data_9M15
# 
_entry.id   9M15 
# 
_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   9M15         pdb_00009m15 10.2210/pdb9m15/pdb 
WWPDB D_1300056755 ?            ?                   
# 
_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                        9M15 
_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 syn 
'(4~{S})-5-[4-[[4-(2-ethyl-2-oxidanyl-butoxy)-2-methyl-phenyl]-dimethyl-silyl]-3-methyl-phenoxy]-4-oxidanyl-pentanoic acid' 
488.688   1  ? ? ? ? 
4 water       nat water 18.015    76 ? ? ? ? 
# 
_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)-2-methyl-phenyl]-dimethyl-silyl]-3-methyl-phenoxy]-4-oxidanyl-pentanoic acid' 
A1L73 
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 
A1L73 non-polymer         . 
'(4~{S})-5-[4-[[4-(2-ethyl-2-oxidanyl-butoxy)-2-methyl-phenyl]-dimethyl-silyl]-3-methyl-phenoxy]-4-oxidanyl-pentanoic acid' ? 
'C27 H40 O6 Si'  488.688 
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        A1L73 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1L73 
_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 A1L73 1  501 501 A1L73 LIG A . 
D 4 HOH   1  601 98  HOH   HOH A . 
D 4 HOH   2  602 56  HOH   HOH A . 
D 4 HOH   3  603 103 HOH   HOH A . 
D 4 HOH   4  604 82  HOH   HOH A . 
D 4 HOH   5  605 11  HOH   HOH A . 
D 4 HOH   6  606 10  HOH   HOH A . 
D 4 HOH   7  607 28  HOH   HOH A . 
D 4 HOH   8  608 17  HOH   HOH A . 
D 4 HOH   9  609 85  HOH   HOH A . 
D 4 HOH   10 610 16  HOH   HOH A . 
D 4 HOH   11 611 7   HOH   HOH A . 
D 4 HOH   12 612 21  HOH   HOH A . 
D 4 HOH   13 613 4   HOH   HOH A . 
D 4 HOH   14 614 19  HOH   HOH A . 
D 4 HOH   15 615 65  HOH   HOH A . 
D 4 HOH   16 616 13  HOH   HOH A . 
D 4 HOH   17 617 72  HOH   HOH A . 
D 4 HOH   18 618 39  HOH   HOH A . 
D 4 HOH   19 619 3   HOH   HOH A . 
D 4 HOH   20 620 80  HOH   HOH A . 
D 4 HOH   21 621 81  HOH   HOH A . 
D 4 HOH   22 622 38  HOH   HOH A . 
D 4 HOH   23 623 36  HOH   HOH A . 
D 4 HOH   24 624 12  HOH   HOH A . 
D 4 HOH   25 625 25  HOH   HOH A . 
D 4 HOH   26 626 1   HOH   HOH A . 
D 4 HOH   27 627 2   HOH   HOH A . 
D 4 HOH   28 628 104 HOH   HOH A . 
D 4 HOH   29 629 62  HOH   HOH A . 
D 4 HOH   30 630 35  HOH   HOH A . 
D 4 HOH   31 631 22  HOH   HOH A . 
D 4 HOH   32 632 24  HOH   HOH A . 
D 4 HOH   33 633 69  HOH   HOH A . 
D 4 HOH   34 634 14  HOH   HOH A . 
D 4 HOH   35 635 45  HOH   HOH A . 
D 4 HOH   36 636 32  HOH   HOH A . 
D 4 HOH   37 637 88  HOH   HOH A . 
D 4 HOH   38 638 26  HOH   HOH A . 
D 4 HOH   39 639 6   HOH   HOH A . 
D 4 HOH   40 640 49  HOH   HOH A . 
D 4 HOH   41 641 15  HOH   HOH A . 
D 4 HOH   42 642 99  HOH   HOH A . 
D 4 HOH   43 643 93  HOH   HOH A . 
D 4 HOH   44 644 89  HOH   HOH A . 
D 4 HOH   45 645 55  HOH   HOH A . 
D 4 HOH   46 646 33  HOH   HOH A . 
D 4 HOH   47 647 46  HOH   HOH A . 
D 4 HOH   48 648 9   HOH   HOH A . 
D 4 HOH   49 649 73  HOH   HOH A . 
D 4 HOH   50 650 37  HOH   HOH A . 
D 4 HOH   51 651 79  HOH   HOH A . 
D 4 HOH   52 652 70  HOH   HOH A . 
D 4 HOH   53 653 76  HOH   HOH A . 
D 4 HOH   54 654 27  HOH   HOH A . 
D 4 HOH   55 655 67  HOH   HOH A . 
D 4 HOH   56 656 68  HOH   HOH A . 
D 4 HOH   57 657 94  HOH   HOH A . 
D 4 HOH   58 658 101 HOH   HOH A . 
D 4 HOH   59 659 41  HOH   HOH A . 
D 4 HOH   60 660 105 HOH   HOH A . 
D 4 HOH   61 661 34  HOH   HOH A . 
D 4 HOH   62 662 18  HOH   HOH A . 
D 4 HOH   63 663 29  HOH   HOH A . 
D 4 HOH   64 664 58  HOH   HOH A . 
D 4 HOH   65 665 97  HOH   HOH A . 
D 4 HOH   66 666 92  HOH   HOH A . 
D 4 HOH   67 667 44  HOH   HOH A . 
D 4 HOH   68 668 86  HOH   HOH A . 
D 4 HOH   69 669 90  HOH   HOH A . 
D 4 HOH   70 670 95  HOH   HOH A . 
D 4 HOH   71 671 100 HOH   HOH A . 
D 4 HOH   72 672 42  HOH   HOH A . 
D 4 HOH   73 673 75  HOH   HOH A . 
E 4 HOH   1  701 31  HOH   HOH C . 
E 4 HOH   2  702 47  HOH   HOH C . 
E 4 HOH   3  703 102 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                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   95.83 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9M15 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     152.660 
_cell.length_a_esd                 ? 
_cell.length_b                     44.670 
_cell.length_b_esd                 ? 
_cell.length_c                     42.060 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_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                         9M15 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                5 
_symmetry.space_group_name_Hall            ? 
_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                   9M15 
_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             2.22 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          44.54 
_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, Magnesium acetate tetrahydrate, pH 7.9' 
_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 PILATUS 6M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2023-05-16 
_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 BL45XU' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        1.0 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   BL45XU 
_diffrn_source.pdbx_synchrotron_site       SPring-8 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9M15 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.18 
_reflns.d_resolution_low                               42.86 
_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                                     14961 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           100 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                14.2 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          10.52 
_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                                   0.993 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.43 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    2.18 
_reflns_shell.d_res_low                                     2.31 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           1.85 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             2353 
_reflns_shell.percent_possible_obs                          ? 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               ? 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               ? 
_reflns_shell.pdbx_Rpim_I_all                               ? 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.811 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          100 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  2.24 
_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                               ? 
_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                                 9M15 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            2.180 
_refine.ls_d_res_low                             42.855 
_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                     14952 
_refine.ls_number_reflns_R_free                  747 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.93 
_refine.ls_percent_reflns_R_free                 5.00 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1944 
_refine.ls_R_factor_R_free                       0.2293 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1925 
_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                          1.35 
_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       ML 
_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             1.11 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.90 
_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                 24.93 
_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                            0.19 
_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.pdbx_number_atoms_protein        2015 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         34 
_refine_hist.number_atoms_solvent             76 
_refine_hist.number_atoms_total               2125 
_refine_hist.d_res_high                       2.180 
_refine_hist.d_res_low                        42.855 
# 
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' ? 0.004 ? 2180 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.804 ? 2958 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 9.096 ? 2289 ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.039 ? 328  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.004 ? 379  ? f_plane_restr      ? ? 
# 
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' 2.180  2.3482 . . 149 2831 100.00 . . . . 0.2282 . . . . . . . . . . . . . . . 0.2606 
'X-RAY DIFFRACTION' 2.3482 2.5844 . . 147 2790 100.00 . . . . 0.2176 . . . . . . . . . . . . . . . 0.2969 
'X-RAY DIFFRACTION' 2.5844 2.9583 . . 149 2829 100.00 . . . . 0.1966 . . . . . . . . . . . . . . . 0.2473 
'X-RAY DIFFRACTION' 2.9583 3.7269 . . 148 2833 100.00 . . . . 0.1796 . . . . . . . . . . . . . . . 0.2147 
'X-RAY DIFFRACTION' 3.7269 42.855 . . 154 2922 100.00 . . . . 0.1785 . . . . . . . . . . . . . . . 0.1973 
# 
_struct.entry_id                     9M15 
_struct.title                        'Vitamin D receptor complex with a dimethyldi(o-tolyl)silane 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        9M15 
_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 9M15 A 11 ? 271 ? P13053 116 ? 423 ? 116 423 
2 2 9M15 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 9M15 GLY A 1  ? UNP P13053 ?   ?   'expression tag' 106 1  
1 9M15 SER A 2  ? UNP P13053 ?   ?   'expression tag' 107 2  
1 9M15 HIS A 3  ? UNP P13053 ?   ?   'expression tag' 108 3  
1 9M15 MET A 4  ? UNP P13053 ?   ?   'expression tag' 109 4  
1 9M15 GLY A 5  ? UNP P13053 ?   ?   'expression tag' 110 5  
1 9M15 SER A 6  ? UNP P13053 ?   ?   'expression tag' 111 6  
1 9M15 PRO A 7  ? UNP P13053 ?   ?   'expression tag' 112 7  
1 9M15 ASN A 8  ? UNP P13053 ?   ?   'expression tag' 113 8  
1 9M15 SER A 9  ? UNP P13053 ?   ?   'expression tag' 114 9  
1 9M15 PRO A 10 ? UNP P13053 ?   ?   'expression tag' 115 10 
1 9M15 ?   A ?  ? UNP P13053 TYR 166 deletion         ?   11 
1 9M15 ?   A ?  ? UNP P13053 SER 167 deletion         ?   12 
1 9M15 ?   A ?  ? UNP P13053 PRO 168 deletion         ?   13 
1 9M15 ?   A ?  ? UNP P13053 ARG 169 deletion         ?   14 
1 9M15 ?   A ?  ? UNP P13053 PRO 170 deletion         ?   15 
1 9M15 ?   A ?  ? UNP P13053 THR 171 deletion         ?   16 
1 9M15 ?   A ?  ? UNP P13053 LEU 172 deletion         ?   17 
1 9M15 ?   A ?  ? UNP P13053 SER 173 deletion         ?   18 
1 9M15 ?   A ?  ? UNP P13053 PHE 174 deletion         ?   19 
1 9M15 ?   A ?  ? UNP P13053 SER 175 deletion         ?   20 
1 9M15 ?   A ?  ? UNP P13053 GLY 176 deletion         ?   21 
1 9M15 ?   A ?  ? UNP P13053 ASN 177 deletion         ?   22 
1 9M15 ?   A ?  ? UNP P13053 SER 178 deletion         ?   23 
1 9M15 ?   A ?  ? UNP P13053 SER 179 deletion         ?   24 
1 9M15 ?   A ?  ? UNP P13053 SER 180 deletion         ?   25 
1 9M15 ?   A ?  ? UNP P13053 SER 181 deletion         ?   26 
1 9M15 ?   A ?  ? UNP P13053 SER 182 deletion         ?   27 
1 9M15 ?   A ?  ? UNP P13053 SER 183 deletion         ?   28 
1 9M15 ?   A ?  ? UNP P13053 ASP 184 deletion         ?   29 
1 9M15 ?   A ?  ? UNP P13053 LEU 185 deletion         ?   30 
1 9M15 ?   A ?  ? UNP P13053 TYR 186 deletion         ?   31 
1 9M15 ?   A ?  ? UNP P13053 THR 187 deletion         ?   32 
1 9M15 ?   A ?  ? UNP P13053 THR 188 deletion         ?   33 
1 9M15 ?   A ?  ? UNP P13053 SER 189 deletion         ?   34 
1 9M15 ?   A ?  ? UNP P13053 LEU 190 deletion         ?   35 
1 9M15 ?   A ?  ? UNP P13053 ASP 191 deletion         ?   36 
1 9M15 ?   A ?  ? UNP P13053 MET 192 deletion         ?   37 
1 9M15 ?   A ?  ? UNP P13053 MET 193 deletion         ?   38 
1 9M15 ?   A ?  ? UNP P13053 GLU 194 deletion         ?   39 
1 9M15 ?   A ?  ? UNP P13053 PRO 195 deletion         ?   40 
1 9M15 ?   A ?  ? UNP P13053 SER 196 deletion         ?   41 
1 9M15 ?   A ?  ? UNP P13053 GLY 197 deletion         ?   42 
1 9M15 ?   A ?  ? UNP P13053 PHE 198 deletion         ?   43 
1 9M15 ?   A ?  ? UNP P13053 SER 199 deletion         ?   44 
1 9M15 ?   A ?  ? UNP P13053 ASN 200 deletion         ?   45 
1 9M15 ?   A ?  ? UNP P13053 LEU 201 deletion         ?   46 
1 9M15 ?   A ?  ? UNP P13053 ASP 202 deletion         ?   47 
1 9M15 ?   A ?  ? UNP P13053 LEU 203 deletion         ?   48 
1 9M15 ?   A ?  ? UNP P13053 ASN 204 deletion         ?   49 
1 9M15 ?   A ?  ? UNP P13053 GLY 205 deletion         ?   50 
1 9M15 ?   A ?  ? UNP P13053 GLU 206 deletion         ?   51 
1 9M15 ?   A ?  ? UNP P13053 ASP 207 deletion         ?   52 
1 9M15 ?   A ?  ? UNP P13053 SER 208 deletion         ?   53 
1 9M15 ?   A ?  ? UNP P13053 ASP 209 deletion         ?   54 
1 9M15 ?   A ?  ? UNP P13053 ASP 210 deletion         ?   55 
1 9M15 ?   A ?  ? UNP P13053 PRO 211 deletion         ?   56 
1 9M15 ?   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)' 1200  ? 
1 MORE         -8    ? 
1 'SSA (A^2)'  11860 ? 
# 
_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  ? LYS A 36  ? SER A 125 LYS A 141 1 ? 17 
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  ? SER A 119 ? THR A 251 SER A 271 1 ? 21 
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 PRO A 218 ? PHE A 250 ? PRO A 370 PHE A 402 1 ? 33 
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   ? LYS B 11  ? HIS C 627 LYS C 635 1 ? 9  
# 
_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       0.65 
# 
_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                   9M15 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 LEU A 220 ? ? -113.42 56.50 
2 1 TYR A 289 ? ? -100.04 47.97 
# 
_pdbx_refine_tls.id               1 
_pdbx_refine_tls.pdbx_refine_id   'X-RAY DIFFRACTION' 
_pdbx_refine_tls.details          ? 
_pdbx_refine_tls.method           refined 
_pdbx_refine_tls.origin_x         18.4208 
_pdbx_refine_tls.origin_y         -0.4069 
_pdbx_refine_tls.origin_z         18.5625 
_pdbx_refine_tls.T[1][1]          0.1171 
_pdbx_refine_tls.T[1][1]_esd      ? 
_pdbx_refine_tls.T[1][2]          -0.0589 
_pdbx_refine_tls.T[1][2]_esd      ? 
_pdbx_refine_tls.T[1][3]          -0.0112 
_pdbx_refine_tls.T[1][3]_esd      ? 
_pdbx_refine_tls.T[2][2]          0.1084 
_pdbx_refine_tls.T[2][2]_esd      ? 
_pdbx_refine_tls.T[2][3]          -0.0193 
_pdbx_refine_tls.T[2][3]_esd      ? 
_pdbx_refine_tls.T[3][3]          0.1112 
_pdbx_refine_tls.T[3][3]_esd      ? 
_pdbx_refine_tls.L[1][1]          2.2368 
_pdbx_refine_tls.L[1][1]_esd      ? 
_pdbx_refine_tls.L[1][2]          0.0244 
_pdbx_refine_tls.L[1][2]_esd      ? 
_pdbx_refine_tls.L[1][3]          -0.5122 
_pdbx_refine_tls.L[1][3]_esd      ? 
_pdbx_refine_tls.L[2][2]          0.3731 
_pdbx_refine_tls.L[2][2]_esd      ? 
_pdbx_refine_tls.L[2][3]          0.0528 
_pdbx_refine_tls.L[2][3]_esd      ? 
_pdbx_refine_tls.L[3][3]          1.8035 
_pdbx_refine_tls.L[3][3]_esd      ? 
_pdbx_refine_tls.S[1][1]          0.1664 
_pdbx_refine_tls.S[1][1]_esd      ? 
_pdbx_refine_tls.S[1][2]          -0.0611 
_pdbx_refine_tls.S[1][2]_esd      ? 
_pdbx_refine_tls.S[1][3]          -0.0070 
_pdbx_refine_tls.S[1][3]_esd      ? 
_pdbx_refine_tls.S[2][1]          0.0202 
_pdbx_refine_tls.S[2][1]_esd      ? 
_pdbx_refine_tls.S[2][2]          -0.0207 
_pdbx_refine_tls.S[2][2]_esd      ? 
_pdbx_refine_tls.S[2][3]          0.0047 
_pdbx_refine_tls.S[2][3]_esd      ? 
_pdbx_refine_tls.S[3][1]          -0.1582 
_pdbx_refine_tls.S[3][1]_esd      ? 
_pdbx_refine_tls.S[3][2]          0.2548 
_pdbx_refine_tls.S[3][2]_esd      ? 
_pdbx_refine_tls.S[3][3]          -0.0605 
_pdbx_refine_tls.S[3][3]_esd      ? 
# 
_pdbx_refine_tls_group.id                  1 
_pdbx_refine_tls_group.pdbx_refine_id      'X-RAY DIFFRACTION' 
_pdbx_refine_tls_group.refine_tls_id       1 
_pdbx_refine_tls_group.beg_label_asym_id   ? 
_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   all 
# 
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 
A1L73 C10  C  Y N 1   
A1L73 C13  C  Y N 2   
A1L73 C15  C  N N 3   
A1L73 C20  C  N N 4   
A1L73 C21  C  N N 5   
A1L73 C22  C  N N 6   
A1L73 C24  C  N N 7   
A1L73 C26  C  N N 8   
A1L73 C28  C  N N 9   
A1L73 C01  C  Y N 10  
A1L73 C02  C  Y N 11  
A1L73 C03  C  Y N 12  
A1L73 C04  C  Y N 13  
A1L73 C05  C  Y N 14  
A1L73 C06  C  Y N 15  
A1L73 C08  C  Y N 16  
A1L73 C09  C  Y N 17  
A1L73 C11  C  Y N 18  
A1L73 C12  C  Y N 19  
A1L73 C14  C  N N 20  
A1L73 C18  C  N N 21  
A1L73 C19  C  N S 22  
A1L73 C23  C  N N 23  
A1L73 C25  C  N N 24  
A1L73 C27  C  N N 25  
A1L73 C33  C  N N 26  
A1L73 C34  C  N N 27  
A1L73 O16  O  N N 28  
A1L73 O17  O  N N 29  
A1L73 O29  O  N N 30  
A1L73 O30  O  N N 31  
A1L73 O31  O  N N 32  
A1L73 O32  O  N N 33  
A1L73 SI07 SI N N 34  
A1L73 H1   H  N N 35  
A1L73 H2   H  N N 36  
A1L73 H3   H  N N 37  
A1L73 H4   H  N N 38  
A1L73 H5   H  N N 39  
A1L73 H6   H  N N 40  
A1L73 H7   H  N N 41  
A1L73 H8   H  N N 42  
A1L73 H9   H  N N 43  
A1L73 H10  H  N N 44  
A1L73 H11  H  N N 45  
A1L73 H12  H  N N 46  
A1L73 H13  H  N N 47  
A1L73 H14  H  N N 48  
A1L73 H15  H  N N 49  
A1L73 H16  H  N N 50  
A1L73 H17  H  N N 51  
A1L73 H18  H  N N 52  
A1L73 H19  H  N N 53  
A1L73 H20  H  N N 54  
A1L73 H21  H  N N 55  
A1L73 H22  H  N N 56  
A1L73 H23  H  N N 57  
A1L73 H24  H  N N 58  
A1L73 H25  H  N N 59  
A1L73 H26  H  N N 60  
A1L73 H27  H  N N 61  
A1L73 H28  H  N N 62  
A1L73 H29  H  N N 63  
A1L73 H30  H  N N 64  
A1L73 H31  H  N N 65  
A1L73 H32  H  N N 66  
A1L73 H33  H  N N 67  
A1L73 H34  H  N N 68  
A1L73 H35  H  N N 69  
A1L73 H36  H  N N 70  
A1L73 H37  H  N N 71  
A1L73 H38  H  N N 72  
A1L73 H39  H  N N 73  
A1L73 H40  H  N N 74  
ALA   N    N  N N 75  
ALA   CA   C  N S 76  
ALA   C    C  N N 77  
ALA   O    O  N N 78  
ALA   CB   C  N N 79  
ALA   OXT  O  N N 80  
ALA   H    H  N N 81  
ALA   H2   H  N N 82  
ALA   HA   H  N N 83  
ALA   HB1  H  N N 84  
ALA   HB2  H  N N 85  
ALA   HB3  H  N N 86  
ALA   HXT  H  N N 87  
ARG   N    N  N N 88  
ARG   CA   C  N S 89  
ARG   C    C  N N 90  
ARG   O    O  N N 91  
ARG   CB   C  N N 92  
ARG   CG   C  N N 93  
ARG   CD   C  N N 94  
ARG   NE   N  N N 95  
ARG   CZ   C  N N 96  
ARG   NH1  N  N N 97  
ARG   NH2  N  N N 98  
ARG   OXT  O  N N 99  
ARG   H    H  N N 100 
ARG   H2   H  N N 101 
ARG   HA   H  N N 102 
ARG   HB2  H  N N 103 
ARG   HB3  H  N N 104 
ARG   HG2  H  N N 105 
ARG   HG3  H  N N 106 
ARG   HD2  H  N N 107 
ARG   HD3  H  N N 108 
ARG   HE   H  N N 109 
ARG   HH11 H  N N 110 
ARG   HH12 H  N N 111 
ARG   HH21 H  N N 112 
ARG   HH22 H  N N 113 
ARG   HXT  H  N N 114 
ASN   N    N  N N 115 
ASN   CA   C  N S 116 
ASN   C    C  N N 117 
ASN   O    O  N N 118 
ASN   CB   C  N N 119 
ASN   CG   C  N N 120 
ASN   OD1  O  N N 121 
ASN   ND2  N  N N 122 
ASN   OXT  O  N N 123 
ASN   H    H  N N 124 
ASN   H2   H  N N 125 
ASN   HA   H  N N 126 
ASN   HB2  H  N N 127 
ASN   HB3  H  N N 128 
ASN   HD21 H  N N 129 
ASN   HD22 H  N N 130 
ASN   HXT  H  N N 131 
ASP   N    N  N N 132 
ASP   CA   C  N S 133 
ASP   C    C  N N 134 
ASP   O    O  N N 135 
ASP   CB   C  N N 136 
ASP   CG   C  N N 137 
ASP   OD1  O  N N 138 
ASP   OD2  O  N N 139 
ASP   OXT  O  N N 140 
ASP   H    H  N N 141 
ASP   H2   H  N N 142 
ASP   HA   H  N N 143 
ASP   HB2  H  N N 144 
ASP   HB3  H  N N 145 
ASP   HD2  H  N N 146 
ASP   HXT  H  N N 147 
CYS   N    N  N N 148 
CYS   CA   C  N R 149 
CYS   C    C  N N 150 
CYS   O    O  N N 151 
CYS   CB   C  N N 152 
CYS   SG   S  N N 153 
CYS   OXT  O  N N 154 
CYS   H    H  N N 155 
CYS   H2   H  N N 156 
CYS   HA   H  N N 157 
CYS   HB2  H  N N 158 
CYS   HB3  H  N N 159 
CYS   HG   H  N N 160 
CYS   HXT  H  N N 161 
GLN   N    N  N N 162 
GLN   CA   C  N S 163 
GLN   C    C  N N 164 
GLN   O    O  N N 165 
GLN   CB   C  N N 166 
GLN   CG   C  N N 167 
GLN   CD   C  N N 168 
GLN   OE1  O  N N 169 
GLN   NE2  N  N N 170 
GLN   OXT  O  N N 171 
GLN   H    H  N N 172 
GLN   H2   H  N N 173 
GLN   HA   H  N N 174 
GLN   HB2  H  N N 175 
GLN   HB3  H  N N 176 
GLN   HG2  H  N N 177 
GLN   HG3  H  N N 178 
GLN   HE21 H  N N 179 
GLN   HE22 H  N N 180 
GLN   HXT  H  N N 181 
GLU   N    N  N N 182 
GLU   CA   C  N S 183 
GLU   C    C  N N 184 
GLU   O    O  N N 185 
GLU   CB   C  N N 186 
GLU   CG   C  N N 187 
GLU   CD   C  N N 188 
GLU   OE1  O  N N 189 
GLU   OE2  O  N N 190 
GLU   OXT  O  N N 191 
GLU   H    H  N N 192 
GLU   H2   H  N N 193 
GLU   HA   H  N N 194 
GLU   HB2  H  N N 195 
GLU   HB3  H  N N 196 
GLU   HG2  H  N N 197 
GLU   HG3  H  N N 198 
GLU   HE2  H  N N 199 
GLU   HXT  H  N N 200 
GLY   N    N  N N 201 
GLY   CA   C  N N 202 
GLY   C    C  N N 203 
GLY   O    O  N N 204 
GLY   OXT  O  N N 205 
GLY   H    H  N N 206 
GLY   H2   H  N N 207 
GLY   HA2  H  N N 208 
GLY   HA3  H  N N 209 
GLY   HXT  H  N N 210 
HIS   N    N  N N 211 
HIS   CA   C  N S 212 
HIS   C    C  N N 213 
HIS   O    O  N N 214 
HIS   CB   C  N N 215 
HIS   CG   C  Y N 216 
HIS   ND1  N  Y N 217 
HIS   CD2  C  Y N 218 
HIS   CE1  C  Y N 219 
HIS   NE2  N  Y N 220 
HIS   OXT  O  N N 221 
HIS   H    H  N N 222 
HIS   H2   H  N N 223 
HIS   HA   H  N N 224 
HIS   HB2  H  N N 225 
HIS   HB3  H  N N 226 
HIS   HD1  H  N N 227 
HIS   HD2  H  N N 228 
HIS   HE1  H  N N 229 
HIS   HE2  H  N N 230 
HIS   HXT  H  N N 231 
HOH   O    O  N N 232 
HOH   H1   H  N N 233 
HOH   H2   H  N N 234 
ILE   N    N  N N 235 
ILE   CA   C  N S 236 
ILE   C    C  N N 237 
ILE   O    O  N N 238 
ILE   CB   C  N S 239 
ILE   CG1  C  N N 240 
ILE   CG2  C  N N 241 
ILE   CD1  C  N N 242 
ILE   OXT  O  N N 243 
ILE   H    H  N N 244 
ILE   H2   H  N N 245 
ILE   HA   H  N N 246 
ILE   HB   H  N N 247 
ILE   HG12 H  N N 248 
ILE   HG13 H  N N 249 
ILE   HG21 H  N N 250 
ILE   HG22 H  N N 251 
ILE   HG23 H  N N 252 
ILE   HD11 H  N N 253 
ILE   HD12 H  N N 254 
ILE   HD13 H  N N 255 
ILE   HXT  H  N N 256 
LEU   N    N  N N 257 
LEU   CA   C  N S 258 
LEU   C    C  N N 259 
LEU   O    O  N N 260 
LEU   CB   C  N N 261 
LEU   CG   C  N N 262 
LEU   CD1  C  N N 263 
LEU   CD2  C  N N 264 
LEU   OXT  O  N N 265 
LEU   H    H  N N 266 
LEU   H2   H  N N 267 
LEU   HA   H  N N 268 
LEU   HB2  H  N N 269 
LEU   HB3  H  N N 270 
LEU   HG   H  N N 271 
LEU   HD11 H  N N 272 
LEU   HD12 H  N N 273 
LEU   HD13 H  N N 274 
LEU   HD21 H  N N 275 
LEU   HD22 H  N N 276 
LEU   HD23 H  N N 277 
LEU   HXT  H  N N 278 
LYS   N    N  N N 279 
LYS   CA   C  N S 280 
LYS   C    C  N N 281 
LYS   O    O  N N 282 
LYS   CB   C  N N 283 
LYS   CG   C  N N 284 
LYS   CD   C  N N 285 
LYS   CE   C  N N 286 
LYS   NZ   N  N N 287 
LYS   OXT  O  N N 288 
LYS   H    H  N N 289 
LYS   H2   H  N N 290 
LYS   HA   H  N N 291 
LYS   HB2  H  N N 292 
LYS   HB3  H  N N 293 
LYS   HG2  H  N N 294 
LYS   HG3  H  N N 295 
LYS   HD2  H  N N 296 
LYS   HD3  H  N N 297 
LYS   HE2  H  N N 298 
LYS   HE3  H  N N 299 
LYS   HZ1  H  N N 300 
LYS   HZ2  H  N N 301 
LYS   HZ3  H  N N 302 
LYS   HXT  H  N N 303 
MET   N    N  N N 304 
MET   CA   C  N S 305 
MET   C    C  N N 306 
MET   O    O  N N 307 
MET   CB   C  N N 308 
MET   CG   C  N N 309 
MET   SD   S  N N 310 
MET   CE   C  N N 311 
MET   OXT  O  N N 312 
MET   H    H  N N 313 
MET   H2   H  N N 314 
MET   HA   H  N N 315 
MET   HB2  H  N N 316 
MET   HB3  H  N N 317 
MET   HG2  H  N N 318 
MET   HG3  H  N N 319 
MET   HE1  H  N N 320 
MET   HE2  H  N N 321 
MET   HE3  H  N N 322 
MET   HXT  H  N N 323 
PHE   N    N  N N 324 
PHE   CA   C  N S 325 
PHE   C    C  N N 326 
PHE   O    O  N N 327 
PHE   CB   C  N N 328 
PHE   CG   C  Y N 329 
PHE   CD1  C  Y N 330 
PHE   CD2  C  Y N 331 
PHE   CE1  C  Y N 332 
PHE   CE2  C  Y N 333 
PHE   CZ   C  Y N 334 
PHE   OXT  O  N N 335 
PHE   H    H  N N 336 
PHE   H2   H  N N 337 
PHE   HA   H  N N 338 
PHE   HB2  H  N N 339 
PHE   HB3  H  N N 340 
PHE   HD1  H  N N 341 
PHE   HD2  H  N N 342 
PHE   HE1  H  N N 343 
PHE   HE2  H  N N 344 
PHE   HZ   H  N N 345 
PHE   HXT  H  N N 346 
PRO   N    N  N N 347 
PRO   CA   C  N S 348 
PRO   C    C  N N 349 
PRO   O    O  N N 350 
PRO   CB   C  N N 351 
PRO   CG   C  N N 352 
PRO   CD   C  N N 353 
PRO   OXT  O  N N 354 
PRO   H    H  N N 355 
PRO   HA   H  N N 356 
PRO   HB2  H  N N 357 
PRO   HB3  H  N N 358 
PRO   HG2  H  N N 359 
PRO   HG3  H  N N 360 
PRO   HD2  H  N N 361 
PRO   HD3  H  N N 362 
PRO   HXT  H  N N 363 
SER   N    N  N N 364 
SER   CA   C  N S 365 
SER   C    C  N N 366 
SER   O    O  N N 367 
SER   CB   C  N N 368 
SER   OG   O  N N 369 
SER   OXT  O  N N 370 
SER   H    H  N N 371 
SER   H2   H  N N 372 
SER   HA   H  N N 373 
SER   HB2  H  N N 374 
SER   HB3  H  N N 375 
SER   HG   H  N N 376 
SER   HXT  H  N N 377 
THR   N    N  N N 378 
THR   CA   C  N S 379 
THR   C    C  N N 380 
THR   O    O  N N 381 
THR   CB   C  N R 382 
THR   OG1  O  N N 383 
THR   CG2  C  N N 384 
THR   OXT  O  N N 385 
THR   H    H  N N 386 
THR   H2   H  N N 387 
THR   HA   H  N N 388 
THR   HB   H  N N 389 
THR   HG1  H  N N 390 
THR   HG21 H  N N 391 
THR   HG22 H  N N 392 
THR   HG23 H  N N 393 
THR   HXT  H  N N 394 
TRP   N    N  N N 395 
TRP   CA   C  N S 396 
TRP   C    C  N N 397 
TRP   O    O  N N 398 
TRP   CB   C  N N 399 
TRP   CG   C  Y N 400 
TRP   CD1  C  Y N 401 
TRP   CD2  C  Y N 402 
TRP   NE1  N  Y N 403 
TRP   CE2  C  Y N 404 
TRP   CE3  C  Y N 405 
TRP   CZ2  C  Y N 406 
TRP   CZ3  C  Y N 407 
TRP   CH2  C  Y N 408 
TRP   OXT  O  N N 409 
TRP   H    H  N N 410 
TRP   H2   H  N N 411 
TRP   HA   H  N N 412 
TRP   HB2  H  N N 413 
TRP   HB3  H  N N 414 
TRP   HD1  H  N N 415 
TRP   HE1  H  N N 416 
TRP   HE3  H  N N 417 
TRP   HZ2  H  N N 418 
TRP   HZ3  H  N N 419 
TRP   HH2  H  N N 420 
TRP   HXT  H  N N 421 
TYR   N    N  N N 422 
TYR   CA   C  N S 423 
TYR   C    C  N N 424 
TYR   O    O  N N 425 
TYR   CB   C  N N 426 
TYR   CG   C  Y N 427 
TYR   CD1  C  Y N 428 
TYR   CD2  C  Y N 429 
TYR   CE1  C  Y N 430 
TYR   CE2  C  Y N 431 
TYR   CZ   C  Y N 432 
TYR   OH   O  N N 433 
TYR   OXT  O  N N 434 
TYR   H    H  N N 435 
TYR   H2   H  N N 436 
TYR   HA   H  N N 437 
TYR   HB2  H  N N 438 
TYR   HB3  H  N N 439 
TYR   HD1  H  N N 440 
TYR   HD2  H  N N 441 
TYR   HE1  H  N N 442 
TYR   HE2  H  N N 443 
TYR   HH   H  N N 444 
TYR   HXT  H  N N 445 
VAL   N    N  N N 446 
VAL   CA   C  N S 447 
VAL   C    C  N N 448 
VAL   O    O  N N 449 
VAL   CB   C  N N 450 
VAL   CG1  C  N N 451 
VAL   CG2  C  N N 452 
VAL   OXT  O  N N 453 
VAL   H    H  N N 454 
VAL   H2   H  N N 455 
VAL   HA   H  N N 456 
VAL   HB   H  N N 457 
VAL   HG11 H  N N 458 
VAL   HG12 H  N N 459 
VAL   HG13 H  N N 460 
VAL   HG21 H  N N 461 
VAL   HG22 H  N N 462 
VAL   HG23 H  N N 463 
VAL   HXT  H  N N 464 
# 
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 
A1L73 O31  C22  doub N N 1   
A1L73 O30  C22  sing N N 2   
A1L73 C22  C21  sing N N 3   
A1L73 C21  C20  sing N N 4   
A1L73 C20  C19  sing N N 5   
A1L73 C19  O32  sing N N 6   
A1L73 C19  C18  sing N N 7   
A1L73 C18  O17  sing N N 8   
A1L73 O17  C02  sing N N 9   
A1L73 C02  C01  doub Y N 10  
A1L73 C02  C03  sing Y N 11  
A1L73 C01  C06  sing Y N 12  
A1L73 C03  C04  doub Y N 13  
A1L73 C06  C33  sing N N 14  
A1L73 C06  C05  doub Y N 15  
A1L73 C04  C05  sing Y N 16  
A1L73 C05  SI07 sing N N 17  
A1L73 C34  C13  sing N N 18  
A1L73 SI07 C08  sing N N 19  
A1L73 SI07 C14  sing N N 20  
A1L73 SI07 C15  sing N N 21  
A1L73 C28  C26  sing N N 22  
A1L73 C13  C08  doub Y N 23  
A1L73 C13  C12  sing Y N 24  
A1L73 C08  C09  sing Y N 25  
A1L73 C12  C11  doub Y N 26  
A1L73 C26  C24  sing N N 27  
A1L73 C09  C10  doub Y N 28  
A1L73 C11  C10  sing Y N 29  
A1L73 C11  O16  sing N N 30  
A1L73 O16  C23  sing N N 31  
A1L73 C23  C24  sing N N 32  
A1L73 C24  O29  sing N N 33  
A1L73 C24  C25  sing N N 34  
A1L73 C25  C27  sing N N 35  
A1L73 C10  H1   sing N N 36  
A1L73 C15  H2   sing N N 37  
A1L73 C15  H3   sing N N 38  
A1L73 C15  H4   sing N N 39  
A1L73 C20  H5   sing N N 40  
A1L73 C20  H6   sing N N 41  
A1L73 C21  H7   sing N N 42  
A1L73 C21  H8   sing N N 43  
A1L73 C26  H9   sing N N 44  
A1L73 C26  H10  sing N N 45  
A1L73 C28  H11  sing N N 46  
A1L73 C28  H12  sing N N 47  
A1L73 C28  H13  sing N N 48  
A1L73 C01  H14  sing N N 49  
A1L73 C03  H15  sing N N 50  
A1L73 C04  H16  sing N N 51  
A1L73 C09  H17  sing N N 52  
A1L73 C12  H18  sing N N 53  
A1L73 C14  H19  sing N N 54  
A1L73 C14  H20  sing N N 55  
A1L73 C14  H21  sing N N 56  
A1L73 C18  H22  sing N N 57  
A1L73 C18  H23  sing N N 58  
A1L73 C19  H24  sing N N 59  
A1L73 C23  H25  sing N N 60  
A1L73 C23  H26  sing N N 61  
A1L73 C25  H27  sing N N 62  
A1L73 C25  H28  sing N N 63  
A1L73 C27  H29  sing N N 64  
A1L73 C27  H30  sing N N 65  
A1L73 C27  H31  sing N N 66  
A1L73 C33  H32  sing N N 67  
A1L73 C33  H33  sing N N 68  
A1L73 C33  H34  sing N N 69  
A1L73 C34  H35  sing N N 70  
A1L73 C34  H36  sing N N 71  
A1L73 C34  H37  sing N N 72  
A1L73 O29  H38  sing N N 73  
A1L73 O30  H39  sing N N 74  
A1L73 O32  H40  sing N N 75  
ALA   N    CA   sing N N 76  
ALA   N    H    sing N N 77  
ALA   N    H2   sing N N 78  
ALA   CA   C    sing N N 79  
ALA   CA   CB   sing N N 80  
ALA   CA   HA   sing N N 81  
ALA   C    O    doub N N 82  
ALA   C    OXT  sing N N 83  
ALA   CB   HB1  sing N N 84  
ALA   CB   HB2  sing N N 85  
ALA   CB   HB3  sing N N 86  
ALA   OXT  HXT  sing N N 87  
ARG   N    CA   sing N N 88  
ARG   N    H    sing N N 89  
ARG   N    H2   sing N N 90  
ARG   CA   C    sing N N 91  
ARG   CA   CB   sing N N 92  
ARG   CA   HA   sing N N 93  
ARG   C    O    doub N N 94  
ARG   C    OXT  sing N N 95  
ARG   CB   CG   sing N N 96  
ARG   CB   HB2  sing N N 97  
ARG   CB   HB3  sing N N 98  
ARG   CG   CD   sing N N 99  
ARG   CG   HG2  sing N N 100 
ARG   CG   HG3  sing N N 101 
ARG   CD   NE   sing N N 102 
ARG   CD   HD2  sing N N 103 
ARG   CD   HD3  sing N N 104 
ARG   NE   CZ   sing N N 105 
ARG   NE   HE   sing N N 106 
ARG   CZ   NH1  sing N N 107 
ARG   CZ   NH2  doub N N 108 
ARG   NH1  HH11 sing N N 109 
ARG   NH1  HH12 sing N N 110 
ARG   NH2  HH21 sing N N 111 
ARG   NH2  HH22 sing N N 112 
ARG   OXT  HXT  sing N N 113 
ASN   N    CA   sing N N 114 
ASN   N    H    sing N N 115 
ASN   N    H2   sing N N 116 
ASN   CA   C    sing N N 117 
ASN   CA   CB   sing N N 118 
ASN   CA   HA   sing N N 119 
ASN   C    O    doub N N 120 
ASN   C    OXT  sing N N 121 
ASN   CB   CG   sing N N 122 
ASN   CB   HB2  sing N N 123 
ASN   CB   HB3  sing N N 124 
ASN   CG   OD1  doub N N 125 
ASN   CG   ND2  sing N N 126 
ASN   ND2  HD21 sing N N 127 
ASN   ND2  HD22 sing N N 128 
ASN   OXT  HXT  sing N N 129 
ASP   N    CA   sing N N 130 
ASP   N    H    sing N N 131 
ASP   N    H2   sing N N 132 
ASP   CA   C    sing N N 133 
ASP   CA   CB   sing N N 134 
ASP   CA   HA   sing N N 135 
ASP   C    O    doub N N 136 
ASP   C    OXT  sing N N 137 
ASP   CB   CG   sing N N 138 
ASP   CB   HB2  sing N N 139 
ASP   CB   HB3  sing N N 140 
ASP   CG   OD1  doub N N 141 
ASP   CG   OD2  sing N N 142 
ASP   OD2  HD2  sing N N 143 
ASP   OXT  HXT  sing N N 144 
CYS   N    CA   sing N N 145 
CYS   N    H    sing N N 146 
CYS   N    H2   sing N N 147 
CYS   CA   C    sing N N 148 
CYS   CA   CB   sing N N 149 
CYS   CA   HA   sing N N 150 
CYS   C    O    doub N N 151 
CYS   C    OXT  sing N N 152 
CYS   CB   SG   sing N N 153 
CYS   CB   HB2  sing N N 154 
CYS   CB   HB3  sing N N 155 
CYS   SG   HG   sing N N 156 
CYS   OXT  HXT  sing N N 157 
GLN   N    CA   sing N N 158 
GLN   N    H    sing N N 159 
GLN   N    H2   sing N N 160 
GLN   CA   C    sing N N 161 
GLN   CA   CB   sing N N 162 
GLN   CA   HA   sing N N 163 
GLN   C    O    doub N N 164 
GLN   C    OXT  sing N N 165 
GLN   CB   CG   sing N N 166 
GLN   CB   HB2  sing N N 167 
GLN   CB   HB3  sing N N 168 
GLN   CG   CD   sing N N 169 
GLN   CG   HG2  sing N N 170 
GLN   CG   HG3  sing N N 171 
GLN   CD   OE1  doub N N 172 
GLN   CD   NE2  sing N N 173 
GLN   NE2  HE21 sing N N 174 
GLN   NE2  HE22 sing N N 175 
GLN   OXT  HXT  sing N N 176 
GLU   N    CA   sing N N 177 
GLU   N    H    sing N N 178 
GLU   N    H2   sing N N 179 
GLU   CA   C    sing N N 180 
GLU   CA   CB   sing N N 181 
GLU   CA   HA   sing N N 182 
GLU   C    O    doub N N 183 
GLU   C    OXT  sing N N 184 
GLU   CB   CG   sing N N 185 
GLU   CB   HB2  sing N N 186 
GLU   CB   HB3  sing N N 187 
GLU   CG   CD   sing N N 188 
GLU   CG   HG2  sing N N 189 
GLU   CG   HG3  sing N N 190 
GLU   CD   OE1  doub N N 191 
GLU   CD   OE2  sing N N 192 
GLU   OE2  HE2  sing N N 193 
GLU   OXT  HXT  sing N N 194 
GLY   N    CA   sing N N 195 
GLY   N    H    sing N N 196 
GLY   N    H2   sing N N 197 
GLY   CA   C    sing N N 198 
GLY   CA   HA2  sing N N 199 
GLY   CA   HA3  sing N N 200 
GLY   C    O    doub N N 201 
GLY   C    OXT  sing N N 202 
GLY   OXT  HXT  sing N N 203 
HIS   N    CA   sing N N 204 
HIS   N    H    sing N N 205 
HIS   N    H2   sing N N 206 
HIS   CA   C    sing N N 207 
HIS   CA   CB   sing N N 208 
HIS   CA   HA   sing N N 209 
HIS   C    O    doub N N 210 
HIS   C    OXT  sing N N 211 
HIS   CB   CG   sing N N 212 
HIS   CB   HB2  sing N N 213 
HIS   CB   HB3  sing N N 214 
HIS   CG   ND1  sing Y N 215 
HIS   CG   CD2  doub Y N 216 
HIS   ND1  CE1  doub Y N 217 
HIS   ND1  HD1  sing N N 218 
HIS   CD2  NE2  sing Y N 219 
HIS   CD2  HD2  sing N N 220 
HIS   CE1  NE2  sing Y N 221 
HIS   CE1  HE1  sing N N 222 
HIS   NE2  HE2  sing N N 223 
HIS   OXT  HXT  sing N N 224 
HOH   O    H1   sing N N 225 
HOH   O    H2   sing N N 226 
ILE   N    CA   sing N N 227 
ILE   N    H    sing N N 228 
ILE   N    H2   sing N N 229 
ILE   CA   C    sing N N 230 
ILE   CA   CB   sing N N 231 
ILE   CA   HA   sing N N 232 
ILE   C    O    doub N N 233 
ILE   C    OXT  sing N N 234 
ILE   CB   CG1  sing N N 235 
ILE   CB   CG2  sing N N 236 
ILE   CB   HB   sing N N 237 
ILE   CG1  CD1  sing N N 238 
ILE   CG1  HG12 sing N N 239 
ILE   CG1  HG13 sing N N 240 
ILE   CG2  HG21 sing N N 241 
ILE   CG2  HG22 sing N N 242 
ILE   CG2  HG23 sing N N 243 
ILE   CD1  HD11 sing N N 244 
ILE   CD1  HD12 sing N N 245 
ILE   CD1  HD13 sing N N 246 
ILE   OXT  HXT  sing N N 247 
LEU   N    CA   sing N N 248 
LEU   N    H    sing N N 249 
LEU   N    H2   sing N N 250 
LEU   CA   C    sing N N 251 
LEU   CA   CB   sing N N 252 
LEU   CA   HA   sing N N 253 
LEU   C    O    doub N N 254 
LEU   C    OXT  sing N N 255 
LEU   CB   CG   sing N N 256 
LEU   CB   HB2  sing N N 257 
LEU   CB   HB3  sing N N 258 
LEU   CG   CD1  sing N N 259 
LEU   CG   CD2  sing N N 260 
LEU   CG   HG   sing N N 261 
LEU   CD1  HD11 sing N N 262 
LEU   CD1  HD12 sing N N 263 
LEU   CD1  HD13 sing N N 264 
LEU   CD2  HD21 sing N N 265 
LEU   CD2  HD22 sing N N 266 
LEU   CD2  HD23 sing N N 267 
LEU   OXT  HXT  sing N N 268 
LYS   N    CA   sing N N 269 
LYS   N    H    sing N N 270 
LYS   N    H2   sing N N 271 
LYS   CA   C    sing N N 272 
LYS   CA   CB   sing N N 273 
LYS   CA   HA   sing N N 274 
LYS   C    O    doub N N 275 
LYS   C    OXT  sing N N 276 
LYS   CB   CG   sing N N 277 
LYS   CB   HB2  sing N N 278 
LYS   CB   HB3  sing N N 279 
LYS   CG   CD   sing N N 280 
LYS   CG   HG2  sing N N 281 
LYS   CG   HG3  sing N N 282 
LYS   CD   CE   sing N N 283 
LYS   CD   HD2  sing N N 284 
LYS   CD   HD3  sing N N 285 
LYS   CE   NZ   sing N N 286 
LYS   CE   HE2  sing N N 287 
LYS   CE   HE3  sing N N 288 
LYS   NZ   HZ1  sing N N 289 
LYS   NZ   HZ2  sing N N 290 
LYS   NZ   HZ3  sing N N 291 
LYS   OXT  HXT  sing N N 292 
MET   N    CA   sing N N 293 
MET   N    H    sing N N 294 
MET   N    H2   sing N N 295 
MET   CA   C    sing N N 296 
MET   CA   CB   sing N N 297 
MET   CA   HA   sing N N 298 
MET   C    O    doub N N 299 
MET   C    OXT  sing N N 300 
MET   CB   CG   sing N N 301 
MET   CB   HB2  sing N N 302 
MET   CB   HB3  sing N N 303 
MET   CG   SD   sing N N 304 
MET   CG   HG2  sing N N 305 
MET   CG   HG3  sing N N 306 
MET   SD   CE   sing N N 307 
MET   CE   HE1  sing N N 308 
MET   CE   HE2  sing N N 309 
MET   CE   HE3  sing N N 310 
MET   OXT  HXT  sing N N 311 
PHE   N    CA   sing N N 312 
PHE   N    H    sing N N 313 
PHE   N    H2   sing N N 314 
PHE   CA   C    sing N N 315 
PHE   CA   CB   sing N N 316 
PHE   CA   HA   sing N N 317 
PHE   C    O    doub N N 318 
PHE   C    OXT  sing N N 319 
PHE   CB   CG   sing N N 320 
PHE   CB   HB2  sing N N 321 
PHE   CB   HB3  sing N N 322 
PHE   CG   CD1  doub Y N 323 
PHE   CG   CD2  sing Y N 324 
PHE   CD1  CE1  sing Y N 325 
PHE   CD1  HD1  sing N N 326 
PHE   CD2  CE2  doub Y N 327 
PHE   CD2  HD2  sing N N 328 
PHE   CE1  CZ   doub Y N 329 
PHE   CE1  HE1  sing N N 330 
PHE   CE2  CZ   sing Y N 331 
PHE   CE2  HE2  sing N N 332 
PHE   CZ   HZ   sing N N 333 
PHE   OXT  HXT  sing N N 334 
PRO   N    CA   sing N N 335 
PRO   N    CD   sing N N 336 
PRO   N    H    sing N N 337 
PRO   CA   C    sing N N 338 
PRO   CA   CB   sing N N 339 
PRO   CA   HA   sing N N 340 
PRO   C    O    doub N N 341 
PRO   C    OXT  sing N N 342 
PRO   CB   CG   sing N N 343 
PRO   CB   HB2  sing N N 344 
PRO   CB   HB3  sing N N 345 
PRO   CG   CD   sing N N 346 
PRO   CG   HG2  sing N N 347 
PRO   CG   HG3  sing N N 348 
PRO   CD   HD2  sing N N 349 
PRO   CD   HD3  sing N N 350 
PRO   OXT  HXT  sing N N 351 
SER   N    CA   sing N N 352 
SER   N    H    sing N N 353 
SER   N    H2   sing N N 354 
SER   CA   C    sing N N 355 
SER   CA   CB   sing N N 356 
SER   CA   HA   sing N N 357 
SER   C    O    doub N N 358 
SER   C    OXT  sing N N 359 
SER   CB   OG   sing N N 360 
SER   CB   HB2  sing N N 361 
SER   CB   HB3  sing N N 362 
SER   OG   HG   sing N N 363 
SER   OXT  HXT  sing N N 364 
THR   N    CA   sing N N 365 
THR   N    H    sing N N 366 
THR   N    H2   sing N N 367 
THR   CA   C    sing N N 368 
THR   CA   CB   sing N N 369 
THR   CA   HA   sing N N 370 
THR   C    O    doub N N 371 
THR   C    OXT  sing N N 372 
THR   CB   OG1  sing N N 373 
THR   CB   CG2  sing N N 374 
THR   CB   HB   sing N N 375 
THR   OG1  HG1  sing N N 376 
THR   CG2  HG21 sing N N 377 
THR   CG2  HG22 sing N N 378 
THR   CG2  HG23 sing N N 379 
THR   OXT  HXT  sing N N 380 
TRP   N    CA   sing N N 381 
TRP   N    H    sing N N 382 
TRP   N    H2   sing N N 383 
TRP   CA   C    sing N N 384 
TRP   CA   CB   sing N N 385 
TRP   CA   HA   sing N N 386 
TRP   C    O    doub N N 387 
TRP   C    OXT  sing N N 388 
TRP   CB   CG   sing N N 389 
TRP   CB   HB2  sing N N 390 
TRP   CB   HB3  sing N N 391 
TRP   CG   CD1  doub Y N 392 
TRP   CG   CD2  sing Y N 393 
TRP   CD1  NE1  sing Y N 394 
TRP   CD1  HD1  sing N N 395 
TRP   CD2  CE2  doub Y N 396 
TRP   CD2  CE3  sing Y N 397 
TRP   NE1  CE2  sing Y N 398 
TRP   NE1  HE1  sing N N 399 
TRP   CE2  CZ2  sing Y N 400 
TRP   CE3  CZ3  doub Y N 401 
TRP   CE3  HE3  sing N N 402 
TRP   CZ2  CH2  doub Y N 403 
TRP   CZ2  HZ2  sing N N 404 
TRP   CZ3  CH2  sing Y N 405 
TRP   CZ3  HZ3  sing N N 406 
TRP   CH2  HH2  sing N N 407 
TRP   OXT  HXT  sing N N 408 
TYR   N    CA   sing N N 409 
TYR   N    H    sing N N 410 
TYR   N    H2   sing N N 411 
TYR   CA   C    sing N N 412 
TYR   CA   CB   sing N N 413 
TYR   CA   HA   sing N N 414 
TYR   C    O    doub N N 415 
TYR   C    OXT  sing N N 416 
TYR   CB   CG   sing N N 417 
TYR   CB   HB2  sing N N 418 
TYR   CB   HB3  sing N N 419 
TYR   CG   CD1  doub Y N 420 
TYR   CG   CD2  sing Y N 421 
TYR   CD1  CE1  sing Y N 422 
TYR   CD1  HD1  sing N N 423 
TYR   CD2  CE2  doub Y N 424 
TYR   CD2  HD2  sing N N 425 
TYR   CE1  CZ   doub Y N 426 
TYR   CE1  HE1  sing N N 427 
TYR   CE2  CZ   sing Y N 428 
TYR   CE2  HE2  sing N N 429 
TYR   CZ   OH   sing N N 430 
TYR   OH   HH   sing N N 431 
TYR   OXT  HXT  sing N N 432 
VAL   N    CA   sing N N 433 
VAL   N    H    sing N N 434 
VAL   N    H2   sing N N 435 
VAL   CA   C    sing N N 436 
VAL   CA   CB   sing N N 437 
VAL   CA   HA   sing N N 438 
VAL   C    O    doub N N 439 
VAL   C    OXT  sing N N 440 
VAL   CB   CG1  sing N N 441 
VAL   CB   CG2  sing N N 442 
VAL   CB   HB   sing N N 443 
VAL   CG1  HG11 sing N N 444 
VAL   CG1  HG12 sing N N 445 
VAL   CG1  HG13 sing N N 446 
VAL   CG2  HG21 sing N N 447 
VAL   CG2  HG22 sing N N 448 
VAL   CG2  HG23 sing N N 449 
VAL   OXT  HXT  sing N N 450 
# 
_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                    9M15 
_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]   0.006551 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000669 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.022386 
_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]   0.023899 
_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  ? 42.705 2.690   1.525  1.00 54.61 ?  123 LYS   A N    1 
ATOM   2    C  CA   . LYS   A 1 18  ? 42.633 1.464   2.316  1.00 51.17 ?  123 LYS   A CA   1 
ATOM   3    C  C    . LYS   A 1 18  ? 41.206 0.927   2.388  1.00 43.73 ?  123 LYS   A C    1 
ATOM   4    O  O    . LYS   A 1 18  ? 40.997 -0.290  2.402  1.00 44.17 ?  123 LYS   A O    1 
ATOM   5    C  CB   . LYS   A 1 18  ? 43.173 1.694   3.727  1.00 50.79 ?  123 LYS   A CB   1 
ATOM   6    C  CG   . LYS   A 1 18  ? 44.309 2.694   3.818  1.00 51.77 ?  123 LYS   A CG   1 
ATOM   7    C  CD   . LYS   A 1 18  ? 44.868 2.737   5.232  1.00 54.48 ?  123 LYS   A CD   1 
ATOM   8    C  CE   . LYS   A 1 18  ? 46.243 3.383   5.266  1.00 59.14 ?  123 LYS   A CE   1 
ATOM   9    N  NZ   . LYS   A 1 18  ? 46.165 4.871   5.266  1.00 61.83 ?  123 LYS   A NZ   1 
ATOM   10   N  N    . LEU   A 1 19  ? 40.225 1.827   2.448  1.00 40.67 ?  124 LEU   A N    1 
ATOM   11   C  CA   . LEU   A 1 19  ? 38.829 1.423   2.290  1.00 37.31 ?  124 LEU   A CA   1 
ATOM   12   C  C    . LEU   A 1 19  ? 38.616 0.958   0.856  1.00 37.11 ?  124 LEU   A C    1 
ATOM   13   O  O    . LEU   A 1 19  ? 38.662 1.766   -0.077 1.00 33.72 ?  124 LEU   A O    1 
ATOM   14   C  CB   . LEU   A 1 19  ? 37.881 2.571   2.622  1.00 35.82 ?  124 LEU   A CB   1 
ATOM   15   C  CG   . LEU   A 1 19  ? 37.400 2.813   4.056  1.00 34.86 ?  124 LEU   A CG   1 
ATOM   16   C  CD1  . LEU   A 1 19  ? 36.345 3.905   4.036  1.00 36.73 ?  124 LEU   A CD1  1 
ATOM   17   C  CD2  . LEU   A 1 19  ? 36.860 1.546   4.721  1.00 26.47 ?  124 LEU   A CD2  1 
ATOM   18   N  N    . SER   A 1 20  ? 38.383 -0.340  0.676  1.00 36.39 ?  125 SER   A N    1 
ATOM   19   C  CA   . SER   A 1 20  ? 38.140 -0.878  -0.651 1.00 31.13 ?  125 SER   A CA   1 
ATOM   20   C  C    . SER   A 1 20  ? 36.829 -0.337  -1.220 1.00 34.35 ?  125 SER   A C    1 
ATOM   21   O  O    . SER   A 1 20  ? 36.045 0.338   -0.541 1.00 33.85 ?  125 SER   A O    1 
ATOM   22   C  CB   . SER   A 1 20  ? 38.102 -2.405  -0.613 1.00 29.22 ?  125 SER   A CB   1 
ATOM   23   O  OG   . SER   A 1 20  ? 36.903 -2.869  -0.005 1.00 30.71 ?  125 SER   A OG   1 
ATOM   24   N  N    . GLU   A 1 21  ? 36.607 -0.646  -2.501 1.00 31.16 ?  126 GLU   A N    1 
ATOM   25   C  CA   . GLU   A 1 21  ? 35.368 -0.272  -3.177 1.00 30.53 ?  126 GLU   A CA   1 
ATOM   26   C  C    . GLU   A 1 21  ? 34.150 -0.873  -2.483 1.00 25.29 ?  126 GLU   A C    1 
ATOM   27   O  O    . GLU   A 1 21  ? 33.119 -0.209  -2.334 1.00 25.21 ?  126 GLU   A O    1 
ATOM   28   C  CB   . GLU   A 1 21  ? 35.427 -0.720  -4.643 1.00 35.77 ?  126 GLU   A CB   1 
ATOM   29   C  CG   . GLU   A 1 21  ? 35.386 -2.250  -4.862 1.00 44.26 ?  126 GLU   A CG   1 
ATOM   30   C  CD   . GLU   A 1 21  ? 36.559 -2.989  -4.213 1.00 52.67 ?  126 GLU   A CD   1 
ATOM   31   O  OE1  . GLU   A 1 21  ? 37.720 -2.743  -4.617 1.00 58.43 ?  126 GLU   A OE1  1 
ATOM   32   O  OE2  . GLU   A 1 21  ? 36.319 -3.799  -3.286 1.00 47.24 ?  126 GLU   A OE2  1 
ATOM   33   N  N    . GLU   A 1 22  ? 34.250 -2.137  -2.070 1.00 27.32 ?  127 GLU   A N    1 
ATOM   34   C  CA   . GLU   A 1 22  ? 33.147 -2.810  -1.404 1.00 29.38 ?  127 GLU   A CA   1 
ATOM   35   C  C    . GLU   A 1 22  ? 32.853 -2.171  -0.052 1.00 26.27 ?  127 GLU   A C    1 
ATOM   36   O  O    . GLU   A 1 22  ? 31.687 -2.061  0.349  1.00 23.61 ?  127 GLU   A O    1 
ATOM   37   C  CB   . GLU   A 1 22  ? 33.484 -4.295  -1.254 1.00 36.68 ?  127 GLU   A CB   1 
ATOM   38   C  CG   . GLU   A 1 22  ? 32.569 -5.083  -0.339 1.00 47.74 ?  127 GLU   A CG   1 
ATOM   39   C  CD   . GLU   A 1 22  ? 32.800 -6.579  -0.451 1.00 58.71 ?  127 GLU   A CD   1 
ATOM   40   O  OE1  . GLU   A 1 22  ? 33.341 -7.175  0.505  1.00 62.81 ?  127 GLU   A OE1  1 
ATOM   41   O  OE2  . GLU   A 1 22  ? 32.448 -7.158  -1.501 1.00 62.76 ?  127 GLU   A OE2  1 
ATOM   42   N  N    . GLN   A 1 23  ? 33.898 -1.731  0.657  1.00 22.91 ?  128 GLN   A N    1 
ATOM   43   C  CA   . GLN   A 1 23  ? 33.707 -1.161  1.989  1.00 25.28 ?  128 GLN   A CA   1 
ATOM   44   C  C    . GLN   A 1 23  ? 33.036 0.206   1.916  1.00 24.34 ?  128 GLN   A C    1 
ATOM   45   O  O    . GLN   A 1 23  ? 32.114 0.491   2.691  1.00 23.00 ?  128 GLN   A O    1 
ATOM   46   C  CB   . GLN   A 1 23  ? 35.049 -1.074  2.718  1.00 21.86 ?  128 GLN   A CB   1 
ATOM   47   C  CG   . GLN   A 1 23  ? 35.533 -2.422  3.228  1.00 22.24 ?  128 GLN   A CG   1 
ATOM   48   C  CD   . GLN   A 1 23  ? 36.999 -2.421  3.594  1.00 28.84 ?  128 GLN   A CD   1 
ATOM   49   O  OE1  . GLN   A 1 23  ? 37.728 -1.477  3.286  1.00 33.69 ?  128 GLN   A OE1  1 
ATOM   50   N  NE2  . GLN   A 1 23  ? 37.446 -3.493  4.241  1.00 29.71 ?  128 GLN   A NE2  1 
ATOM   51   N  N    . GLN   A 1 24  ? 33.485 1.065   0.995  1.00 26.01 ?  129 GLN   A N    1 
ATOM   52   C  CA   . GLN   A 1 24  ? 32.800 2.336   0.781  1.00 26.77 ?  129 GLN   A CA   1 
ATOM   53   C  C    . GLN   A 1 24  ? 31.348 2.106   0.380  1.00 24.12 ?  129 GLN   A C    1 
ATOM   54   O  O    . GLN   A 1 24  ? 30.452 2.848   0.800  1.00 23.78 ?  129 GLN   A O    1 
ATOM   55   C  CB   . GLN   A 1 24  ? 33.526 3.158   -0.287 1.00 28.42 ?  129 GLN   A CB   1 
ATOM   56   C  CG   . GLN   A 1 24  ? 35.001 3.419   0.007  1.00 33.11 ?  129 GLN   A CG   1 
ATOM   57   C  CD   . GLN   A 1 24  ? 35.735 4.057   -1.165 1.00 41.85 ?  129 GLN   A CD   1 
ATOM   58   O  OE1  . GLN   A 1 24  ? 35.122 4.681   -2.033 1.00 43.16 ?  129 GLN   A OE1  1 
ATOM   59   N  NE2  . GLN   A 1 24  ? 37.056 3.906   -1.190 1.00 45.98 ?  129 GLN   A NE2  1 
ATOM   60   N  N    . HIS   A 1 25  ? 31.103 1.069   -0.424 1.00 22.50 ?  130 HIS   A N    1 
ATOM   61   C  CA   . HIS   A 1 25  ? 29.752 0.753   -0.881 1.00 25.70 ?  130 HIS   A CA   1 
ATOM   62   C  C    . HIS   A 1 25  ? 28.865 0.336   0.288  1.00 25.79 ?  130 HIS   A C    1 
ATOM   63   O  O    . HIS   A 1 25  ? 27.735 0.818   0.425  1.00 22.97 ?  130 HIS   A O    1 
ATOM   64   C  CB   . HIS   A 1 25  ? 29.837 -0.350  -1.944 1.00 23.78 ?  130 HIS   A CB   1 
ATOM   65   C  CG   . HIS   A 1 25  ? 28.515 -0.856  -2.431 1.00 30.49 ?  130 HIS   A CG   1 
ATOM   66   N  ND1  . HIS   A 1 25  ? 27.581 -0.047  -3.043 1.00 31.67 ?  130 HIS   A ND1  1 
ATOM   67   C  CD2  . HIS   A 1 25  ? 27.991 -2.106  -2.441 1.00 31.58 ?  130 HIS   A CD2  1 
ATOM   68   C  CE1  . HIS   A 1 25  ? 26.530 -0.771  -3.385 1.00 30.72 ?  130 HIS   A CE1  1 
ATOM   69   N  NE2  . HIS   A 1 25  ? 26.753 -2.024  -3.032 1.00 30.80 ?  130 HIS   A NE2  1 
ATOM   70   N  N    . ILE   A 1 26  ? 29.372 -0.556  1.145  1.00 22.34 ?  131 ILE   A N    1 
ATOM   71   C  CA   . ILE   A 1 26  ? 28.631 -0.990  2.328  1.00 21.83 ?  131 ILE   A CA   1 
ATOM   72   C  C    . ILE   A 1 26  ? 28.311 0.199   3.222  1.00 22.13 ?  131 ILE   A C    1 
ATOM   73   O  O    . ILE   A 1 26  ? 27.191 0.334   3.735  1.00 19.60 ?  131 ILE   A O    1 
ATOM   74   C  CB   . ILE   A 1 26  ? 29.441 -2.055  3.089  1.00 24.39 ?  131 ILE   A CB   1 
ATOM   75   C  CG1  . ILE   A 1 26  ? 29.446 -3.381  2.331  1.00 24.40 ?  131 ILE   A CG1  1 
ATOM   76   C  CG2  . ILE   A 1 26  ? 28.915 -2.231  4.516  1.00 21.85 ?  131 ILE   A CG2  1 
ATOM   77   C  CD1  . ILE   A 1 26  ? 30.533 -4.326  2.814  1.00 24.62 ?  131 ILE   A CD1  1 
ATOM   78   N  N    . ILE   A 1 27  ? 29.292 1.079   3.423  1.00 21.71 ?  132 ILE   A N    1 
ATOM   79   C  CA   . ILE   A 1 27  ? 29.095 2.227   4.300  1.00 23.79 ?  132 ILE   A CA   1 
ATOM   80   C  C    . ILE   A 1 27  ? 28.040 3.163   3.727  1.00 24.92 ?  132 ILE   A C    1 
ATOM   81   O  O    . ILE   A 1 27  ? 27.153 3.631   4.450  1.00 22.27 ?  132 ILE   A O    1 
ATOM   82   C  CB   . ILE   A 1 27  ? 30.438 2.940   4.542  1.00 25.23 ?  132 ILE   A CB   1 
ATOM   83   C  CG1  . ILE   A 1 27  ? 31.283 2.128   5.526  1.00 23.12 ?  132 ILE   A CG1  1 
ATOM   84   C  CG2  . ILE   A 1 27  ? 30.222 4.345   5.077  1.00 23.96 ?  132 ILE   A CG2  1 
ATOM   85   C  CD1  . ILE   A 1 27  ? 32.710 2.623   5.664  1.00 24.64 ?  132 ILE   A CD1  1 
ATOM   86   N  N    . ALA   A 1 28  ? 28.099 3.431   2.417  1.00 23.94 ?  133 ALA   A N    1 
ATOM   87   C  CA   . ALA   A 1 28  ? 27.094 4.286   1.785  1.00 23.80 ?  133 ALA   A CA   1 
ATOM   88   C  C    . ALA   A 1 28  ? 25.694 3.699   1.923  1.00 21.66 ?  133 ALA   A C    1 
ATOM   89   O  O    . ALA   A 1 28  ? 24.717 4.432   2.122  1.00 17.19 ?  133 ALA   A O    1 
ATOM   90   C  CB   . ALA   A 1 28  ? 27.434 4.498   0.307  1.00 25.72 ?  133 ALA   A CB   1 
ATOM   91   N  N    . ILE   A 1 29  ? 25.577 2.376   1.814  1.00 21.49 ?  134 ILE   A N    1 
ATOM   92   C  CA   . ILE   A 1 29  ? 24.279 1.724   1.949  1.00 19.30 ?  134 ILE   A CA   1 
ATOM   93   C  C    . ILE   A 1 29  ? 23.735 1.906   3.363  1.00 21.42 ?  134 ILE   A C    1 
ATOM   94   O  O    . ILE   A 1 29  ? 22.572 2.285   3.561  1.00 22.11 ?  134 ILE   A O    1 
ATOM   95   C  CB   . ILE   A 1 29  ? 24.394 0.236   1.574  1.00 22.17 ?  134 ILE   A CB   1 
ATOM   96   C  CG1  . ILE   A 1 29  ? 24.498 0.081   0.057  1.00 26.38 ?  134 ILE   A CG1  1 
ATOM   97   C  CG2  . ILE   A 1 29  ? 23.214 -0.550  2.121  1.00 22.46 ?  134 ILE   A CG2  1 
ATOM   98   C  CD1  . ILE   A 1 29  ? 24.734 -1.346  -0.390 1.00 28.02 ?  134 ILE   A CD1  1 
ATOM   99   N  N    . LEU   A 1 30  ? 24.573 1.646   4.370  1.00 22.23 ?  135 LEU   A N    1 
ATOM   100  C  CA   . LEU   A 1 30  ? 24.106 1.729   5.752  1.00 19.32 ?  135 LEU   A CA   1 
ATOM   101  C  C    . LEU   A 1 30  ? 23.780 3.164   6.144  1.00 15.97 ?  135 LEU   A C    1 
ATOM   102  O  O    . LEU   A 1 30  ? 22.841 3.397   6.912  1.00 21.27 ?  135 LEU   A O    1 
ATOM   103  C  CB   . LEU   A 1 30  ? 25.149 1.131   6.697  1.00 16.01 ?  135 LEU   A CB   1 
ATOM   104  C  CG   . LEU   A 1 30  ? 25.337 -0.385  6.595  1.00 16.57 ?  135 LEU   A CG   1 
ATOM   105  C  CD1  . LEU   A 1 30  ? 26.505 -0.843  7.465  1.00 19.48 ?  135 LEU   A CD1  1 
ATOM   106  C  CD2  . LEU   A 1 30  ? 24.051 -1.121  6.974  1.00 12.98 ?  135 LEU   A CD2  1 
ATOM   107  N  N    A LEU   A 1 31  ? 24.517 4.139   5.615  0.64 16.44 ?  136 LEU   A N    1 
ATOM   108  N  N    B LEU   A 1 31  ? 24.558 4.133   5.645  0.36 16.79 ?  136 LEU   A N    1 
ATOM   109  C  CA   A LEU   A 1 31  ? 24.197 5.529   5.916  0.64 18.12 ?  136 LEU   A CA   1 
ATOM   110  C  CA   B LEU   A 1 31  ? 24.236 5.541   5.867  0.36 18.38 ?  136 LEU   A CA   1 
ATOM   111  C  C    A LEU   A 1 31  ? 22.871 5.941   5.294  0.64 21.02 ?  136 LEU   A C    1 
ATOM   112  C  C    B LEU   A 1 31  ? 22.856 5.872   5.320  0.36 20.53 ?  136 LEU   A C    1 
ATOM   113  O  O    A LEU   A 1 31  ? 22.090 6.672   5.917  0.64 19.93 ?  136 LEU   A O    1 
ATOM   114  O  O    B LEU   A 1 31  ? 22.027 6.479   6.010  0.36 19.36 ?  136 LEU   A O    1 
ATOM   115  C  CB   A LEU   A 1 31  ? 25.320 6.441   5.439  0.64 19.37 ?  136 LEU   A CB   1 
ATOM   116  C  CB   B LEU   A 1 31  ? 25.281 6.449   5.209  0.36 19.45 ?  136 LEU   A CB   1 
ATOM   117  C  CG   A LEU   A 1 31  ? 26.539 6.387   6.350  0.64 19.35 ?  136 LEU   A CG   1 
ATOM   118  C  CG   B LEU   A 1 31  ? 26.778 6.400   5.533  0.36 20.12 ?  136 LEU   A CG   1 
ATOM   119  C  CD1  A LEU   A 1 31  ? 27.782 6.823   5.597  0.64 21.42 ?  136 LEU   A CD1  1 
ATOM   120  C  CD1  B LEU   A 1 31  ? 27.443 7.743   5.241  0.36 21.35 ?  136 LEU   A CD1  1 
ATOM   121  C  CD2  A LEU   A 1 31  ? 26.303 7.254   7.565  0.64 19.50 ?  136 LEU   A CD2  1 
ATOM   122  C  CD2  B LEU   A 1 31  ? 27.035 5.973   6.962  0.36 20.02 ?  136 LEU   A CD2  1 
ATOM   123  N  N    . ASP   A 1 32  ? 22.598 5.482   4.068  1.00 22.19 ?  137 ASP   A N    1 
ATOM   124  C  CA   . ASP   A 1 32  ? 21.312 5.767   3.446  1.00 22.66 ?  137 ASP   A CA   1 
ATOM   125  C  C    . ASP   A 1 32  ? 20.179 5.075   4.186  1.00 20.64 ?  137 ASP   A C    1 
ATOM   126  O  O    . ASP   A 1 32  ? 19.113 5.666   4.395  1.00 22.28 ?  137 ASP   A O    1 
ATOM   127  C  CB   . ASP   A 1 32  ? 21.339 5.324   1.984  1.00 30.14 ?  137 ASP   A CB   1 
ATOM   128  C  CG   . ASP   A 1 32  ? 20.075 5.688   1.241  1.00 34.18 ?  137 ASP   A CG   1 
ATOM   129  O  OD1  . ASP   A 1 32  ? 19.351 4.760   0.819  1.00 41.16 ?  137 ASP   A OD1  1 
ATOM   130  O  OD2  . ASP   A 1 32  ? 19.806 6.898   1.075  1.00 32.44 ?  137 ASP   A OD2  1 
ATOM   131  N  N    . ALA   A 1 33  ? 20.399 3.821   4.592  1.00 18.44 ?  138 ALA   A N    1 
ATOM   132  C  CA   . ALA   A 1 33  ? 19.399 3.092   5.360  1.00 18.93 ?  138 ALA   A CA   1 
ATOM   133  C  C    . ALA   A 1 33  ? 19.064 3.813   6.660  1.00 19.23 ?  138 ALA   A C    1 
ATOM   134  O  O    . ALA   A 1 33  ? 17.897 3.873   7.061  1.00 18.48 ?  138 ALA   A O    1 
ATOM   135  C  CB   . ALA   A 1 33  ? 19.897 1.676   5.647  1.00 19.65 ?  138 ALA   A CB   1 
ATOM   136  N  N    . HIS   A 1 34  ? 20.077 4.383   7.318  1.00 17.24 ?  139 HIS   A N    1 
ATOM   137  C  CA   . HIS   A 1 34  ? 19.861 5.071   8.586  1.00 18.65 ?  139 HIS   A CA   1 
ATOM   138  C  C    . HIS   A 1 34  ? 19.162 6.406   8.385  1.00 20.04 ?  139 HIS   A C    1 
ATOM   139  O  O    . HIS   A 1 34  ? 18.301 6.788   9.186  1.00 17.33 ?  139 HIS   A O    1 
ATOM   140  C  CB   . HIS   A 1 34  ? 21.197 5.276   9.302  1.00 21.36 ?  139 HIS   A CB   1 
ATOM   141  C  CG   . HIS   A 1 34  ? 21.085 6.010   10.604 1.00 25.63 ?  139 HIS   A CG   1 
ATOM   142  N  ND1  . HIS   A 1 34  ? 20.228 5.618   11.611 1.00 27.10 ?  139 HIS   A ND1  1 
ATOM   143  C  CD2  . HIS   A 1 34  ? 21.731 7.108   11.066 1.00 26.96 ?  139 HIS   A CD2  1 
ATOM   144  C  CE1  . HIS   A 1 34  ? 20.349 6.444   12.636 1.00 25.99 ?  139 HIS   A CE1  1 
ATOM   145  N  NE2  . HIS   A 1 34  ? 21.254 7.357   12.330 1.00 28.15 ?  139 HIS   A NE2  1 
ATOM   146  N  N    . HIS   A 1 35  ? 19.525 7.143   7.334  1.00 21.39 ?  140 HIS   A N    1 
ATOM   147  C  CA   . HIS   A 1 35  ? 18.848 8.405   7.071  1.00 28.52 ?  140 HIS   A CA   1 
ATOM   148  C  C    . HIS   A 1 35  ? 17.410 8.188   6.626  1.00 24.68 ?  140 HIS   A C    1 
ATOM   149  O  O    . HIS   A 1 35  ? 16.591 9.105   6.742  1.00 24.64 ?  140 HIS   A O    1 
ATOM   150  C  CB   . HIS   A 1 35  ? 19.619 9.213   6.025  1.00 42.72 ?  140 HIS   A CB   1 
ATOM   151  C  CG   . HIS   A 1 35  ? 20.782 9.970   6.588  1.00 54.16 ?  140 HIS   A CG   1 
ATOM   152  N  ND1  . HIS   A 1 35  ? 22.045 9.427   6.694  1.00 56.93 ?  140 HIS   A ND1  1 
ATOM   153  C  CD2  . HIS   A 1 35  ? 20.870 11.224  7.093  1.00 58.06 ?  140 HIS   A CD2  1 
ATOM   154  C  CE1  . HIS   A 1 35  ? 22.862 10.316  7.231  1.00 57.82 ?  140 HIS   A CE1  1 
ATOM   155  N  NE2  . HIS   A 1 35  ? 22.174 11.415  7.484  1.00 58.13 ?  140 HIS   A NE2  1 
ATOM   156  N  N    A LYS   A 1 36  ? 17.086 6.999   6.119  0.48 23.75 ?  141 LYS   A N    1 
ATOM   157  N  N    C LYS   A 1 36  ? 17.083 7.001   6.122  0.52 23.71 ?  141 LYS   A N    1 
ATOM   158  C  CA   A LYS   A 1 36  ? 15.719 6.670   5.743  0.48 24.38 ?  141 LYS   A CA   1 
ATOM   159  C  CA   C LYS   A 1 36  ? 15.714 6.682   5.746  0.52 24.38 ?  141 LYS   A CA   1 
ATOM   160  C  C    A LYS   A 1 36  ? 14.882 6.188   6.920  0.48 23.64 ?  141 LYS   A C    1 
ATOM   161  C  C    C LYS   A 1 36  ? 14.883 6.168   6.914  0.52 23.66 ?  141 LYS   A C    1 
ATOM   162  O  O    A LYS   A 1 36  ? 13.657 6.103   6.791  0.48 24.38 ?  141 LYS   A O    1 
ATOM   163  O  O    C LYS   A 1 36  ? 13.663 6.042   6.773  0.52 24.44 ?  141 LYS   A O    1 
ATOM   164  C  CB   A LYS   A 1 36  ? 15.715 5.596   4.653  0.48 24.95 ?  141 LYS   A CB   1 
ATOM   165  C  CB   C LYS   A 1 36  ? 15.702 5.642   4.621  0.52 25.00 ?  141 LYS   A CB   1 
ATOM   166  C  CG   A LYS   A 1 36  ? 15.898 6.126   3.240  0.48 26.86 ?  141 LYS   A CG   1 
ATOM   167  C  CG   C LYS   A 1 36  ? 15.785 6.229   3.219  0.52 26.90 ?  141 LYS   A CG   1 
ATOM   168  C  CD   A LYS   A 1 36  ? 16.022 4.986   2.247  0.48 28.36 ?  141 LYS   A CD   1 
ATOM   169  C  CD   C LYS   A 1 36  ? 16.446 5.255   2.261  0.52 28.64 ?  141 LYS   A CD   1 
ATOM   170  C  CE   A LYS   A 1 36  ? 15.967 5.496   0.815  0.48 31.32 ?  141 LYS   A CE   1 
ATOM   171  C  CE   C LYS   A 1 36  ? 16.097 5.574   0.816  0.52 31.38 ?  141 LYS   A CE   1 
ATOM   172  N  NZ   A LYS   A 1 36  ? 16.823 6.701   0.625  0.48 33.03 ?  141 LYS   A NZ   1 
ATOM   173  N  NZ   C LYS   A 1 36  ? 15.842 4.336   0.023  0.52 31.83 ?  141 LYS   A NZ   1 
ATOM   174  N  N    . THR   A 1 37  ? 15.507 5.870   8.055  1.00 20.30 ?  142 THR   A N    1 
ATOM   175  C  CA   . THR   A 1 37  ? 14.803 5.308   9.201  1.00 20.50 ?  142 THR   A CA   1 
ATOM   176  C  C    . THR   A 1 37  ? 14.979 6.123   10.477 1.00 25.01 ?  142 THR   A C    1 
ATOM   177  O  O    . THR   A 1 37  ? 14.546 5.676   11.546 1.00 25.81 ?  142 THR   A O    1 
ATOM   178  C  CB   . THR   A 1 37  ? 15.255 3.866   9.444  1.00 18.76 ?  142 THR   A CB   1 
ATOM   179  O  OG1  . THR   A 1 37  ? 16.687 3.817   9.513  1.00 21.45 ?  142 THR   A OG1  1 
ATOM   180  C  CG2  . THR   A 1 37  ? 14.785 2.966   8.322  1.00 10.87 ?  142 THR   A CG2  1 
ATOM   181  N  N    . TYR   A 1 38  ? 15.597 7.302   10.405 1.00 25.93 ?  143 TYR   A N    1 
ATOM   182  C  CA   . TYR   A 1 38  ? 15.763 8.171   11.569 1.00 26.80 ?  143 TYR   A CA   1 
ATOM   183  C  C    . TYR   A 1 38  ? 15.387 9.591   11.170 1.00 31.76 ?  143 TYR   A C    1 
ATOM   184  O  O    . TYR   A 1 38  ? 16.131 10.251  10.438 1.00 32.53 ?  143 TYR   A O    1 
ATOM   185  C  CB   . TYR   A 1 38  ? 17.194 8.116   12.109 1.00 21.44 ?  143 TYR   A CB   1 
ATOM   186  C  CG   . TYR   A 1 38  ? 17.373 8.785   13.460 1.00 21.71 ?  143 TYR   A CG   1 
ATOM   187  C  CD1  . TYR   A 1 38  ? 17.339 10.173  13.587 1.00 23.44 ?  143 TYR   A CD1  1 
ATOM   188  C  CD2  . TYR   A 1 38  ? 17.576 8.028   14.611 1.00 17.29 ?  143 TYR   A CD2  1 
ATOM   189  C  CE1  . TYR   A 1 38  ? 17.497 10.783  14.822 1.00 24.92 ?  143 TYR   A CE1  1 
ATOM   190  C  CE2  . TYR   A 1 38  ? 17.734 8.630   15.841 1.00 19.80 ?  143 TYR   A CE2  1 
ATOM   191  C  CZ   . TYR   A 1 38  ? 17.692 10.007  15.943 1.00 23.31 ?  143 TYR   A CZ   1 
ATOM   192  O  OH   . TYR   A 1 38  ? 17.857 10.605  17.172 1.00 26.21 ?  143 TYR   A OH   1 
ATOM   193  N  N    . ASP   A 1 39  ? 14.244 10.065  11.669 1.00 33.13 ?  144 ASP   A N    1 
ATOM   194  C  CA   . ASP   A 1 39  ? 13.785 11.420  11.398 1.00 33.75 ?  144 ASP   A CA   1 
ATOM   195  C  C    . ASP   A 1 39  ? 14.313 12.346  12.486 1.00 37.51 ?  144 ASP   A C    1 
ATOM   196  O  O    . ASP   A 1 39  ? 13.865 12.246  13.637 1.00 40.19 ?  144 ASP   A O    1 
ATOM   197  C  CB   . ASP   A 1 39  ? 12.264 11.461  11.350 1.00 33.48 ?  144 ASP   A CB   1 
ATOM   198  C  CG   . ASP   A 1 39  ? 11.715 12.851  11.085 1.00 39.72 ?  144 ASP   A CG   1 
ATOM   199  O  OD1  . ASP   A 1 39  ? 12.500 13.806  10.925 1.00 40.41 ?  144 ASP   A OD1  1 
ATOM   200  O  OD2  . ASP   A 1 39  ? 10.476 12.990  11.040 1.00 43.59 ?  144 ASP   A OD2  1 
ATOM   201  N  N    . PRO   A 1 40  ? 15.251 13.249  12.186 1.00 39.50 ?  145 PRO   A N    1 
ATOM   202  C  CA   . PRO   A 1 40  ? 15.720 14.198  13.203 1.00 37.21 ?  145 PRO   A CA   1 
ATOM   203  C  C    . PRO   A 1 40  ? 14.757 15.343  13.483 1.00 36.87 ?  145 PRO   A C    1 
ATOM   204  O  O    . PRO   A 1 40  ? 15.031 16.147  14.381 1.00 39.08 ?  145 PRO   A O    1 
ATOM   205  C  CB   . PRO   A 1 40  ? 17.039 14.716  12.607 1.00 36.33 ?  145 PRO   A CB   1 
ATOM   206  C  CG   . PRO   A 1 40  ? 16.856 14.600  11.145 1.00 37.77 ?  145 PRO   A CG   1 
ATOM   207  C  CD   . PRO   A 1 40  ? 15.985 13.389  10.915 1.00 38.88 ?  145 PRO   A CD   1 
ATOM   208  N  N    . THR   A 1 41  ? 13.647 15.452  12.751 1.00 36.05 ?  146 THR   A N    1 
ATOM   209  C  CA   . THR   A 1 41  ? 12.605 16.400  13.128 1.00 38.39 ?  146 THR   A CA   1 
ATOM   210  C  C    . THR   A 1 41  ? 11.659 15.833  14.180 1.00 37.66 ?  146 THR   A C    1 
ATOM   211  O  O    . THR   A 1 41  ? 10.940 16.605  14.825 1.00 37.82 ?  146 THR   A O    1 
ATOM   212  C  CB   . THR   A 1 41  ? 11.788 16.833  11.910 1.00 36.37 ?  146 THR   A CB   1 
ATOM   213  O  OG1  . THR   A 1 41  ? 11.005 15.727  11.444 1.00 37.91 ?  146 THR   A OG1  1 
ATOM   214  C  CG2  . THR   A 1 41  ? 12.694 17.313  10.797 1.00 37.00 ?  146 THR   A CG2  1 
ATOM   215  N  N    . TYR   A 1 42  ? 11.642 14.510  14.355 1.00 37.13 ?  147 TYR   A N    1 
ATOM   216  C  CA   . TYR   A 1 42  ? 10.787 13.844  15.338 1.00 37.27 ?  147 TYR   A CA   1 
ATOM   217  C  C    . TYR   A 1 42  ? 9.328  14.248  15.154 1.00 38.56 ?  147 TYR   A C    1 
ATOM   218  O  O    . TYR   A 1 42  ? 8.577  14.414  16.118 1.00 39.76 ?  147 TYR   A O    1 
ATOM   219  C  CB   . TYR   A 1 42  ? 11.265 14.130  16.763 1.00 36.34 ?  147 TYR   A CB   1 
ATOM   220  C  CG   . TYR   A 1 42  ? 12.735 13.847  16.977 1.00 34.20 ?  147 TYR   A CG   1 
ATOM   221  C  CD1  . TYR   A 1 42  ? 13.655 14.883  17.078 1.00 36.04 ?  147 TYR   A CD1  1 
ATOM   222  C  CD2  . TYR   A 1 42  ? 13.203 12.543  17.071 1.00 31.99 ?  147 TYR   A CD2  1 
ATOM   223  C  CE1  . TYR   A 1 42  ? 14.998 14.630  17.271 1.00 36.09 ?  147 TYR   A CE1  1 
ATOM   224  C  CE2  . TYR   A 1 42  ? 14.547 12.279  17.261 1.00 34.61 ?  147 TYR   A CE2  1 
ATOM   225  C  CZ   . TYR   A 1 42  ? 15.440 13.327  17.361 1.00 34.23 ?  147 TYR   A CZ   1 
ATOM   226  O  OH   . TYR   A 1 42  ? 16.778 13.072  17.555 1.00 33.51 ?  147 TYR   A OH   1 
ATOM   227  N  N    . ALA   A 1 43  ? 8.924  14.405  13.892 1.00 37.09 ?  148 ALA   A N    1 
ATOM   228  C  CA   . ALA   A 1 43  ? 7.587  14.904  13.594 1.00 35.03 ?  148 ALA   A CA   1 
ATOM   229  C  C    . ALA   A 1 43  ? 6.508  13.894  13.953 1.00 34.57 ?  148 ALA   A C    1 
ATOM   230  O  O    . ALA   A 1 43  ? 5.388  14.285  14.293 1.00 35.08 ?  148 ALA   A O    1 
ATOM   231  C  CB   . ALA   A 1 43  ? 7.482  15.277  12.116 1.00 32.32 ?  148 ALA   A CB   1 
ATOM   232  N  N    . ASP   A 1 44  ? 6.819  12.601  13.880 1.00 35.75 ?  149 ASP   A N    1 
ATOM   233  C  CA   . ASP   A 1 44  ? 5.820  11.570  14.129 1.00 37.26 ?  149 ASP   A CA   1 
ATOM   234  C  C    . ASP   A 1 44  ? 5.524  11.362  15.607 1.00 34.30 ?  149 ASP   A C    1 
ATOM   235  O  O    . ASP   A 1 44  ? 4.534  10.697  15.929 1.00 35.90 ?  149 ASP   A O    1 
ATOM   236  C  CB   . ASP   A 1 44  ? 6.268  10.254  13.503 1.00 39.06 ?  149 ASP   A CB   1 
ATOM   237  C  CG   . ASP   A 1 44  ? 6.457  10.366  12.012 1.00 42.23 ?  149 ASP   A CG   1 
ATOM   238  O  OD1  . ASP   A 1 44  ? 5.607  11.008  11.358 1.00 41.89 ?  149 ASP   A OD1  1 
ATOM   239  O  OD2  . ASP   A 1 44  ? 7.458  9.824   11.498 1.00 45.40 ?  149 ASP   A OD2  1 
ATOM   240  N  N    . PHE   A 1 45  ? 6.345  11.914  16.506 1.00 33.06 ?  150 PHE   A N    1 
ATOM   241  C  CA   . PHE   A 1 45  ? 6.070  11.811  17.935 1.00 31.72 ?  150 PHE   A CA   1 
ATOM   242  C  C    . PHE   A 1 45  ? 4.753  12.475  18.300 1.00 35.07 ?  150 PHE   A C    1 
ATOM   243  O  O    . PHE   A 1 45  ? 4.171  12.159  19.346 1.00 33.75 ?  150 PHE   A O    1 
ATOM   244  C  CB   . PHE   A 1 45  ? 7.211  12.441  18.741 1.00 32.73 ?  150 PHE   A CB   1 
ATOM   245  C  CG   . PHE   A 1 45  ? 8.454  11.590  18.815 1.00 32.31 ?  150 PHE   A CG   1 
ATOM   246  C  CD1  . PHE   A 1 45  ? 8.957  10.959  17.687 1.00 29.26 ?  150 PHE   A CD1  1 
ATOM   247  C  CD2  . PHE   A 1 45  ? 9.121  11.427  20.018 1.00 29.41 ?  150 PHE   A CD2  1 
ATOM   248  C  CE1  . PHE   A 1 45  ? 10.099 10.180  17.760 1.00 28.12 ?  150 PHE   A CE1  1 
ATOM   249  C  CE2  . PHE   A 1 45  ? 10.260 10.652  20.095 1.00 27.99 ?  150 PHE   A CE2  1 
ATOM   250  C  CZ   . PHE   A 1 45  ? 10.753 10.031  18.966 1.00 25.25 ?  150 PHE   A CZ   1 
ATOM   251  N  N    . ARG   A 1 46  ? 4.272  13.385  17.451 1.00 37.49 ?  151 ARG   A N    1 
ATOM   252  C  CA   . ARG   A 1 46  ? 3.000  14.054  17.672 1.00 41.48 ?  151 ARG   A CA   1 
ATOM   253  C  C    . ARG   A 1 46  ? 1.814  13.114  17.476 1.00 39.94 ?  151 ARG   A C    1 
ATOM   254  O  O    . ARG   A 1 46  ? 0.727  13.387  17.996 1.00 42.25 ?  151 ARG   A O    1 
ATOM   255  C  CB   . ARG   A 1 46  ? 2.915  15.269  16.740 1.00 47.20 ?  151 ARG   A CB   1 
ATOM   256  C  CG   . ARG   A 1 46  ? 1.581  15.999  16.696 1.00 55.14 ?  151 ARG   A CG   1 
ATOM   257  C  CD   . ARG   A 1 46  ? 0.792  15.607  15.451 1.00 62.24 ?  151 ARG   A CD   1 
ATOM   258  N  NE   . ARG   A 1 46  ? -0.627 15.926  15.569 1.00 66.60 ?  151 ARG   A NE   1 
ATOM   259  C  CZ   . ARG   A 1 46  ? -1.535 15.636  14.643 1.00 68.52 ?  151 ARG   A CZ   1 
ATOM   260  N  NH1  . ARG   A 1 46  ? -2.807 15.965  14.831 1.00 69.37 ?  151 ARG   A NH1  1 
ATOM   261  N  NH2  . ARG   A 1 46  ? -1.173 15.010  13.530 1.00 67.99 ?  151 ARG   A NH2  1 
ATOM   262  N  N    . ASP   A 1 47  ? 1.996  12.009  16.758 1.00 36.79 ?  152 ASP   A N    1 
ATOM   263  C  CA   . ASP   A 1 47  ? 0.914  11.060  16.536 1.00 38.55 ?  152 ASP   A CA   1 
ATOM   264  C  C    . ASP   A 1 47  ? 0.862  9.955   17.584 1.00 30.34 ?  152 ASP   A C    1 
ATOM   265  O  O    . ASP   A 1 47  ? -0.018 9.091   17.508 1.00 28.44 ?  152 ASP   A O    1 
ATOM   266  C  CB   . ASP   A 1 47  ? 1.031  10.448  15.137 1.00 47.71 ?  152 ASP   A CB   1 
ATOM   267  C  CG   . ASP   A 1 47  ? 1.001  11.499  14.041 1.00 57.22 ?  152 ASP   A CG   1 
ATOM   268  O  OD1  . ASP   A 1 47  ? 0.219  11.338  13.083 1.00 61.65 ?  152 ASP   A OD1  1 
ATOM   269  O  OD2  . ASP   A 1 47  ? 1.757  12.488  14.137 1.00 61.00 ?  152 ASP   A OD2  1 
ATOM   270  N  N    . PHE   A 1 48  ? 1.776  9.958   18.549 1.00 25.77 ?  153 PHE   A N    1 
ATOM   271  C  CA   . PHE   A 1 48  ? 1.712  9.030   19.665 1.00 22.49 ?  153 PHE   A CA   1 
ATOM   272  C  C    . PHE   A 1 48  ? 0.671  9.498   20.675 1.00 24.07 ?  153 PHE   A C    1 
ATOM   273  O  O    . PHE   A 1 48  ? 0.280  10.670  20.708 1.00 25.43 ?  153 PHE   A O    1 
ATOM   274  C  CB   . PHE   A 1 48  ? 3.065  8.916   20.375 1.00 22.36 ?  153 PHE   A CB   1 
ATOM   275  C  CG   . PHE   A 1 48  ? 4.204  8.496   19.486 1.00 25.33 ?  153 PHE   A CG   1 
ATOM   276  C  CD1  . PHE   A 1 48  ? 5.513  8.773   19.854 1.00 28.22 ?  153 PHE   A CD1  1 
ATOM   277  C  CD2  . PHE   A 1 48  ? 3.976  7.818   18.298 1.00 26.05 ?  153 PHE   A CD2  1 
ATOM   278  C  CE1  . PHE   A 1 48  ? 6.578  8.396   19.048 1.00 30.18 ?  153 PHE   A CE1  1 
ATOM   279  C  CE2  . PHE   A 1 48  ? 5.033  7.440   17.486 1.00 29.05 ?  153 PHE   A CE2  1 
ATOM   280  C  CZ   . PHE   A 1 48  ? 6.337  7.729   17.865 1.00 31.52 ?  153 PHE   A CZ   1 
ATOM   281  N  N    . ARG   A 1 49  ? 0.228  8.571   21.515 1.00 17.84 ?  154 ARG   A N    1 
ATOM   282  C  CA   . ARG   A 1 49  ? -0.518 8.983   22.688 1.00 21.45 ?  154 ARG   A CA   1 
ATOM   283  C  C    . ARG   A 1 49  ? 0.330  9.971   23.487 1.00 25.10 ?  154 ARG   A C    1 
ATOM   284  O  O    . ARG   A 1 49  ? 1.552  9.794   23.602 1.00 21.39 ?  154 ARG   A O    1 
ATOM   285  C  CB   . ARG   A 1 49  ? -0.908 7.773   23.538 1.00 18.88 ?  154 ARG   A CB   1 
ATOM   286  C  CG   . ARG   A 1 49  ? -2.010 6.930   22.893 1.00 19.77 ?  154 ARG   A CG   1 
ATOM   287  C  CD   . ARG   A 1 49  ? -2.229 5.618   23.632 1.00 20.20 ?  154 ARG   A CD   1 
ATOM   288  N  NE   . ARG   A 1 49  ? -1.145 4.675   23.385 1.00 18.06 ?  154 ARG   A NE   1 
ATOM   289  C  CZ   . ARG   A 1 49  ? -0.993 3.525   24.028 1.00 21.20 ?  154 ARG   A CZ   1 
ATOM   290  N  NH1  . ARG   A 1 49  ? -1.853 3.166   24.968 1.00 23.30 ?  154 ARG   A NH1  1 
ATOM   291  N  NH2  . ARG   A 1 49  ? 0.026  2.733   23.730 1.00 22.86 ?  154 ARG   A NH2  1 
ATOM   292  N  N    . PRO   A 1 50  ? -0.271 11.044  24.006 1.00 29.25 ?  155 PRO   A N    1 
ATOM   293  C  CA   . PRO   A 1 50  ? 0.531  12.129  24.557 1.00 32.17 ?  155 PRO   A CA   1 
ATOM   294  C  C    . PRO   A 1 50  ? 1.275  11.683  25.802 1.00 33.24 ?  155 PRO   A C    1 
ATOM   295  O  O    . PRO   A 1 50  ? 0.858  10.732  26.486 1.00 28.61 ?  155 PRO   A O    1 
ATOM   296  C  CB   . PRO   A 1 50  ? -0.515 13.209  24.888 1.00 36.17 ?  155 PRO   A CB   1 
ATOM   297  C  CG   . PRO   A 1 50  ? -1.792 12.452  25.054 1.00 35.68 ?  155 PRO   A CG   1 
ATOM   298  C  CD   . PRO   A 1 50  ? -1.713 11.340  24.054 1.00 34.63 ?  155 PRO   A CD   1 
ATOM   299  N  N    . PRO   A 1 51  ? 2.392  12.327  26.125 1.00 35.41 ?  156 PRO   A N    1 
ATOM   300  C  CA   . PRO   A 1 51  ? 3.042  12.053  27.406 1.00 34.45 ?  156 PRO   A CA   1 
ATOM   301  C  C    . PRO   A 1 51  ? 2.240  12.670  28.538 1.00 34.97 ?  156 PRO   A C    1 
ATOM   302  O  O    . PRO   A 1 51  ? 1.755  13.799  28.434 1.00 35.87 ?  156 PRO   A O    1 
ATOM   303  C  CB   . PRO   A 1 51  ? 4.415  12.716  27.259 1.00 33.69 ?  156 PRO   A CB   1 
ATOM   304  C  CG   . PRO   A 1 51  ? 4.177  13.829  26.300 1.00 35.63 ?  156 PRO   A CG   1 
ATOM   305  C  CD   . PRO   A 1 51  ? 3.116  13.342  25.340 1.00 34.17 ?  156 PRO   A CD   1 
ATOM   306  N  N    . VAL   A 1 52  ? 2.074  11.901  29.608 1.00 34.82 ?  157 VAL   A N    1 
ATOM   307  C  CA   . VAL   A 1 52  ? 1.432  12.371  30.829 1.00 38.16 ?  157 VAL   A CA   1 
ATOM   308  C  C    . VAL   A 1 52  ? 2.444  12.231  31.952 1.00 42.44 ?  157 VAL   A C    1 
ATOM   309  O  O    . VAL   A 1 52  ? 2.892  11.119  32.255 1.00 43.09 ?  157 VAL   A O    1 
ATOM   310  C  CB   . VAL   A 1 52  ? 0.147  11.593  31.149 1.00 32.95 ?  157 VAL   A CB   1 
ATOM   311  C  CG1  . VAL   A 1 52  ? -0.489 12.139  32.416 1.00 29.26 ?  157 VAL   A CG1  1 
ATOM   312  C  CG2  . VAL   A 1 52  ? -0.825 11.663  29.981 1.00 33.64 ?  157 VAL   A CG2  1 
ATOM   313  N  N    . ARG   A 1 53  ? 2.816  13.349  32.552 1.00 45.89 ?  158 ARG   A N    1 
ATOM   314  C  CA   . ARG   A 1 53  ? 3.766  13.369  33.659 1.00 51.58 ?  158 ARG   A CA   1 
ATOM   315  C  C    . ARG   A 1 53  ? 2.955  13.628  34.928 1.00 60.50 ?  158 ARG   A C    1 
ATOM   316  O  O    . ARG   A 1 53  ? 2.613  14.775  35.229 1.00 63.10 ?  158 ARG   A O    1 
ATOM   317  C  CB   . ARG   A 1 53  ? 4.849  14.410  33.395 1.00 49.51 ?  158 ARG   A CB   1 
ATOM   318  C  CG   . ARG   A 1 53  ? 5.526  14.171  32.042 1.00 46.72 ?  158 ARG   A CG   1 
ATOM   319  C  CD   . ARG   A 1 53  ? 6.711  15.083  31.768 1.00 47.18 ?  158 ARG   A CD   1 
ATOM   320  N  NE   . ARG   A 1 53  ? 7.619  14.501  30.778 1.00 45.78 ?  158 ARG   A NE   1 
ATOM   321  C  CZ   . ARG   A 1 53  ? 7.407  14.496  29.463 1.00 45.34 ?  158 ARG   A CZ   1 
ATOM   322  N  NH1  . ARG   A 1 53  ? 6.310  15.046  28.957 1.00 45.80 ?  158 ARG   A NH1  1 
ATOM   323  N  NH2  . ARG   A 1 53  ? 8.294  13.940  28.647 1.00 41.93 ?  158 ARG   A NH2  1 
ATOM   324  N  N    . MET   A 1 54  ? 2.661  12.545  35.659 1.00 66.26 ?  159 MET   A N    1 
ATOM   325  C  CA   . MET   A 1 54  ? 1.605  12.462  36.689 1.00 70.46 ?  159 MET   A CA   1 
ATOM   326  C  C    . MET   A 1 54  ? 1.184  13.781  37.327 1.00 70.41 ?  159 MET   A C    1 
ATOM   327  O  O    . MET   A 1 54  ? 0.004  14.130  37.307 1.00 70.36 ?  159 MET   A O    1 
ATOM   328  C  CB   . MET   A 1 54  ? 2.026  11.496  37.807 1.00 76.31 ?  159 MET   A CB   1 
ATOM   329  C  CG   . MET   A 1 54  ? 2.491  10.127  37.331 1.00 79.54 ?  159 MET   A CG   1 
ATOM   330  S  SD   . MET   A 1 54  ? 2.797  8.940   38.657 1.00 85.00 ?  159 MET   A SD   1 
ATOM   331  C  CE   . MET   A 1 54  ? 4.413  8.319   38.203 1.00 82.41 ?  159 MET   A CE   1 
ATOM   332  N  N    . SER   A 1 66  ? -2.663 4.478   38.639 1.00 64.61 ?  218 SER   A N    1 
ATOM   333  C  CA   . SER   A 1 66  ? -1.768 4.442   37.485 1.00 62.38 ?  218 SER   A CA   1 
ATOM   334  C  C    . SER   A 1 66  ? -0.502 5.274   37.695 1.00 59.96 ?  218 SER   A C    1 
ATOM   335  O  O    . SER   A 1 66  ? -0.388 6.380   37.168 1.00 61.08 ?  218 SER   A O    1 
ATOM   336  C  CB   . SER   A 1 66  ? -2.494 4.938   36.233 1.00 63.11 ?  218 SER   A CB   1 
ATOM   337  O  OG   . SER   A 1 66  ? -3.291 6.075   36.522 1.00 65.45 ?  218 SER   A OG   1 
ATOM   338  N  N    . PRO   A 1 67  ? 0.449  4.752   38.472 1.00 55.68 ?  219 PRO   A N    1 
ATOM   339  C  CA   . PRO   A 1 67  ? 1.781  5.359   38.536 1.00 54.49 ?  219 PRO   A CA   1 
ATOM   340  C  C    . PRO   A 1 67  ? 2.639  5.113   37.306 1.00 49.36 ?  219 PRO   A C    1 
ATOM   341  O  O    . PRO   A 1 67  ? 3.848  5.351   37.363 1.00 53.63 ?  219 PRO   A O    1 
ATOM   342  C  CB   . PRO   A 1 67  ? 2.392  4.680   39.769 1.00 52.74 ?  219 PRO   A CB   1 
ATOM   343  C  CG   . PRO   A 1 67  ? 1.788  3.325   39.766 1.00 52.66 ?  219 PRO   A CG   1 
ATOM   344  C  CD   . PRO   A 1 67  ? 0.372  3.521   39.279 1.00 53.79 ?  219 PRO   A CD   1 
ATOM   345  N  N    . LEU   A 1 68  ? 2.048  4.614   36.224 1.00 39.28 ?  220 LEU   A N    1 
ATOM   346  C  CA   . LEU   A 1 68  ? 2.759  4.399   34.974 1.00 31.15 ?  220 LEU   A CA   1 
ATOM   347  C  C    . LEU   A 1 68  ? 2.205  5.345   33.923 1.00 26.95 ?  220 LEU   A C    1 
ATOM   348  O  O    . LEU   A 1 68  ? 1.753  4.911   32.859 1.00 25.75 ?  220 LEU   A O    1 
ATOM   349  C  CB   . LEU   A 1 68  ? 2.630  2.947   34.514 1.00 28.53 ?  220 LEU   A CB   1 
ATOM   350  C  CG   . LEU   A 1 68  ? 3.238  1.893   35.436 1.00 32.07 ?  220 LEU   A CG   1 
ATOM   351  C  CD1  . LEU   A 1 68  ? 3.536  0.621   34.670 1.00 33.31 ?  220 LEU   A CD1  1 
ATOM   352  C  CD2  . LEU   A 1 68  ? 4.499  2.420   36.116 1.00 33.41 ?  220 LEU   A CD2  1 
ATOM   353  N  N    . SER   A 1 69  ? 2.238  6.643   34.221 1.00 26.30 ?  221 SER   A N    1 
ATOM   354  C  CA   . SER   A 1 69  ? 1.584  7.620   33.362 1.00 27.69 ?  221 SER   A CA   1 
ATOM   355  C  C    . SER   A 1 69  ? 2.288  7.791   32.022 1.00 21.89 ?  221 SER   A C    1 
ATOM   356  O  O    . SER   A 1 69  ? 1.654  8.242   31.063 1.00 24.42 ?  221 SER   A O    1 
ATOM   357  C  CB   . SER   A 1 69  ? 1.501  8.965   34.078 1.00 28.46 ?  221 SER   A CB   1 
ATOM   358  O  OG   . SER   A 1 69  ? 2.797  9.406   34.444 1.00 28.88 ?  221 SER   A OG   1 
ATOM   359  N  N    . MET   A 1 70  ? 3.573  7.457   31.932 1.00 19.96 ?  222 MET   A N    1 
ATOM   360  C  CA   . MET   A 1 70  ? 4.300  7.546   30.670 1.00 20.65 ?  222 MET   A CA   1 
ATOM   361  C  C    . MET   A 1 70  ? 4.235  6.261   29.853 1.00 17.55 ?  222 MET   A C    1 
ATOM   362  O  O    . MET   A 1 70  ? 4.769  6.226   28.740 1.00 20.98 ?  222 MET   A O    1 
ATOM   363  C  CB   . MET   A 1 70  ? 5.771  7.916   30.926 1.00 23.23 ?  222 MET   A CB   1 
ATOM   364  C  CG   . MET   A 1 70  ? 6.009  9.368   31.346 1.00 22.77 ?  222 MET   A CG   1 
ATOM   365  S  SD   . MET   A 1 70  ? 5.463  10.576  30.114 1.00 23.35 ?  222 MET   A SD   1 
ATOM   366  C  CE   . MET   A 1 70  ? 6.869  10.583  29.005 1.00 22.37 ?  222 MET   A CE   1 
ATOM   367  N  N    . LEU   A 1 71  ? 3.600  5.209   30.372 1.00 15.79 ?  223 LEU   A N    1 
ATOM   368  C  CA   . LEU   A 1 71  ? 3.576  3.930   29.663 1.00 17.82 ?  223 LEU   A CA   1 
ATOM   369  C  C    . LEU   A 1 71  ? 2.893  4.011   28.303 1.00 17.29 ?  223 LEU   A C    1 
ATOM   370  O  O    . LEU   A 1 71  ? 3.439  3.456   27.334 1.00 19.62 ?  223 LEU   A O    1 
ATOM   371  C  CB   . LEU   A 1 71  ? 2.921  2.860   30.542 1.00 21.30 ?  223 LEU   A CB   1 
ATOM   372  C  CG   . LEU   A 1 71  ? 2.988  1.444   29.964 1.00 17.98 ?  223 LEU   A CG   1 
ATOM   373  C  CD1  . LEU   A 1 71  ? 4.433  1.098   29.613 1.00 13.12 ?  223 LEU   A CD1  1 
ATOM   374  C  CD2  . LEU   A 1 71  ? 2.393  0.425   30.933 1.00 18.02 ?  223 LEU   A CD2  1 
ATOM   375  N  N    . PRO   A 1 72  ? 1.725  4.644   28.148 1.00 19.57 ?  224 PRO   A N    1 
ATOM   376  C  CA   . PRO   A 1 72  ? 1.151  4.743   26.794 1.00 19.71 ?  224 PRO   A CA   1 
ATOM   377  C  C    . PRO   A 1 72  ? 2.052  5.475   25.813 1.00 18.91 ?  224 PRO   A C    1 
ATOM   378  O  O    . PRO   A 1 72  ? 2.230  5.014   24.679 1.00 15.41 ?  224 PRO   A O    1 
ATOM   379  C  CB   . PRO   A 1 72  ? -0.170 5.484   27.035 1.00 17.34 ?  224 PRO   A CB   1 
ATOM   380  C  CG   . PRO   A 1 72  ? -0.533 5.133   28.445 1.00 21.46 ?  224 PRO   A CG   1 
ATOM   381  C  CD   . PRO   A 1 72  ? 0.775  5.127   29.173 1.00 20.27 ?  224 PRO   A CD   1 
ATOM   382  N  N    . HIS   A 1 73  ? 2.625  6.611   26.215 1.00 22.71 ?  225 HIS   A N    1 
ATOM   383  C  CA   . HIS   A 1 73  ? 3.496  7.354   25.313 1.00 23.20 ?  225 HIS   A CA   1 
ATOM   384  C  C    . HIS   A 1 73  ? 4.738  6.545   24.956 1.00 25.10 ?  225 HIS   A C    1 
ATOM   385  O  O    . HIS   A 1 73  ? 5.067  6.380   23.774 1.00 19.92 ?  225 HIS   A O    1 
ATOM   386  C  CB   . HIS   A 1 73  ? 3.894  8.695   25.932 1.00 22.54 ?  225 HIS   A CB   1 
ATOM   387  C  CG   . HIS   A 1 73  ? 4.665  9.577   24.998 1.00 23.29 ?  225 HIS   A CG   1 
ATOM   388  N  ND1  . HIS   A 1 73  ? 4.116  10.100  23.848 1.00 23.60 ?  225 HIS   A ND1  1 
ATOM   389  C  CD2  . HIS   A 1 73  ? 5.950  10.004  25.030 1.00 23.78 ?  225 HIS   A CD2  1 
ATOM   390  C  CE1  . HIS   A 1 73  ? 5.025  10.822  23.217 1.00 24.13 ?  225 HIS   A CE1  1 
ATOM   391  N  NE2  . HIS   A 1 73  ? 6.148  10.779  23.913 1.00 24.28 ?  225 HIS   A NE2  1 
ATOM   392  N  N    . LEU   A 1 74  ? 5.441  6.024   25.968 1.00 23.47 ?  226 LEU   A N    1 
ATOM   393  C  CA   . LEU   A 1 74  ? 6.697  5.333   25.693 1.00 21.89 ?  226 LEU   A CA   1 
ATOM   394  C  C    . LEU   A 1 74  ? 6.466  4.000   24.990 1.00 17.10 ?  226 LEU   A C    1 
ATOM   395  O  O    . LEU   A 1 74  ? 7.313  3.572   24.199 1.00 18.57 ?  226 LEU   A O    1 
ATOM   396  C  CB   . LEU   A 1 74  ? 7.496  5.152   26.988 1.00 18.14 ?  226 LEU   A CB   1 
ATOM   397  C  CG   . LEU   A 1 74  ? 7.941  6.490   27.599 1.00 20.58 ?  226 LEU   A CG   1 
ATOM   398  C  CD1  . LEU   A 1 74  ? 8.840  6.312   28.832 1.00 21.84 ?  226 LEU   A CD1  1 
ATOM   399  C  CD2  . LEU   A 1 74  ? 8.629  7.369   26.551 1.00 20.74 ?  226 LEU   A CD2  1 
ATOM   400  N  N    . ALA   A 1 75  ? 5.329  3.343   25.242 1.00 16.63 ?  227 ALA   A N    1 
ATOM   401  C  CA   . ALA   A 1 75  ? 4.984  2.149   24.473 1.00 14.26 ?  227 ALA   A CA   1 
ATOM   402  C  C    . ALA   A 1 75  ? 4.843  2.478   22.993 1.00 14.44 ?  227 ALA   A C    1 
ATOM   403  O  O    . ALA   A 1 75  ? 5.345  1.747   22.131 1.00 15.16 ?  227 ALA   A O    1 
ATOM   404  C  CB   . ALA   A 1 75  ? 3.693  1.525   25.000 1.00 16.24 ?  227 ALA   A CB   1 
ATOM   405  N  N    . ASP   A 1 76  ? 4.152  3.576   22.677 1.00 13.67 ?  228 ASP   A N    1 
ATOM   406  C  CA   . ASP   A 1 76  ? 4.039  3.982   21.280 1.00 14.57 ?  228 ASP   A CA   1 
ATOM   407  C  C    . ASP   A 1 76  ? 5.408  4.309   20.706 1.00 16.74 ?  228 ASP   A C    1 
ATOM   408  O  O    . ASP   A 1 76  ? 5.694  3.995   19.545 1.00 14.83 ?  228 ASP   A O    1 
ATOM   409  C  CB   . ASP   A 1 76  ? 3.096  5.178   21.143 1.00 15.30 ?  228 ASP   A CB   1 
ATOM   410  C  CG   . ASP   A 1 76  ? 1.631  4.803   21.334 1.00 18.08 ?  228 ASP   A CG   1 
ATOM   411  O  OD1  . ASP   A 1 76  ? 1.301  3.595   21.383 1.00 17.95 ?  228 ASP   A OD1  1 
ATOM   412  O  OD2  . ASP   A 1 76  ? 0.804  5.730   21.433 1.00 20.05 ?  228 ASP   A OD2  1 
ATOM   413  N  N    . LEU   A 1 77  ? 6.282  4.908   21.520 1.00 16.22 ?  229 LEU   A N    1 
ATOM   414  C  CA   . LEU   A 1 77  ? 7.625  5.242   21.057 1.00 15.76 ?  229 LEU   A CA   1 
ATOM   415  C  C    . LEU   A 1 77  ? 8.427  3.984   20.736 1.00 14.83 ?  229 LEU   A C    1 
ATOM   416  O  O    . LEU   A 1 77  ? 9.042  3.878   19.668 1.00 15.01 ?  229 LEU   A O    1 
ATOM   417  C  CB   . LEU   A 1 77  ? 8.335  6.089   22.113 1.00 16.41 ?  229 LEU   A CB   1 
ATOM   418  C  CG   . LEU   A 1 77  ? 9.828  6.361   21.920 1.00 19.24 ?  229 LEU   A CG   1 
ATOM   419  C  CD1  . LEU   A 1 77  ? 10.074 7.025   20.573 1.00 18.96 ?  229 LEU   A CD1  1 
ATOM   420  C  CD2  . LEU   A 1 77  ? 10.399 7.204   23.079 1.00 18.22 ?  229 LEU   A CD2  1 
ATOM   421  N  N    . VAL   A 1 78  ? 8.424  3.018   21.655 1.00 14.42 ?  230 VAL   A N    1 
ATOM   422  C  CA   . VAL   A 1 78  ? 9.125  1.755   21.437 1.00 8.86  ?  230 VAL   A CA   1 
ATOM   423  C  C    . VAL   A 1 78  ? 8.582  1.051   20.199 1.00 18.51 ?  230 VAL   A C    1 
ATOM   424  O  O    . VAL   A 1 78  ? 9.346  0.557   19.361 1.00 17.95 ?  230 VAL   A O    1 
ATOM   425  C  CB   . VAL   A 1 78  ? 9.009  0.865   22.687 1.00 14.60 ?  230 VAL   A CB   1 
ATOM   426  C  CG1  . VAL   A 1 78  ? 9.451  -0.559  22.381 1.00 11.27 ?  230 VAL   A CG1  1 
ATOM   427  C  CG2  . VAL   A 1 78  ? 9.801  1.468   23.853 1.00 9.16  ?  230 VAL   A CG2  1 
ATOM   428  N  N    . SER   A 1 79  ? 7.248  0.996   20.071 1.00 17.89 ?  231 SER   A N    1 
ATOM   429  C  CA   . SER   A 1 79  ? 6.616  0.380   18.900 1.00 12.94 ?  231 SER   A CA   1 
ATOM   430  C  C    . SER   A 1 79  ? 7.075  1.042   17.608 1.00 13.76 ?  231 SER   A C    1 
ATOM   431  O  O    . SER   A 1 79  ? 7.411  0.362   16.630 1.00 14.21 ?  231 SER   A O    1 
ATOM   432  C  CB   . SER   A 1 79  ? 5.093  0.459   19.013 1.00 13.41 ?  231 SER   A CB   1 
ATOM   433  O  OG   . SER   A 1 79  ? 4.472  -0.563  18.243 1.00 14.39 ?  231 SER   A OG   1 
ATOM   434  N  N    . TYR   A 1 80  ? 7.067  2.376   17.579 1.00 11.95 ?  232 TYR   A N    1 
ATOM   435  C  CA   . TYR   A 1 80  ? 7.585  3.125   16.436 1.00 15.49 ?  232 TYR   A CA   1 
ATOM   436  C  C    . TYR   A 1 80  ? 9.047  2.779   16.170 1.00 15.55 ?  232 TYR   A C    1 
ATOM   437  O  O    . TYR   A 1 80  ? 9.457  2.606   15.016 1.00 14.75 ?  232 TYR   A O    1 
ATOM   438  C  CB   . TYR   A 1 80  ? 7.399  4.616   16.722 1.00 18.55 ?  232 TYR   A CB   1 
ATOM   439  C  CG   . TYR   A 1 80  ? 8.008  5.605   15.752 1.00 24.41 ?  232 TYR   A CG   1 
ATOM   440  C  CD1  . TYR   A 1 80  ? 7.263  6.126   14.702 1.00 26.25 ?  232 TYR   A CD1  1 
ATOM   441  C  CD2  . TYR   A 1 80  ? 9.306  6.067   15.925 1.00 28.31 ?  232 TYR   A CD2  1 
ATOM   442  C  CE1  . TYR   A 1 80  ? 7.805  7.054   13.830 1.00 26.14 ?  232 TYR   A CE1  1 
ATOM   443  C  CE2  . TYR   A 1 80  ? 9.858  6.994   15.056 1.00 27.29 ?  232 TYR   A CE2  1 
ATOM   444  C  CZ   . TYR   A 1 80  ? 9.103  7.486   14.013 1.00 28.64 ?  232 TYR   A CZ   1 
ATOM   445  O  OH   . TYR   A 1 80  ? 9.648  8.409   13.146 1.00 32.15 ?  232 TYR   A OH   1 
ATOM   446  N  N    . SER   A 1 81  ? 9.840  2.639   17.233 1.00 14.30 ?  233 SER   A N    1 
ATOM   447  C  CA   . SER   A 1 81  ? 11.269 2.390   17.075 1.00 9.03  ?  233 SER   A CA   1 
ATOM   448  C  C    . SER   A 1 81  ? 11.535 0.988   16.537 1.00 11.67 ?  233 SER   A C    1 
ATOM   449  O  O    . SER   A 1 81  ? 12.474 0.783   15.757 1.00 14.21 ?  233 SER   A O    1 
ATOM   450  C  CB   . SER   A 1 81  ? 11.974 2.592   18.416 1.00 9.73  ?  233 SER   A CB   1 
ATOM   451  O  OG   . SER   A 1 81  ? 11.813 3.924   18.882 1.00 13.14 ?  233 SER   A OG   1 
ATOM   452  N  N    . ILE   A 1 82  ? 10.743 0.006   16.970 1.00 8.23  ?  234 ILE   A N    1 
ATOM   453  C  CA   . ILE   A 1 82  ? 10.860 -1.344  16.423 1.00 12.09 ?  234 ILE   A CA   1 
ATOM   454  C  C    . ILE   A 1 82  ? 10.673 -1.318  14.910 1.00 15.47 ?  234 ILE   A C    1 
ATOM   455  O  O    . ILE   A 1 82  ? 11.443 -1.927  14.156 1.00 12.84 ?  234 ILE   A O    1 
ATOM   456  C  CB   . ILE   A 1 82  ? 9.847  -2.284  17.104 1.00 12.29 ?  234 ILE   A CB   1 
ATOM   457  C  CG1  . ILE   A 1 82  ? 10.223 -2.514  18.576 1.00 12.28 ?  234 ILE   A CG1  1 
ATOM   458  C  CG2  . ILE   A 1 82  ? 9.747  -3.616  16.369 1.00 10.04 ?  234 ILE   A CG2  1 
ATOM   459  C  CD1  . ILE   A 1 82  ? 9.113  -3.190  19.385 1.00 8.27  ?  234 ILE   A CD1  1 
ATOM   460  N  N    . GLN   A 1 83  ? 9.654  -0.594  14.443 1.00 14.23 ?  235 GLN   A N    1 
ATOM   461  C  CA   . GLN   A 1 83  ? 9.404  -0.513  13.009 1.00 19.40 ?  235 GLN   A CA   1 
ATOM   462  C  C    . GLN   A 1 83  ? 10.579 0.130   12.281 1.00 17.76 ?  235 GLN   A C    1 
ATOM   463  O  O    . GLN   A 1 83  ? 10.921 -0.270  11.163 1.00 14.94 ?  235 GLN   A O    1 
ATOM   464  C  CB   . GLN   A 1 83  ? 8.114  0.264   12.756 1.00 23.42 ?  235 GLN   A CB   1 
ATOM   465  C  CG   . GLN   A 1 83  ? 7.919  0.679   11.315 1.00 31.79 ?  235 GLN   A CG   1 
ATOM   466  C  CD   . GLN   A 1 83  ? 6.464  0.645   10.913 1.00 39.33 ?  235 GLN   A CD   1 
ATOM   467  O  OE1  . GLN   A 1 83  ? 5.573  0.566   11.766 1.00 37.30 ?  235 GLN   A OE1  1 
ATOM   468  N  NE2  . GLN   A 1 83  ? 6.210  0.702   9.608  1.00 42.35 ?  235 GLN   A NE2  1 
ATOM   469  N  N    . LYS   A 1 84  ? 11.212 1.128   12.902 1.00 18.40 ?  236 LYS   A N    1 
ATOM   470  C  CA   . LYS   A 1 84  ? 12.386 1.745   12.294 1.00 21.97 ?  236 LYS   A CA   1 
ATOM   471  C  C    . LYS   A 1 84  ? 13.558 0.771   12.250 1.00 22.16 ?  236 LYS   A C    1 
ATOM   472  O  O    . LYS   A 1 84  ? 14.319 0.753   11.274 1.00 20.30 ?  236 LYS   A O    1 
ATOM   473  C  CB   . LYS   A 1 84  ? 12.770 3.014   13.058 1.00 20.00 ?  236 LYS   A CB   1 
ATOM   474  C  CG   . LYS   A 1 84  ? 11.731 4.131   12.979 1.00 20.15 ?  236 LYS   A CG   1 
ATOM   475  C  CD   . LYS   A 1 84  ? 11.419 4.504   11.539 1.00 20.52 ?  236 LYS   A CD   1 
ATOM   476  C  CE   . LYS   A 1 84  ? 10.659 5.813   11.477 1.00 20.87 ?  236 LYS   A CE   1 
ATOM   477  N  NZ   . LYS   A 1 84  ? 11.474 6.953   11.976 1.00 22.19 ?  236 LYS   A NZ   1 
ATOM   478  N  N    . VAL   A 1 85  ? 13.718 -0.045  13.296 1.00 17.77 ?  237 VAL   A N    1 
ATOM   479  C  CA   . VAL   A 1 85  ? 14.823 -0.999  13.339 1.00 17.91 ?  237 VAL   A CA   1 
ATOM   480  C  C    . VAL   A 1 85  ? 14.650 -2.069  12.265 1.00 16.64 ?  237 VAL   A C    1 
ATOM   481  O  O    . VAL   A 1 85  ? 15.624 -2.487  11.624 1.00 15.71 ?  237 VAL   A O    1 
ATOM   482  C  CB   . VAL   A 1 85  ? 14.945 -1.613  14.749 1.00 15.70 ?  237 VAL   A CB   1 
ATOM   483  C  CG1  . VAL   A 1 85  ? 15.913 -2.784  14.742 1.00 13.89 ?  237 VAL   A CG1  1 
ATOM   484  C  CG2  . VAL   A 1 85  ? 15.412 -0.562  15.746 1.00 15.07 ?  237 VAL   A CG2  1 
ATOM   485  N  N    . ILE   A 1 86  ? 13.411 -2.516  12.038 1.00 15.03 ?  238 ILE   A N    1 
ATOM   486  C  CA   . ILE   A 1 86  ? 13.152 -3.511  10.996 1.00 13.40 ?  238 ILE   A CA   1 
ATOM   487  C  C    . ILE   A 1 86  ? 13.450 -2.934  9.617  1.00 16.27 ?  238 ILE   A C    1 
ATOM   488  O  O    . ILE   A 1 86  ? 13.944 -3.638  8.727  1.00 20.18 ?  238 ILE   A O    1 
ATOM   489  C  CB   . ILE   A 1 86  ? 11.702 -4.025  11.091 1.00 15.89 ?  238 ILE   A CB   1 
ATOM   490  C  CG1  . ILE   A 1 86  ? 11.471 -4.780  12.404 1.00 12.66 ?  238 ILE   A CG1  1 
ATOM   491  C  CG2  . ILE   A 1 86  ? 11.343 -4.929  9.893  1.00 11.71 ?  238 ILE   A CG2  1 
ATOM   492  C  CD1  . ILE   A 1 86  ? 10.006 -4.799  12.831 1.00 12.04 ?  238 ILE   A CD1  1 
ATOM   493  N  N    . GLY   A 1 87  ? 13.148 -1.649  9.412  1.00 13.76 ?  239 GLY   A N    1 
ATOM   494  C  CA   . GLY   A 1 87  ? 13.419 -1.035  8.124  1.00 11.72 ?  239 GLY   A CA   1 
ATOM   495  C  C    . GLY   A 1 87  ? 14.904 -0.872  7.874  1.00 14.30 ?  239 GLY   A C    1 
ATOM   496  O  O    . GLY   A 1 87  ? 15.389 -1.102  6.761  1.00 14.53 ?  239 GLY   A O    1 
ATOM   497  N  N    . PHE   A 1 88  ? 15.648 -0.478  8.908  1.00 14.95 ?  240 PHE   A N    1 
ATOM   498  C  CA   . PHE   A 1 88  ? 17.099 -0.429  8.805  1.00 12.59 ?  240 PHE   A CA   1 
ATOM   499  C  C    . PHE   A 1 88  ? 17.669 -1.811  8.522  1.00 15.51 ?  240 PHE   A C    1 
ATOM   500  O  O    . PHE   A 1 88  ? 18.475 -1.986  7.603  1.00 18.60 ?  240 PHE   A O    1 
ATOM   501  C  CB   . PHE   A 1 88  ? 17.684 0.148   10.094 1.00 14.88 ?  240 PHE   A CB   1 
ATOM   502  C  CG   . PHE   A 1 88  ? 19.186 0.129   10.152 1.00 18.49 ?  240 PHE   A CG   1 
ATOM   503  C  CD1  . PHE   A 1 88  ? 19.930 1.113   9.519  1.00 17.19 ?  240 PHE   A CD1  1 
ATOM   504  C  CD2  . PHE   A 1 88  ? 19.854 -0.855  10.870 1.00 18.38 ?  240 PHE   A CD2  1 
ATOM   505  C  CE1  . PHE   A 1 88  ? 21.310 1.109   9.587  1.00 18.59 ?  240 PHE   A CE1  1 
ATOM   506  C  CE2  . PHE   A 1 88  ? 21.237 -0.863  10.946 1.00 15.08 ?  240 PHE   A CE2  1 
ATOM   507  C  CZ   . PHE   A 1 88  ? 21.964 0.118   10.303 1.00 18.61 ?  240 PHE   A CZ   1 
ATOM   508  N  N    . ALA   A 1 89  ? 17.246 -2.812  9.301  1.00 15.67 ?  241 ALA   A N    1 
ATOM   509  C  CA   . ALA   A 1 89  ? 17.831 -4.144  9.178  1.00 15.64 ?  241 ALA   A CA   1 
ATOM   510  C  C    . ALA   A 1 89  ? 17.647 -4.707  7.776  1.00 19.39 ?  241 ALA   A C    1 
ATOM   511  O  O    . ALA   A 1 89  ? 18.548 -5.367  7.243  1.00 18.10 ?  241 ALA   A O    1 
ATOM   512  C  CB   . ALA   A 1 89  ? 17.221 -5.088  10.215 1.00 11.62 ?  241 ALA   A CB   1 
ATOM   513  N  N    A LYS   A 1 90  ? 16.489 -4.451  7.160  0.49 18.14 ?  242 LYS   A N    1 
ATOM   514  N  N    B LYS   A 1 90  ? 16.493 -4.443  7.156  0.51 18.10 ?  242 LYS   A N    1 
ATOM   515  C  CA   A LYS   A 1 90  ? 16.209 -4.985  5.832  0.49 20.52 ?  242 LYS   A CA   1 
ATOM   516  C  CA   B LYS   A 1 90  ? 16.216 -4.987  5.831  0.51 20.52 ?  242 LYS   A CA   1 
ATOM   517  C  C    A LYS   A 1 90  ? 17.179 -4.467  4.780  0.49 19.99 ?  242 LYS   A C    1 
ATOM   518  C  C    B LYS   A 1 90  ? 17.208 -4.484  4.790  0.51 19.97 ?  242 LYS   A C    1 
ATOM   519  O  O    A LYS   A 1 90  ? 17.356 -5.117  3.745  0.49 20.73 ?  242 LYS   A O    1 
ATOM   520  O  O    B LYS   A 1 90  ? 17.432 -5.153  3.776  0.51 20.80 ?  242 LYS   A O    1 
ATOM   521  C  CB   A LYS   A 1 90  ? 14.773 -4.647  5.421  0.49 23.02 ?  242 LYS   A CB   1 
ATOM   522  C  CB   B LYS   A 1 90  ? 14.791 -4.634  5.404  0.51 23.01 ?  242 LYS   A CB   1 
ATOM   523  C  CG   A LYS   A 1 90  ? 13.738 -5.620  5.958  0.49 26.44 ?  242 LYS   A CG   1 
ATOM   524  C  CG   B LYS   A 1 90  ? 13.718 -5.460  6.091  0.51 26.35 ?  242 LYS   A CG   1 
ATOM   525  C  CD   A LYS   A 1 90  ? 12.325 -5.041  5.922  0.49 27.80 ?  242 LYS   A CD   1 
ATOM   526  C  CD   B LYS   A 1 90  ? 12.380 -4.733  6.099  0.51 27.59 ?  242 LYS   A CD   1 
ATOM   527  C  CE   A LYS   A 1 90  ? 12.041 -4.315  4.614  0.49 28.95 ?  242 LYS   A CE   1 
ATOM   528  C  CE   B LYS   A 1 90  ? 11.847 -4.544  4.690  0.51 28.92 ?  242 LYS   A CE   1 
ATOM   529  N  NZ   A LYS   A 1 90  ? 11.047 -3.215  4.796  0.49 28.65 ?  242 LYS   A NZ   1 
ATOM   530  N  NZ   B LYS   A 1 90  ? 11.199 -5.782  4.185  0.51 28.55 ?  242 LYS   A NZ   1 
ATOM   531  N  N    . MET   A 1 91  ? 17.807 -3.319  5.020  1.00 17.38 ?  243 MET   A N    1 
ATOM   532  C  CA   . MET   A 1 91  ? 18.740 -2.722  4.079  1.00 19.33 ?  243 MET   A CA   1 
ATOM   533  C  C    . MET   A 1 91  ? 20.194 -3.069  4.377  1.00 22.02 ?  243 MET   A C    1 
ATOM   534  O  O    . MET   A 1 91  ? 21.086 -2.613  3.652  1.00 18.63 ?  243 MET   A O    1 
ATOM   535  C  CB   . MET   A 1 91  ? 18.542 -1.203  4.066  1.00 21.83 ?  243 MET   A CB   1 
ATOM   536  C  CG   . MET   A 1 91  ? 17.143 -0.796  3.580  1.00 25.83 ?  243 MET   A CG   1 
ATOM   537  S  SD   . MET   A 1 91  ? 16.920 0.985   3.388  1.00 31.13 ?  243 MET   A SD   1 
ATOM   538  C  CE   . MET   A 1 91  ? 16.172 1.423   4.959  1.00 27.16 ?  243 MET   A CE   1 
ATOM   539  N  N    . ILE   A 1 92  ? 20.453 -3.856  5.420  1.00 18.96 ?  244 ILE   A N    1 
ATOM   540  C  CA   . ILE   A 1 92  ? 21.802 -4.319  5.734  1.00 19.87 ?  244 ILE   A CA   1 
ATOM   541  C  C    . ILE   A 1 92  ? 22.235 -5.294  4.648  1.00 23.00 ?  244 ILE   A C    1 
ATOM   542  O  O    . ILE   A 1 92  ? 21.559 -6.310  4.438  1.00 18.52 ?  244 ILE   A O    1 
ATOM   543  C  CB   . ILE   A 1 92  ? 21.870 -4.993  7.115  1.00 19.16 ?  244 ILE   A CB   1 
ATOM   544  C  CG1  . ILE   A 1 92  ? 21.494 -4.012  8.229  1.00 15.17 ?  244 ILE   A CG1  1 
ATOM   545  C  CG2  . ILE   A 1 92  ? 23.262 -5.579  7.353  1.00 20.95 ?  244 ILE   A CG2  1 
ATOM   546  C  CD1  . ILE   A 1 92  ? 21.320 -4.680  9.560  1.00 14.08 ?  244 ILE   A CD1  1 
ATOM   547  N  N    . PRO   A 1 93  ? 23.347 -5.046  3.956  1.00 26.25 ?  245 PRO   A N    1 
ATOM   548  C  CA   . PRO   A 1 93  ? 23.786 -5.972  2.899  1.00 26.33 ?  245 PRO   A CA   1 
ATOM   549  C  C    . PRO   A 1 93  ? 23.957 -7.381  3.442  1.00 27.86 ?  245 PRO   A C    1 
ATOM   550  O  O    . PRO   A 1 93  ? 24.710 -7.615  4.394  1.00 28.10 ?  245 PRO   A O    1 
ATOM   551  C  CB   . PRO   A 1 93  ? 25.120 -5.374  2.437  1.00 27.97 ?  245 PRO   A CB   1 
ATOM   552  C  CG   . PRO   A 1 93  ? 25.053 -3.931  2.834  1.00 29.21 ?  245 PRO   A CG   1 
ATOM   553  C  CD   . PRO   A 1 93  ? 24.270 -3.909  4.116  1.00 28.98 ?  245 PRO   A CD   1 
ATOM   554  N  N    . GLY   A 1 94  ? 23.231 -8.321  2.840  1.00 25.13 ?  246 GLY   A N    1 
ATOM   555  C  CA   . GLY   A 1 94  ? 23.270 -9.712  3.229  1.00 26.11 ?  246 GLY   A CA   1 
ATOM   556  C  C    . GLY   A 1 94  ? 22.092 -10.167 4.064  1.00 25.38 ?  246 GLY   A C    1 
ATOM   557  O  O    . GLY   A 1 94  ? 21.788 -11.366 4.079  1.00 26.38 ?  246 GLY   A O    1 
ATOM   558  N  N    . PHE   A 1 95  ? 21.418 -9.241  4.754  1.00 22.11 ?  247 PHE   A N    1 
ATOM   559  C  CA   . PHE   A 1 95  ? 20.317 -9.622  5.632  1.00 24.77 ?  247 PHE   A CA   1 
ATOM   560  C  C    . PHE   A 1 95  ? 19.205 -10.327 4.863  1.00 29.42 ?  247 PHE   A C    1 
ATOM   561  O  O    . PHE   A 1 95  ? 18.587 -11.269 5.376  1.00 29.39 ?  247 PHE   A O    1 
ATOM   562  C  CB   . PHE   A 1 95  ? 19.771 -8.391  6.347  1.00 20.25 ?  247 PHE   A CB   1 
ATOM   563  C  CG   . PHE   A 1 95  ? 18.808 -8.708  7.445  1.00 19.86 ?  247 PHE   A CG   1 
ATOM   564  C  CD1  . PHE   A 1 95  ? 19.255 -9.248  8.643  1.00 22.42 ?  247 PHE   A CD1  1 
ATOM   565  C  CD2  . PHE   A 1 95  ? 17.451 -8.463  7.287  1.00 22.68 ?  247 PHE   A CD2  1 
ATOM   566  C  CE1  . PHE   A 1 95  ? 18.367 -9.539  9.663  1.00 20.85 ?  247 PHE   A CE1  1 
ATOM   567  C  CE2  . PHE   A 1 95  ? 16.555 -8.748  8.307  1.00 22.44 ?  247 PHE   A CE2  1 
ATOM   568  C  CZ   . PHE   A 1 95  ? 17.015 -9.287  9.493  1.00 22.64 ?  247 PHE   A CZ   1 
ATOM   569  N  N    A ARG   A 1 96  ? 18.945 -9.862  3.631  0.54 31.31 ?  248 ARG   A N    1 
ATOM   570  N  N    B ARG   A 1 96  ? 18.924 -9.906  3.637  0.46 31.37 ?  248 ARG   A N    1 
ATOM   571  C  CA   A ARG   A 1 96  ? 17.947 -10.461 2.750  0.54 33.64 ?  248 ARG   A CA   1 
ATOM   572  C  CA   B ARG   A 1 96  ? 17.829 -10.584 2.955  0.46 33.58 ?  248 ARG   A CA   1 
ATOM   573  C  C    A ARG   A 1 96  ? 18.251 -11.925 2.464  0.54 35.40 ?  248 ARG   A C    1 
ATOM   574  C  C    B ARG   A 1 96  ? 18.243 -11.918 2.335  0.46 35.37 ?  248 ARG   A C    1 
ATOM   575  O  O    A ARG   A 1 96  ? 17.329 -12.738 2.331  0.54 35.56 ?  248 ARG   A O    1 
ATOM   576  O  O    B ARG   A 1 96  ? 17.374 -12.643 1.844  0.46 36.01 ?  248 ARG   A O    1 
ATOM   577  C  CB   A ARG   A 1 96  ? 17.874 -9.672  1.434  0.54 33.73 ?  248 ARG   A CB   1 
ATOM   578  C  CB   B ARG   A 1 96  ? 17.204 -9.656  1.910  0.46 33.64 ?  248 ARG   A CB   1 
ATOM   579  C  CG   A ARG   A 1 96  ? 19.190 -9.616  0.631  0.54 34.84 ?  248 ARG   A CG   1 
ATOM   580  C  CG   B ARG   A 1 96  ? 16.437 -8.490  2.547  0.46 30.35 ?  248 ARG   A CG   1 
ATOM   581  C  CD   A ARG   A 1 96  ? 19.132 -8.620  -0.535 0.54 35.00 ?  248 ARG   A CD   1 
ATOM   582  C  CD   B ARG   A 1 96  ? 15.006 -8.375  2.040  0.46 28.47 ?  248 ARG   A CD   1 
ATOM   583  N  NE   A ARG   A 1 96  ? 20.377 -8.595  -1.307 0.54 36.78 ?  248 ARG   A NE   1 
ATOM   584  N  NE   B ARG   A 1 96  ? 14.157 -9.479  2.486  0.46 27.46 ?  248 ARG   A NE   1 
ATOM   585  C  CZ   A ARG   A 1 96  ? 20.533 -7.979  -2.479 0.54 36.83 ?  248 ARG   A CZ   1 
ATOM   586  C  CZ   B ARG   A 1 96  ? 13.529 -9.516  3.656  0.46 24.21 ?  248 ARG   A CZ   1 
ATOM   587  N  NH1  A ARG   A 1 96  ? 19.522 -7.324  -3.036 0.54 36.88 ?  248 ARG   A NH1  1 
ATOM   588  N  NH1  B ARG   A 1 96  ? 12.777 -10.560 3.973  0.46 23.19 ?  248 ARG   A NH1  1 
ATOM   589  N  NH2  A ARG   A 1 96  ? 21.706 -8.016  -3.098 0.54 37.72 ?  248 ARG   A NH2  1 
ATOM   590  N  NH2  B ARG   A 1 96  ? 13.651 -8.510  4.511  0.46 23.58 ?  248 ARG   A NH2  1 
ATOM   591  N  N    . ASP   A 1 97  ? 19.531 -12.278 2.375  1.00 36.03 ?  249 ASP   A N    1 
ATOM   592  C  CA   . ASP   A 1 97  ? 19.940 -13.630 2.016  1.00 39.89 ?  249 ASP   A CA   1 
ATOM   593  C  C    . ASP   A 1 97  ? 19.646 -14.647 3.112  1.00 40.66 ?  249 ASP   A C    1 
ATOM   594  O  O    . ASP   A 1 97  ? 19.693 -15.852 2.843  1.00 44.35 ?  249 ASP   A O    1 
ATOM   595  C  CB   . ASP   A 1 97  ? 21.433 -13.661 1.685  1.00 44.72 ?  249 ASP   A CB   1 
ATOM   596  C  CG   . ASP   A 1 97  ? 21.778 -12.815 0.477  1.00 47.71 ?  249 ASP   A CG   1 
ATOM   597  O  OD1  . ASP   A 1 97  ? 20.887 -12.607 -0.374 1.00 48.84 ?  249 ASP   A OD1  1 
ATOM   598  O  OD2  . ASP   A 1 97  ? 22.939 -12.355 0.383  1.00 47.08 ?  249 ASP   A OD2  1 
ATOM   599  N  N    . LEU   A 1 98  ? 19.359 -14.197 4.331  1.00 35.82 ?  250 LEU   A N    1 
ATOM   600  C  CA   . LEU   A 1 98  ? 19.007 -15.106 5.407  1.00 29.36 ?  250 LEU   A CA   1 
ATOM   601  C  C    . LEU   A 1 98  ? 17.588 -15.630 5.227  1.00 25.49 ?  250 LEU   A C    1 
ATOM   602  O  O    . LEU   A 1 98  ? 16.740 -14.989 4.606  1.00 23.45 ?  250 LEU   A O    1 
ATOM   603  C  CB   . LEU   A 1 98  ? 19.116 -14.401 6.758  1.00 27.22 ?  250 LEU   A CB   1 
ATOM   604  C  CG   . LEU   A 1 98  ? 20.480 -13.849 7.169  1.00 21.99 ?  250 LEU   A CG   1 
ATOM   605  C  CD1  . LEU   A 1 98  ? 20.337 -12.957 8.397  1.00 20.08 ?  250 LEU   A CD1  1 
ATOM   606  C  CD2  . LEU   A 1 98  ? 21.430 -14.993 7.444  1.00 20.63 ?  250 LEU   A CD2  1 
ATOM   607  N  N    . THR   A 1 99  ? 17.332 -16.804 5.799  1.00 25.37 ?  251 THR   A N    1 
ATOM   608  C  CA   . THR   A 1 99  ? 15.979 -17.330 5.850  1.00 23.35 ?  251 THR   A CA   1 
ATOM   609  C  C    . THR   A 1 99  ? 15.082 -16.405 6.666  1.00 25.72 ?  251 THR   A C    1 
ATOM   610  O  O    . THR   A 1 99  ? 15.548 -15.577 7.457  1.00 26.93 ?  251 THR   A O    1 
ATOM   611  C  CB   . THR   A 1 99  ? 15.967 -18.733 6.461  1.00 25.97 ?  251 THR   A CB   1 
ATOM   612  O  OG1  . THR   A 1 99  ? 16.540 -18.691 7.775  1.00 24.93 ?  251 THR   A OG1  1 
ATOM   613  C  CG2  . THR   A 1 99  ? 16.765 -19.707 5.591  1.00 26.30 ?  251 THR   A CG2  1 
ATOM   614  N  N    . SER   A 1 100 ? 13.769 -16.558 6.467  1.00 23.25 ?  252 SER   A N    1 
ATOM   615  C  CA   . SER   A 1 100 ? 12.816 -15.745 7.212  1.00 23.76 ?  252 SER   A CA   1 
ATOM   616  C  C    . SER   A 1 100 ? 12.918 -16.009 8.707  1.00 18.84 ?  252 SER   A C    1 
ATOM   617  O  O    . SER   A 1 100 ? 12.838 -15.077 9.511  1.00 18.82 ?  252 SER   A O    1 
ATOM   618  C  CB   . SER   A 1 100 ? 11.393 -16.004 6.721  1.00 27.78 ?  252 SER   A CB   1 
ATOM   619  O  OG   . SER   A 1 100 ? 11.036 -15.045 5.743  1.00 33.87 ?  252 SER   A OG   1 
ATOM   620  N  N    . ASP   A 1 101 ? 13.102 -17.274 9.095  1.00 21.49 ?  253 ASP   A N    1 
ATOM   621  C  CA   . ASP   A 1 101 ? 13.241 -17.612 10.510 1.00 24.15 ?  253 ASP   A CA   1 
ATOM   622  C  C    . ASP   A 1 101 ? 14.421 -16.886 11.140 1.00 26.06 ?  253 ASP   A C    1 
ATOM   623  O  O    . ASP   A 1 101 ? 14.309 -16.338 12.244 1.00 29.67 ?  253 ASP   A O    1 
ATOM   624  C  CB   . ASP   A 1 101 ? 13.395 -19.124 10.685 1.00 25.63 ?  253 ASP   A CB   1 
ATOM   625  C  CG   . ASP   A 1 101 ? 12.084 -19.867 10.512 1.00 34.92 ?  253 ASP   A CG   1 
ATOM   626  O  OD1  . ASP   A 1 101 ? 12.123 -21.091 10.267 1.00 40.22 ?  253 ASP   A OD1  1 
ATOM   627  O  OD2  . ASP   A 1 101 ? 11.015 -19.225 10.613 1.00 34.77 ?  253 ASP   A OD2  1 
ATOM   628  N  N    . ASP   A 1 102 ? 15.571 -16.878 10.459 1.00 24.94 ?  254 ASP   A N    1 
ATOM   629  C  CA   . ASP   A 1 102 ? 16.742 -16.217 11.030 1.00 24.37 ?  254 ASP   A CA   1 
ATOM   630  C  C    . ASP   A 1 102 ? 16.572 -14.706 11.053 1.00 19.81 ?  254 ASP   A C    1 
ATOM   631  O  O    . ASP   A 1 102 ? 17.066 -14.042 11.972 1.00 20.37 ?  254 ASP   A O    1 
ATOM   632  C  CB   . ASP   A 1 102 ? 18.010 -16.601 10.261 1.00 26.44 ?  254 ASP   A CB   1 
ATOM   633  C  CG   . ASP   A 1 102 ? 18.592 -17.926 10.725 1.00 32.26 ?  254 ASP   A CG   1 
ATOM   634  O  OD1  . ASP   A 1 102 ? 19.316 -18.578 9.944  1.00 35.21 ?  254 ASP   A OD1  1 
ATOM   635  O  OD2  . ASP   A 1 102 ? 18.314 -18.325 11.873 1.00 37.70 ?  254 ASP   A OD2  1 
ATOM   636  N  N    . GLN   A 1 103 ? 15.874 -14.147 10.063 1.00 18.10 ?  255 GLN   A N    1 
ATOM   637  C  CA   . GLN   A 1 103 ? 15.583 -12.719 10.098 1.00 17.43 ?  255 GLN   A CA   1 
ATOM   638  C  C    . GLN   A 1 103 ? 14.718 -12.374 11.300 1.00 18.92 ?  255 GLN   A C    1 
ATOM   639  O  O    . GLN   A 1 103 ? 14.908 -11.328 11.931 1.00 18.37 ?  255 GLN   A O    1 
ATOM   640  C  CB   . GLN   A 1 103 ? 14.904 -12.288 8.799  1.00 16.15 ?  255 GLN   A CB   1 
ATOM   641  C  CG   . GLN   A 1 103 ? 15.815 -12.350 7.587  1.00 18.89 ?  255 GLN   A CG   1 
ATOM   642  C  CD   . GLN   A 1 103 ? 15.086 -12.032 6.295  1.00 22.76 ?  255 GLN   A CD   1 
ATOM   643  O  OE1  . GLN   A 1 103 ? 15.613 -12.235 5.204  1.00 28.42 ?  255 GLN   A OE1  1 
ATOM   644  N  NE2  . GLN   A 1 103 ? 13.869 -11.534 6.415  1.00 25.91 ?  255 GLN   A NE2  1 
ATOM   645  N  N    A ILE   A 1 104 ? 13.785 -13.257 11.658 0.60 20.84 ?  256 ILE   A N    1 
ATOM   646  N  N    B ILE   A 1 104 ? 13.757 -13.244 11.625 0.40 20.75 ?  256 ILE   A N    1 
ATOM   647  C  CA   A ILE   A 1 104 ? 12.880 -12.971 12.768 0.60 20.72 ?  256 ILE   A CA   1 
ATOM   648  C  CA   B ILE   A 1 104 ? 12.871 -13.014 12.767 0.40 20.68 ?  256 ILE   A CA   1 
ATOM   649  C  C    A ILE   A 1 104 ? 13.616 -13.067 14.102 0.60 20.01 ?  256 ILE   A C    1 
ATOM   650  C  C    B ILE   A 1 104 ? 13.666 -13.041 14.065 0.40 20.04 ?  256 ILE   A C    1 
ATOM   651  O  O    A ILE   A 1 104 ? 13.505 -12.177 14.954 0.60 20.13 ?  256 ILE   A O    1 
ATOM   652  O  O    B ILE   A 1 104 ? 13.636 -12.091 14.856 0.40 19.79 ?  256 ILE   A O    1 
ATOM   653  C  CB   A ILE   A 1 104 ? 11.659 -13.907 12.714 0.60 21.28 ?  256 ILE   A CB   1 
ATOM   654  C  CB   B ILE   A 1 104 ? 11.739 -14.057 12.792 0.40 21.43 ?  256 ILE   A CB   1 
ATOM   655  C  CG1  A ILE   A 1 104 ? 10.720 -13.474 11.587 0.60 22.10 ?  256 ILE   A CG1  1 
ATOM   656  C  CG1  B ILE   A 1 104 ? 10.870 -13.951 11.540 0.40 22.47 ?  256 ILE   A CG1  1 
ATOM   657  C  CG2  A ILE   A 1 104 ? 10.924 -13.917 14.047 0.60 20.97 ?  256 ILE   A CG2  1 
ATOM   658  C  CG2  B ILE   A 1 104 ? 10.888 -13.897 14.044 0.40 21.01 ?  256 ILE   A CG2  1 
ATOM   659  C  CD1  A ILE   A 1 104 ? 9.539  -14.405 11.374 0.60 22.06 ?  256 ILE   A CD1  1 
ATOM   660  C  CD1  B ILE   A 1 104 ? 10.179 -12.634 11.387 0.40 21.38 ?  256 ILE   A CD1  1 
ATOM   661  N  N    . VAL   A 1 105 ? 14.385 -14.142 14.304 1.00 20.24 ?  257 VAL   A N    1 
ATOM   662  C  CA   . VAL   A 1 105 ? 15.101 -14.301 15.569 1.00 22.15 ?  257 VAL   A CA   1 
ATOM   663  C  C    . VAL   A 1 105 ? 16.132 -13.197 15.761 1.00 17.81 ?  257 VAL   A C    1 
ATOM   664  O  O    . VAL   A 1 105 ? 16.356 -12.738 16.888 1.00 17.88 ?  257 VAL   A O    1 
ATOM   665  C  CB   . VAL   A 1 105 ? 15.747 -15.702 15.672 1.00 25.89 ?  257 VAL   A CB   1 
ATOM   666  C  CG1  . VAL   A 1 105 ? 14.704 -16.786 15.444 1.00 26.29 ?  257 VAL   A CG1  1 
ATOM   667  C  CG2  . VAL   A 1 105 ? 16.904 -15.858 14.700 1.00 29.27 ?  257 VAL   A CG2  1 
ATOM   668  N  N    . LEU   A 1 106 ? 16.755 -12.730 14.675 1.00 16.86 ?  258 LEU   A N    1 
ATOM   669  C  CA   . LEU   A 1 106 ? 17.749 -11.672 14.810 1.00 17.67 ?  258 LEU   A CA   1 
ATOM   670  C  C    . LEU   A 1 106 ? 17.101 -10.360 15.231 1.00 14.54 ?  258 LEU   A C    1 
ATOM   671  O  O    . LEU   A 1 106 ? 17.639 -9.641  16.079 1.00 14.41 ?  258 LEU   A O    1 
ATOM   672  C  CB   . LEU   A 1 106 ? 18.522 -11.496 13.504 1.00 15.82 ?  258 LEU   A CB   1 
ATOM   673  C  CG   . LEU   A 1 106 ? 19.618 -12.521 13.192 1.00 17.48 ?  258 LEU   A CG   1 
ATOM   674  C  CD1  . LEU   A 1 106 ? 20.349 -12.136 11.909 1.00 14.16 ?  258 LEU   A CD1  1 
ATOM   675  C  CD2  . LEU   A 1 106 ? 20.598 -12.663 14.356 1.00 16.50 ?  258 LEU   A CD2  1 
ATOM   676  N  N    . LEU   A 1 107 ? 15.942 -10.034 14.659 1.00 16.15 ?  259 LEU   A N    1 
ATOM   677  C  CA   . LEU   A 1 107 ? 15.281 -8.783  15.019 1.00 17.63 ?  259 LEU   A CA   1 
ATOM   678  C  C    . LEU   A 1 107 ? 14.638 -8.863  16.400 1.00 15.24 ?  259 LEU   A C    1 
ATOM   679  O  O    . LEU   A 1 107 ? 14.621 -7.869  17.137 1.00 16.32 ?  259 LEU   A O    1 
ATOM   680  C  CB   . LEU   A 1 107 ? 14.246 -8.412  13.957 1.00 18.55 ?  259 LEU   A CB   1 
ATOM   681  C  CG   . LEU   A 1 107 ? 14.848 -7.624  12.794 1.00 21.70 ?  259 LEU   A CG   1 
ATOM   682  C  CD1  . LEU   A 1 107 ? 14.164 -7.973  11.481 1.00 22.73 ?  259 LEU   A CD1  1 
ATOM   683  C  CD2  . LEU   A 1 107 ? 14.763 -6.137  13.077 1.00 22.92 ?  259 LEU   A CD2  1 
ATOM   684  N  N    . LYS   A 1 108 ? 14.105 -10.033 16.773 1.00 15.05 ?  260 LYS   A N    1 
ATOM   685  C  CA   . LYS   A 1 108 ? 13.506 -10.182 18.102 1.00 16.40 ?  260 LYS   A CA   1 
ATOM   686  C  C    . LYS   A 1 108 ? 14.545 -10.021 19.209 1.00 13.08 ?  260 LYS   A C    1 
ATOM   687  O  O    . LYS   A 1 108 ? 14.279 -9.383  20.235 1.00 11.96 ?  260 LYS   A O    1 
ATOM   688  C  CB   . LYS   A 1 108 ? 12.812 -11.541 18.224 1.00 17.30 ?  260 LYS   A CB   1 
ATOM   689  C  CG   . LYS   A 1 108 ? 11.444 -11.616 17.566 1.00 25.09 ?  260 LYS   A CG   1 
ATOM   690  C  CD   . LYS   A 1 108 ? 10.876 -13.031 17.624 1.00 26.80 ?  260 LYS   A CD   1 
ATOM   691  C  CE   . LYS   A 1 108 ? 10.573 -13.465 19.050 1.00 30.49 ?  260 LYS   A CE   1 
ATOM   692  N  NZ   . LYS   A 1 108 ? 9.306  -12.877 19.591 1.00 29.33 ?  260 LYS   A NZ   1 
ATOM   693  N  N    . SER   A 1 109 ? 15.734 -10.595 19.030 1.00 20.16 ?  261 SER   A N    1 
ATOM   694  C  CA   . SER   A 1 109 ? 16.736 -10.493 20.081 1.00 20.95 ?  261 SER   A CA   1 
ATOM   695  C  C    . SER   A 1 109 ? 17.453 -9.151  20.064 1.00 20.75 ?  261 SER   A C    1 
ATOM   696  O  O    . SER   A 1 109 ? 17.847 -8.656  21.125 1.00 20.53 ?  261 SER   A O    1 
ATOM   697  C  CB   . SER   A 1 109 ? 17.752 -11.628 19.968 1.00 26.57 ?  261 SER   A CB   1 
ATOM   698  O  OG   . SER   A 1 109 ? 18.198 -11.784 18.642 1.00 32.94 ?  261 SER   A OG   1 
ATOM   699  N  N    . SER   A 1 110 ? 17.609 -8.539  18.894 1.00 17.46 ?  262 SER   A N    1 
ATOM   700  C  CA   . SER   A 1 110 ? 18.396 -7.319  18.759 1.00 13.55 ?  262 SER   A CA   1 
ATOM   701  C  C    . SER   A 1 110 ? 17.610 -6.026  18.957 1.00 11.29 ?  262 SER   A C    1 
ATOM   702  O  O    . SER   A 1 110 ? 18.232 -4.992  19.238 1.00 16.95 ?  262 SER   A O    1 
ATOM   703  C  CB   . SER   A 1 110 ? 19.043 -7.279  17.372 1.00 19.04 ?  262 SER   A CB   1 
ATOM   704  O  OG   . SER   A 1 110 ? 18.166 -6.686  16.422 1.00 18.96 ?  262 SER   A OG   1 
ATOM   705  N  N    . ALA   A 1 111 ? 16.276 -6.055  18.829 1.00 11.22 ?  263 ALA   A N    1 
ATOM   706  C  CA   . ALA   A 1 111 ? 15.496 -4.821  18.700 1.00 11.89 ?  263 ALA   A CA   1 
ATOM   707  C  C    . ALA   A 1 111 ? 15.756 -3.854  19.848 1.00 12.01 ?  263 ALA   A C    1 
ATOM   708  O  O    . ALA   A 1 111 ? 16.026 -2.668  19.622 1.00 15.56 ?  263 ALA   A O    1 
ATOM   709  C  CB   . ALA   A 1 111 ? 13.997 -5.128  18.607 1.00 8.92  ?  263 ALA   A CB   1 
ATOM   710  N  N    . ILE   A 1 112 ? 15.652 -4.329  21.094 1.00 13.88 ?  264 ILE   A N    1 
ATOM   711  C  CA   . ILE   A 1 112 ? 15.823 -3.414  22.219 1.00 11.39 ?  264 ILE   A CA   1 
ATOM   712  C  C    . ILE   A 1 112 ? 17.234 -2.844  22.238 1.00 10.12 ?  264 ILE   A C    1 
ATOM   713  O  O    . ILE   A 1 112 ? 17.439 -1.683  22.619 1.00 10.94 ?  264 ILE   A O    1 
ATOM   714  C  CB   . ILE   A 1 112 ? 15.465 -4.105  23.552 1.00 15.91 ?  264 ILE   A CB   1 
ATOM   715  C  CG1  . ILE   A 1 112 ? 15.323 -3.064  24.664 1.00 11.39 ?  264 ILE   A CG1  1 
ATOM   716  C  CG2  . ILE   A 1 112 ? 16.495 -5.178  23.926 1.00 12.82 ?  264 ILE   A CG2  1 
ATOM   717  C  CD1  . ILE   A 1 112 ? 14.259 -2.031  24.378 1.00 10.90 ?  264 ILE   A CD1  1 
ATOM   718  N  N    . GLU   A 1 113 ? 18.222 -3.633  21.809 1.00 10.53 ?  265 GLU   A N    1 
ATOM   719  C  CA   . GLU   A 1 113 ? 19.603 -3.164  21.776 1.00 13.04 ?  265 GLU   A CA   1 
ATOM   720  C  C    . GLU   A 1 113 ? 19.802 -2.084  20.718 1.00 14.64 ?  265 GLU   A C    1 
ATOM   721  O  O    . GLU   A 1 113 ? 20.471 -1.074  20.972 1.00 16.50 ?  265 GLU   A O    1 
ATOM   722  C  CB   . GLU   A 1 113 ? 20.547 -4.338  21.514 1.00 17.19 ?  265 GLU   A CB   1 
ATOM   723  C  CG   . GLU   A 1 113 ? 20.587 -5.394  22.618 1.00 14.16 ?  265 GLU   A CG   1 
ATOM   724  C  CD   . GLU   A 1 113 ? 21.504 -6.554  22.267 1.00 17.99 ?  265 GLU   A CD   1 
ATOM   725  O  OE1  . GLU   A 1 113 ? 22.537 -6.324  21.600 1.00 20.43 ?  265 GLU   A OE1  1 
ATOM   726  O  OE2  . GLU   A 1 113 ? 21.189 -7.703  22.640 1.00 19.42 ?  265 GLU   A OE2  1 
ATOM   727  N  N    . VAL   A 1 114 ? 19.249 -2.266  19.524 1.00 13.10 ?  266 VAL   A N    1 
ATOM   728  C  CA   . VAL   A 1 114 ? 19.396 -1.245  18.454 1.00 9.15  ?  266 VAL   A CA   1 
ATOM   729  C  C    . VAL   A 1 114 ? 18.625 0.009   18.859 1.00 12.28 ?  266 VAL   A C    1 
ATOM   730  O  O    . VAL   A 1 114 ? 19.068 1.076   18.558 1.00 14.40 ?  266 VAL   A O    1 
ATOM   731  C  CB   . VAL   A 1 114 ? 18.990 -1.761  17.070 1.00 14.43 ?  266 VAL   A CB   1 
ATOM   732  C  CG1  . VAL   A 1 114 ? 19.201 -0.718  15.994 1.00 12.06 ?  266 VAL   A CG1  1 
ATOM   733  C  CG2  . VAL   A 1 114 ? 19.731 -3.038  16.742 1.00 14.57 ?  266 VAL   A CG2  1 
ATOM   734  N  N    . ILE   A 1 115 ? 17.502 -0.162  19.545 1.00 10.11 ?  267 ILE   A N    1 
ATOM   735  C  CA   . ILE   A 1 115 ? 16.751 0.999   20.012 1.00 11.09 ?  267 ILE   A CA   1 
ATOM   736  C  C    . ILE   A 1 115 ? 17.581 1.795   21.012 1.00 12.89 ?  267 ILE   A C    1 
ATOM   737  O  O    . ILE   A 1 115 ? 17.699 3.023   20.915 1.00 16.91 ?  267 ILE   A O    1 
ATOM   738  C  CB   . ILE   A 1 115 ? 15.407 0.556   20.620 1.00 11.61 ?  267 ILE   A CB   1 
ATOM   739  C  CG1  . ILE   A 1 115 ? 14.433 0.119   19.528 1.00 8.37  ?  267 ILE   A CG1  1 
ATOM   740  C  CG2  . ILE   A 1 115 ? 14.813 1.662   21.448 1.00 11.32 ?  267 ILE   A CG2  1 
ATOM   741  C  CD1  . ILE   A 1 115 ? 13.267 -0.697  20.050 1.00 8.42  ?  267 ILE   A CD1  1 
ATOM   742  N  N    . MET   A 1 116 ? 18.153 1.108   22.003 1.00 15.91 ?  268 MET   A N    1 
ATOM   743  C  CA   . MET   A 1 116 ? 19.014 1.786   22.968 1.00 18.93 ?  268 MET   A CA   1 
ATOM   744  C  C    . MET   A 1 116 ? 20.202 2.437   22.275 1.00 17.62 ?  268 MET   A C    1 
ATOM   745  O  O    . MET   A 1 116 ? 20.589 3.562   22.612 1.00 18.25 ?  268 MET   A O    1 
ATOM   746  C  CB   . MET   A 1 116 ? 19.490 0.791   24.027 1.00 17.84 ?  268 MET   A CB   1 
ATOM   747  C  CG   . MET   A 1 116 ? 18.405 0.364   25.015 1.00 18.14 ?  268 MET   A CG   1 
ATOM   748  S  SD   . MET   A 1 116 ? 18.937 -1.005  26.066 1.00 20.77 ?  268 MET   A SD   1 
ATOM   749  C  CE   . MET   A 1 116 ? 17.543 -1.135  27.180 1.00 14.95 ?  268 MET   A CE   1 
ATOM   750  N  N    . LEU   A 1 117 ? 20.782 1.742   21.291 1.00 17.58 ?  269 LEU   A N    1 
ATOM   751  C  CA   . LEU   A 1 117 ? 21.921 2.265   20.544 1.00 20.92 ?  269 LEU   A CA   1 
ATOM   752  C  C    . LEU   A 1 117 ? 21.530 3.493   19.725 1.00 20.86 ?  269 LEU   A C    1 
ATOM   753  O  O    . LEU   A 1 117 ? 22.142 4.562   19.855 1.00 17.92 ?  269 LEU   A O    1 
ATOM   754  C  CB   . LEU   A 1 117 ? 22.480 1.158   19.644 1.00 25.30 ?  269 LEU   A CB   1 
ATOM   755  C  CG   . LEU   A 1 117 ? 23.729 1.328   18.779 1.00 30.80 ?  269 LEU   A CG   1 
ATOM   756  C  CD1  . LEU   A 1 117 ? 24.765 2.178   19.472 1.00 32.94 ?  269 LEU   A CD1  1 
ATOM   757  C  CD2  . LEU   A 1 117 ? 24.312 -0.037  18.431 1.00 32.83 ?  269 LEU   A CD2  1 
ATOM   758  N  N    . ARG   A 1 118 ? 20.496 3.366   18.886 1.00 19.81 ?  270 ARG   A N    1 
ATOM   759  C  CA   . ARG   A 1 118 ? 20.108 4.476   18.022 1.00 16.95 ?  270 ARG   A CA   1 
ATOM   760  C  C    . ARG   A 1 118 ? 19.558 5.660   18.805 1.00 16.30 ?  270 ARG   A C    1 
ATOM   761  O  O    . ARG   A 1 118 ? 19.608 6.788   18.303 1.00 16.45 ?  270 ARG   A O    1 
ATOM   762  C  CB   . ARG   A 1 118 ? 19.087 4.008   16.971 1.00 16.46 ?  270 ARG   A CB   1 
ATOM   763  C  CG   . ARG   A 1 118 ? 17.662 3.830   17.483 1.00 20.84 ?  270 ARG   A CG   1 
ATOM   764  C  CD   . ARG   A 1 118 ? 16.865 2.857   16.609 1.00 23.10 ?  270 ARG   A CD   1 
ATOM   765  N  NE   . ARG   A 1 118 ? 16.792 3.308   15.221 1.00 22.27 ?  270 ARG   A NE   1 
ATOM   766  C  CZ   . ARG   A 1 118 ? 15.897 4.181   14.773 1.00 23.70 ?  270 ARG   A CZ   1 
ATOM   767  N  NH1  . ARG   A 1 118 ? 14.995 4.680   15.609 1.00 17.73 ?  270 ARG   A NH1  1 
ATOM   768  N  NH2  . ARG   A 1 118 ? 15.897 4.548   13.494 1.00 22.96 ?  270 ARG   A NH2  1 
ATOM   769  N  N    . SER   A 1 119 ? 19.053 5.445   20.026 1.00 15.40 ?  271 SER   A N    1 
ATOM   770  C  CA   . SER   A 1 119 ? 18.529 6.561   20.807 1.00 19.19 ?  271 SER   A CA   1 
ATOM   771  C  C    . SER   A 1 119 ? 19.617 7.541   21.226 1.00 19.96 ?  271 SER   A C    1 
ATOM   772  O  O    . SER   A 1 119 ? 19.298 8.680   21.580 1.00 25.30 ?  271 SER   A O    1 
ATOM   773  C  CB   . SER   A 1 119 ? 17.795 6.052   22.050 1.00 20.37 ?  271 SER   A CB   1 
ATOM   774  O  OG   . SER   A 1 119 ? 18.688 5.441   22.962 1.00 19.90 ?  271 SER   A OG   1 
ATOM   775  N  N    . ASN   A 1 120 ? 20.886 7.124   21.191 1.00 20.55 ?  272 ASN   A N    1 
ATOM   776  C  CA   . ASN   A 1 120 ? 21.981 7.987   21.631 1.00 20.03 ?  272 ASN   A CA   1 
ATOM   777  C  C    . ASN   A 1 120 ? 22.083 9.251   20.785 1.00 20.73 ?  272 ASN   A C    1 
ATOM   778  O  O    . ASN   A 1 120 ? 22.508 10.301  21.281 1.00 20.92 ?  272 ASN   A O    1 
ATOM   779  C  CB   . ASN   A 1 120 ? 23.292 7.204   21.592 1.00 19.37 ?  272 ASN   A CB   1 
ATOM   780  C  CG   . ASN   A 1 120 ? 24.456 7.973   22.185 1.00 21.88 ?  272 ASN   A CG   1 
ATOM   781  O  OD1  . ASN   A 1 120 ? 25.371 8.377   21.466 1.00 23.65 ?  272 ASN   A OD1  1 
ATOM   782  N  ND2  . ASN   A 1 120 ? 24.436 8.167   23.507 1.00 20.85 ?  272 ASN   A ND2  1 
ATOM   783  N  N    . GLN   A 1 121 ? 21.684 9.178   19.517 1.00 22.20 ?  273 GLN   A N    1 
ATOM   784  C  CA   . GLN   A 1 121 ? 21.694 10.358  18.663 1.00 24.73 ?  273 GLN   A CA   1 
ATOM   785  C  C    . GLN   A 1 121 ? 20.738 11.439  19.163 1.00 26.85 ?  273 GLN   A C    1 
ATOM   786  O  O    . GLN   A 1 121 ? 20.920 12.617  18.837 1.00 29.66 ?  273 GLN   A O    1 
ATOM   787  C  CB   . GLN   A 1 121 ? 21.361 9.935   17.227 1.00 28.37 ?  273 GLN   A CB   1 
ATOM   788  C  CG   . GLN   A 1 121 ? 21.129 11.067  16.253 1.00 28.14 ?  273 GLN   A CG   1 
ATOM   789  C  CD   . GLN   A 1 121 ? 21.184 10.606  14.817 1.00 27.83 ?  273 GLN   A CD   1 
ATOM   790  O  OE1  . GLN   A 1 121 ? 21.315 9.411   14.539 1.00 23.93 ?  273 GLN   A OE1  1 
ATOM   791  N  NE2  . GLN   A 1 121 ? 21.088 11.553  13.891 1.00 28.19 ?  273 GLN   A NE2  1 
ATOM   792  N  N    . SER   A 1 122 ? 19.734 11.073  19.960 1.00 25.74 ?  274 SER   A N    1 
ATOM   793  C  CA   . SER   A 1 122 ? 18.864 12.049  20.604 1.00 26.42 ?  274 SER   A CA   1 
ATOM   794  C  C    . SER   A 1 122 ? 19.289 12.375  22.031 1.00 27.52 ?  274 SER   A C    1 
ATOM   795  O  O    . SER   A 1 122 ? 18.767 13.330  22.616 1.00 28.34 ?  274 SER   A O    1 
ATOM   796  C  CB   . SER   A 1 122 ? 17.413 11.548  20.608 1.00 24.10 ?  274 SER   A CB   1 
ATOM   797  O  OG   . SER   A 1 122 ? 17.240 10.516  21.564 1.00 25.43 ?  274 SER   A OG   1 
ATOM   798  N  N    . PHE   A 1 123 ? 20.213 11.606  22.599 1.00 28.97 ?  275 PHE   A N    1 
ATOM   799  C  CA   . PHE   A 1 123 ? 20.650 11.826  23.969 1.00 28.87 ?  275 PHE   A CA   1 
ATOM   800  C  C    . PHE   A 1 123 ? 21.437 13.127  24.079 1.00 35.43 ?  275 PHE   A C    1 
ATOM   801  O  O    . PHE   A 1 123 ? 22.358 13.378  23.296 1.00 36.30 ?  275 PHE   A O    1 
ATOM   802  C  CB   . PHE   A 1 123 ? 21.505 10.648  24.431 1.00 26.31 ?  275 PHE   A CB   1 
ATOM   803  C  CG   . PHE   A 1 123 ? 21.713 10.588  25.914 1.00 26.75 ?  275 PHE   A CG   1 
ATOM   804  C  CD1  . PHE   A 1 123 ? 20.702 10.142  26.753 1.00 26.86 ?  275 PHE   A CD1  1 
ATOM   805  C  CD2  . PHE   A 1 123 ? 22.925 10.966  26.471 1.00 25.70 ?  275 PHE   A CD2  1 
ATOM   806  C  CE1  . PHE   A 1 123 ? 20.896 10.082  28.124 1.00 23.98 ?  275 PHE   A CE1  1 
ATOM   807  C  CE2  . PHE   A 1 123 ? 23.128 10.910  27.838 1.00 27.70 ?  275 PHE   A CE2  1 
ATOM   808  C  CZ   . PHE   A 1 123 ? 22.115 10.467  28.665 1.00 27.34 ?  275 PHE   A CZ   1 
ATOM   809  N  N    . THR   A 1 124 ? 21.064 13.959  25.048 1.00 38.47 ?  276 THR   A N    1 
ATOM   810  C  CA   . THR   A 1 124 ? 21.791 15.179  25.374 1.00 42.66 ?  276 THR   A CA   1 
ATOM   811  C  C    . THR   A 1 124 ? 22.297 15.069  26.803 1.00 44.23 ?  276 THR   A C    1 
ATOM   812  O  O    . THR   A 1 124 ? 21.540 14.706  27.709 1.00 42.88 ?  276 THR   A O    1 
ATOM   813  C  CB   . THR   A 1 124 ? 20.906 16.429  25.205 1.00 44.36 ?  276 THR   A CB   1 
ATOM   814  O  OG1  . THR   A 1 124 ? 21.613 17.590  25.662 1.00 45.70 ?  276 THR   A OG1  1 
ATOM   815  C  CG2  . THR   A 1 124 ? 19.595 16.294  25.976 1.00 44.57 ?  276 THR   A CG2  1 
ATOM   816  N  N    . MET   A 1 125 ? 23.576 15.363  27.003 1.00 46.33 ?  277 MET   A N    1 
ATOM   817  C  CA   . MET   A 1 125 ? 24.159 15.229  28.329 1.00 51.47 ?  277 MET   A CA   1 
ATOM   818  C  C    . MET   A 1 125 ? 24.022 16.488  29.169 1.00 54.01 ?  277 MET   A C    1 
ATOM   819  O  O    . MET   A 1 125 ? 24.495 16.504  30.310 1.00 57.13 ?  277 MET   A O    1 
ATOM   820  C  CB   . MET   A 1 125 ? 25.629 14.830  28.228 1.00 54.13 ?  277 MET   A CB   1 
ATOM   821  C  CG   . MET   A 1 125 ? 25.851 13.361  28.504 1.00 54.23 ?  277 MET   A CG   1 
ATOM   822  S  SD   . MET   A 1 125 ? 27.575 12.921  28.322 1.00 57.66 ?  277 MET   A SD   1 
ATOM   823  C  CE   . MET   A 1 125 ? 27.975 13.819  26.824 1.00 59.83 ?  277 MET   A CE   1 
ATOM   824  N  N    . ASP   A 1 126 ? 23.394 17.536  28.631 1.00 54.31 ?  278 ASP   A N    1 
ATOM   825  C  CA   . ASP   A 1 126 ? 23.044 18.701  29.437 1.00 55.36 ?  278 ASP   A CA   1 
ATOM   826  C  C    . ASP   A 1 126 ? 22.307 18.280  30.701 1.00 54.00 ?  278 ASP   A C    1 
ATOM   827  O  O    . ASP   A 1 126 ? 22.757 18.542  31.821 1.00 55.54 ?  278 ASP   A O    1 
ATOM   828  C  CB   . ASP   A 1 126 ? 22.185 19.661  28.614 1.00 58.12 ?  278 ASP   A CB   1 
ATOM   829  C  CG   . ASP   A 1 126 ? 22.851 20.075  27.325 1.00 61.32 ?  278 ASP   A CG   1 
ATOM   830  O  OD1  . ASP   A 1 126 ? 24.029 19.715  27.130 1.00 61.97 ?  278 ASP   A OD1  1 
ATOM   831  O  OD2  . ASP   A 1 126 ? 22.193 20.751  26.505 1.00 63.11 ?  278 ASP   A OD2  1 
ATOM   832  N  N    . ASP   A 1 127 ? 21.169 17.604  30.531 1.00 51.22 ?  279 ASP   A N    1 
ATOM   833  C  CA   . ASP   A 1 127 ? 20.365 17.133  31.650 1.00 53.45 ?  279 ASP   A CA   1 
ATOM   834  C  C    . ASP   A 1 127 ? 20.182 15.621  31.629 1.00 51.90 ?  279 ASP   A C    1 
ATOM   835  O  O    . ASP   A 1 127 ? 19.225 15.110  32.224 1.00 50.56 ?  279 ASP   A O    1 
ATOM   836  C  CB   . ASP   A 1 127 ? 19.009 17.839  31.661 1.00 56.95 ?  279 ASP   A CB   1 
ATOM   837  C  CG   . ASP   A 1 127 ? 18.461 18.058  30.272 1.00 60.38 ?  279 ASP   A CG   1 
ATOM   838  O  OD1  . ASP   A 1 127 ? 18.676 17.187  29.403 1.00 61.14 ?  279 ASP   A OD1  1 
ATOM   839  O  OD2  . ASP   A 1 127 ? 17.828 19.111  30.046 1.00 63.24 ?  279 ASP   A OD2  1 
ATOM   840  N  N    . MET   A 1 128 ? 21.081 14.896  30.958 1.00 50.20 ?  280 MET   A N    1 
ATOM   841  C  CA   . MET   A 1 128 ? 21.073 13.430  30.948 1.00 46.90 ?  280 MET   A CA   1 
ATOM   842  C  C    . MET   A 1 128 ? 19.725 12.886  30.481 1.00 40.77 ?  280 MET   A C    1 
ATOM   843  O  O    . MET   A 1 128 ? 19.144 11.990  31.096 1.00 40.75 ?  280 MET   A O    1 
ATOM   844  C  CB   . MET   A 1 128 ? 21.433 12.873  32.327 1.00 48.49 ?  280 MET   A CB   1 
ATOM   845  C  CG   . MET   A 1 128 ? 22.757 13.362  32.846 1.00 49.14 ?  280 MET   A CG   1 
ATOM   846  S  SD   . MET   A 1 128 ? 24.107 12.524  32.015 1.00 48.35 ?  280 MET   A SD   1 
ATOM   847  C  CE   . MET   A 1 128 ? 24.587 11.358  33.286 1.00 50.74 ?  280 MET   A CE   1 
ATOM   848  N  N    . SER   A 1 129 ? 19.218 13.446  29.388 1.00 35.18 ?  281 SER   A N    1 
ATOM   849  C  CA   . SER   A 1 129 ? 17.911 13.064  28.884 1.00 33.02 ?  281 SER   A CA   1 
ATOM   850  C  C    . SER   A 1 129 ? 17.992 12.786  27.389 1.00 34.88 ?  281 SER   A C    1 
ATOM   851  O  O    . SER   A 1 129 ? 19.013 13.027  26.733 1.00 29.57 ?  281 SER   A O    1 
ATOM   852  C  CB   . SER   A 1 129 ? 16.862 14.147  29.177 1.00 36.49 ?  281 SER   A CB   1 
ATOM   853  O  OG   . SER   A 1 129 ? 17.030 15.273  28.336 1.00 41.18 ?  281 SER   A OG   1 
ATOM   854  N  N    . TRP   A 1 130 ? 16.895 12.247  26.862 1.00 28.61 ?  282 TRP   A N    1 
ATOM   855  C  CA   . TRP   A 1 130 ? 16.727 12.010  25.433 1.00 25.89 ?  282 TRP   A CA   1 
ATOM   856  C  C    . TRP   A 1 130 ? 15.838 13.131  24.906 1.00 30.16 ?  282 TRP   A C    1 
ATOM   857  O  O    . TRP   A 1 130 ? 14.629 13.145  25.155 1.00 33.92 ?  282 TRP   A O    1 
ATOM   858  C  CB   . TRP   A 1 130 ? 16.111 10.638  25.175 1.00 21.43 ?  282 TRP   A CB   1 
ATOM   859  C  CG   . TRP   A 1 130 ? 17.015 9.472   25.461 1.00 20.54 ?  282 TRP   A CG   1 
ATOM   860  C  CD1  . TRP   A 1 130 ? 17.849 8.850   24.579 1.00 20.27 ?  282 TRP   A CD1  1 
ATOM   861  C  CD2  . TRP   A 1 130 ? 17.155 8.770   26.707 1.00 24.84 ?  282 TRP   A CD2  1 
ATOM   862  N  NE1  . TRP   A 1 130 ? 18.503 7.811   25.194 1.00 21.64 ?  282 TRP   A NE1  1 
ATOM   863  C  CE2  . TRP   A 1 130 ? 18.100 7.743   26.502 1.00 21.23 ?  282 TRP   A CE2  1 
ATOM   864  C  CE3  . TRP   A 1 130 ? 16.578 8.913   27.974 1.00 24.16 ?  282 TRP   A CE3  1 
ATOM   865  C  CZ2  . TRP   A 1 130 ? 18.479 6.863   27.512 1.00 21.20 ?  282 TRP   A CZ2  1 
ATOM   866  C  CZ3  . TRP   A 1 130 ? 16.958 8.035   28.982 1.00 21.96 ?  282 TRP   A CZ3  1 
ATOM   867  C  CH2  . TRP   A 1 130 ? 17.896 7.024   28.744 1.00 23.54 ?  282 TRP   A CH2  1 
ATOM   868  N  N    . ASP   A 1 131 ? 16.441 14.081  24.195 1.00 33.25 ?  283 ASP   A N    1 
ATOM   869  C  CA   . ASP   A 1 131 ? 15.722 15.237  23.673 1.00 38.57 ?  283 ASP   A CA   1 
ATOM   870  C  C    . ASP   A 1 131 ? 15.210 14.901  22.279 1.00 36.18 ?  283 ASP   A C    1 
ATOM   871  O  O    . ASP   A 1 131 ? 16.001 14.709  21.351 1.00 38.37 ?  283 ASP   A O    1 
ATOM   872  C  CB   . ASP   A 1 131 ? 16.620 16.474  23.645 1.00 43.79 ?  283 ASP   A CB   1 
ATOM   873  C  CG   . ASP   A 1 131 ? 15.852 17.749  23.322 1.00 49.89 ?  283 ASP   A CG   1 
ATOM   874  O  OD1  . ASP   A 1 131 ? 14.739 17.671  22.761 1.00 52.01 ?  283 ASP   A OD1  1 
ATOM   875  O  OD2  . ASP   A 1 131 ? 16.367 18.842  23.640 1.00 54.80 ?  283 ASP   A OD2  1 
ATOM   876  N  N    . CYS   A 1 132 ? 13.890 14.857  22.124 1.00 35.12 ?  284 CYS   A N    1 
ATOM   877  C  CA   . CYS   A 1 132 ? 13.324 14.419  20.860 1.00 32.74 ?  284 CYS   A CA   1 
ATOM   878  C  C    . CYS   A 1 132 ? 12.443 15.516  20.274 1.00 35.27 ?  284 CYS   A C    1 
ATOM   879  O  O    . CYS   A 1 132 ? 11.315 15.246  19.847 1.00 37.69 ?  284 CYS   A O    1 
ATOM   880  C  CB   . CYS   A 1 132 ? 12.511 13.132  21.063 1.00 31.26 ?  284 CYS   A CB   1 
ATOM   881  S  SG   . CYS   A 1 132 ? 13.499 11.647  21.424 1.00 29.95 ?  284 CYS   A SG   1 
ATOM   882  N  N    . GLY   A 1 133 ? 12.928 16.762  20.266 1.00 37.30 ?  285 GLY   A N    1 
ATOM   883  C  CA   . GLY   A 1 133 ? 12.325 17.837  19.503 1.00 40.55 ?  285 GLY   A CA   1 
ATOM   884  C  C    . GLY   A 1 133 ? 11.710 18.953  20.331 1.00 44.04 ?  285 GLY   A C    1 
ATOM   885  O  O    . GLY   A 1 133 ? 11.655 20.097  19.861 1.00 45.03 ?  285 GLY   A O    1 
ATOM   886  N  N    . SER   A 1 134 ? 11.234 18.652  21.537 1.00 44.66 ?  286 SER   A N    1 
ATOM   887  C  CA   . SER   A 1 134 ? 10.528 19.643  22.340 1.00 43.94 ?  286 SER   A CA   1 
ATOM   888  C  C    . SER   A 1 134 ? 10.578 19.217  23.801 1.00 43.68 ?  286 SER   A C    1 
ATOM   889  O  O    . SER   A 1 134 ? 11.086 18.146  24.140 1.00 43.06 ?  286 SER   A O    1 
ATOM   890  C  CB   . SER   A 1 134 ? 9.084  19.813  21.861 1.00 43.84 ?  286 SER   A CB   1 
ATOM   891  O  OG   . SER   A 1 134 ? 8.240  18.828  22.426 1.00 44.85 ?  286 SER   A OG   1 
ATOM   892  N  N    . GLN   A 1 135 ? 10.043 20.079  24.670 1.00 45.36 ?  287 GLN   A N    1 
ATOM   893  C  CA   . GLN   A 1 135 ? 9.981  19.758  26.092 1.00 48.20 ?  287 GLN   A CA   1 
ATOM   894  C  C    . GLN   A 1 135 ? 9.007  18.614  26.353 1.00 45.36 ?  287 GLN   A C    1 
ATOM   895  O  O    . GLN   A 1 135 ? 9.238  17.784  27.241 1.00 39.57 ?  287 GLN   A O    1 
ATOM   896  C  CB   . GLN   A 1 135 ? 9.588  21.004  26.888 1.00 55.42 ?  287 GLN   A CB   1 
ATOM   897  C  CG   . GLN   A 1 135 ? 9.687  20.852  28.402 1.00 60.69 ?  287 GLN   A CG   1 
ATOM   898  C  CD   . GLN   A 1 135 ? 8.643  21.678  29.142 1.00 66.41 ?  287 GLN   A CD   1 
ATOM   899  O  OE1  . GLN   A 1 135 ? 8.948  22.734  29.703 1.00 69.87 ?  287 GLN   A OE1  1 
ATOM   900  N  NE2  . GLN   A 1 135 ? 7.401  21.200  29.142 1.00 66.47 ?  287 GLN   A NE2  1 
ATOM   901  N  N    . ASP   A 1 136 ? 7.914  18.555  25.586 1.00 48.53 ?  288 ASP   A N    1 
ATOM   902  C  CA   . ASP   A 1 136 ? 6.986  17.431  25.683 1.00 47.11 ?  288 ASP   A CA   1 
ATOM   903  C  C    . ASP   A 1 136 ? 7.698  16.114  25.409 1.00 40.73 ?  288 ASP   A C    1 
ATOM   904  O  O    . ASP   A 1 136 ? 7.547  15.139  26.155 1.00 37.23 ?  288 ASP   A O    1 
ATOM   905  C  CB   . ASP   A 1 136 ? 5.831  17.618  24.698 1.00 53.61 ?  288 ASP   A CB   1 
ATOM   906  C  CG   . ASP   A 1 136 ? 4.670  18.393  25.291 1.00 59.91 ?  288 ASP   A CG   1 
ATOM   907  O  OD1  . ASP   A 1 136 ? 4.502  18.370  26.530 1.00 61.86 ?  288 ASP   A OD1  1 
ATOM   908  O  OD2  . ASP   A 1 136 ? 3.921  19.019  24.510 1.00 62.17 ?  288 ASP   A OD2  1 
ATOM   909  N  N    . TYR   A 1 137 ? 8.484  16.072  24.341 1.00 39.65 ?  289 TYR   A N    1 
ATOM   910  C  CA   . TYR   A 1 137 ? 9.152  14.851  23.894 1.00 39.11 ?  289 TYR   A CA   1 
ATOM   911  C  C    . TYR   A 1 137 ? 10.606 14.833  24.340 1.00 39.12 ?  289 TYR   A C    1 
ATOM   912  O  O    . TYR   A 1 137 ? 11.527 14.581  23.564 1.00 39.06 ?  289 TYR   A O    1 
ATOM   913  C  CB   . TYR   A 1 137 ? 9.023  14.723  22.381 1.00 38.51 ?  289 TYR   A CB   1 
ATOM   914  C  CG   . TYR   A 1 137 ? 7.598  14.932  21.913 1.00 40.47 ?  289 TYR   A CG   1 
ATOM   915  C  CD1  . TYR   A 1 137 ? 7.318  15.680  20.778 1.00 41.28 ?  289 TYR   A CD1  1 
ATOM   916  C  CD2  . TYR   A 1 137 ? 6.532  14.386  22.619 1.00 38.15 ?  289 TYR   A CD2  1 
ATOM   917  C  CE1  . TYR   A 1 137 ? 6.018  15.874  20.359 1.00 42.49 ?  289 TYR   A CE1  1 
ATOM   918  C  CE2  . TYR   A 1 137 ? 5.232  14.575  22.208 1.00 39.14 ?  289 TYR   A CE2  1 
ATOM   919  C  CZ   . TYR   A 1 137 ? 4.978  15.319  21.078 1.00 40.70 ?  289 TYR   A CZ   1 
ATOM   920  O  OH   . TYR   A 1 137 ? 3.679  15.508  20.664 1.00 38.75 ?  289 TYR   A OH   1 
ATOM   921  N  N    . LYS   A 1 138 ? 10.811 15.135  25.619 1.00 35.66 ?  290 LYS   A N    1 
ATOM   922  C  CA   . LYS   A 1 138 ? 12.109 15.048  26.271 1.00 34.19 ?  290 LYS   A CA   1 
ATOM   923  C  C    . LYS   A 1 138 ? 11.956 14.128  27.473 1.00 33.96 ?  290 LYS   A C    1 
ATOM   924  O  O    . LYS   A 1 138 ? 11.117 14.378  28.345 1.00 38.85 ?  290 LYS   A O    1 
ATOM   925  C  CB   . LYS   A 1 138 ? 12.604 16.431  26.693 1.00 40.66 ?  290 LYS   A CB   1 
ATOM   926  C  CG   . LYS   A 1 138 ? 14.005 16.439  27.268 1.00 44.19 ?  290 LYS   A CG   1 
ATOM   927  C  CD   . LYS   A 1 138 ? 14.704 17.752  26.974 1.00 50.05 ?  290 LYS   A CD   1 
ATOM   928  C  CE   . LYS   A 1 138 ? 15.586 18.171  28.134 1.00 53.30 ?  290 LYS   A CE   1 
ATOM   929  N  NZ   . LYS   A 1 138 ? 15.140 19.457  28.746 1.00 56.67 ?  290 LYS   A NZ   1 
ATOM   930  N  N    . TYR   A 1 139 ? 12.761 13.069  27.517 1.00 30.39 ?  291 TYR   A N    1 
ATOM   931  C  CA   . TYR   A 1 139 ? 12.562 11.965  28.449 1.00 27.60 ?  291 TYR   A CA   1 
ATOM   932  C  C    . TYR   A 1 139 ? 13.783 11.829  29.342 1.00 28.04 ?  291 TYR   A C    1 
ATOM   933  O  O    . TYR   A 1 139 ? 14.897 11.632  28.846 1.00 29.34 ?  291 TYR   A O    1 
ATOM   934  C  CB   . TYR   A 1 139 ? 12.291 10.666  27.684 1.00 26.00 ?  291 TYR   A CB   1 
ATOM   935  C  CG   . TYR   A 1 139 ? 11.348 10.853  26.511 1.00 24.74 ?  291 TYR   A CG   1 
ATOM   936  C  CD1  . TYR   A 1 139 ? 11.811 10.796  25.201 1.00 25.85 ?  291 TYR   A CD1  1 
ATOM   937  C  CD2  . TYR   A 1 139 ? 9.994  11.101  26.717 1.00 24.57 ?  291 TYR   A CD2  1 
ATOM   938  C  CE1  . TYR   A 1 139 ? 10.949 10.974  24.125 1.00 24.93 ?  291 TYR   A CE1  1 
ATOM   939  C  CE2  . TYR   A 1 139 ? 9.122  11.284  25.651 1.00 22.32 ?  291 TYR   A CE2  1 
ATOM   940  C  CZ   . TYR   A 1 139 ? 9.604  11.216  24.359 1.00 23.79 ?  291 TYR   A CZ   1 
ATOM   941  O  OH   . TYR   A 1 139 ? 8.740  11.396  23.301 1.00 21.31 ?  291 TYR   A OH   1 
ATOM   942  N  N    . ASP   A 1 140 ? 13.575 11.934  30.657 1.00 26.84 ?  292 ASP   A N    1 
ATOM   943  C  CA   . ASP   A 1 140 ? 14.653 11.854  31.633 1.00 33.54 ?  292 ASP   A CA   1 
ATOM   944  C  C    . ASP   A 1 140 ? 14.521 10.579  32.458 1.00 30.80 ?  292 ASP   A C    1 
ATOM   945  O  O    . ASP   A 1 140 ? 13.704 9.698   32.157 1.00 28.31 ?  292 ASP   A O    1 
ATOM   946  C  CB   . ASP   A 1 140 ? 14.667 13.099  32.529 1.00 43.73 ?  292 ASP   A CB   1 
ATOM   947  C  CG   . ASP   A 1 140 ? 13.303 13.417  33.112 1.00 52.41 ?  292 ASP   A CG   1 
ATOM   948  O  OD1  . ASP   A 1 140 ? 12.809 14.545  32.893 1.00 56.92 ?  292 ASP   A OD1  1 
ATOM   949  O  OD2  . ASP   A 1 140 ? 12.723 12.542  33.788 1.00 54.24 ?  292 ASP   A OD2  1 
ATOM   950  N  N    . VAL   A 1 141 ? 15.336 10.489  33.516 1.00 31.92 ?  293 VAL   A N    1 
ATOM   951  C  CA   . VAL   A 1 141 ? 15.358 9.296   34.364 1.00 32.23 ?  293 VAL   A CA   1 
ATOM   952  C  C    . VAL   A 1 141 ? 13.961 8.968   34.879 1.00 31.90 ?  293 VAL   A C    1 
ATOM   953  O  O    . VAL   A 1 141 ? 13.552 7.802   34.910 1.00 28.69 ?  293 VAL   A O    1 
ATOM   954  C  CB   . VAL   A 1 141 ? 16.365 9.481   35.519 1.00 34.73 ?  293 VAL   A CB   1 
ATOM   955  C  CG1  . VAL   A 1 141 ? 16.045 10.729  36.338 1.00 39.78 ?  293 VAL   A CG1  1 
ATOM   956  C  CG2  . VAL   A 1 141 ? 16.372 8.258   36.428 1.00 30.01 ?  293 VAL   A CG2  1 
ATOM   957  N  N    . THR   A 1 142 ? 13.200 9.990   35.274 1.00 32.96 ?  294 THR   A N    1 
ATOM   958  C  CA   . THR   A 1 142 ? 11.901 9.752   35.888 1.00 33.42 ?  294 THR   A CA   1 
ATOM   959  C  C    . THR   A 1 142 ? 10.814 9.476   34.862 1.00 28.06 ?  294 THR   A C    1 
ATOM   960  O  O    . THR   A 1 142 ? 9.810  8.845   35.205 1.00 26.99 ?  294 THR   A O    1 
ATOM   961  C  CB   . THR   A 1 142 ? 11.500 10.941  36.763 1.00 38.02 ?  294 THR   A CB   1 
ATOM   962  O  OG1  . THR   A 1 142 ? 10.964 11.986  35.940 1.00 44.93 ?  294 THR   A OG1  1 
ATOM   963  C  CG2  . THR   A 1 142 ? 12.697 11.465  37.526 1.00 36.64 ?  294 THR   A CG2  1 
ATOM   964  N  N    . ASP   A 1 143 ? 10.987 9.935   33.620 1.00 28.06 ?  295 ASP   A N    1 
ATOM   965  C  CA   . ASP   A 1 143 ? 10.047 9.560   32.568 1.00 28.41 ?  295 ASP   A CA   1 
ATOM   966  C  C    . ASP   A 1 143 ? 10.096 8.059   32.304 1.00 25.82 ?  295 ASP   A C    1 
ATOM   967  O  O    . ASP   A 1 143 ? 9.055  7.416   32.127 1.00 21.78 ?  295 ASP   A O    1 
ATOM   968  C  CB   . ASP   A 1 143 ? 10.345 10.345  31.289 1.00 29.64 ?  295 ASP   A CB   1 
ATOM   969  C  CG   . ASP   A 1 143 ? 9.864  11.784  31.358 1.00 35.28 ?  295 ASP   A CG   1 
ATOM   970  O  OD1  . ASP   A 1 143 ? 8.781  12.017  31.930 1.00 36.57 ?  295 ASP   A OD1  1 
ATOM   971  O  OD2  . ASP   A 1 143 ? 10.560 12.683  30.837 1.00 37.24 ?  295 ASP   A OD2  1 
ATOM   972  N  N    . VAL   A 1 144 ? 11.299 7.482   32.278 1.00 25.80 ?  296 VAL   A N    1 
ATOM   973  C  CA   . VAL   A 1 144 ? 11.426 6.048   32.032 1.00 23.59 ?  296 VAL   A CA   1 
ATOM   974  C  C    . VAL   A 1 144 ? 10.867 5.254   33.207 1.00 25.59 ?  296 VAL   A C    1 
ATOM   975  O  O    . VAL   A 1 144 ? 10.210 4.222   33.023 1.00 21.30 ?  296 VAL   A O    1 
ATOM   976  C  CB   . VAL   A 1 144 ? 12.894 5.689   31.742 1.00 20.95 ?  296 VAL   A CB   1 
ATOM   977  C  CG1  . VAL   A 1 144 ? 13.045 4.197   31.502 1.00 18.66 ?  296 VAL   A CG1  1 
ATOM   978  C  CG2  . VAL   A 1 144 ? 13.398 6.475   30.548 1.00 20.96 ?  296 VAL   A CG2  1 
ATOM   979  N  N    . SER   A 1 145 ? 11.114 5.720   34.433 1.00 27.20 ?  297 SER   A N    1 
ATOM   980  C  CA   . SER   A 1 145 ? 10.520 5.059   35.589 1.00 32.51 ?  297 SER   A CA   1 
ATOM   981  C  C    . SER   A 1 145 ? 8.994  5.087   35.522 1.00 30.30 ?  297 SER   A C    1 
ATOM   982  O  O    . SER   A 1 145 ? 8.339  4.119   35.925 1.00 28.33 ?  297 SER   A O    1 
ATOM   983  C  CB   . SER   A 1 145 ? 11.022 5.708   36.879 1.00 35.68 ?  297 SER   A CB   1 
ATOM   984  O  OG   . SER   A 1 145 ? 10.503 7.020   37.016 1.00 37.63 ?  297 SER   A OG   1 
ATOM   985  N  N    . LYS   A 1 146 ? 8.413  6.166   34.987 1.00 27.74 ?  298 LYS   A N    1 
ATOM   986  C  CA   . LYS   A 1 146 ? 6.969  6.255   34.795 1.00 25.31 ?  298 LYS   A CA   1 
ATOM   987  C  C    . LYS   A 1 146 ? 6.445  5.333   33.699 1.00 24.14 ?  298 LYS   A C    1 
ATOM   988  O  O    . LYS   A 1 146 ? 5.256  5.413   33.373 1.00 24.61 ?  298 LYS   A O    1 
ATOM   989  C  CB   . LYS   A 1 146 ? 6.558  7.692   34.473 1.00 32.79 ?  298 LYS   A CB   1 
ATOM   990  C  CG   . LYS   A 1 146 ? 6.797  8.696   35.585 1.00 40.17 ?  298 LYS   A CG   1 
ATOM   991  C  CD   . LYS   A 1 146 ? 5.935  9.935   35.383 1.00 47.23 ?  298 LYS   A CD   1 
ATOM   992  C  CE   . LYS   A 1 146 ? 6.639  11.198  35.864 1.00 53.78 ?  298 LYS   A CE   1 
ATOM   993  N  NZ   . LYS   A 1 146 ? 7.559  11.752  34.818 1.00 55.42 ?  298 LYS   A NZ   1 
ATOM   994  N  N    . ALA   A 1 147 ? 7.287  4.499   33.093 1.00 19.62 ?  299 ALA   A N    1 
ATOM   995  C  CA   . ALA   A 1 147 ? 6.820  3.410   32.246 1.00 16.44 ?  299 ALA   A CA   1 
ATOM   996  C  C    . ALA   A 1 147 ? 7.037  2.056   32.904 1.00 20.79 ?  299 ALA   A C    1 
ATOM   997  O  O    . ALA   A 1 147 ? 6.803  1.023   32.266 1.00 19.42 ?  299 ALA   A O    1 
ATOM   998  C  CB   . ALA   A 1 147 ? 7.503  3.452   30.877 1.00 13.86 ?  299 ALA   A CB   1 
ATOM   999  N  N    . GLY   A 1 148 ? 7.493  2.039   34.161 1.00 22.99 ?  300 GLY   A N    1 
ATOM   1000 C  CA   . GLY   A 1 148 ? 7.580  0.829   34.955 1.00 23.67 ?  300 GLY   A CA   1 
ATOM   1001 C  C    . GLY   A 1 148 ? 8.978  0.357   35.305 1.00 24.23 ?  300 GLY   A C    1 
ATOM   1002 O  O    . GLY   A 1 148 ? 9.103  -0.620  36.054 1.00 26.03 ?  300 GLY   A O    1 
ATOM   1003 N  N    . HIS   A 1 149 ? 10.030 0.993   34.804 1.00 19.25 ?  301 HIS   A N    1 
ATOM   1004 C  CA   . HIS   A 1 149 ? 11.370 0.464   35.021 1.00 23.92 ?  301 HIS   A CA   1 
ATOM   1005 C  C    . HIS   A 1 149 ? 12.038 1.109   36.232 1.00 23.98 ?  301 HIS   A C    1 
ATOM   1006 O  O    . HIS   A 1 149 ? 11.718 2.236   36.620 1.00 23.62 ?  301 HIS   A O    1 
ATOM   1007 C  CB   . HIS   A 1 149 ? 12.233 0.657   33.772 1.00 20.33 ?  301 HIS   A CB   1 
ATOM   1008 C  CG   . HIS   A 1 149 ? 11.778 -0.155  32.601 1.00 17.73 ?  301 HIS   A CG   1 
ATOM   1009 N  ND1  . HIS   A 1 149 ? 11.819 -1.534  32.591 1.00 18.50 ?  301 HIS   A ND1  1 
ATOM   1010 C  CD2  . HIS   A 1 149 ? 11.255 0.214   31.409 1.00 14.81 ?  301 HIS   A CD2  1 
ATOM   1011 C  CE1  . HIS   A 1 149 ? 11.351 -1.980  31.439 1.00 13.32 ?  301 HIS   A CE1  1 
ATOM   1012 N  NE2  . HIS   A 1 149 ? 11.004 -0.940  30.703 1.00 16.84 ?  301 HIS   A NE2  1 
ATOM   1013 N  N    . THR   A 1 150 ? 12.966 0.365   36.831 1.00 24.32 ?  302 THR   A N    1 
ATOM   1014 C  CA   . THR   A 1 150 ? 13.729 0.782   38.001 1.00 26.02 ?  302 THR   A CA   1 
ATOM   1015 C  C    . THR   A 1 150 ? 15.157 1.175   37.614 1.00 24.11 ?  302 THR   A C    1 
ATOM   1016 O  O    . THR   A 1 150 ? 15.596 0.999   36.474 1.00 22.83 ?  302 THR   A O    1 
ATOM   1017 C  CB   . THR   A 1 150 ? 13.771 -0.346  39.036 1.00 28.25 ?  302 THR   A CB   1 
ATOM   1018 O  OG1  . THR   A 1 150 ? 14.532 -1.443  38.505 1.00 29.24 ?  302 THR   A OG1  1 
ATOM   1019 C  CG2  . THR   A 1 150 ? 12.364 -0.824  39.362 1.00 17.64 ?  302 THR   A CG2  1 
ATOM   1020 N  N    . LEU   A 1 151 ? 15.900 1.692   38.601 1.00 23.31 ?  303 LEU   A N    1 
ATOM   1021 C  CA   . LEU   A 1 151 ? 17.296 2.037   38.360 1.00 20.23 ?  303 LEU   A CA   1 
ATOM   1022 C  C    . LEU   A 1 151 ? 18.148 0.825   38.032 1.00 19.74 ?  303 LEU   A C    1 
ATOM   1023 O  O    . LEU   A 1 151 ? 19.241 0.989   37.481 1.00 21.37 ?  303 LEU   A O    1 
ATOM   1024 C  CB   . LEU   A 1 151 ? 17.914 2.761   39.552 1.00 26.04 ?  303 LEU   A CB   1 
ATOM   1025 C  CG   . LEU   A 1 151 ? 17.441 4.184   39.821 1.00 29.15 ?  303 LEU   A CG   1 
ATOM   1026 C  CD1  . LEU   A 1 151 ? 18.430 4.840   40.742 1.00 32.00 ?  303 LEU   A CD1  1 
ATOM   1027 C  CD2  . LEU   A 1 151 ? 17.302 4.962   38.523 1.00 25.91 ?  303 LEU   A CD2  1 
ATOM   1028 N  N    . GLU   A 1 152 ? 17.686 -0.382  38.364 1.00 18.27 ?  304 GLU   A N    1 
ATOM   1029 C  CA   . GLU   A 1 152 ? 18.400 -1.587  37.954 1.00 23.09 ?  304 GLU   A CA   1 
ATOM   1030 C  C    . GLU   A 1 152 ? 18.682 -1.595  36.455 1.00 25.73 ?  304 GLU   A C    1 
ATOM   1031 O  O    . GLU   A 1 152 ? 19.715 -2.118  36.018 1.00 26.59 ?  304 GLU   A O    1 
ATOM   1032 C  CB   . GLU   A 1 152 ? 17.593 -2.826  38.339 1.00 29.12 ?  304 GLU   A CB   1 
ATOM   1033 C  CG   . GLU   A 1 152 ? 17.745 -3.241  39.787 1.00 37.36 ?  304 GLU   A CG   1 
ATOM   1034 C  CD   . GLU   A 1 152 ? 18.981 -4.086  40.018 1.00 47.87 ?  304 GLU   A CD   1 
ATOM   1035 O  OE1  . GLU   A 1 152 ? 19.804 -4.220  39.085 1.00 48.89 ?  304 GLU   A OE1  1 
ATOM   1036 O  OE2  . GLU   A 1 152 ? 19.137 -4.610  41.142 1.00 53.21 ?  304 GLU   A OE2  1 
ATOM   1037 N  N    . LEU   A 1 153 ? 17.778 -1.027  35.656 1.00 21.93 ?  305 LEU   A N    1 
ATOM   1038 C  CA   . LEU   A 1 153 ? 17.969 -0.861  34.222 1.00 17.97 ?  305 LEU   A CA   1 
ATOM   1039 C  C    . LEU   A 1 153 ? 18.432 0.542   33.862 1.00 19.06 ?  305 LEU   A C    1 
ATOM   1040 O  O    . LEU   A 1 153 ? 19.356 0.708   33.062 1.00 21.87 ?  305 LEU   A O    1 
ATOM   1041 C  CB   . LEU   A 1 153 ? 16.662 -1.174  33.475 1.00 15.68 ?  305 LEU   A CB   1 
ATOM   1042 C  CG   . LEU   A 1 153 ? 16.619 -0.791  31.988 1.00 15.84 ?  305 LEU   A CG   1 
ATOM   1043 C  CD1  . LEU   A 1 153 ? 17.682 -1.535  31.204 1.00 13.85 ?  305 LEU   A CD1  1 
ATOM   1044 C  CD2  . LEU   A 1 153 ? 15.228 -1.015  31.370 1.00 16.77 ?  305 LEU   A CD2  1 
ATOM   1045 N  N    . ILE   A 1 154 ? 17.799 1.560   34.444 1.00 19.41 ?  306 ILE   A N    1 
ATOM   1046 C  CA   . ILE   A 1 154 ? 17.977 2.920   33.950 1.00 20.00 ?  306 ILE   A CA   1 
ATOM   1047 C  C    . ILE   A 1 154 ? 19.383 3.429   34.240 1.00 22.16 ?  306 ILE   A C    1 
ATOM   1048 O  O    . ILE   A 1 154 ? 20.004 4.084   33.393 1.00 24.08 ?  306 ILE   A O    1 
ATOM   1049 C  CB   . ILE   A 1 154 ? 16.903 3.839   34.551 1.00 22.91 ?  306 ILE   A CB   1 
ATOM   1050 C  CG1  . ILE   A 1 154 ? 15.514 3.408   34.075 1.00 21.82 ?  306 ILE   A CG1  1 
ATOM   1051 C  CG2  . ILE   A 1 154 ? 17.180 5.289   34.195 1.00 25.56 ?  306 ILE   A CG2  1 
ATOM   1052 C  CD1  . ILE   A 1 154 ? 14.396 3.915   34.963 1.00 15.69 ?  306 ILE   A CD1  1 
ATOM   1053 N  N    . GLU   A 1 155 ? 19.906 3.151   35.436 1.00 23.22 ?  307 GLU   A N    1 
ATOM   1054 C  CA   . GLU   A 1 155 ? 21.246 3.630   35.769 1.00 24.15 ?  307 GLU   A CA   1 
ATOM   1055 C  C    . GLU   A 1 155 ? 22.294 3.099   34.802 1.00 21.93 ?  307 GLU   A C    1 
ATOM   1056 O  O    . GLU   A 1 155 ? 23.054 3.911   34.247 1.00 25.79 ?  307 GLU   A O    1 
ATOM   1057 C  CB   . GLU   A 1 155 ? 21.576 3.291   37.230 1.00 29.37 ?  307 GLU   A CB   1 
ATOM   1058 C  CG   . GLU   A 1 155 ? 22.826 3.980   37.772 1.00 40.00 ?  307 GLU   A CG   1 
ATOM   1059 C  CD   . GLU   A 1 155 ? 24.068 3.105   37.698 1.00 47.97 ?  307 GLU   A CD   1 
ATOM   1060 O  OE1  . GLU   A 1 155 ? 25.129 3.526   38.205 1.00 53.08 ?  307 GLU   A OE1  1 
ATOM   1061 O  OE2  . GLU   A 1 155 ? 23.990 1.993   37.141 1.00 49.67 ?  307 GLU   A OE2  1 
ATOM   1062 N  N    . PRO   A 1 156 ? 22.395 1.792   34.537 1.00 21.94 ?  308 PRO   A N    1 
ATOM   1063 C  CA   . PRO   A 1 156 ? 23.324 1.352   33.482 1.00 22.84 ?  308 PRO   A CA   1 
ATOM   1064 C  C    . PRO   A 1 156 ? 22.957 1.875   32.101 1.00 23.12 ?  308 PRO   A C    1 
ATOM   1065 O  O    . PRO   A 1 156 ? 23.848 2.032   31.258 1.00 21.31 ?  308 PRO   A O    1 
ATOM   1066 C  CB   . PRO   A 1 156 ? 23.239 -0.180  33.547 1.00 25.59 ?  308 PRO   A CB   1 
ATOM   1067 C  CG   . PRO   A 1 156 ? 22.704 -0.479  34.917 1.00 22.71 ?  308 PRO   A CG   1 
ATOM   1068 C  CD   . PRO   A 1 156 ? 21.780 0.646   35.235 1.00 19.48 ?  308 PRO   A CD   1 
ATOM   1069 N  N    . LEU   A 1 157 ? 21.673 2.151   31.841 1.00 22.81 ?  309 LEU   A N    1 
ATOM   1070 C  CA   . LEU   A 1 157 ? 21.280 2.692   30.542 1.00 20.35 ?  309 LEU   A CA   1 
ATOM   1071 C  C    . LEU   A 1 157 ? 21.813 4.107   30.346 1.00 21.58 ?  309 LEU   A C    1 
ATOM   1072 O  O    . LEU   A 1 157 ? 22.304 4.445   29.260 1.00 21.80 ?  309 LEU   A O    1 
ATOM   1073 C  CB   . LEU   A 1 157 ? 19.757 2.671   30.396 1.00 21.49 ?  309 LEU   A CB   1 
ATOM   1074 C  CG   . LEU   A 1 157 ? 19.229 3.315   29.109 1.00 22.18 ?  309 LEU   A CG   1 
ATOM   1075 C  CD1  . LEU   A 1 157 ? 19.822 2.633   27.881 1.00 17.23 ?  309 LEU   A CD1  1 
ATOM   1076 C  CD2  . LEU   A 1 157 ? 17.706 3.305   29.055 1.00 20.34 ?  309 LEU   A CD2  1 
ATOM   1077 N  N    . ILE   A 1 158 ? 21.735 4.942   31.387 1.00 23.28 ?  310 ILE   A N    1 
ATOM   1078 C  CA   . ILE   A 1 158 ? 22.228 6.316   31.297 1.00 24.64 ?  310 ILE   A CA   1 
ATOM   1079 C  C    . ILE   A 1 158 ? 23.744 6.336   31.122 1.00 26.80 ?  310 ILE   A C    1 
ATOM   1080 O  O    . ILE   A 1 158 ? 24.283 7.087   30.297 1.00 27.67 ?  310 ILE   A O    1 
ATOM   1081 C  CB   . ILE   A 1 158 ? 21.807 7.117   32.541 1.00 26.40 ?  310 ILE   A CB   1 
ATOM   1082 C  CG1  . ILE   A 1 158 ? 20.296 7.367   32.552 1.00 27.42 ?  310 ILE   A CG1  1 
ATOM   1083 C  CG2  . ILE   A 1 158 ? 22.581 8.423   32.606 1.00 23.89 ?  310 ILE   A CG2  1 
ATOM   1084 C  CD1  . ILE   A 1 158 ? 19.840 8.420   31.567 1.00 30.57 ?  310 ILE   A CD1  1 
ATOM   1085 N  N    . LYS   A 1 159 ? 24.457 5.527   31.908 1.00 23.27 ?  311 LYS   A N    1 
ATOM   1086 C  CA   . LYS   A 1 159 ? 25.911 5.503   31.792 1.00 28.27 ?  311 LYS   A CA   1 
ATOM   1087 C  C    . LYS   A 1 159 ? 26.347 4.935   30.449 1.00 31.27 ?  311 LYS   A C    1 
ATOM   1088 O  O    . LYS   A 1 159 ? 27.354 5.379   29.886 1.00 34.12 ?  311 LYS   A O    1 
ATOM   1089 C  CB   . LYS   A 1 159 ? 26.527 4.703   32.942 1.00 34.00 ?  311 LYS   A CB   1 
ATOM   1090 C  CG   . LYS   A 1 159 ? 26.326 5.335   34.327 1.00 45.52 ?  311 LYS   A CG   1 
ATOM   1091 C  CD   . LYS   A 1 159 ? 27.083 6.657   34.471 1.00 53.70 ?  311 LYS   A CD   1 
ATOM   1092 C  CE   . LYS   A 1 159 ? 26.205 7.749   35.079 1.00 56.72 ?  311 LYS   A CE   1 
ATOM   1093 N  NZ   . LYS   A 1 159 ? 26.681 9.119   34.723 1.00 58.05 ?  311 LYS   A NZ   1 
ATOM   1094 N  N    . PHE   A 1 160 ? 25.597 3.963   29.921 1.00 30.73 ?  312 PHE   A N    1 
ATOM   1095 C  CA   . PHE   A 1 160 ? 25.843 3.480   28.567 1.00 26.94 ?  312 PHE   A CA   1 
ATOM   1096 C  C    . PHE   A 1 160 ? 25.763 4.623   27.565 1.00 23.74 ?  312 PHE   A C    1 
ATOM   1097 O  O    . PHE   A 1 160 ? 26.642 4.781   26.709 1.00 21.88 ?  312 PHE   A O    1 
ATOM   1098 C  CB   . PHE   A 1 160 ? 24.839 2.375   28.217 1.00 28.45 ?  312 PHE   A CB   1 
ATOM   1099 C  CG   . PHE   A 1 160 ? 24.842 1.983   26.760 1.00 24.88 ?  312 PHE   A CG   1 
ATOM   1100 C  CD1  . PHE   A 1 160 ? 25.663 0.965   26.306 1.00 24.60 ?  312 PHE   A CD1  1 
ATOM   1101 C  CD2  . PHE   A 1 160 ? 24.022 2.627   25.849 1.00 24.33 ?  312 PHE   A CD2  1 
ATOM   1102 C  CE1  . PHE   A 1 160 ? 25.672 0.602   24.966 1.00 23.08 ?  312 PHE   A CE1  1 
ATOM   1103 C  CE2  . PHE   A 1 160 ? 24.032 2.269   24.512 1.00 24.19 ?  312 PHE   A CE2  1 
ATOM   1104 C  CZ   . PHE   A 1 160 ? 24.858 1.257   24.074 1.00 21.43 ?  312 PHE   A CZ   1 
ATOM   1105 N  N    . GLN   A 1 161 ? 24.703 5.430   27.651 1.00 25.35 ?  313 GLN   A N    1 
ATOM   1106 C  CA   . GLN   A 1 161 ? 24.559 6.550   26.731 1.00 22.96 ?  313 GLN   A CA   1 
ATOM   1107 C  C    . GLN   A 1 161 ? 25.704 7.538   26.894 1.00 24.39 ?  313 GLN   A C    1 
ATOM   1108 O  O    . GLN   A 1 161 ? 26.207 8.083   25.905 1.00 23.37 ?  313 GLN   A O    1 
ATOM   1109 C  CB   . GLN   A 1 161 ? 23.219 7.248   26.949 1.00 20.38 ?  313 GLN   A CB   1 
ATOM   1110 C  CG   . GLN   A 1 161 ? 22.020 6.328   26.861 1.00 23.83 ?  313 GLN   A CG   1 
ATOM   1111 C  CD   . GLN   A 1 161 ? 21.846 5.734   25.481 1.00 22.31 ?  313 GLN   A CD   1 
ATOM   1112 O  OE1  . GLN   A 1 161 ? 22.179 6.361   24.479 1.00 25.88 ?  313 GLN   A OE1  1 
ATOM   1113 N  NE2  . GLN   A 1 161 ? 21.326 4.516   25.421 1.00 21.54 ?  313 GLN   A NE2  1 
ATOM   1114 N  N    . VAL   A 1 162 ? 26.128 7.779   28.137 1.00 25.65 ?  314 VAL   A N    1 
ATOM   1115 C  CA   . VAL   A 1 162 ? 27.222 8.713   28.383 1.00 23.46 ?  314 VAL   A CA   1 
ATOM   1116 C  C    . VAL   A 1 162 ? 28.524 8.164   27.815 1.00 26.66 ?  314 VAL   A C    1 
ATOM   1117 O  O    . VAL   A 1 162 ? 29.262 8.873   27.121 1.00 27.88 ?  314 VAL   A O    1 
ATOM   1118 C  CB   . VAL   A 1 162 ? 27.339 9.021   29.888 1.00 26.81 ?  314 VAL   A CB   1 
ATOM   1119 C  CG1  . VAL   A 1 162 ? 28.705 9.638   30.214 1.00 25.09 ?  314 VAL   A CG1  1 
ATOM   1120 C  CG2  . VAL   A 1 162 ? 26.212 9.944   30.319 1.00 24.62 ?  314 VAL   A CG2  1 
ATOM   1121 N  N    . GLY   A 1 163 ? 28.821 6.892   28.091 1.00 25.31 ?  315 GLY   A N    1 
ATOM   1122 C  CA   . GLY   A 1 163 ? 30.008 6.284   27.513 1.00 26.00 ?  315 GLY   A CA   1 
ATOM   1123 C  C    . GLY   A 1 163 ? 30.006 6.331   25.997 1.00 30.57 ?  315 GLY   A C    1 
ATOM   1124 O  O    . GLY   A 1 163 ? 31.033 6.604   25.373 1.00 31.16 ?  315 GLY   A O    1 
ATOM   1125 N  N    . LEU   A 1 164 ? 28.849 6.069   25.385 1.00 31.20 ?  316 LEU   A N    1 
ATOM   1126 C  CA   . LEU   A 1 164 ? 28.724 6.172   23.935 1.00 29.68 ?  316 LEU   A CA   1 
ATOM   1127 C  C    . LEU   A 1 164 ? 29.058 7.578   23.456 1.00 29.49 ?  316 LEU   A C    1 
ATOM   1128 O  O    . LEU   A 1 164 ? 29.803 7.757   22.484 1.00 29.75 ?  316 LEU   A O    1 
ATOM   1129 C  CB   . LEU   A 1 164 ? 27.306 5.789   23.514 1.00 31.25 ?  316 LEU   A CB   1 
ATOM   1130 C  CG   . LEU   A 1 164 ? 27.106 5.048   22.200 1.00 33.48 ?  316 LEU   A CG   1 
ATOM   1131 C  CD1  . LEU   A 1 164 ? 28.210 4.032   21.992 1.00 33.10 ?  316 LEU   A CD1  1 
ATOM   1132 C  CD2  . LEU   A 1 164 ? 25.730 4.382   22.191 1.00 32.43 ?  316 LEU   A CD2  1 
ATOM   1133 N  N    . LYS   A 1 165 ? 28.514 8.592   24.135 1.00 27.38 ?  317 LYS   A N    1 
ATOM   1134 C  CA   . LYS   A 1 165 ? 28.794 9.973   23.758 1.00 32.09 ?  317 LYS   A CA   1 
ATOM   1135 C  C    . LYS   A 1 165 ? 30.286 10.271  23.830 1.00 36.35 ?  317 LYS   A C    1 
ATOM   1136 O  O    . LYS   A 1 165 ? 30.834 10.940  22.945 1.00 36.44 ?  317 LYS   A O    1 
ATOM   1137 C  CB   . LYS   A 1 165 ? 28.020 10.935  24.658 1.00 37.37 ?  317 LYS   A CB   1 
ATOM   1138 C  CG   . LYS   A 1 165 ? 26.591 11.205  24.219 1.00 40.91 ?  317 LYS   A CG   1 
ATOM   1139 C  CD   . LYS   A 1 165 ? 26.536 11.886  22.863 1.00 40.44 ?  317 LYS   A CD   1 
ATOM   1140 C  CE   . LYS   A 1 165 ? 25.355 12.836  22.791 1.00 39.16 ?  317 LYS   A CE   1 
ATOM   1141 N  NZ   . LYS   A 1 165 ? 24.584 12.696  21.532 1.00 35.37 ?  317 LYS   A NZ   1 
ATOM   1142 N  N    . LYS   A 1 166 ? 30.960 9.775   24.877 1.00 33.22 ?  318 LYS   A N    1 
ATOM   1143 C  CA   . LYS   A 1 166 ? 32.391 10.028  25.030 1.00 34.53 ?  318 LYS   A CA   1 
ATOM   1144 C  C    . LYS   A 1 166 ? 33.182 9.547   23.824 1.00 29.49 ?  318 LYS   A C    1 
ATOM   1145 O  O    . LYS   A 1 166 ? 34.183 10.170  23.457 1.00 33.83 ?  318 LYS   A O    1 
ATOM   1146 C  CB   . LYS   A 1 166 ? 32.930 9.353   26.296 1.00 34.71 ?  318 LYS   A CB   1 
ATOM   1147 C  CG   . LYS   A 1 166 ? 32.191 9.677   27.584 1.00 36.88 ?  318 LYS   A CG   1 
ATOM   1148 C  CD   . LYS   A 1 166 ? 31.961 11.168  27.770 1.00 40.58 ?  318 LYS   A CD   1 
ATOM   1149 C  CE   . LYS   A 1 166 ? 31.773 11.500  29.249 1.00 45.17 ?  318 LYS   A CE   1 
ATOM   1150 N  NZ   . LYS   A 1 166 ? 31.607 12.963  29.494 1.00 48.53 ?  318 LYS   A NZ   1 
ATOM   1151 N  N    . LEU   A 1 167 ? 32.755 8.446   23.196 1.00 26.18 ?  319 LEU   A N    1 
ATOM   1152 C  CA   . LEU   A 1 167 ? 33.498 7.884   22.070 1.00 31.04 ?  319 LEU   A CA   1 
ATOM   1153 C  C    . LEU   A 1 167 ? 33.533 8.811   20.862 1.00 31.53 ?  319 LEU   A C    1 
ATOM   1154 O  O    . LEU   A 1 167 ? 34.446 8.689   20.038 1.00 35.09 ?  319 LEU   A O    1 
ATOM   1155 C  CB   . LEU   A 1 167 ? 32.903 6.535   21.656 1.00 32.39 ?  319 LEU   A CB   1 
ATOM   1156 C  CG   . LEU   A 1 167 ? 33.083 5.393   22.656 1.00 33.75 ?  319 LEU   A CG   1 
ATOM   1157 C  CD1  . LEU   A 1 167 ? 32.664 4.063   22.046 1.00 28.86 ?  319 LEU   A CD1  1 
ATOM   1158 C  CD2  . LEU   A 1 167 ? 34.524 5.341   23.135 1.00 34.14 ?  319 LEU   A CD2  1 
ATOM   1159 N  N    . ASN   A 1 168 ? 32.567 9.720   20.731 1.00 29.55 ?  320 ASN   A N    1 
ATOM   1160 C  CA   . ASN   A 1 168 ? 32.531 10.673  19.624 1.00 37.40 ?  320 ASN   A CA   1 
ATOM   1161 C  C    . ASN   A 1 168 ? 32.559 9.942   18.278 1.00 35.84 ?  320 ASN   A C    1 
ATOM   1162 O  O    . ASN   A 1 168 ? 33.419 10.180  17.428 1.00 38.69 ?  320 ASN   A O    1 
ATOM   1163 C  CB   . ASN   A 1 168 ? 33.688 11.674  19.737 1.00 40.92 ?  320 ASN   A CB   1 
ATOM   1164 C  CG   . ASN   A 1 168 ? 33.357 13.029  19.140 1.00 44.16 ?  320 ASN   A CG   1 
ATOM   1165 O  OD1  . ASN   A 1 168 ? 32.193 13.350  18.897 1.00 43.63 ?  320 ASN   A OD1  1 
ATOM   1166 N  ND2  . ASN   A 1 168 ? 34.388 13.836  18.906 1.00 46.29 ?  320 ASN   A ND2  1 
ATOM   1167 N  N    . LEU   A 1 169 ? 31.602 9.033   18.103 1.00 32.76 ?  321 LEU   A N    1 
ATOM   1168 C  CA   . LEU   A 1 169 ? 31.590 8.183   16.920 1.00 32.91 ?  321 LEU   A CA   1 
ATOM   1169 C  C    . LEU   A 1 169 ? 31.165 8.966   15.689 1.00 33.40 ?  321 LEU   A C    1 
ATOM   1170 O  O    . LEU   A 1 169 ? 30.270 9.814   15.748 1.00 35.14 ?  321 LEU   A O    1 
ATOM   1171 C  CB   . LEU   A 1 169 ? 30.647 6.996   17.113 1.00 34.04 ?  321 LEU   A CB   1 
ATOM   1172 C  CG   . LEU   A 1 169 ? 31.054 5.934   18.133 1.00 34.70 ?  321 LEU   A CG   1 
ATOM   1173 C  CD1  . LEU   A 1 169 ? 30.034 4.808   18.161 1.00 32.56 ?  321 LEU   A CD1  1 
ATOM   1174 C  CD2  . LEU   A 1 169 ? 32.440 5.407   17.817 1.00 33.47 ?  321 LEU   A CD2  1 
ATOM   1175 N  N    . HIS   A 1 170 ? 31.829 8.685   14.570 1.00 32.18 ?  322 HIS   A N    1 
ATOM   1176 C  CA   . HIS   A 1 170 ? 31.311 9.107   13.279 1.00 30.56 ?  322 HIS   A CA   1 
ATOM   1177 C  C    . HIS   A 1 170 ? 29.988 8.404   13.016 1.00 25.33 ?  322 HIS   A C    1 
ATOM   1178 O  O    . HIS   A 1 170 ? 29.755 7.285   13.480 1.00 26.05 ?  322 HIS   A O    1 
ATOM   1179 C  CB   . HIS   A 1 170 ? 32.300 8.768   12.160 1.00 35.24 ?  322 HIS   A CB   1 
ATOM   1180 C  CG   . HIS   A 1 170 ? 33.500 9.659   12.113 1.00 39.89 ?  322 HIS   A CG   1 
ATOM   1181 N  ND1  . HIS   A 1 170 ? 34.110 10.020  10.931 1.00 42.33 ?  322 HIS   A ND1  1 
ATOM   1182 C  CD2  . HIS   A 1 170 ? 34.211 10.252  13.101 1.00 41.91 ?  322 HIS   A CD2  1 
ATOM   1183 C  CE1  . HIS   A 1 170 ? 35.139 10.806  11.193 1.00 44.23 ?  322 HIS   A CE1  1 
ATOM   1184 N  NE2  . HIS   A 1 170 ? 35.222 10.962  12.502 1.00 42.97 ?  322 HIS   A NE2  1 
ATOM   1185 N  N    . GLU   A 1 171 ? 29.114 9.066   12.258 1.00 27.74 ?  323 GLU   A N    1 
ATOM   1186 C  CA   . GLU   A 1 171 ? 27.883 8.406   11.838 1.00 29.19 ?  323 GLU   A CA   1 
ATOM   1187 C  C    . GLU   A 1 171 ? 28.187 7.085   11.140 1.00 29.01 ?  323 GLU   A C    1 
ATOM   1188 O  O    . GLU   A 1 171 ? 27.469 6.094   11.331 1.00 25.81 ?  323 GLU   A O    1 
ATOM   1189 C  CB   . GLU   A 1 171 ? 27.074 9.328   10.925 1.00 34.80 ?  323 GLU   A CB   1 
ATOM   1190 C  CG   . GLU   A 1 171 ? 25.679 8.807   10.614 1.00 40.86 ?  323 GLU   A CG   1 
ATOM   1191 C  CD   . GLU   A 1 171 ? 24.803 9.846   9.948  1.00 47.98 ?  323 GLU   A CD   1 
ATOM   1192 O  OE1  . GLU   A 1 171 ? 23.571 9.803   10.145 1.00 51.20 ?  323 GLU   A OE1  1 
ATOM   1193 O  OE2  . GLU   A 1 171 ? 25.347 10.710  9.231  1.00 53.17 ?  323 GLU   A OE2  1 
ATOM   1194 N  N    . GLU   A 1 172 ? 29.276 7.048   10.357 1.00 25.78 ?  324 GLU   A N    1 
ATOM   1195 C  CA   . GLU   A 1 172 ? 29.684 5.825   9.665  1.00 20.38 ?  324 GLU   A CA   1 
ATOM   1196 C  C    . GLU   A 1 172 ? 29.887 4.673   10.639 1.00 22.20 ?  324 GLU   A C    1 
ATOM   1197 O  O    . GLU   A 1 172 ? 29.388 3.565   10.419 1.00 25.78 ?  324 GLU   A O    1 
ATOM   1198 C  CB   . GLU   A 1 172 ? 30.973 6.073   8.875  1.00 21.79 ?  324 GLU   A CB   1 
ATOM   1199 C  CG   . GLU   A 1 172 ? 30.805 6.945   7.643  1.00 26.02 ?  324 GLU   A CG   1 
ATOM   1200 C  CD   . GLU   A 1 172 ? 30.755 8.429   7.965  1.00 32.51 ?  324 GLU   A CD   1 
ATOM   1201 O  OE1  . GLU   A 1 172 ? 30.811 9.234   7.012  1.00 36.63 ?  324 GLU   A OE1  1 
ATOM   1202 O  OE2  . GLU   A 1 172 ? 30.658 8.793   9.159  1.00 31.40 ?  324 GLU   A OE2  1 
ATOM   1203 N  N    . GLU   A 1 173 ? 30.649 4.905   11.712 1.00 20.32 ?  325 GLU   A N    1 
ATOM   1204 C  CA   . GLU   A 1 173 ? 30.876 3.841   12.684 1.00 22.62 ?  325 GLU   A CA   1 
ATOM   1205 C  C    . GLU   A 1 173 ? 29.614 3.529   13.482 1.00 19.62 ?  325 GLU   A C    1 
ATOM   1206 O  O    . GLU   A 1 173 ? 29.413 2.381   13.894 1.00 19.61 ?  325 GLU   A O    1 
ATOM   1207 C  CB   . GLU   A 1 173 ? 32.025 4.224   13.614 1.00 33.95 ?  325 GLU   A CB   1 
ATOM   1208 C  CG   . GLU   A 1 173 ? 33.216 4.817   12.879 1.00 35.41 ?  325 GLU   A CG   1 
ATOM   1209 C  CD   . GLU   A 1 173 ? 34.032 5.751   13.743 1.00 38.51 ?  325 GLU   A CD   1 
ATOM   1210 O  OE1  . GLU   A 1 173 ? 35.278 5.698   13.656 1.00 42.76 ?  325 GLU   A OE1  1 
ATOM   1211 O  OE2  . GLU   A 1 173 ? 33.430 6.538   14.507 1.00 37.64 ?  325 GLU   A OE2  1 
ATOM   1212 N  N    . HIS   A 1 174 ? 28.751 4.528   13.688 1.00 17.99 ?  326 HIS   A N    1 
ATOM   1213 C  CA   . HIS   A 1 174 ? 27.483 4.310   14.379 1.00 18.86 ?  326 HIS   A CA   1 
ATOM   1214 C  C    . HIS   A 1 174 ? 26.587 3.338   13.614 1.00 19.18 ?  326 HIS   A C    1 
ATOM   1215 O  O    . HIS   A 1 174 ? 26.036 2.394   14.196 1.00 18.52 ?  326 HIS   A O    1 
ATOM   1216 C  CB   . HIS   A 1 174 ? 26.774 5.650   14.585 1.00 23.05 ?  326 HIS   A CB   1 
ATOM   1217 C  CG   . HIS   A 1 174 ? 25.452 5.545   15.288 1.00 27.24 ?  326 HIS   A CG   1 
ATOM   1218 N  ND1  . HIS   A 1 174 ? 25.338 5.179   16.612 1.00 27.28 ?  326 HIS   A ND1  1 
ATOM   1219 C  CD2  . HIS   A 1 174 ? 24.190 5.777   14.854 1.00 26.57 ?  326 HIS   A CD2  1 
ATOM   1220 C  CE1  . HIS   A 1 174 ? 24.065 5.184   16.963 1.00 26.34 ?  326 HIS   A CE1  1 
ATOM   1221 N  NE2  . HIS   A 1 174 ? 23.347 5.544   15.914 1.00 28.35 ?  326 HIS   A NE2  1 
ATOM   1222 N  N    . VAL   A 1 175 ? 26.419 3.552   12.304 1.00 20.91 ?  327 VAL   A N    1 
ATOM   1223 C  CA   . VAL   A 1 175 ? 25.528 2.670   11.554 1.00 15.28 ?  327 VAL   A CA   1 
ATOM   1224 C  C    . VAL   A 1 175 ? 26.163 1.302   11.365 1.00 15.26 ?  327 VAL   A C    1 
ATOM   1225 O  O    . VAL   A 1 175 ? 25.457 0.289   11.304 1.00 15.73 ?  327 VAL   A O    1 
ATOM   1226 C  CB   . VAL   A 1 175 ? 25.126 3.302   10.207 1.00 20.20 ?  327 VAL   A CB   1 
ATOM   1227 C  CG1  . VAL   A 1 175 ? 24.447 4.641   10.443 1.00 20.17 ?  327 VAL   A CG1  1 
ATOM   1228 C  CG2  . VAL   A 1 175 ? 26.341 3.455   9.291  1.00 19.91 ?  327 VAL   A CG2  1 
ATOM   1229 N  N    . LEU   A 1 176 ? 27.493 1.238   11.264 1.00 19.22 ?  328 LEU   A N    1 
ATOM   1230 C  CA   . LEU   A 1 176 ? 28.157 -0.059  11.223 1.00 15.41 ?  328 LEU   A CA   1 
ATOM   1231 C  C    . LEU   A 1 176 ? 27.923 -0.826  12.520 1.00 14.65 ?  328 LEU   A C    1 
ATOM   1232 O  O    . LEU   A 1 176 ? 27.698 -2.041  12.501 1.00 16.39 ?  328 LEU   A O    1 
ATOM   1233 C  CB   . LEU   A 1 176 ? 29.653 0.130   10.956 1.00 14.28 ?  328 LEU   A CB   1 
ATOM   1234 C  CG   . LEU   A 1 176 ? 30.030 0.333   9.481  1.00 15.60 ?  328 LEU   A CG   1 
ATOM   1235 C  CD1  . LEU   A 1 176 ? 31.435 0.906   9.334  1.00 15.16 ?  328 LEU   A CD1  1 
ATOM   1236 C  CD2  . LEU   A 1 176 ? 29.903 -0.976  8.717  1.00 14.21 ?  328 LEU   A CD2  1 
ATOM   1237 N  N    . LEU   A 1 177 ? 27.965 -0.126  13.655 1.00 18.59 ?  329 LEU   A N    1 
ATOM   1238 C  CA   . LEU   A 1 177 ? 27.731 -0.765  14.948 1.00 20.80 ?  329 LEU   A CA   1 
ATOM   1239 C  C    . LEU   A 1 177 ? 26.312 -1.307  15.054 1.00 18.19 ?  329 LEU   A C    1 
ATOM   1240 O  O    . LEU   A 1 177 ? 26.096 -2.423  15.546 1.00 15.82 ?  329 LEU   A O    1 
ATOM   1241 C  CB   . LEU   A 1 177 ? 28.002 0.235   16.069 1.00 26.55 ?  329 LEU   A CB   1 
ATOM   1242 C  CG   . LEU   A 1 177 ? 28.662 -0.305  17.331 1.00 32.13 ?  329 LEU   A CG   1 
ATOM   1243 C  CD1  . LEU   A 1 177 ? 30.089 -0.703  17.023 1.00 31.85 ?  329 LEU   A CD1  1 
ATOM   1244 C  CD2  . LEU   A 1 177 ? 28.607 0.743   18.436 1.00 32.49 ?  329 LEU   A CD2  1 
ATOM   1245 N  N    . MET   A 1 178 ? 25.325 -0.528  14.599 1.00 15.51 ?  330 MET   A N    1 
ATOM   1246 C  CA   . MET   A 1 178 ? 23.947 -1.006  14.629 1.00 15.46 ?  330 MET   A CA   1 
ATOM   1247 C  C    . MET   A 1 178 ? 23.785 -2.256  13.776 1.00 15.28 ?  330 MET   A C    1 
ATOM   1248 O  O    . MET   A 1 178 ? 23.096 -3.206  14.174 1.00 15.15 ?  330 MET   A O    1 
ATOM   1249 C  CB   . MET   A 1 178 ? 22.994 0.095   14.165 1.00 17.67 ?  330 MET   A CB   1 
ATOM   1250 C  CG   . MET   A 1 178 ? 22.913 1.280   15.117 1.00 18.23 ?  330 MET   A CG   1 
ATOM   1251 S  SD   . MET   A 1 178 ? 21.587 2.424   14.690 1.00 27.54 ?  330 MET   A SD   1 
ATOM   1252 C  CE   . MET   A 1 178 ? 22.240 3.155   13.191 1.00 22.31 ?  330 MET   A CE   1 
ATOM   1253 N  N    . ALA   A 1 179 ? 24.446 -2.292  12.615 1.00 11.96 ?  331 ALA   A N    1 
ATOM   1254 C  CA   . ALA   A 1 179 ? 24.326 -3.451  11.737 1.00 14.42 ?  331 ALA   A CA   1 
ATOM   1255 C  C    . ALA   A 1 179 ? 25.014 -4.673  12.332 1.00 12.23 ?  331 ALA   A C    1 
ATOM   1256 O  O    . ALA   A 1 179 ? 24.505 -5.797  12.218 1.00 11.46 ?  331 ALA   A O    1 
ATOM   1257 C  CB   . ALA   A 1 179 ? 24.900 -3.125  10.353 1.00 11.30 ?  331 ALA   A CB   1 
ATOM   1258 N  N    . ILE   A 1 180 ? 26.173 -4.475  12.967 1.00 12.60 ?  332 ILE   A N    1 
ATOM   1259 C  CA   . ILE   A 1 180 ? 26.890 -5.588  13.579 1.00 14.73 ?  332 ILE   A CA   1 
ATOM   1260 C  C    . ILE   A 1 180 ? 26.114 -6.124  14.773 1.00 15.40 ?  332 ILE   A C    1 
ATOM   1261 O  O    . ILE   A 1 180 ? 26.098 -7.334  15.037 1.00 20.19 ?  332 ILE   A O    1 
ATOM   1262 C  CB   . ILE   A 1 180 ? 28.315 -5.145  13.980 1.00 15.66 ?  332 ILE   A CB   1 
ATOM   1263 C  CG1  . ILE   A 1 180 ? 29.191 -4.958  12.747 1.00 15.18 ?  332 ILE   A CG1  1 
ATOM   1264 C  CG2  . ILE   A 1 180 ? 28.957 -6.142  14.943 1.00 14.61 ?  332 ILE   A CG2  1 
ATOM   1265 C  CD1  . ILE   A 1 180 ? 30.373 -4.036  12.990 1.00 16.23 ?  332 ILE   A CD1  1 
ATOM   1266 N  N    . CYS   A 1 181 ? 25.469 -5.230  15.522 1.00 15.84 ?  333 CYS   A N    1 
ATOM   1267 C  CA   . CYS   A 1 181 ? 24.600 -5.652  16.615 1.00 18.27 ?  333 CYS   A CA   1 
ATOM   1268 C  C    . CYS   A 1 181 ? 23.495 -6.586  16.121 1.00 18.57 ?  333 CYS   A C    1 
ATOM   1269 O  O    . CYS   A 1 181 ? 23.191 -7.599  16.764 1.00 16.95 ?  333 CYS   A O    1 
ATOM   1270 C  CB   . CYS   A 1 181 ? 24.009 -4.418  17.292 1.00 20.11 ?  333 CYS   A CB   1 
ATOM   1271 S  SG   . CYS   A 1 181 ? 22.864 -4.741  18.627 1.00 20.70 ?  333 CYS   A SG   1 
ATOM   1272 N  N    . ILE   A 1 182 ? 22.901 -6.277  14.965 1.00 19.48 ?  334 ILE   A N    1 
ATOM   1273 C  CA   . ILE   A 1 182 ? 21.761 -7.055  14.476 1.00 16.07 ?  334 ILE   A CA   1 
ATOM   1274 C  C    . ILE   A 1 182 ? 22.208 -8.428  13.978 1.00 17.82 ?  334 ILE   A C    1 
ATOM   1275 O  O    . ILE   A 1 182 ? 21.648 -9.460  14.369 1.00 17.07 ?  334 ILE   A O    1 
ATOM   1276 C  CB   . ILE   A 1 182 ? 21.015 -6.275  13.378 1.00 16.97 ?  334 ILE   A CB   1 
ATOM   1277 C  CG1  . ILE   A 1 182 ? 20.238 -5.110  13.989 1.00 17.77 ?  334 ILE   A CG1  1 
ATOM   1278 C  CG2  . ILE   A 1 182 ? 20.083 -7.206  12.580 1.00 16.62 ?  334 ILE   A CG2  1 
ATOM   1279 C  CD1  . ILE   A 1 182 ? 20.049 -3.939  13.058 1.00 17.34 ?  334 ILE   A CD1  1 
ATOM   1280 N  N    A VAL   A 1 183 ? 23.211 -8.468  13.100 0.38 16.36 ?  335 VAL   A N    1 
ATOM   1281 N  N    B VAL   A 1 183 ? 23.229 -8.457  13.125 0.62 15.57 ?  335 VAL   A N    1 
ATOM   1282 C  CA   A VAL   A 1 183 ? 23.623 -9.734  12.500 0.38 18.53 ?  335 VAL   A CA   1 
ATOM   1283 C  CA   B VAL   A 1 183 ? 23.690 -9.709  12.499 0.62 18.49 ?  335 VAL   A CA   1 
ATOM   1284 C  C    A VAL   A 1 183 ? 24.703 -10.375 13.371 0.38 20.76 ?  335 VAL   A C    1 
ATOM   1285 C  C    B VAL   A 1 183 ? 24.749 -10.291 13.429 0.62 21.31 ?  335 VAL   A C    1 
ATOM   1286 O  O    A VAL   A 1 183 ? 25.896 -10.368 13.042 0.38 20.08 ?  335 VAL   A O    1 
ATOM   1287 O  O    B VAL   A 1 183 ? 25.955 -10.184 13.208 0.62 19.45 ?  335 VAL   A O    1 
ATOM   1288 C  CB   A VAL   A 1 183 ? 24.064 -9.536  11.031 0.38 19.29 ?  335 VAL   A CB   1 
ATOM   1289 C  CB   B VAL   A 1 183 ? 24.211 -9.479  11.073 0.62 19.51 ?  335 VAL   A CB   1 
ATOM   1290 C  CG1  A VAL   A 1 183 ? 25.176 -8.509  10.903 0.38 17.63 ?  335 VAL   A CG1  1 
ATOM   1291 C  CG1  B VAL   A 1 183 ? 24.418 -10.800 10.351 0.62 19.63 ?  335 VAL   A CG1  1 
ATOM   1292 C  CG2  A VAL   A 1 183 ? 24.438 -10.860 10.370 0.38 19.79 ?  335 VAL   A CG2  1 
ATOM   1293 C  CG2  B VAL   A 1 183 ? 23.245 -8.582  10.281 0.62 18.16 ?  335 VAL   A CG2  1 
ATOM   1294 N  N    . SER   A 1 184 ? 24.284 -10.927 14.504 1.00 21.95 ?  336 SER   A N    1 
ATOM   1295 C  CA   . SER   A 1 184 ? 25.175 -11.605 15.431 1.00 25.51 ?  336 SER   A CA   1 
ATOM   1296 C  C    . SER   A 1 184 ? 24.864 -13.093 15.443 1.00 22.63 ?  336 SER   A C    1 
ATOM   1297 O  O    . SER   A 1 184 ? 23.708 -13.476 15.668 1.00 18.78 ?  336 SER   A O    1 
ATOM   1298 C  CB   . SER   A 1 184 ? 25.052 -11.029 16.846 1.00 29.22 ?  336 SER   A CB   1 
ATOM   1299 O  OG   . SER   A 1 184 ? 25.210 -9.622  16.831 1.00 32.88 ?  336 SER   A OG   1 
ATOM   1300 N  N    . PRO   A 1 185 ? 25.851 -13.960 15.185 1.00 23.04 ?  337 PRO   A N    1 
ATOM   1301 C  CA   . PRO   A 1 185 ? 25.574 -15.407 15.129 1.00 22.61 ?  337 PRO   A CA   1 
ATOM   1302 C  C    . PRO   A 1 185 ? 25.323 -16.044 16.485 1.00 23.21 ?  337 PRO   A C    1 
ATOM   1303 O  O    . PRO   A 1 185 ? 24.952 -17.221 16.523 1.00 25.54 ?  337 PRO   A O    1 
ATOM   1304 C  CB   . PRO   A 1 185 ? 26.838 -15.987 14.473 1.00 21.31 ?  337 PRO   A CB   1 
ATOM   1305 C  CG   . PRO   A 1 185 ? 27.912 -14.984 14.714 1.00 21.10 ?  337 PRO   A CG   1 
ATOM   1306 C  CD   . PRO   A 1 185 ? 27.236 -13.635 14.796 1.00 21.07 ?  337 PRO   A CD   1 
ATOM   1307 N  N    . ASP   A 1 186 ? 25.498 -15.317 17.590 1.00 24.02 ?  338 ASP   A N    1 
ATOM   1308 C  CA   . ASP   A 1 186 ? 25.333 -15.880 18.924 1.00 33.48 ?  338 ASP   A CA   1 
ATOM   1309 C  C    . ASP   A 1 186 ? 23.968 -15.572 19.536 1.00 32.79 ?  338 ASP   A C    1 
ATOM   1310 O  O    . ASP   A 1 186 ? 23.810 -15.661 20.758 1.00 38.07 ?  338 ASP   A O    1 
ATOM   1311 C  CB   . ASP   A 1 186 ? 26.446 -15.386 19.851 1.00 35.06 ?  338 ASP   A CB   1 
ATOM   1312 C  CG   . ASP   A 1 186 ? 26.580 -13.878 19.847 1.00 36.67 ?  338 ASP   A CG   1 
ATOM   1313 O  OD1  . ASP   A 1 186 ? 27.155 -13.328 20.809 1.00 37.40 ?  338 ASP   A OD1  1 
ATOM   1314 O  OD2  . ASP   A 1 186 ? 26.115 -13.239 18.877 1.00 39.00 ?  338 ASP   A OD2  1 
ATOM   1315 N  N    . ARG   A 1 187 ? 22.986 -15.211 18.723 1.00 29.14 ?  339 ARG   A N    1 
ATOM   1316 C  CA   . ARG   A 1 187 ? 21.646 -15.020 19.266 1.00 27.08 ?  339 ARG   A CA   1 
ATOM   1317 C  C    . ARG   A 1 187 ? 20.953 -16.370 19.440 1.00 24.70 ?  339 ARG   A C    1 
ATOM   1318 O  O    . ARG   A 1 187 ? 21.100 -17.257 18.596 1.00 24.75 ?  339 ARG   A O    1 
ATOM   1319 C  CB   . ARG   A 1 187 ? 20.805 -14.135 18.346 1.00 25.15 ?  339 ARG   A CB   1 
ATOM   1320 C  CG   . ARG   A 1 187 ? 21.426 -12.795 18.020 1.00 27.70 ?  339 ARG   A CG   1 
ATOM   1321 C  CD   . ARG   A 1 187 ? 21.371 -11.861 19.207 1.00 29.93 ?  339 ARG   A CD   1 
ATOM   1322 N  NE   . ARG   A 1 187 ? 21.793 -10.511 18.850 1.00 30.26 ?  339 ARG   A NE   1 
ATOM   1323 C  CZ   . ARG   A 1 187 ? 21.737 -9.474  19.678 1.00 30.77 ?  339 ARG   A CZ   1 
ATOM   1324 N  NH1  . ARG   A 1 187 ? 22.149 -8.275  19.282 1.00 31.14 ?  339 ARG   A NH1  1 
ATOM   1325 N  NH2  . ARG   A 1 187 ? 21.270 -9.638  20.906 1.00 32.11 ?  339 ARG   A NH2  1 
ATOM   1326 N  N    . PRO   A 1 188 ? 20.183 -16.547 20.510 1.00 25.09 ?  340 PRO   A N    1 
ATOM   1327 C  CA   . PRO   A 1 188 ? 19.423 -17.792 20.660 1.00 27.48 ?  340 PRO   A CA   1 
ATOM   1328 C  C    . PRO   A 1 188 ? 18.464 -17.971 19.495 1.00 28.30 ?  340 PRO   A C    1 
ATOM   1329 O  O    . PRO   A 1 188 ? 17.867 -17.011 19.009 1.00 28.77 ?  340 PRO   A O    1 
ATOM   1330 C  CB   . PRO   A 1 188 ? 18.674 -17.599 21.984 1.00 25.56 ?  340 PRO   A CB   1 
ATOM   1331 C  CG   . PRO   A 1 188 ? 19.400 -16.481 22.684 1.00 26.18 ?  340 PRO   A CG   1 
ATOM   1332 C  CD   . PRO   A 1 188 ? 19.903 -15.594 21.593 1.00 25.37 ?  340 PRO   A CD   1 
ATOM   1333 N  N    . GLY   A 1 189 ? 18.351 -19.211 19.025 1.00 31.53 ?  341 GLY   A N    1 
ATOM   1334 C  CA   . GLY   A 1 189 ? 17.435 -19.548 17.960 1.00 34.16 ?  341 GLY   A CA   1 
ATOM   1335 C  C    . GLY   A 1 189 ? 17.987 -19.432 16.556 1.00 35.73 ?  341 GLY   A C    1 
ATOM   1336 O  O    . GLY   A 1 189 ? 17.290 -19.811 15.607 1.00 38.75 ?  341 GLY   A O    1 
ATOM   1337 N  N    . VAL   A 1 190 ? 19.212 -18.932 16.388 1.00 37.57 ?  342 VAL   A N    1 
ATOM   1338 C  CA   . VAL   A 1 190 ? 19.761 -18.710 15.054 1.00 35.86 ?  342 VAL   A CA   1 
ATOM   1339 C  C    . VAL   A 1 190 ? 20.016 -20.048 14.369 1.00 38.20 ?  342 VAL   A C    1 
ATOM   1340 O  O    . VAL   A 1 190 ? 20.586 -20.971 14.966 1.00 38.05 ?  342 VAL   A O    1 
ATOM   1341 C  CB   . VAL   A 1 190 ? 21.037 -17.860 15.140 1.00 32.92 ?  342 VAL   A CB   1 
ATOM   1342 C  CG1  . VAL   A 1 190 ? 21.921 -18.088 13.925 1.00 36.78 ?  342 VAL   A CG1  1 
ATOM   1343 C  CG2  . VAL   A 1 190 ? 20.674 -16.389 15.262 1.00 27.30 ?  342 VAL   A CG2  1 
ATOM   1344 N  N    . GLN   A 1 191 ? 19.576 -20.160 13.109 1.00 40.32 ?  343 GLN   A N    1 
ATOM   1345 C  CA   . GLN   A 1 191 ? 19.697 -21.400 12.324 1.00 42.49 ?  343 GLN   A CA   1 
ATOM   1346 C  C    . GLN   A 1 191 ? 21.038 -21.468 11.602 1.00 40.04 ?  343 GLN   A C    1 
ATOM   1347 O  O    . GLN   A 1 191 ? 21.865 -22.341 11.880 1.00 45.27 ?  343 GLN   A O    1 
ATOM   1348 C  CB   . GLN   A 1 191 ? 18.565 -21.498 11.299 1.00 47.71 ?  343 GLN   A CB   1 
ATOM   1349 C  CG   . GLN   A 1 191 ? 17.226 -21.995 11.809 1.00 53.33 ?  343 GLN   A CG   1 
ATOM   1350 C  CD   . GLN   A 1 191 ? 16.201 -22.095 10.687 1.00 57.40 ?  343 GLN   A CD   1 
ATOM   1351 O  OE1  . GLN   A 1 191 ? 15.050 -22.470 10.911 1.00 59.65 ?  343 GLN   A OE1  1 
ATOM   1352 N  NE2  . GLN   A 1 191 ? 16.622 -21.757 9.469  1.00 57.00 ?  343 GLN   A NE2  1 
ATOM   1353 N  N    . ASP   A 1 192 ? 21.240 -20.568 10.641 1.00 32.95 ?  344 ASP   A N    1 
ATOM   1354 C  CA   . ASP   A 1 192 ? 22.444 -20.538 9.814  1.00 29.96 ?  344 ASP   A CA   1 
ATOM   1355 C  C    . ASP   A 1 192 ? 23.460 -19.590 10.450 1.00 27.98 ?  344 ASP   A C    1 
ATOM   1356 O  O    . ASP   A 1 192 ? 23.750 -18.499 9.953  1.00 27.54 ?  344 ASP   A O    1 
ATOM   1357 C  CB   . ASP   A 1 192 ? 22.094 -20.123 8.390  1.00 29.72 ?  344 ASP   A CB   1 
ATOM   1358 C  CG   . ASP   A 1 192 ? 23.175 -20.489 7.382  1.00 33.05 ?  344 ASP   A CG   1 
ATOM   1359 O  OD1  . ASP   A 1 192 ? 22.868 -20.518 6.169  1.00 32.99 ?  344 ASP   A OD1  1 
ATOM   1360 O  OD2  . ASP   A 1 192 ? 24.328 -20.736 7.795  1.00 33.02 ?  344 ASP   A OD2  1 
ATOM   1361 N  N    . ALA   A 1 193 ? 23.996 -20.038 11.592 1.00 26.54 ?  345 ALA   A N    1 
ATOM   1362 C  CA   . ALA   A 1 193 ? 24.964 -19.231 12.330 1.00 28.29 ?  345 ALA   A CA   1 
ATOM   1363 C  C    . ALA   A 1 193 ? 26.160 -18.862 11.463 1.00 25.15 ?  345 ALA   A C    1 
ATOM   1364 O  O    . ALA   A 1 193 ? 26.682 -17.746 11.560 1.00 23.90 ?  345 ALA   A O    1 
ATOM   1365 C  CB   . ALA   A 1 193 ? 25.422 -19.974 13.586 1.00 28.42 ?  345 ALA   A CB   1 
ATOM   1366 N  N    . LYS   A 1 194 ? 26.591 -19.778 10.590 1.00 29.00 ?  346 LYS   A N    1 
ATOM   1367 C  CA   . LYS   A 1 194 ? 27.770 -19.523 9.766  1.00 29.36 ?  346 LYS   A CA   1 
ATOM   1368 C  C    . LYS   A 1 194 ? 27.520 -18.409 8.756  1.00 29.98 ?  346 LYS   A C    1 
ATOM   1369 O  O    . LYS   A 1 194 ? 28.383 -17.544 8.560  1.00 30.00 ?  346 LYS   A O    1 
ATOM   1370 C  CB   . LYS   A 1 194 ? 28.205 -20.807 9.058  1.00 36.52 ?  346 LYS   A CB   1 
ATOM   1371 C  CG   . LYS   A 1 194 ? 28.722 -21.896 9.989  1.00 44.00 ?  346 LYS   A CG   1 
ATOM   1372 C  CD   . LYS   A 1 194 ? 30.125 -21.577 10.480 1.00 51.36 ?  346 LYS   A CD   1 
ATOM   1373 C  CE   . LYS   A 1 194 ? 30.123 -21.203 11.958 1.00 56.09 ?  346 LYS   A CE   1 
ATOM   1374 N  NZ   . LYS   A 1 194 ? 31.493 -20.900 12.464 1.00 58.14 ?  346 LYS   A NZ   1 
ATOM   1375 N  N    . LEU   A 1 195 ? 26.357 -18.418 8.096  1.00 25.68 ?  347 LEU   A N    1 
ATOM   1376 C  CA   . LEU   A 1 195 ? 26.016 -17.327 7.187  1.00 22.41 ?  347 LEU   A CA   1 
ATOM   1377 C  C    . LEU   A 1 195 ? 25.943 -16.004 7.940  1.00 24.28 ?  347 LEU   A C    1 
ATOM   1378 O  O    . LEU   A 1 195 ? 26.535 -15.001 7.522  1.00 27.69 ?  347 LEU   A O    1 
ATOM   1379 C  CB   . LEU   A 1 195 ? 24.686 -17.628 6.486  1.00 24.83 ?  347 LEU   A CB   1 
ATOM   1380 C  CG   . LEU   A 1 195 ? 24.141 -16.666 5.427  1.00 18.92 ?  347 LEU   A CG   1 
ATOM   1381 C  CD1  . LEU   A 1 195 ? 25.139 -16.491 4.303  1.00 22.56 ?  347 LEU   A CD1  1 
ATOM   1382 C  CD2  . LEU   A 1 195 ? 22.830 -17.172 4.876  1.00 19.23 ?  347 LEU   A CD2  1 
ATOM   1383 N  N    . VAL   A 1 196 ? 25.234 -15.997 9.072  1.00 22.92 ?  348 VAL   A N    1 
ATOM   1384 C  CA   . VAL   A 1 196 ? 25.134 -14.800 9.906  1.00 21.17 ?  348 VAL   A CA   1 
ATOM   1385 C  C    . VAL   A 1 196 ? 26.518 -14.290 10.277 1.00 18.03 ?  348 VAL   A C    1 
ATOM   1386 O  O    . VAL   A 1 196 ? 26.797 -13.085 10.205 1.00 16.67 ?  348 VAL   A O    1 
ATOM   1387 C  CB   . VAL   A 1 196 ? 24.285 -15.102 11.157 1.00 20.85 ?  348 VAL   A CB   1 
ATOM   1388 C  CG1  . VAL   A 1 196 ? 24.293 -13.925 12.106 1.00 14.89 ?  348 VAL   A CG1  1 
ATOM   1389 C  CG2  . VAL   A 1 196 ? 22.852 -15.459 10.760 1.00 15.81 ?  348 VAL   A CG2  1 
ATOM   1390 N  N    . GLU   A 1 197 ? 27.412 -15.202 10.665 1.00 19.18 ?  349 GLU   A N    1 
ATOM   1391 C  CA   . GLU   A 1 197 ? 28.772 -14.812 11.028 1.00 25.55 ?  349 GLU   A CA   1 
ATOM   1392 C  C    . GLU   A 1 197 ? 29.535 -14.268 9.828  1.00 23.49 ?  349 GLU   A C    1 
ATOM   1393 O  O    . GLU   A 1 197 ? 30.342 -13.340 9.964  1.00 22.07 ?  349 GLU   A O    1 
ATOM   1394 C  CB   . GLU   A 1 197 ? 29.512 -16.007 11.628 1.00 27.52 ?  349 GLU   A CB   1 
ATOM   1395 C  CG   . GLU   A 1 197 ? 30.943 -15.715 12.039 1.00 35.54 ?  349 GLU   A CG   1 
ATOM   1396 C  CD   . GLU   A 1 197 ? 31.563 -16.871 12.792 1.00 43.03 ?  349 GLU   A CD   1 
ATOM   1397 O  OE1  . GLU   A 1 197 ? 31.668 -17.969 12.206 1.00 47.06 ?  349 GLU   A OE1  1 
ATOM   1398 O  OE2  . GLU   A 1 197 ? 31.935 -16.686 13.970 1.00 48.31 ?  349 GLU   A OE2  1 
ATOM   1399 N  N    . ALA   A 1 198 ? 29.304 -14.841 8.646  1.00 23.56 ?  350 ALA   A N    1 
ATOM   1400 C  CA   . ALA   A 1 198 ? 29.965 -14.339 7.448  1.00 23.81 ?  350 ALA   A CA   1 
ATOM   1401 C  C    . ALA   A 1 198 ? 29.495 -12.929 7.108  1.00 27.54 ?  350 ALA   A C    1 
ATOM   1402 O  O    . ALA   A 1 198 ? 30.297 -12.092 6.679  1.00 27.95 ?  350 ALA   A O    1 
ATOM   1403 C  CB   . ALA   A 1 198 ? 29.726 -15.291 6.275  1.00 21.80 ?  350 ALA   A CB   1 
ATOM   1404 N  N    . ILE   A 1 199 ? 28.203 -12.642 7.301  1.00 25.12 ?  351 ILE   A N    1 
ATOM   1405 C  CA   . ILE   A 1 199 ? 27.717 -11.284 7.070  1.00 21.84 ?  351 ILE   A CA   1 
ATOM   1406 C  C    . ILE   A 1 199 ? 28.303 -10.326 8.099  1.00 23.12 ?  351 ILE   A C    1 
ATOM   1407 O  O    . ILE   A 1 199 ? 28.746 -9.223  7.757  1.00 21.59 ?  351 ILE   A O    1 
ATOM   1408 C  CB   . ILE   A 1 199 ? 26.178 -11.250 7.079  1.00 23.92 ?  351 ILE   A CB   1 
ATOM   1409 C  CG1  . ILE   A 1 199 ? 25.615 -12.070 5.916  1.00 23.43 ?  351 ILE   A CG1  1 
ATOM   1410 C  CG2  . ILE   A 1 199 ? 25.672 -9.809  6.994  1.00 20.59 ?  351 ILE   A CG2  1 
ATOM   1411 C  CD1  . ILE   A 1 199 ? 24.146 -12.433 6.081  1.00 20.81 ?  351 ILE   A CD1  1 
ATOM   1412 N  N    . GLN   A 1 200 ? 28.313 -10.725 9.374  1.00 25.45 ?  352 GLN   A N    1 
ATOM   1413 C  CA   . GLN   A 1 200 ? 28.886 -9.869  10.406 1.00 23.95 ?  352 GLN   A CA   1 
ATOM   1414 C  C    . GLN   A 1 200 ? 30.365 -9.614  10.150 1.00 24.27 ?  352 GLN   A C    1 
ATOM   1415 O  O    . GLN   A 1 200 ? 30.861 -8.505  10.382 1.00 24.68 ?  352 GLN   A O    1 
ATOM   1416 C  CB   . GLN   A 1 200 ? 28.695 -10.495 11.786 1.00 20.64 ?  352 GLN   A CB   1 
ATOM   1417 C  CG   . GLN   A 1 200 ? 29.004 -9.541  12.937 1.00 18.65 ?  352 GLN   A CG   1 
ATOM   1418 C  CD   . GLN   A 1 200 ? 28.885 -10.205 14.290 1.00 20.24 ?  352 GLN   A CD   1 
ATOM   1419 O  OE1  . GLN   A 1 200 ? 28.125 -9.757  15.155 1.00 20.01 ?  352 GLN   A OE1  1 
ATOM   1420 N  NE2  . GLN   A 1 200 ? 29.630 -11.290 14.481 1.00 20.36 ?  352 GLN   A NE2  1 
ATOM   1421 N  N    . ASP   A 1 201 ? 31.081 -10.630 9.662  1.00 25.74 ?  353 ASP   A N    1 
ATOM   1422 C  CA   . ASP   A 1 201 ? 32.515 -10.491 9.427  1.00 27.90 ?  353 ASP   A CA   1 
ATOM   1423 C  C    . ASP   A 1 201 ? 32.809 -9.359  8.454  1.00 28.17 ?  353 ASP   A C    1 
ATOM   1424 O  O    . ASP   A 1 201 ? 33.714 -8.547  8.683  1.00 30.16 ?  353 ASP   A O    1 
ATOM   1425 C  CB   . ASP   A 1 201 ? 33.090 -11.807 8.905  1.00 29.22 ?  353 ASP   A CB   1 
ATOM   1426 C  CG   . ASP   A 1 201 ? 33.381 -12.788 10.016 1.00 30.15 ?  353 ASP   A CG   1 
ATOM   1427 O  OD1  . ASP   A 1 201 ? 33.353 -12.374 11.190 1.00 30.65 ?  353 ASP   A OD1  1 
ATOM   1428 O  OD2  . ASP   A 1 201 ? 33.632 -13.973 9.719  1.00 35.81 ?  353 ASP   A OD2  1 
ATOM   1429 N  N    A ARG   A 1 202 ? 32.051 -9.289  7.357  0.42 25.55 ?  354 ARG   A N    1 
ATOM   1430 N  N    B ARG   A 1 202 ? 32.051 -9.284  7.360  0.58 25.42 ?  354 ARG   A N    1 
ATOM   1431 C  CA   A ARG   A 1 202 ? 32.292 -8.243  6.369  0.42 25.32 ?  354 ARG   A CA   1 
ATOM   1432 C  CA   B ARG   A 1 202 ? 32.313 -8.241  6.378  0.58 25.35 ?  354 ARG   A CA   1 
ATOM   1433 C  C    A ARG   A 1 202 ? 32.013 -6.866  6.953  0.42 22.66 ?  354 ARG   A C    1 
ATOM   1434 C  C    B ARG   A 1 202 ? 32.000 -6.861  6.937  0.58 22.64 ?  354 ARG   A C    1 
ATOM   1435 O  O    A ARG   A 1 202 ? 32.729 -5.901  6.659  0.42 22.46 ?  354 ARG   A O    1 
ATOM   1436 O  O    B ARG   A 1 202 ? 32.689 -5.888  6.606  0.58 22.47 ?  354 ARG   A O    1 
ATOM   1437 C  CB   A ARG   A 1 202 ? 31.437 -8.485  5.124  0.42 26.83 ?  354 ARG   A CB   1 
ATOM   1438 C  CB   B ARG   A 1 202 ? 31.514 -8.509  5.103  0.58 26.76 ?  354 ARG   A CB   1 
ATOM   1439 C  CG   A ARG   A 1 202 ? 31.484 -9.911  4.595  0.42 29.96 ?  354 ARG   A CG   1 
ATOM   1440 C  CG   B ARG   A 1 202 ? 31.880 -9.820  4.418  0.58 30.21 ?  354 ARG   A CG   1 
ATOM   1441 C  CD   A ARG   A 1 202 ? 32.745 -10.165 3.767  0.42 32.55 ?  354 ARG   A CD   1 
ATOM   1442 C  CD   B ARG   A 1 202 ? 31.503 -9.800  2.938  0.58 31.43 ?  354 ARG   A CD   1 
ATOM   1443 N  NE   A ARG   A 1 202 ? 32.708 -11.442 3.050  0.42 33.44 ?  354 ARG   A NE   1 
ATOM   1444 N  NE   B ARG   A 1 202 ? 30.147 -9.303  2.737  0.58 31.02 ?  354 ARG   A NE   1 
ATOM   1445 C  CZ   A ARG   A 1 202 ? 32.726 -12.638 3.635  0.42 31.62 ?  354 ARG   A CZ   1 
ATOM   1446 C  CZ   B ARG   A 1 202 ? 29.071 -10.078 2.652  0.58 35.91 ?  354 ARG   A CZ   1 
ATOM   1447 N  NH1  A ARG   A 1 202 ? 32.780 -12.741 4.957  0.42 27.42 ?  354 ARG   A NH1  1 
ATOM   1448 N  NH1  B ARG   A 1 202 ? 27.873 -9.533  2.475  0.58 34.22 ?  354 ARG   A NH1  1 
ATOM   1449 N  NH2  A ARG   A 1 202 ? 32.691 -13.738 2.893  0.42 30.93 ?  354 ARG   A NH2  1 
ATOM   1450 N  NH2  B ARG   A 1 202 ? 29.187 -11.399 2.741  0.58 36.27 ?  354 ARG   A NH2  1 
ATOM   1451 N  N    . LEU   A 1 203 ? 30.976 -6.752  7.784  1.00 19.43 ?  355 LEU   A N    1 
ATOM   1452 C  CA   . LEU   A 1 203 ? 30.704 -5.476  8.438  1.00 17.78 ?  355 LEU   A CA   1 
ATOM   1453 C  C    . LEU   A 1 203 ? 31.795 -5.147  9.450  1.00 18.54 ?  355 LEU   A C    1 
ATOM   1454 O  O    . LEU   A 1 203 ? 32.249 -3.998  9.529  1.00 16.92 ?  355 LEU   A O    1 
ATOM   1455 C  CB   . LEU   A 1 203 ? 29.333 -5.507  9.116  1.00 16.94 ?  355 LEU   A CB   1 
ATOM   1456 C  CG   . LEU   A 1 203 ? 28.121 -5.870  8.253  1.00 15.67 ?  355 LEU   A CG   1 
ATOM   1457 C  CD1  . LEU   A 1 203 ? 26.905 -6.061  9.131  1.00 12.79 ?  355 LEU   A CD1  1 
ATOM   1458 C  CD2  . LEU   A 1 203 ? 27.851 -4.799  7.200  1.00 15.88 ?  355 LEU   A CD2  1 
ATOM   1459 N  N    . SER   A 1 204 ? 32.221 -6.144  10.234 1.00 17.79 ?  356 SER   A N    1 
ATOM   1460 C  CA   . SER   A 1 204 ? 33.298 -5.940  11.201 1.00 25.03 ?  356 SER   A CA   1 
ATOM   1461 C  C    . SER   A 1 204 ? 34.570 -5.470  10.507 1.00 25.73 ?  356 SER   A C    1 
ATOM   1462 O  O    . SER   A 1 204 ? 35.177 -4.469  10.907 1.00 27.40 ?  356 SER   A O    1 
ATOM   1463 C  CB   . SER   A 1 204 ? 33.565 -7.236  11.968 1.00 26.15 ?  356 SER   A CB   1 
ATOM   1464 O  OG   . SER   A 1 204 ? 32.580 -7.461  12.958 1.00 35.57 ?  356 SER   A OG   1 
ATOM   1465 N  N    . ASN   A 1 205 ? 34.993 -6.197  9.468  1.00 25.43 ?  357 ASN   A N    1 
ATOM   1466 C  CA   . ASN   A 1 205 ? 36.154 -5.786  8.684  1.00 31.12 ?  357 ASN   A CA   1 
ATOM   1467 C  C    . ASN   A 1 205 ? 35.990 -4.365  8.173  1.00 26.76 ?  357 ASN   A C    1 
ATOM   1468 O  O    . ASN   A 1 205 ? 36.939 -3.576  8.183  1.00 26.96 ?  357 ASN   A O    1 
ATOM   1469 C  CB   . ASN   A 1 205 ? 36.365 -6.739  7.506  1.00 40.97 ?  357 ASN   A CB   1 
ATOM   1470 C  CG   . ASN   A 1 205 ? 36.714 -8.146  7.944  1.00 52.64 ?  357 ASN   A CG   1 
ATOM   1471 O  OD1  . ASN   A 1 205 ? 36.506 -9.106  7.200  1.00 56.41 ?  357 ASN   A OD1  1 
ATOM   1472 N  ND2  . ASN   A 1 205 ? 37.252 -8.277  9.153  1.00 58.07 ?  357 ASN   A ND2  1 
ATOM   1473 N  N    . THR   A 1 206 ? 34.785 -4.024  7.717  1.00 25.95 ?  358 THR   A N    1 
ATOM   1474 C  CA   . THR   A 1 206 ? 34.544 -2.688  7.185  1.00 23.90 ?  358 THR   A CA   1 
ATOM   1475 C  C    . THR   A 1 206 ? 34.743 -1.626  8.258  1.00 23.29 ?  358 THR   A C    1 
ATOM   1476 O  O    . THR   A 1 206 ? 35.325 -0.567  7.997  1.00 24.54 ?  358 THR   A O    1 
ATOM   1477 C  CB   . THR   A 1 206 ? 33.133 -2.615  6.600  1.00 21.29 ?  358 THR   A CB   1 
ATOM   1478 O  OG1  . THR   A 1 206 ? 33.016 -3.557  5.525  1.00 23.71 ?  358 THR   A OG1  1 
ATOM   1479 C  CG2  . THR   A 1 206 ? 32.840 -1.218  6.083  1.00 21.83 ?  358 THR   A CG2  1 
ATOM   1480 N  N    . LEU   A 1 207 ? 34.272 -1.896  9.476  1.00 19.80 ?  359 LEU   A N    1 
ATOM   1481 C  CA   . LEU   A 1 207 ? 34.416 -0.926  10.555 1.00 20.48 ?  359 LEU   A CA   1 
ATOM   1482 C  C    . LEU   A 1 207 ? 35.862 -0.846  11.035 1.00 22.17 ?  359 LEU   A C    1 
ATOM   1483 O  O    . LEU   A 1 207 ? 36.390 0.252   11.247 1.00 19.79 ?  359 LEU   A O    1 
ATOM   1484 C  CB   . LEU   A 1 207 ? 33.471 -1.295  11.698 1.00 16.74 ?  359 LEU   A CB   1 
ATOM   1485 C  CG   . LEU   A 1 207 ? 33.730 -0.734  13.094 1.00 21.97 ?  359 LEU   A CG   1 
ATOM   1486 C  CD1  . LEU   A 1 207 ? 33.356 0.743   13.167 1.00 21.23 ?  359 LEU   A CD1  1 
ATOM   1487 C  CD2  . LEU   A 1 207 ? 32.932 -1.560  14.099 1.00 21.64 ?  359 LEU   A CD2  1 
ATOM   1488 N  N    . GLN   A 1 208 ? 36.518 -1.998  11.206 1.00 25.47 ?  360 GLN   A N    1 
ATOM   1489 C  CA   . GLN   A 1 208 ? 37.933 -1.999  11.573 1.00 31.86 ?  360 GLN   A CA   1 
ATOM   1490 C  C    . GLN   A 1 208 ? 38.754 -1.177  10.594 1.00 33.44 ?  360 GLN   A C    1 
ATOM   1491 O  O    . GLN   A 1 208 ? 39.648 -0.421  10.997 1.00 33.88 ?  360 GLN   A O    1 
ATOM   1492 C  CB   . GLN   A 1 208 ? 38.473 -3.428  11.620 1.00 36.46 ?  360 GLN   A CB   1 
ATOM   1493 C  CG   . GLN   A 1 208 ? 37.870 -4.309  12.693 1.00 41.57 ?  360 GLN   A CG   1 
ATOM   1494 C  CD   . GLN   A 1 208 ? 38.127 -5.782  12.431 1.00 51.45 ?  360 GLN   A CD   1 
ATOM   1495 O  OE1  . GLN   A 1 208 ? 37.632 -6.648  13.152 1.00 52.42 ?  360 GLN   A OE1  1 
ATOM   1496 N  NE2  . GLN   A 1 208 ? 38.905 -6.074  11.389 1.00 55.82 ?  360 GLN   A NE2  1 
ATOM   1497 N  N    . THR   A 1 209 ? 38.460 -1.309  9.296  1.00 30.13 ?  361 THR   A N    1 
ATOM   1498 C  CA   . THR   A 1 209 ? 39.216 -0.579  8.286  1.00 27.19 ?  361 THR   A CA   1 
ATOM   1499 C  C    . THR   A 1 209 ? 38.910 0.913   8.343  1.00 29.61 ?  361 THR   A C    1 
ATOM   1500 O  O    . THR   A 1 209 ? 39.813 1.743   8.187  1.00 30.69 ?  361 THR   A O    1 
ATOM   1501 C  CB   . THR   A 1 209 ? 38.919 -1.158  6.903  1.00 28.45 ?  361 THR   A CB   1 
ATOM   1502 O  OG1  . THR   A 1 209 ? 39.252 -2.552  6.901  1.00 30.09 ?  361 THR   A OG1  1 
ATOM   1503 C  CG2  . THR   A 1 209 ? 39.728 -0.451  5.820  1.00 27.11 ?  361 THR   A CG2  1 
ATOM   1504 N  N    . TYR   A 1 210 ? 37.648 1.275   8.587  1.00 27.89 ?  362 TYR   A N    1 
ATOM   1505 C  CA   . TYR   A 1 210 ? 37.298 2.687   8.715  1.00 27.04 ?  362 TYR   A CA   1 
ATOM   1506 C  C    . TYR   A 1 210 ? 38.015 3.325   9.901  1.00 27.72 ?  362 TYR   A C    1 
ATOM   1507 O  O    . TYR   A 1 210 ? 38.430 4.489   9.833  1.00 29.84 ?  362 TYR   A O    1 
ATOM   1508 C  CB   . TYR   A 1 210 ? 35.776 2.845   8.850  1.00 23.18 ?  362 TYR   A CB   1 
ATOM   1509 C  CG   . TYR   A 1 210 ? 35.300 4.288   8.857  1.00 25.13 ?  362 TYR   A CG   1 
ATOM   1510 C  CD1  . TYR   A 1 210 ? 35.282 5.035   10.034 1.00 22.24 ?  362 TYR   A CD1  1 
ATOM   1511 C  CD2  . TYR   A 1 210 ? 34.866 4.904   7.685  1.00 26.99 ?  362 TYR   A CD2  1 
ATOM   1512 C  CE1  . TYR   A 1 210 ? 34.852 6.356   10.045 1.00 23.32 ?  362 TYR   A CE1  1 
ATOM   1513 C  CE2  . TYR   A 1 210 ? 34.432 6.224   7.686  1.00 27.96 ?  362 TYR   A CE2  1 
ATOM   1514 C  CZ   . TYR   A 1 210 ? 34.431 6.943   8.867  1.00 31.49 ?  362 TYR   A CZ   1 
ATOM   1515 O  OH   . TYR   A 1 210 ? 34.005 8.252   8.869  1.00 37.19 ?  362 TYR   A OH   1 
ATOM   1516 N  N    . ILE   A 1 211 ? 38.165 2.585   10.998 1.00 24.13 ?  363 ILE   A N    1 
ATOM   1517 C  CA   . ILE   A 1 211 ? 38.886 3.116   12.151 1.00 25.88 ?  363 ILE   A CA   1 
ATOM   1518 C  C    . ILE   A 1 211 ? 40.359 3.318   11.809 1.00 30.51 ?  363 ILE   A C    1 
ATOM   1519 O  O    . ILE   A 1 211 ? 40.945 4.366   12.111 1.00 30.08 ?  363 ILE   A O    1 
ATOM   1520 C  CB   . ILE   A 1 211 ? 38.708 2.192   13.368 1.00 26.16 ?  363 ILE   A CB   1 
ATOM   1521 C  CG1  . ILE   A 1 211 ? 37.278 2.275   13.900 1.00 27.24 ?  363 ILE   A CG1  1 
ATOM   1522 C  CG2  . ILE   A 1 211 ? 39.713 2.534   14.475 1.00 24.30 ?  363 ILE   A CG2  1 
ATOM   1523 C  CD1  . ILE   A 1 211 ? 36.877 1.051   14.671 1.00 26.22 ?  363 ILE   A CD1  1 
ATOM   1524 N  N    . ARG   A 1 212 ? 40.972 2.325   11.154 1.00 32.80 ?  364 ARG   A N    1 
ATOM   1525 C  CA   . ARG   A 1 212 ? 42.396 2.403   10.824 1.00 35.34 ?  364 ARG   A CA   1 
ATOM   1526 C  C    . ARG   A 1 212 ? 42.696 3.524   9.834  1.00 36.67 ?  364 ARG   A C    1 
ATOM   1527 O  O    . ARG   A 1 212 ? 43.787 4.102   9.874  1.00 40.29 ?  364 ARG   A O    1 
ATOM   1528 C  CB   . ARG   A 1 212 ? 42.886 1.065   10.266 1.00 37.65 ?  364 ARG   A CB   1 
ATOM   1529 C  CG   . ARG   A 1 212 ? 42.807 -0.099  11.241 1.00 44.91 ?  364 ARG   A CG   1 
ATOM   1530 C  CD   . ARG   A 1 212 ? 43.633 -1.289  10.756 1.00 54.00 ?  364 ARG   A CD   1 
ATOM   1531 N  NE   . ARG   A 1 212 ? 42.798 -2.463  10.497 1.00 59.62 ?  364 ARG   A NE   1 
ATOM   1532 C  CZ   . ARG   A 1 212 ? 42.185 -2.710  9.340  1.00 61.45 ?  364 ARG   A CZ   1 
ATOM   1533 N  NH1  . ARG   A 1 212 ? 42.322 -1.872  8.319  1.00 59.96 ?  364 ARG   A NH1  1 
ATOM   1534 N  NH2  . ARG   A 1 212 ? 41.440 -3.802  9.198  1.00 62.13 ?  364 ARG   A NH2  1 
ATOM   1535 N  N    . CYS   A 1 213 ? 41.758 3.835   8.934  1.00 35.37 ?  365 CYS   A N    1 
ATOM   1536 C  CA   . CYS   A 1 213 ? 41.930 4.982   8.049  1.00 36.64 ?  365 CYS   A CA   1 
ATOM   1537 C  C    . CYS   A 1 213 ? 41.836 6.299   8.799  1.00 38.23 ?  365 CYS   A C    1 
ATOM   1538 O  O    . CYS   A 1 213 ? 42.273 7.331   8.278  1.00 43.04 ?  365 CYS   A O    1 
ATOM   1539 C  CB   . CYS   A 1 213 ? 40.885 4.969   6.928  1.00 39.09 ?  365 CYS   A CB   1 
ATOM   1540 S  SG   . CYS   A 1 213 ? 40.995 3.600   5.768  1.00 43.42 ?  365 CYS   A SG   1 
ATOM   1541 N  N    . ARG   A 1 214 ? 41.276 6.287   10.004 1.00 36.08 ?  366 ARG   A N    1 
ATOM   1542 C  CA   . ARG   A 1 214 ? 41.045 7.499   10.775 1.00 42.01 ?  366 ARG   A CA   1 
ATOM   1543 C  C    . ARG   A 1 214 ? 41.987 7.658   11.962 1.00 44.44 ?  366 ARG   A C    1 
ATOM   1544 O  O    . ARG   A 1 214 ? 42.382 8.785   12.268 1.00 47.55 ?  366 ARG   A O    1 
ATOM   1545 C  CB   . ARG   A 1 214 ? 39.585 7.529   11.255 1.00 47.07 ?  366 ARG   A CB   1 
ATOM   1546 C  CG   . ARG   A 1 214 ? 39.309 8.293   12.540 1.00 53.52 ?  366 ARG   A CG   1 
ATOM   1547 C  CD   . ARG   A 1 214 ? 38.017 7.807   13.199 1.00 56.69 ?  366 ARG   A CD   1 
ATOM   1548 N  NE   . ARG   A 1 214 ? 37.452 8.796   14.115 1.00 59.54 ?  366 ARG   A NE   1 
ATOM   1549 C  CZ   . ARG   A 1 214 ? 36.614 8.505   15.106 1.00 58.10 ?  366 ARG   A CZ   1 
ATOM   1550 N  NH1  . ARG   A 1 214 ? 36.149 9.466   15.894 1.00 59.03 ?  366 ARG   A NH1  1 
ATOM   1551 N  NH2  . ARG   A 1 214 ? 36.247 7.250   15.313 1.00 57.10 ?  366 ARG   A NH2  1 
ATOM   1552 N  N    . HIS   A 1 215 ? 42.388 6.564   12.612 1.00 43.90 ?  367 HIS   A N    1 
ATOM   1553 C  CA   . HIS   A 1 215 ? 43.194 6.626   13.828 1.00 43.21 ?  367 HIS   A CA   1 
ATOM   1554 C  C    . HIS   A 1 215 ? 44.406 5.713   13.694 1.00 39.73 ?  367 HIS   A C    1 
ATOM   1555 O  O    . HIS   A 1 215 ? 44.258 4.547   13.294 1.00 40.62 ?  367 HIS   A O    1 
ATOM   1556 C  CB   . HIS   A 1 215 ? 42.372 6.212   15.057 1.00 46.82 ?  367 HIS   A CB   1 
ATOM   1557 C  CG   . HIS   A 1 215 ? 41.373 7.237   15.495 1.00 54.72 ?  367 HIS   A CG   1 
ATOM   1558 N  ND1  . HIS   A 1 215 ? 41.712 8.549   15.746 1.00 58.41 ?  367 HIS   A ND1  1 
ATOM   1559 C  CD2  . HIS   A 1 215 ? 40.045 7.138   15.736 1.00 56.27 ?  367 HIS   A CD2  1 
ATOM   1560 C  CE1  . HIS   A 1 215 ? 40.634 9.217   16.117 1.00 58.69 ?  367 HIS   A CE1  1 
ATOM   1561 N  NE2  . HIS   A 1 215 ? 39.609 8.384   16.118 1.00 57.43 ?  367 HIS   A NE2  1 
ATOM   1562 N  N    . PRO   A 1 216 ? 45.603 6.181   14.040 1.00 42.59 ?  368 PRO   A N    1 
ATOM   1563 C  CA   . PRO   A 1 216 ? 46.778 5.299   14.044 1.00 41.51 ?  368 PRO   A CA   1 
ATOM   1564 C  C    . PRO   A 1 216 ? 46.779 4.410   15.274 1.00 39.78 ?  368 PRO   A C    1 
ATOM   1565 O  O    . PRO   A 1 216 ? 46.062 4.680   16.250 1.00 37.90 ?  368 PRO   A O    1 
ATOM   1566 C  CB   . PRO   A 1 216 ? 47.965 6.278   14.072 1.00 45.10 ?  368 PRO   A CB   1 
ATOM   1567 C  CG   . PRO   A 1 216 ? 47.368 7.672   14.024 1.00 46.52 ?  368 PRO   A CG   1 
ATOM   1568 C  CD   . PRO   A 1 216 ? 45.946 7.547   14.462 1.00 43.84 ?  368 PRO   A CD   1 
ATOM   1569 N  N    . PRO   A 1 217 ? 47.558 3.326   15.263 1.00 39.89 ?  369 PRO   A N    1 
ATOM   1570 C  CA   . PRO   A 1 217 ? 47.722 2.539   16.484 1.00 39.25 ?  369 PRO   A CA   1 
ATOM   1571 C  C    . PRO   A 1 217 ? 48.504 3.320   17.526 1.00 41.58 ?  369 PRO   A C    1 
ATOM   1572 O  O    . PRO   A 1 217 ? 49.304 4.207   17.184 1.00 42.09 ?  369 PRO   A O    1 
ATOM   1573 C  CB   . PRO   A 1 217 ? 48.501 1.299   16.007 1.00 40.68 ?  369 PRO   A CB   1 
ATOM   1574 C  CG   . PRO   A 1 217 ? 49.077 1.675   14.673 1.00 44.06 ?  369 PRO   A CG   1 
ATOM   1575 C  CD   . PRO   A 1 217 ? 48.142 2.672   14.080 1.00 41.69 ?  369 PRO   A CD   1 
ATOM   1576 N  N    . PRO   A 1 218 ? 48.298 3.031   18.820 1.00 39.98 ?  370 PRO   A N    1 
ATOM   1577 C  CA   . PRO   A 1 218 ? 47.381 2.004   19.316 1.00 37.38 ?  370 PRO   A CA   1 
ATOM   1578 C  C    . PRO   A 1 218 ? 45.958 2.516   19.476 1.00 33.21 ?  370 PRO   A C    1 
ATOM   1579 O  O    . PRO   A 1 218 ? 45.075 1.730   19.801 1.00 33.37 ?  370 PRO   A O    1 
ATOM   1580 C  CB   . PRO   A 1 218 ? 47.976 1.646   20.676 1.00 39.48 ?  370 PRO   A CB   1 
ATOM   1581 C  CG   . PRO   A 1 218 ? 48.549 2.939   21.160 1.00 41.24 ?  370 PRO   A CG   1 
ATOM   1582 C  CD   . PRO   A 1 218 ? 48.998 3.710   19.926 1.00 41.95 ?  370 PRO   A CD   1 
ATOM   1583 N  N    . GLY   A 1 219 ? 45.750 3.818   19.261 1.00 32.72 ?  371 GLY   A N    1 
ATOM   1584 C  CA   . GLY   A 1 219 ? 44.432 4.395   19.472 1.00 28.71 ?  371 GLY   A CA   1 
ATOM   1585 C  C    . GLY   A 1 219 ? 43.351 3.729   18.647 1.00 29.37 ?  371 GLY   A C    1 
ATOM   1586 O  O    . GLY   A 1 219 ? 42.204 3.617   19.094 1.00 27.44 ?  371 GLY   A O    1 
ATOM   1587 N  N    . SER   A 1 220 ? 43.702 3.275   17.440 1.00 30.21 ?  372 SER   A N    1 
ATOM   1588 C  CA   . SER   A 1 220 ? 42.758 2.546   16.597 1.00 29.98 ?  372 SER   A CA   1 
ATOM   1589 C  C    . SER   A 1 220 ? 42.221 1.313   17.311 1.00 32.35 ?  372 SER   A C    1 
ATOM   1590 O  O    . SER   A 1 220 ? 41.011 1.062   17.315 1.00 30.99 ?  372 SER   A O    1 
ATOM   1591 C  CB   . SER   A 1 220 ? 43.435 2.153   15.282 1.00 30.86 ?  372 SER   A CB   1 
ATOM   1592 O  OG   . SER   A 1 220 ? 44.472 1.212   15.517 1.00 35.72 ?  372 SER   A OG   1 
ATOM   1593 N  N    . HIS   A 1 221 ? 43.112 0.526   17.922 1.00 34.80 ?  373 HIS   A N    1 
ATOM   1594 C  CA   . HIS   A 1 221 ? 42.670 -0.680  18.614 1.00 31.75 ?  373 HIS   A CA   1 
ATOM   1595 C  C    . HIS   A 1 221 ? 41.935 -0.352  19.904 1.00 31.59 ?  373 HIS   A C    1 
ATOM   1596 O  O    . HIS   A 1 221 ? 41.063 -1.119  20.329 1.00 30.85 ?  373 HIS   A O    1 
ATOM   1597 C  CB   . HIS   A 1 221 ? 43.853 -1.597  18.916 1.00 32.89 ?  373 HIS   A CB   1 
ATOM   1598 C  CG   . HIS   A 1 221 ? 44.711 -1.897  17.727 1.00 37.19 ?  373 HIS   A CG   1 
ATOM   1599 N  ND1  . HIS   A 1 221 ? 44.267 -2.645  16.658 1.00 36.51 ?  373 HIS   A ND1  1 
ATOM   1600 C  CD2  . HIS   A 1 221 ? 45.997 -1.571  17.450 1.00 37.61 ?  373 HIS   A CD2  1 
ATOM   1601 C  CE1  . HIS   A 1 221 ? 45.236 -2.756  15.767 1.00 36.67 ?  373 HIS   A CE1  1 
ATOM   1602 N  NE2  . HIS   A 1 221 ? 46.297 -2.114  16.225 1.00 37.92 ?  373 HIS   A NE2  1 
ATOM   1603 N  N    . GLN   A 1 222 ? 42.273 0.767   20.548 1.00 29.50 ?  374 GLN   A N    1 
ATOM   1604 C  CA   . GLN   A 1 222 ? 41.562 1.129   21.768 1.00 30.12 ?  374 GLN   A CA   1 
ATOM   1605 C  C    . GLN   A 1 222 ? 40.129 1.547   21.471 1.00 28.01 ?  374 GLN   A C    1 
ATOM   1606 O  O    . GLN   A 1 222 ? 39.231 1.296   22.283 1.00 32.93 ?  374 GLN   A O    1 
ATOM   1607 C  CB   . GLN   A 1 222 ? 42.312 2.235   22.513 1.00 29.21 ?  374 GLN   A CB   1 
ATOM   1608 C  CG   . GLN   A 1 222 ? 43.758 1.872   22.816 1.00 32.36 ?  374 GLN   A CG   1 
ATOM   1609 C  CD   . GLN   A 1 222 ? 44.570 3.051   23.305 1.00 38.03 ?  374 GLN   A CD   1 
ATOM   1610 O  OE1  . GLN   A 1 222 ? 45.633 2.882   23.909 1.00 40.16 ?  374 GLN   A OE1  1 
ATOM   1611 N  NE2  . GLN   A 1 222 ? 44.078 4.256   23.045 1.00 39.77 ?  374 GLN   A NE2  1 
ATOM   1612 N  N    . LEU   A 1 223 ? 39.887 2.171   20.318 1.00 26.63 ?  375 LEU   A N    1 
ATOM   1613 C  CA   . LEU   A 1 223 ? 38.518 2.526   19.970 1.00 31.24 ?  375 LEU   A CA   1 
ATOM   1614 C  C    . LEU   A 1 223 ? 37.707 1.286   19.621 1.00 32.97 ?  375 LEU   A C    1 
ATOM   1615 O  O    . LEU   A 1 223 ? 36.621 1.073   20.171 1.00 31.62 ?  375 LEU   A O    1 
ATOM   1616 C  CB   . LEU   A 1 223 ? 38.496 3.529   18.820 1.00 32.62 ?  375 LEU   A CB   1 
ATOM   1617 C  CG   . LEU   A 1 223 ? 37.069 3.940   18.442 1.00 37.78 ?  375 LEU   A CG   1 
ATOM   1618 C  CD1  . LEU   A 1 223 ? 36.462 4.847   19.507 1.00 37.83 ?  375 LEU   A CD1  1 
ATOM   1619 C  CD2  . LEU   A 1 223 ? 37.056 4.619   17.086 1.00 40.16 ?  375 LEU   A CD2  1 
ATOM   1620 N  N    . TYR   A 1 224 ? 38.225 0.448   18.718 1.00 32.38 ?  376 TYR   A N    1 
ATOM   1621 C  CA   . TYR   A 1 224 ? 37.527 -0.789  18.376 1.00 31.26 ?  376 TYR   A CA   1 
ATOM   1622 C  C    . TYR   A 1 224 ? 37.215 -1.615  19.622 1.00 30.96 ?  376 TYR   A C    1 
ATOM   1623 O  O    . TYR   A 1 224 ? 36.146 -2.229  19.720 1.00 30.31 ?  376 TYR   A O    1 
ATOM   1624 C  CB   . TYR   A 1 224 ? 38.356 -1.608  17.385 1.00 29.75 ?  376 TYR   A CB   1 
ATOM   1625 C  CG   . TYR   A 1 224 ? 37.639 -2.824  16.846 1.00 28.36 ?  376 TYR   A CG   1 
ATOM   1626 C  CD1  . TYR   A 1 224 ? 36.403 -2.707  16.223 1.00 31.01 ?  376 TYR   A CD1  1 
ATOM   1627 C  CD2  . TYR   A 1 224 ? 38.193 -4.090  16.967 1.00 31.45 ?  376 TYR   A CD2  1 
ATOM   1628 C  CE1  . TYR   A 1 224 ? 35.739 -3.820  15.731 1.00 33.01 ?  376 TYR   A CE1  1 
ATOM   1629 C  CE2  . TYR   A 1 224 ? 37.542 -5.207  16.479 1.00 32.76 ?  376 TYR   A CE2  1 
ATOM   1630 C  CZ   . TYR   A 1 224 ? 36.315 -5.067  15.861 1.00 35.89 ?  376 TYR   A CZ   1 
ATOM   1631 O  OH   . TYR   A 1 224 ? 35.662 -6.179  15.377 1.00 37.60 ?  376 TYR   A OH   1 
ATOM   1632 N  N    . ALA   A 1 225 ? 38.133 -1.635  20.589 1.00 29.60 ?  377 ALA   A N    1 
ATOM   1633 C  CA   . ALA   A 1 225 ? 37.880 -2.367  21.825 1.00 30.85 ?  377 ALA   A CA   1 
ATOM   1634 C  C    . ALA   A 1 225 ? 36.761 -1.722  22.637 1.00 27.06 ?  377 ALA   A C    1 
ATOM   1635 O  O    . ALA   A 1 225 ? 35.983 -2.422  23.295 1.00 29.46 ?  377 ALA   A O    1 
ATOM   1636 C  CB   . ALA   A 1 225 ? 39.162 -2.457  22.656 1.00 31.71 ?  377 ALA   A CB   1 
ATOM   1637 N  N    . LYS   A 1 226 ? 36.675 -0.388  22.624 1.00 23.88 ?  378 LYS   A N    1 
ATOM   1638 C  CA   . LYS   A 1 226 ? 35.605 0.282   23.358 1.00 20.92 ?  378 LYS   A CA   1 
ATOM   1639 C  C    . LYS   A 1 226 ? 34.251 0.071   22.689 1.00 22.20 ?  378 LYS   A C    1 
ATOM   1640 O  O    . LYS   A 1 226 ? 33.213 0.071   23.363 1.00 22.34 ?  378 LYS   A O    1 
ATOM   1641 C  CB   . LYS   A 1 226 ? 35.912 1.775   23.490 1.00 20.99 ?  378 LYS   A CB   1 
ATOM   1642 C  CG   . LYS   A 1 226 ? 37.005 2.100   24.503 1.00 27.66 ?  378 LYS   A CG   1 
ATOM   1643 C  CD   . LYS   A 1 226 ? 37.443 3.563   24.401 1.00 31.69 ?  378 LYS   A CD   1 
ATOM   1644 C  CE   . LYS   A 1 226 ? 38.768 3.819   25.114 1.00 34.86 ?  378 LYS   A CE   1 
ATOM   1645 N  NZ   . LYS   A 1 226 ? 38.721 3.447   26.559 1.00 35.56 ?  378 LYS   A NZ   1 
ATOM   1646 N  N    . MET   A 1 227 ? 34.236 -0.123  21.373 1.00 21.39 ?  379 MET   A N    1 
ATOM   1647 C  CA   . MET   A 1 227 ? 32.973 -0.374  20.689 1.00 22.52 ?  379 MET   A CA   1 
ATOM   1648 C  C    . MET   A 1 227 ? 32.505 -1.811  20.898 1.00 23.23 ?  379 MET   A C    1 
ATOM   1649 O  O    . MET   A 1 227 ? 31.308 -2.052  21.091 1.00 22.59 ?  379 MET   A O    1 
ATOM   1650 C  CB   . MET   A 1 227 ? 33.117 -0.058  19.201 1.00 21.64 ?  379 MET   A CB   1 
ATOM   1651 C  CG   . MET   A 1 227 ? 33.335 1.421   18.889 1.00 25.32 ?  379 MET   A CG   1 
ATOM   1652 S  SD   . MET   A 1 227 ? 33.648 1.663   17.126 1.00 32.59 ?  379 MET   A SD   1 
ATOM   1653 C  CE   . MET   A 1 227 ? 34.362 0.075   16.760 1.00 35.96 ?  379 MET   A CE   1 
ATOM   1654 N  N    . ILE   A 1 228 ? 33.431 -2.773  20.861 1.00 25.64 ?  380 ILE   A N    1 
ATOM   1655 C  CA   . ILE   A 1 228 ? 33.085 -4.158  21.174 1.00 29.07 ?  380 ILE   A CA   1 
ATOM   1656 C  C    . ILE   A 1 228 ? 32.512 -4.257  22.580 1.00 28.06 ?  380 ILE   A C    1 
ATOM   1657 O  O    . ILE   A 1 228 ? 31.514 -4.950  22.812 1.00 30.35 ?  380 ILE   A O    1 
ATOM   1658 C  CB   . ILE   A 1 228 ? 34.313 -5.070  21.012 1.00 35.45 ?  380 ILE   A CB   1 
ATOM   1659 C  CG1  . ILE   A 1 228 ? 34.637 -5.288  19.535 1.00 40.89 ?  380 ILE   A CG1  1 
ATOM   1660 C  CG2  . ILE   A 1 228 ? 34.086 -6.404  21.712 1.00 33.96 ?  380 ILE   A CG2  1 
ATOM   1661 C  CD1  . ILE   A 1 228 ? 35.804 -6.236  19.324 1.00 45.36 ?  380 ILE   A CD1  1 
ATOM   1662 N  N    . GLN   A 1 229 ? 33.136 -3.571  23.542 1.00 26.27 ?  381 GLN   A N    1 
ATOM   1663 C  CA   . GLN   A 1 229 ? 32.645 -3.615  24.917 1.00 28.11 ?  381 GLN   A CA   1 
ATOM   1664 C  C    . GLN   A 1 229 ? 31.226 -3.065  25.012 1.00 26.79 ?  381 GLN   A C    1 
ATOM   1665 O  O    . GLN   A 1 229 ? 30.405 -3.574  25.785 1.00 26.26 ?  381 GLN   A O    1 
ATOM   1666 C  CB   . GLN   A 1 229 ? 33.590 -2.843  25.838 1.00 27.12 ?  381 GLN   A CB   1 
ATOM   1667 C  CG   . GLN   A 1 229 ? 33.262 -2.980  27.311 1.00 36.81 ?  381 GLN   A CG   1 
ATOM   1668 C  CD   . GLN   A 1 229 ? 32.938 -4.411  27.716 1.00 41.96 ?  381 GLN   A CD   1 
ATOM   1669 O  OE1  . GLN   A 1 229 ? 31.876 -4.683  28.279 1.00 39.87 ?  381 GLN   A OE1  1 
ATOM   1670 N  NE2  . GLN   A 1 229 ? 33.860 -5.329  27.445 1.00 47.14 ?  381 GLN   A NE2  1 
ATOM   1671 N  N    . LYS   A 1 230 ? 30.915 -2.035  24.218 1.00 26.92 ?  382 LYS   A N    1 
ATOM   1672 C  CA   . LYS   A 1 230 ? 29.559 -1.500  24.178 1.00 27.44 ?  382 LYS   A CA   1 
ATOM   1673 C  C    . LYS   A 1 230 ? 28.563 -2.525  23.651 1.00 25.83 ?  382 LYS   A C    1 
ATOM   1674 O  O    . LYS   A 1 230 ? 27.396 -2.522  24.062 1.00 21.64 ?  382 LYS   A O    1 
ATOM   1675 C  CB   . LYS   A 1 230 ? 29.521 -0.232  23.323 1.00 29.47 ?  382 LYS   A CB   1 
ATOM   1676 C  CG   . LYS   A 1 230 ? 30.052 1.004   24.039 1.00 32.88 ?  382 LYS   A CG   1 
ATOM   1677 C  CD   . LYS   A 1 230 ? 29.000 1.608   24.955 1.00 32.76 ?  382 LYS   A CD   1 
ATOM   1678 C  CE   . LYS   A 1 230 ? 29.617 2.554   25.969 1.00 37.33 ?  382 LYS   A CE   1 
ATOM   1679 N  NZ   . LYS   A 1 230 ? 30.400 1.818   26.998 1.00 39.26 ?  382 LYS   A NZ   1 
ATOM   1680 N  N    . LEU   A 1 231 ? 28.993 -3.404  22.742 1.00 23.61 ?  383 LEU   A N    1 
ATOM   1681 C  CA   . LEU   A 1 231 ? 28.115 -4.485  22.311 1.00 22.71 ?  383 LEU   A CA   1 
ATOM   1682 C  C    . LEU   A 1 231 ? 27.897 -5.493  23.437 1.00 20.60 ?  383 LEU   A C    1 
ATOM   1683 O  O    . LEU   A 1 231 ? 26.783 -6.002  23.613 1.00 20.27 ?  383 LEU   A O    1 
ATOM   1684 C  CB   . LEU   A 1 231 ? 28.686 -5.159  21.062 1.00 23.41 ?  383 LEU   A CB   1 
ATOM   1685 C  CG   . LEU   A 1 231 ? 28.682 -4.288  19.800 1.00 23.07 ?  383 LEU   A CG   1 
ATOM   1686 C  CD1  . LEU   A 1 231 ? 29.397 -4.975  18.618 1.00 23.70 ?  383 LEU   A CD1  1 
ATOM   1687 C  CD2  . LEU   A 1 231 ? 27.263 -3.875  19.411 1.00 21.15 ?  383 LEU   A CD2  1 
ATOM   1688 N  N    . ALA   A 1 232 ? 28.945 -5.784  24.215 1.00 18.43 ?  384 ALA   A N    1 
ATOM   1689 C  CA   . ALA   A 1 232 ? 28.780 -6.598  25.418 1.00 18.79 ?  384 ALA   A CA   1 
ATOM   1690 C  C    . ALA   A 1 232 ? 27.833 -5.932  26.409 1.00 22.02 ?  384 ALA   A C    1 
ATOM   1691 O  O    . ALA   A 1 232 ? 27.021 -6.606  27.053 1.00 22.60 ?  384 ALA   A O    1 
ATOM   1692 C  CB   . ALA   A 1 232 ? 30.142 -6.849  26.072 1.00 18.91 ?  384 ALA   A CB   1 
ATOM   1693 N  N    . ASP   A 1 233 ? 27.928 -4.605  26.549 1.00 22.96 ?  385 ASP   A N    1 
ATOM   1694 C  CA   . ASP   A 1 233 ? 27.056 -3.893  27.477 1.00 20.06 ?  385 ASP   A CA   1 
ATOM   1695 C  C    . ASP   A 1 233 ? 25.593 -4.013  27.066 1.00 21.75 ?  385 ASP   A C    1 
ATOM   1696 O  O    . ASP   A 1 233 ? 24.718 -4.222  27.917 1.00 20.33 ?  385 ASP   A O    1 
ATOM   1697 C  CB   . ASP   A 1 233 ? 27.461 -2.420  27.558 1.00 18.85 ?  385 ASP   A CB   1 
ATOM   1698 C  CG   . ASP   A 1 233 ? 28.829 -2.222  28.182 1.00 26.94 ?  385 ASP   A CG   1 
ATOM   1699 O  OD1  . ASP   A 1 233 ? 29.385 -1.111  28.044 1.00 26.30 ?  385 ASP   A OD1  1 
ATOM   1700 O  OD2  . ASP   A 1 233 ? 29.347 -3.178  28.802 1.00 27.24 ?  385 ASP   A OD2  1 
ATOM   1701 N  N    . LEU   A 1 234 ? 25.312 -3.873  25.767 1.00 17.22 ?  386 LEU   A N    1 
ATOM   1702 C  CA   . LEU   A 1 234 ? 23.942 -3.976  25.272 1.00 18.55 ?  386 LEU   A CA   1 
ATOM   1703 C  C    . LEU   A 1 234 ? 23.330 -5.339  25.562 1.00 19.64 ?  386 LEU   A C    1 
ATOM   1704 O  O    . LEU   A 1 234 ? 22.118 -5.435  25.800 1.00 17.85 ?  386 LEU   A O    1 
ATOM   1705 C  CB   . LEU   A 1 234 ? 23.915 -3.702  23.766 1.00 18.85 ?  386 LEU   A CB   1 
ATOM   1706 C  CG   . LEU   A 1 234 ? 23.938 -2.226  23.372 1.00 16.76 ?  386 LEU   A CG   1 
ATOM   1707 C  CD1  . LEU   A 1 234 ? 24.307 -2.047  21.898 1.00 16.35 ?  386 LEU   A CD1  1 
ATOM   1708 C  CD2  . LEU   A 1 234 ? 22.593 -1.592  23.678 1.00 13.11 ?  386 LEU   A CD2  1 
ATOM   1709 N  N    . ARG   A 1 235 ? 24.137 -6.405  25.522 1.00 21.49 ?  387 ARG   A N    1 
ATOM   1710 C  CA   . ARG   A 1 235 ? 23.630 -7.726  25.879 1.00 23.76 ?  387 ARG   A CA   1 
ATOM   1711 C  C    . ARG   A 1 235 ? 23.103 -7.744  27.306 1.00 23.84 ?  387 ARG   A C    1 
ATOM   1712 O  O    . ARG   A 1 235 ? 22.034 -8.306  27.570 1.00 25.83 ?  387 ARG   A O    1 
ATOM   1713 C  CB   . ARG   A 1 235 ? 24.720 -8.784  25.720 1.00 25.65 ?  387 ARG   A CB   1 
ATOM   1714 C  CG   . ARG   A 1 235 ? 25.269 -8.927  24.324 1.00 30.81 ?  387 ARG   A CG   1 
ATOM   1715 C  CD   . ARG   A 1 235 ? 24.163 -9.017  23.289 1.00 33.98 ?  387 ARG   A CD   1 
ATOM   1716 N  NE   . ARG   A 1 235 ? 24.705 -9.455  22.007 1.00 35.27 ?  387 ARG   A NE   1 
ATOM   1717 C  CZ   . ARG   A 1 235 ? 24.738 -10.721 21.603 1.00 37.61 ?  387 ARG   A CZ   1 
ATOM   1718 N  NH1  . ARG   A 1 235 ? 24.239 -11.683 22.369 1.00 33.12 ?  387 ARG   A NH1  1 
ATOM   1719 N  NH2  . ARG   A 1 235 ? 25.259 -11.024 20.422 1.00 41.62 ?  387 ARG   A NH2  1 
ATOM   1720 N  N    . SER   A 1 236 ? 23.845 -7.146  28.246 1.00 21.05 ?  388 SER   A N    1 
ATOM   1721 C  CA   . SER   A 1 236 ? 23.398 -7.168  29.634 1.00 24.74 ?  388 SER   A CA   1 
ATOM   1722 C  C    . SER   A 1 236 ? 22.278 -6.168  29.880 1.00 21.81 ?  388 SER   A C    1 
ATOM   1723 O  O    . SER   A 1 236 ? 21.436 -6.401  30.749 1.00 22.55 ?  388 SER   A O    1 
ATOM   1724 C  CB   . SER   A 1 236 ? 24.572 -6.914  30.591 1.00 31.54 ?  388 SER   A CB   1 
ATOM   1725 O  OG   . SER   A 1 236 ? 24.706 -5.544  30.909 1.00 35.43 ?  388 SER   A OG   1 
ATOM   1726 N  N    . LEU   A 1 237 ? 22.239 -5.061  29.131 1.00 22.96 ?  389 LEU   A N    1 
ATOM   1727 C  CA   . LEU   A 1 237 ? 21.065 -4.197  29.186 1.00 20.72 ?  389 LEU   A CA   1 
ATOM   1728 C  C    . LEU   A 1 237 ? 19.853 -4.891  28.584 1.00 19.46 ?  389 LEU   A C    1 
ATOM   1729 O  O    . LEU   A 1 237 ? 18.725 -4.684  29.044 1.00 17.62 ?  389 LEU   A O    1 
ATOM   1730 C  CB   . LEU   A 1 237 ? 21.338 -2.880  28.460 1.00 19.37 ?  389 LEU   A CB   1 
ATOM   1731 C  CG   . LEU   A 1 237 ? 22.312 -1.914  29.143 1.00 21.45 ?  389 LEU   A CG   1 
ATOM   1732 C  CD1  . LEU   A 1 237 ? 23.000 -1.013  28.124 1.00 17.83 ?  389 LEU   A CD1  1 
ATOM   1733 C  CD2  . LEU   A 1 237 ? 21.584 -1.079  30.196 1.00 20.76 ?  389 LEU   A CD2  1 
ATOM   1734 N  N    . ASN   A 1 238 ? 20.075 -5.715  27.559 1.00 20.31 ?  390 ASN   A N    1 
ATOM   1735 C  CA   . ASN   A 1 238 ? 19.006 -6.530  26.990 1.00 18.86 ?  390 ASN   A CA   1 
ATOM   1736 C  C    . ASN   A 1 238 ? 18.411 -7.448  28.050 1.00 21.02 ?  390 ASN   A C    1 
ATOM   1737 O  O    . ASN   A 1 238 ? 17.197 -7.437  28.291 1.00 19.01 ?  390 ASN   A O    1 
ATOM   1738 C  CB   . ASN   A 1 238 ? 19.560 -7.336  25.809 1.00 14.80 ?  390 ASN   A CB   1 
ATOM   1739 C  CG   . ASN   A 1 238 ? 18.480 -7.896  24.906 1.00 16.59 ?  390 ASN   A CG   1 
ATOM   1740 O  OD1  . ASN   A 1 238 ? 17.350 -8.126  25.327 1.00 18.15 ?  390 ASN   A OD1  1 
ATOM   1741 N  ND2  . ASN   A 1 238 ? 18.836 -8.135  23.654 1.00 15.66 ?  390 ASN   A ND2  1 
ATOM   1742 N  N    . GLU   A 1 239 ? 19.262 -8.231  28.715 1.00 22.20 ?  391 GLU   A N    1 
ATOM   1743 C  CA   . GLU   A 1 239 ? 18.781 -9.158  29.738 1.00 30.71 ?  391 GLU   A CA   1 
ATOM   1744 C  C    . GLU   A 1 239 ? 17.998 -8.436  30.832 1.00 26.66 ?  391 GLU   A C    1 
ATOM   1745 O  O    . GLU   A 1 239 ? 16.967 -8.937  31.295 1.00 23.35 ?  391 GLU   A O    1 
ATOM   1746 C  CB   . GLU   A 1 239 ? 19.956 -9.939  30.333 1.00 36.42 ?  391 GLU   A CB   1 
ATOM   1747 C  CG   . GLU   A 1 239 ? 20.555 -10.963 29.363 1.00 47.67 ?  391 GLU   A CG   1 
ATOM   1748 C  CD   . GLU   A 1 239 ? 22.059 -11.162 29.531 1.00 58.69 ?  391 GLU   A CD   1 
ATOM   1749 O  OE1  . GLU   A 1 239 ? 22.745 -10.222 29.985 1.00 62.50 ?  391 GLU   A OE1  1 
ATOM   1750 O  OE2  . GLU   A 1 239 ? 22.559 -12.259 29.191 1.00 61.50 ?  391 GLU   A OE2  1 
ATOM   1751 N  N    . GLU   A 1 240 ? 18.449 -7.247  31.241 1.00 23.44 ?  392 GLU   A N    1 
ATOM   1752 C  CA   . GLU   A 1 240 ? 17.772 -6.553  32.333 1.00 21.49 ?  392 GLU   A CA   1 
ATOM   1753 C  C    . GLU   A 1 240 ? 16.447 -5.939  31.890 1.00 20.28 ?  392 GLU   A C    1 
ATOM   1754 O  O    . GLU   A 1 240 ? 15.468 -5.964  32.647 1.00 22.08 ?  392 GLU   A O    1 
ATOM   1755 C  CB   . GLU   A 1 240 ? 18.685 -5.482  32.925 1.00 20.39 ?  392 GLU   A CB   1 
ATOM   1756 C  CG   . GLU   A 1 240 ? 18.116 -4.774  34.157 1.00 21.71 ?  392 GLU   A CG   1 
ATOM   1757 C  CD   . GLU   A 1 240 ? 17.689 -5.732  35.262 1.00 28.42 ?  392 GLU   A CD   1 
ATOM   1758 O  OE1  . GLU   A 1 240 ? 16.704 -5.423  35.968 1.00 27.66 ?  392 GLU   A OE1  1 
ATOM   1759 O  OE2  . GLU   A 1 240 ? 18.335 -6.789  35.433 1.00 31.11 ?  392 GLU   A OE2  1 
ATOM   1760 N  N    . HIS   A 1 241 ? 16.393 -5.373  30.682 1.00 15.26 ?  393 HIS   A N    1 
ATOM   1761 C  CA   . HIS   A 1 241 ? 15.118 -4.889  30.168 1.00 15.68 ?  393 HIS   A CA   1 
ATOM   1762 C  C    . HIS   A 1 241 ? 14.126 -6.032  30.016 1.00 15.72 ?  393 HIS   A C    1 
ATOM   1763 O  O    . HIS   A 1 241 ? 12.938 -5.874  30.314 1.00 14.47 ?  393 HIS   A O    1 
ATOM   1764 C  CB   . HIS   A 1 241 ? 15.297 -4.176  28.821 1.00 16.41 ?  393 HIS   A CB   1 
ATOM   1765 C  CG   . HIS   A 1 241 ? 13.998 -3.728  28.215 1.00 16.52 ?  393 HIS   A CG   1 
ATOM   1766 N  ND1  . HIS   A 1 241 ? 13.270 -4.513  27.347 1.00 16.15 ?  393 HIS   A ND1  1 
ATOM   1767 C  CD2  . HIS   A 1 241 ? 13.277 -2.593  28.387 1.00 15.26 ?  393 HIS   A CD2  1 
ATOM   1768 C  CE1  . HIS   A 1 241 ? 12.167 -3.874  26.995 1.00 15.78 ?  393 HIS   A CE1  1 
ATOM   1769 N  NE2  . HIS   A 1 241 ? 12.144 -2.709  27.618 1.00 15.94 ?  393 HIS   A NE2  1 
ATOM   1770 N  N    A SER   A 1 242 ? 14.597 -7.195  29.559 0.53 18.93 ?  394 SER   A N    1 
ATOM   1771 N  N    B SER   A 1 242 ? 14.598 -7.192  29.550 0.47 18.92 ?  394 SER   A N    1 
ATOM   1772 C  CA   A SER   A 1 242 ? 13.695 -8.321  29.337 0.53 19.97 ?  394 SER   A CA   1 
ATOM   1773 C  CA   B SER   A 1 242 ? 13.704 -8.326  29.337 0.47 19.99 ?  394 SER   A CA   1 
ATOM   1774 C  C    A SER   A 1 242 ? 13.079 -8.806  30.643 0.53 23.06 ?  394 SER   A C    1 
ATOM   1775 C  C    B SER   A 1 242 ? 13.079 -8.792  30.645 0.47 22.99 ?  394 SER   A C    1 
ATOM   1776 O  O    A SER   A 1 242 ? 11.887 -9.132  30.691 0.53 22.40 ?  394 SER   A O    1 
ATOM   1777 O  O    B SER   A 1 242 ? 11.880 -9.088  30.695 0.47 22.41 ?  394 SER   A O    1 
ATOM   1778 C  CB   A SER   A 1 242 ? 14.438 -9.461  28.642 0.53 19.21 ?  394 SER   A CB   1 
ATOM   1779 C  CB   B SER   A 1 242 ? 14.463 -9.471  28.668 0.47 19.25 ?  394 SER   A CB   1 
ATOM   1780 O  OG   A SER   A 1 242 ? 13.578 -10.569 28.436 0.53 19.57 ?  394 SER   A OG   1 
ATOM   1781 O  OG   B SER   A 1 242 ? 15.007 -9.064  27.426 0.47 20.37 ?  394 SER   A OG   1 
ATOM   1782 N  N    . LYS   A 1 243 ? 13.878 -8.868  31.714 1.00 24.40 ?  395 LYS   A N    1 
ATOM   1783 C  CA   . LYS   A 1 243 ? 13.343 -9.282  33.009 1.00 23.57 ?  395 LYS   A CA   1 
ATOM   1784 C  C    . LYS   A 1 243 ? 12.281 -8.310  33.497 1.00 19.27 ?  395 LYS   A C    1 
ATOM   1785 O  O    . LYS   A 1 243 ? 11.225 -8.726  33.988 1.00 22.05 ?  395 LYS   A O    1 
ATOM   1786 C  CB   . LYS   A 1 243 ? 14.471 -9.391  34.040 1.00 30.16 ?  395 LYS   A CB   1 
ATOM   1787 C  CG   . LYS   A 1 243 ? 15.483 -10.492 33.765 1.00 32.98 ?  395 LYS   A CG   1 
ATOM   1788 C  CD   . LYS   A 1 243 ? 16.645 -10.429 34.749 1.00 36.89 ?  395 LYS   A CD   1 
ATOM   1789 C  CE   . LYS   A 1 243 ? 17.832 -11.249 34.252 1.00 41.39 ?  395 LYS   A CE   1 
ATOM   1790 N  NZ   . LYS   A 1 243 ? 18.887 -11.427 35.294 1.00 45.79 ?  395 LYS   A NZ   1 
ATOM   1791 N  N    . GLN   A 1 244 ? 12.543 -7.009  33.380 1.00 13.67 ?  396 GLN   A N    1 
ATOM   1792 C  CA   . GLN   A 1 244 ? 11.547 -6.037  33.813 1.00 19.00 ?  396 GLN   A CA   1 
ATOM   1793 C  C    . GLN   A 1 244 ? 10.354 -6.010  32.862 1.00 19.59 ?  396 GLN   A C    1 
ATOM   1794 O  O    . GLN   A 1 244 ? 9.209  -5.877  33.308 1.00 19.32 ?  396 GLN   A O    1 
ATOM   1795 C  CB   . GLN   A 1 244 ? 12.193 -4.658  33.954 1.00 16.52 ?  396 GLN   A CB   1 
ATOM   1796 C  CG   . GLN   A 1 244 ? 13.412 -4.691  34.862 1.00 19.04 ?  396 GLN   A CG   1 
ATOM   1797 C  CD   . GLN   A 1 244 ? 13.841 -3.325  35.370 1.00 20.10 ?  396 GLN   A CD   1 
ATOM   1798 O  OE1  . GLN   A 1 244 ? 13.158 -2.318  35.174 1.00 20.52 ?  396 GLN   A OE1  1 
ATOM   1799 N  NE2  . GLN   A 1 244 ? 14.993 -3.287  36.018 1.00 26.19 ?  396 GLN   A NE2  1 
ATOM   1800 N  N    . TYR   A 1 245 ? 10.591 -6.170  31.554 1.00 21.16 ?  397 TYR   A N    1 
ATOM   1801 C  CA   . TYR   A 1 245 ? 9.472  -6.250  30.614 1.00 14.91 ?  397 TYR   A CA   1 
ATOM   1802 C  C    . TYR   A 1 245 ? 8.587  -7.450  30.920 1.00 15.95 ?  397 TYR   A C    1 
ATOM   1803 O  O    . TYR   A 1 245 ? 7.357  -7.344  30.915 1.00 16.05 ?  397 TYR   A O    1 
ATOM   1804 C  CB   . TYR   A 1 245 ? 9.968  -6.326  29.169 1.00 17.67 ?  397 TYR   A CB   1 
ATOM   1805 C  CG   . TYR   A 1 245 ? 8.817  -6.494  28.196 1.00 17.61 ?  397 TYR   A CG   1 
ATOM   1806 C  CD1  . TYR   A 1 245 ? 8.114  -5.390  27.724 1.00 16.13 ?  397 TYR   A CD1  1 
ATOM   1807 C  CD2  . TYR   A 1 245 ? 8.406  -7.757  27.782 1.00 16.92 ?  397 TYR   A CD2  1 
ATOM   1808 C  CE1  . TYR   A 1 245 ? 7.050  -5.537  26.853 1.00 14.09 ?  397 TYR   A CE1  1 
ATOM   1809 C  CE2  . TYR   A 1 245 ? 7.344  -7.913  26.915 1.00 16.94 ?  397 TYR   A CE2  1 
ATOM   1810 C  CZ   . TYR   A 1 245 ? 6.671  -6.800  26.453 1.00 15.36 ?  397 TYR   A CZ   1 
ATOM   1811 O  OH   . TYR   A 1 245 ? 5.615  -6.957  25.586 1.00 17.08 ?  397 TYR   A OH   1 
ATOM   1812 N  N    A ARG   A 1 246 ? 9.199  -8.610  31.178 0.50 19.42 ?  398 ARG   A N    1 
ATOM   1813 N  N    B ARG   A 1 246 ? 9.203  -8.611  31.162 0.50 19.40 ?  398 ARG   A N    1 
ATOM   1814 C  CA   A ARG   A 1 246 ? 8.418  -9.795  31.525 0.50 22.76 ?  398 ARG   A CA   1 
ATOM   1815 C  CA   B ARG   A 1 246 ? 8.450  -9.802  31.542 0.50 22.79 ?  398 ARG   A CA   1 
ATOM   1816 C  C    A ARG   A 1 246 ? 7.585  -9.558  32.780 0.50 24.47 ?  398 ARG   A C    1 
ATOM   1817 C  C    B ARG   A 1 246 ? 7.583  -9.533  32.766 0.50 24.45 ?  398 ARG   A C    1 
ATOM   1818 O  O    A ARG   A 1 246 ? 6.420  -9.967  32.847 0.50 24.58 ?  398 ARG   A O    1 
ATOM   1819 O  O    B ARG   A 1 246 ? 6.401  -9.892  32.800 0.50 24.44 ?  398 ARG   A O    1 
ATOM   1820 C  CB   A ARG   A 1 246 ? 9.340  -11.000 31.716 0.50 24.80 ?  398 ARG   A CB   1 
ATOM   1821 C  CB   B ARG   A 1 246 ? 9.410  -10.959 31.819 0.50 24.76 ?  398 ARG   A CB   1 
ATOM   1822 C  CG   A ARG   A 1 246 ? 8.624  -12.250 32.217 0.50 25.52 ?  398 ARG   A CG   1 
ATOM   1823 C  CG   B ARG   A 1 246 ? 9.839  -11.744 30.595 0.50 24.92 ?  398 ARG   A CG   1 
ATOM   1824 C  CD   A ARG   A 1 246 ? 9.559  -13.452 32.289 0.50 29.59 ?  398 ARG   A CD   1 
ATOM   1825 C  CD   B ARG   A 1 246 ? 10.483 -13.061 31.007 0.50 28.59 ?  398 ARG   A CD   1 
ATOM   1826 N  NE   A ARG   A 1 246 ? 8.825  -14.693 32.527 0.50 33.71 ?  398 ARG   A NE   1 
ATOM   1827 N  NE   B ARG   A 1 246 ? 11.770 -13.280 30.350 0.50 29.78 ?  398 ARG   A NE   1 
ATOM   1828 C  CZ   A ARG   A 1 246 ? 9.140  -15.586 33.460 0.50 34.77 ?  398 ARG   A CZ   1 
ATOM   1829 C  CZ   B ARG   A 1 246 ? 12.947 -12.996 30.896 0.50 30.47 ?  398 ARG   A CZ   1 
ATOM   1830 N  NH1  A ARG   A 1 246 ? 10.185 -15.384 34.253 0.50 32.72 ?  398 ARG   A NH1  1 
ATOM   1831 N  NH1  B ARG   A 1 246 ? 13.009 -12.478 32.114 0.50 32.03 ?  398 ARG   A NH1  1 
ATOM   1832 N  NH2  A ARG   A 1 246 ? 8.408  -16.685 33.600 0.50 35.63 ?  398 ARG   A NH2  1 
ATOM   1833 N  NH2  B ARG   A 1 246 ? 14.064 -13.230 30.225 0.50 31.48 ?  398 ARG   A NH2  1 
ATOM   1834 N  N    . SER   A 1 247 ? 8.163  -8.892  33.782 1.00 24.07 ?  399 SER   A N    1 
ATOM   1835 C  CA   . SER   A 1 247 ? 7.412  -8.588  34.995 1.00 25.93 ?  399 SER   A CA   1 
ATOM   1836 C  C    . SER   A 1 247 ? 6.295  -7.585  34.725 1.00 23.84 ?  399 SER   A C    1 
ATOM   1837 O  O    . SER   A 1 247 ? 5.169  -7.758  35.206 1.00 25.63 ?  399 SER   A O    1 
ATOM   1838 C  CB   . SER   A 1 247 ? 8.364  -8.063  36.071 1.00 28.91 ?  399 SER   A CB   1 
ATOM   1839 O  OG   . SER   A 1 247 ? 7.641  -7.451  37.121 1.00 34.87 ?  399 SER   A OG   1 
ATOM   1840 N  N    . LEU   A 1 248 ? 6.582  -6.535  33.953 1.00 24.79 ?  400 LEU   A N    1 
ATOM   1841 C  CA   . LEU   A 1 248 ? 5.572  -5.514  33.688 1.00 24.15 ?  400 LEU   A CA   1 
ATOM   1842 C  C    . LEU   A 1 248 ? 4.440  -6.062  32.828 1.00 22.63 ?  400 LEU   A C    1 
ATOM   1843 O  O    . LEU   A 1 248 ? 3.259  -5.893  33.157 1.00 22.87 ?  400 LEU   A O    1 
ATOM   1844 C  CB   . LEU   A 1 248 ? 6.212  -4.304  33.008 1.00 23.26 ?  400 LEU   A CB   1 
ATOM   1845 C  CG   . LEU   A 1 248 ? 7.025  -3.344  33.874 1.00 24.95 ?  400 LEU   A CG   1 
ATOM   1846 C  CD1  . LEU   A 1 248 ? 7.815  -2.389  32.982 1.00 25.56 ?  400 LEU   A CD1  1 
ATOM   1847 C  CD2  . LEU   A 1 248 ? 6.112  -2.577  34.821 1.00 25.73 ?  400 LEU   A CD2  1 
ATOM   1848 N  N    . SER   A 1 249 ? 4.781  -6.711  31.713 1.00 22.80 ?  401 SER   A N    1 
ATOM   1849 C  CA   . SER   A 1 249 ? 3.769  -7.171  30.772 1.00 23.97 ?  401 SER   A CA   1 
ATOM   1850 C  C    . SER   A 1 249 ? 2.966  -8.348  31.305 1.00 26.46 ?  401 SER   A C    1 
ATOM   1851 O  O    . SER   A 1 249 ? 1.917  -8.672  30.734 1.00 24.90 ?  401 SER   A O    1 
ATOM   1852 C  CB   . SER   A 1 249 ? 4.418  -7.532  29.430 1.00 22.26 ?  401 SER   A CB   1 
ATOM   1853 O  OG   . SER   A 1 249 ? 5.259  -8.670  29.531 1.00 24.95 ?  401 SER   A OG   1 
ATOM   1854 N  N    . PHE   A 1 250 ? 3.417  -8.984  32.386 1.00 24.76 ?  402 PHE   A N    1 
ATOM   1855 C  CA   . PHE   A 1 250 ? 2.624  -10.042 32.996 1.00 26.71 ?  402 PHE   A CA   1 
ATOM   1856 C  C    . PHE   A 1 250 ? 1.346  -9.504  33.638 1.00 25.08 ?  402 PHE   A C    1 
ATOM   1857 O  O    . PHE   A 1 250 ? 0.378  -10.256 33.780 1.00 27.09 ?  402 PHE   A O    1 
ATOM   1858 C  CB   . PHE   A 1 250 ? 3.468  -10.799 34.025 1.00 32.03 ?  402 PHE   A CB   1 
ATOM   1859 C  CG   . PHE   A 1 250 ? 2.826  -12.062 34.522 1.00 39.55 ?  402 PHE   A CG   1 
ATOM   1860 C  CD1  . PHE   A 1 250 ? 2.822  -13.209 33.739 1.00 42.91 ?  402 PHE   A CD1  1 
ATOM   1861 C  CD2  . PHE   A 1 250 ? 2.215  -12.101 35.771 1.00 41.54 ?  402 PHE   A CD2  1 
ATOM   1862 C  CE1  . PHE   A 1 250 ? 2.223  -14.376 34.195 1.00 46.40 ?  402 PHE   A CE1  1 
ATOM   1863 C  CE2  . PHE   A 1 250 ? 1.617  -13.263 36.234 1.00 43.55 ?  402 PHE   A CE2  1 
ATOM   1864 C  CZ   . PHE   A 1 250 ? 1.620  -14.403 35.445 1.00 46.11 ?  402 PHE   A CZ   1 
ATOM   1865 N  N    . GLN   A 1 251 ? 1.324  -8.231  34.024 1.00 27.81 ?  403 GLN   A N    1 
ATOM   1866 C  CA   . GLN   A 1 251 ? 0.115  -7.602  34.547 1.00 23.97 ?  403 GLN   A CA   1 
ATOM   1867 C  C    . GLN   A 1 251 ? -0.789 -7.188  33.392 1.00 26.37 ?  403 GLN   A C    1 
ATOM   1868 O  O    . GLN   A 1 251 ? -0.375 -6.372  32.558 1.00 22.09 ?  403 GLN   A O    1 
ATOM   1869 C  CB   . GLN   A 1 251 ? 0.468  -6.380  35.384 1.00 26.91 ?  403 GLN   A CB   1 
ATOM   1870 C  CG   . GLN   A 1 251 ? 1.462  -6.643  36.503 1.00 36.46 ?  403 GLN   A CG   1 
ATOM   1871 C  CD   . GLN   A 1 251 ? 0.986  -7.721  37.459 1.00 44.13 ?  403 GLN   A CD   1 
ATOM   1872 O  OE1  . GLN   A 1 251 ? 1.691  -8.703  37.706 1.00 47.01 ?  403 GLN   A OE1  1 
ATOM   1873 N  NE2  . GLN   A 1 251 ? -0.221 -7.548  37.999 1.00 45.01 ?  403 GLN   A NE2  1 
ATOM   1874 N  N    . PRO   A 1 252 ? -2.017 -7.714  33.302 1.00 24.50 ?  404 PRO   A N    1 
ATOM   1875 C  CA   . PRO   A 1 252 ? -2.882 -7.353  32.163 1.00 24.30 ?  404 PRO   A CA   1 
ATOM   1876 C  C    . PRO   A 1 252 ? -3.152 -5.862  32.065 1.00 25.22 ?  404 PRO   A C    1 
ATOM   1877 O  O    . PRO   A 1 252 ? -3.352 -5.355  30.954 1.00 24.31 ?  404 PRO   A O    1 
ATOM   1878 C  CB   . PRO   A 1 252 ? -4.171 -8.148  32.423 1.00 24.46 ?  404 PRO   A CB   1 
ATOM   1879 C  CG   . PRO   A 1 252 ? -3.800 -9.219  33.394 1.00 24.29 ?  404 PRO   A CG   1 
ATOM   1880 C  CD   . PRO   A 1 252 ? -2.620 -8.727  34.183 1.00 22.10 ?  404 PRO   A CD   1 
ATOM   1881 N  N    . GLU   A 1 253 ? -3.131 -5.139  33.191 1.00 23.53 ?  405 GLU   A N    1 
ATOM   1882 C  CA   . GLU   A 1 253 ? -3.324 -3.693  33.151 1.00 28.82 ?  405 GLU   A CA   1 
ATOM   1883 C  C    . GLU   A 1 253 ? -2.181 -2.989  32.438 1.00 27.68 ?  405 GLU   A C    1 
ATOM   1884 O  O    . GLU   A 1 253 ? -2.391 -1.928  31.841 1.00 31.62 ?  405 GLU   A O    1 
ATOM   1885 C  CB   . GLU   A 1 253 ? -3.468 -3.131  34.565 1.00 37.46 ?  405 GLU   A CB   1 
ATOM   1886 C  CG   . GLU   A 1 253 ? -4.190 -4.048  35.527 1.00 50.20 ?  405 GLU   A CG   1 
ATOM   1887 C  CD   . GLU   A 1 253 ? -3.275 -5.109  36.105 1.00 57.00 ?  405 GLU   A CD   1 
ATOM   1888 O  OE1  . GLU   A 1 253 ? -2.740 -4.895  37.212 1.00 61.64 ?  405 GLU   A OE1  1 
ATOM   1889 O  OE2  . GLU   A 1 253 ? -3.084 -6.153  35.450 1.00 59.88 ?  405 GLU   A OE2  1 
ATOM   1890 N  N    . ASN   A 1 254 ? -0.965 -3.539  32.509 1.00 22.24 ?  406 ASN   A N    1 
ATOM   1891 C  CA   . ASN   A 1 254 ? 0.139  -2.979  31.735 1.00 17.57 ?  406 ASN   A CA   1 
ATOM   1892 C  C    . ASN   A 1 254 ? 0.100  -3.459  30.291 1.00 14.71 ?  406 ASN   A C    1 
ATOM   1893 O  O    . ASN   A 1 254 ? 0.307  -2.667  29.364 1.00 16.18 ?  406 ASN   A O    1 
ATOM   1894 C  CB   . ASN   A 1 254 ? 1.487  -3.340  32.365 1.00 15.14 ?  406 ASN   A CB   1 
ATOM   1895 C  CG   . ASN   A 1 254 ? 1.615  -2.860  33.794 1.00 23.64 ?  406 ASN   A CG   1 
ATOM   1896 O  OD1  . ASN   A 1 254 ? 1.075  -1.815  34.164 1.00 27.28 ?  406 ASN   A OD1  1 
ATOM   1897 N  ND2  . ASN   A 1 254 ? 2.350  -3.615  34.605 1.00 22.05 ?  406 ASN   A ND2  1 
ATOM   1898 N  N    . SER   A 1 255 ? -0.129 -4.763  30.085 1.00 16.15 ?  407 SER   A N    1 
ATOM   1899 C  CA   . SER   A 1 255 ? -0.240 -5.305  28.729 1.00 21.85 ?  407 SER   A CA   1 
ATOM   1900 C  C    . SER   A 1 255 ? -1.243 -4.523  27.895 1.00 25.18 ?  407 SER   A C    1 
ATOM   1901 O  O    . SER   A 1 255 ? -1.021 -4.288  26.700 1.00 26.54 ?  407 SER   A O    1 
ATOM   1902 C  CB   . SER   A 1 255 ? -0.648 -6.778  28.776 1.00 23.85 ?  407 SER   A CB   1 
ATOM   1903 O  OG   . SER   A 1 255 ? 0.492  -7.617  28.734 1.00 31.76 ?  407 SER   A OG   1 
ATOM   1904 N  N    . MET   A 1 256 ? -2.356 -4.115  28.514 1.00 25.05 ?  408 MET   A N    1 
ATOM   1905 C  CA   . MET   A 1 256 ? -3.394 -3.374  27.807 1.00 25.93 ?  408 MET   A CA   1 
ATOM   1906 C  C    . MET   A 1 256 ? -2.873 -2.070  27.234 1.00 22.23 ?  408 MET   A C    1 
ATOM   1907 O  O    . MET   A 1 256 ? -3.416 -1.571  26.244 1.00 18.28 ?  408 MET   A O    1 
ATOM   1908 C  CB   . MET   A 1 256 ? -4.559 -3.077  28.745 1.00 26.12 ?  408 MET   A CB   1 
ATOM   1909 C  CG   . MET   A 1 256 ? -5.776 -3.912  28.509 1.00 31.77 ?  408 MET   A CG   1 
ATOM   1910 S  SD   . MET   A 1 256 ? -7.065 -3.546  29.719 1.00 36.52 ?  408 MET   A SD   1 
ATOM   1911 C  CE   . MET   A 1 256 ? -6.737 -1.837  30.135 1.00 30.36 ?  408 MET   A CE   1 
ATOM   1912 N  N    . LYS   A 1 257 ? -1.852 -1.486  27.857 1.00 21.14 ?  409 LYS   A N    1 
ATOM   1913 C  CA   . LYS   A 1 257 ? -1.320 -0.208  27.410 1.00 21.48 ?  409 LYS   A CA   1 
ATOM   1914 C  C    . LYS   A 1 257 ? -0.239 -0.350  26.351 1.00 15.71 ?  409 LYS   A C    1 
ATOM   1915 O  O    . LYS   A 1 257 ? 0.208  0.664   25.805 1.00 16.41 ?  409 LYS   A O    1 
ATOM   1916 C  CB   . LYS   A 1 257 ? -0.768 0.584   28.601 1.00 25.06 ?  409 LYS   A CB   1 
ATOM   1917 C  CG   . LYS   A 1 257 ? -1.805 0.902   29.674 1.00 31.01 ?  409 LYS   A CG   1 
ATOM   1918 C  CD   . LYS   A 1 257 ? -3.144 1.307   29.069 1.00 37.16 ?  409 LYS   A CD   1 
ATOM   1919 C  CE   . LYS   A 1 257 ? -3.259 2.822   28.907 1.00 40.81 ?  409 LYS   A CE   1 
ATOM   1920 N  NZ   . LYS   A 1 257 ? -4.670 3.306   29.022 1.00 40.87 ?  409 LYS   A NZ   1 
ATOM   1921 N  N    . LEU   A 1 258 ? 0.187  -1.569  26.040 1.00 13.99 ?  410 LEU   A N    1 
ATOM   1922 C  CA   . LEU   A 1 258 ? 1.224  -1.762  25.033 1.00 15.31 ?  410 LEU   A CA   1 
ATOM   1923 C  C    . LEU   A 1 258 ? 0.585  -1.681  23.647 1.00 18.48 ?  410 LEU   A C    1 
ATOM   1924 O  O    . LEU   A 1 258 ? -0.589 -1.336  23.496 1.00 15.64 ?  410 LEU   A O    1 
ATOM   1925 C  CB   . LEU   A 1 258 ? 1.955  -3.082  25.276 1.00 11.14 ?  410 LEU   A CB   1 
ATOM   1926 C  CG   . LEU   A 1 258 ? 2.591  -3.205  26.671 1.00 12.94 ?  410 LEU   A CG   1 
ATOM   1927 C  CD1  . LEU   A 1 258 ? 3.319  -4.530  26.840 1.00 13.61 ?  410 LEU   A CD1  1 
ATOM   1928 C  CD2  . LEU   A 1 258 ? 3.538  -2.045  26.941 1.00 12.24 ?  410 LEU   A CD2  1 
ATOM   1929 N  N    . THR   A 1 259 ? 1.352  -1.984  22.612 1.00 19.66 ?  411 THR   A N    1 
ATOM   1930 C  CA   . THR   A 1 259 ? 0.825  -2.061  21.262 1.00 15.49 ?  411 THR   A CA   1 
ATOM   1931 C  C    . THR   A 1 259 ? 0.942  -3.495  20.767 1.00 15.60 ?  411 THR   A C    1 
ATOM   1932 O  O    . THR   A 1 259 ? 1.731  -4.282  21.304 1.00 18.33 ?  411 THR   A O    1 
ATOM   1933 C  CB   . THR   A 1 259 ? 1.575  -1.118  20.310 1.00 14.27 ?  411 THR   A CB   1 
ATOM   1934 O  OG1  . THR   A 1 259 ? 2.859  -1.670  20.010 1.00 15.98 ?  411 THR   A OG1  1 
ATOM   1935 C  CG2  . THR   A 1 259 ? 1.745  0.253   20.935 1.00 17.91 ?  411 THR   A CG2  1 
ATOM   1936 N  N    . PRO   A 1 260 ? 0.160  -3.874  19.749 1.00 13.63 ?  412 PRO   A N    1 
ATOM   1937 C  CA   . PRO   A 1 260 ? 0.261  -5.250  19.231 1.00 13.77 ?  412 PRO   A CA   1 
ATOM   1938 C  C    . PRO   A 1 260 ? 1.651  -5.628  18.744 1.00 10.38 ?  412 PRO   A C    1 
ATOM   1939 O  O    . PRO   A 1 260 ? 2.075  -6.769  18.957 1.00 16.23 ?  412 PRO   A O    1 
ATOM   1940 C  CB   . PRO   A 1 260 ? -0.762 -5.259  18.086 1.00 15.96 ?  412 PRO   A CB   1 
ATOM   1941 C  CG   . PRO   A 1 260 ? -1.755 -4.203  18.472 1.00 17.42 ?  412 PRO   A CG   1 
ATOM   1942 C  CD   . PRO   A 1 260 ? -0.950 -3.128  19.127 1.00 12.60 ?  412 PRO   A CD   1 
ATOM   1943 N  N    . LEU   A 1 261 ? 2.367  -4.713  18.080 1.00 11.84 ?  413 LEU   A N    1 
ATOM   1944 C  CA   . LEU   A 1 261 ? 3.709  -5.027  17.593 1.00 9.35  ?  413 LEU   A CA   1 
ATOM   1945 C  C    . LEU   A 1 261 ? 4.687  -5.253  18.746 1.00 12.72 ?  413 LEU   A C    1 
ATOM   1946 O  O    . LEU   A 1 261 ? 5.574  -6.112  18.656 1.00 15.23 ?  413 LEU   A O    1 
ATOM   1947 C  CB   . LEU   A 1 261 ? 4.221  -3.910  16.685 1.00 19.33 ?  413 LEU   A CB   1 
ATOM   1948 C  CG   . LEU   A 1 261 ? 5.599  -4.135  16.037 1.00 22.10 ?  413 LEU   A CG   1 
ATOM   1949 C  CD1  . LEU   A 1 261 ? 5.573  -5.271  14.998 1.00 21.24 ?  413 LEU   A CD1  1 
ATOM   1950 C  CD2  . LEU   A 1 261 ? 6.160  -2.853  15.417 1.00 16.95 ?  413 LEU   A CD2  1 
ATOM   1951 N  N    . VAL   A 1 262 ? 4.554  -4.489  19.830 1.00 12.57 ?  414 VAL   A N    1 
ATOM   1952 C  CA   . VAL   A 1 262 ? 5.423  -4.704  20.985 1.00 13.57 ?  414 VAL   A CA   1 
ATOM   1953 C  C    . VAL   A 1 262 ? 5.166  -6.080  21.586 1.00 17.44 ?  414 VAL   A C    1 
ATOM   1954 O  O    . VAL   A 1 262 ? 6.103  -6.841  21.857 1.00 17.13 ?  414 VAL   A O    1 
ATOM   1955 C  CB   . VAL   A 1 262 ? 5.231  -3.585  22.024 1.00 17.50 ?  414 VAL   A CB   1 
ATOM   1956 C  CG1  . VAL   A 1 262 ? 5.919  -3.954  23.341 1.00 19.44 ?  414 VAL   A CG1  1 
ATOM   1957 C  CG2  . VAL   A 1 262 ? 5.762  -2.258  21.481 1.00 15.02 ?  414 VAL   A CG2  1 
ATOM   1958 N  N    . LEU   A 1 263 ? 3.887  -6.430  21.777 1.00 15.35 ?  415 LEU   A N    1 
ATOM   1959 C  CA   . LEU   A 1 263 ? 3.554  -7.733  22.351 1.00 14.47 ?  415 LEU   A CA   1 
ATOM   1960 C  C    . LEU   A 1 263 ? 4.053  -8.872  21.469 1.00 14.68 ?  415 LEU   A C    1 
ATOM   1961 O  O    . LEU   A 1 263 ? 4.568  -9.876  21.973 1.00 15.07 ?  415 LEU   A O    1 
ATOM   1962 C  CB   . LEU   A 1 263 ? 2.042  -7.849  22.566 1.00 14.11 ?  415 LEU   A CB   1 
ATOM   1963 C  CG   . LEU   A 1 263 ? 1.439  -6.960  23.655 1.00 16.46 ?  415 LEU   A CG   1 
ATOM   1964 C  CD1  . LEU   A 1 263 ? -0.080 -6.955  23.566 1.00 11.18 ?  415 LEU   A CD1  1 
ATOM   1965 C  CD2  . LEU   A 1 263 ? 1.901  -7.419  25.042 1.00 17.29 ?  415 LEU   A CD2  1 
ATOM   1966 N  N    . GLU   A 1 264 ? 3.913  -8.735  20.149 1.00 13.59 ?  416 GLU   A N    1 
ATOM   1967 C  CA   . GLU   A 1 264 ? 4.418  -9.767  19.248 1.00 18.81 ?  416 GLU   A CA   1 
ATOM   1968 C  C    . GLU   A 1 264 ? 5.939  -9.858  19.305 1.00 18.85 ?  416 GLU   A C    1 
ATOM   1969 O  O    . GLU   A 1 264 ? 6.498  -10.937 19.534 1.00 18.46 ?  416 GLU   A O    1 
ATOM   1970 C  CB   . GLU   A 1 264 ? 3.957  -9.493  17.817 1.00 22.09 ?  416 GLU   A CB   1 
ATOM   1971 C  CG   . GLU   A 1 264 ? 4.149  -10.673 16.883 1.00 27.81 ?  416 GLU   A CG   1 
ATOM   1972 C  CD   . GLU   A 1 264 ? 3.971  -10.298 15.424 1.00 29.64 ?  416 GLU   A CD   1 
ATOM   1973 O  OE1  . GLU   A 1 264 ? 4.982  -9.962  14.762 1.00 28.61 ?  416 GLU   A OE1  1 
ATOM   1974 O  OE2  . GLU   A 1 264 ? 2.821  -10.342 14.940 1.00 30.36 ?  416 GLU   A OE2  1 
ATOM   1975 N  N    . VAL   A 1 265 ? 6.627  -8.732  19.103 1.00 17.01 ?  417 VAL   A N    1 
ATOM   1976 C  CA   . VAL   A 1 265 ? 8.077  -8.769  18.932 1.00 17.64 ?  417 VAL   A CA   1 
ATOM   1977 C  C    . VAL   A 1 265 ? 8.768  -9.097  20.254 1.00 18.05 ?  417 VAL   A C    1 
ATOM   1978 O  O    . VAL   A 1 265 ? 9.653  -9.957  20.306 1.00 19.97 ?  417 VAL   A O    1 
ATOM   1979 C  CB   . VAL   A 1 265 ? 8.581  -7.442  18.333 1.00 16.56 ?  417 VAL   A CB   1 
ATOM   1980 C  CG1  . VAL   A 1 265 ? 10.112 -7.364  18.402 1.00 14.91 ?  417 VAL   A CG1  1 
ATOM   1981 C  CG2  . VAL   A 1 265 ? 8.102  -7.302  16.897 1.00 15.40 ?  417 VAL   A CG2  1 
ATOM   1982 N  N    . PHE   A 1 266 ? 8.361  -8.434  21.343 1.00 19.25 ?  418 PHE   A N    1 
ATOM   1983 C  CA   . PHE   A 1 266 ? 8.947  -8.664  22.663 1.00 22.79 ?  418 PHE   A CA   1 
ATOM   1984 C  C    . PHE   A 1 266 ? 8.385  -9.886  23.377 1.00 29.11 ?  418 PHE   A C    1 
ATOM   1985 O  O    . PHE   A 1 266 ? 8.867  -10.211 24.466 1.00 32.01 ?  418 PHE   A O    1 
ATOM   1986 C  CB   . PHE   A 1 266 ? 8.742  -7.450  23.575 1.00 20.23 ?  418 PHE   A CB   1 
ATOM   1987 C  CG   . PHE   A 1 266 ? 9.605  -6.265  23.236 1.00 20.12 ?  418 PHE   A CG   1 
ATOM   1988 C  CD1  . PHE   A 1 266 ? 9.417  -5.055  23.887 1.00 18.59 ?  418 PHE   A CD1  1 
ATOM   1989 C  CD2  . PHE   A 1 266 ? 10.603 -6.359  22.281 1.00 19.63 ?  418 PHE   A CD2  1 
ATOM   1990 C  CE1  . PHE   A 1 266 ? 10.197 -3.960  23.586 1.00 20.78 ?  418 PHE   A CE1  1 
ATOM   1991 C  CE2  . PHE   A 1 266 ? 11.388 -5.265  21.974 1.00 20.00 ?  418 PHE   A CE2  1 
ATOM   1992 C  CZ   . PHE   A 1 266 ? 11.188 -4.065  22.627 1.00 22.19 ?  418 PHE   A CZ   1 
ATOM   1993 N  N    . GLY   A 1 267 ? 7.382  -10.557 22.820 1.00 35.56 ?  419 GLY   A N    1 
ATOM   1994 C  CA   . GLY   A 1 267 ? 6.776  -11.680 23.511 1.00 43.07 ?  419 GLY   A CA   1 
ATOM   1995 C  C    . GLY   A 1 267 ? 6.986  -13.016 22.829 1.00 51.84 ?  419 GLY   A C    1 
ATOM   1996 O  O    . GLY   A 1 267 ? 8.120  -13.398 22.523 1.00 54.19 ?  419 GLY   A O    1 
ATOM   1997 N  N    . ASN   A 1 268 ? 5.899  -13.742 22.593 1.00 58.52 ?  420 ASN   A N    1 
ATOM   1998 C  CA   . ASN   A 1 268 ? 5.974  -15.021 21.896 1.00 63.25 ?  420 ASN   A CA   1 
ATOM   1999 C  C    . ASN   A 1 268 ? 5.365  -14.905 20.504 1.00 61.80 ?  420 ASN   A C    1 
ATOM   2000 O  O    . ASN   A 1 268 ? 5.537  -13.892 19.826 1.00 59.38 ?  420 ASN   A O    1 
ATOM   2001 C  CB   . ASN   A 1 268 ? 5.267  -16.118 22.697 1.00 67.43 ?  420 ASN   A CB   1 
ATOM   2002 C  CG   . ASN   A 1 268 ? 5.766  -17.509 22.348 1.00 69.18 ?  420 ASN   A CG   1 
ATOM   2003 O  OD1  . ASN   A 1 268 ? 6.912  -17.861 22.634 1.00 68.49 ?  420 ASN   A OD1  1 
ATOM   2004 N  ND2  . ASN   A 1 268 ? 4.907  -18.307 21.722 1.00 68.96 ?  420 ASN   A ND2  1 
ATOM   2005 N  N    . LYS   B 2 1   ? 2.806  -19.501 11.509 1.00 62.25 ?  625 LYS   C N    1 
ATOM   2006 C  CA   . LYS   B 2 1   ? 3.875  -18.784 12.197 1.00 61.34 ?  625 LYS   C CA   1 
ATOM   2007 C  C    . LYS   B 2 1   ? 3.317  -17.833 13.256 1.00 59.11 ?  625 LYS   C C    1 
ATOM   2008 O  O    . LYS   B 2 1   ? 2.150  -17.444 13.210 1.00 59.74 ?  625 LYS   C O    1 
ATOM   2009 C  CB   . LYS   B 2 1   ? 4.738  -18.013 11.195 1.00 61.13 ?  625 LYS   C CB   1 
ATOM   2010 C  CG   . LYS   B 2 1   ? 6.114  -18.626 10.971 1.00 60.96 ?  625 LYS   C CG   1 
ATOM   2011 C  CD   . LYS   B 2 1   ? 6.835  -17.958 9.809  1.00 59.96 ?  625 LYS   C CD   1 
ATOM   2012 C  CE   . LYS   B 2 1   ? 8.053  -18.760 9.380  1.00 58.90 ?  625 LYS   C CE   1 
ATOM   2013 N  NZ   . LYS   B 2 1   ? 9.149  -17.877 8.898  1.00 57.01 ?  625 LYS   C NZ   1 
ATOM   2014 N  N    . ASN   B 2 2   ? 4.173  -17.454 14.202 1.00 54.64 ?  626 ASN   C N    1 
ATOM   2015 C  CA   . ASN   B 2 2   ? 3.758  -16.698 15.373 1.00 50.15 ?  626 ASN   C CA   1 
ATOM   2016 C  C    . ASN   B 2 2   ? 3.841  -15.187 15.196 1.00 42.02 ?  626 ASN   C C    1 
ATOM   2017 O  O    . ASN   B 2 2   ? 3.331  -14.459 16.053 1.00 43.77 ?  626 ASN   C O    1 
ATOM   2018 C  CB   . ASN   B 2 2   ? 4.614  -17.099 16.582 1.00 54.79 ?  626 ASN   C CB   1 
ATOM   2019 C  CG   . ASN   B 2 2   ? 3.884  -18.017 17.537 1.00 57.93 ?  626 ASN   C CG   1 
ATOM   2020 O  OD1  . ASN   B 2 2   ? 2.708  -17.811 17.840 1.00 57.68 ?  626 ASN   C OD1  1 
ATOM   2021 N  ND2  . ASN   B 2 2   ? 4.584  -19.035 18.026 1.00 59.73 ?  626 ASN   C ND2  1 
ATOM   2022 N  N    . HIS   B 2 3   ? 4.455  -14.692 14.121 1.00 32.75 ?  627 HIS   C N    1 
ATOM   2023 C  CA   . HIS   B 2 3   ? 4.840  -13.281 14.021 1.00 26.18 ?  627 HIS   C CA   1 
ATOM   2024 C  C    . HIS   B 2 3   ? 4.331  -12.644 12.733 1.00 24.33 ?  627 HIS   C C    1 
ATOM   2025 O  O    . HIS   B 2 3   ? 5.118  -12.152 11.918 1.00 26.67 ?  627 HIS   C O    1 
ATOM   2026 C  CB   . HIS   B 2 3   ? 6.358  -13.149 14.134 1.00 27.16 ?  627 HIS   C CB   1 
ATOM   2027 C  CG   . HIS   B 2 3   ? 6.905  -13.668 15.426 1.00 26.10 ?  627 HIS   C CG   1 
ATOM   2028 N  ND1  . HIS   B 2 3   ? 7.180  -15.003 15.633 1.00 28.11 ?  627 HIS   C ND1  1 
ATOM   2029 C  CD2  . HIS   B 2 3   ? 7.199  -13.039 16.588 1.00 24.99 ?  627 HIS   C CD2  1 
ATOM   2030 C  CE1  . HIS   B 2 3   ? 7.631  -15.171 16.864 1.00 26.80 ?  627 HIS   C CE1  1 
ATOM   2031 N  NE2  . HIS   B 2 3   ? 7.647  -13.995 17.465 1.00 25.22 ?  627 HIS   C NE2  1 
ATOM   2032 N  N    . PRO   B 2 4   ? 3.006  -12.586 12.543 1.00 22.07 ?  628 PRO   C N    1 
ATOM   2033 C  CA   . PRO   B 2 4   ? 2.484  -12.047 11.275 1.00 22.44 ?  628 PRO   C CA   1 
ATOM   2034 C  C    . PRO   B 2 4   ? 2.791  -10.575 11.071 1.00 21.99 ?  628 PRO   C C    1 
ATOM   2035 O  O    . PRO   B 2 4   ? 3.064  -10.155 9.941  1.00 24.59 ?  628 PRO   C O    1 
ATOM   2036 C  CB   . PRO   B 2 4   ? 0.972  -12.303 11.382 1.00 21.28 ?  628 PRO   C CB   1 
ATOM   2037 C  CG   . PRO   B 2 4   ? 0.703  -12.365 12.839 1.00 22.53 ?  628 PRO   C CG   1 
ATOM   2038 C  CD   . PRO   B 2 4   ? 1.922  -12.986 13.459 1.00 22.66 ?  628 PRO   C CD   1 
ATOM   2039 N  N    . MET   B 2 5   ? 2.765  -9.775  12.135 1.00 20.63 ?  629 MET   C N    1 
ATOM   2040 C  CA   . MET   B 2 5   ? 3.008  -8.346  11.978 1.00 23.76 ?  629 MET   C CA   1 
ATOM   2041 C  C    . MET   B 2 5   ? 4.470  -8.069  11.656 1.00 22.25 ?  629 MET   C C    1 
ATOM   2042 O  O    . MET   B 2 5   ? 4.775  -7.219  10.811 1.00 24.33 ?  629 MET   C O    1 
ATOM   2043 C  CB   . MET   B 2 5   ? 2.569  -7.604  13.242 1.00 26.76 ?  629 MET   C CB   1 
ATOM   2044 C  CG   . MET   B 2 5   ? 1.060  -7.660  13.471 1.00 30.54 ?  629 MET   C CG   1 
ATOM   2045 S  SD   . MET   B 2 5   ? 0.524  -6.844  14.991 1.00 33.48 ?  629 MET   C SD   1 
ATOM   2046 C  CE   . MET   B 2 5   ? 0.826  -8.132  16.185 1.00 34.38 ?  629 MET   C CE   1 
ATOM   2047 N  N    . LEU   B 2 6   ? 5.385  -8.784  12.315 1.00 16.33 ?  630 LEU   C N    1 
ATOM   2048 C  CA   . LEU   B 2 6   ? 6.804  -8.656  12.002 1.00 18.16 ?  630 LEU   C CA   1 
ATOM   2049 C  C    . LEU   B 2 6   ? 7.109  -9.204  10.612 1.00 21.44 ?  630 LEU   C C    1 
ATOM   2050 O  O    . LEU   B 2 6   ? 7.836  -8.570  9.836  1.00 21.57 ?  630 LEU   C O    1 
ATOM   2051 C  CB   . LEU   B 2 6   ? 7.628  -9.373  13.074 1.00 18.50 ?  630 LEU   C CB   1 
ATOM   2052 C  CG   . LEU   B 2 6   ? 9.130  -9.589  12.880 1.00 22.06 ?  630 LEU   C CG   1 
ATOM   2053 C  CD1  . LEU   B 2 6   ? 9.842  -8.308  12.506 1.00 20.22 ?  630 LEU   C CD1  1 
ATOM   2054 C  CD2  . LEU   B 2 6   ? 9.736  -10.176 14.143 1.00 23.79 ?  630 LEU   C CD2  1 
ATOM   2055 N  N    . MET   B 2 7   ? 6.560  -10.378 10.281 1.00 23.52 ?  631 MET   C N    1 
ATOM   2056 C  CA   . MET   B 2 7   ? 6.693  -10.909 8.927  1.00 31.61 ?  631 MET   C CA   1 
ATOM   2057 C  C    . MET   B 2 7   ? 6.194  -9.908  7.893  1.00 31.99 ?  631 MET   C C    1 
ATOM   2058 O  O    . MET   B 2 7   ? 6.832  -9.704  6.854  1.00 31.37 ?  631 MET   C O    1 
ATOM   2059 C  CB   . MET   B 2 7   ? 5.920  -12.224 8.801  1.00 39.32 ?  631 MET   C CB   1 
ATOM   2060 C  CG   . MET   B 2 7   ? 6.751  -13.470 9.035  1.00 44.72 ?  631 MET   C CG   1 
ATOM   2061 S  SD   . MET   B 2 7   ? 8.109  -13.633 7.854  1.00 45.90 ?  631 MET   C SD   1 
ATOM   2062 C  CE   . MET   B 2 7   ? 7.576  -15.068 6.923  1.00 46.62 ?  631 MET   C CE   1 
ATOM   2063 N  N    . ASN   B 2 8   ? 5.057  -9.266  8.170  1.00 29.53 ?  632 ASN   C N    1 
ATOM   2064 C  CA   . ASN   B 2 8   ? 4.517  -8.273  7.248  1.00 27.80 ?  632 ASN   C CA   1 
ATOM   2065 C  C    . ASN   B 2 8   ? 5.473  -7.101  7.071  1.00 24.79 ?  632 ASN   C C    1 
ATOM   2066 O  O    . ASN   B 2 8   ? 5.684  -6.627  5.949  1.00 22.43 ?  632 ASN   C O    1 
ATOM   2067 C  CB   . ASN   B 2 8   ? 3.157  -7.784  7.752  1.00 28.55 ?  632 ASN   C CB   1 
ATOM   2068 C  CG   . ASN   B 2 8   ? 2.443  -6.903  6.744  1.00 28.69 ?  632 ASN   C CG   1 
ATOM   2069 O  OD1  . ASN   B 2 8   ? 2.522  -5.674  6.808  1.00 28.21 ?  632 ASN   C OD1  1 
ATOM   2070 N  ND2  . ASN   B 2 8   ? 1.745  -7.529  5.805  1.00 27.29 ?  632 ASN   C ND2  1 
ATOM   2071 N  N    . LEU   B 2 9   ? 6.053  -6.610  8.171  1.00 23.01 ?  633 LEU   C N    1 
ATOM   2072 C  CA   . LEU   B 2 9   ? 7.006  -5.509  8.071  1.00 20.48 ?  633 LEU   C CA   1 
ATOM   2073 C  C    . LEU   B 2 9   ? 8.288  -5.938  7.366  1.00 20.25 ?  633 LEU   C C    1 
ATOM   2074 O  O    . LEU   B 2 9   ? 8.972  -5.103  6.761  1.00 17.05 ?  633 LEU   C O    1 
ATOM   2075 C  CB   . LEU   B 2 9   ? 7.313  -4.953  9.463  1.00 15.93 ?  633 LEU   C CB   1 
ATOM   2076 C  CG   . LEU   B 2 9   ? 6.150  -4.158  10.067 1.00 18.97 ?  633 LEU   C CG   1 
ATOM   2077 C  CD1  . LEU   B 2 9   ? 6.362  -3.905  11.554 1.00 19.81 ?  633 LEU   C CD1  1 
ATOM   2078 C  CD2  . LEU   B 2 9   ? 5.937  -2.851  9.313  1.00 16.25 ?  633 LEU   C CD2  1 
ATOM   2079 N  N    . LEU   B 2 10  ? 8.638  -7.221  7.442  1.00 20.66 ?  634 LEU   C N    1 
ATOM   2080 C  CA   . LEU   B 2 10  ? 9.713  -7.748  6.614  1.00 30.02 ?  634 LEU   C CA   1 
ATOM   2081 C  C    . LEU   B 2 10  ? 9.271  -7.992  5.178  1.00 41.63 ?  634 LEU   C C    1 
ATOM   2082 O  O    . LEU   B 2 10  ? 10.131 -8.157  4.306  1.00 45.40 ?  634 LEU   C O    1 
ATOM   2083 C  CB   . LEU   B 2 10  ? 10.253 -9.049  7.212  1.00 22.07 ?  634 LEU   C CB   1 
ATOM   2084 C  CG   . LEU   B 2 10  ? 11.168 -8.889  8.428  1.00 24.12 ?  634 LEU   C CG   1 
ATOM   2085 C  CD1  . LEU   B 2 10  ? 11.334 -10.212 9.141  1.00 19.04 ?  634 LEU   C CD1  1 
ATOM   2086 C  CD2  . LEU   B 2 10  ? 12.523 -8.320  8.025  1.00 22.83 ?  634 LEU   C CD2  1 
ATOM   2087 N  N    . LYS   B 2 11  ? 7.963  -8.001  4.923  1.00 48.45 ?  635 LYS   C N    1 
ATOM   2088 C  CA   . LYS   B 2 11  ? 7.386  -8.336  3.622  1.00 53.56 ?  635 LYS   C CA   1 
ATOM   2089 C  C    . LYS   B 2 11  ? 7.881  -9.698  3.153  1.00 55.75 ?  635 LYS   C C    1 
ATOM   2090 O  O    . LYS   B 2 11  ? 8.019  -10.623 3.956  1.00 55.02 ?  635 LYS   C O    1 
ATOM   2091 C  CB   . LYS   B 2 11  ? 7.705  -7.255  2.587  1.00 55.04 ?  635 LYS   C CB   1 
ATOM   2092 C  CG   . LYS   B 2 11  ? 7.006  -5.927  2.852  1.00 57.05 ?  635 LYS   C CG   1 
ATOM   2093 C  CD   . LYS   B 2 11  ? 7.600  -4.819  2.004  1.00 60.15 ?  635 LYS   C CD   1 
ATOM   2094 C  CE   . LYS   B 2 11  ? 8.653  -4.046  2.775  1.00 60.63 ?  635 LYS   C CE   1 
ATOM   2095 N  NZ   . LYS   B 2 11  ? 9.942  -3.958  2.026  1.00 61.76 ?  635 LYS   C NZ   1 
HETATM 2096 C  C10  . A1L73 C 3 .   ? 10.907 2.666   27.064 1.00 15.80 ?  501 A1L73 A C10  1 
HETATM 2097 C  C13  . A1L73 C 3 .   ? 13.414 2.430   25.954 1.00 14.70 ?  501 A1L73 A C13  1 
HETATM 2098 C  C15  . A1L73 C 3 .   ? 13.064 6.703   26.518 1.00 26.27 ?  501 A1L73 A C15  1 
HETATM 2099 C  C20  . A1L73 C 3 .   ? 14.452 7.624   16.707 1.00 45.01 ?  501 A1L73 A C20  1 
HETATM 2100 C  C21  . A1L73 C 3 .   ? 13.812 8.790   15.985 1.00 40.75 ?  501 A1L73 A C21  1 
HETATM 2101 C  C22  . A1L73 C 3 .   ? 13.329 8.320   14.641 1.00 32.12 ?  501 A1L73 A C22  1 
HETATM 2102 C  C24  . A1L73 C 3 .   ? 8.819  -1.021  27.985 1.00 16.23 ?  501 A1L73 A C24  1 
HETATM 2103 C  C26  . A1L73 C 3 .   ? 8.385  -1.506  26.566 1.00 16.09 ?  501 A1L73 A C26  1 
HETATM 2104 C  C28  . A1L73 C 3 .   ? 7.372  -0.585  25.864 1.00 16.18 ?  501 A1L73 A C28  1 
HETATM 2105 C  C01  . A1L73 C 3 .   ? 13.377 5.749   21.515 1.00 30.32 ?  501 A1L73 A C01  1 
HETATM 2106 C  C02  . A1L73 C 3 .   ? 14.036 6.967   21.403 1.00 34.98 ?  501 A1L73 A C02  1 
HETATM 2107 C  C03  . A1L73 C 3 .   ? 14.571 7.586   22.506 1.00 32.17 ?  501 A1L73 A C03  1 
HETATM 2108 C  C04  . A1L73 C 3 .   ? 14.483 7.006   23.718 1.00 32.02 ?  501 A1L73 A C04  1 
HETATM 2109 C  C05  . A1L73 C 3 .   ? 13.868 5.819   23.865 1.00 27.88 ?  501 A1L73 A C05  1 
HETATM 2110 C  C06  . A1L73 C 3 .   ? 13.295 5.170   22.773 1.00 28.21 ?  501 A1L73 A C06  1 
HETATM 2111 C  C08  . A1L73 C 3 .   ? 12.888 3.670   26.147 1.00 18.24 ?  501 A1L73 A C08  1 
HETATM 2112 C  C09  . A1L73 C 3 .   ? 11.641 3.781   26.706 1.00 16.16 ?  501 A1L73 A C09  1 
HETATM 2113 C  C11  . A1L73 C 3 .   ? 11.437 1.416   26.854 1.00 18.30 ?  501 A1L73 A C11  1 
HETATM 2114 C  C12  . A1L73 C 3 .   ? 12.702 1.295   26.289 1.00 15.91 ?  501 A1L73 A C12  1 
HETATM 2115 C  C14  . A1L73 C 3 .   ? 15.655 5.072   26.299 1.00 25.78 ?  501 A1L73 A C14  1 
HETATM 2116 C  C18  . A1L73 C 3 .   ? 13.967 7.175   19.053 1.00 44.04 ?  501 A1L73 A C18  1 
HETATM 2117 C  C19  . A1L73 C 3 .   ? 14.789 8.010   18.097 1.00 45.99 ?  501 A1L73 A C19  1 
HETATM 2118 C  C23  . A1L73 C 3 .   ? 9.532  0.360   27.911 1.00 17.83 ?  501 A1L73 A C23  1 
HETATM 2119 C  C25  . A1L73 C 3 .   ? 7.601  -0.921  28.940 1.00 16.12 ?  501 A1L73 A C25  1 
HETATM 2120 C  C27  . A1L73 C 3 .   ? 6.937  -2.277  29.148 1.00 16.12 ?  501 A1L73 A C27  1 
HETATM 2121 C  C33  . A1L73 C 3 .   ? 12.607 3.858   23.016 1.00 25.20 ?  501 A1L73 A C33  1 
HETATM 2122 C  C34  . A1L73 C 3 .   ? 14.783 2.300   25.332 1.00 20.70 ?  501 A1L73 A C34  1 
HETATM 2123 O  O16  . A1L73 C 3 .   ? 10.731 0.243   27.204 1.00 18.50 ?  501 A1L73 A O16  1 
HETATM 2124 O  O17  . A1L73 C 3 .   ? 14.250 7.733   20.262 1.00 38.74 ?  501 A1L73 A O17  1 
HETATM 2125 O  O29  . A1L73 C 3 .   ? 9.712  -1.885  28.490 1.00 16.41 ?  501 A1L73 A O29  1 
HETATM 2126 O  O30  . A1L73 C 3 .   ? 13.561 7.214   14.277 1.00 29.90 ?  501 A1L73 A O30  1 
HETATM 2127 O  O31  . A1L73 C 3 .   ? 12.676 9.035   13.928 1.00 32.68 -1 501 A1L73 A O31  1 
HETATM 2128 O  O32  . A1L73 C 3 .   ? 16.046 7.581   18.208 1.00 49.85 ?  501 A1L73 A O32  1 
HETATM 2129 SI SI07 . A1L73 C 3 .   ? 13.878 5.247   25.683 1.00 27.43 ?  501 A1L73 A SI07 1 
HETATM 2130 O  O    . HOH   D 4 .   ? 39.359 -1.357  -3.989 1.00 42.63 ?  601 HOH   A O    1 
HETATM 2131 O  O    . HOH   D 4 .   ? 11.412 -12.291 4.663  1.00 44.53 ?  602 HOH   A O    1 
HETATM 2132 O  O    . HOH   D 4 .   ? 33.877 -21.253 12.124 1.00 59.90 ?  603 HOH   A O    1 
HETATM 2133 O  O    . HOH   D 4 .   ? 26.061 -11.143 2.177  1.00 54.05 ?  604 HOH   A O    1 
HETATM 2134 O  O    . HOH   D 4 .   ? 10.910 15.171  31.421 1.00 44.68 ?  605 HOH   A O    1 
HETATM 2135 O  O    . HOH   D 4 .   ? 20.522 -10.033 16.738 1.00 30.28 ?  606 HOH   A O    1 
HETATM 2136 O  O    . HOH   D 4 .   ? 20.445 -20.055 5.665  1.00 27.40 ?  607 HOH   A O    1 
HETATM 2137 O  O    . HOH   D 4 .   ? 19.363 -18.157 7.453  1.00 33.35 ?  608 HOH   A O    1 
HETATM 2138 O  O    . HOH   D 4 .   ? 19.898 -8.670  34.756 1.00 50.28 ?  609 HOH   A O    1 
HETATM 2139 O  O    . HOH   D 4 .   ? 4.993  -9.391  25.116 1.00 31.12 ?  610 HOH   A O    1 
HETATM 2140 O  O    A HOH   D 4 .   ? 25.048 -6.785  21.210 0.55 12.11 ?  611 HOH   A O    1 
HETATM 2141 O  O    B HOH   D 4 .   ? 26.003 -8.001  19.702 0.45 12.64 ?  611 HOH   A O    1 
HETATM 2142 O  O    . HOH   D 4 .   ? 13.793 -7.133  26.189 1.00 40.99 ?  612 HOH   A O    1 
HETATM 2143 O  O    . HOH   D 4 .   ? 17.581 11.795  33.560 1.00 33.71 ?  613 HOH   A O    1 
HETATM 2144 O  O    A HOH   D 4 .   ? 29.340 8.020   19.911 0.51 17.34 ?  614 HOH   A O    1 
HETATM 2145 O  O    B HOH   D 4 .   ? 28.479 9.637   19.833 0.49 18.74 ?  614 HOH   A O    1 
HETATM 2146 O  O    . HOH   D 4 .   ? 24.539 7.006   1.610  1.00 31.38 ?  615 HOH   A O    1 
HETATM 2147 O  O    . HOH   D 4 .   ? 1.580  8.430   28.427 1.00 27.52 ?  616 HOH   A O    1 
HETATM 2148 O  O    . HOH   D 4 .   ? 3.565  0.371   15.918 1.00 39.43 ?  617 HOH   A O    1 
HETATM 2149 O  O    . HOH   D 4 .   ? -2.832 0.074   23.839 1.00 42.37 ?  618 HOH   A O    1 
HETATM 2150 O  O    . HOH   D 4 .   ? -5.768 -2.041  25.033 1.00 15.93 ?  619 HOH   A O    1 
HETATM 2151 O  O    . HOH   D 4 .   ? 18.213 3.779   11.743 1.00 19.65 ?  620 HOH   A O    1 
HETATM 2152 O  O    . HOH   D 4 .   ? 14.578 4.456   18.275 1.00 21.02 ?  621 HOH   A O    1 
HETATM 2153 O  O    A HOH   D 4 .   ? 2.372  12.248  21.433 0.51 18.82 ?  622 HOH   A O    1 
HETATM 2154 O  O    B HOH   D 4 .   ? 1.773  14.130  21.879 0.49 21.20 ?  622 HOH   A O    1 
HETATM 2155 O  O    A HOH   D 4 .   ? 21.012 -6.543  38.332 0.51 32.59 ?  623 HOH   A O    1 
HETATM 2156 O  O    B HOH   D 4 .   ? 21.796 -4.955  38.023 0.49 32.82 ?  623 HOH   A O    1 
HETATM 2157 O  O    . HOH   D 4 .   ? -0.986 2.690   20.175 1.00 22.85 ?  624 HOH   A O    1 
HETATM 2158 O  O    . HOH   D 4 .   ? 30.701 9.230   4.268  1.00 32.91 ?  625 HOH   A O    1 
HETATM 2159 O  O    . HOH   D 4 .   ? 20.761 6.971   15.721 1.00 19.95 ?  626 HOH   A O    1 
HETATM 2160 O  O    . HOH   D 4 .   ? 14.675 -6.889  21.487 1.00 16.13 ?  627 HOH   A O    1 
HETATM 2161 O  O    . HOH   D 4 .   ? 32.948 0.703   26.054 1.00 39.42 ?  628 HOH   A O    1 
HETATM 2162 O  O    . HOH   D 4 .   ? 20.671 19.182  23.573 1.00 52.40 ?  629 HOH   A O    1 
HETATM 2163 O  O    . HOH   D 4 .   ? 36.513 -10.151 11.132 1.00 42.10 ?  630 HOH   A O    1 
HETATM 2164 O  O    . HOH   D 4 .   ? 14.817 -8.626  24.107 1.00 30.23 ?  631 HOH   A O    1 
HETATM 2165 O  O    A HOH   D 4 .   ? 24.854 -15.604 23.429 0.57 17.65 ?  632 HOH   A O    1 
HETATM 2166 O  O    B HOH   D 4 .   ? 22.707 -14.824 23.564 0.43 31.94 ?  632 HOH   A O    1 
HETATM 2167 O  O    . HOH   D 4 .   ? 20.583 -3.338  0.916  1.00 45.37 ?  633 HOH   A O    1 
HETATM 2168 O  O    . HOH   D 4 .   ? 0.632  -11.362 16.506 1.00 26.98 ?  634 HOH   A O    1 
HETATM 2169 O  O    . HOH   D 4 .   ? 32.280 -10.377 12.974 1.00 35.49 ?  635 HOH   A O    1 
HETATM 2170 O  O    . HOH   D 4 .   ? 21.630 -8.144  33.080 1.00 31.81 ?  636 HOH   A O    1 
HETATM 2171 O  O    A HOH   D 4 .   ? 14.761 -21.253 15.411 0.51 29.89 ?  637 HOH   A O    1 
HETATM 2172 O  O    B HOH   D 4 .   ? 14.521 -21.636 17.223 0.49 31.06 ?  637 HOH   A O    1 
HETATM 2173 O  O    . HOH   D 4 .   ? 12.117 8.035   9.333  1.00 34.55 ?  638 HOH   A O    1 
HETATM 2174 O  O    . HOH   D 4 .   ? 18.454 1.772   13.348 1.00 22.04 ?  639 HOH   A O    1 
HETATM 2175 O  O    . HOH   D 4 .   ? 14.126 20.765  23.809 1.00 45.94 ?  640 HOH   A O    1 
HETATM 2176 O  O    . HOH   D 4 .   ? 9.555  11.490  13.418 1.00 46.18 ?  641 HOH   A O    1 
HETATM 2177 O  O    . HOH   D 4 .   ? 0.304  -9.177  19.190 1.00 38.68 ?  642 HOH   A O    1 
HETATM 2178 O  O    . HOH   D 4 .   ? 3.666  16.284  29.732 1.00 43.21 ?  643 HOH   A O    1 
HETATM 2179 O  O    A HOH   D 4 .   ? 3.357  13.962  12.035 0.56 24.94 ?  644 HOH   A O    1 
HETATM 2180 O  O    B HOH   D 4 .   ? 1.694  13.395  11.202 0.44 25.36 ?  644 HOH   A O    1 
HETATM 2181 O  O    . HOH   D 4 .   ? 26.206 0.053   31.025 1.00 26.12 ?  645 HOH   A O    1 
HETATM 2182 O  O    . HOH   D 4 .   ? 41.188 -3.936  19.051 1.00 44.26 ?  646 HOH   A O    1 
HETATM 2183 O  O    . HOH   D 4 .   ? -1.815 9.307   27.210 1.00 54.19 ?  647 HOH   A O    1 
HETATM 2184 O  O    . HOH   D 4 .   ? 29.610 12.123  11.794 1.00 31.80 ?  648 HOH   A O    1 
HETATM 2185 O  O    . HOH   D 4 .   ? 12.664 -18.577 4.333  1.00 30.86 ?  649 HOH   A O    1 
HETATM 2186 O  O    . HOH   D 4 .   ? 32.264 2.420   -3.834 1.00 51.11 ?  650 HOH   A O    1 
HETATM 2187 O  O    . HOH   D 4 .   ? 20.490 -21.308 20.017 1.00 45.29 ?  651 HOH   A O    1 
HETATM 2188 O  O    . HOH   D 4 .   ? 34.336 -14.274 13.520 1.00 52.92 ?  652 HOH   A O    1 
HETATM 2189 O  O    . HOH   D 4 .   ? 6.278  21.015  23.773 1.00 46.57 ?  653 HOH   A O    1 
HETATM 2190 O  O    . HOH   D 4 .   ? 25.493 -13.576 1.915  1.00 50.32 ?  654 HOH   A O    1 
HETATM 2191 O  O    A HOH   D 4 .   ? 28.390 -10.843 18.174 0.46 21.43 ?  655 HOH   A O    1 
HETATM 2192 O  O    B HOH   D 4 .   ? 29.891 -12.354 17.827 0.54 25.86 ?  655 HOH   A O    1 
HETATM 2193 O  O    A HOH   D 4 .   ? 23.482 -9.322  -0.745 0.46 33.60 ?  656 HOH   A O    1 
HETATM 2194 O  O    B HOH   D 4 .   ? 25.579 -8.688  -0.273 0.54 26.93 ?  656 HOH   A O    1 
HETATM 2195 O  O    . HOH   D 4 .   ? 18.781 -4.192  -2.587 1.00 48.66 ?  657 HOH   A O    1 
HETATM 2196 O  O    . HOH   D 4 .   ? -0.712 0.921   34.098 1.00 45.50 ?  658 HOH   A O    1 
HETATM 2197 O  O    A HOH   D 4 .   ? 26.959 7.361   18.725 0.59 29.17 ?  659 HOH   A O    1 
HETATM 2198 O  O    B HOH   D 4 .   ? 25.838 8.806   18.383 0.41 29.97 ?  659 HOH   A O    1 
HETATM 2199 O  O    . HOH   D 4 .   ? -6.615 -5.137  31.577 1.00 30.31 ?  660 HOH   A O    1 
HETATM 2200 O  O    A HOH   D 4 .   ? 3.494  8.777   12.669 0.44 16.06 ?  661 HOH   A O    1 
HETATM 2201 O  O    B HOH   D 4 .   ? 3.406  6.988   13.647 0.56 17.12 ?  661 HOH   A O    1 
HETATM 2202 O  O    . HOH   D 4 .   ? 11.947 -8.807  25.897 1.00 30.29 ?  662 HOH   A O    1 
HETATM 2203 O  O    A HOH   D 4 .   ? 7.586  3.868   9.714  0.53 18.32 ?  663 HOH   A O    1 
HETATM 2204 O  O    B HOH   D 4 .   ? 6.565  4.945   10.581 0.47 19.27 ?  663 HOH   A O    1 
HETATM 2205 O  O    . HOH   D 4 .   ? 25.904 -2.298  31.191 1.00 44.02 ?  664 HOH   A O    1 
HETATM 2206 O  O    . HOH   D 4 .   ? 26.554 -7.053  33.444 1.00 48.89 ?  665 HOH   A O    1 
HETATM 2207 O  O    . HOH   D 4 .   ? 20.235 11.198  10.372 1.00 35.84 ?  666 HOH   A O    1 
HETATM 2208 O  O    . HOH   D 4 .   ? 13.407 9.642   8.311  1.00 40.92 ?  667 HOH   A O    1 
HETATM 2209 O  O    . HOH   D 4 .   ? 9.153  2.885   39.122 1.00 53.77 ?  668 HOH   A O    1 
HETATM 2210 O  O    A HOH   D 4 .   ? 40.981 -6.266  14.325 0.51 34.19 ?  669 HOH   A O    1 
HETATM 2211 O  O    B HOH   D 4 .   ? 41.427 -4.984  15.815 0.49 34.24 ?  669 HOH   A O    1 
HETATM 2212 O  O    . HOH   D 4 .   ? 29.275 -19.235 14.760 1.00 41.83 ?  670 HOH   A O    1 
HETATM 2213 O  O    . HOH   D 4 .   ? 1.250  11.915  9.401  1.00 54.58 ?  671 HOH   A O    1 
HETATM 2214 O  O    . HOH   D 4 .   ? 6.716  6.345   8.706  1.00 44.46 ?  672 HOH   A O    1 
HETATM 2215 O  O    . HOH   D 4 .   ? -2.275 -10.471 15.856 1.00 35.06 ?  673 HOH   A O    1 
HETATM 2216 O  O    . HOH   E 4 .   ? 1.839  -10.000 5.531  1.00 36.61 ?  701 HOH   C O    1 
HETATM 2217 O  O    . HOH   E 4 .   ? 2.035  -11.468 7.831  1.00 40.87 ?  702 HOH   C O    1 
HETATM 2218 O  O    A HOH   E 4 .   ? 8.932  -18.334 17.963 0.52 21.65 ?  703 HOH   C O    1 
HETATM 2219 O  O    B HOH   E 4 .   ? 7.989  -17.795 19.766 0.48 21.28 ?  703 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  ? 0.5482 0.9859 0.5407 -0.1090 0.0224  -0.0627 123 LYS   A N    
2    C  CA   . LYS   A 18  ? 0.5023 0.9436 0.4984 -0.0953 0.0172  -0.0704 123 LYS   A CA   
3    C  C    . LYS   A 18  ? 0.4145 0.8341 0.4129 -0.0858 0.0157  -0.0698 123 LYS   A C    
4    O  O    . LYS   A 18  ? 0.4172 0.8415 0.4195 -0.0699 0.0123  -0.0763 123 LYS   A O    
5    C  CB   . LYS   A 18  ? 0.4997 0.9364 0.4936 -0.1019 0.0178  -0.0719 123 LYS   A CB   
6    C  CG   . LYS   A 18  ? 0.5094 0.9581 0.4994 -0.1175 0.0209  -0.0710 123 LYS   A CG   
7    C  CD   . LYS   A 18  ? 0.5443 0.9933 0.5323 -0.1215 0.0208  -0.0742 123 LYS   A CD   
8    C  CE   . LYS   A 18  ? 0.5969 1.0683 0.5818 -0.1334 0.0227  -0.0764 123 LYS   A CE   
9    N  NZ   . LYS   A 18  ? 0.6388 1.0914 0.6191 -0.1530 0.0284  -0.0722 123 LYS   A NZ   
10   N  N    . LEU   A 19  ? 0.3854 0.7792 0.3808 -0.0949 0.0196  -0.0619 124 LEU   A N    
11   C  CA   . LEU   A 19  ? 0.3482 0.7243 0.3452 -0.0867 0.0187  -0.0604 124 LEU   A CA   
12   C  C    . LEU   A 19  ? 0.3401 0.7315 0.3386 -0.0771 0.0174  -0.0615 124 LEU   A C    
13   O  O    . LEU   A 19  ? 0.2981 0.6912 0.2918 -0.0834 0.0217  -0.0543 124 LEU   A O    
14   C  CB   . LEU   A 19  ? 0.3418 0.6862 0.3329 -0.0980 0.0244  -0.0508 124 LEU   A CB   
15   C  CG   . LEU   A 19  ? 0.3379 0.6584 0.3285 -0.1035 0.0247  -0.0506 124 LEU   A CG   
16   C  CD1  . LEU   A 19  ? 0.3744 0.6628 0.3582 -0.1116 0.0309  -0.0410 124 LEU   A CD1  
17   C  CD2  . LEU   A 19  ? 0.2289 0.5498 0.2268 -0.0902 0.0187  -0.0568 124 LEU   A CD2  
18   N  N    . SER   A 20  ? 0.3258 0.7267 0.3300 -0.0614 0.0120  -0.0707 125 SER   A N    
19   C  CA   . SER   A 20  ? 0.2535 0.6690 0.2604 -0.0516 0.0098  -0.0741 125 SER   A CA   
20   C  C    . SER   A 20  ? 0.3021 0.6991 0.3040 -0.0529 0.0132  -0.0660 125 SER   A C    
21   O  O    . SER   A 20  ? 0.3062 0.6774 0.3025 -0.0598 0.0167  -0.0586 125 SER   A O    
22   C  CB   . SER   A 20  ? 0.2269 0.6423 0.2412 -0.0332 0.0061  -0.0853 125 SER   A CB   
23   O  OG   . SER   A 20  ? 0.2532 0.6446 0.2690 -0.0270 0.0056  -0.0867 125 SER   A OG   
24   N  N    . GLU   A 21  ? 0.2571 0.6676 0.2593 -0.0457 0.0122  -0.0675 126 GLU   A N    
25   C  CA   . GLU   A 21  ? 0.2563 0.6525 0.2512 -0.0441 0.0143  -0.0605 126 GLU   A CA   
26   C  C    . GLU   A 21  ? 0.1970 0.5706 0.1932 -0.0370 0.0117  -0.0642 126 GLU   A C    
27   O  O    . GLU   A 21  ? 0.2066 0.5578 0.1934 -0.0406 0.0143  -0.0553 126 GLU   A O    
28   C  CB   . GLU   A 21  ? 0.3141 0.7341 0.3110 -0.0361 0.0122  -0.0643 126 GLU   A CB   
29   C  CG   . GLU   A 21  ? 0.4131 0.8460 0.4228 -0.0214 0.0060  -0.0804 126 GLU   A CG   
30   C  CD   . GLU   A 21  ? 0.5135 0.9562 0.5313 -0.0178 0.0034  -0.0899 126 GLU   A CD   
31   O  OE1  . GLU   A 21  ? 0.5798 1.0436 0.5965 -0.0216 0.0039  -0.0898 126 GLU   A OE1  
32   O  OE2  . GLU   A 21  ? 0.4493 0.8739 0.4719 -0.0105 0.0018  -0.0962 126 GLU   A OE2  
33   N  N    . GLU   A 22  ? 0.2176 0.5954 0.2251 -0.0262 0.0068  -0.0769 127 GLU   A N    
34   C  CA   . GLU   A 22  ? 0.2518 0.6041 0.2602 -0.0189 0.0035  -0.0810 127 GLU   A CA   
35   C  C    . GLU   A 22  ? 0.2225 0.5505 0.2250 -0.0280 0.0037  -0.0743 127 GLU   A C    
36   O  O    . GLU   A 22  ? 0.1991 0.5006 0.1973 -0.0277 0.0013  -0.0704 127 GLU   A O    
37   C  CB   . GLU   A 22  ? 0.3385 0.6955 0.3596 -0.0051 -0.0003 -0.0949 127 GLU   A CB   
38   C  CG   . GLU   A 22  ? 0.4880 0.8140 0.5117 0.0012  -0.0060 -0.0984 127 GLU   A CG   
39   C  CD   . GLU   A 22  ? 0.6222 0.9516 0.6569 0.0153  -0.0098 -0.1127 127 GLU   A CD   
40   O  OE1  . GLU   A 22  ? 0.6740 0.9978 0.7148 0.0194  -0.0128 -0.1156 127 GLU   A OE1  
41   O  OE2  . GLU   A 22  ? 0.6693 1.0080 0.7074 0.0221  -0.0103 -0.1208 127 GLU   A OE2  
42   N  N    . GLN   A 23  ? 0.1764 0.5138 0.1805 -0.0366 0.0063  -0.0726 128 GLN   A N    
43   C  CA   . GLN   A 23  ? 0.2146 0.5277 0.2182 -0.0454 0.0067  -0.0662 128 GLN   A CA   
44   C  C    . GLN   A 23  ? 0.2134 0.5057 0.2056 -0.0570 0.0134  -0.0536 128 GLN   A C    
45   O  O    . GLN   A 23  ? 0.2071 0.4698 0.1971 -0.0588 0.0124  -0.0489 128 GLN   A O    
46   C  CB   . GLN   A 23  ? 0.1627 0.4953 0.1725 -0.0518 0.0079  -0.0687 128 GLN   A CB   
47   C  CG   . GLN   A 23  ? 0.1641 0.4976 0.1831 -0.0372 0.0032  -0.0766 128 GLN   A CG   
48   C  CD   . GLN   A 23  ? 0.2409 0.5945 0.2606 -0.0394 0.0056  -0.0785 128 GLN   A CD   
49   O  OE1  . GLN   A 23  ? 0.3001 0.6677 0.3121 -0.0515 0.0098  -0.0754 128 GLN   A OE1  
50   N  NE2  . GLN   A 23  ? 0.2489 0.6031 0.2766 -0.0279 0.0014  -0.0833 128 GLN   A NE2  
51   N  N    . GLN   A 24  ? 0.2319 0.5393 0.2173 -0.0644 0.0206  -0.0474 129 GLN   A N    
52   C  CA   . GLN   A 24  ? 0.2521 0.5383 0.2269 -0.0733 0.0277  -0.0339 129 GLN   A CA   
53   C  C    . GLN   A 24  ? 0.2261 0.4937 0.1967 -0.0634 0.0243  -0.0308 129 GLN   A C    
54   O  O    . GLN   A 24  ? 0.2330 0.4722 0.1984 -0.0669 0.0269  -0.0218 129 GLN   A O    
55   C  CB   . GLN   A 24  ? 0.2701 0.5685 0.2411 -0.0790 0.0320  -0.0265 129 GLN   A CB   
56   C  CG   . GLN   A 24  ? 0.3231 0.6365 0.2986 -0.0880 0.0327  -0.0297 129 GLN   A CG   
57   C  CD   . GLN   A 24  ? 0.4297 0.7587 0.4016 -0.0921 0.0364  -0.0237 129 GLN   A CD   
58   O  OE1  . GLN   A 24  ? 0.4513 0.7727 0.4160 -0.0915 0.0405  -0.0134 129 GLN   A OE1  
59   N  NE2  . GLN   A 24  ? 0.4728 0.8248 0.4495 -0.0958 0.0348  -0.0295 129 GLN   A NE2  
60   N  N    . HIS   A 25  ? 0.1990 0.4836 0.1723 -0.0510 0.0186  -0.0391 130 HIS   A N    
61   C  CA   . HIS   A 25  ? 0.2445 0.5173 0.2146 -0.0420 0.0148  -0.0380 130 HIS   A CA   
62   C  C    . HIS   A 25  ? 0.2540 0.4972 0.2289 -0.0391 0.0094  -0.0403 130 HIS   A C    
63   O  O    . HIS   A 25  ? 0.2270 0.4486 0.1971 -0.0388 0.0101  -0.0325 130 HIS   A O    
64   C  CB   . HIS   A 25  ? 0.2099 0.5103 0.1832 -0.0308 0.0100  -0.0499 130 HIS   A CB   
65   C  CG   . HIS   A 25  ? 0.2976 0.5913 0.2696 -0.0219 0.0051  -0.0523 130 HIS   A CG   
66   N  ND1  . HIS   A 25  ? 0.3175 0.6065 0.2795 -0.0225 0.0082  -0.0404 130 HIS   A ND1  
67   C  CD2  . HIS   A 25  ? 0.3092 0.5998 0.2910 -0.0122 -0.0019 -0.0645 130 HIS   A CD2  
68   C  CE1  . HIS   A 25  ? 0.3051 0.5924 0.2696 -0.0141 0.0024  -0.0464 130 HIS   A CE1  
69   N  NE2  . HIS   A 25  ? 0.3022 0.5886 0.2794 -0.0085 -0.0034 -0.0612 130 HIS   A NE2  
70   N  N    . ILE   A 26  ? 0.2069 0.4502 0.1916 -0.0365 0.0043  -0.0500 131 ILE   A N    
71   C  CA   . ILE   A 26  ? 0.2075 0.4249 0.1970 -0.0344 -0.0005 -0.0514 131 ILE   A CA   
72   C  C    . ILE   A 26  ? 0.2212 0.4147 0.2050 -0.0449 0.0046  -0.0407 131 ILE   A C    
73   O  O    . ILE   A 26  ? 0.1975 0.3674 0.1797 -0.0436 0.0034  -0.0368 131 ILE   A O    
74   C  CB   . ILE   A 26  ? 0.2336 0.4587 0.2344 -0.0300 -0.0057 -0.0613 131 ILE   A CB   
75   C  CG1  . ILE   A 26  ? 0.2264 0.4662 0.2344 -0.0175 -0.0111 -0.0732 131 ILE   A CG1  
76   C  CG2  . ILE   A 26  ? 0.2086 0.4087 0.2130 -0.0313 -0.0089 -0.0593 131 ILE   A CG2  
77   C  CD1  . ILE   A 26  ? 0.2214 0.4734 0.2405 -0.0117 -0.0138 -0.0813 131 ILE   A CD1  
78   N  N    . ILE   A 27  ? 0.2146 0.4145 0.1957 -0.0558 0.0109  -0.0368 132 ILE   A N    
79   C  CA   . ILE   A 27  ? 0.2502 0.4271 0.2265 -0.0671 0.0167  -0.0289 132 ILE   A CA   
80   C  C    . ILE   A 27  ? 0.2736 0.4321 0.2410 -0.0675 0.0220  -0.0177 132 ILE   A C    
81   O  O    . ILE   A 27  ? 0.2496 0.3819 0.2148 -0.0689 0.0232  -0.0132 132 ILE   A O    
82   C  CB   . ILE   A 27  ? 0.2640 0.4544 0.2401 -0.0802 0.0228  -0.0287 132 ILE   A CB   
83   C  CG1  . ILE   A 27  ? 0.2299 0.4334 0.2152 -0.0799 0.0173  -0.0381 132 ILE   A CG1  
84   C  CG2  . ILE   A 27  ? 0.2582 0.4246 0.2277 -0.0933 0.0314  -0.0203 132 ILE   A CG2  
85   C  CD1  . ILE   A 27  ? 0.2410 0.4671 0.2280 -0.0916 0.0219  -0.0401 132 ILE   A CD1  
86   N  N    . ALA   A 28  ? 0.2579 0.4317 0.2201 -0.0652 0.0251  -0.0127 133 ALA   A N    
87   C  CA   . ALA   A 28  ? 0.2636 0.4233 0.2174 -0.0635 0.0299  -0.0003 133 ALA   A CA   
88   C  C    . ALA   A 28  ? 0.2405 0.3871 0.1956 -0.0527 0.0235  -0.0015 133 ALA   A C    
89   O  O    . ALA   A 28  ? 0.1927 0.3173 0.1433 -0.0522 0.0269  0.0078  133 ALA   A O    
90   C  CB   . ALA   A 28  ? 0.2814 0.4661 0.2296 -0.0615 0.0333  0.0051  133 ALA   A CB   
91   N  N    . ILE   A 29  ? 0.2316 0.3915 0.1935 -0.0441 0.0148  -0.0130 134 ILE   A N    
92   C  CA   . ILE   A 29  ? 0.2065 0.3560 0.1709 -0.0353 0.0086  -0.0155 134 ILE   A CA   
93   C  C    . ILE   A 29  ? 0.2418 0.3633 0.2088 -0.0386 0.0082  -0.0143 134 ILE   A C    
94   O  O    . ILE   A 29  ? 0.2571 0.3616 0.2215 -0.0359 0.0088  -0.0081 134 ILE   A O    
95   C  CB   . ILE   A 29  ? 0.2341 0.4020 0.2064 -0.0270 0.0003  -0.0296 134 ILE   A CB   
96   C  CG1  . ILE   A 29  ? 0.2796 0.4750 0.2479 -0.0220 0.0005  -0.0311 134 ILE   A CG1  
97   C  CG2  . ILE   A 29  ? 0.2409 0.3937 0.2187 -0.0211 -0.0061 -0.0341 134 ILE   A CG2  
98   C  CD1  . ILE   A 29  ? 0.2914 0.5055 0.2677 -0.0144 -0.0064 -0.0471 134 ILE   A CD1  
99   N  N    . LEU   A 30  ? 0.2511 0.3702 0.2232 -0.0440 0.0072  -0.0200 135 LEU   A N    
100  C  CA   . LEU   A 30  ? 0.2210 0.3176 0.1954 -0.0471 0.0063  -0.0199 135 LEU   A CA   
101  C  C    . LEU   A 30  ? 0.1880 0.2637 0.1551 -0.0549 0.0148  -0.0101 135 LEU   A C    
102  O  O    . LEU   A 30  ? 0.2620 0.3174 0.2287 -0.0542 0.0150  -0.0076 135 LEU   A O    
103  C  CB   . LEU   A 30  ? 0.1744 0.2781 0.1556 -0.0508 0.0033  -0.0276 135 LEU   A CB   
104  C  CG   . LEU   A 30  ? 0.1739 0.2912 0.1643 -0.0415 -0.0051 -0.0371 135 LEU   A CG   
105  C  CD1  . LEU   A 30  ? 0.2053 0.3329 0.2020 -0.0443 -0.0072 -0.0423 135 LEU   A CD1  
106  C  CD2  . LEU   A 30  ? 0.1323 0.2344 0.1265 -0.0346 -0.0106 -0.0383 135 LEU   A CD2  
107  N  N    A LEU   A 31  ? 0.1945 0.2742 0.1561 -0.0623 0.0225  -0.0045 136 LEU   A N    
108  N  N    B LEU   A 31  ? 0.1988 0.2786 0.1605 -0.0626 0.0225  -0.0047 136 LEU   A N    
109  C  CA   A LEU   A 31  ? 0.2256 0.2820 0.1808 -0.0695 0.0318  0.0049  136 LEU   A CA   
110  C  CA   B LEU   A 31  ? 0.2287 0.2859 0.1837 -0.0696 0.0320  0.0051  136 LEU   A CA   
111  C  C    A LEU   A 31  ? 0.2679 0.3124 0.2185 -0.0608 0.0335  0.0148  136 LEU   A C    
112  C  C    B LEU   A 31  ? 0.2615 0.3063 0.2124 -0.0605 0.0330  0.0142  136 LEU   A C    
113  O  O    A LEU   A 31  ? 0.2630 0.2831 0.2113 -0.0615 0.0378  0.0200  136 LEU   A O    
114  O  O    B LEU   A 31  ? 0.2551 0.2762 0.2044 -0.0606 0.0362  0.0184  136 LEU   A O    
115  C  CB   A LEU   A 31  ? 0.2406 0.3037 0.1918 -0.0803 0.0402  0.0091  136 LEU   A CB   
116  C  CB   B LEU   A 31  ? 0.2412 0.3063 0.1917 -0.0791 0.0404  0.0104  136 LEU   A CB   
117  C  CG   A LEU   A 31  ? 0.2365 0.3069 0.1918 -0.0918 0.0406  0.0004  136 LEU   A CG   
118  C  CG   B LEU   A 31  ? 0.2430 0.3249 0.1967 -0.0902 0.0417  0.0032  136 LEU   A CG   
119  C  CD1  A LEU   A 31  ? 0.2567 0.3468 0.2104 -0.1004 0.0461  0.0020  136 LEU   A CD1  
120  C  CD1  B LEU   A 31  ? 0.2625 0.3380 0.2108 -0.1033 0.0533  0.0110  136 LEU   A CD1  
121  C  CD2  A LEU   A 31  ? 0.2476 0.2918 0.2015 -0.1012 0.0461  0.0003  136 LEU   A CD2  
122  C  CD2  B LEU   A 31  ? 0.2413 0.3187 0.2007 -0.0945 0.0375  -0.0064 136 LEU   A CD2  
123  N  N    . ASP   A 32  ? 0.2768 0.3402 0.2260 -0.0521 0.0302  0.0171  137 ASP   A N    
124  C  CA   . ASP   A 32  ? 0.2858 0.3439 0.2313 -0.0427 0.0306  0.0263  137 ASP   A CA   
125  C  C    . ASP   A 32  ? 0.2619 0.3101 0.2124 -0.0362 0.0239  0.0212  137 ASP   A C    
126  O  O    . ASP   A 32  ? 0.2888 0.3206 0.2370 -0.0321 0.0267  0.0288  137 ASP   A O    
127  C  CB   . ASP   A 32  ? 0.3718 0.4583 0.3149 -0.0355 0.0278  0.0278  137 ASP   A CB   
128  C  CG   . ASP   A 32  ? 0.4245 0.5112 0.3629 -0.0258 0.0284  0.0385  137 ASP   A CG   
129  O  OD1  . ASP   A 32  ? 0.5068 0.6090 0.4483 -0.0175 0.0205  0.0325  137 ASP   A OD1  
130  O  OD2  . ASP   A 32  ? 0.4095 0.4815 0.3418 -0.0264 0.0369  0.0530  137 ASP   A OD2  
131  N  N    . ALA   A 33  ? 0.2282 0.2864 0.1860 -0.0349 0.0156  0.0088  138 ALA   A N    
132  C  CA   . ALA   A 33  ? 0.2356 0.2847 0.1991 -0.0303 0.0095  0.0040  138 ALA   A CA   
133  C  C    . ALA   A 33  ? 0.2481 0.2717 0.2108 -0.0355 0.0138  0.0070  138 ALA   A C    
134  O  O    . ALA   A 33  ? 0.2421 0.2542 0.2056 -0.0310 0.0131  0.0098  138 ALA   A O    
135  C  CB   . ALA   A 33  ? 0.2379 0.2991 0.2098 -0.0292 0.0012  -0.0087 138 ALA   A CB   
136  N  N    . HIS   A 34  ? 0.2257 0.2424 0.1870 -0.0453 0.0188  0.0059  139 HIS   A N    
137  C  CA   . HIS   A 34  ? 0.2513 0.2458 0.2116 -0.0515 0.0233  0.0063  139 HIS   A CA   
138  C  C    . HIS   A 34  ? 0.2775 0.2523 0.2315 -0.0509 0.0324  0.0169  139 HIS   A C    
139  O  O    . HIS   A 34  ? 0.2493 0.2061 0.2032 -0.0496 0.0346  0.0182  139 HIS   A O    
140  C  CB   . HIS   A 34  ? 0.2846 0.2815 0.2455 -0.0632 0.0258  0.0005  139 HIS   A CB   
141  C  CG   . HIS   A 34  ? 0.3458 0.3229 0.3052 -0.0711 0.0308  -0.0011 139 HIS   A CG   
142  N  ND1  . HIS   A 34  ? 0.3665 0.3347 0.3286 -0.0680 0.0273  -0.0038 139 HIS   A ND1  
143  C  CD2  . HIS   A 34  ? 0.3676 0.3335 0.3233 -0.0827 0.0395  -0.0013 139 HIS   A CD2  
144  C  CE1  . HIS   A 34  ? 0.3582 0.3117 0.3177 -0.0768 0.0334  -0.0061 139 HIS   A CE1  
145  N  NE2  . HIS   A 34  ? 0.3876 0.3386 0.3434 -0.0861 0.0409  -0.0053 139 HIS   A NE2  
146  N  N    . HIS   A 35  ? 0.2954 0.2731 0.2442 -0.0514 0.0384  0.0252  140 HIS   A N    
147  C  CA   . HIS   A 35  ? 0.3942 0.3519 0.3375 -0.0491 0.0476  0.0373  140 HIS   A CA   
148  C  C    . HIS   A 35  ? 0.3449 0.3041 0.2886 -0.0355 0.0442  0.0436  140 HIS   A C    
149  O  O    . HIS   A 35  ? 0.3517 0.2919 0.2927 -0.0312 0.0508  0.0525  140 HIS   A O    
150  C  CB   . HIS   A 35  ? 0.5746 0.5362 0.5123 -0.0530 0.0551  0.0465  140 HIS   A CB   
151  C  CG   . HIS   A 35  ? 0.7237 0.6741 0.6602 -0.0681 0.0629  0.0435  140 HIS   A CG   
152  N  ND1  . HIS   A 35  ? 0.7516 0.7207 0.6907 -0.0770 0.0597  0.0343  140 HIS   A ND1  
153  C  CD2  . HIS   A 35  ? 0.7831 0.7061 0.7166 -0.0762 0.0740  0.0477  140 HIS   A CD2  
154  C  CE1  . HIS   A 35  ? 0.7676 0.7240 0.7054 -0.0909 0.0682  0.0328  140 HIS   A CE1  
155  N  NE2  . HIS   A 35  ? 0.7813 0.7101 0.7173 -0.0894 0.0756  0.0397  140 HIS   A NE2  
156  N  N    A LYS   A 36  ? 0.3244 0.3062 0.2718 -0.0286 0.0343  0.0386  141 LYS   A N    
157  N  N    C LYS   A 36  ? 0.3239 0.3056 0.2714 -0.0286 0.0344  0.0386  141 LYS   A N    
158  C  CA   A LYS   A 36  ? 0.3300 0.3175 0.2789 -0.0171 0.0301  0.0424  141 LYS   A CA   
159  C  CA   C LYS   A 36  ? 0.3301 0.3174 0.2789 -0.0171 0.0302  0.0425  141 LYS   A CA   
160  C  C    A LYS   A 36  ? 0.3222 0.2993 0.2767 -0.0160 0.0261  0.0360  141 LYS   A C    
161  C  C    C LYS   A 36  ? 0.3223 0.2998 0.2769 -0.0160 0.0260  0.0359  141 LYS   A C    
162  O  O    A LYS   A 36  ? 0.3304 0.3094 0.2864 -0.0074 0.0241  0.0398  141 LYS   A O    
163  O  O    C LYS   A 36  ? 0.3307 0.3108 0.2870 -0.0074 0.0236  0.0394  141 LYS   A O    
164  C  CB   A LYS   A 36  ? 0.3266 0.3439 0.2774 -0.0116 0.0217  0.0380  141 LYS   A CB   
165  C  CB   C LYS   A 36  ? 0.3274 0.3446 0.2780 -0.0115 0.0220  0.0386  141 LYS   A CB   
166  C  CG   A LYS   A 36  ? 0.3477 0.3808 0.2920 -0.0075 0.0252  0.0483  141 LYS   A CG   
167  C  CG   C LYS   A 36  ? 0.3487 0.3806 0.2926 -0.0067 0.0258  0.0497  141 LYS   A CG   
168  C  CD   A LYS   A 36  ? 0.3554 0.4200 0.3019 -0.0035 0.0168  0.0403  141 LYS   A CD   
169  C  CD   C LYS   A 36  ? 0.3606 0.4222 0.3055 -0.0064 0.0194  0.0417  141 LYS   A CD   
170  C  CE   A LYS   A 36  ? 0.3886 0.4734 0.3279 0.0022  0.0198  0.0514  141 LYS   A CE   
171  C  CE   C LYS   A 36  ? 0.3898 0.4737 0.3286 0.0013  0.0206  0.0519  141 LYS   A CE   
172  N  NZ   A LYS   A 36  ? 0.4164 0.4898 0.3489 -0.0034 0.0300  0.0632  141 LYS   A NZ   
173  N  NZ   C LYS   A 36  ? 0.3843 0.4985 0.3265 0.0063  0.0112  0.0410  141 LYS   A NZ   
174  N  N    . THR   A 37  ? 0.2817 0.2505 0.2393 -0.0245 0.0250  0.0269  142 THR   A N    
175  C  CA   . THR   A 37  ? 0.2847 0.2468 0.2475 -0.0242 0.0209  0.0210  142 THR   A CA   
176  C  C    . THR   A 37  ? 0.3497 0.2900 0.3106 -0.0315 0.0276  0.0197  142 THR   A C    
177  O  O    . THR   A 37  ? 0.3600 0.2962 0.3245 -0.0327 0.0246  0.0145  142 THR   A O    
178  C  CB   . THR   A 37  ? 0.2555 0.2325 0.2250 -0.0261 0.0114  0.0106  142 THR   A CB   
179  O  OG1  . THR   A 37  ? 0.2882 0.2699 0.2569 -0.0338 0.0122  0.0061  142 THR   A OG1  
180  C  CG2  . THR   A 37  ? 0.1478 0.1446 0.1205 -0.0185 0.0046  0.0093  142 THR   A CG2  
181  N  N    . TYR   A 38  ? 0.3677 0.2944 0.3231 -0.0372 0.0369  0.0239  143 TYR   A N    
182  C  CA   . TYR   A 38  ? 0.3864 0.2919 0.3398 -0.0451 0.0444  0.0209  143 TYR   A CA   
183  C  C    . TYR   A 38  ? 0.4580 0.3423 0.4062 -0.0427 0.0557  0.0308  143 TYR   A C    
184  O  O    . TYR   A 38  ? 0.4701 0.3516 0.4145 -0.0468 0.0615  0.0362  143 TYR   A O    
185  C  CB   . TYR   A 38  ? 0.3174 0.2268 0.2705 -0.0582 0.0449  0.0126  143 TYR   A CB   
186  C  CG   . TYR   A 38  ? 0.3266 0.2197 0.2785 -0.0678 0.0508  0.0060  143 TYR   A CG   
187  C  CD1  . TYR   A 38  ? 0.3541 0.2320 0.3044 -0.0675 0.0587  0.0079  143 TYR   A CD1  
188  C  CD2  . TYR   A 38  ? 0.2659 0.1693 0.2216 -0.0709 0.0443  -0.0032 143 TYR   A CD2  
189  C  CE1  . TYR   A 38  ? 0.3742 0.2471 0.3255 -0.0715 0.0607  -0.0004 143 TYR   A CE1  
190  C  CE2  . TYR   A 38  ? 0.2986 0.1990 0.2546 -0.0738 0.0463  -0.0097 143 TYR   A CE2  
191  C  CZ   . TYR   A 38  ? 0.3490 0.2341 0.3024 -0.0747 0.0547  -0.0091 143 TYR   A CZ   
192  O  OH   . TYR   A 38  ? 0.3869 0.2695 0.3396 -0.0789 0.0575  -0.0169 143 TYR   A OH   
193  N  N    . ASP   A 39  ? 0.4803 0.3498 0.4289 -0.0361 0.0593  0.0337  144 ASP   A N    
194  C  CA   . ASP   A 39  ? 0.4957 0.3451 0.4417 -0.0312 0.0693  0.0426  144 ASP   A CA   
195  C  C    . ASP   A 39  ? 0.5465 0.3842 0.4944 -0.0395 0.0733  0.0327  144 ASP   A C    
196  O  O    . ASP   A 39  ? 0.5806 0.4157 0.5307 -0.0401 0.0721  0.0245  144 ASP   A O    
197  C  CB   . ASP   A 39  ? 0.4928 0.3389 0.4403 -0.0172 0.0695  0.0496  144 ASP   A CB   
198  C  CG   . ASP   A 39  ? 0.5766 0.4085 0.5243 -0.0095 0.0771  0.0572  144 ASP   A CG   
199  O  OD1  . ASP   A 39  ? 0.5891 0.4110 0.5354 -0.0154 0.0826  0.0574  144 ASP   A OD1  
200  O  OD2  . ASP   A 39  ? 0.6252 0.4562 0.5748 0.0028  0.0778  0.0630  144 ASP   A OD2  
201  N  N    . PRO   A 40  ? 0.5742 0.4059 0.5207 -0.0461 0.0785  0.0333  145 PRO   A N    
202  C  CA   . PRO   A 40  ? 0.5488 0.3689 0.4961 -0.0537 0.0835  0.0240  145 PRO   A CA   
203  C  C    . PRO   A 40  ? 0.5510 0.3511 0.4987 -0.0463 0.0912  0.0269  145 PRO   A C    
204  O  O    . PRO   A 40  ? 0.5826 0.3719 0.5304 -0.0522 0.0964  0.0185  145 PRO   A O    
205  C  CB   . PRO   A 40  ? 0.5378 0.3590 0.4837 -0.0632 0.0867  0.0251  145 PRO   A CB   
206  C  CG   . PRO   A 40  ? 0.5553 0.3805 0.4992 -0.0566 0.0870  0.0394  145 PRO   A CG   
207  C  CD   . PRO   A 40  ? 0.5654 0.4026 0.5091 -0.0479 0.0802  0.0423  145 PRO   A CD   
208  N  N    . THR   A 41  ? 0.5419 0.3380 0.4897 -0.0332 0.0924  0.0385  146 THR   A N    
209  C  CA   . THR   A 41  ? 0.5767 0.3561 0.5258 -0.0245 0.0992  0.0406  146 THR   A CA   
210  C  C    . THR   A 41  ? 0.5656 0.3485 0.5168 -0.0205 0.0964  0.0335  146 THR   A C    
211  O  O    . THR   A 41  ? 0.5716 0.3414 0.5240 -0.0160 0.1027  0.0313  146 THR   A O    
212  C  CB   . THR   A 41  ? 0.5522 0.3286 0.5010 -0.0106 0.1021  0.0569  146 THR   A CB   
213  O  OG1  . THR   A 41  ? 0.5657 0.3595 0.5150 -0.0015 0.0948  0.0625  146 THR   A OG1  
214  C  CG2  . THR   A 41  ? 0.5614 0.3368 0.5077 -0.0144 0.1045  0.0656  146 THR   A CG2  
215  N  N    . TYR   A 42  ? 0.5529 0.3529 0.5048 -0.0221 0.0875  0.0302  147 TYR   A N    
216  C  CA   . TYR   A 42  ? 0.5523 0.3574 0.5064 -0.0195 0.0841  0.0242  147 TYR   A CA   
217  C  C    . TYR   A 42  ? 0.5702 0.3688 0.5262 -0.0049 0.0880  0.0323  147 TYR   A C    
218  O  O    . TYR   A 42  ? 0.5863 0.3803 0.5440 -0.0024 0.0907  0.0270  147 TYR   A O    
219  C  CB   . TYR   A 42  ? 0.5417 0.3437 0.4955 -0.0297 0.0862  0.0104  147 TYR   A CB   
220  C  CG   . TYR   A 42  ? 0.5120 0.3232 0.4642 -0.0430 0.0828  0.0030  147 TYR   A CG   
221  C  CD1  . TYR   A 42  ? 0.5390 0.3408 0.4894 -0.0508 0.0892  -0.0009 147 TYR   A CD1  
222  C  CD2  . TYR   A 42  ? 0.4775 0.3072 0.4307 -0.0474 0.0735  0.0000  147 TYR   A CD2  
223  C  CE1  . TYR   A 42  ? 0.5364 0.3490 0.4857 -0.0623 0.0863  -0.0075 147 TYR   A CE1  
224  C  CE2  . TYR   A 42  ? 0.5074 0.3478 0.4597 -0.0580 0.0706  -0.0062 147 TYR   A CE2  
225  C  CZ   . TYR   A 42  ? 0.5059 0.3386 0.4561 -0.0653 0.0769  -0.0099 147 TYR   A CZ   
226  O  OH   . TYR   A 42  ? 0.4929 0.3381 0.4423 -0.0754 0.0743  -0.0159 147 TYR   A OH   
227  N  N    . ALA   A 43  ? 0.5510 0.3516 0.5068 0.0054  0.0885  0.0456  148 ALA   A N    
228  C  CA   . ALA   A 43  ? 0.5250 0.3228 0.4831 0.0208  0.0923  0.0548  148 ALA   A CA   
229  C  C    . ALA   A 43  ? 0.5136 0.3250 0.4749 0.0280  0.0866  0.0548  148 ALA   A C    
230  O  O    . ALA   A 43  ? 0.5199 0.3289 0.4842 0.0382  0.0902  0.0571  148 ALA   A O    
231  C  CB   . ALA   A 43  ? 0.4896 0.2918 0.4466 0.0301  0.0933  0.0699  148 ALA   A CB   
232  N  N    . ASP   A 44  ? 0.5237 0.3495 0.4849 0.0229  0.0780  0.0523  149 ASP   A N    
233  C  CA   . ASP   A 44  ? 0.5361 0.3782 0.5016 0.0290  0.0712  0.0524  149 ASP   A CA   
234  C  C    . ASP   A 44  ? 0.4991 0.3375 0.4668 0.0233  0.0717  0.0409  149 ASP   A C    
235  O  O    . ASP   A 44  ? 0.5119 0.3672 0.4849 0.0284  0.0663  0.0399  149 ASP   A O    
236  C  CB   . ASP   A 44  ? 0.5497 0.4175 0.5169 0.0241  0.0589  0.0502  149 ASP   A CB   
237  C  CG   . ASP   A 44  ? 0.5874 0.4649 0.5523 0.0303  0.0577  0.0609  149 ASP   A CG   
238  O  OD1  . ASP   A 44  ? 0.5828 0.4611 0.5478 0.0435  0.0617  0.0724  149 ASP   A OD1  
239  O  OD2  . ASP   A 44  ? 0.6254 0.5113 0.5884 0.0227  0.0529  0.0582  149 ASP   A OD2  
240  N  N    . PHE   A 45  ? 0.4896 0.3123 0.4542 0.0122  0.0770  0.0312  150 PHE   A N    
241  C  CA   . PHE   A 45  ? 0.4732 0.2933 0.4387 0.0070  0.0786  0.0205  150 PHE   A CA   
242  C  C    . PHE   A 45  ? 0.5169 0.3305 0.4851 0.0194  0.0854  0.0231  150 PHE   A C    
243  O  O    . PHE   A 45  ? 0.4979 0.3162 0.4681 0.0186  0.0854  0.0163  150 PHE   A O    
244  C  CB   . PHE   A 45  ? 0.4896 0.3023 0.4516 -0.0063 0.0820  0.0094  150 PHE   A CB   
245  C  CG   . PHE   A 45  ? 0.4807 0.3054 0.4414 -0.0189 0.0743  0.0040  150 PHE   A CG   
246  C  CD1  . PHE   A 45  ? 0.4394 0.2720 0.4001 -0.0187 0.0685  0.0105  150 PHE   A CD1  
247  C  CD2  . PHE   A 45  ? 0.4428 0.2727 0.4021 -0.0301 0.0732  -0.0073 150 PHE   A CD2  
248  C  CE1  . PHE   A 45  ? 0.4213 0.2656 0.3816 -0.0290 0.0619  0.0054  150 PHE   A CE1  
249  C  CE2  . PHE   A 45  ? 0.4203 0.2641 0.3792 -0.0396 0.0659  -0.0111 150 PHE   A CE2  
250  C  CZ   . PHE   A 45  ? 0.3830 0.2335 0.3428 -0.0388 0.0603  -0.0050 150 PHE   A CZ   
251  N  N    . ARG   A 46  ? 0.5492 0.3571 0.5181 0.0309  0.0904  0.0329  151 ARG   A N    
252  C  CA   . ARG   A 46  ? 0.5998 0.4044 0.5721 0.0446  0.0966  0.0367  151 ARG   A CA   
253  C  C    . ARG   A 46  ? 0.5718 0.3961 0.5496 0.0563  0.0909  0.0431  151 ARG   A C    
254  O  O    . ARG   A 46  ? 0.5986 0.4261 0.5805 0.0659  0.0946  0.0429  151 ARG   A O    
255  C  CB   . ARG   A 46  ? 0.6755 0.4704 0.6472 0.0531  0.1029  0.0465  151 ARG   A CB   
256  C  CG   . ARG   A 46  ? 0.7750 0.5694 0.7507 0.0693  0.1087  0.0534  151 ARG   A CG   
257  C  CD   . ARG   A 46  ? 0.8570 0.6722 0.8358 0.0833  0.1034  0.0681  151 ARG   A CD   
258  N  NE   . ARG   A 46  ? 0.9075 0.7318 0.8914 0.0987  0.1061  0.0733  151 ARG   A NE   
259  C  CZ   . ARG   A 46  ? 0.9227 0.7705 0.9102 0.1118  0.1015  0.0850  151 ARG   A CZ   
260  N  NH1  . ARG   A 46  ? 0.9285 0.7864 0.9209 0.1249  0.1041  0.0888  151 ARG   A NH1  
261  N  NH2  . ARG   A 46  ? 0.9110 0.7751 0.8973 0.1114  0.0941  0.0922  151 ARG   A NH2  
262  N  N    . ASP   A 47  ? 0.5234 0.3714 0.5029 0.0531  0.0792  0.0460  152 ASP   A N    
263  C  CA   . ASP   A 47  ? 0.5334 0.4116 0.5196 0.0595  0.0703  0.0488  152 ASP   A CA   
264  C  C    . ASP   A 47  ? 0.4236 0.3161 0.4130 0.0485  0.0631  0.0382  152 ASP   A C    
265  O  O    . ASP   A 47  ? 0.3893 0.3063 0.3851 0.0512  0.0559  0.0394  152 ASP   A O    
266  C  CB   . ASP   A 47  ? 0.6428 0.5401 0.6298 0.0624  0.0620  0.0570  152 ASP   A CB   
267  C  CG   . ASP   A 47  ? 0.7676 0.6551 0.7513 0.0744  0.0688  0.0701  152 ASP   A CG   
268  O  OD1  . ASP   A 47  ? 0.8155 0.7246 0.8023 0.0858  0.0649  0.0798  152 ASP   A OD1  
269  O  OD2  . ASP   A 47  ? 0.8268 0.6859 0.8051 0.0722  0.0782  0.0712  152 ASP   A OD2  
270  N  N    . PHE   A 48  ? 0.3715 0.2508 0.3569 0.0358  0.0650  0.0285  153 PHE   A N    
271  C  CA   . PHE   A 48  ? 0.3249 0.2168 0.3126 0.0263  0.0596  0.0201  153 PHE   A CA   
272  C  C    . PHE   A 48  ? 0.3440 0.2365 0.3340 0.0318  0.0660  0.0169  153 PHE   A C    
273  O  O    . PHE   A 48  ? 0.3671 0.2436 0.3556 0.0409  0.0761  0.0182  153 PHE   A O    
274  C  CB   . PHE   A 48  ? 0.3287 0.2101 0.3109 0.0116  0.0596  0.0113  153 PHE   A CB   
275  C  CG   . PHE   A 48  ? 0.3671 0.2483 0.3471 0.0057  0.0542  0.0131  153 PHE   A CG   
276  C  CD1  . PHE   A 48  ? 0.4096 0.2786 0.3840 -0.0054 0.0566  0.0068  153 PHE   A CD1  
277  C  CD2  . PHE   A 48  ? 0.3702 0.2659 0.3538 0.0109  0.0468  0.0201  153 PHE   A CD2  
278  C  CE1  . PHE   A 48  ? 0.4343 0.3053 0.4071 -0.0105 0.0520  0.0082  153 PHE   A CE1  
279  C  CE2  . PHE   A 48  ? 0.4085 0.3054 0.3900 0.0059  0.0423  0.0207  153 PHE   A CE2  
280  C  CZ   . PHE   A 48  ? 0.4456 0.3301 0.4219 -0.0045 0.0450  0.0152  153 PHE   A CZ   
281  N  N    . ARG   A 49  ? 0.2577 0.1685 0.2515 0.0264  0.0605  0.0128  154 ARG   A N    
282  C  CA   . ARG   A 49  ? 0.3028 0.2149 0.2974 0.0284  0.0670  0.0075  154 ARG   A CA   
283  C  C    . ARG   A 49  ? 0.3595 0.2479 0.3464 0.0223  0.0763  -0.0018 154 ARG   A C    
284  O  O    . ARG   A 49  ? 0.3166 0.1975 0.2985 0.0108  0.0742  -0.0062 154 ARG   A O    
285  C  CB   . ARG   A 49  ? 0.2612 0.1964 0.2599 0.0206  0.0596  0.0049  154 ARG   A CB   
286  C  CG   . ARG   A 49  ? 0.2614 0.2205 0.2692 0.0265  0.0525  0.0123  154 ARG   A CG   
287  C  CD   . ARG   A 49  ? 0.2587 0.2376 0.2711 0.0164  0.0450  0.0109  154 ARG   A CD   
288  N  NE   . ARG   A 49  ? 0.2327 0.2095 0.2439 0.0058  0.0370  0.0105  154 ARG   A NE   
289  C  CZ   . ARG   A 49  ? 0.2678 0.2557 0.2819 -0.0040 0.0308  0.0099  154 ARG   A CZ   
290  N  NH1  . ARG   A 49  ? 0.2882 0.2909 0.3061 -0.0060 0.0316  0.0100  154 ARG   A NH1  
291  N  NH2  . ARG   A 49  ? 0.2902 0.2745 0.3037 -0.0115 0.0243  0.0099  154 ARG   A NH2  
292  N  N    . PRO   A 50  ? 0.4162 0.2928 0.4024 0.0300  0.0872  -0.0056 155 PRO   A N    
293  C  CA   . PRO   A 50  ? 0.4642 0.3146 0.4436 0.0246  0.0975  -0.0151 155 PRO   A CA   
294  C  C    . PRO   A 50  ? 0.4769 0.3344 0.4517 0.0088  0.0954  -0.0269 155 PRO   A C    
295  O  O    . PRO   A 50  ? 0.4095 0.2907 0.3867 0.0051  0.0889  -0.0276 155 PRO   A O    
296  C  CB   . PRO   A 50  ? 0.5176 0.3576 0.4991 0.0381  0.1091  -0.0169 155 PRO   A CB   
297  C  CG   . PRO   A 50  ? 0.4993 0.3684 0.4880 0.0458  0.1036  -0.0120 155 PRO   A CG   
298  C  CD   . PRO   A 50  ? 0.4789 0.3657 0.4712 0.0443  0.0910  -0.0017 155 PRO   A CD   
299  N  N    . PRO   A 51  ? 0.5127 0.3518 0.4810 -0.0013 0.1009  -0.0358 156 PRO   A N    
300  C  CA   . PRO   A 51  ? 0.4991 0.3476 0.4625 -0.0155 0.1002  -0.0480 156 PRO   A CA   
301  C  C    . PRO   A 51  ? 0.5054 0.3551 0.4681 -0.0124 0.1091  -0.0580 156 PRO   A C    
302  O  O    . PRO   A 51  ? 0.5236 0.3526 0.4868 -0.0035 0.1202  -0.0612 156 PRO   A O    
303  C  CB   . PRO   A 51  ? 0.4980 0.3265 0.4554 -0.0264 0.1045  -0.0549 156 PRO   A CB   
304  C  CG   . PRO   A 51  ? 0.5297 0.3350 0.4891 -0.0162 0.1118  -0.0486 156 PRO   A CG   
305  C  CD   . PRO   A 51  ? 0.5076 0.3181 0.4726 -0.0009 0.1082  -0.0350 156 PRO   A CD   
306  N  N    . VAL   A 52  ? 0.4955 0.3701 0.4574 -0.0191 0.1044  -0.0623 157 VAL   A N    
307  C  CA   . VAL   A 52  ? 0.5361 0.4176 0.4962 -0.0186 0.1122  -0.0735 157 VAL   A CA   
308  C  C    . VAL   A 52  ? 0.5895 0.4810 0.5421 -0.0350 0.1115  -0.0858 157 VAL   A C    
309  O  O    . VAL   A 52  ? 0.5905 0.5043 0.5425 -0.0431 0.1013  -0.0811 157 VAL   A O    
310  C  CB   . VAL   A 52  ? 0.4593 0.3672 0.4254 -0.0109 0.1078  -0.0665 157 VAL   A CB   
311  C  CG1  . VAL   A 52  ? 0.4105 0.3269 0.3743 -0.0102 0.1167  -0.0789 157 VAL   A CG1  
312  C  CG2  . VAL   A 52  ? 0.4669 0.3701 0.4410 0.0048  0.1072  -0.0541 157 VAL   A CG2  
313  N  N    . ARG   A 53  ? 0.6402 0.5158 0.5875 -0.0398 0.1226  -0.1014 158 ARG   A N    
314  C  CA   . ARG   A 53  ? 0.7095 0.5993 0.6510 -0.0554 0.1211  -0.1128 158 ARG   A CA   
315  C  C    . ARG   A 53  ? 0.8171 0.7238 0.7577 -0.0540 0.1259  -0.1223 158 ARG   A C    
316  O  O    . ARG   A 53  ? 0.8539 0.7472 0.7966 -0.0498 0.1336  -0.1295 158 ARG   A O    
317  C  CB   . ARG   A 53  ? 0.6892 0.5604 0.6314 -0.0623 0.1235  -0.1160 158 ARG   A CB   
318  C  CG   . ARG   A 53  ? 0.6579 0.5153 0.6017 -0.0615 0.1188  -0.1045 158 ARG   A CG   
319  C  CD   . ARG   A 53  ? 0.6677 0.5133 0.6117 -0.0694 0.1211  -0.1065 158 ARG   A CD   
320  N  NE   . ARG   A 53  ? 0.6497 0.4959 0.5938 -0.0723 0.1138  -0.0969 158 ARG   A NE   
321  C  CZ   . ARG   A 53  ? 0.6481 0.4796 0.5950 -0.0630 0.1126  -0.0851 158 ARG   A CZ   
322  N  NH1  . ARG   A 53  ? 0.6585 0.4733 0.6084 -0.0497 0.1183  -0.0802 158 ARG   A NH1  
323  N  NH2  . ARG   A 53  ? 0.6034 0.4394 0.5502 -0.0662 0.1054  -0.0777 158 ARG   A NH2  
324  N  N    . MET   A 54  ? 0.8808 0.8183 0.8183 -0.0577 0.1212  -0.1214 159 MET   A N    
325  C  CA   . MET   A 54  ? 0.9264 0.8866 0.8642 -0.0537 0.1244  -0.1255 159 MET   A CA   
326  C  C    . MET   A 54  ? 0.9288 0.8784 0.8680 -0.0495 0.1330  -0.1373 159 MET   A C    
327  O  O    . MET   A 54  ? 0.9275 0.8750 0.8708 -0.0367 0.1388  -0.1370 159 MET   A O    
328  C  CB   . MET   A 54  ? 0.9902 0.9865 0.9226 -0.0657 0.1171  -0.1258 159 MET   A CB   
329  C  CG   . MET   A 54  ? 1.0258 1.0356 0.9609 -0.0692 0.1033  -0.1084 159 MET   A CG   
330  S  SD   . MET   A 54  ? 1.0821 1.1350 1.0124 -0.0801 0.0952  -0.1042 159 MET   A SD   
331  C  CE   . MET   A 54  ? 1.0507 1.1019 0.9788 -0.0901 0.0853  -0.0986 159 MET   A CE   
332  N  N    . SER   A 66  ? 0.7835 0.9200 0.7513 -0.0565 0.0753  -0.0372 218 SER   A N    
333  C  CA   . SER   A 66  ? 0.7635 0.8736 0.7328 -0.0559 0.0700  -0.0348 218 SER   A CA   
334  C  C    . SER   A 66  ? 0.7408 0.8372 0.7003 -0.0609 0.0732  -0.0475 218 SER   A C    
335  O  O    . SER   A 66  ? 0.7631 0.8367 0.7210 -0.0557 0.0797  -0.0577 218 SER   A O    
336  C  CB   . SER   A 66  ? 0.7768 0.8674 0.7538 -0.0443 0.0720  -0.0340 218 SER   A CB   
337  O  OG   . SER   A 66  ? 0.8071 0.8963 0.7831 -0.0360 0.0826  -0.0445 218 SER   A OG   
338  N  N    . PRO   A 67  ? 0.6838 0.7948 0.6370 -0.0711 0.0689  -0.0466 219 PRO   A N    
339  C  CA   . PRO   A 67  ? 0.6749 0.7753 0.6201 -0.0774 0.0699  -0.0572 219 PRO   A CA   
340  C  C    . PRO   A 67  ? 0.6163 0.6941 0.5650 -0.0768 0.0637  -0.0516 219 PRO   A C    
341  O  O    . PRO   A 67  ? 0.6735 0.7474 0.6167 -0.0835 0.0625  -0.0575 219 PRO   A O    
342  C  CB   . PRO   A 67  ? 0.6448 0.7755 0.5835 -0.0874 0.0660  -0.0546 219 PRO   A CB   
343  C  CG   . PRO   A 67  ? 0.6365 0.7816 0.5826 -0.0861 0.0585  -0.0357 219 PRO   A CG   
344  C  CD   . PRO   A 67  ? 0.6503 0.7891 0.6041 -0.0772 0.0626  -0.0340 219 PRO   A CD   
345  N  N    . LEU   A 68  ? 0.4894 0.5557 0.4472 -0.0694 0.0594  -0.0409 220 LEU   A N    
346  C  CA   . LEU   A 68  ? 0.3920 0.4383 0.3534 -0.0678 0.0540  -0.0361 220 LEU   A CA   
347  C  C    . LEU   A 68  ? 0.3456 0.3682 0.3101 -0.0582 0.0597  -0.0399 220 LEU   A C    
348  O  O    . LEU   A 68  ? 0.3303 0.3457 0.3023 -0.0518 0.0554  -0.0311 220 LEU   A O    
349  C  CB   . LEU   A 68  ? 0.3536 0.4072 0.3232 -0.0675 0.0438  -0.0206 220 LEU   A CB   
350  C  CG   . LEU   A 68  ? 0.3922 0.4666 0.3599 -0.0755 0.0377  -0.0132 220 LEU   A CG   
351  C  CD1  . LEU   A 68  ? 0.4065 0.4769 0.3824 -0.0750 0.0282  -0.0002 220 LEU   A CD1  
352  C  CD2  . LEU   A 68  ? 0.4107 0.4900 0.3687 -0.0827 0.0393  -0.0224 220 LEU   A CD2  
353  N  N    . SER   A 69  ? 0.3431 0.3542 0.3019 -0.0572 0.0697  -0.0531 221 SER   A N    
354  C  CA   . SER   A 69  ? 0.3670 0.3562 0.3289 -0.0464 0.0767  -0.0556 221 SER   A CA   
355  C  C    . SER   A 69  ? 0.3007 0.2672 0.2641 -0.0442 0.0740  -0.0516 221 SER   A C    
356  O  O    . SER   A 69  ? 0.3359 0.2883 0.3038 -0.0337 0.0767  -0.0476 221 SER   A O    
357  C  CB   . SER   A 69  ? 0.3819 0.3616 0.3377 -0.0462 0.0891  -0.0714 221 SER   A CB   
358  O  OG   . SER   A 69  ? 0.3922 0.3650 0.3402 -0.0573 0.0909  -0.0818 221 SER   A OG   
359  N  N    . MET   A 70  ? 0.2779 0.2429 0.2377 -0.0534 0.0690  -0.0521 222 MET   A N    
360  C  CA   . MET   A 70  ? 0.2921 0.2390 0.2533 -0.0520 0.0662  -0.0481 222 MET   A CA   
361  C  C    . MET   A 70  ? 0.2477 0.2031 0.2159 -0.0496 0.0552  -0.0351 222 MET   A C    
362  O  O    . MET   A 70  ? 0.2946 0.2383 0.2643 -0.0478 0.0522  -0.0313 222 MET   A O    
363  C  CB   . MET   A 70  ? 0.3289 0.2706 0.2832 -0.0633 0.0672  -0.0565 222 MET   A CB   
364  C  CG   . MET   A 70  ? 0.3308 0.2554 0.2789 -0.0665 0.0793  -0.0710 222 MET   A CG   
365  S  SD   . MET   A 70  ? 0.3484 0.2395 0.2992 -0.0547 0.0886  -0.0694 222 MET   A SD   
366  C  CE   . MET   A 70  ? 0.3409 0.2187 0.2905 -0.0609 0.0849  -0.0660 222 MET   A CE   
367  N  N    . LEU   A 71  ? 0.2173 0.1927 0.1898 -0.0500 0.0495  -0.0286 223 LEU   A N    
368  C  CA   . LEU   A 71  ? 0.2384 0.2204 0.2182 -0.0492 0.0395  -0.0178 223 LEU   A CA   
369  C  C    . LEU   A 71  ? 0.2328 0.2053 0.2187 -0.0397 0.0385  -0.0126 223 LEU   A C    
370  O  O    . LEU   A 71  ? 0.2629 0.2310 0.2517 -0.0396 0.0324  -0.0084 223 LEU   A O    
371  C  CB   . LEU   A 71  ? 0.2740 0.2774 0.2578 -0.0521 0.0352  -0.0116 223 LEU   A CB   
372  C  CG   . LEU   A 71  ? 0.2275 0.2362 0.2193 -0.0532 0.0254  -0.0013 223 LEU   A CG   
373  C  CD1  . LEU   A 71  ? 0.1689 0.1712 0.1584 -0.0575 0.0205  -0.0014 223 LEU   A CD1  
374  C  CD2  . LEU   A 71  ? 0.2204 0.2483 0.2161 -0.0574 0.0224  0.0057  223 LEU   A CD2  
375  N  N    . PRO   A 72  ? 0.2612 0.2327 0.2496 -0.0311 0.0441  -0.0126 224 PRO   A N    
376  C  CA   . PRO   A 72  ? 0.2631 0.2289 0.2569 -0.0216 0.0427  -0.0070 224 PRO   A CA   
377  C  C    . PRO   A 72  ? 0.2610 0.2070 0.2506 -0.0196 0.0448  -0.0082 224 PRO   A C    
378  O  O    . PRO   A 72  ? 0.2157 0.1611 0.2087 -0.0172 0.0391  -0.0029 224 PRO   A O    
379  C  CB   . PRO   A 72  ? 0.2310 0.2006 0.2272 -0.0122 0.0500  -0.0077 224 PRO   A CB   
380  C  CG   . PRO   A 72  ? 0.2781 0.2636 0.2735 -0.0181 0.0512  -0.0108 224 PRO   A CG   
381  C  CD   . PRO   A 72  ? 0.2672 0.2479 0.2549 -0.0288 0.0509  -0.0166 224 PRO   A CD   
382  N  N    . HIS   A 73  ? 0.3167 0.2470 0.2991 -0.0214 0.0532  -0.0156 225 HIS   A N    
383  C  CA   . HIS   A 73  ? 0.3307 0.2415 0.3093 -0.0208 0.0562  -0.0162 225 HIS   A CA   
384  C  C    . HIS   A 73  ? 0.3540 0.2681 0.3317 -0.0294 0.0482  -0.0152 225 HIS   A C    
385  O  O    . HIS   A 73  ? 0.2892 0.1993 0.2685 -0.0263 0.0447  -0.0102 225 HIS   A O    
386  C  CB   . HIS   A 73  ? 0.3308 0.2232 0.3025 -0.0233 0.0675  -0.0257 225 HIS   A CB   
387  C  CG   . HIS   A 73  ? 0.3488 0.2190 0.3172 -0.0227 0.0724  -0.0253 225 HIS   A CG   
388  N  ND1  . HIS   A 73  ? 0.3555 0.2149 0.3263 -0.0110 0.0752  -0.0169 225 HIS   A ND1  
389  C  CD2  . HIS   A 73  ? 0.3605 0.2194 0.3234 -0.0327 0.0749  -0.0312 225 HIS   A CD2  
390  C  CE1  . HIS   A 73  ? 0.3697 0.2104 0.3365 -0.0138 0.0797  -0.0170 225 HIS   A CE1  
391  N  NE2  . HIS   A 73  ? 0.3735 0.2133 0.3357 -0.0275 0.0796  -0.0261 225 HIS   A NE2  
392  N  N    . LEU   A 74  ? 0.3310 0.2545 0.3061 -0.0394 0.0453  -0.0198 226 LEU   A N    
393  C  CA   . LEU   A 74  ? 0.3100 0.2371 0.2845 -0.0465 0.0386  -0.0192 226 LEU   A CA   
394  C  C    . LEU   A 74  ? 0.2432 0.1813 0.2251 -0.0435 0.0286  -0.0111 226 LEU   A C    
395  O  O    . LEU   A 74  ? 0.2619 0.1988 0.2448 -0.0448 0.0238  -0.0095 226 LEU   A O    
396  C  CB   . LEU   A 74  ? 0.2607 0.1978 0.2306 -0.0570 0.0382  -0.0254 226 LEU   A CB   
397  C  CG   . LEU   A 74  ? 0.2979 0.2238 0.2601 -0.0623 0.0482  -0.0364 226 LEU   A CG   
398  C  CD1  . LEU   A 74  ? 0.3106 0.2513 0.2679 -0.0737 0.0473  -0.0435 226 LEU   A CD1  
399  C  CD2  . LEU   A 74  ? 0.3073 0.2133 0.2673 -0.0622 0.0528  -0.0379 226 LEU   A CD2  
400  N  N    . ALA   A 75  ? 0.2317 0.1807 0.2195 -0.0400 0.0259  -0.0068 227 ALA   A N    
401  C  CA   . ALA   A 75  ? 0.1963 0.1536 0.1921 -0.0375 0.0175  -0.0005 227 ALA   A CA   
402  C  C    . ALA   A 75  ? 0.2003 0.1507 0.1977 -0.0303 0.0172  0.0017  227 ALA   A C    
403  O  O    . ALA   A 75  ? 0.2077 0.1602 0.2083 -0.0307 0.0110  0.0034  227 ALA   A O    
404  C  CB   . ALA   A 75  ? 0.2148 0.1852 0.2170 -0.0360 0.0160  0.0033  227 ALA   A CB   
405  N  N    . ASP   A 76  ? 0.1936 0.1369 0.1889 -0.0231 0.0242  0.0020  228 ASP   A N    
406  C  CA   . ASP   A 76  ? 0.2064 0.1449 0.2022 -0.0155 0.0245  0.0058  228 ASP   A CA   
407  C  C    . ASP   A 76  ? 0.2393 0.1669 0.2297 -0.0193 0.0249  0.0040  228 ASP   A C    
408  O  O    . ASP   A 76  ? 0.2137 0.1441 0.2057 -0.0167 0.0209  0.0069  228 ASP   A O    
409  C  CB   . ASP   A 76  ? 0.2184 0.1501 0.2128 -0.0058 0.0329  0.0079  228 ASP   A CB   
410  C  CG   . ASP   A 76  ? 0.2461 0.1935 0.2475 0.0002  0.0315  0.0110  228 ASP   A CG   
411  O  OD1  . ASP   A 76  ? 0.2371 0.2001 0.2448 -0.0036 0.0238  0.0120  228 ASP   A OD1  
412  O  OD2  . ASP   A 76  ? 0.2722 0.2163 0.2733 0.0088  0.0386  0.0124  228 ASP   A OD2  
413  N  N    . LEU   A 77  ? 0.2380 0.1559 0.2223 -0.0264 0.0298  -0.0014 229 LEU   A N    
414  C  CA   . LEU   A 77  ? 0.2364 0.1462 0.2161 -0.0316 0.0307  -0.0037 229 LEU   A CA   
415  C  C    . LEU   A 77  ? 0.2194 0.1412 0.2027 -0.0357 0.0212  -0.0034 229 LEU   A C    
416  O  O    . LEU   A 77  ? 0.2218 0.1435 0.2050 -0.0346 0.0189  -0.0018 229 LEU   A O    
417  C  CB   . LEU   A 77  ? 0.2500 0.1502 0.2232 -0.0399 0.0377  -0.0112 229 LEU   A CB   
418  C  CG   . LEU   A 77  ? 0.2888 0.1847 0.2577 -0.0484 0.0386  -0.0152 229 LEU   A CG   
419  C  CD1  . LEU   A 77  ? 0.2895 0.1739 0.2569 -0.0441 0.0420  -0.0106 229 LEU   A CD1  
420  C  CD2  . LEU   A 77  ? 0.2788 0.1709 0.2424 -0.0566 0.0450  -0.0241 229 LEU   A CD2  
421  N  N    . VAL   A 78  ? 0.2096 0.1422 0.1962 -0.0401 0.0160  -0.0045 230 VAL   A N    
422  C  CA   . VAL   A 78  ? 0.1344 0.0767 0.1256 -0.0427 0.0075  -0.0037 230 VAL   A CA   
423  C  C    . VAL   A 78  ? 0.2531 0.1998 0.2506 -0.0364 0.0022  -0.0003 230 VAL   A C    
424  O  O    . VAL   A 78  ? 0.2446 0.1938 0.2436 -0.0362 -0.0019 -0.0010 230 VAL   A O    
425  C  CB   . VAL   A 78  ? 0.2028 0.1548 0.1969 -0.0471 0.0038  -0.0031 230 VAL   A CB   
426  C  CG1  . VAL   A 78  ? 0.1558 0.1154 0.1571 -0.0473 -0.0047 -0.0005 230 VAL   A CG1  
427  C  CG2  . VAL   A 78  ? 0.1360 0.0887 0.1233 -0.0544 0.0080  -0.0077 230 VAL   A CG2  
428  N  N    . SER   A 79  ? 0.2428 0.1928 0.2441 -0.0313 0.0024  0.0026  231 SER   A N    
429  C  CA   . SER   A 79  ? 0.1756 0.1332 0.1830 -0.0260 -0.0024 0.0046  231 SER   A CA   
430  C  C    . SER   A 79  ? 0.1883 0.1428 0.1917 -0.0215 -0.0006 0.0053  231 SER   A C    
431  O  O    . SER   A 79  ? 0.1907 0.1521 0.1971 -0.0205 -0.0058 0.0042  231 SER   A O    
432  C  CB   . SER   A 79  ? 0.1779 0.1420 0.1894 -0.0213 -0.0012 0.0075  231 SER   A CB   
433  O  OG   . SER   A 79  ? 0.1838 0.1598 0.2034 -0.0198 -0.0077 0.0077  231 SER   A OG   
434  N  N    . TYR   A 80  ? 0.1711 0.1152 0.1677 -0.0188 0.0072  0.0071  232 TYR   A N    
435  C  CA   . TYR   A 80  ? 0.2190 0.1586 0.2109 -0.0153 0.0103  0.0096  232 TYR   A CA   
436  C  C    . TYR   A 80  ? 0.2204 0.1600 0.2103 -0.0215 0.0077  0.0060  232 TYR   A C    
437  O  O    . TYR   A 80  ? 0.2084 0.1541 0.1981 -0.0191 0.0053  0.0070  232 TYR   A O    
438  C  CB   . TYR   A 80  ? 0.2652 0.1890 0.2508 -0.0127 0.0205  0.0123  232 TYR   A CB   
439  C  CG   . TYR   A 80  ? 0.3445 0.2588 0.3243 -0.0103 0.0261  0.0164  232 TYR   A CG   
440  C  CD1  . TYR   A 80  ? 0.3672 0.2837 0.3465 0.0000  0.0283  0.0244  232 TYR   A CD1  
441  C  CD2  . TYR   A 80  ? 0.3990 0.3032 0.3736 -0.0185 0.0297  0.0130  232 TYR   A CD2  
442  C  CE1  . TYR   A 80  ? 0.3706 0.2782 0.3445 0.0023  0.0342  0.0303  232 TYR   A CE1  
443  C  CE2  . TYR   A 80  ? 0.3907 0.2857 0.3603 -0.0175 0.0357  0.0176  232 TYR   A CE2  
444  C  CZ   . TYR   A 80  ? 0.4079 0.3035 0.3769 -0.0069 0.0381  0.0269  232 TYR   A CZ   
445  O  OH   . TYR   A 80  ? 0.4571 0.3435 0.4209 -0.0058 0.0445  0.0335  232 TYR   A OH   
446  N  N    . SER   A 81  ? 0.2062 0.1423 0.1947 -0.0293 0.0080  0.0017  233 SER   A N    
447  C  CA   . SER   A 81  ? 0.1393 0.0777 0.1263 -0.0350 0.0060  -0.0017 233 SER   A CA   
448  C  C    . SER   A 81  ? 0.1662 0.1172 0.1600 -0.0336 -0.0029 -0.0033 233 SER   A C    
449  O  O    . SER   A 81  ? 0.1968 0.1529 0.1903 -0.0340 -0.0047 -0.0050 233 SER   A O    
450  C  CB   . SER   A 81  ? 0.1500 0.0854 0.1342 -0.0433 0.0083  -0.0058 233 SER   A CB   
451  O  OG   . SER   A 81  ? 0.1997 0.1219 0.1776 -0.0455 0.0174  -0.0067 233 SER   A OG   
452  N  N    . ILE   A 82  ? 0.1187 0.0747 0.1193 -0.0324 -0.0078 -0.0031 234 ILE   A N    
453  C  CA   . ILE   A 82  ? 0.1620 0.1269 0.1704 -0.0309 -0.0154 -0.0054 234 ILE   A CA   
454  C  C    . ILE   A 82  ? 0.2026 0.1738 0.2112 -0.0256 -0.0167 -0.0060 234 ILE   A C    
455  O  O    . ILE   A 82  ? 0.1665 0.1442 0.1773 -0.0251 -0.0203 -0.0098 234 ILE   A O    
456  C  CB   . ILE   A 82  ? 0.1614 0.1284 0.1772 -0.0313 -0.0192 -0.0043 234 ILE   A CB   
457  C  CG1  . ILE   A 82  ? 0.1621 0.1267 0.1777 -0.0365 -0.0188 -0.0030 234 ILE   A CG1  
458  C  CG2  . ILE   A 82  ? 0.1278 0.1012 0.1526 -0.0297 -0.0259 -0.0075 234 ILE   A CG2  
459  C  CD1  . ILE   A 82  ? 0.1088 0.0751 0.1303 -0.0376 -0.0206 0.0001  234 ILE   A CD1  
460  N  N    . GLN   A 83  ? 0.1876 0.1592 0.1939 -0.0210 -0.0136 -0.0023 235 GLN   A N    
461  C  CA   . GLN   A 83  ? 0.2498 0.2314 0.2557 -0.0155 -0.0148 -0.0017 235 GLN   A CA   
462  C  C    . GLN   A 83  ? 0.2315 0.2124 0.2307 -0.0158 -0.0117 -0.0012 235 GLN   A C    
463  O  O    . GLN   A 83  ? 0.1917 0.1843 0.1916 -0.0135 -0.0148 -0.0037 235 GLN   A O    
464  C  CB   . GLN   A 83  ? 0.3007 0.2841 0.3050 -0.0094 -0.0113 0.0042  235 GLN   A CB   
465  C  CG   . GLN   A 83  ? 0.4039 0.3988 0.4053 -0.0028 -0.0109 0.0075  235 GLN   A CG   
466  C  CD   . GLN   A 83  ? 0.4939 0.5016 0.4990 0.0036  -0.0124 0.0105  235 GLN   A CD   
467  O  OE1  . GLN   A 83  ? 0.4676 0.4730 0.4767 0.0034  -0.0120 0.0113  235 GLN   A OE1  
468  N  NE2  . GLN   A 83  ? 0.5270 0.5513 0.5309 0.0092  -0.0142 0.0123  235 GLN   A NE2  
469  N  N    . LYS   A 84  ? 0.2459 0.2144 0.2388 -0.0195 -0.0053 0.0012  236 LYS   A N    
470  C  CA   . LYS   A 84  ? 0.2932 0.2611 0.2803 -0.0218 -0.0018 0.0017  236 LYS   A CA   
471  C  C    . LYS   A 84  ? 0.2915 0.2682 0.2822 -0.0256 -0.0071 -0.0049 236 LYS   A C    
472  O  O    . LYS   A 84  ? 0.2654 0.2512 0.2545 -0.0250 -0.0074 -0.0061 236 LYS   A O    
473  C  CB   . LYS   A 84  ? 0.2758 0.2276 0.2564 -0.0268 0.0068  0.0042  236 LYS   A CB   
474  C  CG   . LYS   A 84  ? 0.2827 0.2233 0.2596 -0.0214 0.0136  0.0113  236 LYS   A CG   
475  C  CD   . LYS   A 84  ? 0.2858 0.2336 0.2602 -0.0138 0.0147  0.0183  236 LYS   A CD   
476  C  CE   . LYS   A 84  ? 0.2964 0.2303 0.2664 -0.0081 0.0235  0.0271  236 LYS   A CE   
477  N  NZ   . LYS   A 84  ? 0.3218 0.2353 0.2861 -0.0149 0.0328  0.0277  236 LYS   A NZ   
478  N  N    . VAL   A 85  ? 0.2346 0.2100 0.2304 -0.0290 -0.0109 -0.0087 237 VAL   A N    
479  C  CA   . VAL   A 85  ? 0.2322 0.2157 0.2325 -0.0309 -0.0157 -0.0140 237 VAL   A CA   
480  C  C    . VAL   A 85  ? 0.2104 0.2050 0.2169 -0.0256 -0.0216 -0.0183 237 VAL   A C    
481  O  O    . VAL   A 85  ? 0.1951 0.1989 0.2029 -0.0248 -0.0235 -0.0226 237 VAL   A O    
482  C  CB   . VAL   A 85  ? 0.2040 0.1840 0.2083 -0.0345 -0.0181 -0.0148 237 VAL   A CB   
483  C  CG1  . VAL   A 85  ? 0.1760 0.1646 0.1870 -0.0336 -0.0237 -0.0189 237 VAL   A CG1  
484  C  CG2  . VAL   A 85  ? 0.2005 0.1740 0.1982 -0.0410 -0.0122 -0.0134 237 VAL   A CG2  
485  N  N    . ILE   A 86  ? 0.1884 0.1837 0.1990 -0.0222 -0.0243 -0.0181 238 ILE   A N    
486  C  CA   . ILE   A 86  ? 0.1621 0.1685 0.1787 -0.0183 -0.0295 -0.0242 238 ILE   A CA   
487  C  C    . ILE   A 86  ? 0.1963 0.2147 0.2072 -0.0151 -0.0277 -0.0243 238 ILE   A C    
488  O  O    . ILE   A 86  ? 0.2408 0.2711 0.2547 -0.0130 -0.0310 -0.0312 238 ILE   A O    
489  C  CB   . ILE   A 86  ? 0.1916 0.1983 0.2140 -0.0171 -0.0323 -0.0243 238 ILE   A CB   
490  C  CG1  . ILE   A 86  ? 0.1518 0.1485 0.1808 -0.0207 -0.0343 -0.0238 238 ILE   A CG1  
491  C  CG2  . ILE   A 86  ? 0.1321 0.1524 0.1602 -0.0143 -0.0371 -0.0322 238 ILE   A CG2  
492  C  CD1  . ILE   A 86  ? 0.1433 0.1387 0.1753 -0.0212 -0.0344 -0.0207 238 ILE   A CD1  
493  N  N    . GLY   A 87  ? 0.1681 0.1837 0.1708 -0.0142 -0.0220 -0.0165 239 GLY   A N    
494  C  CA   . GLY   A 87  ? 0.1405 0.1678 0.1371 -0.0110 -0.0195 -0.0140 239 GLY   A CA   
495  C  C    . GLY   A 87  ? 0.1730 0.2038 0.1665 -0.0142 -0.0176 -0.0160 239 GLY   A C    
496  O  O    . GLY   A 87  ? 0.1710 0.2176 0.1634 -0.0118 -0.0188 -0.0192 239 GLY   A O    
497  N  N    . PHE   A 88  ? 0.1858 0.2045 0.1779 -0.0199 -0.0145 -0.0148 240 PHE   A N    
498  C  CA   . PHE   A 88  ? 0.1543 0.1791 0.1450 -0.0239 -0.0132 -0.0177 240 PHE   A CA   
499  C  C    . PHE   A 88  ? 0.1844 0.2217 0.1831 -0.0213 -0.0199 -0.0271 240 PHE   A C    
500  O  O    . PHE   A 88  ? 0.2188 0.2709 0.2170 -0.0198 -0.0202 -0.0309 240 PHE   A O    
501  C  CB   . PHE   A 88  ? 0.1881 0.2003 0.1769 -0.0312 -0.0094 -0.0160 240 PHE   A CB   
502  C  CG   . PHE   A 88  ? 0.2308 0.2521 0.2195 -0.0361 -0.0085 -0.0196 240 PHE   A CG   
503  C  CD1  . PHE   A 88  ? 0.2153 0.2404 0.1975 -0.0403 -0.0024 -0.0165 240 PHE   A CD1  
504  C  CD2  . PHE   A 88  ? 0.2253 0.2522 0.2209 -0.0366 -0.0135 -0.0253 240 PHE   A CD2  
505  C  CE1  . PHE   A 88  ? 0.2291 0.2654 0.2119 -0.0457 -0.0015 -0.0201 240 PHE   A CE1  
506  C  CE2  . PHE   A 88  ? 0.1795 0.2181 0.1756 -0.0404 -0.0129 -0.0284 240 PHE   A CE2  
507  C  CZ   . PHE   A 88  ? 0.2243 0.2686 0.2141 -0.0454 -0.0069 -0.0264 240 PHE   A CZ   
508  N  N    . ALA   A 89  ? 0.1858 0.2171 0.1923 -0.0203 -0.0248 -0.0309 241 ALA   A N    
509  C  CA   . ALA   A 89  ? 0.1800 0.2187 0.1954 -0.0173 -0.0303 -0.0394 241 ALA   A CA   
510  C  C    . ALA   A 89  ? 0.2221 0.2752 0.2394 -0.0123 -0.0329 -0.0464 241 ALA   A C    
511  O  O    . ALA   A 89  ? 0.2008 0.2650 0.2220 -0.0097 -0.0348 -0.0539 241 ALA   A O    
512  C  CB   . ALA   A 89  ? 0.1303 0.1576 0.1538 -0.0171 -0.0343 -0.0402 241 ALA   A CB   
513  N  N    A LYS   A 90  ? 0.2063 0.2617 0.2213 -0.0105 -0.0330 -0.0447 242 LYS   A N    
514  N  N    B LYS   A 90  ? 0.2058 0.2613 0.2207 -0.0105 -0.0330 -0.0447 242 LYS   A N    
515  C  CA   A LYS   A 90  ? 0.2301 0.3027 0.2466 -0.0063 -0.0358 -0.0523 242 LYS   A CA   
516  C  CA   B LYS   A 90  ? 0.2302 0.3028 0.2466 -0.0063 -0.0358 -0.0524 242 LYS   A CA   
517  C  C    A LYS   A 90  ? 0.2199 0.3097 0.2298 -0.0051 -0.0329 -0.0528 242 LYS   A C    
518  C  C    B LYS   A 90  ? 0.2196 0.3094 0.2297 -0.0051 -0.0330 -0.0530 242 LYS   A C    
519  O  O    A LYS   A 90  ? 0.2229 0.3298 0.2351 -0.0017 -0.0355 -0.0620 242 LYS   A O    
520  O  O    B LYS   A 90  ? 0.2238 0.3305 0.2363 -0.0017 -0.0355 -0.0624 242 LYS   A O    
521  C  CB   A LYS   A 90  ? 0.2616 0.3373 0.2759 -0.0048 -0.0361 -0.0487 242 LYS   A CB   
522  C  CB   B LYS   A 90  ? 0.2614 0.3374 0.2755 -0.0048 -0.0361 -0.0487 242 LYS   A CB   
523  C  CG   A LYS   A 90  ? 0.3043 0.3726 0.3279 -0.0056 -0.0406 -0.0536 242 LYS   A CG   
524  C  CG   B LYS   A 90  ? 0.3041 0.3704 0.3268 -0.0059 -0.0400 -0.0518 242 LYS   A CG   
525  C  CD   A LYS   A 90  ? 0.3218 0.3917 0.3429 -0.0048 -0.0399 -0.0470 242 LYS   A CD   
526  C  CD   B LYS   A 90  ? 0.3208 0.3877 0.3400 -0.0051 -0.0385 -0.0439 242 LYS   A CD   
527  C  CE   A LYS   A 90  ? 0.3322 0.4223 0.3456 -0.0006 -0.0384 -0.0440 242 LYS   A CE   
528  C  CE   B LYS   A 90  ? 0.3312 0.4210 0.3468 -0.0010 -0.0394 -0.0457 242 LYS   A CE   
529  N  NZ   A LYS   A 90  ? 0.3311 0.4187 0.3389 0.0017  -0.0348 -0.0316 242 LYS   A NZ   
530  N  NZ   B LYS   A 90  ? 0.3197 0.4209 0.3443 -0.0014 -0.0453 -0.0584 242 LYS   A NZ   
531  N  N    . MET   A 91  ? 0.1907 0.2768 0.1928 -0.0084 -0.0273 -0.0436 243 MET   A N    
532  C  CA   . MET   A 91  ? 0.2123 0.3144 0.2079 -0.0087 -0.0236 -0.0421 243 MET   A CA   
533  C  C    . MET   A 91  ? 0.2436 0.3505 0.2424 -0.0109 -0.0234 -0.0473 243 MET   A C    
534  O  O    . MET   A 91  ? 0.1972 0.3192 0.1914 -0.0120 -0.0200 -0.0465 243 MET   A O    
535  C  CB   . MET   A 91  ? 0.2498 0.3446 0.2352 -0.0117 -0.0164 -0.0284 243 MET   A CB   
536  C  CG   . MET   A 91  ? 0.3014 0.3966 0.2834 -0.0073 -0.0162 -0.0219 243 MET   A CG   
537  S  SD   . MET   A 91  ? 0.3754 0.4613 0.3461 -0.0083 -0.0069 -0.0046 243 MET   A SD   
538  C  CE   . MET   A 91  ? 0.3342 0.3907 0.3070 -0.0112 -0.0048 -0.0003 243 MET   A CE   
539  N  N    . ILE   A 92  ? 0.2056 0.3022 0.2125 -0.0112 -0.0267 -0.0517 244 ILE   A N    
540  C  CA   . ILE   A 92  ? 0.2131 0.3171 0.2247 -0.0115 -0.0273 -0.0567 244 ILE   A CA   
541  C  C    . ILE   A 92  ? 0.2447 0.3675 0.2615 -0.0050 -0.0304 -0.0682 244 ILE   A C    
542  O  O    . ILE   A 92  ? 0.1866 0.3067 0.2102 -0.0003 -0.0349 -0.0760 244 ILE   A O    
543  C  CB   . ILE   A 92  ? 0.2064 0.2961 0.2256 -0.0118 -0.0305 -0.0571 244 ILE   A CB   
544  C  CG1  . ILE   A 92  ? 0.1629 0.2367 0.1766 -0.0187 -0.0271 -0.0475 244 ILE   A CG1  
545  C  CG2  . ILE   A 92  ? 0.2232 0.3246 0.2484 -0.0098 -0.0317 -0.0621 244 ILE   A CG2  
546  C  CD1  . ILE   A 92  ? 0.1511 0.2126 0.1713 -0.0188 -0.0304 -0.0468 244 ILE   A CD1  
547  N  N    . PRO   A 93  ? 0.2803 0.4225 0.2945 -0.0050 -0.0278 -0.0704 245 PRO   A N    
548  C  CA   . PRO   A 93  ? 0.2731 0.4350 0.2922 0.0018  -0.0301 -0.0827 245 PRO   A CA   
549  C  C    . PRO   A 93  ? 0.2913 0.4441 0.3232 0.0080  -0.0343 -0.0916 245 PRO   A C    
550  O  O    . PRO   A 93  ? 0.2937 0.4431 0.3308 0.0081  -0.0356 -0.0909 245 PRO   A O    
551  C  CB   . PRO   A 93  ? 0.2883 0.4711 0.3032 -0.0006 -0.0258 -0.0815 245 PRO   A CB   
552  C  CG   . PRO   A 93  ? 0.3101 0.4844 0.3152 -0.0096 -0.0202 -0.0676 245 PRO   A CG   
553  C  CD   . PRO   A 93  ? 0.3154 0.4632 0.3226 -0.0119 -0.0220 -0.0626 245 PRO   A CD   
554  N  N    . GLY   A 94  ? 0.2558 0.4060 0.2930 0.0131  -0.0364 -0.0999 246 GLY   A N    
555  C  CA   . GLY   A 94  ? 0.2671 0.4078 0.3172 0.0190  -0.0404 -0.1098 246 GLY   A CA   
556  C  C    . GLY   A 94  ? 0.2641 0.3812 0.3190 0.0171  -0.0437 -0.1075 246 GLY   A C    
557  O  O    . GLY   A 94  ? 0.2762 0.3844 0.3416 0.0213  -0.0465 -0.1167 246 GLY   A O    
558  N  N    . PHE   A 95  ? 0.2285 0.3353 0.2764 0.0108  -0.0431 -0.0960 247 PHE   A N    
559  C  CA   . PHE   A 95  ? 0.2675 0.3536 0.3199 0.0085  -0.0457 -0.0928 247 PHE   A CA   
560  C  C    . PHE   A 95  ? 0.3259 0.4102 0.3818 0.0098  -0.0463 -0.0992 247 PHE   A C    
561  O  O    . PHE   A 95  ? 0.3275 0.3967 0.3923 0.0100  -0.0487 -0.1020 247 PHE   A O    
562  C  CB   . PHE   A 95  ? 0.2158 0.2944 0.2593 0.0021  -0.0438 -0.0802 247 PHE   A CB   
563  C  CG   . PHE   A 95  ? 0.2160 0.2748 0.2639 -0.0004 -0.0456 -0.0751 247 PHE   A CG   
564  C  CD1  . PHE   A 95  ? 0.2503 0.2972 0.3044 0.0000  -0.0468 -0.0716 247 PHE   A CD1  
565  C  CD2  . PHE   A 95  ? 0.2539 0.3084 0.2996 -0.0029 -0.0460 -0.0731 247 PHE   A CD2  
566  C  CE1  . PHE   A 95  ? 0.2347 0.2651 0.2923 -0.0027 -0.0481 -0.0660 247 PHE   A CE1  
567  C  CE2  . PHE   A 95  ? 0.2549 0.2931 0.3048 -0.0056 -0.0473 -0.0682 247 PHE   A CE2  
568  C  CZ   . PHE   A 95  ? 0.2595 0.2854 0.3152 -0.0058 -0.0482 -0.0647 247 PHE   A CZ   
569  N  N    A ARG   A 96  ? 0.3466 0.4476 0.3955 0.0102  -0.0441 -0.1011 248 ARG   A N    
570  N  N    B ARG   A 96  ? 0.3474 0.4480 0.3966 0.0102  -0.0441 -0.1013 248 ARG   A N    
571  C  CA   A ARG   A 96  ? 0.3737 0.4794 0.4253 0.0109  -0.0444 -0.1079 248 ARG   A CA   
572  C  CA   B ARG   A 96  ? 0.3737 0.4754 0.4268 0.0105  -0.0449 -0.1076 248 ARG   A CA   
573  C  C    A ARG   A 96  ? 0.3923 0.4960 0.4566 0.0151  -0.0457 -0.1213 248 ARG   A C    
574  C  C    B ARG   A 96  ? 0.3914 0.4970 0.4553 0.0153  -0.0456 -0.1219 248 ARG   A C    
575  O  O    A ARG   A 96  ? 0.3944 0.4916 0.4652 0.0139  -0.0468 -0.1266 248 ARG   A O    
576  O  O    B ARG   A 96  ? 0.3979 0.5034 0.4670 0.0145  -0.0461 -0.1286 248 ARG   A O    
577  C  CB   A ARG   A 96  ? 0.3701 0.4992 0.4122 0.0115  -0.0418 -0.1074 248 ARG   A CB   
578  C  CB   B ARG   A 96  ? 0.3720 0.4914 0.4148 0.0094  -0.0429 -0.1042 248 ARG   A CB   
579  C  CG   A ARG   A 96  ? 0.3784 0.5263 0.4189 0.0153  -0.0393 -0.1124 248 ARG   A CG   
580  C  CG   B ARG   A 96  ? 0.3350 0.4483 0.3700 0.0053  -0.0431 -0.0916 248 ARG   A CG   
581  C  CD   A ARG   A 96  ? 0.3764 0.5474 0.4060 0.0151  -0.0362 -0.1080 248 ARG   A CD   
582  C  CD   B ARG   A 96  ? 0.3096 0.4292 0.3430 0.0043  -0.0439 -0.0908 248 ARG   A CD   
583  N  NE   A ARG   A 96  ? 0.3927 0.5833 0.4214 0.0181  -0.0334 -0.1125 248 ARG   A NE   
584  N  NE   B ARG   A 96  ? 0.2978 0.4044 0.3410 0.0026  -0.0461 -0.0961 248 ARG   A NE   
585  C  CZ   A ARG   A 96  ? 0.3877 0.6024 0.4093 0.0187  -0.0303 -0.1106 248 ARG   A CZ   
586  C  CZ   B ARG   A 96  ? 0.2615 0.3503 0.3080 -0.0008 -0.0475 -0.0905 248 ARG   A CZ   
587  N  NH1  A ARG   A 96  ? 0.3881 0.6108 0.4025 0.0174  -0.0299 -0.1041 248 ARG   A NH1  
588  N  NH1  B ARG   A 96  ? 0.2490 0.3278 0.3043 -0.0030 -0.0488 -0.0950 248 ARG   A NH1  
589  N  NH2  A ARG   A 96  ? 0.3926 0.6257 0.4149 0.0211  -0.0276 -0.1147 248 ARG   A NH2  
590  N  NH2  B ARG   A 96  ? 0.2576 0.3394 0.2990 -0.0025 -0.0472 -0.0805 248 ARG   A NH2  
591  N  N    . ASP   A 97  ? 0.3969 0.5067 0.4653 0.0200  -0.0457 -0.1274 249 ASP   A N    
592  C  CA   . ASP   A 97  ? 0.4417 0.5510 0.5229 0.0253  -0.0469 -0.1414 249 ASP   A CA   
593  C  C    . ASP   A 97  ? 0.4560 0.5396 0.5491 0.0255  -0.0498 -0.1422 249 ASP   A C    
594  O  O    . ASP   A 97  ? 0.5008 0.5787 0.6055 0.0286  -0.0503 -0.1526 249 ASP   A O    
595  C  CB   . ASP   A 97  ? 0.4974 0.6220 0.5800 0.0315  -0.0461 -0.1473 249 ASP   A CB   
596  C  CG   . ASP   A 97  ? 0.5295 0.6811 0.6021 0.0313  -0.0425 -0.1469 249 ASP   A CG   
597  O  OD1  . ASP   A 97  ? 0.5424 0.7026 0.6106 0.0287  -0.0411 -0.1471 249 ASP   A OD1  
598  O  OD2  . ASP   A 97  ? 0.5180 0.6836 0.5872 0.0337  -0.0408 -0.1459 249 ASP   A OD2  
599  N  N    . LEU   A 98  ? 0.4008 0.4686 0.4916 0.0218  -0.0511 -0.1307 250 LEU   A N    
600  C  CA   . LEU   A 98  ? 0.3235 0.3670 0.4250 0.0215  -0.0533 -0.1289 250 LEU   A CA   
601  C  C    . LEU   A 98  ? 0.2763 0.3115 0.3806 0.0161  -0.0525 -0.1291 250 LEU   A C    
602  O  O    . LEU   A 98  ? 0.2497 0.2959 0.3455 0.0120  -0.0512 -0.1273 250 LEU   A O    
603  C  CB   . LEU   A 98  ? 0.3012 0.3340 0.3990 0.0186  -0.0550 -0.1161 250 LEU   A CB   
604  C  CG   . LEU   A 98  ? 0.2332 0.2751 0.3274 0.0223  -0.0546 -0.1112 250 LEU   A CG   
605  C  CD1  . LEU   A 98  ? 0.2135 0.2488 0.3007 0.0170  -0.0537 -0.0947 250 LEU   A CD1  
606  C  CD2  . LEU   A 98  ? 0.2138 0.2496 0.3203 0.0313  -0.0552 -0.1157 250 LEU   A CD2  
607  N  N    . THR   A 99  ? 0.2774 0.2932 0.3933 0.0162  -0.0532 -0.1307 251 THR   A N    
608  C  CA   . THR   A 99  ? 0.2539 0.2606 0.3725 0.0097  -0.0523 -0.1297 251 THR   A CA   
609  C  C    . THR   A 99  ? 0.2879 0.2910 0.3982 0.0037  -0.0525 -0.1163 251 THR   A C    
610  O  O    . THR   A 99  ? 0.3056 0.3069 0.4107 0.0042  -0.0533 -0.1070 251 THR   A O    
611  C  CB   . THR   A 99  ? 0.2902 0.2746 0.4221 0.0104  -0.0520 -0.1312 251 THR   A CB   
612  O  OG1  . THR   A 99  ? 0.2810 0.2503 0.4158 0.0130  -0.0533 -0.1202 251 THR   A OG1  
613  C  CG2  . THR   A 99  ? 0.2907 0.2775 0.4310 0.0164  -0.0510 -0.1453 251 THR   A CG2  
614  N  N    . SER   A 100 ? 0.2569 0.2600 0.3663 -0.0024 -0.0516 -0.1162 252 SER   A N    
615  C  CA   . SER   A 100 ? 0.2665 0.2673 0.3689 -0.0077 -0.0515 -0.1045 252 SER   A CA   
616  C  C    . SER   A 100 ? 0.2091 0.1906 0.3161 -0.0089 -0.0519 -0.0938 252 SER   A C    
617  O  O    . SER   A 100 ? 0.2114 0.1921 0.3117 -0.0104 -0.0520 -0.0832 252 SER   A O    
618  C  CB   . SER   A 100 ? 0.3156 0.3216 0.4181 -0.0137 -0.0509 -0.1078 252 SER   A CB   
619  O  OG   . SER   A 100 ? 0.3890 0.4159 0.4822 -0.0135 -0.0509 -0.1096 252 SER   A OG   
620  N  N    . ASP   A 101 ? 0.2442 0.2101 0.3624 -0.0081 -0.0518 -0.0961 253 ASP   A N    
621  C  CA   . ASP   A 101 ? 0.2821 0.2306 0.4050 -0.0085 -0.0520 -0.0847 253 ASP   A CA   
622  C  C    . ASP   A 101 ? 0.3068 0.2562 0.4270 -0.0035 -0.0540 -0.0786 253 ASP   A C    
623  O  O    . ASP   A 101 ? 0.3552 0.3002 0.4721 -0.0058 -0.0544 -0.0668 253 ASP   A O    
624  C  CB   . ASP   A 101 ? 0.3024 0.2337 0.4377 -0.0071 -0.0509 -0.0879 253 ASP   A CB   
625  C  CG   . ASP   A 101 ? 0.4209 0.3468 0.5590 -0.0147 -0.0487 -0.0907 253 ASP   A CG   
626  O  OD1  . ASP   A 101 ? 0.4891 0.4028 0.6361 -0.0146 -0.0471 -0.0972 253 ASP   A OD1  
627  O  OD2  . ASP   A 101 ? 0.4188 0.3523 0.5501 -0.0209 -0.0485 -0.0867 253 ASP   A OD2  
628  N  N    . ASP   A 102 ? 0.2897 0.2464 0.4115 0.0031  -0.0552 -0.0871 254 ASP   A N    
629  C  CA   . ASP   A 102 ? 0.2825 0.2414 0.4022 0.0074  -0.0575 -0.0832 254 ASP   A CA   
630  C  C    . ASP   A 102 ? 0.2247 0.1973 0.3307 0.0029  -0.0574 -0.0779 254 ASP   A C    
631  O  O    . ASP   A 102 ? 0.2332 0.2076 0.3333 0.0026  -0.0566 -0.0667 254 ASP   A O    
632  C  CB   . ASP   A 102 ? 0.3048 0.2706 0.4293 0.0162  -0.0583 -0.0948 254 ASP   A CB   
633  C  CG   . ASP   A 102 ? 0.3794 0.3285 0.5177 0.0238  -0.0582 -0.0947 254 ASP   A CG   
634  O  OD1  . ASP   A 102 ? 0.4136 0.3668 0.5575 0.0309  -0.0573 -0.1053 254 ASP   A OD1  
635  O  OD2  . ASP   A 102 ? 0.4520 0.3854 0.5950 0.0227  -0.0583 -0.0825 254 ASP   A OD2  
636  N  N    . GLN   A 103 ? 0.2015 0.1869 0.2993 0.0002  -0.0552 -0.0816 255 GLN   A N    
637  C  CA   . GLN   A 103 ? 0.1940 0.1893 0.2789 -0.0035 -0.0537 -0.0746 255 GLN   A CA   
638  C  C    . GLN   A 103 ? 0.2171 0.2021 0.2999 -0.0087 -0.0530 -0.0629 255 GLN   A C    
639  O  O    . GLN   A 103 ? 0.2118 0.1988 0.2872 -0.0110 -0.0522 -0.0554 255 GLN   A O    
640  C  CB   . GLN   A 103 ? 0.1753 0.1849 0.2536 -0.0042 -0.0519 -0.0799 255 GLN   A CB   
641  C  CG   . GLN   A 103 ? 0.2053 0.2299 0.2825 0.0006  -0.0517 -0.0898 255 GLN   A CG   
642  C  CD   . GLN   A 103 ? 0.2510 0.2912 0.3224 -0.0001 -0.0503 -0.0945 255 GLN   A CD   
643  O  OE1  . GLN   A 103 ? 0.3181 0.3723 0.3893 0.0035  -0.0496 -0.1032 255 GLN   A OE1  
644  N  NE2  . GLN   A 103 ? 0.2923 0.3324 0.3597 -0.0042 -0.0500 -0.0889 255 GLN   A NE2  
645  N  N    A ILE   A 104 ? 0.2425 0.2173 0.3320 -0.0110 -0.0527 -0.0616 256 ILE   A N    
646  N  N    B ILE   A 104 ? 0.2413 0.2165 0.3307 -0.0111 -0.0527 -0.0617 256 ILE   A N    
647  C  CA   A ILE   A 104 ? 0.2440 0.2120 0.3314 -0.0160 -0.0515 -0.0509 256 ILE   A CA   
648  C  CA   B ILE   A 104 ? 0.2435 0.2112 0.3312 -0.0159 -0.0515 -0.0510 256 ILE   A CA   
649  C  C    A ILE   A 104 ? 0.2371 0.1958 0.3275 -0.0157 -0.0529 -0.0422 256 ILE   A C    
650  C  C    B ILE   A 104 ? 0.2374 0.1965 0.3276 -0.0155 -0.0529 -0.0425 256 ILE   A C    
651  O  O    A ILE   A 104 ? 0.2404 0.2005 0.3241 -0.0187 -0.0519 -0.0338 256 ILE   A O    
652  O  O    B ILE   A 104 ? 0.2359 0.1971 0.3189 -0.0183 -0.0520 -0.0346 256 ILE   A O    
653  C  CB   A ILE   A 104 ? 0.2509 0.2135 0.3443 -0.0194 -0.0506 -0.0523 256 ILE   A CB   
654  C  CB   B ILE   A 104 ? 0.2529 0.2138 0.3476 -0.0192 -0.0507 -0.0522 256 ILE   A CB   
655  C  CG1  A ILE   A 104 ? 0.2585 0.2340 0.3471 -0.0214 -0.0499 -0.0587 256 ILE   A CG1  
656  C  CG1  B ILE   A 104 ? 0.2630 0.2354 0.3551 -0.0209 -0.0501 -0.0607 256 ILE   A CG1  
657  C  CG2  A ILE   A 104 ? 0.2495 0.2042 0.3431 -0.0238 -0.0494 -0.0412 256 ILE   A CG2  
658  C  CG2  B ILE   A 104 ? 0.2500 0.2049 0.3434 -0.0239 -0.0493 -0.0411 256 ILE   A CG2  
659  C  CD1  A ILE   A 104 ? 0.2567 0.2301 0.3514 -0.0260 -0.0494 -0.0625 256 ILE   A CD1  
660  C  CD1  B ILE   A 104 ? 0.2487 0.2324 0.3313 -0.0228 -0.0494 -0.0569 256 ILE   A CD1  
661  N  N    . VAL   A 105 ? 0.2395 0.1889 0.3407 -0.0117 -0.0552 -0.0441 257 VAL   A N    
662  C  CA   . VAL   A 105 ? 0.2648 0.2086 0.3681 -0.0100 -0.0559 -0.0333 257 VAL   A CA   
663  C  C    . VAL   A 105 ? 0.2087 0.1669 0.3010 -0.0082 -0.0548 -0.0301 257 VAL   A C    
664  O  O    . VAL   A 105 ? 0.2104 0.1712 0.2977 -0.0101 -0.0539 -0.0200 257 VAL   A O    
665  C  CB   . VAL   A 105 ? 0.3118 0.2437 0.4282 -0.0034 -0.0572 -0.0341 257 VAL   A CB   
666  C  CG1  . VAL   A 105 ? 0.3183 0.2375 0.4432 -0.0064 -0.0560 -0.0372 257 VAL   A CG1  
667  C  CG2  . VAL   A 105 ? 0.3514 0.2913 0.4692 0.0044  -0.0578 -0.0443 257 VAL   A CG2  
668  N  N    . LEU   A 106 ? 0.1944 0.1636 0.2825 -0.0056 -0.0544 -0.0389 258 LEU   A N    
669  C  CA   . LEU   A 106 ? 0.2034 0.1862 0.2817 -0.0056 -0.0527 -0.0363 258 LEU   A CA   
670  C  C    . LEU   A 106 ? 0.1669 0.1519 0.2338 -0.0126 -0.0498 -0.0309 258 LEU   A C    
671  O  O    . LEU   A 106 ? 0.1657 0.1558 0.2262 -0.0152 -0.0481 -0.0248 258 LEU   A O    
672  C  CB   . LEU   A 106 ? 0.1766 0.1714 0.2533 -0.0017 -0.0524 -0.0464 258 LEU   A CB   
673  C  CG   . LEU   A 106 ? 0.1935 0.1913 0.2796 0.0067  -0.0542 -0.0518 258 LEU   A CG   
674  C  CD1  . LEU   A 106 ? 0.1472 0.1610 0.2297 0.0093  -0.0532 -0.0616 258 LEU   A CD1  
675  C  CD2  . LEU   A 106 ? 0.1793 0.1806 0.2671 0.0096  -0.0547 -0.0426 258 LEU   A CD2  
676  N  N    . LEU   A 107 ? 0.1889 0.1711 0.2538 -0.0155 -0.0491 -0.0335 259 LEU   A N    
677  C  CA   . LEU   A 107 ? 0.2107 0.1937 0.2656 -0.0205 -0.0457 -0.0284 259 LEU   A CA   
678  C  C    . LEU   A 107 ? 0.1826 0.1582 0.2383 -0.0242 -0.0453 -0.0199 259 LEU   A C    
679  O  O    . LEU   A 107 ? 0.1984 0.1756 0.2459 -0.0278 -0.0421 -0.0151 259 LEU   A O    
680  C  CB   . LEU   A 107 ? 0.2222 0.2076 0.2751 -0.0207 -0.0451 -0.0327 259 LEU   A CB   
681  C  CG   . LEU   A 107 ? 0.2608 0.2570 0.3067 -0.0187 -0.0433 -0.0370 259 LEU   A CG   
682  C  CD1  . LEU   A 107 ? 0.2706 0.2738 0.3192 -0.0164 -0.0451 -0.0444 259 LEU   A CD1  
683  C  CD2  . LEU   A 107 ? 0.2800 0.2762 0.3147 -0.0218 -0.0382 -0.0307 259 LEU   A CD2  
684  N  N    . LYS   A 108 ? 0.1796 0.1473 0.2451 -0.0238 -0.0479 -0.0183 260 LYS   A N    
685  C  CA   . LYS   A 108 ? 0.1981 0.1607 0.2645 -0.0275 -0.0473 -0.0092 260 LYS   A CA   
686  C  C    . LYS   A 108 ? 0.1554 0.1230 0.2183 -0.0272 -0.0469 -0.0024 260 LYS   A C    
687  O  O    . LYS   A 108 ? 0.1425 0.1130 0.1991 -0.0313 -0.0447 0.0036  260 LYS   A O    
688  C  CB   . LYS   A 108 ? 0.2088 0.1612 0.2874 -0.0277 -0.0498 -0.0081 260 LYS   A CB   
689  C  CG   . LYS   A 108 ? 0.3074 0.2610 0.3849 -0.0290 -0.0471 -0.0119 260 LYS   A CG   
690  C  CD   . LYS   A 108 ? 0.3284 0.2737 0.4161 -0.0294 -0.0477 -0.0119 260 LYS   A CD   
691  C  CE   . LYS   A 108 ? 0.3761 0.3158 0.4666 -0.0324 -0.0471 -0.0005 260 LYS   A CE   
692  N  NZ   . LYS   A 108 ? 0.3613 0.3067 0.4463 -0.0371 -0.0440 0.0035  260 LYS   A NZ   
693  N  N    . SER   A 109 ? 0.2427 0.2136 0.3097 -0.0221 -0.0490 -0.0037 261 SER   A N    
694  C  CA   . SER   A 109 ? 0.2506 0.2305 0.3148 -0.0214 -0.0491 0.0030  261 SER   A CA   
695  C  C    . SER   A 109 ? 0.2478 0.2398 0.3008 -0.0249 -0.0463 -0.0001 261 SER   A C    
696  O  O    . SER   A 109 ? 0.2439 0.2447 0.2914 -0.0284 -0.0450 0.0047  261 SER   A O    
697  C  CB   . SER   A 109 ? 0.3183 0.2990 0.3921 -0.0135 -0.0522 0.0038  261 SER   A CB   
698  O  OG   . SER   A 109 ? 0.3978 0.3790 0.4746 -0.0093 -0.0529 -0.0065 261 SER   A OG   
699  N  N    . SER   A 110 ? 0.2068 0.2002 0.2563 -0.0248 -0.0448 -0.0080 262 SER   A N    
700  C  CA   . SER   A 110 ? 0.1571 0.1604 0.1972 -0.0287 -0.0414 -0.0110 262 SER   A CA   
701  C  C    . SER   A 110 ? 0.1333 0.1319 0.1638 -0.0352 -0.0365 -0.0107 262 SER   A C    
702  O  O    . SER   A 110 ? 0.2057 0.2102 0.2284 -0.0402 -0.0328 -0.0120 262 SER   A O    
703  C  CB   . SER   A 110 ? 0.2248 0.2330 0.2657 -0.0252 -0.0415 -0.0184 262 SER   A CB   
704  O  OG   . SER   A 110 ? 0.2270 0.2292 0.2640 -0.0263 -0.0393 -0.0217 262 SER   A OG   
705  N  N    . ALA   A 111 ? 0.1355 0.1241 0.1669 -0.0352 -0.0360 -0.0095 263 ALA   A N    
706  C  CA   . ALA   A 111 ? 0.1483 0.1320 0.1716 -0.0387 -0.0310 -0.0100 263 ALA   A CA   
707  C  C    . ALA   A 111 ? 0.1518 0.1374 0.1672 -0.0449 -0.0266 -0.0082 263 ALA   A C    
708  O  O    . ALA   A 111 ? 0.1997 0.1839 0.2076 -0.0484 -0.0215 -0.0109 263 ALA   A O    
709  C  CB   . ALA   A 111 ? 0.1118 0.0884 0.1387 -0.0373 -0.0316 -0.0081 263 ALA   A CB   
710  N  N    . ILE   A 112 ? 0.1738 0.1627 0.1909 -0.0467 -0.0281 -0.0039 264 ILE   A N    
711  C  CA   . ILE   A 112 ? 0.1434 0.1365 0.1527 -0.0532 -0.0239 -0.0039 264 ILE   A CA   
712  C  C    . ILE   A 112 ? 0.1255 0.1285 0.1304 -0.0572 -0.0224 -0.0081 264 ILE   A C    
713  O  O    . ILE   A 112 ? 0.1385 0.1415 0.1356 -0.0639 -0.0168 -0.0120 264 ILE   A O    
714  C  CB   . ILE   A 112 ? 0.1980 0.1968 0.2096 -0.0542 -0.0261 0.0023  264 ILE   A CB   
715  C  CG1  . ILE   A 112 ? 0.1422 0.1454 0.1450 -0.0611 -0.0209 0.0005  264 ILE   A CG1  
716  C  CG2  . ILE   A 112 ? 0.1532 0.1633 0.1706 -0.0514 -0.0314 0.0065  264 ILE   A CG2  
717  C  CD1  . ILE   A 112 ? 0.1416 0.1326 0.1398 -0.0621 -0.0149 -0.0029 264 ILE   A CD1  
718  N  N    . GLU   A 113 ? 0.1260 0.1378 0.1363 -0.0535 -0.0268 -0.0080 265 GLU   A N    
719  C  CA   . GLU   A 113 ? 0.1544 0.1794 0.1617 -0.0573 -0.0258 -0.0120 265 GLU   A CA   
720  C  C    . GLU   A 113 ? 0.1785 0.1974 0.1805 -0.0605 -0.0206 -0.0175 265 GLU   A C    
721  O  O    . GLU   A 113 ? 0.2027 0.2258 0.1985 -0.0672 -0.0156 -0.0211 265 GLU   A O    
722  C  CB   . GLU   A 113 ? 0.2002 0.2369 0.2159 -0.0505 -0.0317 -0.0102 265 GLU   A CB   
723  C  CG   . GLU   A 113 ? 0.1575 0.2018 0.1786 -0.0469 -0.0363 -0.0028 265 GLU   A CG   
724  C  CD   . GLU   A 113 ? 0.2000 0.2531 0.2305 -0.0382 -0.0414 -0.0006 265 GLU   A CD   
725  O  OE1  . GLU   A 113 ? 0.2274 0.2910 0.2581 -0.0376 -0.0411 -0.0057 265 GLU   A OE1  
726  O  OE2  . GLU   A 113 ? 0.2168 0.2659 0.2551 -0.0317 -0.0451 0.0063  265 GLU   A OE2  
727  N  N    . VAL   A 114 ? 0.1612 0.1708 0.1657 -0.0549 -0.0213 -0.0176 266 VAL   A N    
728  C  CA   . VAL   A 114 ? 0.1145 0.1194 0.1137 -0.0571 -0.0162 -0.0205 266 VAL   A CA   
729  C  C    . VAL   A 114 ? 0.1611 0.1526 0.1527 -0.0624 -0.0091 -0.0203 266 VAL   A C    
730  O  O    . VAL   A 114 ? 0.1912 0.1790 0.1769 -0.0674 -0.0028 -0.0223 266 VAL   A O    
731  C  CB   . VAL   A 114 ? 0.1810 0.1829 0.1843 -0.0494 -0.0188 -0.0205 266 VAL   A CB   
732  C  CG1  . VAL   A 114 ? 0.1534 0.1539 0.1508 -0.0512 -0.0135 -0.0217 266 VAL   A CG1  
733  C  CG2  . VAL   A 114 ? 0.1764 0.1892 0.1881 -0.0436 -0.0252 -0.0221 266 VAL   A CG2  
734  N  N    . ILE   A 115 ? 0.1360 0.1199 0.1282 -0.0606 -0.0094 -0.0176 267 ILE   A N    
735  C  CA   . ILE   A 115 ? 0.1544 0.1266 0.1404 -0.0633 -0.0023 -0.0178 267 ILE   A CA   
736  C  C    . ILE   A 115 ? 0.1770 0.1547 0.1581 -0.0690 0.0022  -0.0213 267 ILE   A C    
737  O  O    . ILE   A 115 ? 0.2325 0.2020 0.2080 -0.0719 0.0094  -0.0236 267 ILE   A O    
738  C  CB   . ILE   A 115 ? 0.1619 0.1291 0.1503 -0.0605 -0.0040 -0.0146 267 ILE   A CB   
739  C  CG1  . ILE   A 115 ? 0.1210 0.0832 0.1138 -0.0524 -0.0064 -0.0114 267 ILE   A CG1  
740  C  CG2  . ILE   A 115 ? 0.1626 0.1222 0.1453 -0.0627 0.0032  -0.0160 267 ILE   A CG2  
741  C  CD1  . ILE   A 115 ? 0.1197 0.0823 0.1180 -0.0492 -0.0100 -0.0080 267 ILE   A CD1  
742  N  N    . MET   A 116 ? 0.2100 0.2016 0.1929 -0.0711 -0.0018 -0.0216 268 MET   A N    
743  C  CA   . MET   A 116 ? 0.2469 0.2476 0.2247 -0.0774 0.0020  -0.0258 268 MET   A CA   
744  C  C    . MET   A 116 ? 0.2299 0.2340 0.2054 -0.0807 0.0052  -0.0291 268 MET   A C    
745  O  O    . MET   A 116 ? 0.2406 0.2422 0.2104 -0.0863 0.0118  -0.0335 268 MET   A O    
746  C  CB   . MET   A 116 ? 0.2261 0.2451 0.2066 -0.0788 -0.0039 -0.0241 268 MET   A CB   
747  C  CG   . MET   A 116 ? 0.2300 0.2484 0.2108 -0.0787 -0.0055 -0.0210 268 MET   A CG   
748  S  SD   . MET   A 116 ? 0.2539 0.2956 0.2395 -0.0795 -0.0139 -0.0152 268 MET   A SD   
749  C  CE   . MET   A 116 ? 0.1815 0.2211 0.1654 -0.0815 -0.0133 -0.0115 268 MET   A CE   
750  N  N    . LEU   A 117 ? 0.2258 0.2361 0.2061 -0.0779 0.0008  -0.0276 269 LEU   A N    
751  C  CA   . LEU   A 117 ? 0.2667 0.2829 0.2454 -0.0816 0.0036  -0.0304 269 LEU   A CA   
752  C  C    . LEU   A 117 ? 0.2735 0.2723 0.2470 -0.0838 0.0111  -0.0308 269 LEU   A C    
753  O  O    . LEU   A 117 ? 0.2385 0.2355 0.2070 -0.0901 0.0175  -0.0340 269 LEU   A O    
754  C  CB   . LEU   A 117 ? 0.3160 0.3438 0.3016 -0.0772 -0.0030 -0.0292 269 LEU   A CB   
755  C  CG   . LEU   A 117 ? 0.3813 0.4215 0.3674 -0.0798 -0.0020 -0.0317 269 LEU   A CG   
756  C  CD1  . LEU   A 117 ? 0.4069 0.4562 0.3882 -0.0875 0.0032  -0.0351 269 LEU   A CD1  
757  C  CD2  . LEU   A 117 ? 0.3986 0.4557 0.3932 -0.0733 -0.0101 -0.0315 269 LEU   A CD2  
758  N  N    . ARG   A 118 ? 0.2640 0.2499 0.2387 -0.0790 0.0106  -0.0272 270 ARG   A N    
759  C  CA   . ARG   A 118 ? 0.2347 0.2045 0.2048 -0.0803 0.0177  -0.0256 270 ARG   A CA   
760  C  C    . ARG   A 118 ? 0.2327 0.1884 0.1980 -0.0818 0.0249  -0.0269 270 ARG   A C    
761  O  O    . ARG   A 118 ? 0.2401 0.1835 0.2016 -0.0841 0.0321  -0.0263 270 ARG   A O    
762  C  CB   . ARG   A 118 ? 0.2307 0.1922 0.2026 -0.0748 0.0155  -0.0211 270 ARG   A CB   
763  C  CG   . ARG   A 118 ? 0.2893 0.2405 0.2622 -0.0692 0.0146  -0.0186 270 ARG   A CG   
764  C  CD   . ARG   A 118 ? 0.3149 0.2699 0.2929 -0.0590 0.0081  -0.0145 270 ARG   A CD   
765  N  NE   . ARG   A 118 ? 0.3058 0.2588 0.2816 -0.0548 0.0106  -0.0107 270 ARG   A NE   
766  C  CZ   . ARG   A 118 ? 0.3292 0.2698 0.3014 -0.0509 0.0162  -0.0056 270 ARG   A CZ   
767  N  NH1  . ARG   A 118 ? 0.2581 0.1865 0.2290 -0.0505 0.0199  -0.0048 270 ARG   A NH1  
768  N  NH2  . ARG   A 118 ? 0.3201 0.2622 0.2901 -0.0467 0.0182  -0.0007 270 ARG   A NH2  
769  N  N    . SER   A 119 ? 0.2206 0.1782 0.1863 -0.0809 0.0234  -0.0287 271 SER   A N    
770  C  CA   . SER   A 119 ? 0.2740 0.2199 0.2354 -0.0829 0.0305  -0.0316 271 SER   A CA   
771  C  C    . SER   A 119 ? 0.2843 0.2325 0.2413 -0.0912 0.0364  -0.0377 271 SER   A C    
772  O  O    . SER   A 119 ? 0.3575 0.2927 0.3110 -0.0936 0.0439  -0.0408 271 SER   A O    
773  C  CB   . SER   A 119 ? 0.2871 0.2376 0.2493 -0.0817 0.0279  -0.0329 271 SER   A CB   
774  O  OG   . SER   A 119 ? 0.2749 0.2440 0.2373 -0.0861 0.0240  -0.0359 271 SER   A OG   
775  N  N    . ASN   A 120 ? 0.2861 0.2510 0.2437 -0.0957 0.0334  -0.0397 272 ASN   A N    
776  C  CA   . ASN   A 120 ? 0.2791 0.2492 0.2326 -0.1047 0.0387  -0.0461 272 ASN   A CA   
777  C  C    . ASN   A 120 ? 0.2949 0.2474 0.2455 -0.1077 0.0467  -0.0462 272 ASN   A C    
778  O  O    . ASN   A 120 ? 0.3001 0.2478 0.2470 -0.1149 0.0536  -0.0521 272 ASN   A O    
779  C  CB   . ASN   A 120 ? 0.2625 0.2557 0.2180 -0.1078 0.0336  -0.0471 272 ASN   A CB   
780  C  CG   . ASN   A 120 ? 0.2923 0.2954 0.2437 -0.1177 0.0386  -0.0543 272 ASN   A CG   
781  O  OD1  . ASN   A 120 ? 0.3140 0.3200 0.2644 -0.1225 0.0410  -0.0555 272 ASN   A OD1  
782  N  ND2  . ASN   A 120 ? 0.2777 0.2877 0.2266 -0.1217 0.0403  -0.0594 272 ASN   A ND2  
783  N  N    . GLN   A 121 ? 0.3161 0.2590 0.2684 -0.1028 0.0463  -0.0395 273 GLN   A N    
784  C  CA   . GLN   A 121 ? 0.3548 0.2802 0.3048 -0.1048 0.0541  -0.0372 273 GLN   A CA   
785  C  C    . GLN   A 121 ? 0.3892 0.2938 0.3372 -0.1030 0.0613  -0.0381 273 GLN   A C    
786  O  O    . GLN   A 121 ? 0.4303 0.3201 0.3764 -0.1065 0.0693  -0.0382 273 GLN   A O    
787  C  CB   . GLN   A 121 ? 0.4013 0.3233 0.3532 -0.0993 0.0520  -0.0285 273 GLN   A CB   
788  C  CG   . GLN   A 121 ? 0.4054 0.3085 0.3554 -0.0988 0.0599  -0.0224 273 GLN   A CG   
789  C  CD   . GLN   A 121 ? 0.4000 0.3069 0.3506 -0.0961 0.0584  -0.0140 273 GLN   A CD   
790  O  OE1  . GLN   A 121 ? 0.3447 0.2672 0.2974 -0.0947 0.0515  -0.0140 273 GLN   A OE1  
791  N  NE2  . GLN   A 121 ? 0.4097 0.3029 0.3584 -0.0954 0.0654  -0.0063 273 GLN   A NE2  
792  N  N    . SER   A 122 ? 0.3752 0.2785 0.3241 -0.0979 0.0593  -0.0389 274 SER   A N    
793  C  CA   . SER   A 122 ? 0.3900 0.2766 0.3373 -0.0967 0.0665  -0.0415 274 SER   A CA   
794  C  C    . SER   A 122 ? 0.4023 0.2963 0.3470 -0.1046 0.0694  -0.0518 274 SER   A C    
795  O  O    . SER   A 122 ? 0.4177 0.2982 0.3608 -0.1059 0.0770  -0.0562 274 SER   A O    
796  C  CB   . SER   A 122 ? 0.3618 0.2426 0.3113 -0.0868 0.0639  -0.0364 274 SER   A CB   
797  O  OG   . SER   A 122 ? 0.3730 0.2695 0.3237 -0.0869 0.0573  -0.0394 274 SER   A OG   
798  N  N    . PHE   A 123 ? 0.4134 0.3294 0.3578 -0.1098 0.0639  -0.0556 275 PHE   A N    
799  C  CA   . PHE   A 123 ? 0.4092 0.3366 0.3511 -0.1177 0.0663  -0.0649 275 PHE   A CA   
800  C  C    . PHE   A 123 ? 0.4958 0.4158 0.4346 -0.1274 0.0755  -0.0721 275 PHE   A C    
801  O  O    . PHE   A 123 ? 0.5067 0.4273 0.4452 -0.1313 0.0763  -0.0711 275 PHE   A O    
802  C  CB   . PHE   A 123 ? 0.3676 0.3219 0.3103 -0.1199 0.0581  -0.0653 275 PHE   A CB   
803  C  CG   . PHE   A 123 ? 0.3686 0.3387 0.3091 -0.1261 0.0589  -0.0726 275 PHE   A CG   
804  C  CD1  . PHE   A 123 ? 0.3693 0.3411 0.3102 -0.1226 0.0571  -0.0724 275 PHE   A CD1  
805  C  CD2  . PHE   A 123 ? 0.3510 0.3365 0.2891 -0.1361 0.0618  -0.0799 275 PHE   A CD2  
806  C  CE1  . PHE   A 123 ? 0.3278 0.3168 0.2667 -0.1290 0.0581  -0.0790 275 PHE   A CE1  
807  C  CE2  . PHE   A 123 ? 0.3710 0.3743 0.3073 -0.1422 0.0629  -0.0867 275 PHE   A CE2  
808  C  CZ   . PHE   A 123 ? 0.3656 0.3709 0.3022 -0.1386 0.0610  -0.0861 275 PHE   A CZ   
809  N  N    . THR   A 124 ? 0.5373 0.4501 0.4742 -0.1318 0.0828  -0.0799 276 THR   A N    
810  C  CA   . THR   A 124 ? 0.5932 0.4999 0.5276 -0.1424 0.0921  -0.0889 276 THR   A CA   
811  C  C    . THR   A 124 ? 0.6066 0.5347 0.5391 -0.1514 0.0929  -0.0992 276 THR   A C    
812  O  O    . THR   A 124 ? 0.5875 0.5214 0.5203 -0.1490 0.0916  -0.1012 276 THR   A O    
813  C  CB   . THR   A 124 ? 0.6244 0.5017 0.5592 -0.1404 0.1021  -0.0898 276 THR   A CB   
814  O  OG1  . THR   A 124 ? 0.6440 0.5154 0.5771 -0.1519 0.1116  -0.0999 276 THR   A OG1  
815  C  CG2  . THR   A 124 ? 0.6284 0.5011 0.5641 -0.1341 0.1028  -0.0908 276 THR   A CG2  
816  N  N    . MET   A 125 ? 0.6294 0.5709 0.5600 -0.1619 0.0950  -0.1057 277 MET   A N    
817  C  CA   . MET   A 125 ? 0.6868 0.6530 0.6159 -0.1709 0.0956  -0.1152 277 MET   A CA   
818  C  C    . MET   A 125 ? 0.7225 0.6791 0.6504 -0.1802 0.1068  -0.1273 277 MET   A C    
819  O  O    . MET   A 125 ? 0.7552 0.7332 0.6821 -0.1889 0.1084  -0.1365 277 MET   A O    
820  C  CB   . MET   A 125 ? 0.7127 0.7033 0.6406 -0.1778 0.0921  -0.1166 277 MET   A CB   
821  C  CG   . MET   A 125 ? 0.7046 0.7219 0.6340 -0.1723 0.0813  -0.1104 277 MET   A CG   
822  S  SD   . MET   A 125 ? 0.7385 0.7849 0.6673 -0.1791 0.0777  -0.1117 277 MET   A SD   
823  C  CE   . MET   A 125 ? 0.7743 0.7965 0.7024 -0.1813 0.0825  -0.1101 277 MET   A CE   
824  N  N    . ASP   A 126 ? 0.7364 0.6621 0.6651 -0.1784 0.1146  -0.1274 278 ASP   A N    
825  C  CA   . ASP   A 126 ? 0.7540 0.6668 0.6827 -0.1854 0.1255  -0.1388 278 ASP   A CA   
826  C  C    . ASP   A 126 ? 0.7318 0.6589 0.6611 -0.1845 0.1241  -0.1438 278 ASP   A C    
827  O  O    . ASP   A 126 ? 0.7457 0.6904 0.6744 -0.1949 0.1278  -0.1554 278 ASP   A O    
828  C  CB   . ASP   A 126 ? 0.8006 0.6768 0.7311 -0.1790 0.1326  -0.1346 278 ASP   A CB   
829  C  CG   . ASP   A 126 ? 0.8458 0.7081 0.7762 -0.1798 0.1339  -0.1283 278 ASP   A CG   
830  O  OD1  . ASP   A 126 ? 0.8484 0.7291 0.7771 -0.1866 0.1302  -0.1292 278 ASP   A OD1  
831  O  OD2  . ASP   A 126 ? 0.8772 0.7112 0.8093 -0.1733 0.1386  -0.1219 278 ASP   A OD2  
832  N  N    . ASP   A 127 ? 0.6981 0.6194 0.6287 -0.1725 0.1188  -0.1353 279 ASP   A N    
833  C  CA   . ASP   A 127 ? 0.7218 0.6559 0.6530 -0.1710 0.1169  -0.1387 279 ASP   A CA   
834  C  C    . ASP   A 127 ? 0.6955 0.6496 0.6269 -0.1636 0.1049  -0.1289 279 ASP   A C    
835  O  O    . ASP   A 127 ? 0.6768 0.6353 0.6089 -0.1589 0.1023  -0.1279 279 ASP   A O    
836  C  CB   . ASP   A 127 ? 0.7745 0.6819 0.7074 -0.1643 0.1235  -0.1396 279 ASP   A CB   
837  C  CG   . ASP   A 127 ? 0.8267 0.7065 0.7608 -0.1535 0.1237  -0.1284 279 ASP   A CG   
838  O  OD1  . ASP   A 127 ? 0.8346 0.7198 0.7686 -0.1475 0.1153  -0.1177 279 ASP   A OD1  
839  O  OD2  . ASP   A 127 ? 0.8713 0.7248 0.8068 -0.1509 0.1325  -0.1303 279 ASP   A OD2  
840  N  N    . MET   A 128 ? 0.6703 0.6361 0.6012 -0.1627 0.0978  -0.1221 280 MET   A N    
841  C  CA   . MET   A 128 ? 0.6216 0.6070 0.5532 -0.1564 0.0864  -0.1132 280 MET   A CA   
842  C  C    . MET   A 128 ? 0.5485 0.5187 0.4818 -0.1446 0.0825  -0.1045 280 MET   A C    
843  O  O    . MET   A 128 ? 0.5438 0.5268 0.4776 -0.1414 0.0769  -0.1019 280 MET   A O    
844  C  CB   . MET   A 128 ? 0.6315 0.6486 0.5625 -0.1628 0.0838  -0.1185 280 MET   A CB   
845  C  CG   . MET   A 128 ? 0.6338 0.6700 0.5635 -0.1748 0.0877  -0.1274 280 MET   A CG   
846  S  SD   . MET   A 128 ? 0.6182 0.6708 0.5481 -0.1736 0.0798  -0.1197 280 MET   A SD   
847  C  CE   . MET   A 128 ? 0.6342 0.7288 0.5650 -0.1756 0.0726  -0.1187 280 MET   A CE   
848  N  N    . SER   A 129 ? 0.4862 0.4299 0.4206 -0.1383 0.0856  -0.0999 281 SER   A N    
849  C  CA   . SER   A 129 ? 0.4631 0.3922 0.3995 -0.1273 0.0831  -0.0921 281 SER   A CA   
850  C  C    . SER   A 129 ? 0.4897 0.4076 0.4280 -0.1197 0.0789  -0.0817 281 SER   A C    
851  O  O    . SER   A 129 ? 0.4222 0.3410 0.3602 -0.1233 0.0791  -0.0811 281 SER   A O    
852  C  CB   . SER   A 129 ? 0.5142 0.4217 0.4507 -0.1257 0.0928  -0.0971 281 SER   A CB   
853  O  OG   . SER   A 129 ? 0.5811 0.4658 0.5179 -0.1253 0.1001  -0.0967 281 SER   A OG   
854  N  N    . TRP   A 130 ? 0.4124 0.3216 0.3531 -0.1098 0.0753  -0.0739 282 TRP   A N    
855  C  CA   . TRP   A 130 ? 0.3805 0.2793 0.3238 -0.1018 0.0719  -0.0640 282 TRP   A CA   
856  C  C    . TRP   A 130 ? 0.4432 0.3162 0.3867 -0.0966 0.0804  -0.0623 282 TRP   A C    
857  O  O    . TRP   A 130 ? 0.4932 0.3580 0.4378 -0.0903 0.0823  -0.0611 282 TRP   A O    
858  C  CB   . TRP   A 130 ? 0.3200 0.2279 0.2664 -0.0946 0.0623  -0.0565 282 TRP   A CB   
859  C  CG   . TRP   A 130 ? 0.3007 0.2318 0.2481 -0.0978 0.0535  -0.0558 282 TRP   A CG   
860  C  CD1  . TRP   A 130 ? 0.2939 0.2327 0.2436 -0.0967 0.0476  -0.0511 282 TRP   A CD1  
861  C  CD2  . TRP   A 130 ? 0.3491 0.2993 0.2955 -0.1020 0.0498  -0.0593 282 TRP   A CD2  
862  N  NE1  . TRP   A 130 ? 0.3037 0.2640 0.2545 -0.0991 0.0407  -0.0513 282 TRP   A NE1  
863  C  CE2  . TRP   A 130 ? 0.2967 0.2647 0.2454 -0.1024 0.0417  -0.0557 282 TRP   A CE2  
864  C  CE3  . TRP   A 130 ? 0.3397 0.2949 0.2836 -0.1056 0.0529  -0.0652 282 TRP   A CE3  
865  C  CZ2  . TRP   A 130 ? 0.2890 0.2789 0.2376 -0.1056 0.0365  -0.0563 282 TRP   A CZ2  
866  C  CZ3  . TRP   A 130 ? 0.3041 0.2829 0.2473 -0.1098 0.0474  -0.0662 282 TRP   A CZ3  
867  C  CH2  . TRP   A 130 ? 0.3177 0.3133 0.2632 -0.1094 0.0392  -0.0611 282 TRP   A CH2  
868  N  N    . ASP   A 131 ? 0.4867 0.3473 0.4295 -0.0990 0.0861  -0.0619 283 ASP   A N    
869  C  CA   . ASP   A 131 ? 0.5623 0.3976 0.5056 -0.0940 0.0950  -0.0593 283 ASP   A CA   
870  C  C    . ASP   A 131 ? 0.5336 0.3619 0.4792 -0.0838 0.0914  -0.0467 283 ASP   A C    
871  O  O    . ASP   A 131 ? 0.5600 0.3921 0.5058 -0.0853 0.0883  -0.0421 283 ASP   A O    
872  C  CB   . ASP   A 131 ? 0.6325 0.4570 0.5741 -0.1026 0.1036  -0.0649 283 ASP   A CB   
873  C  CG   . ASP   A 131 ? 0.7187 0.5157 0.6612 -0.0977 0.1140  -0.0629 283 ASP   A CG   
874  O  OD1  . ASP   A 131 ? 0.7483 0.5351 0.6927 -0.0860 0.1139  -0.0543 283 ASP   A OD1  
875  O  OD2  . ASP   A 131 ? 0.7849 0.5706 0.7265 -0.1054 0.1227  -0.0700 283 ASP   A OD2  
876  N  N    . CYS   A 132 ? 0.5226 0.3416 0.4700 -0.0735 0.0925  -0.0414 284 CYS   A N    
877  C  CA   . CYS   A 132 ? 0.4928 0.3088 0.4423 -0.0636 0.0887  -0.0295 284 CYS   A CA   
878  C  C    . CYS   A 132 ? 0.5320 0.3261 0.4822 -0.0545 0.0974  -0.0230 284 CYS   A C    
879  O  O    . CYS   A 132 ? 0.5629 0.3542 0.5151 -0.0434 0.0965  -0.0154 284 CYS   A O    
880  C  CB   . CYS   A 132 ? 0.4690 0.2979 0.4207 -0.0582 0.0805  -0.0270 284 CYS   A CB   
881  S  SG   . CYS   A 132 ? 0.4436 0.2985 0.3960 -0.0658 0.0689  -0.0304 284 CYS   A SG   
882  N  N    . GLY   A 133 ? 0.5632 0.3420 0.5121 -0.0588 0.1061  -0.0256 285 GLY   A N    
883  C  CA   . GLY   A 133 ? 0.6110 0.3687 0.5609 -0.0502 0.1143  -0.0173 285 GLY   A CA   
884  C  C    . GLY   A 133 ? 0.6610 0.4008 0.6114 -0.0488 0.1247  -0.0233 285 GLY   A C    
885  O  O    . GLY   A 133 ? 0.6800 0.4000 0.6310 -0.0460 0.1333  -0.0191 285 GLY   A O    
886  N  N    . SER   A 134 ? 0.6668 0.4128 0.6173 -0.0505 0.1244  -0.0325 286 SER   A N    
887  C  CA   . SER   A 134 ? 0.6627 0.3927 0.6142 -0.0482 0.1343  -0.0387 286 SER   A CA   
888  C  C    . SER   A 134 ? 0.6555 0.3985 0.6058 -0.0565 0.1329  -0.0523 286 SER   A C    
889  O  O    . SER   A 134 ? 0.6412 0.4051 0.5900 -0.0628 0.1242  -0.0552 286 SER   A O    
890  C  CB   . SER   A 134 ? 0.6636 0.3840 0.6181 -0.0315 0.1369  -0.0286 286 SER   A CB   
891  O  OG   . SER   A 134 ? 0.6713 0.4059 0.6267 -0.0270 0.1313  -0.0301 286 SER   A OG   
892  N  N    . GLN   A 135 ? 0.6805 0.4113 0.6315 -0.0563 0.1417  -0.0605 287 GLN   A N    
893  C  CA   . GLN   A 135 ? 0.7126 0.4563 0.6625 -0.0638 0.1412  -0.0737 287 GLN   A CA   
894  C  C    . GLN   A 135 ? 0.6715 0.4297 0.6221 -0.0564 0.1343  -0.0705 287 GLN   A C    
895  O  O    . GLN   A 135 ? 0.5922 0.3700 0.5411 -0.0638 0.1290  -0.0776 287 GLN   A O    
896  C  CB   . GLN   A 135 ? 0.8095 0.5359 0.7605 -0.0646 0.1527  -0.0836 287 GLN   A CB   
897  C  CG   . GLN   A 135 ? 0.8719 0.6126 0.8215 -0.0745 0.1534  -0.0992 287 GLN   A CG   
898  C  CD   . GLN   A 135 ? 0.9482 0.6753 0.9000 -0.0685 0.1622  -0.1066 287 GLN   A CD   
899  O  OE1  . GLN   A 135 ? 0.9958 0.7109 0.9480 -0.0749 0.1710  -0.1173 287 GLN   A OE1  
900  N  NE2  . GLN   A 135 ? 0.9475 0.6769 0.9010 -0.0558 0.1602  -0.1016 287 GLN   A NE2  
901  N  N    . ASP   A 136 ? 0.7136 0.4634 0.6670 -0.0417 0.1346  -0.0596 288 ASP   A N    
902  C  CA   . ASP   A 136 ? 0.6906 0.4539 0.6453 -0.0344 0.1282  -0.0557 288 ASP   A CA   
903  C  C    . ASP   A 136 ? 0.6040 0.3866 0.5571 -0.0408 0.1169  -0.0528 288 ASP   A C    
904  O  O    . ASP   A 136 ? 0.5545 0.3533 0.5069 -0.0447 0.1116  -0.0573 288 ASP   A O    
905  C  CB   . ASP   A 136 ? 0.7751 0.5283 0.7334 -0.0171 0.1300  -0.0427 288 ASP   A CB   
906  C  CG   . ASP   A 136 ? 0.8575 0.6003 0.8185 -0.0073 0.1385  -0.0460 288 ASP   A CG   
907  O  OD1  . ASP   A 136 ? 0.8807 0.6291 0.8406 -0.0128 0.1407  -0.0585 288 ASP   A OD1  
908  O  OD2  . ASP   A 136 ? 0.8890 0.6199 0.8531 0.0063  0.1428  -0.0360 288 ASP   A OD2  
909  N  N    . TYR   A 137 ? 0.5906 0.3723 0.5435 -0.0419 0.1133  -0.0453 289 TYR   A N    
910  C  CA   . TYR   A 137 ? 0.5782 0.3773 0.5306 -0.0460 0.1025  -0.0414 289 TYR   A CA   
911  C  C    . TYR   A 137 ? 0.5758 0.3852 0.5254 -0.0598 0.1002  -0.0491 289 TYR   A C    
912  O  O    . TYR   A 137 ? 0.5735 0.3880 0.5227 -0.0629 0.0956  -0.0450 289 TYR   A O    
913  C  CB   . TYR   A 137 ? 0.5714 0.3662 0.5257 -0.0372 0.0995  -0.0282 289 TYR   A CB   
914  C  CG   . TYR   A 137 ? 0.5983 0.3840 0.5555 -0.0222 0.1030  -0.0197 289 TYR   A CG   
915  C  CD1  . TYR   A 137 ? 0.6121 0.3859 0.5705 -0.0126 0.1071  -0.0090 289 TYR   A CD1  
916  C  CD2  . TYR   A 137 ? 0.5666 0.3575 0.5256 -0.0171 0.1026  -0.0218 289 TYR   A CD2  
917  C  CE1  . TYR   A 137 ? 0.6278 0.3973 0.5893 0.0025  0.1100  -0.0003 289 TYR   A CE1  
918  C  CE2  . TYR   A 137 ? 0.5795 0.3654 0.5421 -0.0021 0.1058  -0.0139 289 TYR   A CE2  
919  C  CZ   . TYR   A 137 ? 0.6021 0.3784 0.5659 0.0081  0.1092  -0.0028 289 TYR   A CZ   
920  O  OH   . TYR   A 137 ? 0.5762 0.3520 0.5440 0.0242  0.1118  0.0061  289 TYR   A OH   
921  N  N    . LYS   A 138 ? 0.5312 0.3450 0.4789 -0.0681 0.1040  -0.0607 290 LYS   A N    
922  C  CA   . LYS   A 138 ? 0.5085 0.3367 0.4536 -0.0811 0.1020  -0.0689 290 LYS   A CA   
923  C  C    . LYS   A 138 ? 0.4993 0.3479 0.4432 -0.0859 0.0972  -0.0751 290 LYS   A C    
924  O  O    . LYS   A 138 ? 0.5619 0.4085 0.5057 -0.0850 0.1018  -0.0812 290 LYS   A O    
925  C  CB   . LYS   A 138 ? 0.5952 0.4107 0.5391 -0.0879 0.1123  -0.0776 290 LYS   A CB   
926  C  CG   . LYS   A 138 ? 0.6356 0.4665 0.5771 -0.1013 0.1112  -0.0858 290 LYS   A CG   
927  C  CD   . LYS   A 138 ? 0.7154 0.5298 0.6563 -0.1070 0.1202  -0.0898 290 LYS   A CD   
928  C  CE   . LYS   A 138 ? 0.7534 0.5794 0.6924 -0.1208 0.1242  -0.1036 290 LYS   A CE   
929  N  NZ   . LYS   A 138 ? 0.8020 0.6095 0.7418 -0.1233 0.1360  -0.1130 290 LYS   A NZ   
930  N  N    . TYR   A 139 ? 0.4475 0.3165 0.3908 -0.0906 0.0879  -0.0733 291 TYR   A N    
931  C  CA   . TYR   A 139 ? 0.4056 0.2951 0.3481 -0.0936 0.0815  -0.0755 291 TYR   A CA   
932  C  C    . TYR   A 139 ? 0.4049 0.3154 0.3449 -0.1048 0.0797  -0.0825 291 TYR   A C    
933  O  O    . TYR   A 139 ? 0.4190 0.3366 0.3590 -0.1077 0.0758  -0.0800 291 TYR   A O    
934  C  CB   . TYR   A 139 ? 0.3821 0.2781 0.3275 -0.0874 0.0715  -0.0650 291 TYR   A CB   
935  C  CG   . TYR   A 139 ? 0.3715 0.2488 0.3199 -0.0764 0.0730  -0.0565 291 TYR   A CG   
936  C  CD1  . TYR   A 139 ? 0.3864 0.2590 0.3369 -0.0723 0.0698  -0.0485 291 TYR   A CD1  
937  C  CD2  . TYR   A 139 ? 0.3728 0.2388 0.3220 -0.0697 0.0781  -0.0567 291 TYR   A CD2  
938  C  CE1  . TYR   A 139 ? 0.3785 0.2371 0.3315 -0.0621 0.0713  -0.0402 291 TYR   A CE1  
939  C  CE2  . TYR   A 139 ? 0.3482 0.1994 0.3005 -0.0584 0.0799  -0.0480 291 TYR   A CE2  
940  C  CZ   . TYR   A 139 ? 0.3672 0.2155 0.3212 -0.0548 0.0762  -0.0394 291 TYR   A CZ   
941  O  OH   . TYR   A 139 ? 0.3387 0.1755 0.2954 -0.0434 0.0780  -0.0300 291 TYR   A OH   
942  N  N    . ASP   A 140 ? 0.3865 0.3087 0.3245 -0.1109 0.0826  -0.0915 292 ASP   A N    
943  C  CA   . ASP   A 140 ? 0.4644 0.4099 0.4003 -0.1216 0.0815  -0.0985 292 ASP   A CA   
944  C  C    . ASP   A 140 ? 0.4213 0.3927 0.3562 -0.1232 0.0733  -0.0963 292 ASP   A C    
945  O  O    . ASP   A 140 ? 0.3900 0.3601 0.3257 -0.1168 0.0678  -0.0891 292 ASP   A O    
946  C  CB   . ASP   A 140 ? 0.5949 0.5368 0.5299 -0.1288 0.0918  -0.1112 292 ASP   A CB   
947  C  CG   . ASP   A 140 ? 0.7077 0.6408 0.6429 -0.1247 0.0968  -0.1157 292 ASP   A CG   
948  O  OD1  . ASP   A 140 ? 0.7721 0.6820 0.7085 -0.1219 0.1057  -0.1197 292 ASP   A OD1  
949  O  OD2  . ASP   A 140 ? 0.7257 0.6754 0.6598 -0.1240 0.0919  -0.1151 292 ASP   A OD2  
950  N  N    . VAL   A 141 ? 0.4278 0.4241 0.3610 -0.1321 0.0726  -0.1023 293 VAL   A N    
951  C  CA   . VAL   A 141 ? 0.4226 0.4474 0.3548 -0.1340 0.0646  -0.0988 293 VAL   A CA   
952  C  C    . VAL   A 141 ? 0.4189 0.4434 0.3499 -0.1307 0.0646  -0.0990 293 VAL   A C    
953  O  O    . VAL   A 141 ? 0.3747 0.4102 0.3051 -0.1277 0.0566  -0.0908 293 VAL   A O    
954  C  CB   . VAL   A 141 ? 0.4451 0.4981 0.3764 -0.1440 0.0657  -0.1061 293 VAL   A CB   
955  C  CG1  . VAL   A 141 ? 0.5104 0.5596 0.4415 -0.1503 0.0758  -0.1196 293 VAL   A CG1  
956  C  CG2  . VAL   A 141 ? 0.3750 0.4598 0.3056 -0.1449 0.0573  -0.1004 293 VAL   A CG2  
957  N  N    . THR   A 142 ? 0.4367 0.4485 0.3672 -0.1311 0.0736  -0.1082 294 THR   A N    
958  C  CA   . THR   A 142 ? 0.4422 0.4571 0.3707 -0.1279 0.0745  -0.1101 294 THR   A CA   
959  C  C    . THR   A 142 ? 0.3817 0.3734 0.3109 -0.1178 0.0743  -0.1034 294 THR   A C    
960  O  O    . THR   A 142 ? 0.3667 0.3659 0.2930 -0.1143 0.0727  -0.1016 294 THR   A O    
961  C  CB   . THR   A 142 ? 0.5014 0.5133 0.4299 -0.1309 0.0842  -0.1231 294 THR   A CB   
962  O  OG1  . THR   A 142 ? 0.5994 0.5776 0.5301 -0.1246 0.0925  -0.1254 294 THR   A OG1  
963  C  CG2  . THR   A 142 ? 0.4779 0.5071 0.4072 -0.1417 0.0861  -0.1312 294 THR   A CG2  
964  N  N    . ASP   A 143 ? 0.3891 0.3554 0.3216 -0.1127 0.0763  -0.0991 295 ASP   A N    
965  C  CA   . ASP   A 143 ? 0.3990 0.3466 0.3338 -0.1030 0.0749  -0.0911 295 ASP   A CA   
966  C  C    . ASP   A 143 ? 0.3598 0.3239 0.2975 -0.1012 0.0628  -0.0787 295 ASP   A C    
967  O  O    . ASP   A 143 ? 0.3060 0.2730 0.2486 -0.0919 0.0594  -0.0688 295 ASP   A O    
968  C  CB   . ASP   A 143 ? 0.4217 0.3443 0.3601 -0.0972 0.0784  -0.0865 295 ASP   A CB   
969  C  CG   . ASP   A 143 ? 0.4997 0.4020 0.4386 -0.0940 0.0900  -0.0932 295 ASP   A CG   
970  O  OD1  . ASP   A 143 ? 0.5172 0.4166 0.4555 -0.0899 0.0951  -0.0981 295 ASP   A OD1  
971  O  OD2  . ASP   A 143 ? 0.5284 0.4182 0.4683 -0.0951 0.0941  -0.0934 295 ASP   A OD2  
972  N  N    . VAL   A 144 ? 0.3551 0.3328 0.2923 -0.1078 0.0560  -0.0767 296 VAL   A N    
973  C  CA   . VAL   A 144 ? 0.3202 0.3133 0.2627 -0.1039 0.0446  -0.0630 296 VAL   A CA   
974  C  C    . VAL   A 144 ? 0.3376 0.3551 0.2797 -0.1039 0.0409  -0.0587 296 VAL   A C    
975  O  O    . VAL   A 144 ? 0.2796 0.3020 0.2276 -0.0971 0.0348  -0.0462 296 VAL   A O    
976  C  CB   . VAL   A 144 ? 0.2835 0.2861 0.2262 -0.1084 0.0391  -0.0614 296 VAL   A CB   
977  C  CG1  . VAL   A 144 ? 0.2481 0.2642 0.1968 -0.1049 0.0280  -0.0486 296 VAL   A CG1  
978  C  CG2  . VAL   A 144 ? 0.2902 0.2720 0.2344 -0.1039 0.0428  -0.0615 296 VAL   A CG2  
979  N  N    . SER   A 145 ? 0.3548 0.3887 0.2898 -0.1122 0.0450  -0.0690 297 SER   A N    
980  C  CA   . SER   A 145 ? 0.4143 0.4730 0.3480 -0.1121 0.0426  -0.0645 297 SER   A CA   
981  C  C    . SER   A 145 ? 0.3880 0.4381 0.3252 -0.1035 0.0461  -0.0606 297 SER   A C    
982  O  O    . SER   A 145 ? 0.3568 0.4219 0.2975 -0.1002 0.0413  -0.0494 297 SER   A O    
983  C  CB   . SER   A 145 ? 0.4507 0.5299 0.3752 -0.1228 0.0475  -0.0786 297 SER   A CB   
984  O  OG   . SER   A 145 ? 0.4821 0.5447 0.4029 -0.1242 0.0587  -0.0939 297 SER   A OG   
985  N  N    . LYS   A 146 ? 0.3635 0.3896 0.3007 -0.0995 0.0546  -0.0686 298 LYS   A N    
986  C  CA   . LYS   A 146 ? 0.3339 0.3525 0.2755 -0.0899 0.0580  -0.0647 298 LYS   A CA   
987  C  C    . LYS   A 146 ? 0.3182 0.3299 0.2690 -0.0812 0.0508  -0.0496 298 LYS   A C    
988  O  O    . LYS   A 146 ? 0.3244 0.3307 0.2798 -0.0730 0.0531  -0.0460 298 LYS   A O    
989  C  CB   . LYS   A 146 ? 0.4374 0.4315 0.3771 -0.0864 0.0694  -0.0766 298 LYS   A CB   
990  C  CG   . LYS   A 146 ? 0.5321 0.5306 0.4636 -0.0943 0.0787  -0.0943 298 LYS   A CG   
991  C  CD   . LYS   A 146 ? 0.6292 0.6040 0.5611 -0.0871 0.0906  -0.1035 298 LYS   A CD   
992  C  CE   . LYS   A 146 ? 0.7170 0.6810 0.6453 -0.0949 0.0990  -0.1195 298 LYS   A CE   
993  N  NZ   . LYS   A 146 ? 0.7445 0.6852 0.6760 -0.0963 0.0992  -0.1167 298 LYS   A NZ   
994  N  N    . ALA   A 147 ? 0.2597 0.2722 0.2135 -0.0828 0.0424  -0.0417 299 ALA   A N    
995  C  CA   . ALA   A 147 ? 0.2170 0.2280 0.1797 -0.0763 0.0347  -0.0284 299 ALA   A CA   
996  C  C    . ALA   A 147 ? 0.2642 0.2960 0.2296 -0.0796 0.0267  -0.0184 299 ALA   A C    
997  O  O    . ALA   A 147 ? 0.2447 0.2750 0.2180 -0.0759 0.0201  -0.0080 299 ALA   A O    
998  C  CB   . ALA   A 147 ? 0.1892 0.1827 0.1547 -0.0737 0.0319  -0.0268 299 ALA   A CB   
999  N  N    . GLY   A 148 ? 0.2877 0.3391 0.2468 -0.0864 0.0274  -0.0212 300 GLY   A N    
1000 C  CA   . GLY   A 148 ? 0.2884 0.3614 0.2495 -0.0887 0.0210  -0.0099 300 GLY   A CA   
1001 C  C    . GLY   A 148 ? 0.2921 0.3781 0.2505 -0.0936 0.0157  -0.0077 300 GLY   A C    
1002 O  O    . GLY   A 148 ? 0.3081 0.4132 0.2677 -0.0948 0.0108  0.0030  300 GLY   A O    
1003 N  N    . HIS   A 149 ? 0.2328 0.3106 0.1880 -0.0963 0.0164  -0.0163 301 HIS   A N    
1004 C  CA   . HIS   A 149 ? 0.2874 0.3797 0.2416 -0.0998 0.0106  -0.0133 301 HIS   A CA   
1005 C  C    . HIS   A 149 ? 0.2837 0.3992 0.2281 -0.1088 0.0139  -0.0231 301 HIS   A C    
1006 O  O    . HIS   A 149 ? 0.2823 0.3949 0.2203 -0.1132 0.0219  -0.0367 301 HIS   A O    
1007 C  CB   . HIS   A 149 ? 0.2467 0.3218 0.2039 -0.0984 0.0089  -0.0164 301 HIS   A CB   
1008 C  CG   . HIS   A 149 ? 0.2163 0.2743 0.1829 -0.0902 0.0042  -0.0069 301 HIS   A CG   
1009 N  ND1  . HIS   A 149 ? 0.2215 0.2859 0.1954 -0.0861 -0.0032 0.0062  301 HIS   A ND1  
1010 C  CD2  . HIS   A 149 ? 0.1856 0.2213 0.1557 -0.0854 0.0062  -0.0090 301 HIS   A CD2  
1011 C  CE1  . HIS   A 149 ? 0.1592 0.2059 0.1409 -0.0801 -0.0055 0.0099  301 HIS   A CE1  
1012 N  NE2  . HIS   A 149 ? 0.2099 0.2410 0.1891 -0.0795 -0.0002 0.0011  301 HIS   A NE2  
1013 N  N    . THR   A 150 ? 0.2803 0.4198 0.2241 -0.1109 0.0078  -0.0162 302 THR   A N    
1014 C  CA   . THR   A 150 ? 0.2949 0.4638 0.2298 -0.1196 0.0092  -0.0239 302 THR   A CA   
1015 C  C    . THR   A 150 ? 0.2699 0.4425 0.2036 -0.1245 0.0078  -0.0318 302 THR   A C    
1016 O  O    . THR   A 150 ? 0.2578 0.4123 0.1973 -0.1208 0.0051  -0.0295 302 THR   A O    
1017 C  CB   . THR   A 150 ? 0.3132 0.5122 0.2481 -0.1179 0.0032  -0.0086 302 THR   A CB   
1018 O  OG1  . THR   A 150 ? 0.3229 0.5225 0.2656 -0.1119 -0.0050 0.0053  302 THR   A OG1  
1019 C  CG2  . THR   A 150 ? 0.1790 0.3746 0.1166 -0.1136 0.0047  0.0009  302 THR   A CG2  
1020 N  N    . LEU   A 151 ? 0.2529 0.4475 0.1854 -0.1295 0.0120  -0.0385 303 LEU   A N    
1021 C  CA   . LEU   A 151 ? 0.2116 0.4106 0.1466 -0.1314 0.0133  -0.0430 303 LEU   A CA   
1022 C  C    . LEU   A 151 ? 0.2000 0.4104 0.1396 -0.1250 0.0042  -0.0288 303 LEU   A C    
1023 O  O    . LEU   A 151 ? 0.2204 0.4292 0.1622 -0.1246 0.0043  -0.0314 303 LEU   A O    
1024 C  CB   . LEU   A 151 ? 0.2766 0.5013 0.2117 -0.1391 0.0186  -0.0526 303 LEU   A CB   
1025 C  CG   . LEU   A 151 ? 0.3209 0.5331 0.2538 -0.1461 0.0287  -0.0696 303 LEU   A CG   
1026 C  CD1  . LEU   A 151 ? 0.3479 0.5852 0.2828 -0.1544 0.0330  -0.0790 303 LEU   A CD1  
1027 C  CD2  . LEU   A 151 ? 0.2928 0.4671 0.2246 -0.1446 0.0338  -0.0759 303 LEU   A CD2  
1028 N  N    . GLU   A 152 ? 0.1768 0.3987 0.1188 -0.1196 -0.0032 -0.0132 304 GLU   A N    
1029 C  CA   . GLU   A 152 ? 0.2337 0.4615 0.1822 -0.1117 -0.0116 0.0014  304 GLU   A CA   
1030 C  C    . GLU   A 152 ? 0.2746 0.4755 0.2276 -0.1081 -0.0138 -0.0007 304 GLU   A C    
1031 O  O    . GLU   A 152 ? 0.2820 0.4881 0.2401 -0.1034 -0.0178 0.0039  304 GLU   A O    
1032 C  CB   . GLU   A 152 ? 0.3070 0.5411 0.2585 -0.1056 -0.0181 0.0198  304 GLU   A CB   
1033 C  CG   . GLU   A 152 ? 0.4004 0.6667 0.3523 -0.1055 -0.0179 0.0280  304 GLU   A CG   
1034 C  CD   . GLU   A 152 ? 0.5248 0.8108 0.4833 -0.0991 -0.0224 0.0387  304 GLU   A CD   
1035 O  OE1  . GLU   A 152 ? 0.5401 0.8158 0.5018 -0.0955 -0.0249 0.0375  304 GLU   A OE1  
1036 O  OE2  . GLU   A 152 ? 0.5827 0.8953 0.5437 -0.0972 -0.0232 0.0483  304 GLU   A OE2  
1037 N  N    . LEU   A 153 ? 0.2358 0.4091 0.1884 -0.1097 -0.0107 -0.0076 305 LEU   A N    
1038 C  CA   . LEU   A 153 ? 0.1926 0.3398 0.1503 -0.1064 -0.0108 -0.0107 305 LEU   A CA   
1039 C  C    . LEU   A 153 ? 0.2127 0.3469 0.1647 -0.1111 -0.0018 -0.0257 305 LEU   A C    
1040 O  O    . LEU   A 153 ? 0.2494 0.3780 0.2037 -0.1094 -0.0016 -0.0280 305 LEU   A O    
1041 C  CB   . LEU   A 153 ? 0.1708 0.2911 0.1339 -0.1004 -0.0106 -0.0055 305 LEU   A CB   
1042 C  CG   . LEU   A 153 ? 0.1807 0.2736 0.1476 -0.0974 -0.0088 -0.0102 305 LEU   A CG   
1043 C  CD1  . LEU   A 153 ? 0.1523 0.2483 0.1257 -0.0927 -0.0149 -0.0054 305 LEU   A CD1  
1044 C  CD2  . LEU   A 153 ? 0.1985 0.2686 0.1699 -0.0910 -0.0077 -0.0056 305 LEU   A CD2  
1045 N  N    . ILE   A 154 ? 0.2207 0.3505 0.1662 -0.1168 0.0060  -0.0356 306 ILE   A N    
1046 C  CA   . ILE   A 154 ? 0.2357 0.3462 0.1781 -0.1200 0.0151  -0.0479 306 ILE   A CA   
1047 C  C    . ILE   A 154 ? 0.2582 0.3843 0.1995 -0.1249 0.0181  -0.0537 306 ILE   A C    
1048 O  O    . ILE   A 154 ? 0.2870 0.3992 0.2289 -0.1253 0.0217  -0.0580 306 ILE   A O    
1049 C  CB   . ILE   A 154 ? 0.2769 0.3791 0.2146 -0.1242 0.0230  -0.0568 306 ILE   A CB   
1050 C  CG1  . ILE   A 154 ? 0.2679 0.3532 0.2079 -0.1194 0.0207  -0.0514 306 ILE   A CG1  
1051 C  CG2  . ILE   A 154 ? 0.3170 0.4011 0.2530 -0.1277 0.0330  -0.0684 306 ILE   A CG2  
1052 C  CD1  . ILE   A 154 ? 0.1912 0.2784 0.1264 -0.1232 0.0262  -0.0581 306 ILE   A CD1  
1053 N  N    . GLU   A 155 ? 0.2617 0.4185 0.2019 -0.1290 0.0170  -0.0532 307 GLU   A N    
1054 C  CA   . GLU   A 155 ? 0.2674 0.4423 0.2078 -0.1345 0.0202  -0.0590 307 GLU   A CA   
1055 C  C    . GLU   A 155 ? 0.2381 0.4126 0.1824 -0.1297 0.0153  -0.0535 307 GLU   A C    
1056 O  O    . GLU   A 155 ? 0.2896 0.4570 0.2334 -0.1335 0.0202  -0.0606 307 GLU   A O    
1057 C  CB   . GLU   A 155 ? 0.3213 0.5329 0.2617 -0.1385 0.0191  -0.0578 307 GLU   A CB   
1058 C  CG   . GLU   A 155 ? 0.4485 0.6819 0.3894 -0.1466 0.0240  -0.0666 307 GLU   A CG   
1059 C  CD   . GLU   A 155 ? 0.5404 0.7972 0.4849 -0.1427 0.0178  -0.0582 307 GLU   A CD   
1060 O  OE1  . GLU   A 155 ? 0.5971 0.8772 0.5423 -0.1491 0.0212  -0.0643 307 GLU   A OE1  
1061 O  OE2  . GLU   A 155 ? 0.5623 0.8152 0.5097 -0.1332 0.0098  -0.0459 307 GLU   A OE2  
1062 N  N    . PRO   A 156 ? 0.2343 0.4162 0.1833 -0.1217 0.0060  -0.0412 308 PRO   A N    
1063 C  CA   . PRO   A 156 ? 0.2449 0.4239 0.1990 -0.1167 0.0020  -0.0375 308 PRO   A CA   
1064 C  C    . PRO   A 156 ? 0.2589 0.4058 0.2138 -0.1148 0.0045  -0.0409 308 PRO   A C    
1065 O  O    . PRO   A 156 ? 0.2359 0.3806 0.1930 -0.1141 0.0049  -0.0424 308 PRO   A O    
1066 C  CB   . PRO   A 156 ? 0.2738 0.4643 0.2341 -0.1078 -0.0080 -0.0233 308 PRO   A CB   
1067 C  CG   . PRO   A 156 ? 0.2318 0.4418 0.1893 -0.1096 -0.0087 -0.0189 308 PRO   A CG   
1068 C  CD   . PRO   A 156 ? 0.1978 0.3939 0.1486 -0.1170 -0.0009 -0.0296 308 PRO   A CD   
1069 N  N    . LEU   A 157 ? 0.2632 0.3871 0.2165 -0.1136 0.0065  -0.0416 309 LEU   A N    
1070 C  CA   . LEU   A 157 ? 0.2412 0.3363 0.1956 -0.1107 0.0094  -0.0436 309 LEU   A CA   
1071 C  C    . LEU   A 157 ? 0.2610 0.3479 0.2111 -0.1171 0.0185  -0.0535 309 LEU   A C    
1072 O  O    . LEU   A 157 ? 0.2670 0.3426 0.2186 -0.1157 0.0199  -0.0539 309 LEU   A O    
1073 C  CB   . LEU   A 157 ? 0.2623 0.3376 0.2168 -0.1075 0.0098  -0.0416 309 LEU   A CB   
1074 C  CG   . LEU   A 157 ? 0.2799 0.3271 0.2357 -0.1036 0.0137  -0.0428 309 LEU   A CG   
1075 C  CD1  . LEU   A 157 ? 0.2159 0.2607 0.1779 -0.0979 0.0083  -0.0373 309 LEU   A CD1  
1076 C  CD2  . LEU   A 157 ? 0.2619 0.2928 0.2182 -0.1003 0.0147  -0.0407 309 LEU   A CD2  
1077 N  N    . ILE   A 158 ? 0.2821 0.3754 0.2270 -0.1246 0.0251  -0.0615 310 ILE   A N    
1078 C  CA   . ILE   A 158 ? 0.3031 0.3884 0.2447 -0.1318 0.0344  -0.0713 310 ILE   A CA   
1079 C  C    . ILE   A 158 ? 0.3243 0.4272 0.2668 -0.1360 0.0340  -0.0730 310 ILE   A C    
1080 O  O    . ILE   A 158 ? 0.3394 0.4306 0.2811 -0.1385 0.0383  -0.0763 310 ILE   A O    
1081 C  CB   . ILE   A 158 ? 0.3247 0.4159 0.2625 -0.1395 0.0415  -0.0804 310 ILE   A CB   
1082 C  CG1  . ILE   A 158 ? 0.3450 0.4150 0.2819 -0.1357 0.0440  -0.0806 310 ILE   A CG1  
1083 C  CG2  . ILE   A 158 ? 0.2944 0.3832 0.2300 -0.1486 0.0506  -0.0910 310 ILE   A CG2  
1084 C  CD1  . ILE   A 158 ? 0.3954 0.4341 0.3321 -0.1337 0.0508  -0.0833 310 ILE   A CD1  
1085 N  N    . LYS   A 159 ? 0.2691 0.4019 0.2131 -0.1369 0.0290  -0.0703 311 LYS   A N    
1086 C  CA   . LYS   A 159 ? 0.3254 0.4782 0.2705 -0.1405 0.0287  -0.0718 311 LYS   A CA   
1087 C  C    . LYS   A 159 ? 0.3647 0.5092 0.3142 -0.1335 0.0237  -0.0654 311 LYS   A C    
1088 O  O    . LYS   A 159 ? 0.3996 0.5479 0.3489 -0.1374 0.0264  -0.0688 311 LYS   A O    
1089 C  CB   . LYS   A 159 ? 0.3855 0.5741 0.3323 -0.1412 0.0243  -0.0688 311 LYS   A CB   
1090 C  CG   . LYS   A 159 ? 0.5273 0.7315 0.4707 -0.1499 0.0300  -0.0766 311 LYS   A CG   
1091 C  CD   . LYS   A 159 ? 0.6312 0.8375 0.5715 -0.1615 0.0395  -0.0894 311 LYS   A CD   
1092 C  CE   . LYS   A 159 ? 0.6751 0.8676 0.6122 -0.1684 0.0479  -0.0993 311 LYS   A CE   
1093 N  NZ   . LYS   A 159 ? 0.6975 0.8761 0.6319 -0.1776 0.0575  -0.1106 311 LYS   A NZ   
1094 N  N    . PHE   A 160 ? 0.3599 0.4942 0.3135 -0.1240 0.0168  -0.0567 312 PHE   A N    
1095 C  CA   . PHE   A 160 ? 0.3134 0.4379 0.2721 -0.1175 0.0128  -0.0518 312 PHE   A CA   
1096 C  C    . PHE   A 160 ? 0.2817 0.3830 0.2374 -0.1207 0.0197  -0.0567 312 PHE   A C    
1097 O  O    . PHE   A 160 ? 0.2569 0.3606 0.2138 -0.1218 0.0204  -0.0574 312 PHE   A O    
1098 C  CB   . PHE   A 160 ? 0.3342 0.4488 0.2980 -0.1081 0.0054  -0.0432 312 PHE   A CB   
1099 C  CG   . PHE   A 160 ? 0.2916 0.3930 0.2608 -0.1018 0.0024  -0.0397 312 PHE   A CG   
1100 C  CD1  . PHE   A 160 ? 0.2807 0.3972 0.2569 -0.0965 -0.0040 -0.0354 312 PHE   A CD1  
1101 C  CD2  . PHE   A 160 ? 0.2937 0.3693 0.2615 -0.1007 0.0062  -0.0408 312 PHE   A CD2  
1102 C  CE1  . PHE   A 160 ? 0.2630 0.3696 0.2443 -0.0912 -0.0064 -0.0335 312 PHE   A CE1  
1103 C  CE2  . PHE   A 160 ? 0.2932 0.3601 0.2657 -0.0955 0.0037  -0.0378 312 PHE   A CE2  
1104 C  CZ   . PHE   A 160 ? 0.2509 0.3335 0.2300 -0.0912 -0.0025 -0.0348 312 PHE   A CZ   
1105 N  N    . GLN   A 161 ? 0.3106 0.3902 0.2625 -0.1219 0.0249  -0.0596 313 GLN   A N    
1106 C  CA   . GLN   A 161 ? 0.2886 0.3456 0.2380 -0.1240 0.0317  -0.0628 313 GLN   A CA   
1107 C  C    . GLN   A 161 ? 0.3054 0.3703 0.2510 -0.1341 0.0384  -0.0707 313 GLN   A C    
1108 O  O    . GLN   A 161 ? 0.2956 0.3518 0.2406 -0.1361 0.0413  -0.0714 313 GLN   A O    
1109 C  CB   . GLN   A 161 ? 0.2643 0.2988 0.2111 -0.1228 0.0366  -0.0644 313 GLN   A CB   
1110 C  CG   . GLN   A 161 ? 0.3092 0.3368 0.2595 -0.1140 0.0307  -0.0574 313 GLN   A CG   
1111 C  CD   . GLN   A 161 ? 0.2914 0.3095 0.2466 -0.1063 0.0260  -0.0503 313 GLN   A CD   
1112 O  OE1  . GLN   A 161 ? 0.3402 0.3481 0.2949 -0.1070 0.0294  -0.0506 313 GLN   A OE1  
1113 N  NE2  . GLN   A 161 ? 0.2787 0.3009 0.2388 -0.0998 0.0184  -0.0440 313 GLN   A NE2  
1114 N  N    . VAL   A 162 ? 0.3163 0.3991 0.2591 -0.1413 0.0410  -0.0769 314 VAL   A N    
1115 C  CA   . VAL   A 162 ? 0.2865 0.3790 0.2259 -0.1523 0.0477  -0.0856 314 VAL   A CA   
1116 C  C    . VAL   A 162 ? 0.3197 0.4319 0.2615 -0.1527 0.0437  -0.0833 314 VAL   A C    
1117 O  O    . VAL   A 162 ? 0.3371 0.4453 0.2769 -0.1583 0.0481  -0.0869 314 VAL   A O    
1118 C  CB   . VAL   A 162 ? 0.3236 0.4345 0.2605 -0.1601 0.0514  -0.0932 314 VAL   A CB   
1119 C  CG1  . VAL   A 162 ? 0.2959 0.4269 0.2306 -0.1714 0.0564  -0.1016 314 VAL   A CG1  
1120 C  CG2  . VAL   A 162 ? 0.3040 0.3931 0.2383 -0.1622 0.0584  -0.0987 314 VAL   A CG2  
1121 N  N    . GLY   A 163 ? 0.2937 0.4277 0.2401 -0.1465 0.0355  -0.0769 315 GLY   A N    
1122 C  CA   . GLY   A 163 ? 0.2949 0.4483 0.2448 -0.1450 0.0315  -0.0742 315 GLY   A CA   
1123 C  C    . GLY   A 163 ? 0.3579 0.4938 0.3097 -0.1413 0.0309  -0.0709 315 GLY   A C    
1124 O  O    . GLY   A 163 ? 0.3626 0.5073 0.3140 -0.1456 0.0327  -0.0732 315 GLY   A O    
1125 N  N    . LEU   A 164 ? 0.3728 0.4858 0.3266 -0.1337 0.0285  -0.0656 316 LEU   A N    
1126 C  CA   . LEU   A 164 ? 0.3584 0.4553 0.3138 -0.1304 0.0285  -0.0625 316 LEU   A CA   
1127 C  C    . LEU   A 164 ? 0.3625 0.4459 0.3121 -0.1395 0.0372  -0.0683 316 LEU   A C    
1128 O  O    . LEU   A 164 ? 0.3649 0.4509 0.3148 -0.1420 0.0382  -0.0682 316 LEU   A O    
1129 C  CB   . LEU   A 164 ? 0.3848 0.4599 0.3426 -0.1218 0.0256  -0.0567 316 LEU   A CB   
1130 C  CG   . LEU   A 164 ? 0.4129 0.4831 0.3762 -0.1142 0.0208  -0.0508 316 LEU   A CG   
1131 C  CD1  . LEU   A 164 ? 0.3975 0.4932 0.3667 -0.1116 0.0150  -0.0492 316 LEU   A CD1  
1132 C  CD2  . LEU   A 164 ? 0.4031 0.4594 0.3696 -0.1058 0.0165  -0.0456 316 LEU   A CD2  
1133 N  N    . LYS   A 165 ? 0.3423 0.4112 0.2870 -0.1448 0.0439  -0.0736 317 LYS   A N    
1134 C  CA   . LYS   A 165 ? 0.4085 0.4621 0.3487 -0.1536 0.0527  -0.0792 317 LYS   A CA   
1135 C  C    . LYS   A 165 ? 0.4561 0.5308 0.3944 -0.1635 0.0550  -0.0851 317 LYS   A C    
1136 O  O    . LYS   A 165 ? 0.4600 0.5276 0.3968 -0.1688 0.0590  -0.0863 317 LYS   A O    
1137 C  CB   . LYS   A 165 ? 0.4817 0.5197 0.4184 -0.1575 0.0597  -0.0851 317 LYS   A CB   
1138 C  CG   . LYS   A 165 ? 0.5357 0.5453 0.4733 -0.1497 0.0611  -0.0803 317 LYS   A CG   
1139 C  CD   . LYS   A 165 ? 0.5367 0.5255 0.4745 -0.1491 0.0648  -0.0764 317 LYS   A CD   
1140 C  CE   . LYS   A 165 ? 0.5303 0.4902 0.4673 -0.1464 0.0715  -0.0758 317 LYS   A CE   
1141 N  NZ   . LYS   A 165 ? 0.4870 0.4301 0.4267 -0.1374 0.0698  -0.0660 317 LYS   A NZ   
1142 N  N    . LYS   A 166 ? 0.4072 0.5094 0.3456 -0.1663 0.0527  -0.0885 318 LYS   A N    
1143 C  CA   . LYS   A 166 ? 0.4165 0.5425 0.3530 -0.1758 0.0550  -0.0945 318 LYS   A CA   
1144 C  C    . LYS   A 166 ? 0.3487 0.4836 0.2880 -0.1733 0.0512  -0.0900 318 LYS   A C    
1145 O  O    . LYS   A 166 ? 0.4022 0.5446 0.3388 -0.1825 0.0552  -0.0949 318 LYS   A O    
1146 C  CB   . LYS   A 166 ? 0.4076 0.5658 0.3453 -0.1767 0.0518  -0.0965 318 LYS   A CB   
1147 C  CG   . LYS   A 166 ? 0.4366 0.5926 0.3721 -0.1793 0.0549  -0.1009 318 LYS   A CG   
1148 C  CD   . LYS   A 166 ? 0.4919 0.6276 0.4223 -0.1899 0.0653  -0.1106 318 LYS   A CD   
1149 C  CE   . LYS   A 166 ? 0.5465 0.6948 0.4751 -0.1964 0.0693  -0.1185 318 LYS   A CE   
1150 N  NZ   . LYS   A 166 ? 0.5965 0.7260 0.5213 -0.2073 0.0802  -0.1294 318 LYS   A NZ   
1151 N  N    . LEU   A 167 ? 0.3049 0.4399 0.2498 -0.1617 0.0438  -0.0813 319 LEU   A N    
1152 C  CA   . LEU   A 167 ? 0.3613 0.5081 0.3100 -0.1587 0.0402  -0.0775 319 LEU   A CA   
1153 C  C    . LEU   A 167 ? 0.3749 0.5025 0.3206 -0.1640 0.0453  -0.0781 319 LEU   A C    
1154 O  O    . LEU   A 167 ? 0.4150 0.5564 0.3619 -0.1663 0.0446  -0.0778 319 LEU   A O    
1155 C  CB   . LEU   A 167 ? 0.3753 0.5240 0.3316 -0.1451 0.0319  -0.0691 319 LEU   A CB   
1156 C  CG   . LEU   A 167 ? 0.3830 0.5545 0.3447 -0.1384 0.0255  -0.0664 319 LEU   A CG   
1157 C  CD1  . LEU   A 167 ? 0.3178 0.4906 0.2883 -0.1253 0.0175  -0.0588 319 LEU   A CD1  
1158 C  CD2  . LEU   A 167 ? 0.3773 0.5809 0.3388 -0.1437 0.0262  -0.0704 319 LEU   A CD2  
1159 N  N    . ASN   A 168 ? 0.3609 0.4582 0.3036 -0.1656 0.0504  -0.0782 320 ASN   A N    
1160 C  CA   . ASN   A 168 ? 0.4676 0.5447 0.4086 -0.1704 0.0560  -0.0770 320 ASN   A CA   
1161 C  C    . ASN   A 168 ? 0.4451 0.5263 0.3904 -0.1639 0.0513  -0.0696 320 ASN   A C    
1162 O  O    . ASN   A 168 ? 0.4783 0.5682 0.4237 -0.1692 0.0528  -0.0696 320 ASN   A O    
1163 C  CB   . ASN   A 168 ? 0.5112 0.5954 0.4483 -0.1843 0.0625  -0.0846 320 ASN   A CB   
1164 C  CG   . ASN   A 168 ? 0.5627 0.6174 0.4978 -0.1908 0.0711  -0.0846 320 ASN   A CG   
1165 O  OD1  . ASN   A 168 ? 0.5645 0.5929 0.5004 -0.1849 0.0732  -0.0798 320 ASN   A OD1  
1166 N  ND2  . ASN   A 168 ? 0.5887 0.6482 0.5219 -0.2029 0.0766  -0.0893 320 ASN   A ND2  
1167 N  N    . LEU   A 169 ? 0.4064 0.4828 0.3556 -0.1527 0.0458  -0.0637 321 LEU   A N    
1168 C  CA   . LEU   A 169 ? 0.4040 0.4882 0.3582 -0.1462 0.0410  -0.0579 321 LEU   A CA   
1169 C  C    . LEU   A 169 ? 0.4174 0.4814 0.3702 -0.1483 0.0461  -0.0532 321 LEU   A C    
1170 O  O    . LEU   A 169 ? 0.4492 0.4866 0.3994 -0.1485 0.0512  -0.0511 321 LEU   A O    
1171 C  CB   . LEU   A 169 ? 0.4166 0.5007 0.3760 -0.1345 0.0340  -0.0537 321 LEU   A CB   
1172 C  CG   . LEU   A 169 ? 0.4161 0.5224 0.3799 -0.1296 0.0278  -0.0550 321 LEU   A CG   
1173 C  CD1  . LEU   A 169 ? 0.3885 0.4903 0.3585 -0.1181 0.0209  -0.0500 321 LEU   A CD1  
1174 C  CD2  . LEU   A 169 ? 0.3894 0.5255 0.3566 -0.1304 0.0255  -0.0567 321 LEU   A CD2  
1175 N  N    . HIS   A 170 ? 0.3962 0.4749 0.3514 -0.1492 0.0452  -0.0507 322 HIS   A N    
1176 C  CA   . HIS   A 170 ? 0.3804 0.4450 0.3358 -0.1484 0.0490  -0.0432 322 HIS   A CA   
1177 C  C    . HIS   A 170 ? 0.3170 0.3708 0.2747 -0.1381 0.0455  -0.0378 322 HIS   A C    
1178 O  O    . HIS   A 170 ? 0.3209 0.3864 0.2826 -0.1314 0.0384  -0.0398 322 HIS   A O    
1179 C  CB   . HIS   A 170 ? 0.4308 0.5195 0.3886 -0.1504 0.0480  -0.0417 322 HIS   A CB   
1180 C  CG   . HIS   A 170 ? 0.4882 0.5840 0.4435 -0.1616 0.0529  -0.0450 322 HIS   A CG   
1181 N  ND1  . HIS   A 170 ? 0.5162 0.6200 0.4720 -0.1657 0.0564  -0.0406 322 HIS   A ND1  
1182 C  CD2  . HIS   A 170 ? 0.5142 0.6118 0.4664 -0.1701 0.0552  -0.0525 322 HIS   A CD2  
1183 C  CE1  . HIS   A 170 ? 0.5393 0.6481 0.4931 -0.1766 0.0604  -0.0451 322 HIS   A CE1  
1184 N  NE2  . HIS   A 170 ? 0.5253 0.6307 0.4766 -0.1797 0.0599  -0.0528 322 HIS   A NE2  
1185 N  N    . GLU   A 171 ? 0.3555 0.3873 0.3111 -0.1364 0.0507  -0.0302 323 GLU   A N    
1186 C  CA   . GLU   A 171 ? 0.3759 0.4001 0.3330 -0.1273 0.0480  -0.0245 323 GLU   A CA   
1187 C  C    . GLU   A 171 ? 0.3625 0.4147 0.3251 -0.1232 0.0414  -0.0250 323 GLU   A C    
1188 O  O    . GLU   A 171 ? 0.3196 0.3747 0.2864 -0.1156 0.0350  -0.0258 323 GLU   A O    
1189 C  CB   . GLU   A 171 ? 0.4558 0.4576 0.4090 -0.1253 0.0554  -0.0142 323 GLU   A CB   
1190 C  CG   . GLU   A 171 ? 0.5361 0.5276 0.4887 -0.1159 0.0536  -0.0081 323 GLU   A CG   
1191 C  CD   . GLU   A 171 ? 0.6359 0.6032 0.5839 -0.1118 0.0613  0.0030  323 GLU   A CD   
1192 O  OE1  . GLU   A 171 ? 0.6823 0.6337 0.6292 -0.1043 0.0611  0.0066  323 GLU   A OE1  
1193 O  OE2  . GLU   A 171 ? 0.7029 0.6680 0.6492 -0.1154 0.0675  0.0086  323 GLU   A OE2  
1194 N  N    . GLU   A 172 ? 0.3139 0.3879 0.2776 -0.1267 0.0422  -0.0255 324 GLU   A N    
1195 C  CA   . GLU   A 172 ? 0.2331 0.3377 0.2034 -0.1208 0.0362  -0.0276 324 GLU   A CA   
1196 C  C    . GLU   A 172 ? 0.2494 0.3673 0.2269 -0.1150 0.0267  -0.0352 324 GLU   A C    
1197 O  O    . GLU   A 172 ? 0.2922 0.4136 0.2739 -0.1011 0.0189  -0.0358 324 GLU   A O    
1198 C  CB   . GLU   A 172 ? 0.2436 0.3707 0.2136 -0.1257 0.0387  -0.0282 324 GLU   A CB   
1199 C  CG   . GLU   A 172 ? 0.3019 0.4210 0.2658 -0.1272 0.0462  -0.0187 324 GLU   A CG   
1200 C  CD   . GLU   A 172 ? 0.3957 0.4856 0.3540 -0.1354 0.0539  -0.0145 324 GLU   A CD   
1201 O  OE1  . GLU   A 172 ? 0.4511 0.5349 0.4058 -0.1372 0.0604  -0.0058 324 GLU   A OE1  
1202 O  OE2  . GLU   A 172 ? 0.3871 0.4612 0.3449 -0.1391 0.0538  -0.0196 324 GLU   A OE2  
1203 N  N    . GLU   A 173 ? 0.2249 0.3459 0.2011 -0.1199 0.0266  -0.0399 325 GLU   A N    
1204 C  CA   . GLU   A 173 ? 0.2481 0.3813 0.2299 -0.1123 0.0190  -0.0439 325 GLU   A CA   
1205 C  C    . GLU   A 173 ? 0.2170 0.3294 0.1991 -0.1068 0.0157  -0.0422 325 GLU   A C    
1206 O  O    . GLU   A 173 ? 0.2124 0.3316 0.2010 -0.0969 0.0082  -0.0428 325 GLU   A O    
1207 C  CB   . GLU   A 173 ? 0.3889 0.5333 0.3677 -0.1183 0.0210  -0.0478 325 GLU   A CB   
1208 C  CG   . GLU   A 173 ? 0.4030 0.5633 0.3790 -0.1262 0.0252  -0.0495 325 GLU   A CG   
1209 C  CD   . GLU   A 173 ? 0.4445 0.6047 0.4140 -0.1366 0.0297  -0.0537 325 GLU   A CD   
1210 O  OE1  . GLU   A 173 ? 0.4903 0.6744 0.4601 -0.1400 0.0297  -0.0570 325 GLU   A OE1  
1211 O  OE2  . GLU   A 173 ? 0.4427 0.5802 0.4072 -0.1411 0.0332  -0.0543 325 GLU   A OE2  
1212 N  N    . HIS   A 174 ? 0.2073 0.2934 0.1828 -0.1117 0.0215  -0.0395 326 HIS   A N    
1213 C  CA   . HIS   A 174 ? 0.2248 0.2915 0.2001 -0.1063 0.0191  -0.0377 326 HIS   A CA   
1214 C  C    . HIS   A 174 ? 0.2275 0.2933 0.2078 -0.0967 0.0130  -0.0352 326 HIS   A C    
1215 O  O    . HIS   A 174 ? 0.2180 0.2830 0.2026 -0.0887 0.0062  -0.0356 326 HIS   A O    
1216 C  CB   . HIS   A 174 ? 0.2897 0.3290 0.2573 -0.1112 0.0273  -0.0353 326 HIS   A CB   
1217 C  CG   . HIS   A 174 ? 0.3491 0.3697 0.3162 -0.1054 0.0259  -0.0335 326 HIS   A CG   
1218 N  ND1  . HIS   A 174 ? 0.3483 0.3718 0.3164 -0.1030 0.0226  -0.0362 326 HIS   A ND1  
1219 C  CD2  . HIS   A 174 ? 0.3478 0.3486 0.3133 -0.1014 0.0279  -0.0286 326 HIS   A CD2  
1220 C  CE1  . HIS   A 174 ? 0.3422 0.3488 0.3097 -0.0981 0.0223  -0.0336 326 HIS   A CE1  
1221 N  NE2  . HIS   A 174 ? 0.3729 0.3654 0.3390 -0.0966 0.0254  -0.0293 326 HIS   A NE2  
1222 N  N    . VAL   A 175 ? 0.2508 0.3148 0.2288 -0.0928 0.0154  -0.0312 327 VAL   A N    
1223 C  CA   . VAL   A 175 ? 0.1794 0.2412 0.1600 -0.0792 0.0098  -0.0289 327 VAL   A CA   
1224 C  C    . VAL   A 175 ? 0.1693 0.2527 0.1580 -0.0710 0.0017  -0.0340 327 VAL   A C    
1225 O  O    . VAL   A 175 ? 0.1746 0.2550 0.1681 -0.0609 -0.0046 -0.0348 327 VAL   A O    
1226 C  CB   . VAL   A 175 ? 0.2452 0.3020 0.2203 -0.0769 0.0146  -0.0228 327 VAL   A CB   
1227 C  CG1  . VAL   A 175 ? 0.2554 0.2876 0.2233 -0.0831 0.0232  -0.0166 327 VAL   A CG1  
1228 C  CG2  . VAL   A 175 ? 0.2344 0.3126 0.2092 -0.0808 0.0171  -0.0238 327 VAL   A CG2  
1229 N  N    . LEU   A 176 ? 0.2112 0.3166 0.2025 -0.0753 0.0020  -0.0377 328 LEU   A N    
1230 C  CA   . LEU   A 176 ? 0.1532 0.2790 0.1535 -0.0664 -0.0052 -0.0427 328 LEU   A CA   
1231 C  C    . LEU   A 176 ? 0.1431 0.2650 0.1486 -0.0630 -0.0109 -0.0433 328 LEU   A C    
1232 O  O    . LEU   A 176 ? 0.1621 0.2857 0.1749 -0.0519 -0.0173 -0.0447 328 LEU   A O    
1233 C  CB   . LEU   A 176 ? 0.1292 0.2818 0.1313 -0.0720 -0.0031 -0.0461 328 LEU   A CB   
1234 C  CG   . LEU   A 176 ? 0.1426 0.3076 0.1426 -0.0706 0.0001  -0.0463 328 LEU   A CG   
1235 C  CD1  . LEU   A 176 ? 0.1289 0.3181 0.1290 -0.0806 0.0047  -0.0483 328 LEU   A CD1  
1236 C  CD2  . LEU   A 176 ? 0.1195 0.2942 0.1263 -0.0558 -0.0064 -0.0507 328 LEU   A CD2  
1237 N  N    . LEU   A 177 ? 0.1961 0.3123 0.1980 -0.0723 -0.0080 -0.0421 329 LEU   A N    
1238 C  CA   . LEU   A 177 ? 0.2242 0.3367 0.2293 -0.0683 -0.0121 -0.0405 329 LEU   A CA   
1239 C  C    . LEU   A 177 ? 0.1970 0.2906 0.2034 -0.0624 -0.0160 -0.0382 329 LEU   A C    
1240 O  O    . LEU   A 177 ? 0.1644 0.2591 0.1777 -0.0542 -0.0221 -0.0371 329 LEU   A O    
1241 C  CB   . LEU   A 177 ? 0.3005 0.4090 0.2991 -0.0779 -0.0065 -0.0396 329 LEU   A CB   
1242 C  CG   . LEU   A 177 ? 0.3656 0.4880 0.3673 -0.0761 -0.0096 -0.0392 329 LEU   A CG   
1243 C  CD1  . LEU   A 177 ? 0.3519 0.5001 0.3581 -0.0740 -0.0106 -0.0413 329 LEU   A CD1  
1244 C  CD2  . LEU   A 177 ? 0.3749 0.4906 0.3688 -0.0854 -0.0038 -0.0397 329 LEU   A CD2  
1245 N  N    . MET   A 178 ? 0.1716 0.2460 0.1718 -0.0647 -0.0116 -0.0359 330 MET   A N    
1246 C  CA   . MET   A 178 ? 0.1764 0.2333 0.1778 -0.0577 -0.0143 -0.0330 330 MET   A CA   
1247 C  C    . MET   A 178 ? 0.1700 0.2316 0.1788 -0.0464 -0.0202 -0.0348 330 MET   A C    
1248 O  O    . MET   A 178 ? 0.1688 0.2235 0.1833 -0.0403 -0.0251 -0.0339 330 MET   A O    
1249 C  CB   . MET   A 178 ? 0.2129 0.2518 0.2065 -0.0608 -0.0081 -0.0297 330 MET   A CB   
1250 C  CG   . MET   A 178 ? 0.2258 0.2540 0.2129 -0.0712 -0.0016 -0.0290 330 MET   A CG   
1251 S  SD   . MET   A 178 ? 0.3542 0.3580 0.3343 -0.0712 0.0054  -0.0239 330 MET   A SD   
1252 C  CE   . MET   A 178 ? 0.2877 0.2961 0.2637 -0.0728 0.0107  -0.0216 330 MET   A CE   
1253 N  N    . ALA   A 179 ? 0.1237 0.1977 0.1329 -0.0441 -0.0196 -0.0379 331 ALA   A N    
1254 C  CA   . ALA   A 179 ? 0.1507 0.2302 0.1671 -0.0338 -0.0246 -0.0420 331 ALA   A CA   
1255 C  C    . ALA   A 179 ? 0.1166 0.2052 0.1428 -0.0275 -0.0301 -0.0446 331 ALA   A C    
1256 O  O    . ALA   A 179 ? 0.1064 0.1888 0.1401 -0.0193 -0.0346 -0.0467 331 ALA   A O    
1257 C  CB   . ALA   A 179 ? 0.1073 0.2010 0.1209 -0.0331 -0.0219 -0.0451 331 ALA   A CB   
1258 N  N    . ILE   A 180 ? 0.1161 0.2197 0.1430 -0.0311 -0.0294 -0.0445 332 ILE   A N    
1259 C  CA   . ILE   A 180 ? 0.1362 0.2508 0.1727 -0.0238 -0.0344 -0.0451 332 ILE   A CA   
1260 C  C    . ILE   A 180 ? 0.1485 0.2487 0.1878 -0.0222 -0.0375 -0.0395 332 ILE   A C    
1261 O  O    . ILE   A 180 ? 0.2068 0.3050 0.2553 -0.0129 -0.0421 -0.0386 332 ILE   A O    
1262 C  CB   . ILE   A 180 ? 0.1400 0.2788 0.1761 -0.0287 -0.0328 -0.0458 332 ILE   A CB   
1263 C  CG1  . ILE   A 180 ? 0.1279 0.2846 0.1642 -0.0279 -0.0305 -0.0514 332 ILE   A CG1  
1264 C  CG2  . ILE   A 180 ? 0.1198 0.2704 0.1648 -0.0215 -0.0378 -0.0434 332 ILE   A CG2  
1265 C  CD1  . ILE   A 180 ? 0.1373 0.3107 0.1687 -0.0370 -0.0252 -0.0506 332 ILE   A CD1  
1266 N  N    . CYS   A 181 ? 0.1601 0.2500 0.1917 -0.0311 -0.0346 -0.0356 333 CYS   A N    
1267 C  CA   . CYS   A 181 ? 0.1947 0.2717 0.2278 -0.0303 -0.0369 -0.0300 333 CYS   A CA   
1268 C  C    . CYS   A 181 ? 0.2021 0.2624 0.2410 -0.0229 -0.0399 -0.0300 333 CYS   A C    
1269 O  O    . CYS   A 181 ? 0.1811 0.2357 0.2272 -0.0176 -0.0436 -0.0262 333 CYS   A O    
1270 C  CB   . CYS   A 181 ? 0.2241 0.2927 0.2474 -0.0410 -0.0322 -0.0279 333 CYS   A CB   
1271 S  SG   . CYS   A 181 ? 0.2359 0.2914 0.2592 -0.0415 -0.0338 -0.0215 333 CYS   A SG   
1272 N  N    . ILE   A 182 ? 0.2168 0.2703 0.2530 -0.0227 -0.0381 -0.0340 334 ILE   A N    
1273 C  CA   . ILE   A 182 ? 0.1765 0.2163 0.2177 -0.0176 -0.0407 -0.0353 334 ILE   A CA   
1274 C  C    . ILE   A 182 ? 0.1939 0.2369 0.2463 -0.0082 -0.0448 -0.0403 334 ILE   A C    
1275 O  O    . ILE   A 182 ? 0.1855 0.2172 0.2459 -0.0041 -0.0479 -0.0388 334 ILE   A O    
1276 C  CB   . ILE   A 182 ? 0.1913 0.2275 0.2260 -0.0199 -0.0377 -0.0379 334 ILE   A CB   
1277 C  CG1  . ILE   A 182 ? 0.2076 0.2341 0.2335 -0.0271 -0.0335 -0.0323 334 ILE   A CG1  
1278 C  CG2  . ILE   A 182 ? 0.1869 0.2166 0.2280 -0.0143 -0.0409 -0.0425 334 ILE   A CG2  
1279 C  CD1  . ILE   A 182 ? 0.2048 0.2319 0.2221 -0.0300 -0.0285 -0.0322 334 ILE   A CD1  
1280 N  N    A VAL   A 183 ? 0.1701 0.2278 0.2235 -0.0048 -0.0445 -0.0464 335 VAL   A N    
1281 N  N    B VAL   A 183 ? 0.1601 0.2179 0.2134 -0.0049 -0.0444 -0.0462 335 VAL   A N    
1282 C  CA   A VAL   A 183 ? 0.1931 0.2535 0.2574 0.0050  -0.0476 -0.0531 335 VAL   A CA   
1283 C  CA   B VAL   A 183 ? 0.1923 0.2536 0.2564 0.0050  -0.0475 -0.0531 335 VAL   A CA   
1284 C  C    A VAL   A 183 ? 0.2162 0.2849 0.2876 0.0106  -0.0496 -0.0494 335 VAL   A C    
1285 C  C    B VAL   A 183 ? 0.2231 0.2927 0.2938 0.0100  -0.0494 -0.0489 335 VAL   A C    
1286 O  O    A VAL   A 183 ? 0.2009 0.2882 0.2740 0.0142  -0.0492 -0.0527 335 VAL   A O    
1287 O  O    B VAL   A 183 ? 0.1928 0.2815 0.2645 0.0127  -0.0489 -0.0514 335 VAL   A O    
1288 C  CB   A VAL   A 183 ? 0.1989 0.2729 0.2612 0.0071  -0.0460 -0.0625 335 VAL   A CB   
1289 C  CB   B VAL   A 183 ? 0.2011 0.2770 0.2631 0.0070  -0.0459 -0.0622 335 VAL   A CB   
1290 C  CG1  A VAL   A 183 ? 0.1738 0.2671 0.2289 0.0026  -0.0427 -0.0612 335 VAL   A CG1  
1291 C  CG1  B VAL   A 183 ? 0.1988 0.2752 0.2720 0.0172  -0.0485 -0.0717 335 VAL   A CG1  
1292 C  CG2  A VAL   A 183 ? 0.2007 0.2768 0.2744 0.0176  -0.0487 -0.0718 335 VAL   A CG2  
1293 C  CG2  B VAL   A 183 ? 0.1883 0.2606 0.2411 0.0011  -0.0433 -0.0628 335 VAL   A CG2  
1294 N  N    . SER   A 184 ? 0.2337 0.2909 0.3093 0.0116  -0.0516 -0.0416 336 SER   A N    
1295 C  CA   . SER   A 184 ? 0.2738 0.3388 0.3565 0.0181  -0.0538 -0.0355 336 SER   A CA   
1296 C  C    . SER   A 184 ? 0.2383 0.2874 0.3340 0.0282  -0.0565 -0.0352 336 SER   A C    
1297 O  O    . SER   A 184 ? 0.1955 0.2246 0.2932 0.0258  -0.0570 -0.0328 336 SER   A O    
1298 C  CB   . SER   A 184 ? 0.3221 0.3895 0.3988 0.0112  -0.0537 -0.0249 336 SER   A CB   
1299 O  OG   . SER   A 184 ? 0.3691 0.4464 0.4340 0.0006  -0.0503 -0.0264 336 SER   A OG   
1300 N  N    . PRO   A 185 ? 0.2377 0.2946 0.3433 0.0395  -0.0577 -0.0380 337 PRO   A N    
1301 C  CA   . PRO   A 185 ? 0.2339 0.2720 0.3532 0.0497  -0.0592 -0.0387 337 PRO   A CA   
1302 C  C    . PRO   A 185 ? 0.2435 0.2704 0.3680 0.0523  -0.0607 -0.0241 337 PRO   A C    
1303 O  O    . PRO   A 185 ? 0.2759 0.2827 0.4118 0.0592  -0.0612 -0.0229 337 PRO   A O    
1304 C  CB   . PRO   A 185 ? 0.2098 0.2625 0.3375 0.0619  -0.0592 -0.0459 337 PRO   A CB   
1305 C  CG   . PRO   A 185 ? 0.1999 0.2822 0.3197 0.0588  -0.0588 -0.0433 337 PRO   A CG   
1306 C  CD   . PRO   A 185 ? 0.2041 0.2873 0.3093 0.0435  -0.0571 -0.0421 337 PRO   A CD   
1307 N  N    . ASP   A 186 ? 0.2522 0.2917 0.3688 0.0466  -0.0611 -0.0132 338 ASP   A N    
1308 C  CA   . ASP   A 186 ? 0.3725 0.4066 0.4929 0.0493  -0.0626 0.0019  338 ASP   A CA   
1309 C  C    . ASP   A 186 ? 0.3711 0.3892 0.4856 0.0386  -0.0619 0.0076  338 ASP   A C    
1310 O  O    . ASP   A 186 ? 0.4377 0.4578 0.5510 0.0374  -0.0626 0.0207  338 ASP   A O    
1311 C  CB   . ASP   A 186 ? 0.3843 0.4472 0.5005 0.0505  -0.0638 0.0103  338 ASP   A CB   
1312 C  CG   . ASP   A 186 ? 0.4036 0.4842 0.5056 0.0375  -0.0621 0.0054  338 ASP   A CG   
1313 O  OD1  . ASP   A 186 ? 0.4076 0.5094 0.5041 0.0339  -0.0627 0.0120  338 ASP   A OD1  
1314 O  OD2  . ASP   A 186 ? 0.4372 0.5110 0.5336 0.0308  -0.0600 -0.0051 338 ASP   A OD2  
1315 N  N    . ARG   A 187 ? 0.3304 0.3356 0.4413 0.0313  -0.0604 -0.0016 339 ARG   A N    
1316 C  CA   . ARG   A 187 ? 0.3103 0.3011 0.4174 0.0224  -0.0597 0.0035  339 ARG   A CA   
1317 C  C    . ARG   A 187 ? 0.2838 0.2513 0.4034 0.0266  -0.0602 0.0081  339 ARG   A C    
1318 O  O    . ARG   A 187 ? 0.2847 0.2409 0.4145 0.0334  -0.0604 0.0001  339 ARG   A O    
1319 C  CB   . ARG   A 187 ? 0.2896 0.2772 0.3888 0.0137  -0.0579 -0.0069 339 ARG   A CB   
1320 C  CG   . ARG   A 187 ? 0.3195 0.3257 0.4070 0.0090  -0.0562 -0.0117 339 ARG   A CG   
1321 C  CD   . ARG   A 187 ? 0.3481 0.3632 0.4259 0.0015  -0.0549 -0.0033 339 ARG   A CD   
1322 N  NE   . ARG   A 187 ? 0.3517 0.3796 0.4185 -0.0051 -0.0522 -0.0087 339 ARG   A NE   
1323 C  CZ   . ARG   A 187 ? 0.3591 0.3940 0.4162 -0.0133 -0.0498 -0.0053 339 ARG   A CZ   
1324 N  NH1  . ARG   A 187 ? 0.3637 0.4073 0.4121 -0.0196 -0.0465 -0.0107 339 ARG   A NH1  
1325 N  NH2  . ARG   A 187 ? 0.3768 0.4099 0.4333 -0.0155 -0.0504 0.0034  339 ARG   A NH2  
1326 N  N    . PRO   A 188 ? 0.2915 0.2512 0.4107 0.0222  -0.0600 0.0201  340 PRO   A N    
1327 C  CA   . PRO   A 188 ? 0.3257 0.2614 0.4570 0.0240  -0.0597 0.0249  340 PRO   A CA   
1328 C  C    . PRO   A 188 ? 0.3400 0.2605 0.4748 0.0190  -0.0588 0.0107  340 PRO   A C    
1329 O  O    . PRO   A 188 ? 0.3468 0.2740 0.4725 0.0111  -0.0583 0.0033  340 PRO   A O    
1330 C  CB   . PRO   A 188 ? 0.3028 0.2389 0.4295 0.0171  -0.0592 0.0396  340 PRO   A CB   
1331 C  CG   . PRO   A 188 ? 0.3061 0.2681 0.4203 0.0153  -0.0597 0.0438  340 PRO   A CG   
1332 C  CD   . PRO   A 188 ? 0.2946 0.2669 0.4025 0.0141  -0.0594 0.0289  340 PRO   A CD   
1333 N  N    . GLY   A 189 ? 0.3829 0.2837 0.5315 0.0240  -0.0584 0.0067  341 GLY   A N    
1334 C  CA   . GLY   A 189 ? 0.4189 0.3063 0.5725 0.0187  -0.0577 -0.0076 341 GLY   A CA   
1335 C  C    . GLY   A 189 ? 0.4363 0.3310 0.5901 0.0229  -0.0581 -0.0256 341 GLY   A C    
1336 O  O    . GLY   A 189 ? 0.4755 0.3665 0.6303 0.0184  -0.0562 -0.0378 341 GLY   A O    
1337 N  N    . VAL   A 190 ? 0.4554 0.3682 0.6041 0.0301  -0.0588 -0.0267 342 VAL   A N    
1338 C  CA   . VAL   A 190 ? 0.4304 0.3542 0.5778 0.0335  -0.0588 -0.0431 342 VAL   A CA   
1339 C  C    . VAL   A 190 ? 0.4604 0.3683 0.6228 0.0418  -0.0580 -0.0537 342 VAL   A C    
1340 O  O    . VAL   A 190 ? 0.4589 0.3568 0.6302 0.0503  -0.0571 -0.0457 342 VAL   A O    
1341 C  CB   . VAL   A 190 ? 0.3879 0.3361 0.5269 0.0382  -0.0592 -0.0406 342 VAL   A CB   
1342 C  CG1  . VAL   A 190 ? 0.4322 0.3904 0.5748 0.0459  -0.0589 -0.0552 342 VAL   A CG1  
1343 C  CG2  . VAL   A 190 ? 0.3170 0.2799 0.4405 0.0280  -0.0588 -0.0381 342 VAL   A CG2  
1344 N  N    . GLN   A 191 ? 0.4867 0.3966 0.6485 0.0382  -0.0570 -0.0703 343 GLN   A N    
1345 C  CA   . GLN   A 191 ? 0.5144 0.4162 0.6838 0.0419  -0.0539 -0.0805 343 GLN   A CA   
1346 C  C    . GLN   A 191 ? 0.4781 0.3927 0.6505 0.0535  -0.0541 -0.0904 343 GLN   A C    
1347 O  O    . GLN   A 191 ? 0.5442 0.4516 0.7243 0.0637  -0.0524 -0.0871 343 GLN   A O    
1348 C  CB   . GLN   A 191 ? 0.5808 0.4851 0.7470 0.0320  -0.0524 -0.0924 343 GLN   A CB   
1349 C  CG   . GLN   A 191 ? 0.6565 0.5466 0.8233 0.0222  -0.0503 -0.0857 343 GLN   A CG   
1350 C  CD   . GLN   A 191 ? 0.7067 0.6037 0.8708 0.0143  -0.0489 -0.0985 343 GLN   A CD   
1351 O  OE1  . GLN   A 191 ? 0.7377 0.6268 0.9019 0.0060  -0.0472 -0.0958 343 GLN   A OE1  
1352 N  NE2  . GLN   A 191 ? 0.6967 0.6108 0.8582 0.0169  -0.0497 -0.1122 343 GLN   A NE2  
1353 N  N    . ASP   A 192 ? 0.3839 0.3189 0.5491 0.0523  -0.0555 -0.1021 344 ASP   A N    
1354 C  CA   . ASP   A 192 ? 0.3398 0.2924 0.5061 0.0621  -0.0551 -0.1130 344 ASP   A CA   
1355 C  C    . ASP   A 192 ? 0.3104 0.2822 0.4705 0.0666  -0.0565 -0.1025 344 ASP   A C    
1356 O  O    . ASP   A 192 ? 0.3012 0.2961 0.4493 0.0623  -0.0565 -0.1046 344 ASP   A O    
1357 C  CB   . ASP   A 192 ? 0.3335 0.3030 0.4928 0.0564  -0.0546 -0.1288 344 ASP   A CB   
1358 C  CG   . ASP   A 192 ? 0.3694 0.3548 0.5314 0.0653  -0.0531 -0.1415 344 ASP   A CG   
1359 O  OD1  . ASP   A 192 ? 0.3658 0.3632 0.5246 0.0614  -0.0522 -0.1542 344 ASP   A OD1  
1360 O  OD2  . ASP   A 192 ? 0.3663 0.3550 0.5332 0.0762  -0.0527 -0.1379 344 ASP   A OD2  
1361 N  N    . ALA   A 193 ? 0.2926 0.2571 0.4588 0.0735  -0.0569 -0.0884 345 ALA   A N    
1362 C  CA   . ALA   A 193 ? 0.3099 0.2963 0.4687 0.0755  -0.0578 -0.0760 345 ALA   A CA   
1363 C  C    . ALA   A 193 ? 0.2619 0.2752 0.4185 0.0817  -0.0570 -0.0857 345 ALA   A C    
1364 O  O    . ALA   A 193 ? 0.2419 0.2785 0.3875 0.0767  -0.0571 -0.0816 345 ALA   A O    
1365 C  CB   . ALA   A 193 ? 0.3116 0.2890 0.4794 0.0843  -0.0585 -0.0604 345 ALA   A CB   
1366 N  N    . LYS   A 194 ? 0.3079 0.3187 0.4752 0.0920  -0.0557 -0.0995 346 LYS   A N    
1367 C  CA   . LYS   A 194 ? 0.3036 0.3419 0.4700 0.0990  -0.0546 -0.1091 346 LYS   A CA   
1368 C  C    . LYS   A 194 ? 0.3096 0.3671 0.4623 0.0883  -0.0539 -0.1179 346 LYS   A C    
1369 O  O    . LYS   A 194 ? 0.3033 0.3880 0.4484 0.0871  -0.0532 -0.1165 346 LYS   A O    
1370 C  CB   . LYS   A 194 ? 0.3936 0.4231 0.5708 0.1098  -0.0521 -0.1206 346 LYS   A CB   
1371 C  CG   . LYS   A 194 ? 0.4903 0.5040 0.6775 0.1206  -0.0509 -0.1084 346 LYS   A CG   
1372 C  CD   . LYS   A 194 ? 0.5742 0.6153 0.7620 0.1305  -0.0514 -0.0999 346 LYS   A CD   
1373 C  CE   . LYS   A 194 ? 0.6337 0.6761 0.8215 0.1303  -0.0545 -0.0799 346 LYS   A CE   
1374 N  NZ   . LYS   A 194 ? 0.6493 0.7227 0.8371 0.1382  -0.0551 -0.0713 346 LYS   A NZ   
1375 N  N    . LEU   A 195 ? 0.2603 0.3054 0.4101 0.0804  -0.0538 -0.1265 347 LEU   A N    
1376 C  CA   . LEU   A 195 ? 0.2174 0.2806 0.3536 0.0707  -0.0531 -0.1319 347 LEU   A CA   
1377 C  C    . LEU   A 195 ? 0.2428 0.3139 0.3659 0.0608  -0.0533 -0.1165 347 LEU   A C    
1378 O  O    . LEU   A 195 ? 0.2815 0.3754 0.3950 0.0572  -0.0518 -0.1158 347 LEU   A O    
1379 C  CB   . LEU   A 195 ? 0.2526 0.3020 0.3889 0.0643  -0.0535 -0.1422 347 LEU   A CB   
1380 C  CG   . LEU   A 195 ? 0.1761 0.2434 0.2995 0.0557  -0.0530 -0.1482 347 LEU   A CG   
1381 C  CD1  . LEU   A 195 ? 0.2137 0.3088 0.3347 0.0611  -0.0512 -0.1594 347 LEU   A CD1  
1382 C  CD2  . LEU   A 195 ? 0.1831 0.2386 0.3089 0.0500  -0.0536 -0.1559 347 LEU   A CD2  
1383 N  N    . VAL   A 196 ? 0.2319 0.2840 0.3549 0.0561  -0.0547 -0.1042 348 VAL   A N    
1384 C  CA   . VAL   A 196 ? 0.2117 0.2692 0.3233 0.0469  -0.0544 -0.0907 348 VAL   A CA   
1385 C  C    . VAL   A 196 ? 0.1652 0.2453 0.2744 0.0497  -0.0536 -0.0856 348 VAL   A C    
1386 O  O    . VAL   A 196 ? 0.1467 0.2421 0.2447 0.0418  -0.0518 -0.0824 348 VAL   A O    
1387 C  CB   . VAL   A 196 ? 0.2143 0.2497 0.3284 0.0436  -0.0559 -0.0789 348 VAL   A CB   
1388 C  CG1  . VAL   A 196 ? 0.1403 0.1824 0.2432 0.0351  -0.0553 -0.0664 348 VAL   A CG1  
1389 C  CG2  . VAL   A 196 ? 0.1561 0.1727 0.2718 0.0385  -0.0563 -0.0841 348 VAL   A CG2  
1390 N  N    . GLU   A 197 ? 0.1752 0.2581 0.2955 0.0611  -0.0547 -0.0848 349 GLU   A N    
1391 C  CA   . GLU   A 197 ? 0.2476 0.3560 0.3672 0.0644  -0.0543 -0.0804 349 GLU   A CA   
1392 C  C    . GLU   A 197 ? 0.2145 0.3480 0.3298 0.0641  -0.0519 -0.0910 349 GLU   A C    
1393 O  O    . GLU   A 197 ? 0.1913 0.3475 0.2998 0.0589  -0.0505 -0.0873 349 GLU   A O    
1394 C  CB   . GLU   A 197 ? 0.2683 0.3752 0.4022 0.0790  -0.0559 -0.0770 349 GLU   A CB   
1395 C  CG   . GLU   A 197 ? 0.3595 0.4966 0.4944 0.0840  -0.0560 -0.0724 349 GLU   A CG   
1396 C  CD   . GLU   A 197 ? 0.4503 0.5854 0.5992 0.0994  -0.0579 -0.0654 349 GLU   A CD   
1397 O  OE1  . GLU   A 197 ? 0.5009 0.6252 0.6618 0.1121  -0.0573 -0.0735 349 GLU   A OE1  
1398 O  OE2  . GLU   A 197 ? 0.5144 0.6590 0.6624 0.0992  -0.0596 -0.0520 349 GLU   A OE2  
1399 N  N    . ALA   A 198 ? 0.2150 0.3460 0.3342 0.0691  -0.0512 -0.1046 350 ALA   A N    
1400 C  CA   . ALA   A 198 ? 0.2111 0.3678 0.3256 0.0687  -0.0487 -0.1145 350 ALA   A CA   
1401 C  C    . ALA   A 198 ? 0.2613 0.4247 0.3603 0.0544  -0.0466 -0.1105 350 ALA   A C    
1402 O  O    . ALA   A 198 ? 0.2607 0.4482 0.3531 0.0503  -0.0439 -0.1105 350 ALA   A O    
1403 C  CB   . ALA   A 198 ? 0.1845 0.3377 0.3062 0.0767  -0.0483 -0.1310 350 ALA   A CB   
1404 N  N    . ILE   A 199 ? 0.2396 0.3818 0.3331 0.0468  -0.0473 -0.1065 351 ILE   A N    
1405 C  CA   . ILE   A 199 ? 0.2016 0.3474 0.2810 0.0346  -0.0448 -0.1010 351 ILE   A CA   
1406 C  C    . ILE   A 199 ? 0.2177 0.3695 0.2912 0.0272  -0.0433 -0.0893 351 ILE   A C    
1407 O  O    . ILE   A 199 ? 0.1964 0.3632 0.2608 0.0195  -0.0397 -0.0870 351 ILE   A O    
1408 C  CB   . ILE   A 199 ? 0.2365 0.3598 0.3126 0.0297  -0.0459 -0.0994 351 ILE   A CB   
1409 C  CG1  . ILE   A 199 ? 0.2290 0.3515 0.3097 0.0348  -0.0470 -0.1130 351 ILE   A CG1  
1410 C  CG2  . ILE   A 199 ? 0.1985 0.3233 0.2607 0.0188  -0.0429 -0.0915 351 ILE   A CG2  
1411 C  CD1  . ILE   A 199 ? 0.2027 0.3030 0.2850 0.0316  -0.0491 -0.1131 351 ILE   A CD1  
1412 N  N    . GLN   A 200 ? 0.2491 0.3901 0.3277 0.0288  -0.0457 -0.0819 352 GLN   A N    
1413 C  CA   . GLN   A 200 ? 0.2290 0.3786 0.3023 0.0214  -0.0445 -0.0726 352 GLN   A CA   
1414 C  C    . GLN   A 200 ? 0.2227 0.4022 0.2973 0.0227  -0.0428 -0.0752 352 GLN   A C    
1415 O  O    . GLN   A 200 ? 0.2262 0.4186 0.2930 0.0123  -0.0397 -0.0715 352 GLN   A O    
1416 C  CB   . GLN   A 200 ? 0.1892 0.3266 0.2685 0.0245  -0.0477 -0.0644 352 GLN   A CB   
1417 C  CG   . GLN   A 200 ? 0.1639 0.3085 0.2361 0.0147  -0.0466 -0.0555 352 GLN   A CG   
1418 C  CD   . GLN   A 200 ? 0.1845 0.3221 0.2623 0.0186  -0.0499 -0.0468 352 GLN   A CD   
1419 O  OE1  . GLN   A 200 ? 0.1876 0.3130 0.2598 0.0112  -0.0497 -0.0402 352 GLN   A OE1  
1420 N  NE2  . GLN   A 200 ? 0.1795 0.3253 0.2687 0.0311  -0.0527 -0.0462 352 GLN   A NE2  
1421 N  N    . ASP   A 201 ? 0.2339 0.4250 0.3191 0.0351  -0.0444 -0.0823 353 ASP   A N    
1422 C  CA   . ASP   A 201 ? 0.2498 0.4725 0.3378 0.0378  -0.0430 -0.0852 353 ASP   A CA   
1423 C  C    . ASP   A 201 ? 0.2523 0.4891 0.3288 0.0275  -0.0375 -0.0877 353 ASP   A C    
1424 O  O    . ASP   A 201 ? 0.2748 0.5266 0.3447 0.0198  -0.0333 -0.0834 353 ASP   A O    
1425 C  CB   . ASP   A 201 ? 0.2597 0.4897 0.3609 0.0545  -0.0448 -0.0938 353 ASP   A CB   
1426 C  CG   . ASP   A 201 ? 0.2696 0.4939 0.3822 0.0654  -0.0484 -0.0875 353 ASP   A CG   
1427 O  OD1  . ASP   A 201 ? 0.2775 0.5003 0.3869 0.0594  -0.0496 -0.0767 353 ASP   A OD1  
1428 O  OD2  . ASP   A 201 ? 0.3382 0.5594 0.4629 0.0802  -0.0496 -0.0934 353 ASP   A OD2  
1429 N  N    A ARG   A 202 ? 0.2223 0.4530 0.2954 0.0271  -0.0367 -0.0939 354 ARG   A N    
1430 N  N    B ARG   A 202 ? 0.2207 0.4514 0.2937 0.0270  -0.0367 -0.0938 354 ARG   A N    
1431 C  CA   A ARG   A 202 ? 0.2194 0.4619 0.2808 0.0184  -0.0306 -0.0939 354 ARG   A CA   
1432 C  CA   B ARG   A 202 ? 0.2196 0.4625 0.2811 0.0184  -0.0306 -0.0939 354 ARG   A CA   
1433 C  C    A ARG   A 202 ? 0.1922 0.4264 0.2426 0.0035  -0.0269 -0.0835 354 ARG   A C    
1434 C  C    B ARG   A 202 ? 0.1920 0.4261 0.2423 0.0035  -0.0269 -0.0835 354 ARG   A C    
1435 O  O    A ARG   A 202 ? 0.1870 0.4356 0.2306 -0.0052 -0.0214 -0.0807 354 ARG   A O    
1436 O  O    B ARG   A 202 ? 0.1874 0.4358 0.2307 -0.0052 -0.0213 -0.0808 354 ARG   A O    
1437 C  CB   A ARG   A 202 ? 0.2406 0.4790 0.2999 0.0216  -0.0308 -0.1015 354 ARG   A CB   
1438 C  CB   B ARG   A 202 ? 0.2391 0.4789 0.2988 0.0220  -0.0307 -0.1018 354 ARG   A CB   
1439 C  CG   A ARG   A 202 ? 0.2748 0.5169 0.3466 0.0360  -0.0349 -0.1145 354 ARG   A CG   
1440 C  CG   B ARG   A 202 ? 0.2755 0.5259 0.3465 0.0362  -0.0335 -0.1152 354 ARG   A CG   
1441 C  CD   A ARG   A 202 ? 0.2978 0.5676 0.3713 0.0421  -0.0316 -0.1222 354 ARG   A CD   
1442 C  CD   B ARG   A 202 ? 0.2897 0.5489 0.3554 0.0372  -0.0311 -0.1239 354 ARG   A CD   
1443 N  NE   A ARG   A 202 ? 0.3047 0.5771 0.3889 0.0555  -0.0342 -0.1369 354 ARG   A NE   
1444 N  NE   B ARG   A 202 ? 0.2936 0.5338 0.3512 0.0305  -0.0311 -0.1194 354 ARG   A NE   
1445 C  CZ   A ARG   A 202 ? 0.2812 0.5408 0.3794 0.0670  -0.0378 -0.1410 354 ARG   A CZ   
1446 C  CZ   B ARG   A 202 ? 0.3599 0.5826 0.4220 0.0346  -0.0353 -0.1257 354 ARG   A CZ   
1447 N  NH1  A ARG   A 202 ? 0.2307 0.4776 0.3336 0.0673  -0.0402 -0.1306 354 ARG   A NH1  
1448 N  NH1  B ARG   A 202 ? 0.3462 0.5539 0.4002 0.0283  -0.0343 -0.1197 354 ARG   A NH1  
1449 N  NH2  A ARG   A 202 ? 0.2712 0.5275 0.3763 0.0773  -0.0385 -0.1545 354 ARG   A NH2  
1450 N  NH2  B ARG   A 202 ? 0.3621 0.5791 0.4370 0.0452  -0.0386 -0.1362 354 ARG   A NH2  
1451 N  N    . LEU   A 203 ? 0.1593 0.3706 0.2084 0.0000  -0.0296 -0.0784 355 LEU   A N    
1452 C  CA   . LEU   A 203 ? 0.1447 0.3469 0.1842 -0.0136 -0.0259 -0.0700 355 LEU   A CA   
1453 C  C    . LEU   A 203 ? 0.1502 0.3640 0.1902 -0.0186 -0.0241 -0.0662 355 LEU   A C    
1454 O  O    . LEU   A 203 ? 0.1303 0.3497 0.1630 -0.0304 -0.0185 -0.0629 355 LEU   A O    
1455 C  CB   . LEU   A 203 ? 0.1440 0.3181 0.1815 -0.0148 -0.0284 -0.0657 355 LEU   A CB   
1456 C  CG   . LEU   A 203 ? 0.1332 0.2924 0.1696 -0.0098 -0.0297 -0.0683 355 LEU   A CG   
1457 C  CD1  . LEU   A 203 ? 0.1052 0.2390 0.1419 -0.0103 -0.0321 -0.0635 355 LEU   A CD1  
1458 C  CD2  . LEU   A 203 ? 0.1381 0.3010 0.1642 -0.0161 -0.0245 -0.0664 355 LEU   A CD2  
1459 N  N    . SER   A 204 ? 0.1361 0.3544 0.1853 -0.0100 -0.0288 -0.0666 356 SER   A N    
1460 C  CA   . SER   A 204 ? 0.2229 0.4557 0.2725 -0.0133 -0.0275 -0.0630 356 SER   A CA   
1461 C  C    . SER   A 204 ? 0.2244 0.4817 0.2715 -0.0165 -0.0222 -0.0659 356 SER   A C    
1462 O  O    . SER   A 204 ? 0.2452 0.5102 0.2857 -0.0282 -0.0173 -0.0632 356 SER   A O    
1463 C  CB   . SER   A 204 ? 0.2319 0.4689 0.2929 -0.0005 -0.0338 -0.0622 356 SER   A CB   
1464 O  OG   . SER   A 204 ? 0.3568 0.5754 0.4192 -0.0009 -0.0378 -0.0570 356 SER   A OG   
1465 N  N    . ASN   A 205 ? 0.2146 0.4849 0.2669 -0.0063 -0.0230 -0.0725 357 ASN   A N    
1466 C  CA   . ASN   A 205 ? 0.2792 0.5745 0.3286 -0.0090 -0.0178 -0.0757 357 ASN   A CA   
1467 C  C    . ASN   A 205 ? 0.2279 0.5224 0.2667 -0.0243 -0.0113 -0.0729 357 ASN   A C    
1468 O  O    . ASN   A 205 ? 0.2264 0.5375 0.2605 -0.0338 -0.0062 -0.0718 357 ASN   A O    
1469 C  CB   . ASN   A 205 ? 0.3985 0.7047 0.4536 0.0042  -0.0192 -0.0844 357 ASN   A CB   
1470 C  CG   . ASN   A 205 ? 0.5415 0.8503 0.6084 0.0200  -0.0249 -0.0878 357 ASN   A CG   
1471 O  OD1  . ASN   A 205 ? 0.5873 0.8950 0.6609 0.0320  -0.0275 -0.0957 357 ASN   A OD1  
1472 N  ND2  . ASN   A 205 ? 0.6081 0.9206 0.6779 0.0202  -0.0268 -0.0818 357 ASN   A ND2  
1473 N  N    . THR   A 206 ? 0.2251 0.5008 0.2600 -0.0271 -0.0114 -0.0716 358 THR   A N    
1474 C  CA   . THR   A 206 ? 0.2027 0.4772 0.2281 -0.0411 -0.0056 -0.0678 358 THR   A CA   
1475 C  C    . THR   A 206 ? 0.1992 0.4665 0.2192 -0.0556 -0.0018 -0.0626 358 THR   A C    
1476 O  O    . THR   A 206 ? 0.2140 0.4907 0.2276 -0.0684 0.0044  -0.0609 358 THR   A O    
1477 C  CB   . THR   A 206 ? 0.1772 0.4325 0.1991 -0.0397 -0.0075 -0.0668 358 THR   A CB   
1478 O  OG1  . THR   A 206 ? 0.2037 0.4675 0.2296 -0.0271 -0.0100 -0.0734 358 THR   A OG1  
1479 C  CG2  . THR   A 206 ? 0.1883 0.4410 0.2000 -0.0536 -0.0013 -0.0612 358 THR   A CG2  
1480 N  N    . LEU   A 207 ? 0.1600 0.4106 0.1817 -0.0541 -0.0053 -0.0603 359 LEU   A N    
1481 C  CA   . LEU   A 207 ? 0.1731 0.4161 0.1889 -0.0671 -0.0016 -0.0568 359 LEU   A CA   
1482 C  C    . LEU   A 207 ? 0.1866 0.4528 0.2029 -0.0701 0.0007  -0.0585 359 LEU   A C    
1483 O  O    . LEU   A 207 ? 0.1580 0.4271 0.1667 -0.0838 0.0065  -0.0581 359 LEU   A O    
1484 C  CB   . LEU   A 207 ? 0.1324 0.3539 0.1496 -0.0638 -0.0060 -0.0541 359 LEU   A CB   
1485 C  CG   . LEU   A 207 ? 0.2013 0.4190 0.2146 -0.0721 -0.0039 -0.0520 359 LEU   A CG   
1486 C  CD1  . LEU   A 207 ? 0.2005 0.4025 0.2035 -0.0873 0.0033  -0.0508 359 LEU   A CD1  
1487 C  CD2  . LEU   A 207 ? 0.2000 0.4047 0.2175 -0.0642 -0.0102 -0.0494 359 LEU   A CD2  
1488 N  N    . GLN   A 208 ? 0.2204 0.5026 0.2449 -0.0574 -0.0039 -0.0607 360 GLN   A N    
1489 C  CA   . GLN   A 208 ? 0.2925 0.6004 0.3174 -0.0589 -0.0022 -0.0623 360 GLN   A CA   
1490 C  C    . GLN   A 208 ? 0.3090 0.6337 0.3277 -0.0681 0.0039  -0.0648 360 GLN   A C    
1491 O  O    . GLN   A 208 ? 0.3126 0.6493 0.3253 -0.0790 0.0078  -0.0654 360 GLN   A O    
1492 C  CB   . GLN   A 208 ? 0.3425 0.6653 0.3776 -0.0418 -0.0080 -0.0643 360 GLN   A CB   
1493 C  CG   . GLN   A 208 ? 0.4094 0.7197 0.4506 -0.0329 -0.0146 -0.0608 360 GLN   A CG   
1494 C  CD   . GLN   A 208 ? 0.5280 0.8466 0.5803 -0.0147 -0.0206 -0.0628 360 GLN   A CD   
1495 O  OE1  . GLN   A 208 ? 0.5413 0.8502 0.6001 -0.0057 -0.0264 -0.0595 360 GLN   A OE1  
1496 N  NE2  . GLN   A 208 ? 0.5766 0.9132 0.6310 -0.0090 -0.0189 -0.0683 360 GLN   A NE2  
1497 N  N    . THR   A 209 ? 0.2663 0.5929 0.2856 -0.0643 0.0045  -0.0665 361 THR   A N    
1498 C  CA   . THR   A 209 ? 0.2253 0.5695 0.2381 -0.0728 0.0096  -0.0680 361 THR   A CA   
1499 C  C    . THR   A 209 ? 0.2647 0.5937 0.2668 -0.0915 0.0146  -0.0643 361 THR   A C    
1500 O  O    . THR   A 209 ? 0.2770 0.6168 0.2725 -0.1030 0.0178  -0.0649 361 THR   A O    
1501 C  CB   . THR   A 209 ? 0.2379 0.5895 0.2535 -0.0630 0.0086  -0.0708 361 THR   A CB   
1502 O  OG1  . THR   A 209 ? 0.2522 0.6138 0.2774 -0.0455 0.0037  -0.0758 361 THR   A OG1  
1503 C  CG2  . THR   A 209 ? 0.2167 0.5885 0.2248 -0.0714 0.0125  -0.0717 361 THR   A CG2  
1504 N  N    . TYR   A 210 ? 0.2523 0.5543 0.2530 -0.0945 0.0148  -0.0607 362 TYR   A N    
1505 C  CA   . TYR   A 210 ? 0.2515 0.5331 0.2430 -0.1108 0.0200  -0.0571 362 TYR   A CA   
1506 C  C    . TYR   A 210 ? 0.2623 0.5421 0.2488 -0.1205 0.0220  -0.0590 362 TYR   A C    
1507 O  O    . TYR   A 210 ? 0.2935 0.5672 0.2732 -0.1341 0.0267  -0.0588 362 TYR   A O    
1508 C  CB   . TYR   A 210 ? 0.2122 0.4649 0.2036 -0.1101 0.0201  -0.0530 362 TYR   A CB   
1509 C  CG   . TYR   A 210 ? 0.2487 0.4749 0.2314 -0.1238 0.0270  -0.0480 362 TYR   A CG   
1510 C  CD1  . TYR   A 210 ? 0.2200 0.4276 0.1976 -0.1319 0.0293  -0.0491 362 TYR   A CD1  
1511 C  CD2  . TYR   A 210 ? 0.2758 0.4943 0.2553 -0.1263 0.0320  -0.0417 362 TYR   A CD2  
1512 C  CE1  . TYR   A 210 ? 0.2452 0.4252 0.2159 -0.1419 0.0362  -0.0454 362 TYR   A CE1  
1513 C  CE2  . TYR   A 210 ? 0.3000 0.4900 0.2723 -0.1357 0.0393  -0.0355 362 TYR   A CE2  
1514 C  CZ   . TYR   A 210 ? 0.3526 0.5226 0.3212 -0.1433 0.0413  -0.0380 362 TYR   A CZ   
1515 O  OH   . TYR   A 210 ? 0.4364 0.5772 0.3994 -0.1508 0.0490  -0.0329 362 TYR   A OH   
1516 N  N    . ILE   A 211 ? 0.2137 0.4985 0.2046 -0.1134 0.0185  -0.0607 363 ILE   A N    
1517 C  CA   . ILE   A 211 ? 0.2361 0.5249 0.2224 -0.1219 0.0204  -0.0632 363 ILE   A CA   
1518 C  C    . ILE   A 211 ? 0.2859 0.6032 0.2699 -0.1270 0.0220  -0.0668 363 ILE   A C    
1519 O  O    . ILE   A 211 ? 0.2831 0.5999 0.2598 -0.1409 0.0259  -0.0694 363 ILE   A O    
1520 C  CB   . ILE   A 211 ? 0.2367 0.5279 0.2294 -0.1120 0.0159  -0.0625 363 ILE   A CB   
1521 C  CG1  . ILE   A 211 ? 0.2605 0.5215 0.2529 -0.1108 0.0147  -0.0593 363 ILE   A CG1  
1522 C  CG2  . ILE   A 211 ? 0.2091 0.5162 0.1981 -0.1189 0.0175  -0.0656 363 ILE   A CG2  
1523 C  CD1  . ILE   A 211 ? 0.2443 0.5064 0.2455 -0.0973 0.0079  -0.0571 363 ILE   A CD1  
1524 N  N    . ARG   A 212 ? 0.3045 0.6465 0.2952 -0.1155 0.0190  -0.0678 364 ARG   A N    
1525 C  CA   . ARG   A 212 ? 0.3273 0.6991 0.3162 -0.1188 0.0199  -0.0714 364 ARG   A CA   
1526 C  C    . ARG   A 212 ? 0.3471 0.7173 0.3291 -0.1327 0.0235  -0.0716 364 ARG   A C    
1527 O  O    . ARG   A 212 ? 0.3886 0.7755 0.3667 -0.1426 0.0254  -0.0746 364 ARG   A O    
1528 C  CB   . ARG   A 212 ? 0.3456 0.7413 0.3435 -0.1016 0.0162  -0.0728 364 ARG   A CB   
1529 C  CG   . ARG   A 212 ? 0.4334 0.8323 0.4408 -0.0871 0.0117  -0.0719 364 ARG   A CG   
1530 C  CD   . ARG   A 212 ? 0.5372 0.9618 0.5526 -0.0713 0.0084  -0.0746 364 ARG   A CD   
1531 N  NE   . ARG   A 212 ? 0.6093 1.0216 0.6346 -0.0544 0.0034  -0.0740 364 ARG   A NE   
1532 C  CZ   . ARG   A 212 ? 0.6345 1.0392 0.6612 -0.0491 0.0032  -0.0758 364 ARG   A CZ   
1533 N  NH1  . ARG   A 212 ? 0.6165 1.0262 0.6355 -0.0589 0.0077  -0.0769 364 ARG   A NH1  
1534 N  NH2  . ARG   A 212 ? 0.6443 1.0369 0.6795 -0.0341 -0.0019 -0.0766 364 ARG   A NH2  
1535 N  N    . CYS   A 213 ? 0.3368 0.6882 0.3187 -0.1335 0.0246  -0.0677 365 CYS   A N    
1536 C  CA   . CYS   A 213 ? 0.3563 0.7016 0.3342 -0.1466 0.0291  -0.0650 365 CYS   A CA   
1537 C  C    . CYS   A 213 ? 0.3866 0.7080 0.3582 -0.1623 0.0346  -0.0647 365 CYS   A C    
1538 O  O    . CYS   A 213 ? 0.4495 0.7673 0.4184 -0.1744 0.0399  -0.0629 365 CYS   A O    
1539 C  CB   . CYS   A 213 ? 0.3914 0.7227 0.3712 -0.1419 0.0300  -0.0590 365 CYS   A CB   
1540 S  SG   . CYS   A 213 ? 0.4347 0.7939 0.4212 -0.1245 0.0248  -0.0610 365 CYS   A SG   
1541 N  N    . ARG   A 214 ? 0.3653 0.6703 0.3351 -0.1618 0.0341  -0.0664 366 ARG   A N    
1542 C  CA   . ARG   A 214 ? 0.4508 0.7307 0.4147 -0.1748 0.0396  -0.0675 366 ARG   A CA   
1543 C  C    . ARG   A 214 ? 0.4775 0.7729 0.4380 -0.1811 0.0398  -0.0746 366 ARG   A C    
1544 O  O    . ARG   A 214 ? 0.5213 0.8082 0.4770 -0.1952 0.0454  -0.0778 366 ARG   A O    
1545 C  CB   . ARG   A 214 ? 0.5257 0.7735 0.4891 -0.1701 0.0398  -0.0642 366 ARG   A CB   
1546 C  CG   . ARG   A 214 ? 0.6157 0.8437 0.5740 -0.1776 0.0432  -0.0679 366 ARG   A CG   
1547 C  CD   . ARG   A 214 ? 0.6621 0.8702 0.6215 -0.1683 0.0406  -0.0656 366 ARG   A CD   
1548 N  NE   . ARG   A 214 ? 0.7088 0.8904 0.6630 -0.1755 0.0455  -0.0679 366 ARG   A NE   
1549 C  CZ   . ARG   A 214 ? 0.6946 0.8644 0.6485 -0.1700 0.0437  -0.0683 366 ARG   A CZ   
1550 N  NH1  . ARG   A 214 ? 0.7154 0.8630 0.6645 -0.1764 0.0489  -0.0712 366 ARG   A NH1  
1551 N  NH2  . ARG   A 214 ? 0.6765 0.8571 0.6358 -0.1579 0.0370  -0.0657 366 ARG   A NH2  
1552 N  N    . HIS   A 215 ? 0.4619 0.7807 0.4254 -0.1710 0.0347  -0.0768 367 HIS   A N    
1553 C  CA   . HIS   A 215 ? 0.4484 0.7842 0.4091 -0.1755 0.0352  -0.0823 367 HIS   A CA   
1554 C  C    . HIS   A 215 ? 0.3898 0.7652 0.3544 -0.1683 0.0317  -0.0839 367 HIS   A C    
1555 O  O    . HIS   A 215 ? 0.3952 0.7812 0.3671 -0.1528 0.0274  -0.0805 367 HIS   A O    
1556 C  CB   . HIS   A 215 ? 0.4979 0.8214 0.4596 -0.1690 0.0336  -0.0814 367 HIS   A CB   
1557 C  CG   . HIS   A 215 ? 0.6115 0.8997 0.5679 -0.1773 0.0379  -0.0820 367 HIS   A CG   
1558 N  ND1  . HIS   A 215 ? 0.6638 0.9418 0.6136 -0.1930 0.0443  -0.0872 367 HIS   A ND1  
1559 C  CD2  . HIS   A 215 ? 0.6399 0.9008 0.5973 -0.1715 0.0372  -0.0782 367 HIS   A CD2  
1560 C  CE1  . HIS   A 215 ? 0.6792 0.9244 0.6263 -0.1955 0.0478  -0.0866 367 HIS   A CE1  
1561 N  NE2  . HIS   A 215 ? 0.6653 0.9002 0.6165 -0.1827 0.0433  -0.0810 367 HIS   A NE2  
1562 N  N    . PRO   A 216 ? 0.4198 0.8181 0.3805 -0.1783 0.0338  -0.0893 368 PRO   A N    
1563 C  CA   . PRO   A 216 ? 0.3917 0.8295 0.3561 -0.1705 0.0308  -0.0907 368 PRO   A CA   
1564 C  C    . PRO   A 216 ? 0.3642 0.8143 0.3329 -0.1598 0.0281  -0.0896 368 PRO   A C    
1565 O  O    . PRO   A 216 ? 0.3470 0.7791 0.3139 -0.1625 0.0291  -0.0894 368 PRO   A O    
1566 C  CB   . PRO   A 216 ? 0.4334 0.8891 0.3913 -0.1875 0.0346  -0.0970 368 PRO   A CB   
1567 C  CG   . PRO   A 216 ? 0.4643 0.8866 0.4165 -0.2039 0.0402  -0.0987 368 PRO   A CG   
1568 C  CD   . PRO   A 216 ? 0.4411 0.8304 0.3943 -0.1972 0.0397  -0.0948 368 PRO   A CD   
1569 N  N    . PRO   A 217 ? 0.3531 0.8339 0.3285 -0.1469 0.0246  -0.0885 369 PRO   A N    
1570 C  CA   . PRO   A 217 ? 0.3382 0.8343 0.3187 -0.1376 0.0219  -0.0867 369 PRO   A CA   
1571 C  C    . PRO   A 217 ? 0.3644 0.8774 0.3380 -0.1516 0.0252  -0.0920 369 PRO   A C    
1572 O  O    . PRO   A 217 ? 0.3696 0.8920 0.3376 -0.1655 0.0284  -0.0974 369 PRO   A O    
1573 C  CB   . PRO   A 217 ? 0.3438 0.8686 0.3333 -0.1208 0.0178  -0.0846 369 PRO   A CB   
1574 C  CG   . PRO   A 217 ? 0.3850 0.9181 0.3711 -0.1257 0.0196  -0.0878 369 PRO   A CG   
1575 C  CD   . PRO   A 217 ? 0.3681 0.8676 0.3482 -0.1376 0.0225  -0.0879 369 PRO   A CD   
1576 N  N    . PRO   A 218 ? 0.3422 0.8598 0.3172 -0.1488 0.0242  -0.0907 370 PRO   A N    
1577 C  CA   . PRO   A 218 ? 0.3104 0.8160 0.2940 -0.1331 0.0194  -0.0836 370 PRO   A CA   
1578 C  C    . PRO   A 218 ? 0.2718 0.7374 0.2528 -0.1375 0.0206  -0.0822 370 PRO   A C    
1579 O  O    . PRO   A 218 ? 0.2761 0.7280 0.2638 -0.1257 0.0162  -0.0764 370 PRO   A O    
1580 C  CB   . PRO   A 218 ? 0.3273 0.8608 0.3120 -0.1312 0.0181  -0.0831 370 PRO   A CB   
1581 C  CG   . PRO   A 218 ? 0.3505 0.8911 0.3252 -0.1511 0.0239  -0.0914 370 PRO   A CG   
1582 C  CD   . PRO   A 218 ? 0.3629 0.8978 0.3334 -0.1610 0.0269  -0.0959 370 PRO   A CD   
1583 N  N    . GLY   A 219 ? 0.2750 0.7219 0.2462 -0.1540 0.0261  -0.0876 371 GLY   A N    
1584 C  CA   . GLY   A 219 ? 0.2378 0.6471 0.2058 -0.1582 0.0278  -0.0868 371 GLY   A CA   
1585 C  C    . GLY   A 219 ? 0.2519 0.6375 0.2265 -0.1460 0.0241  -0.0803 371 GLY   A C    
1586 O  O    . GLY   A 219 ? 0.2349 0.5967 0.2108 -0.1423 0.0227  -0.0771 371 GLY   A O    
1587 N  N    . SER   A 220 ? 0.2585 0.6520 0.2372 -0.1397 0.0224  -0.0788 372 SER   A N    
1588 C  CA   . SER   A 220 ? 0.2592 0.6350 0.2449 -0.1275 0.0189  -0.0736 372 SER   A CA   
1589 C  C    . SER   A 220 ? 0.2860 0.6618 0.2814 -0.1120 0.0128  -0.0685 372 SER   A C    
1590 O  O    . SER   A 220 ? 0.2763 0.6267 0.2743 -0.1069 0.0104  -0.0650 372 SER   A O    
1591 C  CB   . SER   A 220 ? 0.2638 0.6563 0.2526 -0.1223 0.0182  -0.0742 372 SER   A CB   
1592 O  OG   . SER   A 220 ? 0.3124 0.7372 0.3076 -0.1122 0.0151  -0.0744 372 SER   A OG   
1593 N  N    . HIS   A 221 ? 0.3058 0.7101 0.3063 -0.1042 0.0096  -0.0678 373 HIS   A N    
1594 C  CA   . HIS   A 221 ? 0.2642 0.6685 0.2737 -0.0892 0.0029  -0.0622 373 HIS   A CA   
1595 C  C    . HIS   A 221 ? 0.2677 0.6591 0.2736 -0.0944 0.0029  -0.0604 373 HIS   A C    
1596 O  O    . HIS   A 221 ? 0.2609 0.6389 0.2722 -0.0847 -0.0024 -0.0551 373 HIS   A O    
1597 C  CB   . HIS   A 221 ? 0.2651 0.7037 0.2807 -0.0787 -0.0005 -0.0610 373 HIS   A CB   
1598 C  CG   . HIS   A 221 ? 0.3130 0.7686 0.3314 -0.0735 0.0000  -0.0638 373 HIS   A CG   
1599 N  ND1  . HIS   A 221 ? 0.3058 0.7504 0.3311 -0.0615 -0.0030 -0.0629 373 HIS   A ND1  
1600 C  CD2  . HIS   A 221 ? 0.3099 0.7943 0.3248 -0.0786 0.0031  -0.0680 373 HIS   A CD2  
1601 C  CE1  . HIS   A 221 ? 0.3005 0.7664 0.3263 -0.0592 -0.0015 -0.0665 373 HIS   A CE1  
1602 N  NE2  . HIS   A 221 ? 0.3104 0.8006 0.3299 -0.0694 0.0020  -0.0693 373 HIS   A NE2  
1603 N  N    . GLN   A 222 ? 0.2429 0.6386 0.2394 -0.1098 0.0086  -0.0653 374 GLN   A N    
1604 C  CA   . GLN   A 222 ? 0.2559 0.6403 0.2484 -0.1149 0.0093  -0.0649 374 GLN   A CA   
1605 C  C    . GLN   A 222 ? 0.2427 0.5888 0.2328 -0.1170 0.0101  -0.0638 374 GLN   A C    
1606 O  O    . GLN   A 222 ? 0.3090 0.6424 0.2997 -0.1138 0.0075  -0.0605 374 GLN   A O    
1607 C  CB   . GLN   A 222 ? 0.2425 0.6418 0.2254 -0.1309 0.0157  -0.0722 374 GLN   A CB   
1608 C  CG   . GLN   A 222 ? 0.2683 0.7084 0.2528 -0.1297 0.0152  -0.0736 374 GLN   A CG   
1609 C  CD   . GLN   A 222 ? 0.3384 0.7936 0.3130 -0.1473 0.0221  -0.0826 374 GLN   A CD   
1610 O  OE1  . GLN   A 222 ? 0.3538 0.8439 0.3282 -0.1485 0.0223  -0.0845 374 GLN   A OE1  
1611 N  NE2  . GLN   A 222 ? 0.3720 0.8010 0.3382 -0.1608 0.0277  -0.0884 374 GLN   A NE2  
1612 N  N    . LEU   A 223 ? 0.2322 0.5607 0.2190 -0.1219 0.0134  -0.0659 375 LEU   A N    
1613 C  CA   . LEU   A 223 ? 0.3028 0.5964 0.2876 -0.1225 0.0141  -0.0641 375 LEU   A CA   
1614 C  C    . LEU   A 223 ? 0.3244 0.6094 0.3189 -0.1072 0.0069  -0.0578 375 LEU   A C    
1615 O  O    . LEU   A 223 ? 0.3134 0.5797 0.3084 -0.1039 0.0043  -0.0547 375 LEU   A O    
1616 C  CB   . LEU   A 223 ? 0.3273 0.6060 0.3059 -0.1318 0.0194  -0.0672 375 LEU   A CB   
1617 C  CG   . LEU   A 223 ? 0.4053 0.6486 0.3815 -0.1319 0.0205  -0.0648 375 LEU   A CG   
1618 C  CD1  . LEU   A 223 ? 0.4145 0.6398 0.3833 -0.1402 0.0245  -0.0677 375 LEU   A CD1  
1619 C  CD2  . LEU   A 223 ? 0.4403 0.6725 0.4130 -0.1373 0.0241  -0.0654 375 LEU   A CD2  
1620 N  N    . TYR   A 224 ? 0.3099 0.6084 0.3118 -0.0975 0.0035  -0.0565 376 TYR   A N    
1621 C  CA   . TYR   A 224 ? 0.2953 0.5860 0.3065 -0.0824 -0.0036 -0.0520 376 TYR   A CA   
1622 C  C    . TYR   A 224 ? 0.2893 0.5827 0.3045 -0.0748 -0.0094 -0.0474 376 TYR   A C    
1623 O  O    . TYR   A 224 ? 0.2858 0.5610 0.3047 -0.0677 -0.0141 -0.0435 376 TYR   A O    
1624 C  CB   . TYR   A 224 ? 0.2673 0.5773 0.2859 -0.0723 -0.0061 -0.0529 376 TYR   A CB   
1625 C  CG   . TYR   A 224 ? 0.2500 0.5498 0.2778 -0.0570 -0.0128 -0.0503 376 TYR   A CG   
1626 C  CD1  . TYR   A 224 ? 0.2925 0.5663 0.3195 -0.0570 -0.0133 -0.0499 376 TYR   A CD1  
1627 C  CD2  . TYR   A 224 ? 0.2805 0.5966 0.3177 -0.0424 -0.0186 -0.0485 376 TYR   A CD2  
1628 C  CE1  . TYR   A 224 ? 0.3181 0.5830 0.3531 -0.0437 -0.0194 -0.0489 376 TYR   A CE1  
1629 C  CE2  . TYR   A 224 ? 0.2979 0.6032 0.3437 -0.0286 -0.0245 -0.0471 376 TYR   A CE2  
1630 C  CZ   . TYR   A 224 ? 0.3463 0.6264 0.3909 -0.0297 -0.0249 -0.0479 376 TYR   A CZ   
1631 O  OH   . TYR   A 224 ? 0.3684 0.6385 0.4217 -0.0165 -0.0307 -0.0479 376 TYR   A OH   
1632 N  N    . ALA   A 225 ? 0.2643 0.5818 0.2785 -0.0767 -0.0090 -0.0474 377 ALA   A N    
1633 C  CA   . ALA   A 225 ? 0.2773 0.6004 0.2944 -0.0702 -0.0140 -0.0419 377 ALA   A CA   
1634 C  C    . ALA   A 225 ? 0.2386 0.5405 0.2491 -0.0782 -0.0122 -0.0416 377 ALA   A C    
1635 O  O    . ALA   A 225 ? 0.2706 0.5649 0.2840 -0.0714 -0.0173 -0.0360 377 ALA   A O    
1636 C  CB   . ALA   A 225 ? 0.2770 0.6342 0.2937 -0.0710 -0.0133 -0.0421 377 ALA   A CB   
1637 N  N    . LYS   A 226 ? 0.2046 0.4968 0.2060 -0.0925 -0.0048 -0.0476 378 LYS   A N    
1638 C  CA   . LYS   A 226 ? 0.1763 0.4474 0.1711 -0.0994 -0.0022 -0.0483 378 LYS   A CA   
1639 C  C    . LYS   A 226 ? 0.2022 0.4426 0.1987 -0.0944 -0.0046 -0.0454 378 LYS   A C    
1640 O  O    . LYS   A 226 ? 0.2097 0.4350 0.2041 -0.0943 -0.0057 -0.0432 378 LYS   A O    
1641 C  CB   . LYS   A 226 ? 0.1818 0.4493 0.1665 -0.1150 0.0067  -0.0561 378 LYS   A CB   
1642 C  CG   . LYS   A 226 ? 0.2577 0.5544 0.2389 -0.1222 0.0096  -0.0602 378 LYS   A CG   
1643 C  CD   . LYS   A 226 ? 0.3132 0.6059 0.2849 -0.1379 0.0184  -0.0693 378 LYS   A CD   
1644 C  CE   . LYS   A 226 ? 0.3429 0.6696 0.3120 -0.1453 0.0212  -0.0744 378 LYS   A CE   
1645 N  NZ   . LYS   A 226 ? 0.3455 0.6906 0.3152 -0.1441 0.0194  -0.0732 378 LYS   A NZ   
1646 N  N    . MET   A 227 ? 0.1931 0.4262 0.1933 -0.0903 -0.0053 -0.0454 379 MET   A N    
1647 C  CA   . MET   A 227 ? 0.2156 0.4227 0.2176 -0.0854 -0.0077 -0.0430 379 MET   A CA   
1648 C  C    . MET   A 227 ? 0.2212 0.4295 0.2321 -0.0721 -0.0166 -0.0374 379 MET   A C    
1649 O  O    . MET   A 227 ? 0.2194 0.4086 0.2304 -0.0697 -0.0191 -0.0346 379 MET   A O    
1650 C  CB   . MET   A 227 ? 0.2061 0.4079 0.2084 -0.0863 -0.0051 -0.0453 379 MET   A CB   
1651 C  CG   . MET   A 227 ? 0.2584 0.4525 0.2511 -0.0999 0.0036  -0.0496 379 MET   A CG   
1652 S  SD   . MET   A 227 ? 0.3501 0.5448 0.3435 -0.1007 0.0061  -0.0509 379 MET   A SD   
1653 C  CE   . MET   A 227 ? 0.3805 0.6000 0.3859 -0.0859 -0.0016 -0.0497 379 MET   A CE   
1654 N  N    . ILE   A 228 ? 0.2417 0.4723 0.2602 -0.0631 -0.0211 -0.0355 380 ILE   A N    
1655 C  CA   . ILE   A 228 ? 0.2814 0.5140 0.3090 -0.0499 -0.0293 -0.0294 380 ILE   A CA   
1656 C  C    . ILE   A 228 ? 0.2700 0.5013 0.2949 -0.0515 -0.0312 -0.0244 380 ILE   A C    
1657 O  O    . ILE   A 228 ? 0.3021 0.5205 0.3307 -0.0458 -0.0362 -0.0193 380 ILE   A O    
1658 C  CB   . ILE   A 228 ? 0.3509 0.6091 0.3868 -0.0394 -0.0327 -0.0280 380 ILE   A CB   
1659 C  CG1  . ILE   A 228 ? 0.4183 0.6763 0.4588 -0.0344 -0.0323 -0.0326 380 ILE   A CG1  
1660 C  CG2  . ILE   A 228 ? 0.3277 0.5901 0.3725 -0.0261 -0.0404 -0.0196 380 ILE   A CG2  
1661 C  CD1  . ILE   A 228 ? 0.4641 0.7462 0.5133 -0.0224 -0.0353 -0.0318 380 ILE   A CD1  
1662 N  N    . GLN   A 229 ? 0.2444 0.4909 0.2628 -0.0598 -0.0271 -0.0259 381 GLN   A N    
1663 C  CA   . GLN   A 229 ? 0.2680 0.5170 0.2829 -0.0619 -0.0281 -0.0217 381 GLN   A CA   
1664 C  C    . GLN   A 229 ? 0.2623 0.4839 0.2717 -0.0676 -0.0262 -0.0227 381 GLN   A C    
1665 O  O    . GLN   A 229 ? 0.2568 0.4741 0.2669 -0.0646 -0.0298 -0.0169 381 GLN   A O    
1666 C  CB   . GLN   A 229 ? 0.2501 0.5219 0.2584 -0.0711 -0.0228 -0.0254 381 GLN   A CB   
1667 C  CG   . GLN   A 229 ? 0.3705 0.6524 0.3756 -0.0725 -0.0239 -0.0211 381 GLN   A CG   
1668 C  CD   . GLN   A 229 ? 0.4315 0.7182 0.4446 -0.0587 -0.0323 -0.0096 381 GLN   A CD   
1669 O  OE1  . GLN   A 229 ? 0.4093 0.6842 0.4214 -0.0577 -0.0347 -0.0045 381 GLN   A OE1  
1670 N  NE2  . GLN   A 229 ? 0.4887 0.7928 0.5098 -0.0478 -0.0364 -0.0049 381 GLN   A NE2  
1671 N  N    . LYS   A 230 ? 0.2718 0.4751 0.2759 -0.0753 -0.0203 -0.0291 382 LYS   A N    
1672 C  CA   . LYS   A 230 ? 0.2890 0.4653 0.2883 -0.0791 -0.0179 -0.0298 382 LYS   A CA   
1673 C  C    . LYS   A 230 ? 0.2711 0.4331 0.2773 -0.0698 -0.0246 -0.0247 382 LYS   A C    
1674 O  O    . LYS   A 230 ? 0.2237 0.3705 0.2279 -0.0706 -0.0251 -0.0224 382 LYS   A O    
1675 C  CB   . LYS   A 230 ? 0.3221 0.4826 0.3151 -0.0873 -0.0102 -0.0361 382 LYS   A CB   
1676 C  CG   . LYS   A 230 ? 0.3662 0.5324 0.3507 -0.0988 -0.0025 -0.0421 382 LYS   A CG   
1677 C  CD   . LYS   A 230 ? 0.3717 0.5231 0.3499 -0.1032 0.0007  -0.0433 382 LYS   A CD   
1678 C  CE   . LYS   A 230 ? 0.4278 0.5917 0.3991 -0.1135 0.0070  -0.0497 382 LYS   A CE   
1679 N  NZ   . LYS   A 230 ? 0.4410 0.6356 0.4150 -0.1120 0.0031  -0.0474 382 LYS   A NZ   
1680 N  N    . LEU   A 231 ? 0.2381 0.4059 0.2529 -0.0611 -0.0293 -0.0233 383 LEU   A N    
1681 C  CA   . LEU   A 231 ? 0.2276 0.3848 0.2504 -0.0520 -0.0361 -0.0190 383 LEU   A CA   
1682 C  C    . LEU   A 231 ? 0.1959 0.3629 0.2240 -0.0459 -0.0423 -0.0102 383 LEU   A C    
1683 O  O    . LEU   A 231 ? 0.1960 0.3478 0.2264 -0.0430 -0.0451 -0.0052 383 LEU   A O    
1684 C  CB   . LEU   A 231 ? 0.2318 0.3945 0.2630 -0.0436 -0.0390 -0.0213 383 LEU   A CB   
1685 C  CG   . LEU   A 231 ? 0.2327 0.3848 0.2591 -0.0486 -0.0335 -0.0280 383 LEU   A CG   
1686 C  CD1  . LEU   A 231 ? 0.2345 0.3974 0.2687 -0.0400 -0.0360 -0.0311 383 LEU   A CD1  
1687 C  CD2  . LEU   A 231 ? 0.2183 0.3446 0.2405 -0.0520 -0.0318 -0.0285 383 LEU   A CD2  
1688 N  N    . ALA   A 232 ? 0.1602 0.3506 0.1895 -0.0431 -0.0434 -0.0070 384 ALA   A N    
1689 C  CA   . ALA   A 232 ? 0.1602 0.3613 0.1925 -0.0376 -0.0480 0.0033  384 ALA   A CA   
1690 C  C    . ALA   A 232 ? 0.2068 0.4000 0.2299 -0.0471 -0.0450 0.0039  384 ALA   A C    
1691 O  O    . ALA   A 232 ? 0.2143 0.4042 0.2401 -0.0434 -0.0490 0.0129  384 ALA   A O    
1692 C  CB   . ALA   A 232 ? 0.1519 0.3811 0.1853 -0.0339 -0.0481 0.0059  384 ALA   A CB   
1693 N  N    . ASP   A 233 ? 0.2232 0.4131 0.2359 -0.0588 -0.0374 -0.0051 385 ASP   A N    
1694 C  CA   . ASP   A 233 ? 0.1918 0.3744 0.1959 -0.0671 -0.0335 -0.0063 385 ASP   A CA   
1695 C  C    . ASP   A 233 ? 0.2214 0.3786 0.2264 -0.0668 -0.0347 -0.0047 385 ASP   A C    
1696 O  O    . ASP   A 233 ? 0.2046 0.3600 0.2077 -0.0679 -0.0360 0.0004  385 ASP   A O    
1697 C  CB   . ASP   A 233 ? 0.1802 0.3614 0.1747 -0.0784 -0.0244 -0.0168 385 ASP   A CB   
1698 C  CG   . ASP   A 233 ? 0.2738 0.4830 0.2668 -0.0812 -0.0225 -0.0189 385 ASP   A CG   
1699 O  OD1  . ASP   A 233 ? 0.2674 0.4773 0.2547 -0.0901 -0.0154 -0.0274 385 ASP   A OD1  
1700 O  OD2  . ASP   A 233 ? 0.2689 0.4996 0.2667 -0.0743 -0.0277 -0.0114 385 ASP   A OD2  
1701 N  N    . LEU   A 234 ? 0.1692 0.3082 0.1767 -0.0655 -0.0340 -0.0087 386 LEU   A N    
1702 C  CA   . LEU   A 234 ? 0.1936 0.3091 0.2022 -0.0652 -0.0347 -0.0075 386 LEU   A CA   
1703 C  C    . LEU   A 234 ? 0.2067 0.3163 0.2232 -0.0545 -0.0400 0.0033  386 LEU   A C    
1704 O  O    . LEU   A 234 ? 0.1900 0.2829 0.2055 -0.0545 -0.0390 0.0065  386 LEU   A O    
1705 C  CB   . LEU   A 234 ? 0.2020 0.3021 0.2120 -0.0636 -0.0327 -0.0129 386 LEU   A CB   
1706 C  CG   . LEU   A 234 ? 0.1825 0.2710 0.1833 -0.0708 -0.0237 -0.0203 386 LEU   A CG   
1707 C  CD1  . LEU   A 234 ? 0.1785 0.2614 0.1812 -0.0687 -0.0224 -0.0238 386 LEU   A CD1  
1708 C  CD2  . LEU   A 234 ? 0.1447 0.2133 0.1400 -0.0739 -0.0195 -0.0204 386 LEU   A CD2  
1709 N  N    . ARG   A 235 ? 0.2232 0.3452 0.2482 -0.0452 -0.0451 0.0090  387 ARG   A N    
1710 C  CA   . ARG   A 235 ? 0.2517 0.3662 0.2849 -0.0352 -0.0493 0.0203  387 ARG   A CA   
1711 C  C    . ARG   A 235 ? 0.2514 0.3740 0.2803 -0.0388 -0.0494 0.0284  387 ARG   A C    
1712 O  O    . ARG   A 235 ? 0.2811 0.3879 0.3125 -0.0365 -0.0497 0.0353  387 ARG   A O    
1713 C  CB   . ARG   A 235 ? 0.2678 0.3961 0.3109 -0.0238 -0.0540 0.0255  387 ARG   A CB   
1714 C  CG   . ARG   A 235 ? 0.3330 0.4560 0.3815 -0.0187 -0.0540 0.0176  387 ARG   A CG   
1715 C  CD   . ARG   A 235 ? 0.3824 0.4763 0.4323 -0.0182 -0.0524 0.0130  387 ARG   A CD   
1716 N  NE   . ARG   A 235 ? 0.3973 0.4886 0.4540 -0.0109 -0.0533 0.0067  387 ARG   A NE   
1717 C  CZ   . ARG   A 235 ? 0.4263 0.5088 0.4942 0.0005  -0.0562 0.0093  387 ARG   A CZ   
1718 N  NH1  . ARG   A 235 ? 0.3703 0.4436 0.4444 0.0057  -0.0584 0.0196  387 ARG   A NH1  
1719 N  NH2  . ARG   A 235 ? 0.4752 0.5577 0.5484 0.0065  -0.0565 0.0014  387 ARG   A NH2  
1720 N  N    . SER   A 236 ? 0.2093 0.3587 0.2318 -0.0452 -0.0490 0.0273  388 SER   A N    
1721 C  CA   . SER   A 236 ? 0.2536 0.4152 0.2711 -0.0486 -0.0491 0.0347  388 SER   A CA   
1722 C  C    . SER   A 236 ? 0.2241 0.3719 0.2326 -0.0588 -0.0437 0.0278  388 SER   A C    
1723 O  O    . SER   A 236 ? 0.2344 0.3817 0.2408 -0.0596 -0.0433 0.0347  388 SER   A O    
1724 C  CB   . SER   A 236 ? 0.3295 0.5261 0.3428 -0.0513 -0.0498 0.0349  388 SER   A CB   
1725 O  OG   . SER   A 236 ? 0.3817 0.5808 0.3838 -0.0632 -0.0423 0.0218  388 SER   A OG   
1726 N  N    . LEU   A 237 ? 0.2441 0.3807 0.2475 -0.0660 -0.0389 0.0150  389 LEU   A N    
1727 C  CA   . LEU   A 237 ? 0.2241 0.3425 0.2208 -0.0727 -0.0333 0.0094  389 LEU   A CA   
1728 C  C    . LEU   A 237 ? 0.2145 0.3077 0.2173 -0.0657 -0.0343 0.0153  389 LEU   A C    
1729 O  O    . LEU   A 237 ? 0.1950 0.2796 0.1949 -0.0680 -0.0316 0.0166  389 LEU   A O    
1730 C  CB   . LEU   A 237 ? 0.2120 0.3213 0.2028 -0.0801 -0.0272 -0.0038 389 LEU   A CB   
1731 C  CG   . LEU   A 237 ? 0.2362 0.3601 0.2188 -0.0862 -0.0213 -0.0114 389 LEU   A CG   
1732 C  CD1  . LEU   A 237 ? 0.1943 0.3081 0.1749 -0.0881 -0.0159 -0.0197 389 LEU   A CD1  
1733 C  CD2  . LEU   A 237 ? 0.2305 0.3538 0.2044 -0.0931 -0.0155 -0.0158 389 LEU   A CD2  
1734 N  N    . ASN   A 238 ? 0.2256 0.3089 0.2371 -0.0574 -0.0378 0.0178  390 ASN   A N    
1735 C  CA   . ASN   A 238 ? 0.2119 0.2741 0.2306 -0.0513 -0.0393 0.0227  390 ASN   A CA   
1736 C  C    . ASN   A 238 ? 0.2370 0.3023 0.2592 -0.0489 -0.0415 0.0349  390 ASN   A C    
1737 O  O    . ASN   A 238 ? 0.2153 0.2699 0.2369 -0.0510 -0.0396 0.0372  390 ASN   A O    
1738 C  CB   . ASN   A 238 ? 0.1598 0.2150 0.1876 -0.0430 -0.0427 0.0220  390 ASN   A CB   
1739 C  CG   . ASN   A 238 ? 0.1878 0.2207 0.2219 -0.0392 -0.0432 0.0218  390 ASN   A CG   
1740 O  OD1  . ASN   A 238 ? 0.2101 0.2342 0.2452 -0.0406 -0.0425 0.0263  390 ASN   A OD1  
1741 N  ND2  . ASN   A 238 ? 0.1766 0.2030 0.2154 -0.0346 -0.0443 0.0160  390 ASN   A ND2  
1742 N  N    . GLU   A 239 ? 0.2452 0.3271 0.2712 -0.0442 -0.0454 0.0436  391 GLU   A N    
1743 C  CA   . GLU   A 239 ? 0.3505 0.4363 0.3800 -0.0414 -0.0474 0.0578  391 GLU   A CA   
1744 C  C    . GLU   A 239 ? 0.2993 0.3941 0.3194 -0.0498 -0.0438 0.0582  391 GLU   A C    
1745 O  O    . GLU   A 239 ? 0.2591 0.3468 0.2814 -0.0499 -0.0433 0.0664  391 GLU   A O    
1746 C  CB   . GLU   A 239 ? 0.4146 0.5211 0.4483 -0.0344 -0.0517 0.0678  391 GLU   A CB   
1747 C  CG   . GLU   A 239 ? 0.5568 0.6519 0.6025 -0.0235 -0.0550 0.0699  391 GLU   A CG   
1748 C  CD   . GLU   A 239 ? 0.6876 0.8070 0.7353 -0.0173 -0.0582 0.0721  391 GLU   A CD   
1749 O  OE1  . GLU   A 239 ? 0.7307 0.8742 0.7697 -0.0239 -0.0574 0.0662  391 GLU   A OE1  
1750 O  OE2  . GLU   A 239 ? 0.7211 0.8359 0.7798 -0.0059 -0.0612 0.0791  391 GLU   A OE2  
1751 N  N    . GLU   A 240 ? 0.2568 0.3671 0.2666 -0.0576 -0.0408 0.0486  392 GLU   A N    
1752 C  CA   . GLU   A 240 ? 0.2317 0.3525 0.2324 -0.0653 -0.0370 0.0473  392 GLU   A CA   
1753 C  C    . GLU   A 240 ? 0.2243 0.3232 0.2230 -0.0687 -0.0322 0.0408  392 GLU   A C    
1754 O  O    . GLU   A 240 ? 0.2472 0.3480 0.2437 -0.0710 -0.0301 0.0451  392 GLU   A O    
1755 C  CB   . GLU   A 240 ? 0.2133 0.3573 0.2042 -0.0734 -0.0348 0.0372  392 GLU   A CB   
1756 C  CG   . GLU   A 240 ? 0.2283 0.3872 0.2093 -0.0816 -0.0306 0.0341  392 GLU   A CG   
1757 C  CD   . GLU   A 240 ? 0.3077 0.4821 0.2901 -0.0783 -0.0334 0.0499  392 GLU   A CD   
1758 O  OE1  . GLU   A 240 ? 0.2991 0.4754 0.2765 -0.0826 -0.0297 0.0498  392 GLU   A OE1  
1759 O  OE2  . GLU   A 240 ? 0.3360 0.5212 0.3247 -0.0711 -0.0388 0.0630  392 GLU   A OE2  
1760 N  N    . HIS   A 241 ? 0.1666 0.2472 0.1662 -0.0685 -0.0302 0.0311  393 HIS   A N    
1761 C  CA   . HIS   A 241 ? 0.1786 0.2396 0.1776 -0.0694 -0.0262 0.0268  393 HIS   A CA   
1762 C  C    . HIS   A 241 ? 0.1795 0.2299 0.1877 -0.0645 -0.0290 0.0369  393 HIS   A C    
1763 O  O    . HIS   A 241 ? 0.1655 0.2113 0.1729 -0.0664 -0.0261 0.0380  393 HIS   A O    
1764 C  CB   . HIS   A 241 ? 0.1932 0.2383 0.1920 -0.0688 -0.0241 0.0169  393 HIS   A CB   
1765 C  CG   . HIS   A 241 ? 0.2005 0.2278 0.1995 -0.0679 -0.0204 0.0140  393 HIS   A CG   
1766 N  ND1  . HIS   A 241 ? 0.1972 0.2117 0.2046 -0.0624 -0.0232 0.0179  393 HIS   A ND1  
1767 C  CD2  . HIS   A 241 ? 0.1885 0.2104 0.1810 -0.0715 -0.0140 0.0075  393 HIS   A CD2  
1768 C  CE1  . HIS   A 241 ? 0.1963 0.2010 0.2022 -0.0625 -0.0192 0.0146  393 HIS   A CE1  
1769 N  NE2  . HIS   A 241 ? 0.2002 0.2083 0.1973 -0.0672 -0.0135 0.0088  393 HIS   A NE2  
1770 N  N    A SER   A 242 ? 0.2185 0.2648 0.2359 -0.0583 -0.0341 0.0439  394 SER   A N    
1771 N  N    B SER   A 242 ? 0.2184 0.2646 0.2358 -0.0583 -0.0341 0.0438  394 SER   A N    
1772 C  CA   A SER   A 242 ? 0.2327 0.2662 0.2600 -0.0548 -0.0363 0.0523  394 SER   A CA   
1773 C  CA   B SER   A 242 ? 0.2329 0.2665 0.2602 -0.0548 -0.0363 0.0523  394 SER   A CA   
1774 C  C    A SER   A 242 ? 0.2684 0.3123 0.2954 -0.0572 -0.0358 0.0640  394 SER   A C    
1775 C  C    B SER   A 242 ? 0.2676 0.3115 0.2945 -0.0573 -0.0358 0.0639  394 SER   A C    
1776 O  O    A SER   A 242 ? 0.2615 0.2972 0.2924 -0.0589 -0.0344 0.0677  394 SER   A O    
1777 O  O    B SER   A 242 ? 0.2617 0.2976 0.2923 -0.0590 -0.0343 0.0673  394 SER   A O    
1778 C  CB   A SER   A 242 ? 0.2221 0.2483 0.2596 -0.0476 -0.0411 0.0563  394 SER   A CB   
1779 C  CB   B SER   A 242 ? 0.2225 0.2491 0.2600 -0.0475 -0.0411 0.0565  394 SER   A CB   
1780 O  OG   A SER   A 242 ? 0.2280 0.2398 0.2758 -0.0455 -0.0425 0.0632  394 SER   A OG   
1781 O  OG   B SER   A 242 ? 0.2389 0.2582 0.2767 -0.0453 -0.0414 0.0457  394 SER   A OG   
1782 N  N    . LYS   A 243 ? 0.2801 0.3445 0.3025 -0.0577 -0.0369 0.0703  395 LYS   A N    
1783 C  CA   . LYS   A 243 ? 0.2655 0.3437 0.2863 -0.0601 -0.0362 0.0824  395 LYS   A CA   
1784 C  C    . LYS   A 243 ? 0.2124 0.2947 0.2253 -0.0670 -0.0308 0.0759  395 LYS   A C    
1785 O  O    . LYS   A 243 ? 0.2468 0.3289 0.2622 -0.0689 -0.0293 0.0836  395 LYS   A O    
1786 C  CB   . LYS   A 243 ? 0.3418 0.4464 0.3577 -0.0592 -0.0384 0.0893  395 LYS   A CB   
1787 C  CG   . LYS   A 243 ? 0.3748 0.4786 0.3996 -0.0504 -0.0436 0.0991  395 LYS   A CG   
1788 C  CD   . LYS   A 243 ? 0.4157 0.5508 0.4349 -0.0492 -0.0458 0.1047  395 LYS   A CD   
1789 C  CE   . LYS   A 243 ? 0.4698 0.6052 0.4976 -0.0393 -0.0506 0.1103  395 LYS   A CE   
1790 N  NZ   . LYS   A 243 ? 0.5155 0.6845 0.5397 -0.0362 -0.0534 0.1200  395 LYS   A NZ   
1791 N  N    . GLN   A 244 ? 0.1431 0.2292 0.1469 -0.0708 -0.0273 0.0618  396 GLN   A N    
1792 C  CA   . GLN   A 244 ? 0.2123 0.3005 0.2091 -0.0760 -0.0214 0.0545  396 GLN   A CA   
1793 C  C    . GLN   A 244 ? 0.2248 0.2918 0.2276 -0.0742 -0.0196 0.0516  396 GLN   A C    
1794 O  O    . GLN   A 244 ? 0.2208 0.2901 0.2232 -0.0762 -0.0163 0.0531  396 GLN   A O    
1795 C  CB   . GLN   A 244 ? 0.1821 0.2774 0.1683 -0.0807 -0.0173 0.0398  396 GLN   A CB   
1796 C  CG   . GLN   A 244 ? 0.2074 0.3279 0.1881 -0.0835 -0.0195 0.0414  396 GLN   A CG   
1797 C  CD   . GLN   A 244 ? 0.2206 0.3530 0.1901 -0.0912 -0.0142 0.0263  396 GLN   A CD   
1798 O  OE1  . GLN   A 244 ? 0.2312 0.3516 0.1967 -0.0942 -0.0080 0.0152  396 GLN   A OE1  
1799 N  NE2  . GLN   A 244 ? 0.2913 0.4476 0.2563 -0.0945 -0.0164 0.0255  396 GLN   A NE2  
1800 N  N    . TYR   A 245 ? 0.2488 0.2979 0.2574 -0.0701 -0.0219 0.0477  397 TYR   A N    
1801 C  CA   . TYR   A 245 ? 0.1729 0.2059 0.1878 -0.0682 -0.0210 0.0456  397 TYR   A CA   
1802 C  C    . TYR   A 245 ? 0.1832 0.2155 0.2072 -0.0684 -0.0231 0.0572  397 TYR   A C    
1803 O  O    . TYR   A 245 ? 0.1841 0.2151 0.2104 -0.0700 -0.0205 0.0571  397 TYR   A O    
1804 C  CB   . TYR   A 245 ? 0.2114 0.2292 0.2308 -0.0639 -0.0236 0.0399  397 TYR   A CB   
1805 C  CG   . TYR   A 245 ? 0.2125 0.2181 0.2386 -0.0620 -0.0234 0.0380  397 TYR   A CG   
1806 C  CD1  . TYR   A 245 ? 0.1965 0.1982 0.2182 -0.0615 -0.0189 0.0303  397 TYR   A CD1  
1807 C  CD2  . TYR   A 245 ? 0.2022 0.2009 0.2395 -0.0607 -0.0274 0.0439  397 TYR   A CD2  
1808 C  CE1  . TYR   A 245 ? 0.1708 0.1660 0.1987 -0.0593 -0.0191 0.0291  397 TYR   A CE1  
1809 C  CE2  . TYR   A 245 ? 0.2029 0.1943 0.2465 -0.0602 -0.0274 0.0409  397 TYR   A CE2  
1810 C  CZ   . TYR   A 245 ? 0.1844 0.1760 0.2231 -0.0592 -0.0235 0.0338  397 TYR   A CZ   
1811 O  OH   . TYR   A 245 ? 0.2051 0.1937 0.2501 -0.0581 -0.0239 0.0314  397 TYR   A OH   
1812 N  N    A ARG   A 246 ? 0.2249 0.2580 0.2550 -0.0667 -0.0275 0.0676  398 ARG   A N    
1813 N  N    B ARG   A 246 ? 0.2247 0.2576 0.2548 -0.0666 -0.0275 0.0675  398 ARG   A N    
1814 C  CA   A ARG   A 246 ? 0.2650 0.2953 0.3044 -0.0679 -0.0287 0.0798  398 ARG   A CA   
1815 C  CA   B ARG   A 246 ? 0.2654 0.2959 0.3047 -0.0678 -0.0287 0.0799  398 ARG   A CA   
1816 C  C    A ARG   A 246 ? 0.2828 0.3296 0.3173 -0.0729 -0.0249 0.0860  398 ARG   A C    
1817 C  C    B ARG   A 246 ? 0.2827 0.3294 0.3170 -0.0729 -0.0248 0.0856  398 ARG   A C    
1818 O  O    A ARG   A 246 ? 0.2832 0.3277 0.3232 -0.0753 -0.0233 0.0897  398 ARG   A O    
1819 O  O    B ARG   A 246 ? 0.2816 0.3259 0.3213 -0.0753 -0.0232 0.0888  398 ARG   A O    
1820 C  CB   A ARG   A 246 ? 0.2894 0.3173 0.3355 -0.0640 -0.0331 0.0911  398 ARG   A CB   
1821 C  CB   B ARG   A 246 ? 0.2887 0.3185 0.3338 -0.0641 -0.0330 0.0915  398 ARG   A CB   
1822 C  CG   A ARG   A 246 ? 0.2968 0.3205 0.3524 -0.0656 -0.0334 0.1056  398 ARG   A CG   
1823 C  CG   B ARG   A 246 ? 0.2938 0.3040 0.3493 -0.0590 -0.0366 0.0888  398 ARG   A CG   
1824 C  CD   A ARG   A 246 ? 0.3478 0.3652 0.4112 -0.0596 -0.0370 0.1163  398 ARG   A CD   
1825 C  CD   B ARG   A 246 ? 0.3385 0.3456 0.4023 -0.0548 -0.0397 0.1029  398 ARG   A CD   
1826 N  NE   A ARG   A 246 ? 0.3998 0.4082 0.4727 -0.0585 -0.0360 0.1230  398 ARG   A NE   
1827 N  NE   B ARG   A 246 ? 0.3541 0.3570 0.4202 -0.0475 -0.0430 0.0991  398 ARG   A NE   
1828 C  CZ   A ARG   A 246 ? 0.4104 0.4243 0.4863 -0.0557 -0.0361 0.1370  398 ARG   A CZ   
1829 C  CZ   B ARG   A 246 ? 0.3595 0.3789 0.4194 -0.0440 -0.0445 0.1016  398 ARG   A CZ   
1830 N  NH1  A ARG   A 246 ? 0.3806 0.4120 0.4507 -0.0526 -0.0377 0.1457  398 ARG   A NH1  
1831 N  NH1  B ARG   A 246 ? 0.3751 0.4164 0.4256 -0.0475 -0.0430 0.1073  398 ARG   A NH1  
1832 N  NH2  A ARG   A 246 ? 0.4221 0.4252 0.5064 -0.0560 -0.0342 0.1421  398 ARG   A NH2  
1833 N  NH2  B ARG   A 246 ? 0.3720 0.3887 0.4353 -0.0372 -0.0474 0.0978  398 ARG   A NH2  
1834 N  N    . SER   A 247 ? 0.2750 0.3406 0.2987 -0.0745 -0.0232 0.0855  399 SER   A N    
1835 C  CA   . SER   A 247 ? 0.2944 0.3788 0.3122 -0.0793 -0.0191 0.0897  399 SER   A CA   
1836 C  C    . SER   A 247 ? 0.2696 0.3517 0.2846 -0.0811 -0.0139 0.0784  399 SER   A C    
1837 O  O    . SER   A 247 ? 0.2891 0.3782 0.3063 -0.0841 -0.0111 0.0831  399 SER   A O    
1838 C  CB   . SER   A 247 ? 0.3282 0.4355 0.3348 -0.0808 -0.0186 0.0893  399 SER   A CB   
1839 O  OG   . SER   A 247 ? 0.3999 0.5263 0.3987 -0.0856 -0.0136 0.0878  399 SER   A OG   
1840 N  N    . LEU   A 248 ? 0.2862 0.3591 0.2967 -0.0791 -0.0121 0.0643  400 LEU   A N    
1841 C  CA   . LEU   A 248 ? 0.2799 0.3499 0.2877 -0.0790 -0.0066 0.0543  400 LEU   A CA   
1842 C  C    . LEU   A 248 ? 0.2607 0.3198 0.2792 -0.0774 -0.0076 0.0569  400 LEU   A C    
1843 O  O    . LEU   A 248 ? 0.2607 0.3274 0.2808 -0.0787 -0.0040 0.0576  400 LEU   A O    
1844 C  CB   . LEU   A 248 ? 0.2741 0.3342 0.2753 -0.0768 -0.0042 0.0404  400 LEU   A CB   
1845 C  CG   . LEU   A 248 ? 0.2955 0.3674 0.2850 -0.0803 -0.0006 0.0326  400 LEU   A CG   
1846 C  CD1  . LEU   A 248 ? 0.3094 0.3669 0.2949 -0.0790 0.0010  0.0209  400 LEU   A CD1  
1847 C  CD2  . LEU   A 248 ? 0.3033 0.3875 0.2868 -0.0828 0.0063  0.0278  400 LEU   A CD2  
1848 N  N    . SER   A 249 ? 0.2654 0.3090 0.2917 -0.0747 -0.0123 0.0575  401 SER   A N    
1849 C  CA   . SER   A 249 ? 0.2799 0.3147 0.3162 -0.0738 -0.0135 0.0574  401 SER   A CA   
1850 C  C    . SER   A 249 ? 0.3073 0.3465 0.3515 -0.0766 -0.0145 0.0673  401 SER   A C    
1851 O  O    . SER   A 249 ? 0.2861 0.3226 0.3375 -0.0765 -0.0142 0.0656  401 SER   A O    
1852 C  CB   . SER   A 249 ? 0.2619 0.2805 0.3034 -0.0701 -0.0180 0.0530  401 SER   A CB   
1853 O  OG   . SER   A 249 ? 0.2962 0.3096 0.3423 -0.0696 -0.0224 0.0598  401 SER   A OG   
1854 N  N    . PHE   A 250 ? 0.2838 0.3307 0.3262 -0.0783 -0.0153 0.0770  402 PHE   A N    
1855 C  CA   . PHE   A 250 ? 0.3053 0.3559 0.3537 -0.0802 -0.0153 0.0862  402 PHE   A CA   
1856 C  C    . PHE   A 250 ? 0.2803 0.3463 0.3265 -0.0833 -0.0104 0.0857  402 PHE   A C    
1857 O  O    . PHE   A 250 ? 0.3030 0.3704 0.3559 -0.0854 -0.0099 0.0901  402 PHE   A O    
1858 C  CB   . PHE   A 250 ? 0.3711 0.4279 0.4180 -0.0804 -0.0173 0.0983  402 PHE   A CB   
1859 C  CG   . PHE   A 250 ? 0.4641 0.5200 0.5187 -0.0818 -0.0176 0.1087  402 PHE   A CG   
1860 C  CD1  . PHE   A 250 ? 0.5093 0.5466 0.5746 -0.0803 -0.0201 0.1100  402 PHE   A CD1  
1861 C  CD2  . PHE   A 250 ? 0.4844 0.5583 0.5355 -0.0850 -0.0148 0.1164  402 PHE   A CD2  
1862 C  CE1  . PHE   A 250 ? 0.5520 0.5866 0.6245 -0.0827 -0.0192 0.1191  402 PHE   A CE1  
1863 C  CE2  . PHE   A 250 ? 0.5079 0.5805 0.5663 -0.0870 -0.0146 0.1264  402 PHE   A CE2  
1864 C  CZ   . PHE   A 250 ? 0.5437 0.5956 0.6128 -0.0862 -0.0166 0.1280  402 PHE   A CZ   
1865 N  N    . GLN   A 251 ? 0.3138 0.3917 0.3512 -0.0841 -0.0062 0.0797  403 GLN   A N    
1866 C  CA   . GLN   A 251 ? 0.2605 0.3539 0.2963 -0.0860 -0.0007 0.0775  403 GLN   A CA   
1867 C  C    . GLN   A 251 ? 0.2906 0.3782 0.3333 -0.0844 0.0005  0.0703  403 GLN   A C    
1868 O  O    . GLN   A 251 ? 0.2404 0.3184 0.2804 -0.0805 0.0007  0.0615  403 GLN   A O    
1869 C  CB   . GLN   A 251 ? 0.2968 0.4052 0.3205 -0.0870 0.0046  0.0718  403 GLN   A CB   
1870 C  CG   . GLN   A 251 ? 0.4169 0.5359 0.4326 -0.0887 0.0031  0.0775  403 GLN   A CG   
1871 C  CD   . GLN   A 251 ? 0.5095 0.6391 0.5283 -0.0902 0.0014  0.0899  403 GLN   A CD   
1872 O  OE1  . GLN   A 251 ? 0.5462 0.6726 0.5675 -0.0897 -0.0032 0.0998  403 GLN   A OE1  
1873 N  NE2  . GLN   A 251 ? 0.5160 0.6588 0.5352 -0.0916 0.0055  0.0898  403 GLN   A NE2  
1874 N  N    . PRO   A 252 ? 0.2624 0.3555 0.3132 -0.0859 0.0011  0.0729  404 PRO   A N    
1875 C  CA   . PRO   A 252 ? 0.2576 0.3497 0.3160 -0.0844 0.0015  0.0667  404 PRO   A CA   
1876 C  C    . PRO   A 252 ? 0.2694 0.3678 0.3210 -0.0784 0.0068  0.0574  404 PRO   A C    
1877 O  O    . PRO   A 252 ? 0.2598 0.3505 0.3134 -0.0724 0.0063  0.0503  404 PRO   A O    
1878 C  CB   . PRO   A 252 ? 0.2535 0.3560 0.3200 -0.0879 0.0022  0.0712  404 PRO   A CB   
1879 C  CG   . PRO   A 252 ? 0.2527 0.3527 0.3176 -0.0911 0.0005  0.0805  404 PRO   A CG   
1880 C  CD   . PRO   A 252 ? 0.2283 0.3293 0.2822 -0.0895 0.0009  0.0820  404 PRO   A CD   
1881 N  N    . GLU   A 253 ? 0.2471 0.3575 0.2894 -0.0781 0.0122  0.0559  405 GLU   A N    
1882 C  CA   . GLU   A 253 ? 0.3164 0.4275 0.3512 -0.0704 0.0183  0.0449  405 GLU   A CA   
1883 C  C    . GLU   A 253 ? 0.3110 0.4016 0.3389 -0.0656 0.0172  0.0372  405 GLU   A C    
1884 O  O    . GLU   A 253 ? 0.3641 0.4476 0.3895 -0.0581 0.0210  0.0291  405 GLU   A O    
1885 C  CB   . GLU   A 253 ? 0.4229 0.5513 0.4491 -0.0721 0.0245  0.0434  405 GLU   A CB   
1886 C  CG   . GLU   A 253 ? 0.5756 0.7254 0.6064 -0.0796 0.0248  0.0541  405 GLU   A CG   
1887 C  CD   . GLU   A 253 ? 0.6626 0.8112 0.6921 -0.0867 0.0198  0.0648  405 GLU   A CD   
1888 O  OE1  . GLU   A 253 ? 0.7211 0.8799 0.7409 -0.0881 0.0216  0.0649  405 GLU   A OE1  
1889 O  OE2  . GLU   A 253 ? 0.7013 0.8355 0.7386 -0.0876 0.0134  0.0707  405 GLU   A OE2  
1890 N  N    . ASN   A 254 ? 0.2461 0.3279 0.2712 -0.0694 0.0126  0.0402  406 ASN   A N    
1891 C  CA   . ASN   A 254 ? 0.1945 0.2585 0.2146 -0.0658 0.0112  0.0335  406 ASN   A CA   
1892 C  C    . ASN   A 254 ? 0.1599 0.2111 0.1881 -0.0627 0.0061  0.0340  406 ASN   A C    
1893 O  O    . ASN   A 254 ? 0.1830 0.2230 0.2088 -0.0569 0.0072  0.0274  406 ASN   A O    
1894 C  CB   . ASN   A 254 ? 0.1659 0.2293 0.1800 -0.0704 0.0083  0.0359  406 ASN   A CB   
1895 C  CG   . ASN   A 254 ? 0.2711 0.3508 0.2762 -0.0740 0.0130  0.0344  406 ASN   A CG   
1896 O  OD1  . ASN   A 254 ? 0.3175 0.4018 0.3173 -0.0719 0.0198  0.0262  406 ASN   A OD1  
1897 N  ND2  . ASN   A 254 ? 0.2485 0.3377 0.2515 -0.0790 0.0096  0.0421  406 ASN   A ND2  
1898 N  N    . SER   A 255 ? 0.1743 0.2269 0.2122 -0.0670 0.0007  0.0416  407 SER   A N    
1899 C  CA   . SER   A 255 ? 0.2469 0.2899 0.2933 -0.0651 -0.0041 0.0405  407 SER   A CA   
1900 C  C    . SER   A 255 ? 0.2873 0.3339 0.3357 -0.0589 -0.0015 0.0350  407 SER   A C    
1901 O  O    . SER   A 255 ? 0.3071 0.3451 0.3564 -0.0541 -0.0036 0.0307  407 SER   A O    
1902 C  CB   . SER   A 255 ? 0.2676 0.3130 0.3254 -0.0718 -0.0084 0.0484  407 SER   A CB   
1903 O  OG   . SER   A 255 ? 0.3715 0.4052 0.4302 -0.0737 -0.0130 0.0519  407 SER   A OG   
1904 N  N    . MET   A 256 ? 0.2803 0.3417 0.3296 -0.0582 0.0033  0.0358  408 MET   A N    
1905 C  CA   . MET   A 256 ? 0.2884 0.3566 0.3404 -0.0509 0.0062  0.0320  408 MET   A CA   
1906 C  C    . MET   A 256 ? 0.2485 0.3042 0.2920 -0.0418 0.0098  0.0256  408 MET   A C    
1907 O  O    . MET   A 256 ? 0.1973 0.2539 0.2433 -0.0343 0.0104  0.0237  408 MET   A O    
1908 C  CB   . MET   A 256 ? 0.2838 0.3712 0.3373 -0.0509 0.0116  0.0336  408 MET   A CB   
1909 C  CG   . MET   A 256 ? 0.3455 0.4501 0.4114 -0.0548 0.0094  0.0377  408 MET   A CG   
1910 S  SD   . MET   A 256 ? 0.3967 0.5269 0.4639 -0.0550 0.0164  0.0398  408 MET   A SD   
1911 C  CE   . MET   A 256 ? 0.3254 0.4486 0.3797 -0.0438 0.0246  0.0318  408 MET   A CE   
1912 N  N    . LYS   A 257 ? 0.2415 0.2868 0.2750 -0.0427 0.0127  0.0226  409 LYS   A N    
1913 C  CA   . LYS   A 257 ? 0.2531 0.2845 0.2787 -0.0357 0.0173  0.0164  409 LYS   A CA   
1914 C  C    . LYS   A 257 ? 0.1855 0.2020 0.2096 -0.0354 0.0128  0.0154  409 LYS   A C    
1915 O  O    . LYS   A 257 ? 0.2003 0.2045 0.2186 -0.0301 0.0165  0.0116  409 LYS   A O    
1916 C  CB   . LYS   A 257 ? 0.3026 0.3313 0.3182 -0.0381 0.0235  0.0115  409 LYS   A CB   
1917 C  CG   . LYS   A 257 ? 0.3727 0.4170 0.3883 -0.0375 0.0294  0.0107  409 LYS   A CG   
1918 C  CD   . LYS   A 257 ? 0.4461 0.4976 0.4683 -0.0283 0.0323  0.0115  409 LYS   A CD   
1919 C  CE   . LYS   A 257 ? 0.4981 0.5379 0.5147 -0.0184 0.0411  0.0047  409 LYS   A CE   
1920 N  NZ   . LYS   A 257 ? 0.4925 0.5462 0.5141 -0.0095 0.0465  0.0049  409 LYS   A NZ   
1921 N  N    . LEU   A 258 ? 0.1617 0.1788 0.1913 -0.0408 0.0054  0.0188  410 LEU   A N    
1922 C  CA   . LEU   A 258 ? 0.1826 0.1879 0.2113 -0.0401 0.0012  0.0172  410 LEU   A CA   
1923 C  C    . LEU   A 258 ? 0.2204 0.2275 0.2541 -0.0338 -0.0006 0.0166  410 LEU   A C    
1924 O  O    . LEU   A 258 ? 0.1801 0.1970 0.2172 -0.0291 0.0018  0.0176  410 LEU   A O    
1925 C  CB   . LEU   A 258 ? 0.1285 0.1333 0.1615 -0.0470 -0.0052 0.0204  410 LEU   A CB   
1926 C  CG   . LEU   A 258 ? 0.1521 0.1596 0.1799 -0.0526 -0.0039 0.0227  410 LEU   A CG   
1927 C  CD1  . LEU   A 258 ? 0.1593 0.1656 0.1922 -0.0574 -0.0101 0.0280  410 LEU   A CD1  
1928 C  CD2  . LEU   A 258 ? 0.1492 0.1499 0.1661 -0.0517 0.0006  0.0170  410 LEU   A CD2  
1929 N  N    . THR   A 259 ? 0.2376 0.2378 0.2717 -0.0331 -0.0049 0.0150  411 THR   A N    
1930 C  CA   . THR   A 259 ? 0.1814 0.1869 0.2202 -0.0279 -0.0076 0.0143  411 THR   A CA   
1931 C  C    . THR   A 259 ? 0.1786 0.1878 0.2262 -0.0334 -0.0150 0.0134  411 THR   A C    
1932 O  O    . THR   A 259 ? 0.2150 0.2177 0.2638 -0.0393 -0.0177 0.0139  411 THR   A O    
1933 C  CB   . THR   A 259 ? 0.1715 0.1676 0.2030 -0.0219 -0.0054 0.0126  411 THR   A CB   
1934 O  OG1  . THR   A 259 ? 0.1963 0.1846 0.2264 -0.0260 -0.0094 0.0102  411 THR   A OG1  
1935 C  CG2  . THR   A 259 ? 0.2238 0.2100 0.2465 -0.0185 0.0028  0.0125  411 THR   A CG2  
1936 N  N    . PRO   A 260 ? 0.1477 0.1679 0.2022 -0.0315 -0.0183 0.0117  412 PRO   A N    
1937 C  CA   . PRO   A 260 ? 0.1458 0.1680 0.2095 -0.0375 -0.0247 0.0086  412 PRO   A CA   
1938 C  C    . PRO   A 260 ? 0.1078 0.1177 0.1689 -0.0380 -0.0278 0.0053  412 PRO   A C    
1939 O  O    . PRO   A 260 ? 0.1817 0.1859 0.2490 -0.0437 -0.0314 0.0043  412 PRO   A O    
1940 C  CB   . PRO   A 260 ? 0.1660 0.2051 0.2352 -0.0342 -0.0268 0.0057  412 PRO   A CB   
1941 C  CG   . PRO   A 260 ? 0.1822 0.2312 0.2486 -0.0282 -0.0215 0.0100  412 PRO   A CG   
1942 C  CD   . PRO   A 260 ? 0.1299 0.1636 0.1853 -0.0241 -0.0160 0.0126  412 PRO   A CD   
1943 N  N    . LEU   A 261 ? 0.1305 0.1361 0.1832 -0.0321 -0.0259 0.0039  413 LEU   A N    
1944 C  CA   . LEU   A 261 ? 0.1026 0.0995 0.1529 -0.0324 -0.0285 0.0005  413 LEU   A CA   
1945 C  C    . LEU   A 261 ? 0.1499 0.1360 0.1976 -0.0365 -0.0278 0.0030  413 LEU   A C    
1946 O  O    . LEU   A 261 ? 0.1822 0.1633 0.2332 -0.0386 -0.0314 0.0010  413 LEU   A O    
1947 C  CB   . LEU   A 261 ? 0.2322 0.2285 0.2738 -0.0260 -0.0257 -0.0002 413 LEU   A CB   
1948 C  CG   . LEU   A 261 ? 0.2699 0.2609 0.3088 -0.0260 -0.0279 -0.0040 413 LEU   A CG   
1949 C  CD1  . LEU   A 261 ? 0.2539 0.2525 0.3008 -0.0266 -0.0339 -0.0104 413 LEU   A CD1  
1950 C  CD2  . LEU   A 261 ? 0.2088 0.1973 0.2379 -0.0211 -0.0234 -0.0024 413 LEU   A CD2  
1951 N  N    . VAL   A 262 ? 0.1506 0.1347 0.1925 -0.0372 -0.0230 0.0069  414 VAL   A N    
1952 C  CA   . VAL   A 262 ? 0.1659 0.1446 0.2050 -0.0415 -0.0226 0.0093  414 VAL   A CA   
1953 C  C    . VAL   A 262 ? 0.2113 0.1914 0.2597 -0.0463 -0.0266 0.0128  414 VAL   A C    
1954 O  O    . VAL   A 262 ? 0.2083 0.1838 0.2588 -0.0480 -0.0294 0.0141  414 VAL   A O    
1955 C  CB   . VAL   A 262 ? 0.2184 0.1971 0.2494 -0.0418 -0.0163 0.0111  414 VAL   A CB   
1956 C  CG1  . VAL   A 262 ? 0.2435 0.2228 0.2724 -0.0471 -0.0164 0.0140  414 VAL   A CG1  
1957 C  CG2  . VAL   A 262 ? 0.1921 0.1645 0.2141 -0.0380 -0.0116 0.0078  414 VAL   A CG2  
1958 N  N    . LEU   A 263 ? 0.1806 0.1673 0.2353 -0.0484 -0.0264 0.0150  415 LEU   A N    
1959 C  CA   . LEU   A 263 ? 0.1665 0.1532 0.2301 -0.0537 -0.0290 0.0191  415 LEU   A CA   
1960 C  C    . LEU   A 263 ? 0.1696 0.1503 0.2378 -0.0516 -0.0322 0.0145  415 LEU   A C    
1961 O  O    . LEU   A 263 ? 0.1758 0.1507 0.2462 -0.0521 -0.0329 0.0176  415 LEU   A O    
1962 C  CB   . LEU   A 263 ? 0.1562 0.1533 0.2264 -0.0572 -0.0278 0.0213  415 LEU   A CB   
1963 C  CG   . LEU   A 263 ? 0.1854 0.1907 0.2493 -0.0571 -0.0225 0.0254  415 LEU   A CG   
1964 C  CD1  . LEU   A 263 ? 0.1119 0.1308 0.1822 -0.0582 -0.0211 0.0258  415 LEU   A CD1  
1965 C  CD2  . LEU   A 263 ? 0.1968 0.2011 0.2591 -0.0619 -0.0217 0.0327  415 LEU   A CD2  
1966 N  N    . GLU   A 264 ? 0.1544 0.1372 0.2250 -0.0495 -0.0343 0.0075  416 GLU   A N    
1967 C  CA   . GLU   A 264 ? 0.2207 0.1988 0.2951 -0.0479 -0.0367 0.0016  416 GLU   A CA   
1968 C  C    . GLU   A 264 ? 0.2252 0.1956 0.2954 -0.0442 -0.0374 0.0016  416 GLU   A C    
1969 O  O    . GLU   A 264 ? 0.2212 0.1848 0.2956 -0.0439 -0.0385 0.0027  416 GLU   A O    
1970 C  CB   . GLU   A 264 ? 0.2586 0.2449 0.3357 -0.0466 -0.0392 -0.0064 416 GLU   A CB   
1971 C  CG   . GLU   A 264 ? 0.3301 0.3144 0.4122 -0.0466 -0.0410 -0.0140 416 GLU   A CG   
1972 C  CD   . GLU   A 264 ? 0.3494 0.3447 0.4319 -0.0445 -0.0437 -0.0225 416 GLU   A CD   
1973 O  OE1  . GLU   A 264 ? 0.3382 0.3323 0.4164 -0.0400 -0.0447 -0.0259 416 GLU   A OE1  
1974 O  OE2  . GLU   A 264 ? 0.3527 0.3606 0.4402 -0.0473 -0.0449 -0.0257 416 GLU   A OE2  
1975 N  N    . VAL   A 265 ? 0.2041 0.1755 0.2668 -0.0417 -0.0368 0.0007  417 VAL   A N    
1976 C  CA   . VAL   A 265 ? 0.2144 0.1818 0.2741 -0.0388 -0.0378 -0.0009 417 VAL   A CA   
1977 C  C    . VAL   A 265 ? 0.2209 0.1850 0.2800 -0.0404 -0.0376 0.0062  417 VAL   A C    
1978 O  O    . VAL   A 265 ? 0.2450 0.2049 0.3090 -0.0388 -0.0404 0.0068  417 VAL   A O    
1979 C  CB   . VAL   A 265 ? 0.2025 0.1722 0.2544 -0.0373 -0.0368 -0.0038 417 VAL   A CB   
1980 C  CG1  . VAL   A 265 ? 0.1834 0.1513 0.2318 -0.0359 -0.0373 -0.0046 417 VAL   A CG1  
1981 C  CG2  . VAL   A 265 ? 0.1853 0.1603 0.2395 -0.0350 -0.0386 -0.0102 417 VAL   A CG2  
1982 N  N    . PHE   A 266 ? 0.2367 0.2037 0.2911 -0.0436 -0.0350 0.0117  418 PHE   A N    
1983 C  CA   . PHE   A 266 ? 0.2815 0.2493 0.3350 -0.0462 -0.0353 0.0192  418 PHE   A CA   
1984 C  C    . PHE   A 266 ? 0.3595 0.3255 0.4210 -0.0480 -0.0364 0.0262  418 PHE   A C    
1985 O  O    . PHE   A 266 ? 0.3955 0.3632 0.4575 -0.0501 -0.0374 0.0347  418 PHE   A O    
1986 C  CB   . PHE   A 266 ? 0.2501 0.2238 0.2949 -0.0499 -0.0315 0.0213  418 PHE   A CB   
1987 C  CG   . PHE   A 266 ? 0.2516 0.2260 0.2869 -0.0487 -0.0290 0.0158  418 PHE   A CG   
1988 C  CD1  . PHE   A 266 ? 0.2343 0.2118 0.2604 -0.0509 -0.0236 0.0146  418 PHE   A CD1  
1989 C  CD2  . PHE   A 266 ? 0.2460 0.2181 0.2818 -0.0457 -0.0312 0.0111  418 PHE   A CD2  
1990 C  CE1  . PHE   A 266 ? 0.2652 0.2412 0.2831 -0.0510 -0.0203 0.0092  418 PHE   A CE1  
1991 C  CE2  . PHE   A 266 ? 0.2531 0.2264 0.2804 -0.0457 -0.0281 0.0066  418 PHE   A CE2  
1992 C  CZ   . PHE   A 266 ? 0.2835 0.2576 0.3020 -0.0488 -0.0225 0.0058  418 PHE   A CZ   
1993 N  N    . GLY   A 267 ? 0.4400 0.4036 0.5075 -0.0480 -0.0362 0.0237  419 GLY   A N    
1994 C  CA   . GLY   A 267 ? 0.5336 0.4946 0.6081 -0.0508 -0.0362 0.0303  419 GLY   A CA   
1995 C  C    . GLY   A 267 ? 0.6449 0.5960 0.7287 -0.0491 -0.0383 0.0276  419 GLY   A C    
1996 O  O    . GLY   A 267 ? 0.6757 0.6209 0.7622 -0.0454 -0.0409 0.0267  419 GLY   A O    
1997 N  N    . ASN   A 268 ? 0.7282 0.6775 0.8177 -0.0524 -0.0371 0.0259  420 ASN   A N    
1998 C  CA   . ASN   A 268 ? 0.7887 0.7276 0.8870 -0.0522 -0.0380 0.0215  420 ASN   A CA   
1999 C  C    . ASN   A 268 ? 0.7689 0.7114 0.8678 -0.0530 -0.0382 0.0094  420 ASN   A C    
2000 O  O    . ASN   A 268 ? 0.7377 0.6877 0.8308 -0.0502 -0.0389 0.0041  420 ASN   A O    
2001 C  CB   . ASN   A 268 ? 0.8414 0.7744 0.9463 -0.0571 -0.0361 0.0288  420 ASN   A CB   
2002 C  CG   . ASN   A 268 ? 0.8656 0.7834 0.9795 -0.0559 -0.0366 0.0276  420 ASN   A CG   
2003 O  OD1  . ASN   A 268 ? 0.8583 0.7692 0.9747 -0.0507 -0.0383 0.0323  420 ASN   A OD1  
2004 N  ND2  . ASN   A 268 ? 0.8627 0.7754 0.9821 -0.0608 -0.0350 0.0210  420 ASN   A ND2  
2005 N  N    . LYS   B 1   ? 0.7598 0.7181 0.8874 -0.0717 -0.0450 -0.0786 625 LYS   C N    
2006 C  CA   . LYS   B 1   ? 0.7515 0.7045 0.8746 -0.0633 -0.0446 -0.0695 625 LYS   C CA   
2007 C  C    . LYS   B 1   ? 0.7230 0.6814 0.8413 -0.0647 -0.0439 -0.0574 625 LYS   C C    
2008 O  O    . LYS   B 1   ? 0.7269 0.6985 0.8444 -0.0703 -0.0443 -0.0571 625 LYS   C O    
2009 C  CB   . LYS   B 1   ? 0.7468 0.7112 0.8648 -0.0553 -0.0465 -0.0756 625 LYS   C CB   
2010 C  CG   . LYS   B 1   ? 0.7474 0.6999 0.8691 -0.0487 -0.0463 -0.0797 625 LYS   C CG   
2011 C  CD   . LYS   B 1   ? 0.7314 0.6985 0.8484 -0.0422 -0.0480 -0.0877 625 LYS   C CD   
2012 C  CE   . LYS   B 1   ? 0.7189 0.6773 0.8419 -0.0365 -0.0478 -0.0952 625 LYS   C CE   
2013 N  NZ   . LYS   B 1   ? 0.6934 0.6621 0.8107 -0.0288 -0.0491 -0.0963 625 LYS   C NZ   
2014 N  N    . ASN   B 2   ? 0.6701 0.6199 0.7859 -0.0593 -0.0431 -0.0478 626 ASN   C N    
2015 C  CA   . ASN   B 2   ? 0.6136 0.5662 0.7257 -0.0604 -0.0418 -0.0363 626 ASN   C CA   
2016 C  C    . ASN   B 2   ? 0.5087 0.4750 0.6128 -0.0560 -0.0428 -0.0345 626 ASN   C C    
2017 O  O    . ASN   B 2   ? 0.5303 0.5011 0.6317 -0.0572 -0.0416 -0.0267 626 ASN   C O    
2018 C  CB   . ASN   B 2   ? 0.6768 0.6144 0.7906 -0.0574 -0.0406 -0.0261 626 ASN   C CB   
2019 C  CG   . ASN   B 2   ? 0.7177 0.6463 0.8371 -0.0640 -0.0381 -0.0195 626 ASN   C CG   
2020 O  OD1  . ASN   B 2   ? 0.7118 0.6487 0.8310 -0.0705 -0.0368 -0.0176 626 ASN   C OD1  
2021 N  ND2  . ASN   B 2   ? 0.7440 0.6562 0.8691 -0.0623 -0.0374 -0.0153 626 ASN   C ND2  
2022 N  N    . HIS   B 3   ? 0.3902 0.3634 0.4908 -0.0510 -0.0447 -0.0414 627 HIS   C N    
2023 C  CA   . HIS   B 3   ? 0.3068 0.2885 0.3996 -0.0461 -0.0453 -0.0386 627 HIS   C CA   
2024 C  C    . HIS   B 3   ? 0.2780 0.2775 0.3688 -0.0452 -0.0474 -0.0460 627 HIS   C C    
2025 O  O    . HIS   B 3   ? 0.3076 0.3119 0.3940 -0.0401 -0.0485 -0.0500 627 HIS   C O    
2026 C  CB   . HIS   B 3   ? 0.3230 0.2964 0.4127 -0.0401 -0.0455 -0.0373 627 HIS   C CB   
2027 C  CG   . HIS   B 3   ? 0.3132 0.2733 0.4052 -0.0400 -0.0445 -0.0288 627 HIS   C CG   
2028 N  ND1  . HIS   B 3   ? 0.3399 0.2881 0.4400 -0.0407 -0.0445 -0.0295 627 HIS   C ND1  
2029 C  CD2  . HIS   B 3   ? 0.3013 0.2590 0.3891 -0.0396 -0.0434 -0.0191 627 HIS   C CD2  
2030 C  CE1  . HIS   B 3   ? 0.3257 0.2657 0.4269 -0.0402 -0.0440 -0.0196 627 HIS   C CE1  
2031 N  NE2  . HIS   B 3   ? 0.3062 0.2528 0.3994 -0.0398 -0.0435 -0.0135 627 HIS   C NE2  
2032 N  N    . PRO   B 4   ? 0.2442 0.2562 0.3381 -0.0498 -0.0481 -0.0473 628 PRO   C N    
2033 C  CA   . PRO   B 4   ? 0.2424 0.2752 0.3351 -0.0481 -0.0506 -0.0538 628 PRO   C CA   
2034 C  C    . PRO   B 4   ? 0.2354 0.2780 0.3222 -0.0415 -0.0515 -0.0501 628 PRO   C C    
2035 O  O    . PRO   B 4   ? 0.2652 0.3208 0.3481 -0.0369 -0.0530 -0.0550 628 PRO   C O    
2036 C  CB   . PRO   B 4   ? 0.2216 0.2669 0.3202 -0.0546 -0.0513 -0.0539 628 PRO   C CB   
2037 C  CG   . PRO   B 4   ? 0.2404 0.2742 0.3413 -0.0583 -0.0487 -0.0449 628 PRO   C CG   
2038 C  CD   . PRO   B 4   ? 0.2504 0.2614 0.3492 -0.0566 -0.0466 -0.0424 628 PRO   C CD   
2039 N  N    . MET   B 5   ? 0.2204 0.2571 0.3064 -0.0408 -0.0504 -0.0414 629 MET   C N    
2040 C  CA   . MET   B 5   ? 0.2609 0.3034 0.3383 -0.0337 -0.0489 -0.0358 629 MET   C CA   
2041 C  C    . MET   B 5   ? 0.2474 0.2806 0.3174 -0.0296 -0.0483 -0.0367 629 MET   C C    
2042 O  O    . MET   B 5   ? 0.2735 0.3156 0.3354 -0.0237 -0.0471 -0.0360 629 MET   C O    
2043 C  CB   . MET   B 5   ? 0.3024 0.3381 0.3762 -0.0333 -0.0447 -0.0251 629 MET   C CB   
2044 C  CG   . MET   B 5   ? 0.3435 0.3934 0.4235 -0.0359 -0.0446 -0.0234 629 MET   C CG   
2045 S  SD   . MET   B 5   ? 0.3841 0.4278 0.4603 -0.0352 -0.0391 -0.0122 629 MET   C SD   
2046 C  CE   . MET   B 5   ? 0.3979 0.4262 0.4822 -0.0452 -0.0404 -0.0114 629 MET   C CE   
2047 N  N    . LEU   B 6   ? 0.1768 0.1936 0.2500 -0.0324 -0.0489 -0.0376 630 LEU   C N    
2048 C  CA   . LEU   B 6   ? 0.2037 0.2146 0.2716 -0.0289 -0.0487 -0.0394 630 LEU   C CA   
2049 C  C    . LEU   B 6   ? 0.2418 0.2630 0.3099 -0.0265 -0.0501 -0.0490 630 LEU   C C    
2050 O  O    . LEU   B 6   ? 0.2426 0.2715 0.3052 -0.0225 -0.0506 -0.0515 630 LEU   C O    
2051 C  CB   . LEU   B 6   ? 0.2135 0.2078 0.2819 -0.0301 -0.0466 -0.0352 630 LEU   C CB   
2052 C  CG   . LEU   B 6   ? 0.2609 0.2504 0.3270 -0.0268 -0.0467 -0.0375 630 LEU   C CG   
2053 C  CD1  . LEU   B 6   ? 0.2383 0.2330 0.2967 -0.0245 -0.0465 -0.0369 630 LEU   C CD1  
2054 C  CD2  . LEU   B 6   ? 0.2861 0.2632 0.3545 -0.0276 -0.0457 -0.0315 630 LEU   C CD2  
2055 N  N    . MET   B 7   ? 0.2659 0.2878 0.3399 -0.0294 -0.0504 -0.0547 631 MET   C N    
2056 C  CA   . MET   B 7   ? 0.3645 0.3976 0.4388 -0.0277 -0.0515 -0.0648 631 MET   C CA   
2057 C  C    . MET   B 7   ? 0.3636 0.4191 0.4326 -0.0246 -0.0529 -0.0660 631 MET   C C    
2058 O  O    . MET   B 7   ? 0.3538 0.4199 0.4181 -0.0205 -0.0530 -0.0706 631 MET   C O    
2059 C  CB   . MET   B 7   ? 0.4603 0.4910 0.5425 -0.0328 -0.0517 -0.0708 631 MET   C CB   
2060 C  CG   . MET   B 7   ? 0.5324 0.5465 0.6204 -0.0329 -0.0508 -0.0748 631 MET   C CG   
2061 S  SD   . MET   B 7   ? 0.5459 0.5658 0.6323 -0.0263 -0.0512 -0.0845 631 MET   C SD   
2062 C  CE   . MET   B 7   ? 0.5513 0.5739 0.6463 -0.0298 -0.0513 -0.0981 631 MET   C CE   
2063 N  N    . ASN   B 8   ? 0.3289 0.3942 0.3988 -0.0256 -0.0537 -0.0612 632 ASN   C N    
2064 C  CA   . ASN   B 8   ? 0.3006 0.3902 0.3655 -0.0207 -0.0547 -0.0601 632 ASN   C CA   
2065 C  C    . ASN   B 8   ? 0.2666 0.3547 0.3207 -0.0141 -0.0520 -0.0529 632 ASN   C C    
2066 O  O    . ASN   B 8   ? 0.2330 0.3382 0.2808 -0.0093 -0.0520 -0.0537 632 ASN   C O    
2067 C  CB   . ASN   B 8   ? 0.3057 0.4051 0.3738 -0.0212 -0.0548 -0.0539 632 ASN   C CB   
2068 C  CG   . ASN   B 8   ? 0.3007 0.4266 0.3628 -0.0144 -0.0546 -0.0502 632 ASN   C CG   
2069 O  OD1  . ASN   B 8   ? 0.2982 0.4228 0.3510 -0.0069 -0.0504 -0.0384 632 ASN   C OD1  
2070 N  ND2  . ASN   B 8   ? 0.2762 0.4198 0.3410 -0.0161 -0.0564 -0.0573 632 ASN   C ND2  
2071 N  N    . LEU   B 9   ? 0.2522 0.3193 0.3026 -0.0142 -0.0484 -0.0444 633 LEU   C N    
2072 C  CA   . LEU   B 9   ? 0.2257 0.2875 0.2651 -0.0097 -0.0441 -0.0371 633 LEU   C CA   
2073 C  C    . LEU   B 9   ? 0.2225 0.2864 0.2607 -0.0094 -0.0455 -0.0445 633 LEU   C C    
2074 O  O    . LEU   B 9   ? 0.1831 0.2521 0.2126 -0.0057 -0.0426 -0.0405 633 LEU   C O    
2075 C  CB   . LEU   B 9   ? 0.1759 0.2168 0.2124 -0.0115 -0.0400 -0.0287 633 LEU   C CB   
2076 C  CG   . LEU   B 9   ? 0.2152 0.2555 0.2501 -0.0098 -0.0367 -0.0202 633 LEU   C CG   
2077 C  CD1  . LEU   B 9   ? 0.2324 0.2540 0.2664 -0.0132 -0.0335 -0.0152 633 LEU   C CD1  
2078 C  CD2  . LEU   B 9   ? 0.1811 0.2293 0.2069 -0.0025 -0.0325 -0.0125 633 LEU   C CD2  
2079 N  N    . LEU   B 10  ? 0.2261 0.2858 0.2733 -0.0129 -0.0493 -0.0549 634 LEU   C N    
2080 C  CA   . LEU   B 10  ? 0.3425 0.4081 0.3901 -0.0114 -0.0508 -0.0641 634 LEU   C CA   
2081 C  C    . LEU   B 10  ? 0.4831 0.5697 0.5290 -0.0091 -0.0512 -0.0704 634 LEU   C C    
2082 O  O    . LEU   B 10  ? 0.5292 0.6237 0.5721 -0.0064 -0.0502 -0.0754 634 LEU   C O    
2083 C  CB   . LEU   B 10  ? 0.2451 0.2934 0.3002 -0.0136 -0.0504 -0.0680 634 LEU   C CB   
2084 C  CG   . LEU   B 10  ? 0.2766 0.3081 0.3318 -0.0144 -0.0495 -0.0620 634 LEU   C CG   
2085 C  CD1  . LEU   B 10  ? 0.2143 0.2310 0.2782 -0.0156 -0.0496 -0.0636 634 LEU   C CD1  
2086 C  CD2  . LEU   B 10  ? 0.2604 0.2974 0.3097 -0.0114 -0.0486 -0.0630 634 LEU   C CD2  
2087 N  N    . LYS   B 11  ? 0.5652 0.6627 0.6130 -0.0100 -0.0523 -0.0701 635 LYS   C N    
2088 C  CA   . LYS   B 11  ? 0.6233 0.7416 0.6703 -0.0087 -0.0526 -0.0763 635 LYS   C CA   
2089 C  C    . LYS   B 11  ? 0.6507 0.7640 0.7037 -0.0106 -0.0522 -0.0883 635 LYS   C C    
2090 O  O    . LYS   B 11  ? 0.6453 0.7393 0.7058 -0.0142 -0.0524 -0.0910 635 LYS   C O    
2091 C  CB   . LYS   B 11  ? 0.6384 0.7778 0.6750 -0.0026 -0.0514 -0.0718 635 LYS   C CB   
2092 C  CG   . LYS   B 11  ? 0.6626 0.8114 0.6936 0.0014  -0.0515 -0.0591 635 LYS   C CG   
2093 C  CD   . LYS   B 11  ? 0.7009 0.8642 0.7202 0.0078  -0.0488 -0.0508 635 LYS   C CD   
2094 C  CE   . LYS   B 11  ? 0.7173 0.8558 0.7307 0.0079  -0.0434 -0.0412 635 LYS   C CE   
2095 N  NZ   . LYS   B 11  ? 0.7312 0.8765 0.7390 0.0088  -0.0420 -0.0439 635 LYS   C NZ   
2096 C  C10  . A1L73 C .   ? 0.2200 0.1883 0.1921 -0.0729 0.0174  -0.0209 501 A1L73 A C10  
2097 C  C13  . A1L73 C .   ? 0.2045 0.1771 0.1769 -0.0764 0.0114  -0.0225 501 A1L73 A C13  
2098 C  C15  . A1L73 C .   ? 0.3689 0.3053 0.3239 -0.0828 0.0407  -0.0440 501 A1L73 A C15  
2099 C  C20  . A1L73 C .   ? 0.6202 0.5092 0.5808 -0.0556 0.0413  -0.0039 501 A1L73 A C20  
2100 C  C21  . A1L73 C .   ? 0.5730 0.4445 0.5306 -0.0492 0.0499  0.0032  501 A1L73 A C21  
2101 C  C22  . A1L73 C .   ? 0.4613 0.3396 0.4195 -0.0407 0.0465  0.0122  501 A1L73 A C22  
2102 C  C24  . A1L73 C .   ? 0.2096 0.2047 0.2024 -0.0648 -0.0001 0.0044  501 A1L73 A C24  
2103 C  C26  . A1L73 C .   ? 0.2085 0.1939 0.2090 -0.0589 -0.0037 0.0070  501 A1L73 A C26  
2104 C  C28  . A1L73 C .   ? 0.2129 0.1895 0.2122 -0.0542 0.0017  0.0037  501 A1L73 A C28  
2105 C  C01  . A1L73 C .   ? 0.4227 0.3398 0.3895 -0.0628 0.0302  -0.0213 501 A1L73 A C01  
2106 C  C02  . A1L73 C .   ? 0.4858 0.3949 0.4483 -0.0660 0.0372  -0.0245 501 A1L73 A C02  
2107 C  C03  . A1L73 C .   ? 0.4504 0.3627 0.4093 -0.0727 0.0412  -0.0317 501 A1L73 A C03  
2108 C  C04  . A1L73 C .   ? 0.4444 0.3689 0.4032 -0.0760 0.0380  -0.0351 501 A1L73 A C04  
2109 C  C05  . A1L73 C .   ? 0.3879 0.3203 0.3510 -0.0728 0.0310  -0.0308 501 A1L73 A C05  
2110 C  C06  . A1L73 C .   ? 0.3920 0.3202 0.3596 -0.0662 0.0268  -0.0240 501 A1L73 A C06  
2111 C  C08  . A1L73 C .   ? 0.2550 0.2160 0.2220 -0.0778 0.0202  -0.0283 501 A1L73 A C08  
2112 C  C09  . A1L73 C .   ? 0.2300 0.1876 0.1966 -0.0771 0.0234  -0.0283 501 A1L73 A C09  
2113 C  C11  . A1L73 C .   ? 0.2466 0.2245 0.2243 -0.0718 0.0087  -0.0145 501 A1L73 A C11  
2114 C  C12  . A1L73 C .   ? 0.2157 0.1950 0.1936 -0.0737 0.0059  -0.0158 501 A1L73 A C12  
2115 C  C14  . A1L73 C .   ? 0.3510 0.3196 0.3088 -0.0880 0.0274  -0.0406 501 A1L73 A C14  
2116 C  C18  . A1L73 C .   ? 0.6045 0.5010 0.5678 -0.0584 0.0383  -0.0138 501 A1L73 A C18  
2117 C  C19  . A1L73 C .   ? 0.6314 0.5239 0.5920 -0.0612 0.0422  -0.0122 501 A1L73 A C19  
2118 C  C23  . A1L73 C .   ? 0.2353 0.2225 0.2197 -0.0671 0.0065  -0.0053 501 A1L73 A C23  
2119 C  C25  . A1L73 C .   ? 0.2057 0.2086 0.1982 -0.0655 0.0035  0.0062  501 A1L73 A C25  
2120 C  C27  . A1L73 C .   ? 0.2002 0.2106 0.2015 -0.0650 -0.0022 0.0164  501 A1L73 A C27  
2121 C  C33  . A1L73 C .   ? 0.3495 0.2852 0.3226 -0.0635 0.0195  -0.0194 501 A1L73 A C33  
2122 C  C34  . A1L73 C .   ? 0.2779 0.2567 0.2518 -0.0761 0.0078  -0.0225 501 A1L73 A C34  
2123 O  O16  . A1L73 C .   ? 0.2441 0.2303 0.2284 -0.0685 0.0030  -0.0064 501 A1L73 A O16  
2124 O  O17  . A1L73 C .   ? 0.5377 0.4354 0.4988 -0.0637 0.0416  -0.0207 501 A1L73 A O17  
2125 O  O29  . A1L73 C .   ? 0.2080 0.2134 0.2021 -0.0677 -0.0053 0.0086  501 A1L73 A O29  
2126 O  O30  . A1L73 C .   ? 0.4256 0.3231 0.3875 -0.0404 0.0371  0.0099  501 A1L73 A O30  
2127 O  O31  . A1L73 C .   ? 0.4719 0.3417 0.4281 -0.0324 0.0515  0.0212  501 A1L73 A O31  
2128 O  O32  . A1L73 C .   ? 0.6756 0.5820 0.6364 -0.0684 0.0387  -0.0172 501 A1L73 A O32  
2129 SI SI07 . A1L73 C .   ? 0.3772 0.3270 0.3382 -0.0799 0.0288  -0.0355 501 A1L73 A SI07 
2130 O  O    . HOH   D .   ? 0.3776 0.8549 0.3872 -0.0412 0.0076  -0.0802 601 HOH   A O    
2131 O  O    . HOH   D .   ? 0.5205 0.5809 0.5907 -0.0086 -0.0504 -0.1007 602 HOH   A O    
2132 O  O    . HOH   D .   ? 0.6558 0.7719 0.8483 0.1557  -0.0517 -0.0716 603 HOH   A O    
2133 O  O    . HOH   D .   ? 0.6027 0.7836 0.6673 0.0350  -0.0402 -0.1335 604 HOH   A O    
2134 O  O    . HOH   D .   ? 0.6305 0.4967 0.5706 -0.1010 0.1121  -0.1088 605 HOH   A O    
2135 O  O    . HOH   D .   ? 0.3578 0.3711 0.4216 -0.0077 -0.0499 -0.0228 606 HOH   A O    
2136 O  O    . HOH   D .   ? 0.2988 0.2935 0.4488 0.0415  -0.0524 -0.1537 607 HOH   A O    
2137 O  O    . HOH   D .   ? 0.3815 0.3690 0.5167 0.0301  -0.0556 -0.1284 608 HOH   A O    
2138 O  O    . HOH   D .   ? 0.5720 0.7609 0.5774 -0.0531 -0.0487 0.0815  609 HOH   A O    
2139 O  O    . HOH   D .   ? 0.3796 0.3616 0.4411 -0.0577 -0.0288 0.0355  610 HOH   A O    
2140 O  O    A HOH   D .   ? 0.1075 0.2074 0.1451 -0.0314 -0.0445 -0.0091 611 HOH   A O    
2141 O  O    B HOH   D .   ? 0.1081 0.2135 0.1585 -0.0167 -0.0481 -0.0136 611 HOH   A O    
2142 O  O    . HOH   D .   ? 0.5080 0.5135 0.5360 -0.0513 -0.0344 0.0284  612 HOH   A O    
2143 O  O    . HOH   D .   ? 0.4480 0.4522 0.3806 -0.1459 0.0798  -0.1128 613 HOH   A O    
2144 O  O    A HOH   D .   ? 0.2157 0.2755 0.1677 -0.1374 0.0392  -0.0603 614 HOH   A O    
2145 O  O    B HOH   D .   ? 0.2466 0.2724 0.1930 -0.1421 0.0490  -0.0620 614 HOH   A O    
2146 O  O    . HOH   D .   ? 0.3860 0.4837 0.3225 -0.0626 0.0457  0.0345  615 HOH   A O    
2147 O  O    . HOH   D .   ? 0.3814 0.3073 0.3569 -0.0192 0.0729  -0.0328 616 HOH   A O    
2148 O  O    . HOH   D .   ? 0.4971 0.4853 0.5155 -0.0055 -0.0066 0.0119  617 HOH   A O    
2149 O  O    . HOH   D .   ? 0.5114 0.5475 0.5510 -0.0164 0.0119  0.0189  618 HOH   A O    
2150 O  O    . HOH   D .   ? 0.1507 0.2397 0.2148 -0.0289 0.0077  0.0264  619 HOH   A O    
2151 O  O    . HOH   D .   ? 0.2676 0.2406 0.2386 -0.0501 0.0134  -0.0046 620 HOH   A O    
2152 O  O    . HOH   D .   ? 0.3005 0.2259 0.2725 -0.0585 0.0198  -0.0125 621 HOH   A O    
2153 O  O    A HOH   D .   ? 0.3039 0.1317 0.2794 0.0248  0.0908  0.0050  622 HOH   A O    
2154 O  O    B HOH   D .   ? 0.3448 0.1417 0.3189 0.0355  0.1089  0.0020  622 HOH   A O    
2155 O  O    A HOH   D .   ? 0.3278 0.6040 0.3064 -0.0745 -0.0372 0.0659  623 HOH   A O    
2156 O  O    B HOH   D .   ? 0.3324 0.6112 0.3036 -0.0854 -0.0307 0.0418  623 HOH   A O    
2157 O  O    . HOH   D .   ? 0.2826 0.2800 0.3057 0.0073  0.0167  0.0196  624 HOH   A O    
2158 O  O    . HOH   D .   ? 0.3979 0.5055 0.3471 -0.1278 0.0651  0.0117  625 HOH   A O    
2159 O  O    . HOH   D .   ? 0.2838 0.2302 0.2439 -0.0884 0.0351  -0.0202 626 HOH   A O    
2160 O  O    . HOH   D .   ? 0.1981 0.1815 0.2334 -0.0400 -0.0369 0.0049  627 HOH   A O    
2161 O  O    . HOH   D .   ? 0.4243 0.6643 0.4091 -0.1048 -0.0023 -0.0450 628 HOH   A O    
2162 O  O    . HOH   D .   ? 0.7456 0.5636 0.6818 -0.1412 0.1223  -0.0856 629 HOH   A O    
2163 O  O    . HOH   D .   ? 0.4072 0.6968 0.4956 0.0390  -0.0384 -0.0733 630 HOH   A O    
2164 O  O    . HOH   D .   ? 0.3710 0.3634 0.4143 -0.0403 -0.0413 0.0241  631 HOH   A O    
2165 O  O    A HOH   D .   ? 0.1686 0.2247 0.2774 0.0406  -0.0655 0.0487  632 HOH   A O    
2166 O  O    B HOH   D .   ? 0.3616 0.3923 0.4599 0.0224  -0.0624 0.0460  632 HOH   A O    
2167 O  O    . HOH   D .   ? 0.5223 0.6882 0.5134 -0.0018 -0.0235 -0.0577 633 HOH   A O    
2168 O  O    . HOH   D .   ? 0.3045 0.3173 0.4033 -0.0597 -0.0417 -0.0185 634 HOH   A O    
2169 O  O    . HOH   D .   ? 0.3506 0.5585 0.4391 0.0311  -0.0484 -0.0597 635 HOH   A O    
2170 O  O    . HOH   D .   ? 0.3374 0.5241 0.3473 -0.0505 -0.0505 0.0643  636 HOH   A O    
2171 O  O    A HOH   D .   ? 0.3685 0.2415 0.5257 0.0022  -0.0495 -0.0402 637 HOH   A O    
2172 O  O    B HOH   D .   ? 0.3867 0.2480 0.5455 0.0008  -0.0482 -0.0181 637 HOH   A O    
2173 O  O    . HOH   D .   ? 0.4783 0.4005 0.4338 -0.0072 0.0393  0.0455  638 HOH   A O    
2174 O  O    . HOH   D .   ? 0.2902 0.2747 0.2726 -0.0502 0.0009  -0.0146 639 HOH   A O    
2175 O  O    . HOH   D .   ? 0.6873 0.4256 0.6326 -0.0899 0.1410  -0.0680 640 HOH   A O    
2176 O  O    . HOH   D .   ? 0.6545 0.4899 0.6102 -0.0024 0.0698  0.0430  641 HOH   A O    
2177 O  O    . HOH   D .   ? 0.4547 0.4687 0.5462 -0.0583 -0.0365 0.0031  642 HOH   A O    
2178 O  O    . HOH   D .   ? 0.6290 0.4285 0.5842 -0.0260 0.1340  -0.0855 643 HOH   A O    
2179 O  O    A HOH   D .   ? 0.3778 0.2229 0.3469 0.0701  0.0843  0.0854  644 HOH   A O    
2180 O  O    B HOH   D .   ? 0.3698 0.2490 0.3447 0.0895  0.0778  0.0975  644 HOH   A O    
2181 O  O    . HOH   D .   ? 0.2774 0.4681 0.2468 -0.1039 -0.0080 -0.0297 645 HOH   A O    
2182 O  O    . HOH   D .   ? 0.4204 0.8071 0.4542 -0.0474 -0.0158 -0.0477 646 HOH   A O    
2183 O  O    . HOH   D .   ? 0.7113 0.6450 0.7027 0.0170  0.0816  -0.0190 647 HOH   A O    
2184 O  O    . HOH   D .   ? 0.4220 0.4150 0.3713 -0.1516 0.0699  -0.0245 648 HOH   A O    
2185 O  O    . HOH   D .   ? 0.3457 0.3591 0.4677 -0.0067 -0.0495 -0.1438 649 HOH   A O    
2186 O  O    . HOH   D .   ? 0.5479 0.8831 0.5111 -0.0543 0.0272  -0.0228 650 HOH   A O    
2187 O  O    . HOH   D .   ? 0.5532 0.4449 0.7228 0.0516  -0.0583 0.0258  651 HOH   A O    
2188 O  O    . HOH   D .   ? 0.5511 0.7772 0.6822 0.0836  -0.0564 -0.0575 652 HOH   A O    
2189 O  O    . HOH   D .   ? 0.7033 0.4028 0.6633 -0.0124 0.1529  -0.0390 653 HOH   A O    
2190 O  O    . HOH   D .   ? 0.5543 0.7168 0.6409 0.0474  -0.0456 -0.1575 654 HOH   A O    
2191 O  O    A HOH   D .   ? 0.2010 0.3319 0.2813 0.0177  -0.0558 -0.0181 655 HOH   A O    
2192 O  O    B HOH   D .   ? 0.2450 0.3950 0.3427 0.0387  -0.0593 -0.0185 655 HOH   A O    
2193 O  O    A HOH   D .   ? 0.3453 0.5467 0.3845 0.0243  -0.0318 -0.1227 656 HOH   A O    
2194 O  O    B HOH   D .   ? 0.2562 0.4736 0.2934 0.0238  -0.0285 -0.1189 656 HOH   A O    
2195 O  O    . HOH   D .   ? 0.5460 0.7690 0.5339 0.0110  -0.0267 -0.0697 657 HOH   A O    
2196 O  O    . HOH   D .   ? 0.5512 0.6323 0.5453 -0.0586 0.0378  0.0047  658 HOH   A O    
2197 O  O    A HOH   D .   ? 0.3750 0.4014 0.3317 -0.1213 0.0350  -0.0485 659 HOH   A O    
2198 O  O    B HOH   D .   ? 0.3981 0.3903 0.3502 -0.1221 0.0439  -0.0466 659 HOH   A O    
2199 O  O    . HOH   D .   ? 0.3153 0.4533 0.3829 -0.0732 0.0149  0.0529  660 HOH   A O    
2200 O  O    A HOH   D .   ? 0.2363 0.1572 0.2168 0.0456  0.0441  0.0580  661 HOH   A O    
2201 O  O    B HOH   D .   ? 0.2410 0.1803 0.2290 0.0334  0.0320  0.0439  661 HOH   A O    
2202 O  O    . HOH   D .   ? 0.3729 0.3615 0.4165 -0.0491 -0.0373 0.0371  662 HOH   A O    
2203 O  O    A HOH   D .   ? 0.2420 0.2283 0.2258 0.0132  0.0060  0.0305  663 HOH   A O    
2204 O  O    B HOH   D .   ? 0.2595 0.2302 0.2424 0.0186  0.0138  0.0373  663 HOH   A O    
2205 O  O    . HOH   D .   ? 0.4957 0.6999 0.4770 -0.0876 -0.0228 -0.0096 664 HOH   A O    
2206 O  O    . HOH   D .   ? 0.5294 0.7941 0.5342 -0.0507 -0.0466 0.0442  665 HOH   A O    
2207 O  O    . HOH   D .   ? 0.5077 0.4033 0.4507 -0.0819 0.0692  0.0234  666 HOH   A O    
2208 O  O    . HOH   D .   ? 0.5672 0.4745 0.5131 -0.0125 0.0527  0.0577  667 HOH   A O    
2209 O  O    . HOH   D .   ? 0.6569 0.8010 0.5849 -0.1151 0.0350  -0.0443 668 HOH   A O    
2210 O  O    A HOH   D .   ? 0.2891 0.6650 0.3448 -0.0101 -0.0213 -0.0586 669 HOH   A O    
2211 O  O    B HOH   D .   ? 0.2903 0.6753 0.3353 -0.0288 -0.0168 -0.0553 669 HOH   A O    
2212 O  O    . HOH   D .   ? 0.4560 0.5100 0.6234 0.1076  -0.0607 -0.0425 670 HOH   A O    
2213 O  O    . HOH   D .   ? 0.7223 0.6530 0.6986 0.0979  0.0622  0.1084  671 HOH   A O    
2214 O  O    . HOH   D .   ? 0.5801 0.5552 0.5538 0.0305  0.0211  0.0541  672 HOH   A O    
2215 O  O    . HOH   D .   ? 0.3863 0.4466 0.4990 -0.0649 -0.0445 -0.0210 673 HOH   A O    
2216 O  O    . HOH   E .   ? 0.3965 0.5228 0.4717 -0.0287 -0.0571 -0.0750 701 HOH   C O    
2217 O  O    . HOH   E .   ? 0.4616 0.5429 0.5484 -0.0404 -0.0555 -0.0718 702 HOH   C O    
2218 O  O    A HOH   E .   ? 0.2650 0.1687 0.3888 -0.0369 -0.0440 -0.0119 703 HOH   C O    
2219 O  O    B HOH   E .   ? 0.2606 0.1688 0.3791 -0.0429 -0.0419 0.0053  703 HOH   C O    
# 
