 293 VAL   A N    
923  C  CA   . VAL   A 141 ? 0.71412 0.88803 0.52827 -0.01663 -0.03759 -0.14599 293 VAL   A CA   
924  C  C    . VAL   A 141 ? 0.73474 0.93994 0.54342 -0.00428 -0.02572 -0.15992 293 VAL   A C    
925  O  O    . VAL   A 141 ? 0.70796 0.94831 0.51496 -0.00609 -0.01763 -0.14366 293 VAL   A O    
926  C  CB   . VAL   A 141 ? 0.68007 0.87113 0.47556 -0.03125 -0.04449 -0.14554 293 VAL   A CB   
927  C  CG1  . VAL   A 141 ? 0.70350 0.86679 0.50784 -0.04288 -0.05570 -0.13327 293 VAL   A CG1  
928  C  CG2  . VAL   A 141 ? 0.68146 0.87845 0.45808 -0.02914 -0.04588 -0.17816 293 VAL   A CG2  
929  N  N    . THR   A 142 ? 0.78032 0.97394 0.58795 0.00829  -0.02425 -0.18963 294 THR   A N    
930  C  CA   . THR   A 142 ? 0.78421 1.00973 0.59074 0.02230  -0.01173 -0.20446 294 THR   A CA   
931  C  C    . THR   A 142 ? 0.73524 0.96431 0.56424 0.03123  -0.00501 -0.18718 294 THR   A C    
932  O  O    . THR   A 142 ? 0.70395 0.97371 0.53316 0.03433  0.00623  -0.18184 294 THR   A O    
933  C  CB   . THR   A 142 ? 0.83365 1.04126 0.63847 0.03624  -0.01239 -0.24215 294 THR   A CB   
934  O  OG1  . THR   A 142 ? 0.87469 1.08700 0.65602 0.02662  -0.01775 -0.26108 294 THR   A OG1  
935  C  CG2  . THR   A 142 ? 0.87329 1.11476 0.68229 0.05375  0.00150  -0.25863 294 THR   A CG2  
936  N  N    . ASP   A 143 ? 0.69491 0.88400 0.54262 0.03398  -0.01205 -0.17748 295 ASP   A N    
937  C  CA   . ASP   A 143 ? 0.68623 0.87904 0.55478 0.04141  -0.00742 -0.16147 295 ASP   A CA   
938  C  C    . ASP   A 143 ? 0.65661 0.87429 0.52548 0.02814  -0.00387 -0.13211 295 ASP   A C    
939  O  O    . ASP   A 143 ? 0.59467 0.83852 0.47412 0.03183  0.00438  -0.12268 295 ASP   A O    
940  C  CB   . ASP   A 143 ? 0.68105 0.82647 0.56632 0.04631  -0.01691 -0.15756 295 ASP   A CB   
941  C  CG   . ASP   A 143 ? 0.77524 0.89128 0.66386 0.06044  -0.02131 -0.18492 295 ASP   A CG   
942  O  OD1  . ASP   A 143 ? 0.84170 0.97924 0.72736 0.07293  -0.01400 -0.20820 295 ASP   A OD1  
943  O  OD2  . ASP   A 143 ? 0.79753 0.86939 0.69228 0.05894  -0.03186 -0.18342 295 ASP   A OD2  
944  N  N    . VAL   A 144 ? 0.60843 0.81875 0.46776 0.01272  -0.01034 -0.11774 296 VAL   A N    
945  C  CA   . VAL   A 144 ? 0.57398 0.80692 0.43392 0.00102  -0.00748 -0.09123 296 VAL   A CA   
946  C  C    . VAL   A 144 ? 0.63669 0.91685 0.48511 -0.00023 0.00271  -0.09138 296 VAL   A C    
947  O  O    . VAL   A 144 ? 0.60271 0.90599 0.45910 -0.00385 0.00925  -0.07319 296 VAL   A O    
948  C  CB   . VAL   A 144 ? 0.59261 0.81205 0.44543 -0.01312 -0.01670 -0.07816 296 VAL   A CB   
949  C  CG1  . VAL   A 144 ? 0.57225 0.80066 0.43489 -0.02178 -0.01554 -0.04990 296 VAL   A CG1  
950  C  CG2  . VAL   A 144 ? 0.54773 0.72487 0.40611 -0.01302 -0.02644 -0.08514 296 VAL   A CG2  
951  N  N    . SER   A 145 ? 0.67602 0.97220 0.50483 0.00126  0.00408  -0.11178 297 SER   A N    
952  C  CA   . SER   A 145 ? 0.70513 1.05092 0.51966 -0.00044 0.01459  -0.11317 297 SER   A CA   
953  C  C    . SER   A 145 ? 0.67275 1.04122 0.50181 0.01153  0.02657  -0.11886 297 SER   A C    
954  O  O    . SER   A 145 ? 0.59490 1.00241 0.42382 0.00613  0.03585  -0.10410 297 SER   A O    
955  C  CB   . SER   A 145 ? 0.74862 1.10682 0.53848 0.00031  0.01363  -0.13941 297 SER   A CB   
956  O  OG   . SER   A 145 ? 0.83300 1.20199 0.60425 -0.01508 0.00683  -0.12612 297 SER   A OG   
957  N  N    . LYS   A 146 ? 0.69067 1.03589 0.53407 0.02745  0.02597  -0.13875 298 LYS   A N    
958  C  CA   . LYS   A 146 ? 0.69609 1.06356 0.55684 0.04133  0.03617  -0.14634 298 LYS   A CA   
959  C  C    . LYS   A 146 ? 0.68046 1.04572 0.56393 0.03797  0.03651  -0.12087 298 LYS   A C    
960  O  O    . LYS   A 146 ? 0.65509 1.03399 0.55754 0.04958  0.04233  -0.12566 298 LYS   A O    
961  C  CB   . LYS   A 146 ? 0.72133 1.06256 0.59161 0.06122  0.03359  -0.17597 298 LYS   A CB   
962  C  CG   . LYS   A 146 ? 0.77005 1.11840 0.62043 0.06728  0.03545  -0.20804 298 LYS   A CG   
963  C  CD   . LYS   A 146 ? 0.85128 1.25492 0.67873 0.05730  0.04597  -0.20690 298 LYS   A CD   
964  C  CE   . LYS   A 146 ? 0.93433 1.36997 0.75288 0.07174  0.05658  -0.24231 298 LYS   A CE   
965  N  NZ   . LYS   A 146 ? 0.95358 1.42519 0.73887 0.05941  0.06019  -0.24875 298 LYS   A NZ   
966  N  N    . ALA   A 147 ? 0.65848 1.00769 0.54147 0.02289  0.02996  -0.09559 299 ALA   A N    
967  C  CA   . ALA   A 147 ? 0.60514 0.95797 0.50620 0.01609  0.03108  -0.07135 299 ALA   A CA   
968  C  C    . ALA   A 147 ? 0.58114 0.96470 0.47471 -0.00025 0.03605  -0.04865 299 ALA   A C    
969  O  O    . ALA   A 147 ? 0.47766 0.86123 0.38572 -0.00855 0.03610  -0.02765 299 ALA   A O    
970  C  CB   . ALA   A 147 ? 0.60999 0.91725 0.52038 0.01294  0.01961  -0.06071 299 ALA   A CB   
971  N  N    . GLY   A 148 ? 0.61939 1.02779 0.49045 -0.00569 0.03928  -0.05191 300 GLY   A N    
972  C  CA   . GLY   A 148 ? 0.59936 1.04017 0.46180 -0.02095 0.04388  -0.02867 300 GLY   A CA   
973  C  C    . GLY   A 148 ? 0.55117 0.97705 0.40009 -0.03348 0.03425  -0.01170 300 GLY   A C    
974  O  O    . GLY   A 148 ? 0.50577 0.95702 0.34688 -0.04594 0.03650  0.00984  300 GLY   A O    
975  N  N    . HIS   A 149 ? 0.52880 0.91627 0.37601 -0.03097 0.02334  -0.01910 301 HIS   A N    
976  C  CA   . HIS   A 149 ? 0.54064 0.91460 0.38058 -0.04186 0.01351  -0.00214 301 HIS   A CA   
977  C  C    . HIS   A 149 ? 0.56931 0.95836 0.38264 -0.04442 0.00995  -0.01411 301 HIS   A C    
978  O  O    . HIS   A 149 ? 0.55423 0.94639 0.35663 -0.03594 0.01209  -0.04170 301 HIS   A O    
979  C  CB   . HIS   A 149 ? 0.53251 0.86103 0.38739 -0.03985 0.00395  -0.00126 301 HIS   A CB   
980  C  CG   . HIS   A 149 ? 0.50797 0.82369 0.38617 -0.04118 0.00537  0.01481  301 HIS   A CG   
981  N  ND1  . HIS   A 149 ? 0.49815 0.82277 0.38396 -0.05141 0.00589  0.04025  301 HIS   A ND1  
982  C  CD2  . HIS   A 149 ? 0.46337 0.75859 0.35879 -0.03392 0.00577  0.00857  301 HIS   A CD2  
983  C  CE1  . HIS   A 149 ? 0.45744 0.76692 0.36411 -0.05082 0.00687  0.04653  301 HIS   A CE1  
984  N  NE2  . HIS   A 149 ? 0.46553 0.75892 0.37739 -0.04048 0.00668  0.02801  301 HIS   A NE2  
985  N  N    . THR   A 150 ? 0.63108 1.02929 0.43499 -0.05591 0.00367  0.00646  302 THR   A N    
986  C  CA   . THR   A 150 ? 0.60298 1.02356 0.38019 -0.06132 -0.00082 0.00054  302 THR   A CA   
987  C  C    . THR   A 150 ? 0.62735 1.02021 0.40467 -0.06507 -0.01503 0.00153  302 THR   A C    
988  O  O    . THR   A 150 ? 0.63443 0.99596 0.43228 -0.06510 -0.02042 0.01291  302 THR   A O    
989  C  CB   . THR   A 150 ? 0.62831 1.08930 0.39327 -0.07253 0.00218  0.02682  302 THR   A CB   
990  O  OG1  . THR   A 150 ? 0.64706 1.09182 0.42562 -0.08021 -0.00662 0.05714  302 THR   A OG1  
991  C  CG2  . THR   A 150 ? 0.61468 1.10236 0.38609 -0.07170 0.01651  0.03231  302 THR   A CG2  
992  N  N    . LEU   A 151 ? 0.62452 1.03315 0.37850 -0.06904 -0.02094 -0.01092 303 LEU   A N    
993  C  CA   . LEU   A 151 ? 0.60421 0.99199 0.35808 -0.07372 -0.03479 -0.01266 303 LEU   A CA   
994  C  C    . LEU   A 151 ? 0.57016 0.95271 0.33878 -0.08059 -0.04244 0.02008  303 LEU   A C    
995  O  O    . LEU   A 151 ? 0.55949 0.91809 0.33938 -0.08225 -0.05211 0.02104  303 LEU   A O    
996  C  CB   . LEU   A 151 ? 0.64393 1.05762 0.36876 -0.07907 -0.04032 -0.02957 303 LEU   A CB   
997  C  CG   . LEU   A 151 ? 0.72397 1.11077 0.44760 -0.08033 -0.05135 -0.05220 303 LEU   A CG   
998  C  CD1  . LEU   A 151 ? 0.77172 1.13208 0.49897 -0.06965 -0.04563 -0.08462 303 LEU   A CD1  
999  C  CD2  . LEU   A 151 ? 0.72209 1.13809 0.41933 -0.09013 -0.06096 -0.05973 303 LEU   A CD2  
1000 N  N    . GLU   A 152 ? 0.53812 0.94233 0.30878 -0.08454 -0.03819 0.04680  304 GLU   A N    
1001 C  CA   . GLU   A 152 ? 0.57006 0.96359 0.36018 -0.08852 -0.04460 0.07741  304 GLU   A CA   
1002 C  C    . GLU   A 152 ? 0.60297 0.95477 0.42019 -0.08295 -0.04606 0.07423  304 GLU   A C    
1003 O  O    . GLU   A 152 ? 0.53208 0.86981 0.36403 -0.08460 -0.05464 0.08733  304 GLU   A O    
1004 C  CB   . GLU   A 152 ? 0.62311 1.03590 0.41714 -0.09242 -0.03729 0.10342  304 GLU   A CB   
1005 C  CG   . GLU   A 152 ? 0.74789 1.20355 0.51777 -0.10109 -0.03888 0.11959  304 GLU   A CG   
1006 C  CD   . GLU   A 152 ? 0.88348 1.33823 0.66264 -0.10626 -0.05138 0.14863  304 GLU   A CD   
1007 O  OE1  . GLU   A 152 ? 0.91264 1.34988 0.69910 -0.10438 -0.06248 0.14588  304 GLU   A OE1  
1008 O  OE2  . GLU   A 152 ? 0.94181 1.41148 0.72580 -0.11150 -0.04991 0.17314  304 GLU   A OE2  
1009 N  N    . LEU   A 153 ? 0.56185 0.89623 0.38618 -0.07592 -0.03777 0.05699  305 LEU   A N    
1010 C  CA   . LEU   A 153 ? 0.47490 0.77263 0.32076 -0.07105 -0.03888 0.05192  305 LEU   A CA   
1011 C  C    . LEU   A 153 ? 0.50367 0.78171 0.34432 -0.06839 -0.04372 0.02733  305 LEU   A C    
1012 O  O    . LEU   A 153 ? 0.48985 0.74607 0.34259 -0.06986 -0.05039 0.02883  305 LEU   A O    
1013 C  CB   . LEU   A 153 ? 0.43602 0.72661 0.29460 -0.06560 -0.02864 0.05092  305 LEU   A CB   
1014 C  CG   . LEU   A 153 ? 0.44067 0.69757 0.31901 -0.06047 -0.02874 0.04539  305 LEU   A CG   
1015 C  CD1  . LEU   A 153 ? 0.42993 0.67313 0.32670 -0.06413 -0.03335 0.06475  305 LEU   A CD1  
1016 C  CD2  . LEU   A 153 ? 0.43967 0.69778 0.32561 -0.05469 -0.01936 0.03984  305 LEU   A CD2  
1017 N  N    . ILE   A 154 ? 0.51764 0.80345 0.34134 -0.06487 -0.04041 0.00437  306 ILE   A N    
1018 C  CA   . ILE   A 154 ? 0.59608 0.85648 0.41787 -0.06187 -0.04471 -0.01984 306 ILE   A CA   
1019 C  C    . ILE   A 154 ? 0.56906 0.82572 0.38664 -0.07064 -0.05671 -0.02002 306 ILE   A C    
1020 O  O    . ILE   A 154 ? 0.53154 0.76034 0.35970 -0.07199 -0.06213 -0.02579 306 ILE   A O    
1021 C  CB   . ILE   A 154 ? 0.65243 0.92234 0.45800 -0.05517 -0.03907 -0.04631 306 ILE   A CB   
1022 C  CG1  . ILE   A 154 ? 0.68823 0.95903 0.50408 -0.04492 -0.02779 -0.04817 306 ILE   A CG1  
1023 C  CG2  . ILE   A 154 ? 0.63317 0.87424 0.43638 -0.05362 -0.04570 -0.07092 306 ILE   A CG2  
1024 C  CD1  . ILE   A 154 ? 0.72791 1.03788 0.53692 -0.04609 -0.01854 -0.03657 306 ILE   A CD1  
1025 N  N    . GLU   A 155 ? 0.56563 0.85281 0.36804 -0.07761 -0.06142 -0.01260 307 GLU   A N    
1026 C  CA   . GLU   A 155 ? 0.59849 0.88759 0.39726 -0.08639 -0.07393 -0.01373 307 GLU   A CA   
1027 C  C    . GLU   A 155 ? 0.58882 0.86045 0.41205 -0.08874 -0.07924 0.00414  307 GLU   A C    
1028 O  O    . GLU   A 155 ? 0.68067 0.93159 0.51145 -0.09221 -0.08505 -0.00597 307 GLU   A O    
1029 C  CB   . GLU   A 155 ? 0.62768 0.95749 0.40537 -0.09302 -0.07864 -0.00606 307 GLU   A CB   
1030 C  CG   . GLU   A 155 ? 0.70727 1.04578 0.47750 -0.10269 -0.09265 -0.01193 307 GLU   A CG   
1031 C  CD   . GLU   A 155 ? 0.71644 1.06637 0.50177 -0.10739 -0.10185 0.01656  307 GLU   A CD   
1032 O  OE1  . GLU   A 155 ? 0.68654 1.03382 0.48840 -0.10287 -0.09743 0.04025  307 GLU   A OE1  
1033 O  OE2  . GLU   A 155 ? 0.74534 1.10717 0.52763 -0.11544 -0.11410 0.01436  307 GLU   A OE2  
1034 N  N    . PRO   A 156 ? 0.54369 0.82178 0.38127 -0.08722 -0.07727 0.02954  308 PRO   A N    
1035 C  CA   . PRO   A 156 ? 0.55503 0.81625 0.41741 -0.08759 -0.08103 0.04209  308 PRO   A CA   
1036 C  C    . PRO   A 156 ? 0.54074 0.76923 0.41668 -0.08326 -0.07546 0.03226  308 PRO   A C    
1037 O  O    . PRO   A 156 ? 0.55664 0.77191 0.44857 -0.08545 -0.07903 0.03520  308 PRO   A O    
1038 C  CB   . PRO   A 156 ? 0.57174 0.84507 0.44577 -0.08533 -0.07918 0.06873  308 PRO   A CB   
1039 C  CG   . PRO   A 156 ? 0.58135 0.86961 0.44014 -0.08366 -0.07137 0.07006  308 PRO   A CG   
1040 C  CD   . PRO   A 156 ? 0.51713 0.81865 0.35005 -0.08600 -0.07208 0.04815  308 PRO   A CD   
1041 N  N    . LEU   A 157 ? 0.53029 0.74839 0.40058 -0.07723 -0.06706 0.02119  309 LEU   A N    
1042 C  CA   . LEU   A 157 ? 0.47117 0.65983 0.35288 -0.07292 -0.06314 0.01327  309 LEU   A CA   
1043 C  C    . LEU   A 157 ? 0.49144 0.66110 0.36939 -0.07704 -0.06923 -0.00383 309 LEU   A C    
1044 O  O    . LEU   A 157 ? 0.44719 0.59709 0.33811 -0.07932 -0.07094 -0.00202 309 LEU   A O    
1045 C  CB   . LEU   A 157 ? 0.46958 0.65634 0.34758 -0.06463 -0.05387 0.00653  309 LEU   A CB   
1046 C  CG   . LEU   A 157 ? 0.48409 0.64289 0.37141 -0.05894 -0.05092 -0.00224 309 LEU   A CG   
1047 C  CD1  . LEU   A 157 ? 0.47609 0.62287 0.38185 -0.06055 -0.05086 0.01197  309 LEU   A CD1  
1048 C  CD2  . LEU   A 157 ? 0.47936 0.64303 0.36461 -0.04990 -0.04264 -0.00881 309 LEU   A CD2  
1049 N  N    . ILE   A 158 ? 0.51896 0.69449 0.37903 -0.07882 -0.07239 -0.02107 310 ILE   A N    
1050 C  CA   . ILE   A 158 ? 0.63234 0.78791 0.48922 -0.08464 -0.07955 -0.03817 310 ILE   A CA   
1051 C  C    . ILE   A 158 ? 0.61650 0.77785 0.48198 -0.09598 -0.08855 -0.02893 310 ILE   A C    
1052 O  O    . ILE   A 158 ? 0.66016 0.80063 0.53509 -0.10205 -0.09256 -0.03225 310 ILE   A O    
1053 C  CB   . ILE   A 158 ? 0.69958 0.86245 0.53523 -0.08416 -0.08124 -0.06118 310 ILE   A CB   
1054 C  CG1  . ILE   A 158 ? 0.68249 0.83778 0.51423 -0.07127 -0.07183 -0.07325 310 ILE   A CG1  
1055 C  CG2  . ILE   A 158 ? 0.70708 0.84938 0.54019 -0.09307 -0.09079 -0.07884 310 ILE   A CG2  
1056 C  CD1  . ILE   A 158 ? 0.65696 0.77333 0.49902 -0.06639 -0.07213 -0.08384 310 ILE   A CD1  
1057 N  N    . LYS   A 159 ? 0.54582 0.73735 0.40939 -0.09924 -0.09216 -0.01594 311 LYS   A N    
1058 C  CA   . LYS   A 159 ? 0.58383 0.78549 0.45960 -0.10826 -0.10086 -0.00598 311 LYS   A CA   
1059 C  C    . LYS   A 159 ? 0.55789 0.74559 0.45732 -0.10637 -0.09699 0.00724  311 LYS   A C    
1060 O  O    . LYS   A 159 ? 0.56099 0.74574 0.47289 -0.11412 -0.10191 0.00842  311 LYS   A O    
1061 C  CB   . LYS   A 159 ? 0.51410 0.75150 0.38563 -0.10970 -0.10605 0.00863  311 LYS   A CB   
1062 C  CG   . LYS   A 159 ? 0.65925 0.91710 0.51241 -0.11889 -0.11636 -0.00353 311 LYS   A CG   
1063 C  CD   . LYS   A 159 ? 0.77890 1.07039 0.61536 -0.11698 -0.11740 0.00642  311 LYS   A CD   
1064 C  CE   . LYS   A 159 ? 0.83276 1.15572 0.67142 -0.12469 -0.13051 0.01916  311 LYS   A CE   
1065 N  NZ   . LYS   A 159 ? 0.84804 1.20559 0.66047 -0.12736 -0.13491 0.02038  311 LYS   A NZ   
1066 N  N    . PHE   A 160 ? 0.48140 0.66275 0.38724 -0.09696 -0.08792 0.01636  312 PHE   A N    
1067 C  CA   . PHE   A 160 ? 0.52119 0.68931 0.44685 -0.09481 -0.08341 0.02533  312 PHE   A CA   
1068 C  C    . PHE   A 160 ? 0.56797 0.70893 0.49417 -0.09819 -0.08254 0.01395  312 PHE   A C    
1069 O  O    . PHE   A 160 ? 0.55212 0.68871 0.49126 -0.10421 -0.08401 0.01769  312 PHE   A O    
1070 C  CB   . PHE   A 160 ? 0.50602 0.67288 0.43679 -0.08524 -0.07476 0.03496  312 PHE   A CB   
1071 C  CG   . PHE   A 160 ? 0.47239 0.62333 0.41889 -0.08251 -0.06916 0.03882  312 PHE   A CG   
1072 C  CD1  . PHE   A 160 ? 0.47960 0.63823 0.44506 -0.08269 -0.06929 0.04977  312 PHE   A CD1  
1073 C  CD2  . PHE   A 160 ? 0.49876 0.62917 0.44136 -0.07911 -0.06404 0.03089  312 PHE   A CD2  
1074 C  CE1  . PHE   A 160 ? 0.53806 0.68515 0.51591 -0.08049 -0.06349 0.05093  312 PHE   A CE1  
1075 C  CE2  . PHE   A 160 ? 0.56472 0.68396 0.51909 -0.07753 -0.05952 0.03451  312 PHE   A CE2  
1076 C  CZ   . PHE   A 160 ? 0.56221 0.69033 0.53302 -0.07874 -0.05881 0.04365  312 PHE   A CZ   
1077 N  N    . GLN   A 161 ? 0.58373 0.70742 0.49701 -0.09412 -0.08009 0.00089  313 GLN   A N    
1078 C  CA   . GLN   A 161 ? 0.54923 0.64384 0.46328 -0.09644 -0.08060 -0.00793 313 GLN   A CA   
1079 C  C    . GLN   A 161 ? 0.58855 0.67805 0.50362 -0.10982 -0.08934 -0.01377 313 GLN   A C    
1080 O  O    . GLN   A 161 ? 0.59751 0.67187 0.52196 -0.11657 -0.09020 -0.01026 313 GLN   A O    
1081 C  CB   . GLN   A 161 ? 0.56661 0.64574 0.46821 -0.08798 -0.07807 -0.02242 313 GLN   A CB   
1082 C  CG   . GLN   A 161 ? 0.51123 0.59583 0.41412 -0.07591 -0.06928 -0.01714 313 GLN   A CG   
1083 C  CD   . GLN   A 161 ? 0.52464 0.59727 0.44073 -0.07375 -0.06524 -0.00628 313 GLN   A CD   
1084 O  OE1  . GLN   A 161 ? 0.55858 0.61118 0.47870 -0.07817 -0.06797 -0.00666 313 GLN   A OE1  
1085 N  NE2  . GLN   A 161 ? 0.49064 0.57596 0.41293 -0.06802 -0.05899 0.00358  313 GLN   A NE2  
1086 N  N    . VAL   A 162 ? 0.59011 0.69450 0.49530 -0.11519 -0.09612 -0.02219 314 VAL   A N    
1087 C  CA   . VAL   A 162 ? 0.58919 0.69262 0.49631 -0.12989 -0.10568 -0.02848 314 VAL   A CA   
1088 C  C    . VAL   A 162 ? 0.56259 0.68313 0.48901 -0.13729 -0.10692 -0.01239 314 VAL   A C    
1089 O  O    . VAL   A 162 ? 0.50552 0.61553 0.44171 -0.14833 -0.10966 -0.01164 314 VAL   A O    
1090 C  CB   . VAL   A 162 ? 0.64990 0.77240 0.54129 -0.13389 -0.11309 -0.04092 314 VAL   A CB   
1091 C  CG1  . VAL   A 162 ? 0.61205 0.74468 0.50934 -0.15042 -0.12398 -0.04325 314 VAL   A CG1  
1092 C  CG2  . VAL   A 162 ? 0.69713 0.79926 0.57095 -0.12867 -0.11237 -0.06288 314 VAL   A CG2  
1093 N  N    . GLY   A 163 ? 0.56506 0.71296 0.49858 -0.13127 -0.10483 0.00098  315 GLY   A N    
1094 C  CA   . GLY   A 163 ? 0.49143 0.65865 0.44597 -0.13565 -0.10580 0.01443  315 GLY   A CA   
1095 C  C    . GLY   A 163 ? 0.50970 0.66234 0.47750 -0.13445 -0.09774 0.02085  315 GLY   A C    
1096 O  O    . GLY   A 163 ? 0.44819 0.60910 0.43107 -0.14322 -0.09863 0.02557  315 GLY   A O    
1097 N  N    . LEU   A 164 ? 0.49009 0.62429 0.45226 -0.12424 -0.08973 0.02098  316 LEU   A N    
1098 C  CA   . LEU   A 164 ? 0.49467 0.61578 0.46557 -0.12365 -0.08270 0.02608  316 LEU   A CA   
1099 C  C    . LEU   A 164 ? 0.55058 0.65047 0.51856 -0.13562 -0.08592 0.02098  316 LEU   A C    
1100 O  O    . LEU   A 164 ? 0.57965 0.68275 0.55884 -0.14360 -0.08382 0.02767  316 LEU   A O    
1101 C  CB   . LEU   A 164 ? 0.45802 0.56580 0.42259 -0.11103 -0.07529 0.02647  316 LEU   A CB   
1102 C  CG   . LEU   A 164 ? 0.48977 0.58898 0.46176 -0.10924 -0.06817 0.03210  316 LEU   A CG   
1103 C  CD1  . LEU   A 164 ? 0.45000 0.57154 0.44024 -0.11109 -0.06501 0.04035  316 LEU   A CD1  
1104 C  CD2  . LEU   A 164 ? 0.46841 0.55963 0.43528 -0.09725 -0.06239 0.03197  316 LEU   A CD2  
1105 N  N    . LYS   A 165 ? 0.58362 0.66173 0.53716 -0.13718 -0.09087 0.00911  317 LYS   A N    
1106 C  CA   . LYS   A 165 ? 0.64625 0.69955 0.59840 -0.14948 -0.09579 0.00461  317 LYS   A CA   
1107 C  C    . LYS   A 165 ? 0.68200 0.75153 0.64520 -0.16674 -0.10197 0.00708  317 LYS   A C    
1108 O  O    . LYS   A 165 ? 0.67250 0.73062 0.64222 -0.17943 -0.10299 0.01180  317 LYS   A O    
1109 C  CB   . LYS   A 165 ? 0.68100 0.70878 0.61789 -0.14653 -0.10091 -0.01181 317 LYS   A CB   
1110 C  CG   . LYS   A 165 ? 0.73248 0.72208 0.66772 -0.15062 -0.10326 -0.01427 317 LYS   A CG   
1111 C  CD   . LYS   A 165 ? 0.77689 0.75187 0.70958 -0.13597 -0.09643 -0.00941 317 LYS   A CD   
1112 C  CE   . LYS   A 165 ? 0.80282 0.73770 0.73332 -0.13747 -0.10095 -0.01224 317 LYS   A CE   
1113 N  NZ   . LYS   A 165 ? 0.75213 0.67632 0.68155 -0.12308 -0.09564 -0.00590 317 LYS   A NZ   
1114 N  N    . LYS   A 166 ? 0.67740 0.77603 0.64363 -0.16807 -0.10646 0.00556  318 LYS   A N    
1115 C  CA   . LYS   A 166 ? 0.71059 0.83124 0.68996 -0.18403 -0.11319 0.00793  318 LYS   A CA   
1116 C  C    . LYS   A 166 ? 0.69019 0.82885 0.68947 -0.18789 -0.10659 0.02216  318 LYS   A C    
1117 O  O    . LYS   A 166 ? 0.60391 0.75177 0.61506 -0.20430 -0.10990 0.02501  318 LYS   A O    
1118 C  CB   . LYS   A 166 ? 0.69846 0.85155 0.67798 -0.18185 -0.11963 0.00619  318 LYS   A CB   
1119 C  CG   . LYS   A 166 ? 0.86459 1.04150 0.85628 -0.19940 -0.12955 0.00544  318 LYS   A CG   
1120 C  CD   . LYS   A 166 ? 0.87484 1.09382 0.88801 -0.19529 -0.12849 0.01933  318 LYS   A CD   
1121 C  CE   . LYS   A 166 ? 0.90281 1.15481 0.92308 -0.20639 -0.14125 0.01726  318 LYS   A CE   
1122 N  NZ   . LYS   A 166 ? 0.89540 1.18768 0.93452 -0.19631 -0.14178 0.03082  318 LYS   A NZ   
1123 N  N    . LEU   A 167 ? 0.68586 0.83225 0.68983 -0.17358 -0.09703 0.03019  319 LEU   A N    
1124 C  CA   . LEU   A 167 ? 0.64053 0.80624 0.66263 -0.17553 -0.08949 0.04058  319 LEU   A CA   
1125 C  C    . LEU   A 167 ? 0.63451 0.78107 0.65481 -0.18766 -0.08633 0.04400  319 LEU   A C    
1126 O  O    . LEU   A 167 ? 0.60684 0.77398 0.64187 -0.19635 -0.08180 0.05152  319 LEU   A O    
1127 C  CB   . LEU   A 167 ? 0.56817 0.74106 0.59402 -0.15754 -0.08039 0.04525  319 LEU   A CB   
1128 C  CG   . LEU   A 167 ? 0.52912 0.72085 0.55904 -0.14586 -0.08347 0.04622  319 LEU   A CG   
1129 C  CD1  . LEU   A 167 ? 0.50039 0.69213 0.53447 -0.12974 -0.07496 0.05056  319 LEU   A CD1  
1130 C  CD2  . LEU   A 167 ? 0.53297 0.76012 0.58291 -0.15161 -0.08906 0.05045  319 LEU   A CD2  
1131 N  N    . ASN   A 168 ? 0.67414 0.78352 0.67761 -0.18850 -0.08890 0.03928  320 ASN   A N    
1132 C  CA   . ASN   A 168 ? 0.74980 0.83617 0.75019 -0.19981 -0.08775 0.04522  320 ASN   A CA   
1133 C  C    . ASN   A 168 ? 0.68132 0.78345 0.68827 -0.19693 -0.07668 0.05647  320 ASN   A C    
1134 O  O    . ASN   A 168 ? 0.71636 0.82974 0.73139 -0.21124 -0.07386 0.06534  320 ASN   A O    
1135 C  CB   . ASN   A 168 ? 0.85153 0.93810 0.85937 -0.22239 -0.09548 0.04576  320 ASN   A CB   
1136 C  CG   . ASN   A 168 ? 0.98137 1.02360 0.97826 -0.23184 -0.10183 0.04406  320 ASN   A CG   
1137 O  OD1  . ASN   A 168 ? 1.02039 1.04626 1.01483 -0.23584 -0.09815 0.05505  320 ASN   A OD1  
1138 N  ND2  . ASN   A 168 ? 1.03795 1.06039 1.02817 -0.23515 -0.11195 0.03006  320 ASN   A ND2  
1139 N  N    . LEU   A 169 ? 0.58429 0.68960 0.58771 -0.17911 -0.07020 0.05538  321 LEU   A N    
1140 C  CA   . LEU   A 169 ? 0.56602 0.68986 0.57567 -0.17462 -0.05966 0.06204  321 LEU   A CA   
1141 C  C    . LEU   A 169 ? 0.51990 0.62837 0.52110 -0.18421 -0.05716 0.07084  321 LEU   A C    
1142 O  O    . LEU   A 169 ? 0.51190 0.58686 0.50011 -0.18592 -0.06286 0.07163  321 LEU   A O    
1143 C  CB   . LEU   A 169 ? 0.53499 0.65775 0.54082 -0.15522 -0.05488 0.05793  321 LEU   A CB   
1144 C  CG   . LEU   A 169 ? 0.50447 0.64266 0.51831 -0.14470 -0.05677 0.05298  321 LEU   A CG   
1145 C  CD1  . LEU   A 169 ? 0.45547 0.58920 0.46594 -0.12840 -0.05177 0.05098  321 LEU   A CD1  
1146 C  CD2  . LEU   A 169 ? 0.50862 0.68183 0.54356 -0.14808 -0.05468 0.05572  321 LEU   A CD2  
1147 N  N    . HIS   A 170 ? 0.57480 0.70948 0.58406 -0.19046 -0.04880 0.07783  322 HIS   A N    
1148 C  CA   . HIS   A 170 ? 0.55858 0.68485 0.55685 -0.19559 -0.04446 0.08738  322 HIS   A CA   
1149 C  C    . HIS   A 170 ? 0.54218 0.65462 0.52875 -0.17807 -0.04205 0.08352  322 HIS   A C    
1150 O  O    . HIS   A 170 ? 0.59759 0.71996 0.58930 -0.16357 -0.03903 0.07473  322 HIS   A O    
1151 C  CB   . HIS   A 170 ? 0.50567 0.67040 0.51387 -0.20417 -0.03404 0.09324  322 HIS   A CB   
1152 C  CG   . HIS   A 170 ? 0.51036 0.69438 0.53216 -0.22349 -0.03541 0.09875  322 HIS   A CG   
1153 N  ND1  . HIS   A 170 ? 0.52594 0.75101 0.56021 -0.23251 -0.02556 0.10321  322 HIS   A ND1  
1154 C  CD2  . HIS   A 170 ? 0.54240 0.71269 0.56824 -0.23630 -0.04540 0.09948  322 HIS   A CD2  
1155 C  CE1  . HIS   A 170 ? 0.55521 0.79247 0.60190 -0.25060 -0.02943 0.10804  322 HIS   A CE1  
1156 N  NE2  . HIS   A 170 ? 0.53196 0.73518 0.57353 -0.25377 -0.04201 0.10568  322 HIS   A NE2  
1157 N  N    . GLU   A 171 ? 0.49209 0.58144 0.46399 -0.17996 -0.04428 0.09128  323 GLU   A N    
1158 C  CA   . GLU   A 171 ? 0.49308 0.57436 0.45526 -0.16475 -0.04229 0.08835  323 GLU   A CA   
1159 C  C    . GLU   A 171 ? 0.42730 0.54100 0.39532 -0.15818 -0.03169 0.08353  323 GLU   A C    
1160 O  O    . GLU   A 171 ? 0.46680 0.58091 0.43557 -0.14383 -0.02974 0.07491  323 GLU   A O    
1161 C  CB   . GLU   A 171 ? 0.56747 0.62649 0.51501 -0.16904 -0.04641 0.10034  323 GLU   A CB   
1162 C  CG   . GLU   A 171 ? 0.64088 0.69158 0.57934 -0.15350 -0.04657 0.09739  323 GLU   A CG   
1163 C  CD   . GLU   A 171 ? 0.70103 0.72535 0.62720 -0.15519 -0.05406 0.10976  323 GLU   A CD   
1164 O  OE1  . GLU   A 171 ? 0.75664 0.78371 0.67711 -0.16919 -0.05415 0.12457  323 GLU   A OE1  
1165 O  OE2  . GLU   A 171 ? 0.74510 0.74743 0.66825 -0.14243 -0.05994 0.10565  323 GLU   A OE2  
1166 N  N    . GLU   A 172 ? 0.44334 0.58532 0.41708 -0.16902 -0.02451 0.08800  324 GLU   A N    
1167 C  CA   . GLU   A 172 ? 0.43653 0.61113 0.41887 -0.16231 -0.01381 0.07995  324 GLU   A CA   
1168 C  C    . GLU   A 172 ? 0.44286 0.62350 0.44129 -0.14873 -0.01339 0.06789  324 GLU   A C    
1169 O  O    . GLU   A 172 ? 0.49062 0.67733 0.49234 -0.13621 -0.00875 0.05905  324 GLU   A O    
1170 C  CB   . GLU   A 172 ? 0.41711 0.62521 0.40693 -0.17648 -0.00598 0.08512  324 GLU   A CB   
1171 C  CG   . GLU   A 172 ? 0.47005 0.68067 0.44276 -0.19025 -0.00387 0.09876  324 GLU   A CG   
1172 C  CD   . GLU   A 172 ? 0.50177 0.68632 0.46754 -0.20600 -0.01335 0.11442  324 GLU   A CD   
1173 O  OE1  . GLU   A 172 ? 0.52298 0.68355 0.49464 -0.20490 -0.02216 0.11187  324 GLU   A OE1  
1174 O  OE2  . GLU   A 172 ? 0.51842 0.70634 0.47249 -0.22010 -0.01224 0.12940  324 GLU   A OE2  
1175 N  N    . GLU   A 173 ? 0.37463 0.55344 0.38326 -0.15185 -0.01909 0.06805  325 GLU   A N    
1176 C  CA   . GLU   A 173 ? 0.39883 0.58386 0.42170 -0.13976 -0.02040 0.06010  325 GLU   A CA   
1177 C  C    . GLU   A 173 ? 0.38017 0.53836 0.39302 -0.12824 -0.02574 0.05657  325 GLU   A C    
1178 O  O    . GLU   A 173 ? 0.40955 0.57179 0.43079 -0.11620 -0.02446 0.05115  325 GLU   A O    
1179 C  CB   . GLU   A 173 ? 0.39376 0.58916 0.42900 -0.14788 -0.02610 0.06211  325 GLU   A CB   
1180 C  CG   . GLU   A 173 ? 0.40826 0.63833 0.45923 -0.15862 -0.02005 0.06501  325 GLU   A CG   
1181 C  CD   . GLU   A 173 ? 0.47060 0.70450 0.52687 -0.17509 -0.02730 0.07051  325 GLU   A CD   
1182 O  OE1  . GLU   A 173 ? 0.48407 0.68951 0.52884 -0.17935 -0.03710 0.07128  325 GLU   A OE1  
1183 O  OE2  . GLU   A 173 ? 0.50398 0.77104 0.57702 -0.18425 -0.02302 0.07291  325 GLU   A OE2  
1184 N  N    . HIS   A 174 ? 0.37930 0.51063 0.37587 -0.13173 -0.03173 0.06005  326 HIS   A N    
1185 C  CA   . HIS   A 174 ? 0.45514 0.56501 0.44301 -0.12073 -0.03583 0.05603  326 HIS   A CA   
1186 C  C    . HIS   A 174 ? 0.44134 0.55402 0.42736 -0.11077 -0.03020 0.05285  326 HIS   A C    
1187 O  O    . HIS   A 174 ? 0.37709 0.48891 0.36730 -0.10045 -0.02979 0.04798  326 HIS   A O    
1188 C  CB   . HIS   A 174 ? 0.52330 0.60497 0.49704 -0.12536 -0.04310 0.05921  326 HIS   A CB   
1189 C  CG   . HIS   A 174 ? 0.58969 0.65292 0.55602 -0.11377 -0.04682 0.05372  326 HIS   A CG   
1190 N  ND1  . HIS   A 174 ? 0.58408 0.64710 0.55245 -0.10865 -0.04993 0.04739  326 HIS   A ND1  
1191 C  CD2  . HIS   A 174 ? 0.58363 0.63203 0.54104 -0.10641 -0.04772 0.05386  326 HIS   A CD2  
1192 C  CE1  . HIS   A 174 ? 0.60475 0.65437 0.56564 -0.09896 -0.05138 0.04321  326 HIS   A CE1  
1193 N  NE2  . HIS   A 174 ? 0.61460 0.65516 0.57024 -0.09693 -0.05028 0.04680  326 HIS   A NE2  
1194 N  N    . VAL   A 175 ? 0.44048 0.55801 0.41994 -0.11505 -0.02614 0.05597  327 VAL   A N    
1195 C  CA   . VAL   A 175 ? 0.37205 0.49369 0.34888 -0.10706 -0.02176 0.05119  327 VAL   A CA   
1196 C  C    . VAL   A 175 ? 0.39079 0.53327 0.38363 -0.10137 -0.01464 0.04283  327 VAL   A C    
1197 O  O    . VAL   A 175 ? 0.38812 0.52867 0.38477 -0.09244 -0.01305 0.03632  327 VAL   A O    
1198 C  CB   . VAL   A 175 ? 0.43503 0.55860 0.39796 -0.11371 -0.02048 0.05712  327 VAL   A CB   
1199 C  CG1  . VAL   A 175 ? 0.46088 0.55912 0.41117 -0.11696 -0.02908 0.06642  327 VAL   A CG1  
1200 C  CG2  . VAL   A 175 ? 0.41456 0.56186 0.38018 -0.12473 -0.01400 0.06029  327 VAL   A CG2  
1201 N  N    . LEU   A 176 ? 0.41073 0.57310 0.41552 -0.10620 -0.01069 0.04273  328 LEU   A N    
1202 C  CA   . LEU   A 176 ? 0.41414 0.59553 0.43800 -0.09853 -0.00445 0.03415  328 LEU   A CA   
1203 C  C    . LEU   A 176 ? 0.40417 0.57589 0.43929 -0.08863 -0.00895 0.03291  328 LEU   A C    
1204 O  O    . LEU   A 176 ? 0.40805 0.58217 0.45532 -0.07934 -0.00588 0.02633  328 LEU   A O    
1205 C  CB   . LEU   A 176 ? 0.36638 0.57442 0.40334 -0.10505 0.00020  0.03495  328 LEU   A CB   
1206 C  CG   . LEU   A 176 ? 0.39441 0.62443 0.42630 -0.11227 0.00914  0.03280  328 LEU   A CG   
1207 C  CD1  . LEU   A 176 ? 0.39075 0.64836 0.43501 -0.12164 0.01299  0.03645  328 LEU   A CD1  
1208 C  CD2  . LEU   A 176 ? 0.39812 0.63958 0.43717 -0.10193 0.01705  0.01865  328 LEU   A CD2  
1209 N  N    . LEU   A 177 ? 0.39872 0.55931 0.42960 -0.09111 -0.01649 0.03919  329 LEU   A N    
1210 C  CA   . LEU   A 177 ? 0.38359 0.53884 0.42226 -0.08319 -0.02095 0.04009  329 LEU   A CA   
1211 C  C    . LEU   A 177 ? 0.38617 0.52447 0.41658 -0.07674 -0.02160 0.03839  329 LEU   A C    
1212 O  O    . LEU   A 177 ? 0.31419 0.45163 0.35486 -0.06928 -0.02155 0.03805  329 LEU   A O    
1213 C  CB   . LEU   A 177 ? 0.37160 0.52381 0.40562 -0.08885 -0.02868 0.04528  329 LEU   A CB   
1214 C  CG   . LEU   A 177 ? 0.34947 0.50269 0.38941 -0.08284 -0.03413 0.04814  329 LEU   A CG   
1215 C  CD1  . LEU   A 177 ? 0.31876 0.49061 0.38199 -0.07620 -0.03233 0.04941  329 LEU   A CD1  
1216 C  CD2  . LEU   A 177 ? 0.34845 0.50027 0.37990 -0.09052 -0.04186 0.05023  329 LEU   A CD2  
1217 N  N    . MET   A 178 ? 0.35779 0.48329 0.37139 -0.07977 -0.02264 0.03844  330 MET   A N    
1218 C  CA   . MET   A 178 ? 0.42011 0.53472 0.42830 -0.07401 -0.02280 0.03630  330 MET   A CA   
1219 C  C    . MET   A 178 ? 0.41331 0.53466 0.43154 -0.07000 -0.01719 0.02993  330 MET   A C    
1220 O  O    . MET   A 178 ? 0.37633 0.49308 0.40123 -0.06479 -0.01719 0.02851  330 MET   A O    
1221 C  CB   . MET   A 178 ? 0.43814 0.54075 0.42942 -0.07673 -0.02552 0.03771  330 MET   A CB   
1222 C  CG   . MET   A 178 ? 0.52051 0.61038 0.50316 -0.07735 -0.03165 0.04050  330 MET   A CG   
1223 S  SD   . MET   A 178 ? 0.53080 0.60345 0.49838 -0.07636 -0.03580 0.04179  330 MET   A SD   
1224 C  CE   . MET   A 178 ? 0.42089 0.49494 0.38293 -0.08673 -0.03531 0.04773  330 MET   A CE   
1225 N  N    . ALA   A 179 ? 0.40240 0.53561 0.42226 -0.07317 -0.01218 0.02545  331 ALA   A N    
1226 C  CA   . ALA   A 179 ? 0.36859 0.50831 0.39676 -0.06949 -0.00666 0.01554  331 ALA   A CA   
1227 C  C    . ALA   A 179 ? 0.38602 0.52910 0.43678 -0.06234 -0.00484 0.01219  331 ALA   A C    
1228 O  O    . ALA   A 179 ? 0.38111 0.51784 0.44132 -0.05745 -0.00371 0.00622  331 ALA   A O    
1229 C  CB   . ALA   A 179 ? 0.37205 0.52771 0.39383 -0.07501 -0.00103 0.01054  331 ALA   A CB   
1230 N  N    . ILE   A 180 ? 0.38017 0.53303 0.44142 -0.06190 -0.00539 0.01652  332 ILE   A N    
1231 C  CA   . ILE   A 180 ? 0.35730 0.51330 0.44191 -0.05361 -0.00564 0.01636  332 ILE   A CA   
1232 C  C    . ILE   A 180 ? 0.37327 0.51280 0.45918 -0.05002 -0.01136 0.02391  332 ILE   A C    
1233 O  O    . ILE   A 180 ? 0.45558 0.58844 0.55760 -0.04358 -0.01111 0.02237  332 ILE   A O    
1234 C  CB   . ILE   A 180 ? 0.31136 0.48451 0.40626 -0.05460 -0.00701 0.02162  332 ILE   A CB   
1235 C  CG1  . ILE   A 180 ? 0.28772 0.48284 0.38788 -0.05726 0.00085  0.01325  332 ILE   A CG1  
1236 C  CG2  . ILE   A 180 ? 0.31282 0.48740 0.43042 -0.04533 -0.01082 0.02646  332 ILE   A CG2  
1237 C  CD1  . ILE   A 180 ? 0.31313 0.52833 0.41912 -0.06309 -0.00045 0.01943  332 ILE   A CD1  
1238 N  N    . CYS   A 181 ? 0.39579 0.52883 0.46528 -0.05447 -0.01642 0.03206  333 CYS   A N    
1239 C  CA   . CYS   A 181 ? 0.43075 0.55290 0.49796 -0.05251 -0.02055 0.03921  333 CYS   A CA   
1240 C  C    . CYS   A 181 ? 0.40878 0.52093 0.47951 -0.05081 -0.01788 0.03427  333 CYS   A C    
1241 O  O    . CYS   A 181 ? 0.42340 0.52918 0.50647 -0.04768 -0.01926 0.03900  333 CYS   A O    
1242 C  CB   . CYS   A 181 ? 0.36888 0.48713 0.41536 -0.05722 -0.02435 0.04326  333 CYS   A CB   
1243 S  SG   . CYS   A 181 ? 0.40861 0.52140 0.44988 -0.05557 -0.02789 0.05137  333 CYS   A SG   
1244 N  N    . ILE   A 182 ? 0.39737 0.50870 0.45793 -0.05385 -0.01477 0.02565  334 ILE   A N    
1245 C  CA   . ILE   A 182 ? 0.38348 0.48765 0.44553 -0.05419 -0.01349 0.02013  334 ILE   A CA   
1246 C  C    . ILE   A 182 ? 0.43290 0.53414 0.51565 -0.05039 -0.01050 0.01207  334 ILE   A C    
1247 O  O    . ILE   A 182 ? 0.42370 0.51455 0.51787 -0.04966 -0.01179 0.01372  334 ILE   A O    
1248 C  CB   . ILE   A 182 ? 0.42135 0.52877 0.46667 -0.05835 -0.01242 0.01366  334 ILE   A CB   
1249 C  CG1  . ILE   A 182 ? 0.40276 0.50776 0.43121 -0.06012 -0.01644 0.02140  334 ILE   A CG1  
1250 C  CG2  . ILE   A 182 ? 0.39904 0.50372 0.44791 -0.05959 -0.01144 0.00527  334 ILE   A CG2  
1251 C  CD1  . ILE   A 182 ? 0.40486 0.51238 0.41751 -0.06334 -0.01704 0.01893  334 ILE   A CD1  
1252 N  N    . VAL   A 183 ? 0.48645 0.59692 0.57579 -0.04804 -0.00631 0.00304  335 VAL   A N    
1253 C  CA   . VAL   A 183 ? 0.49511 0.60286 0.60516 -0.04271 -0.00275 -0.00884 335 VAL   A CA   
1254 C  C    . VAL   A 183 ? 0.46740 0.57302 0.60001 -0.03480 -0.00482 -0.00141 335 VAL   A C    
1255 O  O    . VAL   A 183 ? 0.46656 0.58400 0.61218 -0.02917 -0.00143 -0.00762 335 VAL   A O    
1256 C  CB   . VAL   A 183 ? 0.51325 0.63651 0.61944 -0.04328 0.00407  -0.02489 335 VAL   A CB   
1257 C  CG1  . VAL   A 183 ? 0.51172 0.63016 0.63615 -0.03824 0.00802  -0.04261 335 VAL   A CG1  
1258 C  CG2  . VAL   A 183 ? 0.49370 0.62295 0.57389 -0.05166 0.00416  -0.02622 335 VAL   A CG2  
1259 N  N    . SER   A 184 ? 0.49620 0.58953 0.63433 -0.03423 -0.01050 0.01272  336 SER   A N    
1260 C  CA   . SER   A 184 ? 0.47942 0.57076 0.63827 -0.02683 -0.01455 0.02369  336 SER   A CA   
1261 C  C    . SER   A 184 ? 0.47691 0.54871 0.65934 -0.02205 -0.01564 0.02178  336 SER   A C    
1262 O  O    . SER   A 184 ? 0.47437 0.53203 0.65331 -0.02792 -0.01758 0.02634  336 SER   A O    
1263 C  CB   . SER   A 184 ? 0.53057 0.62411 0.67798 -0.03024 -0.02089 0.04301  336 SER   A CB   
1264 O  OG   . SER   A 184 ? 0.55314 0.65857 0.67733 -0.03611 -0.02049 0.04282  336 SER   A OG   
1265 N  N    . PRO   A 185 ? 0.48984 0.55999 0.69836 -0.01160 -0.01474 0.01541  337 PRO   A N    
1266 C  CA   . PRO   A 185 ? 0.47117 0.51780 0.70441 -0.00666 -0.01587 0.01036  337 PRO   A CA   
1267 C  C    . PRO   A 185 ? 0.51403 0.54320 0.75990 -0.00622 -0.02421 0.03340  337 PRO   A C    
1268 O  O    . PRO   A 185 ? 0.62378 0.62899 0.89028 -0.00428 -0.02622 0.03197  337 PRO   A O    
1269 C  CB   . PRO   A 185 ? 0.54568 0.59970 0.80362 0.00668  -0.01194 -0.00469 337 PRO   A CB   
1270 C  CG   . PRO   A 185 ? 0.50785 0.58793 0.76124 0.00948  -0.01293 0.00539  337 PRO   A CG   
1271 C  CD   . PRO   A 185 ? 0.51205 0.60296 0.73051 -0.00375 -0.01226 0.01067  337 PRO   A CD   
1272 N  N    . ASP   A 186 ? 0.48746 0.52753 0.72139 -0.00890 -0.02942 0.05460  338 ASP   A N    
1273 C  CA   . ASP   A 186 ? 0.53136 0.55952 0.77455 -0.00945 -0.03740 0.07890  338 ASP   A CA   
1274 C  C    . ASP   A 186 ? 0.55343 0.57913 0.77484 -0.02281 -0.03814 0.09040  338 ASP   A C    
1275 O  O    . ASP   A 186 ? 0.60653 0.62850 0.82969 -0.02582 -0.04399 0.11289  338 ASP   A O    
1276 C  CB   . ASP   A 186 ? 0.45607 0.50169 0.70242 -0.00306 -0.04376 0.09588  338 ASP   A CB   
1277 C  CG   . ASP   A 186 ? 0.46560 0.53477 0.68150 -0.01054 -0.04328 0.09892  338 ASP   A CG   
1278 O  OD1  . ASP   A 186 ? 0.44976 0.52567 0.64811 -0.01552 -0.03672 0.08259  338 ASP   A OD1  
1279 O  OD2  . ASP   A 186 ? 0.51638 0.59697 0.72595 -0.01153 -0.05011 0.11765  338 ASP   A OD2  
1280 N  N    . ARG   A 187 ? 0.54383 0.57433 0.74537 -0.03061 -0.03246 0.07649  339 ARG   A N    
1281 C  CA   . ARG   A 187 ? 0.52090 0.55217 0.70553 -0.04190 -0.03249 0.08556  339 ARG   A CA   
1282 C  C    . ARG   A 187 ? 0.57645 0.58571 0.77992 -0.04694 -0.03468 0.09286  339 ARG   A C    
1283 O  O    . ARG   A 187 ? 0.55562 0.54636 0.77989 -0.04363 -0.03400 0.08000  339 ARG   A O    
1284 C  CB   . ARG   A 187 ? 0.49769 0.53822 0.66174 -0.04738 -0.02696 0.06856  339 ARG   A CB   
1285 C  CG   . ARG   A 187 ? 0.46972 0.52809 0.61601 -0.04418 -0.02508 0.06181  339 ARG   A CG   
1286 C  CD   . ARG   A 187 ? 0.44082 0.51259 0.56926 -0.04652 -0.02816 0.07660  339 ARG   A CD   
1287 N  NE   . ARG   A 187 ? 0.41474 0.49912 0.52362 -0.04694 -0.02632 0.06799  339 ARG   A NE   
1288 C  CZ   . ARG   A 187 ? 0.45404 0.54949 0.54614 -0.04859 -0.02876 0.07489  339 ARG   A CZ   
1289 N  NH1  . ARG   A 187 ? 0.45946 0.55935 0.54945 -0.04990 -0.03259 0.09016  339 ARG   A NH1  
1290 N  NH2  . ARG   A 187 ? 0.48848 0.59053 0.56551 -0.04960 -0.02764 0.06650  339 ARG   A NH2  
1291 N  N    . PRO   A 188 ? 0.66963 0.68086 0.86691 -0.05560 -0.03715 0.11286  340 PRO   A N    
1292 C  CA   . PRO   A 188 ? 0.70398 0.69402 0.92058 -0.06288 -0.03975 0.12341  340 PRO   A CA   
1293 C  C    . PRO   A 188 ? 0.65994 0.64123 0.87926 -0.07089 -0.03564 0.10405  340 PRO   A C    
1294 O  O    . PRO   A 188 ? 0.61949 0.61798 0.81894 -0.07630 -0.03148 0.09473  340 PRO   A O    
1295 C  CB   . PRO   A 188 ? 0.73884 0.74324 0.94161 -0.07199 -0.04159 0.14904  340 PRO   A CB   
1296 C  CG   . PRO   A 188 ? 0.72246 0.75448 0.89575 -0.07150 -0.03764 0.14203  340 PRO   A CG   
1297 C  CD   . PRO   A 188 ? 0.70813 0.74221 0.88073 -0.05981 -0.03741 0.12636  340 PRO   A CD   
1298 N  N    . GLY   A 189 ? 0.68055 0.63479 0.92579 -0.07123 -0.03768 0.09753  341 GLY   A N    
1299 C  CA   . GLY   A 189 ? 0.70966 0.65430 0.96021 -0.08007 -0.03531 0.07833  341 GLY   A CA   
1300 C  C    . GLY   A 189 ? 0.70213 0.64525 0.95367 -0.07255 -0.03166 0.04739  341 GLY   A C    
1301 O  O    . GLY   A 189 ? 0.70812 0.64465 0.96335 -0.08002 -0.03046 0.02912  341 GLY   A O    
1302 N  N    . VAL   A 190 ? 0.65660 0.60880 0.90452 -0.05914 -0.02982 0.04087  342 VAL   A N    
1303 C  CA   . VAL   A 190 ? 0.63109 0.58696 0.87855 -0.05249 -0.02509 0.01222  342 VAL   A CA   
1304 C  C    . VAL   A 190 ? 0.65315 0.58059 0.93020 -0.04914 -0.02634 -0.00332 342 VAL   A C    
1305 O  O    . VAL   A 190 ? 0.68872 0.59508 0.99068 -0.04227 -0.03080 0.00829  342 VAL   A O    
1306 C  CB   . VAL   A 190 ? 0.59458 0.56900 0.83451 -0.04018 -0.02259 0.01142  342 VAL   A CB   
1307 C  CG1  . VAL   A 190 ? 0.59574 0.57606 0.83810 -0.03336 -0.01672 -0.01706 342 VAL   A CG1  
1308 C  CG2  . VAL   A 190 ? 0.54496 0.54428 0.75504 -0.04463 -0.02154 0.02208  342 VAL   A CG2  
1309 N  N    A GLN   A 191 ? 0.65085 0.57730 0.92569 -0.05365 -0.02311 -0.03012 343 GLN   A N    
1310 N  N    B GLN   A 191 ? 0.65064 0.57693 0.92549 -0.05386 -0.02317 -0.02990 343 GLN   A N    
1311 C  CA   A GLN   A 191 ? 0.66969 0.56856 0.97147 -0.05130 -0.02402 -0.05063 343 GLN   A CA   
1312 C  CA   B GLN   A 191 ? 0.66973 0.56859 0.97153 -0.05129 -0.02399 -0.05087 343 GLN   A CA   
1313 C  C    A GLN   A 191 ? 0.67739 0.58110 0.98821 -0.03495 -0.01881 -0.07350 343 GLN   A C    
1314 C  C    B GLN   A 191 ? 0.67645 0.58111 0.98673 -0.03462 -0.01880 -0.07230 343 GLN   A C    
1315 O  O    A GLN   A 191 ? 0.71338 0.59624 1.05312 -0.02282 -0.02075 -0.07448 343 GLN   A O    
1316 O  O    B GLN   A 191 ? 0.71171 0.59754 1.04979 -0.02199 -0.02079 -0.07090 343 GLN   A O    
1317 C  CB   A GLN   A 191 ? 0.66032 0.55739 0.95566 -0.06609 -0.02397 -0.06984 343 GLN   A CB   
1318 C  CB   B GLN   A 191 ? 0.66031 0.55798 0.95538 -0.06559 -0.02368 -0.07125 343 GLN   A CB   
1319 C  CG   A GLN   A 191 ? 0.68205 0.54789 1.00503 -0.06630 -0.02582 -0.09330 343 GLN   A CG   
1320 C  CG   B GLN   A 191 ? 0.66184 0.54172 0.96674 -0.08170 -0.02967 -0.05557 343 GLN   A CG   
1321 C  CD   A GLN   A 191 ? 0.69796 0.57634 1.01399 -0.06073 -0.01975 -0.13060 343 GLN   A CD   
1322 C  CD   B GLN   A 191 ? 0.65628 0.55504 0.94223 -0.09726 -0.02937 -0.06523 343 GLN   A CD   
1323 O  OE1  A GLN   A 191 ? 0.54576 0.42260 0.87379 -0.04495 -0.01562 -0.14474 343 GLN   A OE1  
1324 O  OE1  B GLN   A 191 ? 0.65331 0.55537 0.93732 -0.11053 -0.03238 -0.04718 343 GLN   A OE1  
1325 N  NE2  A GLN   A 191 ? 0.67216 0.56638 0.96898 -0.07371 -0.01919 -0.14667 343 GLN   A NE2  
1326 N  NE2  B GLN   A 191 ? 0.63564 0.55033 0.90775 -0.09571 -0.02578 -0.09324 343 GLN   A NE2  
1327 N  N    . ASP   A 192 ? 0.65617 0.58878 0.94357 -0.03432 -0.01217 -0.09123 344 ASP   A N    
1328 C  CA   . ASP   A 192 ? 0.68768 0.63294 0.98074 -0.02062 -0.00533 -0.11394 344 ASP   A CA   
1329 C  C    . ASP   A 192 ? 0.72054 0.68880 1.00648 -0.01127 -0.00332 -0.09681 344 ASP   A C    
1330 O  O    . ASP   A 192 ? 0.71220 0.71015 0.97515 -0.01206 0.00216  -0.10158 344 ASP   A O    
1331 C  CB   . ASP   A 192 ? 0.66694 0.63287 0.93830 -0.02697 0.00071  -0.14194 344 ASP   A CB   
1332 C  CG   . ASP   A 192 ? 0.77059 0.74283 1.05471 -0.01479 0.00813  -0.17298 344 ASP   A CG   
1333 O  OD1  . ASP   A 192 ? 0.84038 0.80255 1.15172 0.00037  0.00887  -0.17244 344 ASP   A OD1  
1334 O  OD2  . ASP   A 192 ? 0.79159 0.78137 1.05878 -0.01992 0.01318  -0.19805 344 ASP   A OD2  
1335 N  N    . ALA   A 193 ? 0.73132 0.68518 1.03844 -0.00318 -0.00880 -0.07546 345 ALA   A N    
1336 C  CA   . ALA   A 193 ? 0.70855 0.68399 1.01230 0.00515  -0.00868 -0.05876 345 ALA   A CA   
1337 C  C    . ALA   A 193 ? 0.67576 0.67274 0.98786 0.01796  -0.00086 -0.07993 345 ALA   A C    
1338 O  O    . ALA   A 193 ? 0.63003 0.65477 0.93080 0.02031  0.00166  -0.07245 345 ALA   A O    
1339 C  CB   . ALA   A 193 ? 0.72084 0.67785 1.04725 0.01150  -0.01741 -0.03204 345 ALA   A CB   
1340 N  N    . LYS   A 194 ? 0.70887 0.69485 1.04151 0.02578  0.00331  -0.10727 346 LYS   A N    
1341 C  CA   . LYS   A 194 ? 0.74835 0.76039 1.08742 0.03722  0.01289  -0.13117 346 LYS   A CA   
1342 C  C    . LYS   A 194 ? 0.69131 0.73783 0.99382 0.02637  0.02044  -0.13916 346 LYS   A C    
1343 O  O    . LYS   A 194 ? 0.61365 0.69152 0.91020 0.03017  0.02586  -0.13764 346 LYS   A O    
1344 C  CB   . LYS   A 194 ? 0.84182 0.83540 1.20600 0.04614  0.01661  -0.16346 346 LYS   A CB   
1345 C  CG   . LYS   A 194 ? 0.92290 0.91364 1.32713 0.06835  0.01797  -0.17165 346 LYS   A CG   
1346 C  CD   . LYS   A 194 ? 0.97910 0.94741 1.40658 0.07527  0.00645  -0.13890 346 LYS   A CD   
1347 C  CE   . LYS   A 194 ? 1.05752 0.97634 1.50647 0.07357  -0.00220 -0.13627 346 LYS   A CE   
1348 N  NZ   . LYS   A 194 ? 1.08982 0.98689 1.56472 0.08196  -0.01371 -0.10385 346 LYS   A NZ   
1349 N  N    . LEU   A 195 ? 0.63867 0.68049 0.91747 0.01211  0.02017  -0.14640 347 LEU   A N    
1350 C  CA   . LEU   A 195 ? 0.57842 0.65078 0.82285 0.00187  0.02595  -0.15282 347 LEU   A CA   
1351 C  C    . LEU   A 195 ? 0.52157 0.60753 0.74417 -0.00497 0.02260  -0.12450 347 LEU   A C    
1352 O  O    . LEU   A 195 ? 0.55322 0.66775 0.75719 -0.00787 0.02781  -0.12429 347 LEU   A O    
1353 C  CB   . LEU   A 195 ? 0.59761 0.66171 0.82531 -0.01065 0.02457  -0.16704 347 LEU   A CB   
1354 C  CG   . LEU   A 195 ? 0.60413 0.69931 0.79810 -0.02038 0.02989  -0.17760 347 LEU   A CG   
1355 C  CD1  . LEU   A 195 ? 0.64661 0.76789 0.84355 -0.01262 0.04082  -0.20325 347 LEU   A CD1  
1356 C  CD2  . LEU   A 195 ? 0.55688 0.64298 0.73713 -0.03292 0.02546  -0.18760 347 LEU   A CD2  
1357 N  N    . VAL   A 196 ? 0.54662 0.61275 0.77114 -0.00832 0.01403  -0.10080 348 VAL   A N    
1358 C  CA   . VAL   A 196 ? 0.53464 0.61215 0.73912 -0.01411 0.01063  -0.07667 348 VAL   A CA   
1359 C  C    . VAL   A 196 ? 0.51209 0.60898 0.72525 -0.00572 0.01277  -0.06973 348 VAL   A C    
1360 O  O    . VAL   A 196 ? 0.51081 0.62824 0.70427 -0.01112 0.01425  -0.06201 348 VAL   A O    
1361 C  CB   . VAL   A 196 ? 0.50587 0.56144 0.71221 -0.01860 0.00201  -0.05472 348 VAL   A CB   
1362 C  CG1  . VAL   A 196 ? 0.44818 0.51601 0.63267 -0.02415 -0.00106 -0.03392 348 VAL   A CG1  
1363 C  CG2  . VAL   A 196 ? 0.51743 0.55781 0.71831 -0.02811 0.00020  -0.06223 348 VAL   A CG2  
1364 N  N    . GLU   A 197 ? 0.49602 0.58690 0.74072 0.00751  0.01239  -0.07245 349 GLU   A N    
1365 C  CA   . GLU   A 197 ? 0.55727 0.67091 0.81436 0.01609  0.01396  -0.06667 349 GLU   A CA   
1366 C  C    . GLU   A 197 ? 0.51797 0.66332 0.76831 0.01626  0.02483  -0.08611 349 GLU   A C    
1367 O  O    . GLU   A 197 ? 0.50654 0.67781 0.74889 0.01337  0.02679  -0.07794 349 GLU   A O    
1368 C  CB   . GLU   A 197 ? 0.63164 0.73215 0.92723 0.03202  0.00997  -0.06432 349 GLU   A CB   
1369 C  CG   . GLU   A 197 ? 0.68146 0.79906 0.98852 0.03822  0.00484  -0.04427 349 GLU   A CG   
1370 C  CD   . GLU   A 197 ? 0.73047 0.84390 1.07916 0.05708  0.00212  -0.04549 349 GLU   A CD   
1371 O  OE1  . GLU   A 197 ? 0.77266 0.85398 1.14045 0.06311  -0.00308 -0.04392 349 GLU   A OE1  
1372 O  OE2  . GLU   A 197 ? 0.76497 0.90744 1.12901 0.06576  0.00459  -0.04692 349 GLU   A OE2  
1373 N  N    . ALA   A 198 ? 0.52553 0.67087 0.77833 0.01828  0.03199  -0.11201 350 ALA   A N    
1374 C  CA   . ALA   A 198 ? 0.52046 0.70022 0.76443 0.01740  0.04339  -0.13076 350 ALA   A CA   
1375 C  C    . ALA   A 198 ? 0.53368 0.73050 0.73980 0.00098  0.04441  -0.12068 350 ALA   A C    
1376 O  O    . ALA   A 198 ? 0.56570 0.79411 0.76359 -0.00246 0.05092  -0.12059 350 ALA   A O    
1377 C  CB   . ALA   A 198 ? 0.54385 0.72010 0.79456 0.02184  0.05028  -0.16231 350 ALA   A CB   
1378 N  N    . ILE   A 199 ? 0.48545 0.66217 0.66998 -0.00935 0.03780  -0.11125 351 ILE   A N    
1379 C  CA   . ILE   A 199 ? 0.48841 0.67682 0.63979 -0.02307 0.03686  -0.09937 351 ILE   A CA   
1380 C  C    . ILE   A 199 ? 0.48323 0.67788 0.63265 -0.02522 0.03270  -0.07658 351 ILE   A C    
1381 O  O    . ILE   A 199 ? 0.45867 0.67482 0.59251 -0.03284 0.03582  -0.07113 351 ILE   A O    
1382 C  CB   . ILE   A 199 ? 0.45620 0.62276 0.59000 -0.03120 0.03016  -0.09518 351 ILE   A CB   
1383 C  CG1  . ILE   A 199 ? 0.47942 0.64280 0.61466 -0.03112 0.03362  -0.11971 351 ILE   A CG1  
1384 C  CG2  . ILE   A 199 ? 0.44946 0.62559 0.55225 -0.04288 0.02785  -0.08140 351 ILE   A CG2  
1385 C  CD1  . ILE   A 199 ? 0.49722 0.64713 0.61493 -0.04067 0.02740  -0.11731 351 ILE   A CD1  
1386 N  N    . GLN   A 200 ? 0.51112 0.68731 0.67570 -0.01979 0.02505  -0.06256 352 GLN   A N    
1387 C  CA   . GLN   A 200 ? 0.47857 0.66111 0.64047 -0.02241 0.01995  -0.04270 352 GLN   A CA   
1388 C  C    . GLN   A 200 ? 0.45417 0.66546 0.63222 -0.01797 0.02504  -0.04528 352 GLN   A C    
1389 O  O    . GLN   A 200 ? 0.49212 0.71762 0.66139 -0.02512 0.02323  -0.03330 352 GLN   A O    
1390 C  CB   . GLN   A 200 ? 0.46912 0.62988 0.64287 -0.01764 0.01071  -0.02762 352 GLN   A CB   
1391 C  CG   . GLN   A 200 ? 0.48370 0.64876 0.64693 -0.02300 0.00401  -0.00815 352 GLN   A CG   
1392 C  CD   . GLN   A 200 ? 0.47357 0.62657 0.65212 -0.01672 -0.00432 0.00647  352 GLN   A CD   
1393 O  OE1  . GLN   A 200 ? 0.52085 0.67517 0.72672 -0.00578 -0.00511 0.00558  352 GLN   A OE1  
1394 N  NE2  . GLN   A 200 ? 0.44861 0.59106 0.60994 -0.02310 -0.01067 0.02029  352 GLN   A NE2  
1395 N  N    . ASP   A 201 ? 0.46764 0.68853 0.67100 -0.00631 0.03130  -0.06166 353 ASP   A N    
1396 C  CA   . ASP   A 201 ? 0.54261 0.79619 0.76512 -0.00090 0.03702  -0.06525 353 ASP   A CA   
1397 C  C    . ASP   A 201 ? 0.53856 0.82205 0.74015 -0.01313 0.04572  -0.06968 353 ASP   A C    
1398 O  O    . ASP   A 201 ? 0.50186 0.80993 0.70580 -0.01836 0.04657  -0.06039 353 ASP   A O    
1399 C  CB   . ASP   A 201 ? 0.59165 0.84898 0.84773 0.01638  0.04253  -0.08457 353 ASP   A CB   
1400 C  CG   . ASP   A 201 ? 0.59292 0.82821 0.87754 0.02958  0.03285  -0.07400 353 ASP   A CG   
1401 O  OD1  . ASP   A 201 ? 0.58182 0.81012 0.86143 0.02531  0.02302  -0.05131 353 ASP   A OD1  
1402 O  OD2  . ASP   A 201 ? 0.60168 0.82654 0.91362 0.04415  0.03473  -0.08840 353 ASP   A OD2  
1403 N  N    . ARG   A 202 ? 0.49476 0.77780 0.67580 -0.01903 0.05163  -0.08278 354 ARG   A N    
1404 C  CA   . ARG   A 202 ? 0.48177 0.79240 0.63950 -0.03231 0.05895  -0.08330 354 ARG   A CA   
1405 C  C    . ARG   A 202 ? 0.45153 0.75521 0.58717 -0.04644 0.05126  -0.05981 354 ARG   A C    
1406 O  O    . ARG   A 202 ? 0.41610 0.74416 0.54424 -0.05677 0.05489  -0.05250 354 ARG   A O    
1407 C  CB   . ARG   A 202 ? 0.50458 0.81448 0.64157 -0.03638 0.06420  -0.09952 354 ARG   A CB   
1408 C  CG   . ARG   A 202 ? 0.61586 0.93191 0.77352 -0.02314 0.07221  -0.12721 354 ARG   A CG   
1409 C  CD   . ARG   A 202 ? 0.70636 1.04297 0.84144 -0.03013 0.08118  -0.14571 354 ARG   A CD   
1410 N  NE   . ARG   A 202 ? 0.78795 1.10545 0.89189 -0.04192 0.07382  -0.13712 354 ARG   A NE   
1411 C  CZ   . ARG   A 202 ? 0.86058 1.15149 0.96269 -0.03960 0.06846  -0.14670 354 ARG   A CZ   
1412 N  NH1  . ARG   A 202 ? 0.89034 1.16650 1.01934 -0.02671 0.06951  -0.16513 354 ARG   A NH1  
1413 N  NH2  . ARG   A 202 ? 0.84793 1.12704 0.92333 -0.05024 0.06154  -0.13756 354 ARG   A NH2  
1414 N  N    . LEU   A 203 ? 0.41575 0.68655 0.54177 -0.04742 0.04080  -0.04828 355 LEU   A N    
1415 C  CA   . LEU   A 203 ? 0.39909 0.66087 0.50745 -0.05842 0.03305  -0.02862 355 LEU   A CA   
1416 C  C    . LEU   A 203 ? 0.40361 0.67600 0.52983 -0.05734 0.02931  -0.01822 355 LEU   A C    
1417 O  O    . LEU   A 203 ? 0.40077 0.68247 0.51732 -0.06886 0.02737  -0.00721 355 LEU   A O    
1418 C  CB   . LEU   A 203 ? 0.40146 0.62981 0.49709 -0.05812 0.02403  -0.02153 355 LEU   A CB   
1419 C  CG   . LEU   A 203 ? 0.43380 0.65152 0.51559 -0.05856 0.02568  -0.03170 355 LEU   A CG   
1420 C  CD1  . LEU   A 203 ? 0.43482 0.62376 0.51594 -0.05511 0.01758  -0.02611 355 LEU   A CD1  
1421 C  CD2  . LEU   A 203 ? 0.43309 0.65897 0.48733 -0.07063 0.02683  -0.02736 355 LEU   A CD2  
1422 N  N    . SER   A 204 ? 0.39669 0.66728 0.54972 -0.04413 0.02715  -0.02085 356 SER   A N    
1423 C  CA   . SER   A 204 ? 0.42956 0.71317 0.60087 -0.04228 0.02192  -0.01044 356 SER   A CA   
1424 C  C    . SER   A 204 ? 0.43624 0.75908 0.61952 -0.04639 0.02990  -0.01440 356 SER   A C    
1425 O  O    . SER   A 204 ? 0.40483 0.74128 0.58654 -0.05661 0.02617  -0.00318 356 SER   A O    
1426 C  CB   . SER   A 204 ? 0.45423 0.72838 0.65293 -0.02611 0.01720  -0.01072 356 SER   A CB   
1427 O  OG   . SER   A 204 ? 0.49588 0.73823 0.68327 -0.02582 0.00838  -0.00115 356 SER   A OG   
1428 N  N    A ASN   A 205 ? 0.44528 0.78836 0.64119 -0.03922 0.04117  -0.03138 357 ASN   A N    
1429 N  N    B ASN   A 205 ? 0.44829 0.79156 0.64399 -0.03937 0.04125  -0.03139 357 ASN   A N    
1430 C  CA   A ASN   A 205 ? 0.46035 0.84656 0.66761 -0.04359 0.05091  -0.03623 357 ASN   A CA   
1431 C  CA   B ASN   A 205 ? 0.45492 0.84137 0.66226 -0.04378 0.05076  -0.03587 357 ASN   A CA   
1432 C  C    A ASN   A 205 ? 0.45102 0.84641 0.62906 -0.06448 0.05355  -0.02737 357 ASN   A C    
1433 C  C    B ASN   A 205 ? 0.45127 0.84717 0.62932 -0.06454 0.05375  -0.02752 357 ASN   A C    
1434 O  O    A ASN   A 205 ? 0.45476 0.88014 0.63886 -0.07469 0.05637  -0.02080 357 ASN   A O    
1435 O  O    B ASN   A 205 ? 0.45482 0.88167 0.63892 -0.07470 0.05709  -0.02151 357 ASN   A O    
1436 C  CB   A ASN   A 205 ? 0.46183 0.86801 0.68588 -0.03094 0.06361  -0.05939 357 ASN   A CB   
1437 C  CB   B ASN   A 205 ? 0.46346 0.87153 0.69024 -0.03035 0.06338  -0.05886 357 ASN   A CB   
1438 C  CG   A ASN   A 205 ? 0.46397 0.86551 0.72493 -0.00937 0.06107  -0.06730 357 ASN   A CG   
1439 C  CG   B ASN   A 205 ? 0.48266 0.88252 0.68431 -0.03426 0.07074  -0.07260 357 ASN   A CG   
1440 O  OD1  A ASN   A 205 ? 0.47864 0.88198 0.75921 -0.00449 0.05240  -0.05462 357 ASN   A OD1  
1441 O  OD1  B ASN   A 205 ? 0.49393 0.89266 0.66465 -0.05029 0.07122  -0.06490 357 ASN   A OD1  
1442 N  ND2  A ASN   A 205 ? 0.49411 0.88922 0.76508 0.00353  0.06778  -0.08827 357 ASN   A ND2  
1443 N  ND2  B ASN   A 205 ? 0.49237 0.88681 0.70854 -0.01938 0.07578  -0.09340 357 ASN   A ND2  
1444 N  N    . THR   A 206 ? 0.43334 0.80351 0.58122 -0.07145 0.05192  -0.02578 358 THR   A N    
1445 C  CA   . THR   A 206 ? 0.47271 0.84528 0.59292 -0.09058 0.05194  -0.01388 358 THR   A CA   
1446 C  C    . THR   A 206 ? 0.44323 0.80367 0.56078 -0.10075 0.04109  0.00433  358 THR   A C    
1447 O  O    . THR   A 206 ? 0.44991 0.82753 0.56246 -0.11628 0.04232  0.01403  358 THR   A O    
1448 C  CB   . THR   A 206 ? 0.47176 0.81786 0.56296 -0.09334 0.04990  -0.01473 358 THR   A CB   
1449 O  OG1  . THR   A 206 ? 0.50489 0.86323 0.59757 -0.08523 0.05931  -0.03396 358 THR   A OG1  
1450 C  CG2  . THR   A 206 ? 0.49604 0.84380 0.56030 -0.11189 0.04903  -0.00050 358 THR   A CG2  
1451 N  N    . LEU   A 207 ? 0.40151 0.73308 0.52202 -0.09324 0.03037  0.00882  359 LEU   A N    
1452 C  CA   . LEU   A 207 ? 0.38089 0.70042 0.49696 -0.10239 0.01963  0.02287  359 LEU   A CA   
1453 C  C    . LEU   A 207 ? 0.36380 0.71534 0.50459 -0.10530 0.01947  0.02578  359 LEU   A C    
1454 O  O    . LEU   A 207 ? 0.29413 0.65204 0.43016 -0.12095 0.01563  0.03549  359 LEU   A O    
1455 C  CB   . LEU   A 207 ? 0.40851 0.69562 0.52125 -0.09315 0.00949  0.02557  359 LEU   A CB   
1456 C  CG   . LEU   A 207 ? 0.39536 0.67292 0.50562 -0.09980 -0.00187 0.03633  359 LEU   A CG   
1457 C  CD1  . LEU   A 207 ? 0.41457 0.67980 0.50235 -0.11664 -0.00499 0.04386  359 LEU   A CD1  
1458 C  CD2  . LEU   A 207 ? 0.29043 0.54235 0.39725 -0.08959 -0.00968 0.03791  359 LEU   A CD2  
1459 N  N    . GLN   A 208 ? 0.37405 0.74563 0.54330 -0.09034 0.02281  0.01750  360 GLN   A N    
1460 C  CA   . GLN   A 208 ? 0.42993 0.83721 0.62699 -0.09097 0.02235  0.01988  360 GLN   A CA   
1461 C  C    . GLN   A 208 ? 0.42601 0.86943 0.62419 -0.10592 0.03239  0.01986  360 GLN   A C    
1462 O  O    . GLN   A 208 ? 0.43054 0.89293 0.63536 -0.11980 0.02862  0.02902  360 GLN   A O    
1463 C  CB   . GLN   A 208 ? 0.47410 0.89608 0.70365 -0.06941 0.02494  0.01013  360 GLN   A CB   
1464 C  CG   . GLN   A 208 ? 0.52656 0.91684 0.75914 -0.05592 0.01420  0.01401  360 GLN   A CG   
1465 C  CD   . GLN   A 208 ? 0.59680 1.00180 0.86588 -0.03537 0.01459  0.00812  360 GLN   A CD   
1466 O  OE1  . GLN   A 208 ? 0.61358 1.04917 0.90878 -0.03227 0.01146  0.01216  360 GLN   A OE1  
1467 N  NE2  . GLN   A 208 ? 0.61819 1.00141 0.89121 -0.02117 0.01772  -0.00144 360 GLN   A NE2  
1468 N  N    . THR   A 209 ? 0.42327 0.87879 0.61477 -0.10453 0.04525  0.00956  361 THR   A N    
1469 C  CA   . THR   A 209 ? 0.44014 0.93407 0.63056 -0.11964 0.05633  0.01050  361 THR   A CA   
1470 C  C    . THR   A 209 ? 0.46437 0.94200 0.62746 -0.14334 0.05070  0.02747  361 THR   A C    
1471 O  O    . THR   A 209 ? 0.48184 0.98742 0.65029 -0.16063 0.05325  0.03616  361 THR   A O    
1472 C  CB   . THR   A 209 ? 0.47763 0.98737 0.66176 -0.11320 0.07091  -0.00510 361 THR   A CB   
1473 O  OG1  . THR   A 209 ? 0.48700 1.00829 0.69971 -0.09024 0.07564  -0.02281 361 THR   A OG1  
1474 C  CG2  . THR   A 209 ? 0.45455 1.01038 0.63678 -0.12952 0.08370  -0.00331 361 THR   A CG2  
1475 N  N    . TYR   A 210 ? 0.46764 0.89989 0.60343 -0.14449 0.04261  0.03263  362 TYR   A N    
1476 C  CA   . TYR   A 210 ? 0.44799 0.85872 0.56017 -0.16453 0.03565  0.04839  362 TYR   A CA   
1477 C  C    . TYR   A 210 ? 0.47179 0.88199 0.59596 -0.17478 0.02523  0.05760  362 TYR   A C    
1478 O  O    . TYR   A 210 ? 0.51696 0.93391 0.63651 -0.19551 0.02385  0.06902  362 TYR   A O    
1479 C  CB   . TYR   A 210 ? 0.44674 0.80984 0.53212 -0.16015 0.02803  0.05056  362 TYR   A CB   
1480 C  CG   . TYR   A 210 ? 0.46566 0.80282 0.52991 -0.17824 0.01972  0.06613  362 TYR   A CG   
1481 C  CD1  . TYR   A 210 ? 0.46876 0.80718 0.51298 -0.19132 0.02404  0.07515  362 TYR   A CD1  
1482 C  CD2  . TYR   A 210 ? 0.41450 0.72660 0.47936 -0.18247 0.00717  0.07178  362 TYR   A CD2  
1483 C  CE1  . TYR   A 210 ? 0.45810 0.76957 0.48574 -0.20715 0.01553  0.09071  362 TYR   A CE1  
1484 C  CE2  . TYR   A 210 ? 0.42967 0.71515 0.47778 -0.19830 -0.00065 0.08396  362 TYR   A CE2  
1485 C  CZ   . TYR   A 210 ? 0.45236 0.73583 0.48312 -0.21018 0.00332  0.09410  362 TYR   A CZ   
1486 O  OH   . TYR   A 210 ? 0.46425 0.71770 0.48058 -0.22509 -0.00535 0.10762  362 TYR   A OH   
1487 N  N    . ILE   A 211 ? 0.44321 0.84494 0.58200 -0.16177 0.01699  0.05344  363 ILE   A N    
1488 C  CA   . ILE   A 211 ? 0.41708 0.81958 0.56531 -0.17147 0.00567  0.06054  363 ILE   A CA   
1489 C  C    . ILE   A 211 ? 0.43586 0.88711 0.60851 -0.18347 0.01099  0.06312  363 ILE   A C    
1490 O  O    . ILE   A 211 ? 0.40806 0.86284 0.57985 -0.20406 0.00541  0.07241  363 ILE   A O    
1491 C  CB   . ILE   A 211 ? 0.37685 0.76722 0.53541 -0.15433 -0.00372 0.05641  363 ILE   A CB   
1492 C  CG1  . ILE   A 211 ? 0.38122 0.72448 0.51385 -0.14740 -0.00961 0.05601  363 ILE   A CG1  
1493 C  CG2  . ILE   A 211 ? 0.36726 0.76925 0.53835 -0.16384 -0.01518 0.06191  363 ILE   A CG2  
1494 C  CD1  . ILE   A 211 ? 0.44792 0.78107 0.58869 -0.12876 -0.01517 0.05230  363 ILE   A CD1  
1495 N  N    . ARG   A 212 ? 0.50261 0.99269 0.69814 -0.17144 0.02238  0.05417  364 ARG   A N    
1496 C  CA   . ARG   A 212 ? 0.55732 1.10103 0.77984 -0.18087 0.02915  0.05524  364 ARG   A CA   
1497 C  C    . ARG   A 212 ? 0.56736 1.12350 0.77532 -0.20646 0.03613  0.06515  364 ARG   A C    
1498 O  O    . ARG   A 212 ? 0.55933 1.13635 0.77778 -0.22648 0.03284  0.07452  364 ARG   A O    
1499 C  CB   . ARG   A 212 ? 0.60999 1.19118 0.85909 -0.16017 0.04166  0.04094  364 ARG   A CB   
1500 C  CG   . ARG   A 212 ? 0.68935 1.28673 0.97215 -0.14202 0.03450  0.03666  364 ARG   A CG   
1501 C  CD   . ARG   A 212 ? 0.77930 1.32871 1.05013 -0.12850 0.02128  0.03789  364 ARG   A CD   
1502 N  NE   . ARG   A 212 ? 0.85654 1.41738 1.15178 -0.12049 0.00882  0.04204  364 ARG   A NE   
1503 C  CZ   . ARG   A 212 ? 0.89182 1.47190 1.21819 -0.09829 0.00899  0.03625  364 ARG   A CZ   
1504 N  NH1  . ARG   A 212 ? 0.90883 1.49700 1.24672 -0.08156 0.02175  0.02323  364 ARG   A NH1  
1505 N  NH2  . ARG   A 212 ? 0.88309 1.47400 1.22928 -0.09259 -0.00431 0.04325  364 ARG   A NH2  
1506 N  N    . CYS   A 213 ? 0.53515 1.07917 0.71876 -0.20740 0.04501  0.06445  365 CYS   A N    
1507 C  CA   . CYS   A 213 ? 0.60712 1.17058 0.77800 -0.23051 0.05359  0.07530  365 CYS   A CA   
1508 C  C    . CYS   A 213 ? 0.58060 1.10039 0.72352 -0.25089 0.04294  0.09230  365 CYS   A C    
1509 O  O    . CYS   A 213 ? 0.60862 1.13059 0.74135 -0.26812 0.04407  0.10370  365 CYS   A O    
1510 C  CB   . CYS   A 213 ? 0.68282 1.26283 0.84074 -0.22288 0.06893  0.06675  365 CYS   A CB   
1511 S  SG   . CYS   A 213 ? 0.72367 1.34584 0.91184 -0.19503 0.08237  0.04189  365 CYS   A SG   
1512 N  N    A ARG   A 214 ? 0.55277 1.01972 0.67857 -0.24208 0.03061  0.09181  366 ARG   A N    
1513 N  N    D ARG   A 214 ? 0.55263 1.01952 0.67830 -0.24212 0.03064  0.09185  366 ARG   A N    
1514 C  CA   A ARG   A 214 ? 0.56183 0.98413 0.66149 -0.25725 0.02104  0.10556  366 ARG   A CA   
1515 C  CA   D ARG   A 214 ? 0.56169 0.98416 0.66140 -0.25752 0.02104  0.10571  366 ARG   A CA   
1516 C  C    A ARG   A 214 ? 0.55890 0.94440 0.65894 -0.25975 0.00454  0.10681  366 ARG   A C    
1517 C  C    D ARG   A 214 ? 0.55930 0.94528 0.65958 -0.26013 0.00456  0.10697  366 ARG   A C    
1518 O  O    A ARG   A 214 ? 0.58493 0.93390 0.66779 -0.27364 -0.00408 0.11725  366 ARG   A O    
1519 O  O    D ARG   A 214 ? 0.58483 0.93488 0.66831 -0.27446 -0.00406 0.11754  366 ARG   A O    
1520 C  CB   A ARG   A 214 ? 0.56469 0.95593 0.63710 -0.24572 0.02255  0.10409  366 ARG   A CB   
1521 C  CB   D ARG   A 214 ? 0.56522 0.95614 0.63745 -0.24623 0.02241  0.10445  366 ARG   A CB   
1522 C  CG   A ARG   A 214 ? 0.56833 0.99481 0.63776 -0.23974 0.03825  0.09788  366 ARG   A CG   
1523 C  CG   D ARG   A 214 ? 0.57326 0.99836 0.63943 -0.24451 0.03786  0.10166  366 ARG   A CG   
1524 C  CD   A ARG   A 214 ? 0.60705 1.03656 0.65358 -0.25915 0.04258  0.11419  366 ARG   A CD   
1525 C  CD   D ARG   A 214 ? 0.61031 1.04638 0.66147 -0.26962 0.04178  0.12059  366 ARG   A CD   
1526 N  NE   A ARG   A 214 ? 0.62574 1.07941 0.68112 -0.28020 0.04447  0.12633  366 ARG   A NE   
1527 N  NE   D ARG   A 214 ? 0.62876 1.09149 0.66512 -0.26765 0.05492  0.11842  366 ARG   A NE   
1528 C  CZ   A ARG   A 214 ? 0.65146 1.07700 0.69194 -0.29781 0.03574  0.14442  366 ARG   A CZ   
1529 C  CZ   D ARG   A 214 ? 0.62825 1.13850 0.67677 -0.26097 0.06879  0.10574  366 ARG   A CZ   
1530 N  NH1  A ARG   A 214 ? 0.65654 1.03606 0.67555 -0.30054 0.02609  0.15471  366 ARG   A NH1  
1531 N  NH1  D ARG   A 214 ? 0.63831 1.16723 0.66900 -0.25790 0.07876  0.10125  366 ARG   A NH1  
1532 N  NH2  A ARG   A 214 ? 0.67211 1.11531 0.72088 -0.31229 0.03643  0.15226  366 ARG   A NH2  
1533 N  NH2  D ARG   A 214 ? 0.60901 1.14853 0.68754 -0.25662 0.07201  0.09672  366 ARG   A NH2  
1534 N  N    . HIS   A 215 ? 0.50888 0.90268 0.62751 -0.24663 -0.00053 0.09650  367 HIS   A N    
1535 C  CA   . HIS   A 215 ? 0.52461 0.88959 0.64213 -0.25005 -0.01596 0.09618  367 HIS   A CA   
1536 C  C    . HIS   A 215 ? 0.48782 0.88792 0.63037 -0.26552 -0.01975 0.09858  367 HIS   A C    
1537 O  O    . HIS   A 215 ? 0.48718 0.92480 0.65440 -0.25463 -0.01737 0.09199  367 HIS   A O    
1538 C  CB   . HIS   A 215 ? 0.50837 0.85576 0.62496 -0.22607 -0.02134 0.08520  367 HIS   A CB   
1539 C  CG   . HIS   A 215 ? 0.53261 0.83691 0.63311 -0.22771 -0.03530 0.08429  367 HIS   A CG   
1540 N  ND1  . HIS   A 215 ? 0.51418 0.77983 0.59376 -0.21443 -0.03786 0.08065  367 HIS   A ND1  
1541 C  CD2  . HIS   A 215 ? 0.54574 0.84150 0.64828 -0.24161 -0.04713 0.08494  367 HIS   A CD2  
1542 C  CE1  . HIS   A 215 ? 0.49683 0.73320 0.56647 -0.21867 -0.04974 0.07850  367 HIS   A CE1  
1543 N  NE2  . HIS   A 215 ? 0.53767 0.79014 0.62001 -0.23523 -0.05585 0.08030  367 HIS   A NE2  
1544 N  N    . PRO   A 216 ? 0.48146 0.87111 0.62064 -0.29085 -0.02635 0.10813  368 PRO   A N    
1545 C  CA   . PRO   A 216 ? 0.50271 0.92143 0.66191 -0.30140 -0.02885 0.10871  368 PRO   A CA   
1546 C  C    . PRO   A 216 ? 0.44334 0.86317 0.61454 -0.29663 -0.04221 0.10043  368 PRO   A C    
1547 O  O    . PRO   A 216 ? 0.44346 0.82975 0.60136 -0.29289 -0.05267 0.09610  368 PRO   A O    
1548 C  CB   . PRO   A 216 ? 0.54084 0.93018 0.68499 -0.32427 -0.03301 0.11984  368 PRO   A CB   
1549 C  CG   . PRO   A 216 ? 0.60718 0.96335 0.72603 -0.32397 -0.02908 0.12730  368 PRO   A CG   
1550 C  CD   . PRO   A 216 ? 0.54180 0.88604 0.65588 -0.30492 -0.03067 0.11796  368 PRO   A CD   
1551 N  N    . PRO   A 217 ? 0.40323 0.86291 0.59904 -0.29576 -0.04275 0.09771  369 PRO   A N    
1552 C  CA   . PRO   A 217 ? 0.40054 0.86277 0.60554 -0.29314 -0.05708 0.09139  369 PRO   A CA   
1553 C  C    . PRO   A 217 ? 0.47364 0.90076 0.66437 -0.31385 -0.06987 0.09188  369 PRO   A C    
1554 O  O    . PRO   A 217 ? 0.48002 0.89308 0.66371 -0.33124 -0.06691 0.09904  369 PRO   A O    
1555 C  CB   . PRO   A 217 ? 0.39531 0.91194 0.63166 -0.28801 -0.05289 0.09034  369 PRO   A CB   
1556 C  CG   . PRO   A 217 ? 0.43817 0.97238 0.67754 -0.29857 -0.03907 0.09669  369 PRO   A CG   
1557 C  CD   . PRO   A 217 ? 0.40530 0.91163 0.62130 -0.29644 -0.03026 0.10002  369 PRO   A CD   
1558 N  N    . PRO   A 218 ? 0.47742 0.89078 0.66389 -0.31190 -0.08422 0.08400  370 PRO   A N    
1559 C  CA   . PRO   A 218 ? 0.47570 0.90569 0.66905 -0.29271 -0.09002 0.07784  370 PRO   A CA   
1560 C  C    . PRO   A 218 ? 0.52274 0.92217 0.69657 -0.27867 -0.09036 0.07498  370 PRO   A C    
1561 O  O    . PRO   A 218 ? 0.52328 0.92794 0.69761 -0.25921 -0.09421 0.07089  370 PRO   A O    
1562 C  CB   . PRO   A 218 ? 0.56029 0.98707 0.75241 -0.30180 -0.10581 0.07121  370 PRO   A CB   
1563 C  CG   . PRO   A 218 ? 0.58529 0.96806 0.75828 -0.32233 -0.11017 0.06979  370 PRO   A CG   
1564 C  CD   . PRO   A 218 ? 0.52496 0.90519 0.69924 -0.33067 -0.09669 0.08048  370 PRO   A CD   
1565 N  N    . GLY   A 219 ? 0.49321 0.85243 0.64521 -0.28158 -0.08446 0.07711  371 GLY   A N    
1566 C  CA   . GLY   A 219 ? 0.44990 0.77109 0.57850 -0.26136 -0.08218 0.07278  371 GLY   A CA   
1567 C  C    . GLY   A 219 ? 0.41544 0.75640 0.55259 -0.23703 -0.07207 0.07268  371 GLY   A C    
1568 O  O    . GLY   A 219 ? 0.48572 0.80631 0.61028 -0.21886 -0.07321 0.06831  371 GLY   A O    
1569 N  N    . SER   A 220 ? 0.40919 0.79038 0.56883 -0.23662 -0.06194 0.07670  372 SER   A N    
1570 C  CA   . SER   A 220 ? 0.43127 0.83038 0.60211 -0.21357 -0.05212 0.07435  372 SER   A CA   
1571 C  C    . SER   A 220 ? 0.45818 0.88588 0.65128 -0.19917 -0.05849 0.07237  372 SER   A C    
1572 O  O    . SER   A 220 ? 0.41946 0.85642 0.62343 -0.17839 -0.05224 0.07023  372 SER   A O    
1573 C  CB   . SER   A 220 ? 0.46157 0.89323 0.64706 -0.21761 -0.03736 0.07696  372 SER   A CB   
1574 O  OG   . SER   A 220 ? 0.52474 1.00121 0.73658 -0.23173 -0.03835 0.08021  372 SER   A OG   
1575 N  N    . HIS   A 221 ? 0.45382 0.89556 0.65457 -0.20992 -0.07151 0.07332  373 HIS   A N    
1576 C  CA   . HIS   A 221 ? 0.42939 0.90292 0.65237 -0.19734 -0.07940 0.07420  373 HIS   A CA   
1577 C  C    . HIS   A 221 ? 0.45877 0.90748 0.66907 -0.17524 -0.08216 0.07334  373 HIS   A C    
1578 O  O    . HIS   A 221 ? 0.47010 0.88471 0.65356 -0.17717 -0.08926 0.07110  373 HIS   A O    
1579 C  CB   . HIS   A 221 ? 0.50612 0.99462 0.73269 -0.21508 -0.09496 0.07462  373 HIS   A CB   
1580 C  CG   . HIS   A 221 ? 0.52847 1.05057 0.77537 -0.20305 -0.10570 0.07754  373 HIS   A CG   
1581 N  ND1  . HIS   A 221 ? 0.49216 1.05469 0.77271 -0.18704 -0.10085 0.08150  373 HIS   A ND1  
1582 C  CD2  . HIS   A 221 ? 0.48514 1.00692 0.72318 -0.20378 -0.12148 0.07747  373 HIS   A CD2  
1583 C  CE1  . HIS   A 221 ? 0.49420 1.07713 0.78623 -0.17783 -0.11388 0.08576  373 HIS   A CE1  
1584 N  NE2  . HIS   A 221 ? 0.52097 1.08025 0.78565 -0.18811 -0.12624 0.08370  373 HIS   A NE2  
1585 N  N    . GLN   A 222 ? 0.39566 0.86200 0.62660 -0.15446 -0.07621 0.07478  374 GLN   A N    
1586 C  CA   . GLN   A 222 ? 0.42691 0.87295 0.65138 -0.13375 -0.07835 0.07637  374 GLN   A CA   
1587 C  C    . GLN   A 222 ? 0.45154 0.85085 0.64464 -0.13161 -0.07230 0.07244  374 GLN   A C    
1588 O  O    . GLN   A 222 ? 0.45286 0.83015 0.63296 -0.12054 -0.07619 0.07414  374 GLN   A O    
1589 C  CB   . GLN   A 222 ? 0.41661 0.86888 0.63835 -0.13267 -0.09476 0.08191  374 GLN   A CB   
1590 C  CG   . GLN   A 222 ? 0.54204 1.04190 0.79870 -0.12698 -0.10237 0.08832  374 GLN   A CG   
1591 C  CD   . GLN   A 222 ? 0.61173 1.12200 0.86152 -0.13114 -0.12033 0.09410  374 GLN   A CD   
1592 O  OE1  . GLN   A 222 ? 0.62399 1.10927 0.84269 -0.14239 -0.12651 0.09040  374 GLN   A OE1  
1593 N  NE2  . GLN   A 222 ? 0.64227 1.19140 0.92143 -0.12144 -0.12910 0.10267  374 GLN   A NE2  
1594 N  N    . LEU   A 223 ? 0.45721 0.84347 0.63868 -0.14235 -0.06307 0.06854  375 LEU   A N    
1595 C  CA   . LEU   A 223 ? 0.46276 0.80644 0.61449 -0.14207 -0.05953 0.06556  375 LEU   A CA   
1596 C  C    . LEU   A 223 ? 0.49685 0.82727 0.64873 -0.12211 -0.05294 0.06396  375 LEU   A C    
1597 O  O    . LEU   A 223 ? 0.51926 0.82082 0.65199 -0.11627 -0.05582 0.06371  375 LEU   A O    
1598 C  CB   . LEU   A 223 ? 0.47428 0.81041 0.61625 -0.15695 -0.05167 0.06463  375 LEU   A CB   
1599 C  CG   . LEU   A 223 ? 0.47790 0.77061 0.58970 -0.15861 -0.05067 0.06295  375 LEU   A CG   
1600 C  CD1  . LEU   A 223 ? 0.41896 0.68605 0.51343 -0.15598 -0.06147 0.06086  375 LEU   A CD1  
1601 C  CD2  . LEU   A 223 ? 0.51947 0.80334 0.62121 -0.17763 -0.04833 0.06594  375 LEU   A CD2  
1602 N  N    . TYR   A 224 ? 0.47640 0.82839 0.65080 -0.11188 -0.04377 0.06173  376 TYR   A N    
1603 C  CA   . TYR   A 224 ? 0.50255 0.84008 0.67933 -0.09404 -0.03791 0.05847  376 TYR   A CA   
1604 C  C    . TYR   A 224 ? 0.51710 0.84652 0.69757 -0.08206 -0.04750 0.06461  376 TYR   A C    
1605 O  O    . TYR   A 224 ? 0.49095 0.79300 0.65763 -0.07483 -0.04723 0.06483  376 TYR   A O    
1606 C  CB   . TYR   A 224 ? 0.50131 0.86576 0.70491 -0.08437 -0.02713 0.05225  376 TYR   A CB   
1607 C  CG   . TYR   A 224 ? 0.55266 0.89921 0.75934 -0.06747 -0.02110 0.04617  376 TYR   A CG   
1608 C  CD1  . TYR   A 224 ? 0.58362 0.90287 0.76653 -0.06959 -0.01518 0.04097  376 TYR   A CD1  
1609 C  CD2  . TYR   A 224 ? 0.54295 0.89915 0.77766 -0.04971 -0.02240 0.04595  376 TYR   A CD2  
1610 C  CE1  . TYR   A 224 ? 0.58948 0.89280 0.77582 -0.05627 -0.01047 0.03430  376 TYR   A CE1  
1611 C  CE2  . TYR   A 224 ? 0.57062 0.90683 0.80955 -0.03575 -0.01761 0.03966  376 TYR   A CE2  
1612 C  CZ   . TYR   A 224 ? 0.60189 0.91226 0.81620 -0.03999 -0.01153 0.03315  376 TYR   A CZ   
1613 O  OH   . TYR   A 224 ? 0.63784 0.92885 0.85689 -0.02813 -0.00747 0.02578  376 TYR   A OH   
1614 N  N    . ALA   A 225 ? 0.52259 0.87825 0.72207 -0.08063 -0.05639 0.07094  377 ALA   A N    
1615 C  CA   . ALA   A 225 ? 0.46215 0.81410 0.66421 -0.07062 -0.06687 0.08006  377 ALA   A CA   
1616 C  C    . ALA   A 225 ? 0.41482 0.74112 0.58385 -0.07889 -0.07359 0.08214  377 ALA   A C    
1617 O  O    . ALA   A 225 ? 0.45704 0.76676 0.61754 -0.07055 -0.07650 0.08758  377 ALA   A O    
1618 C  CB   . ALA   A 225 ? 0.45794 0.84746 0.68559 -0.06929 -0.07668 0.08733  377 ALA   A CB   
1619 N  N    A LYS   A 226 ? 0.39532 0.71839 0.54655 -0.09548 -0.07590 0.07757  378 LYS   A N    
1620 N  N    B LYS   A 226 ? 0.40078 0.72360 0.55189 -0.09547 -0.07580 0.07751  378 LYS   A N    
1621 C  CA   A LYS   A 226 ? 0.44087 0.73932 0.56161 -0.10214 -0.08129 0.07590  378 LYS   A CA   
1622 C  CA   B LYS   A 226 ? 0.44072 0.73916 0.56145 -0.10209 -0.08131 0.07593  378 LYS   A CA   
1623 C  C    A LYS   A 226 ? 0.43929 0.70508 0.54215 -0.09707 -0.07274 0.07171  378 LYS   A C    
1624 C  C    B LYS   A 226 ? 0.43910 0.70467 0.54154 -0.09741 -0.07279 0.07157  378 LYS   A C    
1625 O  O    A LYS   A 226 ? 0.45401 0.70265 0.53835 -0.09436 -0.07560 0.07246  378 LYS   A O    
1626 O  O    B LYS   A 226 ? 0.45455 0.70256 0.53773 -0.09526 -0.07570 0.07196  378 LYS   A O    
1627 C  CB   A LYS   A 226 ? 0.48417 0.78336 0.59341 -0.12074 -0.08612 0.07024  378 LYS   A CB   
1628 C  CB   B LYS   A 226 ? 0.48372 0.78376 0.59327 -0.12064 -0.08653 0.07046  378 LYS   A CB   
1629 C  CG   A LYS   A 226 ? 0.51156 0.84383 0.63528 -0.12848 -0.09717 0.07354  378 LYS   A CG   
1630 C  CG   B LYS   A 226 ? 0.51283 0.84520 0.63562 -0.12762 -0.09819 0.07405  378 LYS   A CG   
1631 C  CD   A LYS   A 226 ? 0.55665 0.88021 0.65998 -0.14561 -0.10628 0.06672  378 LYS   A CD   
1632 C  CD   B LYS   A 226 ? 0.54220 0.87916 0.66263 -0.14801 -0.10136 0.06812  378 LYS   A CD   
1633 C  CE   A LYS   A 226 ? 0.57722 0.91120 0.69054 -0.16354 -0.10594 0.06336  378 LYS   A CE   
1634 C  CE   B LYS   A 226 ? 0.58519 0.90205 0.67854 -0.15887 -0.11066 0.06085  378 LYS   A CE   
1635 N  NZ   A LYS   A 226 ? 0.53457 0.91273 0.67537 -0.16790 -0.11263 0.06837  378 LYS   A NZ   
1636 N  NZ   B LYS   A 226 ? 0.61028 0.92700 0.70301 -0.18011 -0.11502 0.05478  378 LYS   A NZ   
1637 N  N    . MET   A 227 ? 0.39804 0.65852 0.50612 -0.09607 -0.06229 0.06717  379 MET   A N    
1638 C  CA   . MET   A 227 ? 0.40899 0.64202 0.50150 -0.09154 -0.05519 0.06326  379 MET   A CA   
1639 C  C    . MET   A 227 ? 0.42521 0.65295 0.52578 -0.07698 -0.05365 0.06696  379 MET   A C    
1640 O  O    . MET   A 227 ? 0.37562 0.58326 0.46051 -0.07405 -0.05350 0.06727  379 MET   A O    
1641 C  CB   . MET   A 227 ? 0.33845 0.57144 0.43304 -0.09552 -0.04536 0.05797  379 MET   A CB   
1642 C  CG   . MET   A 227 ? 0.36628 0.59401 0.44737 -0.11160 -0.04674 0.05669  379 MET   A CG   
1643 S  SD   . MET   A 227 ? 0.41422 0.65010 0.49813 -0.11817 -0.03538 0.05456  379 MET   A SD   
1644 C  CE   . MET   A 227 ? 0.36558 0.56900 0.42703 -0.11205 -0.03146 0.05159  379 MET   A CE   
1645 N  N    . ILE   A 228 ? 0.51626 0.76218 0.64317 -0.06781 -0.05277 0.07005  380 ILE   A N    
1646 C  CA   . ILE   A 228 ? 0.52994 0.76871 0.66835 -0.05449 -0.05312 0.07546  380 ILE   A CA   
1647 C  C    . ILE   A 228 ? 0.50687 0.74226 0.63382 -0.05450 -0.06288 0.08625  380 ILE   A C    
1648 O  O    . ILE   A 228 ? 0.49895 0.71818 0.61999 -0.04939 -0.06247 0.09096  380 ILE   A O    
1649 C  CB   . ILE   A 228 ? 0.55332 0.81266 0.72555 -0.04361 -0.05187 0.07649  380 ILE   A CB   
1650 C  CG1  . ILE   A 228 ? 0.55627 0.82096 0.73757 -0.04297 -0.04006 0.06353  380 ILE   A CG1  
1651 C  CG2  . ILE   A 228 ? 0.57149 0.82009 0.75821 -0.03012 -0.05471 0.08459  380 ILE   A CG2  
1652 C  CD1  . ILE   A 228 ? 0.59590 0.83592 0.76844 -0.03892 -0.03214 0.05569  380 ILE   A CD1  
1653 N  N    . GLN   A 229 ? 0.42457 0.67738 0.54749 -0.06158 -0.07175 0.09014  381 GLN   A N    
1654 C  CA   . GLN   A 229 ? 0.45031 0.70386 0.55769 -0.06315 -0.08084 0.09885  381 GLN   A CA   
1655 C  C    . GLN   A 229 ? 0.45380 0.68394 0.53270 -0.06735 -0.07723 0.09344  381 GLN   A C    
1656 O  O    . GLN   A 229 ? 0.45999 0.68510 0.52924 -0.06412 -0.07920 0.10088  381 GLN   A O    
1657 C  CB   . GLN   A 229 ? 0.51919 0.79621 0.62400 -0.07234 -0.09108 0.09989  381 GLN   A CB   
1658 C  CG   . GLN   A 229 ? 0.54142 0.82310 0.62548 -0.07572 -0.10051 0.10619  381 GLN   A CG   
1659 C  CD   . GLN   A 229 ? 0.57507 0.86149 0.66781 -0.06494 -0.10451 0.12317  381 GLN   A CD   
1660 O  OE1  . GLN   A 229 ? 0.56642 0.84746 0.63937 -0.06568 -0.10637 0.12874  381 GLN   A OE1  
1661 N  NE2  . GLN   A 229 ? 0.57892 0.87593 0.70235 -0.05482 -0.10573 0.13182  381 GLN   A NE2  
1662 N  N    . LYS   A 230 ? 0.44041 0.65759 0.50688 -0.07440 -0.07195 0.08156  382 LYS   A N    
1663 C  CA   . LYS   A 230 ? 0.46532 0.66125 0.50831 -0.07636 -0.06859 0.07556  382 LYS   A CA   
1664 C  C    . LYS   A 230 ? 0.41695 0.59921 0.46330 -0.06790 -0.06168 0.07816  382 LYS   A C    
1665 O  O    . LYS   A 230 ? 0.40475 0.57727 0.43591 -0.06714 -0.06050 0.07813  382 LYS   A O    
1666 C  CB   . LYS   A 230 ? 0.48032 0.66408 0.51324 -0.08464 -0.06563 0.06467  382 LYS   A CB   
1667 C  CG   . LYS   A 230 ? 0.49883 0.68923 0.52319 -0.09558 -0.07352 0.06038  382 LYS   A CG   
1668 C  CD   . LYS   A 230 ? 0.52052 0.70915 0.52496 -0.09629 -0.07934 0.05800  382 LYS   A CD   
1669 C  CE   . LYS   A 230 ? 0.61410 0.81886 0.61500 -0.10606 -0.08968 0.05530  382 LYS   A CE   
1670 N  NZ   . LYS   A 230 ? 0.63390 0.86635 0.65687 -0.10655 -0.09470 0.06481  382 LYS   A NZ   
1671 N  N    . LEU   A 231 ? 0.38544 0.56841 0.45254 -0.06181 -0.05698 0.07923  383 LEU   A N    
1672 C  CA   . LEU   A 231 ? 0.40664 0.57684 0.47990 -0.05473 -0.05206 0.08163  383 LEU   A CA   
1673 C  C    . LEU   A 231 ? 0.40142 0.57526 0.47760 -0.05088 -0.05752 0.09559  383 LEU   A C    
1674 O  O    . LEU   A 231 ? 0.36637 0.52935 0.43634 -0.04991 -0.05512 0.09917  383 LEU   A O    
1675 C  CB   . LEU   A 231 ? 0.36763 0.53851 0.46372 -0.04869 -0.04648 0.07723  383 LEU   A CB   
1676 C  CG   . LEU   A 231 ? 0.35449 0.52234 0.44577 -0.05278 -0.03925 0.06469  383 LEU   A CG   
1677 C  CD1  . LEU   A 231 ? 0.35085 0.52787 0.46575 -0.04653 -0.03386 0.05917  383 LEU   A CD1  
1678 C  CD2  . LEU   A 231 ? 0.35650 0.50605 0.43154 -0.05435 -0.03502 0.05962  383 LEU   A CD2  
1679 N  N    . ALA   A 232 ? 0.40979 0.60117 0.49611 -0.04937 -0.06531 0.10509  384 ALA   A N    
1680 C  CA   . ALA   A 232 ? 0.41435 0.61216 0.50102 -0.04689 -0.07211 0.12169  384 ALA   A CA   
1681 C  C    . ALA   A 232 ? 0.42758 0.62825 0.48512 -0.05413 -0.07406 0.12225  384 ALA   A C    
1682 O  O    . ALA   A 232 ? 0.42877 0.62712 0.47961 -0.05381 -0.07385 0.13243  384 ALA   A O    
1683 C  CB   . ALA   A 232 ? 0.41456 0.63417 0.51852 -0.04345 -0.08153 0.13207  384 ALA   A CB   
1684 N  N    . ASP   A 233 ? 0.37967 0.58617 0.42053 -0.06109 -0.07583 0.11101  385 ASP   A N    
1685 C  CA   . ASP   A 233 ? 0.40462 0.61200 0.41808 -0.06660 -0.07625 0.10604  385 ASP   A CA   
1686 C  C    . ASP   A 233 ? 0.42222 0.61264 0.42785 -0.06472 -0.06736 0.10170  385 ASP   A C    
1687 O  O    . ASP   A 233 ? 0.42768 0.62297 0.41803 -0.06592 -0.06637 0.10476  385 ASP   A O    
1688 C  CB   . ASP   A 233 ? 0.40404 0.61185 0.40464 -0.07387 -0.07864 0.09088  385 ASP   A CB   
1689 C  CG   . ASP   A 233 ? 0.52444 0.75325 0.53138 -0.07830 -0.08849 0.09409  385 ASP   A CG   
1690 O  OD1  . ASP   A 233 ? 0.55748 0.78652 0.55559 -0.08628 -0.09156 0.08218  385 ASP   A OD1  
1691 O  OD2  . ASP   A 233 ? 0.52065 0.76546 0.54265 -0.07411 -0.09392 0.10874  385 ASP   A OD2  
1692 N  N    . LEU   A 234 ? 0.38486 0.55895 0.40092 -0.06219 -0.06081 0.09442  386 LEU   A N    
1693 C  CA   . LEU   A 234 ? 0.43779 0.59823 0.44818 -0.06082 -0.05345 0.08961  386 LEU   A CA   
1694 C  C    . LEU   A 234 ? 0.47670 0.63743 0.49563 -0.05838 -0.05180 0.10283  386 LEU   A C    
1695 O  O    . LEU   A 234 ? 0.47353 0.63345 0.48277 -0.05961 -0.04777 0.10295  386 LEU   A O    
1696 C  CB   . LEU   A 234 ? 0.43166 0.57806 0.45047 -0.05961 -0.04823 0.07962  386 LEU   A CB   
1697 C  CG   . LEU   A 234 ? 0.47117 0.61253 0.47759 -0.06379 -0.04868 0.06773  386 LEU   A CG   
1698 C  CD1  . LEU   A 234 ? 0.52745 0.65986 0.54247 -0.06365 -0.04407 0.06172  386 LEU   A CD1  
1699 C  CD2  . LEU   A 234 ? 0.51964 0.65524 0.50694 -0.06416 -0.04749 0.06099  386 LEU   A CD2  
1700 N  N    . ARG   A 235 ? 0.40517 0.56698 0.44431 -0.05495 -0.05491 0.11429  387 ARG   A N    
1701 C  CA   . ARG   A 235 ? 0.41701 0.57553 0.46610 -0.05383 -0.05469 0.12923  387 ARG   A CA   
1702 C  C    . ARG   A 235 ? 0.47474 0.64933 0.50632 -0.05835 -0.05773 0.14153  387 ARG   A C    
1703 O  O    . ARG   A 235 ? 0.43838 0.61229 0.46730 -0.06124 -0.05420 0.14952  387 ARG   A O    
1704 C  CB   . ARG   A 235 ? 0.41431 0.56972 0.48993 -0.04779 -0.05920 0.13977  387 ARG   A CB   
1705 C  CG   . ARG   A 235 ? 0.44956 0.59353 0.54326 -0.04271 -0.05508 0.12632  387 ARG   A CG   
1706 C  CD   . ARG   A 235 ? 0.44357 0.57032 0.53805 -0.04405 -0.04724 0.11623  387 ARG   A CD   
1707 N  NE   . ARG   A 235 ? 0.39605 0.51430 0.50812 -0.03905 -0.04340 0.10373  387 ARG   A NE   
1708 C  CZ   . ARG   A 235 ? 0.41536 0.52190 0.55162 -0.03339 -0.04315 0.10543  387 ARG   A CZ   
1709 N  NH1  . ARG   A 235 ? 0.35030 0.44930 0.49688 -0.03284 -0.04737 0.12185  387 ARG   A NH1  
1710 N  NH2  . ARG   A 235 ? 0.48094 0.58331 0.63107 -0.02857 -0.03864 0.09058  387 ARG   A NH2  
1711 N  N    . SER   A 236 ? 0.52134 0.71329 0.54050 -0.06011 -0.06421 0.14284  388 SER   A N    
1712 C  CA   . SER   A 236 ? 0.51743 0.72931 0.51626 -0.06492 -0.06702 0.15242  388 SER   A CA   
1713 C  C    . SER   A 236 ? 0.44283 0.65696 0.41960 -0.06801 -0.05977 0.13772  388 SER   A C    
1714 O  O    . SER   A 236 ? 0.43398 0.66017 0.39950 -0.07128 -0.05647 0.14526  388 SER   A O    
1715 C  CB   . SER   A 236 ? 0.57615 0.80771 0.56776 -0.06641 -0.07699 0.15539  388 SER   A CB   
1716 O  OG   . SER   A 236 ? 0.66356 0.91401 0.62706 -0.07198 -0.07790 0.15050  388 SER   A OG   
1717 N  N    . LEU   A 237 ? 0.46429 0.66789 0.43606 -0.06681 -0.05716 0.11750  389 LEU   A N    
1718 C  CA   . LEU   A 237 ? 0.47892 0.68107 0.43469 -0.06698 -0.05061 0.10265  389 LEU   A CA   
1719 C  C    . LEU   A 237 ? 0.48243 0.67732 0.44707 -0.06580 -0.04285 0.10601  389 LEU   A C    
1720 O  O    . LEU   A 237 ? 0.40848 0.61423 0.36211 -0.06670 -0.03756 0.10356  389 LEU   A O    
1721 C  CB   . LEU   A 237 ? 0.44340 0.63093 0.39612 -0.06570 -0.05092 0.08365  389 LEU   A CB   
1722 C  CG   . LEU   A 237 ? 0.49405 0.68972 0.43469 -0.06932 -0.05832 0.07636  389 LEU   A CG   
1723 C  CD1  . LEU   A 237 ? 0.44795 0.62564 0.38972 -0.07009 -0.05922 0.06119  389 LEU   A CD1  
1724 C  CD2  . LEU   A 237 ? 0.52920 0.74192 0.44671 -0.07103 -0.05816 0.07004  389 LEU   A CD2  
1725 N  N    . ASN   A 238 ? 0.48268 0.66141 0.46804 -0.06404 -0.04200 0.11019  390 ASN   A N    
1726 C  CA   . ASN   A 238 ? 0.45189 0.62376 0.44831 -0.06477 -0.03620 0.11407  390 ASN   A CA   
1727 C  C    . ASN   A 238 ? 0.46244 0.64912 0.45754 -0.06968 -0.03549 0.13225  390 ASN   A C    
1728 O  O    . ASN   A 238 ? 0.39057 0.58564 0.38170 -0.07266 -0.02947 0.13234  390 ASN   A O    
1729 C  CB   . ASN   A 238 ? 0.43013 0.58323 0.44912 -0.06245 -0.03687 0.11488  390 ASN   A CB   
1730 C  CG   . ASN   A 238 ? 0.45534 0.59860 0.48584 -0.06409 -0.03158 0.11336  390 ASN   A CG   
1731 O  OD1  . ASN   A 238 ? 0.45536 0.60722 0.48312 -0.06835 -0.02830 0.11965  390 ASN   A OD1  
1732 N  ND2  . ASN   A 238 ? 0.38159 0.50944 0.42527 -0.06159 -0.03069 0.10443  390 ASN   A ND2  
1733 N  N    . GLU   A 239 ? 0.42030 0.61246 0.41967 -0.07090 -0.04190 0.14926  391 GLU   A N    
1734 C  CA   . GLU   A 239 ? 0.52604 0.73265 0.52351 -0.07682 -0.04249 0.17103  391 GLU   A CA   
1735 C  C    . GLU   A 239 ? 0.54715 0.78028 0.51939 -0.08089 -0.03783 0.16772  391 GLU   A C    
1736 O  O    . GLU   A 239 ? 0.51580 0.76052 0.48660 -0.08658 -0.03199 0.17652  391 GLU   A O    
1737 C  CB   . GLU   A 239 ? 0.63602 0.84696 0.63924 -0.07600 -0.05230 0.18957  391 GLU   A CB   
1738 C  CG   . GLU   A 239 ? 0.70446 0.89919 0.73343 -0.07611 -0.05561 0.20977  391 GLU   A CG   
1739 C  CD   . GLU   A 239 ? 0.79313 1.00124 0.82217 -0.07742 -0.06516 0.23582  391 GLU   A CD   
1740 O  OE1  . GLU   A 239 ? 0.79334 1.01060 0.81953 -0.07281 -0.07277 0.23483  391 GLU   A OE1  
1741 O  OE2  . GLU   A 239 ? 0.83541 1.04631 0.86774 -0.08389 -0.06562 0.25855  391 GLU   A OE2  
1742 N  N    . GLU   A 240 ? 0.55288 0.79718 0.50587 -0.07852 -0.04008 0.15402  392 GLU   A N    
1743 C  CA   . GLU   A 240 ? 0.55444 0.82574 0.48280 -0.08123 -0.03581 0.14815  392 GLU   A CA   
1744 C  C    . GLU   A 240 ? 0.50974 0.78081 0.43662 -0.07877 -0.02589 0.13150  392 GLU   A C    
1745 O  O    . GLU   A 240 ? 0.52843 0.82299 0.44609 -0.08225 -0.01901 0.13452  392 GLU   A O    
1746 C  CB   . GLU   A 240 ? 0.55996 0.84036 0.46946 -0.07960 -0.04175 0.13477  392 GLU   A CB   
1747 C  CG   . GLU   A 240 ? 0.50992 0.82144 0.39231 -0.08249 -0.03832 0.12822  392 GLU   A CG   
1748 C  CD   . GLU   A 240 ? 0.50981 0.84877 0.38507 -0.09018 -0.03804 0.15387  392 GLU   A CD   
1749 O  OE1  . GLU   A 240 ? 0.50556 0.84081 0.39201 -0.09301 -0.04586 0.17721  392 GLU   A OE1  
1750 O  OE2  . GLU   A 240 ? 0.54090 0.90605 0.40037 -0.09320 -0.02993 0.15149  392 GLU   A OE2  
1751 N  N    . HIS   A 241 ? 0.47211 0.71996 0.40822 -0.07277 -0.02513 0.11464  393 HIS   A N    
1752 C  CA   . HIS   A 241 ? 0.48872 0.73642 0.42648 -0.06920 -0.01733 0.10062  393 HIS   A CA   
1753 C  C    . HIS   A 241 ? 0.43440 0.68813 0.38659 -0.07454 -0.01179 0.11440  393 HIS   A C    
1754 O  O    . HIS   A 241 ? 0.42198 0.69666 0.37017 -0.07559 -0.00436 0.11165  393 HIS   A O    
1755 C  CB   . HIS   A 241 ? 0.48169 0.70288 0.42772 -0.06290 -0.01909 0.08484  393 HIS   A CB   
1756 C  CG   . HIS   A 241 ? 0.49037 0.71130 0.44097 -0.05844 -0.01296 0.07318  393 HIS   A CG   
1757 N  ND1  . HIS   A 241 ? 0.46505 0.68078 0.43291 -0.06053 -0.01012 0.07871  393 HIS   A ND1  
1758 C  CD2  . HIS   A 241 ? 0.48581 0.71232 0.42740 -0.05154 -0.00988 0.05611  393 HIS   A CD2  
1759 C  CE1  . HIS   A 241 ? 0.48469 0.70557 0.45378 -0.05540 -0.00597 0.06676  393 HIS   A CE1  
1760 N  NE2  . HIS   A 241 ? 0.48403 0.71074 0.43822 -0.04892 -0.00563 0.05327  393 HIS   A NE2  
1761 N  N    . SER   A 242 ? 0.44895 0.68534 0.41956 -0.07821 -0.01533 0.12859  394 SER   A N    
1762 C  CA   . SER   A 242 ? 0.48681 0.72407 0.47376 -0.08514 -0.01137 0.14132  394 SER   A CA   
1763 C  C    . SER   A 242 ? 0.51563 0.78253 0.49386 -0.09359 -0.00721 0.15818  394 SER   A C    
1764 O  O    . SER   A 242 ? 0.52806 0.80920 0.51252 -0.09926 -0.00034 0.16144  394 SER   A O    
1765 C  CB   . SER   A 242 ? 0.46915 0.68057 0.47701 -0.08710 -0.01709 0.15301  394 SER   A CB   
1766 O  OG   . SER   A 242 ? 0.48042 0.66919 0.49607 -0.08030 -0.01923 0.13684  394 SER   A OG   
1767 N  N    . LYS   A 243 ? 0.51234 0.79210 0.47603 -0.09548 -0.01144 0.16982  395 LYS   A N    
1768 C  CA   . LYS   A 243 ? 0.49521 0.80661 0.44755 -0.10472 -0.00773 0.18829  395 LYS   A CA   
1769 C  C    . LYS   A 243 ? 0.48314 0.82660 0.41661 -0.10275 0.00166  0.17168  395 LYS   A C    
1770 O  O    . LYS   A 243 ? 0.51410 0.88476 0.44642 -0.11033 0.00975  0.18065  395 LYS   A O    
1771 C  CB   . LYS   A 243 ? 0.53841 0.85638 0.47942 -0.10691 -0.01644 0.20580  395 LYS   A CB   
1772 C  CG   . LYS   A 243 ? 0.58752 0.94647 0.50229 -0.11312 -0.01343 0.21465  395 LYS   A CG   
1773 C  CD   . LYS   A 243 ? 0.53352 0.89795 0.43699 -0.11404 -0.02476 0.23008  395 LYS   A CD   
1774 C  CE   . LYS   A 243 ? 0.60454 0.99893 0.49701 -0.12592 -0.02516 0.26120  395 LYS   A CE   
1775 N  NZ   . LYS   A 243 ? 0.67021 1.07208 0.55323 -0.12542 -0.03754 0.27408  395 LYS   A NZ   
1776 N  N    . GLN   A 244 ? 0.45898 0.79984 0.37933 -0.09264 0.00093  0.14693  396 GLN   A N    
1777 C  CA   . GLN   A 244 ? 0.41848 0.78596 0.32418 -0.08788 0.00968  0.12730  396 GLN   A CA   
1778 C  C    . GLN   A 244 ? 0.49472 0.85956 0.41774 -0.08416 0.01681  0.11655  396 GLN   A C    
1779 O  O    . GLN   A 244 ? 0.47221 0.86804 0.39164 -0.08380 0.02635  0.11028  396 GLN   A O    
1780 C  CB   . GLN   A 244 ? 0.41256 0.77258 0.30158 -0.07837 0.00543  0.10363  396 GLN   A CB   
1781 C  CG   . GLN   A 244 ? 0.43587 0.80751 0.30528 -0.08283 -0.00162 0.11168  396 GLN   A CG   
1782 C  CD   . GLN   A 244 ? 0.51979 0.88982 0.37093 -0.07578 -0.00496 0.08582  396 GLN   A CD   
1783 O  OE1  . GLN   A 244 ? 0.51451 0.87855 0.36531 -0.06698 -0.00044 0.06180  396 GLN   A OE1  
1784 N  NE2  . GLN   A 244 ? 0.51783 0.89265 0.35508 -0.07976 -0.01387 0.09087  396 GLN   A NE2  
1785 N  N    . TYR   A 245 ? 0.48465 0.81659 0.42666 -0.08132 0.01235  0.11390  397 TYR   A N    
1786 C  CA   . TYR   A 245 ? 0.50042 0.83205 0.45948 -0.07907 0.01741  0.10589  397 TYR   A CA   
1787 C  C    . TYR   A 245 ? 0.47932 0.83158 0.45115 -0.09157 0.02321  0.12494  397 TYR   A C    
1788 O  O    . TYR   A 245 ? 0.47411 0.84980 0.45315 -0.09155 0.03090  0.11898  397 TYR   A O    
1789 C  CB   . TYR   A 245 ? 0.43490 0.72942 0.40888 -0.07495 0.01081  0.09980  397 TYR   A CB   
1790 C  CG   . TYR   A 245 ? 0.39260 0.68828 0.38482 -0.07468 0.01419  0.09440  397 TYR   A CG   
1791 C  CD1  . TYR   A 245 ? 0.38777 0.68827 0.37961 -0.06378 0.01626  0.07524  397 TYR   A CD1  
1792 C  CD2  . TYR   A 245 ? 0.38043 0.67270 0.39134 -0.08551 0.01436  0.10860  397 TYR   A CD2  
1793 C  CE1  . TYR   A 245 ? 0.35364 0.65922 0.36276 -0.06341 0.01802  0.07130  397 TYR   A CE1  
1794 C  CE2  . TYR   A 245 ? 0.36275 0.65937 0.39029 -0.08672 0.01647  0.10287  397 TYR   A CE2  
1795 C  CZ   . TYR   A 245 ? 0.35181 0.65690 0.37805 -0.07554 0.01809  0.08471  397 TYR   A CZ   
1796 O  OH   . TYR   A 245 ? 0.44239 0.75498 0.48584 -0.07658 0.01878  0.07997  397 TYR   A OH   
1797 N  N    . ARG   A 246 ? 0.44467 0.78845 0.42163 -0.10247 0.01914  0.14855  398 ARG   A N    
1798 C  CA   . ARG   A 246 ? 0.52378 0.88376 0.51373 -0.11683 0.02370  0.16960  398 ARG   A CA   
1799 C  C    . ARG   A 246 ? 0.58754 0.99507 0.56235 -0.12182 0.03354  0.17426  398 ARG   A C    
1800 O  O    . ARG   A 246 ? 0.56739 1.00019 0.55324 -0.12980 0.04159  0.17914  398 ARG   A O    
1801 C  CB   . ARG   A 246 ? 0.58932 0.92690 0.58760 -0.12605 0.01595  0.19495  398 ARG   A CB   
1802 C  CG   . ARG   A 246 ? 0.71276 1.05942 0.72707 -0.14287 0.01892  0.21956  398 ARG   A CG   
1803 C  CD   . ARG   A 246 ? 0.82990 1.18937 0.83325 -0.15259 0.01645  0.24872  398 ARG   A CD   
1804 N  NE   . ARG   A 246 ? 0.90640 1.25622 0.93054 -0.16871 0.01486  0.27616  398 ARG   A NE   
1805 C  CZ   . ARG   A 246 ? 0.96763 1.33418 0.98639 -0.18042 0.01433  0.30391  398 ARG   A CZ   
1806 N  NH1  . ARG   A 246 ? 0.97566 1.37143 0.96810 -0.17663 0.01497  0.30478  398 ARG   A NH1  
1807 N  NH2  . ARG   A 246 ? 1.00312 1.35064 1.04405 -0.19175 0.01043  0.32263  398 ARG   A NH2  
1808 N  N    . SER   A 247 ? 0.57442 0.99782 0.52393 -0.11785 0.03327  0.17179  399 SER   A N    
1809 C  CA   . SER   A 247 ? 0.59167 1.06418 0.52343 -0.12146 0.04357  0.17226  399 SER   A CA   
1810 C  C    . SER   A 247 ? 0.54924 1.04254 0.48314 -0.11036 0.05288  0.14466  399 SER   A C    
1811 O  O    . SER   A 247 ? 0.55432 1.08781 0.49127 -0.11567 0.06393  0.14689  399 SER   A O    
1812 C  CB   . SER   A 247 ? 0.57645 1.06039 0.47908 -0.11929 0.03980  0.17238  399 SER   A CB   
1813 O  OG   . SER   A 247 ? 0.59034 1.11403 0.47273 -0.11365 0.04939  0.15312  399 SER   A OG   
1814 N  N    . LEU   A 248 ? 0.50564 0.97302 0.43971 -0.09488 0.04840  0.11954  400 LEU   A N    
1815 C  CA   . LEU   A 248 ? 0.53174 1.01453 0.46983 -0.08173 0.05534  0.09355  400 LEU   A CA   
1816 C  C    . LEU   A 248 ? 0.54386 1.03303 0.50931 -0.08524 0.05936  0.09711  400 LEU   A C    
1817 O  O    . LEU   A 248 ? 0.54330 1.07085 0.51484 -0.08312 0.06954  0.08963  400 LEU   A O    
1818 C  CB   . LEU   A 248 ? 0.49647 0.94401 0.43015 -0.06602 0.04759  0.07021  400 LEU   A CB   
1819 C  CG   . LEU   A 248 ? 0.50207 0.95084 0.40929 -0.05976 0.04524  0.05648  400 LEU   A CG   
1820 C  CD1  . LEU   A 248 ? 0.49948 0.90534 0.40663 -0.04899 0.03538  0.03997  400 LEU   A CD1  
1821 C  CD2  . LEU   A 248 ? 0.46822 0.95878 0.36321 -0.05239 0.05630  0.03772  400 LEU   A CD2  
1822 N  N    . SER   A 249 ? 0.55011 1.00457 0.53309 -0.09078 0.05145  0.10738  401 SER   A N    
1823 C  CA   . SER   A 249 ? 0.53809 0.99603 0.54696 -0.09481 0.05318  0.10847  401 SER   A CA   
1824 C  C    . SER   A 249 ? 0.57668 1.06802 0.59629 -0.11284 0.06077  0.12974  401 SER   A C    
1825 O  O    . SER   A 249 ? 0.58660 1.09286 0.62785 -0.11740 0.06403  0.12910  401 SER   A O    
1826 C  CB   . SER   A 249 ? 0.50207 0.91385 0.52448 -0.09612 0.04248  0.11078  401 SER   A CB   
1827 O  OG   . SER   A 249 ? 0.51339 0.90799 0.53995 -0.11054 0.03831  0.13362  401 SER   A OG   
1828 N  N    . PHE   A 250 ? 0.60018 1.10516 0.60570 -0.12423 0.06305  0.14976  402 PHE   A N    
1829 C  CA   . PHE   A 250 ? 0.62293 1.16220 0.63757 -0.14315 0.07080  0.17260  402 PHE   A CA   
1830 C  C    . PHE   A 250 ? 0.61060 1.20542 0.62629 -0.13993 0.08449  0.16043  402 PHE   A C    
1831 O  O    . PHE   A 250 ? 0.64007 1.25723 0.67449 -0.15116 0.08916  0.16918  402 PHE   A O    
1832 C  CB   . PHE   A 250 ? 0.69070 1.23445 0.68737 -0.15530 0.06952  0.19862  402 PHE   A CB   
1833 C  CG   . PHE   A 250 ? 0.77354 1.32783 0.78201 -0.17260 0.07005  0.22197  402 PHE   A CG   
1834 C  CD1  . PHE   A 250 ? 0.79381 1.31791 0.82723 -0.18537 0.06388  0.23806  402 PHE   A CD1  
1835 C  CD2  . PHE   A 250 ? 0.80875 1.40119 0.80360 -0.17590 0.07602  0.22607  402 PHE   A CD2  
1836 C  CE1  . PHE   A 250 ? 0.81498 1.34462 0.85917 -0.20117 0.06355  0.25861  402 PHE   A CE1  
1837 C  CE2  . PHE   A 250 ? 0.84183 1.44312 0.84715 -0.19225 0.07607  0.24820  402 PHE   A CE2  
1838 C  CZ   . PHE   A 250 ? 0.83984 1.40866 0.86977 -0.20494 0.06976  0.26486  402 PHE   A CZ   
1839 N  N    . GLN   A 251 ? 0.58301 1.19455 0.57992 -0.12292 0.08887  0.13743  403 GLN   A N    
1840 C  CA   . GLN   A 251 ? 0.56289 1.22656 0.56269 -0.11548 0.10207  0.12089  403 GLN   A CA   
1841 C  C    . GLN   A 251 ? 0.48517 1.14257 0.51272 -0.10558 0.10035  0.10479  403 GLN   A C    
1842 O  O    . GLN   A 251 ? 0.44222 1.06201 0.47034 -0.08975 0.09144  0.08715  403 GLN   A O    
1843 C  CB   . GLN   A 251 ? 0.62305 1.29972 0.59643 -0.09819 0.10586  0.09704  403 GLN   A CB   
1844 C  CG   . GLN   A 251 ? 0.75311 1.41542 0.69684 -0.10328 0.10028  0.10740  403 GLN   A CG   
1845 C  CD   . GLN   A 251 ? 0.86306 1.54518 0.79964 -0.11901 0.10047  0.12984  403 GLN   A CD   
1846 O  OE1  . GLN   A 251 ? 0.89470 1.55458 0.83294 -0.13355 0.09255  0.15708  403 GLN   A OE1  
1847 N  NE2  . GLN   A 251 ? 0.91207 1.63657 0.84199 -0.11556 0.10941  0.11835  403 GLN   A NE2  
1848 N  N    . PRO   A 252 ? 0.43323 1.12561 0.48421 -0.11506 0.10725  0.11129  404 PRO   A N    
1849 C  CA   . PRO   A 252 ? 0.40737 1.09714 0.48603 -0.10681 0.10409  0.09787  404 PRO   A CA   
1850 C  C    . PRO   A 252 ? 0.42238 1.11839 0.49929 -0.07965 0.10531  0.06708  404 PRO   A C    
1851 O  O    . PRO   A 252 ? 0.48518 1.15145 0.57400 -0.06759 0.09581  0.05505  404 PRO   A O    
1852 C  CB   . PRO   A 252 ? 0.44397 1.16939 0.54266 -0.12134 0.10973  0.10919  404 PRO   A CB   
1853 C  CG   . PRO   A 252 ? 0.47901 1.19719 0.56308 -0.14078 0.10914  0.13456  404 PRO   A CG   
1854 C  CD   . PRO   A 252 ? 0.46550 1.17893 0.51753 -0.13214 0.11037  0.13048  404 PRO   A CD   
1855 N  N    . GLU   A 253 ? 0.44229 1.17565 0.50424 -0.06963 0.11643  0.05394  405 GLU   A N    
1856 C  CA   . GLU   A 253 ? 0.48651 1.22167 0.54730 -0.04245 0.11726  0.02310  405 GLU   A CA   
1857 C  C    . GLU   A 253 ? 0.48708 1.15923 0.53442 -0.03002 0.10315  0.01280  405 GLU   A C    
1858 O  O    . GLU   A 253 ? 0.46843 1.12363 0.52567 -0.01049 0.09769  -0.00631 405 GLU   A O    
1859 C  CB   . GLU   A 253 ? 0.58324 1.36400 0.62557 -0.03526 0.13119  0.00938  405 GLU   A CB   
1860 C  CG   . GLU   A 253 ? 0.71003 1.47780 0.71764 -0.04602 0.13006  0.01964  405 GLU   A CG   
1861 C  CD   . GLU   A 253 ? 0.79614 1.57228 0.80038 -0.07168 0.12957  0.05082  405 GLU   A CD   
1862 O  OE1  . GLU   A 253 ? 0.82210 1.59516 0.84889 -0.08546 0.12705  0.06913  405 GLU   A OE1  
1863 O  OE2  . GLU   A 253 ? 0.83193 1.61670 0.81136 -0.07802 0.13074  0.05663  405 GLU   A OE2  
1864 N  N    . ASN   A 254 ? 0.44743 1.08594 0.47359 -0.04123 0.09680  0.02644  406 ASN   A N    
1865 C  CA   . ASN   A 254 ? 0.45003 1.03107 0.46574 -0.03249 0.08354  0.01924  406 ASN   A CA   
1866 C  C    . ASN   A 254 ? 0.39442 0.94115 0.43009 -0.03579 0.07290  0.02700  406 ASN   A C    
1867 O  O    . ASN   A 254 ? 0.34815 0.86338 0.38690 -0.02186 0.06442  0.01378  406 ASN   A O    
1868 C  CB   . ASN   A 254 ? 0.50048 1.06181 0.49028 -0.04330 0.07992  0.03172  406 ASN   A CB   
1869 C  CG   . ASN   A 254 ? 0.58091 1.16344 0.54518 -0.03528 0.08615  0.01608  406 ASN   A CG   
1870 O  OD1  . ASN   A 254 ? 0.59154 1.18671 0.55624 -0.01748 0.09046  -0.00939 406 ASN   A OD1  
1871 N  ND2  . ASN   A 254 ? 0.58947 1.17623 0.53184 -0.04804 0.08599  0.03078  406 ASN   A ND2  
1872 N  N    . SER   A 255 ? 0.45556 1.00804 0.50452 -0.05495 0.07299  0.04837  407 SER   A N    
1873 C  CA   . SER   A 255 ? 0.51423 1.03918 0.58232 -0.05956 0.06357  0.05358  407 SER   A CA   
1874 C  C    . SER   A 255 ? 0.45205 0.98844 0.53906 -0.04448 0.06184  0.03713  407 SER   A C    
1875 O  O    . SER   A 255 ? 0.44047 0.94632 0.53506 -0.04081 0.05156  0.03424  407 SER   A O    
1876 C  CB   . SER   A 255 ? 0.57185 1.10945 0.65503 -0.08276 0.06562  0.07602  407 SER   A CB   
1877 O  OG   . SER   A 255 ? 0.63058 1.13480 0.70316 -0.09524 0.06019  0.09274  407 SER   A OG   
1878 N  N    A MET   A 256 ? 0.43376 1.01611 0.52887 -0.03510 0.07162  0.02646  408 MET   A N    
1879 N  N    C MET   A 256 ? 0.42439 1.00681 0.51954 -0.03517 0.07163  0.02652  408 MET   A N    
1880 C  CA   A MET   A 256 ? 0.43548 1.03376 0.55267 -0.01968 0.06952  0.01251  408 MET   A CA   
1881 C  CA   C MET   A 256 ? 0.44058 1.03869 0.55773 -0.01972 0.06949  0.01255  408 MET   A CA   
1882 C  C    A MET   A 256 ? 0.43853 0.99805 0.54797 0.00174  0.05986  -0.00403 408 MET   A C    
1883 C  C    C MET   A 256 ? 0.44532 1.00445 0.55470 0.00157  0.05977  -0.00387 408 MET   A C    
1884 O  O    A MET   A 256 ? 0.43114 0.98428 0.55705 0.01145  0.05197  -0.00925 408 MET   A O    
1885 O  O    C MET   A 256 ? 0.43028 0.98274 0.55604 0.01112  0.05182  -0.00896 408 MET   A O    
1886 C  CB   A MET   A 256 ? 0.44227 1.10089 0.57080 -0.01219 0.08316  0.00319  408 MET   A CB   
1887 C  CB   C MET   A 256 ? 0.43697 1.09508 0.56527 -0.01199 0.08308  0.00303  408 MET   A CB   
1888 C  CG   A MET   A 256 ? 0.44448 1.14921 0.59770 -0.02938 0.08961  0.01668  408 MET   A CG   
1889 C  CG   C MET   A 256 ? 0.44397 1.14783 0.59830 -0.02762 0.08896  0.01527  408 MET   A CG   
1890 S  SD   A MET   A 256 ? 0.46617 1.24835 0.63044 -0.02137 0.10832  0.00574  408 MET   A SD   
1891 S  SD   C MET   A 256 ? 0.46757 1.24725 0.63533 -0.01614 0.10650  0.00163  408 MET   A SD   
1892 C  CE   A MET   A 256 ? 0.47154 1.23918 0.62731 0.01446  0.10659  -0.02566 408 MET   A CE   
1893 C  CE   C MET   A 256 ? 0.45487 1.26012 0.60010 -0.03936 0.12002  0.01956  408 MET   A CE   
1894 N  N    . LYS   A 257 ? 0.42095 0.95551 0.50591 0.00835  0.05962  -0.01144 409 LYS   A N    
1895 C  CA   . LYS   A 257 ? 0.43774 0.93396 0.51539 0.02674  0.05056  -0.02626 409 LYS   A CA   
1896 C  C    . LYS   A 257 ? 0.38000 0.82511 0.44849 0.01900  0.03841  -0.01661 409 LYS   A C    
1897 O  O    . LYS   A 257 ? 0.39216 0.80348 0.45554 0.03122  0.02986  -0.02529 409 LYS   A O    
1898 C  CB   . LYS   A 257 ? 0.49643 0.99235 0.55395 0.03799  0.05591  -0.04262 409 LYS   A CB   
1899 C  CG   . LYS   A 257 ? 0.58260 1.13435 0.64524 0.04390  0.07042  -0.05318 409 LYS   A CG   
1900 C  CD   . LYS   A 257 ? 0.68161 1.25793 0.77172 0.06360  0.07145  -0.06710 409 LYS   A CD   
1901 C  CE   . LYS   A 257 ? 0.76864 1.34594 0.85565 0.08872  0.07441  -0.09468 409 LYS   A CE   
1902 N  NZ   . LYS   A 257 ? 0.78909 1.35155 0.89901 0.11094  0.06534  -0.10534 409 LYS   A NZ   
1903 N  N    . LEU   A 258 ? 0.31973 0.75887 0.38739 -0.00087 0.03759  0.00106  410 LEU   A N    
1904 C  CA   . LEU   A 258 ? 0.40318 0.79914 0.46537 -0.00782 0.02725  0.00879  410 LEU   A CA   
1905 C  C    . LEU   A 258 ? 0.39459 0.78706 0.47498 -0.00595 0.01972  0.00904  410 LEU   A C    
1906 O  O    . LEU   A 258 ? 0.34068 0.76555 0.43977 -0.00131 0.02198  0.00570  410 LEU   A O    
1907 C  CB   . LEU   A 258 ? 0.40901 0.79912 0.46606 -0.02782 0.02888  0.02605  410 LEU   A CB   
1908 C  CG   . LEU   A 258 ? 0.38173 0.77648 0.41928 -0.03190 0.03449  0.02986  410 LEU   A CG   
1909 C  CD1  . LEU   A 258 ? 0.38202 0.76510 0.41787 -0.05019 0.03322  0.04960  410 LEU   A CD1  
1910 C  CD2  . LEU   A 258 ? 0.35784 0.72519 0.37672 -0.01977 0.02980  0.01726  410 LEU   A CD2  
1911 N  N    . THR   A 259 ? 0.40970 0.76595 0.48459 -0.00974 0.01060  0.01280  411 THR   A N    
1912 C  CA   . THR   A 259 ? 0.38824 0.74300 0.47709 -0.01033 0.00290  0.01369  411 THR   A CA   
1913 C  C    . THR   A 259 ? 0.37518 0.73034 0.47205 -0.03009 0.00250  0.02450  411 THR   A C    
1914 O  O    . THR   A 259 ? 0.38788 0.73387 0.47799 -0.04178 0.00634  0.03272  411 THR   A O    
1915 C  CB   . THR   A 259 ? 0.42006 0.73850 0.49817 -0.00169 -0.00702 0.00991  411 THR   A CB   
1916 O  OG1  . THR   A 259 ? 0.46434 0.75291 0.52972 -0.01307 -0.00921 0.01617  411 THR   A OG1  
1917 C  CG2  . THR   A 259 ? 0.43044 0.73882 0.49908 0.01565  -0.00704 -0.00029 411 THR   A CG2  
1918 N  N    . PRO   A 260 ? 0.38125 0.74785 0.49396 -0.03438 -0.00273 0.02461  412 PRO   A N    
1919 C  CA   . PRO   A 260 ? 0.36051 0.72253 0.48140 -0.05370 -0.00416 0.03200  412 PRO   A CA   
1920 C  C    . PRO   A 260 ? 0.35798 0.67934 0.46464 -0.05913 -0.00828 0.03403  412 PRO   A C    
1921 O  O    . PRO   A 260 ? 0.38728 0.69879 0.49701 -0.07325 -0.00633 0.04114  412 PRO   A O    
1922 C  CB   . PRO   A 260 ? 0.38505 0.76652 0.52284 -0.05437 -0.01112 0.02782  412 PRO   A CB   
1923 C  CG   . PRO   A 260 ? 0.42583 0.83694 0.57149 -0.03759 -0.00950 0.02217  412 PRO   A CG   
1924 C  CD   . PRO   A 260 ? 0.37546 0.76479 0.50210 -0.02238 -0.00736 0.01799  412 PRO   A CD   
1925 N  N    . LEU   A 261 ? 0.32739 0.62539 0.42022 -0.04832 -0.01397 0.02854  413 LEU   A N    
1926 C  CA   . LEU   A 261 ? 0.37804 0.64245 0.45865 -0.05302 -0.01681 0.02976  413 LEU   A CA   
1927 C  C    . LEU   A 261 ? 0.38001 0.63236 0.45116 -0.05530 -0.01120 0.03570  413 LEU   A C    
1928 O  O    . LEU   A 261 ? 0.39392 0.63118 0.46616 -0.06526 -0.01069 0.04114  413 LEU   A O    
1929 C  CB   . LEU   A 261 ? 0.41936 0.66565 0.48734 -0.04233 -0.02356 0.02447  413 LEU   A CB   
1930 C  CG   . LEU   A 261 ? 0.44613 0.66310 0.50241 -0.04698 -0.02594 0.02473  413 LEU   A CG   
1931 C  CD1  . LEU   A 261 ? 0.46355 0.67945 0.52859 -0.05944 -0.02778 0.02320  413 LEU   A CD1  
1932 C  CD2  . LEU   A 261 ? 0.36987 0.57204 0.41298 -0.03769 -0.03177 0.02215  413 LEU   A CD2  
1933 N  N    . VAL   A 262 ? 0.39204 0.65182 0.45456 -0.04568 -0.00750 0.03413  414 VAL   A N    
1934 C  CA   . VAL   A 262 ? 0.37968 0.63352 0.43152 -0.04814 -0.00298 0.03972  414 VAL   A CA   
1935 C  C    . VAL   A 262 ? 0.39663 0.66349 0.45847 -0.06220 0.00185  0.05148  414 VAL   A C    
1936 O  O    . VAL   A 262 ? 0.40250 0.65387 0.46087 -0.06933 0.00173  0.06017  414 VAL   A O    
1937 C  CB   . VAL   A 262 ? 0.40723 0.67348 0.44908 -0.03619 0.00065  0.03303  414 VAL   A CB   
1938 C  CG1  . VAL   A 262 ? 0.37654 0.64585 0.40692 -0.04078 0.00549  0.03927  414 VAL   A CG1  
1939 C  CG2  . VAL   A 262 ? 0.39683 0.64114 0.42869 -0.02379 -0.00540 0.02340  414 VAL   A CG2  
1940 N  N    . LEU   A 263 ? 0.39024 0.68625 0.46646 -0.06675 0.00563  0.05317  415 LEU   A N    
1941 C  CA   . LEU   A 263 ? 0.41471 0.72313 0.50222 -0.08252 0.00994  0.06647  415 LEU   A CA   
1942 C  C    . LEU   A 263 ? 0.42405 0.70691 0.52149 -0.09413 0.00468  0.07089  415 LEU   A C    
1943 O  O    . LEU   A 263 ? 0.42222 0.69782 0.52485 -0.10577 0.00607  0.08378  415 LEU   A O    
1944 C  CB   . LEU   A 263 ? 0.44703 0.79481 0.55057 -0.08623 0.01489  0.06653  415 LEU   A CB   
1945 C  CG   . LEU   A 263 ? 0.44518 0.82662 0.54273 -0.07790 0.02333  0.06417  415 LEU   A CG   
1946 C  CD1  . LEU   A 263 ? 0.41687 0.83908 0.53425 -0.07868 0.02725  0.06088  415 LEU   A CD1  
1947 C  CD2  . LEU   A 263 ? 0.43653 0.82525 0.52480 -0.08762 0.02975  0.07851  415 LEU   A CD2  
1948 N  N    . GLU   A 264 ? 0.48397 0.75359 0.58449 -0.09109 -0.00157 0.06030  416 GLU   A N    
1949 C  CA   . GLU   A 264 ? 0.48196 0.72844 0.59148 -0.10106 -0.00613 0.06008  416 GLU   A CA   
1950 C  C    . GLU   A 264 ? 0.48588 0.70128 0.58491 -0.09798 -0.00780 0.06209  416 GLU   A C    
1951 O  O    . GLU   A 264 ? 0.48017 0.67797 0.58830 -0.10668 -0.00872 0.06808  416 GLU   A O    
1952 C  CB   . GLU   A 264 ? 0.46819 0.71552 0.58158 -0.09906 -0.01216 0.04710  416 GLU   A CB   
1953 C  CG   . GLU   A 264 ? 0.49205 0.72293 0.61725 -0.11119 -0.01623 0.04317  416 GLU   A CG   
1954 C  CD   . GLU   A 264 ? 0.53996 0.77114 0.66258 -0.10838 -0.02276 0.02934  416 GLU   A CD   
1955 O  OE1  . GLU   A 264 ? 0.53521 0.74596 0.64555 -0.10263 -0.02516 0.02304  416 GLU   A OE1  
1956 O  OE2  . GLU   A 264 ? 0.51815 0.77284 0.65112 -0.11257 -0.02565 0.02539  416 GLU   A OE2  
1957 N  N    . VAL   A 265 ? 0.46069 0.66901 0.54278 -0.08568 -0.00862 0.05717  417 VAL   A N    
1958 C  CA   . VAL   A 265 ? 0.44963 0.63244 0.52362 -0.08280 -0.01066 0.05783  417 VAL   A CA   
1959 C  C    . VAL   A 265 ? 0.48647 0.66933 0.55572 -0.08400 -0.00789 0.07057  417 VAL   A C    
1960 O  O    . VAL   A 265 ? 0.52215 0.68926 0.59761 -0.08862 -0.00919 0.07840  417 VAL   A O    
1961 C  CB   . VAL   A 265 ? 0.43868 0.61368 0.49779 -0.07176 -0.01356 0.04801  417 VAL   A CB   
1962 C  CG1  . VAL   A 265 ? 0.49278 0.64693 0.54474 -0.06954 -0.01494 0.04927  417 VAL   A CG1  
1963 C  CG2  . VAL   A 265 ? 0.35054 0.52607 0.41312 -0.07181 -0.01741 0.03816  417 VAL   A CG2  
1964 N  N    . PHE   A 266 ? 0.47006 0.67187 0.52863 -0.07938 -0.00443 0.07248  418 PHE   A N    
1965 C  CA   . PHE   A 266 ? 0.49268 0.69912 0.54270 -0.08070 -0.00234 0.08395  418 PHE   A CA   
1966 C  C    . PHE   A 266 ? 0.50631 0.72550 0.56745 -0.09292 0.00096  0.10014  418 PHE   A C    
1967 O  O    . PHE   A 266 ? 0.47417 0.69091 0.53198 -0.09680 0.00054  0.11421  418 PHE   A O    
1968 C  CB   . PHE   A 266 ? 0.42583 0.64941 0.45899 -0.07175 0.00049  0.07742  418 PHE   A CB   
1969 C  CG   . PHE   A 266 ? 0.39722 0.60366 0.41792 -0.06166 -0.00372 0.06573  418 PHE   A CG   
1970 C  CD1  . PHE   A 266 ? 0.36372 0.54590 0.38730 -0.06154 -0.00860 0.06337  418 PHE   A CD1  
1971 C  CD2  . PHE   A 266 ? 0.37716 0.59225 0.38391 -0.05295 -0.00251 0.05668  418 PHE   A CD2  
1972 C  CE1  . PHE   A 266 ? 0.41374 0.58214 0.42649 -0.05459 -0.01214 0.05478  418 PHE   A CE1  
1973 C  CE2  . PHE   A 266 ? 0.38448 0.58119 0.38121 -0.04570 -0.00706 0.04714  418 PHE   A CE2  
1974 C  CZ   . PHE   A 266 ? 0.40237 0.57636 0.40201 -0.04740 -0.01187 0.04758  418 PHE   A CZ   
1975 N  N    . GLY   A 267 ? 0.49863 0.73271 0.57348 -0.09994 0.00359  0.09994  419 GLY   A N    
1976 C  CA   . GLY   A 267 ? 0.55643 0.80219 0.64394 -0.11426 0.00663  0.11667  419 GLY   A CA   
1977 C  C    . GLY   A 267 ? 0.69860 0.98347 0.78782 -0.11780 0.01391  0.11820  419 GLY   A C    
1978 O  O    . GLY   A 267 ? 0.64298 0.94658 0.72102 -0.10653 0.01707  0.10655  419 GLY   A O    
1979 N  N    . ASN   A 268 ? 0.84926 1.14695 0.95410 -0.13349 0.01670  0.13239  420 ASN   A N    
1980 C  CA   . ASN   A 268 ? 0.90417 1.24417 1.01521 -0.13947 0.02454  0.13503  420 ASN   A CA   
1981 C  C    . ASN   A 268 ? 0.98149 1.35177 1.07285 -0.13229 0.03202  0.13658  420 ASN   A C    
1982 O  O    . ASN   A 268 ? 1.03778 1.44847 1.13232 -0.13458 0.04019  0.13648  420 ASN   A O    
1983 C  CB   . ASN   A 268 ? 0.91637 1.26233 1.04688 -0.16097 0.02603  0.15462  420 ASN   A CB   
1984 C  CG   . ASN   A 268 ? 0.94923 1.29859 1.07096 -0.16974 0.02871  0.17870  420 ASN   A CG   
1985 O  OD1  . ASN   A 268 ? 1.01675 1.33293 1.13643 -0.17054 0.02249  0.18864  420 ASN   A OD1  
1986 N  ND2  . ASN   A 268 ? 0.92822 1.32054 1.04525 -0.17615 0.03793  0.18869  420 ASN   A ND2  
1987 N  N    . LYS   B 1   ? 1.59520 1.90738 1.89228 -0.26975 -0.07823 -0.03101 625 LYS   C N    
1988 C  CA   . LYS   B 1   ? 1.61148 1.90729 1.93129 -0.29376 -0.06902 0.01847  625 LYS   C CA   
1989 C  C    . LYS   B 1   ? 1.49946 1.88803 1.82272 -0.29111 -0.04913 0.05643  625 LYS   C C    
1990 O  O    . LYS   B 1   ? 1.50208 1.96641 1.85121 -0.31657 -0.04734 0.06237  625 LYS   C O    
1991 C  CB   . LYS   B 1   ? 1.68590 1.89607 1.98470 -0.26751 -0.06757 0.02976  625 LYS   C CB   
1992 C  CG   . LYS   B 1   ? 1.75702 1.94094 2.07101 -0.28676 -0.05903 0.08612  625 LYS   C CG   
1993 C  CD   . LYS   B 1   ? 1.87019 1.95514 2.20845 -0.31979 -0.07827 0.08366  625 LYS   C CD   
1994 C  CE   . LYS   B 1   ? 1.94435 1.98636 2.29896 -0.34481 -0.07198 0.14659  625 LYS   C CE   
1995 N  NZ   . LYS   B 1   ? 2.02338 2.02345 2.42530 -0.40644 -0.08676 0.15569  625 LYS   C NZ   
1996 N  N    . ASN   B 2   ? 1.36337 1.75298 1.66093 -0.25672 -0.03593 0.07769  626 ASN   C N    
1997 C  CA   . ASN   B 2   ? 1.21543 1.68807 1.51240 -0.24907 -0.01927 0.11185  626 ASN   C CA   
1998 C  C    . ASN   B 2   ? 1.02125 1.55019 1.29350 -0.20829 -0.01642 0.08866  626 ASN   C C    
1999 O  O    . ASN   B 2   ? 1.00078 1.60927 1.27364 -0.19905 -0.00769 0.10301  626 ASN   C O    
2000 C  CB   . ASN   B 2   ? 1.27134 1.71255 1.55918 -0.24166 -0.00867 0.15857  626 ASN   C CB   
2001 C  CG   . ASN   B 2   ? 1.31745 1.67232 1.58025 -0.20930 -0.01519 0.14582  626 ASN   C CG   
2002 O  OD1  . ASN   B 2   ? 1.33416 1.63805 1.59191 -0.20233 -0.02744 0.10564  626 ASN   C OD1  
2003 N  ND2  . ASN   B 2   ? 1.34096 1.68766 1.58675 -0.18584 -0.00721 0.17938  626 ASN   C ND2  
2004 N  N    . HIS   B 3   ? 0.86983 1.36200 1.12138 -0.18373 -0.02417 0.05319  627 HIS   C N    
2005 C  CA   . HIS   B 3   ? 0.70495 1.23841 0.93726 -0.15093 -0.02369 0.03344  627 HIS   C CA   
2006 C  C    . HIS   B 3   ? 0.61665 1.15670 0.84534 -0.15379 -0.03473 -0.00158 627 HIS   C C    
2007 O  O    . HIS   B 3   ? 0.60296 1.11004 0.81194 -0.13613 -0.03822 -0.02427 627 HIS   C O    
2008 C  CB   . HIS   B 3   ? 0.65664 1.15262 0.86839 -0.11888 -0.02068 0.02990  627 HIS   C CB   
2009 C  CG   . HIS   B 3   ? 0.63595 1.11696 0.84665 -0.11137 -0.01333 0.06265  627 HIS   C CG   
2010 N  ND1  . HIS   B 3   ? 0.68936 1.09918 0.90122 -0.11807 -0.01489 0.07496  627 HIS   C ND1  
2011 C  CD2  . HIS   B 3   ? 0.60855 1.13656 0.81416 -0.09426 -0.00660 0.08538  627 HIS   C CD2  
2012 C  CE1  . HIS   B 3   ? 0.63271 1.04482 0.83908 -0.10563 -0.00852 0.10874  627 HIS   C CE1  
2013 N  NE2  . HIS   B 3   ? 0.65902 1.14707 0.86056 -0.09116 -0.00285 0.11509  627 HIS   C NE2  
2014 N  N    . PRO   B 4   ? 0.59440 1.18579 0.84128 -0.17398 -0.04000 -0.00509 628 PRO   C N    
2015 C  CA   . PRO   B 4   ? 0.56982 1.16851 0.81072 -0.17474 -0.05345 -0.03761 628 PRO   C CA   
2016 C  C    . PRO   B 4   ? 0.50542 1.12740 0.72168 -0.14181 -0.05610 -0.05118 628 PRO   C C    
2017 O  O    . PRO   B 4   ? 0.49029 1.09505 0.68754 -0.13353 -0.06446 -0.07333 628 PRO   C O    
2018 C  CB   . PRO   B 4   ? 0.57581 1.23573 0.84943 -0.20439 -0.05871 -0.03432 628 PRO   C CB   
2019 C  CG   . PRO   B 4   ? 0.55824 1.27232 0.84522 -0.20340 -0.04467 -0.00165 628 PRO   C CG   
2020 C  CD   . PRO   B 4   ? 0.58675 1.24346 0.86028 -0.19453 -0.03365 0.02074  628 PRO   C CD   
2021 N  N    . MET   B 5   ? 0.50341 1.16300 0.71841 -0.12222 -0.05080 -0.03841 629 MET   C N    
2022 C  CA   . MET   B 5   ? 0.44523 1.11455 0.64101 -0.09346 -0.05723 -0.05087 629 MET   C CA   
2023 C  C    . MET   B 5   ? 0.47769 1.09575 0.65562 -0.07849 -0.05202 -0.05168 629 MET   C C    
2024 O  O    . MET   B 5   ? 0.43061 1.03516 0.59156 -0.06582 -0.05714 -0.06191 629 MET   C O    
2025 C  CB   . MET   B 5   ? 0.40825 1.13694 0.61159 -0.07545 -0.05864 -0.04499 629 MET   C CB   
2026 C  CG   . MET   B 5   ? 0.48521 1.28431 0.71009 -0.08757 -0.06154 -0.04405 629 MET   C CG   
2027 S  SD   . MET   B 5   ? 0.55572 1.43526 0.78516 -0.05655 -0.06294 -0.04296 629 MET   C SD   
2028 C  CE   . MET   B 5   ? 0.49763 1.37688 0.73059 -0.06337 -0.04398 -0.01284 629 MET   C CE   
2029 N  N    . LEU   B 6   ? 0.41577 1.00956 0.59846 -0.07949 -0.04191 -0.03838 630 LEU   C N    
2030 C  CA   . LEU   B 6   ? 0.41883 0.97219 0.59041 -0.06687 -0.03660 -0.04163 630 LEU   C CA   
2031 C  C    . LEU   B 6   ? 0.51562 1.03293 0.67383 -0.07327 -0.03713 -0.05761 630 LEU   C C    
2032 O  O    . LEU   B 6   ? 0.53209 1.04121 0.67538 -0.06214 -0.03545 -0.06586 630 LEU   C O    
2033 C  CB   . LEU   B 6   ? 0.42893 0.96728 0.60801 -0.06281 -0.02839 -0.02511 630 LEU   C CB   
2034 C  CG   . LEU   B 6   ? 0.52394 1.07512 0.70393 -0.04025 -0.02669 -0.02144 630 LEU   C CG   
2035 C  CD1  . LEU   B 6   ? 0.49744 1.03045 0.68030 -0.03295 -0.02041 -0.00574 630 LEU   C CD1  
2036 C  CD2  . LEU   B 6   ? 0.46026 0.99808 0.63474 -0.03182 -0.02715 -0.03606 630 LEU   C CD2  
2037 N  N    . MET   B 7   ? 0.55836 1.05679 0.72241 -0.09185 -0.04024 -0.06240 631 MET   C N    
2038 C  CA   . MET   B 7   ? 0.61821 1.08464 0.76756 -0.09398 -0.04450 -0.08522 631 MET   C CA   
2039 C  C    . MET   B 7   ? 0.57609 1.06848 0.70608 -0.08876 -0.05166 -0.09976 631 MET   C C    
2040 O  O    . MET   B 7   ? 0.65977 1.14027 0.76609 -0.07683 -0.04976 -0.11327 631 MET   C O    
2041 C  CB   . MET   B 7   ? 0.70346 1.14280 0.86862 -0.11835 -0.05261 -0.09131 631 MET   C CB   
2042 C  CG   . MET   B 7   ? 0.82342 1.20172 0.98130 -0.11227 -0.05394 -0.10681 631 MET   C CG   
2043 S  SD   . MET   B 7   ? 0.99239 1.32395 1.17570 -0.14633 -0.06928 -0.11377 631 MET   C SD   
2044 C  CE   . MET   B 7   ? 0.98123 1.31168 1.19042 -0.16088 -0.05862 -0.06541 631 MET   C CE   
2045 N  N    . ASN   B 8   ? 0.48942 1.02236 0.62705 -0.09419 -0.05985 -0.09593 632 ASN   C N    
2046 C  CA   . ASN   B 8   ? 0.53041 1.08580 0.64706 -0.08490 -0.06971 -0.10662 632 ASN   C CA   
2047 C  C    . ASN   B 8   ? 0.56073 1.11087 0.65816 -0.06458 -0.06385 -0.09570 632 ASN   C C    
2048 O  O    . ASN   B 8   ? 0.48687 1.03507 0.55683 -0.05535 -0.06592 -0.09969 632 ASN   C O    
2049 C  CB   . ASN   B 8   ? 0.53279 1.13723 0.66559 -0.09057 -0.08176 -0.10652 632 ASN   C CB   
2050 C  CG   . ASN   B 8   ? 0.53440 1.16071 0.64353 -0.07367 -0.09471 -0.11404 632 ASN   C CG   
2051 O  OD1  . ASN   B 8   ? 0.52839 1.16575 0.63215 -0.05550 -0.09800 -0.10383 632 ASN   C OD1  
2052 N  ND2  . ASN   B 8   ? 0.55670 1.18604 0.64968 -0.07700 -0.10482 -0.13306 632 ASN   C ND2  
2053 N  N    . LEU   B 9   ? 0.44337 0.99320 0.55550 -0.05861 -0.05750 -0.08078 633 LEU   C N    
2054 C  CA   . LEU   B 9   ? 0.53656 1.07708 0.64036 -0.04588 -0.05377 -0.07069 633 LEU   C CA   
2055 C  C    . LEU   B 9   ? 0.55371 1.07373 0.64798 -0.04459 -0.03934 -0.07040 633 LEU   C C    
2056 O  O    . LEU   B 9   ? 0.45851 0.97668 0.54299 -0.03979 -0.03466 -0.06067 633 LEU   C O    
2057 C  CB   . LEU   B 9   ? 0.47167 1.02160 0.59738 -0.03929 -0.05525 -0.06219 633 LEU   C CB   
2058 C  CG   . LEU   B 9   ? 0.47556 1.05396 0.60659 -0.03047 -0.07048 -0.06471 633 LEU   C CG   
2059 C  CD1  . LEU   B 9   ? 0.45252 1.04477 0.60166 -0.01888 -0.07337 -0.06274 633 LEU   C CD1  
2060 C  CD2  . LEU   B 9   ? 0.50106 1.07030 0.61253 -0.02064 -0.08274 -0.06447 633 LEU   C CD2  
2061 N  N    . LEU   B 10  ? 0.55241 1.05831 0.65100 -0.04823 -0.03268 -0.07983 634 LEU   C N    
2062 C  CA   . LEU   B 10  ? 0.61834 1.11253 0.70617 -0.04047 -0.02036 -0.08652 634 LEU   C CA   
2063 C  C    . LEU   B 10  ? 0.73611 1.23219 0.79301 -0.03726 -0.02225 -0.10342 634 LEU   C C    
2064 O  O    . LEU   B 10  ? 0.80667 1.30019 0.85073 -0.02639 -0.01263 -0.11507 634 LEU   C O    
2065 C  CB   . LEU   B 10  ? 0.54676 1.01817 0.65046 -0.03846 -0.01638 -0.09198 634 LEU   C CB   
2066 C  CG   . LEU   B 10  ? 0.51023 0.98619 0.63789 -0.03352 -0.01205 -0.07615 634 LEU   C CG   
2067 C  CD1  . LEU   B 10  ? 0.53422 0.98174 0.67151 -0.02976 -0.01135 -0.07727 634 LEU   C CD1  
2068 C  CD2  . LEU   B 10  ? 0.54272 1.03786 0.67502 -0.02375 -0.00198 -0.07079 634 LEU   C CD2  
2069 N  N    . LYS   B 11  ? 0.69312 1.20062 0.73701 -0.04229 -0.03559 -0.10767 635 LYS   C N    
2070 C  CA   . LYS   B 11  ? 0.76260 1.27998 0.77309 -0.03615 -0.04131 -0.12546 635 LYS   C CA   
2071 C  C    . LYS   B 11  ? 0.86198 1.35929 0.87058 -0.03570 -0.04461 -0.15626 635 LYS   C C    
2072 O  O    . LYS   B 11  ? 0.89471 1.36780 0.93052 -0.04906 -0.05120 -0.16285 635 LYS   C O    
2073 C  CB   . LYS   B 11  ? 0.79163 1.32633 0.77247 -0.02290 -0.02823 -0.11106 635 LYS   C CB   
2074 C  CG   . LYS   B 11  ? 0.93357 1.48897 0.87083 -0.01131 -0.03391 -0.12578 635 LYS   C CG   
2075 C  CD   . LYS   B 11  ? 0.96532 1.54037 0.87374 -0.00441 -0.02901 -0.09503 635 LYS   C CD   
2076 C  CE   . LYS   B 11  ? 1.01058 1.60891 0.87507 0.00821  -0.04326 -0.10645 635 LYS   C CE   
2077 N  NZ   . LYS   B 11  ? 1.03425 1.63103 0.90986 0.00339  -0.06524 -0.14401 635 LYS   C NZ   
2078 C  C10  A A1L76 C .   ? 0.59459 0.69570 0.50377 -0.02679 -0.03919 -0.02873 501 A1L76 A C10  
2079 C  C10  B A1L76 C .   ? 0.59206 0.69391 0.50079 -0.02692 -0.03916 -0.02891 501 A1L76 A C10  
2080 C  C13  A A1L76 C .   ? 0.46332 0.63172 0.40203 -0.02085 -0.01698 0.00007  501 A1L76 A C13  
2081 C  C13  B A1L76 C .   ? 0.46625 0.63474 0.40490 -0.02086 -0.01697 0.00005  501 A1L76 A C13  
2082 C  C15  A A1L76 C .   ? 0.50891 0.69997 0.43770 -0.00557 -0.01051 -0.02503 501 A1L76 A C15  
2083 C  C15  B A1L76 C .   ? 0.50687 0.69866 0.43567 -0.00560 -0.01033 -0.02493 501 A1L76 A C15  
2084 C  C20  A A1L76 C .   ? 0.41949 0.67870 0.39073 -0.02497 0.00689  0.01994  501 A1L76 A C20  
2085 C  C20  B A1L76 C .   ? 0.41622 0.67545 0.38753 -0.02495 0.00690  0.01993  501 A1L76 A C20  
2086 C  C21  A A1L76 C .   ? 0.41437 0.67625 0.39483 -0.01257 0.00729  0.00687  501 A1L76 A C21  
2087 C  C21  B A1L76 C .   ? 0.42021 0.68218 0.40065 -0.01248 0.00731  0.00676  501 A1L76 A C21  
2088 C  C22  A A1L76 C .   ? 0.43676 0.74666 0.38905 -0.02005 0.01901  0.00793  501 A1L76 A C22  
2089 C  C22  B A1L76 C .   ? 0.43348 0.74354 0.38580 -0.02009 0.01904  0.00799  501 A1L76 A C22  
2090 C  C26  A A1L76 C .   ? 0.65201 0.66351 0.60135 -0.02244 -0.05685 0.01809  501 A1L76 A C26  
2091 C  C26  B A1L76 C .   ? 0.66509 0.65777 0.61082 -0.02002 -0.06081 0.01097  501 A1L76 A C26  
2092 C  C28  A A1L76 C .   ? 0.65181 0.65447 0.60517 -0.01022 -0.06171 0.01721  501 A1L76 A C28  
2093 C  C28  B A1L76 C .   ? 0.64880 0.65164 0.60157 -0.00980 -0.06078 0.01380  501 A1L76 A C28  
2094 C  C01  A A1L76 C .   ? 0.64822 0.67142 0.58367 -0.01033 -0.05110 -0.02367 501 A1L76 A C01  
2095 C  C01  B A1L76 C .   ? 0.64342 0.66972 0.57898 -0.01041 -0.05034 -0.02335 501 A1L76 A C01  
2096 C  C02  A A1L76 C .   ? 0.63210 0.66566 0.57524 -0.01058 -0.04868 -0.01192 501 A1L76 A C02  
2097 C  C02  B A1L76 C .   ? 0.63015 0.66905 0.57342 -0.01064 -0.04732 -0.01200 501 A1L76 A C02  
2098 C  C03  A A1L76 C .   ? 0.61619 0.67699 0.56269 -0.01095 -0.04186 -0.00887 501 A1L76 A C03  
2099 C  C03  B A1L76 C .   ? 0.61442 0.68007 0.56085 -0.01114 -0.04062 -0.00902 501 A1L76 A C03  
2100 C  C04  A A1L76 C .   ? 0.61223 0.69092 0.55341 -0.01124 -0.03743 -0.01463 501 A1L76 A C04  
2101 C  C04  B A1L76 C .   ? 0.61098 0.69354 0.55158 -0.01141 -0.03652 -0.01496 501 A1L76 A C04  
2102 C  C05  A A1L76 C .   ? 0.61599 0.68759 0.54719 -0.01071 -0.03971 -0.02631 501 A1L76 A C05  
2103 C  C05  B A1L76 C .   ? 0.61688 0.69051 0.54755 -0.01074 -0.03927 -0.02671 501 A1L76 A C05  
2104 C  C06  A A1L76 C .   ? 0.63936 0.68220 0.56846 -0.01016 -0.04666 -0.03195 501 A1L76 A C06  
2105 C  C06  B A1L76 C .   ? 0.63608 0.68069 0.56495 -0.01021 -0.04626 -0.03205 501 A1L76 A C06  
2106 C  C09  A A1L76 C .   ? 0.56172 0.70036 0.48679 -0.01116 -0.02440 -0.02495 501 A1L76 A C09  
2107 C  C09  B A1L76 C .   ? 0.56282 0.70234 0.48746 -0.01117 -0.02424 -0.02521 501 A1L76 A C09  
2108 C  C11  A A1L76 C .   ? 0.65312 0.74360 0.56516 0.00031  -0.03566 -0.06005 501 A1L76 A C11  
2109 C  C11  B A1L76 C .   ? 0.65158 0.74312 0.56279 0.00037  -0.03549 -0.06097 501 A1L76 A C11  
2110 C  C12  A A1L76 C .   ? 0.50795 0.65199 0.44064 -0.01923 -0.02338 -0.00829 501 A1L76 A C12  
2111 C  C12  B A1L76 C .   ? 0.50569 0.65003 0.43806 -0.01923 -0.02335 -0.00847 501 A1L76 A C12  
2112 C  C14  A A1L76 C .   ? 0.47066 0.66321 0.40739 -0.01506 -0.01057 -0.00701 501 A1L76 A C14  
2113 C  C14  B A1L76 C .   ? 0.47166 0.66440 0.40848 -0.01508 -0.01051 -0.00691 501 A1L76 A C14  
2114 C  C16  A A1L76 C .   ? 0.55068 0.71254 0.47389 -0.00332 -0.01787 -0.03452 501 A1L76 A C16  
2115 C  C16  B A1L76 C .   ? 0.54751 0.71043 0.47044 -0.00334 -0.01764 -0.03463 501 A1L76 A C16  
2116 C  C18  A A1L76 C .   ? 0.43872 0.68667 0.38064 -0.01510 0.00352  -0.00241 501 A1L76 A C18  
2117 C  C18  B A1L76 C .   ? 0.43664 0.68470 0.37858 -0.01517 0.00354  -0.00229 501 A1L76 A C18  
2118 C  C19  A A1L76 C .   ? 0.42485 0.69654 0.37749 -0.02378 0.00932  0.01380  501 A1L76 A C19  
2119 C  C19  B A1L76 C .   ? 0.42528 0.69708 0.37799 -0.02384 0.00935  0.01390  501 A1L76 A C19  
2120 C  C23  A A1L76 C .   ? 0.40752 0.74253 0.36842 -0.03266 0.02472  0.02710  501 A1L76 A C23  
2121 C  C23  B A1L76 C .   ? 0.41466 0.74979 0.37560 -0.03273 0.02474  0.02720  501 A1L76 A C23  
2122 C  C25  A A1L76 C .   ? 0.63896 0.66347 0.58758 -0.02031 -0.05199 0.00831  501 A1L76 A C25  
2123 C  C25  B A1L76 C .   ? 0.66020 0.65825 0.60390 -0.01435 -0.05823 -0.00306 501 A1L76 A C25  
2124 C  C29  A A1L76 C .   ? 0.66670 0.65141 0.61683 -0.01525 -0.06845 0.02923  501 A1L76 A C29  
2125 C  C29  B A1L76 C .   ? 0.66112 0.65383 0.61268 -0.01400 -0.06612 0.02672  501 A1L76 A C29  
2126 C  C30  A A1L76 C .   ? 0.65687 0.65822 0.60827 -0.01740 -0.06807 0.03895  501 A1L76 A C30  
2127 C  C30  B A1L76 C .   ? 0.64795 0.66258 0.59990 -0.02224 -0.06095 0.03270  501 A1L76 A C30  
2128 C  C33  A A1L76 C .   ? 0.61164 0.68415 0.56736 -0.01247 -0.03944 0.00137  501 A1L76 A C33  
2129 C  C33  B A1L76 C .   ? 0.61254 0.68938 0.56846 -0.01273 -0.03826 0.00126  501 A1L76 A C33  
2130 C  C34  A A1L76 C .   ? 0.43294 0.60210 0.38202 -0.02946 -0.01671 0.01655  501 A1L76 A C34  
2131 C  C34  B A1L76 C .   ? 0.44552 0.61443 0.39462 -0.02944 -0.01677 0.01652  501 A1L76 A C34  
2132 C  C35  A A1L76 C .   ? 0.66713 0.78784 0.56833 0.00238  -0.02928 -0.07055 501 A1L76 A C35  
2133 C  C35  B A1L76 C .   ? 0.66492 0.78786 0.56613 0.00322  -0.02859 -0.07130 501 A1L76 A C35  
2134 C  C36  A A1L76 C .   ? 0.67117 0.79728 0.57216 0.01508  -0.02581 -0.08859 501 A1L76 A C36  
2135 C  C36  B A1L76 C .   ? 0.67928 0.80539 0.57990 0.01583  -0.02572 -0.09020 501 A1L76 A C36  
2136 C  C37  A A1L76 C .   ? 0.56921 0.66868 0.48797 -0.03459 -0.03995 -0.01123 501 A1L76 A C37  
2137 C  C37  B A1L76 C .   ? 0.56659 0.66614 0.48527 -0.03445 -0.03990 -0.01143 501 A1L76 A C37  
2138 C  C38  A A1L76 C .   ? 0.54375 0.66261 0.46566 -0.03864 -0.03664 0.00050  501 A1L76 A C38  
2139 C  C38  B A1L76 C .   ? 0.55277 0.67146 0.47467 -0.03867 -0.03669 0.00047  501 A1L76 A C38  
2140 O  O07  A A1L76 C .   ? 0.65414 0.67068 0.60069 -0.01146 -0.05364 -0.00346 501 A1L76 A O07  
2141 O  O07  B A1L76 C .   ? 0.64416 0.66957 0.59167 -0.01154 -0.05137 -0.00310 501 A1L76 A O07  
2142 O  O17  A A1L76 C .   ? 0.45620 0.67418 0.40027 -0.01949 -0.00414 0.00391  501 A1L76 A O17  
2143 O  O17  B A1L76 C .   ? 0.45299 0.67095 0.39741 -0.01946 -0.00411 0.00401  501 A1L76 A O17  
2144 O  O24  A A1L76 C .   ? 0.42412 0.69565 0.37159 -0.03518 0.00768  0.02941  501 A1L76 A O24  
2145 O  O24  B A1L76 C .   ? 0.42906 0.70071 0.37652 -0.03526 0.00770  0.02953  501 A1L76 A O24  
2146 O  O27  A A1L76 C .   ? 0.63171 0.65966 0.58430 -0.02710 -0.05347 0.02534  501 A1L76 A O27  
2147 O  O27  B A1L76 C .   ? 0.64725 0.65596 0.59285 -0.03004 -0.05618 0.01710  501 A1L76 A O27  
2148 O  O31  A A1L76 C .   ? 0.62750 0.62159 0.57912 -0.01296 -0.07477 0.04702  501 A1L76 A O31  
2149 O  O31  B A1L76 C .   ? 0.63675 0.65570 0.58828 -0.02339 -0.06355 0.04086  501 A1L76 A O31  
2150 O  O32  A A1L76 C .   ? 0.64203 0.66341 0.59422 -0.02370 -0.06198 0.03887  501 A1L76 A O32  
2151 O  O32  B A1L76 C .   ? 0.63052 0.65821 0.58337 -0.02745 -0.05477 0.02905  501 A1L76 A O32  
2152 SI SI08 A A1L76 C .   ? 0.61162 0.71230 0.53076 -0.01205 -0.03433 -0.03461 501 A1L76 A SI08 
2153 SI SI08 B A1L76 C .   ? 0.61198 0.71393 0.53032 -0.01201 -0.03413 -0.03533 501 A1L76 A SI08 
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