data_9M13
# 
_entry.id   9M13 
# 
_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   9M13         pdb_00009m13 10.2210/pdb9m13/pdb 
WWPDB D_1300056750 ?            ?                   
# 
_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                        9M13 
_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)phenyl]-dimethyl-silyl]phenoxy]-4-oxidanyl-pentanoic acid' 460.635 
1   ? ? ? ? 
4 water       nat water                                                                                                   18.015 
239 ? ? ? ? 
# 
_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)phenyl]-dimethyl-silyl]phenoxy]-4-oxidanyl-pentanoic acid' A1L70 
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 
A1L70 non-polymer         . 
'(4~{S})-5-[4-[[4-(2-ethyl-2-oxidanyl-butoxy)phenyl]-dimethyl-silyl]phenoxy]-4-oxidanyl-pentanoic acid' ? 'C25 H36 O6 Si'  460.635 
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        A1L70 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1L70 
_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 A1L70 1   501 501 A1L70 LIG A . 
D 4 HOH   1   601 28  HOH   HOH A . 
D 4 HOH   2   602 34  HOH   HOH A . 
D 4 HOH   3   603 219 HOH   HOH A . 
D 4 HOH   4   604 57  HOH   HOH A . 
D 4 HOH   5   605 232 HOH   HOH A . 
D 4 HOH   6   606 199 HOH   HOH A . 
D 4 HOH   7   607 191 HOH   HOH A . 
D 4 HOH   8   608 104 HOH   HOH A . 
D 4 HOH   9   609 130 HOH   HOH A . 
D 4 HOH   10  610 119 HOH   HOH A . 
D 4 HOH   11  611 114 HOH   HOH A . 
D 4 HOH   12  612 231 HOH   HOH A . 
D 4 HOH   13  613 109 HOH   HOH A . 
D 4 HOH   14  614 149 HOH   HOH A . 
D 4 HOH   15  615 118 HOH   HOH A . 
D 4 HOH   16  616 18  HOH   HOH A . 
D 4 HOH   17  617 72  HOH   HOH A . 
D 4 HOH   18  618 224 HOH   HOH A . 
D 4 HOH   19  619 85  HOH   HOH A . 
D 4 HOH   20  620 213 HOH   HOH A . 
D 4 HOH   21  621 156 HOH   HOH A . 
D 4 HOH   22  622 87  HOH   HOH A . 
D 4 HOH   23  623 6   HOH   HOH A . 
D 4 HOH   24  624 143 HOH   HOH A . 
D 4 HOH   25  625 95  HOH   HOH A . 
D 4 HOH   26  626 164 HOH   HOH A . 
D 4 HOH   27  627 203 HOH   HOH A . 
D 4 HOH   28  628 14  HOH   HOH A . 
D 4 HOH   29  629 186 HOH   HOH A . 
D 4 HOH   30  630 243 HOH   HOH A . 
D 4 HOH   31  631 48  HOH   HOH A . 
D 4 HOH   32  632 49  HOH   HOH A . 
D 4 HOH   33  633 241 HOH   HOH A . 
D 4 HOH   34  634 35  HOH   HOH A . 
D 4 HOH   35  635 9   HOH   HOH A . 
D 4 HOH   36  636 20  HOH   HOH A . 
D 4 HOH   37  637 217 HOH   HOH A . 
D 4 HOH   38  638 66  HOH   HOH A . 
D 4 HOH   39  639 184 HOH   HOH A . 
D 4 HOH   40  640 155 HOH   HOH A . 
D 4 HOH   41  641 93  HOH   HOH A . 
D 4 HOH   42  642 163 HOH   HOH A . 
D 4 HOH   43  643 207 HOH   HOH A . 
D 4 HOH   44  644 13  HOH   HOH A . 
D 4 HOH   45  645 25  HOH   HOH A . 
D 4 HOH   46  646 117 HOH   HOH A . 
D 4 HOH   47  647 10  HOH   HOH A . 
D 4 HOH   48  648 168 HOH   HOH A . 
D 4 HOH   49  649 58  HOH   HOH A . 
D 4 HOH   50  650 78  HOH   HOH A . 
D 4 HOH   51  651 11  HOH   HOH A . 
D 4 HOH   52  652 113 HOH   HOH A . 
D 4 HOH   53  653 101 HOH   HOH A . 
D 4 HOH   54  654 76  HOH   HOH A . 
D 4 HOH   55  655 84  HOH   HOH A . 
D 4 HOH   56  656 23  HOH   HOH A . 
D 4 HOH   57  657 238 HOH   HOH A . 
D 4 HOH   58  658 4   HOH   HOH A . 
D 4 HOH   59  659 105 HOH   HOH A . 
D 4 HOH   60  660 12  HOH   HOH A . 
D 4 HOH   61  661 2   HOH   HOH A . 
D 4 HOH   62  662 30  HOH   HOH A . 
D 4 HOH   63  663 62  HOH   HOH A . 
D 4 HOH   64  664 91  HOH   HOH A . 
D 4 HOH   65  665 193 HOH   HOH A . 
D 4 HOH   66  666 45  HOH   HOH A . 
D 4 HOH   67  667 21  HOH   HOH A . 
D 4 HOH   68  668 90  HOH   HOH A . 
D 4 HOH   69  669 124 HOH   HOH A . 
D 4 HOH   70  670 3   HOH   HOH A . 
D 4 HOH   71  671 75  HOH   HOH A . 
D 4 HOH   72  672 131 HOH   HOH A . 
D 4 HOH   73  673 32  HOH   HOH A . 
D 4 HOH   74  674 129 HOH   HOH A . 
D 4 HOH   75  675 5   HOH   HOH A . 
D 4 HOH   76  676 165 HOH   HOH A . 
D 4 HOH   77  677 51  HOH   HOH A . 
D 4 HOH   78  678 166 HOH   HOH A . 
D 4 HOH   79  679 27  HOH   HOH A . 
D 4 HOH   80  680 69  HOH   HOH A . 
D 4 HOH   81  681 26  HOH   HOH A . 
D 4 HOH   82  682 1   HOH   HOH A . 
D 4 HOH   83  683 67  HOH   HOH A . 
D 4 HOH   84  684 83  HOH   HOH A . 
D 4 HOH   85  685 107 HOH   HOH A . 
D 4 HOH   86  686 214 HOH   HOH A . 
D 4 HOH   87  687 16  HOH   HOH A . 
D 4 HOH   88  688 53  HOH   HOH A . 
D 4 HOH   89  689 46  HOH   HOH A . 
D 4 HOH   90  690 24  HOH   HOH A . 
D 4 HOH   91  691 115 HOH   HOH A . 
D 4 HOH   92  692 187 HOH   HOH A . 
D 4 HOH   93  693 226 HOH   HOH A . 
D 4 HOH   94  694 108 HOH   HOH A . 
D 4 HOH   95  695 17  HOH   HOH A . 
D 4 HOH   96  696 15  HOH   HOH A . 
D 4 HOH   97  697 36  HOH   HOH A . 
D 4 HOH   98  698 81  HOH   HOH A . 
D 4 HOH   99  699 121 HOH   HOH A . 
D 4 HOH   100 700 218 HOH   HOH A . 
D 4 HOH   101 701 97  HOH   HOH A . 
D 4 HOH   102 702 201 HOH   HOH A . 
D 4 HOH   103 703 126 HOH   HOH A . 
D 4 HOH   104 704 60  HOH   HOH A . 
D 4 HOH   105 705 147 HOH   HOH A . 
D 4 HOH   106 706 64  HOH   HOH A . 
D 4 HOH   107 707 227 HOH   HOH A . 
D 4 HOH   108 708 144 HOH   HOH A . 
D 4 HOH   109 709 185 HOH   HOH A . 
D 4 HOH   110 710 7   HOH   HOH A . 
D 4 HOH   111 711 63  HOH   HOH A . 
D 4 HOH   112 712 202 HOH   HOH A . 
D 4 HOH   113 713 216 HOH   HOH A . 
D 4 HOH   114 714 154 HOH   HOH A . 
D 4 HOH   115 715 39  HOH   HOH A . 
D 4 HOH   116 716 89  HOH   HOH A . 
D 4 HOH   117 717 59  HOH   HOH A . 
D 4 HOH   118 718 245 HOH   HOH A . 
D 4 HOH   119 719 106 HOH   HOH A . 
D 4 HOH   120 720 139 HOH   HOH A . 
D 4 HOH   121 721 50  HOH   HOH A . 
D 4 HOH   122 722 103 HOH   HOH A . 
D 4 HOH   123 723 37  HOH   HOH A . 
D 4 HOH   124 724 8   HOH   HOH A . 
D 4 HOH   125 725 71  HOH   HOH A . 
D 4 HOH   126 726 31  HOH   HOH A . 
D 4 HOH   127 727 200 HOH   HOH A . 
D 4 HOH   128 728 40  HOH   HOH A . 
D 4 HOH   129 729 42  HOH   HOH A . 
D 4 HOH   130 730 33  HOH   HOH A . 
D 4 HOH   131 731 82  HOH   HOH A . 
D 4 HOH   132 732 190 HOH   HOH A . 
D 4 HOH   133 733 174 HOH   HOH A . 
D 4 HOH   134 734 189 HOH   HOH A . 
D 4 HOH   135 735 98  HOH   HOH A . 
D 4 HOH   136 736 43  HOH   HOH A . 
D 4 HOH   137 737 92  HOH   HOH A . 
D 4 HOH   138 738 96  HOH   HOH A . 
D 4 HOH   139 739 128 HOH   HOH A . 
D 4 HOH   140 740 194 HOH   HOH A . 
D 4 HOH   141 741 176 HOH   HOH A . 
D 4 HOH   142 742 47  HOH   HOH A . 
D 4 HOH   143 743 86  HOH   HOH A . 
D 4 HOH   144 744 22  HOH   HOH A . 
D 4 HOH   145 745 151 HOH   HOH A . 
D 4 HOH   146 746 55  HOH   HOH A . 
D 4 HOH   147 747 77  HOH   HOH A . 
D 4 HOH   148 748 195 HOH   HOH A . 
D 4 HOH   149 749 88  HOH   HOH A . 
D 4 HOH   150 750 247 HOH   HOH A . 
D 4 HOH   151 751 172 HOH   HOH A . 
D 4 HOH   152 752 188 HOH   HOH A . 
D 4 HOH   153 753 153 HOH   HOH A . 
D 4 HOH   154 754 56  HOH   HOH A . 
D 4 HOH   155 755 74  HOH   HOH A . 
D 4 HOH   156 756 177 HOH   HOH A . 
D 4 HOH   157 757 38  HOH   HOH A . 
D 4 HOH   158 758 44  HOH   HOH A . 
D 4 HOH   159 759 197 HOH   HOH A . 
D 4 HOH   160 760 54  HOH   HOH A . 
D 4 HOH   161 761 120 HOH   HOH A . 
D 4 HOH   162 762 240 HOH   HOH A . 
D 4 HOH   163 763 148 HOH   HOH A . 
D 4 HOH   164 764 159 HOH   HOH A . 
D 4 HOH   165 765 220 HOH   HOH A . 
D 4 HOH   166 766 196 HOH   HOH A . 
D 4 HOH   167 767 70  HOH   HOH A . 
D 4 HOH   168 768 230 HOH   HOH A . 
D 4 HOH   169 769 133 HOH   HOH A . 
D 4 HOH   170 770 138 HOH   HOH A . 
D 4 HOH   171 771 237 HOH   HOH A . 
D 4 HOH   172 772 110 HOH   HOH A . 
D 4 HOH   173 773 141 HOH   HOH A . 
D 4 HOH   174 774 171 HOH   HOH A . 
D 4 HOH   175 775 142 HOH   HOH A . 
D 4 HOH   176 776 246 HOH   HOH A . 
D 4 HOH   177 777 152 HOH   HOH A . 
D 4 HOH   178 778 122 HOH   HOH A . 
D 4 HOH   179 779 150 HOH   HOH A . 
D 4 HOH   180 780 182 HOH   HOH A . 
D 4 HOH   181 781 221 HOH   HOH A . 
D 4 HOH   182 782 215 HOH   HOH A . 
D 4 HOH   183 783 183 HOH   HOH A . 
D 4 HOH   184 784 178 HOH   HOH A . 
D 4 HOH   185 785 205 HOH   HOH A . 
D 4 HOH   186 786 242 HOH   HOH A . 
D 4 HOH   187 787 29  HOH   HOH A . 
D 4 HOH   188 788 181 HOH   HOH A . 
D 4 HOH   189 789 225 HOH   HOH A . 
D 4 HOH   190 790 250 HOH   HOH A . 
D 4 HOH   191 791 223 HOH   HOH A . 
D 4 HOH   192 792 145 HOH   HOH A . 
D 4 HOH   193 793 209 HOH   HOH A . 
D 4 HOH   194 794 94  HOH   HOH A . 
D 4 HOH   195 795 248 HOH   HOH A . 
D 4 HOH   196 796 111 HOH   HOH A . 
D 4 HOH   197 797 146 HOH   HOH A . 
D 4 HOH   198 798 210 HOH   HOH A . 
D 4 HOH   199 799 208 HOH   HOH A . 
D 4 HOH   200 800 158 HOH   HOH A . 
D 4 HOH   201 801 61  HOH   HOH A . 
D 4 HOH   202 802 169 HOH   HOH A . 
D 4 HOH   203 803 137 HOH   HOH A . 
D 4 HOH   204 804 229 HOH   HOH A . 
D 4 HOH   205 805 157 HOH   HOH A . 
D 4 HOH   206 806 233 HOH   HOH A . 
D 4 HOH   207 807 79  HOH   HOH A . 
D 4 HOH   208 808 73  HOH   HOH A . 
D 4 HOH   209 809 180 HOH   HOH A . 
D 4 HOH   210 810 80  HOH   HOH A . 
D 4 HOH   211 811 123 HOH   HOH A . 
D 4 HOH   212 812 244 HOH   HOH A . 
D 4 HOH   213 813 236 HOH   HOH A . 
D 4 HOH   214 814 68  HOH   HOH A . 
D 4 HOH   215 815 204 HOH   HOH A . 
D 4 HOH   216 816 135 HOH   HOH A . 
D 4 HOH   217 817 100 HOH   HOH A . 
D 4 HOH   218 818 198 HOH   HOH A . 
D 4 HOH   219 819 211 HOH   HOH A . 
D 4 HOH   220 820 132 HOH   HOH A . 
D 4 HOH   221 821 162 HOH   HOH A . 
D 4 HOH   222 822 136 HOH   HOH A . 
D 4 HOH   223 823 116 HOH   HOH A . 
D 4 HOH   224 824 228 HOH   HOH A . 
D 4 HOH   225 825 160 HOH   HOH A . 
D 4 HOH   226 826 19  HOH   HOH A . 
D 4 HOH   227 827 170 HOH   HOH A . 
D 4 HOH   228 828 179 HOH   HOH A . 
D 4 HOH   229 829 175 HOH   HOH A . 
D 4 HOH   230 830 235 HOH   HOH A . 
D 4 HOH   231 831 239 HOH   HOH A . 
D 4 HOH   232 832 222 HOH   HOH A . 
D 4 HOH   233 833 192 HOH   HOH A . 
D 4 HOH   234 834 206 HOH   HOH A . 
D 4 HOH   235 835 112 HOH   HOH A . 
E 4 HOH   1   701 52  HOH   HOH C . 
E 4 HOH   2   702 65  HOH   HOH C . 
E 4 HOH   3   703 125 HOH   HOH C . 
E 4 HOH   4   704 41  HOH   HOH C . 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX ? ? ? 1.14_3260 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS    ? ? ? .         2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? XDS    ? ? ? .         3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHENIX ? ? ? .         4 
# 
_cell.angle_alpha                  90.000 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   100.186 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9M13 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     124.699 
_cell.length_a_esd                 ? 
_cell.length_b                     44.798 
_cell.length_b_esd                 ? 
_cell.length_c                     46.786 
_cell.length_c_esd                 ? 
_cell.volume                       257239.713 
_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                         9M13 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                5 
_symmetry.space_group_name_Hall            'C 2y' 
_symmetry.space_group_name_H-M             'C 1 2 1' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   9M13 
_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             2.00 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          38.48 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              ? 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    'PEG 3350, Sodium malonate, pH 6.' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            293 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS EIGER X 4M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2023-07-21 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   1.0 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'SPRING-8 BEAMLINE BL26B1' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        1.0 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   BL26B1 
_diffrn_source.pdbx_synchrotron_site       SPring-8 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9M13 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.68 
_reflns.d_resolution_low                               46.05 
_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                                     29249 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           99.8 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                3.4 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          13.6 
_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                                   0.998 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.049 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    1.68 
_reflns_shell.d_res_low                                     1.74 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           1.7 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             1494 
_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                                  0.726 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  0.697 
_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                               27.47 
_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                                 9M13 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            1.68 
_refine.ls_d_res_low                             46.05 
_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                     29243 
_refine.ls_number_reflns_R_free                  1463 
_refine.ls_number_reflns_R_work                  27780 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.76 
_refine.ls_percent_reflns_R_free                 5.00 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1711 
_refine.ls_R_factor_R_free                       0.1978 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1697 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.correlation_coeff_I_to_Fcsqd_work        ? 
_refine.correlation_coeff_I_to_Fcsqd_free        ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.34 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      2ZLC 
_refine.pdbx_stereochemistry_target_values       'CDL v1.2' 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.1100 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.9000 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 20.4836 
_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                            0.2079 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       1.68 
_refine_hist.d_res_low                        46.05 
_refine_hist.number_atoms_solvent             239 
_refine_hist.number_atoms_total               2286 
_refine_hist.number_reflns_all                ? 
_refine_hist.number_reflns_obs                ? 
_refine_hist.number_reflns_R_free             ? 
_refine_hist.number_reflns_R_work             ? 
_refine_hist.R_factor_all                     ? 
_refine_hist.R_factor_obs                     ? 
_refine_hist.R_factor_R_free                  ? 
_refine_hist.R_factor_R_work                  ? 
_refine_hist.pdbx_number_residues_total       ? 
_refine_hist.pdbx_B_iso_mean_ligand           ? 
_refine_hist.pdbx_B_iso_mean_solvent          ? 
_refine_hist.pdbx_number_atoms_protein        2015 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         32 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.0046  ? 2163 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.7301  ? 2936 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 0.0423  ? 327  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.0044  ? 377  ? f_plane_restr      ? ? 
'X-RAY DIFFRACTION' ? 22.6394 ? 835  ? f_dihedral_angle_d ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.correlation_coeff_Fo_to_Fc 
_refine_ls_shell.correlation_coeff_Fo_to_Fc_free 
_refine_ls_shell.correlation_coeff_I_to_Fcsqd_work 
_refine_ls_shell.correlation_coeff_I_to_Fcsqd_free 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 1.68 1.74  . . 146 2780 99.25 . . . . 0.2589 . . . . . . . . . . . . . . . 0.3021 
'X-RAY DIFFRACTION' 1.74 1.81  . . 144 2732 99.76 . . . . 0.2350 . . . . . . . . . . . . . . . 0.2638 
'X-RAY DIFFRACTION' 1.81 1.89  . . 146 2757 99.86 . . . . 0.2012 . . . . . . . . . . . . . . . 0.2243 
'X-RAY DIFFRACTION' 1.89 1.99  . . 144 2746 99.83 . . . . 0.1880 . . . . . . . . . . . . . . . 0.2034 
'X-RAY DIFFRACTION' 1.99 2.11  . . 146 2776 99.93 . . . . 0.1677 . . . . . . . . . . . . . . . 0.2097 
'X-RAY DIFFRACTION' 2.11 2.28  . . 145 2754 99.72 . . . . 0.1555 . . . . . . . . . . . . . . . 0.1892 
'X-RAY DIFFRACTION' 2.28 2.51  . . 147 2792 99.90 . . . . 0.1578 . . . . . . . . . . . . . . . 0.1916 
'X-RAY DIFFRACTION' 2.51 2.87  . . 146 2789 99.86 . . . . 0.1579 . . . . . . . . . . . . . . . 0.1925 
'X-RAY DIFFRACTION' 2.87 3.62  . . 148 2791 99.73 . . . . 0.1595 . . . . . . . . . . . . . . . 0.1789 
'X-RAY DIFFRACTION' 3.62 46.05 . . 151 2863 99.74 . . . . 0.1657 . . . . . . . . . . . . . . . 0.1899 
# 
_struct.entry_id                     9M13 
_struct.title                        'Vitamin D receptor complex with a dimethyldiphenylsilane 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        9M13 
_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 9M13 A 11 ? 271 ? P13053 116 ? 423 ? 116 423 
2 2 9M13 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 9M13 GLY A 1  ? UNP P13053 ?   ?   'expression tag' 106 1  
1 9M13 SER A 2  ? UNP P13053 ?   ?   'expression tag' 107 2  
1 9M13 HIS A 3  ? UNP P13053 ?   ?   'expression tag' 108 3  
1 9M13 MET A 4  ? UNP P13053 ?   ?   'expression tag' 109 4  
1 9M13 GLY A 5  ? UNP P13053 ?   ?   'expression tag' 110 5  
1 9M13 SER A 6  ? UNP P13053 ?   ?   'expression tag' 111 6  
1 9M13 PRO A 7  ? UNP P13053 ?   ?   'expression tag' 112 7  
1 9M13 ASN A 8  ? UNP P13053 ?   ?   'expression tag' 113 8  
1 9M13 SER A 9  ? UNP P13053 ?   ?   'expression tag' 114 9  
1 9M13 PRO A 10 ? UNP P13053 ?   ?   'expression tag' 115 10 
1 9M13 ?   A ?  ? UNP P13053 TYR 166 deletion         ?   11 
1 9M13 ?   A ?  ? UNP P13053 SER 167 deletion         ?   12 
1 9M13 ?   A ?  ? UNP P13053 PRO 168 deletion         ?   13 
1 9M13 ?   A ?  ? UNP P13053 ARG 169 deletion         ?   14 
1 9M13 ?   A ?  ? UNP P13053 PRO 170 deletion         ?   15 
1 9M13 ?   A ?  ? UNP P13053 THR 171 deletion         ?   16 
1 9M13 ?   A ?  ? UNP P13053 LEU 172 deletion         ?   17 
1 9M13 ?   A ?  ? UNP P13053 SER 173 deletion         ?   18 
1 9M13 ?   A ?  ? UNP P13053 PHE 174 deletion         ?   19 
1 9M13 ?   A ?  ? UNP P13053 SER 175 deletion         ?   20 
1 9M13 ?   A ?  ? UNP P13053 GLY 176 deletion         ?   21 
1 9M13 ?   A ?  ? UNP P13053 ASN 177 deletion         ?   22 
1 9M13 ?   A ?  ? UNP P13053 SER 178 deletion         ?   23 
1 9M13 ?   A ?  ? UNP P13053 SER 179 deletion         ?   24 
1 9M13 ?   A ?  ? UNP P13053 SER 180 deletion         ?   25 
1 9M13 ?   A ?  ? UNP P13053 SER 181 deletion         ?   26 
1 9M13 ?   A ?  ? UNP P13053 SER 182 deletion         ?   27 
1 9M13 ?   A ?  ? UNP P13053 SER 183 deletion         ?   28 
1 9M13 ?   A ?  ? UNP P13053 ASP 184 deletion         ?   29 
1 9M13 ?   A ?  ? UNP P13053 LEU 185 deletion         ?   30 
1 9M13 ?   A ?  ? UNP P13053 TYR 186 deletion         ?   31 
1 9M13 ?   A ?  ? UNP P13053 THR 187 deletion         ?   32 
1 9M13 ?   A ?  ? UNP P13053 THR 188 deletion         ?   33 
1 9M13 ?   A ?  ? UNP P13053 SER 189 deletion         ?   34 
1 9M13 ?   A ?  ? UNP P13053 LEU 190 deletion         ?   35 
1 9M13 ?   A ?  ? UNP P13053 ASP 191 deletion         ?   36 
1 9M13 ?   A ?  ? UNP P13053 MET 192 deletion         ?   37 
1 9M13 ?   A ?  ? UNP P13053 MET 193 deletion         ?   38 
1 9M13 ?   A ?  ? UNP P13053 GLU 194 deletion         ?   39 
1 9M13 ?   A ?  ? UNP P13053 PRO 195 deletion         ?   40 
1 9M13 ?   A ?  ? UNP P13053 SER 196 deletion         ?   41 
1 9M13 ?   A ?  ? UNP P13053 GLY 197 deletion         ?   42 
1 9M13 ?   A ?  ? UNP P13053 PHE 198 deletion         ?   43 
1 9M13 ?   A ?  ? UNP P13053 SER 199 deletion         ?   44 
1 9M13 ?   A ?  ? UNP P13053 ASN 200 deletion         ?   45 
1 9M13 ?   A ?  ? UNP P13053 LEU 201 deletion         ?   46 
1 9M13 ?   A ?  ? UNP P13053 ASP 202 deletion         ?   47 
1 9M13 ?   A ?  ? UNP P13053 LEU 203 deletion         ?   48 
1 9M13 ?   A ?  ? UNP P13053 ASN 204 deletion         ?   49 
1 9M13 ?   A ?  ? UNP P13053 GLY 205 deletion         ?   50 
1 9M13 ?   A ?  ? UNP P13053 GLU 206 deletion         ?   51 
1 9M13 ?   A ?  ? UNP P13053 ASP 207 deletion         ?   52 
1 9M13 ?   A ?  ? UNP P13053 SER 208 deletion         ?   53 
1 9M13 ?   A ?  ? UNP P13053 ASP 209 deletion         ?   54 
1 9M13 ?   A ?  ? UNP P13053 ASP 210 deletion         ?   55 
1 9M13 ?   A ?  ? UNP P13053 PRO 211 deletion         ?   56 
1 9M13 ?   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)' 1100  ? 
1 MORE         -9    ? 
1 'SSA (A^2)'  11800 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'gel filtration' 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 SER A 20  ? TYR A 38  ? SER A 125 TYR A 143 1 ? 19 
HELX_P HELX_P2  AA2 TYR A 42  ? PHE A 48  ? TYR A 147 PHE A 153 5 ? 7  
HELX_P HELX_P3  AA3 MET A 70  ? LYS A 90  ? MET A 222 LYS A 242 1 ? 21 
HELX_P HELX_P4  AA4 GLY A 94  ? LEU A 98  ? GLY A 246 LEU A 250 5 ? 5  
HELX_P HELX_P5  AA5 THR A 99  ? ASN A 120 ? THR A 251 ASN A 272 1 ? 22 
HELX_P HELX_P6  AA6 ASP A 140 ? LYS A 146 ? ASP A 292 LYS A 298 1 ? 7  
HELX_P HELX_P7  AA7 THR A 150 ? LYS A 166 ? THR A 302 LYS A 318 1 ? 17 
HELX_P HELX_P8  AA8 HIS A 170 ? VAL A 183 ? HIS A 322 VAL A 335 1 ? 14 
HELX_P HELX_P9  AA9 ASP A 192 ? HIS A 215 ? ASP A 344 HIS A 367 1 ? 24 
HELX_P HELX_P10 AB1 GLN A 222 ? GLN A 251 ? GLN A 374 GLN A 403 1 ? 30 
HELX_P HELX_P11 AB2 GLN A 251 ? MET A 256 ? GLN A 403 MET A 408 1 ? 6  
HELX_P HELX_P12 AB3 THR A 259 ? GLY A 267 ? THR A 411 GLY A 419 1 ? 9  
HELX_P HELX_P13 AB4 HIS B 3   ? 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       -0.32 
# 
_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                   9M13 
_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 ASP A 279 ? ? -148.65 21.62  
2 1 CYS A 284 ? ? -102.79 49.55  
3 1 ASN A 320 ? A 37.12   63.78  
4 1 HIS A 373 ? ? -56.06  106.88 
# 
loop_
_pdbx_refine_tls.id 
_pdbx_refine_tls.pdbx_refine_id 
_pdbx_refine_tls.details 
_pdbx_refine_tls.method 
_pdbx_refine_tls.origin_x 
_pdbx_refine_tls.origin_y 
_pdbx_refine_tls.origin_z 
_pdbx_refine_tls.T[1][1] 
_pdbx_refine_tls.T[1][1]_esd 
_pdbx_refine_tls.T[1][2] 
_pdbx_refine_tls.T[1][2]_esd 
_pdbx_refine_tls.T[1][3] 
_pdbx_refine_tls.T[1][3]_esd 
_pdbx_refine_tls.T[2][2] 
_pdbx_refine_tls.T[2][2]_esd 
_pdbx_refine_tls.T[2][3] 
_pdbx_refine_tls.T[2][3]_esd 
_pdbx_refine_tls.T[3][3] 
_pdbx_refine_tls.T[3][3]_esd 
_pdbx_refine_tls.L[1][1] 
_pdbx_refine_tls.L[1][1]_esd 
_pdbx_refine_tls.L[1][2] 
_pdbx_refine_tls.L[1][2]_esd 
_pdbx_refine_tls.L[1][3] 
_pdbx_refine_tls.L[1][3]_esd 
_pdbx_refine_tls.L[2][2] 
_pdbx_refine_tls.L[2][2]_esd 
_pdbx_refine_tls.L[2][3] 
_pdbx_refine_tls.L[2][3]_esd 
_pdbx_refine_tls.L[3][3] 
_pdbx_refine_tls.L[3][3]_esd 
_pdbx_refine_tls.S[1][1] 
_pdbx_refine_tls.S[1][1]_esd 
_pdbx_refine_tls.S[1][2] 
_pdbx_refine_tls.S[1][2]_esd 
_pdbx_refine_tls.S[1][3] 
_pdbx_refine_tls.S[1][3]_esd 
_pdbx_refine_tls.S[2][1] 
_pdbx_refine_tls.S[2][1]_esd 
_pdbx_refine_tls.S[2][2] 
_pdbx_refine_tls.S[2][2]_esd 
_pdbx_refine_tls.S[2][3] 
_pdbx_refine_tls.S[2][3]_esd 
_pdbx_refine_tls.S[3][1] 
_pdbx_refine_tls.S[3][1]_esd 
_pdbx_refine_tls.S[3][2] 
_pdbx_refine_tls.S[3][2]_esd 
_pdbx_refine_tls.S[3][3] 
_pdbx_refine_tls.S[3][3]_esd 
1 'X-RAY DIFFRACTION' ? refined 17.8890041531 1.37586787586  11.1866935633  0.159302189354 ? -0.0146105829916 ? -0.00331992120758 
? 0.146473246905 ? -0.000678723431925 ? 0.10972825326  ? 2.34161760123 ? -0.369327218208 ? -0.108467837234 ? 1.41409816128 ? 
0.179883044082 ? 0.94710984336 ? -0.0266780276605 ? -0.271289723049 ? 0.139933777658  ? 0.0896830925659 ? 0.029359663713  ? 
-0.0718608324325 ? -0.044995809825 ? 0.0538408034568  ? 0.00398762835248 ? 
2 'X-RAY DIFFRACTION' ? refined 11.5045572014 -8.95129761649 -3.30534936019 0.239914123866 ? 0.0945096173006  ? -0.0216878484223  
? 0.331817486147 ? -0.0105023426394   ? 0.258189176297 ? 6.67870086057 ? -0.574255765443 ? 1.05508645519   ? 5.17824104571 ? 
0.136411020834 ? 4.41950755416 ? -0.0617878725904 ? 0.378103802652  ? -0.550266730012 ? -0.335813756451 ? -0.077083869847 ? 
0.0300009087733  ? 0.334903084074  ? -0.0925427298422 ? 0.110877212405   ? 
# 
loop_
_pdbx_refine_tls_group.id 
_pdbx_refine_tls_group.pdbx_refine_id 
_pdbx_refine_tls_group.refine_tls_id 
_pdbx_refine_tls_group.beg_label_asym_id 
_pdbx_refine_tls_group.beg_label_seq_id 
_pdbx_refine_tls_group.beg_auth_asym_id 
_pdbx_refine_tls_group.beg_auth_seq_id 
_pdbx_refine_tls_group.beg_PDB_ins_code 
_pdbx_refine_tls_group.end_label_asym_id 
_pdbx_refine_tls_group.end_label_seq_id 
_pdbx_refine_tls_group.end_auth_asym_id 
_pdbx_refine_tls_group.end_auth_seq_id 
_pdbx_refine_tls_group.end_PDB_ins_code 
_pdbx_refine_tls_group.selection 
_pdbx_refine_tls_group.selection_details 
1 'X-RAY DIFFRACTION' 1 ? ? ? ? ? ? ? ? ? ? ? 'Chain A' 
2 'X-RAY DIFFRACTION' 2 ? ? ? ? ? ? ? ? ? ? ? 'Chain C' 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A GLY 106 ? A GLY 1   
2  1 Y 1 A SER 107 ? A SER 2   
3  1 Y 1 A HIS 108 ? A HIS 3   
4  1 Y 1 A MET 109 ? A MET 4   
5  1 Y 1 A GLY 110 ? A GLY 5   
6  1 Y 1 A SER 111 ? A SER 6   
7  1 Y 1 A PRO 112 ? A PRO 7   
8  1 Y 1 A ASN 113 ? A ASN 8   
9  1 Y 1 A SER 114 ? A SER 9   
10 1 Y 1 A PRO 115 ? A PRO 10  
11 1 Y 1 A LEU 116 ? A LEU 11  
12 1 Y 1 A LYS 117 ? A LYS 12  
13 1 Y 1 A ASP 118 ? A ASP 13  
14 1 Y 1 A SER 119 ? A SER 14  
15 1 Y 1 A LEU 120 ? A LEU 15  
16 1 Y 1 A ARG 121 ? A ARG 16  
17 1 Y 1 A PRO 122 ? A PRO 17  
18 1 Y 1 A ASP 207 ? A ASP 55  
19 1 Y 1 A GLY 208 ? A GLY 56  
20 1 Y 1 A SER 209 ? A SER 57  
21 1 Y 1 A THR 210 ? A THR 58  
22 1 Y 1 A GLY 211 ? A GLY 59  
23 1 Y 1 A SER 212 ? A SER 60  
24 1 Y 1 A VAL 213 ? A VAL 61  
25 1 Y 1 A THR 214 ? A THR 62  
26 1 Y 1 A LEU 215 ? A LEU 63  
27 1 Y 1 A ASP 216 ? A ASP 64  
28 1 Y 1 A LEU 217 ? A LEU 65  
29 1 Y 1 A GLU 421 ? A GLU 269 
30 1 Y 1 A ILE 422 ? A ILE 270 
31 1 Y 1 A SER 423 ? A SER 271 
32 1 Y 1 C ASP 636 ? B ASP 12  
33 1 Y 1 C ASN 637 ? B ASN 13  
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
A1L70 C10  C  N N 1   
A1L70 C13  C  Y N 2   
A1L70 C15  C  Y N 3   
A1L70 C20  C  N N 4   
A1L70 C21  C  N N 5   
A1L70 C22  C  N N 6   
A1L70 C26  C  N S 7   
A1L70 C28  C  N N 8   
A1L70 C01  C  Y N 9   
A1L70 C02  C  Y N 10  
A1L70 C03  C  Y N 11  
A1L70 C04  C  Y N 12  
A1L70 C05  C  Y N 13  
A1L70 C06  C  Y N 14  
A1L70 C09  C  Y N 15  
A1L70 C11  C  N N 16  
A1L70 C12  C  Y N 17  
A1L70 C14  C  Y N 18  
A1L70 C16  C  Y N 19  
A1L70 C18  C  N N 20  
A1L70 C19  C  N N 21  
A1L70 C23  C  N N 22  
A1L70 C25  C  N N 23  
A1L70 C29  C  N N 24  
A1L70 C30  C  N N 25  
A1L70 O07  O  N N 26  
A1L70 O17  O  N N 27  
A1L70 O24  O  N N 28  
A1L70 O27  O  N N 29  
A1L70 O31  O  N N 30  
A1L70 O32  O  N N 31  
A1L70 SI08 SI N N 32  
A1L70 H101 H  N N 33  
A1L70 H103 H  N N 34  
A1L70 H102 H  N N 35  
A1L70 H131 H  N N 36  
A1L70 H151 H  N N 37  
A1L70 H201 H  N N 38  
A1L70 H202 H  N N 39  
A1L70 H211 H  N N 40  
A1L70 H212 H  N N 41  
A1L70 H213 H  N N 42  
A1L70 H221 H  N N 43  
A1L70 H222 H  N N 44  
A1L70 H261 H  N N 45  
A1L70 H282 H  N N 46  
A1L70 H281 H  N N 47  
A1L70 H011 H  N N 48  
A1L70 H031 H  N N 49  
A1L70 H041 H  N N 50  
A1L70 H061 H  N N 51  
A1L70 H111 H  N N 52  
A1L70 H112 H  N N 53  
A1L70 H113 H  N N 54  
A1L70 H121 H  N N 55  
A1L70 H161 H  N N 56  
A1L70 H181 H  N N 57  
A1L70 H182 H  N N 58  
A1L70 H232 H  N N 59  
A1L70 H231 H  N N 60  
A1L70 H233 H  N N 61  
A1L70 H252 H  N N 62  
A1L70 H251 H  N N 63  
A1L70 H292 H  N N 64  
A1L70 H291 H  N N 65  
A1L70 H241 H  N N 66  
A1L70 H271 H  N N 67  
A1L70 H1   H  N N 68  
ALA   N    N  N N 69  
ALA   CA   C  N S 70  
ALA   C    C  N N 71  
ALA   O    O  N N 72  
ALA   CB   C  N N 73  
ALA   OXT  O  N N 74  
ALA   H    H  N N 75  
ALA   H2   H  N N 76  
ALA   HA   H  N N 77  
ALA   HB1  H  N N 78  
ALA   HB2  H  N N 79  
ALA   HB3  H  N N 80  
ALA   HXT  H  N N 81  
ARG   N    N  N N 82  
ARG   CA   C  N S 83  
ARG   C    C  N N 84  
ARG   O    O  N N 85  
ARG   CB   C  N N 86  
ARG   CG   C  N N 87  
ARG   CD   C  N N 88  
ARG   NE   N  N N 89  
ARG   CZ   C  N N 90  
ARG   NH1  N  N N 91  
ARG   NH2  N  N N 92  
ARG   OXT  O  N N 93  
ARG   H    H  N N 94  
ARG   H2   H  N N 95  
ARG   HA   H  N N 96  
ARG   HB2  H  N N 97  
ARG   HB3  H  N N 98  
ARG   HG2  H  N N 99  
ARG   HG3  H  N N 100 
ARG   HD2  H  N N 101 
ARG   HD3  H  N N 102 
ARG   HE   H  N N 103 
ARG   HH11 H  N N 104 
ARG   HH12 H  N N 105 
ARG   HH21 H  N N 106 
ARG   HH22 H  N N 107 
ARG   HXT  H  N N 108 
ASN   N    N  N N 109 
ASN   CA   C  N S 110 
ASN   C    C  N N 111 
ASN   O    O  N N 112 
ASN   CB   C  N N 113 
ASN   CG   C  N N 114 
ASN   OD1  O  N N 115 
ASN   ND2  N  N N 116 
ASN   OXT  O  N N 117 
ASN   H    H  N N 118 
ASN   H2   H  N N 119 
ASN   HA   H  N N 120 
ASN   HB2  H  N N 121 
ASN   HB3  H  N N 122 
ASN   HD21 H  N N 123 
ASN   HD22 H  N N 124 
ASN   HXT  H  N N 125 
ASP   N    N  N N 126 
ASP   CA   C  N S 127 
ASP   C    C  N N 128 
ASP   O    O  N N 129 
ASP   CB   C  N N 130 
ASP   CG   C  N N 131 
ASP   OD1  O  N N 132 
ASP   OD2  O  N N 133 
ASP   OXT  O  N N 134 
ASP   H    H  N N 135 
ASP   H2   H  N N 136 
ASP   HA   H  N N 137 
ASP   HB2  H  N N 138 
ASP   HB3  H  N N 139 
ASP   HD2  H  N N 140 
ASP   HXT  H  N N 141 
CYS   N    N  N N 142 
CYS   CA   C  N R 143 
CYS   C    C  N N 144 
CYS   O    O  N N 145 
CYS   CB   C  N N 146 
CYS   SG   S  N N 147 
CYS   OXT  O  N N 148 
CYS   H    H  N N 149 
CYS   H2   H  N N 150 
CYS   HA   H  N N 151 
CYS   HB2  H  N N 152 
CYS   HB3  H  N N 153 
CYS   HG   H  N N 154 
CYS   HXT  H  N N 155 
GLN   N    N  N N 156 
GLN   CA   C  N S 157 
GLN   C    C  N N 158 
GLN   O    O  N N 159 
GLN   CB   C  N N 160 
GLN   CG   C  N N 161 
GLN   CD   C  N N 162 
GLN   OE1  O  N N 163 
GLN   NE2  N  N N 164 
GLN   OXT  O  N N 165 
GLN   H    H  N N 166 
GLN   H2   H  N N 167 
GLN   HA   H  N N 168 
GLN   HB2  H  N N 169 
GLN   HB3  H  N N 170 
GLN   HG2  H  N N 171 
GLN   HG3  H  N N 172 
GLN   HE21 H  N N 173 
GLN   HE22 H  N N 174 
GLN   HXT  H  N N 175 
GLU   N    N  N N 176 
GLU   CA   C  N S 177 
GLU   C    C  N N 178 
GLU   O    O  N N 179 
GLU   CB   C  N N 180 
GLU   CG   C  N N 181 
GLU   CD   C  N N 182 
GLU   OE1  O  N N 183 
GLU   OE2  O  N N 184 
GLU   OXT  O  N N 185 
GLU   H    H  N N 186 
GLU   H2   H  N N 187 
GLU   HA   H  N N 188 
GLU   HB2  H  N N 189 
GLU   HB3  H  N N 190 
GLU   HG2  H  N N 191 
GLU   HG3  H  N N 192 
GLU   HE2  H  N N 193 
GLU   HXT  H  N N 194 
GLY   N    N  N N 195 
GLY   CA   C  N N 196 
GLY   C    C  N N 197 
GLY   O    O  N N 198 
GLY   OXT  O  N N 199 
GLY   H    H  N N 200 
GLY   H2   H  N N 201 
GLY   HA2  H  N N 202 
GLY   HA3  H  N N 203 
GLY   HXT  H  N N 204 
HIS   N    N  N N 205 
HIS   CA   C  N S 206 
HIS   C    C  N N 207 
HIS   O    O  N N 208 
HIS   CB   C  N N 209 
HIS   CG   C  Y N 210 
HIS   ND1  N  Y N 211 
HIS   CD2  C  Y N 212 
HIS   CE1  C  Y N 213 
HIS   NE2  N  Y N 214 
HIS   OXT  O  N N 215 
HIS   H    H  N N 216 
HIS   H2   H  N N 217 
HIS   HA   H  N N 218 
HIS   HB2  H  N N 219 
HIS   HB3  H  N N 220 
HIS   HD1  H  N N 221 
HIS   HD2  H  N N 222 
HIS   HE1  H  N N 223 
HIS   HE2  H  N N 224 
HIS   HXT  H  N N 225 
HOH   O    O  N N 226 
HOH   H1   H  N N 227 
HOH   H2   H  N N 228 
ILE   N    N  N N 229 
ILE   CA   C  N S 230 
ILE   C    C  N N 231 
ILE   O    O  N N 232 
ILE   CB   C  N S 233 
ILE   CG1  C  N N 234 
ILE   CG2  C  N N 235 
ILE   CD1  C  N N 236 
ILE   OXT  O  N N 237 
ILE   H    H  N N 238 
ILE   H2   H  N N 239 
ILE   HA   H  N N 240 
ILE   HB   H  N N 241 
ILE   HG12 H  N N 242 
ILE   HG13 H  N N 243 
ILE   HG21 H  N N 244 
ILE   HG22 H  N N 245 
ILE   HG23 H  N N 246 
ILE   HD11 H  N N 247 
ILE   HD12 H  N N 248 
ILE   HD13 H  N N 249 
ILE   HXT  H  N N 250 
LEU   N    N  N N 251 
LEU   CA   C  N S 252 
LEU   C    C  N N 253 
LEU   O    O  N N 254 
LEU   CB   C  N N 255 
LEU   CG   C  N N 256 
LEU   CD1  C  N N 257 
LEU   CD2  C  N N 258 
LEU   OXT  O  N N 259 
LEU   H    H  N N 260 
LEU   H2   H  N N 261 
LEU   HA   H  N N 262 
LEU   HB2  H  N N 263 
LEU   HB3  H  N N 264 
LEU   HG   H  N N 265 
LEU   HD11 H  N N 266 
LEU   HD12 H  N N 267 
LEU   HD13 H  N N 268 
LEU   HD21 H  N N 269 
LEU   HD22 H  N N 270 
LEU   HD23 H  N N 271 
LEU   HXT  H  N N 272 
LYS   N    N  N N 273 
LYS   CA   C  N S 274 
LYS   C    C  N N 275 
LYS   O    O  N N 276 
LYS   CB   C  N N 277 
LYS   CG   C  N N 278 
LYS   CD   C  N N 279 
LYS   CE   C  N N 280 
LYS   NZ   N  N N 281 
LYS   OXT  O  N N 282 
LYS   H    H  N N 283 
LYS   H2   H  N N 284 
LYS   HA   H  N N 285 
LYS   HB2  H  N N 286 
LYS   HB3  H  N N 287 
LYS   HG2  H  N N 288 
LYS   HG3  H  N N 289 
LYS   HD2  H  N N 290 
LYS   HD3  H  N N 291 
LYS   HE2  H  N N 292 
LYS   HE3  H  N N 293 
LYS   HZ1  H  N N 294 
LYS   HZ2  H  N N 295 
LYS   HZ3  H  N N 296 
LYS   HXT  H  N N 297 
MET   N    N  N N 298 
MET   CA   C  N S 299 
MET   C    C  N N 300 
MET   O    O  N N 301 
MET   CB   C  N N 302 
MET   CG   C  N N 303 
MET   SD   S  N N 304 
MET   CE   C  N N 305 
MET   OXT  O  N N 306 
MET   H    H  N N 307 
MET   H2   H  N N 308 
MET   HA   H  N N 309 
MET   HB2  H  N N 310 
MET   HB3  H  N N 311 
MET   HG2  H  N N 312 
MET   HG3  H  N N 313 
MET   HE1  H  N N 314 
MET   HE2  H  N N 315 
MET   HE3  H  N N 316 
MET   HXT  H  N N 317 
PHE   N    N  N N 318 
PHE   CA   C  N S 319 
PHE   C    C  N N 320 
PHE   O    O  N N 321 
PHE   CB   C  N N 322 
PHE   CG   C  Y N 323 
PHE   CD1  C  Y N 324 
PHE   CD2  C  Y N 325 
PHE   CE1  C  Y N 326 
PHE   CE2  C  Y N 327 
PHE   CZ   C  Y N 328 
PHE   OXT  O  N N 329 
PHE   H    H  N N 330 
PHE   H2   H  N N 331 
PHE   HA   H  N N 332 
PHE   HB2  H  N N 333 
PHE   HB3  H  N N 334 
PHE   HD1  H  N N 335 
PHE   HD2  H  N N 336 
PHE   HE1  H  N N 337 
PHE   HE2  H  N N 338 
PHE   HZ   H  N N 339 
PHE   HXT  H  N N 340 
PRO   N    N  N N 341 
PRO   CA   C  N S 342 
PRO   C    C  N N 343 
PRO   O    O  N N 344 
PRO   CB   C  N N 345 
PRO   CG   C  N N 346 
PRO   CD   C  N N 347 
PRO   OXT  O  N N 348 
PRO   H    H  N N 349 
PRO   HA   H  N N 350 
PRO   HB2  H  N N 351 
PRO   HB3  H  N N 352 
PRO   HG2  H  N N 353 
PRO   HG3  H  N N 354 
PRO   HD2  H  N N 355 
PRO   HD3  H  N N 356 
PRO   HXT  H  N N 357 
SER   N    N  N N 358 
SER   CA   C  N S 359 
SER   C    C  N N 360 
SER   O    O  N N 361 
SER   CB   C  N N 362 
SER   OG   O  N N 363 
SER   OXT  O  N N 364 
SER   H    H  N N 365 
SER   H2   H  N N 366 
SER   HA   H  N N 367 
SER   HB2  H  N N 368 
SER   HB3  H  N N 369 
SER   HG   H  N N 370 
SER   HXT  H  N N 371 
THR   N    N  N N 372 
THR   CA   C  N S 373 
THR   C    C  N N 374 
THR   O    O  N N 375 
THR   CB   C  N R 376 
THR   OG1  O  N N 377 
THR   CG2  C  N N 378 
THR   OXT  O  N N 379 
THR   H    H  N N 380 
THR   H2   H  N N 381 
THR   HA   H  N N 382 
THR   HB   H  N N 383 
THR   HG1  H  N N 384 
THR   HG21 H  N N 385 
THR   HG22 H  N N 386 
THR   HG23 H  N N 387 
THR   HXT  H  N N 388 
TRP   N    N  N N 389 
TRP   CA   C  N S 390 
TRP   C    C  N N 391 
TRP   O    O  N N 392 
TRP   CB   C  N N 393 
TRP   CG   C  Y N 394 
TRP   CD1  C  Y N 395 
TRP   CD2  C  Y N 396 
TRP   NE1  N  Y N 397 
TRP   CE2  C  Y N 398 
TRP   CE3  C  Y N 399 
TRP   CZ2  C  Y N 400 
TRP   CZ3  C  Y N 401 
TRP   CH2  C  Y N 402 
TRP   OXT  O  N N 403 
TRP   H    H  N N 404 
TRP   H2   H  N N 405 
TRP   HA   H  N N 406 
TRP   HB2  H  N N 407 
TRP   HB3  H  N N 408 
TRP   HD1  H  N N 409 
TRP   HE1  H  N N 410 
TRP   HE3  H  N N 411 
TRP   HZ2  H  N N 412 
TRP   HZ3  H  N N 413 
TRP   HH2  H  N N 414 
TRP   HXT  H  N N 415 
TYR   N    N  N N 416 
TYR   CA   C  N S 417 
TYR   C    C  N N 418 
TYR   O    O  N N 419 
TYR   CB   C  N N 420 
TYR   CG   C  Y N 421 
TYR   CD1  C  Y N 422 
TYR   CD2  C  Y N 423 
TYR   CE1  C  Y N 424 
TYR   CE2  C  Y N 425 
TYR   CZ   C  Y N 426 
TYR   OH   O  N N 427 
TYR   OXT  O  N N 428 
TYR   H    H  N N 429 
TYR   H2   H  N N 430 
TYR   HA   H  N N 431 
TYR   HB2  H  N N 432 
TYR   HB3  H  N N 433 
TYR   HD1  H  N N 434 
TYR   HD2  H  N N 435 
TYR   HE1  H  N N 436 
TYR   HE2  H  N N 437 
TYR   HH   H  N N 438 
TYR   HXT  H  N N 439 
VAL   N    N  N N 440 
VAL   CA   C  N S 441 
VAL   C    C  N N 442 
VAL   O    O  N N 443 
VAL   CB   C  N N 444 
VAL   CG1  C  N N 445 
VAL   CG2  C  N N 446 
VAL   OXT  O  N N 447 
VAL   H    H  N N 448 
VAL   H2   H  N N 449 
VAL   HA   H  N N 450 
VAL   HB   H  N N 451 
VAL   HG11 H  N N 452 
VAL   HG12 H  N N 453 
VAL   HG13 H  N N 454 
VAL   HG21 H  N N 455 
VAL   HG22 H  N N 456 
VAL   HG23 H  N N 457 
VAL   HXT  H  N N 458 
# 
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 
A1L70 C01  C02  doub Y N 1   
A1L70 C01  C06  sing Y N 2   
A1L70 C02  C03  sing Y N 3   
A1L70 C02  O07  sing N N 4   
A1L70 C03  C04  doub Y N 5   
A1L70 C04  C05  sing Y N 6   
A1L70 C05  C06  doub Y N 7   
A1L70 C05  SI08 sing N N 8   
A1L70 O07  C25  sing N N 9   
A1L70 SI08 C09  sing N N 10  
A1L70 SI08 C10  sing N N 11  
A1L70 SI08 C11  sing N N 12  
A1L70 C09  C12  doub Y N 13  
A1L70 C09  C16  sing Y N 14  
A1L70 C12  C13  sing Y N 15  
A1L70 C13  C14  doub Y N 16  
A1L70 C14  C15  sing Y N 17  
A1L70 C14  O17  sing N N 18  
A1L70 C15  C16  doub Y N 19  
A1L70 O17  C18  sing N N 20  
A1L70 C18  C19  sing N N 21  
A1L70 C19  C20  sing N N 22  
A1L70 C19  C22  sing N N 23  
A1L70 C19  O24  sing N N 24  
A1L70 C20  C21  sing N N 25  
A1L70 C22  C23  sing N N 26  
A1L70 C25  C26  sing N N 27  
A1L70 C26  O27  sing N N 28  
A1L70 C26  C28  sing N N 29  
A1L70 C28  C29  sing N N 30  
A1L70 C29  C30  sing N N 31  
A1L70 C30  O31  doub N N 32  
A1L70 C30  O32  sing N N 33  
A1L70 C10  H101 sing N N 34  
A1L70 C10  H103 sing N N 35  
A1L70 C10  H102 sing N N 36  
A1L70 C13  H131 sing N N 37  
A1L70 C15  H151 sing N N 38  
A1L70 C20  H201 sing N N 39  
A1L70 C20  H202 sing N N 40  
A1L70 C21  H211 sing N N 41  
A1L70 C21  H212 sing N N 42  
A1L70 C21  H213 sing N N 43  
A1L70 C22  H221 sing N N 44  
A1L70 C22  H222 sing N N 45  
A1L70 C26  H261 sing N N 46  
A1L70 C28  H282 sing N N 47  
A1L70 C28  H281 sing N N 48  
A1L70 C01  H011 sing N N 49  
A1L70 C03  H031 sing N N 50  
A1L70 C04  H041 sing N N 51  
A1L70 C06  H061 sing N N 52  
A1L70 C11  H111 sing N N 53  
A1L70 C11  H112 sing N N 54  
A1L70 C11  H113 sing N N 55  
A1L70 C12  H121 sing N N 56  
A1L70 C16  H161 sing N N 57  
A1L70 C18  H181 sing N N 58  
A1L70 C18  H182 sing N N 59  
A1L70 C23  H232 sing N N 60  
A1L70 C23  H231 sing N N 61  
A1L70 C23  H233 sing N N 62  
A1L70 C25  H252 sing N N 63  
A1L70 C25  H251 sing N N 64  
A1L70 C29  H292 sing N N 65  
A1L70 C29  H291 sing N N 66  
A1L70 O24  H241 sing N N 67  
A1L70 O27  H271 sing N N 68  
A1L70 O32  H1   sing N N 69  
ALA   N    CA   sing N N 70  
ALA   N    H    sing N N 71  
ALA   N    H2   sing N N 72  
ALA   CA   C    sing N N 73  
ALA   CA   CB   sing N N 74  
ALA   CA   HA   sing N N 75  
ALA   C    O    doub N N 76  
ALA   C    OXT  sing N N 77  
ALA   CB   HB1  sing N N 78  
ALA   CB   HB2  sing N N 79  
ALA   CB   HB3  sing N N 80  
ALA   OXT  HXT  sing N N 81  
ARG   N    CA   sing N N 82  
ARG   N    H    sing N N 83  
ARG   N    H2   sing N N 84  
ARG   CA   C    sing N N 85  
ARG   CA   CB   sing N N 86  
ARG   CA   HA   sing N N 87  
ARG   C    O    doub N N 88  
ARG   C    OXT  sing N N 89  
ARG   CB   CG   sing N N 90  
ARG   CB   HB2  sing N N 91  
ARG   CB   HB3  sing N N 92  
ARG   CG   CD   sing N N 93  
ARG   CG   HG2  sing N N 94  
ARG   CG   HG3  sing N N 95  
ARG   CD   NE   sing N N 96  
ARG   CD   HD2  sing N N 97  
ARG   CD   HD3  sing N N 98  
ARG   NE   CZ   sing N N 99  
ARG   NE   HE   sing N N 100 
ARG   CZ   NH1  sing N N 101 
ARG   CZ   NH2  doub N N 102 
ARG   NH1  HH11 sing N N 103 
ARG   NH1  HH12 sing N N 104 
ARG   NH2  HH21 sing N N 105 
ARG   NH2  HH22 sing N N 106 
ARG   OXT  HXT  sing N N 107 
ASN   N    CA   sing N N 108 
ASN   N    H    sing N N 109 
ASN   N    H2   sing N N 110 
ASN   CA   C    sing N N 111 
ASN   CA   CB   sing N N 112 
ASN   CA   HA   sing N N 113 
ASN   C    O    doub N N 114 
ASN   C    OXT  sing N N 115 
ASN   CB   CG   sing N N 116 
ASN   CB   HB2  sing N N 117 
ASN   CB   HB3  sing N N 118 
ASN   CG   OD1  doub N N 119 
ASN   CG   ND2  sing N N 120 
ASN   ND2  HD21 sing N N 121 
ASN   ND2  HD22 sing N N 122 
ASN   OXT  HXT  sing N N 123 
ASP   N    CA   sing N N 124 
ASP   N    H    sing N N 125 
ASP   N    H2   sing N N 126 
ASP   CA   C    sing N N 127 
ASP   CA   CB   sing N N 128 
ASP   CA   HA   sing N N 129 
ASP   C    O    doub N N 130 
ASP   C    OXT  sing N N 131 
ASP   CB   CG   sing N N 132 
ASP   CB   HB2  sing N N 133 
ASP   CB   HB3  sing N N 134 
ASP   CG   OD1  doub N N 135 
ASP   CG   OD2  sing N N 136 
ASP   OD2  HD2  sing N N 137 
ASP   OXT  HXT  sing N N 138 
CYS   N    CA   sing N N 139 
CYS   N    H    sing N N 140 
CYS   N    H2   sing N N 141 
CYS   CA   C    sing N N 142 
CYS   CA   CB   sing N N 143 
CYS   CA   HA   sing N N 144 
CYS   C    O    doub N N 145 
CYS   C    OXT  sing N N 146 
CYS   CB   SG   sing N N 147 
CYS   CB   HB2  sing N N 148 
CYS   CB   HB3  sing N N 149 
CYS   SG   HG   sing N N 150 
CYS   OXT  HXT  sing N N 151 
GLN   N    CA   sing N N 152 
GLN   N    H    sing N N 153 
GLN   N    H2   sing N N 154 
GLN   CA   C    sing N N 155 
GLN   CA   CB   sing N N 156 
GLN   CA   HA   sing N N 157 
GLN   C    O    doub N N 158 
GLN   C    OXT  sing N N 159 
GLN   CB   CG   sing N N 160 
GLN   CB   HB2  sing N N 161 
GLN   CB   HB3  sing N N 162 
GLN   CG   CD   sing N N 163 
GLN   CG   HG2  sing N N 164 
GLN   CG   HG3  sing N N 165 
GLN   CD   OE1  doub N N 166 
GLN   CD   NE2  sing N N 167 
GLN   NE2  HE21 sing N N 168 
GLN   NE2  HE22 sing N N 169 
GLN   OXT  HXT  sing N N 170 
GLU   N    CA   sing N N 171 
GLU   N    H    sing N N 172 
GLU   N    H2   sing N N 173 
GLU   CA   C    sing N N 174 
GLU   CA   CB   sing N N 175 
GLU   CA   HA   sing N N 176 
GLU   C    O    doub N N 177 
GLU   C    OXT  sing N N 178 
GLU   CB   CG   sing N N 179 
GLU   CB   HB2  sing N N 180 
GLU   CB   HB3  sing N N 181 
GLU   CG   CD   sing N N 182 
GLU   CG   HG2  sing N N 183 
GLU   CG   HG3  sing N N 184 
GLU   CD   OE1  doub N N 185 
GLU   CD   OE2  sing N N 186 
GLU   OE2  HE2  sing N N 187 
GLU   OXT  HXT  sing N N 188 
GLY   N    CA   sing N N 189 
GLY   N    H    sing N N 190 
GLY   N    H2   sing N N 191 
GLY   CA   C    sing N N 192 
GLY   CA   HA2  sing N N 193 
GLY   CA   HA3  sing N N 194 
GLY   C    O    doub N N 195 
GLY   C    OXT  sing N N 196 
GLY   OXT  HXT  sing N N 197 
HIS   N    CA   sing N N 198 
HIS   N    H    sing N N 199 
HIS   N    H2   sing N N 200 
HIS   CA   C    sing N N 201 
HIS   CA   CB   sing N N 202 
HIS   CA   HA   sing N N 203 
HIS   C    O    doub N N 204 
HIS   C    OXT  sing N N 205 
HIS   CB   CG   sing N N 206 
HIS   CB   HB2  sing N N 207 
HIS   CB   HB3  sing N N 208 
HIS   CG   ND1  sing Y N 209 
HIS   CG   CD2  doub Y N 210 
HIS   ND1  CE1  doub Y N 211 
HIS   ND1  HD1  sing N N 212 
HIS   CD2  NE2  sing Y N 213 
HIS   CD2  HD2  sing N N 214 
HIS   CE1  NE2  sing Y N 215 
HIS   CE1  HE1  sing N N 216 
HIS   NE2  HE2  sing N N 217 
HIS   OXT  HXT  sing N N 218 
HOH   O    H1   sing N N 219 
HOH   O    H2   sing N N 220 
ILE   N    CA   sing N N 221 
ILE   N    H    sing N N 222 
ILE   N    H2   sing N N 223 
ILE   CA   C    sing N N 224 
ILE   CA   CB   sing N N 225 
ILE   CA   HA   sing N N 226 
ILE   C    O    doub N N 227 
ILE   C    OXT  sing N N 228 
ILE   CB   CG1  sing N N 229 
ILE   CB   CG2  sing N N 230 
ILE   CB   HB   sing N N 231 
ILE   CG1  CD1  sing N N 232 
ILE   CG1  HG12 sing N N 233 
ILE   CG1  HG13 sing N N 234 
ILE   CG2  HG21 sing N N 235 
ILE   CG2  HG22 sing N N 236 
ILE   CG2  HG23 sing N N 237 
ILE   CD1  HD11 sing N N 238 
ILE   CD1  HD12 sing N N 239 
ILE   CD1  HD13 sing N N 240 
ILE   OXT  HXT  sing N N 241 
LEU   N    CA   sing N N 242 
LEU   N    H    sing N N 243 
LEU   N    H2   sing N N 244 
LEU   CA   C    sing N N 245 
LEU   CA   CB   sing N N 246 
LEU   CA   HA   sing N N 247 
LEU   C    O    doub N N 248 
LEU   C    OXT  sing N N 249 
LEU   CB   CG   sing N N 250 
LEU   CB   HB2  sing N N 251 
LEU   CB   HB3  sing N N 252 
LEU   CG   CD1  sing N N 253 
LEU   CG   CD2  sing N N 254 
LEU   CG   HG   sing N N 255 
LEU   CD1  HD11 sing N N 256 
LEU   CD1  HD12 sing N N 257 
LEU   CD1  HD13 sing N N 258 
LEU   CD2  HD21 sing N N 259 
LEU   CD2  HD22 sing N N 260 
LEU   CD2  HD23 sing N N 261 
LEU   OXT  HXT  sing N N 262 
LYS   N    CA   sing N N 263 
LYS   N    H    sing N N 264 
LYS   N    H2   sing N N 265 
LYS   CA   C    sing N N 266 
LYS   CA   CB   sing N N 267 
LYS   CA   HA   sing N N 268 
LYS   C    O    doub N N 269 
LYS   C    OXT  sing N N 270 
LYS   CB   CG   sing N N 271 
LYS   CB   HB2  sing N N 272 
LYS   CB   HB3  sing N N 273 
LYS   CG   CD   sing N N 274 
LYS   CG   HG2  sing N N 275 
LYS   CG   HG3  sing N N 276 
LYS   CD   CE   sing N N 277 
LYS   CD   HD2  sing N N 278 
LYS   CD   HD3  sing N N 279 
LYS   CE   NZ   sing N N 280 
LYS   CE   HE2  sing N N 281 
LYS   CE   HE3  sing N N 282 
LYS   NZ   HZ1  sing N N 283 
LYS   NZ   HZ2  sing N N 284 
LYS   NZ   HZ3  sing N N 285 
LYS   OXT  HXT  sing N N 286 
MET   N    CA   sing N N 287 
MET   N    H    sing N N 288 
MET   N    H2   sing N N 289 
MET   CA   C    sing N N 290 
MET   CA   CB   sing N N 291 
MET   CA   HA   sing N N 292 
MET   C    O    doub N N 293 
MET   C    OXT  sing N N 294 
MET   CB   CG   sing N N 295 
MET   CB   HB2  sing N N 296 
MET   CB   HB3  sing N N 297 
MET   CG   SD   sing N N 298 
MET   CG   HG2  sing N N 299 
MET   CG   HG3  sing N N 300 
MET   SD   CE   sing N N 301 
MET   CE   HE1  sing N N 302 
MET   CE   HE2  sing N N 303 
MET   CE   HE3  sing N N 304 
MET   OXT  HXT  sing N N 305 
PHE   N    CA   sing N N 306 
PHE   N    H    sing N N 307 
PHE   N    H2   sing N N 308 
PHE   CA   C    sing N N 309 
PHE   CA   CB   sing N N 310 
PHE   CA   HA   sing N N 311 
PHE   C    O    doub N N 312 
PHE   C    OXT  sing N N 313 
PHE   CB   CG   sing N N 314 
PHE   CB   HB2  sing N N 315 
PHE   CB   HB3  sing N N 316 
PHE   CG   CD1  doub Y N 317 
PHE   CG   CD2  sing Y N 318 
PHE   CD1  CE1  sing Y N 319 
PHE   CD1  HD1  sing N N 320 
PHE   CD2  CE2  doub Y N 321 
PHE   CD2  HD2  sing N N 322 
PHE   CE1  CZ   doub Y N 323 
PHE   CE1  HE1  sing N N 324 
PHE   CE2  CZ   sing Y N 325 
PHE   CE2  HE2  sing N N 326 
PHE   CZ   HZ   sing N N 327 
PHE   OXT  HXT  sing N N 328 
PRO   N    CA   sing N N 329 
PRO   N    CD   sing N N 330 
PRO   N    H    sing N N 331 
PRO   CA   C    sing N N 332 
PRO   CA   CB   sing N N 333 
PRO   CA   HA   sing N N 334 
PRO   C    O    doub N N 335 
PRO   C    OXT  sing N N 336 
PRO   CB   CG   sing N N 337 
PRO   CB   HB2  sing N N 338 
PRO   CB   HB3  sing N N 339 
PRO   CG   CD   sing N N 340 
PRO   CG   HG2  sing N N 341 
PRO   CG   HG3  sing N N 342 
PRO   CD   HD2  sing N N 343 
PRO   CD   HD3  sing N N 344 
PRO   OXT  HXT  sing N N 345 
SER   N    CA   sing N N 346 
SER   N    H    sing N N 347 
SER   N    H2   sing N N 348 
SER   CA   C    sing N N 349 
SER   CA   CB   sing N N 350 
SER   CA   HA   sing N N 351 
SER   C    O    doub N N 352 
SER   C    OXT  sing N N 353 
SER   CB   OG   sing N N 354 
SER   CB   HB2  sing N N 355 
SER   CB   HB3  sing N N 356 
SER   OG   HG   sing N N 357 
SER   OXT  HXT  sing N N 358 
THR   N    CA   sing N N 359 
THR   N    H    sing N N 360 
THR   N    H2   sing N N 361 
THR   CA   C    sing N N 362 
THR   CA   CB   sing N N 363 
THR   CA   HA   sing N N 364 
THR   C    O    doub N N 365 
THR   C    OXT  sing N N 366 
THR   CB   OG1  sing N N 367 
THR   CB   CG2  sing N N 368 
THR   CB   HB   sing N N 369 
THR   OG1  HG1  sing N N 370 
THR   CG2  HG21 sing N N 371 
THR   CG2  HG22 sing N N 372 
THR   CG2  HG23 sing N N 373 
THR   OXT  HXT  sing N N 374 
TRP   N    CA   sing N N 375 
TRP   N    H    sing N N 376 
TRP   N    H2   sing N N 377 
TRP   CA   C    sing N N 378 
TRP   CA   CB   sing N N 379 
TRP   CA   HA   sing N N 380 
TRP   C    O    doub N N 381 
TRP   C    OXT  sing N N 382 
TRP   CB   CG   sing N N 383 
TRP   CB   HB2  sing N N 384 
TRP   CB   HB3  sing N N 385 
TRP   CG   CD1  doub Y N 386 
TRP   CG   CD2  sing Y N 387 
TRP   CD1  NE1  sing Y N 388 
TRP   CD1  HD1  sing N N 389 
TRP   CD2  CE2  doub Y N 390 
TRP   CD2  CE3  sing Y N 391 
TRP   NE1  CE2  sing Y N 392 
TRP   NE1  HE1  sing N N 393 
TRP   CE2  CZ2  sing Y N 394 
TRP   CE3  CZ3  doub Y N 395 
TRP   CE3  HE3  sing N N 396 
TRP   CZ2  CH2  doub Y N 397 
TRP   CZ2  HZ2  sing N N 398 
TRP   CZ3  CH2  sing Y N 399 
TRP   CZ3  HZ3  sing N N 400 
TRP   CH2  HH2  sing N N 401 
TRP   OXT  HXT  sing N N 402 
TYR   N    CA   sing N N 403 
TYR   N    H    sing N N 404 
TYR   N    H2   sing N N 405 
TYR   CA   C    sing N N 406 
TYR   CA   CB   sing N N 407 
TYR   CA   HA   sing N N 408 
TYR   C    O    doub N N 409 
TYR   C    OXT  sing N N 410 
TYR   CB   CG   sing N N 411 
TYR   CB   HB2  sing N N 412 
TYR   CB   HB3  sing N N 413 
TYR   CG   CD1  doub Y N 414 
TYR   CG   CD2  sing Y N 415 
TYR   CD1  CE1  sing Y N 416 
TYR   CD1  HD1  sing N N 417 
TYR   CD2  CE2  doub Y N 418 
TYR   CD2  HD2  sing N N 419 
TYR   CE1  CZ   doub Y N 420 
TYR   CE1  HE1  sing N N 421 
TYR   CE2  CZ   sing Y N 422 
TYR   CE2  HE2  sing N N 423 
TYR   CZ   OH   sing N N 424 
TYR   OH   HH   sing N N 425 
TYR   OXT  HXT  sing N N 426 
VAL   N    CA   sing N N 427 
VAL   N    H    sing N N 428 
VAL   N    H2   sing N N 429 
VAL   CA   C    sing N N 430 
VAL   CA   CB   sing N N 431 
VAL   CA   HA   sing N N 432 
VAL   C    O    doub N N 433 
VAL   C    OXT  sing N N 434 
VAL   CB   CG1  sing N N 435 
VAL   CB   CG2  sing N N 436 
VAL   CB   HB   sing N N 437 
VAL   CG1  HG11 sing N N 438 
VAL   CG1  HG12 sing N N 439 
VAL   CG1  HG13 sing N N 440 
VAL   CG2  HG21 sing N N 441 
VAL   CG2  HG22 sing N N 442 
VAL   CG2  HG23 sing N N 443 
VAL   OXT  HXT  sing N N 444 
# 
_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                    9M13 
_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]   0.008019 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.001441 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.022322 
_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]   0.021716 
_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  ? 46.59100  -0.12100  12.97100 1.000 52.22378 ?  123 LYS   A N    1 
ATOM   2    C  CA   . LYS   A 1 18  ? 46.23200  0.74700   11.85300 1.000 47.72632 ?  123 LYS   A CA   1 
ATOM   3    C  C    . LYS   A 1 18  ? 45.32600  0.01400   10.86700 1.000 36.05986 ?  123 LYS   A C    1 
ATOM   4    O  O    . LYS   A 1 18  ? 45.38500  -1.20800  10.73800 1.000 34.37808 ?  123 LYS   A O    1 
ATOM   5    C  CB   . LYS   A 1 18  ? 47.48900  1.26300   11.14700 1.000 50.45384 ?  123 LYS   A CB   1 
ATOM   6    C  CG   . LYS   A 1 18  ? 47.23300  2.29800   10.04800 1.000 55.51711 ?  123 LYS   A CG   1 
ATOM   7    C  CD   . LYS   A 1 18  ? 46.88200  3.66800   10.62000 1.000 57.19728 ?  123 LYS   A CD   1 
ATOM   8    C  CE   . LYS   A 1 18  ? 45.70600  4.31700   9.88900  1.000 53.24738 ?  123 LYS   A CE   1 
ATOM   9    N  NZ   . LYS   A 1 18  ? 44.41900  3.60100   10.07500 1.000 47.38648 ?  123 LYS   A NZ   1 
ATOM   10   N  N    . LEU   A 1 19  ? 44.47700  0.77300   10.18200 1.000 35.58650 ?  124 LEU   A N    1 
ATOM   11   C  CA   . LEU   A 1 19  ? 43.58100  0.19600   9.19200  1.000 30.16582 ?  124 LEU   A CA   1 
ATOM   12   C  C    . LEU   A 1 19  ? 44.36800  -0.31200  7.99200  1.000 29.23794 ?  124 LEU   A C    1 
ATOM   13   O  O    . LEU   A 1 19  ? 45.21500  0.39700   7.44100  1.000 33.62191 ?  124 LEU   A O    1 
ATOM   14   C  CB   . LEU   A 1 19  ? 42.55200  1.23100   8.74300  1.000 31.21374 ?  124 LEU   A CB   1 
ATOM   15   C  CG   . LEU   A 1 19  ? 41.48200  1.61600   9.76300  1.000 37.91913 ?  124 LEU   A CG   1 
ATOM   16   C  CD1  . LEU   A 1 19  ? 40.90800  2.99100   9.44800  1.000 40.51307 ?  124 LEU   A CD1  1 
ATOM   17   C  CD2  . LEU   A 1 19  ? 40.37900  0.57700   9.79200  1.000 30.23908 ?  124 LEU   A CD2  1 
ATOM   18   N  N    . SER   A 1 20  ? 44.08700  -1.54600  7.59000  1.000 27.61621 ?  125 SER   A N    1 
ATOM   19   C  CA   . SER   A 1 20  ? 44.62200  -2.06600  6.34700  1.000 28.77389 ?  125 SER   A CA   1 
ATOM   20   C  C    . SER   A 1 20  ? 43.94700  -1.37900  5.16500  1.000 27.98428 ?  125 SER   A C    1 
ATOM   21   O  O    . SER   A 1 20  ? 42.90300  -0.73300  5.30500  1.000 24.57076 ?  125 SER   A O    1 
ATOM   22   C  CB   . SER   A 1 20  ? 44.38900  -3.56800  6.26700  1.000 27.53877 ?  125 SER   A CB   1 
ATOM   23   O  OG   . SER   A 1 20  ? 42.99700  -3.82100  6.16800  1.000 25.77183 ?  125 SER   A OG   1 
ATOM   24   N  N    . GLU   A 1 21  ? 44.54900  -1.53000  3.98000  1.000 25.51877 ?  126 GLU   A N    1 
ATOM   25   C  CA   . GLU   A 1 21  ? 43.89800  -1.02700  2.77500  1.000 25.02108 ?  126 GLU   A CA   1 
ATOM   26   C  C    . GLU   A 1 21  ? 42.52800  -1.67200  2.60600  1.000 23.48392 ?  126 GLU   A C    1 
ATOM   27   O  O    . GLU   A 1 21  ? 41.55400  -1.00000  2.25100  1.000 27.49648 ?  126 GLU   A O    1 
ATOM   28   C  CB   . GLU   A 1 21  ? 44.77300  -1.27800  1.54000  1.000 36.30711 ?  126 GLU   A CB   1 
ATOM   29   C  CG   . GLU   A 1 21  ? 44.34700  -0.46500  0.30600  1.000 44.99026 ?  126 GLU   A CG   1 
ATOM   30   C  CD   . GLU   A 1 21  ? 44.75700  -1.09500  -1.02000 1.000 50.41064 ?  126 GLU   A CD   1 
ATOM   31   O  OE1  . GLU   A 1 21  ? 43.89500  -1.67800  -1.70800 1.000 48.62824 ?  126 GLU   A OE1  1 
ATOM   32   O  OE2  . GLU   A 1 21  ? 45.95200  -1.01300  -1.36200 1.000 51.21702 ?  126 GLU   A OE2  1 
ATOM   33   N  N    . GLU   A 1 22  ? 42.43400  -2.97500  2.89100  1.000 23.16524 ?  127 GLU   A N    1 
ATOM   34   C  CA   . GLU   A 1 22  ? 41.15700  -3.67900  2.81500  1.000 21.86316 ?  127 GLU   A CA   1 
ATOM   35   C  C    . GLU   A 1 22  ? 40.12000  -3.04500  3.73400  1.000 20.85859 ?  127 GLU   A C    1 
ATOM   36   O  O    . GLU   A 1 22  ? 38.97700  -2.81200  3.33300  1.000 19.92118 ?  127 GLU   A O    1 
ATOM   37   C  CB   . GLU   A 1 22  ? 41.36200  -5.15200  3.17500  1.000 34.85560 ?  127 GLU   A CB   1 
ATOM   38   C  CG   . GLU   A 1 22  ? 40.09200  -5.98000  3.20000  1.000 32.78858 ?  127 GLU   A CG   1 
ATOM   39   C  CD   . GLU   A 1 22  ? 40.37800  -7.46900  3.32600  1.000 43.49194 ?  127 GLU   A CD   1 
ATOM   40   O  OE1  . GLU   A 1 22  ? 39.62600  -8.16700  4.03900  1.000 42.58873 ?  127 GLU   A OE1  1 
ATOM   41   O  OE2  . GLU   A 1 22  ? 41.36500  -7.93700  2.71600  1.000 51.27664 ?  127 GLU   A OE2  1 
ATOM   42   N  N    . GLN   A 1 23  ? 40.50600  -2.75900  4.98100  1.000 21.20891 ?  128 GLN   A N    1 
ATOM   43   C  CA   . GLN   A 1 23  ? 39.55600  -2.16800  5.92200  1.000 20.43563 ?  128 GLN   A CA   1 
ATOM   44   C  C    . GLN   A 1 23  ? 39.14400  -0.76800  5.48300  1.000 20.27155 ?  128 GLN   A C    1 
ATOM   45   O  O    . GLN   A 1 23  ? 37.98100  -0.38200  5.63200  1.000 21.60023 ?  128 GLN   A O    1 
ATOM   46   C  CB   . GLN   A 1 23  ? 40.16300  -2.14500  7.32700  1.000 22.40906 ?  128 GLN   A CB   1 
ATOM   47   C  CG   . GLN   A 1 23  ? 40.21900  -3.53300  7.96200  1.000 24.96476 ?  128 GLN   A CG   1 
ATOM   48   C  CD   . GLN   A 1 23  ? 40.99800  -3.56100  9.26100  1.000 27.24133 ?  128 GLN   A CD   1 
ATOM   49   O  OE1  . GLN   A 1 23  ? 41.94000  -2.78900  9.45700  1.000 30.18668 ?  128 GLN   A OE1  1 
ATOM   50   N  NE2  . GLN   A 1 23  ? 40.60700  -4.45600  10.15900 1.000 33.85231 ?  128 GLN   A NE2  1 
ATOM   51   N  N    . GLN   A 1 24  ? 40.08400  0.00100   4.93000  1.000 21.29727 ?  129 GLN   A N    1 
ATOM   52   C  CA   . GLN   A 1 24  ? 39.73500  1.32100   4.41700  1.000 21.35325 ?  129 GLN   A CA   1 
ATOM   53   C  C    . GLN   A 1 24  ? 38.76200  1.21500   3.24800  1.000 20.52030 ?  129 GLN   A C    1 
ATOM   54   O  O    . GLN   A 1 24  ? 37.85100  2.04200   3.11300  1.000 20.00843 ?  129 GLN   A O    1 
ATOM   55   C  CB   . GLN   A 1 24  ? 41.00700  2.07200   4.01500  1.000 22.84530 ?  129 GLN   A CB   1 
ATOM   56   C  CG   . GLN   A 1 24  ? 41.92600  2.34400   5.19200  1.000 26.45621 ?  129 GLN   A CG   1 
ATOM   57   C  CD   . GLN   A 1 24  ? 43.24600  2.95700   4.77000  1.000 38.02208 ?  129 GLN   A CD   1 
ATOM   58   O  OE1  . GLN   A 1 24  ? 43.27300  3.95400   4.05100  1.000 38.63797 ?  129 GLN   A OE1  1 
ATOM   59   N  NE2  . GLN   A 1 24  ? 44.34800  2.35900   5.21200  1.000 40.76758 ?  129 GLN   A NE2  1 
ATOM   60   N  N    . HIS   A 1 25  ? 38.93200  0.19700   2.39800  1.000 20.49738 ?  130 HIS   A N    1 
ATOM   61   C  CA   . HIS   A 1 25  ? 37.99200  -0.02000  1.30000  1.000 21.10855 ?  130 HIS   A CA   1 
ATOM   62   C  C    . HIS   A 1 25  ? 36.59600  -0.33500  1.82600  1.000 18.50103 ?  130 HIS   A C    1 
ATOM   63   O  O    . HIS   A 1 25  ? 35.59900  0.15600   1.28900  1.000 18.12474 ?  130 HIS   A O    1 
ATOM   64   C  CB   . HIS   A 1 25  ? 38.47600  -1.15700  0.39000  1.000 23.24223 ?  130 HIS   A CB   1 
ATOM   65   C  CG   . HIS   A 1 25  ? 39.67100  -0.82200  -0.45200 1.000 26.88954 ?  130 HIS   A CG   1 
ATOM   66   N  ND1  . HIS   A 1 25  ? 39.67800  0.20900   -1.36900 1.000 25.34661 ?  130 HIS   A ND1  1 
ATOM   67   C  CD2  . HIS   A 1 25  ? 40.88700  -1.41300  -0.54500 1.000 28.55507 ?  130 HIS   A CD2  1 
ATOM   68   C  CE1  . HIS   A 1 25  ? 40.85000  0.24900   -1.97700 1.000 25.26538 ?  130 HIS   A CE1  1 
ATOM   69   N  NE2  . HIS   A 1 25  ? 41.60500  -0.72200  -1.49100 1.000 31.26854 ?  130 HIS   A NE2  1 
ATOM   70   N  N    . ILE   A 1 26  ? 36.50200  -1.17700  2.86000  1.000 18.09562 ?  131 ILE   A N    1 
ATOM   71   C  CA   . ILE   A 1 26  ? 35.20400  -1.49100  3.45500  1.000 16.98558 ?  131 ILE   A CA   1 
ATOM   72   C  C    . ILE   A 1 26  ? 34.50900  -0.21500  3.90900  1.000 17.52518 ?  131 ILE   A C    1 
ATOM   73   O  O    . ILE   A 1 26  ? 33.33900  0.02500   3.59000  1.000 15.91828 ?  131 ILE   A O    1 
ATOM   74   C  CB   . ILE   A 1 26  ? 35.37600  -2.48200  4.62000  1.000 17.95709 ?  131 ILE   A CB   1 
ATOM   75   C  CG1  . ILE   A 1 26  ? 35.74100  -3.86400  4.08600  1.000 18.02537 ?  131 ILE   A CG1  1 
ATOM   76   C  CG2  . ILE   A 1 26  ? 34.10300  -2.54100  5.48200  1.000 16.01049 ?  131 ILE   A CG2  1 
ATOM   77   C  CD1  . ILE   A 1 26  ? 36.24200  -4.80800  5.14800  1.000 23.16788 ?  131 ILE   A CD1  1 
ATOM   78   N  N    . ILE   A 1 27  ? 35.23100  0.63600   4.64100  1.000 18.20311 ?  132 ILE   A N    1 
ATOM   79   C  CA   . ILE   A 1 27  ? 34.64800  1.88500   5.12300  1.000 18.32896 ?  132 ILE   A CA   1 
ATOM   80   C  C    . ILE   A 1 27  ? 34.21100  2.76700   3.95400  1.000 18.59715 ?  132 ILE   A C    1 
ATOM   81   O  O    . ILE   A 1 27  ? 33.11600  3.34300   3.96900  1.000 19.51668 ?  132 ILE   A O    1 
ATOM   82   C  CB   . ILE   A 1 27  ? 35.64600  2.60700   6.04900  1.000 20.32379 ?  132 ILE   A CB   1 
ATOM   83   C  CG1  . ILE   A 1 27  ? 35.83700  1.79900   7.34000  1.000 19.27064 ?  132 ILE   A CG1  1 
ATOM   84   C  CG2  . ILE   A 1 27  ? 35.17100  4.01500   6.34900  1.000 18.47923 ?  132 ILE   A CG2  1 
ATOM   85   C  CD1  . ILE   A 1 27  ? 36.94800  2.29900   8.24000  1.000 23.17483 ?  132 ILE   A CD1  1 
ATOM   86   N  N    . ALA   A 1 28  ? 35.04800  2.87800   2.91900  1.000 18.28116 ?  133 ALA   A N    1 
ATOM   87   C  CA   . ALA   A 1 28  ? 34.69700  3.72600   1.78300  1.000 18.33650 ?  133 ALA   A CA   1 
ATOM   88   C  C    . ALA   A 1 28  ? 33.43300  3.22800   1.09800  1.000 17.93720 ?  133 ALA   A C    1 
ATOM   89   O  O    . ALA   A 1 28  ? 32.57000  4.02500   0.70200  1.000 18.40746 ?  133 ALA   A O    1 
ATOM   90   C  CB   . ALA   A 1 28  ? 35.85800  3.78300   0.78800  1.000 19.49564 ?  133 ALA   A CB   1 
ATOM   91   N  N    . ILE   A 1 29  ? 33.30100  1.90800   0.96100  1.000 16.85742 ?  134 ILE   A N    1 
ATOM   92   C  CA   . ILE   A 1 29  ? 32.11100  1.33300   0.34900  1.000 16.06933 ?  134 ILE   A CA   1 
ATOM   93   C  C    . ILE   A 1 29  ? 30.87200  1.64600   1.17600  1.000 15.17387 ?  134 ILE   A C    1 
ATOM   94   O  O    . ILE   A 1 29  ? 29.80800  1.96500   0.62700  1.000 16.70776 ?  134 ILE   A O    1 
ATOM   95   C  CB   . ILE   A 1 29  ? 32.29700  -0.18400  0.16000  1.000 17.31519 ?  134 ILE   A CB   1 
ATOM   96   C  CG1  . ILE   A 1 29  ? 33.27000  -0.44200  -0.99700 1.000 20.80776 ?  134 ILE   A CG1  1 
ATOM   97   C  CG2  . ILE   A 1 29  ? 30.95400  -0.85100  -0.09400 1.000 16.63479 ?  134 ILE   A CG2  1 
ATOM   98   C  CD1  . ILE   A 1 29  ? 33.71000  -1.89200  -1.13200 1.000 23.75554 ?  134 ILE   A CD1  1 
ATOM   99   N  N    . LEU   A 1 30  ? 30.98400  1.55400   2.50600  1.000 15.48388 ?  135 LEU   A N    1 
ATOM   100  C  CA   . LEU   A 1 30  ? 29.81900  1.76500   3.36100  1.000 14.35080 ?  135 LEU   A CA   1 
ATOM   101  C  C    . LEU   A 1 30  ? 29.42900  3.23700   3.42400  1.000 15.67094 ?  135 LEU   A C    1 
ATOM   102  O  O    . LEU   A 1 30  ? 28.23600  3.56200   3.47000  1.000 17.22199 ?  135 LEU   A O    1 
ATOM   103  C  CB   . LEU   A 1 30  ? 30.08500  1.21600   4.76500  1.000 15.91881 ?  135 LEU   A CB   1 
ATOM   104  C  CG   . LEU   A 1 30  ? 30.21600  -0.31000  4.86000  1.000 14.61544 ?  135 LEU   A CG   1 
ATOM   105  C  CD1  . LEU   A 1 30  ? 30.52200  -0.72600  6.28900  1.000 15.98254 ?  135 LEU   A CD1  1 
ATOM   106  C  CD2  . LEU   A 1 30  ? 28.94600  -0.99500  4.35900  1.000 14.74796 ?  135 LEU   A CD2  1 
ATOM   107  N  N    . LEU   A 1 31  ? 30.41600  4.13900   3.43800  1.000 16.69256 ?  136 LEU   A N    1 
ATOM   108  C  CA   . LEU   A 1 31  ? 30.11300  5.56600   3.36800  1.000 16.16962 ?  136 LEU   A CA   1 
ATOM   109  C  C    . LEU   A 1 31  ? 29.40200  5.90500   2.06400  1.000 19.28969 ?  136 LEU   A C    1 
ATOM   110  O  O    . LEU   A 1 31  ? 28.39500  6.62300   2.05900  1.000 18.38886 ?  136 LEU   A O    1 
ATOM   111  C  CB   . LEU   A 1 31  ? 31.39700  6.38400   3.51500  1.000 17.81156 ?  136 LEU   A CB   1 
ATOM   112  C  CG   . LEU   A 1 31  ? 32.02400  6.31300   4.90800  1.000 17.28492 ?  136 LEU   A CG   1 
ATOM   113  C  CD1  . LEU   A 1 31  ? 33.36600  7.02200   4.94800  1.000 18.61149 ?  136 LEU   A CD1  1 
ATOM   114  C  CD2  . LEU   A 1 31  ? 31.07700  6.89600   5.96000  1.000 22.12600 ?  136 LEU   A CD2  1 
ATOM   115  N  N    . ASP   A 1 32  ? 29.91200  5.39100   0.94200  1.000 16.53600 ?  137 ASP   A N    1 
ATOM   116  C  CA   . ASP   A 1 32  ? 29.23200  5.59800   -0.33600 1.000 17.46006 ?  137 ASP   A CA   1 
ATOM   117  C  C    . ASP   A 1 32  ? 27.82200  5.02700   -0.30100 1.000 19.46356 ?  137 ASP   A C    1 
ATOM   118  O  O    . ASP   A 1 32  ? 26.87500  5.66300   -0.77700 1.000 18.94016 ?  137 ASP   A O    1 
ATOM   119  C  CB   . ASP   A 1 32  ? 30.04100  4.96300   -1.47100 1.000 20.09737 ?  137 ASP   A CB   1 
ATOM   120  C  CG   . ASP   A 1 32  ? 29.28800  4.94800   -2.79400 1.000 22.58372 ?  137 ASP   A CG   1 
ATOM   121  O  OD1  . ASP   A 1 32  ? 28.59800  3.94600   -3.08200 1.000 22.24687 ?  137 ASP   A OD1  1 
ATOM   122  O  OD2  . ASP   A 1 32  ? 29.38700  5.93900   -3.54500 1.000 22.86212 ?  137 ASP   A OD2  1 
ATOM   123  N  N    . ALA   A 1 33  ? 27.66200  3.83700   0.28300  1.000 15.85872 ?  138 ALA   A N    1 
ATOM   124  C  CA   . ALA   A 1 33  ? 26.35100  3.19700   0.32400  1.000 16.24845 ?  138 ALA   A CA   1 
ATOM   125  C  C    . ALA   A 1 33  ? 25.35400  4.02500   1.12300  1.000 15.81964 ?  138 ALA   A C    1 
ATOM   126  O  O    . ALA   A 1 33  ? 24.19900  4.19600   0.71000  1.000 17.15463 ?  138 ALA   A O    1 
ATOM   127  C  CB   . ALA   A 1 33  ? 26.47500  1.80100   0.92600  1.000 13.28759 ?  138 ALA   A CB   1 
ATOM   128  N  N    . HIS   A 1 34  ? 25.78100  4.53100   2.27900  1.000 14.72067 ?  139 HIS   A N    1 
ATOM   129  C  CA   . HIS   A 1 34  ? 24.90000  5.36600   3.08700  1.000 16.03062 ?  139 HIS   A CA   1 
ATOM   130  C  C    . HIS   A 1 34  ? 24.53900  6.65300   2.35900  1.000 16.24914 ?  139 HIS   A C    1 
ATOM   131  O  O    . HIS   A 1 34  ? 23.37400  7.06500   2.34100  1.000 17.12212 ?  139 HIS   A O    1 
ATOM   132  C  CB   . HIS   A 1 34  ? 25.57200  5.68000   4.42000  1.000 19.82972 ?  139 HIS   A CB   1 
ATOM   133  C  CG   . HIS   A 1 34  ? 24.72600  6.50300   5.33600  1.000 15.39393 ?  139 HIS   A CG   1 
ATOM   134  N  ND1  . HIS   A 1 34  ? 23.45800  6.12000   5.71400  1.000 17.44628 ?  139 HIS   A ND1  1 
ATOM   135  C  CD2  . HIS   A 1 34  ? 24.96600  7.68600   5.95400  1.000 17.97191 ?  139 HIS   A CD2  1 
ATOM   136  C  CE1  . HIS   A 1 34  ? 22.95000  7.03400   6.52500  1.000 16.13011 ?  139 HIS   A CE1  1 
ATOM   137  N  NE2  . HIS   A 1 34  ? 23.84500  7.99300   6.68600  1.000 17.62137 ?  139 HIS   A NE2  1 
ATOM   138  N  N    . HIS   A 1 35  ? 25.52300  7.30000   1.74200  1.000 16.38131 ?  140 HIS   A N    1 
ATOM   139  C  CA   . HIS   A 1 35  ? 25.23900  8.56600   1.08300  1.000 19.37486 ?  140 HIS   A CA   1 
ATOM   140  C  C    . HIS   A 1 35  ? 24.33600  8.40000   -0.12900 1.000 23.09162 ?  140 HIS   A C    1 
ATOM   141  O  O    . HIS   A 1 35  ? 23.63300  9.35000   -0.49200 1.000 22.91603 ?  140 HIS   A O    1 
ATOM   142  C  CB   . HIS   A 1 35  ? 26.55100  9.24500   0.70400  1.000 22.45437 ?  140 HIS   A CB   1 
ATOM   143  C  CG   . HIS   A 1 35  ? 27.36800  9.63600   1.89200  1.000 21.69739 ?  140 HIS   A CG   1 
ATOM   144  N  ND1  . HIS   A 1 35  ? 28.73300  9.81900   1.83600  1.000 22.31065 ?  140 HIS   A ND1  1 
ATOM   145  C  CD2  . HIS   A 1 35  ? 27.00700  9.86500   3.17600  1.000 20.75079 ?  140 HIS   A CD2  1 
ATOM   146  C  CE1  . HIS   A 1 35  ? 29.17600  10.15200  3.03500  1.000 23.57179 ?  140 HIS   A CE1  1 
ATOM   147  N  NE2  . HIS   A 1 35  ? 28.15000  10.18100  3.86800  1.000 20.96632 ?  140 HIS   A NE2  1 
ATOM   148  N  N    . LYS   A 1 36  ? 24.32400  7.22100   -0.75700 1.000 20.85836 ?  141 LYS   A N    1 
ATOM   149  C  CA   . LYS   A 1 36  ? 23.37300  6.98800   -1.84300 1.000 23.98932 ?  141 LYS   A CA   1 
ATOM   150  C  C    . LYS   A 1 36  ? 21.97300  6.66800   -1.35100 1.000 19.64420 ?  141 LYS   A C    1 
ATOM   151  O  O    . LYS   A 1 36  ? 21.02900  6.71700   -2.14800 1.000 22.25346 ?  141 LYS   A O    1 
ATOM   152  C  CB   . LYS   A 1 36  ? 23.81500  5.83200   -2.74200 1.000 29.96428 ?  141 LYS   A CB   1 
ATOM   153  C  CG   . LYS   A 1 36  ? 25.24000  5.87300   -3.20500 1.000 40.96983 ?  141 LYS   A CG   1 
ATOM   154  C  CD   . LYS   A 1 36  ? 25.40000  5.04000   -4.45300 1.000 45.84107 ?  141 LYS   A CD   1 
ATOM   155  C  CE   . LYS   A 1 36  ? 24.51100  3.80400   -4.39900 1.000 52.06162 ?  141 LYS   A CE   1 
ATOM   156  N  NZ   . LYS   A 1 36  ? 24.99400  2.68600   -5.24100 1.000 57.74484 ?  141 LYS   A NZ   1 
ATOM   157  N  N    . THR   A 1 37  ? 21.81600  6.31300   -0.07800 1.000 16.17103 ?  142 THR   A N    1 
ATOM   158  C  CA   . THR   A 1 37  ? 20.52700  5.87200   0.43500  1.000 15.53685 ?  142 THR   A CA   1 
ATOM   159  C  C    . THR   A 1 37  ? 19.98300  6.74900   1.54900  1.000 14.64357 ?  142 THR   A C    1 
ATOM   160  O  O    . THR   A 1 37  ? 18.91800  6.44300   2.09500  1.000 17.96787 ?  142 THR   A O    1 
ATOM   161  C  CB   . THR   A 1 37  ? 20.62200  4.42200   0.92900  1.000 15.22759 ?  142 THR   A CB   1 
ATOM   162  O  OG1  . THR   A 1 37  ? 21.70600  4.30000   1.85900  1.000 15.36668 ?  142 THR   A OG1  1 
ATOM   163  C  CG2  . THR   A 1 37  ? 20.87300  3.48900   -0.25000 1.000 17.12947 ?  142 THR   A CG2  1 
ATOM   164  N  N    . TYR   A 1 38  ? 20.68300  7.81900   1.91900  1.000 15.31553 ?  143 TYR   A N    1 
ATOM   165  C  CA   . TYR   A 1 38  ? 20.20300  8.74900   2.93000  1.000 17.40870 ?  143 TYR   A CA   1 
ATOM   166  C  C    . TYR   A 1 38  ? 20.20600  10.13400  2.31400  1.000 18.01012 ?  143 TYR   A C    1 
ATOM   167  O  O    . TYR   A 1 38  ? 21.25400  10.61700  1.87500  1.000 18.83513 ?  143 TYR   A O    1 
ATOM   168  C  CB   . TYR   A 1 38  ? 21.06000  8.73000   4.20100  1.000 15.43246 ?  143 TYR   A CB   1 
ATOM   169  C  CG   . TYR   A 1 38  ? 20.39900  9.46400   5.35300  1.000 17.61038 ?  143 TYR   A CG   1 
ATOM   170  C  CD1  . TYR   A 1 38  ? 20.49100  10.84800  5.46600  1.000 20.95123 ?  143 TYR   A CD1  1 
ATOM   171  C  CD2  . TYR   A 1 38  ? 19.66100  8.77500   6.30900  1.000 17.76060 ?  143 TYR   A CD2  1 
ATOM   172  C  CE1  . TYR   A 1 38  ? 19.87700  11.52200  6.50600  1.000 22.93699 ?  143 TYR   A CE1  1 
ATOM   173  C  CE2  . TYR   A 1 38  ? 19.04500  9.44200   7.36000  1.000 19.46204 ?  143 TYR   A CE2  1 
ATOM   174  C  CZ   . TYR   A 1 38  ? 19.15400  10.81500  7.44800  1.000 20.53273 ?  143 TYR   A CZ   1 
ATOM   175  O  OH   . TYR   A 1 38  ? 18.54500  11.49000  8.48600  1.000 20.55884 ?  143 TYR   A OH   1 
ATOM   176  N  N    . ASP   A 1 39  ? 19.03700  10.76700  2.29000  1.000 14.73402 ?  144 ASP   A N    1 
ATOM   177  C  CA   . ASP   A 1 39  ? 18.86800  12.08800  1.70300  1.000 17.65629 ?  144 ASP   A CA   1 
ATOM   178  C  C    . ASP   A 1 39  ? 18.65400  13.10300  2.81200  1.000 19.30785 ?  144 ASP   A C    1 
ATOM   179  O  O    . ASP   A 1 39  ? 17.52700  13.24800  3.31300  1.000 18.95667 ?  144 ASP   A O    1 
ATOM   180  C  CB   . ASP   A 1 39  ? 17.68300  12.08600  0.73400  1.000 19.23798 ?  144 ASP   A CB   1 
ATOM   181  C  CG   . ASP   A 1 39  ? 17.40900  13.45300  0.14100  1.000 24.01529 ?  144 ASP   A CG   1 
ATOM   182  O  OD1  . ASP   A 1 39  ? 18.26600  14.35600  0.26000  1.000 22.94910 ?  144 ASP   A OD1  1 
ATOM   183  O  OD2  . ASP   A 1 39  ? 16.31900  13.62100  -0.43900 1.000 24.52747 ?  144 ASP   A OD2  1 
ATOM   184  N  N    . PRO   A 1 40  ? 19.69400  13.83100  3.22900  1.000 18.62643 ?  145 PRO   A N    1 
ATOM   185  C  CA   . PRO   A 1 40  ? 19.53700  14.79800  4.32200  1.000 18.42835 ?  145 PRO   A CA   1 
ATOM   186  C  C    . PRO   A 1 40  ? 18.78100  16.05600  3.93100  1.000 23.07103 ?  145 PRO   A C    1 
ATOM   187  O  O    . PRO   A 1 40  ? 18.64500  16.95300  4.76800  1.000 25.43057 ?  145 PRO   A O    1 
ATOM   188  C  CB   . PRO   A 1 40  ? 20.98900  15.13100  4.70300  1.000 23.01231 ?  145 PRO   A CB   1 
ATOM   189  C  CG   . PRO   A 1 40  ? 21.75900  14.91100  3.45100  1.000 25.21076 ?  145 PRO   A CG   1 
ATOM   190  C  CD   . PRO   A 1 40  ? 21.06500  13.80700  2.68600  1.000 18.34248 ?  145 PRO   A CD   1 
ATOM   191  N  N    . THR   A 1 41  ? 18.30800  16.17000  2.68900  1.000 21.90389 ?  146 THR   A N    1 
ATOM   192  C  CA   . THR   A 1 41  ? 17.38900  17.23900  2.32900  1.000 22.33803 ?  146 THR   A CA   1 
ATOM   193  C  C    . THR   A 1 41  ? 15.93700  16.82600  2.51400  1.000 21.58279 ?  146 THR   A C    1 
ATOM   194  O  O    . THR   A 1 41  ? 15.05700  17.69500  2.50800  1.000 21.85084 ?  146 THR   A O    1 
ATOM   195  C  CB   . THR   A 1 41  ? 17.62200  17.69700  0.87900  1.000 24.10917 ?  146 THR   A CB   1 
ATOM   196  O  OG1  . THR   A 1 41  ? 17.07100  16.74200  -0.02900 1.000 21.67808 ?  146 THR   A OG1  1 
ATOM   197  C  CG2  . THR   A 1 41  ? 19.11800  17.82100  0.59300  1.000 27.35295 ?  146 THR   A CG2  1 
ATOM   198  N  N    . TYR   A 1 42  ? 15.67000  15.52600  2.68000  1.000 21.61963 ?  147 TYR   A N    1 
ATOM   199  C  CA   . TYR   A 1 42  ? 14.31900  15.01300  2.92300  1.000 22.08574 ?  147 TYR   A CA   1 
ATOM   200  C  C    . TYR   A 1 42  ? 13.34100  15.45400  1.83900  1.000 26.51405 ?  147 TYR   A C    1 
ATOM   201  O  O    . TYR   A 1 42  ? 12.15100  15.64700  2.09900  1.000 22.69339 ?  147 TYR   A O    1 
ATOM   202  C  CB   . TYR   A 1 42  ? 13.82500  15.43100  4.31000  1.000 22.47695 ?  147 TYR   A CB   1 
ATOM   203  C  CG   . TYR   A 1 42  ? 14.83900  15.08400  5.37800  1.000 21.19948 ?  147 TYR   A CG   1 
ATOM   204  C  CD1  . TYR   A 1 42  ? 15.60700  16.07200  5.98500  1.000 24.00098 ?  147 TYR   A CD1  1 
ATOM   205  C  CD2  . TYR   A 1 42  ? 15.05500  13.76500  5.74600  1.000 23.19867 ?  147 TYR   A CD2  1 
ATOM   206  C  CE1  . TYR   A 1 42  ? 16.53900  15.75400  6.94600  1.000 24.01255 ?  147 TYR   A CE1  1 
ATOM   207  C  CE2  . TYR   A 1 42  ? 15.99500  13.43600  6.70200  1.000 26.69631 ?  147 TYR   A CE2  1 
ATOM   208  C  CZ   . TYR   A 1 42  ? 16.73100  14.43000  7.29700  1.000 25.13165 ?  147 TYR   A CZ   1 
ATOM   209  O  OH   . TYR   A 1 42  ? 17.66900  14.09800  8.25300  1.000 25.82839 ?  147 TYR   A OH   1 
ATOM   210  N  N    . ALA   A 1 43  ? 13.83500  15.58200  0.60600  1.000 19.49407 ?  148 ALA   A N    1 
ATOM   211  C  CA   . ALA   A 1 43  ? 13.02700  16.14100  -0.47300 1.000 24.84675 ?  148 ALA   A CA   1 
ATOM   212  C  C    . ALA   A 1 43  ? 11.87800  15.23100  -0.89600 1.000 23.82769 ?  148 ALA   A C    1 
ATOM   213  O  O    . ALA   A 1 43  ? 10.91300  15.71800  -1.49400 1.000 30.30897 ?  148 ALA   A O    1 
ATOM   214  C  CB   . ALA   A 1 43  ? 13.91200  16.44100  -1.68400 1.000 33.91084 ?  148 ALA   A CB   1 
ATOM   215  N  N    . ASP   A 1 44  ? 11.95300  13.93000  -0.61700 1.000 21.70631 ?  149 ASP   A N    1 
ATOM   216  C  CA   . ASP   A 1 44  ? 10.91100  13.01100  -1.06400 1.000 23.67204 ?  149 ASP   A CA   1 
ATOM   217  C  C    . ASP   A 1 44  ? 9.71000   12.96600  -0.13000 1.000 25.30967 ?  149 ASP   A C    1 
ATOM   218  O  O    . ASP   A 1 44  ? 8.70800   12.33100  -0.47600 1.000 25.78105 ?  149 ASP   A O    1 
ATOM   219  C  CB   . ASP   A 1 44  ? 11.47000  11.59300  -1.21600 1.000 20.29896 ?  149 ASP   A CB   1 
ATOM   220  C  CG   . ASP   A 1 44  ? 12.55200  11.50400  -2.26900 1.000 28.58882 ?  149 ASP   A CG   1 
ATOM   221  O  OD1  . ASP   A 1 44  ? 12.44800  12.21500  -3.29000 1.000 31.22136 ?  149 ASP   A OD1  1 
ATOM   222  O  OD2  . ASP   A 1 44  ? 13.50400  10.72200  -2.07800 1.000 31.03601 ?  149 ASP   A OD2  1 
ATOM   223  N  N    . PHE   A 1 45  ? 9.77500   13.62700  1.02700  1.000 21.68625 ?  150 PHE   A N    1 
ATOM   224  C  CA   . PHE   A 1 45  ? 8.71500   13.48600  2.02200  1.000 21.51556 ?  150 PHE   A CA   1 
ATOM   225  C  C    . PHE   A 1 45  ? 7.39500   14.07200  1.52900  1.000 21.73823 ?  150 PHE   A C    1 
ATOM   226  O  O    . PHE   A 1 45  ? 6.32600   13.65800  1.99200  1.000 23.10136 ?  150 PHE   A O    1 
ATOM   227  C  CB   . PHE   A 1 45  ? 9.13800   14.14400  3.33700  1.000 18.59845 ?  150 PHE   A CB   1 
ATOM   228  C  CG   . PHE   A 1 45  ? 10.05600  13.29900  4.18400  1.000 17.35639 ?  150 PHE   A CG   1 
ATOM   229  C  CD1  . PHE   A 1 45  ? 11.15300  12.65300  3.63000  1.000 18.54620 ?  150 PHE   A CD1  1 
ATOM   230  C  CD2  . PHE   A 1 45  ? 9.82300   13.15900  5.54200  1.000 21.00363 ?  150 PHE   A CD2  1 
ATOM   231  C  CE1  . PHE   A 1 45  ? 12.00800  11.88600  4.42200  1.000 20.67693 ?  150 PHE   A CE1  1 
ATOM   232  C  CE2  . PHE   A 1 45  ? 10.66500  12.39000  6.33700  1.000 20.36535 ?  150 PHE   A CE2  1 
ATOM   233  C  CZ   . PHE   A 1 45  ? 11.76200  11.75500  5.77400  1.000 19.97006 ?  150 PHE   A CZ   1 
ATOM   234  N  N    . ARG   A 1 46  ? 7.45100   15.03000  0.59900  1.000 22.93544 ?  151 ARG   A N    1 
ATOM   235  C  CA   . ARG   A 1 46  ? 6.24800   15.55800  -0.03700 1.000 25.34663 ?  151 ARG   A CA   1 
ATOM   236  C  C    . ARG   A 1 46  ? 5.44400   14.48000  -0.75700 1.000 26.37464 ?  151 ARG   A C    1 
ATOM   237  O  O    . ARG   A 1 46  ? 4.24100   14.66200  -0.97300 1.000 30.16365 ?  151 ARG   A O    1 
ATOM   238  C  CB   . ARG   A 1 46  ? 6.63600   16.64700  -1.04200 1.000 34.26198 ?  151 ARG   A CB   1 
ATOM   239  C  CG   . ARG   A 1 46  ? 7.61100   16.11600  -2.08600 1.000 43.72153 ?  151 ARG   A CG   1 
ATOM   240  C  CD   . ARG   A 1 46  ? 7.81200   17.03400  -3.28300 1.000 58.36845 ?  151 ARG   A CD   1 
ATOM   241  N  NE   . ARG   A 1 46  ? 8.09100   16.26700  -4.50000 1.000 67.20271 ?  151 ARG   A NE   1 
ATOM   242  C  CZ   . ARG   A 1 46  ? 9.17400   15.51400  -4.70000 1.000 70.45868 ?  151 ARG   A CZ   1 
ATOM   243  N  NH1  . ARG   A 1 46  ? 10.11600  15.41600  -3.77000 1.000 68.30007 ?  151 ARG   A NH1  1 
ATOM   244  N  NH2  . ARG   A 1 46  ? 9.31800   14.85700  -5.84300 1.000 73.18115 ?  151 ARG   A NH2  1 
ATOM   245  N  N    . ASP   A 1 47  ? 6.07700   13.38100  -1.11700 1.000 24.93703 ?  152 ASP   A N    1 
ATOM   246  C  CA   . ASP   A 1 47  ? 5.38300   12.32100  -1.88400 1.000 24.91840 ?  152 ASP   A CA   1 
ATOM   247  C  C    . ASP   A 1 47  ? 4.53300   11.42600  -0.97200 1.000 24.04157 ?  152 ASP   A C    1 
ATOM   248  O  O    . ASP   A 1 47  ? 3.73200   10.70500  -1.47700 1.000 23.79931 ?  152 ASP   A O    1 
ATOM   249  C  CB   . ASP   A 1 47  ? 6.40100   11.46400  -2.62900 1.000 27.82683 ?  152 ASP   A CB   1 
ATOM   250  C  CG   . ASP   A 1 47  ? 7.28500   12.19100  -3.63500 1.000 36.73162 ?  152 ASP   A CG   1 
ATOM   251  O  OD1  . ASP   A 1 47  ? 6.94300   13.29200  -4.02600 1.000 37.29332 ?  152 ASP   A OD1  1 
ATOM   252  O  OD2  . ASP   A 1 47  ? 8.30300   11.62100  -4.00300 1.000 41.55427 ?  152 ASP   A OD2  1 
ATOM   253  N  N    . PHE   A 1 48  ? 4.79400   11.45100  0.31900  1.000 18.86825 ?  153 PHE   A N    1 
ATOM   254  C  CA   . PHE   A 1 48  ? 4.07800   10.60600  1.25800  1.000 16.18958 ?  153 PHE   A CA   1 
ATOM   255  C  C    . PHE   A 1 48  ? 2.65000   11.11300  1.43100  1.000 17.01042 ?  153 PHE   A C    1 
ATOM   256  O  O    . PHE   A 1 48  ? 2.33900   12.27700  1.16600  1.000 20.05323 ?  153 PHE   A O    1 
ATOM   257  C  CB   . PHE   A 1 48  ? 4.77100   10.59400  2.62900  1.000 15.55875 ?  153 PHE   A CB   1 
ATOM   258  C  CG   . PHE   A 1 48  ? 6.23200   10.18400  2.59200  1.000 14.86246 ?  153 PHE   A CG   1 
ATOM   259  C  CD1  . PHE   A 1 48  ? 7.07800   10.51800  3.63800  1.000 17.83457 ?  153 PHE   A CD1  1 
ATOM   260  C  CD2  . PHE   A 1 48  ? 6.75300   9.48200   1.51900  1.000 17.20969 ?  153 PHE   A CD2  1 
ATOM   261  C  CE1  . PHE   A 1 48  ? 8.41900   10.15400  3.61800  1.000 20.56301 ?  153 PHE   A CE1  1 
ATOM   262  C  CE2  . PHE   A 1 48  ? 8.09200   9.11100   1.49100  1.000 17.01087 ?  153 PHE   A CE2  1 
ATOM   263  C  CZ   . PHE   A 1 48  ? 8.92400   9.44500   2.54300  1.000 18.41663 ?  153 PHE   A CZ   1 
ATOM   264  N  N    . ARG   A 1 49  ? 1.77900   10.22400  1.89300  1.000 20.61003 ?  154 ARG   A N    1 
ATOM   265  C  CA   . ARG   A 1 49  ? 0.47400   10.67100  2.34900  1.000 19.66943 ?  154 ARG   A CA   1 
ATOM   266  C  C    . ARG   A 1 49  ? 0.66600   11.68900  3.47200  1.000 17.76094 ?  154 ARG   A C    1 
ATOM   267  O  O    . ARG   A 1 49  ? 1.60200   11.56200  4.26900  1.000 19.96899 ?  154 ARG   A O    1 
ATOM   268  C  CB   . ARG   A 1 49  ? -0.35900  9.48400   2.82900  1.000 17.15899 ?  154 ARG   A CB   1 
ATOM   269  C  CG   . ARG   A 1 49  ? -0.92500  8.67000   1.67500  1.000 18.95178 ?  154 ARG   A CG   1 
ATOM   270  C  CD   . ARG   A 1 49  ? -1.51500  7.37200   2.18300  1.000 18.44701 ?  154 ARG   A CD   1 
ATOM   271  N  NE   . ARG   A 1 49  ? -0.47600  6.43400   2.58500  1.000 16.53517 ?  154 ARG   A NE   1 
ATOM   272  C  CZ   . ARG   A 1 49  ? -0.70800  5.30300   3.23900  1.000 17.93840 ?  154 ARG   A CZ   1 
ATOM   273  N  NH1  . ARG   A 1 49  ? -1.95000  4.97400   3.56600  1.000 17.79491 ?  154 ARG   A NH1  1 
ATOM   274  N  NH2  . ARG   A 1 49  ? 0.29600   4.49600   3.55200  1.000 18.97453 ?  154 ARG   A NH2  1 
ATOM   275  N  N    . PRO   A 1 50  ? -0.17600  12.71200  3.55100  1.000 21.42372 ?  155 PRO   A N    1 
ATOM   276  C  CA   . PRO   A 1 50  ? 0.11400   13.85100  4.42900  1.000 25.30279 ?  155 PRO   A CA   1 
ATOM   277  C  C    . PRO   A 1 50  ? 0.03200   13.46400  5.89200  1.000 22.51925 ?  155 PRO   A C    1 
ATOM   278  O  O    . PRO   A 1 50  ? -0.81300  12.64400  6.28700  1.000 22.34093 ?  155 PRO   A O    1 
ATOM   279  C  CB   . PRO   A 1 50  ? -0.98300  14.86700  4.07100  1.000 25.48223 ?  155 PRO   A CB   1 
ATOM   280  C  CG   . PRO   A 1 50  ? -1.54800  14.40700  2.77600  1.000 32.76580 ?  155 PRO   A CG   1 
ATOM   281  C  CD   . PRO   A 1 50  ? -1.39100  12.92600  2.75100  1.000 21.88979 ?  155 PRO   A CD   1 
ATOM   282  N  N    . PRO   A 1 51  ? 0.88500   14.04500  6.73000  1.000 21.75364 ?  156 PRO   A N    1 
ATOM   283  C  CA   . PRO   A 1 51  ? 0.71400   13.87700  8.17200  1.000 22.50124 ?  156 PRO   A CA   1 
ATOM   284  C  C    . PRO   A 1 51  ? -0.56200  14.56600  8.61200  1.000 25.72577 ?  156 PRO   A C    1 
ATOM   285  O  O    . PRO   A 1 51  ? -0.98000  15.57400  8.03900  1.000 28.27699 ?  156 PRO   A O    1 
ATOM   286  C  CB   . PRO   A 1 51  ? 1.95800   14.54700  8.76800  1.000 24.56527 ?  156 PRO   A CB   1 
ATOM   287  C  CG   . PRO   A 1 51  ? 2.42000   15.50800  7.72500  1.000 25.89425 ?  156 PRO   A CG   1 
ATOM   288  C  CD   . PRO   A 1 51  ? 2.02500   14.91700  6.39100  1.000 22.57968 ?  156 PRO   A CD   1 
ATOM   289  N  N    . VAL   A 1 52  ? -1.20800  13.98300  9.61400  1.000 23.33663 ?  157 VAL   A N    1 
ATOM   290  C  CA   . VAL   A 1 52  ? -2.40600  14.56600  10.19800 1.000 25.32643 ?  157 VAL   A CA   1 
ATOM   291  C  C    . VAL   A 1 52  ? -2.23200  14.58000  11.70800 1.000 31.11450 ?  157 VAL   A C    1 
ATOM   292  O  O    . VAL   A 1 52  ? -2.05500  13.52400  12.32800 1.000 33.90553 ?  157 VAL   A O    1 
ATOM   293  C  CB   . VAL   A 1 52  ? -3.68100  13.80700  9.79600  1.000 29.53075 ?  157 VAL   A CB   1 
ATOM   294  C  CG1  . VAL   A 1 52  ? -4.88800  14.37500  10.54500 1.000 33.21517 ?  157 VAL   A CG1  1 
ATOM   295  C  CG2  . VAL   A 1 52  ? -3.90000  13.90400  8.29400  1.000 30.65504 ?  157 VAL   A CG2  1 
ATOM   296  N  N    . ARG   A 1 53  ? -2.23900  15.78100  12.28500 1.000 39.37175 ?  158 ARG   A N    1 
ATOM   297  C  CA   . ARG   A 1 53  ? -2.23700  15.99900  13.72200 1.000 41.69930 ?  158 ARG   A CA   1 
ATOM   298  C  C    . ARG   A 1 53  ? -3.23800  17.10500  14.02100 1.000 50.64198 ?  158 ARG   A C    1 
ATOM   299  O  O    . ARG   A 1 53  ? -3.60400  17.87200  13.13000 1.000 49.36177 ?  158 ARG   A O    1 
ATOM   300  C  CB   . ARG   A 1 53  ? -0.84600  16.40500  14.24100 1.000 38.29091 ?  158 ARG   A CB   1 
ATOM   301  C  CG   . ARG   A 1 53  ? 0.35100   15.93900  13.40600 1.000 37.41524 ?  158 ARG   A CG   1 
ATOM   302  C  CD   . ARG   A 1 53  ? 1.59200   16.75300  13.77300 1.000 31.44573 ?  158 ARG   A CD   1 
ATOM   303  N  NE   . ARG   A 1 53  ? 2.84200   16.14900  13.31600 1.000 32.97454 ?  158 ARG   A NE   1 
ATOM   304  C  CZ   . ARG   A 1 53  ? 3.35700   16.27600  12.09500 1.000 29.61416 ?  158 ARG   A CZ   1 
ATOM   305  N  NH1  . ARG   A 1 53  ? 2.74200   16.99600  11.17100 1.000 27.20295 ?  158 ARG   A NH1  1 
ATOM   306  N  NH2  . ARG   A 1 53  ? 4.50500   15.67400  11.80600 1.000 29.78584 ?  158 ARG   A NH2  1 
ATOM   307  N  N    . MET   A 1 54  ? -3.48600  17.19600  15.33000 1.000 59.59307 ?  159 MET   A N    1 
ATOM   308  C  CA   . MET   A 1 54  ? -4.28800  18.24100  16.01500 1.000 69.72077 ?  159 MET   A CA   1 
ATOM   309  C  C    . MET   A 1 54  ? -4.72800  17.75100  17.39600 1.000 70.16906 ?  159 MET   A C    1 
ATOM   310  O  O    . MET   A 1 54  ? -5.36200  16.69400  17.46200 1.000 69.98274 ?  159 MET   A O    1 
ATOM   311  C  CB   . MET   A 1 54  ? -5.49200  18.64800  15.17700 1.000 77.86260 ?  159 MET   A CB   1 
ATOM   312  C  CG   . MET   A 1 54  ? -5.13400  19.65800  14.10300 1.000 84.26134 ?  159 MET   A CG   1 
ATOM   313  S  SD   . MET   A 1 54  ? -5.62300  21.32000  14.59700 1.000 91.22664 ?  159 MET   A SD   1 
ATOM   314  C  CE   . MET   A 1 54  ? -5.76900  22.13300  13.00700 1.000 90.62049 ?  159 MET   A CE   1 
ATOM   315  N  N    . SER   A 1 66  ? -9.16400  10.63200  16.33600 1.000 56.53269 ?  218 SER   A N    1 
ATOM   316  C  CA   . SER   A 1 66  ? -8.27200  9.97800   15.34200 1.000 52.72748 ?  218 SER   A CA   1 
ATOM   317  C  C    . SER   A 1 66  ? -7.03100  9.38500   16.02200 1.000 48.42448 ?  218 SER   A C    1 
ATOM   318  O  O    . SER   A 1 66  ? -5.95500  9.90600   15.80200 1.000 50.16223 ?  218 SER   A O    1 
ATOM   319  C  CB   . SER   A 1 66  ? -7.87900  10.94700  14.26200 1.000 55.56700 ?  218 SER   A CB   1 
ATOM   320  O  OG   . SER   A 1 66  ? -8.99100  11.60800  13.69400 1.000 60.30570 ?  218 SER   A OG   1 
ATOM   321  N  N    . PRO   A 1 67  ? -7.11000  8.28700   16.78900 1.000 43.05571 ?  219 PRO   A N    1 
ATOM   322  C  CA   . PRO   A 1 67  ? -5.91800  7.69200   17.41700 1.000 39.78847 ?  219 PRO   A CA   1 
ATOM   323  C  C    . PRO   A 1 67  ? -4.86000  7.23400   16.42800 1.000 39.55736 ?  219 PRO   A C    1 
ATOM   324  O  O    . PRO   A 1 67  ? -3.73800  6.92800   16.85600 1.000 37.19593 ?  219 PRO   A O    1 
ATOM   325  C  CB   . PRO   A 1 67  ? -6.48600  6.49800   18.20100 1.000 40.46005 ?  219 PRO   A CB   1 
ATOM   326  C  CG   . PRO   A 1 67  ? -7.78400  6.17600   17.50900 1.000 38.55429 ?  219 PRO   A CG   1 
ATOM   327  C  CD   . PRO   A 1 67  ? -8.32800  7.50500   17.06300 1.000 40.88070 ?  219 PRO   A CD   1 
ATOM   328  N  N    . LEU   A 1 68  ? -5.17000  7.16900   15.13000 1.000 32.53879 ?  220 LEU   A N    1 
ATOM   329  C  CA   . LEU   A 1 68  ? -4.22900  6.66000   14.13800 1.000 28.31309 ?  220 LEU   A CA   1 
ATOM   330  C  C    . LEU   A 1 68  ? -4.02800  7.64400   12.99400 1.000 22.47315 ?  220 LEU   A C    1 
ATOM   331  O  O    . LEU   A 1 68  ? -3.71500  7.23500   11.87400 1.000 21.42249 ?  220 LEU   A O    1 
ATOM   332  C  CB   . LEU   A 1 68  ? -4.69300  5.31200   13.58700 1.000 25.28495 ?  220 LEU   A CB   1 
ATOM   333  C  CG   . LEU   A 1 68  ? -4.81900  4.16300   14.58100 1.000 31.41567 ?  220 LEU   A CG   1 
ATOM   334  C  CD1  . LEU   A 1 68  ? -5.21600  2.89300   13.86200 1.000 32.53365 ?  220 LEU   A CD1  1 
ATOM   335  C  CD2  . LEU   A 1 68  ? -3.50800  3.96500   15.28000 1.000 32.60573 ?  220 LEU   A CD2  1 
ATOM   336  N  N    . SER   A 1 69  ? -4.19000  8.94300   13.25900 1.000 22.51551 ?  221 SER   A N    1 
ATOM   337  C  CA   . SER   A 1 69  ? -4.15000  9.92200   12.17600 1.000 25.60045 ?  221 SER   A CA   1 
ATOM   338  C  C    . SER   A 1 69  ? -2.78800  9.98700   11.49500 1.000 23.19678 ?  221 SER   A C    1 
ATOM   339  O  O    . SER   A 1 69  ? -2.71100  10.40100  10.33400 1.000 23.82104 ?  221 SER   A O    1 
ATOM   340  C  CB   . SER   A 1 69  ? -4.54200  11.30500  12.69800 1.000 28.36115 ?  221 SER   A CB   1 
ATOM   341  O  OG   . SER   A 1 69  ? -3.69900  11.71200  13.76200 1.000 29.79665 ?  221 SER   A OG   1 
ATOM   342  N  N    . MET   A 1 70  ? -1.71600  9.59200   12.17800 1.000 20.68281 ?  222 MET   A N    1 
ATOM   343  C  CA   . MET   A 1 70  ? -0.38300  9.63300   11.58800 1.000 19.42681 ?  222 MET   A CA   1 
ATOM   344  C  C    . MET   A 1 70  ? 0.01400   8.32500   10.91700 1.000 20.00831 ?  222 MET   A C    1 
ATOM   345  O  O    . MET   A 1 70  ? 1.11000   8.24600   10.35200 1.000 20.98239 ?  222 MET   A O    1 
ATOM   346  C  CB   . MET   A 1 70  ? 0.66500   9.99500   12.65000 1.000 18.11727 ?  222 MET   A CB   1 
ATOM   347  C  CG   . MET   A 1 70  ? 0.65200   11.47200  13.03900 1.000 21.67160 ?  222 MET   A CG   1 
ATOM   348  S  SD   . MET   A 1 70  ? 1.11600   12.57500  11.68600 1.000 23.09960 ?  222 MET   A SD   1 
ATOM   349  C  CE   . MET   A 1 70  ? 2.87400   12.24700  11.56800 1.000 23.01770 ?  222 MET   A CE   1 
ATOM   350  N  N    . LEU   A 1 71  ? -0.83200  7.29900   10.97200 1.000 16.62388 ?  223 LEU   A N    1 
ATOM   351  C  CA   . LEU   A 1 71  ? -0.45700  6.01300   10.38500 1.000 20.33156 ?  223 LEU   A CA   1 
ATOM   352  C  C    . LEU   A 1 71  ? -0.19300  6.09200   8.88500  1.000 18.35472 ?  223 LEU   A C    1 
ATOM   353  O  O    . LEU   A 1 71  ? 0.81400   5.52000   8.43200  1.000 19.38949 ?  223 LEU   A O    1 
ATOM   354  C  CB   . LEU   A 1 71  ? -1.52400  4.96100   10.71100 1.000 19.97599 ?  223 LEU   A CB   1 
ATOM   355  C  CG   . LEU   A 1 71  ? -1.26000  3.53500   10.21300 1.000 19.03819 ?  223 LEU   A CG   1 
ATOM   356  C  CD1  . LEU   A 1 71  ? 0.10600   3.01500   10.69400 1.000 17.63239 ?  223 LEU   A CD1  1 
ATOM   357  C  CD2  . LEU   A 1 71  ? -2.37300  2.60500   10.66000 1.000 19.72740 ?  223 LEU   A CD2  1 
ATOM   358  N  N    . PRO   A 1 72  ? -1.02300  6.75000   8.06200  1.000 17.39846 ?  224 PRO   A N    1 
ATOM   359  C  CA   . PRO   A 1 72  ? -0.71500  6.77500   6.61600  1.000 17.74262 ?  224 PRO   A CA   1 
ATOM   360  C  C    . PRO   A 1 72  ? 0.62800   7.41800   6.30500  1.000 18.53703 ?  224 PRO   A C    1 
ATOM   361  O  O    . PRO   A 1 72  ? 1.41700   6.85800   5.53000  1.000 16.22579 ?  224 PRO   A O    1 
ATOM   362  C  CB   . PRO   A 1 72  ? -1.89300  7.56500   6.02500  1.000 17.72236 ?  224 PRO   A CB   1 
ATOM   363  C  CG   . PRO   A 1 72  ? -3.02800  7.30800   6.98500  1.000 19.13475 ?  224 PRO   A CG   1 
ATOM   364  C  CD   . PRO   A 1 72  ? -2.36200  7.30400   8.34500  1.000 17.03269 ?  224 PRO   A CD   1 
ATOM   365  N  N    . HIS   A 1 73  ? 0.91500   8.57900   6.90000  1.000 18.13613 ?  225 HIS   A N    1 
ATOM   366  C  CA   . HIS   A 1 73  ? 2.18600   9.24800   6.64800  1.000 17.84672 ?  225 HIS   A CA   1 
ATOM   367  C  C    . HIS   A 1 73  ? 3.35800   8.41900   7.16400  1.000 15.00783 ?  225 HIS   A C    1 
ATOM   368  O  O    . HIS   A 1 73  ? 4.35200   8.22300   6.45600  1.000 15.54678 ?  225 HIS   A O    1 
ATOM   369  C  CB   . HIS   A 1 73  ? 2.18300   10.63400  7.29700  1.000 17.62343 ?  225 HIS   A CB   1 
ATOM   370  C  CG   . HIS   A 1 73  ? 3.45300   11.40200  7.09000  1.000 18.05731 ?  225 HIS   A CG   1 
ATOM   371  N  ND1  . HIS   A 1 73  ? 3.74900   12.04400  5.90700  1.000 18.58376 ?  225 HIS   A ND1  1 
ATOM   372  C  CD2  . HIS   A 1 73  ? 4.49700   11.64000  7.92000  1.000 19.71573 ?  225 HIS   A CD2  1 
ATOM   373  C  CE1  . HIS   A 1 73  ? 4.92100   12.64500  6.01600  1.000 22.46895 ?  225 HIS   A CE1  1 
ATOM   374  N  NE2  . HIS   A 1 73  ? 5.39600   12.41600  7.22700  1.000 18.78392 ?  225 HIS   A NE2  1 
ATOM   375  N  N    . LEU   A 1 74  ? 3.26200   7.91900   8.39600  1.000 14.85005 ?  226 LEU   A N    1 
ATOM   376  C  CA   . LEU   A 1 74  ? 4.39700   7.18700   8.95300  1.000 14.48753 ?  226 LEU   A CA   1 
ATOM   377  C  C    . LEU   A 1 74  ? 4.56300   5.82600   8.29200  1.000 14.22272 ?  226 LEU   A C    1 
ATOM   378  O  O    . LEU   A 1 74  ? 5.69000   5.33900   8.17800  1.000 15.28537 ?  226 LEU   A O    1 
ATOM   379  C  CB   . LEU   A 1 74  ? 4.25600   7.04900   10.46700 1.000 15.13653 ?  226 LEU   A CB   1 
ATOM   380  C  CG   . LEU   A 1 74  ? 4.48600   8.37500   11.20800 1.000 19.66517 ?  226 LEU   A CG   1 
ATOM   381  C  CD1  . LEU   A 1 74  ? 4.30400   8.21700   12.71100 1.000 22.05223 ?  226 LEU   A CD1  1 
ATOM   382  C  CD2  . LEU   A 1 74  ? 5.86200   8.96300   10.88600 1.000 16.63872 ?  226 LEU   A CD2  1 
ATOM   383  N  N    . ALA   A 1 75  ? 3.47000   5.20700   7.82800  1.000 13.39872 ?  227 ALA   A N    1 
ATOM   384  C  CA   . ALA   A 1 75  ? 3.61300   3.99700   7.02100  1.000 15.61589 ?  227 ALA   A CA   1 
ATOM   385  C  C    . ALA   A 1 75  ? 4.39900   4.28400   5.74900  1.000 13.51521 ?  227 ALA   A C    1 
ATOM   386  O  O    . ALA   A 1 75  ? 5.24600   3.48000   5.33700  1.000 14.25280 ?  227 ALA   A O    1 
ATOM   387  C  CB   . ALA   A 1 75  ? 2.23800   3.41400   6.67300  1.000 17.56012 ?  227 ALA   A CB   1 
ATOM   388  N  N    . ASP   A 1 76  ? 4.12400   5.42100   5.10500  1.000 13.84582 ?  228 ASP   A N    1 
ATOM   389  C  CA   . ASP   A 1 76  ? 4.85400   5.77500   3.89000  1.000 13.00627 ?  228 ASP   A CA   1 
ATOM   390  C  C    . ASP   A 1 76  ? 6.31300   6.07200   4.20600  1.000 15.16117 ?  228 ASP   A C    1 
ATOM   391  O  O    . ASP   A 1 76  ? 7.21400   5.67900   3.45400  1.000 14.52185 ?  228 ASP   A O    1 
ATOM   392  C  CB   . ASP   A 1 76  ? 4.19600   6.97500   3.21000  1.000 16.04103 ?  228 ASP   A CB   1 
ATOM   393  C  CG   . ASP   A 1 76  ? 2.92100   6.60100   2.47400  1.000 17.99315 ?  228 ASP   A CG   1 
ATOM   394  O  OD1  . ASP   A 1 76  ? 2.20000   7.52600   2.04000  1.000 18.76128 ?  228 ASP   A OD1  1 
ATOM   395  O  OD2  . ASP   A 1 76  ? 2.65000   5.38700   2.33200  1.000 17.63924 ?  228 ASP   A OD2  1 
ATOM   396  N  N    . LEU   A 1 77  ? 6.56500   6.75300   5.32500  1.000 14.92459 ?  229 LEU   A N    1 
ATOM   397  C  CA   . LEU   A 1 77  ? 7.94000   7.01300   5.73900  1.000 13.96575 ?  229 LEU   A CA   1 
ATOM   398  C  C    . LEU   A 1 77  ? 8.68600   5.71100   6.00700  1.000 16.37871 ?  229 LEU   A C    1 
ATOM   399  O  O    . LEU   A 1 77  ? 9.83700   5.53600   5.57900  1.000 15.55295 ?  229 LEU   A O    1 
ATOM   400  C  CB   . LEU   A 1 77  ? 7.94300   7.90400   6.98100  1.000 15.57099 ?  229 LEU   A CB   1 
ATOM   401  C  CG   . LEU   A 1 77  ? 9.30900   8.10700   7.64200  1.000 17.10930 ?  229 LEU   A CG   1 
ATOM   402  C  CD1  . LEU   A 1 77  ? 10.29200  8.70000   6.63900  1.000 17.22068 ?  229 LEU   A CD1  1 
ATOM   403  C  CD2  . LEU   A 1 77  ? 9.17200   9.00700   8.84800  1.000 19.01265 ?  229 LEU   A CD2  1 
ATOM   404  N  N    . VAL   A 1 78  ? 8.04600   4.78500   6.72500  1.000 14.60807 ?  230 VAL   A N    1 
ATOM   405  C  CA   . VAL   A 1 78  ? 8.68100   3.50100   7.01600  1.000 14.51286 ?  230 VAL   A CA   1 
ATOM   406  C  C    . VAL   A 1 78  ? 8.93100   2.72400   5.73000  1.000 13.68956 ?  230 VAL   A C    1 
ATOM   407  O  O    . VAL   A 1 78  ? 10.00400  2.14500   5.54300  1.000 15.22158 ?  230 VAL   A O    1 
ATOM   408  C  CB   . VAL   A 1 78  ? 7.83000   2.68700   8.00800  1.000 13.13293 ?  230 VAL   A CB   1 
ATOM   409  C  CG1  . VAL   A 1 78  ? 8.31900   1.22800   8.06500  1.000 15.23044 ?  230 VAL   A CG1  1 
ATOM   410  C  CG2  . VAL   A 1 78  ? 7.87400   3.32700   9.38600  1.000 15.03057 ?  230 VAL   A CG2  1 
ATOM   411  N  N    . SER   A 1 79  ? 7.93800   2.68600   4.82800  1.000 15.29420 ?  231 SER   A N    1 
ATOM   412  C  CA   . SER   A 1 79  ? 8.11400   1.97900   3.56100  1.000 12.81419 ?  231 SER   A CA   1 
ATOM   413  C  C    . SER   A 1 79  ? 9.28400   2.54900   2.77400  1.000 14.89999 ?  231 SER   A C    1 
ATOM   414  O  O    . SER   A 1 79  ? 10.12000  1.80500   2.24500  1.000 14.94856 ?  231 SER   A O    1 
ATOM   415  C  CB   . SER   A 1 79  ? 6.83200   2.06100   2.72600  1.000 16.02186 ?  231 SER   A CB   1 
ATOM   416  O  OG   . SER   A 1 79  ? 6.77500   1.00500   1.78200  1.000 17.75472 ?  231 SER   A OG   1 
ATOM   417  N  N    . TYR   A 1 80  ? 9.32100   3.87300   2.64500  1.000 12.77407 ?  232 TYR   A N    1 
ATOM   418  C  CA   . TYR   A 1 80  ? 10.44700  4.56400   2.03000  1.000 15.12215 ?  232 TYR   A CA   1 
ATOM   419  C  C    . TYR   A 1 80  ? 11.76100  4.16100   2.67900  1.000 15.61131 ?  232 TYR   A C    1 
ATOM   420  O  O    . TYR   A 1 80  ? 12.75500  3.89700   1.98500  1.000 15.11921 ?  232 TYR   A O    1 
ATOM   421  C  CB   . TYR   A 1 80  ? 10.20400  6.06700   2.16300  1.000 13.35110 ?  232 TYR   A CB   1 
ATOM   422  C  CG   . TYR   A 1 80  ? 11.32600  6.98700   1.73900  1.000 18.44016 ?  232 TYR   A CG   1 
ATOM   423  C  CD1  . TYR   A 1 80  ? 11.41600  7.42500   0.43100  1.000 21.12914 ?  232 TYR   A CD1  1 
ATOM   424  C  CD2  . TYR   A 1 80  ? 12.24400  7.47200   2.66600  1.000 20.88442 ?  232 TYR   A CD2  1 
ATOM   425  C  CE1  . TYR   A 1 80  ? 12.41000  8.29400   0.03500  1.000 25.63503 ?  232 TYR   A CE1  1 
ATOM   426  C  CE2  . TYR   A 1 80  ? 13.25100  8.34500   2.28000  1.000 22.73241 ?  232 TYR   A CE2  1 
ATOM   427  C  CZ   . TYR   A 1 80  ? 13.32200  8.75100   0.95900  1.000 26.59702 ?  232 TYR   A CZ   1 
ATOM   428  O  OH   . TYR   A 1 80  ? 14.31500  9.61300   0.55100  1.000 40.02650 ?  232 TYR   A OH   1 
ATOM   429  N  N    . SER   A 1 81  ? 11.77100  4.08500   4.01200  1.000 13.10944 ?  233 SER   A N    1 
ATOM   430  C  CA   . SER   A 1 81  ? 12.99300  3.76200   4.74100  1.000 14.71245 ?  233 SER   A CA   1 
ATOM   431  C  C    . SER   A 1 81  ? 13.41400  2.31600   4.51800  1.000 16.63521 ?  233 SER   A C    1 
ATOM   432  O  O    . SER   A 1 81  ? 14.61500  2.02200   4.44600  1.000 16.25921 ?  233 SER   A O    1 
ATOM   433  C  CB   . SER   A 1 81  ? 12.80200  4.04400   6.22900  1.000 14.85566 ?  233 SER   A CB   1 
ATOM   434  O  OG   . SER   A 1 81  ? 12.48000  5.41000   6.44800  1.000 16.09722 ?  233 SER   A OG   1 
ATOM   435  N  N    . ILE   A 1 82  ? 12.44600  1.39700   4.43100  1.000 11.60267 ?  234 ILE   A N    1 
ATOM   436  C  CA   . ILE   A 1 82  ? 12.76800  0.01000   4.09500  1.000 11.88351 ?  234 ILE   A CA   1 
ATOM   437  C  C    . ILE   A 1 82  ? 13.48900  -0.04800  2.75600  1.000 15.17949 ?  234 ILE   A C    1 
ATOM   438  O  O    . ILE   A 1 82  ? 14.50300  -0.74100  2.60800  1.000 14.41667 ?  234 ILE   A O    1 
ATOM   439  C  CB   . ILE   A 1 82  ? 11.49400  -0.86100  4.08600  1.000 13.58744 ?  234 ILE   A CB   1 
ATOM   440  C  CG1  . ILE   A 1 82  ? 10.93400  -1.00500  5.50500  1.000 15.37371 ?  234 ILE   A CG1  1 
ATOM   441  C  CG2  . ILE   A 1 82  ? 11.79100  -2.24400  3.49500  1.000 15.37909 ?  234 ILE   A CG2  1 
ATOM   442  C  CD1  . ILE   A 1 82  ? 9.54300   -1.63600  5.53300  1.000 15.25607 ?  234 ILE   A CD1  1 
ATOM   443  N  N    . GLN   A 1 83  ? 12.98800  0.69300   1.76400  1.000 13.72209 ?  235 GLN   A N    1 
ATOM   444  C  CA   . GLN   A 1 83  ? 13.67000  0.74100   0.47400  1.000 14.88767 ?  235 GLN   A CA   1 
ATOM   445  C  C    . GLN   A 1 83  ? 15.11600  1.19600   0.63400  1.000 13.92230 ?  235 GLN   A C    1 
ATOM   446  O  O    . GLN   A 1 83  ? 16.02000  0.63800   0.00000  1.000 13.78938 ?  235 GLN   A O    1 
ATOM   447  C  CB   . GLN   A 1 83  ? 12.93400  1.67200   -0.48400 1.000 17.34064 ?  235 GLN   A CB   1 
ATOM   448  C  CG   . GLN   A 1 83  ? 11.56900  1.18100   -0.89600 1.000 17.39686 ?  235 GLN   A CG   1 
ATOM   449  C  CD   . GLN   A 1 83  ? 10.95000  2.06500   -1.95600 1.000 23.05377 ?  235 GLN   A CD   1 
ATOM   450  O  OE1  . GLN   A 1 83  ? 11.57100  2.35000   -2.98100 1.000 24.57552 ?  235 GLN   A OE1  1 
ATOM   451  N  NE2  . GLN   A 1 83  ? 9.72800   2.51600   -1.70800 1.000 21.32500 ?  235 GLN   A NE2  1 
ATOM   452  N  N    . LYS   A 1 84  ? 15.35300  2.21500   1.46600  1.000 14.18827 ?  236 LYS   A N    1 
ATOM   453  C  CA   . LYS   A 1 84  ? 16.71800  2.71000   1.64200  1.000 14.92743 ?  236 LYS   A CA   1 
ATOM   454  C  C    . LYS   A 1 84  ? 17.59200  1.66700   2.32500  1.000 13.06725 ?  236 LYS   A C    1 
ATOM   455  O  O    . LYS   A 1 84  ? 18.76100  1.48100   1.95200  1.000 15.56235 ?  236 LYS   A O    1 
ATOM   456  C  CB   . LYS   A 1 84  ? 16.71600  4.00700   2.45200  1.000 15.94568 ?  236 LYS   A CB   1 
ATOM   457  C  CG   . LYS   A 1 84  ? 15.88900  5.13100   1.85200  1.000 17.24052 ?  236 LYS   A CG   1 
ATOM   458  C  CD   . LYS   A 1 84  ? 16.33600  5.44300   0.43200  1.000 16.65693 ?  236 LYS   A CD   1 
ATOM   459  C  CE   . LYS   A 1 84  ? 15.79100  6.78400   -0.03600 1.000 25.68386 ?  236 LYS   A CE   1 
ATOM   460  N  NZ   . LYS   A 1 84  ? 16.42400  7.92400   0.70300  1.000 27.15105 ?  236 LYS   A NZ   1 
ATOM   461  N  N    . VAL   A 1 85  ? 17.04000  0.97300   3.32400  1.000 12.33075 ?  237 VAL   A N    1 
ATOM   462  C  CA   . VAL   A 1 85  ? 17.82400  -0.01400  4.06600  1.000 14.10492 ?  237 VAL   A CA   1 
ATOM   463  C  C    . VAL   A 1 85  ? 18.22500  -1.16300  3.15000  1.000 11.55849 ?  237 VAL   A C    1 
ATOM   464  O  O    . VAL   A 1 85  ? 19.35300  -1.66600  3.21400  1.000 14.54988 ?  237 VAL   A O    1 
ATOM   465  C  CB   . VAL   A 1 85  ? 17.03700  -0.51400  5.29300  1.000 15.50151 ?  237 VAL   A CB   1 
ATOM   466  C  CG1  . VAL   A 1 85  ? 17.74700  -1.71400  5.92500  1.000 13.60524 ?  237 VAL   A CG1  1 
ATOM   467  C  CG2  . VAL   A 1 85  ? 16.88500  0.60700   6.32100  1.000 16.52394 ?  237 VAL   A CG2  1 
ATOM   468  N  N    . ILE   A 1 86  ? 17.31000  -1.59300  2.27700  1.000 11.84561 ?  238 ILE   A N    1 
ATOM   469  C  CA   . ILE   A 1 86  ? 17.65800  -2.62200  1.30100  1.000 13.18745 ?  238 ILE   A CA   1 
ATOM   470  C  C    . ILE   A 1 86  ? 18.76000  -2.12400  0.37800  1.000 14.48489 ?  238 ILE   A C    1 
ATOM   471  O  O    . ILE   A 1 86  ? 19.70600  -2.85600  0.05700  1.000 15.76464 ?  238 ILE   A O    1 
ATOM   472  C  CB   . ILE   A 1 86  ? 16.41800  -3.04500  0.49500  1.000 15.45939 ?  238 ILE   A CB   1 
ATOM   473  C  CG1  . ILE   A 1 86  ? 15.36800  -3.67700  1.40800  1.000 15.01660 ?  238 ILE   A CG1  1 
ATOM   474  C  CG2  . ILE   A 1 86  ? 16.81700  -4.00900  -0.61300 1.000 15.63295 ?  238 ILE   A CG2  1 
ATOM   475  C  CD1  . ILE   A 1 86  ? 13.98300  -3.72200  0.75600  1.000 13.47789 ?  238 ILE   A CD1  1 
ATOM   476  N  N    . GLY   A 1 87  ? 18.64900  -0.87500  -0.07000 1.000 14.68690 ?  239 GLY   A N    1 
ATOM   477  C  CA   . GLY   A 1 87  ? 19.66800  -0.32600  -0.95000 1.000 15.84448 ?  239 GLY   A CA   1 
ATOM   478  C  C    . GLY   A 1 87  ? 21.02500  -0.24500  -0.27600 1.000 14.23217 ?  239 GLY   A C    1 
ATOM   479  O  O    . GLY   A 1 87  ? 22.06100  -0.43000  -0.92200 1.000 16.74744 ?  239 GLY   A O    1 
ATOM   480  N  N    . PHE   A 1 88  ? 21.03700  0.05100   1.02300  1.000 13.75844 ?  240 PHE   A N    1 
ATOM   481  C  CA   . PHE   A 1 88  ? 22.29100  0.06500   1.77000  1.000 13.72252 ?  240 PHE   A CA   1 
ATOM   482  C  C    . PHE   A 1 88  ? 22.84000  -1.34700  1.92300  1.000 14.43193 ?  240 PHE   A C    1 
ATOM   483  O  O    . PHE   A 1 88  ? 24.02400  -1.60300  1.66500  1.000 14.14528 ?  240 PHE   A O    1 
ATOM   484  C  CB   . PHE   A 1 88  ? 22.07000  0.71300   3.13800  1.000 13.93626 ?  240 PHE   A CB   1 
ATOM   485  C  CG   . PHE   A 1 88  ? 23.27100  0.66600   4.04000  1.000 14.09471 ?  240 PHE   A CG   1 
ATOM   486  C  CD1  . PHE   A 1 88  ? 24.31700  1.56300   3.87100  1.000 13.84129 ?  240 PHE   A CD1  1 
ATOM   487  C  CD2  . PHE   A 1 88  ? 23.34600  -0.25700  5.06700  1.000 13.81880 ?  240 PHE   A CD2  1 
ATOM   488  C  CE1  . PHE   A 1 88  ? 25.41800  1.53000   4.70400  1.000 15.50442 ?  240 PHE   A CE1  1 
ATOM   489  C  CE2  . PHE   A 1 88  ? 24.43200  -0.28600  5.91100  1.000 14.86861 ?  240 PHE   A CE2  1 
ATOM   490  C  CZ   . PHE   A 1 88  ? 25.47400  0.60300   5.73000  1.000 15.63273 ?  240 PHE   A CZ   1 
ATOM   491  N  N    . ALA   A 1 89  ? 21.97900  -2.28300  2.32500  1.000 13.59794 ?  241 ALA   A N    1 
ATOM   492  C  CA   . ALA   A 1 89  ? 22.42900  -3.64600  2.58200  1.000 13.35219 ?  241 ALA   A CA   1 
ATOM   493  C  C    . ALA   A 1 89  ? 23.05600  -4.26500  1.34200  1.000 12.70368 ?  241 ALA   A C    1 
ATOM   494  O  O    . ALA   A 1 89  ? 24.07100  -4.96500  1.43300  1.000 14.82339 ?  241 ALA   A O    1 
ATOM   495  C  CB   . ALA   A 1 89  ? 21.25300  -4.49700  3.06600  1.000 13.63007 ?  241 ALA   A CB   1 
ATOM   496  N  N    . LYS   A 1 90  ? 22.48000  -4.00700  0.16400  1.000 14.26275 ?  242 LYS   A N    1 
ATOM   497  C  CA   . LYS   A 1 90  ? 22.98900  -4.65400  -1.03800 1.000 17.50067 ?  242 LYS   A CA   1 
ATOM   498  C  C    . LYS   A 1 90  ? 24.41100  -4.21900  -1.37000 1.000 15.01917 ?  242 LYS   A C    1 
ATOM   499  O  O    . LYS   A 1 90  ? 25.09000  -4.89900  -2.14800 1.000 18.30313 ?  242 LYS   A O    1 
ATOM   500  C  CB   . LYS   A 1 90  ? 22.05000  -4.38300  -2.21600 1.000 20.41707 ?  242 LYS   A CB   1 
ATOM   501  C  CG   . LYS   A 1 90  ? 22.20500  -3.01700  -2.83000 1.000 20.88903 ?  242 LYS   A CG   1 
ATOM   502  C  CD   . LYS   A 1 90  ? 21.04700  -2.69500  -3.78000 1.000 26.56867 ?  242 LYS   A CD   1 
ATOM   503  C  CE   . LYS   A 1 90  ? 20.83200  -3.80600  -4.78500 1.000 33.15427 ?  242 LYS   A CE   1 
ATOM   504  N  NZ   . LYS   A 1 90  ? 19.71200  -3.49900  -5.72900 1.000 38.60014 ?  242 LYS   A NZ   1 
ATOM   505  N  N    A MET   A 1 91  ? 24.87000  -3.10000  -0.80400 0.620 13.20719 ?  243 MET   A N    1 
ATOM   506  N  N    B MET   A 1 91  ? 24.89000  -3.12400  -0.79000 0.380 13.52107 ?  243 MET   A N    1 
ATOM   507  C  CA   A MET   A 1 91  ? 26.23600  -2.62400  -0.99100 0.620 14.12193 ?  243 MET   A CA   1 
ATOM   508  C  CA   B MET   A 1 91  ? 26.25900  -2.69000  -1.02500 0.380 14.34301 ?  243 MET   A CA   1 
ATOM   509  C  C    A MET   A 1 91  ? 27.21200  -3.14500  0.05800  0.620 15.49065 ?  243 MET   A C    1 
ATOM   510  C  C    B MET   A 1 91  ? 27.21200  -3.07500  0.10000  0.380 15.26006 ?  243 MET   A C    1 
ATOM   511  O  O    A MET   A 1 91  ? 28.42800  -3.00200  -0.12900 0.620 15.83311 ?  243 MET   A O    1 
ATOM   512  O  O    B MET   A 1 91  ? 28.40900  -2.78500  0.00300  0.380 16.61140 ?  243 MET   A O    1 
ATOM   513  C  CB   A MET   A 1 91  ? 26.26900  -1.09200  -0.98100 0.620 15.64648 ?  243 MET   A CB   1 
ATOM   514  C  CB   B MET   A 1 91  ? 26.29400  -1.18000  -1.26100 0.380 16.70399 ?  243 MET   A CB   1 
ATOM   515  C  CG   A MET   A 1 91  ? 25.27100  -0.44200  -1.91300 0.620 18.90245 ?  243 MET   A CG   1 
ATOM   516  C  CG   B MET   A 1 91  ? 25.71300  -0.80400  -2.61000 0.380 19.22755 ?  243 MET   A CG   1 
ATOM   517  S  SD   A MET   A 1 91  ? 25.45600  -1.01900  -3.60800 0.620 21.56996 ?  243 MET   A SD   1 
ATOM   518  S  SD   B MET   A 1 91  ? 25.64500  0.96500   -2.88800 0.380 23.82486 ?  243 MET   A SD   1 
ATOM   519  C  CE   A MET   A 1 91  ? 27.11200  -0.46200  -3.99900 0.620 20.55930 ?  243 MET   A CE   1 
ATOM   520  C  CE   B MET   A 1 91  ? 24.28900  1.42000   -1.82200 0.380 22.33403 ?  243 MET   A CE   1 
ATOM   521  N  N    . ILE   A 1 92  ? 26.72000  -3.72300  1.15200  1.000 13.29471 ?  244 ILE   A N    1 
ATOM   522  C  CA   . ILE   A 1 92  ? 27.63300  -4.22800  2.18900  1.000 15.98589 ?  244 ILE   A CA   1 
ATOM   523  C  C    . ILE   A 1 92  ? 28.53000  -5.29300  1.57300  1.000 13.73886 ?  244 ILE   A C    1 
ATOM   524  O  O    . ILE   A 1 92  ? 28.01400  -6.26200  0.99200  1.000 16.03345 ?  244 ILE   A O    1 
ATOM   525  C  CB   . ILE   A 1 92  ? 26.84600  -4.82000  3.37200  1.000 15.06294 ?  244 ILE   A CB   1 
ATOM   526  C  CG1  . ILE   A 1 92  ? 26.03200  -3.76100  4.10800  1.000 13.79245 ?  244 ILE   A CG1  1 
ATOM   527  C  CG2  . ILE   A 1 92  ? 27.81300  -5.49600  4.35800  1.000 16.97276 ?  244 ILE   A CG2  1 
ATOM   528  C  CD1  . ILE   A 1 92  ? 25.09000  -4.37700  5.13200  1.000 14.42779 ?  244 ILE   A CD1  1 
ATOM   529  N  N    . PRO   A 1 93  ? 29.87300  -5.17100  1.66100  1.000 17.59774 ?  245 PRO   A N    1 
ATOM   530  C  CA   . PRO   A 1 93  ? 30.74700  -6.19500  1.07500  1.000 19.19596 ?  245 PRO   A CA   1 
ATOM   531  C  C    . PRO   A 1 93  ? 30.35200  -7.60000  1.49800  1.000 20.45530 ?  245 PRO   A C    1 
ATOM   532  O  O    . PRO   A 1 93  ? 30.26100  -7.90300  2.69300  1.000 18.19477 ?  245 PRO   A O    1 
ATOM   533  C  CB   . PRO   A 1 93  ? 32.13800  -5.81700  1.60600  1.000 17.57003 ?  245 PRO   A CB   1 
ATOM   534  C  CG   . PRO   A 1 93  ? 32.05300  -4.33300  1.79100  1.000 19.27784 ?  245 PRO   A CG   1 
ATOM   535  C  CD   . PRO   A 1 93  ? 30.64200  -4.06200  2.25200  1.000 15.20332 ?  245 PRO   A CD   1 
ATOM   536  N  N    . GLY   A 1 94  ? 30.07400  -8.44600  0.51000  1.000 17.84420 ?  246 GLY   A N    1 
ATOM   537  C  CA   . GLY   A 1 94  ? 29.70600  -9.81700  0.74600  1.000 16.11720 ?  246 GLY   A CA   1 
ATOM   538  C  C    . GLY   A 1 94  ? 28.21800  -10.07800 0.87000  1.000 15.17015 ?  246 GLY   A C    1 
ATOM   539  O  O    . GLY   A 1 94  ? 27.79700  -11.22300 0.68300  1.000 15.99743 ?  246 GLY   A O    1 
ATOM   540  N  N    . PHE   A 1 95  ? 27.40900  -9.05900  1.19300  1.000 15.86374 ?  247 PHE   A N    1 
ATOM   541  C  CA   . PHE   A 1 95  ? 25.99200  -9.31400  1.45400  1.000 15.89724 ?  247 PHE   A CA   1 
ATOM   542  C  C    . PHE   A 1 95  ? 25.31100  -9.94800  0.24700  1.000 18.62794 ?  247 PHE   A C    1 
ATOM   543  O  O    . PHE   A 1 95  ? 24.54500  -10.90900 0.39200  1.000 15.53186 ?  247 PHE   A O    1 
ATOM   544  C  CB   . PHE   A 1 95  ? 25.26900  -8.02400  1.85000  1.000 12.84373 ?  247 PHE   A CB   1 
ATOM   545  C  CG   . PHE   A 1 95  ? 23.81200  -8.22100  2.18200  1.000 13.07884 ?  247 PHE   A CG   1 
ATOM   546  C  CD1  . PHE   A 1 95  ? 23.42200  -8.57800  3.46500  1.000 17.21537 ?  247 PHE   A CD1  1 
ATOM   547  C  CD2  . PHE   A 1 95  ? 22.83600  -8.06500  1.20600  1.000 12.74143 ?  247 PHE   A CD2  1 
ATOM   548  C  CE1  . PHE   A 1 95  ? 22.07900  -8.76800  3.77800  1.000 17.32890 ?  247 PHE   A CE1  1 
ATOM   549  C  CE2  . PHE   A 1 95  ? 21.48400  -8.25800  1.51100  1.000 16.87384 ?  247 PHE   A CE2  1 
ATOM   550  C  CZ   . PHE   A 1 95  ? 21.11200  -8.60000  2.79300  1.000 15.23273 ?  247 PHE   A CZ   1 
ATOM   551  N  N    . ARG   A 1 96  ? 25.58200  -9.43300  -0.95400 1.000 15.68086 ?  248 ARG   A N    1 
ATOM   552  C  CA   . ARG   A 1 96  ? 24.89400  -9.95200  -2.13300 1.000 18.54432 ?  248 ARG   A CA   1 
ATOM   553  C  C    . ARG   A 1 96  ? 25.41000  -11.32000 -2.55000 1.000 18.56768 ?  248 ARG   A C    1 
ATOM   554  O  O    . ARG   A 1 96  ? 24.82800  -11.94000 -3.44700 1.000 20.53937 ?  248 ARG   A O    1 
ATOM   555  C  CB   . ARG   A 1 96  ? 25.02700  -8.97400  -3.29800 1.000 24.45254 ?  248 ARG   A CB   1 
ATOM   556  C  CG   . ARG   A 1 96  ? 26.46100  -8.71200  -3.69800 1.000 32.28977 ?  248 ARG   A CG   1 
ATOM   557  C  CD   . ARG   A 1 96  ? 26.55300  -7.78100  -4.89500 1.000 45.28126 ?  248 ARG   A CD   1 
ATOM   558  N  NE   . ARG   A 1 96  ? 27.90200  -7.76900  -5.44400 1.000 54.90878 ?  248 ARG   A NE   1 
ATOM   559  C  CZ   . ARG   A 1 96  ? 28.33900  -8.62500  -6.36100 1.000 63.86051 ?  248 ARG   A CZ   1 
ATOM   560  N  NH1  . ARG   A 1 96  ? 27.52800  -9.56300  -6.83200 1.000 65.81585 ?  248 ARG   A NH1  1 
ATOM   561  N  NH2  . ARG   A 1 96  ? 29.58700  -8.54500  -6.80600 1.000 65.38347 ?  248 ARG   A NH2  1 
ATOM   562  N  N    . ASP   A 1 97  ? 26.47600  -11.80000 -1.91600 1.000 16.20326 ?  249 ASP   A N    1 
ATOM   563  C  CA   . ASP   A 1 97  ? 27.02200  -13.12200 -2.18500 1.000 17.86645 ?  249 ASP   A CA   1 
ATOM   564  C  C    . ASP   A 1 97  ? 26.37700  -14.20400 -1.33700 1.000 17.99432 ?  249 ASP   A C    1 
ATOM   565  O  O    . ASP   A 1 97  ? 26.59700  -15.39100 -1.59600 1.000 20.23195 ?  249 ASP   A O    1 
ATOM   566  C  CB   . ASP   A 1 97  ? 28.53200  -13.11900 -1.94600 1.000 18.70012 ?  249 ASP   A CB   1 
ATOM   567  C  CG   . ASP   A 1 97  ? 29.25900  -12.16500 -2.87100 1.000 24.77800 ?  249 ASP   A CG   1 
ATOM   568  O  OD1  . ASP   A 1 97  ? 28.79100  -11.96300 -4.01200 1.000 23.40098 ?  249 ASP   A OD1  1 
ATOM   569  O  OD2  . ASP   A 1 97  ? 30.29700  -11.61500 -2.45600 1.000 25.53858 ?  249 ASP   A OD2  1 
ATOM   570  N  N    . LEU   A 1 98  ? 25.60000  -13.81800 -0.33300 1.000 15.66542 ?  250 LEU   A N    1 
ATOM   571  C  CA   . LEU   A 1 98  ? 24.78100  -14.76800 0.39400  1.000 16.07694 ?  250 LEU   A CA   1 
ATOM   572  C  C    . LEU   A 1 98  ? 23.65100  -15.26200 -0.50000 1.000 18.36820 ?  250 LEU   A C    1 
ATOM   573  O  O    . LEU   A 1 98  ? 23.32800  -14.65400 -1.52100 1.000 20.23693 ?  250 LEU   A O    1 
ATOM   574  C  CB   . LEU   A 1 98  ? 24.20300  -14.11800 1.64600  1.000 14.58308 ?  250 LEU   A CB   1 
ATOM   575  C  CG   . LEU   A 1 98  ? 25.23700  -13.56200 2.62500  1.000 15.50397 ?  250 LEU   A CG   1 
ATOM   576  C  CD1  . LEU   A 1 98  ? 24.51700  -12.75800 3.69900  1.000 17.03017 ?  250 LEU   A CD1  1 
ATOM   577  C  CD2  . LEU   A 1 98  ? 26.00600  -14.72100 3.24200  1.000 16.10355 ?  250 LEU   A CD2  1 
ATOM   578  N  N    . THR   A 1 99  ? 23.04200  -16.38000 -0.11000 1.000 17.08286 ?  251 THR   A N    1 
ATOM   579  C  CA   . THR   A 1 99  ? 21.87000  -16.82400 -0.85200 1.000 18.34709 ?  251 THR   A CA   1 
ATOM   580  C  C    . THR   A 1 99  ? 20.77200  -15.77900 -0.72000 1.000 19.88541 ?  251 THR   A C    1 
ATOM   581  O  O    . THR   A 1 99  ? 20.72400  -15.01700 0.25200  1.000 17.49288 ?  251 THR   A O    1 
ATOM   582  C  CB   . THR   A 1 99  ? 21.36800  -18.18000 -0.35300 1.000 22.47424 ?  251 THR   A CB   1 
ATOM   583  O  OG1  . THR   A 1 99  ? 20.87200  -18.05300 0.98900  1.000 20.10104 ?  251 THR   A OG1  1 
ATOM   584  C  CG2  . THR   A 1 99  ? 22.49100  -19.21700 -0.40200 1.000 18.40886 ?  251 THR   A CG2  1 
ATOM   585  N  N    A SER   A 1 100 ? 19.88100  -15.73200 -1.71200 0.540 18.19800 ?  252 SER   A N    1 
ATOM   586  N  N    B SER   A 1 100 ? 19.89500  -15.73500 -1.72700 0.460 18.25017 ?  252 SER   A N    1 
ATOM   587  C  CA   A SER   A 1 100 ? 18.81100  -14.74200 -1.64600 0.540 18.90607 ?  252 SER   A CA   1 
ATOM   588  C  CA   B SER   A 1 100 ? 18.77800  -14.79500 -1.69100 0.460 19.27692 ?  252 SER   A CA   1 
ATOM   589  C  C    A SER   A 1 100 ? 17.90400  -14.98800 -0.44700 0.540 18.54516 ?  252 SER   A C    1 
ATOM   590  C  C    B SER   A 1 100 ? 17.93900  -14.99500 -0.43900 0.460 18.68380 ?  252 SER   A C    1 
ATOM   591  O  O    A SER   A 1 100 ? 17.39100  -14.03200 0.14500  0.540 19.86577 ?  252 SER   A O    1 
ATOM   592  O  O    B SER   A 1 100 ? 17.50500  -14.02300 0.19100  0.460 18.60732 ?  252 SER   A O    1 
ATOM   593  C  CB   A SER   A 1 100 ? 18.00300  -14.73300 -2.94500 0.540 19.63178 ?  252 SER   A CB   1 
ATOM   594  C  CB   B SER   A 1 100 ? 17.91400  -14.95800 -2.94200 0.460 18.87223 ?  252 SER   A CB   1 
ATOM   595  O  OG   A SER   A 1 100 ? 17.69900  -16.04200 -3.38100 0.540 22.67116 ?  252 SER   A OG   1 
ATOM   596  O  OG   B SER   A 1 100 ? 18.68000  -14.78000 -4.11800 0.460 21.11699 ?  252 SER   A OG   1 
ATOM   597  N  N    . ASP   A 1 101 ? 17.72100  -16.25300 -0.05300 1.000 18.64545 ?  253 ASP   A N    1 
ATOM   598  C  CA   . ASP   A 1 101 ? 16.91900  -16.54100 1.13400  1.000 19.32796 ?  253 ASP   A CA   1 
ATOM   599  C  C    . ASP   A 1 101 ? 17.54600  -15.93800 2.38500  1.000 17.91422 ?  253 ASP   A C    1 
ATOM   600  O  O    . ASP   A 1 101 ? 16.84100  -15.37200 3.22600  1.000 20.09878 ?  253 ASP   A O    1 
ATOM   601  C  CB   . ASP   A 1 101 ? 16.74400  -18.05000 1.30100  1.000 23.02354 ?  253 ASP   A CB   1 
ATOM   602  C  CG   . ASP   A 1 101 ? 15.63700  -18.62200 0.41600  1.000 33.29648 ?  253 ASP   A CG   1 
ATOM   603  O  OD1  . ASP   A 1 101 ? 14.86800  -17.84400 -0.18700 1.000 34.00214 ?  253 ASP   A OD1  1 
ATOM   604  O  OD2  . ASP   A 1 101 ? 15.54200  -19.86000 0.32700  1.000 39.91212 ?  253 ASP   A OD2  1 
ATOM   605  N  N    . ASP   A 1 102 ? 18.87000  -16.04700 2.53000  1.000 17.05482 ?  254 ASP   A N    1 
ATOM   606  C  CA   . ASP   A 1 102 ? 19.52100  -15.45200 3.69500  1.000 17.60527 ?  254 ASP   A CA   1 
ATOM   607  C  C    . ASP   A 1 102 ? 19.47900  -13.93000 3.63600  1.000 15.35627 ?  254 ASP   A C    1 
ATOM   608  O  O    . ASP   A 1 102 ? 19.29800  -13.26700 4.66400  1.000 16.13190 ?  254 ASP   A O    1 
ATOM   609  C  CB   . ASP   A 1 102 ? 20.96100  -15.95400 3.81300  1.000 18.33073 ?  254 ASP   A CB   1 
ATOM   610  C  CG   . ASP   A 1 102 ? 21.05600  -17.24400 4.59700  1.000 22.38698 ?  254 ASP   A CG   1 
ATOM   611  O  OD1  . ASP   A 1 102 ? 22.13900  -17.86400 4.61700  1.000 20.52387 ?  254 ASP   A OD1  1 
ATOM   612  O  OD2  . ASP   A 1 102 ? 20.03400  -17.64500 5.19100  1.000 24.99485 ?  254 ASP   A OD2  1 
ATOM   613  N  N    . GLN   A 1 103 ? 19.63400  -13.35300 2.44400  1.000 14.26101 ?  255 GLN   A N    1 
ATOM   614  C  CA   . GLN   A 1 103 ? 19.49900  -11.90500 2.31400  1.000 14.52268 ?  255 GLN   A CA   1 
ATOM   615  C  C    . GLN   A 1 103 ? 18.12900  -11.44400 2.78700  1.000 17.14383 ?  255 GLN   A C    1 
ATOM   616  O  O    . GLN   A 1 103 ? 18.01500  -10.45600 3.51900  1.000 16.53670 ?  255 GLN   A O    1 
ATOM   617  C  CB   . GLN   A 1 103 ? 19.73100  -11.48100 0.87200  1.000 15.83290 ?  255 GLN   A CB   1 
ATOM   618  C  CG   . GLN   A 1 103 ? 21.15900  -11.70200 0.39800  1.000 14.41627 ?  255 GLN   A CG   1 
ATOM   619  C  CD   . GLN   A 1 103 ? 21.32400  -11.32300 -1.04700 1.000 17.95049 ?  255 GLN   A CD   1 
ATOM   620  O  OE1  . GLN   A 1 103 ? 20.85600  -10.26900 -1.46800 1.000 21.62122 ?  255 GLN   A OE1  1 
ATOM   621  N  NE2  . GLN   A 1 103 ? 21.95500  -12.19800 -1.83100 1.000 17.51280 ?  255 GLN   A NE2  1 
ATOM   622  N  N    . ILE   A 1 104 ? 17.08500  -12.17700 2.40200  1.000 18.52291 ?  256 ILE   A N    1 
ATOM   623  C  CA   . ILE   A 1 104 ? 15.72400  -11.82900 2.79800  1.000 16.75836 ?  256 ILE   A CA   1 
ATOM   624  C  C    . ILE   A 1 104 ? 15.54600  -11.95800 4.30800  1.000 17.21272 ?  256 ILE   A C    1 
ATOM   625  O  O    . ILE   A 1 104 ? 14.98400  -11.06900 4.96200  1.000 18.58616 ?  256 ILE   A O    1 
ATOM   626  C  CB   . ILE   A 1 104 ? 14.72400  -12.71200 2.03700  1.000 16.40104 ?  256 ILE   A CB   1 
ATOM   627  C  CG1  . ILE   A 1 104 ? 14.66500  -12.30300 0.56200  1.000 17.59912 ?  256 ILE   A CG1  1 
ATOM   628  C  CG2  . ILE   A 1 104 ? 13.35600  -12.66900 2.71400  1.000 16.35786 ?  256 ILE   A CG2  1 
ATOM   629  C  CD1  . ILE   A 1 104 ? 13.97400  -13.32100 -0.32200 1.000 22.82578 ?  256 ILE   A CD1  1 
ATOM   630  N  N    A VAL   A 1 105 ? 16.02200  -13.05700 4.89700  0.370 15.29833 ?  257 VAL   A N    1 
ATOM   631  N  N    B VAL   A 1 105 ? 16.00100  -13.08100 4.87200  0.630 14.23525 ?  257 VAL   A N    1 
ATOM   632  C  CA   A VAL   A 1 105 ? 15.78700  -13.22500 6.33000  0.370 17.48421 ?  257 VAL   A CA   1 
ATOM   633  C  CA   B VAL   A 1 105 ? 15.88400  -13.30600 6.31100  0.630 18.09571 ?  257 VAL   A CA   1 
ATOM   634  C  C    A VAL   A 1 105 ? 16.59400  -12.21200 7.13900  0.370 15.40348 ?  257 VAL   A C    1 
ATOM   635  C  C    B VAL   A 1 105 ? 16.56500  -12.18100 7.07800  0.630 15.13121 ?  257 VAL   A C    1 
ATOM   636  O  O    A VAL   A 1 105 ? 16.14000  -11.75600 8.19600  0.370 15.20177 ?  257 VAL   A O    1 
ATOM   637  O  O    B VAL   A 1 105 ? 16.00800  -11.62400 8.03300  0.630 14.06144 ?  257 VAL   A O    1 
ATOM   638  C  CB   A VAL   A 1 105 ? 16.07200  -14.67200 6.78100  0.370 20.72190 ?  257 VAL   A CB   1 
ATOM   639  C  CB   B VAL   A 1 105 ? 16.47600  -14.67800 6.68800  0.630 20.17322 ?  257 VAL   A CB   1 
ATOM   640  C  CG1  A VAL   A 1 105 ? 15.20800  -15.65300 6.00100  0.370 22.36646 ?  257 VAL   A CG1  1 
ATOM   641  C  CG1  B VAL   A 1 105 ? 16.83300  -14.71800 8.16700  0.630 22.11492 ?  257 VAL   A CG1  1 
ATOM   642  C  CG2  A VAL   A 1 105 ? 17.53900  -15.01300 6.64000  0.370 19.75415 ?  257 VAL   A CG2  1 
ATOM   643  C  CG2  B VAL   A 1 105 ? 15.50600  -15.79900 6.33400  0.630 22.72448 ?  257 VAL   A CG2  1 
ATOM   644  N  N    . LEU   A 1 106 ? 17.78400  -11.82800 6.66400  1.000 14.26655 ?  258 LEU   A N    1 
ATOM   645  C  CA   . LEU   A 1 106 ? 18.54000  -10.79800 7.36500  1.000 16.83342 ?  258 LEU   A CA   1 
ATOM   646  C  C    . LEU   A 1 106 ? 17.84800  -9.44700  7.26700  1.000 16.81395 ?  258 LEU   A C    1 
ATOM   647  O  O    . LEU   A 1 106 ? 17.81000  -8.69300  8.24700  1.000 13.97444 ?  258 LEU   A O    1 
ATOM   648  C  CB   . LEU   A 1 106 ? 19.95900  -10.70300 6.80800  1.000 14.49195 ?  258 LEU   A CB   1 
ATOM   649  C  CG   . LEU   A 1 106 ? 20.86100  -11.90600 7.07100  1.000 14.81156 ?  258 LEU   A CG   1 
ATOM   650  C  CD1  . LEU   A 1 106 ? 22.17400  -11.73200 6.30500  1.000 16.27403 ?  258 LEU   A CD1  1 
ATOM   651  C  CD2  . LEU   A 1 106 ? 21.11600  -12.08800 8.56500  1.000 17.66584 ?  258 LEU   A CD2  1 
ATOM   652  N  N    . LEU   A 1 107 ? 17.29000  -9.12200  6.09500  1.000 14.15540 ?  259 LEU   A N    1 
ATOM   653  C  CA   . LEU   A 1 107 ? 16.64300  -7.82200  5.93700  1.000 13.07549 ?  259 LEU   A CA   1 
ATOM   654  C  C    . LEU   A 1 107 ? 15.30100  -7.77600  6.66000  1.000 15.20229 ?  259 LEU   A C    1 
ATOM   655  O  O    . LEU   A 1 107 ? 14.97500  -6.77500  7.30600  1.000 17.30133 ?  259 LEU   A O    1 
ATOM   656  C  CB   . LEU   A 1 107 ? 16.47700  -7.49500  4.45400  1.000 15.34775 ?  259 LEU   A CB   1 
ATOM   657  C  CG   . LEU   A 1 107 ? 17.75600  -6.87100  3.89100  1.000 17.50115 ?  259 LEU   A CG   1 
ATOM   658  C  CD1  . LEU   A 1 107 ? 17.76000  -6.90900  2.38300  1.000 19.91275 ?  259 LEU   A CD1  1 
ATOM   659  C  CD2  . LEU   A 1 107 ? 17.91500  -5.43000  4.40200  1.000 21.52329 ?  259 LEU   A CD2  1 
ATOM   660  N  N    . LYS   A 1 108 ? 14.51400  -8.84800  6.56700  1.000 15.50320 ?  260 LYS   A N    1 
ATOM   661  C  CA   . LYS   A 1 108 ? 13.24700  -8.89600  7.29500  1.000 17.74570 ?  260 LYS   A CA   1 
ATOM   662  C  C    . LYS   A 1 108 ? 13.46800  -8.73600  8.79100  1.000 20.13512 ?  260 LYS   A C    1 
ATOM   663  O  O    . LYS   A 1 108 ? 12.68700  -8.06000  9.47300  1.000 18.34799 ?  260 LYS   A O    1 
ATOM   664  C  CB   . LYS   A 1 108 ? 12.51800  -10.21300 7.01100  1.000 18.64755 ?  260 LYS   A CB   1 
ATOM   665  C  CG   . LYS   A 1 108 ? 11.83600  -10.27300 5.66600  1.000 21.88318 ?  260 LYS   A CG   1 
ATOM   666  C  CD   . LYS   A 1 108 ? 11.13000  -11.61600 5.47700  1.000 26.33071 ?  260 LYS   A CD   1 
ATOM   667  C  CE   . LYS   A 1 108 ? 10.02300  -11.81300 6.50300  1.000 32.49341 ?  260 LYS   A CE   1 
ATOM   668  N  NZ   . LYS   A 1 108 ? 8.85400   -10.90900 6.29300  1.000 29.54324 ?  260 LYS   A NZ   1 
ATOM   669  N  N    A SER   A 1 109 ? 14.53100  -9.34600  9.32600  0.500 16.38581 ?  261 SER   A N    1 
ATOM   670  N  N    B SER   A 1 109 ? 14.52900  -9.34500  9.31900  0.500 16.38242 ?  261 SER   A N    1 
ATOM   671  C  CA   A SER   A 1 109 ? 14.77700  -9.27600  10.76500 0.500 15.83216 ?  261 SER   A CA   1 
ATOM   672  C  CA   B SER   A 1 109 ? 14.77800  -9.27300  10.75300 0.500 15.82725 ?  261 SER   A CA   1 
ATOM   673  C  C    A SER   A 1 109 ? 15.41400  -7.96100  11.19200 0.500 18.90324 ?  261 SER   A C    1 
ATOM   674  C  C    B SER   A 1 109 ? 15.39300  -7.94700  11.17900 0.500 18.83839 ?  261 SER   A C    1 
ATOM   675  O  O    A SER   A 1 109 ? 15.15400  -7.49200  12.30600 0.500 22.15343 ?  261 SER   A O    1 
ATOM   676  O  O    B SER   A 1 109 ? 15.09700  -7.46100  12.27600 0.500 22.13066 ?  261 SER   A O    1 
ATOM   677  C  CB   A SER   A 1 109 ? 15.65700  -10.44500 11.21500 0.500 16.25117 ?  261 SER   A CB   1 
ATOM   678  C  CB   B SER   A 1 109 ? 15.68600  -10.41800 11.18600 0.500 15.98186 ?  261 SER   A CB   1 
ATOM   679  O  OG   A SER   A 1 109 ? 16.90500  -10.44400 10.54800 0.500 18.88105 ?  261 SER   A OG   1 
ATOM   680  O  OG   B SER   A 1 109 ? 15.98900  -10.28900 12.55600 0.500 17.21563 ?  261 SER   A OG   1 
ATOM   681  N  N    . SER   A 1 110 ? 16.24200  -7.35000  10.34400 1.000 14.58112 ?  262 SER   A N    1 
ATOM   682  C  CA   . SER   A 1 110 ? 16.98900  -6.17100  10.76400 1.000 14.22845 ?  262 SER   A CA   1 
ATOM   683  C  C    . SER   A 1 110 ? 16.36400  -4.84500  10.35600 1.000 14.50222 ?  262 SER   A C    1 
ATOM   684  O  O    . SER   A 1 110 ? 16.71400  -3.81900  10.94700 1.000 16.64977 ?  262 SER   A O    1 
ATOM   685  C  CB   . SER   A 1 110 ? 18.41600  -6.21400  10.21200 1.000 15.47495 ?  262 SER   A CB   1 
ATOM   686  O  OG   . SER   A 1 110 ? 18.38200  -6.09600  8.80400  1.000 17.26824 ?  262 SER   A OG   1 
ATOM   687  N  N    . ALA   A 1 111 ? 15.44800  -4.83200  9.38400  1.000 13.68438 ?  263 ALA   A N    1 
ATOM   688  C  CA   . ALA   A 1 111 ? 15.00700  -3.57100  8.79500  1.000 15.42243 ?  263 ALA   A CA   1 
ATOM   689  C  C    . ALA   A 1 111 ? 14.52800  -2.58200  9.85200  1.000 14.52072 ?  263 ALA   A C    1 
ATOM   690  O  O    . ALA   A 1 111 ? 14.92400  -1.41700  9.83200  1.000 14.85297 ?  263 ALA   A O    1 
ATOM   691  C  CB   . ALA   A 1 111 ? 13.91200  -3.82500  7.75000  1.000 16.53856 ?  263 ALA   A CB   1 
ATOM   692  N  N    . ILE   A 1 112 ? 13.67900  -3.02100  10.79300 1.000 14.62503 ?  264 ILE   A N    1 
ATOM   693  C  CA   . ILE   A 1 112 ? 13.18400  -2.07400  11.79900 1.000 17.67243 ?  264 ILE   A CA   1 
ATOM   694  C  C    . ILE   A 1 112 ? 14.33600  -1.52300  12.63000 1.000 18.64300 ?  264 ILE   A C    1 
ATOM   695  O  O    . ILE   A 1 112 ? 14.33200  -0.35000  13.02400 1.000 17.11744 ?  264 ILE   A O    1 
ATOM   696  C  CB   . ILE   A 1 112 ? 12.10800  -2.72500  12.69300 1.000 14.49879 ?  264 ILE   A CB   1 
ATOM   697  C  CG1  . ILE   A 1 112 ? 11.51500  -1.69900  13.66900 1.000 15.62591 ?  264 ILE   A CG1  1 
ATOM   698  C  CG2  . ILE   A 1 112 ? 12.69100  -3.88500  13.50000 1.000 17.31683 ?  264 ILE   A CG2  1 
ATOM   699  C  CD1  . ILE   A 1 112 ? 10.86500  -0.50800  12.99200 1.000 17.52727 ?  264 ILE   A CD1  1 
ATOM   700  N  N    . GLU   A 1 113 ? 15.34900  -2.35300  12.90100 1.000 12.62296 ?  265 GLU   A N    1 
ATOM   701  C  CA   . GLU   A 1 113 ? 16.46900  -1.90100  13.72100 1.000 13.23357 ?  265 GLU   A CA   1 
ATOM   702  C  C    . GLU   A 1 113 ? 17.32000  -0.88200  12.97700 1.000 15.81616 ?  265 GLU   A C    1 
ATOM   703  O  O    . GLU   A 1 113 ? 17.75400  0.11600   13.56400 1.000 15.88266 ?  265 GLU   A O    1 
ATOM   704  C  CB   . GLU   A 1 113 ? 17.33000  -3.08600  14.14100 1.000 17.66744 ?  265 GLU   A CB   1 
ATOM   705  C  CG   . GLU   A 1 113 ? 16.60700  -4.09000  15.00400 1.000 15.76751 ?  265 GLU   A CG   1 
ATOM   706  C  CD   . GLU   A 1 113 ? 17.48200  -5.28400  15.34400 1.000 21.12902 ?  265 GLU   A CD   1 
ATOM   707  O  OE1  . GLU   A 1 113 ? 18.72100  -5.16200  15.25600 1.000 17.09452 ?  265 GLU   A OE1  1 
ATOM   708  O  OE2  . GLU   A 1 113 ? 16.92800  -6.34500  15.69200 1.000 23.78174 ?  265 GLU   A OE2  1 
ATOM   709  N  N    . VAL   A 1 114 ? 17.57900  -1.12700  11.69300 1.000 15.80019 ?  266 VAL   A N    1 
ATOM   710  C  CA   . VAL   A 1 114 ? 18.36400  -0.18200  10.90300 1.000 14.49082 ?  266 VAL   A CA   1 
ATOM   711  C  C    . VAL   A 1 114 ? 17.60100  1.12300   10.72000 1.000 15.15268 ?  266 VAL   A C    1 
ATOM   712  O  O    . VAL   A 1 114 ? 18.20000  2.20500   10.67700 1.000 16.66162 ?  266 VAL   A O    1 
ATOM   713  C  CB   . VAL   A 1 114 ? 18.75100  -0.80300  9.55100  1.000 15.38485 ?  266 VAL   A CB   1 
ATOM   714  C  CG1  . VAL   A 1 114 ? 19.66400  0.14400   8.75600  1.000 14.77453 ?  266 VAL   A CG1  1 
ATOM   715  C  CG2  . VAL   A 1 114 ? 19.41900  -2.14300  9.77100  1.000 15.73261 ?  266 VAL   A CG2  1 
ATOM   716  N  N    . ILE   A 1 115 ? 16.27300  1.04800   10.59100 1.000 12.92562 ?  267 ILE   A N    1 
ATOM   717  C  CA   . ILE   A 1 115 ? 15.48100  2.27400   10.56000 1.000 12.85465 ?  267 ILE   A CA   1 
ATOM   718  C  C    . ILE   A 1 115 ? 15.66200  3.05000   11.85800 1.000 15.12635 ?  267 ILE   A C    1 
ATOM   719  O  O    . ILE   A 1 115 ? 15.90500  4.25900   11.84800 1.000 14.02043 ?  267 ILE   A O    1 
ATOM   720  C  CB   . ILE   A 1 115 ? 13.99900  1.95800   10.28700 1.000 15.31053 ?  267 ILE   A CB   1 
ATOM   721  C  CG1  . ILE   A 1 115 ? 13.82100  1.46400   8.85000  1.000 15.40984 ?  267 ILE   A CG1  1 
ATOM   722  C  CG2  . ILE   A 1 115 ? 13.13800  3.19800   10.54800 1.000 15.37048 ?  267 ILE   A CG2  1 
ATOM   723  C  CD1  . ILE   A 1 115 ? 12.43500  0.87600   8.58200  1.000 15.07164 ?  267 ILE   A CD1  1 
ATOM   724  N  N    . MET   A 1 116 ? 15.56500  2.36400   13.00100 1.000 16.59849 ?  268 MET   A N    1 
ATOM   725  C  CA   . MET   A 1 116 ? 15.76500  3.04900   14.27500 1.000 15.85327 ?  268 MET   A CA   1 
ATOM   726  C  C    . MET   A 1 116 ? 17.15700  3.66800   14.35300 1.000 15.29453 ?  268 MET   A C    1 
ATOM   727  O  O    . MET   A 1 116 ? 17.30800  4.81400   14.79200 1.000 18.62279 ?  268 MET   A O    1 
ATOM   728  C  CB   . MET   A 1 116 ? 15.52800  2.07900   15.43000 1.000 15.25383 ?  268 MET   A CB   1 
ATOM   729  C  CG   . MET   A 1 116 ? 14.07700  1.62300   15.51400 1.000 19.09982 ?  268 MET   A CG   1 
ATOM   730  S  SD   . MET   A 1 116 ? 13.80100  0.44300   16.84500 1.000 20.65989 ?  268 MET   A SD   1 
ATOM   731  C  CE   . MET   A 1 116 ? 12.01500  0.47600   16.94400 1.000 23.14646 ?  268 MET   A CE   1 
ATOM   732  N  N    . LEU   A 1 117 ? 18.17800  2.94300   13.87800 1.000 16.20681 ?  269 LEU   A N    1 
ATOM   733  C  CA   . LEU   A 1 117 ? 19.54900  3.46300   13.89500 1.000 13.81615 ?  269 LEU   A CA   1 
ATOM   734  C  C    . LEU   A 1 117 ? 19.70200  4.65300   12.95800 1.000 16.31189 ?  269 LEU   A C    1 
ATOM   735  O  O    . LEU   A 1 117 ? 20.21900  5.70500   13.35000 1.000 17.45862 ?  269 LEU   A O    1 
ATOM   736  C  CB   . LEU   A 1 117 ? 20.54100  2.37400   13.47400 1.000 17.81865 ?  269 LEU   A CB   1 
ATOM   737  C  CG   . LEU   A 1 117 ? 21.18600  1.39600   14.44600 1.000 26.04210 ?  269 LEU   A CG   1 
ATOM   738  C  CD1  . LEU   A 1 117 ? 22.06300  0.41300   13.67500 1.000 22.19351 ?  269 LEU   A CD1  1 
ATOM   739  C  CD2  . LEU   A 1 117 ? 22.00100  2.11100   15.51900 1.000 29.59520 ?  269 LEU   A CD2  1 
ATOM   740  N  N    . ARG   A 1 118 ? 19.30500  4.48200   11.69500 1.000 15.71511 ?  270 ARG   A N    1 
ATOM   741  C  CA   . ARG   A 1 118 ? 19.52600  5.53200   10.70800 1.000 14.10131 ?  270 ARG   A CA   1 
ATOM   742  C  C    . ARG   A 1 118 ? 18.70200  6.77100   11.02600 1.000 12.87472 ?  270 ARG   A C    1 
ATOM   743  O  O    . ARG   A 1 118 ? 19.12500  7.88400   10.70400 1.000 15.96239 ?  270 ARG   A O    1 
ATOM   744  C  CB   . ARG   A 1 118 ? 19.22400  5.00400   9.29400  1.000 14.41940 ?  270 ARG   A CB   1 
ATOM   745  C  CG   . ARG   A 1 118 ? 17.73200  4.85100   8.95000  1.000 12.29116 ?  270 ARG   A CG   1 
ATOM   746  C  CD   . ARG   A 1 118 ? 17.54300  3.90000   7.75100  1.000 15.03914 ?  270 ARG   A CD   1 
ATOM   747  N  NE   . ARG   A 1 118 ? 18.42700  4.25100   6.63800  1.000 18.46339 ?  270 ARG   A NE   1 
ATOM   748  C  CZ   . ARG   A 1 118 ? 18.12200  5.14000   5.69500  1.000 15.02756 ?  270 ARG   A CZ   1 
ATOM   749  N  NH1  . ARG   A 1 118 ? 16.94400  5.76100   5.72000  1.000 17.32203 ?  270 ARG   A NH1  1 
ATOM   750  N  NH2  . ARG   A 1 118 ? 18.99100  5.41100   4.72300  1.000 15.59519 ?  270 ARG   A NH2  1 
ATOM   751  N  N    . SER   A 1 119 ? 17.54700  6.59300   11.68300 1.000 13.30675 ?  271 SER   A N    1 
ATOM   752  C  CA   . SER   A 1 119 ? 16.72800  7.72900   12.09700 1.000 13.23535 ?  271 SER   A CA   1 
ATOM   753  C  C    . SER   A 1 119 ? 17.46100  8.62900   13.08800 1.000 15.37873 ?  271 SER   A C    1 
ATOM   754  O  O    . SER   A 1 119 ? 17.10800  9.80700   13.22200 1.000 17.78054 ?  271 SER   A O    1 
ATOM   755  C  CB   . SER   A 1 119 ? 15.40800  7.25200   12.69400 1.000 16.48185 ?  271 SER   A CB   1 
ATOM   756  O  OG   . SER   A 1 119 ? 15.56900  6.80100   14.03000 1.000 18.07956 ?  271 SER   A OG   1 
ATOM   757  N  N    . ASN   A 1 120 ? 18.49500  8.11200   13.76400 1.000 15.76093 ?  272 ASN   A N    1 
ATOM   758  C  CA   . ASN   A 1 120 ? 19.20500  8.91100   14.75700 1.000 18.16660 ?  272 ASN   A CA   1 
ATOM   759  C  C    . ASN   A 1 120 ? 19.83800  10.14000  14.12800 1.000 19.46216 ?  272 ASN   A C    1 
ATOM   760  O  O    . ASN   A 1 120 ? 20.02800  11.15400  14.80600 1.000 19.02379 ?  272 ASN   A O    1 
ATOM   761  C  CB   . ASN   A 1 120 ? 20.26200  8.05300   15.44900 1.000 17.20938 ?  272 ASN   A CB   1 
ATOM   762  C  CG   . ASN   A 1 120 ? 20.79800  8.69300   16.72200 1.000 21.93873 ?  272 ASN   A CG   1 
ATOM   763  O  OD1  . ASN   A 1 120 ? 21.96600  9.06700   16.79800 1.000 20.56606 ?  272 ASN   A OD1  1 
ATOM   764  N  ND2  . ASN   A 1 120 ? 19.94500  8.80200   17.73300 1.000 19.59176 ?  272 ASN   A ND2  1 
ATOM   765  N  N    . GLN   A 1 121 ? 20.14800  10.07200  12.83100 1.000 19.07705 ?  273 GLN   A N    1 
ATOM   766  C  CA   . GLN   A 1 121 ? 20.72400  11.21700  12.13500 1.000 21.41127 ?  273 GLN   A CA   1 
ATOM   767  C  C    . GLN   A 1 121 ? 19.78500  12.41600  12.14600 1.000 21.34829 ?  273 GLN   A C    1 
ATOM   768  O  O    . GLN   A 1 121 ? 20.24600  13.56200  12.19600 1.000 23.97803 ?  273 GLN   A O    1 
ATOM   769  C  CB   . GLN   A 1 121 ? 21.08200  10.81500  10.70000 1.000 23.98271 ?  273 GLN   A CB   1 
ATOM   770  C  CG   . GLN   A 1 121 ? 21.90700  11.83900  9.93100  1.000 25.67256 ?  273 GLN   A CG   1 
ATOM   771  C  CD   . GLN   A 1 121 ? 22.59900  11.23900  8.71600  1.000 27.89043 ?  273 GLN   A CD   1 
ATOM   772  O  OE1  . GLN   A 1 121 ? 22.82800  10.02800  8.64700  1.000 25.54273 ?  273 GLN   A OE1  1 
ATOM   773  N  NE2  . GLN   A 1 121 ? 22.94700  12.08900  7.75700  1.000 27.07988 ?  273 GLN   A NE2  1 
ATOM   774  N  N    . SER   A 1 122 ? 18.47100  12.18500  12.10600 1.000 20.95796 ?  274 SER   A N    1 
ATOM   775  C  CA   . SER   A 1 122 ? 17.52300  13.28900  12.18100 1.000 22.05252 ?  274 SER   A CA   1 
ATOM   776  C  C    . SER   A 1 122 ? 17.07800  13.59400  13.60200 1.000 22.57697 ?  274 SER   A C    1 
ATOM   777  O  O    . SER   A 1 122 ? 16.40600  14.60600  13.81300 1.000 24.10906 ?  274 SER   A O    1 
ATOM   778  C  CB   . SER   A 1 122 ? 16.26600  13.01700  11.35700 1.000 21.31755 ?  274 SER   A CB   1 
ATOM   779  O  OG   . SER   A 1 122 ? 15.54000  11.93300  11.90000 1.000 20.17947 ?  274 SER   A OG   1 
ATOM   780  N  N    . PHE   A 1 123 ? 17.40700  12.74100  14.57000 1.000 21.14587 ?  275 PHE   A N    1 
ATOM   781  C  CA   . PHE   A 1 123 ? 16.94400  12.93800  15.93800 1.000 19.27683 ?  275 PHE   A CA   1 
ATOM   782  C  C    . PHE   A 1 123 ? 17.65700  14.12400  16.57400 1.000 22.61891 ?  275 PHE   A C    1 
ATOM   783  O  O    . PHE   A 1 123 ? 18.87400  14.26700  16.44100 1.000 23.10095 ?  275 PHE   A O    1 
ATOM   784  C  CB   . PHE   A 1 123 ? 17.19100  11.66400  16.75000 1.000 20.28656 ?  275 PHE   A CB   1 
ATOM   785  C  CG   . PHE   A 1 123 ? 16.54600  11.67100  18.10700 1.000 22.08414 ?  275 PHE   A CG   1 
ATOM   786  C  CD1  . PHE   A 1 123 ? 15.20600  11.34700  18.25400 1.000 20.40122 ?  275 PHE   A CD1  1 
ATOM   787  C  CD2  . PHE   A 1 123 ? 17.28400  11.99700  19.23400 1.000 27.58520 ?  275 PHE   A CD2  1 
ATOM   788  C  CE1  . PHE   A 1 123 ? 14.61300  11.35700  19.50200 1.000 22.76566 ?  275 PHE   A CE1  1 
ATOM   789  C  CE2  . PHE   A 1 123 ? 16.70000  12.00100  20.48600 1.000 28.30628 ?  275 PHE   A CE2  1 
ATOM   790  C  CZ   . PHE   A 1 123 ? 15.36600  11.68300  20.62200 1.000 26.49212 ?  275 PHE   A CZ   1 
ATOM   791  N  N    . THR   A 1 124 ? 16.90100  14.98000  17.25700 1.000 21.48337 ?  276 THR   A N    1 
ATOM   792  C  CA   . THR   A 1 124 ? 17.46100  16.12700  17.96600 1.000 29.06971 ?  276 THR   A CA   1 
ATOM   793  C  C    . THR   A 1 124 ? 17.16100  16.00300  19.45400 1.000 32.19774 ?  276 THR   A C    1 
ATOM   794  O  O    . THR   A 1 124 ? 16.02000  15.73000  19.84400 1.000 30.95906 ?  276 THR   A O    1 
ATOM   795  C  CB   . THR   A 1 124 ? 16.90500  17.45200  17.42500 1.000 35.58989 ?  276 THR   A CB   1 
ATOM   796  O  OG1  . THR   A 1 124 ? 17.26300  18.52000  18.30900 1.000 45.41466 ?  276 THR   A OG1  1 
ATOM   797  C  CG2  . THR   A 1 124 ? 15.39600  17.40300  17.30900 1.000 35.68466 ?  276 THR   A CG2  1 
ATOM   798  N  N    . MET   A 1 125 ? 18.18100  16.21800  20.28500 1.000 36.75833 ?  277 MET   A N    1 
ATOM   799  C  CA   . MET   A 1 125 ? 17.98300  16.09300  21.72200 1.000 33.81974 ?  277 MET   A CA   1 
ATOM   800  C  C    . MET   A 1 125 ? 17.31800  17.31400  22.34100 1.000 35.69546 ?  277 MET   A C    1 
ATOM   801  O  O    . MET   A 1 125 ? 16.93100  17.26300  23.51300 1.000 43.02662 ?  277 MET   A O    1 
ATOM   802  C  CB   . MET   A 1 125 ? 19.31600  15.80300  22.41900 1.000 30.56670 ?  277 MET   A CB   1 
ATOM   803  C  CG   . MET   A 1 125 ? 19.60700  14.29800  22.49900 1.000 31.75817 ?  277 MET   A CG   1 
ATOM   804  S  SD   . MET   A 1 125 ? 21.17600  13.90000  23.27400 1.000 47.38894 ?  277 MET   A SD   1 
ATOM   805  C  CE   . MET   A 1 125 ? 22.25400  15.09800  22.49100 1.000 49.07471 ?  277 MET   A CE   1 
ATOM   806  N  N    . ASP   A 1 126 ? 17.14800  18.39300  21.57900 1.000 35.46931 ?  278 ASP   A N    1 
ATOM   807  C  CA   . ASP   A 1 126 ? 16.54400  19.60500  22.11500 1.000 39.06002 ?  278 ASP   A CA   1 
ATOM   808  C  C    . ASP   A 1 126 ? 15.05800  19.45100  22.40600 1.000 38.81704 ?  278 ASP   A C    1 
ATOM   809  O  O    . ASP   A 1 126 ? 14.53000  20.17700  23.25100 1.000 42.20077 ?  278 ASP   A O    1 
ATOM   810  C  CB   . ASP   A 1 126 ? 16.78200  20.75000  21.14300 1.000 42.30390 ?  278 ASP   A CB   1 
ATOM   811  C  CG   . ASP   A 1 126 ? 18.23400  20.87100  20.77300 1.000 48.64123 ?  278 ASP   A CG   1 
ATOM   812  O  OD1  . ASP   A 1 126 ? 19.05200  21.07400  21.70300 1.000 39.29276 ?  278 ASP   A OD1  1 
ATOM   813  O  OD2  . ASP   A 1 126 ? 18.56400  20.75000  19.57200 1.000 49.85331 ?  278 ASP   A OD2  1 
ATOM   814  N  N    . ASP   A 1 127 ? 14.37000  18.53200  21.72500 1.000 35.71741 ?  279 ASP   A N    1 
ATOM   815  C  CA   . ASP   A 1 127 ? 12.98400  18.26200  22.09100 1.000 37.59296 ?  279 ASP   A CA   1 
ATOM   816  C  C    . ASP   A 1 127 ? 12.59500  16.81100  21.83000 1.000 33.83191 ?  279 ASP   A C    1 
ATOM   817  O  O    . ASP   A 1 127 ? 11.39900  16.52600  21.68500 1.000 34.96555 ?  279 ASP   A O    1 
ATOM   818  C  CB   . ASP   A 1 127 ? 12.02900  19.19400  21.34800 1.000 42.55092 ?  279 ASP   A CB   1 
ATOM   819  C  CG   . ASP   A 1 127 ? 12.20800  19.13400  19.85000 1.000 44.93566 ?  279 ASP   A CG   1 
ATOM   820  O  OD1  . ASP   A 1 127 ? 11.42200  19.79000  19.13600 1.000 49.02704 ?  279 ASP   A OD1  1 
ATOM   821  O  OD2  . ASP   A 1 127 ? 13.13200  18.43500  19.38700 1.000 43.95593 ?  279 ASP   A OD2  1 
ATOM   822  N  N    . MET   A 1 128 ? 13.56500  15.89800  21.75000 1.000 29.87525 ?  280 MET   A N    1 
ATOM   823  C  CA   . MET   A 1 128 ? 13.29700  14.46500  21.66800 1.000 25.84883 ?  280 MET   A CA   1 
ATOM   824  C  C    . MET   A 1 128 ? 12.41000  14.14500  20.47100 1.000 24.75365 ?  280 MET   A C    1 
ATOM   825  O  O    . MET   A 1 128 ? 11.37600  13.48400  20.59500 1.000 27.95123 ?  280 MET   A O    1 
ATOM   826  C  CB   . MET   A 1 128 ? 12.65600  13.94900  22.96000 1.000 30.02909 ?  280 MET   A CB   1 
ATOM   827  C  CG   . MET   A 1 128 ? 13.40000  14.29000  24.22400 1.000 39.49482 ?  280 MET   A CG   1 
ATOM   828  S  SD   . MET   A 1 128 ? 14.82300  13.22300  24.42200 1.000 46.05355 ?  280 MET   A SD   1 
ATOM   829  C  CE   . MET   A 1 128 ? 16.13100  14.30100  23.91900 1.000 49.31157 ?  280 MET   A CE   1 
ATOM   830  N  N    . SER   A 1 129 ? 12.81600  14.63400  19.30100 1.000 23.42538 ?  281 SER   A N    1 
ATOM   831  C  CA   . SER   A 1 129 ? 12.02400  14.47200  18.09200 1.000 21.84438 ?  281 SER   A CA   1 
ATOM   832  C  C    . SER   A 1 129 ? 12.93700  14.15700  16.92000 1.000 20.91402 ?  281 SER   A C    1 
ATOM   833  O  O    . SER   A 1 129 ? 14.14300  14.41300  16.95300 1.000 21.30260 ?  281 SER   A O    1 
ATOM   834  C  CB   . SER   A 1 129 ? 11.21200  15.73300  17.78200 1.000 31.61043 ?  281 SER   A CB   1 
ATOM   835  O  OG   . SER   A 1 129 ? 12.07100  16.75400  17.30900 1.000 39.76750 ?  281 SER   A OG   1 
ATOM   836  N  N    . TRP   A 1 130 ? 12.33400  13.61300  15.86800 1.000 20.46135 ?  282 TRP   A N    1 
ATOM   837  C  CA   . TRP   A 1 130 ? 13.02500  13.35900  14.60800 1.000 22.00616 ?  282 TRP   A CA   1 
ATOM   838  C  C    . TRP   A 1 130 ? 12.68100  14.49600  13.65100 1.000 24.43618 ?  282 TRP   A C    1 
ATOM   839  O  O    . TRP   A 1 130 ? 11.55400  14.57800  13.15200 1.000 22.23186 ?  282 TRP   A O    1 
ATOM   840  C  CB   . TRP   A 1 130 ? 12.62300  12.00900  14.02100 1.000 17.80930 ?  282 TRP   A CB   1 
ATOM   841  C  CG   . TRP   A 1 130 ? 13.04800  10.80300  14.81200 1.000 20.82251 ?  282 TRP   A CG   1 
ATOM   842  C  CD1  . TRP   A 1 130 ? 14.16000  10.03900  14.60300 1.000 19.45290 ?  282 TRP   A CD1  1 
ATOM   843  C  CD2  . TRP   A 1 130 ? 12.34800  10.19700  15.90600 1.000 18.65916 ?  282 TRP   A CD2  1 
ATOM   844  N  NE1  . TRP   A 1 130 ? 14.20500  9.00500   15.50300 1.000 20.46416 ?  282 TRP   A NE1  1 
ATOM   845  C  CE2  . TRP   A 1 130 ? 13.10300  9.07500   16.31400 1.000 18.44481 ?  282 TRP   A CE2  1 
ATOM   846  C  CE3  . TRP   A 1 130 ? 11.16100  10.49900  16.58600 1.000 18.85662 ?  282 TRP   A CE3  1 
ATOM   847  C  CZ2  . TRP   A 1 130 ? 12.71500  8.25300   17.36400 1.000 18.87337 ?  282 TRP   A CZ2  1 
ATOM   848  C  CZ3  . TRP   A 1 130 ? 10.77600  9.68200   17.63800 1.000 22.41452 ?  282 TRP   A CZ3  1 
ATOM   849  C  CH2  . TRP   A 1 130 ? 11.55100  8.57100   18.01800 1.000 20.64896 ?  282 TRP   A CH2  1 
ATOM   850  N  N    . ASP   A 1 131 ? 13.65700  15.36200  13.39300 1.000 22.03361 ?  283 ASP   A N    1 
ATOM   851  C  CA   . ASP   A 1 131 ? 13.46400  16.58400  12.61500 1.000 20.27355 ?  283 ASP   A CA   1 
ATOM   852  C  C    . ASP   A 1 131 ? 13.92100  16.32100  11.18500 1.000 21.68359 ?  283 ASP   A C    1 
ATOM   853  O  O    . ASP   A 1 131 ? 15.11700  16.35200  10.88500 1.000 28.85614 ?  283 ASP   A O    1 
ATOM   854  C  CB   . ASP   A 1 131 ? 14.23600  17.73800  13.24700 1.000 24.88405 ?  283 ASP   A CB   1 
ATOM   855  C  CG   . ASP   A 1 131 ? 13.95800  19.07100  12.58100 1.000 32.06144 ?  283 ASP   A CG   1 
ATOM   856  O  OD1  . ASP   A 1 131 ? 13.27300  19.11100  11.53600 1.000 32.17642 ?  283 ASP   A OD1  1 
ATOM   857  O  OD2  . ASP   A 1 131 ? 14.44000  20.09400  13.11500 1.000 35.68051 ?  283 ASP   A OD2  1 
ATOM   858  N  N    . CYS   A 1 132 ? 12.96300  16.08000  10.29900 1.000 18.71661 ?  284 CYS   A N    1 
ATOM   859  C  CA   . CYS   A 1 132 ? 13.26000  15.79900  8.89600  1.000 22.17166 ?  284 CYS   A CA   1 
ATOM   860  C  C    . CYS   A 1 132 ? 12.99600  17.00800  7.99500  1.000 27.63891 ?  284 CYS   A C    1 
ATOM   861  O  O    . CYS   A 1 132 ? 12.32900  16.90600  6.96600  1.000 26.33625 ?  284 CYS   A O    1 
ATOM   862  C  CB   . CYS   A 1 132 ? 12.46300  14.58300  8.44200  1.000 22.08785 ?  284 CYS   A CB   1 
ATOM   863  S  SG   . CYS   A 1 132 ? 12.92700  13.08800  9.29200  1.000 21.39108 ?  284 CYS   A SG   1 
ATOM   864  N  N    . GLY   A 1 133 ? 13.51700  18.17800  8.37200  1.000 33.38056 ?  285 GLY   A N    1 
ATOM   865  C  CA   . GLY   A 1 133 ? 13.62100  19.31300  7.47300  1.000 35.72614 ?  285 GLY   A CA   1 
ATOM   866  C  C    . GLY   A 1 133 ? 12.54300  20.37500  7.60700  1.000 37.60841 ?  285 GLY   A C    1 
ATOM   867  O  O    . GLY   A 1 133 ? 12.75400  21.50700  7.15100  1.000 38.33073 ?  285 GLY   A O    1 
ATOM   868  N  N    . SER   A 1 134 ? 11.39700  20.05300  8.20000  1.000 38.86137 ?  286 SER   A N    1 
ATOM   869  C  CA   . SER   A 1 134 ? 10.33300  21.04100  8.32600  1.000 39.29353 ?  286 SER   A CA   1 
ATOM   870  C  C    . SER   A 1 134 ? 9.42100   20.64300  9.47400  1.000 35.03109 ?  286 SER   A C    1 
ATOM   871  O  O    . SER   A 1 134 ? 9.47400   19.51600  9.96800  1.000 32.44021 ?  286 SER   A O    1 
ATOM   872  C  CB   . SER   A 1 134 ? 9.53000   21.17800  7.03000  1.000 46.39939 ?  286 SER   A CB   1 
ATOM   873  O  OG   . SER   A 1 134 ? 9.16400   19.90700  6.53300  1.000 50.36462 ?  286 SER   A OG   1 
ATOM   874  N  N    . GLN   A 1 135 ? 8.58100   21.59300  9.89400  1.000 35.70987 ?  287 GLN   A N    1 
ATOM   875  C  CA   . GLN   A 1 135 ? 7.65400   21.32200  10.98900 1.000 36.20575 ?  287 GLN   A CA   1 
ATOM   876  C  C    . GLN   A 1 135 ? 6.71000   20.17900  10.64000 1.000 32.32146 ?  287 GLN   A C    1 
ATOM   877  O  O    . GLN   A 1 135 ? 6.44600   19.30600  11.47600 1.000 34.20374 ?  287 GLN   A O    1 
ATOM   878  C  CB   . GLN   A 1 135 ? 6.86500   22.58400  11.33400 1.000 42.62649 ?  287 GLN   A CB   1 
ATOM   879  C  CG   . GLN   A 1 135 ? 6.26800   22.57200  12.72800 1.000 49.91454 ?  287 GLN   A CG   1 
ATOM   880  C  CD   . GLN   A 1 135 ? 7.29700   22.27300  13.80500 1.000 53.90470 ?  287 GLN   A CD   1 
ATOM   881  O  OE1  . GLN   A 1 135 ? 8.43400   22.74200  13.74600 1.000 54.24121 ?  287 GLN   A OE1  1 
ATOM   882  N  NE2  . GLN   A 1 135 ? 6.89900   21.48600  14.79700 1.000 54.57584 ?  287 GLN   A NE2  1 
ATOM   883  N  N    . ASP   A 1 136 ? 6.18800   20.17300  9.41000  1.000 29.74320 ?  288 ASP   A N    1 
ATOM   884  C  CA   . ASP   A 1 136 ? 5.30900   19.08800  8.97600  1.000 29.65755 ?  288 ASP   A CA   1 
ATOM   885  C  C    . ASP   A 1 136 ? 5.97000   17.72800  9.14100  1.000 25.39227 ?  288 ASP   A C    1 
ATOM   886  O  O    . ASP   A 1 136 ? 5.29100   16.74000  9.44800  1.000 25.65783 ?  288 ASP   A O    1 
ATOM   887  C  CB   . ASP   A 1 136 ? 4.90700   19.27700  7.51400  1.000 33.11934 ?  288 ASP   A CB   1 
ATOM   888  C  CG   . ASP   A 1 136 ? 3.98300   20.45600  7.30400  1.000 47.80232 ?  288 ASP   A CG   1 
ATOM   889  O  OD1  . ASP   A 1 136 ? 3.07000   20.66100  8.13200  1.000 52.78908 ?  288 ASP   A OD1  1 
ATOM   890  O  OD2  . ASP   A 1 136 ? 4.16900   21.17300  6.29700  1.000 53.47277 ?  288 ASP   A OD2  1 
ATOM   891  N  N    . TYR   A 1 137 ? 7.28100   17.65300  8.93000  1.000 22.96407 ?  289 TYR   A N    1 
ATOM   892  C  CA   . TYR   A 1 137 ? 8.02200   16.39900  8.96300  1.000 21.34122 ?  289 TYR   A CA   1 
ATOM   893  C  C    . TYR   A 1 137 ? 8.94000   16.34000  10.17800 1.000 23.53893 ?  289 TYR   A C    1 
ATOM   894  O  O    . TYR   A 1 137 ? 10.06700  15.85500  10.11100 1.000 24.21215 ?  289 TYR   A O    1 
ATOM   895  C  CB   . TYR   A 1 137 ? 8.80600   16.20600  7.67000  1.000 23.50958 ?  289 TYR   A CB   1 
ATOM   896  C  CG   . TYR   A 1 137 ? 7.95100   16.43400  6.44800  1.000 24.30820 ?  289 TYR   A CG   1 
ATOM   897  C  CD1  . TYR   A 1 137 ? 8.41900   17.18700  5.37700  1.000 31.31077 ?  289 TYR   A CD1  1 
ATOM   898  C  CD2  . TYR   A 1 137 ? 6.66500   15.91100  6.37000  1.000 22.42612 ?  289 TYR   A CD2  1 
ATOM   899  C  CE1  . TYR   A 1 137 ? 7.63400   17.40700  4.26300  1.000 31.71452 ?  289 TYR   A CE1  1 
ATOM   900  C  CE2  . TYR   A 1 137 ? 5.87000   16.13100  5.25500  1.000 23.82316 ?  289 TYR   A CE2  1 
ATOM   901  C  CZ   . TYR   A 1 137 ? 6.35900   16.87800  4.20700  1.000 30.46593 ?  289 TYR   A CZ   1 
ATOM   902  O  OH   . TYR   A 1 137 ? 5.56900   17.10200  3.09800  1.000 29.44961 ?  289 TYR   A OH   1 
ATOM   903  N  N    . LYS   A 1 138 ? 8.45700   16.84900  11.30300 1.000 25.07442 ?  290 LYS   A N    1 
ATOM   904  C  CA   . LYS   A 1 138 ? 9.13700   16.72800  12.58400 1.000 24.20584 ?  290 LYS   A CA   1 
ATOM   905  C  C    . LYS   A 1 138 ? 8.25500   15.86900  13.48100 1.000 24.39113 ?  290 LYS   A C    1 
ATOM   906  O  O    . LYS   A 1 138 ? 7.10800   16.23400  13.75600 1.000 27.16008 ?  290 LYS   A O    1 
ATOM   907  C  CB   . LYS   A 1 138 ? 9.38500   18.10700  13.19300 1.000 25.68850 ?  290 LYS   A CB   1 
ATOM   908  C  CG   . LYS   A 1 138 ? 10.13000  18.08700  14.50700 1.000 29.12279 ?  290 LYS   A CG   1 
ATOM   909  C  CD   . LYS   A 1 138 ? 9.92300   19.40500  15.24200 1.000 41.34279 ?  290 LYS   A CD   1 
ATOM   910  C  CE   . LYS   A 1 138 ? 11.18600  20.23800  15.24000 1.000 49.15406 ?  290 LYS   A CE   1 
ATOM   911  N  NZ   . LYS   A 1 138 ? 12.16200  19.74700  16.24900 1.000 53.65438 ?  290 LYS   A NZ   1 
ATOM   912  N  N    . TYR   A 1 139 ? 8.76800   14.71300  13.89000 1.000 23.01195 ?  291 TYR   A N    1 
ATOM   913  C  CA   . TYR   A 1 139 ? 7.96800   13.69300  14.55800 1.000 22.99656 ?  291 TYR   A CA   1 
ATOM   914  C  C    . TYR   A 1 139 ? 8.35900   13.60600  16.02400 1.000 24.53414 ?  291 TYR   A C    1 
ATOM   915  O  O    . TYR   A 1 139 ? 9.53000   13.37100  16.34500 1.000 24.19752 ?  291 TYR   A O    1 
ATOM   916  C  CB   . TYR   A 1 139 ? 8.14500   12.34400  13.86500 1.000 22.86551 ?  291 TYR   A CB   1 
ATOM   917  C  CG   . TYR   A 1 139 ? 8.06200   12.48100  12.36400 1.000 20.61225 ?  291 TYR   A CG   1 
ATOM   918  C  CD1  . TYR   A 1 139 ? 9.18900   12.31500  11.56300 1.000 20.93647 ?  291 TYR   A CD1  1 
ATOM   919  C  CD2  . TYR   A 1 139 ? 6.86500   12.82200  11.75200 1.000 20.13547 ?  291 TYR   A CD2  1 
ATOM   920  C  CE1  . TYR   A 1 139 ? 9.11400   12.46000  10.17900 1.000 22.36626 ?  291 TYR   A CE1  1 
ATOM   921  C  CE2  . TYR   A 1 139 ? 6.77800   12.97100  10.37400 1.000 21.58616 ?  291 TYR   A CE2  1 
ATOM   922  C  CZ   . TYR   A 1 139 ? 7.90500   12.78800  9.59500  1.000 23.18731 ?  291 TYR   A CZ   1 
ATOM   923  O  OH   . TYR   A 1 139 ? 7.82000   12.94000  8.22900  1.000 20.00607 ?  291 TYR   A OH   1 
ATOM   924  N  N    . ASP   A 1 140 ? 7.38100   13.78500  16.90600 1.000 24.88662 ?  292 ASP   A N    1 
ATOM   925  C  CA   . ASP   A 1 140 ? 7.60700   13.65100  18.33500 1.000 26.76468 ?  292 ASP   A CA   1 
ATOM   926  C  C    . ASP   A 1 140 ? 6.91400   12.38700  18.83800 1.000 25.08257 ?  292 ASP   A C    1 
ATOM   927  O  O    . ASP   A 1 140 ? 6.38300   11.58700  18.05600 1.000 24.71543 ?  292 ASP   A O    1 
ATOM   928  C  CB   . ASP   A 1 140 ? 7.14000   14.91200  19.07400 1.000 26.26115 ?  292 ASP   A CB   1 
ATOM   929  C  CG   . ASP   A 1 140 ? 5.66200   15.20800  18.87600 1.000 32.68595 ?  292 ASP   A CG   1 
ATOM   930  O  OD1  . ASP   A 1 140 ? 5.23300   16.31700  19.25900 1.000 34.81718 ?  292 ASP   A OD1  1 
ATOM   931  O  OD2  . ASP   A 1 140 ? 4.92500   14.35200  18.35100 1.000 30.11719 ?  292 ASP   A OD2  1 
ATOM   932  N  N    . VAL   A 1 141 ? 6.91500   12.20600  20.16000 1.000 26.75259 ?  293 VAL   A N    1 
ATOM   933  C  CA   . VAL   A 1 141 ? 6.36200   10.97900  20.72300 1.000 28.53517 ?  293 VAL   A CA   1 
ATOM   934  C  C    . VAL   A 1 141 ? 4.86900   10.88400  20.45500 1.000 24.37807 ?  293 VAL   A C    1 
ATOM   935  O  O    . VAL   A 1 141 ? 4.34200   9.78600   20.24900 1.000 25.56215 ?  293 VAL   A O    1 
ATOM   936  C  CB   . VAL   A 1 141 ? 6.68000   10.89300  22.22600 1.000 25.99019 ?  293 VAL   A CB   1 
ATOM   937  C  CG1  . VAL   A 1 141 ? 8.17600   10.78200  22.42200 1.000 29.54913 ?  293 VAL   A CG1  1 
ATOM   938  C  CG2  . VAL   A 1 141 ? 6.14100   12.10600  22.95500 1.000 28.99946 ?  293 VAL   A CG2  1 
ATOM   939  N  N    . THR   A 1 142 ? 4.17100   12.02300  20.43500 1.000 25.50164 ?  294 THR   A N    1 
ATOM   940  C  CA   . THR   A 1 142 ? 2.74600   12.01600  20.12000 1.000 23.37204 ?  294 THR   A CA   1 
ATOM   941  C  C    . THR   A 1 142 ? 2.50000   11.49900  18.71000 1.000 25.53102 ?  294 THR   A C    1 
ATOM   942  O  O    . THR   A 1 142 ? 1.59900   10.68300  18.49100 1.000 25.68424 ?  294 THR   A O    1 
ATOM   943  C  CB   . THR   A 1 142 ? 2.16600   13.42200  20.28900 1.000 27.00479 ?  294 THR   A CB   1 
ATOM   944  O  OG1  . THR   A 1 142 ? 2.30400   13.82900  21.65700 1.000 32.98536 ?  294 THR   A OG1  1 
ATOM   945  C  CG2  . THR   A 1 142 ? 0.69400   13.45200  19.90400 1.000 33.13539 ?  294 THR   A CG2  1 
ATOM   946  N  N    . ASP   A 1 143 ? 3.30000   11.95500  17.74200 1.000 26.82461 ?  295 ASP   A N    1 
ATOM   947  C  CA   . ASP   A 1 143 ? 3.14700   11.48100  16.36800 1.000 20.83743 ?  295 ASP   A CA   1 
ATOM   948  C  C    . ASP   A 1 143 ? 3.32800   9.97100   16.27400 1.000 21.62265 ?  295 ASP   A C    1 
ATOM   949  O  O    . ASP   A 1 143 ? 2.59000   9.29300   15.55200 1.000 20.22366 ?  295 ASP   A O    1 
ATOM   950  C  CB   . ASP   A 1 143 ? 4.14200   12.19100  15.45000 1.000 22.86051 ?  295 ASP   A CB   1 
ATOM   951  C  CG   . ASP   A 1 143 ? 3.81600   13.65200  15.26000 1.000 29.66671 ?  295 ASP   A CG   1 
ATOM   952  O  OD1  . ASP   A 1 143 ? 2.62200   14.00300  15.32300 1.000 30.44741 ?  295 ASP   A OD1  1 
ATOM   953  O  OD2  . ASP   A 1 143 ? 4.75100   14.44900  15.04600 1.000 29.78352 ?  295 ASP   A OD2  1 
ATOM   954  N  N    . VAL   A 1 144 ? 4.31000   9.42200   16.99100 1.000 20.58149 ?  296 VAL   A N    1 
ATOM   955  C  CA   . VAL   A 1 144 ? 4.52100   7.98100   16.94000 1.000 17.91743 ?  296 VAL   A CA   1 
ATOM   956  C  C    . VAL   A 1 144 ? 3.34600   7.25000   17.57400 1.000 17.73871 ?  296 VAL   A C    1 
ATOM   957  O  O    . VAL   A 1 144 ? 2.89900   6.21300   17.06900 1.000 20.87639 ?  296 VAL   A O    1 
ATOM   958  C  CB   . VAL   A 1 144 ? 5.85800   7.60200   17.60300 1.000 20.67245 ?  296 VAL   A CB   1 
ATOM   959  C  CG1  . VAL   A 1 144 ? 6.06400   6.09100   17.53900 1.000 19.44787 ?  296 VAL   A CG1  1 
ATOM   960  C  CG2  . VAL   A 1 144 ? 7.00700   8.32200   16.90100 1.000 20.33820 ?  296 VAL   A CG2  1 
ATOM   961  N  N    . SER   A 1 145 ? 2.80800   7.79200   18.67200 1.000 19.23716 ?  297 SER   A N    1 
ATOM   962  C  CA   . SER   A 1 145 ? 1.62000   7.19300   19.27100 1.000 22.46285 ?  297 SER   A CA   1 
ATOM   963  C  C    . SER   A 1 145 ? 0.42900   7.26100   18.32100 1.000 24.54290 ?  297 SER   A C    1 
ATOM   964  O  O    . SER   A 1 145 ? -0.45000  6.39400   18.36600 1.000 23.13710 ?  297 SER   A O    1 
ATOM   965  C  CB   . SER   A 1 145 ? 1.29900   7.87200   20.60600 1.000 25.86266 ?  297 SER   A CB   1 
ATOM   966  O  OG   . SER   A 1 145 ? 0.61300   9.10000   20.42700 1.000 29.39559 ?  297 SER   A OG   1 
ATOM   967  N  N    . LYS   A 1 146 ? 0.39700   8.26700   17.44700 1.000 21.20671 ?  298 LYS   A N    1 
ATOM   968  C  CA   . LYS   A 1 146 ? -0.67200  8.42000   16.46700 1.000 24.43140 ?  298 LYS   A CA   1 
ATOM   969  C  C    . LYS   A 1 146 ? -0.49700  7.51000   15.25900 1.000 21.28477 ?  298 LYS   A C    1 
ATOM   970  O  O    . LYS   A 1 146 ? -1.27700  7.61400   14.30200 1.000 23.49610 ?  298 LYS   A O    1 
ATOM   971  C  CB   . LYS   A 1 146 ? -0.76400  9.87500   16.00900 1.000 24.82726 ?  298 LYS   A CB   1 
ATOM   972  C  CG   . LYS   A 1 146 ? -1.26500  10.83600  17.08200 1.000 32.32903 ?  298 LYS   A CG   1 
ATOM   973  C  CD   . LYS   A 1 146 ? -2.56800  10.35700  17.68800 1.000 40.17257 ?  298 LYS   A CD   1 
ATOM   974  C  CE   . LYS   A 1 146 ? -3.22500  11.45200  18.52000 1.000 45.05874 ?  298 LYS   A CE   1 
ATOM   975  N  NZ   . LYS   A 1 146 ? -4.60600  11.07700  18.93900 1.000 45.79321 ?  298 LYS   A NZ   1 
ATOM   976  N  N    . ALA   A 1 147 ? 0.50900   6.64300   15.27000 1.000 20.46462 ?  299 ALA   A N    1 
ATOM   977  C  CA   . ALA   A 1 147 ? 0.56800   5.51700   14.35300 1.000 22.97240 ?  299 ALA   A CA   1 
ATOM   978  C  C    . ALA   A 1 147 ? 0.17100   4.21900   15.03200 1.000 22.34366 ?  299 ALA   A C    1 
ATOM   979  O  O    . ALA   A 1 147 ? 0.23700   3.15800   14.40300 1.000 23.34852 ?  299 ALA   A O    1 
ATOM   980  C  CB   . ALA   A 1 147 ? 1.97000   5.38800   13.74800 1.000 23.73362 ?  299 ALA   A CB   1 
ATOM   981  N  N    . GLY   A 1 148 ? -0.24200  4.28300   16.30000 1.000 20.41377 ?  300 GLY   A N    1 
ATOM   982  C  CA   . GLY   A 1 148 ? -0.71800  3.13200   17.04000 1.000 24.27341 ?  300 GLY   A CA   1 
ATOM   983  C  C    . GLY   A 1 148 ? 0.20900   2.65200   18.13100 1.000 23.99243 ?  300 GLY   A C    1 
ATOM   984  O  O    . GLY   A 1 148 ? -0.16600  1.74300   18.88200 1.000 24.77921 ?  300 GLY   A O    1 
ATOM   985  N  N    . HIS   A 1 149 ? 1.39900   3.21800   18.25400 1.000 20.41508 ?  301 HIS   A N    1 
ATOM   986  C  CA   . HIS   A 1 149 ? 2.33500   2.66900   19.21600 1.000 18.51598 ?  301 HIS   A CA   1 
ATOM   987  C  C    . HIS   A 1 149 ? 2.13400   3.29900   20.58800 1.000 21.82441 ?  301 HIS   A C    1 
ATOM   988  O  O    . HIS   A 1 149 ? 1.55200   4.37500   20.73300 1.000 23.81872 ?  301 HIS   A O    1 
ATOM   989  C  CB   . HIS   A 1 149 ? 3.76300   2.84400   18.70900 1.000 19.34134 ?  301 HIS   A CB   1 
ATOM   990  C  CG   . HIS   A 1 149 ? 4.08600   1.91700   17.58200 1.000 17.90412 ?  301 HIS   A CG   1 
ATOM   991  N  ND1  . HIS   A 1 149 ? 4.11200   0.54800   17.73600 1.000 19.37308 ?  301 HIS   A ND1  1 
ATOM   992  C  CD2  . HIS   A 1 149 ? 4.35000   2.15500   16.27600 1.000 19.02907 ?  301 HIS   A CD2  1 
ATOM   993  C  CE1  . HIS   A 1 149 ? 4.39400   -0.01900  16.57600 1.000 18.39614 ?  301 HIS   A CE1  1 
ATOM   994  N  NE2  . HIS   A 1 149 ? 4.54600   0.93600   15.67300 1.000 18.53502 ?  301 HIS   A NE2  1 
ATOM   995  N  N    . THR   A 1 150 ? 2.57800   2.57400   21.60500 1.000 21.20028 ?  302 THR   A N    1 
ATOM   996  C  CA   . THR   A 1 150 ? 2.37000   2.91900   23.00000 1.000 23.58027 ?  302 THR   A CA   1 
ATOM   997  C  C    . THR   A 1 150 ? 3.70000   3.27200   23.64600 1.000 22.87987 ?  302 THR   A C    1 
ATOM   998  O  O    . THR   A 1 150 ? 4.76900   3.12400   23.04800 1.000 25.86492 ?  302 THR   A O    1 
ATOM   999  C  CB   . THR   A 1 150 ? 1.71900   1.74900   23.74100 1.000 27.39937 ?  302 THR   A CB   1 
ATOM   1000 O  OG1  . THR   A 1 150 ? 2.64500   0.65700   23.78000 1.000 27.43177 ?  302 THR   A OG1  1 
ATOM   1001 C  CG2  . THR   A 1 150 ? 0.45900   1.30400   23.01900 1.000 30.86456 ?  302 THR   A CG2  1 
ATOM   1002 N  N    . LEU   A 1 151 ? 3.62200   3.73500   24.89500 1.000 23.74055 ?  303 LEU   A N    1 
ATOM   1003 C  CA   . LEU   A 1 151 ? 4.83600   4.11400   25.60800 1.000 25.90344 ?  303 LEU   A CA   1 
ATOM   1004 C  C    . LEU   A 1 151 ? 5.76400   2.93100   25.84500 1.000 28.78098 ?  303 LEU   A C    1 
ATOM   1005 O  O    . LEU   A 1 151 ? 6.97200   3.13800   25.99900 1.000 28.26991 ?  303 LEU   A O    1 
ATOM   1006 C  CB   . LEU   A 1 151 ? 4.48000   4.79000   26.93500 1.000 30.13577 ?  303 LEU   A CB   1 
ATOM   1007 C  CG   . LEU   A 1 151 ? 3.92100   6.20700   26.75700 1.000 37.45874 ?  303 LEU   A CG   1 
ATOM   1008 C  CD1  . LEU   A 1 151 ? 3.47800   6.79700   28.07900 1.000 39.03136 ?  303 LEU   A CD1  1 
ATOM   1009 C  CD2  . LEU   A 1 151 ? 4.93200   7.12000   26.07500 1.000 41.11813 ?  303 LEU   A CD2  1 
ATOM   1010 N  N    . GLU   A 1 152 ? 5.24000   1.69800   25.85900 1.000 27.28764 ?  304 GLU   A N    1 
ATOM   1011 C  CA   . GLU   A 1 152 ? 6.10100   0.53300   26.04500 1.000 29.55254 ?  304 GLU   A CA   1 
ATOM   1012 C  C    . GLU   A 1 152 ? 7.15100   0.42200   24.94700 1.000 27.89454 ?  304 GLU   A C    1 
ATOM   1013 O  O    . GLU   A 1 152 ? 8.22900   -0.13300  25.18400 1.000 27.30643 ?  304 GLU   A O    1 
ATOM   1014 C  CB   . GLU   A 1 152 ? 5.26600   -0.74400  26.10600 1.000 37.44684 ?  304 GLU   A CB   1 
ATOM   1015 C  CG   . GLU   A 1 152 ? 6.03800   -1.98300  26.54200 1.000 53.61533 ?  304 GLU   A CG   1 
ATOM   1016 C  CD   . GLU   A 1 152 ? 6.11700   -2.13600  28.05600 1.000 66.15071 ?  304 GLU   A CD   1 
ATOM   1017 O  OE1  . GLU   A 1 152 ? 6.74400   -3.11600  28.51600 1.000 70.61690 ?  304 GLU   A OE1  1 
ATOM   1018 O  OE2  . GLU   A 1 152 ? 5.55400   -1.28400  28.77900 1.000 68.88992 ?  304 GLU   A OE2  1 
ATOM   1019 N  N    . LEU   A 1 153 ? 6.86300   0.93300   23.75100 1.000 20.61769 ?  305 LEU   A N    1 
ATOM   1020 C  CA   . LEU   A 1 153 ? 7.88000   1.06300   22.71800 1.000 25.02369 ?  305 LEU   A CA   1 
ATOM   1021 C  C    . LEU   A 1 153 ? 8.51700   2.44100   22.70900 1.000 23.78828 ?  305 LEU   A C    1 
ATOM   1022 O  O    . LEU   A 1 153 ? 9.73900   2.55000   22.62000 1.000 23.75632 ?  305 LEU   A O    1 
ATOM   1023 C  CB   . LEU   A 1 153 ? 7.28200   0.77600   21.33800 1.000 23.24978 ?  305 LEU   A CB   1 
ATOM   1024 C  CG   . LEU   A 1 153 ? 8.22500   1.03900   20.16100 1.000 19.42520 ?  305 LEU   A CG   1 
ATOM   1025 C  CD1  . LEU   A 1 153 ? 9.41500   0.08200   20.22200 1.000 21.21339 ?  305 LEU   A CD1  1 
ATOM   1026 C  CD2  . LEU   A 1 153 ? 7.48300   0.91000   18.82100 1.000 19.64934 ?  305 LEU   A CD2  1 
ATOM   1027 N  N    . ILE   A 1 154 ? 7.71000   3.49400   22.83100 1.000 22.78586 ?  306 ILE   A N    1 
ATOM   1028 C  CA   . ILE   A 1 154 ? 8.20000   4.84200   22.57300 1.000 24.38939 ?  306 ILE   A CA   1 
ATOM   1029 C  C    . ILE   A 1 154 ? 9.22400   5.26200   23.62000 1.000 22.23858 ?  306 ILE   A C    1 
ATOM   1030 O  O    . ILE   A 1 154 ? 10.23500  5.89600   23.29200 1.000 24.86254 ?  306 ILE   A O    1 
ATOM   1031 C  CB   . ILE   A 1 154 ? 7.01800   5.82300   22.49500 1.000 26.56607 ?  306 ILE   A CB   1 
ATOM   1032 C  CG1  . ILE   A 1 154 ? 6.15700   5.50400   21.26900 1.000 25.55774 ?  306 ILE   A CG1  1 
ATOM   1033 C  CG2  . ILE   A 1 154 ? 7.50900   7.24800   22.41600 1.000 25.69632 ?  306 ILE   A CG2  1 
ATOM   1034 C  CD1  . ILE   A 1 154 ? 4.83900   6.25700   21.23500 1.000 27.71627 ?  306 ILE   A CD1  1 
ATOM   1035 N  N    . GLU   A 1 155 ? 8.99100   4.91500   24.88800 1.000 23.54810 ?  307 GLU   A N    1 
ATOM   1036 C  CA   . GLU   A 1 155 ? 9.94000   5.29200   25.93600 1.000 24.02376 ?  307 GLU   A CA   1 
ATOM   1037 C  C    . GLU   A 1 155 ? 11.31100  4.65300   25.74600 1.000 26.43344 ?  307 GLU   A C    1 
ATOM   1038 O  O    . GLU   A 1 155 ? 12.31300  5.38900   25.74900 1.000 29.58605 ?  307 GLU   A O    1 
ATOM   1039 C  CB   . GLU   A 1 155 ? 9.34800   4.97000   27.31300 1.000 32.06317 ?  307 GLU   A CB   1 
ATOM   1040 C  CG   . GLU   A 1 155 ? 10.12900  5.56500   28.46700 1.000 46.18218 ?  307 GLU   A CG   1 
ATOM   1041 C  CD   . GLU   A 1 155 ? 9.34900   5.53700   29.76200 1.000 58.04211 ?  307 GLU   A CD   1 
ATOM   1042 O  OE1  . GLU   A 1 155 ? 9.72500   4.76000   30.66500 1.000 63.38347 ?  307 GLU   A OE1  1 
ATOM   1043 O  OE2  . GLU   A 1 155 ? 8.35400   6.28400   29.87000 1.000 62.81154 ?  307 GLU   A OE2  1 
ATOM   1044 N  N    . PRO   A 1 156 ? 11.44400  3.33000   25.57800 1.000 27.23010 ?  308 PRO   A N    1 
ATOM   1045 C  CA   . PRO   A 1 156 ? 12.77500  2.77800   25.26700 1.000 24.53335 ?  308 PRO   A CA   1 
ATOM   1046 C  C    . PRO   A 1 156 ? 13.34200  3.28300   23.95300 1.000 25.92918 ?  308 PRO   A C    1 
ATOM   1047 O  O    . PRO   A 1 156 ? 14.56600  3.39500   23.81700 1.000 24.79749 ?  308 PRO   A O    1 
ATOM   1048 C  CB   . PRO   A 1 156 ? 12.53100  1.26200   25.21600 1.000 31.07454 ?  308 PRO   A CB   1 
ATOM   1049 C  CG   . PRO   A 1 156 ? 11.23900  1.04400   25.89800 1.000 38.27219 ?  308 PRO   A CG   1 
ATOM   1050 C  CD   . PRO   A 1 156 ? 10.42900  2.26800   25.68800 1.000 31.35527 ?  308 PRO   A CD   1 
ATOM   1051 N  N    . LEU   A 1 157 ? 12.48300  3.57000   22.97100 1.000 21.11312 ?  309 LEU   A N    1 
ATOM   1052 C  CA   . LEU   A 1 157 ? 12.95300  4.09100   21.69200 1.000 20.38850 ?  309 LEU   A CA   1 
ATOM   1053 C  C    . LEU   A 1 157 ? 13.62400  5.44700   21.86600 1.000 18.58430 ?  309 LEU   A C    1 
ATOM   1054 O  O    . LEU   A 1 157 ? 14.71500  5.69100   21.33300 1.000 21.79939 ?  309 LEU   A O    1 
ATOM   1055 C  CB   . LEU   A 1 157 ? 11.78400  4.19600   20.71700 1.000 17.23972 ?  309 LEU   A CB   1 
ATOM   1056 C  CG   . LEU   A 1 157 ? 12.11600  4.76800   19.34100 1.000 16.20830 ?  309 LEU   A CG   1 
ATOM   1057 C  CD1  . LEU   A 1 157 ? 13.26200  3.98700   18.68200 1.000 19.30655 ?  309 LEU   A CD1  1 
ATOM   1058 C  CD2  . LEU   A 1 157 ? 10.87100  4.77000   18.45100 1.000 17.72502 ?  309 LEU   A CD2  1 
ATOM   1059 N  N    . ILE   A 1 158 ? 12.98500  6.34600   22.61500 1.000 19.63724 ?  310 ILE   A N    1 
ATOM   1060 C  CA   . ILE   A 1 158 ? 13.60100  7.64200   22.88600 1.000 22.36196 ?  310 ILE   A CA   1 
ATOM   1061 C  C    . ILE   A 1 158 ? 14.87800  7.46500   23.69800 1.000 23.54061 ?  310 ILE   A C    1 
ATOM   1062 O  O    . ILE   A 1 158 ? 15.90200  8.10200   23.41800 1.000 23.52676 ?  310 ILE   A O    1 
ATOM   1063 C  CB   . ILE   A 1 158 ? 12.60100  8.57600   23.58900 1.000 25.12968 ?  310 ILE   A CB   1 
ATOM   1064 C  CG1  . ILE   A 1 158 ? 11.44700  8.89900   22.64700 1.000 25.95224 ?  310 ILE   A CG1  1 
ATOM   1065 C  CG2  . ILE   A 1 158 ? 13.29000  9.85900   24.02100 1.000 27.50136 ?  310 ILE   A CG2  1 
ATOM   1066 C  CD1  . ILE   A 1 158 ? 11.85700  9.79600   21.50300 1.000 26.33358 ?  310 ILE   A CD1  1 
ATOM   1067 N  N    . LYS   A 1 159 ? 14.84800  6.59500   24.71000 1.000 26.84255 ?  311 LYS   A N    1 
ATOM   1068 C  CA   . LYS   A 1 159 ? 16.05400  6.37100   25.50300 1.000 24.77146 ?  311 LYS   A CA   1 
ATOM   1069 C  C    . LYS   A 1 159 ? 17.19500  5.87700   24.62500 1.000 27.23160 ?  311 LYS   A C    1 
ATOM   1070 O  O    . LYS   A 1 159 ? 18.35200  6.27700   24.81300 1.000 27.41147 ?  311 LYS   A O    1 
ATOM   1071 C  CB   . LYS   A 1 159 ? 15.78400  5.37300   26.62700 1.000 30.07726 ?  311 LYS   A CB   1 
ATOM   1072 C  CG   . LYS   A 1 159 ? 16.97900  5.19700   27.55500 1.000 40.75027 ?  311 LYS   A CG   1 
ATOM   1073 C  CD   . LYS   A 1 159 ? 16.83000  4.00300   28.48300 1.000 44.53030 ?  311 LYS   A CD   1 
ATOM   1074 C  CE   . LYS   A 1 159 ? 18.13300  3.73100   29.23100 1.000 49.91411 ?  311 LYS   A CE   1 
ATOM   1075 N  NZ   . LYS   A 1 159 ? 18.89600  4.98800   29.51800 1.000 53.25695 ?  311 LYS   A NZ   1 
ATOM   1076 N  N    . PHE   A 1 160 ? 16.87800  5.02200   23.65000 1.000 24.91245 ?  312 PHE   A N    1 
ATOM   1077 C  CA   . PHE   A 1 160 ? 17.88500  4.53300   22.71600 1.000 24.46493 ?  312 PHE   A CA   1 
ATOM   1078 C  C    . PHE   A 1 160 ? 18.43100  5.66600   21.85800 1.000 23.31124 ?  312 PHE   A C    1 
ATOM   1079 O  O    . PHE   A 1 160 ? 19.64600  5.76900   21.65100 1.000 21.85486 ?  312 PHE   A O    1 
ATOM   1080 C  CB   . PHE   A 1 160 ? 17.28600  3.43400   21.83400 1.000 21.34883 ?  312 PHE   A CB   1 
ATOM   1081 C  CG   . PHE   A 1 160 ? 18.14200  3.07300   20.64500 1.000 22.08798 ?  312 PHE   A CG   1 
ATOM   1082 C  CD1  . PHE   A 1 160 ? 19.14000  2.12400   20.76200 1.000 26.13902 ?  312 PHE   A CD1  1 
ATOM   1083 C  CD2  . PHE   A 1 160 ? 17.93100  3.67300   19.40800 1.000 20.87888 ?  312 PHE   A CD2  1 
ATOM   1084 C  CE1  . PHE   A 1 160 ? 19.92400  1.78300   19.66800 1.000 24.36818 ?  312 PHE   A CE1  1 
ATOM   1085 C  CE2  . PHE   A 1 160 ? 18.71800  3.34300   18.31600 1.000 26.00350 ?  312 PHE   A CE2  1 
ATOM   1086 C  CZ   . PHE   A 1 160 ? 19.71300  2.39700   18.45000 1.000 24.57799 ?  312 PHE   A CZ   1 
ATOM   1087 N  N    . GLN   A 1 161 ? 17.54100  6.51200   21.32100 1.000 21.49160 ?  313 GLN   A N    1 
ATOM   1088 C  CA   . GLN   A 1 161 ? 18.00400  7.60200   20.46800 1.000 22.62895 ?  313 GLN   A CA   1 
ATOM   1089 C  C    . GLN   A 1 161 ? 18.94400  8.52500   21.23000 1.000 22.02125 ?  313 GLN   A C    1 
ATOM   1090 O  O    . GLN   A 1 161 ? 19.99500  8.91200   20.71300 1.000 23.09468 ?  313 GLN   A O    1 
ATOM   1091 C  CB   . GLN   A 1 161 ? 16.82300  8.39500   19.91100 1.000 21.18323 ?  313 GLN   A CB   1 
ATOM   1092 C  CG   . GLN   A 1 161 ? 15.88600  7.59600   19.01900 1.000 20.20472 ?  313 GLN   A CG   1 
ATOM   1093 C  CD   . GLN   A 1 161 ? 16.53300  7.14500   17.72500 1.000 19.79258 ?  313 GLN   A CD   1 
ATOM   1094 O  OE1  . GLN   A 1 161 ? 17.37100  7.84400   17.15700 1.000 20.79688 ?  313 GLN   A OE1  1 
ATOM   1095 N  NE2  . GLN   A 1 161 ? 16.13500  5.97100   17.24600 1.000 20.00359 ?  313 GLN   A NE2  1 
ATOM   1096 N  N    . VAL   A 1 162 ? 18.57900  8.88800   22.46300 1.000 21.15670 ?  314 VAL   A N    1 
ATOM   1097 C  CA   . VAL   A 1 162 ? 19.44200  9.75200   23.26800 1.000 23.88134 ?  314 VAL   A CA   1 
ATOM   1098 C  C    . VAL   A 1 162 ? 20.76800  9.06400   23.56200 1.000 24.31831 ?  314 VAL   A C    1 
ATOM   1099 O  O    . VAL   A 1 162 ? 21.83600  9.67900   23.46700 1.000 24.44008 ?  314 VAL   A O    1 
ATOM   1100 C  CB   . VAL   A 1 162 ? 18.73600  10.17100  24.57200 1.000 26.06758 ?  314 VAL   A CB   1 
ATOM   1101 C  CG1  . VAL   A 1 162 ? 19.66400  11.05900  25.40000 1.000 27.32354 ?  314 VAL   A CG1  1 
ATOM   1102 C  CG2  . VAL   A 1 162 ? 17.45800  10.90500  24.27400 1.000 27.89422 ?  314 VAL   A CG2  1 
ATOM   1103 N  N    . GLY   A 1 163 ? 20.72200  7.78500   23.93700 1.000 28.36312 ?  315 GLY   A N    1 
ATOM   1104 C  CA   . GLY   A 1 163 ? 21.95600  7.07400   24.23800 1.000 27.58564 ?  315 GLY   A CA   1 
ATOM   1105 C  C    . GLY   A 1 163 ? 22.86800  6.96800   23.03300 1.000 27.01224 ?  315 GLY   A C    1 
ATOM   1106 O  O    . GLY   A 1 163 ? 24.08100  7.17800   23.13800 1.000 29.12041 ?  315 GLY   A O    1 
ATOM   1107 N  N    . LEU   A 1 164 ? 22.29200  6.65900   21.86800 1.000 22.98317 ?  316 LEU   A N    1 
ATOM   1108 C  CA   . LEU   A 1 164 ? 23.07700  6.59900   20.64000 1.000 20.51055 ?  316 LEU   A CA   1 
ATOM   1109 C  C    . LEU   A 1 164 ? 23.63500  7.96800   20.28100 1.000 22.73853 ?  316 LEU   A C    1 
ATOM   1110 O  O    . LEU   A 1 164 ? 24.81300  8.09400   19.92400 1.000 24.75358 ?  316 LEU   A O    1 
ATOM   1111 C  CB   . LEU   A 1 164 ? 22.21500  6.05400   19.50000 1.000 20.01812 ?  316 LEU   A CB   1 
ATOM   1112 C  CG   . LEU   A 1 164 ? 22.90100  5.88600   18.14100 1.000 22.14572 ?  316 LEU   A CG   1 
ATOM   1113 C  CD1  . LEU   A 1 164 ? 24.08200  4.93600   18.25400 1.000 22.90673 ?  316 LEU   A CD1  1 
ATOM   1114 C  CD2  . LEU   A 1 164 ? 21.92000  5.39400   17.09000 1.000 21.77273 ?  316 LEU   A CD2  1 
ATOM   1115 N  N    . LYS   A 1 165 ? 22.80300  9.00800   20.36900 1.000 26.21267 ?  317 LYS   A N    1 
ATOM   1116 C  CA   . LYS   A 1 165 ? 23.25100  10.34600  20.00300 1.000 27.23433 ?  317 LYS   A CA   1 
ATOM   1117 C  C    . LYS   A 1 165 ? 24.41600  10.79300  20.87600 1.000 34.31240 ?  317 LYS   A C    1 
ATOM   1118 O  O    . LYS   A 1 165 ? 25.36200  11.42400  20.38800 1.000 38.45491 ?  317 LYS   A O    1 
ATOM   1119 C  CB   . LYS   A 1 165 ? 22.08400  11.33100  20.10600 1.000 27.31568 ?  317 LYS   A CB   1 
ATOM   1120 C  CG   . LYS   A 1 165 ? 22.23500  12.58400  19.25700 1.000 26.92926 ?  317 LYS   A CG   1 
ATOM   1121 C  CD   . LYS   A 1 165 ? 21.82700  12.36300  17.80900 1.000 27.67189 ?  317 LYS   A CD   1 
ATOM   1122 C  CE   . LYS   A 1 165 ? 21.85700  13.67600  17.04300 1.000 32.44388 ?  317 LYS   A CE   1 
ATOM   1123 N  NZ   . LYS   A 1 165 ? 21.48100  13.52300  15.61200 1.000 25.50649 ?  317 LYS   A NZ   1 
ATOM   1124 N  N    . LYS   A 1 166 ? 24.37700  10.45200  22.16800 1.000 34.17526 ?  318 LYS   A N    1 
ATOM   1125 C  CA   . LYS   A 1 166 ? 25.43500  10.83400  23.09500 1.000 32.52013 ?  318 LYS   A CA   1 
ATOM   1126 C  C    . LYS   A 1 166 ? 26.74000  10.08700  22.85700 1.000 32.05330 ?  318 LYS   A C    1 
ATOM   1127 O  O    . LYS   A 1 166 ? 27.75800  10.46000  23.44700 1.000 35.71883 ?  318 LYS   A O    1 
ATOM   1128 C  CB   . LYS   A 1 166 ? 24.96900  10.62100  24.53700 1.000 33.07804 ?  318 LYS   A CB   1 
ATOM   1129 C  CG   . LYS   A 1 166 ? 23.88200  11.59200  24.96900 1.000 34.96355 ?  318 LYS   A CG   1 
ATOM   1130 C  CD   . LYS   A 1 166 ? 23.59100  11.48800  26.45700 1.000 39.60706 ?  318 LYS   A CD   1 
ATOM   1131 C  CE   . LYS   A 1 166 ? 22.62400  12.57900  26.90400 1.000 43.66087 ?  318 LYS   A CE   1 
ATOM   1132 N  NZ   . LYS   A 1 166 ? 22.10900  12.33200  28.28100 1.000 47.93789 ?  318 LYS   A NZ   1 
ATOM   1133 N  N    . LEU   A 1 167 ? 26.74400  9.05000   22.01900 1.000 29.95575 ?  319 LEU   A N    1 
ATOM   1134 C  CA   . LEU   A 1 167 ? 28.00300  8.42200   21.63500 1.000 28.70093 ?  319 LEU   A CA   1 
ATOM   1135 C  C    . LEU   A 1 167 ? 28.78700  9.26200   20.63600 1.000 28.84628 ?  319 LEU   A C    1 
ATOM   1136 O  O    . LEU   A 1 167 ? 29.98500  9.01000   20.45700 1.000 28.06771 ?  319 LEU   A O    1 
ATOM   1137 C  CB   . LEU   A 1 167 ? 27.75400  7.02900   21.04000 1.000 26.21796 ?  319 LEU   A CB   1 
ATOM   1138 C  CG   . LEU   A 1 167 ? 27.17700  5.94800   21.96300 1.000 28.00616 ?  319 LEU   A CG   1 
ATOM   1139 C  CD1  . LEU   A 1 167 ? 27.04200  4.62300   21.22900 1.000 30.44165 ?  319 LEU   A CD1  1 
ATOM   1140 C  CD2  . LEU   A 1 167 ? 28.03100  5.77800   23.22100 1.000 29.28868 ?  319 LEU   A CD2  1 
ATOM   1141 N  N    A ASN   A 1 168 ? 28.15000  10.25900  20.01900 0.380 27.01922 ?  320 ASN   A N    1 
ATOM   1142 N  N    B ASN   A 1 168 ? 28.14100  10.21900  19.97000 0.620 26.32704 ?  320 ASN   A N    1 
ATOM   1143 C  CA   A ASN   A 1 168 ? 28.73000  11.07400  18.94700 0.380 29.40087 ?  320 ASN   A CA   1 
ATOM   1144 C  CA   B ASN   A 1 168 ? 28.79100  11.07800  18.98100 0.620 29.51077 ?  320 ASN   A CA   1 
ATOM   1145 C  C    A ASN   A 1 168 ? 29.61000  10.23100  18.02900 0.380 28.43020 ?  320 ASN   A C    1 
ATOM   1146 C  C    B ASN   A 1 168 ? 29.62300  10.25400  17.99600 0.620 28.37916 ?  320 ASN   A C    1 
ATOM   1147 O  O    A ASN   A 1 168 ? 30.82600  10.40900  17.93300 0.380 29.15539 ?  320 ASN   A O    1 
ATOM   1148 O  O    B ASN   A 1 168 ? 30.82500  10.46500  17.82200 0.620 29.50885 ?  320 ASN   A O    1 
ATOM   1149 C  CB   A ASN   A 1 168 ? 29.51100  12.26500  19.49600 0.380 34.16681 ?  320 ASN   A CB   1 
ATOM   1150 C  CB   B ASN   A 1 168 ? 29.65300  12.14100  19.67000 0.620 34.23453 ?  320 ASN   A CB   1 
ATOM   1151 C  CG   A ASN   A 1 168 ? 29.83500  13.28600  18.41600 0.380 35.95191 ?  320 ASN   A CG   1 
ATOM   1152 C  CG   B ASN   A 1 168 ? 28.89500  12.89900  20.74100 0.620 33.08060 ?  320 ASN   A CG   1 
ATOM   1153 O  OD1  A ASN   A 1 168 ? 28.98000  14.07800  18.01900 0.380 37.02022 ?  320 ASN   A OD1  1 
ATOM   1154 O  OD1  B ASN   A 1 168 ? 27.76200  13.33400  20.52200 0.620 31.04725 ?  320 ASN   A OD1  1 
ATOM   1155 N  ND2  A ASN   A 1 168 ? 31.06900  13.25800  17.92500 0.380 38.62574 ?  320 ASN   A ND2  1 
ATOM   1156 N  ND2  B ASN   A 1 168 ? 29.51500  13.06500  21.90600 0.620 37.77547 ?  320 ASN   A ND2  1 
ATOM   1157 N  N    . LEU   A 1 169 ? 28.96200  9.28300   17.36700 1.000 26.84762 ?  321 LEU   A N    1 
ATOM   1158 C  CA   . LEU   A 1 169 ? 29.65900  8.40400   16.44100 1.000 25.61708 ?  321 LEU   A CA   1 
ATOM   1159 C  C    . LEU   A 1 169 ? 30.18500  9.18600   15.24500 1.000 26.14481 ?  321 LEU   A C    1 
ATOM   1160 O  O    . LEU   A 1 169 ? 29.52500  10.09700  14.73700 1.000 25.29450 ?  321 LEU   A O    1 
ATOM   1161 C  CB   . LEU   A 1 169 ? 28.72600  7.29300   15.95600 1.000 21.45264 ?  321 LEU   A CB   1 
ATOM   1162 C  CG   . LEU   A 1 169 ? 28.21100  6.29600   16.99700 1.000 21.62281 ?  321 LEU   A CG   1 
ATOM   1163 C  CD1  . LEU   A 1 169 ? 27.39000  5.19800   16.32000 1.000 22.67053 ?  321 LEU   A CD1  1 
ATOM   1164 C  CD2  . LEU   A 1 169 ? 29.36800  5.69700   17.78000 1.000 21.82239 ?  321 LEU   A CD2  1 
ATOM   1165 N  N    . HIS   A 1 170 ? 31.38500  8.82600   14.80000 1.000 23.03063 ?  322 HIS   A N    1 
ATOM   1166 C  CA   . HIS   A 1 170 ? 31.80700  9.20600   13.46200 1.000 22.48637 ?  322 HIS   A CA   1 
ATOM   1167 C  C    . HIS   A 1 170 ? 30.88900  8.54700   12.44700 1.000 25.68849 ?  322 HIS   A C    1 
ATOM   1168 O  O    . HIS   A 1 170 ? 30.29200  7.50000   12.71100 1.000 25.12944 ?  322 HIS   A O    1 
ATOM   1169 C  CB   . HIS   A 1 170 ? 33.24900  8.77200   13.20100 1.000 21.48735 ?  322 HIS   A CB   1 
ATOM   1170 C  CG   . HIS   A 1 170 ? 34.24400  9.37000   14.13900 1.000 24.92593 ?  322 HIS   A CG   1 
ATOM   1171 N  ND1  . HIS   A 1 170 ? 35.60000  9.15100   14.01600 1.000 26.24751 ?  322 HIS   A ND1  1 
ATOM   1172 C  CD2  . HIS   A 1 170 ? 34.08800  10.17200  15.21900 1.000 26.40041 ?  322 HIS   A CD2  1 
ATOM   1173 C  CE1  . HIS   A 1 170 ? 36.23600  9.79600   14.97800 1.000 31.36832 ?  322 HIS   A CE1  1 
ATOM   1174 N  NE2  . HIS   A 1 170 ? 35.34200  10.42400  15.72100 1.000 31.00195 ?  322 HIS   A NE2  1 
ATOM   1175 N  N    . GLU   A 1 171 ? 30.77000  9.16200   11.27000 1.000 19.77952 ?  323 GLU   A N    1 
ATOM   1176 C  CA   . GLU   A 1 171 ? 29.92700  8.55000   10.25100 1.000 21.75992 ?  323 GLU   A CA   1 
ATOM   1177 C  C    . GLU   A 1 171 ? 30.43800  7.16000   9.89600  1.000 20.52722 ?  323 GLU   A C    1 
ATOM   1178 O  O    . GLU   A 1 171 ? 29.65000  6.24900   9.63600  1.000 18.80511 ?  323 GLU   A O    1 
ATOM   1179 C  CB   . GLU   A 1 171 ? 29.84900  9.43200   9.00900  1.000 21.94551 ?  323 GLU   A CB   1 
ATOM   1180 C  CG   . GLU   A 1 171 ? 28.77200  8.95700   8.06200  1.000 23.51669 ?  323 GLU   A CG   1 
ATOM   1181 C  CD   . GLU   A 1 171 ? 28.48000  9.94300   6.95800  1.000 26.75801 ?  323 GLU   A CD   1 
ATOM   1182 O  OE1  . GLU   A 1 171 ? 29.43500  10.56000  6.44800  1.000 33.31591 ?  323 GLU   A OE1  1 
ATOM   1183 O  OE2  . GLU   A 1 171 ? 27.29400  10.09100  6.60400  1.000 30.70300 ?  323 GLU   A OE2  1 
ATOM   1184 N  N    . GLU   A 1 172 ? 31.76100  6.98300   9.90300  1.000 19.55133 ?  324 GLU   A N    1 
ATOM   1185 C  CA   . GLU   A 1 172 ? 32.36700  5.66700   9.72200  1.000 17.71825 ?  324 GLU   A CA   1 
ATOM   1186 C  C    . GLU   A 1 172 ? 31.79600  4.64800   10.70000 1.000 18.44762 ?  324 GLU   A C    1 
ATOM   1187 O  O    . GLU   A 1 172 ? 31.46000  3.52200   10.31900 1.000 17.25472 ?  324 GLU   A O    1 
ATOM   1188 C  CB   . GLU   A 1 172 ? 33.88100  5.78500   9.91200  1.000 19.38650 ?  324 GLU   A CB   1 
ATOM   1189 C  CG   . GLU   A 1 172 ? 34.58600  6.54000   8.80600  1.000 19.58009 ?  324 GLU   A CG   1 
ATOM   1190 C  CD   . GLU   A 1 172 ? 34.66600  8.04500   9.04400  1.000 21.07434 ?  324 GLU   A CD   1 
ATOM   1191 O  OE1  . GLU   A 1 172 ? 35.54500  8.67200   8.42700  1.000 23.27520 ?  324 GLU   A OE1  1 
ATOM   1192 O  OE2  . GLU   A 1 172 ? 33.85900  8.60300   9.82300  1.000 21.02337 ?  324 GLU   A OE2  1 
ATOM   1193 N  N    . GLU   A 1 173 ? 31.71700  5.02200   11.98100 1.000 19.91853 ?  325 GLU   A N    1 
ATOM   1194 C  CA   . GLU   A 1 173 ? 31.20900  4.10500   12.99700 1.000 18.19106 ?  325 GLU   A CA   1 
ATOM   1195 C  C    . GLU   A 1 173 ? 29.72300  3.85800   12.81600 1.000 18.39605 ?  325 GLU   A C    1 
ATOM   1196 O  O    . GLU   A 1 173 ? 29.24600  2.73500   13.00600 1.000 17.75060 ?  325 GLU   A O    1 
ATOM   1197 C  CB   . GLU   A 1 173 ? 31.49900  4.66100   14.39300 1.000 19.39285 ?  325 GLU   A CB   1 
ATOM   1198 C  CG   . GLU   A 1 173 ? 32.97700  4.62500   14.74900 1.000 21.26965 ?  325 GLU   A CG   1 
ATOM   1199 C  CD   . GLU   A 1 173 ? 33.40000  5.73100   15.70300 1.000 25.19871 ?  325 GLU   A CD   1 
ATOM   1200 O  OE1  . GLU   A 1 173 ? 34.59400  5.75400   16.09100 1.000 24.36182 ?  325 GLU   A OE1  1 
ATOM   1201 O  OE2  . GLU   A 1 173 ? 32.55000  6.58100   16.06000 1.000 23.78102 ?  325 GLU   A OE2  1 
ATOM   1202 N  N    . HIS   A 1 174 ? 28.98700  4.90000   12.42400 1.000 17.70708 ?  326 HIS   A N    1 
ATOM   1203 C  CA   . HIS   A 1 174 ? 27.55200  4.79000   12.18900 1.000 19.74844 ?  326 HIS   A CA   1 
ATOM   1204 C  C    . HIS   A 1 174 ? 27.24500  3.80300   11.06600 1.000 17.72673 ?  326 HIS   A C    1 
ATOM   1205 O  O    . HIS   A 1 174 ? 26.37500  2.93300   11.21000 1.000 16.60999 ?  326 HIS   A O    1 
ATOM   1206 C  CB   . HIS   A 1 174 ? 27.01100  6.18600   11.87400 1.000 18.13968 ?  326 HIS   A CB   1 
ATOM   1207 C  CG   . HIS   A 1 174 ? 25.54200  6.24200   11.60400 1.000 20.92206 ?  326 HIS   A CG   1 
ATOM   1208 N  ND1  . HIS   A 1 174 ? 24.59400  6.05700   12.58800 1.000 23.49347 ?  326 HIS   A ND1  1 
ATOM   1209 C  CD2  . HIS   A 1 174 ? 24.85800  6.51700   10.46800 1.000 18.49346 ?  326 HIS   A CD2  1 
ATOM   1210 C  CE1  . HIS   A 1 174 ? 23.38800  6.19100   12.06300 1.000 21.37250 ?  326 HIS   A CE1  1 
ATOM   1211 N  NE2  . HIS   A 1 174 ? 23.52000  6.47500   10.77900 1.000 19.62620 ?  326 HIS   A NE2  1 
ATOM   1212 N  N    . VAL   A 1 175 ? 27.96700  3.90000   9.94500  1.000 15.25301 ?  327 VAL   A N    1 
ATOM   1213 C  CA   . VAL   A 1 175 ? 27.65800  3.01100   8.82400  1.000 15.00228 ?  327 VAL   A CA   1 
ATOM   1214 C  C    . VAL   A 1 175 ? 28.16400  1.59900   9.08900  1.000 13.57436 ?  327 VAL   A C    1 
ATOM   1215 O  O    . VAL   A 1 175 ? 27.55500  0.62200   8.63400  1.000 13.32296 ?  327 VAL   A O    1 
ATOM   1216 C  CB   . VAL   A 1 175 ? 28.21400  3.57000   7.50200  1.000 16.07900 ?  327 VAL   A CB   1 
ATOM   1217 C  CG1  . VAL   A 1 175 ? 27.64500  4.96300   7.23300  1.000 15.93572 ?  327 VAL   A CG1  1 
ATOM   1218 C  CG2  . VAL   A 1 175 ? 29.74000  3.60700   7.51600  1.000 15.27069 ?  327 VAL   A CG2  1 
ATOM   1219 N  N    . LEU   A 1 176 ? 29.27300  1.46000   9.81700  1.000 15.66791 ?  328 LEU   A N    1 
ATOM   1220 C  CA   . LEU   A 1 176 ? 29.70600  0.13100   10.24000 1.000 16.79763 ?  328 LEU   A CA   1 
ATOM   1221 C  C    . LEU   A 1 176 ? 28.67300  -0.51100  11.16300 1.000 17.26123 ?  328 LEU   A C    1 
ATOM   1222 O  O    . LEU   A 1 176 ? 28.36100  -1.70000  11.02800 1.000 16.06561 ?  328 LEU   A O    1 
ATOM   1223 C  CB   . LEU   A 1 176 ? 31.07300  0.22000   10.92600 1.000 16.22159 ?  328 LEU   A CB   1 
ATOM   1224 C  CG   . LEU   A 1 176 ? 32.26900  0.31600   9.96800  1.000 16.29500 ?  328 LEU   A CG   1 
ATOM   1225 C  CD1  . LEU   A 1 176 ? 33.51400  0.79700   10.69200 1.000 17.98519 ?  328 LEU   A CD1  1 
ATOM   1226 C  CD2  . LEU   A 1 176 ? 32.53000  -1.02700  9.27100  1.000 16.62404 ?  328 LEU   A CD2  1 
ATOM   1227 N  N    . LEU   A 1 177 ? 28.11000  0.26600   12.09400 1.000 15.00323 ?  329 LEU   A N    1 
ATOM   1228 C  CA   . LEU   A 1 177 ? 27.13600  -0.30700  13.02300 1.000 16.21802 ?  329 LEU   A CA   1 
ATOM   1229 C  C    . LEU   A 1 177 ? 25.87300  -0.76900  12.29800 1.000 15.20039 ?  329 LEU   A C    1 
ATOM   1230 O  O    . LEU   A 1 177 ? 25.31200  -1.82200  12.62700 1.000 15.16558 ?  329 LEU   A O    1 
ATOM   1231 C  CB   . LEU   A 1 177 ? 26.79700  0.70100   14.12000 1.000 17.12763 ?  329 LEU   A CB   1 
ATOM   1232 C  CG   . LEU   A 1 177 ? 25.92900  0.16700   15.27100 1.000 19.66724 ?  329 LEU   A CG   1 
ATOM   1233 C  CD1  . LEU   A 1 177 ? 26.60600  -0.97800  16.00400 1.000 19.42647 ?  329 LEU   A CD1  1 
ATOM   1234 C  CD2  . LEU   A 1 177 ? 25.58500  1.29100   16.23500 1.000 21.18852 ?  329 LEU   A CD2  1 
ATOM   1235 N  N    . MET   A 1 178 ? 25.40600  -0.00200  11.31100 1.000 14.36539 ?  330 MET   A N    1 
ATOM   1236 C  CA   . MET   A 1 178 ? 24.24300  -0.45200  10.54700 1.000 11.93226 ?  330 MET   A CA   1 
ATOM   1237 C  C    . MET   A 1 178 ? 24.56200  -1.73000  9.79000  1.000 12.58839 ?  330 MET   A C    1 
ATOM   1238 O  O    . MET   A 1 178 ? 23.73800  -2.65000  9.72500  1.000 14.48214 ?  330 MET   A O    1 
ATOM   1239 C  CB   . MET   A 1 178 ? 23.78000  0.64300   9.58600  1.000 11.66357 ?  330 MET   A CB   1 
ATOM   1240 C  CG   . MET   A 1 178 ? 23.17800  1.85800   10.29000 1.000 13.03635 ?  330 MET   A CG   1 
ATOM   1241 S  SD   . MET   A 1 178 ? 22.47700  3.03200   9.10900  1.000 16.62126 ?  330 MET   A SD   1 
ATOM   1242 C  CE   . MET   A 1 178 ? 23.95500  3.59800   8.27200  1.000 15.17275 ?  330 MET   A CE   1 
ATOM   1243 N  N    . ALA   A 1 179 ? 25.76300  -1.81000  9.21700  1.000 12.01502 ?  331 ALA   A N    1 
ATOM   1244 C  CA   . ALA   A 1 179 ? 26.12800  -3.00100  8.45900  1.000 13.64786 ?  331 ALA   A CA   1 
ATOM   1245 C  C    . ALA   A 1 179 ? 26.24900  -4.21900  9.36800  1.000 14.77751 ?  331 ALA   A C    1 
ATOM   1246 O  O    . ALA   A 1 179 ? 25.75600  -5.29800  9.02900  1.000 16.35055 ?  331 ALA   A O    1 
ATOM   1247 C  CB   . ALA   A 1 179 ? 27.43000  -2.75900  7.69700  1.000 14.11164 ?  331 ALA   A CB   1 
ATOM   1248 N  N    . ILE   A 1 180 ? 26.90400  -4.06100  10.52400 1.000 15.45486 ?  332 ILE   A N    1 
ATOM   1249 C  CA   . ILE   A 1 180 ? 27.01500  -5.14900  11.49500 1.000 14.96562 ?  332 ILE   A CA   1 
ATOM   1250 C  C    . ILE   A 1 180 ? 25.63300  -5.59600  11.94600 1.000 17.18505 ?  332 ILE   A C    1 
ATOM   1251 O  O    . ILE   A 1 180 ? 25.35800  -6.79400  12.09100 1.000 15.83858 ?  332 ILE   A O    1 
ATOM   1252 C  CB   . ILE   A 1 180 ? 27.88800  -4.70100  12.68700 1.000 16.42628 ?  332 ILE   A CB   1 
ATOM   1253 C  CG1  . ILE   A 1 180 ? 29.34700  -4.55300  12.24300 1.000 14.68442 ?  332 ILE   A CG1  1 
ATOM   1254 C  CG2  . ILE   A 1 180 ? 27.75100  -5.66600  13.85600 1.000 14.81530 ?  332 ILE   A CG2  1 
ATOM   1255 C  CD1  . ILE   A 1 180 ? 30.20800  -3.71400  13.18700 1.000 17.02228 ?  332 ILE   A CD1  1 
ATOM   1256 N  N    . CYS   A 1 181 ? 24.73800  -4.63600  12.15800 1.000 13.30578 ?  333 CYS   A N    1 
ATOM   1257 C  CA   . CYS   A 1 181 ? 23.37100  -4.95400  12.54600 1.000 15.74121 ?  333 CYS   A CA   1 
ATOM   1258 C  C    . CYS   A 1 181 ? 22.69600  -5.85900  11.52100 1.000 16.33424 ?  333 CYS   A C    1 
ATOM   1259 O  O    . CYS   A 1 181 ? 22.06000  -6.86100  11.88100 1.000 15.21886 ?  333 CYS   A O    1 
ATOM   1260 C  CB   . CYS   A 1 181 ? 22.59400  -3.65200  12.72900 1.000 14.77091 ?  333 CYS   A CB   1 
ATOM   1261 S  SG   . CYS   A 1 181 ? 20.86200  -3.88300  13.14900 1.000 17.93525 ?  333 CYS   A SG   1 
ATOM   1262 N  N    . ILE   A 1 182 ? 22.84200  -5.53000  10.23500 1.000 14.60391 ?  334 ILE   A N    1 
ATOM   1263 C  CA   . ILE   A 1 182 ? 22.17700  -6.28900  9.17800  1.000 12.41198 ?  334 ILE   A CA   1 
ATOM   1264 C  C    . ILE   A 1 182 ? 22.74000  -7.70500  9.07800  1.000 15.88612 ?  334 ILE   A C    1 
ATOM   1265 O  O    . ILE   A 1 182 ? 21.98800  -8.68700  9.02000  1.000 15.72624 ?  334 ILE   A O    1 
ATOM   1266 C  CB   . ILE   A 1 182 ? 22.30000  -5.54300  7.83700  1.000 13.28559 ?  334 ILE   A CB   1 
ATOM   1267 C  CG1  . ILE   A 1 182 ? 21.44800  -4.27500  7.85800  1.000 12.21949 ?  334 ILE   A CG1  1 
ATOM   1268 C  CG2  . ILE   A 1 182 ? 21.91500  -6.46900  6.68800  1.000 15.90483 ?  334 ILE   A CG2  1 
ATOM   1269 C  CD1  . ILE   A 1 182 ? 21.83800  -3.23300  6.80300  1.000 12.99806 ?  334 ILE   A CD1  1 
ATOM   1270 N  N    A VAL   A 1 183 ? 24.06900  -7.84600  9.02500  0.530 15.10295 ?  335 VAL   A N    1 
ATOM   1271 N  N    B VAL   A 1 183 ? 24.06300  -7.82200  9.05700  0.470 15.06683 ?  335 VAL   A N    1 
ATOM   1272 C  CA   A VAL   A 1 183 ? 24.64400  -9.17900  8.82700  0.530 15.33584 ?  335 VAL   A CA   1 
ATOM   1273 C  CA   B VAL   A 1 183 ? 24.72500  -9.10500  8.87600  0.470 14.95796 ?  335 VAL   A CA   1 
ATOM   1274 C  C    A VAL   A 1 183 ? 24.90200  -9.85600  10.16800 0.530 17.20515 ?  335 VAL   A C    1 
ATOM   1275 C  C    B VAL   A 1 183 ? 24.93700  -9.74800  10.24100 0.470 17.22343 ?  335 VAL   A C    1 
ATOM   1276 O  O    A VAL   A 1 183 ? 26.04000  -10.20700 10.50000 0.530 20.09711 ?  335 VAL   A O    1 
ATOM   1277 O  O    B VAL   A 1 183 ? 26.07500  -9.93800  10.68200 0.470 19.20407 ?  335 VAL   A O    1 
ATOM   1278 C  CB   A VAL   A 1 183 ? 25.93100  -9.14200  7.98000  0.530 15.25079 ?  335 VAL   A CB   1 
ATOM   1279 C  CB   B VAL   A 1 183 ? 26.04800  -8.91900  8.10900  0.470 15.93426 ?  335 VAL   A CB   1 
ATOM   1280 C  CG1  A VAL   A 1 183 ? 25.59700  -8.91100  6.51500  0.530 16.57919 ?  335 VAL   A CG1  1 
ATOM   1281 C  CG1  B VAL   A 1 183 ? 26.56100  -10.23600 7.57600  0.470 14.56720 ?  335 VAL   A CG1  1 
ATOM   1282 C  CG2  A VAL   A 1 183 ? 26.89700  -8.09300  8.49300  0.530 14.34656 ?  335 VAL   A CG2  1 
ATOM   1283 C  CG2  B VAL   A 1 183 ? 25.85200  -7.92900  6.96200  0.470 16.06332 ?  335 VAL   A CG2  1 
ATOM   1284 N  N    . SER   A 1 184 ? 23.84300  -10.07300 10.93400 1.000 16.69241 ?  336 SER   A N    1 
ATOM   1285 C  CA   . SER   A 1 184 ? 23.94400  -10.77900 12.19900 1.000 19.01007 ?  336 SER   A CA   1 
ATOM   1286 C  C    . SER   A 1 184 ? 23.60700  -12.24300 11.99200 1.000 19.51963 ?  336 SER   A C    1 
ATOM   1287 O  O    . SER   A 1 184 ? 22.50600  -12.55800 11.51500 1.000 18.46331 ?  336 SER   A O    1 
ATOM   1288 C  CB   . SER   A 1 184 ? 23.02900  -10.16400 13.25000 1.000 24.12758 ?  336 SER   A CB   1 
ATOM   1289 O  OG   . SER   A 1 184 ? 23.38900  -8.81200  13.50000 1.000 25.76855 ?  336 SER   A OG   1 
ATOM   1290 N  N    . PRO   A 1 185 ? 24.51200  -13.16400 12.32600 1.000 18.05074 ?  337 PRO   A N    1 
ATOM   1291 C  CA   . PRO   A 1 185 ? 24.25300  -14.58000 12.03300 1.000 19.19661 ?  337 PRO   A CA   1 
ATOM   1292 C  C    . PRO   A 1 185 ? 23.20800  -15.20400 12.93300 1.000 25.32070 ?  337 PRO   A C    1 
ATOM   1293 O  O    . PRO   A 1 185 ? 22.65600  -16.25400 12.57600 1.000 26.37665 ?  337 PRO   A O    1 
ATOM   1294 C  CB   . PRO   A 1 185 ? 25.62400  -15.23700 12.23500 1.000 22.18309 ?  337 PRO   A CB   1 
ATOM   1295 C  CG   . PRO   A 1 185 ? 26.31800  -14.34200 13.22600 1.000 25.39366 ?  337 PRO   A CG   1 
ATOM   1296 C  CD   . PRO   A 1 185 ? 25.85000  -12.94700 12.90600 1.000 21.64383 ?  337 PRO   A CD   1 
ATOM   1297 N  N    . ASP   A 1 186 ? 22.90200  -14.59800 14.07800 1.000 24.11837 ?  338 ASP   A N    1 
ATOM   1298 C  CA   . ASP   A 1 186 ? 21.96300  -15.20100 15.01400 1.000 26.95621 ?  338 ASP   A CA   1 
ATOM   1299 C  C    . ASP   A 1 186 ? 20.51800  -14.79500 14.74500 1.000 32.68154 ?  338 ASP   A C    1 
ATOM   1300 O  O    . ASP   A 1 186 ? 19.66800  -14.95200 15.62500 1.000 39.03052 ?  338 ASP   A O    1 
ATOM   1301 C  CB   . ASP   A 1 186 ? 22.35400  -14.86300 16.45800 1.000 32.59581 ?  338 ASP   A CB   1 
ATOM   1302 C  CG   . ASP   A 1 186 ? 22.64300  -13.38700 16.66700 1.000 36.83712 ?  338 ASP   A CG   1 
ATOM   1303 O  OD1  . ASP   A 1 186 ? 22.50400  -12.92000 17.81800 1.000 38.85292 ?  338 ASP   A OD1  1 
ATOM   1304 O  OD2  . ASP   A 1 186 ? 23.01600  -12.69200 15.69500 1.000 36.58138 ?  338 ASP   A OD2  1 
ATOM   1305 N  N    . ARG   A 1 187 ? 20.21700  -14.29300 13.55100 1.000 26.18253 ?  339 ARG   A N    1 
ATOM   1306 C  CA   . ARG   A 1 187 ? 18.83800  -13.98400 13.22500 1.000 24.44261 ?  339 ARG   A CA   1 
ATOM   1307 C  C    . ARG   A 1 187 ? 18.06000  -15.27200 12.96600 1.000 33.38023 ?  339 ARG   A C    1 
ATOM   1308 O  O    . ARG   A 1 187 ? 18.60500  -16.24100 12.42800 1.000 26.19896 ?  339 ARG   A O    1 
ATOM   1309 C  CB   . ARG   A 1 187 ? 18.76200  -13.08200 12.00200 1.000 19.68097 ?  339 ARG   A CB   1 
ATOM   1310 C  CG   . ARG   A 1 187 ? 19.54000  -11.79800 12.13700 1.000 23.08783 ?  339 ARG   A CG   1 
ATOM   1311 C  CD   . ARG   A 1 187 ? 18.92600  -10.84800 13.13600 1.000 26.97883 ?  339 ARG   A CD   1 
ATOM   1312 N  NE   . ARG   A 1 187 ? 19.45200  -9.49500  12.95400 1.000 32.00871 ?  339 ARG   A NE   1 
ATOM   1313 C  CZ   . ARG   A 1 187 ? 19.04800  -8.43300  13.64300 1.000 27.52112 ?  339 ARG   A CZ   1 
ATOM   1314 N  NH1  . ARG   A 1 187 ? 18.10500  -8.55400  14.56800 1.000 30.52125 ?  339 ARG   A NH1  1 
ATOM   1315 N  NH2  . ARG   A 1 187 ? 19.59800  -7.25300  13.41800 1.000 19.40034 ?  339 ARG   A NH2  1 
ATOM   1316 N  N    . PRO   A 1 188 ? 16.78200  -15.31100 13.33900 1.000 38.03238 ?  340 PRO   A N    1 
ATOM   1317 C  CA   . PRO   A 1 188 ? 16.00400  -16.53700 13.13400 1.000 35.38362 ?  340 PRO   A CA   1 
ATOM   1318 C  C    . PRO   A 1 188 ? 15.84200  -16.80600 11.64700 1.000 29.69969 ?  340 PRO   A C    1 
ATOM   1319 O  O    . PRO   A 1 188 ? 15.53100  -15.90100 10.87100 1.000 29.79317 ?  340 PRO   A O    1 
ATOM   1320 C  CB   . PRO   A 1 188 ? 14.66400  -16.22500 13.81000 1.000 42.24130 ?  340 PRO   A CB   1 
ATOM   1321 C  CG   . PRO   A 1 188 ? 14.53700  -14.73600 13.70000 1.000 45.36802 ?  340 PRO   A CG   1 
ATOM   1322 C  CD   . PRO   A 1 188 ? 15.94200  -14.18600 13.79200 1.000 43.12598 ?  340 PRO   A CD   1 
ATOM   1323 N  N    . GLY   A 1 189 ? 16.09500  -18.05100 11.24700 1.000 30.84683 ?  341 GLY   A N    1 
ATOM   1324 C  CA   . GLY   A 1 189 ? 15.94000  -18.44800 9.86500  1.000 32.12180 ?  341 GLY   A CA   1 
ATOM   1325 C  C    . GLY   A 1 189 ? 17.19600  -18.37900 9.02100  1.000 28.39518 ?  341 GLY   A C    1 
ATOM   1326 O  O    . GLY   A 1 189 ? 17.16900  -18.83200 7.86900  1.000 27.25809 ?  341 GLY   A O    1 
ATOM   1327 N  N    . VAL   A 1 190 ? 18.29200  -17.82600 9.54700  1.000 22.17221 ?  342 VAL   A N    1 
ATOM   1328 C  CA   . VAL   A 1 190 ? 19.53700  -17.79600 8.78600  1.000 19.92060 ?  342 VAL   A CA   1 
ATOM   1329 C  C    . VAL   A 1 190 ? 19.99900  -19.22300 8.54700  1.000 21.36733 ?  342 VAL   A C    1 
ATOM   1330 O  O    . VAL   A 1 190 ? 20.01600  -20.04800 9.46800  1.000 22.23220 ?  342 VAL   A O    1 
ATOM   1331 C  CB   . VAL   A 1 190 ? 20.60000  -16.97200 9.52600  1.000 19.62422 ?  342 VAL   A CB   1 
ATOM   1332 C  CG1  . VAL   A 1 190 ? 21.97800  -17.19900 8.92300  1.000 19.18055 ?  342 VAL   A CG1  1 
ATOM   1333 C  CG2  . VAL   A 1 190 ? 20.23700  -15.49900 9.47100  1.000 20.21633 ?  342 VAL   A CG2  1 
ATOM   1334 N  N    . GLN   A 1 191 ? 20.35800  -19.52700 7.30000  1.000 19.75137 ?  343 GLN   A N    1 
ATOM   1335 C  CA   . GLN   A 1 191 ? 20.78500  -20.86700 6.91200  1.000 19.96120 ?  343 GLN   A CA   1 
ATOM   1336 C  C    . GLN   A 1 191 ? 22.30100  -21.01900 6.90900  1.000 22.56285 ?  343 GLN   A C    1 
ATOM   1337 O  O    . GLN   A 1 191 ? 22.83700  -21.93900 7.53000  1.000 29.58419 ?  343 GLN   A O    1 
ATOM   1338 C  CB   . GLN   A 1 191 ? 20.22500  -21.21100 5.52800  1.000 28.01506 ?  343 GLN   A CB   1 
ATOM   1339 C  CG   . GLN   A 1 191 ? 18.71000  -21.30800 5.48900  1.000 35.30205 ?  343 GLN   A CG   1 
ATOM   1340 C  CD   . GLN   A 1 191 ? 18.17700  -22.37800 6.42200  1.000 47.44077 ?  343 GLN   A CD   1 
ATOM   1341 O  OE1  . GLN   A 1 191 ? 18.53100  -23.55200 6.30400  1.000 51.12883 ?  343 GLN   A OE1  1 
ATOM   1342 N  NE2  . GLN   A 1 191 ? 17.32500  -21.97600 7.36100  1.000 47.55497 ?  343 GLN   A NE2  1 
ATOM   1343 N  N    . ASP   A 1 192 ? 23.00300  -20.12600 6.22000  1.000 20.60519 ?  344 ASP   A N    1 
ATOM   1344 C  CA   . ASP   A 1 192 ? 24.46200  -20.16800 6.16100  1.000 21.60836 ?  344 ASP   A CA   1 
ATOM   1345 C  C    . ASP   A 1 192 ? 25.04300  -19.22600 7.21600  1.000 20.86628 ?  344 ASP   A C    1 
ATOM   1346 O  O    . ASP   A 1 192 ? 25.65700  -18.20500 6.91200  1.000 18.70286 ?  344 ASP   A O    1 
ATOM   1347 C  CB   . ASP   A 1 192 ? 24.94300  -19.79900 4.75900  1.000 20.10047 ?  344 ASP   A CB   1 
ATOM   1348 C  CG   . ASP   A 1 192 ? 24.56600  -20.83600 3.72000  1.000 24.34538 ?  344 ASP   A CG   1 
ATOM   1349 O  OD1  . ASP   A 1 192 ? 24.33100  -20.45100 2.55100  1.000 23.31924 ?  344 ASP   A OD1  1 
ATOM   1350 O  OD2  . ASP   A 1 192 ? 24.50100  -22.03200 4.07200  1.000 26.73796 ?  344 ASP   A OD2  1 
ATOM   1351 N  N    . ALA   A 1 193 ? 24.84800  -19.60500 8.48400  1.000 22.00475 ?  345 ALA   A N    1 
ATOM   1352 C  CA   . ALA   A 1 193 ? 25.23100  -18.71600 9.58100  1.000 19.61393 ?  345 ALA   A CA   1 
ATOM   1353 C  C    . ALA   A 1 193 ? 26.72900  -18.43000 9.57300  1.000 18.80320 ?  345 ALA   A C    1 
ATOM   1354 O  O    . ALA   A 1 193 ? 27.15700  -17.31300 9.89700  1.000 20.41730 ?  345 ALA   A O    1 
ATOM   1355 C  CB   . ALA   A 1 193 ? 24.80200  -19.31700 10.92300 1.000 23.64038 ?  345 ALA   A CB   1 
ATOM   1356 N  N    . LYS   A 1 194 ? 27.54300  -19.41900 9.19300  1.000 19.80006 ?  346 LYS   A N    1 
ATOM   1357 C  CA   . LYS   A 1 194 ? 28.98800  -19.21400 9.17400  1.000 20.64485 ?  346 LYS   A CA   1 
ATOM   1358 C  C    . LYS   A 1 194 ? 29.40500  -18.20900 8.10900  1.000 21.16332 ?  346 LYS   A C    1 
ATOM   1359 O  O    . LYS   A 1 194 ? 30.37800  -17.46900 8.30200  1.000 21.15787 ?  346 LYS   A O    1 
ATOM   1360 C  CB   . LYS   A 1 194 ? 29.70700  -20.54200 8.94400  1.000 23.96792 ?  346 LYS   A CB   1 
ATOM   1361 C  CG   . LYS   A 1 194 ? 29.76500  -21.43500 10.17000 1.000 30.53835 ?  346 LYS   A CG   1 
ATOM   1362 C  CD   . LYS   A 1 194 ? 30.61900  -22.66200 9.91200  1.000 36.86368 ?  346 LYS   A CD   1 
ATOM   1363 C  CE   . LYS   A 1 194 ? 30.04800  -23.50900 8.78500  1.000 41.84027 ?  346 LYS   A CE   1 
ATOM   1364 N  NZ   . LYS   A 1 194 ? 31.02000  -24.54300 8.31600  1.000 50.30080 ?  346 LYS   A NZ   1 
ATOM   1365 N  N    . LEU   A 1 195 ? 28.71100  -18.18800 6.97000  1.000 19.14986 ?  347 LEU   A N    1 
ATOM   1366 C  CA   . LEU   A 1 195 ? 29.03200  -17.19700 5.95200  1.000 19.72613 ?  347 LEU   A CA   1 
ATOM   1367 C  C    . LEU   A 1 195 ? 28.62400  -15.80300 6.40400  1.000 17.77118 ?  347 LEU   A C    1 
ATOM   1368 O  O    . LEU   A 1 195 ? 29.34200  -14.82600 6.16000  1.000 19.64247 ?  347 LEU   A O    1 
ATOM   1369 C  CB   . LEU   A 1 195 ? 28.33700  -17.54300 4.63600  1.000 18.96146 ?  347 LEU   A CB   1 
ATOM   1370 C  CG   . LEU   A 1 195 ? 28.61800  -18.91100 4.02600  1.000 20.11407 ?  347 LEU   A CG   1 
ATOM   1371 C  CD1  . LEU   A 1 195 ? 27.99100  -18.93800 2.63700  1.000 19.38117 ?  347 LEU   A CD1  1 
ATOM   1372 C  CD2  . LEU   A 1 195 ? 30.10400  -19.17600 3.94900  1.000 23.31122 ?  347 LEU   A CD2  1 
ATOM   1373 N  N    . VAL   A 1 196 ? 27.45400  -15.68900 7.03600  1.000 16.49862 ?  348 VAL   A N    1 
ATOM   1374 C  CA   . VAL   A 1 196 ? 27.03100  -14.40100 7.57800  1.000 16.09609 ?  348 VAL   A CA   1 
ATOM   1375 C  C    . VAL   A 1 196 ? 28.02100  -13.92600 8.63200  1.000 18.83114 ?  348 VAL   A C    1 
ATOM   1376 O  O    . VAL   A 1 196 ? 28.42400  -12.75700 8.65100  1.000 17.31148 ?  348 VAL   A O    1 
ATOM   1377 C  CB   . VAL   A 1 196 ? 25.60900  -14.50600 8.15000  1.000 16.78139 ?  348 VAL   A CB   1 
ATOM   1378 C  CG1  . VAL   A 1 196 ? 25.17100  -13.17700 8.73800  1.000 17.94308 ?  348 VAL   A CG1  1 
ATOM   1379 C  CG2  . VAL   A 1 196 ? 24.64600  -14.96100 7.06400  1.000 15.08992 ?  348 VAL   A CG2  1 
ATOM   1380 N  N    . GLU   A 1 197 ? 28.42700  -14.83300 9.52600  1.000 16.84093 ?  349 GLU   A N    1 
ATOM   1381 C  CA   . GLU   A 1 197 ? 29.37000  -14.46700 10.57900 1.000 18.06366 ?  349 GLU   A CA   1 
ATOM   1382 C  C    . GLU   A 1 197 ? 30.69100  -13.98100 9.99700  1.000 24.42715 ?  349 GLU   A C    1 
ATOM   1383 O  O    . GLU   A 1 197 ? 31.31600  -13.05900 10.53800 1.000 22.18100 ?  349 GLU   A O    1 
ATOM   1384 C  CB   . GLU   A 1 197 ? 29.59900  -15.65900 11.50700 1.000 22.34386 ?  349 GLU   A CB   1 
ATOM   1385 C  CG   . GLU   A 1 197 ? 30.64700  -15.41600 12.57000 1.000 27.85303 ?  349 GLU   A CG   1 
ATOM   1386 C  CD   . GLU   A 1 197 ? 30.90900  -16.64100 13.41700 1.000 38.87084 ?  349 GLU   A CD   1 
ATOM   1387 O  OE1  . GLU   A 1 197 ? 30.90300  -17.76300 12.86600 1.000 41.19213 ?  349 GLU   A OE1  1 
ATOM   1388 O  OE2  . GLU   A 1 197 ? 31.12100  -16.48000 14.63400 1.000 44.10328 ?  349 GLU   A OE2  1 
ATOM   1389 N  N    . ALA   A 1 198 ? 31.12600  -14.58000 8.88600  1.000 20.50980 ?  350 ALA   A N    1 
ATOM   1390 C  CA   . ALA   A 1 198 ? 32.38900  -14.17800 8.27900  1.000 21.63765 ?  350 ALA   A CA   1 
ATOM   1391 C  C    . ALA   A 1 198 ? 32.33900  -12.73300 7.80400  1.000 18.59471 ?  350 ALA   A C    1 
ATOM   1392 O  O    . ALA   A 1 198 ? 33.31200  -11.98900 7.96300  1.000 19.34402 ?  350 ALA   A O    1 
ATOM   1393 C  CB   . ALA   A 1 198 ? 32.73000  -15.10500 7.11900  1.000 26.07933 ?  350 ALA   A CB   1 
ATOM   1394 N  N    . ILE   A 1 199 ? 31.21800  -12.32200 7.21000  1.000 17.62663 ?  351 ILE   A N    1 
ATOM   1395 C  CA   . ILE   A 1 199 ? 31.06600  -10.92400 6.82700  1.000 16.72771 ?  351 ILE   A CA   1 
ATOM   1396 C  C    . ILE   A 1 199 ? 31.05600  -10.03800 8.06600  1.000 16.69137 ?  351 ILE   A C    1 
ATOM   1397 O  O    . ILE   A 1 199 ? 31.76200  -9.02900  8.13300  1.000 15.51579 ?  351 ILE   A O    1 
ATOM   1398 C  CB   . ILE   A 1 199 ? 29.79000  -10.72200 5.99500  1.000 16.89559 ?  351 ILE   A CB   1 
ATOM   1399 C  CG1  . ILE   A 1 199 ? 29.84400  -11.54400 4.71300  1.000 22.46809 ?  351 ILE   A CG1  1 
ATOM   1400 C  CG2  . ILE   A 1 199 ? 29.62200  -9.24700  5.68000  1.000 17.04314 ?  351 ILE   A CG2  1 
ATOM   1401 C  CD1  . ILE   A 1 199 ? 28.51100  -11.61500 3.99100  1.000 21.06322 ?  351 ILE   A CD1  1 
ATOM   1402 N  N    . GLN   A 1 200 ? 30.23800  -10.39500 9.05900  1.000 19.25154 ?  352 GLN   A N    1 
ATOM   1403 C  CA   . GLN   A 1 200 ? 30.13000  -9.56100  10.25200 1.000 18.45690 ?  352 GLN   A CA   1 
ATOM   1404 C  C    . GLN   A 1 200 ? 31.47500  -9.40900  10.94000 1.000 16.47748 ?  352 GLN   A C    1 
ATOM   1405 O  O    . GLN   A 1 200 ? 31.80900  -8.32300  11.42900 1.000 18.80091 ?  352 GLN   A O    1 
ATOM   1406 C  CB   . GLN   A 1 200 ? 29.11000  -10.14000 11.23000 1.000 15.67437 ?  352 GLN   A CB   1 
ATOM   1407 C  CG   . GLN   A 1 200 ? 28.61700  -9.10500  12.24800 1.000 18.15153 ?  352 GLN   A CG   1 
ATOM   1408 C  CD   . GLN   A 1 200 ? 27.86100  -9.73100  13.40100 1.000 23.04413 ?  352 GLN   A CD   1 
ATOM   1409 O  OE1  . GLN   A 1 200 ? 28.32700  -10.69000 14.01300 1.000 23.43936 ?  352 GLN   A OE1  1 
ATOM   1410 N  NE2  . GLN   A 1 200 ? 26.69500  -9.18200  13.71300 1.000 18.09445 ?  352 GLN   A NE2  1 
ATOM   1411 N  N    . ASP   A 1 201 ? 32.27200  -10.48300 10.96600 1.000 17.75418 ?  353 ASP   A N    1 
ATOM   1412 C  CA   . ASP   A 1 201 ? 33.59100  -10.41700 11.59100 1.000 19.73589 ?  353 ASP   A CA   1 
ATOM   1413 C  C    . ASP   A 1 201 ? 34.49900  -9.42400  10.87100 1.000 18.69220 ?  353 ASP   A C    1 
ATOM   1414 O  O    . ASP   A 1 201 ? 35.25200  -8.68000  11.51600 1.000 21.52654 ?  353 ASP   A O    1 
ATOM   1415 C  CB   . ASP   A 1 201 ? 34.23600  -11.80600 11.60800 1.000 23.44449 ?  353 ASP   A CB   1 
ATOM   1416 C  CG   . ASP   A 1 201 ? 33.66700  -12.71300 12.68900 1.000 25.22944 ?  353 ASP   A CG   1 
ATOM   1417 O  OD1  . ASP   A 1 201 ? 32.84600  -12.24300 13.50300 1.000 22.68999 ?  353 ASP   A OD1  1 
ATOM   1418 O  OD2  . ASP   A 1 201 ? 34.05200  -13.90500 12.73100 1.000 24.67862 ?  353 ASP   A OD2  1 
ATOM   1419 N  N    . ARG   A 1 202 ? 34.47500  -9.42600  9.53100  1.000 18.62200 ?  354 ARG   A N    1 
ATOM   1420 C  CA   . ARG   A 1 202 ? 35.23300  -8.42800  8.77900  1.000 21.59659 ?  354 ARG   A CA   1 
ATOM   1421 C  C    . ARG   A 1 202 ? 34.80200  -7.02400  9.16500  1.000 20.56289 ?  354 ARG   A C    1 
ATOM   1422 O  O    . ARG   A 1 202 ? 35.64200  -6.13600  9.35700  1.000 20.68696 ?  354 ARG   A O    1 
ATOM   1423 C  CB   . ARG   A 1 202 ? 35.04500  -8.61500  7.27300  1.000 21.45107 ?  354 ARG   A CB   1 
ATOM   1424 C  CG   . ARG   A 1 202 ? 35.83200  -9.73600  6.62500  1.000 30.04105 ?  354 ARG   A CG   1 
ATOM   1425 C  CD   . ARG   A 1 202 ? 35.54600  -9.74100  5.12400  1.000 29.03757 ?  354 ARG   A CD   1 
ATOM   1426 N  NE   . ARG   A 1 202 ? 36.52800  -8.95600  4.37800  1.000 34.01374 ?  354 ARG   A NE   1 
ATOM   1427 C  CZ   . ARG   A 1 202 ? 36.24900  -8.10800  3.39000  1.000 35.08928 ?  354 ARG   A CZ   1 
ATOM   1428 N  NH1  . ARG   A 1 202 ? 34.99700  -7.89400  3.00300  1.000 33.05638 ?  354 ARG   A NH1  1 
ATOM   1429 N  NH2  . ARG   A 1 202 ? 37.24000  -7.46600  2.78100  1.000 35.35989 ?  354 ARG   A NH2  1 
ATOM   1430 N  N    . LEU   A 1 203 ? 33.48900  -6.80700  9.27400  1.000 16.85103 ?  355 LEU   A N    1 
ATOM   1431 C  CA   . LEU   A 1 203 ? 32.98100  -5.49000  9.63600  1.000 15.93983 ?  355 LEU   A CA   1 
ATOM   1432 C  C    . LEU   A 1 203 ? 33.32900  -5.13800  11.07500 1.000 20.84878 ?  355 LEU   A C    1 
ATOM   1433 O  O    . LEU   A 1 203 ? 33.70000  -3.99500  11.36400 1.000 19.93343 ?  355 LEU   A O    1 
ATOM   1434 C  CB   . LEU   A 1 203 ? 31.47100  -5.44100  9.43000  1.000 14.94937 ?  355 LEU   A CB   1 
ATOM   1435 C  CG   . LEU   A 1 203 ? 30.98800  -5.71700  8.00500  1.000 16.48212 ?  355 LEU   A CG   1 
ATOM   1436 C  CD1  . LEU   A 1 203 ? 29.48200  -5.83200  7.99900  1.000 18.13522 ?  355 LEU   A CD1  1 
ATOM   1437 C  CD2  . LEU   A 1 203 ? 31.42900  -4.61400  7.05700  1.000 20.71660 ?  355 LEU   A CD2  1 
ATOM   1438 N  N    . SER   A 1 204 ? 33.19800  -6.10200  11.99400 1.000 17.54251 ?  356 SER   A N    1 
ATOM   1439 C  CA   . SER   A 1 204 ? 33.51900  -5.84000  13.39400 1.000 18.88338 ?  356 SER   A CA   1 
ATOM   1440 C  C    . SER   A 1 204 ? 34.99600  -5.52700  13.56800 1.000 19.42258 ?  356 SER   A C    1 
ATOM   1441 O  O    . SER   A 1 204 ? 35.36000  -4.59200  14.29200 1.000 22.94569 ?  356 SER   A O    1 
ATOM   1442 C  CB   . SER   A 1 204 ? 33.13500  -7.03700  14.26500 1.000 22.85743 ?  356 SER   A CB   1 
ATOM   1443 O  OG   . SER   A 1 204 ? 31.74300  -7.28000  14.22800 1.000 27.57527 ?  356 SER   A OG   1 
ATOM   1444 N  N    . ASN   A 1 205 ? 35.86200  -6.30600  12.91800 1.000 19.31635 ?  357 ASN   A N    1 
ATOM   1445 C  CA   . ASN   A 1 205 ? 37.29300  -6.04800  13.00500 1.000 22.23191 ?  357 ASN   A CA   1 
ATOM   1446 C  C    . ASN   A 1 205 ? 37.63700  -4.69000  12.41100 1.000 24.42694 ?  357 ASN   A C    1 
ATOM   1447 O  O    . ASN   A 1 205 ? 38.50700  -3.98100  12.92400 1.000 24.65901 ?  357 ASN   A O    1 
ATOM   1448 C  CB   . ASN   A 1 205 ? 38.07100  -7.15700  12.30100 1.000 28.37788 ?  357 ASN   A CB   1 
ATOM   1449 C  CG   . ASN   A 1 205 ? 38.00900  -8.47700  13.05300 1.000 29.86603 ?  357 ASN   A CG   1 
ATOM   1450 O  OD1  . ASN   A 1 205 ? 37.75900  -8.50900  14.25800 1.000 31.13061 ?  357 ASN   A OD1  1 
ATOM   1451 N  ND2  . ASN   A 1 205 ? 38.24300  -9.57200  12.34300 1.000 31.39324 ?  357 ASN   A ND2  1 
ATOM   1452 N  N    . THR   A 1 206 ? 36.95100  -4.30600  11.33300 1.000 20.24110 ?  358 THR   A N    1 
ATOM   1453 C  CA   . THR   A 1 206 ? 37.13600  -2.97000  10.77500 1.000 19.28498 ?  358 THR   A CA   1 
ATOM   1454 C  C    . THR   A 1 206 ? 36.70400  -1.89900  11.76800 1.000 19.39887 ?  358 THR   A C    1 
ATOM   1455 O  O    . THR   A 1 206 ? 37.38000  -0.87400  11.92300 1.000 21.31416 ?  358 THR   A O    1 
ATOM   1456 C  CB   . THR   A 1 206 ? 36.34900  -2.84000  9.46700  1.000 20.95436 ?  358 THR   A CB   1 
ATOM   1457 O  OG1  . THR   A 1 206 ? 36.85900  -3.78000  8.50800  1.000 19.65119 ?  358 THR   A OG1  1 
ATOM   1458 C  CG2  . THR   A 1 206 ? 36.48700  -1.43800  8.90800  1.000 18.36042 ?  358 THR   A CG2  1 
ATOM   1459 N  N    . LEU   A 1 207 ? 35.58300  -2.12100  12.45500 1.000 18.78846 ?  359 LEU   A N    1 
ATOM   1460 C  CA   . LEU   A 1 207 ? 35.10200  -1.12900  13.41300 1.000 21.38596 ?  359 LEU   A CA   1 
ATOM   1461 C  C    . LEU   A 1 207 ? 36.06200  -0.98900  14.58600 1.000 21.87830 ?  359 LEU   A C    1 
ATOM   1462 O  O    . LEU   A 1 207 ? 36.39700  0.13000   14.99400 1.000 21.24900 ?  359 LEU   A O    1 
ATOM   1463 C  CB   . LEU   A 1 207 ? 33.70500  -1.50500  13.90400 1.000 20.93555 ?  359 LEU   A CB   1 
ATOM   1464 C  CG   . LEU   A 1 207 ? 33.15800  -0.65600  15.05200 1.000 20.54981 ?  359 LEU   A CG   1 
ATOM   1465 C  CD1  . LEU   A 1 207 ? 33.16200  0.83300   14.69900 1.000 19.03621 ?  359 LEU   A CD1  1 
ATOM   1466 C  CD2  . LEU   A 1 207 ? 31.76500  -1.12600  15.42800 1.000 21.15298 ?  359 LEU   A CD2  1 
ATOM   1467 N  N    . GLN   A 1 208 ? 36.51500  -2.11800  15.14000 1.000 22.83997 ?  360 GLN   A N    1 
ATOM   1468 C  CA   . GLN   A 1 208 ? 37.45200  -2.08100  16.26200 1.000 22.44901 ?  360 GLN   A CA   1 
ATOM   1469 C  C    . GLN   A 1 208 ? 38.74600  -1.38900  15.87600 1.000 23.39431 ?  360 GLN   A C    1 
ATOM   1470 O  O    . GLN   A 1 208 ? 39.29400  -0.59200  16.65000 1.000 24.54420 ?  360 GLN   A O    1 
ATOM   1471 C  CB   . GLN   A 1 208 ? 37.75100  -3.49800  16.73800 1.000 27.10855 ?  360 GLN   A CB   1 
ATOM   1472 C  CG   . GLN   A 1 208 ? 36.57300  -4.24700  17.31300 1.000 27.41378 ?  360 GLN   A CG   1 
ATOM   1473 C  CD   . GLN   A 1 208 ? 37.00800  -5.56100  17.93300 1.000 40.12886 ?  360 GLN   A CD   1 
ATOM   1474 O  OE1  . GLN   A 1 208 ? 36.53900  -6.63200  17.55000 1.000 46.37538 ?  360 GLN   A OE1  1 
ATOM   1475 N  NE2  . GLN   A 1 208 ? 37.92600  -5.48300  18.88400 1.000 42.92609 ?  360 GLN   A NE2  1 
ATOM   1476 N  N    . THR   A 1 209 ? 39.27000  -1.70600  14.68900 1.000 24.46500 ?  361 THR   A N    1 
ATOM   1477 C  CA   . THR   A 1 209 ? 40.50600  -1.08000  14.23700 1.000 27.60922 ?  361 THR   A CA   1 
ATOM   1478 C  C    . THR   A 1 209 ? 40.30600  0.40800   13.97800 1.000 24.04603 ?  361 THR   A C    1 
ATOM   1479 O  O    . THR   A 1 209 ? 41.18100  1.22200   14.30200 1.000 27.68683 ?  361 THR   A O    1 
ATOM   1480 C  CB   . THR   A 1 209 ? 41.02500  -1.79400  12.98700 1.000 28.53133 ?  361 THR   A CB   1 
ATOM   1481 O  OG1  . THR   A 1 209 ? 41.29300  -3.16500  13.30600 1.000 31.43121 ?  361 THR   A OG1  1 
ATOM   1482 C  CG2  . THR   A 1 209 ? 42.31000  -1.13900  12.47600 1.000 24.96317 ?  361 THR   A CG2  1 
ATOM   1483 N  N    . TYR   A 1 210 ? 39.15200  0.78600   13.41800 1.000 23.98880 ?  362 TYR   A N    1 
ATOM   1484 C  CA   . TYR   A 1 210 ? 38.85300  2.20000   13.22700 1.000 22.80808 ?  362 TYR   A CA   1 
ATOM   1485 C  C    . TYR   A 1 210 ? 38.83700  2.93800   14.55800 1.000 27.29633 ?  362 TYR   A C    1 
ATOM   1486 O  O    . TYR   A 1 210 ? 39.44400  4.00500   14.69700 1.000 28.97229 ?  362 TYR   A O    1 
ATOM   1487 C  CB   . TYR   A 1 210 ? 37.50700  2.38000   12.51200 1.000 23.10977 ?  362 TYR   A CB   1 
ATOM   1488 C  CG   . TYR   A 1 210 ? 37.21600  3.84300   12.27300 1.000 25.38104 ?  362 TYR   A CG   1 
ATOM   1489 C  CD1  . TYR   A 1 210 ? 36.50800  4.59200   13.20200 1.000 24.80092 ?  362 TYR   A CD1  1 
ATOM   1490 C  CD2  . TYR   A 1 210 ? 37.70800  4.48800   11.14900 1.000 23.00705 ?  362 TYR   A CD2  1 
ATOM   1491 C  CE1  . TYR   A 1 210 ? 36.27900  5.93900   13.00900 1.000 23.31645 ?  362 TYR   A CE1  1 
ATOM   1492 C  CE2  . TYR   A 1 210 ? 37.47100  5.83500   10.94000 1.000 25.67104 ?  362 TYR   A CE2  1 
ATOM   1493 C  CZ   . TYR   A 1 210 ? 36.75700  6.55400   11.87700 1.000 26.05207 ?  362 TYR   A CZ   1 
ATOM   1494 O  OH   . TYR   A 1 210 ? 36.52200  7.89600   11.68700 1.000 30.80131 ?  362 TYR   A OH   1 
ATOM   1495 N  N    . ILE   A 1 211 ? 38.11600  2.39800   15.54100 1.000 28.62942 ?  363 ILE   A N    1 
ATOM   1496 C  CA   . ILE   A 1 211 ? 38.01900  3.06300   16.83800 1.000 25.88824 ?  363 ILE   A CA   1 
ATOM   1497 C  C    . ILE   A 1 211 ? 39.40400  3.26700   17.43200 1.000 31.03592 ?  363 ILE   A C    1 
ATOM   1498 O  O    . ILE   A 1 211 ? 39.73300  4.35300   17.92300 1.000 33.00360 ?  363 ILE   A O    1 
ATOM   1499 C  CB   . ILE   A 1 211 ? 37.10300  2.26200   17.78200 1.000 24.15483 ?  363 ILE   A CB   1 
ATOM   1500 C  CG1  . ILE   A 1 211 ? 35.65100  2.34600   17.29300 1.000 24.17718 ?  363 ILE   A CG1  1 
ATOM   1501 C  CG2  . ILE   A 1 211 ? 37.25400  2.75500   19.22400 1.000 27.49344 ?  363 ILE   A CG2  1 
ATOM   1502 C  CD1  . ILE   A 1 211 ? 34.68500  1.40300   18.00500 1.000 22.08260 ?  363 ILE   A CD1  1 
ATOM   1503 N  N    . ARG   A 1 212 ? 40.25500  2.24500   17.34600 1.000 28.50365 ?  364 ARG   A N    1 
ATOM   1504 C  CA   . ARG   A 1 212 ? 41.55800  2.30800   17.99900 1.000 33.48299 ?  364 ARG   A CA   1 
ATOM   1505 C  C    . ARG   A 1 212 ? 42.49900  3.29700   17.32400 1.000 33.31979 ?  364 ARG   A C    1 
ATOM   1506 O  O    . ARG   A 1 212 ? 43.30100  3.94600   18.00400 1.000 35.78007 ?  364 ARG   A O    1 
ATOM   1507 C  CB   . ARG   A 1 212 ? 42.19900  0.92100   18.02200 1.000 36.70711 ?  364 ARG   A CB   1 
ATOM   1508 C  CG   . ARG   A 1 212 ? 41.51700  -0.07500  18.94100 1.000 41.29673 ?  364 ARG   A CG   1 
ATOM   1509 C  CD   . ARG   A 1 212 ? 42.40200  -1.29300  19.17700 1.000 53.16687 ?  364 ARG   A CD   1 
ATOM   1510 N  NE   . ARG   A 1 212 ? 42.56800  -2.08700  17.96300 1.000 58.62568 ?  364 ARG   A NE   1 
ATOM   1511 C  CZ   . ARG   A 1 212 ? 41.94100  -3.23400  17.72800 1.000 55.30534 ?  364 ARG   A CZ   1 
ATOM   1512 N  NH1  . ARG   A 1 212 ? 41.10200  -3.72900  18.63000 1.000 52.71418 ?  364 ARG   A NH1  1 
ATOM   1513 N  NH2  . ARG   A 1 212 ? 42.15400  -3.88900  16.59400 1.000 51.34839 ?  364 ARG   A NH2  1 
ATOM   1514 N  N    A CYS   A 1 213 ? 42.41500  3.42800   15.99900 0.420 32.90157 ?  365 CYS   A N    1 
ATOM   1515 N  N    B CYS   A 1 213 ? 42.42900  3.43400   16.00100 0.580 31.95970 ?  365 CYS   A N    1 
ATOM   1516 C  CA   A CYS   A 1 213 ? 43.38500  4.20200   15.24000 0.420 38.77110 ?  365 CYS   A CA   1 
ATOM   1517 C  CA   B CYS   A 1 213 ? 43.41100  4.23500   15.28600 0.580 39.05150 ?  365 CYS   A CA   1 
ATOM   1518 C  C    A CYS   A 1 213 ? 42.86500  5.54000   14.74200 0.420 38.82697 ?  365 CYS   A C    1 
ATOM   1519 C  C    B CYS   A 1 213 ? 42.86800  5.54000   14.72300 0.580 38.76727 ?  365 CYS   A C    1 
ATOM   1520 O  O    A CYS   A 1 213 ? 43.67700  6.40400   14.39600 0.420 39.59336 ?  365 CYS   A O    1 
ATOM   1521 O  O    B CYS   A 1 213 ? 43.66700  6.38600   14.30700 0.580 39.93325 ?  365 CYS   A O    1 
ATOM   1522 C  CB   A CYS   A 1 213 ? 43.88200  3.38500   14.03900 0.420 41.79376 ?  365 CYS   A CB   1 
ATOM   1523 C  CB   B CYS   A 1 213 ? 44.03700  3.41400   14.14800 0.580 42.69559 ?  365 CYS   A CB   1 
ATOM   1524 S  SG   A CYS   A 1 213 ? 44.27200  1.67200   14.46000 0.420 46.05834 ?  365 CYS   A SG   1 
ATOM   1525 S  SG   B CYS   A 1 213 ? 43.12200  3.45400   12.60700 0.580 41.19729 ?  365 CYS   A SG   1 
ATOM   1526 N  N    . ARG   A 1 214 ? 41.55000  5.74000   14.70300 1.000 38.71987 ?  366 ARG   A N    1 
ATOM   1527 C  CA   . ARG   A 1 214 ? 40.97600  6.96200   14.15100 1.000 40.59714 ?  366 ARG   A CA   1 
ATOM   1528 C  C    . ARG   A 1 214 ? 40.02700  7.70100   15.07700 1.000 41.76328 ?  366 ARG   A C    1 
ATOM   1529 O  O    . ARG   A 1 214 ? 39.73900  8.87300   14.81000 1.000 46.89548 ?  366 ARG   A O    1 
ATOM   1530 C  CB   . ARG   A 1 214 ? 40.23300  6.66700   12.83900 1.000 36.32632 ?  366 ARG   A CB   1 
ATOM   1531 C  CG   . ARG   A 1 214 ? 41.15000  6.26500   11.69800 1.000 47.30378 ?  366 ARG   A CG   1 
ATOM   1532 C  CD   . ARG   A 1 214 ? 41.39300  7.41700   10.73500 1.000 55.20101 ?  366 ARG   A CD   1 
ATOM   1533 N  NE   . ARG   A 1 214 ? 42.07600  6.96400   9.52700  1.000 59.67988 ?  366 ARG   A NE   1 
ATOM   1534 C  CZ   . ARG   A 1 214 ? 41.45100  6.57400   8.41900  1.000 59.98401 ?  366 ARG   A CZ   1 
ATOM   1535 N  NH1  . ARG   A 1 214 ? 40.12600  6.58400   8.36700  1.000 58.72402 ?  366 ARG   A NH1  1 
ATOM   1536 N  NH2  . ARG   A 1 214 ? 42.14900  6.17400   7.36400  1.000 59.63436 ?  366 ARG   A NH2  1 
ATOM   1537 N  N    . HIS   A 1 215 ? 39.51200  7.07800   16.12800 1.000 41.46953 ?  367 HIS   A N    1 
ATOM   1538 C  CA   . HIS   A 1 215 ? 38.65500  7.80500   17.04900 1.000 41.14064 ?  367 HIS   A CA   1 
ATOM   1539 C  C    . HIS   A 1 215 ? 39.51400  8.41300   18.14600 1.000 46.14157 ?  367 HIS   A C    1 
ATOM   1540 O  O    . HIS   A 1 215 ? 40.16000  7.66800   18.89600 1.000 46.14529 ?  367 HIS   A O    1 
ATOM   1541 C  CB   . HIS   A 1 215 ? 37.58600  6.90600   17.64700 1.000 33.78097 ?  367 HIS   A CB   1 
ATOM   1542 C  CG   . HIS   A 1 215 ? 36.41300  7.66200   18.19000 1.000 29.73359 ?  367 HIS   A CG   1 
ATOM   1543 N  ND1  . HIS   A 1 215 ? 35.14300  7.54700   17.66900 1.000 28.09322 ?  367 HIS   A ND1  1 
ATOM   1544 C  CD2  . HIS   A 1 215 ? 36.32800  8.57300   19.19000 1.000 29.23019 ?  367 HIS   A CD2  1 
ATOM   1545 C  CE1  . HIS   A 1 215 ? 34.32100  8.34000   18.33500 1.000 29.83107 ?  367 HIS   A CE1  1 
ATOM   1546 N  NE2  . HIS   A 1 215 ? 35.01600  8.97500   19.26200 1.000 31.20862 ?  367 HIS   A NE2  1 
ATOM   1547 N  N    . PRO   A 1 216 ? 39.56400  9.73600   18.26900 1.000 46.07915 ?  368 PRO   A N    1 
ATOM   1548 C  CA   . PRO   A 1 216 ? 40.46100  10.35800  19.23900 1.000 46.60529 ?  368 PRO   A CA   1 
ATOM   1549 C  C    . PRO   A 1 216 ? 40.03300  10.03000  20.65600 1.000 46.37192 ?  368 PRO   A C    1 
ATOM   1550 O  O    . PRO   A 1 216 ? 38.82900  9.92900   20.94200 1.000 42.06221 ?  368 PRO   A O    1 
ATOM   1551 C  CB   . PRO   A 1 216 ? 40.31400  11.85800  18.94300 1.000 48.71882 ?  368 PRO   A CB   1 
ATOM   1552 C  CG   . PRO   A 1 216 ? 38.93700  11.99000  18.38800 1.000 47.86716 ?  368 PRO   A CG   1 
ATOM   1553 C  CD   . PRO   A 1 216 ? 38.68800  10.72100  17.60700 1.000 45.35000 ?  368 PRO   A CD   1 
ATOM   1554 N  N    . PRO   A 1 217 ? 40.98500  9.82800   21.56700 1.000 49.26917 ?  369 PRO   A N    1 
ATOM   1555 C  CA   . PRO   A 1 217 ? 40.62800  9.67300   22.97100 1.000 51.93839 ?  369 PRO   A CA   1 
ATOM   1556 C  C    . PRO   A 1 217 ? 40.09400  10.98000  23.52700 1.000 58.64811 ?  369 PRO   A C    1 
ATOM   1557 O  O    . PRO   A 1 217 ? 40.41000  12.06700  23.00900 1.000 61.53155 ?  369 PRO   A O    1 
ATOM   1558 C  CB   . PRO   A 1 217 ? 41.95800  9.27500   23.63800 1.000 54.91623 ?  369 PRO   A CB   1 
ATOM   1559 C  CG   . PRO   A 1 217 ? 42.83700  8.81000   22.51700 1.000 55.90176 ?  369 PRO   A CG   1 
ATOM   1560 C  CD   . PRO   A 1 217 ? 42.42800  9.63800   21.34100 1.000 53.17264 ?  369 PRO   A CD   1 
ATOM   1561 N  N    . PRO   A 1 218 ? 39.27300  10.93200  24.58600 1.000 64.47818 ?  370 PRO   A N    1 
ATOM   1562 C  CA   . PRO   A 1 218 ? 38.84100  9.70100   25.25200 1.000 66.98213 ?  370 PRO   A CA   1 
ATOM   1563 C  C    . PRO   A 1 218 ? 37.61600  9.07100   24.60100 1.000 64.10574 ?  370 PRO   A C    1 
ATOM   1564 O  O    . PRO   A 1 218 ? 37.14800  8.05300   25.09400 1.000 64.24109 ?  370 PRO   A O    1 
ATOM   1565 C  CB   . PRO   A 1 218 ? 38.51100  10.18000  26.66300 1.000 70.84544 ?  370 PRO   A CB   1 
ATOM   1566 C  CG   . PRO   A 1 218 ? 37.98500  11.56000  26.44800 1.000 71.26438 ?  370 PRO   A CG   1 
ATOM   1567 C  CD   . PRO   A 1 218 ? 38.73200  12.12900  25.25600 1.000 69.29518 ?  370 PRO   A CD   1 
ATOM   1568 N  N    . GLY   A 1 219 ? 37.11900  9.66900   23.51300 1.000 60.08531 ?  371 GLY   A N    1 
ATOM   1569 C  CA   . GLY   A 1 219 ? 35.89600  9.17900   22.89300 1.000 57.66343 ?  371 GLY   A CA   1 
ATOM   1570 C  C    . GLY   A 1 219 ? 35.91700  7.69500   22.58000 1.000 56.08073 ?  371 GLY   A C    1 
ATOM   1571 O  O    . GLY   A 1 219 ? 34.86800  7.04600   22.56000 1.000 56.81326 ?  371 GLY   A O    1 
ATOM   1572 N  N    . SER   A 1 220 ? 37.10400  7.13500   22.34000 1.000 50.60840 ?  372 SER   A N    1 
ATOM   1573 C  CA   . SER   A 1 220 ? 37.23200  5.70400   22.09700 1.000 50.70107 ?  372 SER   A CA   1 
ATOM   1574 C  C    . SER   A 1 220 ? 36.96200  4.86400   23.34000 1.000 58.84742 ?  372 SER   A C    1 
ATOM   1575 O  O    . SER   A 1 220 ? 36.88600  3.63500   23.22500 1.000 54.20558 ?  372 SER   A O    1 
ATOM   1576 C  CB   . SER   A 1 220 ? 38.63000  5.39200   21.55800 1.000 50.29540 ?  372 SER   A CB   1 
ATOM   1577 O  OG   . SER   A 1 220 ? 39.62100  6.15400   22.22900 1.000 53.28300 ?  372 SER   A OG   1 
ATOM   1578 N  N    . HIS   A 1 221 ? 36.81100  5.49400   24.51000 1.000 61.31567 ?  373 HIS   A N    1 
ATOM   1579 C  CA   . HIS   A 1 221 ? 36.64800  4.80200   25.78600 1.000 63.08250 ?  373 HIS   A CA   1 
ATOM   1580 C  C    . HIS   A 1 221 ? 35.47600  3.83500   25.77700 1.000 53.96474 ?  373 HIS   A C    1 
ATOM   1581 O  O    . HIS   A 1 221 ? 34.31500  4.25500   25.82300 1.000 55.12836 ?  373 HIS   A O    1 
ATOM   1582 C  CB   . HIS   A 1 221 ? 36.46000  5.80800   26.92400 1.000 69.09699 ?  373 HIS   A CB   1 
ATOM   1583 C  CG   . HIS   A 1 221 ? 35.90900  5.20700   28.18000 1.000 74.97415 ?  373 HIS   A CG   1 
ATOM   1584 N  ND1  . HIS   A 1 221 ? 36.70700  4.61400   29.13400 1.000 77.85513 ?  373 HIS   A ND1  1 
ATOM   1585 C  CD2  . HIS   A 1 221 ? 34.63800  5.10700   28.63800 1.000 75.74222 ?  373 HIS   A CD2  1 
ATOM   1586 C  CE1  . HIS   A 1 221 ? 35.95200  4.17800   30.12700 1.000 78.41077 ?  373 HIS   A CE1  1 
ATOM   1587 N  NE2  . HIS   A 1 221 ? 34.69300  4.46300   29.85000 1.000 77.56367 ?  373 HIS   A NE2  1 
ATOM   1588 N  N    . GLN   A 1 222 ? 35.77800  2.53700   25.73800 1.000 47.32691 ?  374 GLN   A N    1 
ATOM   1589 C  CA   . GLN   A 1 222 ? 34.75800  1.48700   25.72700 1.000 37.99994 ?  374 GLN   A CA   1 
ATOM   1590 C  C    . GLN   A 1 222 ? 33.69500  1.74200   24.66400 1.000 31.53582 ?  374 GLN   A C    1 
ATOM   1591 O  O    . GLN   A 1 222 ? 32.54800  1.30600   24.79500 1.000 29.40215 ?  374 GLN   A O    1 
ATOM   1592 C  CB   . GLN   A 1 222 ? 34.11800  1.31400   27.10600 1.000 40.77744 ?  374 GLN   A CB   1 
ATOM   1593 C  CG   . GLN   A 1 222 ? 35.11000  1.43300   28.25500 1.000 49.88077 ?  374 GLN   A CG   1 
ATOM   1594 C  CD   . GLN   A 1 222 ? 34.56100  0.89300   29.55800 1.000 59.64951 ?  374 GLN   A CD   1 
ATOM   1595 O  OE1  . GLN   A 1 222 ? 33.45000  1.23300   29.96800 1.000 61.06403 ?  374 GLN   A OE1  1 
ATOM   1596 N  NE2  . GLN   A 1 222 ? 35.34500  0.05000   30.22500 1.000 66.28997 ?  374 GLN   A NE2  1 
ATOM   1597 N  N    . LEU   A 1 223 ? 34.07400  2.44800   23.59900 1.000 27.43295 ?  375 LEU   A N    1 
ATOM   1598 C  CA   . LEU   A 1 223 ? 33.10800  2.75800   22.55200 1.000 25.40150 ?  375 LEU   A CA   1 
ATOM   1599 C  C    . LEU   A 1 223 ? 32.59600  1.49100   21.89000 1.000 28.08817 ?  375 LEU   A C    1 
ATOM   1600 O  O    . LEU   A 1 223 ? 31.39300  1.36000   21.63500 1.000 26.55827 ?  375 LEU   A O    1 
ATOM   1601 C  CB   . LEU   A 1 223 ? 33.73000  3.69200   21.51800 1.000 31.08863 ?  375 LEU   A CB   1 
ATOM   1602 C  CG   . LEU   A 1 223 ? 32.80200  4.13400   20.38800 1.000 30.51555 ?  375 LEU   A CG   1 
ATOM   1603 C  CD1  . LEU   A 1 223 ? 31.49800  4.71600   20.94100 1.000 29.50499 ?  375 LEU   A CD1  1 
ATOM   1604 C  CD2  . LEU   A 1 223 ? 33.51700  5.13900   19.49800 1.000 33.44116 ?  375 LEU   A CD2  1 
ATOM   1605 N  N    . TYR   A 1 224 ? 33.48800  0.53700   21.61300 1.000 29.64047 ?  376 TYR   A N    1 
ATOM   1606 C  CA   . TYR   A 1 224 ? 33.05600  -0.68200  20.93600 1.000 27.58277 ?  376 TYR   A CA   1 
ATOM   1607 C  C    . TYR   A 1 224 ? 32.03600  -1.43800  21.78000 1.000 25.36648 ?  376 TYR   A C    1 
ATOM   1608 O  O    . TYR   A 1 224 ? 30.97500  -1.83500  21.28300 1.000 27.03761 ?  376 TYR   A O    1 
ATOM   1609 C  CB   . TYR   A 1 224 ? 34.26200  -1.56800  20.61800 1.000 27.82298 ?  376 TYR   A CB   1 
ATOM   1610 C  CG   . TYR   A 1 224 ? 33.87900  -2.84200  19.90400 1.000 24.79727 ?  376 TYR   A CG   1 
ATOM   1611 C  CD1  . TYR   A 1 224 ? 33.32000  -2.81000  18.63000 1.000 23.87366 ?  376 TYR   A CD1  1 
ATOM   1612 C  CD2  . TYR   A 1 224 ? 34.05400  -4.08000  20.51100 1.000 31.08370 ?  376 TYR   A CD2  1 
ATOM   1613 C  CE1  . TYR   A 1 224 ? 32.96600  -3.97000  17.97900 1.000 26.14992 ?  376 TYR   A CE1  1 
ATOM   1614 C  CE2  . TYR   A 1 224 ? 33.69500  -5.24800  19.86600 1.000 30.81790 ?  376 TYR   A CE2  1 
ATOM   1615 C  CZ   . TYR   A 1 224 ? 33.15300  -5.18800  18.60200 1.000 29.40464 ?  376 TYR   A CZ   1 
ATOM   1616 O  OH   . TYR   A 1 224 ? 32.79400  -6.35000  17.95500 1.000 32.39326 ?  376 TYR   A OH   1 
ATOM   1617 N  N    . ALA   A 1 225 ? 32.33300  -1.63000  23.06900 1.000 30.81900 ?  377 ALA   A N    1 
ATOM   1618 C  CA   . ALA   A 1 225 ? 31.39000  -2.32000  23.94200 1.000 28.22541 ?  377 ALA   A CA   1 
ATOM   1619 C  C    . ALA   A 1 225 ? 30.05600  -1.58600  24.00800 1.000 27.44973 ?  377 ALA   A C    1 
ATOM   1620 O  O    . ALA   A 1 225 ? 28.99300  -2.21800  24.05200 1.000 26.43722 ?  377 ALA   A O    1 
ATOM   1621 C  CB   . ALA   A 1 225 ? 31.98500  -2.47400  25.34000 1.000 33.05360 ?  377 ALA   A CB   1 
ATOM   1622 N  N    . LYS   A 1 226 ? 30.09200  -0.25100  24.01700 1.000 29.03453 ?  378 LYS   A N    1 
ATOM   1623 C  CA   . LYS   A 1 226 ? 28.85100  0.52100   24.02700 1.000 26.81192 ?  378 LYS   A CA   1 
ATOM   1624 C  C    . LYS   A 1 226 ? 28.07800  0.35200   22.72500 1.000 26.58933 ?  378 LYS   A C    1 
ATOM   1625 O  O    . LYS   A 1 226 ? 26.84100  0.31400   22.73200 1.000 25.85744 ?  378 LYS   A O    1 
ATOM   1626 C  CB   . LYS   A 1 226 ? 29.14900  1.99700   24.27000 1.000 25.84628 ?  378 LYS   A CB   1 
ATOM   1627 C  CG   . LYS   A 1 226 ? 29.69300  2.30200   25.66600 1.000 33.79259 ?  378 LYS   A CG   1 
ATOM   1628 C  CD   . LYS   A 1 226 ? 29.51400  3.77100   26.01500 1.000 37.48439 ?  378 LYS   A CD   1 
ATOM   1629 C  CE   . LYS   A 1 226 ? 30.04100  4.07900   27.40800 1.000 45.57101 ?  378 LYS   A CE   1 
ATOM   1630 N  NZ   . LYS   A 1 226 ? 31.42300  4.62700   27.36600 1.000 52.98842 ?  378 LYS   A NZ   1 
ATOM   1631 N  N    . MET   A 1 227 ? 28.78300  0.27900   21.59500 1.000 23.67758 ?  379 MET   A N    1 
ATOM   1632 C  CA   . MET   A 1 227 ? 28.09800  0.06900   20.32200 1.000 24.28505 ?  379 MET   A CA   1 
ATOM   1633 C  C    . MET   A 1 227 ? 27.48400  -1.32400  20.26000 1.000 24.18728 ?  379 MET   A C    1 
ATOM   1634 O  O    . MET   A 1 227 ? 26.37800  -1.49800  19.73500 1.000 21.73061 ?  379 MET   A O    1 
ATOM   1635 C  CB   . MET   A 1 227 ? 29.06700  0.29100   19.15800 1.000 22.93575 ?  379 MET   A CB   1 
ATOM   1636 C  CG   . MET   A 1 227 ? 29.54900  1.72900   19.03300 1.000 23.81908 ?  379 MET   A CG   1 
ATOM   1637 S  SD   . MET   A 1 227 ? 30.74500  2.01700   17.70800 1.000 21.49000 ?  379 MET   A SD   1 
ATOM   1638 C  CE   . MET   A 1 227 ? 29.69800  1.83700   16.26500 1.000 20.64001 ?  379 MET   A CE   1 
ATOM   1639 N  N    . ILE   A 1 228 ? 28.18500  -2.32500  20.80000 1.000 25.99379 ?  380 ILE   A N    1 
ATOM   1640 C  CA   . ILE   A 1 228 ? 27.63100  -3.67600  20.88100 1.000 26.78638 ?  380 ILE   A CA   1 
ATOM   1641 C  C    . ILE   A 1 228 ? 26.38100  -3.68900  21.75200 1.000 25.46155 ?  380 ILE   A C    1 
ATOM   1642 O  O    . ILE   A 1 228 ? 25.38000  -4.33700  21.42000 1.000 24.79362 ?  380 ILE   A O    1 
ATOM   1643 C  CB   . ILE   A 1 228 ? 28.69700  -4.65900  21.40400 1.000 32.74602 ?  380 ILE   A CB   1 
ATOM   1644 C  CG1  . ILE   A 1 228 ? 29.82700  -4.80600  20.38500 1.000 33.90330 ?  380 ILE   A CG1  1 
ATOM   1645 C  CG2  . ILE   A 1 228 ? 28.07200  -6.01300  21.73000 1.000 34.85203 ?  380 ILE   A CG2  1 
ATOM   1646 C  CD1  . ILE   A 1 228 ? 29.35600  -5.12500  18.98800 1.000 41.71526 ?  380 ILE   A CD1  1 
ATOM   1647 N  N    . GLN   A 1 229 ? 26.41200  -2.97300  22.87900 1.000 28.11670 ?  381 GLN   A N    1 
ATOM   1648 C  CA   . GLN   A 1 229 ? 25.21700  -2.88700  23.71200 1.000 29.08951 ?  381 GLN   A CA   1 
ATOM   1649 C  C    . GLN   A 1 229 ? 24.05900  -2.23400  22.96500 1.000 25.30496 ?  381 GLN   A C    1 
ATOM   1650 O  O    . GLN   A 1 229 ? 22.90000  -2.60300  23.18000 1.000 28.07320 ?  381 GLN   A O    1 
ATOM   1651 C  CB   . GLN   A 1 229 ? 25.51700  -2.12600  25.00400 1.000 31.34271 ?  381 GLN   A CB   1 
ATOM   1652 C  CG   . GLN   A 1 229 ? 24.31300  -1.99200  25.93000 1.000 32.18720 ?  381 GLN   A CG   1 
ATOM   1653 C  CD   . GLN   A 1 229 ? 23.68800  -3.33600  26.28800 1.000 38.42274 ?  381 GLN   A CD   1 
ATOM   1654 O  OE1  . GLN   A 1 229 ? 22.46500  -3.49000  26.27000 1.000 37.01915 ?  381 GLN   A OE1  1 
ATOM   1655 N  NE2  . GLN   A 1 229 ? 24.52600  -4.31100  26.62400 1.000 36.78255 ?  381 GLN   A NE2  1 
ATOM   1656 N  N    . LYS   A 1 230 ? 24.34300  -1.27400  22.07800 1.000 22.38885 ?  382 LYS   A N    1 
ATOM   1657 C  CA   . LYS   A 1 230 ? 23.27000  -0.68700  21.28000 1.000 21.22060 ?  382 LYS   A CA   1 
ATOM   1658 C  C    . LYS   A 1 230 ? 22.62900  -1.72000  20.36700 1.000 19.52356 ?  382 LYS   A C    1 
ATOM   1659 O  O    . LYS   A 1 230 ? 21.41800  -1.66600  20.12300 1.000 21.17430 ?  382 LYS   A O    1 
ATOM   1660 C  CB   . LYS   A 1 230 ? 23.79000  0.49700   20.45900 1.000 22.26999 ?  382 LYS   A CB   1 
ATOM   1661 C  CG   . LYS   A 1 230 ? 24.01800  1.76800   21.28300 1.000 22.87191 ?  382 LYS   A CG   1 
ATOM   1662 C  CD   . LYS   A 1 230 ? 22.72600  2.27200   21.89400 1.000 28.60182 ?  382 LYS   A CD   1 
ATOM   1663 C  CE   . LYS   A 1 230 ? 22.97100  3.43900   22.83100 1.000 35.99321 ?  382 LYS   A CE   1 
ATOM   1664 N  NZ   . LYS   A 1 230 ? 23.34500  2.98400   24.20200 1.000 39.00018 ?  382 LYS   A NZ   1 
ATOM   1665 N  N    . LEU   A 1 231 ? 23.41300  -2.67100  19.85500 1.000 21.71151 ?  383 LEU   A N    1 
ATOM   1666 C  CA   . LEU   A 1 231 ? 22.82700  -3.74300  19.05900 1.000 20.69963 ?  383 LEU   A CA   1 
ATOM   1667 C  C    . LEU   A 1 231 ? 21.91100  -4.60900  19.91000 1.000 19.96058 ?  383 LEU   A C    1 
ATOM   1668 O  O    . LEU   A 1 231 ? 20.85200  -5.04800  19.44300 1.000 20.79605 ?  383 LEU   A O    1 
ATOM   1669 C  CB   . LEU   A 1 231 ? 23.92800  -4.58400  18.42500 1.000 22.16958 ?  383 LEU   A CB   1 
ATOM   1670 C  CG   . LEU   A 1 231 ? 24.77100  -3.86300  17.37700 1.000 21.81146 ?  383 LEU   A CG   1 
ATOM   1671 C  CD1  . LEU   A 1 231 ? 25.97000  -4.73100  16.97800 1.000 25.39599 ?  383 LEU   A CD1  1 
ATOM   1672 C  CD2  . LEU   A 1 231 ? 23.92000  -3.53600  16.16300 1.000 21.99236 ?  383 LEU   A CD2  1 
ATOM   1673 N  N    . ALA   A 1 232 ? 22.29700  -4.85200  21.16700 1.000 23.05424 ?  384 ALA   A N    1 
ATOM   1674 C  CA   . ALA   A 1 232 ? 21.42700  -5.58800  22.07800 1.000 25.41092 ?  384 ALA   A CA   1 
ATOM   1675 C  C    . ALA   A 1 232 ? 20.13800  -4.82200  22.33700 1.000 27.06177 ?  384 ALA   A C    1 
ATOM   1676 O  O    . ALA   A 1 232 ? 19.04600  -5.40400  22.30800 1.000 24.66817 ?  384 ALA   A O    1 
ATOM   1677 C  CB   . ALA   A 1 232 ? 22.15600  -5.87300  23.38900 1.000 25.43482 ?  384 ALA   A CB   1 
ATOM   1678 N  N    . ASP   A 1 233 ? 20.24400  -3.51100  22.58500 1.000 26.87114 ?  385 ASP   A N    1 
ATOM   1679 C  CA   . ASP   A 1 233 ? 19.04700  -2.69400  22.78000 1.000 27.16009 ?  385 ASP   A CA   1 
ATOM   1680 C  C    . ASP   A 1 233 ? 18.13100  -2.76000  21.56500 1.000 26.89436 ?  385 ASP   A C    1 
ATOM   1681 O  O    . ASP   A 1 233 ? 16.90000  -2.78400  21.70200 1.000 25.13826 ?  385 ASP   A O    1 
ATOM   1682 C  CB   . ASP   A 1 233 ? 19.42400  -1.23900  23.04500 1.000 25.48516 ?  385 ASP   A CB   1 
ATOM   1683 C  CG   . ASP   A 1 233 ? 20.26900  -1.06000  24.28200 1.000 29.82638 ?  385 ASP   A CG   1 
ATOM   1684 O  OD1  . ASP   A 1 233 ? 20.88800  0.01400   24.39200 1.000 33.46753 ?  385 ASP   A OD1  1 
ATOM   1685 O  OD2  . ASP   A 1 233 ? 20.31300  -1.96800  25.14000 1.000 30.35124 ?  385 ASP   A OD2  1 
ATOM   1686 N  N    . LEU   A 1 234 ? 18.71400  -2.77000  20.36300 1.000 22.34325 ?  386 LEU   A N    1 
ATOM   1687 C  CA   . LEU   A 1 234 ? 17.89600  -2.80200  19.15600 1.000 22.86481 ?  386 LEU   A CA   1 
ATOM   1688 C  C    . LEU   A 1 234 ? 17.13000  -4.10800  19.04700 1.000 23.67194 ?  386 LEU   A C    1 
ATOM   1689 O  O    . LEU   A 1 234 ? 16.01900  -4.12300  18.51200 1.000 21.08850 ?  386 LEU   A O    1 
ATOM   1690 C  CB   . LEU   A 1 234 ? 18.75900  -2.59000  17.91200 1.000 19.58589 ?  386 LEU   A CB   1 
ATOM   1691 C  CG   . LEU   A 1 234 ? 19.17100  -1.14500  17.62300 1.000 17.15648 ?  386 LEU   A CG   1 
ATOM   1692 C  CD1  . LEU   A 1 234 ? 20.34200  -1.14600  16.66000 1.000 20.31140 ?  386 LEU   A CD1  1 
ATOM   1693 C  CD2  . LEU   A 1 234 ? 18.01200  -0.33100  17.03300 1.000 18.93874 ?  386 LEU   A CD2  1 
ATOM   1694 N  N    . ARG   A 1 235 ? 17.69900  -5.20800  19.54700 1.000 24.06095 ?  387 ARG   A N    1 
ATOM   1695 C  CA   . ARG   A 1 235 ? 16.95900  -6.46400  19.57600 1.000 24.19211 ?  387 ARG   A CA   1 
ATOM   1696 C  C    . ARG   A 1 235 ? 15.72900  -6.33800  20.46300 1.000 23.69173 ?  387 ARG   A C    1 
ATOM   1697 O  O    . ARG   A 1 235 ? 14.64800  -6.82000  20.11200 1.000 22.53343 ?  387 ARG   A O    1 
ATOM   1698 C  CB   . ARG   A 1 235 ? 17.85600  -7.60100  20.07200 1.000 26.91915 ?  387 ARG   A CB   1 
ATOM   1699 C  CG   . ARG   A 1 235 ? 19.09600  -7.83300  19.22800 1.000 29.70155 ?  387 ARG   A CG   1 
ATOM   1700 C  CD   . ARG   A 1 235 ? 18.74300  -8.45500  17.89400 1.000 34.10092 ?  387 ARG   A CD   1 
ATOM   1701 N  NE   . ARG   A 1 235 ? 19.93500  -8.73200  17.10100 1.000 40.85935 ?  387 ARG   A NE   1 
ATOM   1702 C  CZ   . ARG   A 1 235 ? 20.47100  -9.94000  16.95200 1.000 40.20173 ?  387 ARG   A CZ   1 
ATOM   1703 N  NH1  . ARG   A 1 235 ? 19.92200  -10.99300 17.54200 1.000 40.20703 ?  387 ARG   A NH1  1 
ATOM   1704 N  NH2  . ARG   A 1 235 ? 21.55700  -10.09300 16.21000 1.000 33.30329 ?  387 ARG   A NH2  1 
ATOM   1705 N  N    . SER   A 1 236 ? 15.87500  -5.67800  21.61400 1.000 22.60669 ?  388 SER   A N    1 
ATOM   1706 C  CA   . SER   A 1 236 ? 14.73500  -5.49700  22.50600 1.000 22.48058 ?  388 SER   A CA   1 
ATOM   1707 C  C    . SER   A 1 236 ? 13.68800  -4.59500  21.86600 1.000 23.11394 ?  388 SER   A C    1 
ATOM   1708 O  O    . SER   A 1 236 ? 12.48400  -4.87800  21.93400 1.000 22.10611 ?  388 SER   A O    1 
ATOM   1709 C  CB   . SER   A 1 236 ? 15.20400  -4.92400  23.84400 1.000 27.88086 ?  388 SER   A CB   1 
ATOM   1710 O  OG   . SER   A 1 236 ? 14.10800  -4.56300  24.66900 1.000 32.21594 ?  388 SER   A OG   1 
ATOM   1711 N  N    . LEU   A 1 237 ? 14.13400  -3.51400  21.22200 1.000 19.38561 ?  389 LEU   A N    1 
ATOM   1712 C  CA   . LEU   A 1 237 ? 13.20800  -2.63000  20.52400 1.000 22.11714 ?  389 LEU   A CA   1 
ATOM   1713 C  C    . LEU   A 1 237 ? 12.51100  -3.35600  19.38100 1.000 20.05421 ?  389 LEU   A C    1 
ATOM   1714 O  O    . LEU   A 1 237 ? 11.31900  -3.14400  19.14100 1.000 20.45636 ?  389 LEU   A O    1 
ATOM   1715 C  CB   . LEU   A 1 237 ? 13.95500  -1.40400  20.00400 1.000 18.68579 ?  389 LEU   A CB   1 
ATOM   1716 C  CG   . LEU   A 1 237 ? 14.43500  -0.43600  21.08400 1.000 23.48644 ?  389 LEU   A CG   1 
ATOM   1717 C  CD1  . LEU   A 1 237 ? 15.48200  0.50800   20.52400 1.000 20.56449 ?  389 LEU   A CD1  1 
ATOM   1718 C  CD2  . LEU   A 1 237 ? 13.25800  0.34400   21.65700 1.000 25.77757 ?  389 LEU   A CD2  1 
ATOM   1719 N  N    . ASN   A 1 238 ? 13.25000  -4.20400  18.66000 1.000 18.60517 ?  390 ASN   A N    1 
ATOM   1720 C  CA   . ASN   A 1 238 ? 12.66300  -5.01000  17.59600 1.000 21.28623 ?  390 ASN   A CA   1 
ATOM   1721 C  C    . ASN   A 1 238 ? 11.51400  -5.85200  18.12900 1.000 20.54791 ?  390 ASN   A C    1 
ATOM   1722 O  O    . ASN   A 1 238 ? 10.41500  -5.85300  17.56300 1.000 21.51311 ?  390 ASN   A O    1 
ATOM   1723 C  CB   . ASN   A 1 238 ? 13.74600  -5.89800  16.97100 1.000 20.85952 ?  390 ASN   A CB   1 
ATOM   1724 C  CG   . ASN   A 1 238 ? 13.28900  -6.60200  15.71000 1.000 23.51796 ?  390 ASN   A CG   1 
ATOM   1725 O  OD1  . ASN   A 1 238 ? 12.10600  -6.86200  15.52000 1.000 22.18372 ?  390 ASN   A OD1  1 
ATOM   1726 N  ND2  . ASN   A 1 238 ? 14.23900  -6.92700  14.84000 1.000 21.81488 ?  390 ASN   A ND2  1 
ATOM   1727 N  N    . GLU   A 1 239 ? 11.74800  -6.57200  19.22900 1.000 20.88803 ?  391 GLU   A N    1 
ATOM   1728 C  CA   . GLU   A 1 239 ? 10.71400  -7.45000  19.76200 1.000 20.79061 ?  391 GLU   A CA   1 
ATOM   1729 C  C    . GLU   A 1 239 ? 9.47200   -6.66500  20.16600 1.000 21.35719 ?  391 GLU   A C    1 
ATOM   1730 O  O    . GLU   A 1 239 ? 8.34700   -7.08600  19.87300 1.000 22.32861 ?  391 GLU   A O    1 
ATOM   1731 C  CB   . GLU   A 1 239 ? 11.25800  -8.25500  20.94300 1.000 27.22044 ?  391 GLU   A CB   1 
ATOM   1732 C  CG   . GLU   A 1 239 ? 10.34200  -9.40600  21.35500 1.000 42.63781 ?  391 GLU   A CG   1 
ATOM   1733 C  CD   . GLU   A 1 239 ? 10.35100  -10.55000 20.35200 1.000 54.16604 ?  391 GLU   A CD   1 
ATOM   1734 O  OE1  . GLU   A 1 239 ? 9.31800   -11.24400 20.23200 1.000 60.35167 ?  391 GLU   A OE1  1 
ATOM   1735 O  OE2  . GLU   A 1 239 ? 11.38700  -10.75500 19.68300 1.000 57.39661 ?  391 GLU   A OE2  1 
ATOM   1736 N  N    . GLU   A 1 240 ? 9.65200   -5.50700  20.80600 1.000 19.63304 ?  392 GLU   A N    1 
ATOM   1737 C  CA   . GLU   A 1 240 ? 8.48900   -4.72800  21.21900 1.000 19.77420 ?  392 GLU   A CA   1 
ATOM   1738 C  C    . GLU   A 1 240 ? 7.77900   -4.11700  20.01800 1.000 21.00533 ?  392 GLU   A C    1 
ATOM   1739 O  O    . GLU   A 1 240 ? 6.54400   -4.12100  19.95300 1.000 21.84265 ?  392 GLU   A O    1 
ATOM   1740 C  CB   . GLU   A 1 240 ? 8.89400   -3.63900  22.20800 1.000 21.51062 ?  392 GLU   A CB   1 
ATOM   1741 C  CG   . GLU   A 1 240 ? 7.72900   -2.80400  22.73700 1.000 24.15695 ?  392 GLU   A CG   1 
ATOM   1742 C  CD   . GLU   A 1 240 ? 6.70000   -3.62700  23.49400 1.000 28.51251 ?  392 GLU   A CD   1 
ATOM   1743 O  OE1  . GLU   A 1 240 ? 5.50300   -3.26600  23.45800 1.000 27.03603 ?  392 GLU   A OE1  1 
ATOM   1744 O  OE2  . GLU   A 1 240 ? 7.08300   -4.63400  24.12900 1.000 26.14068 ?  392 GLU   A OE2  1 
ATOM   1745 N  N    . HIS   A 1 241 ? 8.53400   -3.58400  19.05300 1.000 18.82967 ?  393 HIS   A N    1 
ATOM   1746 C  CA   . HIS   A 1 241 ? 7.87400   -3.03600  17.87500 1.000 18.73232 ?  393 HIS   A CA   1 
ATOM   1747 C  C    . HIS   A 1 241 ? 7.10900   -4.11700  17.12500 1.000 19.91434 ?  393 HIS   A C    1 
ATOM   1748 O  O    . HIS   A 1 241 ? 5.98900   -3.88000  16.65600 1.000 20.35924 ?  393 HIS   A O    1 
ATOM   1749 C  CB   . HIS   A 1 241 ? 8.87500   -2.36300  16.94200 1.000 16.91048 ?  393 HIS   A CB   1 
ATOM   1750 C  CG   . HIS   A 1 241 ? 8.26800   -1.97800  15.63100 1.000 17.58872 ?  393 HIS   A CG   1 
ATOM   1751 N  ND1  . HIS   A 1 241 ? 8.23100   -2.83100  14.54800 1.000 16.23144 ?  393 HIS   A ND1  1 
ATOM   1752 C  CD2  . HIS   A 1 241 ? 7.60900   -0.85800  15.25300 1.000 17.87709 ?  393 HIS   A CD2  1 
ATOM   1753 C  CE1  . HIS   A 1 241 ? 7.59800   -2.24000  13.54900 1.000 15.09686 ?  393 HIS   A CE1  1 
ATOM   1754 N  NE2  . HIS   A 1 241 ? 7.21600   -1.04000  13.94900 1.000 17.80301 ?  393 HIS   A NE2  1 
ATOM   1755 N  N    . SER   A 1 242 ? 7.70100   -5.30800  16.99000 1.000 18.08511 ?  394 SER   A N    1 
ATOM   1756 C  CA   . SER   A 1 242 ? 7.02400   -6.39700  16.29500 1.000 19.93505 ?  394 SER   A CA   1 
ATOM   1757 C  C    . SER   A 1 242 ? 5.74800   -6.79800  17.01600 1.000 21.66853 ?  394 SER   A C    1 
ATOM   1758 O  O    . SER   A 1 242 ? 4.72500   -7.06800  16.37600 1.000 22.84646 ?  394 SER   A O    1 
ATOM   1759 C  CB   . SER   A 1 242 ? 7.95000   -7.60500  16.15800 1.000 25.33142 ?  394 SER   A CB   1 
ATOM   1760 O  OG   . SER   A 1 242 ? 9.23800   -7.21400  15.71500 1.000 32.03737 ?  394 SER   A OG   1 
ATOM   1761 N  N    A LYS   A 1 243 ? 5.79300   -6.85500  18.34700 0.760 20.99736 ?  395 LYS   A N    1 
ATOM   1762 N  N    B LYS   A 1 243 ? 5.78800   -6.84900  18.34900 0.240 21.11361 ?  395 LYS   A N    1 
ATOM   1763 C  CA   A LYS   A 1 243 ? 4.59500   -7.17700  19.11400 0.760 21.15954 ?  395 LYS   A CA   1 
ATOM   1764 C  CA   B LYS   A 1 243 ? 4.59100   -7.17900  19.11400 0.240 21.62729 ?  395 LYS   A CA   1 
ATOM   1765 C  C    A LYS   A 1 243 ? 3.48800   -6.17000  18.83300 0.760 21.20694 ?  395 LYS   A C    1 
ATOM   1766 C  C    B LYS   A 1 243 ? 3.48300   -6.16800  18.85100 0.240 21.28649 ?  395 LYS   A C    1 
ATOM   1767 O  O    A LYS   A 1 243 ? 2.34000   -6.54500  18.56400 0.760 22.31787 ?  395 LYS   A O    1 
ATOM   1768 O  O    B LYS   A 1 243 ? 2.32700   -6.54100  18.61500 0.240 22.18220 ?  395 LYS   A O    1 
ATOM   1769 C  CB   A LYS   A 1 243 ? 4.93100   -7.21500  20.60300 0.760 23.70016 ?  395 LYS   A CB   1 
ATOM   1770 C  CB   B LYS   A 1 243 ? 4.92600   -7.23700  20.60300 0.240 24.59051 ?  395 LYS   A CB   1 
ATOM   1771 C  CG   A LYS   A 1 243 ? 3.76000   -7.54800  21.50000 0.760 30.51753 ?  395 LYS   A CG   1 
ATOM   1772 C  CG   B LYS   A 1 243 ? 3.78500   -7.72300  21.47900 0.240 29.68547 ?  395 LYS   A CG   1 
ATOM   1773 C  CD   A LYS   A 1 243 ? 4.16200   -7.49000  22.97000 0.760 32.99666 ?  395 LYS   A CD   1 
ATOM   1774 C  CD   B LYS   A 1 243 ? 3.97100   -7.28500  22.92600 0.240 32.37158 ?  395 LYS   A CD   1 
ATOM   1775 C  CE   A LYS   A 1 243 ? 2.97100   -7.76800  23.87800 0.760 32.96626 ?  395 LYS   A CE   1 
ATOM   1776 C  CE   B LYS   A 1 243 ? 5.41700   -7.43100  23.37500 0.240 32.15694 ?  395 LYS   A CE   1 
ATOM   1777 N  NZ   A LYS   A 1 243 ? 3.32900   -7.65500  25.32000 0.760 40.43885 ?  395 LYS   A NZ   1 
ATOM   1778 N  NZ   B LYS   A 1 243 ? 5.87500   -8.84800  23.34000 0.240 33.96064 ?  395 LYS   A NZ   1 
ATOM   1779 N  N    . GLN   A 1 244 ? 3.82100   -4.87800  18.88200 1.000 20.80044 ?  396 GLN   A N    1 
ATOM   1780 C  CA   . GLN   A 1 244 ? 2.82600   -3.85000  18.61100 1.000 22.89197 ?  396 GLN   A CA   1 
ATOM   1781 C  C    . GLN   A 1 244 ? 2.42600   -3.84500  17.13900 1.000 20.91675 ?  396 GLN   A C    1 
ATOM   1782 O  O    . GLN   A 1 244 ? 1.24600   -3.66100  16.81400 1.000 22.31752 ?  396 GLN   A O    1 
ATOM   1783 C  CB   . GLN   A 1 244 ? 3.36000   -2.48900  19.05800 1.000 21.46584 ?  396 GLN   A CB   1 
ATOM   1784 C  CG   . GLN   A 1 244 ? 3.69300   -2.45800  20.55500 1.000 25.47621 ?  396 GLN   A CG   1 
ATOM   1785 C  CD   . GLN   A 1 244 ? 3.88000   -1.05500  21.09900 1.000 24.81554 ?  396 GLN   A CD   1 
ATOM   1786 O  OE1  . GLN   A 1 244 ? 3.53200   -0.07600  20.44500 1.000 25.08253 ?  396 GLN   A OE1  1 
ATOM   1787 N  NE2  . GLN   A 1 244 ? 4.44500   -0.95300  22.30700 1.000 24.10111 ?  396 GLN   A NE2  1 
ATOM   1788 N  N    . TYR   A 1 245 ? 3.38900   -4.05700  16.23600 1.000 18.25573 ?  397 TYR   A N    1 
ATOM   1789 C  CA   . TYR   A 1 245 ? 3.06200   -4.11500  14.81200 1.000 18.41209 ?  397 TYR   A CA   1 
ATOM   1790 C  C    . TYR   A 1 245 ? 2.10200   -5.25700  14.51200 1.000 20.24404 ?  397 TYR   A C    1 
ATOM   1791 O  O    . TYR   A 1 245 ? 1.14900   -5.09200  13.74100 1.000 19.97578 ?  397 TYR   A O    1 
ATOM   1792 C  CB   . TYR   A 1 245 ? 4.33000   -4.26500  13.96900 1.000 20.50225 ?  397 TYR   A CB   1 
ATOM   1793 C  CG   . TYR   A 1 245 ? 4.01800   -4.46200  12.50100 1.000 18.10962 ?  397 TYR   A CG   1 
ATOM   1794 C  CD1  . TYR   A 1 245 ? 3.83700   -3.37000  11.66100 1.000 18.86971 ?  397 TYR   A CD1  1 
ATOM   1795 C  CD2  . TYR   A 1 245 ? 3.87200   -5.74300  11.95800 1.000 17.35689 ?  397 TYR   A CD2  1 
ATOM   1796 C  CE1  . TYR   A 1 245 ? 3.53000   -3.54600  10.32000 1.000 19.44146 ?  397 TYR   A CE1  1 
ATOM   1797 C  CE2  . TYR   A 1 245 ? 3.56200   -5.92000  10.61800 1.000 16.65438 ?  397 TYR   A CE2  1 
ATOM   1798 C  CZ   . TYR   A 1 245 ? 3.39500   -4.81900  9.81100  1.000 16.23278 ?  397 TYR   A CZ   1 
ATOM   1799 O  OH   . TYR   A 1 245 ? 3.08800   -4.99600  8.47900  1.000 18.66069 ?  397 TYR   A OH   1 
ATOM   1800 N  N    . ARG   A 1 246 ? 2.35200   -6.43400  15.09300 1.000 18.23737 ?  398 ARG   A N    1 
ATOM   1801 C  CA   . ARG   A 1 246 ? 1.46100   -7.56800  14.86600 1.000 19.96697 ?  398 ARG   A CA   1 
ATOM   1802 C  C    . ARG   A 1 246 ? 0.05900   -7.26900  15.37500 1.000 22.85650 ?  398 ARG   A C    1 
ATOM   1803 O  O    . ARG   A 1 246 ? -0.93300  -7.61300  14.72300 1.000 23.92721 ?  398 ARG   A O    1 
ATOM   1804 C  CB   . ARG   A 1 246 ? 2.02200   -8.82700  15.53300 1.000 23.63739 ?  398 ARG   A CB   1 
ATOM   1805 C  CG   . ARG   A 1 246 ? 3.28300   -9.37300  14.87300 1.000 28.49190 ?  398 ARG   A CG   1 
ATOM   1806 C  CD   . ARG   A 1 246 ? 3.66100   -10.74600 15.42800 1.000 39.56985 ?  398 ARG   A CD   1 
ATOM   1807 N  NE   . ARG   A 1 246 ? 4.01400   -10.70800 16.84900 1.000 45.77941 ?  398 ARG   A NE   1 
ATOM   1808 C  CZ   . ARG   A 1 246 ? 5.25600   -10.59300 17.31300 1.000 43.17947 ?  398 ARG   A CZ   1 
ATOM   1809 N  NH1  . ARG   A 1 246 ? 6.27400   -10.49700 16.47200 1.000 42.97219 ?  398 ARG   A NH1  1 
ATOM   1810 N  NH2  . ARG   A 1 246 ? 5.48000   -10.57100 18.62000 1.000 42.29970 ?  398 ARG   A NH2  1 
ATOM   1811 N  N    . SER   A 1 247 ? -0.04400  -6.62300  16.53800 1.000 20.61299 ?  399 SER   A N    1 
ATOM   1812 C  CA   . SER   A 1 247 ? -1.35600  -6.28100  17.07700 1.000 23.12615 ?  399 SER   A CA   1 
ATOM   1813 C  C    . SER   A 1 247 ? -2.05600  -5.24400  16.20400 1.000 24.51508 ?  399 SER   A C    1 
ATOM   1814 O  O    . SER   A 1 247 ? -3.26600  -5.33600  15.96000 1.000 25.45198 ?  399 SER   A O    1 
ATOM   1815 C  CB   . SER   A 1 247 ? -1.20700  -5.77100  18.51200 1.000 28.93656 ?  399 SER   A CB   1 
ATOM   1816 O  OG   . SER   A 1 247 ? -2.33700  -5.01400  18.91800 1.000 38.81291 ?  399 SER   A OG   1 
ATOM   1817 N  N    . LEU   A 1 248 ? -1.31300  -4.24900  15.72200 1.000 24.55973 ?  400 LEU   A N    1 
ATOM   1818 C  CA   . LEU   A 1 248 ? -1.91900  -3.22700  14.87600 1.000 20.63054 ?  400 LEU   A CA   1 
ATOM   1819 C  C    . LEU   A 1 248 ? -2.32200  -3.79900  13.52300 1.000 22.24919 ?  400 LEU   A C    1 
ATOM   1820 O  O    . LEU   A 1 248 ? -3.44700  -3.57700  13.05400 1.000 24.51554 ?  400 LEU   A O    1 
ATOM   1821 C  CB   . LEU   A 1 248 ? -0.95500  -2.05800  14.69800 1.000 18.81533 ?  400 LEU   A CB   1 
ATOM   1822 C  CG   . LEU   A 1 248 ? -0.72300  -1.19300  15.93600 1.000 21.98759 ?  400 LEU   A CG   1 
ATOM   1823 C  CD1  . LEU   A 1 248 ? 0.51200   -0.32800  15.72900 1.000 18.36947 ?  400 LEU   A CD1  1 
ATOM   1824 C  CD2  . LEU   A 1 248 ? -1.94800  -0.33300  16.24800 1.000 22.45206 ?  400 LEU   A CD2  1 
ATOM   1825 N  N    . SER   A 1 249 ? -1.41900  -4.55200  12.88600 1.000 22.33817 ?  401 SER   A N    1 
ATOM   1826 C  CA   . SER   A 1 249 ? -1.66800  -5.04800  11.53600 1.000 23.32898 ?  401 SER   A CA   1 
ATOM   1827 C  C    . SER   A 1 249 ? -2.66900  -6.19100  11.51700 1.000 27.09486 ?  401 SER   A C    1 
ATOM   1828 O  O    . SER   A 1 249 ? -3.20800  -6.50500  10.45000 1.000 27.95342 ?  401 SER   A O    1 
ATOM   1829 C  CB   . SER   A 1 249 ? -0.36100  -5.49600  10.87100 1.000 21.63395 ?  401 SER   A CB   1 
ATOM   1830 O  OG   . SER   A 1 249 ? 0.25900   -6.56000  11.57500 1.000 23.35985 ?  401 SER   A OG   1 
ATOM   1831 N  N    . PHE   A 1 250 ? -2.93300  -6.81400  12.67000 1.000 23.58668 ?  402 PHE   A N    1 
ATOM   1832 C  CA   . PHE   A 1 250 ? -3.95800  -7.85000  12.73800 1.000 26.46106 ?  402 PHE   A CA   1 
ATOM   1833 C  C    . PHE   A 1 250 ? -5.33300  -7.29500  12.40500 1.000 31.70752 ?  402 PHE   A C    1 
ATOM   1834 O  O    . PHE   A 1 250 ? -6.19300  -8.03000  11.90700 1.000 28.05752 ?  402 PHE   A O    1 
ATOM   1835 C  CB   . PHE   A 1 250 ? -3.96300  -8.49200  14.12600 1.000 30.72695 ?  402 PHE   A CB   1 
ATOM   1836 C  CG   . PHE   A 1 250 ? -4.81700  -9.72600  14.22200 1.000 39.02371 ?  402 PHE   A CG   1 
ATOM   1837 C  CD1  . PHE   A 1 250 ? -6.03900  -9.69000  14.87300 1.000 43.45025 ?  402 PHE   A CD1  1 
ATOM   1838 C  CD2  . PHE   A 1 250 ? -4.39300  -10.92400 13.66400 1.000 40.92086 ?  402 PHE   A CD2  1 
ATOM   1839 C  CE1  . PHE   A 1 250 ? -6.82700  -10.82300 14.96500 1.000 47.09426 ?  402 PHE   A CE1  1 
ATOM   1840 C  CE2  . PHE   A 1 250 ? -5.17500  -12.06000 13.75200 1.000 45.21440 ?  402 PHE   A CE2  1 
ATOM   1841 C  CZ   . PHE   A 1 250 ? -6.39500  -12.00900 14.40500 1.000 45.42165 ?  402 PHE   A CZ   1 
ATOM   1842 N  N    . GLN   A 1 251 ? -5.56300  -6.01600  12.68000 1.000 25.29509 ?  403 GLN   A N    1 
ATOM   1843 C  CA   . GLN   A 1 251 ? -6.82600  -5.38300  12.32300 1.000 25.50589 ?  403 GLN   A CA   1 
ATOM   1844 C  C    . GLN   A 1 251 ? -6.78700  -5.00500  10.84900 1.000 23.36730 ?  403 GLN   A C    1 
ATOM   1845 O  O    . GLN   A 1 251 ? -5.96800  -4.16500  10.46000 1.000 20.59830 ?  403 GLN   A O    1 
ATOM   1846 C  CB   . GLN   A 1 251 ? -7.07200  -4.14500  13.17600 1.000 28.37036 ?  403 GLN   A CB   1 
ATOM   1847 C  CG   . GLN   A 1 251 ? -7.03300  -4.39800  14.67300 1.000 34.68173 ?  403 GLN   A CG   1 
ATOM   1848 C  CD   . GLN   A 1 251 ? -8.10200  -5.37600  15.12300 1.000 42.12241 ?  403 GLN   A CD   1 
ATOM   1849 O  OE1  . GLN   A 1 251 ? -7.82300  -6.32300  15.86200 1.000 47.29935 ?  403 GLN   A OE1  1 
ATOM   1850 N  NE2  . GLN   A 1 251 ? -9.33400  -5.15500  14.67500 1.000 42.92799 ?  403 GLN   A NE2  1 
ATOM   1851 N  N    . PRO   A 1 252 ? -7.63400  -5.59300  10.00100 1.000 26.57887 ?  404 PRO   A N    1 
ATOM   1852 C  CA   . PRO   A 1 252 ? -7.51100  -5.32800  8.55900  1.000 23.75935 ?  404 PRO   A CA   1 
ATOM   1853 C  C    . PRO   A 1 252 ? -7.65700  -3.86400  8.20900  1.000 24.09488 ?  404 PRO   A C    1 
ATOM   1854 O  O    . PRO   A 1 252 ? -7.03100  -3.40700  7.24400  1.000 24.85846 ?  404 PRO   A O    1 
ATOM   1855 C  CB   . PRO   A 1 252 ? -8.63600  -6.17800  7.94500  1.000 29.27719 ?  404 PRO   A CB   1 
ATOM   1856 C  CG   . PRO   A 1 252 ? -8.95400  -7.20900  8.99100  1.000 35.11958 ?  404 PRO   A CG   1 
ATOM   1857 C  CD   . PRO   A 1 252 ? -8.72800  -6.53100  10.30400 1.000 30.44716 ?  404 PRO   A CD   1 
ATOM   1858 N  N    . GLU   A 1 253 ? -8.44300  -3.10300  8.97800  1.000 27.53050 ?  405 GLU   A N    1 
ATOM   1859 C  CA   . GLU   A 1 253 ? -8.58300  -1.67900  8.69400  1.000 30.40648 ?  405 GLU   A CA   1 
ATOM   1860 C  C    . GLU   A 1 253 ? -7.26900  -0.93500  8.88400  1.000 27.23489 ?  405 GLU   A C    1 
ATOM   1861 O  O    . GLU   A 1 253 ? -7.03500  0.07700   8.21600  1.000 23.91362 ?  405 GLU   A O    1 
ATOM   1862 C  CB   . GLU   A 1 253 ? -9.68000  -1.06600  9.56400  1.000 33.63145 ?  405 GLU   A CB   1 
ATOM   1863 C  CG   . GLU   A 1 253 ? -9.38500  -1.06400  11.04600 1.000 43.38765 ?  405 GLU   A CG   1 
ATOM   1864 C  CD   . GLU   A 1 253 ? -9.85600  -2.32600  11.73900 1.000 46.18470 ?  405 GLU   A CD   1 
ATOM   1865 O  OE1  . GLU   A 1 253 ? -10.12900 -2.26600  12.95700 1.000 50.83884 ?  405 GLU   A OE1  1 
ATOM   1866 O  OE2  . GLU   A 1 253 ? -9.94800  -3.37900  11.07200 1.000 42.08709 ?  405 GLU   A OE2  1 
ATOM   1867 N  N    . ASN   A 1 254 ? -6.39400  -1.42200  9.77000  1.000 24.12466 ?  406 ASN   A N    1 
ATOM   1868 C  CA   . ASN   A 1 254 ? -5.07400  -0.81700  9.91200  1.000 22.32288 ?  406 ASN   A CA   1 
ATOM   1869 C  C    . ASN   A 1 254 ? -4.12400  -1.29600  8.82000  1.000 18.57878 ?  406 ASN   A C    1 
ATOM   1870 O  O    . ASN   A 1 254 ? -3.37100  -0.49200  8.25900  1.000 18.64100 ?  406 ASN   A O    1 
ATOM   1871 C  CB   . ASN   A 1 254 ? -4.48200  -1.12600  11.29300 1.000 21.88832 ?  406 ASN   A CB   1 
ATOM   1872 C  CG   . ASN   A 1 254 ? -5.26400  -0.48300  12.42300 1.000 26.88689 ?  406 ASN   A CG   1 
ATOM   1873 O  OD1  . ASN   A 1 254 ? -6.07700  0.40600   12.19500 1.000 26.82437 ?  406 ASN   A OD1  1 
ATOM   1874 N  ND2  . ASN   A 1 254 ? -5.01900  -0.93300  13.65100 1.000 26.36863 ?  406 ASN   A ND2  1 
ATOM   1875 N  N    . SER   A 1 255 ? -4.14100  -2.59800  8.51000  1.000 20.66370 ?  407 SER   A N    1 
ATOM   1876 C  CA   . SER   A 1 255 ? -3.29500  -3.11600  7.43600  1.000 21.25004 ?  407 SER   A CA   1 
ATOM   1877 C  C    . SER   A 1 255 ? -3.59600  -2.42500  6.11400  1.000 21.55468 ?  407 SER   A C    1 
ATOM   1878 O  O    . SER   A 1 255 ? -2.68700  -2.18400  5.31100  1.000 19.17254 ?  407 SER   A O    1 
ATOM   1879 C  CB   . SER   A 1 255 ? -3.48600  -4.62500  7.30100  1.000 26.84298 ?  407 SER   A CB   1 
ATOM   1880 O  OG   . SER   A 1 255 ? -2.66700  -5.31300  8.23000  1.000 32.10762 ?  407 SER   A OG   1 
ATOM   1881 N  N    . MET   A 1 256 ? -4.86500  -2.09100  5.88300  1.000 19.04579 ?  408 MET   A N    1 
ATOM   1882 C  CA   . MET   A 1 256 ? -5.26600  -1.35800  4.68500  1.000 22.86087 ?  408 MET   A CA   1 
ATOM   1883 C  C    . MET   A 1 256 ? -4.50800  -0.04300  4.52900  1.000 24.37738 ?  408 MET   A C    1 
ATOM   1884 O  O    . MET   A 1 256 ? -4.30300  0.42700   3.40400  1.000 19.48218 ?  408 MET   A O    1 
ATOM   1885 C  CB   . MET   A 1 256 ? -6.76900  -1.09500  4.75100  1.000 23.58128 ?  408 MET   A CB   1 
ATOM   1886 C  CG   . MET   A 1 256 ? -7.44100  -0.83900  3.44900  1.000 29.02227 ?  408 MET   A CG   1 
ATOM   1887 S  SD   . MET   A 1 256 ? -9.21300  -1.00200  3.71400  1.000 27.52806 ?  408 MET   A SD   1 
ATOM   1888 C  CE   . MET   A 1 256 ? -9.52500  0.25000   4.96000  1.000 26.22356 ?  408 MET   A CE   1 
ATOM   1889 N  N    . LYS   A 1 257 ? -4.08600  0.56400   5.63900  1.000 18.76622 ?  409 LYS   A N    1 
ATOM   1890 C  CA   . LYS   A 1 257 ? -3.37000  1.83000   5.60300  1.000 16.36236 ?  409 LYS   A CA   1 
ATOM   1891 C  C    . LYS   A 1 257 ? -1.86500  1.66300   5.41800  1.000 16.16197 ?  409 LYS   A C    1 
ATOM   1892 O  O    . LYS   A 1 257 ? -1.16200  2.66700   5.26500  1.000 20.04839 ?  409 LYS   A O    1 
ATOM   1893 C  CB   . LYS   A 1 257 ? -3.63400  2.62800   6.89000  1.000 20.40444 ?  409 LYS   A CB   1 
ATOM   1894 C  CG   . LYS   A 1 257 ? -5.10400  2.94000   7.15500  1.000 28.02243 ?  409 LYS   A CG   1 
ATOM   1895 C  CD   . LYS   A 1 257 ? -5.67900  3.84000   6.06900  1.000 39.26192 ?  409 LYS   A CD   1 
ATOM   1896 C  CE   . LYS   A 1 257 ? -7.20500  3.88000   6.11500  1.000 46.73566 ?  409 LYS   A CE   1 
ATOM   1897 N  NZ   . LYS   A 1 257 ? -7.80900  3.77600   4.75100  1.000 47.87152 ?  409 LYS   A NZ   1 
ATOM   1898 N  N    . LEU   A 1 258 ? -1.35400  0.43600   5.42800  1.000 15.54434 ?  410 LEU   A N    1 
ATOM   1899 C  CA   . LEU   A 1 258 ? 0.07700   0.21500   5.25500  1.000 16.60729 ?  410 LEU   A CA   1 
ATOM   1900 C  C    . LEU   A 1 258 ? 0.40500   0.24000   3.76100  1.000 14.66666 ?  410 LEU   A C    1 
ATOM   1901 O  O    . LEU   A 1 258 ? -0.39800  0.67700   2.93100  1.000 17.87322 ?  410 LEU   A O    1 
ATOM   1902 C  CB   . LEU   A 1 258 ? 0.49500   -1.08700  5.93300  1.000 16.64679 ?  410 LEU   A CB   1 
ATOM   1903 C  CG   . LEU   A 1 258 ? 0.13900   -1.11500  7.42300  1.000 16.64320 ?  410 LEU   A CG   1 
ATOM   1904 C  CD1  . LEU   A 1 258 ? 0.48800   -2.46700  8.03100  1.000 20.92234 ?  410 LEU   A CD1  1 
ATOM   1905 C  CD2  . LEU   A 1 258 ? 0.83500   0.03700   8.17500  1.000 15.79868 ?  410 LEU   A CD2  1 
ATOM   1906 N  N    . THR   A 1 259 ? 1.60500   -0.20000  3.40300  1.000 15.72119 ?  411 THR   A N    1 
ATOM   1907 C  CA   . THR   A 1 259 ? 2.03800   -0.26300  2.01800  1.000 17.35869 ?  411 THR   A CA   1 
ATOM   1908 C  C    . THR   A 1 259 ? 2.36100   -1.70200  1.66700  1.000 16.02224 ?  411 THR   A C    1 
ATOM   1909 O  O    . THR   A 1 259 ? 2.60900   -2.52300  2.55700  1.000 16.71490 ?  411 THR   A O    1 
ATOM   1910 C  CB   . THR   A 1 259 ? 3.28600   0.59500   1.76000  1.000 13.00481 ?  411 THR   A CB   1 
ATOM   1911 O  OG1  . THR   A 1 259 ? 4.42500   -0.06100  2.33500  1.000 15.03024 ?  411 THR   A OG1  1 
ATOM   1912 C  CG2  . THR   A 1 259 ? 3.13200   1.99000   2.35500  1.000 16.79680 ?  411 THR   A CG2  1 
ATOM   1913 N  N    . PRO   A 1 260 ? 2.37000   -2.04400  0.37500  1.000 16.48121 ?  412 PRO   A N    1 
ATOM   1914 C  CA   . PRO   A 1 260 ? 2.74100   -3.41300  -0.00300 1.000 15.98824 ?  412 PRO   A CA   1 
ATOM   1915 C  C    . PRO   A 1 260 ? 4.09200   -3.83400  0.53700  1.000 15.81569 ?  412 PRO   A C    1 
ATOM   1916 O  O    . PRO   A 1 260 ? 4.24000   -4.96700  1.01400  1.000 17.64625 ?  412 PRO   A O    1 
ATOM   1917 C  CB   . PRO   A 1 260 ? 2.73100   -3.35600  -1.53400 1.000 18.43405 ?  412 PRO   A CB   1 
ATOM   1918 C  CG   . PRO   A 1 260 ? 1.71300   -2.30900  -1.85300 1.000 17.04199 ?  412 PRO   A CG   1 
ATOM   1919 C  CD   . PRO   A 1 260 ? 1.88700   -1.26500  -0.77800 1.000 14.50503 ?  412 PRO   A CD   1 
ATOM   1920 N  N    . LEU   A 1 261 ? 5.08700   -2.94000  0.49700  1.000 14.82566 ?  413 LEU   A N    1 
ATOM   1921 C  CA   . LEU   A 1 261 ? 6.42100   -3.32000  0.95900  1.000 16.61075 ?  413 LEU   A CA   1 
ATOM   1922 C  C    . LEU   A 1 261 ? 6.46100   -3.51300  2.46900  1.000 16.24091 ?  413 LEU   A C    1 
ATOM   1923 O  O    . LEU   A 1 261 ? 7.12800   -4.43000  2.96300  1.000 16.08522 ?  413 LEU   A O    1 
ATOM   1924 C  CB   . LEU   A 1 261 ? 7.44700   -2.27500  0.53400  1.000 15.24395 ?  413 LEU   A CB   1 
ATOM   1925 C  CG   . LEU   A 1 261 ? 8.90100   -2.65800  0.83800  1.000 17.10022 ?  413 LEU   A CG   1 
ATOM   1926 C  CD1  . LEU   A 1 261 ? 9.32500   -3.86600  -0.01900 1.000 17.62558 ?  413 LEU   A CD1  1 
ATOM   1927 C  CD2  . LEU   A 1 261 ? 9.76700   -1.46600  0.55500  1.000 17.58893 ?  413 LEU   A CD2  1 
ATOM   1928 N  N    . VAL   A 1 262 ? 5.76100   -2.66200  3.22600  1.000 15.89518 ?  414 VAL   A N    1 
ATOM   1929 C  CA   . VAL   A 1 262 ? 5.71300   -2.85300  4.67400  1.000 15.07573 ?  414 VAL   A CA   1 
ATOM   1930 C  C    . VAL   A 1 262 ? 5.10200   -4.21000  5.00600  1.000 15.30608 ?  414 VAL   A C    1 
ATOM   1931 O  O    . VAL   A 1 262 ? 5.64600   -4.97600  5.80900  1.000 18.34558 ?  414 VAL   A O    1 
ATOM   1932 C  CB   . VAL   A 1 262 ? 4.95100   -1.70000  5.34700  1.000 16.14680 ?  414 VAL   A CB   1 
ATOM   1933 C  CG1  . VAL   A 1 262 ? 4.57700   -2.07800  6.78700  1.000 16.48144 ?  414 VAL   A CG1  1 
ATOM   1934 C  CG2  . VAL   A 1 262 ? 5.81100   -0.43200  5.31400  1.000 14.07234 ?  414 VAL   A CG2  1 
ATOM   1935 N  N    . LEU   A 1 263 ? 3.98000   -4.54300  4.36600  1.000 15.64887 ?  415 LEU   A N    1 
ATOM   1936 C  CA   . LEU   A 1 263 ? 3.35900   -5.84600  4.60200  1.000 16.38280 ?  415 LEU   A CA   1 
ATOM   1937 C  C    . LEU   A 1 263 ? 4.30000   -6.99300  4.23300  1.000 17.57860 ?  415 LEU   A C    1 
ATOM   1938 O  O    . LEU   A 1 263 ? 4.36900   -8.00500  4.94100  1.000 21.48232 ?  415 LEU   A O    1 
ATOM   1939 C  CB   . LEU   A 1 263 ? 2.05200   -5.94600  3.81500  1.000 18.16087 ?  415 LEU   A CB   1 
ATOM   1940 C  CG   . LEU   A 1 263 ? 0.93800   -5.06900  4.39200  1.000 19.51559 ?  415 LEU   A CG   1 
ATOM   1941 C  CD1  . LEU   A 1 263 ? -0.31000  -5.11300  3.52200  1.000 17.41441 ?  415 LEU   A CD1  1 
ATOM   1942 C  CD2  . LEU   A 1 263 ? 0.62100   -5.50500  5.81300  1.000 17.81400 ?  415 LEU   A CD2  1 
ATOM   1943 N  N    . GLU   A 1 264 ? 5.03700   -6.85500  3.13200  1.000 19.15172 ?  416 GLU   A N    1 
ATOM   1944 C  CA   . GLU   A 1 264 ? 5.92100   -7.93600  2.70700  1.000 23.20569 ?  416 GLU   A CA   1 
ATOM   1945 C  C    . GLU   A 1 264 ? 7.08600   -8.11400  3.67500  1.000 22.98312 ?  416 GLU   A C    1 
ATOM   1946 O  O    . GLU   A 1 264 ? 7.43800   -9.24400  4.04100  1.000 22.46327 ?  416 GLU   A O    1 
ATOM   1947 C  CB   . GLU   A 1 264 ? 6.43900   -7.66500  1.29400  1.000 23.13350 ?  416 GLU   A CB   1 
ATOM   1948 C  CG   . GLU   A 1 264 ? 7.11700   -8.86600  0.66000  1.000 25.48835 ?  416 GLU   A CG   1 
ATOM   1949 C  CD   . GLU   A 1 264 ? 7.75900   -8.53600  -0.66800 1.000 25.51339 ?  416 GLU   A CD   1 
ATOM   1950 O  OE1  . GLU   A 1 264 ? 8.97800   -8.26800  -0.68800 1.000 25.92413 ?  416 GLU   A OE1  1 
ATOM   1951 O  OE2  . GLU   A 1 264 ? 7.04900   -8.54900  -1.69100 1.000 27.47143 ?  416 GLU   A OE2  1 
ATOM   1952 N  N    . VAL   A 1 265 ? 7.68200   -7.01200  4.11600  1.000 17.89643 ?  417 VAL   A N    1 
ATOM   1953 C  CA   . VAL   A 1 265 ? 8.91300   -7.08100  4.89400  1.000 16.06899 ?  417 VAL   A CA   1 
ATOM   1954 C  C    . VAL   A 1 265 ? 8.63500   -7.21800  6.38600  1.000 23.24401 ?  417 VAL   A C    1 
ATOM   1955 O  O    . VAL   A 1 265 ? 9.30500   -7.99100  7.07500  1.000 26.48468 ?  417 VAL   A O    1 
ATOM   1956 C  CB   . VAL   A 1 265 ? 9.77900   -5.84600  4.58600  1.000 17.11839 ?  417 VAL   A CB   1 
ATOM   1957 C  CG1  . VAL   A 1 265 ? 11.00600  -5.80600  5.49300  1.000 19.63143 ?  417 VAL   A CG1  1 
ATOM   1958 C  CG2  . VAL   A 1 265 ? 10.19900  -5.86500  3.12000  1.000 18.72778 ?  417 VAL   A CG2  1 
ATOM   1959 N  N    . PHE   A 1 266 ? 7.65500   -6.47900  6.91600  1.000 23.37262 ?  418 PHE   A N    1 
ATOM   1960 C  CA   . PHE   A 1 266 ? 7.33500   -6.57200  8.33600  1.000 20.42683 ?  418 PHE   A CA   1 
ATOM   1961 C  C    . PHE   A 1 266 ? 6.37900   -7.71600  8.64100  1.000 24.73907 ?  418 PHE   A C    1 
ATOM   1962 O  O    . PHE   A 1 266 ? 6.33700   -8.18300  9.78400  1.000 27.48706 ?  418 PHE   A O    1 
ATOM   1963 C  CB   . PHE   A 1 266 ? 6.71200   -5.26900  8.85200  1.000 18.98899 ?  418 PHE   A CB   1 
ATOM   1964 C  CG   . PHE   A 1 266 ? 7.69600   -4.15200  9.09400  1.000 19.33012 ?  418 PHE   A CG   1 
ATOM   1965 C  CD1  . PHE   A 1 266 ? 7.26100   -2.94900  9.62700  1.000 19.48982 ?  418 PHE   A CD1  1 
ATOM   1966 C  CD2  . PHE   A 1 266 ? 9.04800   -4.29500  8.80100  1.000 22.14342 ?  418 PHE   A CD2  1 
ATOM   1967 C  CE1  . PHE   A 1 266 ? 8.13500   -1.90900  9.85900  1.000 20.45811 ?  418 PHE   A CE1  1 
ATOM   1968 C  CE2  . PHE   A 1 266 ? 9.93700   -3.25100  9.03100  1.000 20.23099 ?  418 PHE   A CE2  1 
ATOM   1969 C  CZ   . PHE   A 1 266 ? 9.48300   -2.06000  9.56400  1.000 21.20498 ?  418 PHE   A CZ   1 
ATOM   1970 N  N    . GLY   A 1 267 ? 5.61300   -8.17400  7.65700  1.000 28.46134 ?  419 GLY   A N    1 
ATOM   1971 C  CA   . GLY   A 1 267 ? 4.72200   -9.29100  7.88200  1.000 33.24690 ?  419 GLY   A CA   1 
ATOM   1972 C  C    . GLY   A 1 267 ? 3.27100   -8.97500  7.59600  1.000 38.06033 ?  419 GLY   A C    1 
ATOM   1973 O  O    . GLY   A 1 267 ? 2.83800   -7.82100  7.70300  1.000 27.89269 ?  419 GLY   A O    1 
ATOM   1974 N  N    . ASN   A 1 268 ? 2.51700   -10.01100 7.23600  1.000 42.20244 ?  420 ASN   A N    1 
ATOM   1975 C  CA   . ASN   A 1 268 ? 1.10900   -9.89400  6.88300  1.000 49.20184 ?  420 ASN   A CA   1 
ATOM   1976 C  C    . ASN   A 1 268 ? 0.30900   -11.02300 7.52400  1.000 55.57466 ?  420 ASN   A C    1 
ATOM   1977 O  O    . ASN   A 1 268 ? 0.54300   -12.19800 7.24200  1.000 63.14041 ?  420 ASN   A O    1 
ATOM   1978 C  CB   . ASN   A 1 268 ? 0.93600   -9.92100  5.36200  1.000 53.13755 ?  420 ASN   A CB   1 
ATOM   1979 C  CG   . ASN   A 1 268 ? -0.38800  -9.32600  4.91200  1.000 57.87153 ?  420 ASN   A CG   1 
ATOM   1980 O  OD1  . ASN   A 1 268 ? -0.65500  -9.21900  3.71500  1.000 56.61679 ?  420 ASN   A OD1  1 
ATOM   1981 N  ND2  . ASN   A 1 268 ? -1.22300  -8.93600  5.87000  1.000 61.29100 ?  420 ASN   A ND2  1 
ATOM   1982 N  N    . LYS   B 2 1   ? 6.17400   -17.39200 2.35900  1.000 69.99168 ?  625 LYS   C N    1 
ATOM   1983 C  CA   . LYS   B 2 1   ? 5.70200   -16.63600 1.20500  1.000 66.33495 ?  625 LYS   C CA   1 
ATOM   1984 C  C    . LYS   B 2 1   ? 6.86500   -16.22500 0.31300  1.000 63.19419 ?  625 LYS   C C    1 
ATOM   1985 O  O    . LYS   B 2 1   ? 8.02800   -16.43600 0.65300  1.000 62.46399 ?  625 LYS   C O    1 
ATOM   1986 C  CB   . LYS   B 2 1   ? 4.92700   -15.39300 1.65400  1.000 65.25862 ?  625 LYS   C CB   1 
ATOM   1987 C  CG   . LYS   B 2 1   ? 5.79000   -14.32100 2.31300  1.000 62.46132 ?  625 LYS   C CG   1 
ATOM   1988 C  CD   . LYS   B 2 1   ? 4.99400   -13.05000 2.59600  1.000 61.07268 ?  625 LYS   C CD   1 
ATOM   1989 C  CE   . LYS   B 2 1   ? 5.82600   -12.03000 3.37000  1.000 56.14049 ?  625 LYS   C CE   1 
ATOM   1990 N  NZ   . LYS   B 2 1   ? 4.99200   -11.17300 4.25500  1.000 52.10228 ?  625 LYS   C NZ   1 
ATOM   1991 N  N    . ASN   B 2 2   ? 6.54400   -15.64900 -0.83700 1.000 59.71499 ?  626 ASN   C N    1 
ATOM   1992 C  CA   . ASN   B 2 2   ? 7.55600   -15.02500 -1.67000 1.000 55.85820 ?  626 ASN   C CA   1 
ATOM   1993 C  C    . ASN   B 2 2   ? 7.70300   -13.56100 -1.27500 1.000 45.32958 ?  626 ASN   C C    1 
ATOM   1994 O  O    . ASN   B 2 2   ? 6.80800   -12.96000 -0.67500 1.000 42.55998 ?  626 ASN   C O    1 
ATOM   1995 C  CB   . ASN   B 2 2   ? 7.19800   -15.15000 -3.15200 1.000 61.71489 ?  626 ASN   C CB   1 
ATOM   1996 C  CG   . ASN   B 2 2   ? 7.46100   -16.54100 -3.69700 1.000 70.75770 ?  626 ASN   C CG   1 
ATOM   1997 O  OD1  . ASN   B 2 2   ? 7.25200   -17.53900 -3.00600 1.000 72.69211 ?  626 ASN   C OD1  1 
ATOM   1998 N  ND2  . ASN   B 2 2   ? 7.92800   -16.61300 -4.93900 1.000 73.77717 ?  626 ASN   C ND2  1 
ATOM   1999 N  N    . HIS   B 2 3   ? 8.85900   -12.99300 -1.60000 1.000 36.33289 ?  627 HIS   C N    1 
ATOM   2000 C  CA   . HIS   B 2 3   ? 9.15700   -11.59100 -1.30900 1.000 28.95019 ?  627 HIS   C CA   1 
ATOM   2001 C  C    . HIS   B 2 3   ? 9.61600   -10.91500 -2.59200 1.000 24.28371 ?  627 HIS   C C    1 
ATOM   2002 O  O    . HIS   B 2 3   ? 10.77500  -10.49800 -2.71300 1.000 23.99532 ?  627 HIS   C O    1 
ATOM   2003 C  CB   . HIS   B 2 3   ? 10.20300  -11.46600 -0.20200 1.000 29.27283 ?  627 HIS   C CB   1 
ATOM   2004 C  CG   . HIS   B 2 3   ? 9.81200   -12.15200 1.06900  1.000 30.37178 ?  627 HIS   C CG   1 
ATOM   2005 N  ND1  . HIS   B 2 3   ? 9.91600   -13.51600 1.24200  1.000 32.85044 ?  627 HIS   C ND1  1 
ATOM   2006 C  CD2  . HIS   B 2 3   ? 9.30600   -11.66400 2.22600  1.000 29.76615 ?  627 HIS   C CD2  1 
ATOM   2007 C  CE1  . HIS   B 2 3   ? 9.49900   -13.83700 2.45300  1.000 34.19099 ?  627 HIS   C CE1  1 
ATOM   2008 N  NE2  . HIS   B 2 3   ? 9.11900   -12.73200 3.07000  1.000 33.45373 ?  627 HIS   C NE2  1 
ATOM   2009 N  N    . PRO   B 2 4   ? 8.71500   -10.77400 -3.57200 1.000 26.72708 ?  628 PRO   C N    1 
ATOM   2010 C  CA   . PRO   B 2 4   ? 9.14600   -10.24900 -4.87800 1.000 24.96897 ?  628 PRO   C CA   1 
ATOM   2011 C  C    . PRO   B 2 4   ? 9.60500   -8.80700  -4.83000 1.000 24.60422 ?  628 PRO   C C    1 
ATOM   2012 O  O    . PRO   B 2 4   ? 10.52600  -8.43300  -5.56400 1.000 27.20406 ?  628 PRO   C O    1 
ATOM   2013 C  CB   . PRO   B 2 4   ? 7.89300   -10.41800 -5.75200 1.000 26.70229 ?  628 PRO   C CB   1 
ATOM   2014 C  CG   . PRO   B 2 4   ? 6.75900   -10.41400 -4.78600 1.000 27.20772 ?  628 PRO   C CG   1 
ATOM   2015 C  CD   . PRO   B 2 4   ? 7.27700   -11.10300 -3.55900 1.000 27.44695 ?  628 PRO   C CD   1 
ATOM   2016 N  N    A MET   B 2 5   ? 8.98500   -7.97000  -3.99500 0.520 24.64801 ?  629 MET   C N    1 
ATOM   2017 N  N    B MET   B 2 5   ? 8.98200   -7.97200  -3.99600 0.480 24.62634 ?  629 MET   C N    1 
ATOM   2018 C  CA   A MET   B 2 5   ? 9.39900   -6.57200  -3.95000 0.520 23.54145 ?  629 MET   C CA   1 
ATOM   2019 C  CA   B MET   B 2 5   ? 9.39500   -6.57600  -3.94600 0.480 23.55855 ?  629 MET   C CA   1 
ATOM   2020 C  C    A MET   B 2 5   ? 10.74400  -6.42100  -3.25700 0.520 24.50224 ?  629 MET   C C    1 
ATOM   2021 C  C    B MET   B 2 5   ? 10.74600  -6.43100  -3.26300 0.480 24.47231 ?  629 MET   C C    1 
ATOM   2022 O  O    A MET   B 2 5   ? 11.60100  -5.65700  -3.71500 0.520 25.81846 ?  629 MET   C O    1 
ATOM   2023 O  O    B MET   B 2 5   ? 11.61000  -5.68600  -3.73900 0.480 25.57708 ?  629 MET   C O    1 
ATOM   2024 C  CB   A MET   B 2 5   ? 8.32700   -5.72400  -3.26800 0.520 22.46026 ?  629 MET   C CB   1 
ATOM   2025 C  CB   B MET   B 2 5   ? 8.32500   -5.73800  -3.24800 0.480 22.48159 ?  629 MET   C CB   1 
ATOM   2026 C  CG   A MET   B 2 5   ? 7.09100   -5.54100  -4.13800 0.520 25.17606 ?  629 MET   C CG   1 
ATOM   2027 C  CG   B MET   B 2 5   ? 7.03000   -5.68300  -4.04700 0.480 24.97691 ?  629 MET   C CG   1 
ATOM   2028 S  SD   A MET   B 2 5   ? 5.75700   -4.66600  -3.30100 0.520 27.87413 ?  629 MET   C SD   1 
ATOM   2029 S  SD   B MET   B 2 5   ? 5.67100   -4.88400  -3.17000 0.480 28.11301 ?  629 MET   C SD   1 
ATOM   2030 C  CE   A MET   B 2 5   ? 5.26200   -5.91000  -2.11700 0.520 23.68066 ?  629 MET   C CE   1 
ATOM   2031 C  CE   B MET   B 2 5   ? 4.26800   -5.71400  -3.90800 0.480 28.02579 ?  629 MET   C CE   1 
ATOM   2032 N  N    . LEU   B 2 6   ? 10.94800  -7.14600  -2.15500 1.000 22.96245 ?  630 LEU   C N    1 
ATOM   2033 C  CA   . LEU   B 2 6   ? 12.25800  -7.17900  -1.51500 1.000 21.99564 ?  630 LEU   C CA   1 
ATOM   2034 C  C    . LEU   B 2 6   ? 13.31400  -7.72000  -2.47300 1.000 25.64975 ?  630 LEU   C C    1 
ATOM   2035 O  O    . LEU   B 2 6   ? 14.40200  -7.14600  -2.60800 1.000 26.52720 ?  630 LEU   C O    1 
ATOM   2036 C  CB   . LEU   B 2 6   ? 12.16800  -8.03900  -0.25200 1.000 23.78647 ?  630 LEU   C CB   1 
ATOM   2037 C  CG   . LEU   B 2 6   ? 13.37600  -8.34900  0.63200  1.000 33.09831 ?  630 LEU   C CG   1 
ATOM   2038 C  CD1  . LEU   B 2 6   ? 14.28400  -7.16300  0.79700  1.000 34.14098 ?  630 LEU   C CD1  1 
ATOM   2039 C  CD2  . LEU   B 2 6   ? 12.89200  -8.85400  1.98400  1.000 29.73428 ?  630 LEU   C CD2  1 
ATOM   2040 N  N    . MET   B 2 7   ? 12.99600  -8.81400  -3.16600 1.000 24.39732 ?  631 MET   C N    1 
ATOM   2041 C  CA   . MET   B 2 7   ? 13.95200  -9.40800  -4.09800 1.000 31.67557 ?  631 MET   C CA   1 
ATOM   2042 C  C    . MET   B 2 7   ? 14.29100  -8.45100  -5.23100 1.000 30.40021 ?  631 MET   C C    1 
ATOM   2043 O  O    . MET   B 2 7   ? 15.45700  -8.32800  -5.61800 1.000 31.48616 ?  631 MET   C O    1 
ATOM   2044 C  CB   . MET   B 2 7   ? 13.40400  -10.72000 -4.65300 1.000 33.60799 ?  631 MET   C CB   1 
ATOM   2045 C  CG   . MET   B 2 7   ? 13.64100  -11.90200 -3.74300 1.000 40.06761 ?  631 MET   C CG   1 
ATOM   2046 S  SD   . MET   B 2 7   ? 15.37600  -12.38400 -3.76000 1.000 45.59516 ?  631 MET   C SD   1 
ATOM   2047 C  CE   . MET   B 2 7   ? 15.57000  -12.85000 -5.47400 1.000 49.42101 ?  631 MET   C CE   1 
ATOM   2048 N  N    . ASN   B 2 8   ? 13.28900  -7.75200  -5.77100 1.000 25.66054 ?  632 ASN   C N    1 
ATOM   2049 C  CA   . ASN   B 2 8   ? 13.56900  -6.81300  -6.85100 1.000 27.05678 ?  632 ASN   C CA   1 
ATOM   2050 C  C    . ASN   B 2 8   ? 14.45800  -5.67100  -6.37800 1.000 29.31205 ?  632 ASN   C C    1 
ATOM   2051 O  O    . ASN   B 2 8   ? 15.31500  -5.19300  -7.13100 1.000 32.00661 ?  632 ASN   C O    1 
ATOM   2052 C  CB   . ASN   B 2 8   ? 12.27100  -6.25700  -7.43200 1.000 29.14325 ?  632 ASN   C CB   1 
ATOM   2053 C  CG   . ASN   B 2 8   ? 12.52300  -5.32300  -8.59900 1.000 38.60173 ?  632 ASN   C CG   1 
ATOM   2054 O  OD1  . ASN   B 2 8   ? 12.79900  -5.76700  -9.71200 1.000 42.09694 ?  632 ASN   C OD1  1 
ATOM   2055 N  ND2  . ASN   B 2 8   ? 12.44700  -4.02200  -8.34600 1.000 40.95679 ?  632 ASN   C ND2  1 
ATOM   2056 N  N    . LEU   B 2 9   ? 14.26900  -5.21000  -5.14000 1.000 23.04755 ?  633 LEU   C N    1 
ATOM   2057 C  CA   . LEU   B 2 9   ? 15.12500  -4.14600  -4.63700 1.000 25.07347 ?  633 LEU   C CA   1 
ATOM   2058 C  C    . LEU   B 2 9   ? 16.53700  -4.64300  -4.35500 1.000 27.06204 ?  633 LEU   C C    1 
ATOM   2059 O  O    . LEU   B 2 9   ? 17.46200  -3.82900  -4.29100 1.000 29.31254 ?  633 LEU   C O    1 
ATOM   2060 C  CB   . LEU   B 2 9   ? 14.51900  -3.52200  -3.37900 1.000 24.66645 ?  633 LEU   C CB   1 
ATOM   2061 C  CG   . LEU   B 2 9   ? 13.24400  -2.70900  -3.63200 1.000 25.02131 ?  633 LEU   C CG   1 
ATOM   2062 C  CD1  . LEU   B 2 9   ? 12.56000  -2.33000  -2.32300 1.000 22.97973 ?  633 LEU   C CD1  1 
ATOM   2063 C  CD2  . LEU   B 2 9   ? 13.57800  -1.47200  -4.44600 1.000 29.32697 ?  633 LEU   C CD2  1 
ATOM   2064 N  N    . LEU   B 2 10  ? 16.71800  -5.95600  -4.20400 1.000 25.20721 ?  634 LEU   C N    1 
ATOM   2065 C  CA   . LEU   B 2 10  ? 18.04400  -6.53500  -4.01400 1.000 28.32021 ?  634 LEU   C CA   1 
ATOM   2066 C  C    . LEU   B 2 10  ? 18.80600  -6.71400  -5.32200 1.000 36.00616 ?  634 LEU   C C    1 
ATOM   2067 O  O    . LEU   B 2 10  ? 20.04200  -6.76600  -5.29800 1.000 36.88883 ?  634 LEU   C O    1 
ATOM   2068 C  CB   . LEU   B 2 10  ? 17.93000  -7.88400  -3.30100 1.000 28.84588 ?  634 LEU   C CB   1 
ATOM   2069 C  CG   . LEU   B 2 10  ? 17.65000  -7.81800  -1.80100 1.000 24.56602 ?  634 LEU   C CG   1 
ATOM   2070 C  CD1  . LEU   B 2 10  ? 17.25000  -9.19200  -1.27300 1.000 27.94346 ?  634 LEU   C CD1  1 
ATOM   2071 C  CD2  . LEU   B 2 10  ? 18.86000  -7.25600  -1.04700 1.000 26.11062 ?  634 LEU   C CD2  1 
ATOM   2072 N  N    . LYS   B 2 11  ? 18.11100  -6.82400  -6.45100 1.000 40.25092 ?  635 LYS   C N    1 
ATOM   2073 C  CA   . LYS   B 2 11  ? 18.77900  -6.96100  -7.74500 1.000 50.22251 ?  635 LYS   C CA   1 
ATOM   2074 C  C    . LYS   B 2 11  ? 19.39400  -5.63600  -8.16700 1.000 51.70795 ?  635 LYS   C C    1 
ATOM   2075 O  O    . LYS   B 2 11  ? 18.70700  -4.61700  -8.22200 1.000 53.96046 ?  635 LYS   C O    1 
ATOM   2076 C  CB   . LYS   B 2 11  ? 17.80600  -7.45000  -8.82200 1.000 53.61110 ?  635 LYS   C CB   1 
ATOM   2077 C  CG   . LYS   B 2 11  ? 16.77200  -8.43700  -8.32800 1.000 56.92030 ?  635 LYS   C CG   1 
ATOM   2078 C  CD   . LYS   B 2 11  ? 17.35700  -9.82700  -8.15500 1.000 60.27424 ?  635 LYS   C CD   1 
ATOM   2079 C  CE   . LYS   B 2 11  ? 16.30400  -10.90100 -8.38000 1.000 62.03464 ?  635 LYS   C CE   1 
ATOM   2080 N  NZ   . LYS   B 2 11  ? 15.43200  -10.59900 -9.54300 1.000 61.57923 ?  635 LYS   C NZ   1 
HETATM 2081 C  C10  . A1L70 C 3 .   ? 9.89400   7.77500   14.57600 1.000 21.54635 ?  501 A1L70 A C10  1 
HETATM 2082 C  C13  . A1L70 C 3 .   ? 7.07400   4.45800   12.87500 1.000 17.49730 ?  501 A1L70 A C13  1 
HETATM 2083 C  C15  . A1L70 C 3 .   ? 8.82200   2.80800   12.74500 1.000 18.73916 ?  501 A1L70 A C15  1 
HETATM 2084 C  C20  . A1L70 C 3 .   ? 2.93000   1.45100   12.15700 1.000 18.65153 ?  501 A1L70 A C20  1 
HETATM 2085 C  C21  . A1L70 C 3 .   ? 2.11400   0.15700   12.07200 1.000 18.52921 ?  501 A1L70 A C21  1 
HETATM 2086 C  C22  . A1L70 C 3 .   ? 4.81100   0.54800   10.74800 1.000 15.19073 ?  501 A1L70 A C22  1 
HETATM 2087 C  C26  . A1L70 C 3 .   ? 15.41900  9.48000   7.68800  1.000 22.36076 ?  501 A1L70 A C26  1 
HETATM 2088 C  C28  . A1L70 C 3 .   ? 14.83300  9.38800   6.27500  1.000 26.59013 ?  501 A1L70 A C28  1 
HETATM 2089 C  C01  . A1L70 C 3 .   ? 12.63100  8.94700   10.89900 1.000 19.06161 ?  501 A1L70 A C01  1 
HETATM 2090 C  C02  . A1L70 C 3 .   ? 12.70300  8.19200   9.73900  1.000 19.49967 ?  501 A1L70 A C02  1 
HETATM 2091 C  C03  . A1L70 C 3 .   ? 12.16000  6.91300   9.71100  1.000 18.37463 ?  501 A1L70 A C03  1 
HETATM 2092 C  C04  . A1L70 C 3 .   ? 11.54600  6.36900   10.82600 1.000 17.08784 ?  501 A1L70 A C04  1 
HETATM 2093 C  C05  . A1L70 C 3 .   ? 11.46800  7.13300   11.98400 1.000 18.73959 ?  501 A1L70 A C05  1 
HETATM 2094 C  C06  . A1L70 C 3 .   ? 12.00800  8.41300   12.02100 1.000 16.29097 ?  501 A1L70 A C06  1 
HETATM 2095 C  C09  . A1L70 C 3 .   ? 9.36800   5.09900   13.17900 1.000 20.17783 ?  501 A1L70 A C09  1 
HETATM 2096 C  C11  . A1L70 C 3 .   ? 12.08300  5.60700   14.51400 1.000 19.45191 ?  501 A1L70 A C11  1 
HETATM 2097 C  C12  . A1L70 C 3 .   ? 8.02200   5.44400   13.12300 1.000 20.60867 ?  501 A1L70 A C12  1 
HETATM 2098 C  C14  . A1L70 C 3 .   ? 7.47600   3.14200   12.68500 1.000 17.35036 ?  501 A1L70 A C14  1 
HETATM 2099 C  C16  . A1L70 C 3 .   ? 9.76600   3.78800   12.99600 1.000 18.34873 ?  501 A1L70 A C16  1 
HETATM 2100 C  C18  . A1L70 C 3 .   ? 5.20600   2.42800   12.41800 1.000 14.59027 ?  501 A1L70 A C18  1 
HETATM 2101 C  C19  . A1L70 C 3 .   ? 4.43200   1.14500   12.10600 1.000 16.50130 ?  501 A1L70 A C19  1 
HETATM 2102 C  C23  . A1L70 C 3 .   ? 4.36900   1.42300   9.57400  1.000 16.81454 ?  501 A1L70 A C23  1 
HETATM 2103 C  C25  . A1L70 C 3 .   ? 14.33300  9.63500   8.76400  1.000 22.86440 ?  501 A1L70 A C25  1 
HETATM 2104 C  C29  . A1L70 C 3 .   ? 15.80600  10.05500  5.29400  1.000 27.45576 ?  501 A1L70 A C29  1 
HETATM 2105 C  C30  . A1L70 C 3 .   ? 16.28000  9.10400   4.18600  1.000 23.99394 ?  501 A1L70 A C30  1 
HETATM 2106 O  O07  . A1L70 C 3 .   ? 13.31900  8.68500   8.58000  1.000 21.55743 ?  501 A1L70 A O07  1 
HETATM 2107 O  O17  . A1L70 C 3 .   ? 6.56900   2.10400   12.42800 1.000 18.16904 ?  501 A1L70 A O17  1 
HETATM 2108 O  O24  . A1L70 C 3 .   ? 4.77100   0.20500   13.09100 1.000 14.38976 ?  501 A1L70 A O24  1 
HETATM 2109 O  O27  . A1L70 C 3 .   ? 16.14300  8.31700   7.94000  1.000 25.25644 ?  501 A1L70 A O27  1 
HETATM 2110 O  O31  . A1L70 C 3 .   ? 16.60800  9.56100   3.05600  1.000 20.42238 ?  501 A1L70 A O31  1 
HETATM 2111 O  O32  . A1L70 C 3 .   ? 16.35300  7.86500   4.38200  1.000 27.13031 -1 501 A1L70 A O32  1 
HETATM 2112 SI SI08 . A1L70 C 3 .   ? 10.68300  6.40700   13.53300 1.000 18.74396 ?  501 A1L70 A SI08 1 
HETATM 2113 O  O    . HOH   D 4 .   ? 24.08700  -12.73700 -5.35800 1.000 20.06412 ?  601 HOH   A O    1 
HETATM 2114 O  O    . HOH   D 4 .   ? 41.58300  5.41600   4.07100  1.000 34.72663 ?  602 HOH   A O    1 
HETATM 2115 O  O    . HOH   D 4 .   ? 18.712    -24.741   4.329    1.000 57.50965 ?  603 HOH   A O    1 
HETATM 2116 O  O    . HOH   D 4 .   ? 17.52600  10.09300  10.09200 1.000 46.94788 ?  604 HOH   A O    1 
HETATM 2117 O  O    . HOH   D 4 .   ? 42.10000  6.31800   18.96700 1.000 59.03566 ?  605 HOH   A O    1 
HETATM 2118 O  O    . HOH   D 4 .   ? 0.69900   14.50100  16.66000 1.000 52.48678 ?  606 HOH   A O    1 
HETATM 2119 O  O    A HOH   D 4 .   ? 13.24300  -2.31500  24.86900 0.620 26.95643 ?  607 HOH   A O    1 
HETATM 2120 O  O    B HOH   D 4 .   ? 11.72100  -2.25800  24.38900 0.380 27.59008 ?  607 HOH   A O    1 
HETATM 2121 O  O    . HOH   D 4 .   ? 41.42200  -7.28300  0.37800  1.000 43.67355 ?  608 HOH   A O    1 
HETATM 2122 O  O    . HOH   D 4 .   ? 39.11600  -10.17800 5.31100  1.000 41.11094 ?  609 HOH   A O    1 
HETATM 2123 O  O    . HOH   D 4 .   ? 7.63500   -9.67100  19.30600 1.000 46.91754 ?  610 HOH   A O    1 
HETATM 2124 O  O    . HOH   D 4 .   ? 30.83900  -6.35100  16.32200 1.000 39.76563 ?  611 HOH   A O    1 
HETATM 2125 O  O    . HOH   D 4 .   ? 7.01100   -11.53800 7.80500  1.000 56.62307 ?  612 HOH   A O    1 
HETATM 2126 O  O    . HOH   D 4 .   ? 15.25300  -19.71200 6.58800  1.000 41.00081 ?  613 HOH   A O    1 
HETATM 2127 O  O    . HOH   D 4 .   ? 17.54000  16.94000  11.00900 1.000 52.31329 ?  614 HOH   A O    1 
HETATM 2128 O  O    . HOH   D 4 .   ? 38.08100  7.79000   7.56800  1.000 39.38084 ?  615 HOH   A O    1 
HETATM 2129 O  O    . HOH   D 4 .   ? 19.88500  -9.19100  10.28900 1.000 27.36411 ?  616 HOH   A O    1 
HETATM 2130 O  O    . HOH   D 4 .   ? 4.62900   -9.25100  -1.77700 1.000 31.50746 ?  617 HOH   A O    1 
HETATM 2131 O  O    A HOH   D 4 .   ? 12.52600  21.51900  11.15500 0.560 35.13949 ?  618 HOH   A O    1 
HETATM 2132 O  O    B HOH   D 4 .   ? 11.71100  22.31600  11.95200 0.440 36.45409 ?  618 HOH   A O    1 
HETATM 2133 O  O    . HOH   D 4 .   ? 30.83300  -9.26600  -3.31600 1.000 34.96722 ?  619 HOH   A O    1 
HETATM 2134 O  O    . HOH   D 4 .   ? 26.98700  -6.82300  -1.29400 1.000 18.62534 ?  620 HOH   A O    1 
HETATM 2135 O  O    . HOH   D 4 .   ? 11.07700  17.88800  2.79000  1.000 46.87670 ?  621 HOH   A O    1 
HETATM 2136 O  O    . HOH   D 4 .   ? 21.22700  -18.31700 13.19000 1.000 44.65095 ?  622 HOH   A O    1 
HETATM 2137 O  O    . HOH   D 4 .   ? 7.33200   1.60100   -0.67000 1.000 21.62767 ?  623 HOH   A O    1 
HETATM 2138 O  O    . HOH   D 4 .   ? 0.74000   18.52000  10.58100 1.000 44.45775 ?  624 HOH   A O    1 
HETATM 2139 O  O    . HOH   D 4 .   ? 19.44000  15.78700  9.09800  1.000 40.59539 ?  625 HOH   A O    1 
HETATM 2140 O  O    . HOH   D 4 .   ? 8.84400   17.01600  21.68900 1.000 39.30900 ?  626 HOH   A O    1 
HETATM 2141 O  O    . HOH   D 4 .   ? 24.70000  -23.87300 5.90400  1.000 51.15204 ?  627 HOH   A O    1 
HETATM 2142 O  O    . HOH   D 4 .   ? 20.86100  -5.66000  16.65700 1.000 23.39923 ?  628 HOH   A O    1 
HETATM 2143 O  O    . HOH   D 4 .   ? 16.60100  0.92300   -2.53300 1.000 31.82654 ?  629 HOH   A O    1 
HETATM 2144 O  O    A HOH   D 4 .   ? 27.73700  3.08600   -5.39800 0.530 71.41403 ?  630 HOH   A O    1 
HETATM 2145 O  O    B HOH   D 4 .   ? 28.93800  2.73100   -6.07900 0.470 72.29459 ?  630 HOH   A O    1 
HETATM 2146 O  O    . HOH   D 4 .   ? 1.10000   -8.72400  19.39900 1.000 36.10445 ?  631 HOH   A O    1 
HETATM 2147 O  O    . HOH   D 4 .   ? 3.02600   16.45400  3.04500  1.000 30.76096 ?  632 HOH   A O    1 
HETATM 2148 O  O    . HOH   D 4 .   ? 48.04900  -0.21800  -2.73600 1.000 54.12142 ?  633 HOH   A O    1 
HETATM 2149 O  O    . HOH   D 4 .   ? 30.64000  9.79600   0.02100  1.000 32.28248 ?  634 HOH   A O    1 
HETATM 2150 O  O    . HOH   D 4 .   ? 29.62000  -2.96900  -2.48100 1.000 23.21660 ?  635 HOH   A O    1 
HETATM 2151 O  O    . HOH   D 4 .   ? 8.96100   13.89700  21.58400 1.000 28.65550 ?  636 HOH   A O    1 
HETATM 2152 O  O    A HOH   D 4 .   ? 4.79400   17.04100  15.56400 0.490 29.26472 ?  637 HOH   A O    1 
HETATM 2153 O  O    B HOH   D 4 .   ? 3.43400   16.52700  17.04000 0.510 30.23128 ?  637 HOH   A O    1 
HETATM 2154 O  O    . HOH   D 4 .   ? -1.74300  9.37400   21.61400 1.000 40.08299 ?  638 HOH   A O    1 
HETATM 2155 O  O    . HOH   D 4 .   ? -5.32900  -6.52000  17.13400 1.000 43.70682 ?  639 HOH   A O    1 
HETATM 2156 O  O    . HOH   D 4 .   ? 3.13200   -4.31000  24.03600 1.000 39.93047 ?  640 HOH   A O    1 
HETATM 2157 O  O    . HOH   D 4 .   ? 28.74900  -4.43100  25.50000 1.000 33.80074 ?  641 HOH   A O    1 
HETATM 2158 O  O    . HOH   D 4 .   ? 21.20300  7.51000   -4.69200 1.000 39.78965 ?  642 HOH   A O    1 
HETATM 2159 O  O    . HOH   D 4 .   ? 13.98600  -11.24600 14.04300 1.000 54.35272 ?  643 HOH   A O    1 
HETATM 2160 O  O    . HOH   D 4 .   ? 32.55200  -9.08700  3.39700  1.000 25.61291 ?  644 HOH   A O    1 
HETATM 2161 O  O    . HOH   D 4 .   ? 31.31100  7.79700   -3.65500 1.000 29.33028 ?  645 HOH   A O    1 
HETATM 2162 O  O    . HOH   D 4 .   ? 30.05500  -11.46900 -6.32000 1.000 40.31407 ?  646 HOH   A O    1 
HETATM 2163 O  O    . HOH   D 4 .   ? 1.49400   4.60900   0.04500  1.000 19.93260 ?  647 HOH   A O    1 
HETATM 2164 O  O    . HOH   D 4 .   ? 32.11600  8.63300   22.04800 1.000 43.88549 ?  648 HOH   A O    1 
HETATM 2165 O  O    . HOH   D 4 .   ? -3.23000  11.63500  5.68600  1.000 27.43579 ?  649 HOH   A O    1 
HETATM 2166 O  O    . HOH   D 4 .   ? 35.54200  12.17300  17.76300 1.000 40.41276 ?  650 HOH   A O    1 
HETATM 2167 O  O    . HOH   D 4 .   ? 23.70200  -17.72300 2.42100  1.000 20.73077 ?  651 HOH   A O    1 
HETATM 2168 O  O    . HOH   D 4 .   ? -2.68700  1.42800   19.79500 1.000 44.16085 ?  652 HOH   A O    1 
HETATM 2169 O  O    . HOH   D 4 .   ? 8.59200   -6.85600  23.84000 1.000 36.41310 ?  653 HOH   A O    1 
HETATM 2170 O  O    . HOH   D 4 .   ? 25.41900  1.13900   24.87700 1.000 37.69871 ?  654 HOH   A O    1 
HETATM 2171 O  O    . HOH   D 4 .   ? 17.56000  -18.50300 4.51800  1.000 33.72334 ?  655 HOH   A O    1 
HETATM 2172 O  O    . HOH   D 4 .   ? 33.41600  6.40900   -0.25600 1.000 27.81242 ?  656 HOH   A O    1 
HETATM 2173 O  O    . HOH   D 4 .   ? -2.85900  17.13800  6.87200  1.000 46.72045 ?  657 HOH   A O    1 
HETATM 2174 O  O    . HOH   D 4 .   ? -5.29800  -0.39800  1.01400  1.000 17.62408 ?  658 HOH   A O    1 
HETATM 2175 O  O    . HOH   D 4 .   ? 19.78100  17.57800  7.16400  1.000 38.74482 ?  659 HOH   A O    1 
HETATM 2176 O  O    . HOH   D 4 .   ? 12.31100  -5.56700  10.52600 1.000 21.52103 ?  660 HOH   A O    1 
HETATM 2177 O  O    . HOH   D 4 .   ? 14.88500  5.89400   7.76900  1.000 16.72960 ?  661 HOH   A O    1 
HETATM 2178 O  O    . HOH   D 4 .   ? 44.409    3.614     1.586    1.000 24.89876 ?  662 HOH   A O    1 
HETATM 2179 O  O    . HOH   D 4 .   ? -4.72000  10.27000  8.48100  1.000 31.89797 ?  663 HOH   A O    1 
HETATM 2180 O  O    . HOH   D 4 .   ? 25.66200  7.01100   25.36500 1.000 41.91347 ?  664 HOH   A O    1 
HETATM 2181 O  O    . HOH   D 4 .   ? 32.77000  6.47300   24.22200 1.000 45.30364 ?  665 HOH   A O    1 
HETATM 2182 O  O    . HOH   D 4 .   ? -1.23200  2.01400   0.68800  1.000 30.78761 ?  666 HOH   A O    1 
HETATM 2183 O  O    . HOH   D 4 .   ? 31.28400  -10.13600 14.30100 1.000 26.84401 ?  667 HOH   A O    1 
HETATM 2184 O  O    . HOH   D 4 .   ? 1.52100   14.86500  0.77400  1.000 43.33109 ?  668 HOH   A O    1 
HETATM 2185 O  O    . HOH   D 4 .   ? 1.56800   -1.79900  24.35700 1.000 40.68159 ?  669 HOH   A O    1 
HETATM 2186 O  O    . HOH   D 4 .   ? 21.52700  7.68600   9.24100  1.000 18.21189 ?  670 HOH   A O    1 
HETATM 2187 O  O    . HOH   D 4 .   ? 16.31000  1.60700   24.95400 1.000 33.76096 ?  671 HOH   A O    1 
HETATM 2188 O  O    . HOH   D 4 .   ? 22.87900  -10.84800 19.58000 1.000 41.37508 ?  672 HOH   A O    1 
HETATM 2189 O  O    . HOH   D 4 .   ? -5.17700  5.85800   10.00000 1.000 25.01623 ?  673 HOH   A O    1 
HETATM 2190 O  O    . HOH   D 4 .   ? 15.02700  11.78000  2.68800  1.000 54.99689 ?  674 HOH   A O    1 
HETATM 2191 O  O    . HOH   D 4 .   ? -0.94200  10.64500  8.24200  1.000 20.57198 ?  675 HOH   A O    1 
HETATM 2192 O  O    . HOH   D 4 .   ? 5.56600   -5.75800  26.13400 1.000 55.08884 ?  676 HOH   A O    1 
HETATM 2193 O  O    . HOH   D 4 .   ? 22.51900  -14.13900 -4.10300 1.000 41.00456 ?  677 HOH   A O    1 
HETATM 2194 O  O    . HOH   D 4 .   ? 6.97600   18.01700  20.55700 1.000 44.13402 ?  678 HOH   A O    1 
HETATM 2195 O  O    . HOH   D 4 .   ? 35.85600  -13.00900 8.32200  1.000 22.05820 ?  679 HOH   A O    1 
HETATM 2196 O  O    . HOH   D 4 .   ? 5.06600   19.17200  13.87000 1.000 40.16203 ?  680 HOH   A O    1 
HETATM 2197 O  O    . HOH   D 4 .   ? 31.77600  11.73300  11.05200 1.000 31.03362 ?  681 HOH   A O    1 
HETATM 2198 O  O    . HOH   D 4 .   ? 21.60800  4.25800   4.62800  1.000 16.54732 ?  682 HOH   A O    1 
HETATM 2199 O  O    . HOH   D 4 .   ? 2.61300   -7.07400  0.24400  1.000 29.69792 ?  683 HOH   A O    1 
HETATM 2200 O  O    . HOH   D 4 .   ? -6.07400  -0.55600  16.19200 1.000 39.11200 ?  684 HOH   A O    1 
HETATM 2201 O  O    . HOH   D 4 .   ? 17.30300  -16.19000 -6.12600 1.000 36.97778 ?  685 HOH   A O    1 
HETATM 2202 O  O    . HOH   D 4 .   ? 29.10600  1.42100   -2.00700 1.000 19.81930 ?  686 HOH   A O    1 
HETATM 2203 O  O    . HOH   D 4 .   ? 23.79600  11.15300  2.86600  1.000 22.49503 ?  687 HOH   A O    1 
HETATM 2204 O  O    . HOH   D 4 .   ? -1.17700  4.84400   21.02700 1.000 38.31726 ?  688 HOH   A O    1 
HETATM 2205 O  O    . HOH   D 4 .   ? 28.02000  12.18500  15.82100 1.000 32.64608 ?  689 HOH   A O    1 
HETATM 2206 O  O    . HOH   D 4 .   ? 14.01100  12.42500  0.59200  1.000 24.83548 ?  690 HOH   A O    1 
HETATM 2207 O  O    . HOH   D 4 .   ? 6.23800   22.45000  7.78700  1.000 42.27778 ?  691 HOH   A O    1 
HETATM 2208 O  O    . HOH   D 4 .   ? 28.98900  -11.13400 -8.63200 1.000 45.39937 ?  692 HOH   A O    1 
HETATM 2209 O  O    . HOH   D 4 .   ? 29.26600  13.12100  5.32400  1.000 50.73272 ?  693 HOH   A O    1 
HETATM 2210 O  O    . HOH   D 4 .   ? 32.47200  -17.96300 10.10400 1.000 32.06790 ?  694 HOH   A O    1 
HETATM 2211 O  O    . HOH   D 4 .   ? 3.77700   9.48200   -4.01100 1.000 20.10605 ?  695 HOH   A O    1 
HETATM 2212 O  O    . HOH   D 4 .   ? 3.78300   13.97900  3.15900  1.000 19.66605 ?  696 HOH   A O    1 
HETATM 2213 O  O    . HOH   D 4 .   ? 8.82500   -5.28800  13.30400 1.000 32.24489 ?  697 HOH   A O    1 
HETATM 2214 O  O    . HOH   D 4 .   ? 13.86600  -12.99600 9.31000  1.000 50.58049 ?  698 HOH   A O    1 
HETATM 2215 O  O    . HOH   D 4 .   ? 11.28100  -6.34400  24.02300 1.000 32.87230 ?  699 HOH   A O    1 
HETATM 2216 O  O    . HOH   D 4 .   ? 35.712    9.817     5.853    1.000 41.83563 ?  700 HOH   A O    1 
HETATM 2217 O  O    . HOH   D 4 .   ? 19.35800  -19.96800 2.41000  1.000 51.67378 ?  701 HOH   A O    1 
HETATM 2218 O  O    . HOH   D 4 .   ? 34.00700  -16.14100 11.00300 1.000 54.13384 ?  702 HOH   A O    1 
HETATM 2219 O  O    . HOH   D 4 .   ? -3.11000  5.91000   19.41700 1.000 40.71332 ?  703 HOH   A O    1 
HETATM 2220 O  O    . HOH   D 4 .   ? 14.74900  -16.44400 -2.64000 1.000 39.74951 ?  704 HOH   A O    1 
HETATM 2221 O  O    . HOH   D 4 .   ? 9.95700   -8.76600  9.73800  1.000 41.25921 ?  705 HOH   A O    1 
HETATM 2222 O  O    . HOH   D 4 .   ? 22.91600  -7.53100  15.98700 1.000 29.96767 ?  706 HOH   A O    1 
HETATM 2223 O  O    . HOH   D 4 .   ? 16.08000  20.98800  17.55900 1.000 53.84071 ?  707 HOH   A O    1 
HETATM 2224 O  O    . HOH   D 4 .   ? -2.50200  18.20900  10.53600 1.000 48.96187 ?  708 HOH   A O    1 
HETATM 2225 O  O    . HOH   D 4 .   ? 23.57700  11.72500  14.95100 1.000 32.88471 ?  709 HOH   A O    1 
HETATM 2226 O  O    . HOH   D 4 .   ? 25.98000  9.09500   17.53400 1.000 24.26903 ?  710 HOH   A O    1 
HETATM 2227 O  O    . HOH   D 4 .   ? -7.57400  7.35100   13.62000 1.000 43.65767 ?  711 HOH   A O    1 
HETATM 2228 O  O    . HOH   D 4 .   ? -7.511    -10.483   11.288   1.000 49.53702 ?  712 HOH   A O    1 
HETATM 2229 O  O    A HOH   D 4 .   ? 12.99100  -16.38400 1.38900  0.570 27.13473 ?  713 HOH   A O    1 
HETATM 2230 O  O    B HOH   D 4 .   ? 13.82100  -16.34300 3.06900  0.430 24.65927 ?  713 HOH   A O    1 
HETATM 2231 O  O    . HOH   D 4 .   ? 25.19900  -4.82400  -5.00000 1.000 46.16656 ?  714 HOH   A O    1 
HETATM 2232 O  O    . HOH   D 4 .   ? 18.67400  8.70000   -0.87700 1.000 34.47139 ?  715 HOH   A O    1 
HETATM 2233 O  O    . HOH   D 4 .   ? -8.53900  0.67200   13.62600 1.000 39.49914 ?  716 HOH   A O    1 
HETATM 2234 O  O    . HOH   D 4 .   ? 29.91100  -7.20300  -2.07000 1.000 27.88727 ?  717 HOH   A O    1 
HETATM 2235 O  O    . HOH   D 4 .   ? 42.33300  5.75800   21.35700 1.000 47.64435 ?  718 HOH   A O    1 
HETATM 2236 O  O    . HOH   D 4 .   ? 17.790    22.759    23.663   1.000 38.73193 ?  719 HOH   A O    1 
HETATM 2237 O  O    . HOH   D 4 .   ? 43.73000  -6.25300  16.12800 1.000 41.39998 ?  720 HOH   A O    1 
HETATM 2238 O  O    . HOH   D 4 .   ? 25.07400  -24.41000 2.55200  1.000 40.54775 ?  721 HOH   A O    1 
HETATM 2239 O  O    . HOH   D 4 .   ? 42.51000  -6.59500  6.78200  1.000 34.05414 ?  722 HOH   A O    1 
HETATM 2240 O  O    . HOH   D 4 .   ? 14.30400  2.04100   -3.84800 1.000 29.37078 ?  723 HOH   A O    1 
HETATM 2241 O  O    . HOH   D 4 .   ? 20.59800  2.38000   6.28900  1.000 18.11066 ?  724 HOH   A O    1 
HETATM 2242 O  O    . HOH   D 4 .   ? 25.64800  13.85400  18.61800 1.000 42.69956 ?  725 HOH   A O    1 
HETATM 2243 O  O    A HOH   D 4 .   ? 6.71200   5.72100   0.60600  0.730 19.16274 ?  726 HOH   A O    1 
HETATM 2244 O  O    B HOH   D 4 .   ? 5.00200   4.75900   0.01000  0.270 18.74752 ?  726 HOH   A O    1 
HETATM 2245 O  O    . HOH   D 4 .   ? 1.54800   -8.97300  10.62400 1.000 43.06896 ?  727 HOH   A O    1 
HETATM 2246 O  O    A HOH   D 4 .   ? 24.59600  11.73500  5.40200  0.580 25.20465 ?  728 HOH   A O    1 
HETATM 2247 O  O    B HOH   D 4 .   ? 25.42900  11.20400  7.00000  0.420 25.31016 ?  728 HOH   A O    1 
HETATM 2248 O  O    A HOH   D 4 .   ? 21.01200  10.44100  -1.08100 0.710 29.89936 ?  729 HOH   A O    1 
HETATM 2249 O  O    B HOH   D 4 .   ? 20.17400  11.57500  -2.52000 0.290 31.01085 ?  729 HOH   A O    1 
HETATM 2250 O  O    . HOH   D 4 .   ? 0.97700   4.68400   25.64000 1.000 26.50053 ?  730 HOH   A O    1 
HETATM 2251 O  O    . HOH   D 4 .   ? 9.01800   24.34300  9.05200  1.000 44.23516 ?  731 HOH   A O    1 
HETATM 2252 O  O    . HOH   D 4 .   ? 41.803    13.939    21.257   1.000 48.36358 ?  732 HOH   A O    1 
HETATM 2253 O  O    . HOH   D 4 .   ? 37.91600  -12.40800 12.95200 1.000 52.39951 ?  733 HOH   A O    1 
HETATM 2254 O  O    . HOH   D 4 .   ? 19.06900  2.22600   24.97800 1.000 36.47646 ?  734 HOH   A O    1 
HETATM 2255 O  O    . HOH   D 4 .   ? 20.84400  16.68500  19.17200 1.000 34.20299 ?  735 HOH   A O    1 
HETATM 2256 O  O    . HOH   D 4 .   ? -4.53500  6.33200   3.40300  1.000 28.48556 ?  736 HOH   A O    1 
HETATM 2257 O  O    A HOH   D 4 .   ? 27.27000  9.65300   12.92700 0.640 28.26394 ?  737 HOH   A O    1 
HETATM 2258 O  O    B HOH   D 4 .   ? 26.62300  10.51500  11.96900 0.360 30.00753 ?  737 HOH   A O    1 
HETATM 2259 O  O    . HOH   D 4 .   ? 11.52000  18.86900  4.95000  1.000 36.59227 ?  738 HOH   A O    1 
HETATM 2260 O  O    . HOH   D 4 .   ? 47.10700  -2.80500  8.98200  1.000 52.94289 ?  739 HOH   A O    1 
HETATM 2261 O  O    . HOH   D 4 .   ? -6.86200  12.28800  17.27700 1.000 50.28222 ?  740 HOH   A O    1 
HETATM 2262 O  O    . HOH   D 4 .   ? 38.60600  9.28500   10.13700 1.000 51.69440 ?  741 HOH   A O    1 
HETATM 2263 O  O    . HOH   D 4 .   ? 17.49300  17.50800  -2.84300 1.000 26.83383 ?  742 HOH   A O    1 
HETATM 2264 O  O    A HOH   D 4 .   ? 45.68800  -2.22800  14.83600 0.700 39.83742 ?  743 HOH   A O    1 
HETATM 2265 O  O    B HOH   D 4 .   ? 45.60600  -4.62900  14.94700 0.300 26.97744 ?  743 HOH   A O    1 
HETATM 2266 O  O    . HOH   D 4 .   ? 25.33500  -16.07900 -4.18500 1.000 28.06784 ?  744 HOH   A O    1 
HETATM 2267 O  O    . HOH   D 4 .   ? 18.63200  -7.99500  23.70500 1.000 45.83612 ?  745 HOH   A O    1 
HETATM 2268 O  O    A HOH   D 4 .   ? 25.20900  -10.69000 15.94400 0.630 26.07580 ?  746 HOH   A O    1 
HETATM 2269 O  O    B HOH   D 4 .   ? 25.16000  -8.55600  16.93500 0.370 26.74739 ?  746 HOH   A O    1 
HETATM 2270 O  O    . HOH   D 4 .   ? 46.97900  -3.25600  3.79300  1.000 38.49414 ?  747 HOH   A O    1 
HETATM 2271 O  O    . HOH   D 4 .   ? 17.53300  -2.58800  26.06600 1.000 48.33603 ?  748 HOH   A O    1 
HETATM 2272 O  O    . HOH   D 4 .   ? 22.04000  0.53500   -3.76000 1.000 48.20817 ?  749 HOH   A O    1 
HETATM 2273 O  O    . HOH   D 4 .   ? 47.334    2.062     5.201    1.000 64.01472 ?  750 HOH   A O    1 
HETATM 2274 O  O    . HOH   D 4 .   ? 20.60000  19.57500  17.69200 1.000 46.14175 ?  751 HOH   A O    1 
HETATM 2275 O  O    . HOH   D 4 .   ? 24.06300  -14.53100 19.82700 1.000 43.79985 ?  752 HOH   A O    1 
HETATM 2276 O  O    . HOH   D 4 .   ? 18.17600  17.05100  13.82500 1.000 42.78068 ?  753 HOH   A O    1 
HETATM 2277 O  O    . HOH   D 4 .   ? 7.38300   -7.26100  12.49600 1.000 35.57295 ?  754 HOH   A O    1 
HETATM 2278 O  O    . HOH   D 4 .   ? 24.75800  -7.32500  21.22900 1.000 36.40483 ?  755 HOH   A O    1 
HETATM 2279 O  O    . HOH   D 4 .   ? 22.26400  14.97900  8.53900  1.000 41.17366 ?  756 HOH   A O    1 
HETATM 2280 O  O    . HOH   D 4 .   ? 38.59500  -6.74400  8.76500  1.000 34.39731 ?  757 HOH   A O    1 
HETATM 2281 O  O    . HOH   D 4 .   ? 24.87700  7.78200   15.12200 1.000 30.15580 ?  758 HOH   A O    1 
HETATM 2282 O  O    . HOH   D 4 .   ? 11.00500  -9.67400  16.46300 1.000 48.73281 ?  759 HOH   A O    1 
HETATM 2283 O  O    . HOH   D 4 .   ? 26.59900  -22.30800 8.37900  1.000 36.36303 ?  760 HOH   A O    1 
HETATM 2284 O  O    . HOH   D 4 .   ? -3.80800  8.49000   20.56300 1.000 50.32853 ?  761 HOH   A O    1 
HETATM 2285 O  O    . HOH   D 4 .   ? 7.80600   -10.96600 10.03900 1.000 58.80704 ?  762 HOH   A O    1 
HETATM 2286 O  O    . HOH   D 4 .   ? 35.78500  -14.85000 10.25800 1.000 43.54702 ?  763 HOH   A O    1 
HETATM 2287 O  O    . HOH   D 4 .   ? 44.228    -6.946    3.631    1.000 47.34412 ?  764 HOH   A O    1 
HETATM 2288 O  O    . HOH   D 4 .   ? -6.68000  3.08700   10.61600 1.000 35.80838 ?  765 HOH   A O    1 
HETATM 2289 O  O    . HOH   D 4 .   ? 16.40800  -10.96300 15.75600 1.000 41.28854 ?  766 HOH   A O    1 
HETATM 2290 O  O    . HOH   D 4 .   ? 38.99100  -8.88600  9.32200  1.000 39.92494 ?  767 HOH   A O    1 
HETATM 2291 O  O    . HOH   D 4 .   ? 15.505    -20.341   -2.846   1.000 54.30589 ?  768 HOH   A O    1 
HETATM 2292 O  O    . HOH   D 4 .   ? 38.582    4.793     4.692    1.000 33.48182 ?  769 HOH   A O    1 
HETATM 2293 O  O    . HOH   D 4 .   ? 1.80400   1.91000   26.92500 1.000 68.40112 ?  770 HOH   A O    1 
HETATM 2294 O  O    . HOH   D 4 .   ? -1.40900  -11.79100 9.86600  1.000 66.00688 ?  771 HOH   A O    1 
HETATM 2295 O  O    . HOH   D 4 .   ? 8.56800   5.55100   -1.15300 1.000 38.24611 ?  772 HOH   A O    1 
HETATM 2296 O  O    . HOH   D 4 .   ? -5.293    3.255     2.003    1.000 40.91850 ?  773 HOH   A O    1 
HETATM 2297 O  O    . HOH   D 4 .   ? -1.80900  14.95300  17.10900 1.000 44.63792 ?  774 HOH   A O    1 
HETATM 2298 O  O    A HOH   D 4 .   ? -0.26100  -1.46900  19.71200 0.500 29.08641 ?  775 HOH   A O    1 
HETATM 2299 O  O    B HOH   D 4 .   ? 0.02800   -2.03800  21.66800 0.500 28.10555 ?  775 HOH   A O    1 
HETATM 2300 O  O    . HOH   D 4 .   ? 30.57900  0.04800   28.66700 1.000 59.49647 ?  776 HOH   A O    1 
HETATM 2301 O  O    . HOH   D 4 .   ? 27.407    8.677     -3.472   1.000 54.71624 ?  777 HOH   A O    1 
HETATM 2302 O  O    . HOH   D 4 .   ? 16.08500  -1.00000  24.46500 1.000 40.88382 ?  778 HOH   A O    1 
HETATM 2303 O  O    . HOH   D 4 .   ? 10.96800  -3.96600  25.84600 1.000 48.92048 ?  779 HOH   A O    1 
HETATM 2304 O  O    . HOH   D 4 .   ? 15.19700  -18.09300 -4.47200 1.000 53.57671 ?  780 HOH   A O    1 
HETATM 2305 O  O    . HOH   D 4 .   ? 16.280    20.957    26.111   1.000 38.80393 ?  781 HOH   A O    1 
HETATM 2306 O  O    A HOH   D 4 .   ? 35.74100  -5.28400  0.54100  0.600 29.88819 ?  782 HOH   A O    1 
HETATM 2307 O  O    B HOH   D 4 .   ? 37.71400  -4.94000  1.16000  0.400 25.85256 ?  782 HOH   A O    1 
HETATM 2308 O  O    . HOH   D 4 .   ? 8.38000   18.37600  18.22400 1.000 49.18496 ?  783 HOH   A O    1 
HETATM 2309 O  O    . HOH   D 4 .   ? 2.40000   -9.38900  1.92700  1.000 40.79929 ?  784 HOH   A O    1 
HETATM 2310 O  O    . HOH   D 4 .   ? 33.35400  -10.51500 1.26200  1.000 56.23179 ?  785 HOH   A O    1 
HETATM 2311 O  O    . HOH   D 4 .   ? 26.17300  4.22000   25.95800 1.000 47.71392 ?  786 HOH   A O    1 
HETATM 2312 O  O    . HOH   D 4 .   ? 25.61600  11.71600  16.81000 1.000 28.74889 ?  787 HOH   A O    1 
HETATM 2313 O  O    . HOH   D 4 .   ? 27.72800  -4.21200  -4.66300 1.000 47.50714 ?  788 HOH   A O    1 
HETATM 2314 O  O    A HOH   D 4 .   ? -4.86200  -10.14000 9.21200  0.580 33.31115 ?  789 HOH   A O    1 
HETATM 2315 O  O    B HOH   D 4 .   ? -3.07100  -10.95100 8.60900  0.420 29.35051 ?  789 HOH   A O    1 
HETATM 2316 O  O    . HOH   D 4 .   ? 28.36000  4.62400   -6.82700 1.000 75.63168 ?  790 HOH   A O    1 
HETATM 2317 O  O    . HOH   D 4 .   ? 0.92300   -4.86600  21.58600 1.000 45.31266 ?  791 HOH   A O    1 
HETATM 2318 O  O    . HOH   D 4 .   ? 22.81200  -8.35200  20.11100 1.000 43.71990 ?  792 HOH   A O    1 
HETATM 2319 O  O    . HOH   D 4 .   ? 0.81600   -0.54100  26.76900 1.000 47.24650 ?  793 HOH   A O    1 
HETATM 2320 O  O    . HOH   D 4 .   ? 33.19400  -12.38900 4.07000  1.000 40.74278 ?  794 HOH   A O    1 
HETATM 2321 O  O    . HOH   D 4 .   ? -0.71900  20.17900  12.76200 1.000 66.45750 ?  795 HOH   A O    1 
HETATM 2322 O  O    . HOH   D 4 .   ? 4.41600   16.41800  -5.00400 1.000 38.37105 ?  796 HOH   A O    1 
HETATM 2323 O  O    . HOH   D 4 .   ? 25.339    14.009    29.030   1.000 47.46761 ?  797 HOH   A O    1 
HETATM 2324 O  O    . HOH   D 4 .   ? 44.85100  -4.32800  12.74700 1.000 53.46800 ?  798 HOH   A O    1 
HETATM 2325 O  O    . HOH   D 4 .   ? 3.12900   20.26500  13.06200 1.000 45.97854 ?  799 HOH   A O    1 
HETATM 2326 O  O    . HOH   D 4 .   ? 39.896    -3.729    -3.062   1.000 44.34571 ?  800 HOH   A O    1 
HETATM 2327 O  O    . HOH   D 4 .   ? 24.85400  12.66700  0.96300  1.000 45.12431 ?  801 HOH   A O    1 
HETATM 2328 O  O    . HOH   D 4 .   ? 44.44700  -6.47900  18.22100 1.000 57.68618 ?  802 HOH   A O    1 
HETATM 2329 O  O    . HOH   D 4 .   ? 10.28900  -6.39200  12.04200 1.000 40.95711 ?  803 HOH   A O    1 
HETATM 2330 O  O    . HOH   D 4 .   ? 40.75600  -7.97300  16.72200 1.000 52.65740 ?  804 HOH   A O    1 
HETATM 2331 O  O    . HOH   D 4 .   ? 4.837     6.965     -1.043   1.000 57.03170 ?  805 HOH   A O    1 
HETATM 2332 O  O    . HOH   D 4 .   ? 28.71900  13.73800  1.37600  1.000 51.80865 ?  806 HOH   A O    1 
HETATM 2333 O  O    . HOH   D 4 .   ? 23.21100  -11.41800 -7.02900 1.000 47.52148 ?  807 HOH   A O    1 
HETATM 2334 O  O    . HOH   D 4 .   ? 12.04600  -11.87700 11.11900 1.000 41.37291 ?  808 HOH   A O    1 
HETATM 2335 O  O    . HOH   D 4 .   ? 14.85200  4.59000   -2.84700 1.000 45.61199 ?  809 HOH   A O    1 
HETATM 2336 O  O    . HOH   D 4 .   ? 30.493    -14.112   1.249    1.000 32.71441 ?  810 HOH   A O    1 
HETATM 2337 O  O    . HOH   D 4 .   ? -6.13200  7.58700   8.71500  1.000 40.66349 ?  811 HOH   A O    1 
HETATM 2338 O  O    . HOH   D 4 .   ? 2.64800   9.39900   23.91200 1.000 53.50915 ?  812 HOH   A O    1 
HETATM 2339 O  O    . HOH   D 4 .   ? 41.70700  -7.58600  14.22200 1.000 48.73039 ?  813 HOH   A O    1 
HETATM 2340 O  O    . HOH   D 4 .   ? 31.64000  -4.76400  -2.20200 1.000 35.91947 ?  814 HOH   A O    1 
HETATM 2341 O  O    . HOH   D 4 .   ? 23.71300  7.25400   27.37000 1.000 39.30161 ?  815 HOH   A O    1 
HETATM 2342 O  O    . HOH   D 4 .   ? 39.94900  -4.96600  -0.24500 1.000 33.06155 ?  816 HOH   A O    1 
HETATM 2343 O  O    . HOH   D 4 .   ? 14.30800  -18.80200 4.37500  1.000 52.87417 ?  817 HOH   A O    1 
HETATM 2344 O  O    . HOH   D 4 .   ? 6.092     7.898     -4.752   1.000 58.04622 ?  818 HOH   A O    1 
HETATM 2345 O  O    . HOH   D 4 .   ? 13.78400  -1.30100  27.64400 1.000 50.22533 ?  819 HOH   A O    1 
HETATM 2346 O  O    . HOH   D 4 .   ? -8.567    -10.668   9.245    1.000 39.53087 ?  820 HOH   A O    1 
HETATM 2347 O  O    . HOH   D 4 .   ? -8.93000  5.31000   13.68300 1.000 53.34842 ?  821 HOH   A O    1 
HETATM 2348 O  O    . HOH   D 4 .   ? 37.04100  -14.25600 6.55700  1.000 40.49509 ?  822 HOH   A O    1 
HETATM 2349 O  O    . HOH   D 4 .   ? 14.34900  1.68300   -6.57500 1.000 44.02945 ?  823 HOH   A O    1 
HETATM 2350 O  O    . HOH   D 4 .   ? 24.85100  13.35500  12.18200 1.000 42.91649 ?  824 HOH   A O    1 
HETATM 2351 O  O    . HOH   D 4 .   ? 38.21300  -15.72000 11.35200 1.000 51.10963 ?  825 HOH   A O    1 
HETATM 2352 O  O    . HOH   D 4 .   ? 30.46800  -0.46600  -3.59700 1.000 29.12569 ?  826 HOH   A O    1 
HETATM 2353 O  O    . HOH   D 4 .   ? 12.02600  -14.29400 7.63200  1.000 47.29720 ?  827 HOH   A O    1 
HETATM 2354 O  O    . HOH   D 4 .   ? 26.801    13.366    27.225   1.000 51.37121 ?  828 HOH   A O    1 
HETATM 2355 O  O    . HOH   D 4 .   ? -13.47500 11.38300  18.70700 1.000 53.03884 ?  829 HOH   A O    1 
HETATM 2356 O  O    . HOH   D 4 .   ? -1.95800  -0.22300  25.69900 1.000 44.65000 ?  830 HOH   A O    1 
HETATM 2357 O  O    . HOH   D 4 .   ? 0.759     18.324    -2.178   1.000 63.09111 ?  831 HOH   A O    1 
HETATM 2358 O  O    . HOH   D 4 .   ? 9.81200   10.24200  26.82200 1.000 50.34590 ?  832 HOH   A O    1 
HETATM 2359 O  O    A HOH   D 4 .   ? 44.57000  -8.04500  14.13100 0.530 32.59095 ?  833 HOH   A O    1 
HETATM 2360 O  O    B HOH   D 4 .   ? 43.58200  -9.45700  13.08700 0.470 30.95173 ?  833 HOH   A O    1 
HETATM 2361 O  O    . HOH   D 4 .   ? 24.422    16.652    4.259    1.000 46.07098 ?  834 HOH   A O    1 
HETATM 2362 O  O    . HOH   D 4 .   ? -14.12900 13.23900  17.43800 1.000 59.73434 ?  835 HOH   A O    1 
HETATM 2363 O  O    . HOH   E 4 .   ? 11.11100  -9.84100  -7.86600 1.000 33.91540 ?  701 HOH   C O    1 
HETATM 2364 O  O    . HOH   E 4 .   ? 17.65300  -1.01500  -4.11200 1.000 30.99268 ?  702 HOH   C O    1 
HETATM 2365 O  O    . HOH   E 4 .   ? 4.25200   -11.72600 -0.67600 1.000 46.08921 ?  703 HOH   C O    1 
HETATM 2366 O  O    . HOH   E 4 .   ? 10.35700  -3.66900  -5.40700 1.000 29.70571 ?  704 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  ? 0.44404 0.73983 0.80040 -0.01835 -0.07390 -0.06158 123 LYS   A N    
2    C  CA   . LYS   A 18  ? 0.39181 0.67044 0.75113 -0.02939 -0.05731 -0.06043 123 LYS   A CA   
3    C  C    . LYS   A 18  ? 0.26091 0.51590 0.59330 -0.02489 -0.04355 -0.04813 123 LYS   A C    
4    O  O    . LYS   A 18  ? 0.24193 0.49755 0.56673 -0.01441 -0.04320 -0.04124 123 LYS   A O    
5    C  CB   . LYS   A 18  ? 0.40809 0.70207 0.80686 -0.03674 -0.04897 -0.06386 123 LYS   A CB   
6    C  CG   . LYS   A 18  ? 0.47587 0.75374 0.87978 -0.04877 -0.03195 -0.06155 123 LYS   A CG   
7    C  CD   . LYS   A 18  ? 0.50136 0.76955 0.90232 -0.05883 -0.03705 -0.06956 123 LYS   A CD   
8    C  CE   . LYS   A 18  ? 0.46440 0.70824 0.85052 -0.06545 -0.02560 -0.06487 123 LYS   A CE   
9    N  NZ   . LYS   A 18  ? 0.40954 0.63579 0.75514 -0.05705 -0.02800 -0.05877 123 LYS   A NZ   
10   N  N    . LEU   A 19  ? 0.26634 0.50049 0.58530 -0.03265 -0.03285 -0.04587 124 LEU   A N    
11   C  CA   . LEU   A 19  ? 0.21320 0.42590 0.50706 -0.02932 -0.02034 -0.03567 124 LEU   A CA   
12   C  C    . LEU   A 19  ? 0.19387 0.41255 0.50449 -0.02771 -0.00658 -0.03096 124 LEU   A C    
13   O  O    . LEU   A 19  ? 0.23685 0.46593 0.57470 -0.03525 0.00126  -0.03331 124 LEU   A O    
14   C  CB   . LEU   A 19  ? 0.23878 0.43027 0.51693 -0.03784 -0.01307 -0.03450 124 LEU   A CB   
15   C  CG   . LEU   A 19  ? 0.33491 0.51591 0.58993 -0.03799 -0.02374 -0.03820 124 LEU   A CG   
16   C  CD1  . LEU   A 19  ? 0.37245 0.53934 0.62752 -0.04839 -0.01817 -0.04071 124 LEU   A CD1  
17   C  CD2  . LEU   A 19  ? 0.25360 0.41979 0.47555 -0.02924 -0.02402 -0.03045 124 LEU   A CD2  
18   N  N    . SER   A 20  ? 0.18054 0.39287 0.47589 -0.01793 -0.00310 -0.02468 125 SER   A N    
19   C  CA   . SER   A 20  ? 0.19111 0.40591 0.49625 -0.01556 0.01155  -0.02096 125 SER   A CA   
20   C  C    . SER   A 20  ? 0.19143 0.38914 0.48271 -0.02273 0.02664  -0.01652 125 SER   A C    
21   O  O    . SER   A 20  ? 0.16071 0.34156 0.43131 -0.02739 0.02502  -0.01516 125 SER   A O    
22   C  CB   . SER   A 20  ? 0.18160 0.39159 0.47316 -0.00301 0.01049  -0.01691 125 SER   A CB   
23   O  OG   . SER   A 20  ? 0.17840 0.36484 0.43597 -0.00164 0.01094  -0.01252 125 SER   A OG   
24   N  N    . GLU   A 21  ? 0.15469 0.35774 0.45717 -0.02289 0.04165  -0.01394 126 GLU   A N    
25   C  CA   . GLU   A 21  ? 0.15913 0.34688 0.44468 -0.02767 0.05626  -0.00811 126 GLU   A CA   
26   C  C    . GLU   A 21  ? 0.15918 0.32522 0.40788 -0.02199 0.05447  -0.00472 126 GLU   A C    
27   O  O    . GLU   A 21  ? 0.22212 0.37170 0.45092 -0.02679 0.05765  -0.00102 126 GLU   A O    
28   C  CB   . GLU   A 21  ? 0.29336 0.49252 0.59362 -0.02667 0.07297  -0.00592 126 GLU   A CB   
29   C  CG   . GLU   A 21  ? 0.41101 0.59943 0.69899 -0.03337 0.08888  0.00117  126 GLU   A CG   
30   C  CD   . GLU   A 21  ? 0.47846 0.67287 0.76405 -0.02838 0.10542  0.00383  126 GLU   A CD   
31   O  OE1  . GLU   A 21  ? 0.47032 0.65099 0.72634 -0.02283 0.10940  0.00593  126 GLU   A OE1  
32   O  OE2  . GLU   A 21  ? 0.47254 0.68672 0.78676 -0.02991 0.11433  0.00288  126 GLU   A OE2  
33   N  N    . GLU   A 22  ? 0.15765 0.32349 0.39903 -0.01171 0.04891  -0.00586 127 GLU   A N    
34   C  CA   . GLU   A 22  ? 0.15808 0.30424 0.36838 -0.00658 0.04642  -0.00336 127 GLU   A CA   
35   C  C    . GLU   A 22  ? 0.15498 0.28893 0.34862 -0.01077 0.03600  -0.00267 127 GLU   A C    
36   O  O    . GLU   A 22  ? 0.15660 0.27352 0.32680 -0.01266 0.03866  0.00026  127 GLU   A O    
37   C  CB   . GLU   A 22  ? 0.32123 0.47009 0.53303 0.00465  0.04086  -0.00461 127 GLU   A CB   
38   C  CG   . GLU   A 22  ? 0.31078 0.43996 0.49508 0.00969  0.03764  -0.00233 127 GLU   A CG   
39   C  CD   . GLU   A 22  ? 0.44426 0.57450 0.63373 0.02071  0.03505  -0.00302 127 GLU   A CD   
40   O  OE1  . GLU   A 22  ? 0.44069 0.56008 0.61741 0.02512  0.02651  -0.00040 127 GLU   A OE1  
41   O  OE2  . GLU   A 22  ? 0.53285 0.67483 0.74060 0.02506  0.04213  -0.00590 127 GLU   A OE2  
42   N  N    . GLN   A 23  ? 0.15209 0.29599 0.35776 -0.01178 0.02381  -0.00604 128 GLN   A N    
43   C  CA   . GLN   A 23  ? 0.15077 0.28501 0.34067 -0.01504 0.01410  -0.00682 128 GLN   A CA   
44   C  C    . GLN   A 23  ? 0.15208 0.27794 0.34021 -0.02511 0.01996  -0.00682 128 GLN   A C    
45   O  O    . GLN   A 23  ? 0.18094 0.29141 0.34836 -0.02695 0.01808  -0.00539 128 GLN   A O    
46   C  CB   . GLN   A 23  ? 0.16622 0.31589 0.36934 -0.01343 -0.00025 -0.01165 128 GLN   A CB   
47   C  CG   . GLN   A 23  ? 0.19915 0.35237 0.39703 -0.00236 -0.00815 -0.00894 128 GLN   A CG   
48   C  CD   . GLN   A 23  ? 0.21683 0.38916 0.42905 0.00058  -0.02236 -0.01279 128 GLN   A CD   
49   O  OE1  . GLN   A 23  ? 0.24079 0.42951 0.47666 -0.00456 -0.02486 -0.01903 128 GLN   A OE1  
50   N  NE2  . GLN   A 23  ? 0.30559 0.47660 0.50405 0.00889  -0.03190 -0.00881 128 GLN   A NE2  
51   N  N    . GLN   A 24  ? 0.15402 0.28981 0.36537 -0.03155 0.02760  -0.00780 129 GLN   A N    
52   C  CA   . GLN   A 24  ? 0.15773 0.28403 0.36957 -0.04095 0.03460  -0.00584 129 GLN   A CA   
53   C  C    . GLN   A 24  ? 0.16121 0.27023 0.34824 -0.03968 0.04508  0.00177  129 GLN   A C    
54   O  O    . GLN   A 24  ? 0.16387 0.25834 0.33801 -0.04397 0.04605  0.00442  129 GLN   A O    
55   C  CB   . GLN   A 24  ? 0.16079 0.30193 0.40530 -0.04821 0.04207  -0.00699 129 GLN   A CB   
56   C  CG   . GLN   A 24  ? 0.19163 0.35087 0.46272 -0.05064 0.03020  -0.01614 129 GLN   A CG   
57   C  CD   . GLN   A 24  ? 0.32030 0.49651 0.62786 -0.05780 0.03788  -0.01769 129 GLN   A CD   
58   O  OE1  . GLN   A 24  ? 0.32732 0.49729 0.64346 -0.06642 0.04872  -0.01362 129 GLN   A OE1  
59   N  NE2  . GLN   A 24  ? 0.34008 0.53825 0.67065 -0.05411 0.03256  -0.02278 129 GLN   A NE2  
60   N  N    . HIS   A 25  ? 0.16248 0.27342 0.34291 -0.03325 0.05244  0.00457  130 HIS   A N    
61   C  CA   . HIS   A 25  ? 0.18345 0.27995 0.33863 -0.03101 0.06079  0.01013  130 HIS   A CA   
62   C  C    . HIS   A 25  ? 0.16415 0.24488 0.29393 -0.02788 0.05183  0.00998  130 HIS   A C    
63   O  O    . HIS   A 25  ? 0.16992 0.23702 0.28171 -0.02980 0.05490  0.01400  130 HIS   A O    
64   C  CB   . HIS   A 25  ? 0.20874 0.31181 0.36255 -0.02388 0.06908  0.01017  130 HIS   A CB   
65   C  CG   . HIS   A 25  ? 0.24325 0.36085 0.41758 -0.02672 0.08197  0.01183  130 HIS   A CG   
66   N  ND1  . HIS   A 25  ? 0.22482 0.33983 0.39841 -0.03331 0.09366  0.01848  130 HIS   A ND1  
67   C  CD2  . HIS   A 25  ? 0.25099 0.38638 0.44759 -0.02340 0.08585  0.00847  130 HIS   A CD2  
68   C  CE1  . HIS   A 25  ? 0.21156 0.34255 0.40586 -0.03455 0.10487  0.01936  130 HIS   A CE1  
69   N  NE2  . HIS   A 25  ? 0.27822 0.42234 0.48750 -0.02858 0.10028  0.01263  130 HIS   A NE2  
70   N  N    . ILE   A 26  ? 0.15864 0.24177 0.28714 -0.02266 0.04104  0.00620  131 ILE   A N    
71   C  CA   . ILE   A 26  ? 0.15629 0.22609 0.26300 -0.02010 0.03320  0.00656  131 ILE   A CA   
72   C  C    . ILE   A 26  ? 0.16724 0.22921 0.26943 -0.02671 0.02989  0.00642  131 ILE   A C    
73   O  O    . ILE   A 26  ? 0.15766 0.20585 0.24131 -0.02716 0.03091  0.00913  131 ILE   A O    
74   C  CB   . ILE   A 26  ? 0.16580 0.24156 0.27493 -0.01396 0.02257  0.00417  131 ILE   A CB   
75   C  CG1  . ILE   A 26  ? 0.16555 0.24346 0.27587 -0.00617 0.02604  0.00484  131 ILE   A CG1  
76   C  CG2  . ILE   A 26  ? 0.15129 0.21587 0.24117 -0.01307 0.01445  0.00489  131 ILE   A CG2  
77   C  CD1  . ILE   A 26  ? 0.22497 0.31128 0.34403 0.00042  0.01670  0.00421  131 ILE   A CD1  
78   N  N    . ILE   A 27  ? 0.16651 0.23768 0.28744 -0.03179 0.02572  0.00237  132 ILE   A N    
79   C  CA   . ILE   A 27  ? 0.17091 0.23463 0.29088 -0.03797 0.02244  0.00031  132 ILE   A CA   
80   C  C    . ILE   A 27  ? 0.17965 0.23164 0.29532 -0.04261 0.03291  0.00638  132 ILE   A C    
81   O  O    . ILE   A 27  ? 0.20031 0.23893 0.30231 -0.04381 0.03178  0.00792  132 ILE   A O    
82   C  CB   . ILE   A 27  ? 0.18348 0.26079 0.32794 -0.04286 0.01607  -0.00711 132 ILE   A CB   
83   C  CG1  . ILE   A 27  ? 0.16704 0.25522 0.30993 -0.03712 0.00358  -0.01230 132 ILE   A CG1  
84   C  CG2  . ILE   A 27  ? 0.16179 0.23048 0.30986 -0.05008 0.01477  -0.01038 132 ILE   A CG2  
85   C  CD1  . ILE   A 27  ? 0.20247 0.30833 0.36974 -0.04041 -0.00435 -0.02074 132 ILE   A CD1  
86   N  N    . ALA   A 28  ? 0.16999 0.22751 0.29710 -0.04469 0.04356  0.01064  133 ALA   A N    
87   C  CA   . ALA   A 28  ? 0.17566 0.22315 0.29789 -0.04859 0.05410  0.01852  133 ALA   A CA   
88   C  C    . ALA   A 28  ? 0.18456 0.21915 0.27782 -0.04326 0.05557  0.02328  133 ALA   A C    
89   O  O    . ALA   A 28  ? 0.19808 0.22021 0.28111 -0.04525 0.05753  0.02821  133 ALA   A O    
90   C  CB   . ALA   A 28  ? 0.18152 0.23971 0.31951 -0.05088 0.06645  0.02303  133 ALA   A CB   
91   N  N    . ILE   A 29  ? 0.17385 0.21130 0.25535 -0.03627 0.05412  0.02148  134 ILE   A N    
92   C  CA   . ILE   A 29  ? 0.17585 0.20252 0.23219 -0.03141 0.05434  0.02399  134 ILE   A CA   
93   C  C    . ILE   A 29  ? 0.17187 0.18760 0.21706 -0.03162 0.04528  0.02243  134 ILE   A C    
94   O  O    . ILE   A 29  ? 0.20006 0.20516 0.22960 -0.03102 0.04633  0.02624  134 ILE   A O    
95   C  CB   . ILE   A 29  ? 0.19178 0.22351 0.24261 -0.02436 0.05396  0.02055  134 ILE   A CB   
96   C  CG1  . ILE   A 29  ? 0.23100 0.27198 0.28763 -0.02313 0.06546  0.02233  134 ILE   A CG1  
97   C  CG2  . ILE   A 29  ? 0.19446 0.21496 0.22262 -0.02001 0.05054  0.02038  134 ILE   A CG2  
98   C  CD1  . ILE   A 29  ? 0.26583 0.31332 0.32345 -0.01603 0.06568  0.01724  134 ILE   A CD1  
99   N  N    . LEU   A 30  ? 0.17199 0.19153 0.22480 -0.03192 0.03626  0.01677  135 LEU   A N    
100  C  CA   . LEU   A 30  ? 0.16408 0.17527 0.20592 -0.03146 0.02848  0.01464  135 LEU   A CA   
101  C  C    . LEU   A 30  ? 0.18193 0.18560 0.22790 -0.03686 0.02908  0.01539  135 LEU   A C    
102  O  O    . LEU   A 30  ? 0.20912 0.20259 0.24264 -0.03598 0.02694  0.01643  135 LEU   A O    
103  C  CB   . LEU   A 30  ? 0.17971 0.19884 0.22629 -0.02944 0.01923  0.00893  135 LEU   A CB   
104  C  CG   . LEU   A 30  ? 0.16354 0.18676 0.20502 -0.02302 0.01738  0.00939  135 LEU   A CG   
105  C  CD1  . LEU   A 30  ? 0.17653 0.20828 0.22245 -0.02072 0.00811  0.00592  135 LEU   A CD1  
106  C  CD2  . LEU   A 30  ? 0.17528 0.18728 0.19780 -0.01961 0.01838  0.01215  135 LEU   A CD2  
107  N  N    . LEU   A 31  ? 0.18668 0.19521 0.25236 -0.04247 0.03200  0.01461  136 LEU   A N    
108  C  CA   . LEU   A 31  ? 0.18069 0.18010 0.25357 -0.04785 0.03384  0.01598  136 LEU   A CA   
109  C  C    . LEU   A 31  ? 0.22822 0.21645 0.28826 -0.04690 0.04163  0.02602  136 LEU   A C    
110  O  O    . LEU   A 31  ? 0.22293 0.19959 0.27618 -0.04692 0.04011  0.02798  136 LEU   A O    
111  C  CB   . LEU   A 31  ? 0.18996 0.19700 0.28980 -0.05473 0.03656  0.01362  136 LEU   A CB   
112  C  CG   . LEU   A 31  ? 0.17481 0.19348 0.28846 -0.05603 0.02671  0.00222  136 LEU   A CG   
113  C  CD1  . LEU   A 31  ? 0.17846 0.20697 0.32172 -0.06313 0.02931  -0.00086 136 LEU   A CD1  
114  C  CD2  . LEU   A 31  ? 0.24056 0.25210 0.34803 -0.05602 0.01821  -0.00503 136 LEU   A CD2  
115  N  N    . ASP   A 32  ? 0.19316 0.18574 0.24939 -0.04536 0.04989  0.03229  137 ASP   A N    
116  C  CA   . ASP   A 32  ? 0.21296 0.19729 0.25315 -0.04319 0.05660  0.04190  137 ASP   A CA   
117  C  C    . ASP   A 32  ? 0.24806 0.22511 0.26635 -0.03756 0.05031  0.04069  137 ASP   A C    
118  O  O    . ASP   A 32  ? 0.24795 0.21514 0.25656 -0.03661 0.05062  0.04620  137 ASP   A O    
119  C  CB   . ASP   A 32  ? 0.24438 0.23753 0.28170 -0.04138 0.06621  0.04661  137 ASP   A CB   
120  C  CG   . ASP   A 32  ? 0.28506 0.27245 0.30057 -0.03743 0.07180  0.05526  137 ASP   A CG   
121  O  OD1  . ASP   A 32  ? 0.28691 0.27431 0.28406 -0.03159 0.06841  0.05217  137 ASP   A OD1  
122  O  OD2  . ASP   A 32  ? 0.28943 0.27254 0.30668 -0.04012 0.07934  0.06529  137 ASP   A OD2  
123  N  N    . ALA   A 33  ? 0.20280 0.18476 0.21500 -0.03378 0.04447  0.03393  138 ALA   A N    
124  C  CA   . ALA   A 33  ? 0.21560 0.19175 0.21002 -0.02915 0.03907  0.03252  138 ALA   A CA   
125  C  C    . ALA   A 33  ? 0.21291 0.18093 0.20723 -0.03035 0.03318  0.03094  138 ALA   A C    
126  O  O    . ALA   A 33  ? 0.23620 0.19698 0.21861 -0.02789 0.03180  0.03377  138 ALA   A O    
127  C  CB   . ALA   A 33  ? 0.17676 0.15902 0.16908 -0.02568 0.03458  0.02643  138 ALA   A CB   
128  N  N    . HIS   A 34  ? 0.19366 0.16403 0.20163 -0.03367 0.02932  0.02544  139 HIS   A N    
129  C  CA   . HIS   A 34  ? 0.21217 0.17573 0.22119 -0.03452 0.02435  0.02211  139 HIS   A CA   
130  C  C    . HIS   A 34  ? 0.21729 0.17047 0.22963 -0.03646 0.02850  0.02843  139 HIS   A C    
131  O  O    . HIS   A 34  ? 0.23338 0.17857 0.23861 -0.03411 0.02615  0.02960  139 HIS   A O    
132  C  CB   . HIS   A 34  ? 0.25351 0.22346 0.27647 -0.03758 0.01943  0.01347  139 HIS   A CB   
133  C  CG   . HIS   A 34  ? 0.19878 0.16330 0.22282 -0.03798 0.01456  0.00769  139 HIS   A CG   
134  N  ND1  . HIS   A 34  ? 0.23032 0.19187 0.24069 -0.03386 0.01108  0.00649  139 HIS   A ND1  
135  C  CD2  . HIS   A 34  ? 0.22741 0.18943 0.26601 -0.04196 0.01295  0.00176  139 HIS   A CD2  
136  C  CE1  . HIS   A 34  ? 0.21316 0.17125 0.22845 -0.03470 0.00799  0.00020  139 HIS   A CE1  
137  N  NE2  . HIS   A 34  ? 0.22655 0.18428 0.25870 -0.03948 0.00873  -0.00334 139 HIS   A NE2  
138  N  N    . HIS   A 35  ? 0.21489 0.16823 0.23930 -0.04052 0.03509  0.03340  140 HIS   A N    
139  C  CA   . HIS   A 35  ? 0.25479 0.19707 0.28430 -0.04245 0.03960  0.04131  140 HIS   A CA   
140  C  C    . HIS   A 35  ? 0.30999 0.24691 0.32047 -0.03737 0.04232  0.05122  140 HIS   A C    
141  O  O    . HIS   A 35  ? 0.31128 0.23776 0.32167 -0.03651 0.04298  0.05753  140 HIS   A O    
142  C  CB   . HIS   A 35  ? 0.28670 0.23113 0.33534 -0.04861 0.04715  0.04551  140 HIS   A CB   
143  C  CG   . HIS   A 35  ? 0.26818 0.21768 0.33853 -0.05407 0.04317  0.03478  140 HIS   A CG   
144  N  ND1  . HIS   A 35  ? 0.26663 0.22435 0.35673 -0.05973 0.04783  0.03437  140 HIS   A ND1  
145  C  CD2  . HIS   A 35  ? 0.25465 0.20389 0.32990 -0.05445 0.03464  0.02320  140 HIS   A CD2  
146  C  CE1  . HIS   A 35  ? 0.27552 0.23783 0.38228 -0.06347 0.04122  0.02249  140 HIS   A CE1  
147  N  NE2  . HIS   A 35  ? 0.24751 0.20486 0.34425 -0.06013 0.03322  0.01543  140 HIS   A NE2  
148  N  N    . LYS   A 36  ? 0.28448 0.22852 0.27952 -0.03355 0.04329  0.05215  141 LYS   A N    
149  C  CA   . LYS   A 36  ? 0.33164 0.27252 0.30732 -0.02821 0.04382  0.05904  141 LYS   A CA   
150  C  C    . LYS   A 36  ? 0.28081 0.21835 0.24723 -0.02422 0.03543  0.05406  141 LYS   A C    
151  O  O    . LYS   A 36  ? 0.31920 0.25364 0.27269 -0.01991 0.03416  0.05926  141 LYS   A O    
152  C  CB   . LYS   A 36  ? 0.40858 0.35855 0.37137 -0.02534 0.04765  0.05969  141 LYS   A CB   
153  C  CG   . LYS   A 36  ? 0.54266 0.49954 0.51447 -0.02858 0.05667  0.06308  141 LYS   A CG   
154  C  CD   . LYS   A 36  ? 0.60766 0.57151 0.56258 -0.02421 0.06200  0.06606  141 LYS   A CD   
155  C  CE   . LYS   A 36  ? 0.69080 0.65641 0.63090 -0.01905 0.05464  0.05786  141 LYS   A CE   
156  N  NZ   . LYS   A 36  ? 0.76316 0.73774 0.69314 -0.01550 0.05888  0.05468  141 LYS   A NZ   
157  N  N    . THR   A 37  ? 0.23409 0.17373 0.20660 -0.02526 0.02977  0.04442  142 THR   A N    
158  C  CA   . THR   A 37  ? 0.22900 0.16757 0.19376 -0.02180 0.02313  0.03972  142 THR   A CA   
159  C  C    . THR   A 37  ? 0.21600 0.14974 0.19065 -0.02292 0.01933  0.03484  142 THR   A C    
160  O  O    . THR   A 37  ? 0.25949 0.19358 0.22963 -0.02027 0.01470  0.03064  142 THR   A O    
161  C  CB   . THR   A 37  ? 0.22413 0.17055 0.18390 -0.02072 0.02035  0.03318  142 THR   A CB   
162  O  OG1  . THR   A 37  ? 0.22047 0.17207 0.19132 -0.02396 0.02048  0.02842  142 THR   A OG1  
163  C  CG2  . THR   A 37  ? 0.25056 0.20085 0.19943 -0.01830 0.02338  0.03596  142 THR   A CG2  
164  N  N    . TYR   A 38  ? 0.22093 0.15076 0.21023 -0.02690 0.02146  0.03437  143 TYR   A N    
165  C  CA   . TYR   A 38  ? 0.24565 0.17044 0.24536 -0.02772 0.01814  0.02800  143 TYR   A CA   
166  C  C    . TYR   A 38  ? 0.25364 0.16695 0.26371 -0.02889 0.02176  0.03500  143 TYR   A C    
167  O  O    . TYR   A 38  ? 0.26135 0.17293 0.28137 -0.03313 0.02693  0.03968  143 TYR   A O    
168  C  CB   . TYR   A 38  ? 0.21485 0.14614 0.22537 -0.03160 0.01578  0.01760  143 TYR   A CB   
169  C  CG   . TYR   A 38  ? 0.24115 0.16978 0.25818 -0.03116 0.01157  0.00816  143 TYR   A CG   
170  C  CD1  . TYR   A 38  ? 0.28132 0.20063 0.31411 -0.03360 0.01264  0.00613  143 TYR   A CD1  
171  C  CD2  . TYR   A 38  ? 0.24385 0.17911 0.25186 -0.02811 0.00724  0.00132  143 TYR   A CD2  
172  C  CE1  . TYR   A 38  ? 0.30512 0.22223 0.34414 -0.03258 0.00905  -0.00436 143 TYR   A CE1  
173  C  CE2  . TYR   A 38  ? 0.26411 0.19860 0.27676 -0.02711 0.00433  -0.00804 143 TYR   A CE2  
174  C  CZ   . TYR   A 38  ? 0.27556 0.20111 0.30348 -0.02910 0.00504  -0.01173 143 TYR   A CZ   
175  O  OH   . TYR   A 38  ? 0.27438 0.19934 0.30742 -0.02756 0.00238  -0.02290 143 TYR   A OH   
176  N  N    . ASP   A 39  ? 0.21490 0.12055 0.22438 -0.02504 0.01941  0.03626  144 ASP   A N    
177  C  CA   . ASP   A 39  ? 0.25275 0.14565 0.27246 -0.02478 0.02235  0.04432  144 ASP   A CA   
178  C  C    . ASP   A 39  ? 0.27008 0.15630 0.30722 -0.02623 0.01992  0.03427  144 ASP   A C    
179  O  O    . ASP   A 39  ? 0.26666 0.15142 0.30218 -0.02172 0.01586  0.02903  144 ASP   A O    
180  C  CB   . ASP   A 39  ? 0.27818 0.16755 0.28522 -0.01799 0.02096  0.05394  144 ASP   A CB   
181  C  CG   . ASP   A 39  ? 0.33987 0.21533 0.35727 -0.01629 0.02345  0.06412  144 ASP   A CG   
182  O  OD1  . ASP   A 39  ? 0.32334 0.19092 0.35770 -0.02131 0.02792  0.06580  144 ASP   A OD1  
183  O  OD2  . ASP   A 39  ? 0.34978 0.22231 0.35985 -0.00980 0.02064  0.07060  144 ASP   A OD2  
184  N  N    . PRO   A 40  ? 0.25651 0.13933 0.31187 -0.03239 0.02231  0.03017  145 PRO   A N    
185  C  CA   . PRO   A 40  ? 0.25015 0.12709 0.32295 -0.03389 0.01949  0.01773  145 PRO   A CA   
186  C  C    . PRO   A 40  ? 0.31049 0.17111 0.39500 -0.03089 0.02085  0.02326  145 PRO   A C    
187  O  O    . PRO   A 40  ? 0.33699 0.19095 0.43830 -0.03184 0.01902  0.01226  145 PRO   A O    
188  C  CB   . PRO   A 40  ? 0.30160 0.18085 0.39191 -0.04204 0.02148  0.01223  145 PRO   A CB   
189  C  CG   . PRO   A 40  ? 0.33027 0.20934 0.41828 -0.04450 0.02825  0.02746  145 PRO   A CG   
190  C  CD   . PRO   A 40  ? 0.24982 0.13493 0.31219 -0.03835 0.02795  0.03600  145 PRO   A CD   
191  N  N    . THR   A 41  ? 0.30048 0.15463 0.37714 -0.02686 0.02373  0.03965  146 THR   A N    
192  C  CA   . THR   A 41  ? 0.30785 0.14755 0.39334 -0.02179 0.02371  0.04610  146 THR   A CA   
193  C  C    . THR   A 41  ? 0.30094 0.14511 0.37399 -0.01356 0.01816  0.04290  146 THR   A C    
194  O  O    . THR   A 41  ? 0.30446 0.13852 0.38725 -0.00838 0.01678  0.04418  146 THR   A O    
195  C  CB   . THR   A 41  ? 0.33377 0.16439 0.41788 -0.02090 0.02949  0.06720  146 THR   A CB   
196  O  OG1  . THR   A 41  ? 0.30828 0.14801 0.36738 -0.01540 0.02814  0.07669  146 THR   A OG1  
197  C  CG2  . THR   A 41  ? 0.37158 0.20334 0.46437 -0.02939 0.03606  0.07106  146 THR   A CG2  
198  N  N    . TYR   A 42  ? 0.30277 0.16178 0.35690 -0.01227 0.01520  0.03884  147 TYR   A N    
199  C  CA   . TYR   A 42  ? 0.30976 0.17533 0.35406 -0.00564 0.01037  0.03490  147 TYR   A CA   
200  C  C    . TYR   A 42  ? 0.36891 0.22803 0.41048 0.00157  0.00916  0.04810  147 TYR   A C    
201  O  O    . TYR   A 42  ? 0.31944 0.17911 0.36370 0.00766  0.00545  0.04470  147 TYR   A O    
202  C  CB   . TYR   A 42  ? 0.31074 0.17699 0.36629 -0.00483 0.00801  0.01862  147 TYR   A CB   
203  C  CG   . TYR   A 42  ? 0.29147 0.16500 0.34902 -0.01132 0.00824  0.00598  147 TYR   A CG   
204  C  CD1  . TYR   A 42  ? 0.32325 0.18932 0.39935 -0.01582 0.00941  -0.00227 147 TYR   A CD1  
205  C  CD2  . TYR   A 42  ? 0.31716 0.20509 0.35919 -0.01282 0.00684  0.00260  147 TYR   A CD2  
206  C  CE1  . TYR   A 42  ? 0.31992 0.19475 0.39769 -0.02126 0.00825  -0.01426 147 TYR   A CE1  
207  C  CE2  . TYR   A 42  ? 0.35848 0.25411 0.40176 -0.01774 0.00620  -0.00759 147 TYR   A CE2  
208  C  CZ   . TYR   A 42  ? 0.33479 0.22486 0.39524 -0.02178 0.00648  -0.01620 147 TYR   A CZ   
209  O  OH   . TYR   A 42  ? 0.33997 0.23985 0.40154 -0.02622 0.00449  -0.02699 147 TYR   A OH   
210  N  N    . ALA   A 43  ? 0.28347 0.13814 0.31908 0.00140  0.01229  0.06356  148 ALA   A N    
211  C  CA   . ALA   A 43  ? 0.35435 0.20249 0.38722 0.00873  0.01095  0.07810  148 ALA   A CA   
212  C  C    . ALA   A 43  ? 0.34295 0.20321 0.35918 0.01524  0.00477  0.07860  148 ALA   A C    
213  O  O    . ALA   A 43  ? 0.42588 0.28307 0.44266 0.02280  0.00117  0.08670  148 ALA   A O    
214  C  CB   . ALA   A 43  ? 0.47273 0.31520 0.50053 0.00690  0.01672  0.09531  148 ALA   A CB   
215  N  N    . ASP   A 44  ? 0.31587 0.18980 0.31907 0.01262  0.00313  0.07038  149 ASP   A N    
216  C  CA   . ASP   A 44  ? 0.34137 0.22691 0.33115 0.01766  -0.00267 0.07012  149 ASP   A CA   
217  C  C    . ASP   A 44  ? 0.35752 0.24785 0.35628 0.02102  -0.00705 0.05927  149 ASP   A C    
218  O  O    . ASP   A 44  ? 0.36244 0.26241 0.35471 0.02531  -0.01221 0.05886  149 ASP   A O    
219  C  CB   . ASP   A 44  ? 0.30001 0.19705 0.27421 0.01348  -0.00218 0.06617  149 ASP   A CB   
220  C  CG   . ASP   A 44  ? 0.40908 0.30460 0.37256 0.01131  0.00249  0.07657  149 ASP   A CG   
221  O  OD1  . ASP   A 44  ? 0.44544 0.33546 0.40537 0.01541  0.00319  0.08979  149 ASP   A OD1  
222  O  OD2  . ASP   A 44  ? 0.44001 0.34049 0.39872 0.00598  0.00580  0.07210  149 ASP   A OD2  
223  N  N    . PHE   A 45  ? 0.30831 0.19324 0.32243 0.01923  -0.00500 0.04985  150 PHE   A N    
224  C  CA   . PHE   A 45  ? 0.30138 0.19329 0.32283 0.02203  -0.00751 0.03826  150 PHE   A CA   
225  C  C    . PHE   A 45  ? 0.30202 0.19318 0.33075 0.03079  -0.01194 0.04309  150 PHE   A C    
226  O  O    . PHE   A 45  ? 0.31482 0.21627 0.34665 0.03398  -0.01472 0.03605  150 PHE   A O    
227  C  CB   . PHE   A 45  ? 0.26160 0.14853 0.29653 0.01883  -0.00417 0.02619  150 PHE   A CB   
228  C  CG   . PHE   A 45  ? 0.24579 0.14014 0.27353 0.01171  -0.00193 0.01746  150 PHE   A CG   
229  C  CD1  . PHE   A 45  ? 0.26404 0.15949 0.28114 0.00664  -0.00032 0.02323  150 PHE   A CD1  
230  C  CD2  . PHE   A 45  ? 0.28846 0.18961 0.31997 0.01083  -0.00130 0.00372  150 PHE   A CD2  
231  C  CE1  . PHE   A 45  ? 0.29031 0.19291 0.30240 0.00103  0.00109  0.01575  150 PHE   A CE1  
232  C  CE2  . PHE   A 45  ? 0.28032 0.18904 0.30443 0.00526  0.00002  -0.00302 150 PHE   A CE2  
233  C  CZ   . PHE   A 45  ? 0.27814 0.18725 0.29338 0.00047  0.00082  0.00321  150 PHE   A CZ   
234  N  N    . ARG   A 46  ? 0.31970 0.19947 0.35227 0.03496  -0.01241 0.05579  151 ARG   A N    
235  C  CA   . ARG   A 46  ? 0.34834 0.22806 0.38666 0.04445  -0.01774 0.06296  151 ARG   A CA   
236  C  C    . ARG   A 46  ? 0.36071 0.25631 0.38510 0.04758  -0.02403 0.06522  151 ARG   A C    
237  O  O    . ARG   A 46  ? 0.40445 0.30587 0.43576 0.05511  -0.02969 0.06609  151 ARG   A O    
238  C  CB   . ARG   A 46  ? 0.46533 0.32998 0.50649 0.04803  -0.01674 0.07964  151 ARG   A CB   
239  C  CG   . ARG   A 46  ? 0.59136 0.45707 0.61279 0.04410  -0.01463 0.09111  151 ARG   A CG   
240  C  CD   . ARG   A 46  ? 0.78120 0.63563 0.80090 0.04899  -0.01382 0.11101  151 ARG   A CD   
241  N  NE   . ARG   A 46  ? 0.89808 0.76181 0.89351 0.04967  -0.01514 0.12149  151 ARG   A NE   
242  C  CZ   . ARG   A 46  ? 0.94247 0.81044 0.92420 0.04236  -0.01019 0.12060  151 ARG   A CZ   
243  N  NH1  . ARG   A 46  ? 0.91362 0.77775 0.90373 0.03363  -0.00420 0.11072  151 ARG   A NH1  
244  N  NH2  . ARG   A 46  ? 0.98125 0.85837 0.94093 0.04434  -0.01156 0.12900  151 ARG   A NH2  
245  N  N    . ASP   A 47  ? 0.34580 0.24878 0.35292 0.04214  -0.02342 0.06518  152 ASP   A N    
246  C  CA   . ASP   A 47  ? 0.34493 0.26250 0.33936 0.04454  -0.02980 0.06602  152 ASP   A CA   
247  C  C    . ASP   A 47  ? 0.32736 0.25800 0.32812 0.04284  -0.03160 0.05245  152 ASP   A C    
248  O  O    . ASP   A 47  ? 0.32156 0.26411 0.31859 0.04523  -0.03748 0.05148  152 ASP   A O    
249  C  CB   . ASP   A 47  ? 0.38749 0.30751 0.36229 0.03963  -0.02791 0.06988  152 ASP   A CB   
250  C  CG   . ASP   A 47  ? 0.50652 0.41640 0.47271 0.04077  -0.02475 0.08453  152 ASP   A CG   
251  O  OD1  . ASP   A 47  ? 0.51410 0.41567 0.48721 0.04669  -0.02589 0.09449  152 ASP   A OD1  
252  O  OD2  . ASP   A 47  ? 0.57153 0.48229 0.52505 0.03585  -0.02068 0.08610  152 ASP   A OD2  
253  N  N    . PHE   A 48  ? 0.25956 0.18837 0.26898 0.03834  -0.02627 0.04254  153 PHE   A N    
254  C  CA   . PHE   A 48  ? 0.21980 0.16090 0.23442 0.03626  -0.02604 0.03129  153 PHE   A CA   
255  C  C    . PHE   A 48  ? 0.22282 0.17016 0.25334 0.04347  -0.02966 0.02878  153 PHE   A C    
256  O  O    . PHE   A 48  ? 0.26076 0.20023 0.30094 0.04991  -0.03117 0.03361  153 PHE   A O    
257  C  CB   . PHE   A 48  ? 0.21170 0.15008 0.22938 0.03054  -0.01921 0.02212  153 PHE   A CB   
258  C  CG   . PHE   A 48  ? 0.20873 0.14169 0.21428 0.02379  -0.01569 0.02380  153 PHE   A CG   
259  C  CD1  . PHE   A 48  ? 0.24691 0.17508 0.25564 0.01958  -0.01080 0.01742  153 PHE   A CD1  
260  C  CD2  . PHE   A 48  ? 0.24271 0.17668 0.23450 0.02211  -0.01749 0.03075  153 PHE   A CD2  
261  C  CE1  . PHE   A 48  ? 0.28542 0.21031 0.28558 0.01373  -0.00809 0.01870  153 PHE   A CE1  
262  C  CE2  . PHE   A 48  ? 0.24444 0.17463 0.22727 0.01645  -0.01372 0.03191  153 PHE   A CE2  
263  C  CZ   . PHE   A 48  ? 0.26200 0.18784 0.24991 0.01222  -0.00917 0.02626  153 PHE   A CZ   
264  N  N    . ARG   A 49  ? 0.26208 0.22374 0.29727 0.04240  -0.03062 0.02143  154 ARG   A N    
265  C  CA   . ARG   A 49  ? 0.24141 0.21104 0.29490 0.04832  -0.03194 0.01664  154 ARG   A CA   
266  C  C    . ARG   A 49  ? 0.21639 0.17786 0.28058 0.04953  -0.02551 0.01038  154 ARG   A C    
267  O  O    . ARG   A 49  ? 0.24817 0.20472 0.30583 0.04359  -0.01968 0.00563  154 ARG   A O    
268  C  CB   . ARG   A 49  ? 0.20236 0.18901 0.26060 0.04507  -0.03168 0.00937  154 ARG   A CB   
269  C  CG   . ARG   A 49  ? 0.22289 0.21950 0.27769 0.04588  -0.04004 0.01303  154 ARG   A CG   
270  C  CD   . ARG   A 49  ? 0.20988 0.22088 0.27014 0.04023  -0.03854 0.00584  154 ARG   A CD   
271  N  NE   . ARG   A 49  ? 0.19164 0.19832 0.23830 0.03186  -0.03330 0.00450  154 ARG   A NE   
272  C  CZ   . ARG   A 49  ? 0.20542 0.22061 0.25555 0.02584  -0.02954 -0.00037 154 ARG   A CZ   
273  N  NH1  . ARG   A 49  ? 0.19320 0.22233 0.26060 0.02645  -0.02974 -0.00467 154 ARG   A NH1  
274  N  NH2  . ARG   A 49  ? 0.22433 0.23436 0.26226 0.01935  -0.02538 -0.00023 154 ARG   A NH2  
275  N  N    . PRO   A 50  ? 0.25758 0.21777 0.33865 0.05752  -0.02687 0.00951  155 PRO   A N    
276  C  CA   . PRO   A 50  ? 0.30682 0.25601 0.39856 0.05950  -0.02151 0.00333  155 PRO   A CA   
277  C  C    . PRO   A 50  ? 0.26785 0.22590 0.36188 0.05560  -0.01432 -0.01032 155 PRO   A C    
278  O  O    . PRO   A 50  ? 0.25918 0.23351 0.35617 0.05504  -0.01323 -0.01474 155 PRO   A O    
279  C  CB   . PRO   A 50  ? 0.30291 0.25121 0.41409 0.07025  -0.02549 0.00564  155 PRO   A CB   
280  C  CG   . PRO   A 50  ? 0.39424 0.34988 0.50083 0.07379  -0.03416 0.01648  155 PRO   A CG   
281  C  CD   . PRO   A 50  ? 0.25712 0.22537 0.34922 0.06581  -0.03429 0.01421  155 PRO   A CD   
282  N  N    . PRO   A 51  ? 0.26157 0.21018 0.35479 0.05288  -0.00921 -0.01725 156 PRO   A N    
283  C  CA   . PRO   A 51  ? 0.26721 0.22523 0.36251 0.05123  -0.00256 -0.03092 156 PRO   A CA   
284  C  C    . PRO   A 51  ? 0.29919 0.26396 0.41432 0.05965  -0.00096 -0.03826 156 PRO   A C    
285  O  O    . PRO   A 51  ? 0.32967 0.28551 0.45922 0.06693  -0.00436 -0.03513 156 PRO   A O    
286  C  CB   . PRO   A 51  ? 0.29893 0.24402 0.39041 0.04752  0.00035  -0.03681 156 PRO   A CB   
287  C  CG   . PRO   A 51  ? 0.31981 0.24675 0.41731 0.04984  -0.00363 -0.02751 156 PRO   A CG   
288  C  CD   . PRO   A 51  ? 0.27889 0.20869 0.37035 0.05131  -0.00932 -0.01314 156 PRO   A CD   
289  N  N    . VAL   A 52  ? 0.26296 0.24434 0.37939 0.05904  0.00462  -0.04712 157 VAL   A N    
290  C  CA   . VAL   A 52  ? 0.27862 0.26948 0.41419 0.06684  0.00807  -0.05605 157 VAL   A CA   
291  C  C    . VAL   A 52  ? 0.35075 0.34931 0.48215 0.06517  0.01694  -0.07036 157 VAL   A C    
292  O  O    . VAL   A 52  ? 0.38676 0.39717 0.50432 0.05909  0.02122  -0.07095 157 VAL   A O    
293  C  CB   . VAL   A 52  ? 0.32286 0.33144 0.46773 0.06908  0.00642  -0.05176 157 VAL   A CB   
294  C  CG1  . VAL   A 52  ? 0.35838 0.37935 0.52430 0.07698  0.01169  -0.06226 157 VAL   A CG1  
295  C  CG2  . VAL   A 52  ? 0.33792 0.34038 0.48645 0.07225  -0.00368 -0.03898 157 VAL   A CG2  
296  N  N    . ARG   A 53  ? 0.45392 0.44523 0.59680 0.07079  0.01949  -0.08173 158 ARG   A N    
297  C  CA   . ARG   A 53  ? 0.48113 0.48126 0.62199 0.07154  0.02763  -0.09803 158 ARG   A CA   
298  C  C    . ARG   A 53  ? 0.58605 0.58737 0.75075 0.08200  0.03035  -0.10880 158 ARG   A C    
299  O  O    . ARG   A 53  ? 0.56799 0.55776 0.74978 0.08803  0.02492  -0.10328 158 ARG   A O    
300  C  CB   . ARG   A 53  ? 0.44623 0.43394 0.57471 0.06660  0.02740  -0.10506 158 ARG   A CB   
301  C  CG   . ARG   A 53  ? 0.44400 0.41932 0.55829 0.05869  0.02139  -0.09234 158 ARG   A CG   
302  C  CD   . ARG   A 53  ? 0.37393 0.33458 0.48628 0.05570  0.02027  -0.10059 158 ARG   A CD   
303  N  NE   . ARG   A 53  ? 0.40068 0.35483 0.49737 0.04725  0.01667  -0.09131 158 ARG   A NE   
304  C  CZ   . ARG   A 53  ? 0.36236 0.30229 0.46055 0.04508  0.01168  -0.07791 158 ARG   A CZ   
305  N  NH1  . ARG   A 53  ? 0.33009 0.25995 0.44355 0.05087  0.00889  -0.07074 158 ARG   A NH1  
306  N  NH2  . ARG   A 53  ? 0.37032 0.30704 0.45437 0.03758  0.00971  -0.07128 158 ARG   A NH2  
307  N  N    . MET   A 54  ? 0.69566 0.70986 0.85875 0.08383  0.03883  -0.12441 159 MET   A N    
308  C  CA   . MET   A 54  ? 0.81607 0.83395 0.99905 0.09365  0.04414  -0.14055 159 MET   A CA   
309  C  C    . MET   A 54  ? 0.81695 0.85823 0.99092 0.09397  0.05506  -0.15325 159 MET   A C    
310  O  O    . MET   A 54  ? 0.81011 0.86960 0.97931 0.09141  0.05906  -0.14554 159 MET   A O    
311  C  CB   . MET   A 54  ? 0.91031 0.92924 1.11887 0.10234  0.04120  -0.13441 159 MET   A CB   
312  C  CG   . MET   A 54  ? 0.99522 0.98920 1.21713 0.10609  0.03231  -0.12710 159 MET   A CG   
313  S  SD   . MET   A 54  ? 1.08071 1.06460 1.32089 0.11378  0.03388  -0.13852 159 MET   A SD   
314  C  CE   . MET   A 54  ? 1.07451 1.03710 1.33156 0.11909  0.02338  -0.12054 159 MET   A CE   
315  N  N    . SER   A 66  ? 0.60579 0.75017 0.79202 0.06899  0.07244  -0.09211 218 SER   A N    
316  C  CA   . SER   A 66  ? 0.56749 0.69604 0.73988 0.06165  0.06173  -0.08026 218 SER   A CA   
317  C  C    . SER   A 66  ? 0.52487 0.64683 0.66821 0.05449  0.06500  -0.07798 218 SER   A C    
318  O  O    . SER   A 66  ? 0.55733 0.66165 0.68696 0.05436  0.05888  -0.07914 218 SER   A O    
319  C  CB   . SER   A 66  ? 0.60861 0.71761 0.78508 0.06654  0.04948  -0.07941 218 SER   A CB   
320  O  OG   . SER   A 66  ? 0.65783 0.77269 0.86082 0.07485  0.04586  -0.08144 218 SER   A OG   
321  N  N    . PRO   A 67  ? 0.45542 0.59065 0.58985 0.04843  0.07397  -0.07350 219 PRO   A N    
322  C  CA   . PRO   A 67  ? 0.42510 0.55459 0.53209 0.04257  0.07603  -0.06996 219 PRO   A CA   
323  C  C    . PRO   A 67  ? 0.43216 0.54326 0.52758 0.03687  0.06500  -0.06094 219 PRO   A C    
324  O  O    . PRO   A 67  ? 0.41169 0.51591 0.48568 0.03320  0.06481  -0.05904 219 PRO   A O    
325  C  CB   . PRO   A 67  ? 0.42770 0.57587 0.53373 0.03758  0.08752  -0.06325 219 PRO   A CB   
326  C  CG   . PRO   A 67  ? 0.39060 0.54946 0.52482 0.03738  0.08744  -0.05992 219 PRO   A CG   
327  C  CD   . PRO   A 67  ? 0.41508 0.57159 0.56661 0.04658  0.08253  -0.07010 219 PRO   A CD   
328  N  N    . LEU   A 68  ? 0.34117 0.44551 0.44965 0.03646  0.05579  -0.05563 220 LEU   A N    
329  C  CA   . LEU   A 68  ? 0.29645 0.38540 0.39392 0.03129  0.04627  -0.04726 220 LEU   A CA   
330  C  C    . LEU   A 68  ? 0.22546 0.29985 0.32856 0.03594  0.03565  -0.04792 220 LEU   A C    
331  O  O    . LEU   A 68  ? 0.21567 0.28173 0.31656 0.03315  0.02732  -0.04061 220 LEU   A O    
332  C  CB   . LEU   A 68  ? 0.25370 0.34920 0.35781 0.02478  0.04530  -0.03820 220 LEU   A CB   
333  C  CG   . LEU   A 68  ? 0.32899 0.43635 0.42832 0.01894  0.05573  -0.03371 220 LEU   A CG   
334  C  CD1  . LEU   A 68  ? 0.33885 0.44891 0.44838 0.01212  0.05318  -0.02551 220 LEU   A CD1  
335  C  CD2  . LEU   A 68  ? 0.35524 0.45434 0.42930 0.01648  0.05768  -0.03193 220 LEU   A CD2  
336  N  N    . SER   A 69  ? 0.22477 0.29573 0.33499 0.04330  0.03615  -0.05645 221 SER   A N    
337  C  CA   . SER   A 69  ? 0.26551 0.32293 0.38426 0.04861  0.02689  -0.05520 221 SER   A CA   
338  C  C    . SER   A 69  ? 0.24693 0.28552 0.34892 0.04478  0.02019  -0.04936 221 SER   A C    
339  O  O    . SER   A 69  ? 0.25701 0.28534 0.36275 0.04719  0.01202  -0.04341 221 SER   A O    
340  C  CB   . SER   A 69  ? 0.29678 0.35254 0.42827 0.05731  0.02970  -0.06594 221 SER   A CB   
341  O  OG   . SER   A 69  ? 0.32075 0.37219 0.43920 0.05635  0.03517  -0.07473 221 SER   A OG   
342  N  N    . MET   A 70  ? 0.22234 0.25734 0.30618 0.03928  0.02354  -0.05040 222 MET   A N    
343  C  CA   . MET   A 70  ? 0.21644 0.23542 0.28627 0.03541  0.01809  -0.04539 222 MET   A CA   
344  C  C    . MET   A 70  ? 0.22716 0.24649 0.28658 0.02880  0.01501  -0.03554 222 MET   A C    
345  O  O    . MET   A 70  ? 0.24713 0.25479 0.29531 0.02559  0.01097  -0.03089 222 MET   A O    
346  C  CB   . MET   A 70  ? 0.20525 0.22027 0.26286 0.03352  0.02195  -0.05294 222 MET   A CB   
347  C  CG   . MET   A 70  ? 0.24933 0.25721 0.31688 0.03948  0.02259  -0.06365 222 MET   A CG   
348  S  SD   . MET   A 70  ? 0.27158 0.25791 0.34819 0.04210  0.01445  -0.05780 222 MET   A SD   
349  C  CE   . MET   A 70  ? 0.28021 0.25557 0.33879 0.03400  0.01211  -0.05396 222 MET   A CE   
350  N  N    . LEU   A 71  ? 0.17822 0.21067 0.24275 0.02657  0.01727  -0.03282 223 LEU   A N    
351  C  CA   . LEU   A 71  ? 0.22799 0.25996 0.28456 0.02020  0.01459  -0.02505 223 LEU   A CA   
352  C  C    . LEU   A 71  ? 0.20657 0.22873 0.26210 0.02074  0.00525  -0.01931 223 LEU   A C    
353  O  O    . LEU   A 71  ? 0.22668 0.24095 0.26908 0.01643  0.00284  -0.01481 223 LEU   A O    
354  C  CB   . LEU   A 71  ? 0.21483 0.26238 0.28179 0.01747  0.01899  -0.02381 223 LEU   A CB   
355  C  CG   . LEU   A 71  ? 0.20448 0.25182 0.26707 0.01057  0.01706  -0.01714 223 LEU   A CG   
356  C  CD1  . LEU   A 71  ? 0.19582 0.23490 0.23923 0.00628  0.01925  -0.01407 223 LEU   A CD1  
357  C  CD2  . LEU   A 71  ? 0.20333 0.26587 0.28035 0.00745  0.02270  -0.01629 223 LEU   A CD2  
358  N  N    . PRO   A 72  ? 0.19000 0.21306 0.25800 0.02635  -0.00023 -0.01883 224 PRO   A N    
359  C  CA   . PRO   A 72  ? 0.19867 0.21368 0.26179 0.02726  -0.00912 -0.01229 224 PRO   A CA   
360  C  C    . PRO   A 72  ? 0.21874 0.21753 0.26806 0.02685  -0.01020 -0.00903 224 PRO   A C    
361  O  O    . PRO   A 72  ? 0.19541 0.18856 0.23254 0.02342  -0.01334 -0.00386 224 PRO   A O    
362  C  CB   . PRO   A 72  ? 0.19114 0.21131 0.27092 0.03503  -0.01431 -0.01241 224 PRO   A CB   
363  C  CG   . PRO   A 72  ? 0.19835 0.23440 0.29428 0.03556  -0.00848 -0.01879 224 PRO   A CG   
364  C  CD   . PRO   A 72  ? 0.17518 0.20938 0.26260 0.03220  0.00115  -0.02345 224 PRO   A CD   
365  N  N    . HIS   A 73  ? 0.21502 0.20657 0.26750 0.03011  -0.00725 -0.01273 225 HIS   A N    
366  C  CA   . HIS   A 73  ? 0.21947 0.19587 0.26275 0.02895  -0.00775 -0.01005 225 HIS   A CA   
367  C  C    . HIS   A 73  ? 0.18872 0.16396 0.21755 0.02173  -0.00444 -0.01063 225 HIS   A C    
368  O  O    . HIS   A 73  ? 0.20153 0.16887 0.22031 0.01880  -0.00654 -0.00505 225 HIS   A O    
369  C  CB   . HIS   A 73  ? 0.21566 0.18492 0.26903 0.03341  -0.00513 -0.01613 225 HIS   A CB   
370  C  CG   . HIS   A 73  ? 0.22802 0.18161 0.27646 0.03154  -0.00525 -0.01407 225 HIS   A CG   
371  N  ND1  . HIS   A 73  ? 0.23835 0.18021 0.28754 0.03391  -0.00936 -0.00458 225 HIS   A ND1  
372  C  CD2  . HIS   A 73  ? 0.25216 0.20091 0.29604 0.02743  -0.00168 -0.02010 225 HIS   A CD2  
373  C  CE1  . HIS   A 73  ? 0.29230 0.22210 0.33933 0.03070  -0.00740 -0.00452 225 HIS   A CE1  
374  N  NE2  . HIS   A 73  ? 0.24506 0.17908 0.28956 0.02666  -0.00334 -0.01467 225 HIS   A NE2  
375  N  N    . LEU   A 74  ? 0.18421 0.16820 0.21182 0.01933  0.00098  -0.01679 226 LEU   A N    
376  C  CA   . LEU   A 74  ? 0.18427 0.16755 0.19864 0.01360  0.00346  -0.01671 226 LEU   A CA   
377  C  C    . LEU   A 74  ? 0.18241 0.16822 0.18976 0.00943  0.00154  -0.01015 226 LEU   A C    
378  O  O    . LEU   A 74  ? 0.20089 0.18192 0.19796 0.00567  0.00129  -0.00745 226 LEU   A O    
379  C  CB   . LEU   A 74  ? 0.18981 0.18257 0.20275 0.01311  0.00960  -0.02398 226 LEU   A CB   
380  C  CG   . LEU   A 74  ? 0.24711 0.23593 0.26415 0.01640  0.01129  -0.03319 226 LEU   A CG   
381  C  CD1  . LEU   A 74  ? 0.27477 0.27550 0.28762 0.01672  0.01737  -0.04135 226 LEU   A CD1  
382  C  CD2  . LEU   A 74  ? 0.21468 0.19056 0.22696 0.01402  0.00831  -0.03283 226 LEU   A CD2  
383  N  N    . ALA   A 75  ? 0.16701 0.16050 0.18158 0.01011  -0.00010 -0.00839 227 ALA   A N    
384  C  CA   . ALA   A 75  ? 0.19637 0.19064 0.20633 0.00643  -0.00306 -0.00377 227 ALA   A CA   
385  C  C    . ALA   A 75  ? 0.17576 0.16007 0.17769 0.00712  -0.00829 0.00073  227 ALA   A C    
386  O  O    . ALA   A 75  ? 0.18927 0.17034 0.18193 0.00360  -0.00886 0.00329  227 ALA   A O    
387  C  CB   . ALA   A 75  ? 0.21333 0.21817 0.23570 0.00702  -0.00502 -0.00431 227 ALA   A CB   
388  N  N    . ASP   A 76  ? 0.18023 0.15986 0.18599 0.01208  -0.01164 0.00231  228 ASP   A N    
389  C  CA   . ASP   A 76  ? 0.17541 0.14616 0.17261 0.01316  -0.01547 0.00838  228 ASP   A CA   
390  C  C    . ASP   A 76  ? 0.20846 0.17006 0.19754 0.00992  -0.01178 0.00935  228 ASP   A C    
391  O  O    . ASP   A 76  ? 0.20496 0.16252 0.18429 0.00777  -0.01243 0.01352  228 ASP   A O    
392  C  CB   . ASP   A 76  ? 0.21264 0.18007 0.21678 0.01982  -0.01942 0.01178  228 ASP   A CB   
393  C  CG   . ASP   A 76  ? 0.23198 0.20941 0.24227 0.02347  -0.02559 0.01234  228 ASP   A CG   
394  O  OD1  . ASP   A 76  ? 0.23916 0.21626 0.25743 0.02996  -0.02939 0.01500  228 ASP   A OD1  
395  O  OD2  . ASP   A 76  ? 0.22531 0.21094 0.23397 0.01995  -0.02699 0.00993  228 ASP   A OD2  
396  N  N    . LEU   A 77  ? 0.20458 0.16416 0.19833 0.00961  -0.00792 0.00451  229 LEU   A N    
397  C  CA   . LEU   A 77  ? 0.19633 0.14940 0.18490 0.00608  -0.00519 0.00374  229 LEU   A CA   
398  C  C    . LEU   A 77  ? 0.22847 0.18598 0.20786 0.00136  -0.00381 0.00392  229 LEU   A C    
399  O  O    . LEU   A 77  ? 0.22158 0.17456 0.19479 -0.00123 -0.00351 0.00694  229 LEU   A O    
400  C  CB   . LEU   A 77  ? 0.21444 0.16700 0.21019 0.00687  -0.00229 -0.00415 229 LEU   A CB   
401  C  CG   . LEU   A 77  ? 0.23624 0.18535 0.22848 0.00287  -0.00035 -0.00762 229 LEU   A CG   
402  C  CD1  . LEU   A 77  ? 0.24122 0.17943 0.23366 0.00140  -0.00120 -0.00145 229 LEU   A CD1  
403  C  CD2  . LEU   A 77  ? 0.25767 0.20770 0.25703 0.00429  0.00157  -0.01775 229 LEU   A CD2  
404  N  N    . VAL   A 78  ? 0.20289 0.16938 0.18277 0.00038  -0.00241 0.00129  230 VAL   A N    
405  C  CA   . VAL   A 78  ? 0.20290 0.17263 0.17590 -0.00346 -0.00103 0.00260  230 VAL   A CA   
406  C  C    . VAL   A 78  ? 0.19485 0.16194 0.16335 -0.00442 -0.00385 0.00702  230 VAL   A C    
407  O  O    . VAL   A 78  ? 0.21714 0.18174 0.17948 -0.00675 -0.00321 0.00876  230 VAL   A O    
408  C  CB   . VAL   A 78  ? 0.18123 0.16050 0.15726 -0.00422 0.00189  0.00077  230 VAL   A CB   
409  C  CG1  . VAL   A 78  ? 0.20884 0.18967 0.18018 -0.00770 0.00279  0.00424  230 VAL   A CG1  
410  C  CG2  . VAL   A 78  ? 0.20387 0.18730 0.17992 -0.00323 0.00548  -0.00429 230 VAL   A CG2  
411  N  N    . SER   A 79  ? 0.21347 0.18234 0.18530 -0.00219 -0.00729 0.00804  231 SER   A N    
412  C  CA   . SER   A 79  ? 0.18428 0.15211 0.15049 -0.00248 -0.01061 0.01041  231 SER   A CA   
413  C  C    . SER   A 79  ? 0.21598 0.17647 0.17368 -0.00202 -0.01037 0.01430  231 SER   A C    
414  O  O    . SER   A 79  ? 0.21928 0.17861 0.17009 -0.00377 -0.00979 0.01520  231 SER   A O    
415  C  CB   . SER   A 79  ? 0.22168 0.19427 0.19281 0.00071  -0.01573 0.01009  231 SER   A CB   
416  O  OG   . SER   A 79  ? 0.24408 0.21920 0.21132 -0.00036 -0.01916 0.00911  231 SER   A OG   
417  N  N    . TYR   A 80  ? 0.19007 0.14557 0.14972 0.00051  -0.01033 0.01682  232 TYR   A N    
418  C  CA   . TYR   A 80  ? 0.22396 0.17213 0.17847 0.00026  -0.00856 0.02166  232 TYR   A CA   
419  C  C    . TYR   A 80  ? 0.23105 0.17829 0.18382 -0.00403 -0.00469 0.01988  232 TYR   A C    
420  O  O    . TYR   A 80  ? 0.22737 0.17288 0.17421 -0.00533 -0.00304 0.02294  232 TYR   A O    
421  C  CB   . TYR   A 80  ? 0.20119 0.14299 0.16310 0.00295  -0.00830 0.02379  232 TYR   A CB   
422  C  CG   . TYR   A 80  ? 0.26871 0.20170 0.23023 0.00185  -0.00527 0.02919  232 TYR   A CG   
423  C  CD1  . TYR   A 80  ? 0.30603 0.23503 0.26175 0.00455  -0.00584 0.03814  232 TYR   A CD1  
424  C  CD2  . TYR   A 80  ? 0.29871 0.22815 0.26665 -0.00179 -0.00188 0.02545  232 TYR   A CD2  
425  C  CE1  . TYR   A 80  ? 0.36530 0.28619 0.32253 0.00311  -0.00179 0.04463  232 TYR   A CE1  
426  C  CE2  . TYR   A 80  ? 0.32358 0.24516 0.29500 -0.00366 0.00121  0.03019  232 TYR   A CE2  
427  C  CZ   . TYR   A 80  ? 0.37569 0.29256 0.34231 -0.00142 0.00188  0.04045  232 TYR   A CZ   
428  O  OH   . TYR   A 80  ? 0.54677 0.45585 0.51820 -0.00375 0.00627  0.04678  232 TYR   A OH   
429  N  N    . SER   A 81  ? 0.19681 0.14675 0.15454 -0.00575 -0.00327 0.01486  233 SER   A N    
430  C  CA   . SER   A 81  ? 0.21716 0.16793 0.17392 -0.00903 -0.00089 0.01300  233 SER   A CA   
431  C  C    . SER   A 81  ? 0.24209 0.19647 0.19350 -0.01044 -0.00070 0.01382  233 SER   A C    
432  O  O    . SER   A 81  ? 0.23800 0.19206 0.18772 -0.01216 0.00087  0.01466  233 SER   A O    
433  C  CB   . SER   A 81  ? 0.21626 0.17082 0.17737 -0.00947 -0.00014 0.00727  233 SER   A CB   
434  O  OG   . SER   A 81  ? 0.23113 0.18145 0.19903 -0.00793 -0.00015 0.00469  233 SER   A OG   
435  N  N    . ILE   A 82  ? 0.17729 0.13522 0.12834 -0.00978 -0.00217 0.01311  234 ILE   A N    
436  C  CA   . ILE   A 82  ? 0.18126 0.14069 0.12957 -0.01093 -0.00213 0.01331  234 ILE   A CA   
437  C  C    . ILE   A 82  ? 0.22595 0.18249 0.16832 -0.01024 -0.00218 0.01511  234 ILE   A C    
438  O  O    . ILE   A 82  ? 0.21693 0.17340 0.15744 -0.01115 -0.00039 0.01510  234 ILE   A O    
439  C  CB   . ILE   A 82  ? 0.20036 0.16336 0.15254 -0.01092 -0.00387 0.01168  234 ILE   A CB   
440  C  CG1  . ILE   A 82  ? 0.21978 0.18714 0.17721 -0.01190 -0.00176 0.01107  234 ILE   A CG1  
441  C  CG2  . ILE   A 82  ? 0.22352 0.18597 0.17485 -0.01201 -0.00431 0.01075  234 ILE   A CG2  
442  C  CD1  . ILE   A 82  ? 0.21432 0.18619 0.17914 -0.01239 -0.00247 0.00996  234 ILE   A CD1  
443  N  N    . GLN   A 83  ? 0.20910 0.16404 0.14823 -0.00799 -0.00396 0.01710  235 GLN   A N    
444  C  CA   . GLN   A 83  ? 0.22704 0.18055 0.15807 -0.00679 -0.00309 0.01985  235 GLN   A CA   
445  C  C    . GLN   A 83  ? 0.21541 0.16657 0.14700 -0.00866 0.00154  0.02241  235 GLN   A C    
446  O  O    . GLN   A 83  ? 0.21473 0.16712 0.14208 -0.00884 0.00410  0.02270  235 GLN   A O    
447  C  CB   . GLN   A 83  ? 0.25991 0.21230 0.18665 -0.00338 -0.00565 0.02386  235 GLN   A CB   
448  C  CG   . GLN   A 83  ? 0.25910 0.21617 0.18573 -0.00111 -0.01128 0.02079  235 GLN   A CG   
449  C  CD   . GLN   A 83  ? 0.33257 0.28989 0.25348 0.00345  -0.01477 0.02576  235 GLN   A CD   
450  O  OE1  . GLN   A 83  ? 0.35568 0.31200 0.26608 0.00530  -0.01338 0.03063  235 GLN   A OE1  
451  N  NE2  . GLN   A 83  ? 0.30759 0.26705 0.23561 0.00576  -0.01899 0.02528  235 GLN   A NE2  
452  N  N    . LYS   A 84  ? 0.21742 0.16597 0.15569 -0.01005 0.00270  0.02327  236 LYS   A N    
453  C  CA   . LYS   A 84  ? 0.22590 0.17323 0.16805 -0.01255 0.00652  0.02477  236 LYS   A CA   
454  C  C    . LYS   A 84  ? 0.20004 0.15209 0.14437 -0.01423 0.00729  0.02129  236 LYS   A C    
455  O  O    . LYS   A 84  ? 0.23071 0.18449 0.17610 -0.01527 0.01044  0.02244  236 LYS   A O    
456  C  CB   . LYS   A 84  ? 0.23709 0.18067 0.18810 -0.01391 0.00660  0.02412  236 LYS   A CB   
457  C  CG   . LYS   A 84  ? 0.25530 0.19274 0.20702 -0.01155 0.00590  0.02839  236 LYS   A CG   
458  C  CD   . LYS   A 84  ? 0.25086 0.18546 0.19657 -0.01054 0.00882  0.03660  236 LYS   A CD   
459  C  CE   . LYS   A 84  ? 0.36663 0.29354 0.31571 -0.00828 0.00881  0.04307  236 LYS   A CE   
460  N  NZ   . LYS   A 84  ? 0.38259 0.30306 0.34597 -0.01162 0.01138  0.04218  236 LYS   A NZ   
461  N  N    . VAL   A 85  ? 0.18933 0.14411 0.13508 -0.01414 0.00483  0.01785  237 VAL   A N    
462  C  CA   . VAL   A 85  ? 0.20964 0.16861 0.15767 -0.01484 0.00505  0.01621  237 VAL   A CA   
463  C  C    . VAL   A 85  ? 0.17827 0.13760 0.12330 -0.01366 0.00633  0.01655  237 VAL   A C    
464  O  O    . VAL   A 85  ? 0.21426 0.17621 0.16236 -0.01370 0.00802  0.01642  237 VAL   A O    
465  C  CB   . VAL   A 85  ? 0.22611 0.18783 0.17504 -0.01458 0.00299  0.01454  237 VAL   A CB   
466  C  CG1  . VAL   A 85  ? 0.20044 0.16574 0.15076 -0.01425 0.00298  0.01519  237 VAL   A CG1  
467  C  CG2  . VAL   A 85  ? 0.23766 0.20085 0.18932 -0.01527 0.00221  0.01211  237 VAL   A CG2  
468  N  N    . ILE   A 86  ? 0.18420 0.14168 0.12420 -0.01224 0.00519  0.01594  238 ILE   A N    
469  C  CA   . ILE   A 86  ? 0.20214 0.15999 0.13894 -0.01079 0.00626  0.01404  238 ILE   A CA   
470  C  C    . ILE   A 86  ? 0.21928 0.17828 0.15280 -0.01032 0.01038  0.01594  238 ILE   A C    
471  O  O    . ILE   A 86  ? 0.23426 0.19555 0.16917 -0.00946 0.01315  0.01428  238 ILE   A O    
472  C  CB   . ILE   A 86  ? 0.23271 0.18978 0.16490 -0.00947 0.00315  0.01137  238 ILE   A CB   
473  C  CG1  . ILE   A 86  ? 0.22500 0.18191 0.16365 -0.01065 0.00037  0.00975  238 ILE   A CG1  
474  C  CG2  . ILE   A 86  ? 0.23604 0.19396 0.16397 -0.00766 0.00409  0.00724  238 ILE   A CG2  
475  C  CD1  . ILE   A 86  ? 0.20559 0.16347 0.14303 -0.00998 -0.00357 0.00711  238 ILE   A CD1  
476  N  N    . GLY   A 87  ? 0.22341 0.18090 0.15373 -0.01066 0.01146  0.01996  239 GLY   A N    
477  C  CA   . GLY   A 87  ? 0.23842 0.19720 0.16639 -0.01070 0.01674  0.02365  239 GLY   A CA   
478  C  C    . GLY   A 87  ? 0.21350 0.17531 0.15195 -0.01310 0.02003  0.02366  239 GLY   A C    
479  O  O    . GLY   A 87  ? 0.24381 0.20946 0.18305 -0.01285 0.02509  0.02449  239 GLY   A O    
480  N  N    . PHE   A 88  ? 0.20477 0.16641 0.15158 -0.01515 0.01715  0.02225  240 PHE   A N    
481  C  CA   . PHE   A 88  ? 0.19910 0.16567 0.15663 -0.01708 0.01836  0.02105  240 PHE   A CA   
482  C  C    . PHE   A 88  ? 0.20604 0.17698 0.16533 -0.01480 0.01811  0.01834  240 PHE   A C    
483  O  O    . PHE   A 88  ? 0.19853 0.17471 0.16421 -0.01461 0.02153  0.01813  240 PHE   A O    
484  C  CB   . PHE   A 88  ? 0.19973 0.16636 0.16342 -0.01908 0.01427  0.01889  240 PHE   A CB   
485  C  CG   . PHE   A 88  ? 0.19582 0.16957 0.17015 -0.02059 0.01332  0.01637  240 PHE   A CG   
486  C  CD1  . PHE   A 88  ? 0.18820 0.16456 0.17315 -0.02385 0.01619  0.01667  240 PHE   A CD1  
487  C  CD2  . PHE   A 88  ? 0.19059 0.16908 0.16537 -0.01872 0.00936  0.01424  240 PHE   A CD2  
488  C  CE1  . PHE   A 88  ? 0.20254 0.18741 0.19914 -0.02526 0.01416  0.01327  240 PHE   A CE1  
489  C  CE2  . PHE   A 88  ? 0.19807 0.18481 0.18206 -0.01926 0.00713  0.01206  240 PHE   A CE2  
490  C  CZ   . PHE   A 88  ? 0.20268 0.19329 0.19800 -0.02254 0.00903  0.01076  240 PHE   A CZ   
491  N  N    . ALA   A 89  ? 0.19746 0.16619 0.15301 -0.01296 0.01451  0.01653  241 ALA   A N    
492  C  CA   . ALA   A 89  ? 0.19237 0.16316 0.15179 -0.01053 0.01402  0.01477  241 ALA   A CA   
493  C  C    . ALA   A 89  ? 0.18414 0.15610 0.14245 -0.00831 0.01842  0.01280  241 ALA   A C    
494  O  O    . ALA   A 89  ? 0.20708 0.18309 0.17305 -0.00638 0.02009  0.01158  241 ALA   A O    
495  C  CB   . ALA   A 89  ? 0.19818 0.16479 0.15491 -0.00963 0.01052  0.01417  241 ALA   A CB   
496  N  N    . LYS   A 90  ? 0.20791 0.17750 0.15651 -0.00787 0.02030  0.01219  242 LYS   A N    
497  C  CA   . LYS   A 90  ? 0.24936 0.22129 0.19430 -0.00507 0.02463  0.00890  242 LYS   A CA   
498  C  C    . LYS   A 90  ? 0.21374 0.19243 0.16449 -0.00530 0.03097  0.01081  242 LYS   A C    
499  O  O    . LYS   A 90  ? 0.25394 0.23664 0.20485 -0.00240 0.03554  0.00734  242 LYS   A O    
500  C  CB   . LYS   A 90  ? 0.29159 0.26161 0.22256 -0.00406 0.02451  0.00806  242 LYS   A CB   
501  C  CG   . LYS   A 90  ? 0.29922 0.27061 0.22386 -0.00536 0.02807  0.01443  242 LYS   A CG   
502  C  CD   . LYS   A 90  ? 0.37653 0.34609 0.28687 -0.00360 0.02556  0.01512  242 LYS   A CD   
503  C  CE   . LYS   A 90  ? 0.46193 0.43432 0.36346 0.00012  0.02526  0.00750  242 LYS   A CE   
504  N  NZ   . LYS   A 90  ? 0.53552 0.50849 0.42262 0.00234  0.02139  0.00746  242 LYS   A NZ   
505  N  N    A MET   A 91  ? 0.18806 0.16862 0.14513 -0.00878 0.03164  0.01539  243 MET   A N    
506  N  N    B MET   A 91  ? 0.19192 0.17259 0.14923 -0.00874 0.03163  0.01531  243 MET   A N    
507  C  CA   A MET   A 91  ? 0.19388 0.18183 0.16086 -0.01018 0.03757  0.01731  243 MET   A CA   
508  C  CA   B MET   A 91  ? 0.19664 0.18477 0.16356 -0.00995 0.03772  0.01709  243 MET   A CA   
509  C  C    A MET   A 91  ? 0.20401 0.19808 0.18648 -0.00982 0.03534  0.01511  243 MET   A C    
510  C  C    B MET   A 91  ? 0.20100 0.19507 0.18375 -0.01009 0.03521  0.01530  243 MET   A C    
511  O  O    A MET   A 91  ? 0.20186 0.20422 0.19551 -0.01030 0.04011  0.01531  243 MET   A O    
512  O  O    B MET   A 91  ? 0.21151 0.21369 0.20595 -0.01118 0.03960  0.01588  243 MET   A O    
513  C  CB   A MET   A 91  ? 0.21296 0.19951 0.18202 -0.01473 0.03947  0.02292  243 MET   A CB   
514  C  CB   B MET   A 91  ? 0.22688 0.21380 0.19400 -0.01414 0.04073  0.02304  243 MET   A CB   
515  C  CG   A MET   A 91  ? 0.26113 0.24146 0.21561 -0.01442 0.04067  0.02714  243 MET   A CG   
516  C  CG   B MET   A 91  ? 0.26487 0.24894 0.21674 -0.01277 0.04499  0.02686  243 MET   A CG   
517  S  SD   A MET   A 91  ? 0.29820 0.28276 0.23860 -0.01022 0.04783  0.02735  243 MET   A SD   
518  S  SD   B MET   A 91  ? 0.32407 0.30394 0.27722 -0.01705 0.04857  0.03627  243 MET   A SD   
519  C  CE   A MET   A 91  ? 0.27817 0.27182 0.23117 -0.01274 0.05843  0.03170  243 MET   A CE   
520  C  CE   B MET   A 91  ? 0.30859 0.27932 0.26069 -0.01799 0.03890  0.03483  243 MET   A CE   
521  N  N    . ILE   A 92  ? 0.17665 0.16801 0.16048 -0.00880 0.02839  0.01372  244 ILE   A N    
522  C  CA   . ILE   A 92  ? 0.20405 0.20223 0.20111 -0.00741 0.02520  0.01288  244 ILE   A CA   
523  C  C    . ILE   A 92  ? 0.17169 0.17461 0.17572 -0.00296 0.02931  0.01034  244 ILE   A C    
524  O  O    . ILE   A 92  ? 0.20469 0.20208 0.20242 0.00042  0.03021  0.00773  244 ILE   A O    
525  C  CB   . ILE   A 92  ? 0.19464 0.18884 0.18884 -0.00602 0.01799  0.01351  244 ILE   A CB   
526  C  CG1  . ILE   A 92  ? 0.18126 0.17278 0.17001 -0.00976 0.01428  0.01467  244 ILE   A CG1  
527  C  CG2  . ILE   A 92  ? 0.21227 0.21423 0.21839 -0.00297 0.01432  0.01400  244 ILE   A CG2  
528  C  CD1  . ILE   A 92  ? 0.19222 0.18028 0.17569 -0.00825 0.00910  0.01591  244 ILE   A CD1  
529  N  N    . PRO   A 93  ? 0.21209 0.22568 0.23087 -0.00266 0.03189  0.00996  245 PRO   A N    
530  C  CA   . PRO   A 93  ? 0.22771 0.24669 0.25496 0.00245  0.03636  0.00685  245 PRO   A CA   
531  C  C    . PRO   A 93  ? 0.24565 0.25857 0.27298 0.00791  0.03185  0.00525  245 PRO   A C    
532  O  O    . PRO   A 93  ? 0.21574 0.22829 0.24728 0.00896  0.02481  0.00809  245 PRO   A O    
533  C  CB   . PRO   A 93  ? 0.19608 0.22871 0.24279 0.00173  0.03655  0.00727  245 PRO   A CB   
534  C  CG   . PRO   A 93  ? 0.21747 0.25117 0.26384 -0.00536 0.03662  0.00977  245 PRO   A CG   
535  C  CD   . PRO   A 93  ? 0.17519 0.19697 0.20550 -0.00711 0.03100  0.01130  245 PRO   A CD   
536  N  N    . GLY   A 94  ? 0.21594 0.22386 0.23820 0.01137  0.03598  0.00074  246 GLY   A N    
537  C  CA   . GLY   A 94  ? 0.19563 0.19600 0.22075 0.01622  0.03286  -0.00155 246 GLY   A CA   
538  C  C    . GLY   A 94  ? 0.19182 0.17991 0.20467 0.01431  0.02871  -0.00126 246 GLY   A C    
539  O  O    . GLY   A 94  ? 0.20417 0.18448 0.21918 0.01753  0.02797  -0.00485 246 GLY   A O    
540  N  N    . PHE   A 95  ? 0.20473 0.19093 0.20709 0.00918  0.02609  0.00245  247 PHE   A N    
541  C  CA   . PHE   A 95  ? 0.21129 0.18771 0.20502 0.00744  0.02198  0.00310  247 PHE   A CA   
542  C  C    . PHE   A 95  ? 0.25007 0.22055 0.23715 0.00867  0.02420  -0.00396 247 PHE   A C    
543  O  O    . PHE   A 95  ? 0.21277 0.17526 0.20211 0.00953  0.02148  -0.00610 247 PHE   A O    
544  C  CB   . PHE   A 95  ? 0.17567 0.15220 0.16014 0.00244  0.01970  0.00696  247 PHE   A CB   
545  C  CG   . PHE   A 95  ? 0.18353 0.15223 0.16118 0.00069  0.01590  0.00776  247 PHE   A CG   
546  C  CD1  . PHE   A 95  ? 0.23535 0.20230 0.21646 0.00056  0.01189  0.01234  247 PHE   A CD1  
547  C  CD2  . PHE   A 95  ? 0.18381 0.14839 0.15192 -0.00052 0.01646  0.00418  247 PHE   A CD2  
548  C  CE1  . PHE   A 95  ? 0.24017 0.20126 0.21699 -0.00136 0.00965  0.01343  247 PHE   A CE1  
549  C  CE2  . PHE   A 95  ? 0.23906 0.19811 0.20396 -0.00231 0.01289  0.00442  247 PHE   A CE2  
550  C  CZ   . PHE   A 95  ? 0.21715 0.17441 0.18722 -0.00302 0.01010  0.00906  247 PHE   A CZ   
551  N  N    . ARG   A 96  ? 0.21391 0.18877 0.19312 0.00875  0.02916  -0.00774 248 ARG   A N    
552  C  CA   . ARG   A 96  ? 0.25441 0.22573 0.22447 0.01026  0.03027  -0.01562 248 ARG   A CA   
553  C  C    . ARG   A 96  ? 0.25217 0.22175 0.23157 0.01533  0.03243  -0.02394 248 ARG   A C    
554  O  O    . ARG   A 96  ? 0.28009 0.24633 0.25398 0.01689  0.03236  -0.03292 248 ARG   A O    
555  C  CB   . ARG   A 96  ? 0.33171 0.30940 0.28797 0.00964  0.03517  -0.01594 248 ARG   A CB   
556  C  CG   . ARG   A 96  ? 0.42603 0.41326 0.38757 0.01150  0.04285  -0.01527 248 ARG   A CG   
557  C  CD   . ARG   A 96  ? 0.59338 0.58673 0.54037 0.01095  0.04900  -0.01375 248 ARG   A CD   
558  N  NE   . ARG   A 96  ? 0.70994 0.71347 0.66288 0.01324  0.05806  -0.01458 248 ARG   A NE   
559  C  CZ   . ARG   A 96  ? 0.82244 0.83049 0.77348 0.01837  0.06334  -0.02339 248 ARG   A CZ   
560  N  NH1  . ARG   A 96  ? 0.85156 0.85394 0.79520 0.02139  0.05959  -0.03293 248 ARG   A NH1  
561  N  NH2  . ARG   A 96  ? 0.83581 0.85469 0.79378 0.02040  0.07257  -0.02361 248 ARG   A NH2  
562  N  N    . ASP   A 97  ? 0.21640 0.18852 0.21073 0.01830  0.03377  -0.02188 249 ASP   A N    
563  C  CA   . ASP   A 97  ? 0.23420 0.20365 0.24099 0.02398  0.03571  -0.02922 249 ASP   A CA   
564  C  C    . ASP   A 97  ? 0.23619 0.19382 0.25369 0.02464  0.03024  -0.02787 249 ASP   A C    
565  O  O    . ASP   A 97  ? 0.26259 0.21449 0.29164 0.02913  0.03123  -0.03463 249 ASP   A O    
566  C  CB   . ASP   A 97  ? 0.23710 0.21621 0.25720 0.02777  0.03984  -0.02709 249 ASP   A CB   
567  C  CG   . ASP   A 97  ? 0.31249 0.30372 0.32524 0.02704  0.04724  -0.02838 249 ASP   A CG   
568  O  OD1  . ASP   A 97  ? 0.29982 0.29157 0.29774 0.02666  0.05074  -0.03417 249 ASP   A OD1  
569  O  OD2  . ASP   A 97  ? 0.31573 0.31669 0.33793 0.02682  0.04953  -0.02327 249 ASP   A OD2  
570  N  N    . LEU   A 98  ? 0.20885 0.16271 0.22366 0.02043  0.02520  -0.01916 250 LEU   A N    
571  C  CA   . LEU   A 98  ? 0.21504 0.15771 0.23810 0.01996  0.02114  -0.01657 250 LEU   A CA   
572  C  C    . LEU   A 98  ? 0.24786 0.18307 0.26698 0.01798  0.02031  -0.02635 250 LEU   A C    
573  O  O    . LEU   A 98  ? 0.27445 0.21424 0.28022 0.01656  0.02139  -0.03305 250 LEU   A O    
574  C  CB   . LEU   A 98  ? 0.19737 0.14044 0.21628 0.01594  0.01714  -0.00516 250 LEU   A CB   
575  C  CG   . LEU   A 98  ? 0.20507 0.15700 0.22701 0.01752  0.01624  0.00337  250 LEU   A CG   
576  C  CD1  . LEU   A 98  ? 0.22657 0.18013 0.24037 0.01326  0.01256  0.01161  250 LEU   A CD1  
577  C  CD2  . LEU   A 98  ? 0.20816 0.15735 0.24635 0.02341  0.01547  0.00714  250 LEU   A CD2  
578  N  N    . THR   A 99  ? 0.23113 0.15515 0.26279 0.01792  0.01813  -0.02686 251 THR   A N    
579  C  CA   . THR   A 99  ? 0.24959 0.16732 0.28019 0.01493  0.01614  -0.03670 251 THR   A CA   
580  C  C    . THR   A 99  ? 0.27232 0.19404 0.28919 0.00919  0.01311  -0.03264 251 THR   A C    
581  O  O    . THR   A 99  ? 0.24227 0.16737 0.25501 0.00711  0.01234  -0.02122 251 THR   A O    
582  C  CB   . THR   A 99  ? 0.29986 0.20399 0.35006 0.01470  0.01471  -0.03671 251 THR   A CB   
583  O  OG1  . THR   A 99  ? 0.26962 0.17101 0.32312 0.01154  0.01305  -0.02192 251 THR   A OG1  
584  C  CG2  . THR   A 99  ? 0.24472 0.14376 0.31097 0.02144  0.01758  -0.03970 251 THR   A CG2  
585  N  N    A SER   A 100 ? 0.25308 0.17529 0.26307 0.00714  0.01095  -0.04289 252 SER   A N    
586  N  N    B SER   A 100 ? 0.25374 0.17600 0.26368 0.00721  0.01100  -0.04303 252 SER   A N    
587  C  CA   A SER   A 100 ? 0.26439 0.19097 0.26299 0.00259  0.00768  -0.03930 252 SER   A CA   
588  C  CA   B SER   A 100 ? 0.26906 0.19537 0.26801 0.00259  0.00757  -0.03998 252 SER   A CA   
589  C  C    A SER   A 100 ? 0.25824 0.17923 0.26716 -0.00163 0.00559  -0.03056 252 SER   A C    
590  C  C    B SER   A 100 ? 0.25998 0.18095 0.26897 -0.00152 0.00569  -0.03046 252 SER   A C    
591  O  O    A SER   A 100 ? 0.27595 0.20142 0.27744 -0.00436 0.00452  -0.02272 252 SER   A O    
592  O  O    B SER   A 100 ? 0.25999 0.18555 0.26145 -0.00406 0.00481  -0.02215 252 SER   A O    
593  C  CB   A SER   A 100 ? 0.27537 0.20487 0.26568 0.00200  0.00453  -0.05209 252 SER   A CB   
594  C  CB   B SER   A 100 ? 0.26531 0.19331 0.25844 0.00183  0.00418  -0.05341 252 SER   A CB   
595  O  OG   A SER   A 100 ? 0.31176 0.23402 0.31562 0.00235  0.00301  -0.06394 252 SER   A OG   
596  O  OG   B SER   A 100 ? 0.29558 0.22994 0.27683 0.00619  0.00672  -0.06187 252 SER   A OG   
597  N  N    . ASP   A 101 ? 0.25684 0.16801 0.28360 -0.00199 0.00575  -0.03131 253 ASP   A N    
598  C  CA   . ASP   A 101 ? 0.26368 0.17004 0.30066 -0.00591 0.00541  -0.02095 253 ASP   A CA   
599  C  C    . ASP   A 101 ? 0.24620 0.15646 0.27800 -0.00455 0.00729  -0.00625 253 ASP   A C    
600  O  O    . ASP   A 101 ? 0.27402 0.18752 0.30212 -0.00772 0.00696  0.00197  253 ASP   A O    
601  C  CB   . ASP   A 101 ? 0.30736 0.20113 0.36630 -0.00627 0.00621  -0.02298 253 ASP   A CB   
602  C  CG   . ASP   A 101 ? 0.43564 0.32578 0.50369 -0.01031 0.00309  -0.03656 253 ASP   A CG   
603  O  OD1  . ASP   A 101 ? 0.44553 0.34395 0.50244 -0.01284 -0.00028 -0.04242 253 ASP   A OD1  
604  O  OD2  . ASP   A 101 ? 0.51655 0.39559 0.60434 -0.01077 0.00358  -0.04161 253 ASP   A OD2  
605  N  N    . ASP   A 102 ? 0.23488 0.14623 0.26690 0.00044  0.00908  -0.00370 254 ASP   A N    
606  C  CA   . ASP   A 102 ? 0.24157 0.15868 0.26867 0.00200  0.00950  0.00860  254 ASP   A CA   
607  C  C    . ASP   A 102 ? 0.21515 0.14260 0.22571 0.00010  0.00865  0.00893  254 ASP   A C    
608  O  O    . ASP   A 102 ? 0.22520 0.15726 0.23048 -0.00126 0.00796  0.01728  254 ASP   A O    
609  C  CB   . ASP   A 102 ? 0.24836 0.16573 0.28239 0.00806  0.01076  0.01031  254 ASP   A CB   
610  C  CG   . ASP   A 102 ? 0.29748 0.20528 0.34784 0.01065  0.01120  0.01803  254 ASP   A CG   
611  O  OD1  . ASP   A 102 ? 0.27123 0.17757 0.33101 0.01645  0.01188  0.01878  254 ASP   A OD1  
612  O  OD2  . ASP   A 102 ? 0.33094 0.23276 0.38599 0.00706  0.01124  0.02402  254 ASP   A OD2  
613  N  N    . GLN   A 103 ? 0.20282 0.13398 0.20505 0.00023  0.00893  -0.00002 255 GLN   A N    
614  C  CA   . GLN   A 103 ? 0.20815 0.14703 0.19661 -0.00172 0.00840  0.00109  255 GLN   A CA   
615  C  C    . GLN   A 103 ? 0.24243 0.18114 0.22782 -0.00581 0.00622  0.00392  255 GLN   A C    
616  O  O    . GLN   A 103 ? 0.23518 0.17867 0.21447 -0.00710 0.00581  0.00944  255 GLN   A O    
617  C  CB   . GLN   A 103 ? 0.22658 0.16864 0.20636 -0.00068 0.00955  -0.00750 255 GLN   A CB   
618  C  CG   . GLN   A 103 ? 0.20684 0.15206 0.18886 0.00340  0.01320  -0.01008 255 GLN   A CG   
619  C  CD   . GLN   A 103 ? 0.25367 0.20311 0.22526 0.00465  0.01553  -0.01788 255 GLN   A CD   
620  O  OE1  . GLN   A 103 ? 0.30289 0.25604 0.26257 0.00268  0.01497  -0.01652 255 GLN   A OE1  
621  N  NE2  . GLN   A 103 ? 0.24690 0.19587 0.22263 0.00847  0.01831  -0.02606 255 GLN   A NE2  
622  N  N    . ILE   A 104 ? 0.25949 0.19326 0.25104 -0.00784 0.00486  -0.00072 256 ILE   A N    
623  C  CA   . ILE   A 104 ? 0.23665 0.17159 0.22850 -0.01170 0.00316  0.00129  256 ILE   A CA   
624  C  C    . ILE   A 104 ? 0.24088 0.17576 0.23736 -0.01281 0.00488  0.01200  256 ILE   A C    
625  O  O    . ILE   A 104 ? 0.25842 0.19860 0.24916 -0.01436 0.00484  0.01613  256 ILE   A O    
626  C  CB   . ILE   A 104 ? 0.23044 0.16111 0.23161 -0.01395 0.00103  -0.00708 256 ILE   A CB   
627  C  CG1  . ILE   A 104 ? 0.24763 0.18197 0.23908 -0.01256 -0.00173 -0.01771 256 ILE   A CG1  
628  C  CG2  . ILE   A 104 ? 0.22717 0.15905 0.23530 -0.01826 0.00036  -0.00338 256 ILE   A CG2  
629  C  CD1  . ILE   A 104 ? 0.31186 0.24284 0.31257 -0.01380 -0.00475 -0.02925 256 ILE   A CD1  
630  N  N    A VAL   A 105 ? 0.21515 0.14441 0.22171 -0.01141 0.00662  0.01691  257 VAL   A N    
631  N  N    B VAL   A 105 ? 0.20165 0.13074 0.20849 -0.01147 0.00661  0.01670  257 VAL   A N    
632  C  CA   A VAL   A 105 ? 0.24171 0.17195 0.25066 -0.01197 0.00853  0.02851  257 VAL   A CA   
633  C  CA   B VAL   A 105 ? 0.24943 0.17916 0.25896 -0.01166 0.00855  0.02851  257 VAL   A CA   
634  C  C    A VAL   A 105 ? 0.21657 0.15521 0.21347 -0.00955 0.00809  0.03377  257 VAL   A C    
635  C  C    B VAL   A 105 ? 0.21318 0.15182 0.20992 -0.00967 0.00803  0.03325  257 VAL   A C    
636  O  O    A VAL   A 105 ? 0.21389 0.15775 0.20596 -0.01045 0.00895  0.04025  257 VAL   A O    
637  O  O    B VAL   A 105 ? 0.19958 0.14360 0.19110 -0.01097 0.00878  0.03872  257 VAL   A O    
638  C  CB   A VAL   A 105 ? 0.28088 0.20233 0.30413 -0.01054 0.01048  0.03461  257 VAL   A CB   
639  C  CB   B VAL   A 105 ? 0.27420 0.19569 0.29660 -0.00912 0.01015  0.03402  257 VAL   A CB   
640  C  CG1  A VAL   A 105 ? 0.29969 0.21230 0.33784 -0.01388 0.01067  0.02766  257 VAL   A CG1  
641  C  CG1  B VAL   A 105 ? 0.29854 0.22357 0.31816 -0.00692 0.01151  0.04784  257 VAL   A CG1  
642  C  CG2  A VAL   A 105 ? 0.26877 0.18886 0.29294 -0.00509 0.00991  0.03469  257 VAL   A CG2  
643  C  CG2  B VAL   A 105 ? 0.30425 0.21625 0.34293 -0.01262 0.01132  0.03141  257 VAL   A CG2  
644  N  N    . LEU   A 106 ? 0.20276 0.14386 0.19544 -0.00659 0.00696  0.03025  258 LEU   A N    
645  C  CA   . LEU   A 106 ? 0.23535 0.18506 0.21919 -0.00516 0.00585  0.03327  258 LEU   A CA   
646  C  C    . LEU   A 106 ? 0.23659 0.19105 0.21121 -0.00803 0.00525  0.02987  258 LEU   A C    
647  O  O    . LEU   A 106 ? 0.20049 0.16115 0.16932 -0.00818 0.00467  0.03305  258 LEU   A O    
648  C  CB   . LEU   A 106 ? 0.20452 0.15655 0.18955 -0.00204 0.00540  0.02994  258 LEU   A CB   
649  C  CG   . LEU   A 106 ? 0.20611 0.15526 0.20141 0.00233  0.00554  0.03380  258 LEU   A CG   
650  C  CD1  . LEU   A 106 ? 0.22245 0.17541 0.22048 0.00519  0.00600  0.02847  258 LEU   A CD1  
651  C  CD2  . LEU   A 106 ? 0.24092 0.19464 0.23565 0.00462  0.00384  0.04431  258 LEU   A CD2  
652  N  N    . LEU   A 107 ? 0.20425 0.15620 0.17740 -0.00975 0.00506  0.02310  259 LEU   A N    
653  C  CA   . LEU   A 107 ? 0.19180 0.14735 0.15766 -0.01157 0.00424  0.02075  259 LEU   A CA   
654  C  C    . LEU   A 107 ? 0.21783 0.17468 0.18511 -0.01366 0.00460  0.02314  259 LEU   A C    
655  O  O    . LEU   A 107 ? 0.24442 0.20607 0.20688 -0.01404 0.00459  0.02394  259 LEU   A O    
656  C  CB   . LEU   A 107 ? 0.22228 0.17590 0.18497 -0.01172 0.00352  0.01436  259 LEU   A CB   
657  C  CG   . LEU   A 107 ? 0.25028 0.20599 0.20869 -0.01016 0.00461  0.01320  259 LEU   A CG   
658  C  CD1  . LEU   A 107 ? 0.28269 0.23699 0.23691 -0.00927 0.00503  0.00793  259 LEU   A CD1  
659  C  CD2  . LEU   A 107 ? 0.30138 0.26097 0.25543 -0.01118 0.00440  0.01519  259 LEU   A CD2  
660  N  N    . LYS   A 108 ? 0.22016 0.17313 0.19576 -0.01513 0.00535  0.02369  260 LYS   A N    
661  C  CA   . LYS   A 108 ? 0.24637 0.20191 0.22598 -0.01750 0.00695  0.02676  260 LYS   A CA   
662  C  C    . LYS   A 108 ? 0.27632 0.23699 0.25174 -0.01645 0.00938  0.03450  260 LYS   A C    
663  O  O    . LYS   A 108 ? 0.25266 0.21932 0.22516 -0.01721 0.01090  0.03545  260 LYS   A O    
664  C  CB   . LYS   A 108 ? 0.25518 0.20527 0.24807 -0.01995 0.00792  0.02672  260 LYS   A CB   
665  C  CG   . LYS   A 108 ? 0.29532 0.24370 0.29245 -0.02152 0.00468  0.01738  260 LYS   A CG   
666  C  CD   . LYS   A 108 ? 0.34796 0.29101 0.36147 -0.02468 0.00528  0.01590  260 LYS   A CD   
667  C  CE   . LYS   A 108 ? 0.42175 0.36824 0.44461 -0.02811 0.00900  0.02258  260 LYS   A CE   
668  N  NZ   . LYS   A 108 ? 0.38162 0.33637 0.40451 -0.02965 0.00736  0.01850  260 LYS   A NZ   
669  N  N    A SER   A 109 ? 0.22941 0.18898 0.20419 -0.01403 0.00960  0.03977  261 SER   A N    
670  N  N    B SER   A 109 ? 0.22937 0.18892 0.20417 -0.01404 0.00959  0.03973  261 SER   A N    
671  C  CA   A SER   A 109 ? 0.22220 0.18827 0.19108 -0.01219 0.01104  0.04755  261 SER   A CA   
672  C  CA   B SER   A 109 ? 0.22214 0.18817 0.19105 -0.01220 0.01101  0.04747  261 SER   A CA   
673  C  C    A SER   A 109 ? 0.26209 0.23592 0.22022 -0.01055 0.00862  0.04384  261 SER   A C    
674  C  C    B SER   A 109 ? 0.26128 0.23508 0.21942 -0.01061 0.00863  0.04372  261 SER   A C    
675  O  O    A SER   A 109 ? 0.30300 0.28459 0.25413 -0.00973 0.00963  0.04632  261 SER   A O    
676  O  O    B SER   A 109 ? 0.30270 0.28421 0.25395 -0.00988 0.00971  0.04603  261 SER   A O    
677  C  CB   A SER   A 109 ? 0.22723 0.19004 0.20020 -0.00933 0.01122  0.05557  261 SER   A CB   
678  C  CB   B SER   A 109 ? 0.22386 0.18668 0.19670 -0.00929 0.01109  0.05527  261 SER   A CB   
679  O  OG   A SER   A 109 ? 0.26093 0.22172 0.23475 -0.00688 0.00811  0.05150  261 SER   A OG   
680  O  OG   B SER   A 109 ? 0.23954 0.21053 0.20404 -0.00662 0.01145  0.06303  261 SER   A OG   
681  N  N    . SER   A 110 ? 0.20813 0.18049 0.16540 -0.01017 0.00585  0.03759  262 SER   A N    
682  C  CA   . SER   A 110 ? 0.20364 0.18252 0.15446 -0.00925 0.00351  0.03400  262 SER   A CA   
683  C  C    . SER   A 110 ? 0.20781 0.18697 0.15624 -0.01114 0.00339  0.02739  262 SER   A C    
684  O  O    . SER   A 110 ? 0.23456 0.21894 0.17911 -0.01082 0.00196  0.02396  262 SER   A O    
685  C  CB   . SER   A 110 ? 0.21861 0.19702 0.17235 -0.00786 0.00133  0.03224  262 SER   A CB   
686  O  OG   . SER   A 110 ? 0.24236 0.21453 0.19922 -0.00926 0.00217  0.02778  262 SER   A OG   
687  N  N    . ALA   A 111 ? 0.19815 0.17209 0.14970 -0.01276 0.00431  0.02518  263 ALA   A N    
688  C  CA   . ALA   A 111 ? 0.22087 0.19394 0.17117 -0.01352 0.00355  0.02006  263 ALA   A CA   
689  C  C    . ALA   A 111 ? 0.20854 0.18727 0.15592 -0.01312 0.00399  0.01787  263 ALA   A C    
690  O  O    . ALA   A 111 ? 0.21297 0.19185 0.15953 -0.01307 0.00275  0.01361  263 ALA   A O    
691  C  CB   . ALA   A 111 ? 0.23518 0.20422 0.18899 -0.01444 0.00352  0.01873  263 ALA   A CB   
692  N  N    . ILE   A 112 ? 0.20849 0.19204 0.15515 -0.01285 0.00635  0.02045  264 ILE   A N    
693  C  CA   . ILE   A 112 ? 0.24603 0.23629 0.18915 -0.01180 0.00748  0.01687  264 ILE   A CA   
694  C  C    . ILE   A 112 ? 0.25860 0.25380 0.19595 -0.01056 0.00517  0.01404  264 ILE   A C    
695  O  O    . ILE   A 112 ? 0.23875 0.23656 0.17508 -0.01004 0.00427  0.00710  264 ILE   A O    
696  C  CB   . ILE   A 112 ? 0.20386 0.20033 0.14670 -0.01160 0.01186  0.02106  264 ILE   A CB   
697  C  CG1  . ILE   A 112 ? 0.21673 0.22134 0.15564 -0.00986 0.01389  0.01573  264 ILE   A CG1  
698  C  CG2  . ILE   A 112 ? 0.23994 0.23946 0.17856 -0.01087 0.01308  0.02914  264 ILE   A CG2  
699  C  CD1  . ILE   A 112 ? 0.23993 0.24122 0.18480 -0.00959 0.01289  0.00847  264 ILE   A CD1  
700  N  N    . GLU   A 113 ? 0.18254 0.17935 0.11772 -0.00986 0.00364  0.01859  265 GLU   A N    
701  C  CA   . GLU   A 113 ? 0.18936 0.19322 0.12023 -0.00848 0.00019  0.01551  265 GLU   A CA   
702  C  C    . GLU   A 113 ? 0.22141 0.22143 0.15810 -0.01022 -0.00260 0.00890  265 GLU   A C    
703  O  O    . GLU   A 113 ? 0.22076 0.22552 0.15719 -0.01033 -0.00503 0.00172  265 GLU   A O    
704  C  CB   . GLU   A 113 ? 0.24508 0.25219 0.17401 -0.00648 -0.00129 0.02303  265 GLU   A CB   
705  C  CG   . GLU   A 113 ? 0.22154 0.23245 0.14510 -0.00470 0.00201  0.03171  265 GLU   A CG   
706  C  CD   . GLU   A 113 ? 0.28908 0.30129 0.21244 -0.00198 0.00035  0.04077  265 GLU   A CD   
707  O  OE1  . GLU   A 113 ? 0.23652 0.25118 0.16181 -0.00064 -0.00434 0.03861  265 GLU   A OE1  
708  O  OE2  . GLU   A 113 ? 0.32323 0.33398 0.24639 -0.00114 0.00392  0.05042  265 GLU   A OE2  
709  N  N    . VAL   A 114 ? 0.22202 0.21389 0.16442 -0.01168 -0.00196 0.01100  266 VAL   A N    
710  C  CA   . VAL   A 114 ? 0.20471 0.19285 0.15303 -0.01360 -0.00301 0.00684  266 VAL   A CA   
711  C  C    . VAL   A 114 ? 0.21375 0.19791 0.16408 -0.01460 -0.00224 0.00171  266 VAL   A C    
712  O  O    . VAL   A 114 ? 0.23140 0.21447 0.18719 -0.01617 -0.00336 -0.00323 266 VAL   A O    
713  C  CB   . VAL   A 114 ? 0.21706 0.19880 0.16870 -0.01419 -0.00144 0.01079  266 VAL   A CB   
714  C  CG1  . VAL   A 114 ? 0.20815 0.18737 0.16585 -0.01626 -0.00108 0.00835  266 VAL   A CG1  
715  C  CG2  . VAL   A 114 ? 0.22044 0.20511 0.17221 -0.01239 -0.00198 0.01532  266 VAL   A CG2  
716  N  N    . ILE   A 115 ? 0.18701 0.16879 0.13532 -0.01368 -0.00031 0.00282  267 ILE   A N    
717  C  CA   . ILE   A 115 ? 0.18604 0.16489 0.13749 -0.01341 0.00018  -0.00207 267 ILE   A CA   
718  C  C    . ILE   A 115 ? 0.21288 0.19827 0.16358 -0.01277 -0.00097 -0.00978 267 ILE   A C    
719  O  O    . ILE   A 115 ? 0.19791 0.18000 0.15480 -0.01355 -0.00194 -0.01607 267 ILE   A O    
720  C  CB   . ILE   A 115 ? 0.21755 0.19547 0.16871 -0.01203 0.00209  0.00016  267 ILE   A CB   
721  C  CG1  . ILE   A 115 ? 0.22050 0.19200 0.17301 -0.01254 0.00185  0.00507  267 ILE   A CG1  
722  C  CG2  . ILE   A 115 ? 0.21717 0.19424 0.17260 -0.01047 0.00261  -0.00555 267 ILE   A CG2  
723  C  CD1  . ILE   A 115 ? 0.21532 0.18802 0.16931 -0.01169 0.00259  0.00685  267 ILE   A CD1  
724  N  N    . MET   A 116 ? 0.23087 0.22574 0.17406 -0.01120 -0.00085 -0.00951 268 MET   A N    
725  C  CA   . MET   A 116 ? 0.21971 0.22316 0.15948 -0.00993 -0.00243 -0.01803 268 MET   A CA   
726  C  C    . MET   A 116 ? 0.21064 0.21502 0.15547 -0.01185 -0.00684 -0.02375 268 MET   A C    
727  O  O    . MET   A 116 ? 0.25097 0.25609 0.20052 -0.01234 -0.00858 -0.03400 268 MET   A O    
728  C  CB   . MET   A 116 ? 0.21216 0.22690 0.14052 -0.00741 -0.00134 -0.01430 268 MET   A CB   
729  C  CG   . MET   A 116 ? 0.26130 0.27684 0.18756 -0.00618 0.00405  -0.00996 268 MET   A CG   
730  S  SD   . MET   A 116 ? 0.28108 0.30941 0.19450 -0.00358 0.00717  -0.00247 268 MET   A SD   
731  C  CE   . MET   A 116 ? 0.31097 0.34129 0.22720 -0.00300 0.01450  -0.00176 268 MET   A CE   
732  N  N    . LEU   A 117 ? 0.22172 0.22591 0.16816 -0.01309 -0.00851 -0.01795 269 LEU   A N    
733  C  CA   . LEU   A 117 ? 0.18798 0.19469 0.14228 -0.01534 -0.01243 -0.02291 269 LEU   A CA   
734  C  C    . LEU   A 117 ? 0.21888 0.21513 0.18577 -0.01876 -0.01111 -0.02641 269 LEU   A C    
735  O  O    . LEU   A 117 ? 0.23021 0.22751 0.20563 -0.02081 -0.01355 -0.03564 269 LEU   A O    
736  C  CB   . LEU   A 117 ? 0.23760 0.24656 0.19287 -0.01531 -0.01345 -0.01526 269 LEU   A CB   
737  C  CG   . LEU   A 117 ? 0.33998 0.36083 0.28867 -0.01227 -0.01721 -0.01243 269 LEU   A CG   
738  C  CD1  . LEU   A 117 ? 0.29001 0.30925 0.24399 -0.01205 -0.01696 -0.00481 269 LEU   A CD1  
739  C  CD2  . LEU   A 117 ? 0.38055 0.41331 0.33062 -0.01218 -0.02335 -0.02234 269 LEU   A CD2  
740  N  N    . ARG   A 118 ? 0.21405 0.20031 0.18274 -0.01940 -0.00740 -0.01888 270 ARG   A N    
741  C  CA   . ARG   A 118 ? 0.19334 0.16960 0.17285 -0.02218 -0.00552 -0.01897 270 ARG   A CA   
742  C  C    . ARG   A 118 ? 0.17797 0.14887 0.16234 -0.02172 -0.00529 -0.02583 270 ARG   A C    
743  O  O    . ARG   A 118 ? 0.21525 0.17937 0.21188 -0.02439 -0.00492 -0.02905 270 ARG   A O    
744  C  CB   . ARG   A 118 ? 0.20073 0.16953 0.17761 -0.02183 -0.00199 -0.00906 270 ARG   A CB   
745  C  CG   . ARG   A 118 ? 0.17737 0.14171 0.14793 -0.01894 -0.00063 -0.00606 270 ARG   A CG   
746  C  CD   . ARG   A 118 ? 0.21493 0.17636 0.18013 -0.01814 0.00110  0.00203  270 ARG   A CD   
747  N  NE   . ARG   A 118 ? 0.25852 0.21530 0.22770 -0.02000 0.00322  0.00605  270 ARG   A NE   
748  C  CZ   . ARG   A 118 ? 0.21678 0.16576 0.18844 -0.01995 0.00502  0.00964  270 ARG   A CZ   
749  N  NH1  . ARG   A 118 ? 0.24721 0.19193 0.21903 -0.01770 0.00406  0.00904  270 ARG   A NH1  
750  N  NH2  . ARG   A 118 ? 0.22404 0.17009 0.19842 -0.02170 0.00816  0.01458  270 ARG   A NH2  
751  N  N    . SER   A 119 ? 0.18497 0.15897 0.16166 -0.01831 -0.00501 -0.02818 271 SER   A N    
752  C  CA   . SER   A 119 ? 0.18350 0.15382 0.16556 -0.01681 -0.00457 -0.03617 271 SER   A CA   
753  C  C    . SER   A 119 ? 0.20694 0.18132 0.19606 -0.01843 -0.00771 -0.04908 271 SER   A C    
754  O  O    . SER   A 119 ? 0.23616 0.20414 0.23527 -0.01822 -0.00744 -0.05701 271 SER   A O    
755  C  CB   . SER   A 119 ? 0.22574 0.20176 0.19873 -0.01275 -0.00283 -0.03655 271 SER   A CB   
756  O  OG   . SER   A 119 ? 0.24472 0.23363 0.20860 -0.01144 -0.00414 -0.04215 271 SER   A OG   
757  N  N    . ASN   A 120 ? 0.20943 0.19439 0.19502 -0.01981 -0.01123 -0.05192 272 ASN   A N    
758  C  CA   . ASN   A 120 ? 0.23558 0.22701 0.22766 -0.02129 -0.01564 -0.06595 272 ASN   A CA   
759  C  C    . ASN   A 120 ? 0.24894 0.22924 0.26130 -0.02599 -0.01563 -0.07025 272 ASN   A C    
760  O  O    . ASN   A 120 ? 0.23994 0.22054 0.26233 -0.02724 -0.01831 -0.08407 272 ASN   A O    
761  C  CB   . ASN   A 120 ? 0.22088 0.22673 0.20627 -0.02149 -0.02039 -0.06630 272 ASN   A CB   
762  C  CG   . ASN   A 120 ? 0.27637 0.29376 0.26344 -0.02151 -0.02644 -0.08234 272 ASN   A CG   
763  O  OD1  . ASN   A 120 ? 0.25371 0.27491 0.25280 -0.02523 -0.03100 -0.08838 272 ASN   A OD1  
764  N  ND2  . ASN   A 120 ? 0.24821 0.27272 0.22346 -0.01725 -0.02647 -0.08990 272 ASN   A ND2  
765  N  N    . GLN   A 121 ? 0.24517 0.21559 0.26408 -0.02858 -0.01219 -0.05868 273 GLN   A N    
766  C  CA   . GLN   A 121 ? 0.27198 0.23087 0.31068 -0.03327 -0.01055 -0.05950 273 GLN   A CA   
767  C  C    . GLN   A 121 ? 0.27223 0.21912 0.31979 -0.03172 -0.00892 -0.06500 273 GLN   A C    
768  O  O    . GLN   A 121 ? 0.30174 0.24116 0.36816 -0.03537 -0.00931 -0.07246 273 GLN   A O    
769  C  CB   . GLN   A 121 ? 0.30654 0.25850 0.34620 -0.03507 -0.00588 -0.04407 273 GLN   A CB   
770  C  CG   . GLN   A 121 ? 0.32449 0.26656 0.38440 -0.04062 -0.00284 -0.04174 273 GLN   A CG   
771  C  CD   . GLN   A 121 ? 0.35318 0.29466 0.41187 -0.04254 0.00179  -0.02804 273 GLN   A CD   
772  O  OE1  . GLN   A 121 ? 0.32451 0.27530 0.37069 -0.04067 0.00120  -0.02387 273 GLN   A OE1  
773  N  NE2  . GLN   A 121 ? 0.34205 0.27258 0.41428 -0.04605 0.00695  -0.02089 273 GLN   A NE2  
774  N  N    . SER   A 122 ? 0.27156 0.21643 0.30831 -0.02634 -0.00705 -0.06180 274 SER   A N    
775  C  CA   . SER   A 122 ? 0.28569 0.22041 0.33180 -0.02359 -0.00571 -0.06758 274 SER   A CA   
776  C  C    . SER   A 122 ? 0.29022 0.23386 0.33373 -0.02066 -0.00828 -0.08451 274 SER   A C    
777  O  O    . SER   A 122 ? 0.30870 0.24459 0.36275 -0.01823 -0.00736 -0.09273 274 SER   A O    
778  C  CB   . SER   A 122 ? 0.28071 0.20950 0.31976 -0.01874 -0.00253 -0.05621 274 SER   A CB   
779  O  OG   . SER   A 122 ? 0.26790 0.20889 0.28993 -0.01512 -0.00276 -0.05576 274 SER   A OG   
780  N  N    . PHE   A 123 ? 0.27138 0.23138 0.30069 -0.02009 -0.01122 -0.08956 275 PHE   A N    
781  C  CA   . PHE   A 123 ? 0.24626 0.21741 0.26877 -0.01646 -0.01307 -0.10487 275 PHE   A CA   
782  C  C    . PHE   A 123 ? 0.28371 0.25335 0.32235 -0.01936 -0.01703 -0.12282 275 PHE   A C    
783  O  O    . PHE   A 123 ? 0.28639 0.25638 0.33496 -0.02487 -0.02051 -0.12447 275 PHE   A O    
784  C  CB   . PHE   A 123 ? 0.25987 0.24920 0.26172 -0.01484 -0.01518 -0.10277 275 PHE   A CB   
785  C  CG   . PHE   A 123 ? 0.28224 0.28525 0.27161 -0.00995 -0.01548 -0.11499 275 PHE   A CG   
786  C  CD1  . PHE   A 123 ? 0.26326 0.26850 0.24340 -0.00499 -0.01010 -0.11129 275 PHE   A CD1  
787  C  CD2  . PHE   A 123 ? 0.34861 0.36388 0.33563 -0.01020 -0.02106 -0.13051 275 PHE   A CD2  
788  C  CE1  . PHE   A 123 ? 0.29254 0.31177 0.26069 -0.00031 -0.00890 -0.12206 275 PHE   A CE1  
789  C  CE2  . PHE   A 123 ? 0.35770 0.38727 0.33054 -0.00506 -0.02089 -0.14193 275 PHE   A CE2  
790  C  CZ   . PHE   A 123 ? 0.33735 0.36883 0.30040 -0.00009 -0.01412 -0.13730 275 PHE   A CZ   
791  N  N    . THR   A 124 ? 0.26822 0.23660 0.31144 -0.01572 -0.01641 -0.13721 276 THR   A N    
792  C  CA   . THR   A 124 ? 0.35935 0.32655 0.41862 -0.01798 -0.02049 -0.15765 276 THR   A CA   
793  C  C    . THR   A 124 ? 0.39794 0.38377 0.44166 -0.01326 -0.02320 -0.17498 276 THR   A C    
794  O  O    . THR   A 124 ? 0.38483 0.37611 0.41536 -0.00698 -0.01894 -0.17487 276 THR   A O    
795  C  CB   . THR   A 124 ? 0.44092 0.38784 0.52349 -0.01755 -0.01730 -0.16186 276 THR   A CB   
796  O  OG1  . THR   A 124 ? 0.56055 0.51049 0.65451 -0.01782 -0.02019 -0.17710 276 THR   A OG1  
797  C  CG2  . THR   A 124 ? 0.44539 0.38954 0.52092 -0.01006 -0.01198 -0.15742 276 THR   A CG2  
798  N  N    . MET   A 125 ? 0.45157 0.44900 0.49608 -0.01554 -0.02920 -0.18385 277 MET   A N    
799  C  CA   . MET   A 125 ? 0.41364 0.43050 0.44086 -0.01035 -0.03140 -0.19443 277 MET   A CA   
800  C  C    . MET   A 125 ? 0.43517 0.44872 0.47238 -0.00683 -0.02942 -0.20808 277 MET   A C    
801  O  O    . MET   A 125 ? 0.52782 0.55674 0.55026 -0.00175 -0.02967 -0.21689 277 MET   A O    
802  C  CB   . MET   A 125 ? 0.36861 0.40071 0.39208 -0.01312 -0.03936 -0.19870 277 MET   A CB   
803  C  CG   . MET   A 125 ? 0.38661 0.43257 0.38748 -0.01197 -0.04124 -0.18705 277 MET   A CG   
804  S  SD   . MET   A 125 ? 0.57946 0.64388 0.57723 -0.01398 -0.05124 -0.19028 277 MET   A SD   
805  C  CE   . MET   A 125 ? 0.59379 0.64358 0.62725 -0.02264 -0.05399 -0.19664 277 MET   A CE   
806  N  N    . ASP   A 126 ? 0.43064 0.42469 0.49234 -0.00902 -0.02706 -0.20899 278 ASP   A N    
807  C  CA   . ASP   A 126 ? 0.47339 0.46336 0.54735 -0.00560 -0.02541 -0.22203 278 ASP   A CA   
808  C  C    . ASP   A 126 ? 0.47321 0.46613 0.53553 0.00211  -0.01919 -0.22263 278 ASP   A C    
809  O  O    . ASP   A 126 ? 0.51373 0.51156 0.57815 0.00638  -0.01817 -0.23568 278 ASP   A O    
810  C  CB   . ASP   A 126 ? 0.51195 0.47964 0.61577 -0.00982 -0.02424 -0.21964 278 ASP   A CB   
811  C  CG   . ASP   A 126 ? 0.58860 0.55390 0.70564 -0.01787 -0.02889 -0.21738 278 ASP   A CG   
812  O  OD1  . ASP   A 126 ? 0.46570 0.44424 0.58301 -0.01945 -0.03456 -0.22981 278 ASP   A OD1  
813  O  OD2  . ASP   A 126 ? 0.60520 0.55663 0.73237 -0.02239 -0.02677 -0.20314 278 ASP   A OD2  
814  N  N    . ASP   A 127 ? 0.43831 0.42905 0.48974 0.00400  -0.01481 -0.20939 279 ASP   A N    
815  C  CA   . ASP   A 127 ? 0.46365 0.46109 0.50362 0.01135  -0.00853 -0.20987 279 ASP   A CA   
816  C  C    . ASP   A 127 ? 0.42007 0.42650 0.43889 0.01266  -0.00544 -0.19702 279 ASP   A C    
817  O  O    . ASP   A 127 ? 0.43529 0.44311 0.45013 0.01773  0.00092  -0.19320 279 ASP   A O    
818  C  CB   . ASP   A 127 ? 0.52541 0.50501 0.58633 0.01441  -0.00407 -0.20899 279 ASP   A CB   
819  C  CG   . ASP   A 127 ? 0.55769 0.51765 0.63202 0.01079  -0.00378 -0.19424 279 ASP   A CG   
820  O  OD1  . ASP   A 127 ? 0.60908 0.55434 0.69939 0.01394  -0.00056 -0.18998 279 ASP   A OD1  
821  O  OD2  . ASP   A 127 ? 0.54717 0.50684 0.61611 0.00517  -0.00685 -0.18627 279 ASP   A OD2  
822  N  N    . MET   A 128 ? 0.37170 0.38471 0.37872 0.00833  -0.00965 -0.19017 280 MET   A N    
823  C  CA   . MET   A 128 ? 0.32421 0.34819 0.30974 0.00948  -0.00709 -0.17730 280 MET   A CA   
824  C  C    . MET   A 128 ? 0.31233 0.32361 0.30458 0.00995  -0.00161 -0.15892 280 MET   A C    
825  O  O    . MET   A 128 ? 0.35372 0.37266 0.33564 0.01392  0.00411  -0.15143 280 MET   A O    
826  C  CB   . MET   A 128 ? 0.37744 0.42253 0.34100 0.01523  -0.00360 -0.18063 280 MET   A CB   
827  C  CG   . MET   A 128 ? 0.49536 0.55356 0.45171 0.01562  -0.00891 -0.19128 280 MET   A CG   
828  S  SD   . MET   A 128 ? 0.57961 0.64877 0.52144 0.01172  -0.01659 -0.18278 280 MET   A SD   
829  C  CE   . MET   A 128 ? 0.61662 0.67274 0.58425 0.00496  -0.02474 -0.19227 280 MET   A CE   
830  N  N    . SER   A 129 ? 0.29571 0.28835 0.30600 0.00585  -0.00336 -0.15173 281 SER   A N    
831  C  CA   . SER   A 129 ? 0.27741 0.25791 0.29467 0.00676  0.00044  -0.13557 281 SER   A CA   
832  C  C    . SER   A 129 ? 0.26771 0.23723 0.28970 0.00086  -0.00220 -0.12076 281 SER   A C    
833  O  O    . SER   A 129 ? 0.27154 0.23897 0.29889 -0.00412 -0.00636 -0.12474 281 SER   A O    
834  C  CB   . SER   A 129 ? 0.39886 0.36589 0.43630 0.01060  0.00272  -0.14290 281 SER   A CB   
835  O  OG   . SER   A 129 ? 0.50110 0.45208 0.55780 0.00646  -0.00067 -0.14724 281 SER   A OG   
836  N  N    . TRP   A 130 ? 0.26432 0.22796 0.28516 0.00159  0.00036  -0.10433 282 TRP   A N    
837  C  CA   . TRP   A 130 ? 0.28613 0.23912 0.31088 -0.00284 -0.00091 -0.08980 282 TRP   A CA   
838  C  C    . TRP   A 130 ? 0.31667 0.25164 0.36015 -0.00181 0.00008  -0.08675 282 TRP   A C    
839  O  O    . TRP   A 130 ? 0.28916 0.22056 0.33499 0.00290  0.00222  -0.08099 282 TRP   A O    
840  C  CB   . TRP   A 130 ? 0.23579 0.19430 0.24659 -0.00245 0.00062  -0.07449 282 TRP   A CB   
841  C  CG   . TRP   A 130 ? 0.27455 0.24822 0.26839 -0.00357 -0.00009 -0.07364 282 TRP   A CG   
842  C  CD1  . TRP   A 130 ? 0.25832 0.23459 0.24622 -0.00752 -0.00253 -0.06733 282 TRP   A CD1  
843  C  CD2  . TRP   A 130 ? 0.24646 0.23481 0.22769 -0.00013 0.00221  -0.07769 282 TRP   A CD2  
844  N  NE1  . TRP   A 130 ? 0.27140 0.26197 0.24418 -0.00642 -0.00263 -0.06680 282 TRP   A NE1  
845  C  CE2  . TRP   A 130 ? 0.24498 0.24321 0.21263 -0.00213 0.00059  -0.07241 282 TRP   A CE2  
846  C  CE3  . TRP   A 130 ? 0.24700 0.24170 0.22776 0.00475  0.00611  -0.08480 282 TRP   A CE3  
847  C  CZ2  . TRP   A 130 ? 0.25039 0.26360 0.20312 0.00044  0.00275  -0.07243 282 TRP   A CZ2  
848  C  CZ3  . TRP   A 130 ? 0.29168 0.30262 0.25735 0.00692  0.00902  -0.08567 282 TRP   A CZ3  
849  C  CH2  . TRP   A 130 ? 0.27121 0.29084 0.22252 0.00470  0.00735  -0.07877 282 TRP   A CH2  
850  N  N    . ASP   A 131 ? 0.28501 0.20912 0.34304 -0.00618 -0.00155 -0.08991 283 ASP   A N    
851  C  CA   . ASP   A 131 ? 0.26217 0.16766 0.34047 -0.00545 -0.00032 -0.08733 283 ASP   A CA   
852  C  C    . ASP   A 131 ? 0.28308 0.17941 0.36140 -0.00843 0.00076  -0.06811 283 ASP   A C    
853  O  O    . ASP   A 131 ? 0.37334 0.26696 0.45610 -0.01462 0.00041  -0.06522 283 ASP   A O    
854  C  CB   . ASP   A 131 ? 0.31663 0.21530 0.41355 -0.00891 -0.00202 -0.10310 283 ASP   A CB   
855  C  CG   . ASP   A 131 ? 0.40654 0.28438 0.52726 -0.00762 -0.00021 -0.10120 283 ASP   A CG   
856  O  OD1  . ASP   A 131 ? 0.41072 0.27959 0.53225 -0.00397 0.00194  -0.08562 283 ASP   A OD1  
857  O  OD2  . ASP   A 131 ? 0.44857 0.31900 0.58813 -0.01012 -0.00134 -0.11560 283 ASP   A OD2  
858  N  N    . CYS   A 132 ? 0.24815 0.14104 0.32196 -0.00377 0.00211  -0.05550 284 CYS   A N    
859  C  CA   . CYS   A 132 ? 0.29531 0.18133 0.36578 -0.00524 0.00312  -0.03738 284 CYS   A CA   
860  C  C    . CYS   A 132 ? 0.36504 0.23308 0.45204 -0.00286 0.00456  -0.02912 284 CYS   A C    
861  O  O    . CYS   A 132 ? 0.35124 0.21554 0.43388 0.00140  0.00468  -0.01552 284 CYS   A O    
862  C  CB   . CYS   A 132 ? 0.29683 0.19297 0.34944 -0.00191 0.00258  -0.02854 284 CYS   A CB   
863  S  SG   . CYS   A 132 ? 0.28802 0.20219 0.32256 -0.00515 0.00171  -0.03339 284 CYS   A SG   
864  N  N    . GLY   A 133 ? 0.43489 0.29155 0.54187 -0.00540 0.00534  -0.03719 285 GLY   A N    
865  C  CA   . GLY   A 133 ? 0.46503 0.30254 0.58987 -0.00504 0.00761  -0.02689 285 GLY   A CA   
866  C  C    . GLY   A 133 ? 0.48727 0.31340 0.62828 0.00227  0.00735  -0.03076 285 GLY   A C    
867  O  O    . GLY   A 133 ? 0.49570 0.30486 0.65584 0.00202  0.00923  -0.02552 285 GLY   A O    
868  N  N    . SER   A 134 ? 0.50205 0.33796 0.63654 0.00891  0.00557  -0.03888 286 SER   A N    
869  C  CA   . SER   A 134 ? 0.50507 0.33149 0.65641 0.01688  0.00551  -0.04310 286 SER   A CA   
870  C  C    . SER   A 134 ? 0.44791 0.28981 0.59330 0.02155  0.00480  -0.05962 286 SER   A C    
871  O  O    . SER   A 134 ? 0.41572 0.27502 0.54184 0.01926  0.00436  -0.06311 286 SER   A O    
872  C  CB   . SER   A 134 ? 0.59757 0.41677 0.74863 0.02360  0.00486  -0.02317 286 SER   A CB   
873  O  OG   . SER   A 134 ? 0.65040 0.48480 0.77842 0.02443  0.00311  -0.01406 286 SER   A OG   
874  N  N    . GLN   A 135 ? 0.45282 0.28803 0.61596 0.02844  0.00535  -0.06928 287 GLN   A N    
875  C  CA   . GLN   A 135 ? 0.45531 0.30582 0.61453 0.03363  0.00613  -0.08532 287 GLN   A CA   
876  C  C    . GLN   A 135 ? 0.40654 0.27311 0.54842 0.03732  0.00568  -0.07538 287 GLN   A C    
877  O  O    . GLN   A 135 ? 0.42909 0.31383 0.55667 0.03666  0.00694  -0.08361 287 GLN   A O    
878  C  CB   . GLN   A 135 ? 0.53226 0.37496 0.71239 0.04072  0.00713  -0.09440 287 GLN   A CB   
879  C  CG   . GLN   A 135 ? 0.62012 0.47840 0.79801 0.04412  0.00918  -0.11560 287 GLN   A CG   
880  C  CD   . GLN   A 135 ? 0.67112 0.53904 0.83797 0.03673  0.00901  -0.13068 287 GLN   A CD   
881  O  OE1  . GLN   A 135 ? 0.67654 0.53641 0.84797 0.02958  0.00721  -0.13073 287 GLN   A OE1  
882  N  NE2  . GLN   A 135 ? 0.67815 0.56517 0.83031 0.03863  0.01091  -0.14279 287 GLN   A NE2  
883  N  N    . ASP   A 136 ? 0.37535 0.23591 0.51884 0.04123  0.00378  -0.05755 288 ASP   A N    
884  C  CA   . ASP   A 136 ? 0.37390 0.24967 0.50329 0.04411  0.00231  -0.04862 288 ASP   A CA   
885  C  C    . ASP   A 136 ? 0.32304 0.21213 0.42962 0.03653  0.00247  -0.04667 288 ASP   A C    
886  O  O    . ASP   A 136 ? 0.32448 0.22988 0.42052 0.03741  0.00291  -0.04785 288 ASP   A O    
887  C  CB   . ASP   A 136 ? 0.41966 0.28696 0.55176 0.04852  -0.00118 -0.02923 288 ASP   A CB   
888  C  CG   . ASP   A 136 ? 0.60160 0.45852 0.75616 0.05823  -0.00211 -0.02882 288 ASP   A CG   
889  O  OD1  . ASP   A 136 ? 0.65877 0.52367 0.82330 0.06385  -0.00061 -0.04191 288 ASP   A OD1  
890  O  OD2  . ASP   A 136 ? 0.67605 0.51716 0.83852 0.06071  -0.00394 -0.01464 288 ASP   A OD2  
891  N  N    . TYR   A 137 ? 0.29646 0.17884 0.39723 0.02913  0.00241  -0.04326 289 TYR   A N    
892  C  CA   . TYR   A 137 ? 0.27890 0.17199 0.35998 0.02247  0.00226  -0.03994 289 TYR   A CA   
893  C  C    . TYR   A 137 ? 0.30602 0.20421 0.38414 0.01711  0.00356  -0.05428 289 TYR   A C    
894  O  O    . TYR   A 137 ? 0.31694 0.21619 0.38682 0.01065  0.00306  -0.05168 289 TYR   A O    
895  C  CB   . TYR   A 137 ? 0.31103 0.19578 0.38644 0.01887  0.00109  -0.02369 289 TYR   A CB   
896  C  CG   . TYR   A 137 ? 0.32205 0.20157 0.39998 0.02505  -0.00109 -0.00971 289 TYR   A CG   
897  C  CD1  . TYR   A 137 ? 0.41377 0.27834 0.49756 0.02533  -0.00114 0.00331  289 TYR   A CD1  
898  C  CD2  . TYR   A 137 ? 0.29546 0.18602 0.37061 0.03079  -0.00317 -0.00912 289 TYR   A CD2  
899  C  CE1  . TYR   A 137 ? 0.41991 0.28101 0.50408 0.03199  -0.00391 0.01691  289 TYR   A CE1  
900  C  CE2  . TYR   A 137 ? 0.31321 0.20094 0.39102 0.03708  -0.00663 0.00302  289 TYR   A CE2  
901  C  CZ   . TYR   A 137 ? 0.40113 0.27429 0.48215 0.03808  -0.00736 0.01616  289 TYR   A CZ   
902  O  OH   . TYR   A 137 ? 0.38855 0.26016 0.47023 0.04530  -0.01154 0.02911  289 TYR   A OH   
903  N  N    . LYS   A 138 ? 0.32169 0.22429 0.40674 0.02036  0.00500  -0.07016 290 LYS   A N    
904  C  CA   . LYS   A 138 ? 0.30956 0.22122 0.38893 0.01681  0.00548  -0.08557 290 LYS   A CA   
905  C  C    . LYS   A 138 ? 0.30993 0.24062 0.37620 0.02015  0.00788  -0.09122 290 LYS   A C    
906  O  O    . LYS   A 138 ? 0.34144 0.27536 0.41516 0.02658  0.01026  -0.09647 290 LYS   A O    
907  C  CB   . LYS   A 138 ? 0.32546 0.22688 0.42371 0.01777  0.00549  -0.10133 290 LYS   A CB   
908  C  CG   . LYS   A 138 ? 0.36739 0.27908 0.46006 0.01443  0.00464  -0.11927 290 LYS   A CG   
909  C  CD   . LYS   A 138 ? 0.51822 0.42287 0.62975 0.01777  0.00507  -0.13874 290 LYS   A CD   
910  C  CE   . LYS   A 138 ? 0.61623 0.50859 0.74281 0.01119  0.00211  -0.14567 290 LYS   A CE   
911  N  NZ   . LYS   A 138 ? 0.67243 0.58046 0.78573 0.00610  -0.00098 -0.15704 290 LYS   A NZ   
912  N  N    . TYR   A 139 ? 0.29432 0.23760 0.34243 0.01604  0.00776  -0.08881 291 TYR   A N    
913  C  CA   . TYR   A 139 ? 0.29274 0.25347 0.32755 0.01823  0.01087  -0.08890 291 TYR   A CA   
914  C  C    . TYR   A 139 ? 0.31121 0.28502 0.33596 0.01789  0.01217  -0.10321 291 TYR   A C    
915  O  O    . TYR   A 139 ? 0.30898 0.28440 0.32602 0.01324  0.00914  -0.10520 291 TYR   A O    
916  C  CB   . TYR   A 139 ? 0.29398 0.25880 0.31601 0.01459  0.01003  -0.07339 291 TYR   A CB   
917  C  CG   . TYR   A 139 ? 0.26732 0.21938 0.29647 0.01440  0.00754  -0.06035 291 TYR   A CG   
918  C  CD1  . TYR   A 139 ? 0.27526 0.21888 0.30135 0.00947  0.00493  -0.05210 291 TYR   A CD1  
919  C  CD2  . TYR   A 139 ? 0.25874 0.20845 0.29786 0.01973  0.00780  -0.05650 291 TYR   A CD2  
920  C  CE1  . TYR   A 139 ? 0.29547 0.22877 0.32558 0.00991  0.00321  -0.03983 291 TYR   A CE1  
921  C  CE2  . TYR   A 139 ? 0.27905 0.21856 0.32256 0.02047  0.00479  -0.04418 291 TYR   A CE2  
922  C  CZ   . TYR   A 139 ? 0.30398 0.23533 0.34170 0.01558  0.00278  -0.03577 291 TYR   A CZ   
923  O  OH   . TYR   A 139 ? 0.26598 0.18867 0.30549 0.01688  0.00036  -0.02324 291 TYR   A OH   
924  N  N    . ASP   A 140 ? 0.31210 0.29677 0.33671 0.02324  0.01660  -0.11313 292 ASP   A N    
925  C  CA   . ASP   A 140 ? 0.33505 0.33515 0.34674 0.02416  0.01852  -0.12645 292 ASP   A CA   
926  C  C    . ASP   A 140 ? 0.31321 0.33096 0.30886 0.02521  0.02373  -0.11862 292 ASP   A C    
927  O  O    . ASP   A 140 ? 0.30866 0.32562 0.30480 0.02411  0.02496  -0.10388 292 ASP   A O    
928  C  CB   . ASP   A 140 ? 0.32485 0.32471 0.34825 0.02963  0.02053  -0.14616 292 ASP   A CB   
929  C  CG   . ASP   A 140 ? 0.40177 0.40306 0.43709 0.03629  0.02597  -0.14601 292 ASP   A CG   
930  O  OD1  . ASP   A 140 ? 0.42526 0.42303 0.47461 0.04149  0.02756  -0.16113 292 ASP   A OD1  
931  O  OD2  . ASP   A 140 ? 0.36846 0.37476 0.40109 0.03653  0.02845  -0.13188 292 ASP   A OD2  
932  N  N    . VAL   A 141 ? 0.33355 0.36776 0.31517 0.02735  0.02691  -0.12865 293 VAL   A N    
933  C  CA   . VAL   A 141 ? 0.35576 0.40683 0.32161 0.02786  0.03277  -0.11957 293 VAL   A CA   
934  C  C    . VAL   A 141 ? 0.29816 0.35346 0.27464 0.03160  0.03972  -0.11553 293 VAL   A C    
935  O  O    . VAL   A 141 ? 0.31231 0.37424 0.28469 0.02985  0.04340  -0.10190 293 VAL   A O    
936  C  CB   . VAL   A 141 ? 0.32386 0.39288 0.27076 0.03028  0.03502  -0.13081 293 VAL   A CB   
937  C  CG1  . VAL   A 141 ? 0.37290 0.44000 0.30983 0.02626  0.02689  -0.13248 293 VAL   A CG1  
938  C  CG2  . VAL   A 141 ? 0.35824 0.43151 0.31209 0.03624  0.03806  -0.15157 293 VAL   A CG2  
939  N  N    . THR   A 142 ? 0.30828 0.35974 0.30093 0.03676  0.04141  -0.12746 294 THR   A N    
940  C  CA   . THR   A 142 ? 0.27516 0.33131 0.28155 0.04093  0.04721  -0.12423 294 THR   A CA   
941  C  C    . THR   A 142 ? 0.30277 0.34825 0.31904 0.03777  0.04325  -0.10751 294 THR   A C    
942  O  O    . THR   A 142 ? 0.30080 0.35528 0.31980 0.03756  0.04728  -0.09811 294 THR   A O    
943  C  CB   . THR   A 142 ? 0.31666 0.36849 0.34091 0.04782  0.04856  -0.14055 294 THR   A CB   
944  O  OG1  . THR   A 142 ? 0.39169 0.45620 0.40541 0.05124  0.05284  -0.15804 294 THR   A OG1  
945  C  CG2  . THR   A 142 ? 0.38670 0.44418 0.42811 0.05284  0.05377  -0.13710 294 THR   A CG2  
946  N  N    . ASP   A 143 ? 0.32334 0.35057 0.34530 0.03515  0.03550  -0.10389 295 ASP   A N    
947  C  CA   . ASP   A 143 ? 0.24847 0.26642 0.27683 0.03262  0.03125  -0.08868 295 ASP   A CA   
948  C  C    . ASP   A 143 ? 0.26043 0.28605 0.27508 0.02724  0.03206  -0.07600 295 ASP   A C    
949  O  O    . ASP   A 143 ? 0.24005 0.26791 0.26045 0.02652  0.03215  -0.06623 295 ASP   A O    
950  C  CB   . ASP   A 143 ? 0.27894 0.27741 0.31224 0.03040  0.02410  -0.08635 295 ASP   A CB   
951  C  CG   . ASP   A 143 ? 0.36268 0.34999 0.41453 0.03581  0.02304  -0.09525 295 ASP   A CG   
952  O  OD1  . ASP   A 143 ? 0.36674 0.35924 0.43088 0.04192  0.02613  -0.09858 295 ASP   A OD1  
953  O  OD2  . ASP   A 143 ? 0.36741 0.34069 0.42354 0.03398  0.01933  -0.09872 295 ASP   A OD2  
954  N  N    . VAL   A 144 ? 0.25148 0.28124 0.24929 0.02362  0.03213  -0.07630 296 VAL   A N    
955  C  CA   . VAL   A 144 ? 0.21964 0.25519 0.20596 0.01904  0.03308  -0.06386 296 VAL   A CA   
956  C  C    . VAL   A 144 ? 0.21194 0.26361 0.19844 0.02044  0.04122  -0.06104 296 VAL   A C    
957  O  O    . VAL   A 144 ? 0.25010 0.30394 0.23917 0.01741  0.04232  -0.04986 296 VAL   A O    
958  C  CB   . VAL   A 144 ? 0.25971 0.29665 0.22911 0.01596  0.03079  -0.06437 296 VAL   A CB   
959  C  CG1  . VAL   A 144 ? 0.24598 0.28744 0.20552 0.01198  0.03191  -0.05064 296 VAL   A CG1  
960  C  CG2  . VAL   A 144 ? 0.25932 0.28107 0.23237 0.01376  0.02341  -0.06675 296 VAL   A CG2  
961  N  N    . SER   A 145 ? 0.22737 0.29095 0.21261 0.02497  0.04749  -0.07173 297 SER   A N    
962  C  CA   . SER   A 145 ? 0.26186 0.34209 0.24954 0.02650  0.05687  -0.06899 297 SER   A CA   
963  C  C    . SER   A 145 ? 0.28136 0.36041 0.29075 0.02771  0.05704  -0.06545 297 SER   A C    
964  O  O    . SER   A 145 ? 0.25800 0.34791 0.27319 0.02604  0.06273  -0.05799 297 SER   A O    
965  C  CB   . SER   A 145 ? 0.30230 0.39648 0.28388 0.03202  0.06403  -0.08275 297 SER   A CB   
966  O  OG   . SER   A 145 ? 0.34226 0.43370 0.34094 0.03773  0.06429  -0.09505 297 SER   A OG   
967  N  N    . LYS   A 146 ? 0.23899 0.30529 0.26148 0.03053  0.05060  -0.07005 298 LYS   A N    
968  C  CA   . LYS   A 146 ? 0.27341 0.33866 0.31621 0.03277  0.04867  -0.06661 298 LYS   A CA   
969  C  C    . LYS   A 146 ? 0.23569 0.29364 0.27940 0.02752  0.04229  -0.05358 298 LYS   A C    
970  O  O    . LYS   A 146 ? 0.25896 0.31574 0.31804 0.02930  0.03843  -0.05043 298 LYS   A O    
971  C  CB   . LYS   A 146 ? 0.27775 0.33175 0.33382 0.03884  0.04410  -0.07521 298 LYS   A CB   
972  C  CG   . LYS   A 146 ? 0.36816 0.43034 0.42986 0.04546  0.05070  -0.09035 298 LYS   A CG   
973  C  CD   . LYS   A 146 ? 0.45787 0.54072 0.52778 0.04792  0.06010  -0.09119 298 LYS   A CD   
974  C  CE   . LYS   A 146 ? 0.51379 0.60433 0.59391 0.05618  0.06639  -0.10718 298 LYS   A CE   
975  N  NZ   . LYS   A 146 ? 0.51184 0.62318 0.60492 0.05920  0.07591  -0.10751 298 LYS   A NZ   
976  N  N    . ALA   A 147 ? 0.23198 0.28562 0.25996 0.02177  0.04061  -0.04676 299 ALA   A N    
977  C  CA   . ALA   A 147 ? 0.26471 0.31515 0.29299 0.01658  0.03687  -0.03559 299 ALA   A CA   
978  C  C    . ALA   A 147 ? 0.25351 0.31641 0.27904 0.01250  0.04402  -0.02929 299 ALA   A C    
979  O  O    . ALA   A 147 ? 0.26671 0.32707 0.29336 0.00766  0.04172  -0.02084 299 ALA   A O    
980  C  CB   . ALA   A 147 ? 0.28338 0.31932 0.29908 0.01322  0.03014  -0.03155 299 ALA   A CB   
981  N  N    . GLY   A 148 ? 0.22571 0.30194 0.24798 0.01447  0.05308  -0.03324 300 GLY   A N    
982  C  CA   . GLY   A 148 ? 0.27080 0.35996 0.29152 0.01105  0.06180  -0.02585 300 GLY   A CA   
983  C  C    . GLY   A 148 ? 0.27347 0.36563 0.27250 0.00978  0.06582  -0.02269 300 GLY   A C    
984  O  O    . GLY   A 148 ? 0.28071 0.38402 0.27676 0.00762  0.07431  -0.01514 300 GLY   A O    
985  N  N    . HIS   A 149 ? 0.23586 0.31926 0.22056 0.01109  0.06004  -0.02751 301 HIS   A N    
986  C  CA   . HIS   A 149 ? 0.21733 0.30455 0.18165 0.01011  0.06200  -0.02366 301 HIS   A CA   
987  C  C    . HIS   A 149 ? 0.25798 0.35983 0.21142 0.01512  0.06898  -0.03277 301 HIS   A C    
988  O  O    . HIS   A 149 ? 0.27953 0.38479 0.24068 0.01963  0.07059  -0.04494 301 HIS   A O    
989  C  CB   . HIS   A 149 ? 0.23547 0.30860 0.19082 0.00862  0.05221  -0.02427 301 HIS   A CB   
990  C  CG   . HIS   A 149 ? 0.21917 0.28108 0.18002 0.00378  0.04727  -0.01387 301 HIS   A CG   
991  N  ND1  . HIS   A 149 ? 0.23790 0.30212 0.19607 0.00016  0.05050  -0.00181 301 HIS   A ND1  
992  C  CD2  . HIS   A 149 ? 0.23504 0.28371 0.20427 0.00232  0.03984  -0.01400 301 HIS   A CD2  
993  C  CE1  . HIS   A 149 ? 0.22700 0.27972 0.19225 -0.00333 0.04490  0.00325  301 HIS   A CE1  
994  N  NE2  . HIS   A 149 ? 0.22985 0.27389 0.20051 -0.00197 0.03846  -0.00390 301 HIS   A NE2  
995  N  N    . THR   A 150 ? 0.25293 0.36420 0.18838 0.01483  0.07343  -0.02643 302 THR   A N    
996  C  CA   . THR   A 150 ? 0.28216 0.41074 0.20304 0.01964  0.08120  -0.03294 302 THR   A CA   
997  C  C    . THR   A 150 ? 0.28033 0.40865 0.18036 0.02170  0.07461  -0.03926 302 THR   A C    
998  O  O    . THR   A 150 ? 0.32305 0.43853 0.22118 0.01888  0.06515  -0.03654 302 THR   A O    
999  C  CB   . THR   A 150 ? 0.32750 0.47030 0.24325 0.01821  0.09268  -0.01870 302 THR   A CB   
1000 O  OG1  . THR   A 150 ? 0.33364 0.47115 0.23750 0.01481  0.08938  -0.00455 302 THR   A OG1  
1001 C  CG2  . THR   A 150 ? 0.36317 0.50619 0.30335 0.01483  0.09816  -0.01237 302 THR   A CG2  
1002 N  N    . LEU   A 151 ? 0.29101 0.43540 0.17562 0.02685  0.07978  -0.04846 303 LEU   A N    
1003 C  CA   . LEU   A 151 ? 0.32397 0.47138 0.18886 0.02926  0.07281  -0.05671 303 LEU   A CA   
1004 C  C    . LEU   A 151 ? 0.36539 0.51343 0.21472 0.02691  0.06966  -0.04076 303 LEU   A C    
1005 O  O    . LEU   A 151 ? 0.36329 0.50729 0.20355 0.02706  0.05983  -0.04505 303 LEU   A O    
1006 C  CB   . LEU   A 151 ? 0.37699 0.53678 0.23125 0.03456  0.07703  -0.06826 303 LEU   A CB   
1007 C  CG   . LEU   A 151 ? 0.46562 0.62339 0.33425 0.03817  0.07728  -0.08855 303 LEU   A CG   
1008 C  CD1  . LEU   A 151 ? 0.48490 0.65349 0.34462 0.04305  0.08182  -0.09849 303 LEU   A CD1  
1009 C  CD2  . LEU   A 151 ? 0.51434 0.65848 0.38948 0.03728  0.06567  -0.10172 303 LEU   A CD2  
1010 N  N    . GLU   A 152 ? 0.34544 0.49578 0.19559 0.02432  0.07689  -0.02201 304 GLU   A N    
1011 C  CA   . GLU   A 152 ? 0.37889 0.52497 0.21900 0.02217  0.07308  -0.00562 304 GLU   A CA   
1012 C  C    . GLU   A 152 ? 0.36075 0.49176 0.20736 0.01886  0.06235  -0.00444 304 GLU   A C    
1013 O  O    . GLU   A 152 ? 0.35731 0.48780 0.19242 0.01921  0.05637  0.00236  304 GLU   A O    
1014 C  CB   . GLU   A 152 ? 0.47655 0.62362 0.32263 0.01904  0.08284  0.01356  304 GLU   A CB   
1015 C  CG   . GLU   A 152 ? 0.68604 0.82857 0.52253 0.01789  0.08013  0.03047  304 GLU   A CG   
1016 C  CD   . GLU   A 152 ? 0.84749 1.00032 0.66562 0.02186  0.08262  0.03279  304 GLU   A CD   
1017 O  OE1  . GLU   A 152 ? 0.90755 1.05805 0.71752 0.02197  0.08034  0.04634  304 GLU   A OE1  
1018 O  OE2  . GLU   A 152 ? 0.88060 1.04404 0.69286 0.02522  0.08685  0.02102  304 GLU   A OE2  
1019 N  N    . LEU   A 153 ? 0.26661 0.38326 0.13352 0.01570  0.05894  -0.01037 305 LEU   A N    
1020 C  CA   . LEU   A 153 ? 0.32533 0.42571 0.19974 0.01267  0.04831  -0.01180 305 LEU   A CA   
1021 C  C    . LEU   A 153 ? 0.31053 0.40819 0.18513 0.01451  0.04108  -0.02971 305 LEU   A C    
1022 O  O    . LEU   A 153 ? 0.31295 0.40645 0.18324 0.01379  0.03276  -0.03202 305 LEU   A O    
1023 C  CB   . LEU   A 153 ? 0.30071 0.38693 0.19575 0.00827  0.04823  -0.00662 305 LEU   A CB   
1024 C  CG   . LEU   A 153 ? 0.25503 0.32506 0.15799 0.00554  0.03857  -0.00891 305 LEU   A CG   
1025 C  CD1  . LEU   A 153 ? 0.28141 0.34893 0.17567 0.00431  0.03411  0.00078  305 LEU   A CD1  
1026 C  CD2  . LEU   A 153 ? 0.25554 0.31429 0.17675 0.00239  0.03848  -0.00592 305 LEU   A CD2  
1027 N  N    . ILE   A 154 ? 0.29467 0.39498 0.17611 0.01695  0.04437  -0.04268 306 ILE   A N    
1028 C  CA   . ILE   A 154 ? 0.31509 0.40807 0.20352 0.01780  0.03775  -0.05926 306 ILE   A CA   
1029 C  C    . ILE   A 154 ? 0.28989 0.39265 0.16242 0.02031  0.03265  -0.06995 306 ILE   A C    
1030 O  O    . ILE   A 154 ? 0.32421 0.41892 0.20153 0.01857  0.02412  -0.07804 306 ILE   A O    
1031 C  CB   . ILE   A 154 ? 0.33823 0.43158 0.23958 0.02074  0.04295  -0.07019 306 ILE   A CB   
1032 C  CG1  . ILE   A 154 ? 0.32292 0.40573 0.24244 0.01814  0.04485  -0.06061 306 ILE   A CG1  
1033 C  CG2  . ILE   A 154 ? 0.32716 0.41307 0.23611 0.02221  0.03697  -0.08791 306 ILE   A CG2  
1034 C  CD1  . ILE   A 154 ? 0.34449 0.43067 0.27793 0.02181  0.05072  -0.06849 306 ILE   A CD1  
1035 N  N    . GLU   A 155 ? 0.30657 0.42784 0.16030 0.02437  0.03769  -0.07009 307 GLU   A N    
1036 C  CA   . GLU   A 155 ? 0.31430 0.44550 0.15299 0.02708  0.03140  -0.08008 307 GLU   A CA   
1037 C  C    . GLU   A 155 ? 0.34759 0.47602 0.18074 0.02465  0.02219  -0.07217 307 GLU   A C    
1038 O  O    . GLU   A 155 ? 0.38723 0.51285 0.22406 0.02375  0.01299  -0.08425 307 GLU   A O    
1039 C  CB   . GLU   A 155 ? 0.41622 0.56148 0.24055 0.03108  0.03787  -0.07641 307 GLU   A CB   
1040 C  CG   . GLU   A 155 ? 0.59596 0.74929 0.40945 0.03395  0.03104  -0.08806 307 GLU   A CG   
1041 C  CD   . GLU   A 155 ? 0.74589 0.91310 0.54635 0.03842  0.03856  -0.08866 307 GLU   A CD   
1042 O  OE1  . GLU   A 155 ? 0.81597 0.99247 0.59984 0.04020  0.03804  -0.07854 307 GLU   A OE1  
1043 O  OE2  . GLU   A 155 ? 0.80348 0.97234 0.61074 0.04047  0.04520  -0.09899 307 GLU   A OE2  
1044 N  N    . PRO   A 156 ? 0.35961 0.48829 0.18673 0.02346  0.02401  -0.05265 308 PRO   A N    
1045 C  CA   . PRO   A 156 ? 0.32724 0.45226 0.15266 0.02163  0.01491  -0.04602 308 PRO   A CA   
1046 C  C    . PRO   A 156 ? 0.34417 0.45052 0.19050 0.01651  0.00890  -0.05003 308 PRO   A C    
1047 O  O    . PRO   A 156 ? 0.32966 0.43458 0.17796 0.01520  0.00017  -0.05308 308 PRO   A O    
1048 C  CB   . PRO   A 156 ? 0.41183 0.53636 0.23251 0.02125  0.02006  -0.02334 308 PRO   A CB   
1049 C  CG   . PRO   A 156 ? 0.50215 0.63330 0.31872 0.02310  0.03091  -0.01885 308 PRO   A CG   
1050 C  CD   . PRO   A 156 ? 0.41178 0.54343 0.23615 0.02355  0.03432  -0.03570 308 PRO   A CD   
1051 N  N    . LEU   A 157 ? 0.28227 0.37544 0.14449 0.01380  0.01349  -0.04931 309 LEU   A N    
1052 C  CA   . LEU   A 157 ? 0.27277 0.34878 0.15312 0.00949  0.00873  -0.05184 309 LEU   A CA   
1053 C  C    . LEU   A 157 ? 0.24827 0.32318 0.13467 0.00927  0.00258  -0.06996 309 LEU   A C    
1054 O  O    . LEU   A 157 ? 0.28854 0.35658 0.18316 0.00607  -0.00407 -0.07182 309 LEU   A O    
1055 C  CB   . LEU   A 157 ? 0.23204 0.29695 0.12604 0.00796  0.01446  -0.04799 309 LEU   A CB   
1056 C  CG   . LEU   A 157 ? 0.21909 0.26678 0.12997 0.00435  0.01054  -0.04904 309 LEU   A CG   
1057 C  CD1  . LEU   A 157 ? 0.26013 0.30195 0.17148 0.00116  0.00573  -0.03959 309 LEU   A CD1  
1058 C  CD2  . LEU   A 157 ? 0.23720 0.27703 0.15925 0.00402  0.01539  -0.04433 309 LEU   A CD2  
1059 N  N    . ILE   A 158 ? 0.26005 0.34188 0.14420 0.01253  0.00517  -0.08410 310 ILE   A N    
1060 C  CA   . ILE   A 158 ? 0.29247 0.37327 0.18391 0.01229  -0.00072 -0.10329 310 ILE   A CA   
1061 C  C    . ILE   A 158 ? 0.30694 0.40021 0.18728 0.01259  -0.00897 -0.10838 310 ILE   A C    
1062 O  O    . ILE   A 158 ? 0.30460 0.39278 0.19653 0.00923  -0.01639 -0.11701 310 ILE   A O    
1063 C  CB   . ILE   A 158 ? 0.32567 0.41224 0.21690 0.01665  0.00422  -0.11870 310 ILE   A CB   
1064 C  CG1  . ILE   A 158 ? 0.33521 0.40843 0.24242 0.01645  0.01056  -0.11455 310 ILE   A CG1  
1065 C  CG2  . ILE   A 158 ? 0.35325 0.43972 0.25195 0.01654  -0.00235 -0.14051 310 ILE   A CG2  
1066 C  CD1  . ILE   A 158 ? 0.33936 0.39289 0.26830 0.01265  0.00625  -0.11764 310 ILE   A CD1  
1067 N  N    . LYS   A 159 ? 0.35024 0.46072 0.20894 0.01667  -0.00790 -0.10242 311 LYS   A N    
1068 C  CA   . LYS   A 159 ? 0.32316 0.44415 0.17390 0.01754  -0.01647 -0.10349 311 LYS   A CA   
1069 C  C    . LYS   A 159 ? 0.35363 0.46894 0.21211 0.01356  -0.02326 -0.09644 311 LYS   A C    
1070 O  O    . LYS   A 159 ? 0.35272 0.47154 0.21725 0.01199  -0.03220 -0.10484 311 LYS   A O    
1071 C  CB   . LYS   A 159 ? 0.39257 0.52711 0.22312 0.02234  -0.01313 -0.09092 311 LYS   A CB   
1072 C  CG   . LYS   A 159 ? 0.52652 0.67249 0.34932 0.02429  -0.02226 -0.09228 311 LYS   A CG   
1073 C  CD   . LYS   A 159 ? 0.57713 0.73385 0.38097 0.02881  -0.01928 -0.07579 311 LYS   A CD   
1074 C  CE   . LYS   A 159 ? 0.64378 0.81126 0.44147 0.03103  -0.02952 -0.07566 311 LYS   A CE   
1075 N  NZ   . LYS   A 159 ? 0.68182 0.85315 0.48855 0.02976  -0.03817 -0.09710 311 LYS   A NZ   
1076 N  N    . PHE   A 160 ? 0.32641 0.42946 0.19069 0.01129  -0.01834 -0.07875 312 PHE   A N    
1077 C  CA   . PHE   A 160 ? 0.31995 0.41391 0.19570 0.00745  -0.02284 -0.06974 312 PHE   A CA   
1078 C  C    . PHE   A 160 ? 0.30241 0.38386 0.19944 0.00231  -0.02626 -0.08076 312 PHE   A C    
1079 O  O    . PHE   A 160 ? 0.28073 0.36315 0.18650 -0.00030 -0.03307 -0.08330 312 PHE   A O    
1080 C  CB   . PHE   A 160 ? 0.28344 0.36663 0.16109 0.00638  -0.01622 -0.05098 312 PHE   A CB   
1081 C  CG   . PHE   A 160 ? 0.29209 0.36341 0.18374 0.00239  -0.01901 -0.04369 312 PHE   A CG   
1082 C  CD1  . PHE   A 160 ? 0.34262 0.41944 0.23110 0.00353  -0.02350 -0.03488 312 PHE   A CD1  
1083 C  CD2  . PHE   A 160 ? 0.27675 0.33218 0.18438 -0.00179 -0.01675 -0.04517 312 PHE   A CD2  
1084 C  CE1  . PHE   A 160 ? 0.31900 0.38611 0.22076 0.00039  -0.02509 -0.02912 312 PHE   A CE1  
1085 C  CE2  . PHE   A 160 ? 0.34105 0.38726 0.25971 -0.00503 -0.01829 -0.03863 312 PHE   A CE2  
1086 C  CZ   . PHE   A 160 ? 0.32184 0.37414 0.23787 -0.00402 -0.02212 -0.03130 312 PHE   A CZ   
1087 N  N    . GLN   A 161 ? 0.27994 0.34954 0.18710 0.00091  -0.02120 -0.08623 313 GLN   A N    
1088 C  CA   . GLN   A 161 ? 0.29188 0.34789 0.22003 -0.00384 -0.02339 -0.09425 313 GLN   A CA   
1089 C  C    . GLN   A 161 ? 0.27961 0.34385 0.21324 -0.00495 -0.03110 -0.11237 313 GLN   A C    
1090 O  O    . GLN   A 161 ? 0.28961 0.34902 0.23886 -0.00967 -0.03569 -0.11504 313 GLN   A O    
1091 C  CB   . GLN   A 161 ? 0.27478 0.31794 0.21214 -0.00365 -0.01720 -0.09707 313 GLN   A CB   
1092 C  CG   . GLN   A 161 ? 0.26567 0.30058 0.20144 -0.00320 -0.01074 -0.08093 313 GLN   A CG   
1093 C  CD   . GLN   A 161 ? 0.26130 0.28486 0.20586 -0.00724 -0.01157 -0.06896 313 GLN   A CD   
1094 O  OE1  . GLN   A 161 ? 0.27210 0.28810 0.22999 -0.01091 -0.01452 -0.07270 313 GLN   A OE1  
1095 N  NE2  . GLN   A 161 ? 0.26649 0.28907 0.20449 -0.00667 -0.00840 -0.05482 313 GLN   A NE2  
1096 N  N    . VAL   A 162 ? 0.26817 0.34591 0.18978 -0.00075 -0.03242 -0.12567 314 VAL   A N    
1097 C  CA   . VAL   A 162 ? 0.29786 0.38541 0.22411 -0.00153 -0.04085 -0.14557 314 VAL   A CA   
1098 C  C    . VAL   A 162 ? 0.30043 0.40016 0.22339 -0.00233 -0.04916 -0.14112 314 VAL   A C    
1099 O  O    . VAL   A 162 ? 0.29646 0.39558 0.23658 -0.00658 -0.05560 -0.14949 314 VAL   A O    
1100 C  CB   . VAL   A 162 ? 0.32617 0.42397 0.24031 0.00413  -0.03861 -0.15435 314 VAL   A CB   
1101 C  CG1  . VAL   A 162 ? 0.33691 0.44157 0.25969 0.00325  -0.04626 -0.16947 314 VAL   A CG1  
1102 C  CG2  . VAL   A 162 ? 0.35083 0.43766 0.27137 0.00542  -0.03075 -0.15991 314 VAL   A CG2  
1103 N  N    . GLY   A 163 ? 0.35465 0.46534 0.25767 0.00193  -0.04870 -0.12680 315 GLY   A N    
1104 C  CA   . GLY   A 163 ? 0.34173 0.46393 0.24246 0.00248  -0.05664 -0.12099 315 GLY   A CA   
1105 C  C    . GLY   A 163 ? 0.33105 0.44283 0.25245 -0.00339 -0.05861 -0.11504 315 GLY   A C    
1106 O  O    . GLY   A 163 ? 0.35135 0.47100 0.28409 -0.00577 -0.06703 -0.12188 315 GLY   A O    
1107 N  N    . LEU   A 164 ? 0.28377 0.37770 0.21179 -0.00575 -0.05023 -0.10162 316 LEU   A N    
1108 C  CA   . LEU   A 164 ? 0.24984 0.33228 0.19719 -0.01106 -0.04978 -0.09451 316 LEU   A CA   
1109 C  C    . LEU   A 164 ? 0.27265 0.34830 0.24301 -0.01716 -0.05222 -0.10902 316 LEU   A C    
1110 O  O    . LEU   A 164 ? 0.29205 0.36988 0.27859 -0.02127 -0.05655 -0.11054 316 LEU   A O    
1111 C  CB   . LEU   A 164 ? 0.24918 0.31508 0.19634 -0.01165 -0.04051 -0.07903 316 LEU   A CB   
1112 C  CG   . LEU   A 164 ? 0.27458 0.32895 0.23790 -0.01619 -0.03841 -0.07024 316 LEU   A CG   
1113 C  CD1  . LEU   A 164 ? 0.28047 0.34566 0.24422 -0.01508 -0.04343 -0.06396 316 LEU   A CD1  
1114 C  CD2  . LEU   A 164 ? 0.27563 0.31554 0.23609 -0.01601 -0.03021 -0.05740 316 LEU   A CD2  
1115 N  N    . LYS   A 165 ? 0.31815 0.38542 0.29239 -0.01784 -0.04907 -0.11962 317 LYS   A N    
1116 C  CA   . LYS   A 165 ? 0.32611 0.38399 0.32468 -0.02378 -0.05049 -0.13258 317 LYS   A CA   
1117 C  C    . LYS   A 165 ? 0.40772 0.48120 0.41480 -0.02583 -0.06084 -0.14915 317 LYS   A C    
1118 O  O    . LYS   A 165 ? 0.45353 0.52288 0.48470 -0.03235 -0.06334 -0.15413 317 LYS   A O    
1119 C  CB   . LYS   A 165 ? 0.33006 0.37719 0.33062 -0.02252 -0.04579 -0.14183 317 LYS   A CB   
1120 C  CG   . LYS   A 165 ? 0.32231 0.35104 0.34983 -0.02846 -0.04340 -0.14700 317 LYS   A CG   
1121 C  CD   . LYS   A 165 ? 0.33587 0.34690 0.36863 -0.03008 -0.03545 -0.12819 317 LYS   A CD   
1122 C  CE   . LYS   A 165 ? 0.39410 0.38655 0.45206 -0.03489 -0.03247 -0.13191 317 LYS   A CE   
1123 N  NZ   . LYS   A 165 ? 0.31042 0.28694 0.37177 -0.03581 -0.02521 -0.11329 317 LYS   A NZ   
1124 N  N    . LYS   A 166 ? 0.40622 0.49819 0.39410 -0.02012 -0.06639 -0.15602 318 LYS   A N    
1125 C  CA   . LYS   A 166 ? 0.37877 0.48429 0.37256 -0.02006 -0.07452 -0.16590 318 LYS   A CA   
1126 C  C    . LYS   A 166 ? 0.36696 0.48318 0.36775 -0.02196 -0.08108 -0.15938 318 LYS   A C    
1127 O  O    . LYS   A 166 ? 0.40649 0.53323 0.41743 -0.02304 -0.08818 -0.16783 318 LYS   A O    
1128 C  CB   . LYS   A 166 ? 0.38895 0.50938 0.35849 -0.01228 -0.07639 -0.16980 318 LYS   A CB   
1129 C  CG   . LYS   A 166 ? 0.41576 0.52917 0.38352 -0.01041 -0.07109 -0.18064 318 LYS   A CG   
1130 C  CD   . LYS   A 166 ? 0.47602 0.60631 0.42256 -0.00337 -0.07322 -0.18633 318 LYS   A CD   
1131 C  CE   . LYS   A 166 ? 0.52844 0.65319 0.47729 -0.00169 -0.06847 -0.19969 318 LYS   A CE   
1132 N  NZ   . LYS   A 166 ? 0.58507 0.72634 0.51001 0.00567  -0.06827 -0.20293 318 LYS   A NZ   
1133 N  N    . LEU   A 167 ? 0.34224 0.45690 0.33905 -0.02208 -0.07898 -0.14505 319 LEU   A N    
1134 C  CA   . LEU   A 167 ? 0.31980 0.44223 0.32847 -0.02388 -0.08346 -0.13758 319 LEU   A CA   
1135 C  C    . LEU   A 167 ? 0.31447 0.42616 0.35540 -0.03291 -0.08151 -0.14128 319 LEU   A C    
1136 O  O    . LEU   A 167 ? 0.29619 0.41772 0.35254 -0.03538 -0.08636 -0.14040 319 LEU   A O    
1137 C  CB   . LEU   A 167 ? 0.29422 0.41233 0.28961 -0.01971 -0.07751 -0.11487 319 LEU   A CB   
1138 C  CG   . LEU   A 167 ? 0.32285 0.45229 0.28896 -0.01099 -0.07893 -0.10638 319 LEU   A CG   
1139 C  CD1  . LEU   A 167 ? 0.35812 0.48032 0.31821 -0.00830 -0.07289 -0.08487 319 LEU   A CD1  
1140 C  CD2  . LEU   A 167 ? 0.33319 0.48767 0.29198 -0.00659 -0.09158 -0.11522 319 LEU   A CD2  
1141 N  N    A ASN   A 168 ? 0.29385 0.38658 0.34618 -0.03753 -0.07444 -0.14499 320 ASN   A N    
1142 N  N    B ASN   A 168 ? 0.28531 0.37756 0.33744 -0.03749 -0.07406 -0.14402 320 ASN   A N    
1143 C  CA   A ASN   A 168 ? 0.31866 0.39777 0.40067 -0.04608 -0.06992 -0.14468 320 ASN   A CA   
1144 C  CA   B ASN   A 168 ? 0.31954 0.39957 0.40217 -0.04619 -0.07043 -0.14526 320 ASN   A CA   
1145 C  C    A ASN   A 168 ? 0.30310 0.38395 0.39317 -0.04773 -0.06704 -0.12907 320 ASN   A C    
1146 C  C    B ASN   A 168 ? 0.30233 0.38277 0.39318 -0.04797 -0.06685 -0.12901 320 ASN   A C    
1147 O  O    A ASN   A 168 ? 0.30195 0.39206 0.41376 -0.05249 -0.07117 -0.13348 320 ASN   A O    
1148 O  O    B ASN   A 168 ? 0.30642 0.39486 0.41992 -0.05308 -0.07028 -0.13288 320 ASN   A O    
1149 C  CB   A ASN   A 168 ? 0.37046 0.45330 0.47442 -0.05079 -0.07524 -0.16144 320 ASN   A CB   
1150 C  CB   B ASN   A 168 ? 0.37053 0.45744 0.47279 -0.05004 -0.07693 -0.16202 320 ASN   A CB   
1151 C  CG   A ASN   A 168 ? 0.38927 0.45404 0.52270 -0.05926 -0.06808 -0.15961 320 ASN   A CG   
1152 C  CG   B ASN   A 168 ? 0.35996 0.44638 0.45058 -0.04571 -0.07841 -0.17457 320 ASN   A CG   
1153 O  OD1  A ASN   A 168 ? 0.40778 0.45426 0.54456 -0.06035 -0.06159 -0.15974 320 ASN   A OD1  
1154 O  OD1  B ASN   A 168 ? 0.34085 0.41293 0.42588 -0.04455 -0.07220 -0.17474 320 ASN   A OD1  
1155 N  ND2  A ASN   A 168 ? 0.41416 0.48430 0.56914 -0.06471 -0.06860 -0.15637 320 ASN   A ND2  
1156 N  ND2  B ASN   A 168 ? 0.41491 0.51774 0.50264 -0.04297 -0.08653 -0.18534 320 ASN   A ND2  
1157 N  N    . LEU   A 169 ? 0.29143 0.36418 0.36447 -0.04352 -0.05983 -0.11157 321 LEU   A N    
1158 C  CA   . LEU   A 169 ? 0.27397 0.34718 0.35218 -0.04391 -0.05591 -0.09699 321 LEU   A CA   
1159 C  C    . LEU   A 169 ? 0.27624 0.33743 0.37971 -0.05180 -0.04871 -0.09413 321 LEU   A C    
1160 O  O    . LEU   A 169 ? 0.26920 0.31385 0.37803 -0.05509 -0.04284 -0.09466 321 LEU   A O    
1161 C  CB   . LEU   A 169 ? 0.23148 0.29667 0.28695 -0.03806 -0.04951 -0.08090 321 LEU   A CB   
1162 C  CG   . LEU   A 169 ? 0.23829 0.31436 0.26892 -0.03017 -0.05429 -0.07859 321 LEU   A CG   
1163 C  CD1  . LEU   A 169 ? 0.26008 0.32630 0.27500 -0.02613 -0.04697 -0.06225 321 LEU   A CD1  
1164 C  CD2  . LEU   A 169 ? 0.23307 0.32986 0.26622 -0.02745 -0.06384 -0.08136 321 LEU   A CD2  
1165 N  N    . HIS   A 170 ? 0.22843 0.29856 0.34807 -0.05443 -0.04879 -0.09032 322 HIS   A N    
1166 C  CA   . HIS   A 170 ? 0.21911 0.27827 0.35700 -0.06039 -0.03889 -0.08158 322 HIS   A CA   
1167 C  C    . HIS   A 170 ? 0.27083 0.31560 0.38961 -0.05644 -0.02952 -0.06561 322 HIS   A C    
1168 O  O    . HIS   A 170 ? 0.27047 0.31749 0.36684 -0.04954 -0.03100 -0.06006 322 HIS   A O    
1169 C  CB   . HIS   A 170 ? 0.19488 0.26918 0.35236 -0.06277 -0.03996 -0.08000 322 HIS   A CB   
1170 C  CG   . HIS   A 170 ? 0.22557 0.31661 0.40489 -0.06695 -0.05015 -0.09613 322 HIS   A CG   
1171 N  ND1  . HIS   A 170 ? 0.22918 0.33641 0.43169 -0.06987 -0.05236 -0.09737 322 HIS   A ND1  
1172 C  CD2  . HIS   A 170 ? 0.24171 0.33725 0.42414 -0.06853 -0.05918 -0.11297 322 HIS   A CD2  
1173 C  CE1  . HIS   A 170 ? 0.28364 0.40491 0.50330 -0.07342 -0.06307 -0.11421 322 HIS   A CE1  
1174 N  NE2  . HIS   A 170 ? 0.28549 0.39979 0.49265 -0.07265 -0.06746 -0.12443 322 HIS   A NE2  
1175 N  N    . GLU   A 171 ? 0.19773 0.22793 0.32587 -0.06086 -0.01988 -0.05794 323 GLU   A N    
1176 C  CA   . GLU   A 171 ? 0.23284 0.25116 0.34277 -0.05693 -0.01195 -0.04383 323 GLU   A CA   
1177 C  C    . GLU   A 171 ? 0.21671 0.24456 0.31867 -0.05256 -0.01087 -0.03581 323 GLU   A C    
1178 O  O    . GLU   A 171 ? 0.20313 0.22662 0.28476 -0.04696 -0.00919 -0.02857 323 GLU   A O    
1179 C  CB   . GLU   A 171 ? 0.23652 0.23995 0.35736 -0.06182 -0.00207 -0.03577 323 GLU   A CB   
1180 C  CG   . GLU   A 171 ? 0.26743 0.25884 0.36726 -0.05712 0.00412  -0.02352 323 GLU   A CG   
1181 C  CD   . GLU   A 171 ? 0.31123 0.28736 0.41809 -0.06054 0.01258  -0.01510 323 GLU   A CD   
1182 O  OE1  . GLU   A 171 ? 0.38734 0.36383 0.51467 -0.06657 0.01777  -0.01266 323 GLU   A OE1  
1183 O  OE2  . GLU   A 171 ? 0.36984 0.33426 0.46247 -0.05700 0.01412  -0.01023 323 GLU   A OE2  
1184 N  N    . GLU   A 172 ? 0.19385 0.23509 0.31392 -0.05502 -0.01199 -0.03783 324 GLU   A N    
1185 C  CA   . GLU   A 172 ? 0.16838 0.22042 0.28441 -0.05008 -0.01209 -0.03219 324 GLU   A CA   
1186 C  C    . GLU   A 172 ? 0.18273 0.23997 0.27823 -0.04250 -0.01991 -0.03296 324 GLU   A C    
1187 O  O    . GLU   A 172 ? 0.17305 0.22789 0.25466 -0.03704 -0.01734 -0.02471 324 GLU   A O    
1188 C  CB   . GLU   A 172 ? 0.17520 0.24409 0.31731 -0.05365 -0.01468 -0.03743 324 GLU   A CB   
1189 C  CG   . GLU   A 172 ? 0.17144 0.23716 0.33535 -0.06092 -0.00452 -0.03354 324 GLU   A CG   
1190 C  CD   . GLU   A 172 ? 0.18576 0.24613 0.36884 -0.06941 -0.00499 -0.04129 324 GLU   A CD   
1191 O  OE1  . GLU   A 172 ? 0.20457 0.26728 0.41250 -0.07634 0.00152  -0.03985 324 GLU   A OE1  
1192 O  OE2  . GLU   A 172 ? 0.19008 0.24379 0.36492 -0.06923 -0.01109 -0.04881 324 GLU   A OE2  
1193 N  N    . GLU   A 173 ? 0.19923 0.26425 0.29334 -0.04209 -0.02934 -0.04306 325 GLU   A N    
1194 C  CA   . GLU   A 173 ? 0.18186 0.25335 0.25597 -0.03483 -0.03629 -0.04263 325 GLU   A CA   
1195 C  C    . GLU   A 173 ? 0.19665 0.25358 0.24873 -0.03190 -0.03187 -0.03673 325 GLU   A C    
1196 O  O    . GLU   A 173 ? 0.19363 0.25079 0.23002 -0.02606 -0.03222 -0.02957 325 GLU   A O    
1197 C  CB   . GLU   A 173 ? 0.19169 0.27688 0.26827 -0.03495 -0.04720 -0.05573 325 GLU   A CB   
1198 C  CG   . GLU   A 173 ? 0.20228 0.30632 0.29955 -0.03618 -0.05418 -0.06160 325 GLU   A CG   
1199 C  CD   . GLU   A 173 ? 0.24432 0.35891 0.35421 -0.04047 -0.06315 -0.07833 325 GLU   A CD   
1200 O  OE1  . GLU   A 173 ? 0.22168 0.35400 0.34996 -0.04166 -0.07052 -0.08497 325 GLU   A OE1  
1201 O  OE2  . GLU   A 173 ? 0.23157 0.33742 0.33458 -0.04252 -0.06311 -0.08586 325 GLU   A OE2  
1202 N  N    . HIS   A 174 ? 0.19189 0.23599 0.24491 -0.03593 -0.02757 -0.03929 326 HIS   A N    
1203 C  CA   . HIS   A 174 ? 0.22792 0.25912 0.26330 -0.03341 -0.02350 -0.03443 326 HIS   A CA   
1204 C  C    . HIS   A 174 ? 0.20744 0.23107 0.23503 -0.03096 -0.01687 -0.02232 326 HIS   A C    
1205 O  O    . HIS   A 174 ? 0.19945 0.22037 0.21128 -0.02652 -0.01657 -0.01728 326 HIS   A O    
1206 C  CB   . HIS   A 174 ? 0.20902 0.22838 0.25182 -0.03799 -0.02038 -0.03931 326 HIS   A CB   
1207 C  CG   . HIS   A 174 ? 0.25319 0.26030 0.28145 -0.03540 -0.01664 -0.03527 326 HIS   A CG   
1208 N  ND1  . HIS   A 174 ? 0.28961 0.29945 0.30359 -0.03144 -0.01987 -0.03925 326 HIS   A ND1  
1209 C  CD2  . HIS   A 174 ? 0.22749 0.22092 0.25426 -0.03605 -0.01007 -0.02781 326 HIS   A CD2  
1210 C  CE1  . HIS   A 174 ? 0.26904 0.26757 0.27544 -0.03002 -0.01538 -0.03478 326 HIS   A CE1  
1211 N  NE2  . HIS   A 174 ? 0.24788 0.23635 0.26147 -0.03255 -0.01010 -0.02792 326 HIS   A NE2  
1212 N  N    . VAL   A 175 ? 0.17314 0.19414 0.21227 -0.03386 -0.01125 -0.01800 327 VAL   A N    
1213 C  CA   . VAL   A 175 ? 0.17496 0.18934 0.20572 -0.03125 -0.00499 -0.00852 327 VAL   A CA   
1214 C  C    . VAL   A 175 ? 0.15505 0.17809 0.18262 -0.02627 -0.00740 -0.00546 327 VAL   A C    
1215 O  O    . VAL   A 175 ? 0.15741 0.17497 0.17383 -0.02257 -0.00490 0.00024  327 VAL   A O    
1216 C  CB   . VAL   A 175 ? 0.18663 0.19621 0.22809 -0.03521 0.00292  -0.00439 327 VAL   A CB   
1217 C  CG1  . VAL   A 175 ? 0.18713 0.18600 0.23235 -0.03949 0.00542  -0.00538 327 VAL   A CG1  
1218 C  CG2  . VAL   A 175 ? 0.16584 0.18763 0.22674 -0.03783 0.00307  -0.00674 327 VAL   A CG2  
1219 N  N    . LEU   A 176 ? 0.17330 0.20993 0.21208 -0.02589 -0.01267 -0.00939 328 LEU   A N    
1220 C  CA   . LEU   A 176 ? 0.18576 0.23057 0.22190 -0.01995 -0.01618 -0.00583 328 LEU   A CA   
1221 C  C    . LEU   A 176 ? 0.19825 0.24102 0.21658 -0.01547 -0.02027 -0.00342 328 LEU   A C    
1222 O  O    . LEU   A 176 ? 0.18661 0.22615 0.19766 -0.01091 -0.01902 0.00331  328 LEU   A O    
1223 C  CB   . LEU   A 176 ? 0.16738 0.22908 0.21988 -0.01993 -0.02249 -0.01079 328 LEU   A CB   
1224 C  CG   . LEU   A 176 ? 0.15995 0.22682 0.23237 -0.02254 -0.01725 -0.01050 328 LEU   A CG   
1225 C  CD1  . LEU   A 176 ? 0.16889 0.25313 0.26134 -0.02462 -0.02410 -0.01788 328 LEU   A CD1  
1226 C  CD2  . LEU   A 176 ? 0.16482 0.23101 0.23581 -0.01685 -0.01300 -0.00352 328 LEU   A CD2  
1227 N  N    . LEU   A 177 ? 0.17120 0.21560 0.18326 -0.01680 -0.02445 -0.00903 329 LEU   A N    
1228 C  CA   . LEU   A 177 ? 0.19225 0.23667 0.18729 -0.01259 -0.02712 -0.00624 329 LEU   A CA   
1229 C  C    . LEU   A 177 ? 0.18753 0.21786 0.17216 -0.01213 -0.02065 0.00007  329 LEU   A C    
1230 O  O    . LEU   A 177 ? 0.19064 0.21965 0.16592 -0.00821 -0.02046 0.00664  329 LEU   A O    
1231 C  CB   . LEU   A 177 ? 0.20335 0.25362 0.19380 -0.01390 -0.03201 -0.01531 329 LEU   A CB   
1232 C  CG   . LEU   A 177 ? 0.24009 0.29473 0.21244 -0.00915 -0.03459 -0.01282 329 LEU   A CG   
1233 C  CD1  . LEU   A 177 ? 0.23443 0.30063 0.20307 -0.00333 -0.03977 -0.00630 329 LEU   A CD1  
1234 C  CD2  . LEU   A 177 ? 0.25883 0.31941 0.22682 -0.01044 -0.03839 -0.02420 329 LEU   A CD2  
1235 N  N    . MET   A 178 ? 0.17955 0.19960 0.16667 -0.01605 -0.01555 -0.00140 330 MET   A N    
1236 C  CA   . MET   A 178 ? 0.15544 0.16403 0.13390 -0.01537 -0.01060 0.00378  330 MET   A CA   
1237 C  C    . MET   A 178 ? 0.16420 0.17041 0.14369 -0.01275 -0.00800 0.00991  330 MET   A C    
1238 O  O    . MET   A 178 ? 0.19226 0.19336 0.16464 -0.01048 -0.00669 0.01435  330 MET   A O    
1239 C  CB   . MET   A 178 ? 0.15427 0.15360 0.13529 -0.01914 -0.00652 0.00187  330 MET   A CB   
1240 C  CG   . MET   A 178 ? 0.17212 0.17066 0.15255 -0.02099 -0.00844 -0.00450 330 MET   A CG   
1241 S  SD   . MET   A 178 ? 0.22079 0.20631 0.20443 -0.02392 -0.00359 -0.00389 330 MET   A SD   
1242 C  CE   . MET   A 178 ? 0.19715 0.18346 0.19589 -0.02800 -0.00084 -0.00333 330 MET   A CE   
1243 N  N    . ALA   A 179 ? 0.15204 0.16225 0.14222 -0.01311 -0.00690 0.00951  331 ALA   A N    
1244 C  CA   . ALA   A 179 ? 0.17261 0.18083 0.16511 -0.01002 -0.00397 0.01358  331 ALA   A CA   
1245 C  C    . ALA   A 179 ? 0.18601 0.19833 0.17713 -0.00500 -0.00791 0.01775  331 ALA   A C    
1246 O  O    . ALA   A 179 ? 0.20919 0.21473 0.19733 -0.00236 -0.00585 0.02177  331 ALA   A O    
1247 C  CB   . ALA   A 179 ? 0.17235 0.18597 0.17786 -0.01118 -0.00102 0.01186  331 ALA   A CB   
1248 N  N    . ILE   A 180 ? 0.18996 0.21346 0.18380 -0.00349 -0.01386 0.01691  332 ILE   A N    
1249 C  CA   . ILE   A 180 ? 0.18311 0.21137 0.17414 0.00207  -0.01810 0.02288  332 ILE   A CA   
1250 C  C    . ILE   A 180 ? 0.21811 0.23885 0.19599 0.00274  -0.01676 0.02776  332 ILE   A C    
1251 O  O    . ILE   A 180 ? 0.20286 0.21933 0.17960 0.00640  -0.01594 0.03509  332 ILE   A O    
1252 C  CB   . ILE   A 180 ? 0.19550 0.23934 0.18929 0.00362  -0.02585 0.02018  332 ILE   A CB   
1253 C  CG1  . ILE   A 180 ? 0.16461 0.21748 0.17585 0.00359  -0.02717 0.01656  332 ILE   A CG1  
1254 C  CG2  . ILE   A 180 ? 0.17603 0.22517 0.16171 0.00977  -0.03055 0.02804  332 ILE   A CG2  
1255 C  CD1  . ILE   A 180 ? 0.18673 0.25568 0.20436 0.00268  -0.03503 0.00989  332 ILE   A CD1  
1256 N  N    . CYS   A 181 ? 0.17228 0.19110 0.14218 -0.00085 -0.01601 0.02379  333 CYS   A N    
1257 C  CA   . CYS   A 181 ? 0.20851 0.22172 0.16787 -0.00073 -0.01377 0.02771  333 CYS   A CA   
1258 C  C    . CYS   A 181 ? 0.21933 0.22046 0.18084 -0.00105 -0.00883 0.03150  333 CYS   A C    
1259 O  O    . CYS   A 181 ? 0.20719 0.20469 0.16636 0.00085  -0.00751 0.03823  333 CYS   A O    
1260 C  CB   . CYS   A 181 ? 0.19811 0.21119 0.15192 -0.00433 -0.01323 0.02101  333 CYS   A CB   
1261 S  SG   . CYS   A 181 ? 0.24318 0.25155 0.18674 -0.00448 -0.00953 0.02450  333 CYS   A SG   
1262 N  N    . ILE   A 182 ? 0.19773 0.19301 0.16414 -0.00345 -0.00599 0.02720  334 ILE   A N    
1263 C  CA   . ILE   A 182 ? 0.17298 0.15813 0.14048 -0.00378 -0.00218 0.02819  334 ILE   A CA   
1264 C  C    . ILE   A 182 ? 0.21540 0.19826 0.18994 0.00007  -0.00190 0.03241  334 ILE   A C    
1265 O  O    . ILE   A 182 ? 0.21545 0.19115 0.19093 0.00073  -0.00035 0.03586  334 ILE   A O    
1266 C  CB   . ILE   A 182 ? 0.18485 0.16648 0.15346 -0.00636 0.00054  0.02287  334 ILE   A CB   
1267 C  CG1  . ILE   A 182 ? 0.17366 0.15414 0.13649 -0.00957 0.00059  0.02010  334 ILE   A CG1  
1268 C  CG2  . ILE   A 182 ? 0.22023 0.19408 0.19001 -0.00557 0.00344  0.02222  334 ILE   A CG2  
1269 C  CD1  . ILE   A 182 ? 0.18353 0.16244 0.14789 -0.01187 0.00282  0.01692  334 ILE   A CD1  
1270 N  N    A VAL   A 183 ? 0.20104 0.18971 0.18310 0.00266  -0.00322 0.03188  335 VAL   A N    
1271 N  N    B VAL   A 183 ? 0.20058 0.18945 0.18245 0.00263  -0.00332 0.03192  335 VAL   A N    
1272 C  CA   A VAL   A 183 ? 0.20196 0.18772 0.19301 0.00720  -0.00267 0.03517  335 VAL   A CA   
1273 C  CA   B VAL   A 183 ? 0.19683 0.18357 0.18793 0.00722  -0.00295 0.03508  335 VAL   A CA   
1274 C  C    A VAL   A 183 ? 0.22382 0.21423 0.21567 0.01151  -0.00667 0.04362  335 VAL   A C    
1275 C  C    B VAL   A 183 ? 0.22388 0.21537 0.21517 0.01139  -0.00703 0.04347  335 VAL   A C    
1276 O  O    A VAL   A 183 ? 0.25550 0.25293 0.25517 0.01592  -0.00959 0.04572  335 VAL   A O    
1277 O  O    B VAL   A 183 ? 0.24392 0.24387 0.24188 0.01543  -0.01047 0.04533  335 VAL   A O    
1278 C  CB   A VAL   A 183 ? 0.19616 0.18628 0.19703 0.00885  -0.00115 0.03055  335 VAL   A CB   
1279 C  CB   B VAL   A 183 ? 0.20418 0.19646 0.20478 0.00852  -0.00177 0.03037  335 VAL   A CB   
1280 C  CG1  A VAL   A 183 ? 0.21574 0.19960 0.21460 0.00620  0.00404  0.02426  335 VAL   A CG1  
1281 C  CG1  B VAL   A 183 ? 0.18489 0.17271 0.19588 0.01338  0.00021  0.03109  335 VAL   A CG1  
1282 C  CG2  A VAL   A 183 ? 0.17961 0.18229 0.18320 0.00783  -0.00420 0.02861  335 VAL   A CG2  
1283 C  CG2  B VAL   A 183 ? 0.20770 0.19811 0.20453 0.00399  0.00228  0.02396  335 VAL   A CG2  
1284 N  N    . SER   A 184 ? 0.22091 0.20830 0.20502 0.01072  -0.00661 0.04923  336 SER   A N    
1285 C  CA   . SER   A 184 ? 0.24952 0.24088 0.23189 0.01514  -0.00938 0.05952  336 SER   A CA   
1286 C  C    . SER   A 184 ? 0.25702 0.23664 0.24800 0.01764  -0.00646 0.06673  336 SER   A C    
1287 O  O    . SER   A 184 ? 0.24683 0.21641 0.23827 0.01399  -0.00237 0.06596  336 SER   A O    
1288 C  CB   . SER   A 184 ? 0.31714 0.31368 0.28592 0.01317  -0.00986 0.06235  336 SER   A CB   
1289 O  OG   . SER   A 184 ? 0.33651 0.34323 0.29935 0.01115  -0.01303 0.05441  336 SER   A OG   
1290 N  N    . PRO   A 185 ? 0.23517 0.21556 0.23512 0.02385  -0.00870 0.07343  337 PRO   A N    
1291 C  CA   . PRO   A 185 ? 0.25023 0.21710 0.26205 0.02633  -0.00561 0.07941  337 PRO   A CA   
1292 C  C    . PRO   A 185 ? 0.33088 0.29232 0.33887 0.02575  -0.00339 0.09156  337 PRO   A C    
1293 O  O    . PRO   A 185 ? 0.34513 0.29294 0.36413 0.02521  0.00043  0.09500  337 PRO   A O    
1294 C  CB   . PRO   A 185 ? 0.28288 0.25390 0.30608 0.03417  -0.00924 0.08357  337 PRO   A CB   
1295 C  CG   . PRO   A 185 ? 0.32089 0.30954 0.33442 0.03623  -0.01538 0.08546  337 PRO   A CG   
1296 C  CD   . PRO   A 185 ? 0.27544 0.26911 0.27781 0.02907  -0.01453 0.07481  337 PRO   A CD   
1297 N  N    . ASP   A 186 ? 0.31698 0.28888 0.31053 0.02565  -0.00511 0.09767  338 ASP   A N    
1298 C  CA   . ASP   A 186 ? 0.35540 0.32426 0.34455 0.02559  -0.00175 0.11101  338 ASP   A CA   
1299 C  C    . ASP   A 186 ? 0.43074 0.39525 0.41576 0.01810  0.00363  0.10675  338 ASP   A C    
1300 O  O    . ASP   A 186 ? 0.51267 0.47911 0.49120 0.01710  0.00714  0.11639  338 ASP   A O    
1301 C  CB   . ASP   A 186 ? 0.42669 0.41087 0.40094 0.03046  -0.00589 0.12055  338 ASP   A CB   
1302 C  CG   . ASP   A 186 ? 0.47988 0.47890 0.44087 0.02862  -0.01022 0.10904  338 ASP   A CG   
1303 O  OD1  . ASP   A 186 ? 0.50633 0.51790 0.45201 0.03048  -0.01225 0.11342  338 ASP   A OD1  
1304 O  OD2  . ASP   A 186 ? 0.47521 0.47350 0.44122 0.02545  -0.01134 0.09563  338 ASP   A OD2  
1305 N  N    . ARG   A 187 ? 0.34872 0.30848 0.33761 0.01328  0.00454  0.09315  339 ARG   A N    
1306 C  CA   . ARG   A 187 ? 0.32834 0.28440 0.31597 0.00688  0.00876  0.08909  339 ARG   A CA   
1307 C  C    . ARG   A 187 ? 0.44102 0.38365 0.44363 0.00481  0.01336  0.09489  339 ARG   A C    
1308 O  O    . ARG   A 187 ? 0.34886 0.28162 0.36497 0.00718  0.01302  0.09519  339 ARG   A O    
1309 C  CB   . ARG   A 187 ? 0.26846 0.22401 0.25532 0.00323  0.00758  0.07400  339 ARG   A CB   
1310 C  CG   . ARG   A 187 ? 0.31145 0.27815 0.28763 0.00428  0.00370  0.06778  339 ARG   A CG   
1311 C  CD   . ARG   A 187 ? 0.36178 0.33826 0.32503 0.00295  0.00378  0.06899  339 ARG   A CD   
1312 N  NE   . ARG   A 187 ? 0.42515 0.40911 0.38192 0.00215  0.00052  0.05942  339 ARG   A NE   
1313 C  CZ   . ARG   A 187 ? 0.36889 0.36110 0.31568 0.00101  -0.00007 0.05629  339 ARG   A CZ   
1314 N  NH1  . ARG   A 187 ? 0.40787 0.40364 0.34816 0.00091  0.00286  0.06189  339 ARG   A NH1  
1315 N  NH2  . ARG   A 187 ? 0.26523 0.26222 0.20968 -0.00000 -0.00300 0.04740  339 ARG   A NH2  
1316 N  N    . PRO   A 188 ? 0.50008 0.44225 0.50273 0.00029  0.01798  0.09890  340 PRO   A N    
1317 C  CA   . PRO   A 188 ? 0.46488 0.39444 0.48509 -0.00276 0.02265  0.10442  340 PRO   A CA   
1318 C  C    . PRO   A 188 ? 0.39185 0.31156 0.42504 -0.00596 0.02123  0.09005  340 PRO   A C    
1319 O  O    . PRO   A 188 ? 0.39360 0.31764 0.42076 -0.00871 0.01916  0.07759  340 PRO   A O    
1320 C  CB   . PRO   A 188 ? 0.55101 0.48634 0.56763 -0.00751 0.02799  0.10950  340 PRO   A CB   
1321 C  CG   . PRO   A 188 ? 0.59189 0.53914 0.59275 -0.00837 0.02524  0.09878  340 PRO   A CG   
1322 C  CD   . PRO   A 188 ? 0.56533 0.51816 0.55510 -0.00283 0.01939  0.09601  340 PRO   A CD   
1323 N  N    . GLY   A 189 ? 0.40489 0.31149 0.45566 -0.00491 0.02211  0.09168  341 GLY   A N    
1324 C  CA   . GLY   A 189 ? 0.41987 0.31738 0.48323 -0.00742 0.02074  0.07704  341 GLY   A CA   
1325 C  C    . GLY   A 189 ? 0.37344 0.27027 0.43518 -0.00237 0.01694  0.06737  341 GLY   A C    
1326 O  O    . GLY   A 189 ? 0.35820 0.24768 0.42981 -0.00334 0.01615  0.05491  341 GLY   A O    
1327 N  N    . VAL   A 190 ? 0.29558 0.20111 0.34576 0.00297  0.01465  0.07188  342 VAL   A N    
1328 C  CA   . VAL   A 190 ? 0.26643 0.17274 0.31773 0.00779  0.01208  0.06355  342 VAL   A CA   
1329 C  C    . VAL   A 190 ? 0.28254 0.17572 0.35360 0.01173  0.01324  0.06516  342 VAL   A C    
1330 O  O    . VAL   A 190 ? 0.29257 0.18001 0.37214 0.01423  0.01458  0.07917  342 VAL   A O    
1331 C  CB   . VAL   A 190 ? 0.26250 0.18188 0.30125 0.01229  0.00911  0.06875  342 VAL   A CB   
1332 C  CG1  . VAL   A 190 ? 0.25436 0.17477 0.29965 0.01801  0.00739  0.06316  342 VAL   A CG1  
1333 C  CG2  . VAL   A 190 ? 0.27188 0.20227 0.29398 0.00831  0.00794  0.06291  342 VAL   A CG2  
1334 N  N    . GLN   A 191 ? 0.26123 0.14947 0.33976 0.01267  0.01305  0.05091  343 GLN   A N    
1335 C  CA   . GLN   A 191 ? 0.26145 0.13635 0.36064 0.01666  0.01428  0.04870  343 GLN   A CA   
1336 C  C    . GLN   A 191 ? 0.29198 0.17084 0.39446 0.02515  0.01303  0.04933  343 GLN   A C    
1337 O  O    . GLN   A 191 ? 0.37863 0.25070 0.49473 0.03081  0.01313  0.05957  343 GLN   A O    
1338 C  CB   . GLN   A 191 ? 0.36339 0.23112 0.46994 0.01312  0.01486  0.03055  343 GLN   A CB   
1339 C  CG   . GLN   A 191 ? 0.45611 0.31910 0.56611 0.00499  0.01550  0.02910  343 GLN   A CG   
1340 C  CD   . GLN   A 191 ? 0.60787 0.45865 0.73602 0.00354  0.01828  0.04291  343 GLN   A CD   
1341 O  OE1  . GLN   A 191 ? 0.65235 0.48964 0.80067 0.00664  0.01955  0.04296  343 GLN   A OE1  
1342 N  NE2  . GLN   A 191 ? 0.60989 0.46526 0.73172 -0.00095 0.01990  0.05513  343 GLN   A NE2  
1343 N  N    . ASP   A 192 ? 0.26705 0.15727 0.35859 0.02630  0.01209  0.03928  344 ASP   A N    
1344 C  CA   . ASP   A 192 ? 0.27600 0.17288 0.37214 0.03387  0.01134  0.03872  344 ASP   A CA   
1345 C  C    . ASP   A 192 ? 0.26576 0.17742 0.34964 0.03528  0.00807  0.04948  344 ASP   A C    
1346 O  O    . ASP   A 192 ? 0.23731 0.16167 0.31165 0.03486  0.00730  0.04388  344 ASP   A O    
1347 C  CB   . ASP   A 192 ? 0.25624 0.15777 0.34972 0.03422  0.01342  0.02156  344 ASP   A CB   
1348 C  CG   . ASP   A 192 ? 0.31002 0.19845 0.41654 0.03456  0.01589  0.00876  344 ASP   A CG   
1349 O  OD1  . ASP   A 192 ? 0.29873 0.19013 0.39717 0.03208  0.01736  -0.00566 344 ASP   A OD1  
1350 O  OD2  . ASP   A 192 ? 0.33859 0.21383 0.46351 0.03750  0.01621  0.01305  344 ASP   A OD2  
1351 N  N    . ALA   A 193 ? 0.28037 0.19045 0.36525 0.03704  0.00623  0.06521  345 ALA   A N    
1352 C  CA   . ALA   A 193 ? 0.24970 0.17462 0.32092 0.03807  0.00232  0.07450  345 ALA   A CA   
1353 C  C    . ALA   A 193 ? 0.23394 0.17127 0.30923 0.04445  -0.00092 0.07241  345 ALA   A C    
1354 O  O    . ALA   A 193 ? 0.25319 0.20529 0.31729 0.04312  -0.00390 0.07095  345 ALA   A O    
1355 C  CB   . ALA   A 193 ? 0.30187 0.22361 0.37275 0.04015  0.00134  0.09250  345 ALA   A CB   
1356 N  N    . LYS   A 194 ? 0.24233 0.17419 0.33580 0.05134  -0.00031 0.07137  346 LYS   A N    
1357 C  CA   . LYS   A 194 ? 0.24617 0.19122 0.34703 0.05785  -0.00310 0.06928  346 LYS   A CA   
1358 C  C    . LYS   A 194 ? 0.25121 0.20581 0.34709 0.05394  -0.00048 0.05431  346 LYS   A C    
1359 O  O    . LYS   A 194 ? 0.24589 0.21632 0.34169 0.05554  -0.00312 0.05312  346 LYS   A O    
1360 C  CB   . LYS   A 194 ? 0.28357 0.21991 0.40719 0.06673  -0.00226 0.07079  346 LYS   A CB   
1361 C  CG   . LYS   A 194 ? 0.36603 0.29751 0.49677 0.07335  -0.00614 0.08921  346 LYS   A CG   
1362 C  CD   . LYS   A 194 ? 0.44045 0.36401 0.59620 0.08330  -0.00571 0.09033  346 LYS   A CD   
1363 C  CE   . LYS   A 194 ? 0.50564 0.40976 0.67434 0.08124  0.00082  0.07877  346 LYS   A CE   
1364 N  NZ   . LYS   A 194 ? 0.60626 0.50455 0.80039 0.09122  0.00200  0.07468  346 LYS   A NZ   
1365 N  N    . LEU   A 195 ? 0.22966 0.17558 0.32237 0.04901  0.00464  0.04307  347 LEU   A N    
1366 C  CA   . LEU   A 195 ? 0.23635 0.19129 0.32186 0.04535  0.00783  0.03106  347 LEU   A CA   
1367 C  C    . LEU   A 195 ? 0.21433 0.17852 0.28238 0.03867  0.00559  0.03329  347 LEU   A C    
1368 O  O    . LEU   A 195 ? 0.23473 0.21137 0.30022 0.03724  0.00599  0.02924  347 LEU   A O    
1369 C  CB   . LEU   A 195 ? 0.23064 0.17505 0.31477 0.04257  0.01300  0.01891  347 LEU   A CB   
1370 C  CG   . LEU   A 195 ? 0.24295 0.17656 0.34474 0.04858  0.01579  0.01277  347 LEU   A CG   
1371 C  CD1  . LEU   A 195 ? 0.23744 0.16568 0.33328 0.04514  0.02015  -0.00224 347 LEU   A CD1  
1372 C  CD2  . LEU   A 195 ? 0.27539 0.21837 0.39196 0.05659  0.01679  0.01144  347 LEU   A CD2  
1373 N  N    . VAL   A 196 ? 0.20375 0.16178 0.26134 0.03437  0.00387  0.03923  348 VAL   A N    
1374 C  CA   . VAL   A 196 ? 0.20100 0.16729 0.24328 0.02889  0.00163  0.04101  348 VAL   A CA   
1375 C  C    . VAL   A 196 ? 0.23052 0.21105 0.27392 0.03207  -0.00357 0.04687  348 VAL   A C    
1376 O  O    . VAL   A 196 ? 0.20934 0.20081 0.24761 0.02895  -0.00479 0.04282  348 VAL   A O    
1377 C  CB   . VAL   A 196 ? 0.21542 0.17356 0.24863 0.02481  0.00134  0.04664  348 VAL   A CB   
1378 C  CG1  . VAL   A 196 ? 0.23218 0.19899 0.25059 0.02005  -0.00069 0.04732  348 VAL   A CG1  
1379 C  CG2  . VAL   A 196 ? 0.19768 0.14359 0.23208 0.02141  0.00531  0.03920  348 VAL   A CG2  
1380 N  N    . GLU   A 197 ? 0.20268 0.18340 0.25379 0.03846  -0.00711 0.05656  349 GLU   A N    
1381 C  CA   . GLU   A 197 ? 0.21275 0.20884 0.26474 0.04248  -0.01364 0.06210  349 GLU   A CA   
1382 C  C    . GLU   A 197 ? 0.28546 0.29390 0.34876 0.04404  -0.01391 0.05398  349 GLU   A C    
1383 O  O    . GLU   A 197 ? 0.25255 0.27598 0.31425 0.04295  -0.01851 0.05257  349 GLU   A O    
1384 C  CB   . GLU   A 197 ? 0.26544 0.25893 0.32460 0.05046  -0.01726 0.07520  349 GLU   A CB   
1385 C  CG   . GLU   A 197 ? 0.32882 0.33988 0.38959 0.05626  -0.02540 0.08106  349 GLU   A CG   
1386 C  CD   . GLU   A 197 ? 0.46689 0.47515 0.53487 0.06543  -0.02907 0.09576  349 GLU   A CD   
1387 O  OE1  . GLU   A 197 ? 0.49624 0.49048 0.57840 0.06923  -0.02512 0.09798  349 GLU   A OE1  
1388 O  OE2  . GLU   A 197 ? 0.53205 0.55214 0.59153 0.06918  -0.03601 0.10504  349 GLU   A OE2  
1389 N  N    . ALA   A 198 ? 0.23345 0.23658 0.30925 0.04639  -0.00864 0.04771  350 ALA   A N    
1390 C  CA   . ALA   A 198 ? 0.23934 0.25519 0.32760 0.04799  -0.00715 0.04037  350 ALA   A CA   
1391 C  C    . ALA   A 198 ? 0.20133 0.22442 0.28077 0.03984  -0.00469 0.03306  350 ALA   A C    
1392 O  O    . ALA   A 198 ? 0.20323 0.24141 0.29035 0.03917  -0.00664 0.03049  350 ALA   A O    
1393 C  CB   . ALA   A 198 ? 0.29377 0.30215 0.39498 0.05215  -0.00051 0.03398  350 ALA   A CB   
1394 N  N    . ILE   A 199 ? 0.19731 0.20989 0.26253 0.03365  -0.00056 0.02984  351 ILE   A N    
1395 C  CA   . ILE   A 199 ? 0.18714 0.20465 0.24379 0.02631  0.00150  0.02489  351 ILE   A CA   
1396 C  C    . ILE   A 199 ? 0.18548 0.21192 0.23680 0.02375  -0.00547 0.02830  351 ILE   A C    
1397 O  O    . ILE   A 199 ? 0.16517 0.20301 0.22135 0.02061  -0.00651 0.02461  351 ILE   A O    
1398 C  CB   . ILE   A 199 ? 0.19826 0.20294 0.24076 0.02144  0.00613  0.02177  351 ILE   A CB   
1399 C  CG1  . ILE   A 199 ? 0.26971 0.26757 0.31641 0.02408  0.01248  0.01594  351 ILE   A CG1  
1400 C  CG2  . ILE   A 199 ? 0.20142 0.21029 0.23585 0.01467  0.00782  0.01863  351 ILE   A CG2  
1401 C  CD1  . ILE   A 199 ? 0.26032 0.24593 0.29405 0.02058  0.01494  0.01276  351 ILE   A CD1  
1402 N  N    . GLN   A 200 ? 0.22270 0.24439 0.26439 0.02485  -0.00994 0.03488  352 GLN   A N    
1403 C  CA   . GLN   A 200 ? 0.21224 0.24300 0.24603 0.02290  -0.01633 0.03675  352 GLN   A CA   
1404 C  C    . GLN   A 200 ? 0.17749 0.22535 0.22324 0.02662  -0.02280 0.03660  352 GLN   A C    
1405 O  O    . GLN   A 200 ? 0.20343 0.26228 0.24864 0.02303  -0.02683 0.03201  352 GLN   A O    
1406 C  CB   . GLN   A 200 ? 0.18306 0.20772 0.20477 0.02477  -0.01897 0.04514  352 GLN   A CB   
1407 C  CG   . GLN   A 200 ? 0.21642 0.24831 0.22494 0.02141  -0.02324 0.04442  352 GLN   A CG   
1408 C  CD   . GLN   A 200 ? 0.28257 0.31322 0.27978 0.02469  -0.02579 0.05420  352 GLN   A CD   
1409 O  OE1  . GLN   A 200 ? 0.28533 0.31889 0.28637 0.03127  -0.02911 0.06291  352 GLN   A OE1  
1410 N  NE2  . GLN   A 200 ? 0.22561 0.25250 0.20940 0.02051  -0.02384 0.05356  352 GLN   A NE2  
1411 N  N    . ASP   A 201 ? 0.18844 0.23907 0.24707 0.03398  -0.02422 0.04076  353 ASP   A N    
1412 C  CA   . ASP   A 201 ? 0.20289 0.27161 0.27538 0.03848  -0.03122 0.04069  353 ASP   A CA   
1413 C  C    . ASP   A 201 ? 0.18174 0.26109 0.26739 0.03355  -0.02850 0.03091  353 ASP   A C    
1414 O  O    . ASP   A 201 ? 0.20988 0.30541 0.30262 0.03233  -0.03502 0.02739  353 ASP   A O    
1415 C  CB   . ASP   A 201 ? 0.24549 0.31362 0.33167 0.04810  -0.03232 0.04723  353 ASP   A CB   
1416 C  CG   . ASP   A 201 ? 0.27294 0.33586 0.34980 0.05409  -0.03745 0.05967  353 ASP   A CG   
1417 O  OD1  . ASP   A 201 ? 0.24676 0.30949 0.30587 0.05102  -0.04034 0.06286  353 ASP   A OD1  
1418 O  OD2  . ASP   A 201 ? 0.26352 0.32260 0.35155 0.06224  -0.03807 0.06673  353 ASP   A OD2  
1419 N  N    . ARG   A 202 ? 0.18206 0.25349 0.27200 0.03080  -0.01883 0.02641  354 ARG   A N    
1420 C  CA   . ARG   A 202 ? 0.21298 0.29340 0.31419 0.02527  -0.01415 0.01892  354 ARG   A CA   
1421 C  C    . ARG   A 202 ? 0.20212 0.28438 0.29479 0.01704  -0.01637 0.01533  354 ARG   A C    
1422 O  O    . ARG   A 202 ? 0.19491 0.29060 0.30049 0.01333  -0.01866 0.01042  354 ARG   A O    
1423 C  CB   . ARG   A 202 ? 0.21451 0.28510 0.31542 0.02368  -0.00265 0.01579  354 ARG   A CB   
1424 C  CG   . ARG   A 202 ? 0.31765 0.39037 0.43341 0.03098  0.00168  0.01504  354 ARG   A CG   
1425 C  CD   . ARG   A 202 ? 0.30930 0.37367 0.42033 0.02871  0.01316  0.01026  354 ARG   A CD   
1426 N  NE   . ARG   A 202 ? 0.36386 0.44098 0.48752 0.02530  0.02010  0.00587  354 ARG   A NE   
1427 C  CZ   . ARG   A 202 ? 0.38112 0.45539 0.49673 0.01905  0.02847  0.00364  354 ARG   A CZ   
1428 N  NH1  . ARG   A 202 ? 0.36725 0.42689 0.46185 0.01577  0.02997  0.00447  354 ARG   A NH1  
1429 N  NH2  . ARG   A 202 ? 0.37561 0.46259 0.50531 0.01622  0.03555  0.00131  354 ARG   A NH2  
1430 N  N    . LEU   A 203 ? 0.16609 0.23497 0.23920 0.01405  -0.01560 0.01709  355 LEU   A N    
1431 C  CA   . LEU   A 203 ? 0.15713 0.22603 0.22247 0.00700  -0.01736 0.01316  355 LEU   A CA   
1432 C  C    . LEU   A 203 ? 0.21462 0.29684 0.28070 0.00817  -0.02807 0.01174  355 LEU   A C    
1433 O  O    . LEU   A 203 ? 0.19820 0.28854 0.27064 0.00288  -0.03084 0.00495  355 LEU   A O    
1434 C  CB   . LEU   A 203 ? 0.15652 0.20921 0.20228 0.00477  -0.01413 0.01539  355 LEU   A CB   
1435 C  CG   . LEU   A 203 ? 0.18123 0.22156 0.22346 0.00357  -0.00488 0.01561  355 LEU   A CG   
1436 C  CD1  . LEU   A 203 ? 0.21245 0.23926 0.23735 0.00241  -0.00398 0.01792  355 LEU   A CD1  
1437 C  CD2  . LEU   A 203 ? 0.23204 0.27426 0.28084 -0.00222 0.00122  0.01148  355 LEU   A CD2  
1438 N  N    . SER   A 204 ? 0.17413 0.25875 0.23365 0.01516  -0.03423 0.01805  356 SER   A N    
1439 C  CA   . SER   A 204 ? 0.18710 0.28634 0.24404 0.01756  -0.04506 0.01718  356 SER   A CA   
1440 C  C    . SER   A 204 ? 0.18035 0.29878 0.25884 0.01825  -0.05079 0.01163  356 SER   A C    
1441 O  O    . SER   A 204 ? 0.21966 0.35079 0.30138 0.01507  -0.05788 0.00406  356 SER   A O    
1442 C  CB   . SER   A 204 ? 0.24159 0.33973 0.28716 0.02583  -0.04951 0.02781  356 SER   A CB   
1443 O  OG   . SER   A 204 ? 0.31259 0.39494 0.34021 0.02443  -0.04448 0.03261  356 SER   A OG   
1444 N  N    . ASN   A 205 ? 0.17243 0.29404 0.26746 0.02250  -0.04793 0.01426  357 ASN   A N    
1445 C  CA   . ASN   A 205 ? 0.19476 0.33610 0.31385 0.02322  -0.05262 0.00897  357 ASN   A CA   
1446 C  C    . ASN   A 205 ? 0.21740 0.36208 0.34863 0.01308  -0.04815 -0.00083 357 ASN   A C    
1447 O  O    . ASN   A 205 ? 0.20931 0.37122 0.35640 0.01041  -0.05501 -0.00812 357 ASN   A O    
1448 C  CB   . ASN   A 205 ? 0.26667 0.40954 0.40202 0.03002  -0.04838 0.01334  357 ASN   A CB   
1449 C  CG   . ASN   A 205 ? 0.28745 0.42998 0.41735 0.04092  -0.05479 0.02342  357 ASN   A CG   
1450 O  OD1  . ASN   A 205 ? 0.30545 0.45404 0.42333 0.04415  -0.06454 0.02716  357 ASN   A OD1  
1451 N  ND2  . ASN   A 205 ? 0.30617 0.44161 0.44502 0.04697  -0.04901 0.02800  357 ASN   A ND2  
1452 N  N    . THR   A 206 ? 0.17196 0.30043 0.29668 0.00733  -0.03694 -0.00085 358 THR   A N    
1453 C  CA   . THR   A 206 ? 0.15651 0.28522 0.29101 -0.00239 -0.03186 -0.00778 358 THR   A CA   
1454 C  C    . THR   A 206 ? 0.15943 0.29044 0.28720 -0.00726 -0.03965 -0.01435 358 THR   A C    
1455 O  O    . THR   A 206 ? 0.17457 0.31563 0.31964 -0.01353 -0.04204 -0.02252 358 THR   A O    
1456 C  CB   . THR   A 206 ? 0.18712 0.29743 0.31162 -0.00602 -0.01911 -0.00454 358 THR   A CB   
1457 O  OG1  . THR   A 206 ? 0.16812 0.27839 0.30015 -0.00150 -0.01164 -0.00095 358 THR   A OG1  
1458 C  CG2  . THR   A 206 ? 0.15157 0.26054 0.28550 -0.01565 -0.01347 -0.00922 358 THR   A CG2  
1459 N  N    . LEU   A 207 ? 0.16249 0.28469 0.26669 -0.00457 -0.04330 -0.01159 359 LEU   A N    
1460 C  CA   . LEU   A 207 ? 0.19728 0.32184 0.29346 -0.00832 -0.05004 -0.01903 359 LEU   A CA   
1461 C  C    . LEU   A 207 ? 0.19264 0.33936 0.29928 -0.00599 -0.06291 -0.02584 359 LEU   A C    
1462 O  O    . LEU   A 207 ? 0.17855 0.33321 0.29561 -0.01195 -0.06758 -0.03698 359 LEU   A O    
1463 C  CB   . LEU   A 207 ? 0.20464 0.31713 0.27368 -0.00508 -0.05013 -0.01397 359 LEU   A CB   
1464 C  CG   . LEU   A 207 ? 0.20204 0.31893 0.25983 -0.00679 -0.05732 -0.02182 359 LEU   A CG   
1465 C  CD1  . LEU   A 207 ? 0.18037 0.29339 0.24953 -0.01588 -0.05474 -0.03241 359 LEU   A CD1  
1466 C  CD2  . LEU   A 207 ? 0.22185 0.32747 0.25439 -0.00339 -0.05516 -0.01541 359 LEU   A CD2  
1467 N  N    . GLN   A 208 ? 0.20194 0.35900 0.30687 0.00294  -0.06930 -0.01950 360 GLN   A N    
1468 C  CA   . GLN   A 208 ? 0.18623 0.36665 0.30008 0.00667  -0.08297 -0.02504 360 GLN   A CA   
1469 C  C    . GLN   A 208 ? 0.18274 0.37773 0.32841 0.00109  -0.08427 -0.03439 360 GLN   A C    
1470 O  O    . GLN   A 208 ? 0.18847 0.39964 0.34446 -0.00195 -0.09420 -0.04588 360 GLN   A O    
1471 C  CB   . GLN   A 208 ? 0.24465 0.43198 0.35337 0.01813  -0.08830 -0.01379 360 GLN   A CB   
1472 C  CG   . GLN   A 208 ? 0.26198 0.43792 0.34169 0.02393  -0.08804 -0.00343 360 GLN   A CG   
1473 C  CD   . GLN   A 208 ? 0.42084 0.60543 0.49844 0.03549  -0.09478 0.00822  360 GLN   A CD   
1474 O  OE1  . GLN   A 208 ? 0.50673 0.67741 0.57791 0.04032  -0.08859 0.02014  360 GLN   A OE1  
1475 N  NE2  . GLN   A 208 ? 0.44621 0.65401 0.53077 0.04014  -0.10794 0.00464  360 GLN   A NE2  
1476 N  N    . THR   A 209 ? 0.19208 0.38286 0.35462 -0.00023 -0.07423 -0.03019 361 THR   A N    
1477 C  CA   . THR   A 209 ? 0.21630 0.42138 0.41135 -0.00598 -0.07324 -0.03776 361 THR   A CA   
1478 C  C    . THR   A 209 ? 0.17044 0.36971 0.37348 -0.01792 -0.06931 -0.04738 361 THR   A C    
1479 O  O    . THR   A 209 ? 0.20326 0.41820 0.43052 -0.02359 -0.07502 -0.05801 361 THR   A O    
1480 C  CB   . THR   A 209 ? 0.22460 0.42622 0.43324 -0.00405 -0.06145 -0.03053 361 THR   A CB   
1481 O  OG1  . THR   A 209 ? 0.26056 0.46786 0.46582 0.00755  -0.06613 -0.02266 361 THR   A OG1  
1482 C  CG2  . THR   A 209 ? 0.16229 0.37991 0.40629 -0.01043 -0.05846 -0.03746 361 THR   A CG2  
1483 N  N    . TYR   A 210 ? 0.18330 0.36024 0.36792 -0.02175 -0.06012 -0.04398 362 TYR   A N    
1484 C  CA   . TYR   A 210 ? 0.16879 0.33779 0.36003 -0.03208 -0.05668 -0.05195 362 TYR   A CA   
1485 C  C    . TYR   A 210 ? 0.22221 0.40202 0.41291 -0.03370 -0.07013 -0.06485 362 TYR   A C    
1486 O  O    . TYR   A 210 ? 0.23324 0.42059 0.44699 -0.04170 -0.07286 -0.07618 362 TYR   A O    
1487 C  CB   . TYR   A 210 ? 0.18842 0.33239 0.35726 -0.03377 -0.04635 -0.04526 362 TYR   A CB   
1488 C  CG   . TYR   A 210 ? 0.21738 0.35191 0.39507 -0.04361 -0.04250 -0.05214 362 TYR   A CG   
1489 C  CD1  . TYR   A 210 ? 0.21448 0.34573 0.38211 -0.04526 -0.04961 -0.06106 362 TYR   A CD1  
1490 C  CD2  . TYR   A 210 ? 0.18222 0.31198 0.37997 -0.05097 -0.03156 -0.04980 362 TYR   A CD2  
1491 C  CE1  . TYR   A 210 ? 0.19510 0.31685 0.37396 -0.05383 -0.04639 -0.06803 362 TYR   A CE1  
1492 C  CE2  . TYR   A 210 ? 0.21576 0.33564 0.42398 -0.05983 -0.02788 -0.05471 362 TYR   A CE2  
1493 C  CZ   . TYR   A 210 ? 0.22499 0.34022 0.42465 -0.06116 -0.03566 -0.06418 362 TYR   A CZ   
1494 O  OH   . TYR   A 210 ? 0.28461 0.38868 0.49702 -0.06950 -0.03216 -0.06961 362 TYR   A OH   
1495 N  N    . ILE   A 211 ? 0.24754 0.42813 0.41212 -0.02635 -0.07814 -0.06365 363 ILE   A N    
1496 C  CA   . ILE   A 211 ? 0.21076 0.40261 0.37027 -0.02676 -0.09074 -0.07665 363 ILE   A CA   
1497 C  C    . ILE   A 211 ? 0.25854 0.47647 0.44421 -0.02755 -0.10248 -0.08717 363 ILE   A C    
1498 O  O    . ILE   A 211 ? 0.27577 0.50187 0.47635 -0.03423 -0.10899 -0.10260 363 ILE   A O    
1499 C  CB   . ILE   A 211 ? 0.20016 0.39145 0.32617 -0.01735 -0.09632 -0.07094 363 ILE   A CB   
1500 C  CG1  . ILE   A 211 ? 0.21598 0.38282 0.31982 -0.01853 -0.08560 -0.06440 363 ILE   A CG1  
1501 C  CG2  . ILE   A 211 ? 0.23824 0.44799 0.35840 -0.01553 -0.11105 -0.08452 363 ILE   A CG2  
1502 C  CD1  . ILE   A 211 ? 0.20070 0.36473 0.27362 -0.00979 -0.08750 -0.05534 363 ILE   A CD1  
1503 N  N    . ARG   A 212 ? 0.21902 0.45042 0.41357 -0.02094 -0.10527 -0.07971 364 ARG   A N    
1504 C  CA   . ARG   A 212 ? 0.26469 0.52390 0.48361 -0.01993 -0.11824 -0.08906 364 ARG   A CA   
1505 C  C    . ARG   A 212 ? 0.24861 0.51242 0.50497 -0.03119 -0.11357 -0.09815 364 ARG   A C    
1506 O  O    . ARG   A 212 ? 0.27291 0.54648 0.54010 -0.03419 -0.12063 -0.10751 364 ARG   A O    
1507 C  CB   . ARG   A 212 ? 0.30111 0.57229 0.52131 -0.00893 -0.12158 -0.07731 364 ARG   A CB   
1508 C  CG   . ARG   A 212 ? 0.37020 0.64154 0.55735 0.00285  -0.12889 -0.06801 364 ARG   A CG   
1509 C  CD   . ARG   A 212 ? 0.51223 0.80027 0.70759 0.01396  -0.13591 -0.05885 364 ARG   A CD   
1510 N  NE   . ARG   A 212 ? 0.58211 0.85777 0.78762 0.01565  -0.12268 -0.04726 364 ARG   A NE   
1511 C  CZ   . ARG   A 212 ? 0.55126 0.81229 0.73780 0.02365  -0.11699 -0.03250 364 ARG   A CZ   
1512 N  NH1  . ARG   A 212 ? 0.52971 0.78656 0.68663 0.03038  -0.12264 -0.02561 364 ARG   A NH1  
1513 N  NH2  . ARG   A 212 ? 0.50071 0.75172 0.69857 0.02485  -0.10528 -0.02502 364 ARG   A NH2  
1514 N  N    A CYS   A 213 ? 0.24493 0.49323 0.51195 -0.03687 -0.09766 -0.09081 365 CYS   A N    
1515 N  N    B CYS   A 213 ? 0.23279 0.48133 0.50020 -0.03693 -0.09773 -0.09093 365 CYS   A N    
1516 C  CA   A CYS   A 213 ? 0.30514 0.55881 0.60917 -0.04689 -0.09086 -0.09570 365 CYS   A CA   
1517 C  CA   B CYS   A 213 ? 0.30850 0.56257 0.61271 -0.04699 -0.09134 -0.09620 365 CYS   A CA   
1518 C  C    A CYS   A 213 ? 0.31092 0.54497 0.61936 -0.05842 -0.08154 -0.10012 365 CYS   A C    
1519 C  C    B CYS   A 213 ? 0.31011 0.54407 0.61880 -0.05849 -0.08133 -0.10000 365 CYS   A C    
1520 O  O    A CYS   A 213 ? 0.31273 0.54679 0.64485 -0.06649 -0.07651 -0.10364 365 CYS   A O    
1521 O  O    B CYS   A 213 ? 0.31707 0.55051 0.64970 -0.06666 -0.07551 -0.10289 365 CYS   A O    
1522 C  CB   A CYS   A 213 ? 0.34015 0.59269 0.65513 -0.04440 -0.07801 -0.08287 365 CYS   A CB   
1523 C  CB   B CYS   A 213 ? 0.34913 0.60533 0.66778 -0.04451 -0.07979 -0.08443 365 CYS   A CB   
1524 S  SG   A CYS   A 213 ? 0.39296 0.65963 0.69742 -0.02876 -0.08572 -0.07364 365 CYS   A SG   
1525 S  SG   B CYS   A 213 ? 0.34525 0.57129 0.64877 -0.04803 -0.05822 -0.07086 365 CYS   A SG   
1526 N  N    . ARG   A 214 ? 0.32511 0.53888 0.60718 -0.05820 -0.07787 -0.09756 366 ARG   A N    
1527 C  CA   . ARG   A 214 ? 0.35362 0.54779 0.64109 -0.06811 -0.06876 -0.10026 366 ARG   A CA   
1528 C  C    . ARG   A 214 ? 0.37682 0.56276 0.64723 -0.06890 -0.07634 -0.11118 366 ARG   A C    
1529 O  O    . ARG   A 214 ? 0.44493 0.61472 0.72216 -0.07632 -0.07029 -0.11485 366 ARG   A O    
1530 C  CB   . ARG   A 214 ? 0.31220 0.48366 0.58437 -0.06758 -0.05207 -0.08392 366 ARG   A CB   
1531 C  CG   . ARG   A 214 ? 0.44273 0.61952 0.73508 -0.06918 -0.04080 -0.07461 366 ARG   A CG   
1532 C  CD   . ARG   A 214 ? 0.53821 0.70511 0.85406 -0.08062 -0.02821 -0.07315 366 ARG   A CD   
1533 N  NE   . ARG   A 214 ? 0.58969 0.75990 0.91797 -0.08106 -0.01466 -0.06200 366 ARG   A NE   
1534 C  CZ   . ARG   A 214 ? 0.60533 0.75973 0.91406 -0.07828 -0.00159 -0.04858 366 ARG   A CZ   
1535 N  NH1  . ARG   A 214 ? 0.60639 0.74063 0.88423 -0.07519 -0.00087 -0.04428 366 ARG   A NH1  
1536 N  NH2  . ARG   A 214 ? 0.59512 0.75526 0.91545 -0.07832 0.01064  -0.04021 366 ARG   A NH2  
1537 N  N    . HIS   A 215 ? 0.37977 0.57250 0.62339 -0.06002 -0.08712 -0.11365 367 HIS   A N    
1538 C  CA   . HIS   A 215 ? 0.38383 0.56964 0.60969 -0.05993 -0.09299 -0.12436 367 HIS   A CA   
1539 C  C    . HIS   A 215 ? 0.44029 0.63915 0.67373 -0.06009 -0.10335 -0.13711 367 HIS   A C    
1540 O  O    . HIS   A 215 ? 0.43551 0.65367 0.66414 -0.05330 -0.11342 -0.13735 367 HIS   A O    
1541 C  CB   . HIS   A 215 ? 0.30378 0.48746 0.49228 -0.04990 -0.09642 -0.11831 367 HIS   A CB   
1542 C  CG   . HIS   A 215 ? 0.26270 0.43406 0.43299 -0.05064 -0.09688 -0.12655 367 HIS   A CG   
1543 N  ND1  . HIS   A 215 ? 0.25645 0.40600 0.40497 -0.04880 -0.08663 -0.11633 367 HIS   A ND1  
1544 C  CD2  . HIS   A 215 ? 0.25681 0.42987 0.42394 -0.05147 -0.10316 -0.14074 367 HIS   A CD2  
1545 C  CE1  . HIS   A 215 ? 0.28367 0.42766 0.42212 -0.04954 -0.08925 -0.12760 367 HIS   A CE1  
1546 N  NE2  . HIS   A 215 ? 0.29317 0.45062 0.44200 -0.05096 -0.09882 -0.14254 367 HIS   A NE2  
1547 N  N    . PRO   A 216 ? 0.43857 0.62769 0.68454 -0.06717 -0.10141 -0.14747 368 PRO   A N    
1548 C  CA   . PRO   A 216 ? 0.43705 0.63936 0.69438 -0.06811 -0.11101 -0.16092 368 PRO   A CA   
1549 C  C    . PRO   A 216 ? 0.43997 0.65310 0.66886 -0.05936 -0.12297 -0.16823 368 PRO   A C    
1550 O  O    . PRO   A 216 ? 0.39729 0.60083 0.60005 -0.05531 -0.12161 -0.16726 368 PRO   A O    
1551 C  CB   . PRO   A 216 ? 0.46377 0.64869 0.73863 -0.07705 -0.10435 -0.16917 368 PRO   A CB   
1552 C  CG   . PRO   A 216 ? 0.46574 0.62909 0.72390 -0.07708 -0.09553 -0.16292 368 PRO   A CG   
1553 C  CD   . PRO   A 216 ? 0.43662 0.60159 0.68489 -0.07353 -0.09098 -0.14751 368 PRO   A CD   
1554 N  N    . PRO   A 217 ? 0.46865 0.70233 0.70102 -0.05590 -0.13433 -0.17475 369 PRO   A N    
1555 C  CA   . PRO   A 217 ? 0.50797 0.75194 0.71351 -0.04799 -0.14499 -0.18215 369 PRO   A CA   
1556 C  C    . PRO   A 217 ? 0.59659 0.83064 0.80113 -0.05172 -0.14467 -0.19779 369 PRO   A C    
1557 O  O    . PRO   A 217 ? 0.62763 0.85163 0.85865 -0.06059 -0.13954 -0.20504 369 PRO   A O    
1558 C  CB   . PRO   A 217 ? 0.53397 0.80210 0.75049 -0.04493 -0.15662 -0.18540 369 PRO   A CB   
1559 C  CG   . PRO   A 217 ? 0.53655 0.80774 0.77972 -0.04864 -0.15137 -0.17536 369 PRO   A CG   
1560 C  CD   . PRO   A 217 ? 0.50355 0.75317 0.76360 -0.05833 -0.13762 -0.17429 369 PRO   A CD   
1561 N  N    . PRO   A 218 ? 0.67947 0.91582 0.85458 -0.04483 -0.14930 -0.20295 370 PRO   A N    
1562 C  CA   . PRO   A 218 ? 0.71855 0.96537 0.86109 -0.03421 -0.15417 -0.19294 370 PRO   A CA   
1563 C  C    . PRO   A 218 ? 0.69379 0.92551 0.81642 -0.03163 -0.14486 -0.17932 370 PRO   A C    
1564 O  O    . PRO   A 218 ? 0.70248 0.94038 0.79800 -0.02301 -0.14719 -0.16941 370 PRO   A O    
1565 C  CB   . PRO   A 218 ? 0.77120 1.02628 0.89433 -0.02941 -0.16139 -0.20629 370 PRO   A CB   
1566 C  CG   . PRO   A 218 ? 0.77771 1.01642 0.91359 -0.03645 -0.15514 -0.21959 370 PRO   A CG   
1567 C  CD   . PRO   A 218 ? 0.74358 0.97295 0.91637 -0.04666 -0.14958 -0.21915 370 PRO   A CD   
1568 N  N    . GLY   A 219 ? 0.64479 0.85695 0.78123 -0.03897 -0.13436 -0.17821 371 GLY   A N    
1569 C  CA   . GLY   A 219 ? 0.62498 0.82257 0.74340 -0.03703 -0.12584 -0.16718 371 GLY   A CA   
1570 C  C    . GLY   A 219 ? 0.60673 0.81172 0.71236 -0.03065 -0.12646 -0.15058 371 GLY   A C    
1571 O  O    . GLY   A 219 ? 0.62613 0.82508 0.70744 -0.02559 -0.12274 -0.14171 371 GLY   A O    
1572 N  N    . SER   A 220 ? 0.52725 0.74554 0.65009 -0.03040 -0.13088 -0.14603 372 SER   A N    
1573 C  CA   . SER   A 220 ? 0.52883 0.75528 0.64230 -0.02309 -0.13216 -0.13040 372 SER   A CA   
1574 C  C    . SER   A 220 ? 0.63850 0.87637 0.72106 -0.01210 -0.13982 -0.12503 372 SER   A C    
1575 O  O    . SER   A 220 ? 0.58224 0.82404 0.65328 -0.00477 -0.14014 -0.11013 372 SER   A O    
1576 C  CB   . SER   A 220 ? 0.50984 0.74840 0.65275 -0.02514 -0.13455 -0.12779 372 SER   A CB   
1577 O  OG   . SER   A 220 ? 0.53863 0.78841 0.69748 -0.02831 -0.14193 -0.14044 372 SER   A OG   
1578 N  N    . HIS   A 221 ? 0.67247 0.91519 0.74205 -0.01060 -0.14518 -0.13610 373 HIS   A N    
1579 C  CA   . HIS   A 221 ? 0.70028 0.95503 0.74154 -0.00069 -0.15205 -0.13143 373 HIS   A CA   
1580 C  C    . HIS   A 221 ? 0.59713 0.84364 0.60964 0.00601  -0.14580 -0.11574 373 HIS   A C    
1581 O  O    . HIS   A 221 ? 0.62084 0.85536 0.61842 0.00485  -0.13888 -0.11828 373 HIS   A O    
1582 C  CB   . HIS   A 221 ? 0.77801 1.03711 0.81025 -0.00115 -0.15629 -0.14786 373 HIS   A CB   
1583 C  CG   . HIS   A 221 ? 0.86081 1.12843 0.85943 0.00847  -0.15966 -0.14262 373 HIS   A CG   
1584 N  ND1  . HIS   A 221 ? 0.89362 1.17988 0.88463 0.01529  -0.17001 -0.13969 373 HIS   A ND1  
1585 C  CD2  . HIS   A 221 ? 0.88205 1.14238 0.85343 0.01235  -0.15338 -0.13905 373 HIS   A CD2  
1586 C  CE1  . HIS   A 221 ? 0.90994 1.19951 0.86980 0.02282  -0.16965 -0.13408 373 HIS   A CE1  
1587 N  NE2  . HIS   A 221 ? 0.90826 1.18260 0.85620 0.02106  -0.15923 -0.13362 373 HIS   A NE2  
1588 N  N    . GLN   A 222 ? 0.51319 0.76585 0.51916 0.01328  -0.14791 -0.09918 374 GLN   A N    
1589 C  CA   . GLN   A 222 ? 0.40614 0.65071 0.38698 0.01993  -0.14166 -0.08191 374 GLN   A CA   
1590 C  C    . GLN   A 222 ? 0.33021 0.55678 0.31123 0.01472  -0.13066 -0.08066 374 GLN   A C    
1591 O  O    . GLN   A 222 ? 0.31373 0.53132 0.27210 0.01806  -0.12395 -0.07160 374 GLN   A O    
1592 C  CB   . GLN   A 222 ? 0.45000 0.69903 0.40032 0.02649  -0.14310 -0.07977 374 GLN   A CB   
1593 C  CG   . GLN   A 222 ? 0.55921 0.82698 0.50905 0.03018  -0.15483 -0.08647 374 GLN   A CG   
1594 C  CD   . GLN   A 222 ? 0.69132 0.96520 0.60989 0.03853  -0.15594 -0.07887 374 GLN   A CD   
1595 O  OE1  . GLN   A 222 ? 0.71770 0.98505 0.61741 0.03855  -0.14918 -0.08123 374 GLN   A OE1  
1596 N  NE2  . GLN   A 222 ? 0.77259 1.05960 0.68653 0.04581  -0.16423 -0.06943 374 GLN   A NE2  
1597 N  N    . LEU   A 223 ? 0.27115 0.49239 0.27879 0.00622  -0.12829 -0.08925 375 LEU   A N    
1598 C  CA   . LEU   A 223 ? 0.25152 0.45309 0.26052 0.00068  -0.11703 -0.08754 375 LEU   A CA   
1599 C  C    . LEU   A 223 ? 0.29363 0.48142 0.29217 0.00518  -0.10767 -0.06609 375 LEU   A C    
1600 O  O    . LEU   A 223 ? 0.28484 0.45641 0.26784 0.00510  -0.09833 -0.05941 375 LEU   A O    
1601 C  CB   . LEU   A 223 ? 0.31574 0.50898 0.35651 -0.00952 -0.11304 -0.09618 375 LEU   A CB   
1602 C  CG   . LEU   A 223 ? 0.31658 0.48352 0.35935 -0.01558 -0.09882 -0.09164 375 LEU   A CG   
1603 C  CD1  . LEU   A 223 ? 0.31328 0.47206 0.33571 -0.01511 -0.09624 -0.09775 375 LEU   A CD1  
1604 C  CD2  . LEU   A 223 ? 0.34506 0.50629 0.41927 -0.02540 -0.09556 -0.09978 375 LEU   A CD2  
1605 N  N    . TYR   A 224 ? 0.30776 0.50216 0.31628 0.00933  -0.11023 -0.05585 376 TYR   A N    
1606 C  CA   . TYR   A 224 ? 0.28863 0.46891 0.29048 0.01341  -0.10143 -0.03713 376 TYR   A CA   
1607 C  C    . TYR   A 224 ? 0.27075 0.44988 0.24318 0.02059  -0.10069 -0.02639 376 TYR   A C    
1608 O  O    . TYR   A 224 ? 0.30128 0.46251 0.26352 0.01991  -0.09035 -0.01719 376 TYR   A O    
1609 C  CB   . TYR   A 224 ? 0.28283 0.47232 0.30200 0.01781  -0.10529 -0.02960 376 TYR   A CB   
1610 C  CG   . TYR   A 224 ? 0.25092 0.42532 0.26595 0.02218  -0.09653 -0.01218 376 TYR   A CG   
1611 C  CD1  . TYR   A 224 ? 0.24451 0.39791 0.26467 0.01668  -0.08399 -0.00928 376 TYR   A CD1  
1612 C  CD2  . TYR   A 224 ? 0.33134 0.51232 0.33738 0.03211  -0.10109 0.00127  376 TYR   A CD2  
1613 C  CE1  . TYR   A 224 ? 0.27871 0.41883 0.29604 0.02047  -0.07670 0.00420  376 TYR   A CE1  
1614 C  CE2  . TYR   A 224 ? 0.33342 0.49919 0.33832 0.03579  -0.09308 0.01599  376 TYR   A CE2  
1615 C  CZ   . TYR   A 224 ? 0.32025 0.46589 0.33110 0.02973  -0.08111 0.01628  376 TYR   A CZ   
1616 O  OH   . TYR   A 224 ? 0.36304 0.49402 0.37374 0.03320  -0.07381 0.02862  376 TYR   A OH   
1617 N  N    . ALA   A 225 ? 0.33767 0.53694 0.29637 0.02749  -0.11157 -0.02737 377 ALA   A N    
1618 C  CA   . ALA   A 225 ? 0.31415 0.51419 0.24410 0.03443  -0.11006 -0.01597 377 ALA   A CA   
1619 C  C    . ALA   A 225 ? 0.31294 0.50168 0.22835 0.02985  -0.10181 -0.02216 377 ALA   A C    
1620 O  O    . ALA   A 225 ? 0.30897 0.48720 0.20832 0.03212  -0.09343 -0.00982 377 ALA   A O    
1621 C  CB   . ALA   A 225 ? 0.37395 0.58838 0.29356 0.04022  -0.11877 -0.01641 377 ALA   A CB   
1622 N  N    . LYS   A 226 ? 0.32978 0.52054 0.25286 0.02340  -0.10393 -0.04136 378 LYS   A N    
1623 C  CA   . LYS   A 226 ? 0.30881 0.48847 0.22145 0.01947  -0.09611 -0.04840 378 LYS   A CA   
1624 C  C    . LYS   A 226 ? 0.31161 0.46642 0.23225 0.01445  -0.08316 -0.03985 378 LYS   A C    
1625 O  O    . LYS   A 226 ? 0.31012 0.45491 0.21744 0.01446  -0.07499 -0.03581 378 LYS   A O    
1626 C  CB   . LYS   A 226 ? 0.29143 0.47527 0.21534 0.01361  -0.10070 -0.07070 378 LYS   A CB   
1627 C  CG   . LYS   A 226 ? 0.38980 0.58787 0.30630 0.01725  -0.10838 -0.07853 378 LYS   A CG   
1628 C  CD   . LYS   A 226 ? 0.43489 0.63146 0.35789 0.01205  -0.10893 -0.09918 378 LYS   A CD   
1629 C  CE   . LYS   A 226 ? 0.53479 0.74702 0.44968 0.01596  -0.11688 -0.10799 378 LYS   A CE   
1630 N  NZ   . LYS   A 226 ? 0.61773 0.83929 0.55630 0.01216  -0.12642 -0.11947 378 LYS   A NZ   
1631 N  N    . MET   A 227 ? 0.27033 0.41642 0.21289 0.01027  -0.08114 -0.03772 379 MET   A N    
1632 C  CA   . MET   A 227 ? 0.28331 0.40764 0.23177 0.00628  -0.06972 -0.02976 379 MET   A CA   
1633 C  C    . MET   A 227 ? 0.28845 0.40619 0.22437 0.01158  -0.06451 -0.01193 379 MET   A C    
1634 O  O    . MET   A 227 ? 0.26412 0.36710 0.19444 0.00983  -0.05568 -0.00648 379 MET   A O    
1635 C  CB   . MET   A 227 ? 0.25975 0.37877 0.23294 0.00124  -0.06839 -0.03156 379 MET   A CB   
1636 C  CG   . MET   A 227 ? 0.26474 0.38594 0.25434 -0.00577 -0.07105 -0.04789 379 MET   A CG   
1637 S  SD   . MET   A 227 ? 0.22651 0.34375 0.24626 -0.01207 -0.06801 -0.04857 379 MET   A SD   
1638 C  CE   . MET   A 227 ? 0.22517 0.31768 0.24138 -0.01481 -0.05416 -0.03811 379 MET   A CE   
1639 N  N    . ILE   A 228 ? 0.30863 0.43729 0.24172 0.01817  -0.07021 -0.00270 380 ILE   A N    
1640 C  CA   . ILE   A 228 ? 0.32429 0.44661 0.24686 0.02353  -0.06564 0.01485  380 ILE   A CA   
1641 C  C    . ILE   A 228 ? 0.31472 0.43779 0.21492 0.02546  -0.06188 0.01830  380 ILE   A C    
1642 O  O    . ILE   A 228 ? 0.31226 0.42238 0.20740 0.02514  -0.05320 0.02860  380 ILE   A O    
1643 C  CB   . ILE   A 228 ? 0.39477 0.52973 0.31971 0.03122  -0.07353 0.02421  380 ILE   A CB   
1644 C  CG1  . ILE   A 228 ? 0.40203 0.53468 0.35146 0.02953  -0.07464 0.02229  380 ILE   A CG1  
1645 C  CG2  . ILE   A 228 ? 0.42745 0.55633 0.34044 0.03732  -0.06919 0.04316  380 ILE   A CG2  
1646 C  CD1  . ILE   A 228 ? 0.50468 0.61636 0.46395 0.02505  -0.06385 0.02601  380 ILE   A CD1  
1647 N  N    . GLN   A 229 ? 0.34724 0.48652 0.23455 0.02743  -0.06812 0.00889  381 GLN   A N    
1648 C  CA   . GLN   A 229 ? 0.36586 0.50769 0.23172 0.02935  -0.06336 0.01067  381 GLN   A CA   
1649 C  C    . GLN   A 229 ? 0.32208 0.44774 0.19165 0.02288  -0.05355 0.00500  381 GLN   A C    
1650 O  O    . GLN   A 229 ? 0.36253 0.48346 0.22066 0.02373  -0.04563 0.01263  381 GLN   A O    
1651 C  CB   . GLN   A 229 ? 0.39238 0.55186 0.24664 0.03194  -0.07077 -0.00167 381 GLN   A CB   
1652 C  CG   . GLN   A 229 ? 0.40936 0.56817 0.24544 0.03331  -0.06333 -0.00097 381 GLN   A CG   
1653 C  CD   . GLN   A 229 ? 0.49357 0.64715 0.31916 0.03749  -0.05612 0.02006  381 GLN   A CD   
1654 O  OE1  . GLN   A 229 ? 0.48051 0.62642 0.29962 0.03615  -0.04615 0.02526  381 GLN   A OE1  
1655 N  NE2  . GLN   A 229 ? 0.47130 0.62891 0.29736 0.04243  -0.06108 0.03197  381 GLN   A NE2  
1656 N  N    . LYS   A 230 ? 0.28221 0.39970 0.16876 0.01655  -0.05371 -0.00738 382 LYS   A N    
1657 C  CA   . LYS   A 230 ? 0.27115 0.37288 0.16226 0.01130  -0.04506 -0.01105 382 LYS   A CA   
1658 C  C    . LYS   A 230 ? 0.25368 0.34011 0.14802 0.01059  -0.03699 0.00354  382 LYS   A C    
1659 O  O    . LYS   A 230 ? 0.27866 0.35648 0.16938 0.00892  -0.02959 0.00544  382 LYS   A O    
1660 C  CB   . LYS   A 230 ? 0.28046 0.37572 0.18998 0.00509  -0.04673 -0.02454 382 LYS   A CB   
1661 C  CG   . LYS   A 230 ? 0.28468 0.39087 0.19348 0.00412  -0.05270 -0.04254 382 LYS   A CG   
1662 C  CD   . LYS   A 230 ? 0.36185 0.46797 0.25692 0.00539  -0.04782 -0.04787 382 LYS   A CD   
1663 C  CE   . LYS   A 230 ? 0.45204 0.57042 0.34512 0.00553  -0.05422 -0.06728 382 LYS   A CE   
1664 N  NZ   . LYS   A 230 ? 0.48927 0.62937 0.36319 0.01205  -0.06123 -0.06797 382 LYS   A NZ   
1665 N  N    . LEU   A 231 ? 0.27962 0.36311 0.18221 0.01202  -0.03851 0.01292  383 LEU   A N    
1666 C  CA   . LEU   A 231 ? 0.27031 0.33984 0.17635 0.01175  -0.03151 0.02544  383 LEU   A CA   
1667 C  C    . LEU   A 231 ? 0.26497 0.33683 0.15661 0.01554  -0.02742 0.03731  383 LEU   A C    
1668 O  O    . LEU   A 231 ? 0.27891 0.33977 0.17148 0.01343  -0.01987 0.04314  383 LEU   A O    
1669 C  CB   . LEU   A 231 ? 0.28559 0.35260 0.20416 0.01343  -0.03413 0.03153  383 LEU   A CB   
1670 C  CG   . LEU   A 231 ? 0.27683 0.34024 0.21167 0.00908  -0.03543 0.02210  383 LEU   A CG   
1671 C  CD1  . LEU   A 231 ? 0.31754 0.38298 0.26441 0.01219  -0.03833 0.02759  383 LEU   A CD1  
1672 C  CD2  . LEU   A 231 ? 0.28280 0.33040 0.22241 0.00392  -0.02795 0.02010  383 LEU   A CD2  
1673 N  N    . ALA   A 232 ? 0.30342 0.39057 0.18197 0.02113  -0.03231 0.04120  384 ALA   A N    
1674 C  CA   . ALA   A 232 ? 0.33705 0.42822 0.20022 0.02488  -0.02741 0.05361  384 ALA   A CA   
1675 C  C    . ALA   A 232 ? 0.36066 0.45206 0.21551 0.02202  -0.02075 0.04683  384 ALA   A C    
1676 O  O    . ALA   A 232 ? 0.33309 0.41825 0.18594 0.02110  -0.01221 0.05614  384 ALA   A O    
1677 C  CB   . ALA   A 232 ? 0.33610 0.44593 0.18438 0.03224  -0.03470 0.05872  384 ALA   A CB   
1678 N  N    . ASP   A 233 ? 0.35668 0.45529 0.20901 0.02053  -0.02439 0.03009  385 ASP   A N    
1679 C  CA   . ASP   A 233 ? 0.36213 0.46066 0.20917 0.01842  -0.01815 0.02186  385 ASP   A CA   
1680 C  C    . ASP   A 233 ? 0.36006 0.44095 0.22086 0.01320  -0.01073 0.02379  385 ASP   A C    
1681 O  O    . ASP   A 233 ? 0.33936 0.41891 0.19687 0.01249  -0.00302 0.02607  385 ASP   A O    
1682 C  CB   . ASP   A 233 ? 0.33840 0.44398 0.18594 0.01724  -0.02385 0.00196  385 ASP   A CB   
1683 C  CG   . ASP   A 233 ? 0.39141 0.51683 0.22503 0.02234  -0.03241 -0.00333 385 ASP   A CG   
1684 O  OD1  . ASP   A 233 ? 0.43408 0.56471 0.27283 0.02079  -0.03920 -0.02014 385 ASP   A OD1  
1685 O  OD2  . ASP   A 233 ? 0.39963 0.53108 0.22250 0.02698  -0.03178 0.00890  385 ASP   A OD2  
1686 N  N    . LEU   A 234 ? 0.30125 0.37002 0.17767 0.00974  -0.01298 0.02244  386 LEU   A N    
1687 C  CA   . LEU   A 234 ? 0.30906 0.36259 0.19711 0.00536  -0.00728 0.02338  386 LEU   A CA   
1688 C  C    . LEU   A 234 ? 0.32102 0.36903 0.20938 0.00567  -0.00105 0.03776  386 LEU   A C    
1689 O  O    . LEU   A 234 ? 0.28890 0.32975 0.18261 0.00284  0.00472  0.03825  386 LEU   A O    
1690 C  CB   . LEU   A 234 ? 0.26612 0.30971 0.16835 0.00230  -0.01064 0.01963  386 LEU   A CB   
1691 C  CG   . LEU   A 234 ? 0.23341 0.27686 0.14160 -0.00037 -0.01404 0.00548  386 LEU   A CG   
1692 C  CD1  . LEU   A 234 ? 0.27100 0.30918 0.19157 -0.00247 -0.01733 0.00473  386 LEU   A CD1  
1693 C  CD2  . LEU   A 234 ? 0.25750 0.29242 0.16966 -0.00311 -0.00923 0.00010  386 LEU   A CD2  
1694 N  N    . ARG   A 235 ? 0.32614 0.37740 0.21067 0.00914  -0.00237 0.04958  387 ARG   A N    
1695 C  CA   . ARG   A 235 ? 0.32905 0.37465 0.21550 0.00925  0.00409  0.06398  387 ARG   A CA   
1696 C  C    . ARG   A 235 ? 0.32343 0.37679 0.19996 0.00955  0.01122  0.06689  387 ARG   A C    
1697 O  O    . ARG   A 235 ? 0.30850 0.35526 0.19240 0.00650  0.01836  0.07212  387 ARG   A O    
1698 C  CB   . ARG   A 235 ? 0.36355 0.41138 0.24788 0.01396  0.00113  0.07706  387 ARG   A CB   
1699 C  CG   . ARG   A 235 ? 0.39698 0.43861 0.29293 0.01442  -0.00509 0.07463  387 ARG   A CG   
1700 C  CD   . ARG   A 235 ? 0.45296 0.47789 0.36483 0.01049  -0.00127 0.07564  387 ARG   A CD   
1701 N  NE   . ARG   A 235 ? 0.53658 0.55683 0.45906 0.01161  -0.00595 0.07333  387 ARG   A NE   
1702 C  CZ   . ARG   A 235 ? 0.52745 0.54200 0.45803 0.01477  -0.00630 0.08284  387 ARG   A CZ   
1703 N  NH1  . ARG   A 235 ? 0.52884 0.54026 0.45858 0.01674  -0.00234 0.09645  387 ARG   A NH1  
1704 N  NH2  . ARG   A 235 ? 0.43752 0.44941 0.37844 0.01609  -0.00997 0.07898  387 ARG   A NH2  
1705 N  N    . SER   A 236 ? 0.30992 0.37857 0.17046 0.01321  0.00945  0.06252  388 SER   A N    
1706 C  CA   . SER   A 236 ? 0.30866 0.38702 0.15848 0.01417  0.01718  0.06423  388 SER   A CA   
1707 C  C    . SER   A 236 ? 0.31528 0.38871 0.17423 0.00999  0.02141  0.05259  388 SER   A C    
1708 O  O    . SER   A 236 ? 0.30140 0.37494 0.16358 0.00830  0.03001  0.05747  388 SER   A O    
1709 C  CB   . SER   A 236 ? 0.37756 0.47222 0.20957 0.01920  0.01323  0.05830  388 SER   A CB   
1710 O  OG   . SER   A 236 ? 0.43241 0.53461 0.25703 0.01978  0.02069  0.05547  388 SER   A OG   
1711 N  N    . LEU   A 237 ? 0.26747 0.33664 0.13246 0.00834  0.01557  0.03793  389 LEU   A N    
1712 C  CA   . LEU   A 237 ? 0.30072 0.36391 0.17572 0.00520  0.01857  0.02788  389 LEU   A CA   
1713 C  C    . LEU   A 237 ? 0.27390 0.32404 0.16403 0.00115  0.02228  0.03491  389 LEU   A C    
1714 O  O    . LEU   A 237 ? 0.27701 0.32640 0.17384 -0.00055 0.02774  0.03315  389 LEU   A O    
1715 C  CB   . LEU   A 237 ? 0.25691 0.31617 0.13689 0.00422  0.01150  0.01333  389 LEU   A CB   
1716 C  CG   . LEU   A 237 ? 0.31720 0.38942 0.18576 0.00742  0.00763  0.00144  389 LEU   A CG   
1717 C  CD1  . LEU   A 237 ? 0.27911 0.34602 0.15623 0.00547  -0.00017 -0.01011 389 LEU   A CD1  
1718 C  CD2  . LEU   A 237 ? 0.34518 0.42411 0.21015 0.00889  0.01363  -0.00695 389 LEU   A CD2  
1719 N  N    . ASN   A 238 ? 0.25653 0.29726 0.15312 -0.00012 0.01898  0.04169  390 ASN   A N    
1720 C  CA   . ASN   A 238 ? 0.28975 0.31878 0.20025 -0.00373 0.02171  0.04719  390 ASN   A CA   
1721 C  C    . ASN   A 238 ? 0.27859 0.31099 0.19115 -0.00466 0.02994  0.05718  390 ASN   A C    
1722 O  O    . ASN   A 238 ? 0.28819 0.31741 0.21180 -0.00781 0.03381  0.05555  390 ASN   A O    
1723 C  CB   . ASN   A 238 ? 0.28557 0.30599 0.20101 -0.00372 0.01741  0.05272  390 ASN   A CB   
1724 C  CG   . ASN   A 238 ? 0.31857 0.32650 0.24850 -0.00731 0.01868  0.05433  390 ASN   A CG   
1725 O  OD1  . ASN   A 238 ? 0.29979 0.30630 0.23679 -0.00992 0.02341  0.05585  390 ASN   A OD1  
1726 N  ND2  . ASN   A 238 ? 0.29792 0.29795 0.23300 -0.00734 0.01438  0.05316  390 ASN   A ND2  
1727 N  N    . GLU   A 239 ? 0.28373 0.32349 0.18643 -0.00185 0.03276  0.06822  391 GLU   A N    
1728 C  CA   . GLU   A 239 ? 0.28046 0.32316 0.18633 -0.00316 0.04191  0.08017  391 GLU   A CA   
1729 C  C    . GLU   A 239 ? 0.28460 0.33716 0.18972 -0.00387 0.04848  0.07406  391 GLU   A C    
1730 O  O    . GLU   A 239 ? 0.29296 0.34395 0.21147 -0.00759 0.05503  0.07761  391 GLU   A O    
1731 C  CB   . GLU   A 239 ? 0.36386 0.41379 0.25660 0.00103  0.04386  0.09458  391 GLU   A CB   
1732 C  CG   . GLU   A 239 ? 0.55707 0.60514 0.45783 -0.00121 0.05311  0.10887  391 GLU   A CG   
1733 C  CD   . GLU   A 239 ? 0.70184 0.73361 0.62261 -0.00525 0.05314  0.11603  391 GLU   A CD   
1734 O  OE1  . GLU   A 239 ? 0.77663 0.80435 0.71211 -0.00972 0.06015  0.12145  391 GLU   A OE1  
1735 O  OE2  . GLU   A 239 ? 0.74479 0.76784 0.66818 -0.00405 0.04586  0.11446  391 GLU   A OE2  
1736 N  N    . GLU   A 240 ? 0.26370 0.32674 0.15553 -0.00037 0.04664  0.06357  392 GLU   A N    
1737 C  CA   . GLU   A 240 ? 0.26215 0.33508 0.15410 -0.00006 0.05325  0.05653  392 GLU   A CA   
1738 C  C    . GLU   A 240 ? 0.27469 0.33908 0.18434 -0.00341 0.05169  0.04663  392 GLU   A C    
1739 O  O    . GLU   A 240 ? 0.28045 0.34878 0.20069 -0.00517 0.05842  0.04673  392 GLU   A O    
1740 C  CB   . GLU   A 240 ? 0.28582 0.37163 0.15986 0.00499  0.05126  0.04583  392 GLU   A CB   
1741 C  CG   . GLU   A 240 ? 0.31566 0.41291 0.18928 0.00651  0.05873  0.03716  392 GLU   A CG   
1742 C  CD   . GLU   A 240 ? 0.36769 0.47556 0.24010 0.00629  0.07099  0.04991  392 GLU   A CD   
1743 O  OE1  . GLU   A 240 ? 0.34378 0.45706 0.22640 0.00539  0.07836  0.04568  392 GLU   A OE1  
1744 O  OE2  . GLU   A 240 ? 0.34005 0.44925 0.20393 0.00693  0.07279  0.06394  392 GLU   A OE2  
1745 N  N    . HIS   A 241 ? 0.24938 0.30312 0.16294 -0.00408 0.04298  0.03861  393 HIS   A N    
1746 C  CA   . HIS   A 241 ? 0.24570 0.29168 0.17436 -0.00647 0.04105  0.03110  393 HIS   A CA   
1747 C  C    . HIS   A 241 ? 0.25749 0.29765 0.20151 -0.01072 0.04389  0.03900  393 HIS   A C    
1748 O  O    . HIS   A 241 ? 0.25838 0.30000 0.21519 -0.01227 0.04626  0.03550  393 HIS   A O    
1749 C  CB   . HIS   A 241 ? 0.22588 0.26145 0.15519 -0.00652 0.03221  0.02363  393 HIS   A CB   
1750 C  CG   . HIS   A 241 ? 0.23271 0.25983 0.17575 -0.00849 0.02981  0.01903  393 HIS   A CG   
1751 N  ND1  . HIS   A 241 ? 0.21544 0.23368 0.16760 -0.01155 0.02773  0.02372  393 HIS   A ND1  
1752 C  CD2  . HIS   A 241 ? 0.23432 0.26142 0.18351 -0.00722 0.02906  0.01035  393 HIS   A CD2  
1753 C  CE1  . HIS   A 241 ? 0.19929 0.21359 0.16073 -0.01198 0.02524  0.01822  393 HIS   A CE1  
1754 N  NE2  . HIS   A 241 ? 0.23234 0.25142 0.19267 -0.00923 0.02599  0.01097  393 HIS   A NE2  
1755 N  N    . SER   A 242 ? 0.23621 0.26993 0.18101 -0.01247 0.04319  0.04887  394 SER   A N    
1756 C  CA   . SER   A 242 ? 0.25626 0.28358 0.21760 -0.01694 0.04553  0.05503  394 SER   A CA   
1757 C  C    . SER   A 242 ? 0.27241 0.30951 0.24139 -0.01881 0.05529  0.06117  394 SER   A C    
1758 O  O    . SER   A 242 ? 0.28168 0.31799 0.26840 -0.02260 0.05712  0.05976  394 SER   A O    
1759 C  CB   . SER   A 242 ? 0.32759 0.34576 0.28912 -0.01771 0.04363  0.06430  394 SER   A CB   
1760 O  OG   . SER   A 242 ? 0.41721 0.42957 0.37050 -0.01531 0.03590  0.05937  394 SER   A OG   
1761 N  N    A LYS   A 243 ? 0.26467 0.31240 0.22073 -0.01613 0.06171  0.06805  395 LYS   A N    
1762 N  N    B LYS   A 243 ? 0.26613 0.31392 0.22218 -0.01612 0.06173  0.06800  395 LYS   A N    
1763 C  CA   A LYS   A 243 ? 0.26088 0.32000 0.22309 -0.01765 0.07280  0.07467  395 LYS   A CA   
1764 C  CA   B LYS   A 243 ? 0.26678 0.32591 0.22904 -0.01766 0.07283  0.07469  395 LYS   A CA   
1765 C  C    A LYS   A 243 ? 0.25573 0.32248 0.22755 -0.01763 0.07455  0.06302  395 LYS   A C    
1766 C  C    B LYS   A 243 ? 0.25672 0.32367 0.22840 -0.01760 0.07468  0.06308  395 LYS   A C    
1767 O  O    A LYS   A 243 ? 0.26235 0.33255 0.25309 -0.02151 0.07989  0.06477  395 LYS   A O    
1768 O  O    B LYS   A 243 ? 0.26058 0.33132 0.25093 -0.02141 0.08027  0.06498  395 LYS   A O    
1769 C  CB   A LYS   A 243 ? 0.29586 0.36714 0.23750 -0.01331 0.07895  0.08280  395 LYS   A CB   
1770 C  CB   B LYS   A 243 ? 0.30710 0.37830 0.24892 -0.01337 0.07904  0.08304  395 LYS   A CB   
1771 C  CG   A LYS   A 243 ? 0.37638 0.46135 0.32179 -0.01440 0.09226  0.09122  395 LYS   A CG   
1772 C  CG   B LYS   A 243 ? 0.36587 0.44965 0.31238 -0.01488 0.09249  0.09314  395 LYS   A CG   
1773 C  CD   A LYS   A 243 ? 0.41210 0.50805 0.33356 -0.00912 0.09594  0.09620  395 LYS   A CD   
1774 C  CD   B LYS   A 243 ? 0.40302 0.50119 0.32576 -0.00911 0.09691  0.09405  395 LYS   A CD   
1775 C  CE   A LYS   A 243 ? 0.40691 0.51337 0.33228 -0.01036 0.10747  0.10089  395 LYS   A CE   
1776 C  CE   B LYS   A 243 ? 0.40860 0.50159 0.31163 -0.00484 0.08800  0.09602  395 LYS   A CE   
1777 N  NZ   A LYS   A 243 ? 0.50656 0.62177 0.40815 -0.00506 0.10907  0.10267  395 LYS   A NZ   
1778 N  NZ   B LYS   A 243 ? 0.43357 0.51413 0.34265 -0.00706 0.08663  0.11035  395 LYS   A NZ   
1779 N  N    . GLN   A 244 ? 0.25322 0.32268 0.21442 -0.01322 0.06983  0.05076  396 GLN   A N    
1780 C  CA   . GLN   A 244 ? 0.27434 0.34998 0.24547 -0.01196 0.07089  0.03958  396 GLN   A CA   
1781 C  C    . GLN   A 244 ? 0.24643 0.31211 0.23620 -0.01506 0.06407  0.03490  396 GLN   A C    
1782 O  O    . GLN   A 244 ? 0.25655 0.32828 0.26313 -0.01612 0.06675  0.03154  396 GLN   A O    
1783 C  CB   . GLN   A 244 ? 0.26005 0.33909 0.21647 -0.00636 0.06742  0.02767  396 GLN   A CB   
1784 C  CG   . GLN   A 244 ? 0.31325 0.40513 0.24960 -0.00263 0.07355  0.03027  396 GLN   A CG   
1785 C  CD   . GLN   A 244 ? 0.30619 0.40455 0.23214 0.00279  0.07178  0.01539  396 GLN   A CD   
1786 O  OE1  . GLN   A 244 ? 0.30748 0.40146 0.24408 0.00387  0.06813  0.00417  396 GLN   A OE1  
1787 N  NE2  . GLN   A 244 ? 0.30053 0.40939 0.20581 0.00655  0.07396  0.01506  396 GLN   A NE2  
1788 N  N    . TYR   A 245 ? 0.21820 0.27016 0.20528 -0.01614 0.05523  0.03450  397 TYR   A N    
1789 C  CA   . TYR   A 245 ? 0.21810 0.26171 0.21977 -0.01856 0.04849  0.03027  397 TYR   A CA   
1790 C  C    . TYR   A 245 ? 0.23429 0.27974 0.25515 -0.02384 0.05228  0.03596  397 TYR   A C    
1791 O  O    . TYR   A 245 ? 0.22457 0.27262 0.26180 -0.02519 0.04998  0.03073  397 TYR   A O    
1792 C  CB   . TYR   A 245 ? 0.25170 0.28172 0.24557 -0.01868 0.04003  0.02966  397 TYR   A CB   
1793 C  CG   . TYR   A 245 ? 0.21973 0.24246 0.22590 -0.02086 0.03347  0.02582  397 TYR   A CG   
1794 C  CD1  . TYR   A 245 ? 0.22955 0.25062 0.23680 -0.01816 0.02759  0.01782  397 TYR   A CD1  
1795 C  CD2  . TYR   A 245 ? 0.20822 0.22603 0.22523 -0.02529 0.03305  0.03005  397 TYR   A CD2  
1796 C  CE1  . TYR   A 245 ? 0.23544 0.25185 0.25140 -0.01932 0.02114  0.01470  397 TYR   A CE1  
1797 C  CE2  . TYR   A 245 ? 0.19760 0.21064 0.22455 -0.02687 0.02638  0.02469  397 TYR   A CE2  
1798 C  CZ   . TYR   A 245 ? 0.19285 0.20611 0.21781 -0.02363 0.02033  0.01732  397 TYR   A CZ   
1799 O  OH   . TYR   A 245 ? 0.22217 0.23246 0.25439 -0.02441 0.01322  0.01245  397 TYR   A OH   
1800 N  N    . ARG   A 246 ? 0.20944 0.25344 0.23006 -0.02686 0.05761  0.04680  398 ARG   A N    
1801 C  CA   . ARG   A 246 ? 0.22402 0.26870 0.26594 -0.03280 0.06196  0.05250  398 ARG   A CA   
1802 C  C    . ARG   A 246 ? 0.25088 0.31089 0.30667 -0.03378 0.07011  0.05171  398 ARG   A C    
1803 O  O    . ARG   A 246 ? 0.25592 0.31880 0.33440 -0.03793 0.06966  0.04893  398 ARG   A O    
1804 C  CB   . ARG   A 246 ? 0.27312 0.31257 0.31242 -0.03521 0.06734  0.06613  398 ARG   A CB   
1805 C  CG   . ARG   A 246 ? 0.34190 0.36603 0.37463 -0.03484 0.05949  0.06682  398 ARG   A CG   
1806 C  CD   . ARG   A 246 ? 0.48310 0.50093 0.51944 -0.03724 0.06479  0.08099  398 ARG   A CD   
1807 N  NE   . ARG   A 246 ? 0.56481 0.59056 0.58403 -0.03363 0.07191  0.09202  398 ARG   A NE   
1808 C  CZ   . ARG   A 246 ? 0.53936 0.56259 0.53867 -0.02867 0.06839  0.09536  398 ARG   A CZ   
1809 N  NH1  . ARG   A 246 ? 0.54151 0.55422 0.53702 -0.02710 0.05892  0.08884  398 ARG   A NH1  
1810 N  NH2  . ARG   A 246 ? 0.53040 0.56317 0.51362 -0.02504 0.07435  0.10506  398 ARG   A NH2  
1811 N  N    . SER   A 247 ? 0.22291 0.29424 0.26605 -0.02978 0.07752  0.05312  399 SER   A N    
1812 C  CA   . SER   A 247 ? 0.24499 0.33266 0.30104 -0.02987 0.08654  0.05171  399 SER   A CA   
1813 C  C    . SER   A 247 ? 0.25755 0.34842 0.32549 -0.02747 0.07990  0.03835  399 SER   A C    
1814 O  O    . SER   A 247 ? 0.25859 0.35917 0.34930 -0.02990 0.08299  0.03627  399 SER   A O    
1815 C  CB   . SER   A 247 ? 0.32111 0.42070 0.35765 -0.02501 0.09569  0.05454  399 SER   A CB   
1816 O  OG   . SER   A 247 ? 0.43778 0.55337 0.48357 -0.02266 0.10267  0.04815  399 SER   A OG   
1817 N  N    . LEU   A 248 ? 0.26521 0.34839 0.31955 -0.02259 0.07075  0.02984  400 LEU   A N    
1818 C  CA   . LEU   A 248 ? 0.21144 0.29624 0.27618 -0.01934 0.06407  0.01900  400 LEU   A CA   
1819 C  C    . LEU   A 248 ? 0.22786 0.30720 0.31031 -0.02334 0.05587  0.01752  400 LEU   A C    
1820 O  O    . LEU   A 248 ? 0.24692 0.33521 0.34935 -0.02335 0.05461  0.01279  400 LEU   A O    
1821 C  CB   . LEU   A 248 ? 0.19732 0.27357 0.24401 -0.01366 0.05700  0.01199  400 LEU   A CB   
1822 C  CG   . LEU   A 248 ? 0.23993 0.32349 0.27201 -0.00863 0.06322  0.00838  400 LEU   A CG   
1823 C  CD1  . LEU   A 248 ? 0.20357 0.27560 0.21878 -0.00521 0.05549  0.00289  400 LEU   A CD1  
1824 C  CD2  . LEU   A 248 ? 0.23684 0.33384 0.28239 -0.00459 0.06827  0.00093  400 LEU   A CD2  
1825 N  N    . SER   A 249 ? 0.23562 0.30155 0.31157 -0.02638 0.04995  0.02070  401 SER   A N    
1826 C  CA   . SER   A 249 ? 0.24555 0.30605 0.33479 -0.02941 0.04099  0.01708  401 SER   A CA   
1827 C  C    . SER   A 249 ? 0.28281 0.35005 0.39662 -0.03619 0.04524  0.02009  401 SER   A C    
1828 O  O    . SER   A 249 ? 0.28832 0.35585 0.41793 -0.03860 0.03774  0.01446  401 SER   A O    
1829 C  CB   . SER   A 249 ? 0.23414 0.27891 0.30894 -0.03006 0.03423  0.01825  401 SER   A CB   
1830 O  OG   . SER   A 249 ? 0.25915 0.29887 0.32955 -0.03355 0.04016  0.02712  401 SER   A OG   
1831 N  N    . PHE   A 250 ? 0.23505 0.30834 0.35280 -0.03935 0.05707  0.02887  402 PHE   A N    
1832 C  CA   . PHE   A 250 ? 0.26008 0.34054 0.40478 -0.04653 0.06286  0.03264  402 PHE   A CA   
1833 C  C    . PHE   A 250 ? 0.31374 0.40989 0.48111 -0.04616 0.06202  0.02490  402 PHE   A C    
1834 O  O    . PHE   A 250 ? 0.25692 0.35822 0.45091 -0.05217 0.06098  0.02309  402 PHE   A O    
1835 C  CB   . PHE   A 250 ? 0.31339 0.39832 0.45578 -0.04910 0.07729  0.04571  402 PHE   A CB   
1836 C  CG   . PHE   A 250 ? 0.40778 0.49649 0.57845 -0.05773 0.08443  0.05238  402 PHE   A CG   
1837 C  CD1  . PHE   A 250 ? 0.45149 0.55784 0.64159 -0.06016 0.09528  0.05499  402 PHE   A CD1  
1838 C  CD2  . PHE   A 250 ? 0.43344 0.50810 0.61327 -0.06353 0.08082  0.05565  402 PHE   A CD2  
1839 C  CE1  . PHE   A 250 ? 0.48675 0.59670 0.70592 -0.06902 0.10259  0.06162  402 PHE   A CE1  
1840 C  CE2  . PHE   A 250 ? 0.47741 0.55416 0.68637 -0.07213 0.08750  0.06143  402 PHE   A CE2  
1841 C  CZ   . PHE   A 250 ? 0.46740 0.56185 0.69656 -0.07528 0.09850  0.06488  402 PHE   A CZ   
1842 N  N    . GLN   A 251 ? 0.23251 0.33670 0.39190 -0.03910 0.06224  0.01974  403 GLN   A N    
1843 C  CA   . GLN   A 251 ? 0.22289 0.34214 0.40408 -0.03707 0.06040  0.01202  403 GLN   A CA   
1844 C  C    . GLN   A 251 ? 0.19693 0.31035 0.38057 -0.03459 0.04454  0.00312  403 GLN   A C    
1845 O  O    . GLN   A 251 ? 0.17215 0.27567 0.33482 -0.02864 0.03759  0.00030  403 GLN   A O    
1846 C  CB   . GLN   A 251 ? 0.25870 0.38783 0.43142 -0.02955 0.06675  0.00929  403 GLN   A CB   
1847 C  CG   . GLN   A 251 ? 0.33889 0.47546 0.50340 -0.03045 0.08241  0.01743  403 GLN   A CG   
1848 C  CD   . GLN   A 251 ? 0.41978 0.57011 0.61057 -0.03762 0.09344  0.02387  403 GLN   A CD   
1849 O  OE1  . GLN   A 251 ? 0.48725 0.63575 0.67416 -0.04266 0.10292  0.03517  403 GLN   A OE1  
1850 N  NE2  . GLN   A 251 ? 0.41578 0.58032 0.63497 -0.03806 0.09227  0.01740  403 GLN   A NE2  
1851 N  N    . PRO   A 252 ? 0.22714 0.34701 0.43572 -0.03895 0.03842  -0.00138 404 PRO   A N    
1852 C  CA   . PRO   A 252 ? 0.19366 0.30843 0.40066 -0.03621 0.02262  -0.00937 404 PRO   A CA   
1853 C  C    . PRO   A 252 ? 0.19943 0.31754 0.39852 -0.02651 0.01632  -0.01418 404 PRO   A C    
1854 O  O    . PRO   A 252 ? 0.21744 0.32581 0.40126 -0.02228 0.00548  -0.01694 404 PRO   A O    
1855 C  CB   . PRO   A 252 ? 0.24878 0.37528 0.48834 -0.04257 0.01850  -0.01447 404 PRO   A CB   
1856 C  CG   . PRO   A 252 ? 0.31637 0.44660 0.57142 -0.05095 0.03260  -0.00683 404 PRO   A CG   
1857 C  CD   . PRO   A 252 ? 0.26142 0.39428 0.50115 -0.04671 0.04545  0.00040  404 PRO   A CD   
1858 N  N    . GLU   A 253 ? 0.23520 0.36647 0.44436 -0.02250 0.02350  -0.01484 405 GLU   A N    
1859 C  CA   . GLU   A 253 ? 0.27286 0.40571 0.47674 -0.01266 0.01798  -0.01925 405 GLU   A CA   
1860 C  C    . GLU   A 253 ? 0.24858 0.36448 0.42174 -0.00811 0.01772  -0.01696 405 GLU   A C    
1861 O  O    . GLU   A 253 ? 0.21114 0.32122 0.37625 -0.00114 0.00946  -0.01953 405 GLU   A O    
1862 C  CB   . GLU   A 253 ? 0.30153 0.45213 0.52417 -0.00906 0.02706  -0.02147 405 GLU   A CB   
1863 C  CG   . GLU   A 253 ? 0.42805 0.58010 0.64038 -0.01003 0.04272  -0.01717 405 GLU   A CG   
1864 C  CD   . GLU   A 253 ? 0.45549 0.61682 0.68249 -0.01917 0.05388  -0.01138 405 GLU   A CD   
1865 O  OE1  . GLU   A 253 ? 0.51114 0.68215 0.73836 -0.01904 0.06796  -0.00830 405 GLU   A OE1  
1866 O  OE2  . GLU   A 253 ? 0.40059 0.55950 0.63903 -0.02642 0.04895  -0.00990 405 GLU   A OE2  
1867 N  N    . ASN   A 254 ? 0.21723 0.32531 0.37409 -0.01192 0.02635  -0.01164 406 ASN   A N    
1868 C  CA   . ASN   A 254 ? 0.20856 0.30138 0.33823 -0.00860 0.02514  -0.01019 406 ASN   A CA   
1869 C  C    . ASN   A 254 ? 0.17014 0.24859 0.28718 -0.01082 0.01553  -0.00880 406 ASN   A C    
1870 O  O    . ASN   A 254 ? 0.17935 0.24747 0.28145 -0.00629 0.00928  -0.00978 406 ASN   A O    
1871 C  CB   . ASN   A 254 ? 0.20768 0.29981 0.32416 -0.01085 0.03694  -0.00540 406 ASN   A CB   
1872 C  CG   . ASN   A 254 ? 0.26391 0.37028 0.38739 -0.00721 0.04721  -0.00789 406 ASN   A CG   
1873 O  OD1  . ASN   A 254 ? 0.25623 0.37030 0.39267 -0.00178 0.04516  -0.01397 406 ASN   A OD1  
1874 N  ND2  . ASN   A 254 ? 0.25891 0.36950 0.37348 -0.00952 0.05845  -0.00305 406 ASN   A ND2  
1875 N  N    . SER   A 255 ? 0.19454 0.27213 0.31846 -0.01776 0.01491  -0.00671 407 SER   A N    
1876 C  CA   . SER   A 255 ? 0.20961 0.27497 0.32283 -0.01949 0.00618  -0.00709 407 SER   A CA   
1877 C  C    . SER   A 255 ? 0.21286 0.27906 0.32706 -0.01446 -0.00590 -0.01228 407 SER   A C    
1878 O  O    . SER   A 255 ? 0.19201 0.24738 0.28908 -0.01217 -0.01225 -0.01211 407 SER   A O    
1879 C  CB   . SER   A 255 ? 0.27609 0.34162 0.40220 -0.02751 0.00734  -0.00607 407 SER   A CB   
1880 O  OG   . SER   A 255 ? 0.34856 0.40651 0.46487 -0.03108 0.01597  0.00107  407 SER   A OG   
1881 N  N    . MET   A 256 ? 0.16978 0.24985 0.30402 -0.01226 -0.00893 -0.01625 408 MET   A N    
1882 C  CA   . MET   A 256 ? 0.21659 0.29969 0.35234 -0.00606 -0.02091 -0.01999 408 MET   A CA   
1883 C  C    . MET   A 256 ? 0.24572 0.31838 0.36213 0.00148  -0.02280 -0.01723 408 MET   A C    
1884 O  O    . MET   A 256 ? 0.18783 0.25661 0.29579 0.00606  -0.03247 -0.01715 408 MET   A O    
1885 C  CB   . MET   A 256 ? 0.21061 0.31211 0.37326 -0.00397 -0.02222 -0.02400 408 MET   A CB   
1886 C  CG   . MET   A 256 ? 0.27411 0.38354 0.44506 0.00052  -0.03616 -0.02841 408 MET   A CG   
1887 S  SD   . MET   A 256 ? 0.23427 0.36826 0.44342 -0.00020 -0.03605 -0.03385 408 MET   A SD   
1888 C  CE   . MET   A 256 ? 0.21542 0.35283 0.42812 0.00647  -0.02471 -0.03121 408 MET   A CE   
1889 N  N    . LYS   A 257 ? 0.17838 0.24674 0.28791 0.00283  -0.01365 -0.01497 409 LYS   A N    
1890 C  CA   . LYS   A 257 ? 0.15630 0.21412 0.25128 0.00908  -0.01460 -0.01329 409 LYS   A CA   
1891 C  C    . LYS   A 257 ? 0.16651 0.20884 0.23873 0.00667  -0.01449 -0.00974 409 LYS   A C    
1892 O  O    . LYS   A 257 ? 0.22272 0.25528 0.28375 0.01082  -0.01564 -0.00799 409 LYS   A O    
1893 C  CB   . LYS   A 257 ? 0.20473 0.26618 0.30437 0.01201  -0.00542 -0.01514 409 LYS   A CB   
1894 C  CG   . LYS   A 257 ? 0.28780 0.36559 0.41134 0.01553  -0.00404 -0.01909 409 LYS   A CG   
1895 C  CD   . LYS   A 257 ? 0.42704 0.50609 0.55865 0.02330  -0.01456 -0.01976 409 LYS   A CD   
1896 C  CE   . LYS   A 257 ? 0.50623 0.60431 0.66520 0.02620  -0.01536 -0.02380 409 LYS   A CE   
1897 N  NZ   . LYS   A 257 ? 0.51574 0.61985 0.68331 0.02905  -0.02872 -0.02369 409 LYS   A NZ   
1898 N  N    . LEU   A 258 ? 0.16115 0.20099 0.22848 0.00016  -0.01291 -0.00862 410 LEU   A N    
1899 C  CA   . LEU   A 258 ? 0.18544 0.21217 0.23339 -0.00178 -0.01262 -0.00560 410 LEU   A CA   
1900 C  C    . LEU   A 258 ? 0.16514 0.18707 0.20506 0.00023  -0.02191 -0.00542 410 LEU   A C    
1901 O  O    . LEU   A 258 ? 0.20161 0.22938 0.24810 0.00440  -0.02901 -0.00683 410 LEU   A O    
1902 C  CB   . LEU   A 258 ? 0.18650 0.21234 0.23366 -0.00845 -0.00674 -0.00396 410 LEU   A CB   
1903 C  CG   . LEU   A 258 ? 0.18243 0.21485 0.23509 -0.00982 0.00302  -0.00269 410 LEU   A CG   
1904 C  CD1  . LEU   A 258 ? 0.23696 0.26833 0.28967 -0.01598 0.00862  0.00133  410 LEU   A CD1  
1905 C  CD2  . LEU   A 258 ? 0.17733 0.20526 0.21769 -0.00579 0.00644  -0.00279 410 LEU   A CD2  
1906 N  N    . THR   A 259 ? 0.18666 0.19899 0.21169 -0.00200 -0.02190 -0.00349 411 THR   A N    
1907 C  CA   . THR   A 259 ? 0.21214 0.22069 0.22673 -0.00016 -0.02910 -0.00336 411 THR   A CA   
1908 C  C    . THR   A 259 ? 0.19566 0.20355 0.20956 -0.00530 -0.02983 -0.00649 411 THR   A C    
1909 O  O    . THR   A 259 ? 0.20352 0.20981 0.22176 -0.01008 -0.02377 -0.00619 411 THR   A O    
1910 C  CB   . THR   A 259 ? 0.16621 0.16377 0.16414 0.00238  -0.02779 0.00141  411 THR   A CB   
1911 O  OG1  . THR   A 259 ? 0.19647 0.18759 0.18703 -0.00200 -0.02218 0.00222  411 THR   A OG1  
1912 C  CG2  . THR   A 259 ? 0.21404 0.20930 0.21486 0.00647  -0.02542 0.00381  411 THR   A CG2  
1913 N  N    . PRO   A 260 ? 0.20291 0.21202 0.21128 -0.00397 -0.03718 -0.00960 412 PRO   A N    
1914 C  CA   . PRO   A 260 ? 0.19724 0.20457 0.20567 -0.00848 -0.03788 -0.01447 412 PRO   A CA   
1915 C  C    . PRO   A 260 ? 0.20176 0.19859 0.20058 -0.01106 -0.03088 -0.01120 412 PRO   A C    
1916 O  O    . PRO   A 260 ? 0.22318 0.21780 0.22950 -0.01574 -0.02754 -0.01288 412 PRO   A O    
1917 C  CB   . PRO   A 260 ? 0.23066 0.24102 0.22872 -0.00461 -0.04682 -0.01832 412 PRO   A CB   
1918 C  CG   . PRO   A 260 ? 0.20881 0.22752 0.21118 0.00071  -0.05265 -0.01665 412 PRO   A CG   
1919 C  CD   . PRO   A 260 ? 0.17791 0.19174 0.18148 0.00210  -0.04564 -0.00951 412 PRO   A CD   
1920 N  N    . LEU   A 261 ? 0.19621 0.18663 0.18046 -0.00807 -0.02856 -0.00609 413 LEU   A N    
1921 C  CA   . LEU   A 261 ? 0.22412 0.20643 0.20058 -0.01012 -0.02282 -0.00349 413 LEU   A CA   
1922 C  C    . LEU   A 261 ? 0.21723 0.19885 0.20100 -0.01309 -0.01631 -0.00046 413 LEU   A C    
1923 O  O    . LEU   A 261 ? 0.21635 0.19416 0.20065 -0.01589 -0.01268 0.00049  413 LEU   A O    
1924 C  CB   . LEU   A 261 ? 0.21336 0.19040 0.17543 -0.00682 -0.02185 0.00097  413 LEU   A CB   
1925 C  CG   . LEU   A 261 ? 0.24130 0.21191 0.19652 -0.00858 -0.01682 0.00286  413 LEU   A CG   
1926 C  CD1  . LEU   A 261 ? 0.24919 0.21895 0.20155 -0.00943 -0.01824 -0.00190 413 LEU   A CD1  
1927 C  CD2  . LEU   A 261 ? 0.25203 0.21866 0.19761 -0.00617 -0.01515 0.00764  413 LEU   A CD2  
1928 N  N    . VAL   A 262 ? 0.20969 0.19549 0.19877 -0.01185 -0.01464 0.00120  414 VAL   A N    
1929 C  CA   . VAL   A 262 ? 0.19709 0.18459 0.19114 -0.01409 -0.00817 0.00367  414 VAL   A CA   
1930 C  C    . VAL   A 262 ? 0.19486 0.18556 0.20114 -0.01848 -0.00620 0.00318  414 VAL   A C    
1931 O  O    . VAL   A 262 ? 0.23438 0.22230 0.24037 -0.02099 -0.00136 0.00682  414 VAL   A O    
1932 C  CB   . VAL   A 262 ? 0.20742 0.20025 0.20584 -0.01137 -0.00653 0.00358  414 VAL   A CB   
1933 C  CG1  . VAL   A 262 ? 0.20780 0.20618 0.21224 -0.01359 0.00046  0.00521  414 VAL   A CG1  
1934 C  CG2  . VAL   A 262 ? 0.18663 0.17345 0.17460 -0.00805 -0.00674 0.00471  414 VAL   A CG2  
1935 N  N    . LEU   A 263 ? 0.19318 0.18982 0.21158 -0.01945 -0.01025 -0.00101 415 LEU   A N    
1936 C  CA   . LEU   A 263 ? 0.19649 0.19560 0.23039 -0.02458 -0.00838 -0.00200 415 LEU   A CA   
1937 C  C    . LEU   A 263 ? 0.21568 0.20573 0.24649 -0.02699 -0.00853 -0.00249 415 LEU   A C    
1938 O  O    . LEU   A 263 ? 0.26324 0.25051 0.30249 -0.03080 -0.00350 0.00105  415 LEU   A O    
1939 C  CB   . LEU   A 263 ? 0.21102 0.21907 0.25994 -0.02523 -0.01445 -0.00836 415 LEU   A CB   
1940 C  CG   . LEU   A 263 ? 0.22135 0.24008 0.28008 -0.02335 -0.01275 -0.00764 415 LEU   A CG   
1941 C  CD1  . LEU   A 263 ? 0.18596 0.21521 0.26050 -0.02318 -0.02032 -0.01428 415 LEU   A CD1  
1942 C  CD2  . LEU   A 263 ? 0.19555 0.21772 0.26358 -0.02701 -0.00273 -0.00240 415 LEU   A CD2  
1943 N  N    . GLU   A 264 ? 0.24102 0.22645 0.26020 -0.02440 -0.01367 -0.00633 416 GLU   A N    
1944 C  CA   . GLU   A 264 ? 0.29560 0.27313 0.31298 -0.02587 -0.01368 -0.00846 416 GLU   A CA   
1945 C  C    . GLU   A 264 ? 0.29727 0.26823 0.30776 -0.02569 -0.00740 -0.00112 416 GLU   A C    
1946 O  O    . GLU   A 264 ? 0.29010 0.25566 0.30774 -0.02810 -0.00445 0.00072  416 GLU   A O    
1947 C  CB   . GLU   A 264 ? 0.29927 0.27559 0.30411 -0.02240 -0.01969 -0.01445 416 GLU   A CB   
1948 C  CG   . GLU   A 264 ? 0.33082 0.30093 0.33669 -0.02353 -0.02043 -0.02011 416 GLU   A CG   
1949 C  CD   . GLU   A 264 ? 0.33630 0.30663 0.32645 -0.01940 -0.02464 -0.02539 416 GLU   A CD   
1950 O  OE1  . GLU   A 264 ? 0.34703 0.31279 0.32518 -0.01708 -0.02112 -0.02181 416 GLU   A OE1  
1951 O  OE2  . GLU   A 264 ? 0.35919 0.33551 0.34909 -0.01832 -0.03141 -0.03304 416 GLU   A OE2  
1952 N  N    . VAL   A 265 ? 0.23678 0.20827 0.23493 -0.02271 -0.00571 0.00305  417 VAL   A N    
1953 C  CA   . VAL   A 265 ? 0.21766 0.18471 0.20818 -0.02188 -0.00163 0.00852  417 VAL   A CA   
1954 C  C    . VAL   A 265 ? 0.30615 0.27636 0.30066 -0.02324 0.00381  0.01517  417 VAL   A C    
1955 O  O    . VAL   A 265 ? 0.34819 0.31515 0.34296 -0.02372 0.00696  0.02038  417 VAL   A O    
1956 C  CB   . VAL   A 265 ? 0.23569 0.20211 0.21262 -0.01855 -0.00281 0.00861  417 VAL   A CB   
1957 C  CG1  . VAL   A 265 ? 0.27011 0.23455 0.24125 -0.01784 0.00053  0.01328  417 VAL   A CG1  
1958 C  CG2  . VAL   A 265 ? 0.25892 0.22269 0.22996 -0.01693 -0.00664 0.00389  417 VAL   A CG2  
1959 N  N    . PHE   A 266 ? 0.30446 0.28180 0.30179 -0.02322 0.00519  0.01543  418 PHE   A N    
1960 C  CA   . PHE   A 266 ? 0.26483 0.24726 0.26404 -0.02403 0.01128  0.02140  418 PHE   A CA   
1961 C  C    . PHE   A 266 ? 0.31358 0.29794 0.32845 -0.02814 0.01494  0.02450  418 PHE   A C    
1962 O  O    . PHE   A 266 ? 0.34721 0.33403 0.36314 -0.02912 0.02111  0.03212  418 PHE   A O    
1963 C  CB   . PHE   A 266 ? 0.24504 0.23511 0.24135 -0.02177 0.01243  0.01944  418 PHE   A CB   
1964 C  CG   . PHE   A 266 ? 0.25436 0.24286 0.23724 -0.01843 0.01118  0.01810  418 PHE   A CG   
1965 C  CD1  . PHE   A 266 ? 0.25525 0.24907 0.23620 -0.01603 0.01232  0.01517  418 PHE   A CD1  
1966 C  CD2  . PHE   A 266 ? 0.29490 0.27699 0.26946 -0.01779 0.00909  0.01898  418 PHE   A CD2  
1967 C  CE1  . PHE   A 266 ? 0.27128 0.26303 0.24300 -0.01364 0.01103  0.01273  418 PHE   A CE1  
1968 C  CE2  . PHE   A 266 ? 0.27388 0.25532 0.23948 -0.01561 0.00799  0.01722  418 PHE   A CE2  
1969 C  CZ   . PHE   A 266 ? 0.28517 0.27089 0.24963 -0.01384 0.00878  0.01392  418 PHE   A CZ   
1970 N  N    . GLY   A 267 ? 0.35668 0.34065 0.38408 -0.03061 0.01130  0.01897  419 GLY   A N    
1971 C  CA   . GLY   A 267 ? 0.41061 0.39585 0.45677 -0.03555 0.01465  0.02108  419 GLY   A CA   
1972 C  C    . GLY   A 267 ? 0.46339 0.45851 0.52421 -0.03747 0.01344  0.01615  419 GLY   A C    
1973 O  O    . GLY   A 267 ? 0.33372 0.33632 0.38976 -0.03431 0.01265  0.01405  419 GLY   A O    
1974 N  N    . ASN   A 268 ? 0.50910 0.50434 0.59006 -0.04260 0.01312  0.01383  420 ASN   A N    
1975 C  CA   . ASN   A 268 ? 0.58796 0.59393 0.68755 -0.04517 0.01106  0.00818  420 ASN   A CA   
1976 C  C    . ASN   A 268 ? 0.65999 0.66821 0.78338 -0.05208 0.01816  0.01303  420 ASN   A C    
1977 O  O    . ASN   A 268 ? 0.75514 0.75446 0.88944 -0.05629 0.01795  0.01277  420 ASN   A O    
1978 C  CB   . ASN   A 268 ? 0.63701 0.64256 0.73941 -0.04458 0.00003  -0.00360 420 ASN   A CB   
1979 C  CG   . ASN   A 268 ? 0.68796 0.70721 0.80368 -0.04427 -0.00481 -0.01003 420 ASN   A CG   
1980 O  OD1  . ASN   A 268 ? 0.67077 0.69280 0.78761 -0.04283 -0.01460 -0.01928 420 ASN   A OD1  
1981 N  ND2  . ASN   A 268 ? 0.72466 0.75382 0.85030 -0.04503 0.00196  -0.00525 420 ASN   A ND2  
1982 N  N    . LYS   B 1   ? 0.82537 0.79990 1.03409 -0.02338 0.01456  0.08394  625 LYS   C N    
1983 C  CA   . LYS   B 1   ? 0.76928 0.77250 0.97865 -0.02172 0.00380  0.04826  625 LYS   C CA   
1984 C  C    . LYS   B 1   ? 0.74422 0.73308 0.92378 0.00238  -0.00603 0.02519  625 LYS   C C    
1985 O  O    . LYS   B 1   ? 0.74834 0.71253 0.91247 0.01866  -0.00381 0.03556  625 LYS   C O    
1986 C  CB   . LYS   B 1   ? 0.73839 0.80085 0.94029 -0.02003 0.01038  0.05235  625 LYS   C CB   
1987 C  CG   . LYS   B 1   ? 0.71199 0.78899 0.87227 0.00412  0.01450  0.06198  625 LYS   C CG   
1988 C  CD   . LYS   B 1   ? 0.67841 0.80777 0.83430 0.00906  0.01814  0.05733  625 LYS   C CD   
1989 C  CE   . LYS   B 1   ? 0.62596 0.76404 0.74308 0.03064  0.02038  0.06461  625 LYS   C CE   
1990 N  NZ   . LYS   B 1   ? 0.56093 0.74357 0.67515 0.03391  0.03150  0.06857  625 LYS   C NZ   
1991 N  N    . ASN   B 2   ? 0.69594 0.70394 0.86902 0.00455  -0.01684 -0.00426 626 ASN   C N    
1992 C  CA   . ASN   B 2   ? 0.65823 0.66534 0.79879 0.02590  -0.02164 -0.02136 626 ASN   C CA   
1993 C  C    . ASN   B 2   ? 0.52037 0.56459 0.63735 0.03810  -0.01905 -0.01033 626 ASN   C C    
1994 O  O    . ASN   B 2   ? 0.47255 0.54717 0.59736 0.03184  -0.01685 -0.00065 626 ASN   C O    
1995 C  CB   . ASN   B 2   ? 0.73402 0.74074 0.87012 0.02302  -0.03517 -0.05631 626 ASN   C CB   
1996 C  CG   . ASN   B 2   ? 0.85891 0.81949 1.01006 0.01845  -0.03927 -0.07673 626 ASN   C CG   
1997 O  OD1  . ASN   B 2   ? 0.88299 0.81350 1.06548 0.00567  -0.03611 -0.06389 626 ASN   C OD1  
1998 N  ND2  . ASN   B 2   ? 0.90758 0.86058 1.03504 0.02951  -0.04581 -0.10844 626 ASN   C ND2  
1999 N  N    . HIS   B 3   ? 0.41548 0.45725 0.50776 0.05577  -0.01863 -0.01281 627 HIS   C N    
2000 C  CA   . HIS   B 3   ? 0.31965 0.38777 0.39256 0.06646  -0.01882 -0.00429 627 HIS   C CA   
2001 C  C    . HIS   B 3   ? 0.26535 0.33994 0.31738 0.07470  -0.02422 -0.01960 627 HIS   C C    
2002 O  O    . HIS   B 3   ? 0.26623 0.33939 0.30609 0.08582  -0.02012 -0.01549 627 HIS   C O    
2003 C  CB   . HIS   B 3   ? 0.32758 0.38983 0.39483 0.07661  -0.01304 0.01537  627 HIS   C CB   
2004 C  CG   . HIS   B 3   ? 0.34019 0.39610 0.41770 0.06953  -0.00705 0.03541  627 HIS   C CG   
2005 N  ND1  . HIS   B 3   ? 0.37647 0.40115 0.47055 0.06352  -0.00400 0.04278  627 HIS   C ND1  
2006 C  CD2  . HIS   B 3   ? 0.32787 0.40416 0.39895 0.06780  -0.00249 0.05080  627 HIS   C CD2  
2007 C  CE1  . HIS   B 3   ? 0.39222 0.41850 0.48838 0.05645  0.00256  0.06724  627 HIS   C CE1  
2008 N  NE2  . HIS   B 3   ? 0.37685 0.43762 0.45663 0.05935  0.00490  0.07114  627 HIS   C NE2  
2009 N  N    . PRO   B 4   ? 0.29396 0.37955 0.34200 0.06869  -0.03391 -0.03541 628 PRO   C N    
2010 C  CA   . PRO   B 4   ? 0.27952 0.37033 0.29886 0.07617  -0.03841 -0.04711 628 PRO   C CA   
2011 C  C    . PRO   B 4   ? 0.27521 0.38120 0.27844 0.08487  -0.03867 -0.03165 628 PRO   C C    
2012 O  O    . PRO   B 4   ? 0.31504 0.42124 0.29734 0.09152  -0.03381 -0.03067 628 PRO   C O    
2013 C  CB   . PRO   B 4   ? 0.29778 0.39983 0.31695 0.06712  -0.05404 -0.06498 628 PRO   C CB   
2014 C  CG   . PRO   B 4   ? 0.28811 0.40453 0.34114 0.05683  -0.05702 -0.05660 628 PRO   C CG   
2015 C  CD   . PRO   B 4   ? 0.29149 0.38948 0.36189 0.05438  -0.04196 -0.04219 628 PRO   C CD   
2016 N  N    A MET   B 5   ? 0.26774 0.38657 0.28220 0.08482  -0.04329 -0.02013 629 MET   C N    
2017 N  N    B MET   B 5   ? 0.26746 0.38629 0.28194 0.08480  -0.04330 -0.02017 629 MET   C N    
2018 C  CA   A MET   B 5   ? 0.25536 0.38036 0.25875 0.09260  -0.04660 -0.00784 629 MET   C CA   
2019 C  CA   B MET   B 5   ? 0.25553 0.38055 0.25903 0.09257  -0.04659 -0.00787 629 MET   C CA   
2020 C  C    A MET   B 5   ? 0.26988 0.38594 0.27515 0.09677  -0.03708 0.00291  629 MET   C C    
2021 C  C    B MET   B 5   ? 0.26953 0.38554 0.27477 0.09674  -0.03703 0.00283  629 MET   C C    
2022 O  O    A MET   B 5   ? 0.28969 0.40579 0.28551 0.09967  -0.03605 0.01052  629 MET   C O    
2023 O  O    B MET   B 5   ? 0.28673 0.40276 0.28232 0.09963  -0.03583 0.01028  629 MET   C O    
2024 C  CB   A MET   B 5   ? 0.23220 0.37170 0.24949 0.09498  -0.05520 -0.00476 629 MET   C CB   
2025 C  CB   B MET   B 5   ? 0.23236 0.37186 0.24997 0.09491  -0.05503 -0.00478 629 MET   C CB   
2026 C  CG   A MET   B 5   ? 0.26047 0.41601 0.28010 0.09407  -0.06960 -0.01314 629 MET   C CG   
2027 C  CG   B MET   B 5   ? 0.25680 0.41296 0.27925 0.09297  -0.06860 -0.01410 629 MET   C CG   
2028 S  SD   A MET   B 5   ? 0.27683 0.45716 0.32509 0.10100  -0.07727 -0.01317 629 MET   C SD   
2029 S  SD   B MET   B 5   ? 0.27793 0.46013 0.33010 0.09903  -0.07521 -0.01437 629 MET   C SD   
2030 C  CE   A MET   B 5   ? 0.21101 0.40260 0.28615 0.08928  -0.06100 -0.01632 629 MET   C CE   
2031 C  CE   B MET   B 5   ? 0.26064 0.46824 0.33597 0.08876  -0.08663 -0.02870 629 MET   C CE   
2032 N  N    . LEU   B 6   ? 0.24764 0.35796 0.26687 0.09609  -0.03111 0.00591  630 LEU   C N    
2033 C  CA   . LEU   B 6   ? 0.23564 0.34058 0.25952 0.10114  -0.02618 0.01494  630 LEU   C CA   
2034 C  C    . LEU   B 6   ? 0.28356 0.38459 0.30642 0.10437  -0.01791 0.01067  630 LEU   C C    
2035 O  O    . LEU   B 6   ? 0.29095 0.39951 0.31745 0.10771  -0.01490 0.01745  630 LEU   C O    
2036 C  CB   . LEU   B 6   ? 0.25723 0.35581 0.29074 0.10084  -0.02332 0.02150  630 LEU   C CB   
2037 C  CG   . LEU   B 6   ? 0.37462 0.46848 0.41448 0.10763  -0.02287 0.03244  630 LEU   C CG   
2038 C  CD1  . LEU   B 6   ? 0.38405 0.48890 0.42425 0.11163  -0.02960 0.03553  630 LEU   C CD1  
2039 C  CD2  . LEU   B 6   ? 0.33374 0.42519 0.37084 0.10655  -0.02279 0.04380  630 LEU   C CD2  
2040 N  N    . MET   B 7   ? 0.27159 0.36292 0.29247 0.10315  -0.01368 -0.00274 631 MET   C N    
2041 C  CA   . MET   B 7   ? 0.36542 0.45460 0.38351 0.10994  -0.00328 -0.01291 631 MET   C CA   
2042 C  C    . MET   B 7   ? 0.35077 0.45754 0.34677 0.11036  0.00049  -0.01217 631 MET   C C    
2043 O  O    . MET   B 7   ? 0.35941 0.47795 0.35897 0.11601  0.01273  -0.00903 631 MET   C O    
2044 C  CB   . MET   B 7   ? 0.39625 0.46665 0.41404 0.10862  -0.00259 -0.03359 631 MET   C CB   
2045 C  CG   . MET   B 7   ? 0.47738 0.52375 0.52126 0.11124  -0.00087 -0.03080 631 MET   C CG   
2046 S  SD   . MET   B 7   ? 0.54173 0.58734 0.60333 0.13007  0.01095  -0.03069 631 MET   C SD   
2047 C  CE   . MET   B 7   ? 0.59630 0.64300 0.63847 0.13707  0.02154  -0.06317 631 MET   C CE   
2048 N  N    . ASN   B 8   ? 0.29602 0.40753 0.27143 0.10458  -0.00964 -0.01220 632 ASN   C N    
2049 C  CA   . ASN   B 8   ? 0.31791 0.44278 0.26734 0.10449  -0.00735 -0.00472 632 ASN   C CA   
2050 C  C    . ASN   B 8   ? 0.33953 0.47134 0.30286 0.10288  -0.00445 0.01761  632 ASN   C C    
2051 O  O    . ASN   B 8   ? 0.37233 0.51690 0.32687 0.10193  0.00704  0.02772  632 ASN   C O    
2052 C  CB   . ASN   B 8   ? 0.35089 0.47782 0.27860 0.10094  -0.02411 -0.00565 632 ASN   C CB   
2053 C  CG   . ASN   B 8   ? 0.47848 0.61567 0.37254 0.10127  -0.02341 0.00760  632 ASN   C CG   
2054 O  OD1  . ASN   B 8   ? 0.53053 0.67593 0.39303 0.10366  -0.01505 -0.00193 632 ASN   C OD1  
2055 N  ND2  . ASN   B 8   ? 0.50747 0.64248 0.40622 0.09933  -0.03184 0.03001  632 ASN   C ND2  
2056 N  N    . LEU   B 9   ? 0.25515 0.38024 0.24032 0.10145  -0.01442 0.02484  633 LEU   C N    
2057 C  CA   . LEU   B 9   ? 0.27411 0.40239 0.27618 0.09842  -0.01597 0.04097  633 LEU   C CA   
2058 C  C    . LEU   B 9   ? 0.28718 0.42737 0.31369 0.10050  -0.00377 0.04286  633 LEU   C C    
2059 O  O    . LEU   B 9   ? 0.30625 0.45650 0.35099 0.09509  -0.00225 0.05592  633 LEU   C O    
2060 C  CB   . LEU   B 9   ? 0.26835 0.38676 0.28210 0.09875  -0.03145 0.04172  633 LEU   C CB   
2061 C  CG   . LEU   B 9   ? 0.27945 0.39105 0.28020 0.09957  -0.04435 0.04172  633 LEU   C CG   
2062 C  CD1  . LEU   B 9   ? 0.25119 0.35844 0.26349 0.10401  -0.05475 0.03539  633 LEU   C CD1  
2063 C  CD2  . LEU   B 9   ? 0.33788 0.44409 0.33233 0.09552  -0.04844 0.05829  633 LEU   C CD2  
2064 N  N    . LEU   B 10  ? 0.26197 0.40104 0.29475 0.10812  0.00353  0.03047  634 LEU   C N    
2065 C  CA   . LEU   B 10  ? 0.28739 0.44024 0.34841 0.11490  0.01420  0.03088  634 LEU   C CA   
2066 C  C    . LEU   B 10  ? 0.37934 0.55277 0.43597 0.11800  0.03530  0.02720  634 LEU   C C    
2067 O  O    . LEU   B 10  ? 0.37233 0.56923 0.46004 0.12195  0.04649  0.03176  634 LEU   C O    
2068 C  CB   . LEU   B 10  ? 0.29549 0.43314 0.36738 0.12456  0.01211  0.02128  634 LEU   C CB   
2069 C  CG   . LEU   B 10  ? 0.24185 0.36928 0.32227 0.12381  -0.00385 0.03017  634 LEU   C CG   
2070 C  CD1  . LEU   B 10  ? 0.29084 0.39708 0.37380 0.13007  -0.00452 0.02622  634 LEU   C CD1  
2071 C  CD2  . LEU   B 10  ? 0.24609 0.39165 0.35434 0.12566  -0.01061 0.04116  634 LEU   C CD2  
2072 N  N    . LYS   B 11  ? 0.44669 0.61676 0.46590 0.11720  0.04102  0.01818  635 LYS   C N    
2073 C  CA   . LYS   B 11  ? 0.57066 0.76382 0.57375 0.12120  0.06347  0.01349  635 LYS   C CA   
2074 C  C    . LYS   B 11  ? 0.58161 0.79708 0.58598 0.10943  0.07127  0.03974  635 LYS   C C    
2075 O  O    . LYS   B 11  ? 0.62027 0.82342 0.60656 0.09880  0.05762  0.05545  635 LYS   C O    
2076 C  CB   . LYS   B 11  ? 0.63307 0.81631 0.58760 0.12372  0.06305  -0.00550 635 LYS   C CB   
2077 C  CG   . LYS   B 11  ? 0.68472 0.83836 0.63963 0.12631  0.04697  -0.02589 635 LYS   C CG   
2078 C  CD   . LYS   B 11  ? 0.72263 0.86698 0.70053 0.13980  0.05671  -0.04754 635 LYS   C CD   
2079 C  CE   . LYS   B 11  ? 0.75917 0.87440 0.72346 0.14004  0.04569  -0.07385 635 LYS   C CE   
2080 N  NZ   . LYS   B 11  ? 0.76741 0.88807 0.68426 0.13427  0.03954  -0.08582 635 LYS   C NZ   
2081 C  C10  . A1L70 C .   ? 0.28427 0.27831 0.25608 0.00282  0.01005  -0.04902 501 A1L70 A C10  
2082 C  C13  . A1L70 C .   ? 0.22882 0.23270 0.20330 0.00140  0.01597  -0.02031 501 A1L70 A C13  
2083 C  C15  . A1L70 C .   ? 0.25034 0.25122 0.21045 -0.00414 0.01351  -0.01027 501 A1L70 A C15  
2084 C  C20  . A1L70 C .   ? 0.22462 0.25358 0.23048 -0.00235 0.02503  -0.00568 501 A1L70 A C20  
2085 C  C21  . A1L70 C .   ? 0.21756 0.25316 0.23330 -0.00640 0.02801  -0.00018 501 A1L70 A C21  
2086 C  C22  . A1L70 C .   ? 0.19128 0.20201 0.18389 -0.00679 0.01615  0.00099  501 A1L70 A C22  
2087 C  C26  . A1L70 C .   ? 0.30619 0.23754 0.30587 -0.01515 0.00208  -0.00955 501 A1L70 A C26  
2088 C  C28  . A1L70 C .   ? 0.36305 0.28843 0.35882 -0.01264 0.00301  0.00177  501 A1L70 A C28  
2089 C  C01  . A1L70 C .   ? 0.25970 0.21460 0.24996 -0.00623 0.00141  -0.03170 501 A1L70 A C01  
2090 C  C02  . A1L70 C .   ? 0.26769 0.21960 0.25361 -0.00719 0.00123  -0.02063 501 A1L70 A C02  
2091 C  C03  . A1L70 C .   ? 0.25389 0.21315 0.23111 -0.00663 0.00173  -0.01596 501 A1L70 A C03  
2092 C  C04  . A1L70 C .   ? 0.23567 0.20519 0.20840 -0.00534 0.00328  -0.02002 501 A1L70 A C04  
2093 C  C05  . A1L70 C .   ? 0.25452 0.22832 0.22918 -0.00389 0.00408  -0.03003 501 A1L70 A C05  
2094 C  C06  . A1L70 C .   ? 0.22302 0.18959 0.20637 -0.00423 0.00271  -0.03691 501 A1L70 A C06  
2095 C  C09  . A1L70 C .   ? 0.26889 0.26459 0.23318 -0.00104 0.01116  -0.02472 501 A1L70 A C09  
2096 C  C11  . A1L70 C .   ? 0.26253 0.26119 0.21537 -0.00396 0.00581  -0.03450 501 A1L70 A C11  
2097 C  C12  . A1L70 C .   ? 0.27076 0.26924 0.24304 0.00190  0.01368  -0.02663 501 A1L70 A C12  
2098 C  C14  . A1L70 C .   ? 0.22865 0.23325 0.19733 -0.00201 0.01588  -0.01234 501 A1L70 A C14  
2099 C  C16  . A1L70 C .   ? 0.24729 0.24466 0.20522 -0.00366 0.01107  -0.01640 501 A1L70 A C16  
2100 C  C18  . A1L70 C .   ? 0.18492 0.20003 0.16941 -0.00131 0.02043  -0.00912 501 A1L70 A C18  
2101 C  C19  . A1L70 C .   ? 0.20530 0.22500 0.19667 -0.00440 0.02221  -0.00279 501 A1L70 A C19  
2102 C  C23  . A1L70 C .   ? 0.21111 0.21748 0.21029 -0.00394 0.01043  -0.00180 501 A1L70 A C23  
2103 C  C25  . A1L70 C .   ? 0.31101 0.24717 0.31056 -0.01168 0.00101  -0.01830 501 A1L70 A C25  
2104 C  C29  . A1L70 C .   ? 0.37491 0.29172 0.37656 -0.01541 0.00566  0.00924  501 A1L70 A C29  
2105 C  C30  . A1L70 C .   ? 0.33376 0.25357 0.32433 -0.01595 0.00727  0.01832  501 A1L70 A C30  
2106 O  O07  . A1L70 C .   ? 0.29559 0.23740 0.28609 -0.00876 0.00099  -0.01416 501 A1L70 A O07  
2107 O  O17  . A1L70 C .   ? 0.23591 0.24496 0.20947 -0.00344 0.01805  -0.00664 501 A1L70 A O17  
2108 O  O24  . A1L70 C .   ? 0.17930 0.20411 0.16334 -0.00666 0.02721  0.00201  501 A1L70 A O24  
2109 O  O27  . A1L70 C .   ? 0.34270 0.28297 0.33396 -0.01720 0.00160  -0.00897 501 A1L70 A O27  
2110 O  O31  . A1L70 C .   ? 0.29052 0.20410 0.28134 -0.01602 0.01009  0.02769  501 A1L70 A O31  
2111 O  O32  . A1L70 C .   ? 0.37372 0.30214 0.35497 -0.01604 0.00621  0.01659  501 A1L70 A O32  
2112 SI SI08 . A1L70 C .   ? 0.25220 0.24221 0.21777 -0.00162 0.00771  -0.03437 501 A1L70 A SI08 
# 
