data_8XCL
# 
_entry.id   8XCL 
# 
_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   8XCL         pdb_00008xcl 10.2210/pdb8xcl/pdb 
WWPDB D_1300043204 ?            ?                   
# 
_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       2025-04-23 
_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                        8XCL 
_pdbx_database_status.recvd_initial_deposition_date   2023-12-09 
_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           Y 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              qinwenming@sari.ac.cn 
_pdbx_contact_author.name_first         WENMING 
_pdbx_contact_author.name_last          QIN 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-8157-6647 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Qin, W.M.'  1 ? 
'Zhao, T.'   2 ? 
'Dong, T.'   3 ? 
'Wang, Z.H.' 4 ? 
# 
_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                   US 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            Elife 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           2050-084X 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            13 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     
'Amidase and lysozyme dual functions in TseP reveal a new family of chimeric effectors in the type VI secretion system.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.7554/eLife.101125 
_citation.pdbx_database_id_PubMed   40063082 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Wang, Z.H.' 1 0009-0004-0532-1070 
primary 'An, Y.'     2 0000-0002-8536-6954 
primary 'Zhao, T.'   3 ?                   
primary 'Pei, T.T.'  4 0009-0004-8241-8896 
primary 'Wang, D.Y.' 5 ?                   
primary 'Liang, X.'  6 ?                   
primary 'Qin, W.'    7 ?                   
primary 'Dong, T.'   8 0000-0003-3557-1850 
# 
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 'EF-hand domain-containing protein' 27257.648 1   ? ? ? ? 
2 water   nat water                               18.015    123 ? ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        TseP 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;GTDLITLEMVFAANLNQDKSSCEAILPFLNEYAKTYGMKEERAMAHFLSQVGHESNFKPVSENLRYSPKGMRKIFGCKGG
SKNYDPILDDAKEGRLRPKLWTHESDYAFNPVALGNYVYANRPGSKNGDESSGDGYKYRGRGLIQITHKDAYIKFTEAHN
AANPSDQKDFLASPDDILTLRYATSSAYFFWFIYKKSFNLHSTACTGTVKEVTKIVNGGYAGYADRLKRFNAVAAVIGID
GARE
;
_entity_poly.pdbx_seq_one_letter_code_can   
;GTDLITLEMVFAANLNQDKSSCEAILPFLNEYAKTYGMKEERAMAHFLSQVGHESNFKPVSENLRYSPKGMRKIFGCKGG
SKNYDPILDDAKEGRLRPKLWTHESDYAFNPVALGNYVYANRPGSKNGDESSGDGYKYRGRGLIQITHKDAYIKFTEAHN
AANPSDQKDFLASPDDILTLRYATSSAYFFWFIYKKSFNLHSTACTGTVKEVTKIVNGGYAGYADRLKRFNAVAAVIGID
GARE
;
_entity_poly.pdbx_strand_id                 A 
_entity_poly.pdbx_target_identifier         ? 
# 
_pdbx_entity_nonpoly.entity_id   2 
_pdbx_entity_nonpoly.name        water 
_pdbx_entity_nonpoly.comp_id     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   THR n 
1 3   ASP n 
1 4   LEU n 
1 5   ILE n 
1 6   THR n 
1 7   LEU n 
1 8   GLU n 
1 9   MET n 
1 10  VAL n 
1 11  PHE n 
1 12  ALA n 
1 13  ALA n 
1 14  ASN n 
1 15  LEU n 
1 16  ASN n 
1 17  GLN n 
1 18  ASP n 
1 19  LYS n 
1 20  SER n 
1 21  SER n 
1 22  CYS n 
1 23  GLU n 
1 24  ALA n 
1 25  ILE n 
1 26  LEU n 
1 27  PRO n 
1 28  PHE n 
1 29  LEU n 
1 30  ASN n 
1 31  GLU n 
1 32  TYR n 
1 33  ALA n 
1 34  LYS n 
1 35  THR n 
1 36  TYR n 
1 37  GLY n 
1 38  MET n 
1 39  LYS n 
1 40  GLU n 
1 41  GLU n 
1 42  ARG n 
1 43  ALA n 
1 44  MET n 
1 45  ALA n 
1 46  HIS n 
1 47  PHE n 
1 48  LEU n 
1 49  SER n 
1 50  GLN n 
1 51  VAL n 
1 52  GLY n 
1 53  HIS n 
1 54  GLU n 
1 55  SER n 
1 56  ASN n 
1 57  PHE n 
1 58  LYS n 
1 59  PRO n 
1 60  VAL n 
1 61  SER n 
1 62  GLU n 
1 63  ASN n 
1 64  LEU n 
1 65  ARG n 
1 66  TYR n 
1 67  SER n 
1 68  PRO n 
1 69  LYS n 
1 70  GLY n 
1 71  MET n 
1 72  ARG n 
1 73  LYS n 
1 74  ILE n 
1 75  PHE n 
1 76  GLY n 
1 77  CYS n 
1 78  LYS n 
1 79  GLY n 
1 80  GLY n 
1 81  SER n 
1 82  LYS n 
1 83  ASN n 
1 84  TYR n 
1 85  ASP n 
1 86  PRO n 
1 87  ILE n 
1 88  LEU n 
1 89  ASP n 
1 90  ASP n 
1 91  ALA n 
1 92  LYS n 
1 93  GLU n 
1 94  GLY n 
1 95  ARG n 
1 96  LEU n 
1 97  ARG n 
1 98  PRO n 
1 99  LYS n 
1 100 LEU n 
1 101 TRP n 
1 102 THR n 
1 103 HIS n 
1 104 GLU n 
1 105 SER n 
1 106 ASP n 
1 107 TYR n 
1 108 ALA n 
1 109 PHE n 
1 110 ASN n 
1 111 PRO n 
1 112 VAL n 
1 113 ALA n 
1 114 LEU n 
1 115 GLY n 
1 116 ASN n 
1 117 TYR n 
1 118 VAL n 
1 119 TYR n 
1 120 ALA n 
1 121 ASN n 
1 122 ARG n 
1 123 PRO n 
1 124 GLY n 
1 125 SER n 
1 126 LYS n 
1 127 ASN n 
1 128 GLY n 
1 129 ASP n 
1 130 GLU n 
1 131 SER n 
1 132 SER n 
1 133 GLY n 
1 134 ASP n 
1 135 GLY n 
1 136 TYR n 
1 137 LYS n 
1 138 TYR n 
1 139 ARG n 
1 140 GLY n 
1 141 ARG n 
1 142 GLY n 
1 143 LEU n 
1 144 ILE n 
1 145 GLN n 
1 146 ILE n 
1 147 THR n 
1 148 HIS n 
1 149 LYS n 
1 150 ASP n 
1 151 ALA n 
1 152 TYR n 
1 153 ILE n 
1 154 LYS n 
1 155 PHE n 
1 156 THR n 
1 157 GLU n 
1 158 ALA n 
1 159 HIS n 
1 160 ASN n 
1 161 ALA n 
1 162 ALA n 
1 163 ASN n 
1 164 PRO n 
1 165 SER n 
1 166 ASP n 
1 167 GLN n 
1 168 LYS n 
1 169 ASP n 
1 170 PHE n 
1 171 LEU n 
1 172 ALA n 
1 173 SER n 
1 174 PRO n 
1 175 ASP n 
1 176 ASP n 
1 177 ILE n 
1 178 LEU n 
1 179 THR n 
1 180 LEU n 
1 181 ARG n 
1 182 TYR n 
1 183 ALA n 
1 184 THR n 
1 185 SER n 
1 186 SER n 
1 187 ALA n 
1 188 TYR n 
1 189 PHE n 
1 190 PHE n 
1 191 TRP n 
1 192 PHE n 
1 193 ILE n 
1 194 TYR n 
1 195 LYS n 
1 196 LYS n 
1 197 SER n 
1 198 PHE n 
1 199 ASN n 
1 200 LEU n 
1 201 HIS n 
1 202 SER n 
1 203 THR n 
1 204 ALA n 
1 205 CYS n 
1 206 THR n 
1 207 GLY n 
1 208 THR n 
1 209 VAL n 
1 210 LYS n 
1 211 GLU n 
1 212 VAL n 
1 213 THR n 
1 214 LYS n 
1 215 ILE n 
1 216 VAL n 
1 217 ASN n 
1 218 GLY n 
1 219 GLY n 
1 220 TYR n 
1 221 ALA n 
1 222 GLY n 
1 223 TYR n 
1 224 ALA n 
1 225 ASP n 
1 226 ARG n 
1 227 LEU n 
1 228 LYS n 
1 229 ARG n 
1 230 PHE n 
1 231 ASN n 
1 232 ALA n 
1 233 VAL n 
1 234 ALA n 
1 235 ALA n 
1 236 VAL n 
1 237 ILE n 
1 238 GLY n 
1 239 ILE n 
1 240 ASP n 
1 241 GLY n 
1 242 ALA n 
1 243 ARG n 
1 244 GLU 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                   244 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 HMPREF1171_00947 
_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      'Aeromonas dhakensis' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     196024 
_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                   ? 
# 
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 
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   3   ?   ?   ?   A . n 
A 1 2   THR 2   4   ?   ?   ?   A . n 
A 1 3   ASP 3   5   5   ASP ASP A . n 
A 1 4   LEU 4   6   6   LEU LEU A . n 
A 1 5   ILE 5   7   7   ILE ILE A . n 
A 1 6   THR 6   8   8   THR THR A . n 
A 1 7   LEU 7   9   9   LEU LEU A . n 
A 1 8   GLU 8   10  10  GLU GLU A . n 
A 1 9   MET 9   11  11  MET MET A . n 
A 1 10  VAL 10  12  12  VAL VAL A . n 
A 1 11  PHE 11  13  13  PHE PHE A . n 
A 1 12  ALA 12  14  14  ALA ALA A . n 
A 1 13  ALA 13  15  15  ALA ALA A . n 
A 1 14  ASN 14  16  16  ASN ASN A . n 
A 1 15  LEU 15  17  17  LEU LEU A . n 
A 1 16  ASN 16  18  18  ASN ASN A . n 
A 1 17  GLN 17  19  19  GLN GLN A . n 
A 1 18  ASP 18  20  20  ASP ASP A . n 
A 1 19  LYS 19  21  21  LYS LYS A . n 
A 1 20  SER 20  22  22  SER SER A . n 
A 1 21  SER 21  23  23  SER SER A . n 
A 1 22  CYS 22  24  24  CYS CYS A . n 
A 1 23  GLU 23  25  25  GLU GLU A . n 
A 1 24  ALA 24  26  26  ALA ALA A . n 
A 1 25  ILE 25  27  27  ILE ILE A . n 
A 1 26  LEU 26  28  28  LEU LEU A . n 
A 1 27  PRO 27  29  29  PRO PRO A . n 
A 1 28  PHE 28  30  30  PHE PHE A . n 
A 1 29  LEU 29  31  31  LEU LEU A . n 
A 1 30  ASN 30  32  32  ASN ASN A . n 
A 1 31  GLU 31  33  33  GLU GLU A . n 
A 1 32  TYR 32  34  34  TYR TYR A . n 
A 1 33  ALA 33  35  35  ALA ALA A . n 
A 1 34  LYS 34  36  36  LYS LYS A . n 
A 1 35  THR 35  37  37  THR THR A . n 
A 1 36  TYR 36  38  38  TYR TYR A . n 
A 1 37  GLY 37  39  39  GLY GLY A . n 
A 1 38  MET 38  40  40  MET MET A . n 
A 1 39  LYS 39  41  41  LYS LYS A . n 
A 1 40  GLU 40  42  42  GLU GLU A . n 
A 1 41  GLU 41  43  43  GLU GLU A . n 
A 1 42  ARG 42  44  44  ARG ARG A . n 
A 1 43  ALA 43  45  45  ALA ALA A . n 
A 1 44  MET 44  46  46  MET MET A . n 
A 1 45  ALA 45  47  47  ALA ALA A . n 
A 1 46  HIS 46  48  48  HIS HIS A . n 
A 1 47  PHE 47  49  49  PHE PHE A . n 
A 1 48  LEU 48  50  50  LEU LEU A . n 
A 1 49  SER 49  51  51  SER SER A . n 
A 1 50  GLN 50  52  52  GLN GLN A . n 
A 1 51  VAL 51  53  53  VAL VAL A . n 
A 1 52  GLY 52  54  54  GLY GLY A . n 
A 1 53  HIS 53  55  55  HIS HIS A . n 
A 1 54  GLU 54  56  56  GLU GLU A . n 
A 1 55  SER 55  57  57  SER SER A . n 
A 1 56  ASN 56  58  58  ASN ASN A . n 
A 1 57  PHE 57  59  59  PHE PHE A . n 
A 1 58  LYS 58  60  60  LYS LYS A . n 
A 1 59  PRO 59  61  61  PRO PRO A . n 
A 1 60  VAL 60  62  62  VAL VAL A . n 
A 1 61  SER 61  63  63  SER SER A . n 
A 1 62  GLU 62  64  64  GLU GLU A . n 
A 1 63  ASN 63  65  65  ASN ASN A . n 
A 1 64  LEU 64  66  66  LEU LEU A . n 
A 1 65  ARG 65  67  67  ARG ARG A . n 
A 1 66  TYR 66  68  68  TYR TYR A . n 
A 1 67  SER 67  69  69  SER SER A . n 
A 1 68  PRO 68  70  70  PRO PRO A . n 
A 1 69  LYS 69  71  71  LYS LYS A . n 
A 1 70  GLY 70  72  72  GLY GLY A . n 
A 1 71  MET 71  73  73  MET MET A . n 
A 1 72  ARG 72  74  74  ARG ARG A . n 
A 1 73  LYS 73  75  75  LYS LYS A . n 
A 1 74  ILE 74  76  76  ILE ILE A . n 
A 1 75  PHE 75  77  77  PHE PHE A . n 
A 1 76  GLY 76  78  78  GLY GLY A . n 
A 1 77  CYS 77  79  79  CYS CYS A . n 
A 1 78  LYS 78  80  80  LYS LYS A . n 
A 1 79  GLY 79  81  81  GLY GLY A . n 
A 1 80  GLY 80  82  82  GLY GLY A . n 
A 1 81  SER 81  83  83  SER SER A . n 
A 1 82  LYS 82  84  84  LYS LYS A . n 
A 1 83  ASN 83  85  85  ASN ASN A . n 
A 1 84  TYR 84  86  86  TYR TYR A . n 
A 1 85  ASP 85  87  87  ASP ASP A . n 
A 1 86  PRO 86  88  88  PRO PRO A . n 
A 1 87  ILE 87  89  89  ILE ILE A . n 
A 1 88  LEU 88  90  90  LEU LEU A . n 
A 1 89  ASP 89  91  91  ASP ASP A . n 
A 1 90  ASP 90  92  92  ASP ASP A . n 
A 1 91  ALA 91  93  93  ALA ALA A . n 
A 1 92  LYS 92  94  94  LYS LYS A . n 
A 1 93  GLU 93  95  95  GLU GLU A . n 
A 1 94  GLY 94  96  96  GLY GLY A . n 
A 1 95  ARG 95  97  97  ARG ARG A . n 
A 1 96  LEU 96  98  98  LEU LEU A . n 
A 1 97  ARG 97  99  99  ARG ARG A . n 
A 1 98  PRO 98  100 100 PRO PRO A . n 
A 1 99  LYS 99  101 101 LYS LYS A . n 
A 1 100 LEU 100 102 102 LEU LEU A . n 
A 1 101 TRP 101 103 103 TRP TRP A . n 
A 1 102 THR 102 104 104 THR THR A . n 
A 1 103 HIS 103 105 105 HIS HIS A . n 
A 1 104 GLU 104 106 106 GLU GLU A . n 
A 1 105 SER 105 107 107 SER SER A . n 
A 1 106 ASP 106 108 108 ASP ASP A . n 
A 1 107 TYR 107 109 109 TYR TYR A . n 
A 1 108 ALA 108 110 110 ALA ALA A . n 
A 1 109 PHE 109 111 111 PHE PHE A . n 
A 1 110 ASN 110 112 112 ASN ASN A . n 
A 1 111 PRO 111 113 113 PRO PRO A . n 
A 1 112 VAL 112 114 114 VAL VAL A . n 
A 1 113 ALA 113 115 115 ALA ALA A . n 
A 1 114 LEU 114 116 116 LEU LEU A . n 
A 1 115 GLY 115 117 117 GLY GLY A . n 
A 1 116 ASN 116 118 118 ASN ASN A . n 
A 1 117 TYR 117 119 119 TYR TYR A . n 
A 1 118 VAL 118 120 120 VAL VAL A . n 
A 1 119 TYR 119 121 121 TYR TYR A . n 
A 1 120 ALA 120 122 122 ALA ALA A . n 
A 1 121 ASN 121 123 123 ASN ASN A . n 
A 1 122 ARG 122 124 124 ARG ARG A . n 
A 1 123 PRO 123 125 125 PRO PRO A . n 
A 1 124 GLY 124 126 126 GLY GLY A . n 
A 1 125 SER 125 127 127 SER SER A . n 
A 1 126 LYS 126 128 128 LYS LYS A . n 
A 1 127 ASN 127 129 129 ASN ASN A . n 
A 1 128 GLY 128 130 130 GLY GLY A . n 
A 1 129 ASP 129 131 131 ASP ASP A . n 
A 1 130 GLU 130 132 132 GLU GLU A . n 
A 1 131 SER 131 133 133 SER SER A . n 
A 1 132 SER 132 134 134 SER SER A . n 
A 1 133 GLY 133 135 135 GLY GLY A . n 
A 1 134 ASP 134 136 136 ASP ASP A . n 
A 1 135 GLY 135 137 137 GLY GLY A . n 
A 1 136 TYR 136 138 138 TYR TYR A . n 
A 1 137 LYS 137 139 139 LYS LYS A . n 
A 1 138 TYR 138 140 140 TYR TYR A . n 
A 1 139 ARG 139 141 141 ARG ARG A . n 
A 1 140 GLY 140 142 142 GLY GLY A . n 
A 1 141 ARG 141 143 143 ARG ARG A . n 
A 1 142 GLY 142 144 144 GLY GLY A . n 
A 1 143 LEU 143 145 145 LEU LEU A . n 
A 1 144 ILE 144 146 146 ILE ILE A . n 
A 1 145 GLN 145 147 147 GLN GLN A . n 
A 1 146 ILE 146 148 148 ILE ILE A . n 
A 1 147 THR 147 149 149 THR THR A . n 
A 1 148 HIS 148 150 150 HIS HIS A . n 
A 1 149 LYS 149 151 151 LYS LYS A . n 
A 1 150 ASP 150 152 152 ASP ASP A . n 
A 1 151 ALA 151 153 153 ALA ALA A . n 
A 1 152 TYR 152 154 154 TYR TYR A . n 
A 1 153 ILE 153 155 155 ILE ILE A . n 
A 1 154 LYS 154 156 156 LYS LYS A . n 
A 1 155 PHE 155 157 157 PHE PHE A . n 
A 1 156 THR 156 158 158 THR THR A . n 
A 1 157 GLU 157 159 159 GLU GLU A . n 
A 1 158 ALA 158 160 160 ALA ALA A . n 
A 1 159 HIS 159 161 161 HIS HIS A . n 
A 1 160 ASN 160 162 162 ASN ASN A . n 
A 1 161 ALA 161 163 163 ALA ALA A . n 
A 1 162 ALA 162 164 164 ALA ALA A . n 
A 1 163 ASN 163 165 165 ASN ASN A . n 
A 1 164 PRO 164 166 166 PRO PRO A . n 
A 1 165 SER 165 167 167 SER SER A . n 
A 1 166 ASP 166 168 168 ASP ASP A . n 
A 1 167 GLN 167 169 169 GLN GLN A . n 
A 1 168 LYS 168 170 170 LYS LYS A . n 
A 1 169 ASP 169 171 171 ASP ASP A . n 
A 1 170 PHE 170 172 172 PHE PHE A . n 
A 1 171 LEU 171 173 173 LEU LEU A . n 
A 1 172 ALA 172 174 174 ALA ALA A . n 
A 1 173 SER 173 175 175 SER SER A . n 
A 1 174 PRO 174 176 176 PRO PRO A . n 
A 1 175 ASP 175 177 177 ASP ASP A . n 
A 1 176 ASP 176 178 178 ASP ASP A . n 
A 1 177 ILE 177 179 179 ILE ILE A . n 
A 1 178 LEU 178 180 180 LEU LEU A . n 
A 1 179 THR 179 181 181 THR THR A . n 
A 1 180 LEU 180 182 182 LEU LEU A . n 
A 1 181 ARG 181 183 183 ARG ARG A . n 
A 1 182 TYR 182 184 184 TYR TYR A . n 
A 1 183 ALA 183 185 185 ALA ALA A . n 
A 1 184 THR 184 186 186 THR THR A . n 
A 1 185 SER 185 187 187 SER SER A . n 
A 1 186 SER 186 188 188 SER SER A . n 
A 1 187 ALA 187 189 189 ALA ALA A . n 
A 1 188 TYR 188 190 190 TYR TYR A . n 
A 1 189 PHE 189 191 191 PHE PHE A . n 
A 1 190 PHE 190 192 192 PHE PHE A . n 
A 1 191 TRP 191 193 193 TRP TRP A . n 
A 1 192 PHE 192 194 194 PHE PHE A . n 
A 1 193 ILE 193 195 195 ILE ILE A . n 
A 1 194 TYR 194 196 196 TYR TYR A . n 
A 1 195 LYS 195 197 197 LYS LYS A . n 
A 1 196 LYS 196 198 198 LYS LYS A . n 
A 1 197 SER 197 199 199 SER SER A . n 
A 1 198 PHE 198 200 200 PHE PHE A . n 
A 1 199 ASN 199 201 201 ASN ASN A . n 
A 1 200 LEU 200 202 202 LEU LEU A . n 
A 1 201 HIS 201 203 203 HIS HIS A . n 
A 1 202 SER 202 204 204 SER SER A . n 
A 1 203 THR 203 205 205 THR THR A . n 
A 1 204 ALA 204 206 206 ALA ALA A . n 
A 1 205 CYS 205 207 207 CYS CYS A . n 
A 1 206 THR 206 208 208 THR THR A . n 
A 1 207 GLY 207 209 209 GLY GLY A . n 
A 1 208 THR 208 210 210 THR THR A . n 
A 1 209 VAL 209 211 211 VAL VAL A . n 
A 1 210 LYS 210 212 212 LYS LYS A . n 
A 1 211 GLU 211 213 213 GLU GLU A . n 
A 1 212 VAL 212 214 214 VAL VAL A . n 
A 1 213 THR 213 215 215 THR THR A . n 
A 1 214 LYS 214 216 216 LYS LYS A . n 
A 1 215 ILE 215 217 217 ILE ILE A . n 
A 1 216 VAL 216 218 218 VAL VAL A . n 
A 1 217 ASN 217 219 219 ASN ASN A . n 
A 1 218 GLY 218 220 220 GLY GLY A . n 
A 1 219 GLY 219 221 221 GLY GLY A . n 
A 1 220 TYR 220 222 222 TYR TYR A . n 
A 1 221 ALA 221 223 223 ALA ALA A . n 
A 1 222 GLY 222 224 224 GLY GLY A . n 
A 1 223 TYR 223 225 225 TYR TYR A . n 
A 1 224 ALA 224 226 226 ALA ALA A . n 
A 1 225 ASP 225 227 227 ASP ASP A . n 
A 1 226 ARG 226 228 228 ARG ARG A . n 
A 1 227 LEU 227 229 229 LEU LEU A . n 
A 1 228 LYS 228 230 230 LYS LYS A . n 
A 1 229 ARG 229 231 231 ARG ARG A . n 
A 1 230 PHE 230 232 232 PHE PHE A . n 
A 1 231 ASN 231 233 233 ASN ASN A . n 
A 1 232 ALA 232 234 234 ALA ALA A . n 
A 1 233 VAL 233 235 235 VAL VAL A . n 
A 1 234 ALA 234 236 236 ALA ALA A . n 
A 1 235 ALA 235 237 237 ALA ALA A . n 
A 1 236 VAL 236 238 238 VAL VAL A . n 
A 1 237 ILE 237 239 239 ILE ILE A . n 
A 1 238 GLY 238 240 240 GLY GLY A . n 
A 1 239 ILE 239 241 241 ILE ILE A . n 
A 1 240 ASP 240 242 242 ASP ASP A . n 
A 1 241 GLY 241 243 243 GLY GLY A . n 
A 1 242 ALA 242 244 244 ALA ALA A . n 
A 1 243 ARG 243 245 245 ARG ARG A . n 
A 1 244 GLU 244 246 246 GLU GLU A . n 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
B 2 HOH 1   301 47  HOH HOH A . 
B 2 HOH 2   302 38  HOH HOH A . 
B 2 HOH 3   303 81  HOH HOH A . 
B 2 HOH 4   304 100 HOH HOH A . 
B 2 HOH 5   305 53  HOH HOH A . 
B 2 HOH 6   306 25  HOH HOH A . 
B 2 HOH 7   307 3   HOH HOH A . 
B 2 HOH 8   308 24  HOH HOH A . 
B 2 HOH 9   309 126 HOH HOH A . 
B 2 HOH 10  310 13  HOH HOH A . 
B 2 HOH 11  311 6   HOH HOH A . 
B 2 HOH 12  312 51  HOH HOH A . 
B 2 HOH 13  313 48  HOH HOH A . 
B 2 HOH 14  314 12  HOH HOH A . 
B 2 HOH 15  315 27  HOH HOH A . 
B 2 HOH 16  316 36  HOH HOH A . 
B 2 HOH 17  317 19  HOH HOH A . 
B 2 HOH 18  318 31  HOH HOH A . 
B 2 HOH 19  319 75  HOH HOH A . 
B 2 HOH 20  320 34  HOH HOH A . 
B 2 HOH 21  321 9   HOH HOH A . 
B 2 HOH 22  322 76  HOH HOH A . 
B 2 HOH 23  323 103 HOH HOH A . 
B 2 HOH 24  324 14  HOH HOH A . 
B 2 HOH 25  325 46  HOH HOH A . 
B 2 HOH 26  326 101 HOH HOH A . 
B 2 HOH 27  327 106 HOH HOH A . 
B 2 HOH 28  328 66  HOH HOH A . 
B 2 HOH 29  329 4   HOH HOH A . 
B 2 HOH 30  330 71  HOH HOH A . 
B 2 HOH 31  331 73  HOH HOH A . 
B 2 HOH 32  332 68  HOH HOH A . 
B 2 HOH 33  333 10  HOH HOH A . 
B 2 HOH 34  334 45  HOH HOH A . 
B 2 HOH 35  335 15  HOH HOH A . 
B 2 HOH 36  336 105 HOH HOH A . 
B 2 HOH 37  337 32  HOH HOH A . 
B 2 HOH 38  338 35  HOH HOH A . 
B 2 HOH 39  339 55  HOH HOH A . 
B 2 HOH 40  340 54  HOH HOH A . 
B 2 HOH 41  341 11  HOH HOH A . 
B 2 HOH 42  342 1   HOH HOH A . 
B 2 HOH 43  343 40  HOH HOH A . 
B 2 HOH 44  344 84  HOH HOH A . 
B 2 HOH 45  345 2   HOH HOH A . 
B 2 HOH 46  346 5   HOH HOH A . 
B 2 HOH 47  347 64  HOH HOH A . 
B 2 HOH 48  348 21  HOH HOH A . 
B 2 HOH 49  349 86  HOH HOH A . 
B 2 HOH 50  350 74  HOH HOH A . 
B 2 HOH 51  351 29  HOH HOH A . 
B 2 HOH 52  352 37  HOH HOH A . 
B 2 HOH 53  353 70  HOH HOH A . 
B 2 HOH 54  354 39  HOH HOH A . 
B 2 HOH 55  355 58  HOH HOH A . 
B 2 HOH 56  356 123 HOH HOH A . 
B 2 HOH 57  357 93  HOH HOH A . 
B 2 HOH 58  358 60  HOH HOH A . 
B 2 HOH 59  359 90  HOH HOH A . 
B 2 HOH 60  360 49  HOH HOH A . 
B 2 HOH 61  361 108 HOH HOH A . 
B 2 HOH 62  362 17  HOH HOH A . 
B 2 HOH 63  363 44  HOH HOH A . 
B 2 HOH 64  364 127 HOH HOH A . 
B 2 HOH 65  365 83  HOH HOH A . 
B 2 HOH 66  366 33  HOH HOH A . 
B 2 HOH 67  367 30  HOH HOH A . 
B 2 HOH 68  368 85  HOH HOH A . 
B 2 HOH 69  369 79  HOH HOH A . 
B 2 HOH 70  370 50  HOH HOH A . 
B 2 HOH 71  371 120 HOH HOH A . 
B 2 HOH 72  372 23  HOH HOH A . 
B 2 HOH 73  373 7   HOH HOH A . 
B 2 HOH 74  374 61  HOH HOH A . 
B 2 HOH 75  375 95  HOH HOH A . 
B 2 HOH 76  376 67  HOH HOH A . 
B 2 HOH 77  377 16  HOH HOH A . 
B 2 HOH 78  378 57  HOH HOH A . 
B 2 HOH 79  379 78  HOH HOH A . 
B 2 HOH 80  380 72  HOH HOH A . 
B 2 HOH 81  381 94  HOH HOH A . 
B 2 HOH 82  382 119 HOH HOH A . 
B 2 HOH 83  383 65  HOH HOH A . 
B 2 HOH 84  384 52  HOH HOH A . 
B 2 HOH 85  385 43  HOH HOH A . 
B 2 HOH 86  386 18  HOH HOH A . 
B 2 HOH 87  387 20  HOH HOH A . 
B 2 HOH 88  388 8   HOH HOH A . 
B 2 HOH 89  389 114 HOH HOH A . 
B 2 HOH 90  390 77  HOH HOH A . 
B 2 HOH 91  391 89  HOH HOH A . 
B 2 HOH 92  392 69  HOH HOH A . 
B 2 HOH 93  393 113 HOH HOH A . 
B 2 HOH 94  394 99  HOH HOH A . 
B 2 HOH 95  395 62  HOH HOH A . 
B 2 HOH 96  396 125 HOH HOH A . 
B 2 HOH 97  397 42  HOH HOH A . 
B 2 HOH 98  398 28  HOH HOH A . 
B 2 HOH 99  399 115 HOH HOH A . 
B 2 HOH 100 400 26  HOH HOH A . 
B 2 HOH 101 401 109 HOH HOH A . 
B 2 HOH 102 402 97  HOH HOH A . 
B 2 HOH 103 403 80  HOH HOH A . 
B 2 HOH 104 404 22  HOH HOH A . 
B 2 HOH 105 405 102 HOH HOH A . 
B 2 HOH 106 406 63  HOH HOH A . 
B 2 HOH 107 407 112 HOH HOH A . 
B 2 HOH 108 408 122 HOH HOH A . 
B 2 HOH 109 409 87  HOH HOH A . 
B 2 HOH 110 410 121 HOH HOH A . 
B 2 HOH 111 411 98  HOH HOH A . 
B 2 HOH 112 412 56  HOH HOH A . 
B 2 HOH 113 413 91  HOH HOH A . 
B 2 HOH 114 414 124 HOH HOH A . 
B 2 HOH 115 415 96  HOH HOH A . 
B 2 HOH 116 416 107 HOH HOH A . 
B 2 HOH 117 417 118 HOH HOH A . 
B 2 HOH 118 418 116 HOH HOH A . 
B 2 HOH 119 419 104 HOH HOH A . 
B 2 HOH 120 420 111 HOH HOH A . 
B 2 HOH 121 421 88  HOH HOH A . 
B 2 HOH 122 422 117 HOH HOH A . 
B 2 HOH 123 423 110 HOH HOH A . 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX  ? ? ? 1.16-3549 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS     ? ? ? .         2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? Aimless ? ? ? .         3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHENIX  ? ? ? .         4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.00 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     8XCL 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     44.481 
_cell.length_a_esd                 ? 
_cell.length_b                     138.797 
_cell.length_b_esd                 ? 
_cell.length_c                     95.827 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        8 
_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                         8XCL 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                20 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'C 2 2 21' 
_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                   8XCL 
_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             2.71 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          54.66 
_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, HANGING 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    '0.1 M Sodium formate pH 7.0 ,12% w/v PEG 3350' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            291 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS PILATUS 6M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2021-06-18 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.979 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'SSRF BEAMLINE BL19U1' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.979 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   BL19U1 
_diffrn_source.pdbx_synchrotron_site       SSRF 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       8XCL 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.26 
_reflns.d_resolution_low                               48.1 
_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                                     25776 
_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                           95.9 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                12.9 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          6.10 
_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                                0.236 
_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                                   0.984 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.218 
_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                        ? 
# 
loop_
_reflns_shell.d_res_high 
_reflns_shell.d_res_low 
_reflns_shell.meanI_over_sigI_all 
_reflns_shell.meanI_over_sigI_obs 
_reflns_shell.number_measured_all 
_reflns_shell.number_measured_obs 
_reflns_shell.number_possible 
_reflns_shell.number_unique_all 
_reflns_shell.number_unique_obs 
_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 
_reflns_shell.pdbx_diffrn_id 
_reflns_shell.pdbx_CC_half 
_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 
_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 
2.26 2.4  ? ? ? ? ? ? 4304 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 0.836 ? ? 1 1 0.84  ? ? ? ? 0.771 ? ? ? ? ? ? ? ? ? 
2.40 2.56 ? ? ? ? ? ? 4100 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 0.589 ? ? 2 1 0.919 ? ? ? ? 0.546 ? ? ? ? ? ? ? ? ? 
2.56 2.77 ? ? ? ? ? ? 3790 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 0.422 ? ? 3 1 0.955 ? ? ? ? 0.39  ? ? ? ? ? ? ? ? ? 
2.77 3.03 ? ? ? ? ? ? 3487 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 0.331 ? ? 4 1 0.963 ? ? ? ? 0.306 ? ? ? ? ? ? ? ? ? 
3.03 3.39 ? ? ? ? ? ? 3028 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 0.244 ? ? 5 1 0.974 ? ? ? ? 0.226 ? ? ? ? ? ? ? ? ? 
3.39 3.91 ? ? ? ? ? ? 2040 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 0.188 ? ? 6 1 0.98  ? ? ? ? 0.172 ? ? ? ? ? ? ? ? ? 
3.91 4.78 ? ? ? ? ? ? 2168 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 0.16  ? ? 7 1 0.98  ? ? ? ? 0.147 ? ? ? ? ? ? ? ? ? 
4.78 6.72 ? ? ? ? ? ? 1829 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 0.157 ? ? 8 1 0.981 ? ? ? ? 0.145 ? ? ? ? ? ? ? ? ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               ? 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  ? 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 8XCL 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            2.270 
_refine.ls_d_res_low                             47.914 
_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                     14135 
_refine.ls_number_reflns_R_free                  708 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.94 
_refine.ls_percent_reflns_R_free                 5.01 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1889 
_refine.ls_R_factor_R_free                       0.2274 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1869 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.36 
_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               THROUGHOUT 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      AlphaFold 
_refine.pdbx_stereochemistry_target_values       ML 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.11 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.90 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 21.21 
_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                            0.26 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       2.270 
_refine_hist.d_res_low                        47.914 
_refine_hist.number_atoms_solvent             123 
_refine_hist.number_atoms_total               2033 
_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        1910 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         0 
_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' ? 0.007 ? 1956 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.871 ? 2638 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 6.135 ? 1161 ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.050 ? 272  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.005 ? 345  ? f_plane_restr      ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 2.27   2.4450 . . 138 2623 100.00 . . . . 0.2052 . . . . . . . . . . . 0.2594 
'X-RAY DIFFRACTION' 2.4450 2.6911 . . 139 2642 100.00 . . . . 0.1912 . . . . . . . . . . . 0.2572 
'X-RAY DIFFRACTION' 2.6911 3.0804 . . 140 2654 100.00 . . . . 0.1932 . . . . . . . . . . . 0.2441 
'X-RAY DIFFRACTION' 3.0804 3.8807 . . 142 2706 100.00 . . . . 0.1766 . . . . . . . . . . . 0.2217 
'X-RAY DIFFRACTION' 3.8807 47.9   . . 149 2802 100.00 . . . . 0.1859 . . . . . . . . . . . 0.2073 
# 
_struct.entry_id                     8XCL 
_struct.title                        'Character of TseP: a dual functional effector of type VI secretion system' 
_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        8XCL 
_struct_keywords.text            'T6SS, interspecies interaction, bifunctional effector, peptidoglycan hydrolysis, HYDROLASE' 
_struct_keywords.pdbx_keywords   HYDROLASE 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    K1JFN7_9GAMM 
_struct_ref.pdbx_db_accession          K1JFN7 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;GGDLITLEMVFAANLNQDKSSCEAILPFLNEYAKTYGMKEERAMAHFLSQVGHESNFKPVSENLRYSPKGMRKIFGCKGG
SKNYDPILDDAKEGRLRPKLWTHESDYAFNPVALGNYVYANRPGSKNGDESSGDGYKYRGRGLIQITHKDAYIKFTEAHN
AANPSDQKDFLASPDDILTLRYATSSAYFFWFIYKKSFNLHSTACTGTVKEVTKIVNGGYAGYADRLKRFNAVAAVIGID
GARE
;
_struct_ref.pdbx_align_begin           602 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              8XCL 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 1 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 244 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             K1JFN7 
_struct_ref_seq.db_align_beg                  602 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  845 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       3 
_struct_ref_seq.pdbx_auth_seq_align_end       246 
# 
_struct_ref_seq_dif.align_id                     1 
_struct_ref_seq_dif.pdbx_pdb_id_code             8XCL 
_struct_ref_seq_dif.mon_id                       THR 
_struct_ref_seq_dif.pdbx_pdb_strand_id           A 
_struct_ref_seq_dif.seq_num                      2 
_struct_ref_seq_dif.pdbx_pdb_ins_code            ? 
_struct_ref_seq_dif.pdbx_seq_db_name             UNP 
_struct_ref_seq_dif.pdbx_seq_db_accession_code   K1JFN7 
_struct_ref_seq_dif.db_mon_id                    GLY 
_struct_ref_seq_dif.pdbx_seq_db_seq_num          603 
_struct_ref_seq_dif.details                      conflict 
_struct_ref_seq_dif.pdbx_auth_seq_num            4 
_struct_ref_seq_dif.pdbx_ordinal                 1 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   none 
_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 THR A 6   ? ASN A 14  ? THR A 8   ASN A 16  1 ? 9  
HELX_P HELX_P2  AA2 ASP A 18  ? GLY A 37  ? ASP A 20  GLY A 39  1 ? 20 
HELX_P HELX_P3  AA3 GLU A 40  ? ASN A 56  ? GLU A 42  ASN A 58  1 ? 17 
HELX_P HELX_P4  AA4 SER A 67  ? GLY A 76  ? SER A 69  GLY A 78  1 ? 10 
HELX_P HELX_P5  AA5 GLY A 80  ? LYS A 82  ? GLY A 82  LYS A 84  5 ? 3  
HELX_P HELX_P6  AA6 PRO A 98  ? HIS A 103 ? PRO A 100 HIS A 105 1 ? 6  
HELX_P HELX_P7  AA7 HIS A 103 ? ALA A 108 ? HIS A 105 ALA A 110 1 ? 6  
HELX_P HELX_P8  AA8 ASN A 110 ? TYR A 119 ? ASN A 112 TYR A 121 1 ? 10 
HELX_P HELX_P9  AA9 ASP A 129 ? SER A 132 ? ASP A 131 SER A 134 5 ? 4  
HELX_P HELX_P10 AB1 GLY A 133 ? TYR A 138 ? GLY A 135 TYR A 140 1 ? 6  
HELX_P HELX_P11 AB2 HIS A 148 ? ASN A 163 ? HIS A 150 ASN A 165 1 ? 16 
HELX_P HELX_P12 AB3 SER A 173 ? LEU A 178 ? SER A 175 LEU A 180 5 ? 6  
HELX_P HELX_P13 AB4 THR A 179 ? ILE A 193 ? THR A 181 ILE A 195 1 ? 15 
HELX_P HELX_P14 AB5 LYS A 195 ? PHE A 198 ? LYS A 197 PHE A 200 5 ? 4  
HELX_P HELX_P15 AB6 ASN A 199 ? GLY A 207 ? ASN A 201 GLY A 209 1 ? 9  
HELX_P HELX_P16 AB7 THR A 208 ? GLY A 218 ? THR A 210 GLY A 220 1 ? 11 
HELX_P HELX_P17 AB8 GLY A 222 ? GLY A 238 ? GLY A 224 GLY A 240 1 ? 17 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 2 ? 
AA2 ? 2 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA2 1 2 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 VAL A 60  ? SER A 61  ? VAL A 62  SER A 63  
AA1 2 ARG A 141 ? GLY A 142 ? ARG A 143 GLY A 144 
AA2 1 TYR A 84  ? ASP A 85  ? TYR A 86  ASP A 87  
AA2 2 ASP A 90  ? ALA A 91  ? ASP A 92  ALA A 93  
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N VAL A 60 ? N VAL A 62 O GLY A 142 ? O GLY A 144 
AA2 1 2 N ASP A 85 ? N ASP A 87 O ASP A 90  ? O ASP A 92  
# 
_pdbx_entry_details.entry_id                   8XCL 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_ligand_of_interest     ? 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 LEU A 145 ? ? -96.83 -61.44 
2 1 HIS A 150 ? ? 82.93  156.04 
# 
loop_
_pdbx_struct_special_symmetry.id 
_pdbx_struct_special_symmetry.PDB_model_num 
_pdbx_struct_special_symmetry.auth_asym_id 
_pdbx_struct_special_symmetry.auth_comp_id 
_pdbx_struct_special_symmetry.auth_seq_id 
_pdbx_struct_special_symmetry.PDB_ins_code 
_pdbx_struct_special_symmetry.label_asym_id 
_pdbx_struct_special_symmetry.label_comp_id 
_pdbx_struct_special_symmetry.label_seq_id 
1 1 A HOH 417 ? B HOH . 
2 1 A HOH 421 ? B HOH . 
# 
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 3 ? A GLY 1 
2 1 Y 1 A THR 4 ? A THR 2 
# 
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 
ALA N    N N N 1   
ALA CA   C N S 2   
ALA C    C N N 3   
ALA O    O N N 4   
ALA CB   C N N 5   
ALA OXT  O N N 6   
ALA H    H N N 7   
ALA H2   H N N 8   
ALA HA   H N N 9   
ALA HB1  H N N 10  
ALA HB2  H N N 11  
ALA HB3  H N N 12  
ALA HXT  H N N 13  
ARG N    N N N 14  
ARG CA   C N S 15  
ARG C    C N N 16  
ARG O    O N N 17  
ARG CB   C N N 18  
ARG CG   C N N 19  
ARG CD   C N N 20  
ARG NE   N N N 21  
ARG CZ   C N N 22  
ARG NH1  N N N 23  
ARG NH2  N N N 24  
ARG OXT  O N N 25  
ARG H    H N N 26  
ARG H2   H N N 27  
ARG HA   H N N 28  
ARG HB2  H N N 29  
ARG HB3  H N N 30  
ARG HG2  H N N 31  
ARG HG3  H N N 32  
ARG HD2  H N N 33  
ARG HD3  H N N 34  
ARG HE   H N N 35  
ARG HH11 H N N 36  
ARG HH12 H N N 37  
ARG HH21 H N N 38  
ARG HH22 H N N 39  
ARG HXT  H N N 40  
ASN N    N N N 41  
ASN CA   C N S 42  
ASN C    C N N 43  
ASN O    O N N 44  
ASN CB   C N N 45  
ASN CG   C N N 46  
ASN OD1  O N N 47  
ASN ND2  N N N 48  
ASN OXT  O N N 49  
ASN H    H N N 50  
ASN H2   H N N 51  
ASN HA   H N N 52  
ASN HB2  H N N 53  
ASN HB3  H N N 54  
ASN HD21 H N N 55  
ASN HD22 H N N 56  
ASN HXT  H N N 57  
ASP N    N N N 58  
ASP CA   C N S 59  
ASP C    C N N 60  
ASP O    O N N 61  
ASP CB   C N N 62  
ASP CG   C N N 63  
ASP OD1  O N N 64  
ASP OD2  O N N 65  
ASP OXT  O N N 66  
ASP H    H N N 67  
ASP H2   H N N 68  
ASP HA   H N N 69  
ASP HB2  H N N 70  
ASP HB3  H N N 71  
ASP HD2  H N N 72  
ASP HXT  H N N 73  
CYS N    N N N 74  
CYS CA   C N R 75  
CYS C    C N N 76  
CYS O    O N N 77  
CYS CB   C N N 78  
CYS SG   S N N 79  
CYS OXT  O N N 80  
CYS H    H N N 81  
CYS H2   H N N 82  
CYS HA   H N N 83  
CYS HB2  H N N 84  
CYS HB3  H N N 85  
CYS HG   H N N 86  
CYS HXT  H N N 87  
GLN N    N N N 88  
GLN CA   C N S 89  
GLN C    C N N 90  
GLN O    O N N 91  
GLN CB   C N N 92  
GLN CG   C N N 93  
GLN CD   C N N 94  
GLN OE1  O N N 95  
GLN NE2  N N N 96  
GLN OXT  O N N 97  
GLN H    H N N 98  
GLN H2   H N N 99  
GLN HA   H N N 100 
GLN HB2  H N N 101 
GLN HB3  H N N 102 
GLN HG2  H N N 103 
GLN HG3  H N N 104 
GLN HE21 H N N 105 
GLN HE22 H N N 106 
GLN HXT  H N N 107 
GLU N    N N N 108 
GLU CA   C N S 109 
GLU C    C N N 110 
GLU O    O N N 111 
GLU CB   C N N 112 
GLU CG   C N N 113 
GLU CD   C N N 114 
GLU OE1  O N N 115 
GLU OE2  O N N 116 
GLU OXT  O N N 117 
GLU H    H N N 118 
GLU H2   H N N 119 
GLU HA   H N N 120 
GLU HB2  H N N 121 
GLU HB3  H N N 122 
GLU HG2  H N N 123 
GLU HG3  H N N 124 
GLU HE2  H N N 125 
GLU HXT  H N N 126 
GLY N    N N N 127 
GLY CA   C N N 128 
GLY C    C N N 129 
GLY O    O N N 130 
GLY OXT  O N N 131 
GLY H    H N N 132 
GLY H2   H N N 133 
GLY HA2  H N N 134 
GLY HA3  H N N 135 
GLY HXT  H N N 136 
HIS N    N N N 137 
HIS CA   C N S 138 
HIS C    C N N 139 
HIS O    O N N 140 
HIS CB   C N N 141 
HIS CG   C Y N 142 
HIS ND1  N Y N 143 
HIS CD2  C Y N 144 
HIS CE1  C Y N 145 
HIS NE2  N Y N 146 
HIS OXT  O N N 147 
HIS H    H N N 148 
HIS H2   H N N 149 
HIS HA   H N N 150 
HIS HB2  H N N 151 
HIS HB3  H N N 152 
HIS HD1  H N N 153 
HIS HD2  H N N 154 
HIS HE1  H N N 155 
HIS HE2  H N N 156 
HIS HXT  H N N 157 
HOH O    O N N 158 
HOH H1   H N N 159 
HOH H2   H N N 160 
ILE N    N N N 161 
ILE CA   C N S 162 
ILE C    C N N 163 
ILE O    O N N 164 
ILE CB   C N S 165 
ILE CG1  C N N 166 
ILE CG2  C N N 167 
ILE CD1  C N N 168 
ILE OXT  O N N 169 
ILE H    H N N 170 
ILE H2   H N N 171 
ILE HA   H N N 172 
ILE HB   H N N 173 
ILE HG12 H N N 174 
ILE HG13 H N N 175 
ILE HG21 H N N 176 
ILE HG22 H N N 177 
ILE HG23 H N N 178 
ILE HD11 H N N 179 
ILE HD12 H N N 180 
ILE HD13 H N N 181 
ILE HXT  H N N 182 
LEU N    N N N 183 
LEU CA   C N S 184 
LEU C    C N N 185 
LEU O    O N N 186 
LEU CB   C N N 187 
LEU CG   C N N 188 
LEU CD1  C N N 189 
LEU CD2  C N N 190 
LEU OXT  O N N 191 
LEU H    H N N 192 
LEU H2   H N N 193 
LEU HA   H N N 194 
LEU HB2  H N N 195 
LEU HB3  H N N 196 
LEU HG   H N N 197 
LEU HD11 H N N 198 
LEU HD12 H N N 199 
LEU HD13 H N N 200 
LEU HD21 H N N 201 
LEU HD22 H N N 202 
LEU HD23 H N N 203 
LEU HXT  H N N 204 
LYS N    N N N 205 
LYS CA   C N S 206 
LYS C    C N N 207 
LYS O    O N N 208 
LYS CB   C N N 209 
LYS CG   C N N 210 
LYS CD   C N N 211 
LYS CE   C N N 212 
LYS NZ   N N N 213 
LYS OXT  O N N 214 
LYS H    H N N 215 
LYS H2   H N N 216 
LYS HA   H N N 217 
LYS HB2  H N N 218 
LYS HB3  H N N 219 
LYS HG2  H N N 220 
LYS HG3  H N N 221 
LYS HD2  H N N 222 
LYS HD3  H N N 223 
LYS HE2  H N N 224 
LYS HE3  H N N 225 
LYS HZ1  H N N 226 
LYS HZ2  H N N 227 
LYS HZ3  H N N 228 
LYS HXT  H N N 229 
MET N    N N N 230 
MET CA   C N S 231 
MET C    C N N 232 
MET O    O N N 233 
MET CB   C N N 234 
MET CG   C N N 235 
MET SD   S N N 236 
MET CE   C N N 237 
MET OXT  O N N 238 
MET H    H N N 239 
MET H2   H N N 240 
MET HA   H N N 241 
MET HB2  H N N 242 
MET HB3  H N N 243 
MET HG2  H N N 244 
MET HG3  H N N 245 
MET HE1  H N N 246 
MET HE2  H N N 247 
MET HE3  H N N 248 
MET HXT  H N N 249 
PHE N    N N N 250 
PHE CA   C N S 251 
PHE C    C N N 252 
PHE O    O N N 253 
PHE CB   C N N 254 
PHE CG   C Y N 255 
PHE CD1  C Y N 256 
PHE CD2  C Y N 257 
PHE CE1  C Y N 258 
PHE CE2  C Y N 259 
PHE CZ   C Y N 260 
PHE OXT  O N N 261 
PHE H    H N N 262 
PHE H2   H N N 263 
PHE HA   H N N 264 
PHE HB2  H N N 265 
PHE HB3  H N N 266 
PHE HD1  H N N 267 
PHE HD2  H N N 268 
PHE HE1  H N N 269 
PHE HE2  H N N 270 
PHE HZ   H N N 271 
PHE HXT  H N N 272 
PRO N    N N N 273 
PRO CA   C N S 274 
PRO C    C N N 275 
PRO O    O N N 276 
PRO CB   C N N 277 
PRO CG   C N N 278 
PRO CD   C N N 279 
PRO OXT  O N N 280 
PRO H    H N N 281 
PRO HA   H N N 282 
PRO HB2  H N N 283 
PRO HB3  H N N 284 
PRO HG2  H N N 285 
PRO HG3  H N N 286 
PRO HD2  H N N 287 
PRO HD3  H N N 288 
PRO HXT  H N N 289 
SER N    N N N 290 
SER CA   C N S 291 
SER C    C N N 292 
SER O    O N N 293 
SER CB   C N N 294 
SER OG   O N N 295 
SER OXT  O N N 296 
SER H    H N N 297 
SER H2   H N N 298 
SER HA   H N N 299 
SER HB2  H N N 300 
SER HB3  H N N 301 
SER HG   H N N 302 
SER HXT  H N N 303 
THR N    N N N 304 
THR CA   C N S 305 
THR C    C N N 306 
THR O    O N N 307 
THR CB   C N R 308 
THR OG1  O N N 309 
THR CG2  C N N 310 
THR OXT  O N N 311 
THR H    H N N 312 
THR H2   H N N 313 
THR HA   H N N 314 
THR HB   H N N 315 
THR HG1  H N N 316 
THR HG21 H N N 317 
THR HG22 H N N 318 
THR HG23 H N N 319 
THR HXT  H N N 320 
TRP N    N N N 321 
TRP CA   C N S 322 
TRP C    C N N 323 
TRP O    O N N 324 
TRP CB   C N N 325 
TRP CG   C Y N 326 
TRP CD1  C Y N 327 
TRP CD2  C Y N 328 
TRP NE1  N Y N 329 
TRP CE2  C Y N 330 
TRP CE3  C Y N 331 
TRP CZ2  C Y N 332 
TRP CZ3  C Y N 333 
TRP CH2  C Y N 334 
TRP OXT  O N N 335 
TRP H    H N N 336 
TRP H2   H N N 337 
TRP HA   H N N 338 
TRP HB2  H N N 339 
TRP HB3  H N N 340 
TRP HD1  H N N 341 
TRP HE1  H N N 342 
TRP HE3  H N N 343 
TRP HZ2  H N N 344 
TRP HZ3  H N N 345 
TRP HH2  H N N 346 
TRP HXT  H N N 347 
TYR N    N N N 348 
TYR CA   C N S 349 
TYR C    C N N 350 
TYR O    O N N 351 
TYR CB   C N N 352 
TYR CG   C Y N 353 
TYR CD1  C Y N 354 
TYR CD2  C Y N 355 
TYR CE1  C Y N 356 
TYR CE2  C Y N 357 
TYR CZ   C Y N 358 
TYR OH   O N N 359 
TYR OXT  O N N 360 
TYR H    H N N 361 
TYR H2   H N N 362 
TYR HA   H N N 363 
TYR HB2  H N N 364 
TYR HB3  H N N 365 
TYR HD1  H N N 366 
TYR HD2  H N N 367 
TYR HE1  H N N 368 
TYR HE2  H N N 369 
TYR HH   H N N 370 
TYR HXT  H N N 371 
VAL N    N N N 372 
VAL CA   C N S 373 
VAL C    C N N 374 
VAL O    O N N 375 
VAL CB   C N N 376 
VAL CG1  C N N 377 
VAL CG2  C N N 378 
VAL OXT  O N N 379 
VAL H    H N N 380 
VAL H2   H N N 381 
VAL HA   H N N 382 
VAL HB   H N N 383 
VAL HG11 H N N 384 
VAL HG12 H N N 385 
VAL HG13 H N N 386 
VAL HG21 H N N 387 
VAL HG22 H N N 388 
VAL HG23 H N N 389 
VAL HXT  H N N 390 
# 
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 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
CYS N   CA   sing N N 70  
CYS N   H    sing N N 71  
CYS N   H2   sing N N 72  
CYS CA  C    sing N N 73  
CYS CA  CB   sing N N 74  
CYS CA  HA   sing N N 75  
CYS C   O    doub N N 76  
CYS C   OXT  sing N N 77  
CYS CB  SG   sing N N 78  
CYS CB  HB2  sing N N 79  
CYS CB  HB3  sing N N 80  
CYS SG  HG   sing N N 81  
CYS OXT HXT  sing N N 82  
GLN N   CA   sing N N 83  
GLN N   H    sing N N 84  
GLN N   H2   sing N N 85  
GLN CA  C    sing N N 86  
GLN CA  CB   sing N N 87  
GLN CA  HA   sing N N 88  
GLN C   O    doub N N 89  
GLN C   OXT  sing N N 90  
GLN CB  CG   sing N N 91  
GLN CB  HB2  sing N N 92  
GLN CB  HB3  sing N N 93  
GLN CG  CD   sing N N 94  
GLN CG  HG2  sing N N 95  
GLN CG  HG3  sing N N 96  
GLN CD  OE1  doub N N 97  
GLN CD  NE2  sing N N 98  
GLN NE2 HE21 sing N N 99  
GLN NE2 HE22 sing N N 100 
GLN OXT HXT  sing N N 101 
GLU N   CA   sing N N 102 
GLU N   H    sing N N 103 
GLU N   H2   sing N N 104 
GLU CA  C    sing N N 105 
GLU CA  CB   sing N N 106 
GLU CA  HA   sing N N 107 
GLU C   O    doub N N 108 
GLU C   OXT  sing N N 109 
GLU CB  CG   sing N N 110 
GLU CB  HB2  sing N N 111 
GLU CB  HB3  sing N N 112 
GLU CG  CD   sing N N 113 
GLU CG  HG2  sing N N 114 
GLU CG  HG3  sing N N 115 
GLU CD  OE1  doub N N 116 
GLU CD  OE2  sing N N 117 
GLU OE2 HE2  sing N N 118 
GLU OXT HXT  sing N N 119 
GLY N   CA   sing N N 120 
GLY N   H    sing N N 121 
GLY N   H2   sing N N 122 
GLY CA  C    sing N N 123 
GLY CA  HA2  sing N N 124 
GLY CA  HA3  sing N N 125 
GLY C   O    doub N N 126 
GLY C   OXT  sing N N 127 
GLY OXT HXT  sing N N 128 
HIS N   CA   sing N N 129 
HIS N   H    sing N N 130 
HIS N   H2   sing N N 131 
HIS CA  C    sing N N 132 
HIS CA  CB   sing N N 133 
HIS CA  HA   sing N N 134 
HIS C   O    doub N N 135 
HIS C   OXT  sing N N 136 
HIS CB  CG   sing N N 137 
HIS CB  HB2  sing N N 138 
HIS CB  HB3  sing N N 139 
HIS CG  ND1  sing Y N 140 
HIS CG  CD2  doub Y N 141 
HIS ND1 CE1  doub Y N 142 
HIS ND1 HD1  sing N N 143 
HIS CD2 NE2  sing Y N 144 
HIS CD2 HD2  sing N N 145 
HIS CE1 NE2  sing Y N 146 
HIS CE1 HE1  sing N N 147 
HIS NE2 HE2  sing N N 148 
HIS OXT HXT  sing N N 149 
HOH O   H1   sing N N 150 
HOH O   H2   sing N N 151 
ILE N   CA   sing N N 152 
ILE N   H    sing N N 153 
ILE N   H2   sing N N 154 
ILE CA  C    sing N N 155 
ILE CA  CB   sing N N 156 
ILE CA  HA   sing N N 157 
ILE C   O    doub N N 158 
ILE C   OXT  sing N N 159 
ILE CB  CG1  sing N N 160 
ILE CB  CG2  sing N N 161 
ILE CB  HB   sing N N 162 
ILE CG1 CD1  sing N N 163 
ILE CG1 HG12 sing N N 164 
ILE CG1 HG13 sing N N 165 
ILE CG2 HG21 sing N N 166 
ILE CG2 HG22 sing N N 167 
ILE CG2 HG23 sing N N 168 
ILE CD1 HD11 sing N N 169 
ILE CD1 HD12 sing N N 170 
ILE CD1 HD13 sing N N 171 
ILE OXT HXT  sing N N 172 
LEU N   CA   sing N N 173 
LEU N   H    sing N N 174 
LEU N   H2   sing N N 175 
LEU CA  C    sing N N 176 
LEU CA  CB   sing N N 177 
LEU CA  HA   sing N N 178 
LEU C   O    doub N N 179 
LEU C   OXT  sing N N 180 
LEU CB  CG   sing N N 181 
LEU CB  HB2  sing N N 182 
LEU CB  HB3  sing N N 183 
LEU CG  CD1  sing N N 184 
LEU CG  CD2  sing N N 185 
LEU CG  HG   sing N N 186 
LEU CD1 HD11 sing N N 187 
LEU CD1 HD12 sing N N 188 
LEU CD1 HD13 sing N N 189 
LEU CD2 HD21 sing N N 190 
LEU CD2 HD22 sing N N 191 
LEU CD2 HD23 sing N N 192 
LEU OXT HXT  sing N N 193 
LYS N   CA   sing N N 194 
LYS N   H    sing N N 195 
LYS N   H2   sing N N 196 
LYS CA  C    sing N N 197 
LYS CA  CB   sing N N 198 
LYS CA  HA   sing N N 199 
LYS C   O    doub N N 200 
LYS C   OXT  sing N N 201 
LYS CB  CG   sing N N 202 
LYS CB  HB2  sing N N 203 
LYS CB  HB3  sing N N 204 
LYS CG  CD   sing N N 205 
LYS CG  HG2  sing N N 206 
LYS CG  HG3  sing N N 207 
LYS CD  CE   sing N N 208 
LYS CD  HD2  sing N N 209 
LYS CD  HD3  sing N N 210 
LYS CE  NZ   sing N N 211 
LYS CE  HE2  sing N N 212 
LYS CE  HE3  sing N N 213 
LYS NZ  HZ1  sing N N 214 
LYS NZ  HZ2  sing N N 215 
LYS NZ  HZ3  sing N N 216 
LYS OXT HXT  sing N N 217 
MET N   CA   sing N N 218 
MET N   H    sing N N 219 
MET N   H2   sing N N 220 
MET CA  C    sing N N 221 
MET CA  CB   sing N N 222 
MET CA  HA   sing N N 223 
MET C   O    doub N N 224 
MET C   OXT  sing N N 225 
MET CB  CG   sing N N 226 
MET CB  HB2  sing N N 227 
MET CB  HB3  sing N N 228 
MET CG  SD   sing N N 229 
MET CG  HG2  sing N N 230 
MET CG  HG3  sing N N 231 
MET SD  CE   sing N N 232 
MET CE  HE1  sing N N 233 
MET CE  HE2  sing N N 234 
MET CE  HE3  sing N N 235 
MET OXT HXT  sing N N 236 
PHE N   CA   sing N N 237 
PHE N   H    sing N N 238 
PHE N   H2   sing N N 239 
PHE CA  C    sing N N 240 
PHE CA  CB   sing N N 241 
PHE CA  HA   sing N N 242 
PHE C   O    doub N N 243 
PHE C   OXT  sing N N 244 
PHE CB  CG   sing N N 245 
PHE CB  HB2  sing N N 246 
PHE CB  HB3  sing N N 247 
PHE CG  CD1  doub Y N 248 
PHE CG  CD2  sing Y N 249 
PHE CD1 CE1  sing Y N 250 
PHE CD1 HD1  sing N N 251 
PHE CD2 CE2  doub Y N 252 
PHE CD2 HD2  sing N N 253 
PHE CE1 CZ   doub Y N 254 
PHE CE1 HE1  sing N N 255 
PHE CE2 CZ   sing Y N 256 
PHE CE2 HE2  sing N N 257 
PHE CZ  HZ   sing N N 258 
PHE OXT HXT  sing N N 259 
PRO N   CA   sing N N 260 
PRO N   CD   sing N N 261 
PRO N   H    sing N N 262 
PRO CA  C    sing N N 263 
PRO CA  CB   sing N N 264 
PRO CA  HA   sing N N 265 
PRO C   O    doub N N 266 
PRO C   OXT  sing N N 267 
PRO CB  CG   sing N N 268 
PRO CB  HB2  sing N N 269 
PRO CB  HB3  sing N N 270 
PRO CG  CD   sing N N 271 
PRO CG  HG2  sing N N 272 
PRO CG  HG3  sing N N 273 
PRO CD  HD2  sing N N 274 
PRO CD  HD3  sing N N 275 
PRO OXT HXT  sing N N 276 
SER N   CA   sing N N 277 
SER N   H    sing N N 278 
SER N   H2   sing N N 279 
SER CA  C    sing N N 280 
SER CA  CB   sing N N 281 
SER CA  HA   sing N N 282 
SER C   O    doub N N 283 
SER C   OXT  sing N N 284 
SER CB  OG   sing N N 285 
SER CB  HB2  sing N N 286 
SER CB  HB3  sing N N 287 
SER OG  HG   sing N N 288 
SER OXT HXT  sing N N 289 
THR N   CA   sing N N 290 
THR N   H    sing N N 291 
THR N   H2   sing N N 292 
THR CA  C    sing N N 293 
THR CA  CB   sing N N 294 
THR CA  HA   sing N N 295 
THR C   O    doub N N 296 
THR C   OXT  sing N N 297 
THR CB  OG1  sing N N 298 
THR CB  CG2  sing N N 299 
THR CB  HB   sing N N 300 
THR OG1 HG1  sing N N 301 
THR CG2 HG21 sing N N 302 
THR CG2 HG22 sing N N 303 
THR CG2 HG23 sing N N 304 
THR OXT HXT  sing N N 305 
TRP N   CA   sing N N 306 
TRP N   H    sing N N 307 
TRP N   H2   sing N N 308 
TRP CA  C    sing N N 309 
TRP CA  CB   sing N N 310 
TRP CA  HA   sing N N 311 
TRP C   O    doub N N 312 
TRP C   OXT  sing N N 313 
TRP CB  CG   sing N N 314 
TRP CB  HB2  sing N N 315 
TRP CB  HB3  sing N N 316 
TRP CG  CD1  doub Y N 317 
TRP CG  CD2  sing Y N 318 
TRP CD1 NE1  sing Y N 319 
TRP CD1 HD1  sing N N 320 
TRP CD2 CE2  doub Y N 321 
TRP CD2 CE3  sing Y N 322 
TRP NE1 CE2  sing Y N 323 
TRP NE1 HE1  sing N N 324 
TRP CE2 CZ2  sing Y N 325 
TRP CE3 CZ3  doub Y N 326 
TRP CE3 HE3  sing N N 327 
TRP CZ2 CH2  doub Y N 328 
TRP CZ2 HZ2  sing N N 329 
TRP CZ3 CH2  sing Y N 330 
TRP CZ3 HZ3  sing N N 331 
TRP CH2 HH2  sing N N 332 
TRP OXT HXT  sing N N 333 
TYR N   CA   sing N N 334 
TYR N   H    sing N N 335 
TYR N   H2   sing N N 336 
TYR CA  C    sing N N 337 
TYR CA  CB   sing N N 338 
TYR CA  HA   sing N N 339 
TYR C   O    doub N N 340 
TYR C   OXT  sing N N 341 
TYR CB  CG   sing N N 342 
TYR CB  HB2  sing N N 343 
TYR CB  HB3  sing N N 344 
TYR CG  CD1  doub Y N 345 
TYR CG  CD2  sing Y N 346 
TYR CD1 CE1  sing Y N 347 
TYR CD1 HD1  sing N N 348 
TYR CD2 CE2  doub Y N 349 
TYR CD2 HD2  sing N N 350 
TYR CE1 CZ   doub Y N 351 
TYR CE1 HE1  sing N N 352 
TYR CE2 CZ   sing Y N 353 
TYR CE2 HE2  sing N N 354 
TYR CZ  OH   sing N N 355 
TYR OH  HH   sing N N 356 
TYR OXT HXT  sing N N 357 
VAL N   CA   sing N N 358 
VAL N   H    sing N N 359 
VAL N   H2   sing N N 360 
VAL CA  C    sing N N 361 
VAL CA  CB   sing N N 362 
VAL CA  HA   sing N N 363 
VAL C   O    doub N N 364 
VAL C   OXT  sing N N 365 
VAL CB  CG1  sing N N 366 
VAL CB  CG2  sing N N 367 
VAL CB  HB   sing N N 368 
VAL CG1 HG11 sing N N 369 
VAL CG1 HG12 sing N N 370 
VAL CG1 HG13 sing N N 371 
VAL CG2 HG21 sing N N 372 
VAL CG2 HG22 sing N N 373 
VAL CG2 HG23 sing N N 374 
VAL OXT HXT  sing N N 375 
# 
_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             'in silico model' 
_pdbx_initial_refinement_model.source_name      AlphaFold 
_pdbx_initial_refinement_model.accession_code   ? 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    8XCL 
_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]   0.022482 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.007205 
_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]   0.010435 
_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 
# 
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   . ASP A 1 3   ? 31.280  26.899  3.514   1.00 59.12 ? 5   ASP A N   1 
ATOM   2    C CA  . ASP A 1 3   ? 30.392  26.221  2.572   1.00 55.96 ? 5   ASP A CA  1 
ATOM   3    C C   . ASP A 1 3   ? 29.128  27.021  2.294   1.00 53.15 ? 5   ASP A C   1 
ATOM   4    O O   . ASP A 1 3   ? 28.760  27.914  3.056   1.00 60.74 ? 5   ASP A O   1 
ATOM   5    C CB  . ASP A 1 3   ? 29.979  24.847  3.100   1.00 56.75 ? 5   ASP A CB  1 
ATOM   6    C CG  . ASP A 1 3   ? 31.125  24.085  3.712   1.00 59.89 ? 5   ASP A CG  1 
ATOM   7    O OD1 . ASP A 1 3   ? 31.114  23.901  4.953   1.00 63.65 ? 5   ASP A OD1 1 
ATOM   8    O OD2 . ASP A 1 3   ? 32.022  23.665  2.950   1.00 63.59 ? 5   ASP A OD2 1 
ATOM   9    N N   . LEU A 1 4   ? 28.445  26.673  1.208   1.00 48.90 ? 6   LEU A N   1 
ATOM   10   C CA  . LEU A 1 4   ? 27.108  27.205  0.996   1.00 48.85 ? 6   LEU A CA  1 
ATOM   11   C C   . LEU A 1 4   ? 26.069  26.479  1.848   1.00 47.34 ? 6   LEU A C   1 
ATOM   12   O O   . LEU A 1 4   ? 25.076  27.088  2.267   1.00 43.84 ? 6   LEU A O   1 
ATOM   13   C CB  . LEU A 1 4   ? 26.738  27.116  -0.483  1.00 44.88 ? 6   LEU A CB  1 
ATOM   14   C CG  . LEU A 1 4   ? 25.280  27.515  -0.691  1.00 51.49 ? 6   LEU A CG  1 
ATOM   15   C CD1 . LEU A 1 4   ? 25.091  29.033  -0.729  1.00 51.41 ? 6   LEU A CD1 1 
ATOM   16   C CD2 . LEU A 1 4   ? 24.727  26.848  -1.921  1.00 48.96 ? 6   LEU A CD2 1 
ATOM   17   N N   . ILE A 1 5   ? 26.279  25.195  2.129   1.00 42.81 ? 7   ILE A N   1 
ATOM   18   C CA  . ILE A 1 5   ? 25.324  24.386  2.876   1.00 41.24 ? 7   ILE A CA  1 
ATOM   19   C C   . ILE A 1 5   ? 26.012  23.880  4.140   1.00 41.14 ? 7   ILE A C   1 
ATOM   20   O O   . ILE A 1 5   ? 27.040  23.196  4.064   1.00 39.83 ? 7   ILE A O   1 
ATOM   21   C CB  . ILE A 1 5   ? 24.784  23.226  2.022   1.00 38.93 ? 7   ILE A CB  1 
ATOM   22   C CG1 . ILE A 1 5   ? 24.102  23.774  0.769   1.00 39.65 ? 7   ILE A CG1 1 
ATOM   23   C CG2 . ILE A 1 5   ? 23.796  22.404  2.802   1.00 34.89 ? 7   ILE A CG2 1 
ATOM   24   C CD1 . ILE A 1 5   ? 24.163  22.848  -0.404  1.00 34.72 ? 7   ILE A CD1 1 
ATOM   25   N N   . THR A 1 6   ? 25.456  24.227  5.299   1.00 37.78 ? 8   THR A N   1 
ATOM   26   C CA  . THR A 1 6   ? 25.998  23.799  6.582   1.00 35.95 ? 8   THR A CA  1 
ATOM   27   C C   . THR A 1 6   ? 25.258  22.554  7.062   1.00 36.08 ? 8   THR A C   1 
ATOM   28   O O   . THR A 1 6   ? 24.142  22.259  6.628   1.00 34.46 ? 8   THR A O   1 
ATOM   29   C CB  . THR A 1 6   ? 25.867  24.900  7.647   1.00 40.75 ? 8   THR A CB  1 
ATOM   30   O OG1 . THR A 1 6   ? 24.499  25.312  7.744   1.00 36.76 ? 8   THR A OG1 1 
ATOM   31   C CG2 . THR A 1 6   ? 26.700  26.121  7.280   1.00 37.13 ? 8   THR A CG2 1 
ATOM   32   N N   . LEU A 1 7   ? 25.894  21.828  7.985   1.00 34.85 ? 9   LEU A N   1 
ATOM   33   C CA  . LEU A 1 7   ? 25.227  20.693  8.606   1.00 35.33 ? 9   LEU A CA  1 
ATOM   34   C C   . LEU A 1 7   ? 23.877  21.090  9.211   1.00 39.35 ? 9   LEU A C   1 
ATOM   35   O O   . LEU A 1 7   ? 22.916  20.312  9.148   1.00 35.00 ? 9   LEU A O   1 
ATOM   36   C CB  . LEU A 1 7   ? 26.146  20.073  9.659   1.00 34.91 ? 9   LEU A CB  1 
ATOM   37   C CG  . LEU A 1 7   ? 25.587  18.886  10.438  1.00 36.58 ? 9   LEU A CG  1 
ATOM   38   C CD1 . LEU A 1 7   ? 25.160  17.786  9.476   1.00 33.58 ? 9   LEU A CD1 1 
ATOM   39   C CD2 . LEU A 1 7   ? 26.594  18.350  11.464  1.00 30.28 ? 9   LEU A CD2 1 
ATOM   40   N N   . GLU A 1 8   ? 23.770  22.307  9.759   1.00 40.99 ? 10  GLU A N   1 
ATOM   41   C CA  . GLU A 1 8   ? 22.534  22.716  10.423  1.00 38.64 ? 10  GLU A CA  1 
ATOM   42   C C   . GLU A 1 8   ? 21.393  22.888  9.440   1.00 34.08 ? 10  GLU A C   1 
ATOM   43   O O   . GLU A 1 8   ? 20.230  22.702  9.818   1.00 34.83 ? 10  GLU A O   1 
ATOM   44   C CB  . GLU A 1 8   ? 22.726  24.022  11.212  1.00 39.29 ? 10  GLU A CB  1 
ATOM   45   C CG  . GLU A 1 8   ? 23.980  24.092  12.055  1.00 46.32 ? 10  GLU A CG  1 
ATOM   46   C CD  . GLU A 1 8   ? 25.188  24.553  11.247  1.00 54.30 ? 10  GLU A CD  1 
ATOM   47   O OE1 . GLU A 1 8   ? 25.215  25.739  10.832  1.00 57.47 ? 10  GLU A OE1 1 
ATOM   48   O OE2 . GLU A 1 8   ? 26.100  23.725  11.018  1.00 52.87 ? 10  GLU A OE2 1 
ATOM   49   N N   . MET A 1 9   ? 21.688  23.266  8.192   1.00 33.17 ? 11  MET A N   1 
ATOM   50   C CA  . MET A 1 9   ? 20.624  23.363  7.191   1.00 35.57 ? 11  MET A CA  1 
ATOM   51   C C   . MET A 1 9   ? 20.113  21.985  6.796   1.00 33.42 ? 11  MET A C   1 
ATOM   52   O O   . MET A 1 9   ? 18.906  21.786  6.605   1.00 29.72 ? 11  MET A O   1 
ATOM   53   C CB  . MET A 1 9   ? 21.117  24.103  5.950   1.00 36.55 ? 11  MET A CB  1 
ATOM   54   C CG  . MET A 1 9   ? 21.761  25.428  6.251   1.00 35.97 ? 11  MET A CG  1 
ATOM   55   S SD  . MET A 1 9   ? 22.348  26.196  4.746   1.00 40.85 ? 11  MET A SD  1 
ATOM   56   C CE  . MET A 1 9   ? 22.993  27.701  5.444   1.00 49.16 ? 11  MET A CE  1 
ATOM   57   N N   . VAL A 1 10  ? 21.028  21.028  6.637   1.00 32.92 ? 12  VAL A N   1 
ATOM   58   C CA  . VAL A 1 10  ? 20.633  19.686  6.232   1.00 33.32 ? 12  VAL A CA  1 
ATOM   59   C C   . VAL A 1 10  ? 19.829  19.026  7.344   1.00 29.46 ? 12  VAL A C   1 
ATOM   60   O O   . VAL A 1 10  ? 18.753  18.471  7.108   1.00 30.51 ? 12  VAL A O   1 
ATOM   61   C CB  . VAL A 1 10  ? 21.878  18.863  5.851   1.00 32.53 ? 12  VAL A CB  1 
ATOM   62   C CG1 . VAL A 1 10  ? 21.479  17.493  5.323   1.00 27.53 ? 12  VAL A CG1 1 
ATOM   63   C CG2 . VAL A 1 10  ? 22.701  19.628  4.817   1.00 31.07 ? 12  VAL A CG2 1 
ATOM   64   N N   . PHE A 1 11  ? 20.335  19.109  8.576   1.00 30.36 ? 13  PHE A N   1 
ATOM   65   C CA  . PHE A 1 11  ? 19.635  18.582  9.742   1.00 31.58 ? 13  PHE A CA  1 
ATOM   66   C C   . PHE A 1 11  ? 18.255  19.208  9.896   1.00 32.56 ? 13  PHE A C   1 
ATOM   67   O O   . PHE A 1 11  ? 17.284  18.514  10.221  1.00 33.95 ? 13  PHE A O   1 
ATOM   68   C CB  . PHE A 1 11  ? 20.484  18.841  10.987  1.00 38.23 ? 13  PHE A CB  1 
ATOM   69   C CG  . PHE A 1 11  ? 20.096  18.022  12.197  1.00 36.89 ? 13  PHE A CG  1 
ATOM   70   C CD1 . PHE A 1 11  ? 20.074  16.637  12.147  1.00 34.65 ? 13  PHE A CD1 1 
ATOM   71   C CD2 . PHE A 1 11  ? 19.784  18.648  13.392  1.00 37.73 ? 13  PHE A CD2 1 
ATOM   72   C CE1 . PHE A 1 11  ? 19.728  15.893  13.260  1.00 34.24 ? 13  PHE A CE1 1 
ATOM   73   C CE2 . PHE A 1 11  ? 19.447  17.913  14.511  1.00 38.73 ? 13  PHE A CE2 1 
ATOM   74   C CZ  . PHE A 1 11  ? 19.426  16.533  14.445  1.00 39.32 ? 13  PHE A CZ  1 
ATOM   75   N N   . ALA A 1 12  ? 18.142  20.518  9.663   1.00 29.98 ? 14  ALA A N   1 
ATOM   76   C CA  . ALA A 1 12  ? 16.828  21.151  9.723   1.00 30.64 ? 14  ALA A CA  1 
ATOM   77   C C   . ALA A 1 12  ? 15.901  20.630  8.624   1.00 31.73 ? 14  ALA A C   1 
ATOM   78   O O   . ALA A 1 12  ? 14.715  20.379  8.871   1.00 31.92 ? 14  ALA A O   1 
ATOM   79   C CB  . ALA A 1 12  ? 16.973  22.668  9.634   1.00 30.19 ? 14  ALA A CB  1 
ATOM   80   N N   . ALA A 1 13  ? 16.414  20.469  7.400   1.00 34.51 ? 15  ALA A N   1 
ATOM   81   C CA  . ALA A 1 13  ? 15.589  19.932  6.323   1.00 29.01 ? 15  ALA A CA  1 
ATOM   82   C C   . ALA A 1 13  ? 15.156  18.507  6.619   1.00 30.51 ? 15  ALA A C   1 
ATOM   83   O O   . ALA A 1 13  ? 14.118  18.065  6.115   1.00 28.01 ? 15  ALA A O   1 
ATOM   84   C CB  . ALA A 1 13  ? 16.344  19.978  4.991   1.00 27.68 ? 15  ALA A CB  1 
ATOM   85   N N   . ASN A 1 14  ? 15.940  17.799  7.429   1.00 28.32 ? 16  ASN A N   1 
ATOM   86   C CA  . ASN A 1 14  ? 15.660  16.450  7.875   1.00 30.88 ? 16  ASN A CA  1 
ATOM   87   C C   . ASN A 1 14  ? 14.902  16.420  9.203   1.00 32.91 ? 16  ASN A C   1 
ATOM   88   O O   . ASN A 1 14  ? 14.913  15.390  9.883   1.00 28.65 ? 16  ASN A O   1 
ATOM   89   C CB  . ASN A 1 14  ? 16.969  15.669  7.996   1.00 24.32 ? 16  ASN A CB  1 
ATOM   90   C CG  . ASN A 1 14  ? 16.802  14.219  7.636   1.00 30.40 ? 16  ASN A CG  1 
ATOM   91   O OD1 . ASN A 1 14  ? 15.986  13.878  6.784   1.00 30.40 ? 16  ASN A OD1 1 
ATOM   92   N ND2 . ASN A 1 14  ? 17.577  13.351  8.276   1.00 29.79 ? 16  ASN A ND2 1 
ATOM   93   N N   . LEU A 1 15  ? 14.277  17.535  9.595   1.00 30.73 ? 17  LEU A N   1 
ATOM   94   C CA  . LEU A 1 15  ? 13.428  17.588  10.786  1.00 32.89 ? 17  LEU A CA  1 
ATOM   95   C C   . LEU A 1 15  ? 14.181  17.148  12.036  1.00 34.22 ? 17  LEU A C   1 
ATOM   96   O O   . LEU A 1 15  ? 13.608  16.545  12.949  1.00 32.56 ? 17  LEU A O   1 
ATOM   97   C CB  . LEU A 1 15  ? 12.155  16.759  10.587  1.00 32.62 ? 17  LEU A CB  1 
ATOM   98   C CG  . LEU A 1 15  ? 11.308  17.345  9.447   1.00 30.21 ? 17  LEU A CG  1 
ATOM   99   C CD1 . LEU A 1 15  ? 10.055  16.537  9.149   1.00 30.02 ? 17  LEU A CD1 1 
ATOM   100  C CD2 . LEU A 1 15  ? 10.952  18.785  9.731   1.00 27.09 ? 17  LEU A CD2 1 
ATOM   101  N N   . ASN A 1 16  ? 15.478  17.454  12.068  1.00 34.73 ? 18  ASN A N   1 
ATOM   102  C CA  . ASN A 1 16  ? 16.337  17.176  13.217  1.00 36.81 ? 18  ASN A CA  1 
ATOM   103  C C   . ASN A 1 16  ? 16.403  15.681  13.524  1.00 38.98 ? 18  ASN A C   1 
ATOM   104  O O   . ASN A 1 16  ? 16.371  15.263  14.682  1.00 35.47 ? 18  ASN A O   1 
ATOM   105  C CB  . ASN A 1 16  ? 15.896  17.965  14.448  1.00 37.40 ? 18  ASN A CB  1 
ATOM   106  C CG  . ASN A 1 16  ? 16.032  19.459  14.254  1.00 42.93 ? 18  ASN A CG  1 
ATOM   107  O OD1 . ASN A 1 16  ? 16.888  19.923  13.506  1.00 44.84 ? 18  ASN A OD1 1 
ATOM   108  N ND2 . ASN A 1 16  ? 15.182  20.221  14.921  1.00 52.65 ? 18  ASN A ND2 1 
ATOM   109  N N   . GLN A 1 17  ? 16.522  14.868  12.480  1.00 36.95 ? 19  GLN A N   1 
ATOM   110  C CA  . GLN A 1 17  ? 16.656  13.430  12.639  1.00 38.63 ? 19  GLN A CA  1 
ATOM   111  C C   . GLN A 1 17  ? 17.880  12.940  11.881  1.00 33.71 ? 19  GLN A C   1 
ATOM   112  O O   . GLN A 1 17  ? 18.329  13.575  10.919  1.00 34.28 ? 19  GLN A O   1 
ATOM   113  C CB  . GLN A 1 17  ? 15.386  12.694  12.155  1.00 38.12 ? 19  GLN A CB  1 
ATOM   114  C CG  . GLN A 1 17  ? 14.079  13.217  12.810  1.00 42.07 ? 19  GLN A CG  1 
ATOM   115  C CD  . GLN A 1 17  ? 13.897  12.787  14.283  1.00 40.95 ? 19  GLN A CD  1 
ATOM   116  O OE1 . GLN A 1 17  ? 14.842  12.349  14.946  1.00 47.79 ? 19  GLN A OE1 1 
ATOM   117  N NE2 . GLN A 1 17  ? 12.679  12.930  14.794  1.00 37.12 ? 19  GLN A NE2 1 
ATOM   118  N N   . ASP A 1 18  ? 18.423  11.818  12.353  1.00 33.49 ? 20  ASP A N   1 
ATOM   119  C CA  . ASP A 1 18  ? 19.507  11.076  11.709  1.00 35.53 ? 20  ASP A CA  1 
ATOM   120  C C   . ASP A 1 18  ? 20.677  11.991  11.324  1.00 35.68 ? 20  ASP A C   1 
ATOM   121  O O   . ASP A 1 18  ? 21.016  12.175  10.152  1.00 34.63 ? 20  ASP A O   1 
ATOM   122  C CB  . ASP A 1 18  ? 18.975  10.318  10.492  1.00 38.35 ? 20  ASP A CB  1 
ATOM   123  C CG  . ASP A 1 18  ? 19.937  9.262   9.999   1.00 37.90 ? 20  ASP A CG  1 
ATOM   124  O OD1 . ASP A 1 18  ? 19.613  8.601   8.999   1.00 45.18 ? 20  ASP A OD1 1 
ATOM   125  O OD2 . ASP A 1 18  ? 21.015  9.089   10.605  1.00 40.26 ? 20  ASP A OD2 1 
ATOM   126  N N   . LYS A 1 19  ? 21.296  12.542  12.366  1.00 33.83 ? 21  LYS A N   1 
ATOM   127  C CA  . LYS A 1 19  ? 22.387  13.494  12.186  1.00 35.12 ? 21  LYS A CA  1 
ATOM   128  C C   . LYS A 1 19  ? 23.499  12.941  11.305  1.00 32.11 ? 21  LYS A C   1 
ATOM   129  O O   . LYS A 1 19  ? 24.093  13.678  10.513  1.00 35.71 ? 21  LYS A O   1 
ATOM   130  C CB  . LYS A 1 19  ? 22.949  13.888  13.550  1.00 34.99 ? 21  LYS A CB  1 
ATOM   131  C CG  . LYS A 1 19  ? 24.030  14.953  13.506  1.00 39.15 ? 21  LYS A CG  1 
ATOM   132  C CD  . LYS A 1 19  ? 24.736  15.042  14.855  1.00 47.35 ? 21  LYS A CD  1 
ATOM   133  C CE  . LYS A 1 19  ? 25.154  16.473  15.177  1.00 51.96 ? 21  LYS A CE  1 
ATOM   134  N NZ  . LYS A 1 19  ? 24.023  17.433  15.034  1.00 50.42 ? 21  LYS A NZ  1 
ATOM   135  N N   . SER A 1 20  ? 23.814  11.652  11.441  1.00 28.58 ? 22  SER A N   1 
ATOM   136  C CA  . SER A 1 20  ? 24.973  11.117  10.736  1.00 30.79 ? 22  SER A CA  1 
ATOM   137  C C   . SER A 1 20  ? 24.697  10.953  9.243   1.00 34.83 ? 22  SER A C   1 
ATOM   138  O O   . SER A 1 20  ? 25.596  11.171  8.426   1.00 29.86 ? 22  SER A O   1 
ATOM   139  C CB  . SER A 1 20  ? 25.409  9.797   11.360  1.00 30.79 ? 22  SER A CB  1 
ATOM   140  O OG  . SER A 1 20  ? 24.469  8.786   11.085  1.00 43.80 ? 22  SER A OG  1 
ATOM   141  N N   . SER A 1 21  ? 23.465  10.597  8.867   1.00 35.02 ? 23  SER A N   1 
ATOM   142  C CA  . SER A 1 21  ? 23.083  10.667  7.461   1.00 33.12 ? 23  SER A CA  1 
ATOM   143  C C   . SER A 1 21  ? 23.269  12.081  6.922   1.00 31.75 ? 23  SER A C   1 
ATOM   144  O O   . SER A 1 21  ? 23.751  12.269  5.799   1.00 30.79 ? 23  SER A O   1 
ATOM   145  C CB  . SER A 1 21  ? 21.635  10.211  7.281   1.00 31.38 ? 23  SER A CB  1 
ATOM   146  O OG  . SER A 1 21  ? 21.567  8.797   7.162   1.00 33.84 ? 23  SER A OG  1 
ATOM   147  N N   . CYS A 1 22  ? 22.908  13.090  7.714   1.00 30.37 ? 24  CYS A N   1 
ATOM   148  C CA  . CYS A 1 22  ? 23.117  14.459  7.265   1.00 29.69 ? 24  CYS A CA  1 
ATOM   149  C C   . CYS A 1 22  ? 24.602  14.765  7.109   1.00 30.25 ? 24  CYS A C   1 
ATOM   150  O O   . CYS A 1 22  ? 25.003  15.432  6.153   1.00 31.63 ? 24  CYS A O   1 
ATOM   151  C CB  . CYS A 1 22  ? 22.441  15.436  8.225   1.00 27.72 ? 24  CYS A CB  1 
ATOM   152  S SG  . CYS A 1 22  ? 20.670  15.174  8.387   1.00 29.76 ? 24  CYS A SG  1 
ATOM   153  N N   . GLU A 1 23  ? 25.436  14.256  8.015   1.00 29.14 ? 25  GLU A N   1 
ATOM   154  C CA  . GLU A 1 23  ? 26.874  14.483  7.903   1.00 30.25 ? 25  GLU A CA  1 
ATOM   155  C C   . GLU A 1 23  ? 27.464  13.765  6.694   1.00 31.37 ? 25  GLU A C   1 
ATOM   156  O O   . GLU A 1 23  ? 28.342  14.305  6.016   1.00 34.08 ? 25  GLU A O   1 
ATOM   157  C CB  . GLU A 1 23  ? 27.579  14.019  9.175   1.00 32.22 ? 25  GLU A CB  1 
ATOM   158  C CG  . GLU A 1 23  ? 27.325  14.891  10.368  1.00 33.93 ? 25  GLU A CG  1 
ATOM   159  C CD  . GLU A 1 23  ? 27.755  14.229  11.644  1.00 39.88 ? 25  GLU A CD  1 
ATOM   160  O OE1 . GLU A 1 23  ? 27.517  13.011  11.802  1.00 44.86 ? 25  GLU A OE1 1 
ATOM   161  O OE2 . GLU A 1 23  ? 28.357  14.922  12.483  1.00 49.51 ? 25  GLU A OE2 1 
ATOM   162  N N   . ALA A 1 24  ? 27.002  12.547  6.415   1.00 31.22 ? 26  ALA A N   1 
ATOM   163  C CA  . ALA A 1 24  ? 27.557  11.778  5.304   1.00 32.67 ? 26  ALA A CA  1 
ATOM   164  C C   . ALA A 1 24  ? 27.298  12.454  3.957   1.00 33.15 ? 26  ALA A C   1 
ATOM   165  O O   . ALA A 1 24  ? 28.160  12.435  3.073   1.00 32.49 ? 26  ALA A O   1 
ATOM   166  C CB  . ALA A 1 24  ? 26.984  10.359  5.319   1.00 32.08 ? 26  ALA A CB  1 
ATOM   167  N N   . ILE A 1 25  ? 26.125  13.068  3.778   1.00 32.38 ? 27  ILE A N   1 
ATOM   168  C CA  . ILE A 1 25  ? 25.796  13.623  2.469   1.00 32.11 ? 27  ILE A CA  1 
ATOM   169  C C   . ILE A 1 25  ? 26.248  15.072  2.302   1.00 29.54 ? 27  ILE A C   1 
ATOM   170  O O   . ILE A 1 25  ? 26.351  15.546  1.162   1.00 33.01 ? 27  ILE A O   1 
ATOM   171  C CB  . ILE A 1 25  ? 24.285  13.494  2.184   1.00 33.97 ? 27  ILE A CB  1 
ATOM   172  C CG1 . ILE A 1 25  ? 24.022  13.474  0.673   1.00 29.40 ? 27  ILE A CG1 1 
ATOM   173  C CG2 . ILE A 1 25  ? 23.503  14.601  2.862   1.00 25.55 ? 27  ILE A CG2 1 
ATOM   174  C CD1 . ILE A 1 25  ? 22.657  12.943  0.301   1.00 29.98 ? 27  ILE A CD1 1 
ATOM   175  N N   . LEU A 1 26  ? 26.553  15.769  3.396   1.00 31.48 ? 28  LEU A N   1 
ATOM   176  C CA  . LEU A 1 26  ? 26.953  17.178  3.354   1.00 30.79 ? 28  LEU A CA  1 
ATOM   177  C C   . LEU A 1 26  ? 28.042  17.504  2.335   1.00 28.91 ? 28  LEU A C   1 
ATOM   178  O O   . LEU A 1 26  ? 27.882  18.492  1.600   1.00 33.53 ? 28  LEU A O   1 
ATOM   179  C CB  . LEU A 1 26  ? 27.386  17.613  4.765   1.00 32.75 ? 28  LEU A CB  1 
ATOM   180  C CG  . LEU A 1 26  ? 27.696  19.100  4.954   1.00 33.11 ? 28  LEU A CG  1 
ATOM   181  C CD1 . LEU A 1 26  ? 26.530  19.939  4.469   1.00 32.13 ? 28  LEU A CD1 1 
ATOM   182  C CD2 . LEU A 1 26  ? 27.993  19.391  6.414   1.00 30.47 ? 28  LEU A CD2 1 
ATOM   183  N N   . PRO A 1 27  ? 29.152  16.763  2.230   1.00 29.73 ? 29  PRO A N   1 
ATOM   184  C CA  . PRO A 1 27  ? 30.184  17.168  1.249   1.00 31.10 ? 29  PRO A CA  1 
ATOM   185  C C   . PRO A 1 27  ? 29.695  17.102  -0.188  1.00 32.24 ? 29  PRO A C   1 
ATOM   186  O O   . PRO A 1 27  ? 29.984  18.007  -0.980  1.00 30.87 ? 29  PRO A O   1 
ATOM   187  C CB  . PRO A 1 27  ? 31.334  16.177  1.495   1.00 23.62 ? 29  PRO A CB  1 
ATOM   188  C CG  . PRO A 1 27  ? 31.005  15.483  2.776   1.00 33.04 ? 29  PRO A CG  1 
ATOM   189  C CD  . PRO A 1 27  ? 29.514  15.504  2.904   1.00 30.03 ? 29  PRO A CD  1 
ATOM   190  N N   . PHE A 1 28  ? 28.956  16.048  -0.545  1.00 31.17 ? 30  PHE A N   1 
ATOM   191  C CA  . PHE A 1 28  ? 28.413  15.957  -1.893  1.00 29.20 ? 30  PHE A CA  1 
ATOM   192  C C   . PHE A 1 28  ? 27.430  17.084  -2.157  1.00 28.92 ? 30  PHE A C   1 
ATOM   193  O O   . PHE A 1 28  ? 27.459  17.696  -3.228  1.00 29.36 ? 30  PHE A O   1 
ATOM   194  C CB  . PHE A 1 28  ? 27.756  14.598  -2.096  1.00 26.87 ? 30  PHE A CB  1 
ATOM   195  C CG  . PHE A 1 28  ? 28.649  13.449  -1.725  1.00 28.11 ? 30  PHE A CG  1 
ATOM   196  C CD1 . PHE A 1 28  ? 29.838  13.231  -2.411  1.00 30.51 ? 30  PHE A CD1 1 
ATOM   197  C CD2 . PHE A 1 28  ? 28.317  12.602  -0.687  1.00 26.31 ? 30  PHE A CD2 1 
ATOM   198  C CE1 . PHE A 1 28  ? 30.674  12.175  -2.081  1.00 29.62 ? 30  PHE A CE1 1 
ATOM   199  C CE2 . PHE A 1 28  ? 29.141  11.544  -0.356  1.00 28.31 ? 30  PHE A CE2 1 
ATOM   200  C CZ  . PHE A 1 28  ? 30.330  11.333  -1.050  1.00 26.92 ? 30  PHE A CZ  1 
ATOM   201  N N   . LEU A 1 29  ? 26.574  17.394  -1.180  1.00 27.78 ? 31  LEU A N   1 
ATOM   202  C CA  . LEU A 1 29  ? 25.667  18.532  -1.325  1.00 28.17 ? 31  LEU A CA  1 
ATOM   203  C C   . LEU A 1 29  ? 26.417  19.811  -1.682  1.00 28.55 ? 31  LEU A C   1 
ATOM   204  O O   . LEU A 1 29  ? 25.969  20.586  -2.541  1.00 29.96 ? 31  LEU A O   1 
ATOM   205  C CB  . LEU A 1 29  ? 24.865  18.737  -0.041  1.00 27.75 ? 31  LEU A CB  1 
ATOM   206  C CG  . LEU A 1 29  ? 23.622  17.871  0.150   1.00 28.65 ? 31  LEU A CG  1 
ATOM   207  C CD1 . LEU A 1 29  ? 23.095  17.971  1.575   1.00 23.50 ? 31  LEU A CD1 1 
ATOM   208  C CD2 . LEU A 1 29  ? 22.548  18.251  -0.857  1.00 27.40 ? 31  LEU A CD2 1 
ATOM   209  N N   . ASN A 1 30  ? 27.552  20.062  -1.026  1.00 30.95 ? 32  ASN A N   1 
ATOM   210  C CA  . ASN A 1 30  ? 28.319  21.269  -1.331  1.00 33.94 ? 32  ASN A CA  1 
ATOM   211  C C   . ASN A 1 30  ? 29.076  21.148  -2.650  1.00 29.34 ? 32  ASN A C   1 
ATOM   212  O O   . ASN A 1 30  ? 29.108  22.106  -3.429  1.00 28.75 ? 32  ASN A O   1 
ATOM   213  C CB  . ASN A 1 30  ? 29.274  21.591  -0.181  1.00 31.54 ? 32  ASN A CB  1 
ATOM   214  C CG  . ASN A 1 30  ? 28.576  22.307  0.949   1.00 37.32 ? 32  ASN A CG  1 
ATOM   215  O OD1 . ASN A 1 30  ? 28.025  23.389  0.755   1.00 38.72 ? 32  ASN A OD1 1 
ATOM   216  N ND2 . ASN A 1 30  ? 28.567  21.699  2.131   1.00 35.66 ? 32  ASN A ND2 1 
ATOM   217  N N   . GLU A 1 31  ? 29.664  19.976  -2.929  1.00 28.02 ? 33  GLU A N   1 
ATOM   218  C CA  . GLU A 1 31  ? 30.419  19.801  -4.171  1.00 31.61 ? 33  GLU A CA  1 
ATOM   219  C C   . GLU A 1 31  ? 29.548  20.096  -5.388  1.00 31.03 ? 33  GLU A C   1 
ATOM   220  O O   . GLU A 1 31  ? 29.934  20.877  -6.267  1.00 32.67 ? 33  GLU A O   1 
ATOM   221  C CB  . GLU A 1 31  ? 31.006  18.387  -4.257  1.00 27.39 ? 33  GLU A CB  1 
ATOM   222  C CG  . GLU A 1 31  ? 31.938  18.194  -5.463  1.00 30.85 ? 33  GLU A CG  1 
ATOM   223  C CD  . GLU A 1 31  ? 32.599  16.808  -5.520  1.00 43.67 ? 33  GLU A CD  1 
ATOM   224  O OE1 . GLU A 1 31  ? 32.573  16.080  -4.510  1.00 41.26 ? 33  GLU A OE1 1 
ATOM   225  O OE2 . GLU A 1 31  ? 33.151  16.434  -6.585  1.00 53.45 ? 33  GLU A OE2 1 
ATOM   226  N N   . TYR A 1 32  ? 28.333  19.538  -5.418  1.00 30.42 ? 34  TYR A N   1 
ATOM   227  C CA  . TYR A 1 32  ? 27.484  19.636  -6.601  1.00 27.81 ? 34  TYR A CA  1 
ATOM   228  C C   . TYR A 1 32  ? 26.653  20.920  -6.655  1.00 29.11 ? 34  TYR A C   1 
ATOM   229  O O   . TYR A 1 32  ? 26.186  21.287  -7.739  1.00 32.66 ? 34  TYR A O   1 
ATOM   230  C CB  . TYR A 1 32  ? 26.607  18.386  -6.682  1.00 25.01 ? 34  TYR A CB  1 
ATOM   231  C CG  . TYR A 1 32  ? 27.455  17.174  -6.970  1.00 27.18 ? 34  TYR A CG  1 
ATOM   232  C CD1 . TYR A 1 32  ? 28.205  17.103  -8.141  1.00 29.05 ? 34  TYR A CD1 1 
ATOM   233  C CD2 . TYR A 1 32  ? 27.555  16.131  -6.062  1.00 25.12 ? 34  TYR A CD2 1 
ATOM   234  C CE1 . TYR A 1 32  ? 29.017  16.020  -8.407  1.00 27.16 ? 34  TYR A CE1 1 
ATOM   235  C CE2 . TYR A 1 32  ? 28.351  15.041  -6.321  1.00 27.07 ? 34  TYR A CE2 1 
ATOM   236  C CZ  . TYR A 1 32  ? 29.081  14.987  -7.499  1.00 29.42 ? 34  TYR A CZ  1 
ATOM   237  O OH  . TYR A 1 32  ? 29.892  13.907  -7.762  1.00 29.45 ? 34  TYR A OH  1 
ATOM   238  N N   . ALA A 1 33  ? 26.462  21.613  -5.530  1.00 28.61 ? 35  ALA A N   1 
ATOM   239  C CA  . ALA A 1 33  ? 25.886  22.956  -5.596  1.00 30.64 ? 35  ALA A CA  1 
ATOM   240  C C   . ALA A 1 33  ? 26.845  23.916  -6.282  1.00 30.88 ? 35  ALA A C   1 
ATOM   241  O O   . ALA A 1 33  ? 26.411  24.830  -6.993  1.00 32.02 ? 35  ALA A O   1 
ATOM   242  C CB  . ALA A 1 33  ? 25.537  23.473  -4.197  1.00 30.51 ? 35  ALA A CB  1 
ATOM   243  N N   . LYS A 1 34  ? 28.152  23.719  -6.082  1.00 29.65 ? 36  LYS A N   1 
ATOM   244  C CA  . LYS A 1 34  ? 29.154  24.521  -6.783  1.00 30.34 ? 36  LYS A CA  1 
ATOM   245  C C   . LYS A 1 34  ? 29.161  24.223  -8.283  1.00 31.82 ? 36  LYS A C   1 
ATOM   246  O O   . LYS A 1 34  ? 29.127  25.145  -9.109  1.00 31.44 ? 36  LYS A O   1 
ATOM   247  C CB  . LYS A 1 34  ? 30.546  24.273  -6.180  1.00 30.56 ? 36  LYS A CB  1 
ATOM   248  C CG  . LYS A 1 34  ? 30.646  24.559  -4.664  1.00 40.89 ? 36  LYS A CG  1 
ATOM   249  C CD  . LYS A 1 34  ? 32.093  24.766  -4.183  1.00 41.91 ? 36  LYS A CD  1 
ATOM   250  C CE  . LYS A 1 34  ? 32.235  24.558  -2.667  1.00 44.09 ? 36  LYS A CE  1 
ATOM   251  N NZ  . LYS A 1 34  ? 32.664  23.166  -2.281  1.00 52.67 ? 36  LYS A NZ  1 
ATOM   252  N N   . THR A 1 35  ? 29.219  22.936  -8.662  1.00 28.54 ? 37  THR A N   1 
ATOM   253  C CA  . THR A 1 35  ? 29.358  22.601  -10.081 1.00 27.88 ? 37  THR A CA  1 
ATOM   254  C C   . THR A 1 35  ? 28.060  22.790  -10.851 1.00 32.49 ? 37  THR A C   1 
ATOM   255  O O   . THR A 1 35  ? 28.099  23.137  -12.036 1.00 33.69 ? 37  THR A O   1 
ATOM   256  C CB  . THR A 1 35  ? 29.870  21.164  -10.270 1.00 31.34 ? 37  THR A CB  1 
ATOM   257  O OG1 . THR A 1 35  ? 28.933  20.222  -9.719  1.00 30.46 ? 37  THR A OG1 1 
ATOM   258  C CG2 . THR A 1 35  ? 31.240  20.982  -9.607  1.00 27.58 ? 37  THR A CG2 1 
ATOM   259  N N   . TYR A 1 36  ? 26.904  22.581  -10.220 1.00 32.76 ? 38  TYR A N   1 
ATOM   260  C CA  . TYR A 1 36  ? 25.652  22.826  -10.929 1.00 31.24 ? 38  TYR A CA  1 
ATOM   261  C C   . TYR A 1 36  ? 25.165  24.262  -10.810 1.00 32.92 ? 38  TYR A C   1 
ATOM   262  O O   . TYR A 1 36  ? 24.264  24.652  -11.558 1.00 37.16 ? 38  TYR A O   1 
ATOM   263  C CB  . TYR A 1 36  ? 24.537  21.904  -10.423 1.00 28.64 ? 38  TYR A CB  1 
ATOM   264  C CG  . TYR A 1 36  ? 24.564  20.484  -10.970 1.00 31.10 ? 38  TYR A CG  1 
ATOM   265  C CD1 . TYR A 1 36  ? 23.886  20.144  -12.139 1.00 30.37 ? 38  TYR A CD1 1 
ATOM   266  C CD2 . TYR A 1 36  ? 25.251  19.478  -10.300 1.00 27.48 ? 38  TYR A CD2 1 
ATOM   267  C CE1 . TYR A 1 36  ? 23.902  18.849  -12.623 1.00 22.95 ? 38  TYR A CE1 1 
ATOM   268  C CE2 . TYR A 1 36  ? 25.268  18.182  -10.775 1.00 27.27 ? 38  TYR A CE2 1 
ATOM   269  C CZ  . TYR A 1 36  ? 24.595  17.869  -11.930 1.00 27.75 ? 38  TYR A CZ  1 
ATOM   270  O OH  . TYR A 1 36  ? 24.624  16.563  -12.387 1.00 26.95 ? 38  TYR A OH  1 
ATOM   271  N N   . GLY A 1 37  ? 25.692  25.042  -9.874  1.00 32.63 ? 39  GLY A N   1 
ATOM   272  C CA  . GLY A 1 37  ? 25.317  26.432  -9.745  1.00 40.17 ? 39  GLY A CA  1 
ATOM   273  C C   . GLY A 1 37  ? 24.232  26.769  -8.742  1.00 42.40 ? 39  GLY A C   1 
ATOM   274  O O   . GLY A 1 37  ? 23.454  27.695  -8.989  1.00 46.62 ? 39  GLY A O   1 
ATOM   275  N N   . MET A 1 38  ? 24.158  26.068  -7.617  1.00 39.35 ? 40  MET A N   1 
ATOM   276  C CA  . MET A 1 38  ? 23.229  26.441  -6.554  1.00 40.06 ? 40  MET A CA  1 
ATOM   277  C C   . MET A 1 38  ? 23.914  27.507  -5.704  1.00 43.82 ? 40  MET A C   1 
ATOM   278  O O   . MET A 1 38  ? 24.794  27.202  -4.893  1.00 40.54 ? 40  MET A O   1 
ATOM   279  C CB  . MET A 1 38  ? 22.829  25.220  -5.733  1.00 39.25 ? 40  MET A CB  1 
ATOM   280  C CG  . MET A 1 38  ? 21.946  25.524  -4.528  1.00 37.14 ? 40  MET A CG  1 
ATOM   281  S SD  . MET A 1 38  ? 20.260  25.822  -5.046  1.00 45.07 ? 40  MET A SD  1 
ATOM   282  C CE  . MET A 1 38  ? 19.774  24.193  -5.606  1.00 36.69 ? 40  MET A CE  1 
ATOM   283  N N   . LYS A 1 39  ? 23.528  28.768  -5.913  1.00 44.91 ? 41  LYS A N   1 
ATOM   284  C CA  . LYS A 1 39  ? 24.053  29.902  -5.159  1.00 46.13 ? 41  LYS A CA  1 
ATOM   285  C C   . LYS A 1 39  ? 22.992  30.642  -4.358  1.00 50.84 ? 41  LYS A C   1 
ATOM   286  O O   . LYS A 1 39  ? 23.313  31.228  -3.325  1.00 49.54 ? 41  LYS A O   1 
ATOM   287  C CB  . LYS A 1 39  ? 24.736  30.909  -6.102  1.00 54.04 ? 41  LYS A CB  1 
ATOM   288  C CG  . LYS A 1 39  ? 25.455  30.293  -7.297  1.00 55.52 ? 41  LYS A CG  1 
ATOM   289  C CD  . LYS A 1 39  ? 26.066  31.389  -8.172  1.00 58.50 ? 41  LYS A CD  1 
ATOM   290  C CE  . LYS A 1 39  ? 27.522  31.105  -8.512  1.00 57.23 ? 41  LYS A CE  1 
ATOM   291  N NZ  . LYS A 1 39  ? 27.650  30.009  -9.513  1.00 57.53 ? 41  LYS A NZ  1 
ATOM   292  N N   . GLU A 1 40  ? 21.739  30.597  -4.795  1.00 47.68 ? 42  GLU A N   1 
ATOM   293  C CA  . GLU A 1 40  ? 20.663  31.385  -4.217  1.00 47.77 ? 42  GLU A CA  1 
ATOM   294  C C   . GLU A 1 40  ? 20.067  30.671  -3.005  1.00 50.85 ? 42  GLU A C   1 
ATOM   295  O O   . GLU A 1 40  ? 19.765  29.474  -3.056  1.00 47.25 ? 42  GLU A O   1 
ATOM   296  C CB  . GLU A 1 40  ? 19.599  31.632  -5.290  1.00 50.97 ? 42  GLU A CB  1 
ATOM   297  C CG  . GLU A 1 40  ? 20.165  32.167  -6.650  1.00 56.28 ? 42  GLU A CG  1 
ATOM   298  C CD  . GLU A 1 40  ? 20.721  31.092  -7.630  1.00 59.42 ? 42  GLU A CD  1 
ATOM   299  O OE1 . GLU A 1 40  ? 20.877  29.907  -7.244  1.00 51.77 ? 42  GLU A OE1 1 
ATOM   300  O OE2 . GLU A 1 40  ? 21.022  31.453  -8.798  1.00 58.29 ? 42  GLU A OE2 1 
ATOM   301  N N   . GLU A 1 41  ? 19.888  31.416  -1.911  1.00 50.44 ? 43  GLU A N   1 
ATOM   302  C CA  . GLU A 1 41  ? 19.601  30.780  -0.628  1.00 45.95 ? 43  GLU A CA  1 
ATOM   303  C C   . GLU A 1 41  ? 18.153  30.327  -0.514  1.00 41.26 ? 43  GLU A C   1 
ATOM   304  O O   . GLU A 1 41  ? 17.881  29.272  0.066   1.00 41.19 ? 43  GLU A O   1 
ATOM   305  C CB  . GLU A 1 41  ? 19.965  31.721  0.520   1.00 47.19 ? 43  GLU A CB  1 
ATOM   306  C CG  . GLU A 1 41  ? 21.196  31.234  1.278   1.00 58.43 ? 43  GLU A CG  1 
ATOM   307  C CD  . GLU A 1 41  ? 21.696  32.194  2.333   1.00 69.35 ? 43  GLU A CD  1 
ATOM   308  O OE1 . GLU A 1 41  ? 22.324  31.729  3.312   1.00 66.26 ? 43  GLU A OE1 1 
ATOM   309  O OE2 . GLU A 1 41  ? 21.455  33.412  2.188   1.00 74.85 ? 43  GLU A OE2 1 
ATOM   310  N N   . ARG A 1 42  ? 17.205  31.100  -1.038  1.00 40.88 ? 44  ARG A N   1 
ATOM   311  C CA  . ARG A 1 42  ? 15.817  30.647  -0.992  1.00 46.13 ? 44  ARG A CA  1 
ATOM   312  C C   . ARG A 1 42  ? 15.613  29.418  -1.876  1.00 40.39 ? 44  ARG A C   1 
ATOM   313  O O   . ARG A 1 42  ? 14.879  28.499  -1.503  1.00 40.73 ? 44  ARG A O   1 
ATOM   314  C CB  . ARG A 1 42  ? 14.868  31.786  -1.387  1.00 41.45 ? 44  ARG A CB  1 
ATOM   315  C CG  . ARG A 1 42  ? 13.439  31.351  -1.714  1.00 48.79 ? 44  ARG A CG  1 
ATOM   316  C CD  . ARG A 1 42  ? 12.401  32.438  -1.437  1.00 46.74 ? 44  ARG A CD  1 
ATOM   317  N NE  . ARG A 1 42  ? 12.473  32.929  -0.071  1.00 49.24 ? 44  ARG A NE  1 
ATOM   318  C CZ  . ARG A 1 42  ? 11.514  32.757  0.829   1.00 47.47 ? 44  ARG A CZ  1 
ATOM   319  N NH1 . ARG A 1 42  ? 10.408  32.109  0.507   1.00 48.27 ? 44  ARG A NH1 1 
ATOM   320  N NH2 . ARG A 1 42  ? 11.661  33.238  2.047   1.00 50.23 ? 44  ARG A NH2 1 
ATOM   321  N N   . ALA A 1 43  ? 16.276  29.372  -3.035  1.00 43.13 ? 45  ALA A N   1 
ATOM   322  C CA  . ALA A 1 43  ? 16.217  28.188  -3.890  1.00 43.54 ? 45  ALA A CA  1 
ATOM   323  C C   . ALA A 1 43  ? 16.800  26.977  -3.177  1.00 41.23 ? 45  ALA A C   1 
ATOM   324  O O   . ALA A 1 43  ? 16.245  25.875  -3.231  1.00 35.52 ? 45  ALA A O   1 
ATOM   325  C CB  . ALA A 1 43  ? 16.961  28.447  -5.201  1.00 40.90 ? 45  ALA A CB  1 
ATOM   326  N N   . MET A 1 44  ? 17.918  27.178  -2.489  1.00 40.21 ? 46  MET A N   1 
ATOM   327  C CA  . MET A 1 44  ? 18.552  26.100  -1.746  1.00 42.48 ? 46  MET A CA  1 
ATOM   328  C C   . MET A 1 44  ? 17.653  25.572  -0.646  1.00 38.27 ? 46  MET A C   1 
ATOM   329  O O   . MET A 1 44  ? 17.659  24.371  -0.360  1.00 37.52 ? 46  MET A O   1 
ATOM   330  C CB  . MET A 1 44  ? 19.856  26.594  -1.143  1.00 40.13 ? 46  MET A CB  1 
ATOM   331  C CG  . MET A 1 44  ? 20.585  25.551  -0.373  1.00 48.24 ? 46  MET A CG  1 
ATOM   332  S SD  . MET A 1 44  ? 21.300  26.411  1.030   1.00 75.67 ? 46  MET A SD  1 
ATOM   333  C CE  . MET A 1 44  ? 21.887  27.898  0.194   1.00 55.33 ? 46  MET A CE  1 
ATOM   334  N N   . ALA A 1 45  ? 16.913  26.460  0.023   1.00 42.00 ? 47  ALA A N   1 
ATOM   335  C CA  . ALA A 1 45  ? 16.002  25.998  1.062   1.00 35.85 ? 47  ALA A CA  1 
ATOM   336  C C   . ALA A 1 45  ? 14.885  25.164  0.456   1.00 31.96 ? 47  ALA A C   1 
ATOM   337  O O   . ALA A 1 45  ? 14.462  24.162  1.036   1.00 32.65 ? 47  ALA A O   1 
ATOM   338  C CB  . ALA A 1 45  ? 15.435  27.179  1.843   1.00 31.96 ? 47  ALA A CB  1 
ATOM   339  N N   . HIS A 1 46  ? 14.402  25.546  -0.721  1.00 31.97 ? 48  HIS A N   1 
ATOM   340  C CA  . HIS A 1 46  ? 13.413  24.707  -1.382  1.00 33.60 ? 48  HIS A CA  1 
ATOM   341  C C   . HIS A 1 46  ? 14.015  23.357  -1.751  1.00 35.45 ? 48  HIS A C   1 
ATOM   342  O O   . HIS A 1 46  ? 13.408  22.307  -1.512  1.00 34.12 ? 48  HIS A O   1 
ATOM   343  C CB  . HIS A 1 46  ? 12.866  25.414  -2.615  1.00 34.57 ? 48  HIS A CB  1 
ATOM   344  C CG  . HIS A 1 46  ? 11.865  26.487  -2.302  1.00 41.51 ? 48  HIS A CG  1 
ATOM   345  N ND1 . HIS A 1 46  ? 10.595  26.211  -1.842  1.00 38.82 ? 48  HIS A ND1 1 
ATOM   346  C CD2 . HIS A 1 46  ? 11.943  27.835  -2.403  1.00 37.87 ? 48  HIS A CD2 1 
ATOM   347  C CE1 . HIS A 1 46  ? 9.934   27.342  -1.674  1.00 38.81 ? 48  HIS A CE1 1 
ATOM   348  N NE2 . HIS A 1 46  ? 10.731  28.342  -2.006  1.00 40.30 ? 48  HIS A NE2 1 
ATOM   349  N N   . PHE A 1 47  ? 15.228  23.372  -2.318  1.00 32.51 ? 49  PHE A N   1 
ATOM   350  C CA  . PHE A 1 47  ? 15.886  22.140  -2.738  1.00 31.61 ? 49  PHE A CA  1 
ATOM   351  C C   . PHE A 1 47  ? 16.071  21.200  -1.552  1.00 30.20 ? 49  PHE A C   1 
ATOM   352  O O   . PHE A 1 47  ? 15.696  20.026  -1.615  1.00 29.21 ? 49  PHE A O   1 
ATOM   353  C CB  . PHE A 1 47  ? 17.224  22.487  -3.410  1.00 30.51 ? 49  PHE A CB  1 
ATOM   354  C CG  . PHE A 1 47  ? 18.077  21.290  -3.817  1.00 29.78 ? 49  PHE A CG  1 
ATOM   355  C CD1 . PHE A 1 47  ? 17.848  20.620  -5.009  1.00 28.57 ? 49  PHE A CD1 1 
ATOM   356  C CD2 . PHE A 1 47  ? 19.151  20.887  -3.032  1.00 27.70 ? 49  PHE A CD2 1 
ATOM   357  C CE1 . PHE A 1 47  ? 18.655  19.558  -5.400  1.00 24.69 ? 49  PHE A CE1 1 
ATOM   358  C CE2 . PHE A 1 47  ? 19.956  19.828  -3.412  1.00 29.10 ? 49  PHE A CE2 1 
ATOM   359  C CZ  . PHE A 1 47  ? 19.706  19.164  -4.606  1.00 26.30 ? 49  PHE A CZ  1 
ATOM   360  N N   . LEU A 1 48  ? 16.601  21.713  -0.441  1.00 30.37 ? 50  LEU A N   1 
ATOM   361  C CA  . LEU A 1 48  ? 16.828  20.856  0.721   1.00 30.82 ? 50  LEU A CA  1 
ATOM   362  C C   . LEU A 1 48  ? 15.519  20.309  1.275   1.00 31.39 ? 50  LEU A C   1 
ATOM   363  O O   . LEU A 1 48  ? 15.457  19.155  1.722   1.00 30.37 ? 50  LEU A O   1 
ATOM   364  C CB  . LEU A 1 48  ? 17.577  21.622  1.805   1.00 29.82 ? 50  LEU A CB  1 
ATOM   365  C CG  . LEU A 1 48  ? 19.052  21.920  1.576   1.00 32.40 ? 50  LEU A CG  1 
ATOM   366  C CD1 . LEU A 1 48  ? 19.604  22.560  2.821   1.00 32.65 ? 50  LEU A CD1 1 
ATOM   367  C CD2 . LEU A 1 48  ? 19.815  20.651  1.262   1.00 29.76 ? 50  LEU A CD2 1 
ATOM   368  N N   . SER A 1 49  ? 14.459  21.123  1.259   1.00 29.77 ? 51  SER A N   1 
ATOM   369  C CA  . SER A 1 49  ? 13.198  20.667  1.825   1.00 29.14 ? 51  SER A CA  1 
ATOM   370  C C   . SER A 1 49  ? 12.511  19.664  0.914   1.00 29.10 ? 51  SER A C   1 
ATOM   371  O O   . SER A 1 49  ? 11.861  18.733  1.407   1.00 30.26 ? 51  SER A O   1 
ATOM   372  C CB  . SER A 1 49  ? 12.277  21.858  2.101   1.00 27.57 ? 51  SER A CB  1 
ATOM   373  O OG  . SER A 1 49  ? 11.786  22.448  0.903   1.00 32.04 ? 51  SER A OG  1 
ATOM   374  N N   . GLN A 1 50  ? 12.642  19.834  -0.406  1.00 26.91 ? 52  GLN A N   1 
ATOM   375  C CA  . GLN A 1 50  ? 12.067  18.870  -1.339  1.00 29.57 ? 52  GLN A CA  1 
ATOM   376  C C   . GLN A 1 50  ? 12.846  17.558  -1.317  1.00 29.91 ? 52  GLN A C   1 
ATOM   377  O O   . GLN A 1 50  ? 12.256  16.474  -1.301  1.00 28.77 ? 52  GLN A O   1 
ATOM   378  C CB  . GLN A 1 50  ? 12.039  19.458  -2.754  1.00 31.12 ? 52  GLN A CB  1 
ATOM   379  C CG  . GLN A 1 50  ? 11.185  20.726  -2.906  1.00 28.84 ? 52  GLN A CG  1 
ATOM   380  C CD  . GLN A 1 50  ? 9.695   20.449  -2.840  1.00 29.05 ? 52  GLN A CD  1 
ATOM   381  O OE1 . GLN A 1 50  ? 9.219   19.395  -3.276  1.00 31.43 ? 52  GLN A OE1 1 
ATOM   382  N NE2 . GLN A 1 50  ? 8.946   21.405  -2.310  1.00 30.52 ? 52  GLN A NE2 1 
ATOM   383  N N   . VAL A 1 51  ? 14.179  17.644  -1.319  1.00 27.22 ? 53  VAL A N   1 
ATOM   384  C CA  . VAL A 1 51  ? 15.010  16.447  -1.226  1.00 28.54 ? 53  VAL A CA  1 
ATOM   385  C C   . VAL A 1 51  ? 14.760  15.733  0.097   1.00 26.66 ? 53  VAL A C   1 
ATOM   386  O O   . VAL A 1 51  ? 14.590  14.510  0.137   1.00 27.72 ? 53  VAL A O   1 
ATOM   387  C CB  . VAL A 1 51  ? 16.499  16.810  -1.389  1.00 24.67 ? 53  VAL A CB  1 
ATOM   388  C CG1 . VAL A 1 51  ? 17.351  15.630  -1.022  1.00 21.53 ? 53  VAL A CG1 1 
ATOM   389  C CG2 . VAL A 1 51  ? 16.796  17.276  -2.818  1.00 29.19 ? 53  VAL A CG2 1 
ATOM   390  N N   . GLY A 1 52  ? 14.753  16.489  1.201   1.00 24.97 ? 54  GLY A N   1 
ATOM   391  C CA  . GLY A 1 52  ? 14.539  15.879  2.502   1.00 23.32 ? 54  GLY A CA  1 
ATOM   392  C C   . GLY A 1 52  ? 13.210  15.155  2.594   1.00 26.72 ? 54  GLY A C   1 
ATOM   393  O O   . GLY A 1 52  ? 13.120  14.066  3.166   1.00 27.55 ? 54  GLY A O   1 
ATOM   394  N N   . HIS A 1 53  ? 12.164  15.738  2.013   1.00 27.74 ? 55  HIS A N   1 
ATOM   395  C CA  . HIS A 1 53  ? 10.867  15.082  2.055   1.00 26.40 ? 55  HIS A CA  1 
ATOM   396  C C   . HIS A 1 53  ? 10.862  13.813  1.209   1.00 30.52 ? 55  HIS A C   1 
ATOM   397  O O   . HIS A 1 53  ? 10.240  12.812  1.590   1.00 26.95 ? 55  HIS A O   1 
ATOM   398  C CB  . HIS A 1 53  ? 9.775   16.020  1.571   1.00 27.30 ? 55  HIS A CB  1 
ATOM   399  C CG  . HIS A 1 53  ? 8.491   15.315  1.298   1.00 28.80 ? 55  HIS A CG  1 
ATOM   400  N ND1 . HIS A 1 53  ? 7.595   14.997  2.297   1.00 23.71 ? 55  HIS A ND1 1 
ATOM   401  C CD2 . HIS A 1 53  ? 7.982   14.806  0.152   1.00 25.20 ? 55  HIS A CD2 1 
ATOM   402  C CE1 . HIS A 1 53  ? 6.579   14.342  1.770   1.00 26.29 ? 55  HIS A CE1 1 
ATOM   403  N NE2 . HIS A 1 53  ? 6.789   14.215  0.470   1.00 29.39 ? 55  HIS A NE2 1 
ATOM   404  N N   . GLU A 1 54  ? 11.529  13.839  0.047   1.00 23.80 ? 56  GLU A N   1 
ATOM   405  C CA  . GLU A 1 54  ? 11.466  12.679  -0.830  1.00 28.14 ? 56  GLU A CA  1 
ATOM   406  C C   . GLU A 1 54  ? 12.298  11.530  -0.284  1.00 27.94 ? 56  GLU A C   1 
ATOM   407  O O   . GLU A 1 54  ? 11.910  10.370  -0.436  1.00 24.84 ? 56  GLU A O   1 
ATOM   408  C CB  . GLU A 1 54  ? 11.941  13.028  -2.250  1.00 28.92 ? 56  GLU A CB  1 
ATOM   409  C CG  . GLU A 1 54  ? 11.097  14.082  -2.998  1.00 31.06 ? 56  GLU A CG  1 
ATOM   410  C CD  . GLU A 1 54  ? 9.752   13.565  -3.481  1.00 32.64 ? 56  GLU A CD  1 
ATOM   411  O OE1 . GLU A 1 54  ? 9.571   12.328  -3.575  1.00 33.36 ? 56  GLU A OE1 1 
ATOM   412  O OE2 . GLU A 1 54  ? 8.874   14.403  -3.778  1.00 35.01 ? 56  GLU A OE2 1 
ATOM   413  N N   . SER A 1 55  ? 13.414  11.833  0.387   1.00 26.57 ? 57  SER A N   1 
ATOM   414  C CA  . SER A 1 55  ? 14.464  10.847  0.603   1.00 23.83 ? 57  SER A CA  1 
ATOM   415  C C   . SER A 1 55  ? 15.024  10.804  2.009   1.00 28.66 ? 57  SER A C   1 
ATOM   416  O O   . SER A 1 55  ? 15.713  9.829   2.333   1.00 28.05 ? 57  SER A O   1 
ATOM   417  C CB  . SER A 1 55  ? 15.633  11.113  -0.345  1.00 27.49 ? 57  SER A CB  1 
ATOM   418  O OG  . SER A 1 55  ? 16.380  12.224  0.140   1.00 28.07 ? 57  SER A OG  1 
ATOM   419  N N   . ASN A 1 56  ? 14.815  11.838  2.828   1.00 29.57 ? 58  ASN A N   1 
ATOM   420  C CA  . ASN A 1 56  ? 15.477  11.948  4.127   1.00 28.47 ? 58  ASN A CA  1 
ATOM   421  C C   . ASN A 1 56  ? 16.994  11.814  3.990   1.00 28.69 ? 58  ASN A C   1 
ATOM   422  O O   . ASN A 1 56  ? 17.684  11.350  4.903   1.00 26.76 ? 58  ASN A O   1 
ATOM   423  C CB  . ASN A 1 56  ? 14.899  10.926  5.102   1.00 29.03 ? 58  ASN A CB  1 
ATOM   424  C CG  . ASN A 1 56  ? 13.415  11.153  5.330   1.00 31.17 ? 58  ASN A CG  1 
ATOM   425  O OD1 . ASN A 1 56  ? 13.012  12.155  5.948   1.00 31.28 ? 58  ASN A OD1 1 
ATOM   426  N ND2 . ASN A 1 56  ? 12.590  10.254  4.804   1.00 25.93 ? 58  ASN A ND2 1 
ATOM   427  N N   . PHE A 1 57  ? 17.504  12.223  2.825   1.00 28.51 ? 59  PHE A N   1 
ATOM   428  C CA  . PHE A 1 57  ? 18.925  12.268  2.482   1.00 27.25 ? 59  PHE A CA  1 
ATOM   429  C C   . PHE A 1 57  ? 19.584  10.881  2.479   1.00 27.46 ? 59  PHE A C   1 
ATOM   430  O O   . PHE A 1 57  ? 20.798  10.769  2.661   1.00 25.64 ? 59  PHE A O   1 
ATOM   431  C CB  . PHE A 1 57  ? 19.665  13.255  3.395   1.00 25.30 ? 59  PHE A CB  1 
ATOM   432  C CG  . PHE A 1 57  ? 19.093  14.654  3.348   1.00 27.42 ? 59  PHE A CG  1 
ATOM   433  C CD1 . PHE A 1 57  ? 19.357  15.495  2.272   1.00 27.94 ? 59  PHE A CD1 1 
ATOM   434  C CD2 . PHE A 1 57  ? 18.249  15.111  4.353   1.00 28.30 ? 59  PHE A CD2 1 
ATOM   435  C CE1 . PHE A 1 57  ? 18.810  16.782  2.210   1.00 26.82 ? 59  PHE A CE1 1 
ATOM   436  C CE2 . PHE A 1 57  ? 17.699  16.400  4.296   1.00 31.13 ? 59  PHE A CE2 1 
ATOM   437  C CZ  . PHE A 1 57  ? 17.989  17.232  3.212   1.00 26.71 ? 59  PHE A CZ  1 
ATOM   438  N N   . LYS A 1 58  ? 18.796  9.826   2.244   1.00 25.08 ? 60  LYS A N   1 
ATOM   439  C CA  . LYS A 1 58  ? 19.270  8.464   2.019   1.00 27.96 ? 60  LYS A CA  1 
ATOM   440  C C   . LYS A 1 58  ? 18.851  8.010   0.623   1.00 28.69 ? 60  LYS A C   1 
ATOM   441  O O   . LYS A 1 58  ? 17.675  8.148   0.264   1.00 25.89 ? 60  LYS A O   1 
ATOM   442  C CB  . LYS A 1 58  ? 18.699  7.489   3.077   1.00 27.06 ? 60  LYS A CB  1 
ATOM   443  C CG  . LYS A 1 58  ? 19.232  7.732   4.483   1.00 36.51 ? 60  LYS A CG  1 
ATOM   444  C CD  . LYS A 1 58  ? 18.850  6.623   5.448   1.00 40.79 ? 60  LYS A CD  1 
ATOM   445  C CE  . LYS A 1 58  ? 19.874  5.500   5.434   1.00 47.36 ? 60  LYS A CE  1 
ATOM   446  N NZ  . LYS A 1 58  ? 21.070  5.816   6.281   1.00 47.31 ? 60  LYS A NZ  1 
ATOM   447  N N   . PRO A 1 59  ? 19.768  7.500   -0.201  1.00 26.26 ? 61  PRO A N   1 
ATOM   448  C CA  . PRO A 1 59  ? 19.382  7.083   -1.552  1.00 26.71 ? 61  PRO A CA  1 
ATOM   449  C C   . PRO A 1 59  ? 18.405  5.923   -1.493  1.00 27.98 ? 61  PRO A C   1 
ATOM   450  O O   . PRO A 1 59  ? 18.535  5.026   -0.663  1.00 25.42 ? 61  PRO A O   1 
ATOM   451  C CB  . PRO A 1 59  ? 20.710  6.673   -2.196  1.00 28.74 ? 61  PRO A CB  1 
ATOM   452  C CG  . PRO A 1 59  ? 21.751  7.397   -1.406  1.00 29.19 ? 61  PRO A CG  1 
ATOM   453  C CD  . PRO A 1 59  ? 21.223  7.431   -0.002  1.00 26.86 ? 61  PRO A CD  1 
ATOM   454  N N   . VAL A 1 60  ? 17.425  5.952   -2.390  1.00 28.17 ? 62  VAL A N   1 
ATOM   455  C CA  . VAL A 1 60  ? 16.325  4.997   -2.413  1.00 33.96 ? 62  VAL A CA  1 
ATOM   456  C C   . VAL A 1 60  ? 16.246  4.388   -3.808  1.00 32.32 ? 62  VAL A C   1 
ATOM   457  O O   . VAL A 1 60  ? 16.407  5.091   -4.812  1.00 32.31 ? 62  VAL A O   1 
ATOM   458  C CB  . VAL A 1 60  ? 14.983  5.672   -2.018  1.00 35.29 ? 62  VAL A CB  1 
ATOM   459  C CG1 . VAL A 1 60  ? 14.786  6.969   -2.774  1.00 36.90 ? 62  VAL A CG1 1 
ATOM   460  C CG2 . VAL A 1 60  ? 13.793  4.737   -2.274  1.00 40.18 ? 62  VAL A CG2 1 
ATOM   461  N N   . SER A 1 61  ? 16.027  3.079   -3.874  1.00 26.86 ? 63  SER A N   1 
ATOM   462  C CA  . SER A 1 61  ? 15.708  2.425   -5.130  1.00 32.66 ? 63  SER A CA  1 
ATOM   463  C C   . SER A 1 61  ? 14.272  1.905   -5.095  1.00 32.01 ? 63  SER A C   1 
ATOM   464  O O   . SER A 1 61  ? 13.819  1.378   -4.080  1.00 29.26 ? 63  SER A O   1 
ATOM   465  C CB  . SER A 1 61  ? 16.691  1.296   -5.434  1.00 33.80 ? 63  SER A CB  1 
ATOM   466  O OG  . SER A 1 61  ? 16.404  0.150   -4.681  1.00 37.73 ? 63  SER A OG  1 
ATOM   467  N N   . GLU A 1 62  ? 13.561  2.082   -6.209  1.00 29.99 ? 64  GLU A N   1 
ATOM   468  C CA  . GLU A 1 62  ? 12.171  1.656   -6.321  1.00 31.66 ? 64  GLU A CA  1 
ATOM   469  C C   . GLU A 1 62  ? 12.020  0.174   -5.984  1.00 32.81 ? 64  GLU A C   1 
ATOM   470  O O   . GLU A 1 62  ? 12.820  -0.664  -6.408  1.00 30.29 ? 64  GLU A O   1 
ATOM   471  C CB  . GLU A 1 62  ? 11.658  1.933   -7.741  1.00 27.07 ? 64  GLU A CB  1 
ATOM   472  C CG  . GLU A 1 62  ? 10.199  1.515   -8.011  1.00 27.79 ? 64  GLU A CG  1 
ATOM   473  C CD  . GLU A 1 62  ? 9.696   1.960   -9.390  1.00 26.76 ? 64  GLU A CD  1 
ATOM   474  O OE1 . GLU A 1 62  ? 10.467  2.605   -10.136 1.00 29.41 ? 64  GLU A OE1 1 
ATOM   475  O OE2 . GLU A 1 62  ? 8.524   1.676   -9.733  1.00 26.09 ? 64  GLU A OE2 1 
ATOM   476  N N   . ASN A 1 63  ? 10.994  -0.142  -5.206  1.00 30.65 ? 65  ASN A N   1 
ATOM   477  C CA  . ASN A 1 63  ? 10.674  -1.524  -4.870  1.00 29.04 ? 65  ASN A CA  1 
ATOM   478  C C   . ASN A 1 63  ? 9.636   -2.025  -5.871  1.00 26.61 ? 65  ASN A C   1 
ATOM   479  O O   . ASN A 1 63  ? 8.551   -1.444  -5.986  1.00 29.41 ? 65  ASN A O   1 
ATOM   480  C CB  . ASN A 1 63  ? 10.168  -1.614  -3.421  1.00 32.03 ? 65  ASN A CB  1 
ATOM   481  C CG  . ASN A 1 63  ? 9.594   -2.995  -3.061  1.00 36.21 ? 65  ASN A CG  1 
ATOM   482  O OD1 . ASN A 1 63  ? 10.034  -4.021  -3.566  1.00 29.96 ? 65  ASN A OD1 1 
ATOM   483  N ND2 . ASN A 1 63  ? 8.590   -3.006  -2.186  1.00 44.48 ? 65  ASN A ND2 1 
ATOM   484  N N   . LEU A 1 64  ? 9.978   -3.081  -6.617  1.00 27.68 ? 66  LEU A N   1 
ATOM   485  C CA  . LEU A 1 64  ? 9.064   -3.671  -7.593  1.00 25.87 ? 66  LEU A CA  1 
ATOM   486  C C   . LEU A 1 64  ? 8.667   -5.091  -7.210  1.00 28.65 ? 66  LEU A C   1 
ATOM   487  O O   . LEU A 1 64  ? 8.239   -5.876  -8.070  1.00 24.98 ? 66  LEU A O   1 
ATOM   488  C CB  . LEU A 1 64  ? 9.673   -3.647  -8.996  1.00 23.08 ? 66  LEU A CB  1 
ATOM   489  C CG  . LEU A 1 64  ? 9.825   -2.252  -9.624  1.00 24.82 ? 66  LEU A CG  1 
ATOM   490  C CD1 . LEU A 1 64  ? 10.847  -2.276  -10.748 1.00 23.47 ? 66  LEU A CD1 1 
ATOM   491  C CD2 . LEU A 1 64  ? 8.485   -1.738  -10.136 1.00 26.38 ? 66  LEU A CD2 1 
ATOM   492  N N   . ARG A 1 65  ? 8.804   -5.434  -5.933  1.00 25.27 ? 67  ARG A N   1 
ATOM   493  C CA  . ARG A 1 65  ? 8.274   -6.681  -5.397  1.00 24.16 ? 67  ARG A CA  1 
ATOM   494  C C   . ARG A 1 65  ? 6.849   -6.418  -4.914  1.00 29.59 ? 67  ARG A C   1 
ATOM   495  O O   . ARG A 1 65  ? 6.645   -5.734  -3.899  1.00 27.83 ? 67  ARG A O   1 
ATOM   496  C CB  . ARG A 1 65  ? 9.172   -7.196  -4.274  1.00 29.32 ? 67  ARG A CB  1 
ATOM   497  C CG  . ARG A 1 65  ? 8.640   -8.410  -3.564  1.00 32.46 ? 67  ARG A CG  1 
ATOM   498  C CD  . ARG A 1 65  ? 9.615   -8.876  -2.508  1.00 31.22 ? 67  ARG A CD  1 
ATOM   499  N NE  . ARG A 1 65  ? 9.157   -10.085 -1.838  1.00 28.48 ? 67  ARG A NE  1 
ATOM   500  C CZ  . ARG A 1 65  ? 8.323   -10.103 -0.802  1.00 29.69 ? 67  ARG A CZ  1 
ATOM   501  N NH1 . ARG A 1 65  ? 7.839   -8.970  -0.314  1.00 29.96 ? 67  ARG A NH1 1 
ATOM   502  N NH2 . ARG A 1 65  ? 7.967   -11.257 -0.256  1.00 32.82 ? 67  ARG A NH2 1 
ATOM   503  N N   . TYR A 1 66  ? 5.863   -6.944  -5.650  1.00 26.26 ? 68  TYR A N   1 
ATOM   504  C CA  . TYR A 1 66  ? 4.452   -6.718  -5.364  1.00 27.52 ? 68  TYR A CA  1 
ATOM   505  C C   . TYR A 1 66  ? 3.713   -8.038  -5.211  1.00 28.94 ? 68  TYR A C   1 
ATOM   506  O O   . TYR A 1 66  ? 4.066   -9.044  -5.833  1.00 30.77 ? 68  TYR A O   1 
ATOM   507  C CB  . TYR A 1 66  ? 3.763   -5.915  -6.477  1.00 25.70 ? 68  TYR A CB  1 
ATOM   508  C CG  . TYR A 1 66  ? 3.990   -4.416  -6.444  1.00 23.58 ? 68  TYR A CG  1 
ATOM   509  C CD1 . TYR A 1 66  ? 2.962   -3.544  -6.102  1.00 27.89 ? 68  TYR A CD1 1 
ATOM   510  C CD2 . TYR A 1 66  ? 5.219   -3.881  -6.756  1.00 21.38 ? 68  TYR A CD2 1 
ATOM   511  C CE1 . TYR A 1 66  ? 3.163   -2.169  -6.085  1.00 28.34 ? 68  TYR A CE1 1 
ATOM   512  C CE2 . TYR A 1 66  ? 5.433   -2.525  -6.740  1.00 25.88 ? 68  TYR A CE2 1 
ATOM   513  C CZ  . TYR A 1 66  ? 4.403   -1.668  -6.407  1.00 29.53 ? 68  TYR A CZ  1 
ATOM   514  O OH  . TYR A 1 66  ? 4.629   -0.309  -6.384  1.00 30.83 ? 68  TYR A OH  1 
ATOM   515  N N   . SER A 1 67  ? 2.670   -8.014  -4.387  1.00 28.33 ? 69  SER A N   1 
ATOM   516  C CA  . SER A 1 67  ? 1.731   -9.120  -4.309  1.00 26.41 ? 69  SER A CA  1 
ATOM   517  C C   . SER A 1 67  ? 0.831   -9.137  -5.546  1.00 25.98 ? 69  SER A C   1 
ATOM   518  O O   . SER A 1 67  ? 0.752   -8.151  -6.277  1.00 28.38 ? 69  SER A O   1 
ATOM   519  C CB  . SER A 1 67  ? 0.887   -8.990  -3.046  1.00 28.22 ? 69  SER A CB  1 
ATOM   520  O OG  . SER A 1 67  ? -0.136  -8.028  -3.225  1.00 31.63 ? 69  SER A OG  1 
ATOM   521  N N   . PRO A 1 68  ? 0.144   -10.253 -5.809  1.00 29.42 ? 70  PRO A N   1 
ATOM   522  C CA  . PRO A 1 68  ? -0.754  -10.281 -6.983  1.00 28.77 ? 70  PRO A CA  1 
ATOM   523  C C   . PRO A 1 68  ? -1.762  -9.147  -6.996  1.00 28.18 ? 70  PRO A C   1 
ATOM   524  O O   . PRO A 1 68  ? -1.842  -8.406  -7.990  1.00 28.99 ? 70  PRO A O   1 
ATOM   525  C CB  . PRO A 1 68  ? -1.428  -11.652 -6.865  1.00 26.63 ? 70  PRO A CB  1 
ATOM   526  C CG  . PRO A 1 68  ? -0.391  -12.494 -6.187  1.00 25.42 ? 70  PRO A CG  1 
ATOM   527  C CD  . PRO A 1 68  ? 0.248   -11.576 -5.172  1.00 24.55 ? 70  PRO A CD  1 
ATOM   528  N N   . LYS A 1 69  ? -2.528  -8.976  -5.918  1.00 28.37 ? 71  LYS A N   1 
ATOM   529  C CA  . LYS A 1 69  ? -3.493  -7.880  -5.896  1.00 27.22 ? 71  LYS A CA  1 
ATOM   530  C C   . LYS A 1 69  ? -2.783  -6.534  -5.958  1.00 27.18 ? 71  LYS A C   1 
ATOM   531  O O   . LYS A 1 69  ? -3.293  -5.581  -6.558  1.00 28.01 ? 71  LYS A O   1 
ATOM   532  C CB  . LYS A 1 69  ? -4.368  -7.948  -4.641  1.00 26.17 ? 71  LYS A CB  1 
ATOM   533  C CG  . LYS A 1 69  ? -5.347  -9.131  -4.534  1.00 27.43 ? 71  LYS A CG  1 
ATOM   534  C CD  . LYS A 1 69  ? -5.708  -9.344  -3.060  1.00 33.12 ? 71  LYS A CD  1 
ATOM   535  C CE  . LYS A 1 69  ? -7.114  -9.889  -2.831  1.00 44.36 ? 71  LYS A CE  1 
ATOM   536  N NZ  . LYS A 1 69  ? -7.315  -11.226 -3.437  1.00 37.72 ? 71  LYS A NZ  1 
ATOM   537  N N   . GLY A 1 70  ? -1.613  -6.427  -5.321  1.00 27.19 ? 72  GLY A N   1 
ATOM   538  C CA  . GLY A 1 70  ? -0.929  -5.144  -5.266  1.00 24.79 ? 72  GLY A CA  1 
ATOM   539  C C   . GLY A 1 70  ? -0.497  -4.649  -6.638  1.00 27.06 ? 72  GLY A C   1 
ATOM   540  O O   . GLY A 1 70  ? -0.668  -3.473  -6.971  1.00 26.07 ? 72  GLY A O   1 
ATOM   541  N N   . MET A 1 71  ? 0.065   -5.543  -7.458  1.00 24.36 ? 73  MET A N   1 
ATOM   542  C CA  . MET A 1 71  ? 0.523   -5.118  -8.781  1.00 25.56 ? 73  MET A CA  1 
ATOM   543  C C   . MET A 1 71  ? -0.654  -4.760  -9.680  1.00 26.09 ? 73  MET A C   1 
ATOM   544  O O   . MET A 1 71  ? -0.581  -3.795  -10.457 1.00 24.42 ? 73  MET A O   1 
ATOM   545  C CB  . MET A 1 71  ? 1.394   -6.203  -9.426  1.00 22.18 ? 73  MET A CB  1 
ATOM   546  C CG  . MET A 1 71  ? 0.655   -7.431  -9.922  1.00 22.20 ? 73  MET A CG  1 
ATOM   547  S SD  . MET A 1 71  ? 1.794   -8.815  -10.145 1.00 29.08 ? 73  MET A SD  1 
ATOM   548  C CE  . MET A 1 71  ? 0.720   -10.096 -10.792 1.00 22.82 ? 73  MET A CE  1 
ATOM   549  N N   . ARG A 1 72  ? -1.751  -5.518  -9.578  1.00 26.21 ? 74  ARG A N   1 
ATOM   550  C CA  . ARG A 1 72  ? -2.937  -5.202  -10.359 1.00 24.18 ? 74  ARG A CA  1 
ATOM   551  C C   . ARG A 1 72  ? -3.461  -3.827  -10.000 1.00 23.53 ? 74  ARG A C   1 
ATOM   552  O O   . ARG A 1 72  ? -3.816  -3.038  -10.885 1.00 26.00 ? 74  ARG A O   1 
ATOM   553  C CB  . ARG A 1 72  ? -4.009  -6.267  -10.142 1.00 22.33 ? 74  ARG A CB  1 
ATOM   554  C CG  . ARG A 1 72  ? -3.605  -7.619  -10.718 1.00 27.26 ? 74  ARG A CG  1 
ATOM   555  C CD  . ARG A 1 72  ? -4.774  -8.601  -10.820 1.00 27.36 ? 74  ARG A CD  1 
ATOM   556  N NE  . ARG A 1 72  ? -5.028  -9.299  -9.562  1.00 27.71 ? 74  ARG A NE  1 
ATOM   557  C CZ  . ARG A 1 72  ? -4.449  -10.445 -9.222  1.00 27.07 ? 74  ARG A CZ  1 
ATOM   558  N NH1 . ARG A 1 72  ? -3.590  -11.020 -10.047 1.00 25.92 ? 74  ARG A NH1 1 
ATOM   559  N NH2 . ARG A 1 72  ? -4.726  -11.015 -8.058  1.00 26.73 ? 74  ARG A NH2 1 
ATOM   560  N N   . LYS A 1 73  ? -3.491  -3.511  -8.705  1.00 24.44 ? 75  LYS A N   1 
ATOM   561  C CA  . LYS A 1 73  ? -4.011  -2.222  -8.268  1.00 25.43 ? 75  LYS A CA  1 
ATOM   562  C C   . LYS A 1 73  ? -3.185  -1.078  -8.846  1.00 24.00 ? 75  LYS A C   1 
ATOM   563  O O   . LYS A 1 73  ? -3.732  -0.135  -9.424  1.00 26.01 ? 75  LYS A O   1 
ATOM   564  C CB  . LYS A 1 73  ? -4.041  -2.163  -6.737  1.00 24.64 ? 75  LYS A CB  1 
ATOM   565  C CG  . LYS A 1 73  ? -4.399  -0.797  -6.167  1.00 27.83 ? 75  LYS A CG  1 
ATOM   566  C CD  . LYS A 1 73  ? -4.693  -0.919  -4.670  1.00 29.08 ? 75  LYS A CD  1 
ATOM   567  C CE  . LYS A 1 73  ? -3.409  -1.098  -3.877  1.00 33.24 ? 75  LYS A CE  1 
ATOM   568  N NZ  . LYS A 1 73  ? -3.595  -1.077  -2.397  1.00 31.83 ? 75  LYS A NZ  1 
ATOM   569  N N   . ILE A 1 74  ? -1.859  -1.176  -8.751  1.00 28.35 ? 76  ILE A N   1 
ATOM   570  C CA  . ILE A 1 74  ? -0.989  -0.054  -9.096  1.00 25.79 ? 76  ILE A CA  1 
ATOM   571  C C   . ILE A 1 74  ? -0.719  -0.000  -10.598 1.00 24.93 ? 76  ILE A C   1 
ATOM   572  O O   . ILE A 1 74  ? -0.688  1.083   -11.188 1.00 23.68 ? 76  ILE A O   1 
ATOM   573  C CB  . ILE A 1 74  ? 0.323   -0.143  -8.296  1.00 23.34 ? 76  ILE A CB  1 
ATOM   574  C CG1 . ILE A 1 74  ? 0.055   -0.124  -6.802  1.00 24.22 ? 76  ILE A CG1 1 
ATOM   575  C CG2 . ILE A 1 74  ? 1.222   1.012   -8.641  1.00 24.43 ? 76  ILE A CG2 1 
ATOM   576  C CD1 . ILE A 1 74  ? -0.659  1.125   -6.325  1.00 25.76 ? 76  ILE A CD1 1 
ATOM   577  N N   . PHE A 1 75  ? -0.533  -1.153  -11.246 1.00 20.57 ? 77  PHE A N   1 
ATOM   578  C CA  . PHE A 1 75  ? -0.094  -1.183  -12.639 1.00 24.05 ? 77  PHE A CA  1 
ATOM   579  C C   . PHE A 1 75  ? -1.079  -1.814  -13.624 1.00 25.67 ? 77  PHE A C   1 
ATOM   580  O O   . PHE A 1 75  ? -0.798  -1.827  -14.828 1.00 28.80 ? 77  PHE A O   1 
ATOM   581  C CB  . PHE A 1 75  ? 1.238   -1.943  -12.758 1.00 25.31 ? 77  PHE A CB  1 
ATOM   582  C CG  . PHE A 1 75  ? 2.387   -1.333  -11.983 1.00 27.18 ? 77  PHE A CG  1 
ATOM   583  C CD1 . PHE A 1 75  ? 2.970   -0.138  -12.392 1.00 24.64 ? 77  PHE A CD1 1 
ATOM   584  C CD2 . PHE A 1 75  ? 2.920   -1.987  -10.873 1.00 24.51 ? 77  PHE A CD2 1 
ATOM   585  C CE1 . PHE A 1 75  ? 4.044   0.403   -11.695 1.00 24.86 ? 77  PHE A CE1 1 
ATOM   586  C CE2 . PHE A 1 75  ? 3.998   -1.445  -10.174 1.00 24.48 ? 77  PHE A CE2 1 
ATOM   587  C CZ  . PHE A 1 75  ? 4.564   -0.261  -10.594 1.00 22.62 ? 77  PHE A CZ  1 
ATOM   588  N N   . GLY A 1 76  ? -2.203  -2.350  -13.172 1.00 24.98 ? 78  GLY A N   1 
ATOM   589  C CA  . GLY A 1 76  ? -3.019  -3.146  -14.063 1.00 21.95 ? 78  GLY A CA  1 
ATOM   590  C C   . GLY A 1 76  ? -4.204  -2.470  -14.719 1.00 23.20 ? 78  GLY A C   1 
ATOM   591  O O   . GLY A 1 76  ? -4.677  -2.957  -15.749 1.00 26.56 ? 78  GLY A O   1 
ATOM   592  N N   . CYS A 1 77  ? -4.704  -1.368  -14.166 1.00 17.40 ? 79  CYS A N   1 
ATOM   593  C CA  . CYS A 1 77  ? -5.984  -0.815  -14.607 1.00 24.24 ? 79  CYS A CA  1 
ATOM   594  C C   . CYS A 1 77  ? -5.783  0.413   -15.485 1.00 26.26 ? 79  CYS A C   1 
ATOM   595  O O   . CYS A 1 77  ? -4.890  1.230   -15.229 1.00 22.75 ? 79  CYS A O   1 
ATOM   596  C CB  . CYS A 1 77  ? -6.878  -0.470  -13.406 1.00 26.90 ? 79  CYS A CB  1 
ATOM   597  S SG  . CYS A 1 77  ? -6.885  -1.752  -12.105 1.00 23.61 ? 79  CYS A SG  1 
ATOM   598  N N   . LYS A 1 78  ? -6.610  0.529   -16.534 1.00 24.67 ? 80  LYS A N   1 
ATOM   599  C CA  . LYS A 1 78  ? -6.623  1.749   -17.331 1.00 21.94 ? 80  LYS A CA  1 
ATOM   600  C C   . LYS A 1 78  ? -7.095  2.913   -16.472 1.00 25.57 ? 80  LYS A C   1 
ATOM   601  O O   . LYS A 1 78  ? -8.119  2.823   -15.786 1.00 24.38 ? 80  LYS A O   1 
ATOM   602  C CB  . LYS A 1 78  ? -7.526  1.604   -18.551 1.00 28.72 ? 80  LYS A CB  1 
ATOM   603  C CG  . LYS A 1 78  ? -7.503  2.832   -19.480 1.00 26.59 ? 80  LYS A CG  1 
ATOM   604  C CD  . LYS A 1 78  ? -8.504  2.670   -20.621 1.00 26.70 ? 80  LYS A CD  1 
ATOM   605  C CE  . LYS A 1 78  ? -9.911  3.085   -20.196 1.00 24.92 ? 80  LYS A CE  1 
ATOM   606  N NZ  . LYS A 1 78  ? -10.128 4.543   -20.347 1.00 27.22 ? 80  LYS A NZ  1 
ATOM   607  N N   . GLY A 1 79  ? -6.343  4.007   -16.513 1.00 20.76 ? 81  GLY A N   1 
ATOM   608  C CA  . GLY A 1 79  ? -6.555  5.125   -15.627 1.00 22.71 ? 81  GLY A CA  1 
ATOM   609  C C   . GLY A 1 79  ? -5.854  5.013   -14.287 1.00 28.25 ? 81  GLY A C   1 
ATOM   610  O O   . GLY A 1 79  ? -6.006  5.911   -13.453 1.00 24.62 ? 81  GLY A O   1 
ATOM   611  N N   . GLY A 1 80  ? -5.094  3.943   -14.049 1.00 24.08 ? 82  GLY A N   1 
ATOM   612  C CA  . GLY A 1 80  ? -4.359  3.826   -12.804 1.00 25.08 ? 82  GLY A CA  1 
ATOM   613  C C   . GLY A 1 80  ? -5.189  3.238   -11.674 1.00 28.45 ? 82  GLY A C   1 
ATOM   614  O O   . GLY A 1 80  ? -6.307  2.749   -11.862 1.00 24.31 ? 82  GLY A O   1 
ATOM   615  N N   . SER A 1 81  ? -4.620  3.326   -10.463 1.00 26.38 ? 83  SER A N   1 
ATOM   616  C CA  . SER A 1 81  ? -5.161  2.653   -9.284  1.00 26.14 ? 83  SER A CA  1 
ATOM   617  C C   . SER A 1 81  ? -6.543  3.156   -8.883  1.00 31.48 ? 83  SER A C   1 
ATOM   618  O O   . SER A 1 81  ? -7.284  2.419   -8.214  1.00 27.18 ? 83  SER A O   1 
ATOM   619  C CB  . SER A 1 81  ? -4.196  2.815   -8.109  1.00 24.62 ? 83  SER A CB  1 
ATOM   620  O OG  . SER A 1 81  ? -4.077  4.178   -7.747  1.00 28.68 ? 83  SER A OG  1 
ATOM   621  N N   . LYS A 1 82  ? -6.913  4.384   -9.267  1.00 24.93 ? 84  LYS A N   1 
ATOM   622  C CA  . LYS A 1 82  ? -8.262  4.857   -8.978  1.00 24.75 ? 84  LYS A CA  1 
ATOM   623  C C   . LYS A 1 82  ? -9.322  3.929   -9.553  1.00 26.32 ? 84  LYS A C   1 
ATOM   624  O O   . LYS A 1 82  ? -10.457 3.926   -9.069  1.00 27.99 ? 84  LYS A O   1 
ATOM   625  C CB  . LYS A 1 82  ? -8.452  6.285   -9.509  1.00 26.88 ? 84  LYS A CB  1 
ATOM   626  C CG  . LYS A 1 82  ? -8.972  6.358   -10.942 1.00 30.17 ? 84  LYS A CG  1 
ATOM   627  C CD  . LYS A 1 82  ? -9.060  7.785   -11.432 1.00 25.78 ? 84  LYS A CD  1 
ATOM   628  C CE  . LYS A 1 82  ? -9.285  7.825   -12.929 1.00 26.05 ? 84  LYS A CE  1 
ATOM   629  N NZ  . LYS A 1 82  ? -9.602  9.215   -13.376 1.00 26.18 ? 84  LYS A NZ  1 
ATOM   630  N N   . ASN A 1 83  ? -8.964  3.105   -10.542 1.00 28.89 ? 85  ASN A N   1 
ATOM   631  C CA  . ASN A 1 83  ? -9.909  2.238   -11.233 1.00 24.24 ? 85  ASN A CA  1 
ATOM   632  C C   . ASN A 1 83  ? -9.752  0.775   -10.846 1.00 27.15 ? 85  ASN A C   1 
ATOM   633  O O   . ASN A 1 83  ? -10.269 -0.108  -11.541 1.00 23.10 ? 85  ASN A O   1 
ATOM   634  C CB  . ASN A 1 83  ? -9.770  2.405   -12.739 1.00 22.69 ? 85  ASN A CB  1 
ATOM   635  C CG  . ASN A 1 83  ? -10.479 3.644   -13.231 1.00 30.42 ? 85  ASN A CG  1 
ATOM   636  O OD1 . ASN A 1 83  ? -11.445 4.105   -12.601 1.00 26.79 ? 85  ASN A OD1 1 
ATOM   637  N ND2 . ASN A 1 83  ? -10.009 4.200   -14.344 1.00 27.13 ? 85  ASN A ND2 1 
ATOM   638  N N   . TYR A 1 84  ? -9.042  0.506   -9.755  1.00 24.86 ? 86  TYR A N   1 
ATOM   639  C CA  . TYR A 1 84  ? -8.976  -0.837  -9.210  1.00 23.96 ? 86  TYR A CA  1 
ATOM   640  C C   . TYR A 1 84  ? -10.194 -1.066  -8.325  1.00 28.63 ? 86  TYR A C   1 
ATOM   641  O O   . TYR A 1 84  ? -10.459 -0.285  -7.408  1.00 29.41 ? 86  TYR A O   1 
ATOM   642  C CB  . TYR A 1 84  ? -7.686  -1.027  -8.403  1.00 22.69 ? 86  TYR A CB  1 
ATOM   643  C CG  . TYR A 1 84  ? -7.521  -2.416  -7.841  1.00 27.05 ? 86  TYR A CG  1 
ATOM   644  C CD1 . TYR A 1 84  ? -7.295  -3.508  -8.681  1.00 24.94 ? 86  TYR A CD1 1 
ATOM   645  C CD2 . TYR A 1 84  ? -7.602  -2.642  -6.474  1.00 23.46 ? 86  TYR A CD2 1 
ATOM   646  C CE1 . TYR A 1 84  ? -7.143  -4.786  -8.155  1.00 26.17 ? 86  TYR A CE1 1 
ATOM   647  C CE2 . TYR A 1 84  ? -7.459  -3.896  -5.948  1.00 25.62 ? 86  TYR A CE2 1 
ATOM   648  C CZ  . TYR A 1 84  ? -7.230  -4.975  -6.783  1.00 28.76 ? 86  TYR A CZ  1 
ATOM   649  O OH  . TYR A 1 84  ? -7.088  -6.236  -6.221  1.00 24.96 ? 86  TYR A OH  1 
ATOM   650  N N   . ASP A 1 85  ? -10.937 -2.131  -8.607  1.00 27.09 ? 87  ASP A N   1 
ATOM   651  C CA  . ASP A 1 85  ? -12.046 -2.538  -7.759  1.00 28.13 ? 87  ASP A CA  1 
ATOM   652  C C   . ASP A 1 85  ? -11.526 -3.564  -6.765  1.00 29.35 ? 87  ASP A C   1 
ATOM   653  O O   . ASP A 1 85  ? -11.278 -4.715  -7.159  1.00 30.19 ? 87  ASP A O   1 
ATOM   654  C CB  . ASP A 1 85  ? -13.174 -3.125  -8.598  1.00 29.10 ? 87  ASP A CB  1 
ATOM   655  C CG  . ASP A 1 85  ? -14.386 -3.534  -7.775  1.00 32.90 ? 87  ASP A CG  1 
ATOM   656  O OD1 . ASP A 1 85  ? -15.493 -3.326  -8.283  1.00 35.02 ? 87  ASP A OD1 1 
ATOM   657  O OD2 . ASP A 1 85  ? -14.257 -4.089  -6.658  1.00 31.37 ? 87  ASP A OD2 1 
ATOM   658  N N   . PRO A 1 86  ? -11.345 -3.205  -5.487  1.00 31.44 ? 88  PRO A N   1 
ATOM   659  C CA  . PRO A 1 86  ? -10.803 -4.178  -4.514  1.00 30.59 ? 88  PRO A CA  1 
ATOM   660  C C   . PRO A 1 86  ? -11.689 -5.386  -4.330  1.00 35.24 ? 88  PRO A C   1 
ATOM   661  O O   . PRO A 1 86  ? -11.187 -6.489  -4.064  1.00 35.23 ? 88  PRO A O   1 
ATOM   662  C CB  . PRO A 1 86  ? -10.708 -3.385  -3.197  1.00 28.34 ? 88  PRO A CB  1 
ATOM   663  C CG  . PRO A 1 86  ? -11.084 -1.955  -3.526  1.00 35.22 ? 88  PRO A CG  1 
ATOM   664  C CD  . PRO A 1 86  ? -11.727 -1.917  -4.880  1.00 30.44 ? 88  PRO A CD  1 
ATOM   665  N N   . ILE A 1 87  ? -13.005 -5.198  -4.436  1.00 32.76 ? 89  ILE A N   1 
ATOM   666  C CA  . ILE A 1 87  ? -13.938 -6.276  -4.143  1.00 31.51 ? 89  ILE A CA  1 
ATOM   667  C C   . ILE A 1 87  ? -13.865 -7.337  -5.230  1.00 32.10 ? 89  ILE A C   1 
ATOM   668  O O   . ILE A 1 87  ? -13.787 -8.535  -4.945  1.00 31.23 ? 89  ILE A O   1 
ATOM   669  C CB  . ILE A 1 87  ? -15.357 -5.697  -3.976  1.00 35.04 ? 89  ILE A CB  1 
ATOM   670  C CG1 . ILE A 1 87  ? -15.459 -4.916  -2.664  1.00 29.97 ? 89  ILE A CG1 1 
ATOM   671  C CG2 . ILE A 1 87  ? -16.419 -6.800  -4.038  1.00 37.73 ? 89  ILE A CG2 1 
ATOM   672  C CD1 . ILE A 1 87  ? -16.878 -4.618  -2.257  1.00 43.67 ? 89  ILE A CD1 1 
ATOM   673  N N   . LEU A 1 88  ? -13.846 -6.914  -6.488  1.00 32.33 ? 90  LEU A N   1 
ATOM   674  C CA  . LEU A 1 88  ? -13.727 -7.828  -7.611  1.00 30.73 ? 90  LEU A CA  1 
ATOM   675  C C   . LEU A 1 88  ? -12.290 -8.205  -7.946  1.00 30.53 ? 90  LEU A C   1 
ATOM   676  O O   . LEU A 1 88  ? -12.095 -9.126  -8.747  1.00 28.36 ? 90  LEU A O   1 
ATOM   677  C CB  . LEU A 1 88  ? -14.372 -7.219  -8.857  1.00 28.15 ? 90  LEU A CB  1 
ATOM   678  C CG  . LEU A 1 88  ? -15.888 -7.040  -8.773  1.00 40.64 ? 90  LEU A CG  1 
ATOM   679  C CD1 . LEU A 1 88  ? -16.420 -6.539  -10.106 1.00 29.62 ? 90  LEU A CD1 1 
ATOM   680  C CD2 . LEU A 1 88  ? -16.587 -8.337  -8.350  1.00 33.71 ? 90  LEU A CD2 1 
ATOM   681  N N   . ASP A 1 89  ? -11.288 -7.524  -7.382  1.00 27.82 ? 91  ASP A N   1 
ATOM   682  C CA  . ASP A 1 89  ? -9.896  -7.713  -7.800  1.00 26.62 ? 91  ASP A CA  1 
ATOM   683  C C   . ASP A 1 89  ? -9.786  -7.551  -9.316  1.00 24.67 ? 91  ASP A C   1 
ATOM   684  O O   . ASP A 1 89  ? -9.309  -8.430  -10.033 1.00 27.77 ? 91  ASP A O   1 
ATOM   685  C CB  . ASP A 1 89  ? -9.378  -9.086  -7.350  1.00 24.93 ? 91  ASP A CB  1 
ATOM   686  C CG  . ASP A 1 89  ? -7.847  -9.235  -7.454  1.00 30.92 ? 91  ASP A CG  1 
ATOM   687  O OD1 . ASP A 1 89  ? -7.369  -10.393 -7.380  1.00 26.67 ? 91  ASP A OD1 1 
ATOM   688  O OD2 . ASP A 1 89  ? -7.118  -8.223  -7.591  1.00 26.52 ? 91  ASP A OD2 1 
ATOM   689  N N   . ASP A 1 90  ? -10.274 -6.415  -9.809  1.00 24.78 ? 92  ASP A N   1 
ATOM   690  C CA  . ASP A 1 90  ? -10.399 -6.243  -11.252 1.00 24.99 ? 92  ASP A CA  1 
ATOM   691  C C   . ASP A 1 90  ? -10.482 -4.761  -11.591 1.00 26.98 ? 92  ASP A C   1 
ATOM   692  O O   . ASP A 1 90  ? -10.654 -3.898  -10.724 1.00 24.54 ? 92  ASP A O   1 
ATOM   693  C CB  . ASP A 1 90  ? -11.615 -6.997  -11.807 1.00 25.21 ? 92  ASP A CB  1 
ATOM   694  C CG  . ASP A 1 90  ? -11.428 -7.432  -13.260 1.00 29.14 ? 92  ASP A CG  1 
ATOM   695  O OD1 . ASP A 1 90  ? -10.540 -6.887  -13.964 1.00 27.73 ? 92  ASP A OD1 1 
ATOM   696  O OD2 . ASP A 1 90  ? -12.177 -8.328  -13.695 1.00 33.36 ? 92  ASP A OD2 1 
ATOM   697  N N   . ALA A 1 91  ? -10.344 -4.483  -12.876 1.00 24.61 ? 93  ALA A N   1 
ATOM   698  C CA  . ALA A 1 91  ? -10.334 -3.119  -13.364 1.00 27.95 ? 93  ALA A CA  1 
ATOM   699  C C   . ALA A 1 91  ? -11.754 -2.664  -13.653 1.00 27.25 ? 93  ALA A C   1 
ATOM   700  O O   . ALA A 1 91  ? -12.551 -3.413  -14.222 1.00 33.66 ? 93  ALA A O   1 
ATOM   701  C CB  . ALA A 1 91  ? -9.467  -3.017  -14.617 1.00 24.42 ? 93  ALA A CB  1 
ATOM   702  N N   . LYS A 1 92  ? -12.064 -1.427  -13.261 1.00 24.90 ? 94  LYS A N   1 
ATOM   703  C CA  . LYS A 1 92  ? -13.396 -0.885  -13.501 1.00 27.50 ? 94  LYS A CA  1 
ATOM   704  C C   . LYS A 1 92  ? -13.603 -0.430  -14.946 1.00 26.58 ? 94  LYS A C   1 
ATOM   705  O O   . LYS A 1 92  ? -14.740 -0.417  -15.426 1.00 27.89 ? 94  LYS A O   1 
ATOM   706  C CB  . LYS A 1 92  ? -13.669 0.294   -12.563 1.00 22.72 ? 94  LYS A CB  1 
ATOM   707  C CG  . LYS A 1 92  ? -13.788 -0.071  -11.099 1.00 27.16 ? 94  LYS A CG  1 
ATOM   708  C CD  . LYS A 1 92  ? -14.285 1.135   -10.316 1.00 32.93 ? 94  LYS A CD  1 
ATOM   709  C CE  . LYS A 1 92  ? -13.727 1.213   -8.912  1.00 32.66 ? 94  LYS A CE  1 
ATOM   710  N NZ  . LYS A 1 92  ? -13.734 2.635   -8.488  1.00 36.56 ? 94  LYS A NZ  1 
ATOM   711  N N   . GLU A 1 93  ? -12.546 -0.016  -15.639 1.00 24.36 ? 95  GLU A N   1 
ATOM   712  C CA  . GLU A 1 93  ? -12.689 0.590   -16.955 1.00 24.37 ? 95  GLU A CA  1 
ATOM   713  C C   . GLU A 1 93  ? -11.735 -0.049  -17.950 1.00 25.73 ? 95  GLU A C   1 
ATOM   714  O O   . GLU A 1 93  ? -11.339 0.575   -18.935 1.00 26.58 ? 95  GLU A O   1 
ATOM   715  C CB  . GLU A 1 93  ? -12.479 2.102   -16.885 1.00 23.42 ? 95  GLU A CB  1 
ATOM   716  C CG  . GLU A 1 93  ? -13.548 2.820   -16.060 1.00 21.80 ? 95  GLU A CG  1 
ATOM   717  C CD  . GLU A 1 93  ? -13.464 4.340   -16.112 1.00 26.30 ? 95  GLU A CD  1 
ATOM   718  O OE1 . GLU A 1 93  ? -12.824 4.908   -17.040 1.00 28.32 ? 95  GLU A OE1 1 
ATOM   719  O OE2 . GLU A 1 93  ? -14.046 4.976   -15.209 1.00 30.19 ? 95  GLU A OE2 1 
ATOM   720  N N   . GLY A 1 94  ? -11.362 -1.300  -17.706 1.00 25.05 ? 96  GLY A N   1 
ATOM   721  C CA  . GLY A 1 94  ? -10.473 -1.996  -18.634 1.00 24.57 ? 96  GLY A CA  1 
ATOM   722  C C   . GLY A 1 94  ? -9.135  -2.334  -18.006 1.00 26.67 ? 96  GLY A C   1 
ATOM   723  O O   . GLY A 1 94  ? -8.503  -1.528  -17.324 1.00 24.95 ? 96  GLY A O   1 
ATOM   724  N N   . ARG A 1 95  ? -8.700  -3.567  -18.244 1.00 27.81 ? 97  ARG A N   1 
ATOM   725  C CA  . ARG A 1 95  ? -7.365  -4.016  -17.866 1.00 26.53 ? 97  ARG A CA  1 
ATOM   726  C C   . ARG A 1 95  ? -6.357  -3.443  -18.854 1.00 24.20 ? 97  ARG A C   1 
ATOM   727  O O   . ARG A 1 95  ? -6.362  -3.804  -20.034 1.00 28.21 ? 97  ARG A O   1 
ATOM   728  C CB  . ARG A 1 95  ? -7.302  -5.543  -17.846 1.00 25.37 ? 97  ARG A CB  1 
ATOM   729  C CG  . ARG A 1 95  ? -8.360  -6.203  -16.982 1.00 22.87 ? 97  ARG A CG  1 
ATOM   730  C CD  . ARG A 1 95  ? -8.278  -7.713  -17.042 1.00 22.08 ? 97  ARG A CD  1 
ATOM   731  N NE  . ARG A 1 95  ? -9.206  -8.323  -16.098 1.00 22.21 ? 97  ARG A NE  1 
ATOM   732  C CZ  . ARG A 1 95  ? -9.383  -9.635  -15.949 1.00 27.33 ? 97  ARG A CZ  1 
ATOM   733  N NH1 . ARG A 1 95  ? -8.702  -10.492 -16.687 1.00 25.78 ? 97  ARG A NH1 1 
ATOM   734  N NH2 . ARG A 1 95  ? -10.261 -10.093 -15.064 1.00 29.34 ? 97  ARG A NH2 1 
ATOM   735  N N   . LEU A 1 96  ? -5.489  -2.554  -18.377 1.00 27.47 ? 98  LEU A N   1 
ATOM   736  C CA  . LEU A 1 96  ? -4.396  -2.042  -19.201 1.00 25.92 ? 98  LEU A CA  1 
ATOM   737  C C   . LEU A 1 96  ? -3.281  -3.069  -19.366 1.00 23.97 ? 98  LEU A C   1 
ATOM   738  O O   . LEU A 1 96  ? -2.682  -3.167  -20.440 1.00 23.62 ? 98  LEU A O   1 
ATOM   739  C CB  . LEU A 1 96  ? -3.833  -0.753  -18.587 1.00 26.57 ? 98  LEU A CB  1 
ATOM   740  C CG  . LEU A 1 96  ? -2.698  -0.008  -19.300 1.00 26.69 ? 98  LEU A CG  1 
ATOM   741  C CD1 . LEU A 1 96  ? -3.210  0.633   -20.611 1.00 23.30 ? 98  LEU A CD1 1 
ATOM   742  C CD2 . LEU A 1 96  ? -2.090  1.038   -18.358 1.00 20.25 ? 98  LEU A CD2 1 
ATOM   743  N N   . ARG A 1 97  ? -2.984  -3.839  -18.332 1.00 22.16 ? 99  ARG A N   1 
ATOM   744  C CA  . ARG A 1 97  ? -1.919  -4.836  -18.386 1.00 25.57 ? 99  ARG A CA  1 
ATOM   745  C C   . ARG A 1 97  ? -2.554  -6.168  -18.011 1.00 26.07 ? 99  ARG A C   1 
ATOM   746  O O   . ARG A 1 97  ? -2.457  -6.632  -16.864 1.00 23.43 ? 99  ARG A O   1 
ATOM   747  C CB  . ARG A 1 97  ? -0.741  -4.422  -17.501 1.00 25.35 ? 99  ARG A CB  1 
ATOM   748  C CG  . ARG A 1 97  ? -0.217  -3.020  -17.868 1.00 23.42 ? 99  ARG A CG  1 
ATOM   749  C CD  . ARG A 1 97  ? 1.202   -2.747  -17.392 1.00 23.99 ? 99  ARG A CD  1 
ATOM   750  N NE  . ARG A 1 97  ? 1.720   -1.502  -17.948 1.00 23.01 ? 99  ARG A NE  1 
ATOM   751  C CZ  . ARG A 1 97  ? 1.475   -0.299  -17.426 1.00 28.35 ? 99  ARG A CZ  1 
ATOM   752  N NH1 . ARG A 1 97  ? 0.726   -0.187  -16.330 1.00 25.58 ? 99  ARG A NH1 1 
ATOM   753  N NH2 . ARG A 1 97  ? 1.967   0.796   -17.993 1.00 25.51 ? 99  ARG A NH2 1 
ATOM   754  N N   . PRO A 1 98  ? -3.227  -6.810  -18.975 1.00 25.20 ? 100 PRO A N   1 
ATOM   755  C CA  . PRO A 1 98  ? -4.017  -8.015  -18.668 1.00 26.37 ? 100 PRO A CA  1 
ATOM   756  C C   . PRO A 1 98  ? -3.196  -9.198  -18.198 1.00 25.68 ? 100 PRO A C   1 
ATOM   757  O O   . PRO A 1 98  ? -3.757  -10.100 -17.570 1.00 26.60 ? 100 PRO A O   1 
ATOM   758  C CB  . PRO A 1 98  ? -4.718  -8.342  -19.997 1.00 27.53 ? 100 PRO A CB  1 
ATOM   759  C CG  . PRO A 1 98  ? -4.324  -7.272  -20.967 1.00 24.40 ? 100 PRO A CG  1 
ATOM   760  C CD  . PRO A 1 98  ? -3.237  -6.450  -20.404 1.00 27.17 ? 100 PRO A CD  1 
ATOM   761  N N   . LYS A 1 99  ? -1.895  -9.236  -18.469 1.00 27.80 ? 101 LYS A N   1 
ATOM   762  C CA  . LYS A 1 99  ? -1.102  -10.365 -17.998 1.00 26.50 ? 101 LYS A CA  1 
ATOM   763  C C   . LYS A 1 99  ? -0.930  -10.360 -16.486 1.00 26.89 ? 101 LYS A C   1 
ATOM   764  O O   . LYS A 1 99  ? -0.610  -11.405 -15.908 1.00 29.11 ? 101 LYS A O   1 
ATOM   765  C CB  . LYS A 1 99  ? 0.258   -10.377 -18.689 1.00 28.08 ? 101 LYS A CB  1 
ATOM   766  C CG  . LYS A 1 99  ? 0.156   -10.854 -20.117 1.00 29.80 ? 101 LYS A CG  1 
ATOM   767  C CD  . LYS A 1 99  ? 1.179   -10.204 -20.981 1.00 30.07 ? 101 LYS A CD  1 
ATOM   768  C CE  . LYS A 1 99  ? 2.429   -11.008 -21.015 1.00 31.08 ? 101 LYS A CE  1 
ATOM   769  N NZ  . LYS A 1 99  ? 3.602   -10.108 -21.193 1.00 32.21 ? 101 LYS A NZ  1 
ATOM   770  N N   . LEU A 1 100 ? -1.157  -9.226  -15.823 1.00 25.85 ? 102 LEU A N   1 
ATOM   771  C CA  . LEU A 1 100 ? -1.178  -9.256  -14.364 1.00 26.13 ? 102 LEU A CA  1 
ATOM   772  C C   . LEU A 1 100 ? -2.314  -10.120 -13.836 1.00 26.74 ? 102 LEU A C   1 
ATOM   773  O O   . LEU A 1 100 ? -2.293  -10.509 -12.666 1.00 28.12 ? 102 LEU A O   1 
ATOM   774  C CB  . LEU A 1 100 ? -1.287  -7.840  -13.804 1.00 22.24 ? 102 LEU A CB  1 
ATOM   775  C CG  . LEU A 1 100 ? -0.161  -6.931  -14.280 1.00 23.17 ? 102 LEU A CG  1 
ATOM   776  C CD1 . LEU A 1 100 ? -0.288  -5.586  -13.604 1.00 20.36 ? 102 LEU A CD1 1 
ATOM   777  C CD2 . LEU A 1 100 ? 1.195   -7.605  -13.996 1.00 18.11 ? 102 LEU A CD2 1 
ATOM   778  N N   . TRP A 1 101 ? -3.314  -10.404 -14.671 1.00 27.08 ? 103 TRP A N   1 
ATOM   779  C CA  . TRP A 1 101 ? -4.400  -11.321 -14.342 1.00 29.51 ? 103 TRP A CA  1 
ATOM   780  C C   . TRP A 1 101 ? -4.104  -12.732 -14.851 1.00 31.23 ? 103 TRP A C   1 
ATOM   781  O O   . TRP A 1 101 ? -4.114  -13.694 -14.076 1.00 32.37 ? 103 TRP A O   1 
ATOM   782  C CB  . TRP A 1 101 ? -5.717  -10.806 -14.939 1.00 27.19 ? 103 TRP A CB  1 
ATOM   783  C CG  . TRP A 1 101 ? -6.408  -9.801  -14.094 1.00 25.04 ? 103 TRP A CG  1 
ATOM   784  C CD1 . TRP A 1 101 ? -7.381  -10.039 -13.170 1.00 24.69 ? 103 TRP A CD1 1 
ATOM   785  C CD2 . TRP A 1 101 ? -6.172  -8.395  -14.076 1.00 24.72 ? 103 TRP A CD2 1 
ATOM   786  N NE1 . TRP A 1 101 ? -7.767  -8.868  -12.577 1.00 26.48 ? 103 TRP A NE1 1 
ATOM   787  C CE2 . TRP A 1 101 ? -7.043  -7.841  -13.119 1.00 23.17 ? 103 TRP A CE2 1 
ATOM   788  C CE3 . TRP A 1 101 ? -5.300  -7.549  -14.768 1.00 23.49 ? 103 TRP A CE3 1 
ATOM   789  C CZ2 . TRP A 1 101 ? -7.072  -6.486  -12.841 1.00 23.15 ? 103 TRP A CZ2 1 
ATOM   790  C CZ3 . TRP A 1 101 ? -5.337  -6.210  -14.501 1.00 21.29 ? 103 TRP A CZ3 1 
ATOM   791  C CH2 . TRP A 1 101 ? -6.217  -5.685  -13.547 1.00 23.50 ? 103 TRP A CH2 1 
ATOM   792  N N   . THR A 1 102 ? -3.832  -12.871 -16.156 1.00 29.29 ? 104 THR A N   1 
ATOM   793  C CA  . THR A 1 102 ? -3.686  -14.201 -16.738 1.00 28.67 ? 104 THR A CA  1 
ATOM   794  C C   . THR A 1 102 ? -2.328  -14.829 -16.471 1.00 28.47 ? 104 THR A C   1 
ATOM   795  O O   . THR A 1 102 ? -2.219  -16.058 -16.511 1.00 34.24 ? 104 THR A O   1 
ATOM   796  C CB  . THR A 1 102 ? -3.915  -14.171 -18.254 1.00 32.03 ? 104 THR A CB  1 
ATOM   797  O OG1 . THR A 1 102 ? -3.008  -13.240 -18.855 1.00 32.39 ? 104 THR A OG1 1 
ATOM   798  C CG2 . THR A 1 102 ? -5.372  -13.796 -18.602 1.00 24.02 ? 104 THR A CG2 1 
ATOM   799  N N   . HIS A 1 103 ? -1.292  -14.035 -16.229 1.00 27.48 ? 105 HIS A N   1 
ATOM   800  C CA  . HIS A 1 103 ? 0.052   -14.549 -15.991 1.00 29.92 ? 105 HIS A CA  1 
ATOM   801  C C   . HIS A 1 103 ? 0.545   -14.129 -14.615 1.00 32.39 ? 105 HIS A C   1 
ATOM   802  O O   . HIS A 1 103 ? 1.730   -13.852 -14.407 1.00 30.38 ? 105 HIS A O   1 
ATOM   803  C CB  . HIS A 1 103 ? 1.022   -14.083 -17.073 1.00 32.65 ? 105 HIS A CB  1 
ATOM   804  C CG  . HIS A 1 103 ? 0.693   -14.601 -18.436 1.00 31.23 ? 105 HIS A CG  1 
ATOM   805  N ND1 . HIS A 1 103 ? -0.443  -14.226 -19.118 1.00 32.71 ? 105 HIS A ND1 1 
ATOM   806  C CD2 . HIS A 1 103 ? 1.349   -15.468 -19.243 1.00 34.24 ? 105 HIS A CD2 1 
ATOM   807  C CE1 . HIS A 1 103 ? -0.478  -14.840 -20.286 1.00 32.96 ? 105 HIS A CE1 1 
ATOM   808  N NE2 . HIS A 1 103 ? 0.598   -15.599 -20.388 1.00 36.83 ? 105 HIS A NE2 1 
ATOM   809  N N   . GLU A 1 104 ? -0.399  -14.082 -13.675 1.00 32.23 ? 106 GLU A N   1 
ATOM   810  C CA  . GLU A 1 104 ? -0.181  -13.643 -12.302 1.00 32.04 ? 106 GLU A CA  1 
ATOM   811  C C   . GLU A 1 104 ? 1.133   -14.127 -11.718 1.00 30.87 ? 106 GLU A C   1 
ATOM   812  O O   . GLU A 1 104 ? 1.924   -13.340 -11.187 1.00 30.85 ? 106 GLU A O   1 
ATOM   813  C CB  . GLU A 1 104 ? -1.347  -14.155 -11.455 1.00 28.36 ? 106 GLU A CB  1 
ATOM   814  C CG  . GLU A 1 104 ? -1.547  -13.445 -10.165 1.00 35.25 ? 106 GLU A CG  1 
ATOM   815  C CD  . GLU A 1 104 ? -2.688  -14.051 -9.378  1.00 36.70 ? 106 GLU A CD  1 
ATOM   816  O OE1 . GLU A 1 104 ? -2.733  -15.286 -9.278  1.00 38.92 ? 106 GLU A OE1 1 
ATOM   817  O OE2 . GLU A 1 104 ? -3.558  -13.306 -8.883  1.00 38.63 ? 106 GLU A OE2 1 
ATOM   818  N N   . SER A 1 105 ? 1.366   -15.439 -11.782 1.00 30.61 ? 107 SER A N   1 
ATOM   819  C CA  . SER A 1 105 ? 2.490   -16.017 -11.061 1.00 33.29 ? 107 SER A CA  1 
ATOM   820  C C   . SER A 1 105 ? 3.825   -15.626 -11.680 1.00 29.30 ? 107 SER A C   1 
ATOM   821  O O   . SER A 1 105 ? 4.844   -15.698 -10.992 1.00 29.73 ? 107 SER A O   1 
ATOM   822  C CB  . SER A 1 105 ? 2.333   -17.548 -10.973 1.00 31.08 ? 107 SER A CB  1 
ATOM   823  O OG  . SER A 1 105 ? 2.451   -18.161 -12.247 1.00 38.36 ? 107 SER A OG  1 
ATOM   824  N N   . ASP A 1 106 ? 3.828   -15.178 -12.943 1.00 27.12 ? 108 ASP A N   1 
ATOM   825  C CA  . ASP A 1 106 ? 5.060   -14.738 -13.594 1.00 30.43 ? 108 ASP A CA  1 
ATOM   826  C C   . ASP A 1 106 ? 5.532   -13.384 -13.079 1.00 31.64 ? 108 ASP A C   1 
ATOM   827  O O   . ASP A 1 106 ? 6.725   -13.079 -13.183 1.00 30.99 ? 108 ASP A O   1 
ATOM   828  C CB  . ASP A 1 106 ? 4.882   -14.615 -15.112 1.00 30.59 ? 108 ASP A CB  1 
ATOM   829  C CG  . ASP A 1 106 ? 4.656   -15.945 -15.812 1.00 32.65 ? 108 ASP A CG  1 
ATOM   830  O OD1 . ASP A 1 106 ? 4.799   -17.026 -15.199 1.00 32.59 ? 108 ASP A OD1 1 
ATOM   831  O OD2 . ASP A 1 106 ? 4.310   -15.890 -17.011 1.00 38.64 ? 108 ASP A OD2 1 
ATOM   832  N N   . TYR A 1 107 ? 4.622   -12.541 -12.571 1.00 25.68 ? 109 TYR A N   1 
ATOM   833  C CA  . TYR A 1 107 ? 4.969   -11.157 -12.256 1.00 27.01 ? 109 TYR A CA  1 
ATOM   834  C C   . TYR A 1 107 ? 4.920   -10.821 -10.775 1.00 29.68 ? 109 TYR A C   1 
ATOM   835  O O   . TYR A 1 107 ? 5.662   -9.937  -10.338 1.00 29.72 ? 109 TYR A O   1 
ATOM   836  C CB  . TYR A 1 107 ? 4.062   -10.187 -13.027 1.00 23.00 ? 109 TYR A CB  1 
ATOM   837  C CG  . TYR A 1 107 ? 4.264   -10.316 -14.527 1.00 29.03 ? 109 TYR A CG  1 
ATOM   838  C CD1 . TYR A 1 107 ? 5.429   -9.843  -15.133 1.00 26.44 ? 109 TYR A CD1 1 
ATOM   839  C CD2 . TYR A 1 107 ? 3.312   -10.936 -15.330 1.00 25.48 ? 109 TYR A CD2 1 
ATOM   840  C CE1 . TYR A 1 107 ? 5.633   -9.970  -16.488 1.00 24.57 ? 109 TYR A CE1 1 
ATOM   841  C CE2 . TYR A 1 107 ? 3.509   -11.076 -16.696 1.00 27.53 ? 109 TYR A CE2 1 
ATOM   842  C CZ  . TYR A 1 107 ? 4.671   -10.590 -17.275 1.00 28.83 ? 109 TYR A CZ  1 
ATOM   843  O OH  . TYR A 1 107 ? 4.875   -10.724 -18.636 1.00 27.04 ? 109 TYR A OH  1 
ATOM   844  N N   . ALA A 1 108 ? 4.073   -11.502 -10.002 1.00 26.18 ? 110 ALA A N   1 
ATOM   845  C CA  . ALA A 1 108 ? 4.000   -11.288 -8.564  1.00 29.03 ? 110 ALA A CA  1 
ATOM   846  C C   . ALA A 1 108 ? 5.296   -11.728 -7.884  1.00 29.42 ? 110 ALA A C   1 
ATOM   847  O O   . ALA A 1 108 ? 5.830   -12.805 -8.173  1.00 27.58 ? 110 ALA A O   1 
ATOM   848  C CB  . ALA A 1 108 ? 2.812   -12.061 -7.980  1.00 26.81 ? 110 ALA A CB  1 
ATOM   849  N N   . PHE A 1 109 ? 5.793   -10.891 -6.972  1.00 26.30 ? 111 PHE A N   1 
ATOM   850  C CA  . PHE A 1 109 ? 7.011   -11.154 -6.216  1.00 27.08 ? 111 PHE A CA  1 
ATOM   851  C C   . PHE A 1 109 ? 8.221   -11.365 -7.127  1.00 27.21 ? 111 PHE A C   1 
ATOM   852  O O   . PHE A 1 109 ? 9.217   -11.973 -6.718  1.00 28.59 ? 111 PHE A O   1 
ATOM   853  C CB  . PHE A 1 109 ? 6.797   -12.344 -5.269  1.00 25.21 ? 111 PHE A CB  1 
ATOM   854  C CG  . PHE A 1 109 ? 5.669   -12.125 -4.292  1.00 27.14 ? 111 PHE A CG  1 
ATOM   855  C CD1 . PHE A 1 109 ? 5.760   -11.133 -3.324  1.00 27.98 ? 111 PHE A CD1 1 
ATOM   856  C CD2 . PHE A 1 109 ? 4.519   -12.892 -4.347  1.00 26.10 ? 111 PHE A CD2 1 
ATOM   857  C CE1 . PHE A 1 109 ? 4.733   -10.916 -2.412  1.00 27.36 ? 111 PHE A CE1 1 
ATOM   858  C CE2 . PHE A 1 109 ? 3.480   -12.691 -3.437  1.00 29.60 ? 111 PHE A CE2 1 
ATOM   859  C CZ  . PHE A 1 109 ? 3.585   -11.692 -2.467  1.00 27.72 ? 111 PHE A CZ  1 
ATOM   860  N N   . ASN A 1 110 ? 8.166   -10.843 -8.354  1.00 26.72 ? 112 ASN A N   1 
ATOM   861  C CA  . ASN A 1 110 ? 9.239   -10.981 -9.340  1.00 25.03 ? 112 ASN A CA  1 
ATOM   862  C C   . ASN A 1 110 ? 9.585   -9.585  -9.845  1.00 26.97 ? 112 ASN A C   1 
ATOM   863  O O   . ASN A 1 110 ? 9.116   -9.162  -10.913 1.00 27.04 ? 112 ASN A O   1 
ATOM   864  C CB  . ASN A 1 110 ? 8.813   -11.917 -10.479 1.00 29.01 ? 112 ASN A CB  1 
ATOM   865  C CG  . ASN A 1 110 ? 9.969   -12.303 -11.405 1.00 26.22 ? 112 ASN A CG  1 
ATOM   866  O OD1 . ASN A 1 110 ? 10.820  -11.484 -11.738 1.00 27.77 ? 112 ASN A OD1 1 
ATOM   867  N ND2 . ASN A 1 110 ? 10.001  -13.565 -11.805 1.00 27.85 ? 112 ASN A ND2 1 
ATOM   868  N N   . PRO A 1 111 ? 10.399  -8.832  -9.092  1.00 29.83 ? 113 PRO A N   1 
ATOM   869  C CA  . PRO A 1 111 ? 10.648  -7.426  -9.468  1.00 26.49 ? 113 PRO A CA  1 
ATOM   870  C C   . PRO A 1 111 ? 11.199  -7.223  -10.872 1.00 28.32 ? 113 PRO A C   1 
ATOM   871  O O   . PRO A 1 111 ? 10.829  -6.236  -11.528 1.00 26.03 ? 113 PRO A O   1 
ATOM   872  C CB  . PRO A 1 111 ? 11.635  -6.940  -8.393  1.00 26.97 ? 113 PRO A CB  1 
ATOM   873  C CG  . PRO A 1 111 ? 11.941  -8.138  -7.536  1.00 29.65 ? 113 PRO A CG  1 
ATOM   874  C CD  . PRO A 1 111 ? 10.855  -9.124  -7.725  1.00 24.57 ? 113 PRO A CD  1 
ATOM   875  N N   . VAL A 1 112 ? 12.066  -8.118  -11.359 1.00 26.92 ? 114 VAL A N   1 
ATOM   876  C CA  . VAL A 1 112 ? 12.616  -7.952  -12.704 1.00 25.73 ? 114 VAL A CA  1 
ATOM   877  C C   . VAL A 1 112 ? 11.523  -8.125  -13.754 1.00 27.67 ? 114 VAL A C   1 
ATOM   878  O O   . VAL A 1 112 ? 11.365  -7.289  -14.658 1.00 28.56 ? 114 VAL A O   1 
ATOM   879  C CB  . VAL A 1 112 ? 13.788  -8.928  -12.947 1.00 30.82 ? 114 VAL A CB  1 
ATOM   880  C CG1 . VAL A 1 112 ? 14.158  -8.946  -14.409 1.00 25.13 ? 114 VAL A CG1 1 
ATOM   881  C CG2 . VAL A 1 112 ? 15.005  -8.549  -12.109 1.00 28.05 ? 114 VAL A CG2 1 
ATOM   882  N N   . ALA A 1 113 ? 10.764  -9.218  -13.666 1.00 26.63 ? 115 ALA A N   1 
ATOM   883  C CA  . ALA A 1 113 ? 9.717   -9.459  -14.656 1.00 28.79 ? 115 ALA A CA  1 
ATOM   884  C C   . ALA A 1 113 ? 8.646   -8.376  -14.604 1.00 26.23 ? 115 ALA A C   1 
ATOM   885  O O   . ALA A 1 113 ? 8.181   -7.907  -15.647 1.00 27.90 ? 115 ALA A O   1 
ATOM   886  C CB  . ALA A 1 113 ? 9.086   -10.836 -14.450 1.00 29.25 ? 115 ALA A CB  1 
ATOM   887  N N   . LEU A 1 114 ? 8.257   -7.952  -13.399 1.00 27.05 ? 116 LEU A N   1 
ATOM   888  C CA  . LEU A 1 114 ? 7.221   -6.925  -13.268 1.00 27.63 ? 116 LEU A CA  1 
ATOM   889  C C   . LEU A 1 114 ? 7.687   -5.595  -13.851 1.00 26.13 ? 116 LEU A C   1 
ATOM   890  O O   . LEU A 1 114 ? 6.969   -4.971  -14.641 1.00 26.13 ? 116 LEU A O   1 
ATOM   891  C CB  . LEU A 1 114 ? 6.814   -6.750  -11.795 1.00 23.30 ? 116 LEU A CB  1 
ATOM   892  C CG  . LEU A 1 114 ? 5.698   -5.733  -11.530 1.00 22.75 ? 116 LEU A CG  1 
ATOM   893  C CD1 . LEU A 1 114 ? 4.412   -6.258  -12.134 1.00 21.13 ? 116 LEU A CD1 1 
ATOM   894  C CD2 . LEU A 1 114 ? 5.495   -5.468  -10.038 1.00 22.09 ? 116 LEU A CD2 1 
ATOM   895  N N   . GLY A 1 115 ? 8.882   -5.139  -13.460 1.00 23.81 ? 117 GLY A N   1 
ATOM   896  C CA  . GLY A 1 115 ? 9.377   -3.870  -13.967 1.00 22.97 ? 117 GLY A CA  1 
ATOM   897  C C   . GLY A 1 115 ? 9.555   -3.861  -15.474 1.00 23.34 ? 117 GLY A C   1 
ATOM   898  O O   . GLY A 1 115 ? 9.277   -2.856  -16.136 1.00 23.13 ? 117 GLY A O   1 
ATOM   899  N N   . ASN A 1 116 ? 10.018  -4.979  -16.043 1.00 24.17 ? 118 ASN A N   1 
ATOM   900  C CA  . ASN A 1 116 ? 10.170  -5.033  -17.494 1.00 23.19 ? 118 ASN A CA  1 
ATOM   901  C C   . ASN A 1 116 ? 8.820   -4.970  -18.201 1.00 22.30 ? 118 ASN A C   1 
ATOM   902  O O   . ASN A 1 116 ? 8.732   -4.443  -19.312 1.00 21.93 ? 118 ASN A O   1 
ATOM   903  C CB  . ASN A 1 116 ? 10.936  -6.290  -17.902 1.00 25.31 ? 118 ASN A CB  1 
ATOM   904  C CG  . ASN A 1 116 ? 12.409  -6.212  -17.550 1.00 25.44 ? 118 ASN A CG  1 
ATOM   905  O OD1 . ASN A 1 116 ? 12.939  -5.125  -17.295 1.00 24.13 ? 118 ASN A OD1 1 
ATOM   906  N ND2 . ASN A 1 116 ? 13.076  -7.368  -17.509 1.00 23.25 ? 118 ASN A ND2 1 
ATOM   907  N N   . TYR A 1 117 ? 7.761   -5.477  -17.566 1.00 25.11 ? 119 TYR A N   1 
ATOM   908  C CA  . TYR A 1 117 ? 6.429   -5.461  -18.170 1.00 23.92 ? 119 TYR A CA  1 
ATOM   909  C C   . TYR A 1 117 ? 5.756   -4.102  -18.010 1.00 25.70 ? 119 TYR A C   1 
ATOM   910  O O   . TYR A 1 117 ? 5.317   -3.498  -18.998 1.00 25.21 ? 119 TYR A O   1 
ATOM   911  C CB  . TYR A 1 117 ? 5.561   -6.563  -17.549 1.00 22.87 ? 119 TYR A CB  1 
ATOM   912  C CG  . TYR A 1 117 ? 4.141   -6.685  -18.095 1.00 23.84 ? 119 TYR A CG  1 
ATOM   913  C CD1 . TYR A 1 117 ? 3.864   -6.505  -19.446 1.00 23.92 ? 119 TYR A CD1 1 
ATOM   914  C CD2 . TYR A 1 117 ? 3.081   -7.018  -17.248 1.00 25.21 ? 119 TYR A CD2 1 
ATOM   915  C CE1 . TYR A 1 117 ? 2.562   -6.630  -19.939 1.00 24.67 ? 119 TYR A CE1 1 
ATOM   916  C CE2 . TYR A 1 117 ? 1.783   -7.147  -17.724 1.00 24.17 ? 119 TYR A CE2 1 
ATOM   917  C CZ  . TYR A 1 117 ? 1.535   -6.954  -19.072 1.00 25.58 ? 119 TYR A CZ  1 
ATOM   918  O OH  . TYR A 1 117 ? 0.266   -7.075  -19.558 1.00 25.72 ? 119 TYR A OH  1 
ATOM   919  N N   . VAL A 1 118 ? 5.668   -3.606  -16.772 1.00 20.78 ? 120 VAL A N   1 
ATOM   920  C CA  . VAL A 1 118 ? 4.810   -2.456  -16.503 1.00 22.30 ? 120 VAL A CA  1 
ATOM   921  C C   . VAL A 1 118 ? 5.437   -1.136  -16.945 1.00 25.30 ? 120 VAL A C   1 
ATOM   922  O O   . VAL A 1 118 ? 4.706   -0.159  -17.135 1.00 25.91 ? 120 VAL A O   1 
ATOM   923  C CB  . VAL A 1 118 ? 4.433   -2.370  -15.010 1.00 23.22 ? 120 VAL A CB  1 
ATOM   924  C CG1 . VAL A 1 118 ? 3.847   -3.692  -14.507 1.00 20.43 ? 120 VAL A CG1 1 
ATOM   925  C CG2 . VAL A 1 118 ? 5.627   -1.975  -14.188 1.00 23.04 ? 120 VAL A CG2 1 
ATOM   926  N N   . TYR A 1 119 ? 6.763   -1.075  -17.119 1.00 22.75 ? 121 TYR A N   1 
ATOM   927  C CA  . TYR A 1 119 ? 7.427   0.127   -17.614 1.00 23.30 ? 121 TYR A CA  1 
ATOM   928  C C   . TYR A 1 119 ? 7.874   0.006   -19.072 1.00 25.22 ? 121 TYR A C   1 
ATOM   929  O O   . TYR A 1 119 ? 8.517   0.923   -19.589 1.00 25.55 ? 121 TYR A O   1 
ATOM   930  C CB  . TYR A 1 119 ? 8.623   0.475   -16.723 1.00 20.89 ? 121 TYR A CB  1 
ATOM   931  C CG  . TYR A 1 119 ? 8.221   0.979   -15.356 1.00 23.36 ? 121 TYR A CG  1 
ATOM   932  C CD1 . TYR A 1 119 ? 7.057   1.716   -15.183 1.00 24.75 ? 121 TYR A CD1 1 
ATOM   933  C CD2 . TYR A 1 119 ? 9.000   0.705   -14.232 1.00 23.97 ? 121 TYR A CD2 1 
ATOM   934  C CE1 . TYR A 1 119 ? 6.681   2.175   -13.934 1.00 28.13 ? 121 TYR A CE1 1 
ATOM   935  C CE2 . TYR A 1 119 ? 8.630   1.161   -12.960 1.00 24.28 ? 121 TYR A CE2 1 
ATOM   936  C CZ  . TYR A 1 119 ? 7.472   1.898   -12.818 1.00 26.15 ? 121 TYR A CZ  1 
ATOM   937  O OH  . TYR A 1 119 ? 7.106   2.371   -11.575 1.00 21.06 ? 121 TYR A OH  1 
ATOM   938  N N   . ALA A 1 120 ? 7.538   -1.096  -19.746 1.00 25.78 ? 122 ALA A N   1 
ATOM   939  C CA  . ALA A 1 120 ? 7.850   -1.252  -21.162 1.00 23.32 ? 122 ALA A CA  1 
ATOM   940  C C   . ALA A 1 120 ? 7.207   -0.154  -22.008 1.00 22.67 ? 122 ALA A C   1 
ATOM   941  O O   . ALA A 1 120 ? 6.051   0.211   -21.803 1.00 23.88 ? 122 ALA A O   1 
ATOM   942  C CB  . ALA A 1 120 ? 7.380   -2.627  -21.653 1.00 23.03 ? 122 ALA A CB  1 
ATOM   943  N N   . ASN A 1 121 ? 7.970   0.373   -22.972 1.00 24.48 ? 123 ASN A N   1 
ATOM   944  C CA  . ASN A 1 121 ? 7.451   1.234   -24.037 1.00 25.84 ? 123 ASN A CA  1 
ATOM   945  C C   . ASN A 1 121 ? 6.777   2.506   -23.517 1.00 26.04 ? 123 ASN A C   1 
ATOM   946  O O   . ASN A 1 121 ? 5.992   3.118   -24.240 1.00 28.61 ? 123 ASN A O   1 
ATOM   947  C CB  . ASN A 1 121 ? 6.463   0.473   -24.936 1.00 20.02 ? 123 ASN A CB  1 
ATOM   948  C CG  . ASN A 1 121 ? 7.100   -0.716  -25.631 1.00 25.20 ? 123 ASN A CG  1 
ATOM   949  O OD1 . ASN A 1 121 ? 8.199   -0.612  -26.184 1.00 30.15 ? 123 ASN A OD1 1 
ATOM   950  N ND2 . ASN A 1 121 ? 6.417   -1.854  -25.608 1.00 20.46 ? 123 ASN A ND2 1 
ATOM   951  N N   . ARG A 1 122 ? 7.062   2.924   -22.285 1.00 27.55 ? 124 ARG A N   1 
ATOM   952  C CA  . ARG A 1 122 ? 6.378   4.073   -21.708 1.00 23.94 ? 124 ARG A CA  1 
ATOM   953  C C   . ARG A 1 122 ? 6.571   5.321   -22.573 1.00 29.04 ? 124 ARG A C   1 
ATOM   954  O O   . ARG A 1 122 ? 7.712   5.683   -22.897 1.00 27.57 ? 124 ARG A O   1 
ATOM   955  C CB  . ARG A 1 122 ? 6.880   4.337   -20.297 1.00 25.58 ? 124 ARG A CB  1 
ATOM   956  C CG  . ARG A 1 122 ? 6.292   3.415   -19.248 1.00 31.63 ? 124 ARG A CG  1 
ATOM   957  C CD  . ARG A 1 122 ? 4.909   3.819   -18.761 1.00 34.03 ? 124 ARG A CD  1 
ATOM   958  N NE  . ARG A 1 122 ? 4.389   2.849   -17.782 1.00 34.61 ? 124 ARG A NE  1 
ATOM   959  C CZ  . ARG A 1 122 ? 4.009   3.154   -16.542 1.00 36.07 ? 124 ARG A CZ  1 
ATOM   960  N NH1 . ARG A 1 122 ? 4.079   4.413   -16.114 1.00 31.74 ? 124 ARG A NH1 1 
ATOM   961  N NH2 . ARG A 1 122 ? 3.549   2.200   -15.734 1.00 30.46 ? 124 ARG A NH2 1 
ATOM   962  N N   . PRO A 1 123 ? 5.492   6.001   -22.959 1.00 30.04 ? 125 PRO A N   1 
ATOM   963  C CA  . PRO A 1 123 ? 5.615   7.172   -23.840 1.00 28.19 ? 125 PRO A CA  1 
ATOM   964  C C   . PRO A 1 123 ? 6.530   8.243   -23.259 1.00 27.75 ? 125 PRO A C   1 
ATOM   965  O O   . PRO A 1 123 ? 6.430   8.609   -22.088 1.00 24.90 ? 125 PRO A O   1 
ATOM   966  C CB  . PRO A 1 123 ? 4.170   7.673   -23.969 1.00 27.91 ? 125 PRO A CB  1 
ATOM   967  C CG  . PRO A 1 123 ? 3.380   6.914   -22.928 1.00 28.51 ? 125 PRO A CG  1 
ATOM   968  C CD  . PRO A 1 123 ? 4.093   5.623   -22.723 1.00 27.26 ? 125 PRO A CD  1 
ATOM   969  N N   . GLY A 1 124 ? 7.423   8.750   -24.106 1.00 27.26 ? 126 GLY A N   1 
ATOM   970  C CA  . GLY A 1 124 ? 8.406   9.738   -23.725 1.00 26.47 ? 126 GLY A CA  1 
ATOM   971  C C   . GLY A 1 124 ? 9.593   9.199   -22.962 1.00 32.18 ? 126 GLY A C   1 
ATOM   972  O O   . GLY A 1 124 ? 10.597  9.907   -22.840 1.00 32.46 ? 126 GLY A O   1 
ATOM   973  N N   . SER A 1 125 ? 9.529   7.963   -22.467 1.00 28.91 ? 127 SER A N   1 
ATOM   974  C CA  . SER A 1 125 ? 10.514  7.435   -21.529 1.00 25.81 ? 127 SER A CA  1 
ATOM   975  C C   . SER A 1 125 ? 11.721  6.793   -22.201 1.00 26.83 ? 127 SER A C   1 
ATOM   976  O O   . SER A 1 125 ? 12.702  6.498   -21.511 1.00 26.49 ? 127 SER A O   1 
ATOM   977  C CB  . SER A 1 125 ? 9.853   6.390   -20.629 1.00 22.38 ? 127 SER A CB  1 
ATOM   978  O OG  . SER A 1 125 ? 9.774   5.151   -21.316 1.00 24.43 ? 127 SER A OG  1 
ATOM   979  N N   . LYS A 1 126 ? 11.644  6.527   -23.508 1.00 25.55 ? 128 LYS A N   1 
ATOM   980  C CA  . LYS A 1 126 ? 12.644  5.827   -24.310 1.00 23.38 ? 128 LYS A CA  1 
ATOM   981  C C   . LYS A 1 126 ? 12.864  4.379   -23.890 1.00 22.43 ? 128 LYS A C   1 
ATOM   982  O O   . LYS A 1 126 ? 13.779  3.734   -24.407 1.00 25.20 ? 128 LYS A O   1 
ATOM   983  C CB  . LYS A 1 126 ? 13.980  6.572   -24.308 1.00 23.28 ? 128 LYS A CB  1 
ATOM   984  C CG  . LYS A 1 126 ? 13.947  7.912   -25.065 1.00 24.44 ? 128 LYS A CG  1 
ATOM   985  C CD  . LYS A 1 126 ? 15.335  8.556   -25.096 1.00 23.90 ? 128 LYS A CD  1 
ATOM   986  C CE  . LYS A 1 126 ? 15.379  9.777   -26.020 1.00 28.86 ? 128 LYS A CE  1 
ATOM   987  N NZ  . LYS A 1 126 ? 14.583  10.923  -25.488 1.00 26.06 ? 128 LYS A NZ  1 
ATOM   988  N N   . ASN A 1 127 ? 12.075  3.852   -22.953 1.00 21.66 ? 129 ASN A N   1 
ATOM   989  C CA  . ASN A 1 127 ? 12.137  2.425   -22.640 1.00 23.27 ? 129 ASN A CA  1 
ATOM   990  C C   . ASN A 1 127 ? 11.658  1.613   -23.837 1.00 23.76 ? 129 ASN A C   1 
ATOM   991  O O   . ASN A 1 127 ? 10.637  1.944   -24.448 1.00 23.60 ? 129 ASN A O   1 
ATOM   992  C CB  . ASN A 1 127 ? 11.256  2.100   -21.435 1.00 22.81 ? 129 ASN A CB  1 
ATOM   993  C CG  . ASN A 1 127 ? 11.921  2.431   -20.101 1.00 25.48 ? 129 ASN A CG  1 
ATOM   994  O OD1 . ASN A 1 127 ? 13.063  2.905   -20.051 1.00 24.03 ? 129 ASN A OD1 1 
ATOM   995  N ND2 . ASN A 1 127 ? 11.193  2.194   -19.010 1.00 21.29 ? 129 ASN A ND2 1 
ATOM   996  N N   . GLY A 1 128 ? 12.389  0.548   -24.168 1.00 27.83 ? 130 GLY A N   1 
ATOM   997  C CA  . GLY A 1 128 ? 11.938  -0.431  -25.144 1.00 24.98 ? 130 GLY A CA  1 
ATOM   998  C C   . GLY A 1 128 ? 10.894  -1.383  -24.579 1.00 24.39 ? 130 GLY A C   1 
ATOM   999  O O   . GLY A 1 128 ? 10.279  -1.123  -23.544 1.00 23.98 ? 130 GLY A O   1 
ATOM   1000 N N   . ASP A 1 129 ? 10.709  -2.522  -25.253 1.00 22.52 ? 131 ASP A N   1 
ATOM   1001 C CA  . ASP A 1 129 ? 9.592   -3.391  -24.908 1.00 21.15 ? 131 ASP A CA  1 
ATOM   1002 C C   . ASP A 1 129 ? 9.973   -4.301  -23.734 1.00 24.56 ? 131 ASP A C   1 
ATOM   1003 O O   . ASP A 1 129 ? 11.016  -4.138  -23.102 1.00 24.92 ? 131 ASP A O   1 
ATOM   1004 C CB  . ASP A 1 129 ? 9.109   -4.157  -26.136 1.00 20.22 ? 131 ASP A CB  1 
ATOM   1005 C CG  . ASP A 1 129 ? 10.172  -5.038  -26.747 1.00 26.70 ? 131 ASP A CG  1 
ATOM   1006 O OD1 . ASP A 1 129 ? 11.059  -5.549  -26.015 1.00 26.79 ? 131 ASP A OD1 1 
ATOM   1007 O OD2 . ASP A 1 129 ? 10.104  -5.242  -27.985 1.00 27.70 ? 131 ASP A OD2 1 
ATOM   1008 N N   . GLU A 1 130 ? 9.113   -5.275  -23.430 1.00 23.10 ? 132 GLU A N   1 
ATOM   1009 C CA  . GLU A 1 130 ? 9.297   -6.075  -22.229 1.00 26.29 ? 132 GLU A CA  1 
ATOM   1010 C C   . GLU A 1 130 ? 10.570  -6.907  -22.310 1.00 26.18 ? 132 GLU A C   1 
ATOM   1011 O O   . GLU A 1 130 ? 11.256  -7.100  -21.299 1.00 25.14 ? 132 GLU A O   1 
ATOM   1012 C CB  . GLU A 1 130 ? 8.069   -6.959  -22.008 1.00 24.87 ? 132 GLU A CB  1 
ATOM   1013 C CG  . GLU A 1 130 ? 8.122   -7.813  -20.744 1.00 22.53 ? 132 GLU A CG  1 
ATOM   1014 C CD  . GLU A 1 130 ? 6.864   -8.670  -20.531 1.00 25.99 ? 132 GLU A CD  1 
ATOM   1015 O OE1 . GLU A 1 130 ? 5.844   -8.516  -21.250 1.00 24.25 ? 132 GLU A OE1 1 
ATOM   1016 O OE2 . GLU A 1 130 ? 6.895   -9.505  -19.616 1.00 25.13 ? 132 GLU A OE2 1 
ATOM   1017 N N   . SER A 1 131 ? 10.925  -7.368  -23.498 1.00 24.82 ? 133 SER A N   1 
ATOM   1018 C CA  . SER A 1 131 ? 12.109  -8.192  -23.646 1.00 22.09 ? 133 SER A CA  1 
ATOM   1019 C C   . SER A 1 131 ? 13.401  -7.381  -23.663 1.00 24.17 ? 133 SER A C   1 
ATOM   1020 O O   . SER A 1 131 ? 14.487  -7.974  -23.633 1.00 23.28 ? 133 SER A O   1 
ATOM   1021 C CB  . SER A 1 131 ? 11.979  -9.011  -24.922 1.00 29.66 ? 133 SER A CB  1 
ATOM   1022 O OG  . SER A 1 131 ? 12.250  -8.177  -26.030 1.00 34.95 ? 133 SER A OG  1 
ATOM   1023 N N   . SER A 1 132 ? 13.318  -6.049  -23.706 1.00 22.68 ? 134 SER A N   1 
ATOM   1024 C CA  . SER A 1 132 ? 14.522  -5.232  -23.717 1.00 23.48 ? 134 SER A CA  1 
ATOM   1025 C C   . SER A 1 132 ? 15.185  -5.139  -22.342 1.00 26.48 ? 134 SER A C   1 
ATOM   1026 O O   . SER A 1 132 ? 16.359  -4.769  -22.262 1.00 24.08 ? 134 SER A O   1 
ATOM   1027 C CB  . SER A 1 132 ? 14.180  -3.814  -24.204 1.00 25.22 ? 134 SER A CB  1 
ATOM   1028 O OG  . SER A 1 132 ? 13.575  -3.117  -23.121 1.00 24.01 ? 134 SER A OG  1 
ATOM   1029 N N   . GLY A 1 133 ? 14.457  -5.432  -21.264 1.00 23.32 ? 135 GLY A N   1 
ATOM   1030 C CA  . GLY A 1 133 ? 14.936  -5.236  -19.906 1.00 21.39 ? 135 GLY A CA  1 
ATOM   1031 C C   . GLY A 1 133 ? 15.005  -3.797  -19.432 1.00 24.31 ? 135 GLY A C   1 
ATOM   1032 O O   . GLY A 1 133 ? 15.419  -3.560  -18.291 1.00 26.41 ? 135 GLY A O   1 
ATOM   1033 N N   . ASP A 1 134 ? 14.611  -2.828  -20.262 1.00 22.74 ? 136 ASP A N   1 
ATOM   1034 C CA  . ASP A 1 134 ? 14.672  -1.420  -19.863 1.00 21.82 ? 136 ASP A CA  1 
ATOM   1035 C C   . ASP A 1 134 ? 13.825  -1.129  -18.622 1.00 25.22 ? 136 ASP A C   1 
ATOM   1036 O O   . ASP A 1 134 ? 14.205  -0.300  -17.780 1.00 23.66 ? 136 ASP A O   1 
ATOM   1037 C CB  . ASP A 1 134 ? 14.194  -0.532  -21.008 1.00 23.50 ? 136 ASP A CB  1 
ATOM   1038 C CG  . ASP A 1 134 ? 15.220  -0.397  -22.109 1.00 27.74 ? 136 ASP A CG  1 
ATOM   1039 O OD1 . ASP A 1 134 ? 16.356  -0.879  -21.914 1.00 23.68 ? 136 ASP A OD1 1 
ATOM   1040 O OD2 . ASP A 1 134 ? 14.883  0.196   -23.160 1.00 24.35 ? 136 ASP A OD2 1 
ATOM   1041 N N   . GLY A 1 135 ? 12.654  -1.760  -18.518 1.00 21.38 ? 137 GLY A N   1 
ATOM   1042 C CA  . GLY A 1 135 ? 11.700  -1.376  -17.489 1.00 22.29 ? 137 GLY A CA  1 
ATOM   1043 C C   . GLY A 1 135 ? 12.238  -1.543  -16.077 1.00 24.62 ? 137 GLY A C   1 
ATOM   1044 O O   . GLY A 1 135 ? 12.131  -0.634  -15.249 1.00 23.20 ? 137 GLY A O   1 
ATOM   1045 N N   . TYR A 1 136 ? 12.796  -2.717  -15.772 1.00 22.61 ? 138 TYR A N   1 
ATOM   1046 C CA  . TYR A 1 136 ? 13.417  -2.908  -14.463 1.00 25.02 ? 138 TYR A CA  1 
ATOM   1047 C C   . TYR A 1 136 ? 14.754  -2.171  -14.371 1.00 25.70 ? 138 TYR A C   1 
ATOM   1048 O O   . TYR A 1 136 ? 15.066  -1.563  -13.338 1.00 25.11 ? 138 TYR A O   1 
ATOM   1049 C CB  . TYR A 1 136 ? 13.602  -4.400  -14.179 1.00 22.94 ? 138 TYR A CB  1 
ATOM   1050 C CG  . TYR A 1 136 ? 14.383  -4.707  -12.917 1.00 26.16 ? 138 TYR A CG  1 
ATOM   1051 C CD1 . TYR A 1 136 ? 13.765  -4.678  -11.675 1.00 26.73 ? 138 TYR A CD1 1 
ATOM   1052 C CD2 . TYR A 1 136 ? 15.741  -5.050  -12.968 1.00 28.98 ? 138 TYR A CD2 1 
ATOM   1053 C CE1 . TYR A 1 136 ? 14.474  -4.956  -10.505 1.00 28.52 ? 138 TYR A CE1 1 
ATOM   1054 C CE2 . TYR A 1 136 ? 16.456  -5.346  -11.811 1.00 27.59 ? 138 TYR A CE2 1 
ATOM   1055 C CZ  . TYR A 1 136 ? 15.815  -5.295  -10.583 1.00 31.86 ? 138 TYR A CZ  1 
ATOM   1056 O OH  . TYR A 1 136 ? 16.505  -5.574  -9.431  1.00 32.92 ? 138 TYR A OH  1 
ATOM   1057 N N   . LYS A 1 137 ? 15.547  -2.196  -15.448 1.00 23.69 ? 139 LYS A N   1 
ATOM   1058 C CA  . LYS A 1 137 ? 16.904  -1.660  -15.376 1.00 25.80 ? 139 LYS A CA  1 
ATOM   1059 C C   . LYS A 1 137 ? 16.896  -0.178  -15.004 1.00 26.31 ? 139 LYS A C   1 
ATOM   1060 O O   . LYS A 1 137 ? 17.727  0.266   -14.203 1.00 25.09 ? 139 LYS A O   1 
ATOM   1061 C CB  . LYS A 1 137 ? 17.636  -1.884  -16.705 1.00 26.38 ? 139 LYS A CB  1 
ATOM   1062 C CG  . LYS A 1 137 ? 19.014  -1.193  -16.788 1.00 26.09 ? 139 LYS A CG  1 
ATOM   1063 C CD  . LYS A 1 137 ? 19.852  -1.645  -17.991 1.00 24.44 ? 139 LYS A CD  1 
ATOM   1064 C CE  . LYS A 1 137 ? 21.103  -0.750  -18.137 1.00 33.57 ? 139 LYS A CE  1 
ATOM   1065 N NZ  . LYS A 1 137 ? 22.267  -1.378  -18.831 1.00 35.86 ? 139 LYS A NZ  1 
ATOM   1066 N N   . TYR A 1 138 ? 15.948  0.596   -15.550 1.00 22.63 ? 140 TYR A N   1 
ATOM   1067 C CA  . TYR A 1 138 ? 15.860  2.031   -15.296 1.00 25.07 ? 140 TYR A CA  1 
ATOM   1068 C C   . TYR A 1 138 ? 14.757  2.393   -14.301 1.00 25.94 ? 140 TYR A C   1 
ATOM   1069 O O   . TYR A 1 138 ? 14.216  3.504   -14.341 1.00 27.10 ? 140 TYR A O   1 
ATOM   1070 C CB  . TYR A 1 138 ? 15.675  2.782   -16.616 1.00 25.33 ? 140 TYR A CB  1 
ATOM   1071 C CG  . TYR A 1 138 ? 16.835  2.551   -17.541 1.00 24.59 ? 140 TYR A CG  1 
ATOM   1072 C CD1 . TYR A 1 138 ? 18.106  3.000   -17.194 1.00 23.24 ? 140 TYR A CD1 1 
ATOM   1073 C CD2 . TYR A 1 138 ? 16.680  1.845   -18.735 1.00 24.04 ? 140 TYR A CD2 1 
ATOM   1074 C CE1 . TYR A 1 138 ? 19.189  2.777   -18.006 1.00 26.25 ? 140 TYR A CE1 1 
ATOM   1075 C CE2 . TYR A 1 138 ? 17.773  1.607   -19.562 1.00 27.05 ? 140 TYR A CE2 1 
ATOM   1076 C CZ  . TYR A 1 138 ? 19.023  2.083   -19.186 1.00 28.30 ? 140 TYR A CZ  1 
ATOM   1077 O OH  . TYR A 1 138 ? 20.123  1.880   -19.972 1.00 33.19 ? 140 TYR A OH  1 
ATOM   1078 N N   . ARG A 1 139 ? 14.427  1.481   -13.393 1.00 26.00 ? 141 ARG A N   1 
ATOM   1079 C CA  . ARG A 1 139 ? 13.539  1.795   -12.283 1.00 23.57 ? 141 ARG A CA  1 
ATOM   1080 C C   . ARG A 1 139 ? 14.062  2.999   -11.487 1.00 26.83 ? 141 ARG A C   1 
ATOM   1081 O O   . ARG A 1 139 ? 15.232  3.387   -11.585 1.00 26.02 ? 141 ARG A O   1 
ATOM   1082 C CB  . ARG A 1 139 ? 13.399  0.575   -11.372 1.00 23.00 ? 141 ARG A CB  1 
ATOM   1083 C CG  . ARG A 1 139 ? 14.660  0.219   -10.583 1.00 21.33 ? 141 ARG A CG  1 
ATOM   1084 C CD  . ARG A 1 139 ? 14.544  -1.164  -9.957  1.00 27.51 ? 141 ARG A CD  1 
ATOM   1085 N NE  . ARG A 1 139 ? 15.760  -1.591  -9.258  1.00 25.88 ? 141 ARG A NE  1 
ATOM   1086 C CZ  . ARG A 1 139 ? 16.845  -2.066  -9.860  1.00 25.89 ? 141 ARG A CZ  1 
ATOM   1087 N NH1 . ARG A 1 139 ? 16.892  -2.182  -11.179 1.00 25.25 ? 141 ARG A NH1 1 
ATOM   1088 N NH2 . ARG A 1 139 ? 17.892  -2.422  -9.144  1.00 25.91 ? 141 ARG A NH2 1 
ATOM   1089 N N   . GLY A 1 140 ? 13.175  3.583   -10.679 1.00 26.56 ? 142 GLY A N   1 
ATOM   1090 C CA  . GLY A 1 140 ? 13.483  4.748   -9.870  1.00 27.54 ? 142 GLY A CA  1 
ATOM   1091 C C   . GLY A 1 140 ? 14.682  4.615   -8.949  1.00 27.82 ? 142 GLY A C   1 
ATOM   1092 O O   . GLY A 1 140 ? 14.822  3.626   -8.229  1.00 26.53 ? 142 GLY A O   1 
ATOM   1093 N N   . ARG A 1 141 ? 15.558  5.614   -8.958  1.00 28.16 ? 143 ARG A N   1 
ATOM   1094 C CA  . ARG A 1 141 ? 16.724  5.607   -8.090  1.00 26.87 ? 143 ARG A CA  1 
ATOM   1095 C C   . ARG A 1 141 ? 17.061  7.042   -7.718  1.00 27.78 ? 143 ARG A C   1 
ATOM   1096 O O   . ARG A 1 141 ? 16.786  7.966   -8.482  1.00 25.96 ? 143 ARG A O   1 
ATOM   1097 C CB  . ARG A 1 141 ? 17.944  4.963   -8.761  1.00 25.80 ? 143 ARG A CB  1 
ATOM   1098 C CG  . ARG A 1 141 ? 17.865  3.478   -9.107  1.00 26.25 ? 143 ARG A CG  1 
ATOM   1099 C CD  . ARG A 1 141 ? 19.252  3.082   -9.598  1.00 24.40 ? 143 ARG A CD  1 
ATOM   1100 N NE  . ARG A 1 141 ? 19.437  1.709   -10.054 1.00 22.69 ? 143 ARG A NE  1 
ATOM   1101 C CZ  . ARG A 1 141 ? 18.976  1.227   -11.207 1.00 25.93 ? 143 ARG A CZ  1 
ATOM   1102 N NH1 . ARG A 1 141 ? 18.233  1.981   -12.019 1.00 20.36 ? 143 ARG A NH1 1 
ATOM   1103 N NH2 . ARG A 1 141 ? 19.251  -0.026  -11.545 1.00 24.26 ? 143 ARG A NH2 1 
ATOM   1104 N N   . GLY A 1 142 ? 17.673  7.217   -6.539  1.00 30.22 ? 144 GLY A N   1 
ATOM   1105 C CA  . GLY A 1 142 ? 18.242  8.501   -6.167  1.00 27.18 ? 144 GLY A CA  1 
ATOM   1106 C C   . GLY A 1 142 ? 17.648  9.094   -4.911  1.00 30.24 ? 144 GLY A C   1 
ATOM   1107 O O   . GLY A 1 142 ? 17.171  8.365   -4.040  1.00 27.70 ? 144 GLY A O   1 
ATOM   1108 N N   . LEU A 1 143 ? 17.685  10.422  -4.797  1.00 32.94 ? 145 LEU A N   1 
ATOM   1109 C CA  . LEU A 1 143 ? 17.027  11.130  -3.702  1.00 27.18 ? 145 LEU A CA  1 
ATOM   1110 C C   . LEU A 1 143 ? 15.658  11.634  -4.146  1.00 30.92 ? 145 LEU A C   1 
ATOM   1111 O O   . LEU A 1 143 ? 14.635  11.247  -3.581  1.00 30.39 ? 145 LEU A O   1 
ATOM   1112 C CB  . LEU A 1 143 ? 17.904  12.287  -3.213  1.00 23.95 ? 145 LEU A CB  1 
ATOM   1113 C CG  . LEU A 1 143 ? 19.355  11.969  -2.822  1.00 29.17 ? 145 LEU A CG  1 
ATOM   1114 C CD1 . LEU A 1 143 ? 20.105  13.241  -2.472  1.00 25.62 ? 145 LEU A CD1 1 
ATOM   1115 C CD2 . LEU A 1 143 ? 19.423  10.997  -1.659  1.00 27.72 ? 145 LEU A CD2 1 
ATOM   1116 N N   . ILE A 1 144 ? 15.624  12.502  -5.152  1.00 29.81 ? 146 ILE A N   1 
ATOM   1117 C CA  . ILE A 1 144 ? 14.434  12.682  -5.973  1.00 29.55 ? 146 ILE A CA  1 
ATOM   1118 C C   . ILE A 1 144 ? 14.571  11.672  -7.102  1.00 29.08 ? 146 ILE A C   1 
ATOM   1119 O O   . ILE A 1 144 ? 15.466  11.783  -7.942  1.00 30.78 ? 146 ILE A O   1 
ATOM   1120 C CB  . ILE A 1 144 ? 14.312  14.114  -6.506  1.00 31.18 ? 146 ILE A CB  1 
ATOM   1121 C CG1 . ILE A 1 144 ? 14.251  15.108  -5.343  1.00 28.76 ? 146 ILE A CG1 1 
ATOM   1122 C CG2 . ILE A 1 144 ? 13.096  14.249  -7.450  1.00 26.86 ? 146 ILE A CG2 1 
ATOM   1123 C CD1 . ILE A 1 144 ? 14.429  16.555  -5.764  1.00 25.99 ? 146 ILE A CD1 1 
ATOM   1124 N N   . GLN A 1 145 ? 13.720  10.660  -7.101  1.00 28.40 ? 147 GLN A N   1 
ATOM   1125 C CA  . GLN A 1 145 ? 13.971  9.508   -7.948  1.00 30.51 ? 147 GLN A CA  1 
ATOM   1126 C C   . GLN A 1 145 ? 13.849  9.866   -9.422  1.00 31.87 ? 147 GLN A C   1 
ATOM   1127 O O   . GLN A 1 145 ? 12.969  10.626  -9.826  1.00 31.12 ? 147 GLN A O   1 
ATOM   1128 C CB  . GLN A 1 145 ? 13.009  8.395   -7.591  1.00 32.95 ? 147 GLN A CB  1 
ATOM   1129 C CG  . GLN A 1 145 ? 13.578  7.479   -6.522  1.00 37.03 ? 147 GLN A CG  1 
ATOM   1130 C CD  . GLN A 1 145 ? 12.568  6.470   -6.096  1.00 37.91 ? 147 GLN A CD  1 
ATOM   1131 O OE1 . GLN A 1 145 ? 11.456  6.818   -5.712  1.00 46.18 ? 147 GLN A OE1 1 
ATOM   1132 N NE2 . GLN A 1 145 ? 12.919  5.205   -6.213  1.00 39.33 ? 147 GLN A NE2 1 
ATOM   1133 N N   . ILE A 1 146 ? 14.759  9.338   -10.230 1.00 28.93 ? 148 ILE A N   1 
ATOM   1134 C CA  . ILE A 1 146 ? 14.647  9.459   -11.675 1.00 31.77 ? 148 ILE A CA  1 
ATOM   1135 C C   . ILE A 1 146 ? 14.455  8.060   -12.238 1.00 28.52 ? 148 ILE A C   1 
ATOM   1136 O O   . ILE A 1 146 ? 15.031  7.088   -11.732 1.00 31.02 ? 148 ILE A O   1 
ATOM   1137 C CB  . ILE A 1 146 ? 15.862  10.177  -12.303 1.00 34.55 ? 148 ILE A CB  1 
ATOM   1138 C CG1 . ILE A 1 146 ? 17.112  9.305   -12.249 1.00 27.77 ? 148 ILE A CG1 1 
ATOM   1139 C CG2 . ILE A 1 146 ? 16.118  11.505  -11.586 1.00 32.01 ? 148 ILE A CG2 1 
ATOM   1140 C CD1 . ILE A 1 146 ? 18.198  9.781   -13.201 1.00 26.97 ? 148 ILE A CD1 1 
ATOM   1141 N N   . THR A 1 147 ? 13.613  7.961   -13.258 1.00 24.81 ? 149 THR A N   1 
ATOM   1142 C CA  . THR A 1 147 ? 13.137  6.682   -13.755 1.00 28.30 ? 149 THR A CA  1 
ATOM   1143 C C   . THR A 1 147 ? 13.053  6.731   -15.270 1.00 26.36 ? 149 THR A C   1 
ATOM   1144 O O   . THR A 1 147 ? 12.769  7.782   -15.851 1.00 25.79 ? 149 THR A O   1 
ATOM   1145 C CB  . THR A 1 147 ? 11.752  6.325   -13.187 1.00 26.77 ? 149 THR A CB  1 
ATOM   1146 O OG1 . THR A 1 147 ? 11.680  6.726   -11.815 1.00 37.10 ? 149 THR A OG1 1 
ATOM   1147 C CG2 . THR A 1 147 ? 11.505  4.826   -13.272 1.00 28.07 ? 149 THR A CG2 1 
ATOM   1148 N N   . HIS A 1 148 ? 13.299  5.570   -15.888 1.00 25.97 ? 150 HIS A N   1 
ATOM   1149 C CA  . HIS A 1 148 ? 13.189  5.308   -17.320 1.00 26.17 ? 150 HIS A CA  1 
ATOM   1150 C C   . HIS A 1 148 ? 14.431  5.743   -18.078 1.00 25.52 ? 150 HIS A C   1 
ATOM   1151 O O   . HIS A 1 148 ? 15.175  6.608   -17.618 1.00 27.60 ? 150 HIS A O   1 
ATOM   1152 C CB  . HIS A 1 148 ? 11.949  5.971   -17.915 1.00 25.37 ? 150 HIS A CB  1 
ATOM   1153 C CG  . HIS A 1 148 ? 10.691  5.603   -17.204 1.00 26.09 ? 150 HIS A CG  1 
ATOM   1154 N ND1 . HIS A 1 148 ? 10.447  4.324   -16.751 1.00 25.62 ? 150 HIS A ND1 1 
ATOM   1155 C CD2 . HIS A 1 148 ? 9.613   6.344   -16.855 1.00 25.58 ? 150 HIS A CD2 1 
ATOM   1156 C CE1 . HIS A 1 148 ? 9.266   4.292   -16.158 1.00 28.81 ? 150 HIS A CE1 1 
ATOM   1157 N NE2 . HIS A 1 148 ? 8.739   5.504   -16.210 1.00 31.91 ? 150 HIS A NE2 1 
ATOM   1158 N N   . LYS A 1 149 ? 14.648  5.126   -19.244 1.00 24.93 ? 151 LYS A N   1 
ATOM   1159 C CA  . LYS A 1 149 ? 15.891  5.305   -19.977 1.00 23.62 ? 151 LYS A CA  1 
ATOM   1160 C C   . LYS A 1 149 ? 16.161  6.775   -20.273 1.00 25.39 ? 151 LYS A C   1 
ATOM   1161 O O   . LYS A 1 149 ? 17.301  7.238   -20.155 1.00 26.73 ? 151 LYS A O   1 
ATOM   1162 C CB  . LYS A 1 149 ? 15.838  4.489   -21.266 1.00 24.24 ? 151 LYS A CB  1 
ATOM   1163 C CG  . LYS A 1 149 ? 17.129  4.472   -22.058 1.00 23.38 ? 151 LYS A CG  1 
ATOM   1164 C CD  . LYS A 1 149 ? 16.944  3.622   -23.325 1.00 26.63 ? 151 LYS A CD  1 
ATOM   1165 C CE  . LYS A 1 149 ? 18.255  3.479   -24.112 1.00 29.39 ? 151 LYS A CE  1 
ATOM   1166 N NZ  . LYS A 1 149 ? 18.054  2.745   -25.402 1.00 32.01 ? 151 LYS A NZ  1 
ATOM   1167 N N   . ASP A 1 150 ? 15.123  7.531   -20.634 1.00 26.75 ? 152 ASP A N   1 
ATOM   1168 C CA  . ASP A 1 150 ? 15.323  8.926   -21.016 1.00 26.63 ? 152 ASP A CA  1 
ATOM   1169 C C   . ASP A 1 150 ? 15.976  9.735   -19.894 1.00 26.62 ? 152 ASP A C   1 
ATOM   1170 O O   . ASP A 1 150 ? 16.858  10.565  -20.150 1.00 24.31 ? 152 ASP A O   1 
ATOM   1171 C CB  . ASP A 1 150 ? 13.995  9.551   -21.415 1.00 28.13 ? 152 ASP A CB  1 
ATOM   1172 C CG  . ASP A 1 150 ? 14.116  11.036  -21.682 1.00 30.22 ? 152 ASP A CG  1 
ATOM   1173 O OD1 . ASP A 1 150 ? 14.680  11.411  -22.739 1.00 27.11 ? 152 ASP A OD1 1 
ATOM   1174 O OD2 . ASP A 1 150 ? 13.652  11.821  -20.831 1.00 29.68 ? 152 ASP A OD2 1 
ATOM   1175 N N   . ALA A 1 151 ? 15.574  9.492   -18.642 1.00 23.95 ? 153 ALA A N   1 
ATOM   1176 C CA  . ALA A 1 151 ? 16.167  10.227  -17.530 1.00 25.21 ? 153 ALA A CA  1 
ATOM   1177 C C   . ALA A 1 151 ? 17.633  9.854   -17.333 1.00 27.37 ? 153 ALA A C   1 
ATOM   1178 O O   . ALA A 1 151 ? 18.460  10.718  -17.025 1.00 28.57 ? 153 ALA A O   1 
ATOM   1179 C CB  . ALA A 1 151 ? 15.367  9.983   -16.256 1.00 24.89 ? 153 ALA A CB  1 
ATOM   1180 N N   . TYR A 1 152 ? 17.975  8.574   -17.516 1.00 24.76 ? 154 TYR A N   1 
ATOM   1181 C CA  . TYR A 1 152 ? 19.355  8.143   -17.331 1.00 22.14 ? 154 TYR A CA  1 
ATOM   1182 C C   . TYR A 1 152 ? 20.255  8.612   -18.475 1.00 25.03 ? 154 TYR A C   1 
ATOM   1183 O O   . TYR A 1 152 ? 21.444  8.866   -18.254 1.00 24.25 ? 154 TYR A O   1 
ATOM   1184 C CB  . TYR A 1 152 ? 19.402  6.621   -17.174 1.00 22.03 ? 154 TYR A CB  1 
ATOM   1185 C CG  . TYR A 1 152 ? 18.907  6.134   -15.817 1.00 25.89 ? 154 TYR A CG  1 
ATOM   1186 C CD1 . TYR A 1 152 ? 19.798  5.681   -14.848 1.00 21.14 ? 154 TYR A CD1 1 
ATOM   1187 C CD2 . TYR A 1 152 ? 17.542  6.136   -15.500 1.00 25.25 ? 154 TYR A CD2 1 
ATOM   1188 C CE1 . TYR A 1 152 ? 19.353  5.233   -13.611 1.00 20.49 ? 154 TYR A CE1 1 
ATOM   1189 C CE2 . TYR A 1 152 ? 17.087  5.704   -14.252 1.00 22.35 ? 154 TYR A CE2 1 
ATOM   1190 C CZ  . TYR A 1 152 ? 17.999  5.247   -13.314 1.00 24.17 ? 154 TYR A CZ  1 
ATOM   1191 O OH  . TYR A 1 152 ? 17.562  4.799   -12.075 1.00 24.73 ? 154 TYR A OH  1 
ATOM   1192 N N   . ILE A 1 153 ? 19.720  8.740   -19.696 1.00 26.54 ? 155 ILE A N   1 
ATOM   1193 C CA  . ILE A 1 153 ? 20.471  9.416   -20.756 1.00 27.26 ? 155 ILE A CA  1 
ATOM   1194 C C   . ILE A 1 153 ? 20.753  10.854  -20.352 1.00 27.53 ? 155 ILE A C   1 
ATOM   1195 O O   . ILE A 1 153 ? 21.902  11.312  -20.362 1.00 29.14 ? 155 ILE A O   1 
ATOM   1196 C CB  . ILE A 1 153 ? 19.718  9.377   -22.098 1.00 27.47 ? 155 ILE A CB  1 
ATOM   1197 C CG1 . ILE A 1 153 ? 19.644  7.971   -22.685 1.00 31.14 ? 155 ILE A CG1 1 
ATOM   1198 C CG2 . ILE A 1 153 ? 20.434  10.243  -23.108 1.00 30.30 ? 155 ILE A CG2 1 
ATOM   1199 C CD1 . ILE A 1 153 ? 18.639  7.865   -23.824 1.00 24.86 ? 155 ILE A CD1 1 
ATOM   1200 N N   . LYS A 1 154 ? 19.702  11.586  -19.992 1.00 25.29 ? 156 LYS A N   1 
ATOM   1201 C CA  . LYS A 1 154 ? 19.858  13.003  -19.713 1.00 23.48 ? 156 LYS A CA  1 
ATOM   1202 C C   . LYS A 1 154 ? 20.734  13.241  -18.483 1.00 27.00 ? 156 LYS A C   1 
ATOM   1203 O O   . LYS A 1 154 ? 21.505  14.209  -18.449 1.00 26.79 ? 156 LYS A O   1 
ATOM   1204 C CB  . LYS A 1 154 ? 18.477  13.646  -19.559 1.00 24.17 ? 156 LYS A CB  1 
ATOM   1205 C CG  . LYS A 1 154 ? 17.729  13.820  -20.869 1.00 25.18 ? 156 LYS A CG  1 
ATOM   1206 C CD  . LYS A 1 154 ? 16.265  14.284  -20.678 1.00 28.65 ? 156 LYS A CD  1 
ATOM   1207 C CE  . LYS A 1 154 ? 15.681  14.951  -21.963 1.00 26.94 ? 156 LYS A CE  1 
ATOM   1208 N NZ  . LYS A 1 154 ? 15.735  14.095  -23.219 1.00 26.40 ? 156 LYS A NZ  1 
ATOM   1209 N N   . PHE A 1 155 ? 20.664  12.361  -17.481 1.00 24.61 ? 157 PHE A N   1 
ATOM   1210 C CA  . PHE A 1 155 ? 21.531  12.527  -16.316 1.00 27.53 ? 157 PHE A CA  1 
ATOM   1211 C C   . PHE A 1 155 ? 22.998  12.320  -16.692 1.00 27.90 ? 157 PHE A C   1 
ATOM   1212 O O   . PHE A 1 155 ? 23.867  13.091  -16.271 1.00 28.14 ? 157 PHE A O   1 
ATOM   1213 C CB  . PHE A 1 155 ? 21.112  11.570  -15.187 1.00 25.34 ? 157 PHE A CB  1 
ATOM   1214 C CG  . PHE A 1 155 ? 22.027  11.616  -13.975 1.00 26.39 ? 157 PHE A CG  1 
ATOM   1215 C CD1 . PHE A 1 155 ? 22.506  12.835  -13.487 1.00 25.12 ? 157 PHE A CD1 1 
ATOM   1216 C CD2 . PHE A 1 155 ? 22.392  10.452  -13.314 1.00 24.34 ? 157 PHE A CD2 1 
ATOM   1217 C CE1 . PHE A 1 155 ? 23.351  12.879  -12.397 1.00 22.53 ? 157 PHE A CE1 1 
ATOM   1218 C CE2 . PHE A 1 155 ? 23.232  10.489  -12.196 1.00 23.79 ? 157 PHE A CE2 1 
ATOM   1219 C CZ  . PHE A 1 155 ? 23.708  11.709  -11.736 1.00 24.10 ? 157 PHE A CZ  1 
ATOM   1220 N N   . THR A 1 156 ? 23.288  11.291  -17.487 1.00 27.00 ? 158 THR A N   1 
ATOM   1221 C CA  . THR A 1 156 ? 24.652  11.081  -17.964 1.00 24.17 ? 158 THR A CA  1 
ATOM   1222 C C   . THR A 1 156 ? 25.214  12.351  -18.597 1.00 26.94 ? 158 THR A C   1 
ATOM   1223 O O   . THR A 1 156 ? 26.285  12.833  -18.212 1.00 28.80 ? 158 THR A O   1 
ATOM   1224 C CB  . THR A 1 156 ? 24.677  9.924   -18.964 1.00 22.33 ? 158 THR A CB  1 
ATOM   1225 O OG1 . THR A 1 156 ? 24.329  8.696   -18.300 1.00 24.93 ? 158 THR A OG1 1 
ATOM   1226 C CG2 . THR A 1 156 ? 26.038  9.803   -19.595 1.00 23.01 ? 158 THR A CG2 1 
ATOM   1227 N N   . GLU A 1 157 ? 24.490  12.920  -19.560 1.00 25.07 ? 159 GLU A N   1 
ATOM   1228 C CA  . GLU A 1 157 ? 24.981  14.114  -20.239 1.00 27.07 ? 159 GLU A CA  1 
ATOM   1229 C C   . GLU A 1 157 ? 25.058  15.307  -19.293 1.00 28.47 ? 159 GLU A C   1 
ATOM   1230 O O   . GLU A 1 157 ? 26.017  16.083  -19.353 1.00 28.59 ? 159 GLU A O   1 
ATOM   1231 C CB  . GLU A 1 157 ? 24.094  14.429  -21.446 1.00 27.79 ? 159 GLU A CB  1 
ATOM   1232 C CG  . GLU A 1 157 ? 24.185  13.359  -22.520 1.00 32.41 ? 159 GLU A CG  1 
ATOM   1233 C CD  . GLU A 1 157 ? 25.599  13.251  -23.068 1.00 33.39 ? 159 GLU A CD  1 
ATOM   1234 O OE1 . GLU A 1 157 ? 25.983  14.112  -23.882 1.00 29.10 ? 159 GLU A OE1 1 
ATOM   1235 O OE2 . GLU A 1 157 ? 26.332  12.323  -22.657 1.00 31.91 ? 159 GLU A OE2 1 
ATOM   1236 N N   . ALA A 1 158 ? 24.070  15.473  -18.409 1.00 23.93 ? 160 ALA A N   1 
ATOM   1237 C CA  . ALA A 1 158 ? 24.092  16.633  -17.523 1.00 29.20 ? 160 ALA A CA  1 
ATOM   1238 C C   . ALA A 1 158 ? 25.202  16.518  -16.489 1.00 28.06 ? 160 ALA A C   1 
ATOM   1239 O O   . ALA A 1 158 ? 25.891  17.507  -16.207 1.00 26.37 ? 160 ALA A O   1 
ATOM   1240 C CB  . ALA A 1 158 ? 22.743  16.822  -16.827 1.00 24.85 ? 160 ALA A CB  1 
ATOM   1241 N N   . HIS A 1 159 ? 25.387  15.329  -15.902 1.00 23.75 ? 161 HIS A N   1 
ATOM   1242 C CA  . HIS A 1 159 ? 26.434  15.189  -14.895 1.00 24.72 ? 161 HIS A CA  1 
ATOM   1243 C C   . HIS A 1 159 ? 27.816  15.382  -15.511 1.00 28.92 ? 161 HIS A C   1 
ATOM   1244 O O   . HIS A 1 159 ? 28.690  16.018  -14.912 1.00 27.42 ? 161 HIS A O   1 
ATOM   1245 C CB  . HIS A 1 159 ? 26.363  13.831  -14.200 1.00 25.32 ? 161 HIS A CB  1 
ATOM   1246 C CG  . HIS A 1 159 ? 27.608  13.501  -13.421 1.00 28.14 ? 161 HIS A CG  1 
ATOM   1247 N ND1 . HIS A 1 159 ? 27.741  13.775  -12.075 1.00 26.43 ? 161 HIS A ND1 1 
ATOM   1248 C CD2 . HIS A 1 159 ? 28.792  12.967  -13.813 1.00 24.45 ? 161 HIS A CD2 1 
ATOM   1249 C CE1 . HIS A 1 159 ? 28.941  13.404  -11.669 1.00 26.82 ? 161 HIS A CE1 1 
ATOM   1250 N NE2 . HIS A 1 159 ? 29.597  12.908  -12.704 1.00 26.38 ? 161 HIS A NE2 1 
ATOM   1251 N N   . ASN A 1 160 ? 28.032  14.844  -16.713 1.00 29.56 ? 162 ASN A N   1 
ATOM   1252 C CA  . ASN A 1 160 ? 29.334  15.002  -17.343 1.00 29.00 ? 162 ASN A CA  1 
ATOM   1253 C C   . ASN A 1 160 ? 29.592  16.447  -17.740 1.00 32.82 ? 162 ASN A C   1 
ATOM   1254 O O   . ASN A 1 160 ? 30.744  16.892  -17.682 1.00 29.69 ? 162 ASN A O   1 
ATOM   1255 C CB  . ASN A 1 160 ? 29.449  14.092  -18.554 1.00 24.87 ? 162 ASN A CB  1 
ATOM   1256 C CG  . ASN A 1 160 ? 29.554  12.648  -18.168 1.00 29.91 ? 162 ASN A CG  1 
ATOM   1257 O OD1 . ASN A 1 160 ? 29.909  12.316  -17.021 1.00 25.62 ? 162 ASN A OD1 1 
ATOM   1258 N ND2 . ASN A 1 160 ? 29.234  11.767  -19.112 1.00 26.25 ? 162 ASN A ND2 1 
ATOM   1259 N N   . ALA A 1 161 ? 28.540  17.190  -18.131 1.00 27.53 ? 163 ALA A N   1 
ATOM   1260 C CA  . ALA A 1 161 ? 28.710  18.591  -18.513 1.00 28.59 ? 163 ALA A CA  1 
ATOM   1261 C C   . ALA A 1 161 ? 29.105  19.450  -17.318 1.00 27.96 ? 163 ALA A C   1 
ATOM   1262 O O   . ALA A 1 161 ? 29.947  20.340  -17.444 1.00 33.56 ? 163 ALA A O   1 
ATOM   1263 C CB  . ALA A 1 161 ? 27.432  19.131  -19.148 1.00 24.92 ? 163 ALA A CB  1 
ATOM   1264 N N   . ALA A 1 162 ? 28.517  19.191  -16.150 1.00 28.62 ? 164 ALA A N   1 
ATOM   1265 C CA  . ALA A 1 162 ? 28.803  19.972  -14.955 1.00 27.16 ? 164 ALA A CA  1 
ATOM   1266 C C   . ALA A 1 162 ? 30.061  19.504  -14.246 1.00 27.08 ? 164 ALA A C   1 
ATOM   1267 O O   . ALA A 1 162 ? 30.677  20.283  -13.514 1.00 28.00 ? 164 ALA A O   1 
ATOM   1268 C CB  . ALA A 1 162 ? 27.619  19.894  -13.976 1.00 29.78 ? 164 ALA A CB  1 
ATOM   1269 N N   . ASN A 1 163 ? 30.438  18.239  -14.418 1.00 28.65 ? 165 ASN A N   1 
ATOM   1270 C CA  . ASN A 1 163 ? 31.582  17.650  -13.721 1.00 29.65 ? 165 ASN A CA  1 
ATOM   1271 C C   . ASN A 1 163 ? 32.507  16.971  -14.725 1.00 31.57 ? 165 ASN A C   1 
ATOM   1272 O O   . ASN A 1 163 ? 32.701  15.751  -14.685 1.00 28.12 ? 165 ASN A O   1 
ATOM   1273 C CB  . ASN A 1 163 ? 31.096  16.687  -12.638 1.00 24.38 ? 165 ASN A CB  1 
ATOM   1274 C CG  . ASN A 1 163 ? 30.071  17.345  -11.708 1.00 28.64 ? 165 ASN A CG  1 
ATOM   1275 O OD1 . ASN A 1 163 ? 30.433  17.987  -10.732 1.00 29.92 ? 165 ASN A OD1 1 
ATOM   1276 N ND2 . ASN A 1 163 ? 28.789  17.207  -12.033 1.00 26.78 ? 165 ASN A ND2 1 
ATOM   1277 N N   . PRO A 1 164 ? 33.116  17.744  -15.635 1.00 33.57 ? 166 PRO A N   1 
ATOM   1278 C CA  . PRO A 1 164 ? 33.922  17.128  -16.703 1.00 34.94 ? 166 PRO A CA  1 
ATOM   1279 C C   . PRO A 1 164 ? 35.106  16.326  -16.205 1.00 31.67 ? 166 PRO A C   1 
ATOM   1280 O O   . PRO A 1 164 ? 35.607  15.478  -16.950 1.00 32.16 ? 166 PRO A O   1 
ATOM   1281 C CB  . PRO A 1 164 ? 34.386  18.329  -17.540 1.00 30.25 ? 166 PRO A CB  1 
ATOM   1282 C CG  . PRO A 1 164 ? 34.237  19.504  -16.644 1.00 37.27 ? 166 PRO A CG  1 
ATOM   1283 C CD  . PRO A 1 164 ? 33.027  19.204  -15.804 1.00 32.25 ? 166 PRO A CD  1 
ATOM   1284 N N   . SER A 1 165 ? 35.569  16.558  -14.981 1.00 29.16 ? 167 SER A N   1 
ATOM   1285 C CA  . SER A 1 165 ? 36.676  15.773  -14.457 1.00 30.89 ? 167 SER A CA  1 
ATOM   1286 C C   . SER A 1 165 ? 36.237  14.431  -13.865 1.00 33.89 ? 167 SER A C   1 
ATOM   1287 O O   . SER A 1 165 ? 37.101  13.636  -13.482 1.00 32.14 ? 167 SER A O   1 
ATOM   1288 C CB  . SER A 1 165 ? 37.431  16.593  -13.405 1.00 32.24 ? 167 SER A CB  1 
ATOM   1289 O OG  . SER A 1 165 ? 36.952  16.275  -12.105 1.00 48.43 ? 167 SER A OG  1 
ATOM   1290 N N   . ASP A 1 166 ? 34.922  14.141  -13.793 1.00 30.36 ? 168 ASP A N   1 
ATOM   1291 C CA  . ASP A 1 166 ? 34.421  12.864  -13.264 1.00 30.43 ? 168 ASP A CA  1 
ATOM   1292 C C   . ASP A 1 166 ? 33.380  12.294  -14.236 1.00 33.31 ? 168 ASP A C   1 
ATOM   1293 O O   . ASP A 1 166 ? 32.184  12.259  -13.929 1.00 33.37 ? 168 ASP A O   1 
ATOM   1294 C CB  . ASP A 1 166 ? 33.841  13.041  -11.852 1.00 29.10 ? 168 ASP A CB  1 
ATOM   1295 C CG  . ASP A 1 166 ? 33.313  11.737  -11.258 1.00 32.37 ? 168 ASP A CG  1 
ATOM   1296 O OD1 . ASP A 1 166 ? 32.353  11.801  -10.459 1.00 29.13 ? 168 ASP A OD1 1 
ATOM   1297 O OD2 . ASP A 1 166 ? 33.837  10.655  -11.600 1.00 31.08 ? 168 ASP A OD2 1 
ATOM   1298 N N   . GLN A 1 167 ? 33.842  11.826  -15.400 1.00 29.09 ? 169 GLN A N   1 
ATOM   1299 C CA  . GLN A 1 167 ? 32.916  11.324  -16.408 1.00 29.83 ? 169 GLN A CA  1 
ATOM   1300 C C   . GLN A 1 167 ? 32.317  9.991   -15.983 1.00 27.67 ? 169 GLN A C   1 
ATOM   1301 O O   . GLN A 1 167 ? 33.023  9.103   -15.504 1.00 27.58 ? 169 GLN A O   1 
ATOM   1302 C CB  . GLN A 1 167 ? 33.602  11.162  -17.762 1.00 30.48 ? 169 GLN A CB  1 
ATOM   1303 C CG  . GLN A 1 167 ? 34.407  12.375  -18.213 1.00 36.88 ? 169 GLN A CG  1 
ATOM   1304 C CD  . GLN A 1 167 ? 33.654  13.181  -19.241 1.00 40.72 ? 169 GLN A CD  1 
ATOM   1305 O OE1 . GLN A 1 167 ? 32.833  12.641  -19.987 1.00 46.72 ? 169 GLN A OE1 1 
ATOM   1306 N NE2 . GLN A 1 167 ? 33.917  14.481  -19.284 1.00 40.59 ? 169 GLN A NE2 1 
ATOM   1307 N N   . LYS A 1 168 ? 31.010  9.845   -16.197 1.00 23.97 ? 170 LYS A N   1 
ATOM   1308 C CA  . LYS A 1 168 ? 30.276  8.638   -15.845 1.00 27.10 ? 170 LYS A CA  1 
ATOM   1309 C C   . LYS A 1 168 ? 29.391  8.216   -17.012 1.00 28.01 ? 170 LYS A C   1 
ATOM   1310 O O   . LYS A 1 168 ? 29.243  8.931   -18.005 1.00 25.80 ? 170 LYS A O   1 
ATOM   1311 C CB  . LYS A 1 168 ? 29.413  8.838   -14.586 1.00 24.12 ? 170 LYS A CB  1 
ATOM   1312 C CG  . LYS A 1 168 ? 30.202  8.968   -13.278 1.00 26.81 ? 170 LYS A CG  1 
ATOM   1313 C CD  . LYS A 1 168 ? 30.894  7.657   -12.902 1.00 27.90 ? 170 LYS A CD  1 
ATOM   1314 C CE  . LYS A 1 168 ? 29.906  6.627   -12.382 1.00 26.55 ? 170 LYS A CE  1 
ATOM   1315 N NZ  . LYS A 1 168 ? 30.405  5.236   -12.581 1.00 28.96 ? 170 LYS A NZ  1 
ATOM   1316 N N   . ASP A 1 169 ? 28.800  7.029   -16.880 1.00 28.58 ? 171 ASP A N   1 
ATOM   1317 C CA  . ASP A 1 169 ? 27.816  6.518   -17.840 1.00 27.62 ? 171 ASP A CA  1 
ATOM   1318 C C   . ASP A 1 169 ? 26.769  5.769   -17.023 1.00 24.48 ? 171 ASP A C   1 
ATOM   1319 O O   . ASP A 1 169 ? 26.982  4.610   -16.649 1.00 25.90 ? 171 ASP A O   1 
ATOM   1320 C CB  . ASP A 1 169 ? 28.461  5.618   -18.893 1.00 23.64 ? 171 ASP A CB  1 
ATOM   1321 C CG  . ASP A 1 169 ? 27.465  5.099   -19.934 1.00 25.01 ? 171 ASP A CG  1 
ATOM   1322 O OD1 . ASP A 1 169 ? 27.896  4.443   -20.892 1.00 25.77 ? 171 ASP A OD1 1 
ATOM   1323 O OD2 . ASP A 1 169 ? 26.257  5.340   -19.816 1.00 25.63 ? 171 ASP A OD2 1 
ATOM   1324 N N   . PHE A 1 170 ? 25.658  6.442   -16.723 1.00 23.06 ? 172 PHE A N   1 
ATOM   1325 C CA  . PHE A 1 170 ? 24.610  5.846   -15.900 1.00 26.18 ? 172 PHE A CA  1 
ATOM   1326 C C   . PHE A 1 170 ? 23.650  4.988   -16.714 1.00 25.51 ? 172 PHE A C   1 
ATOM   1327 O O   . PHE A 1 170 ? 22.790  4.322   -16.129 1.00 23.38 ? 172 PHE A O   1 
ATOM   1328 C CB  . PHE A 1 170 ? 23.863  6.936   -15.125 1.00 22.36 ? 172 PHE A CB  1 
ATOM   1329 C CG  . PHE A 1 170 ? 24.772  7.773   -14.277 1.00 22.22 ? 172 PHE A CG  1 
ATOM   1330 C CD1 . PHE A 1 170 ? 25.292  7.267   -13.111 1.00 19.91 ? 172 PHE A CD1 1 
ATOM   1331 C CD2 . PHE A 1 170 ? 25.163  9.037   -14.689 1.00 24.76 ? 172 PHE A CD2 1 
ATOM   1332 C CE1 . PHE A 1 170 ? 26.148  8.011   -12.347 1.00 24.20 ? 172 PHE A CE1 1 
ATOM   1333 C CE2 . PHE A 1 170 ? 26.019  9.788   -13.918 1.00 25.84 ? 172 PHE A CE2 1 
ATOM   1334 C CZ  . PHE A 1 170 ? 26.515  9.271   -12.747 1.00 22.09 ? 172 PHE A CZ  1 
ATOM   1335 N N   . LEU A 1 171 ? 23.800  4.956   -18.040 1.00 21.13 ? 173 LEU A N   1 
ATOM   1336 C CA  . LEU A 1 171 ? 23.232  3.842   -18.793 1.00 24.69 ? 173 LEU A CA  1 
ATOM   1337 C C   . LEU A 1 171 ? 23.993  2.557   -18.491 1.00 26.89 ? 173 LEU A C   1 
ATOM   1338 O O   . LEU A 1 171 ? 23.385  1.509   -18.260 1.00 29.94 ? 173 LEU A O   1 
ATOM   1339 C CB  . LEU A 1 171 ? 23.259  4.136   -20.296 1.00 25.96 ? 173 LEU A CB  1 
ATOM   1340 C CG  . LEU A 1 171 ? 22.584  5.425   -20.774 1.00 25.46 ? 173 LEU A CG  1 
ATOM   1341 C CD1 . LEU A 1 171 ? 22.814  5.610   -22.259 1.00 25.86 ? 173 LEU A CD1 1 
ATOM   1342 C CD2 . LEU A 1 171 ? 21.095  5.404   -20.456 1.00 25.83 ? 173 LEU A CD2 1 
ATOM   1343 N N   . ALA A 1 172 ? 25.329  2.625   -18.462 1.00 25.95 ? 174 ALA A N   1 
ATOM   1344 C CA  . ALA A 1 172 ? 26.103  1.430   -18.145 1.00 29.31 ? 174 ALA A CA  1 
ATOM   1345 C C   . ALA A 1 172 ? 26.035  1.108   -16.660 1.00 25.67 ? 174 ALA A C   1 
ATOM   1346 O O   . ALA A 1 172 ? 26.019  -0.064  -16.284 1.00 24.65 ? 174 ALA A O   1 
ATOM   1347 C CB  . ALA A 1 172 ? 27.565  1.589   -18.588 1.00 27.26 ? 174 ALA A CB  1 
ATOM   1348 N N   . SER A 1 173 ? 25.965  2.123   -15.801 1.00 23.89 ? 175 SER A N   1 
ATOM   1349 C CA  . SER A 1 173 ? 26.079  1.915   -14.356 1.00 24.82 ? 175 SER A CA  1 
ATOM   1350 C C   . SER A 1 173 ? 24.944  2.619   -13.616 1.00 25.53 ? 175 SER A C   1 
ATOM   1351 O O   . SER A 1 173 ? 25.182  3.519   -12.810 1.00 24.67 ? 175 SER A O   1 
ATOM   1352 C CB  . SER A 1 173 ? 27.446  2.395   -13.868 1.00 22.75 ? 175 SER A CB  1 
ATOM   1353 O OG  . SER A 1 173 ? 27.833  1.694   -12.694 1.00 31.65 ? 175 SER A OG  1 
ATOM   1354 N N   . PRO A 1 174 ? 23.686  2.212   -13.850 1.00 25.38 ? 176 PRO A N   1 
ATOM   1355 C CA  . PRO A 1 174 ? 22.561  2.943   -13.235 1.00 22.31 ? 176 PRO A CA  1 
ATOM   1356 C C   . PRO A 1 174 ? 22.541  2.854   -11.718 1.00 25.01 ? 176 PRO A C   1 
ATOM   1357 O O   . PRO A 1 174 ? 22.117  3.809   -11.053 1.00 25.86 ? 176 PRO A O   1 
ATOM   1358 C CB  . PRO A 1 174 ? 21.320  2.289   -13.870 1.00 21.14 ? 176 PRO A CB  1 
ATOM   1359 C CG  . PRO A 1 174 ? 21.767  0.941   -14.292 1.00 22.04 ? 176 PRO A CG  1 
ATOM   1360 C CD  . PRO A 1 174 ? 23.231  1.062   -14.654 1.00 23.82 ? 176 PRO A CD  1 
ATOM   1361 N N   . ASP A 1 175 ? 23.028  1.749   -11.151 1.00 23.91 ? 177 ASP A N   1 
ATOM   1362 C CA  . ASP A 1 175 ? 23.086  1.572   -9.703  1.00 24.99 ? 177 ASP A CA  1 
ATOM   1363 C C   . ASP A 1 175 ? 24.027  2.558   -9.007  1.00 27.01 ? 177 ASP A C   1 
ATOM   1364 O O   . ASP A 1 175 ? 23.980  2.667   -7.779  1.00 24.04 ? 177 ASP A O   1 
ATOM   1365 C CB  . ASP A 1 175 ? 23.505  0.135   -9.382  1.00 23.01 ? 177 ASP A CB  1 
ATOM   1366 C CG  . ASP A 1 175 ? 22.351  -0.839  -9.495  1.00 27.62 ? 177 ASP A CG  1 
ATOM   1367 O OD1 . ASP A 1 175 ? 21.183  -0.382  -9.449  1.00 29.59 ? 177 ASP A OD1 1 
ATOM   1368 O OD2 . ASP A 1 175 ? 22.601  -2.056  -9.628  1.00 31.08 ? 177 ASP A OD2 1 
ATOM   1369 N N   . ASP A 1 176 ? 24.865  3.286   -9.747  1.00 24.20 ? 178 ASP A N   1 
ATOM   1370 C CA  . ASP A 1 176 ? 25.670  4.316   -9.114  1.00 25.50 ? 178 ASP A CA  1 
ATOM   1371 C C   . ASP A 1 176 ? 24.826  5.451   -8.552  1.00 26.30 ? 178 ASP A C   1 
ATOM   1372 O O   . ASP A 1 176 ? 25.262  6.141   -7.624  1.00 27.88 ? 178 ASP A O   1 
ATOM   1373 C CB  . ASP A 1 176 ? 26.688  4.852   -10.110 1.00 26.52 ? 178 ASP A CB  1 
ATOM   1374 C CG  . ASP A 1 176 ? 27.969  4.074   -10.071 1.00 29.11 ? 178 ASP A CG  1 
ATOM   1375 O OD1 . ASP A 1 176 ? 28.346  3.639   -8.961  1.00 31.37 ? 178 ASP A OD1 1 
ATOM   1376 O OD2 . ASP A 1 176 ? 28.584  3.872   -11.139 1.00 30.14 ? 178 ASP A OD2 1 
ATOM   1377 N N   . ILE A 1 177 ? 23.625  5.658   -9.085  1.00 24.36 ? 179 ILE A N   1 
ATOM   1378 C CA  . ILE A 1 177 ? 22.711  6.619   -8.506  1.00 24.40 ? 179 ILE A CA  1 
ATOM   1379 C C   . ILE A 1 177 ? 22.288  6.229   -7.095  1.00 26.53 ? 179 ILE A C   1 
ATOM   1380 O O   . ILE A 1 177 ? 21.741  7.057   -6.373  1.00 27.80 ? 179 ILE A O   1 
ATOM   1381 C CB  . ILE A 1 177 ? 21.511  6.781   -9.459  1.00 25.70 ? 179 ILE A CB  1 
ATOM   1382 C CG1 . ILE A 1 177 ? 22.019  7.155   -10.854 1.00 24.45 ? 179 ILE A CG1 1 
ATOM   1383 C CG2 . ILE A 1 177 ? 20.521  7.807   -8.945  1.00 24.22 ? 179 ILE A CG2 1 
ATOM   1384 C CD1 . ILE A 1 177 ? 20.922  7.580   -11.798 1.00 26.37 ? 179 ILE A CD1 1 
ATOM   1385 N N   . LEU A 1 178 ? 22.547  4.990   -6.671  1.00 25.67 ? 180 LEU A N   1 
ATOM   1386 C CA  . LEU A 1 178 ? 22.323  4.616   -5.279  1.00 25.45 ? 180 LEU A CA  1 
ATOM   1387 C C   . LEU A 1 178 ? 23.495  4.959   -4.362  1.00 24.94 ? 180 LEU A C   1 
ATOM   1388 O O   . LEU A 1 178 ? 23.356  4.824   -3.149  1.00 29.93 ? 180 LEU A O   1 
ATOM   1389 C CB  . LEU A 1 178 ? 22.003  3.123   -5.169  1.00 25.92 ? 180 LEU A CB  1 
ATOM   1390 C CG  . LEU A 1 178 ? 20.706  2.784   -5.912  1.00 29.05 ? 180 LEU A CG  1 
ATOM   1391 C CD1 . LEU A 1 178 ? 20.406  1.311   -5.859  1.00 27.76 ? 180 LEU A CD1 1 
ATOM   1392 C CD2 . LEU A 1 178 ? 19.561  3.585   -5.309  1.00 32.35 ? 180 LEU A CD2 1 
ATOM   1393 N N   . THR A 1 179 ? 24.633  5.401   -4.888  1.00 24.15 ? 181 THR A N   1 
ATOM   1394 C CA  . THR A 1 179 ? 25.666  5.961   -4.027  1.00 26.29 ? 181 THR A CA  1 
ATOM   1395 C C   . THR A 1 179 ? 25.287  7.381   -3.628  1.00 28.94 ? 181 THR A C   1 
ATOM   1396 O O   . THR A 1 179 ? 24.563  8.075   -4.352  1.00 27.85 ? 181 THR A O   1 
ATOM   1397 C CB  . THR A 1 179 ? 27.035  5.992   -4.720  1.00 28.61 ? 181 THR A CB  1 
ATOM   1398 O OG1 . THR A 1 179 ? 26.997  6.913   -5.817  1.00 24.17 ? 181 THR A OG1 1 
ATOM   1399 C CG2 . THR A 1 179 ? 27.439  4.618   -5.221  1.00 23.29 ? 181 THR A CG2 1 
ATOM   1400 N N   . LEU A 1 180 ? 25.794  7.814   -2.465  1.00 26.13 ? 182 LEU A N   1 
ATOM   1401 C CA  . LEU A 1 180 ? 25.503  9.158   -1.984  1.00 24.29 ? 182 LEU A CA  1 
ATOM   1402 C C   . LEU A 1 180 ? 25.984  10.196  -2.975  1.00 25.89 ? 182 LEU A C   1 
ATOM   1403 O O   . LEU A 1 180 ? 25.311  11.211  -3.206  1.00 25.82 ? 182 LEU A O   1 
ATOM   1404 C CB  . LEU A 1 180 ? 26.172  9.401   -0.631  1.00 27.83 ? 182 LEU A CB  1 
ATOM   1405 C CG  . LEU A 1 180 ? 25.461  8.937   0.636   1.00 32.52 ? 182 LEU A CG  1 
ATOM   1406 C CD1 . LEU A 1 180 ? 26.238  9.409   1.871   1.00 24.06 ? 182 LEU A CD1 1 
ATOM   1407 C CD2 . LEU A 1 180 ? 24.019  9.438   0.658   1.00 23.05 ? 182 LEU A CD2 1 
ATOM   1408 N N   . ARG A 1 181 ? 27.154  9.957   -3.572  1.00 26.42 ? 183 ARG A N   1 
ATOM   1409 C CA  . ARG A 1 181 ? 27.719  10.918  -4.512  1.00 28.82 ? 183 ARG A CA  1 
ATOM   1410 C C   . ARG A 1 181 ? 26.785  11.144  -5.700  1.00 25.36 ? 183 ARG A C   1 
ATOM   1411 O O   . ARG A 1 181 ? 26.363  12.276  -5.971  1.00 26.29 ? 183 ARG A O   1 
ATOM   1412 C CB  . ARG A 1 181 ? 29.108  10.452  -4.977  1.00 24.44 ? 183 ARG A CB  1 
ATOM   1413 C CG  . ARG A 1 181 ? 29.672  11.301  -6.099  1.00 22.53 ? 183 ARG A CG  1 
ATOM   1414 C CD  . ARG A 1 181 ? 31.086  10.905  -6.515  1.00 28.51 ? 183 ARG A CD  1 
ATOM   1415 N NE  . ARG A 1 181 ? 32.110  11.250  -5.528  1.00 24.87 ? 183 ARG A NE  1 
ATOM   1416 C CZ  . ARG A 1 181 ? 32.502  12.491  -5.268  1.00 29.86 ? 183 ARG A CZ  1 
ATOM   1417 N NH1 . ARG A 1 181 ? 31.950  13.517  -5.908  1.00 30.49 ? 183 ARG A NH1 1 
ATOM   1418 N NH2 . ARG A 1 181 ? 33.438  12.704  -4.359  1.00 36.96 ? 183 ARG A NH2 1 
ATOM   1419 N N   . TYR A 1 182 ? 26.431  10.077  -6.418  1.00 25.49 ? 184 TYR A N   1 
ATOM   1420 C CA  . TYR A 1 182 ? 25.652  10.292  -7.642  1.00 24.17 ? 184 TYR A CA  1 
ATOM   1421 C C   . TYR A 1 182 ? 24.150  10.407  -7.382  1.00 24.33 ? 184 TYR A C   1 
ATOM   1422 O O   . TYR A 1 182 ? 23.445  10.998  -8.201  1.00 25.32 ? 184 TYR A O   1 
ATOM   1423 C CB  . TYR A 1 182 ? 25.985  9.200   -8.666  1.00 21.84 ? 184 TYR A CB  1 
ATOM   1424 C CG  . TYR A 1 182 ? 27.468  9.236   -8.977  1.00 24.61 ? 184 TYR A CG  1 
ATOM   1425 C CD1 . TYR A 1 182 ? 28.014  10.306  -9.668  1.00 24.05 ? 184 TYR A CD1 1 
ATOM   1426 C CD2 . TYR A 1 182 ? 28.335  8.253   -8.507  1.00 24.34 ? 184 TYR A CD2 1 
ATOM   1427 C CE1 . TYR A 1 182 ? 29.383  10.382  -9.928  1.00 26.90 ? 184 TYR A CE1 1 
ATOM   1428 C CE2 . TYR A 1 182 ? 29.713  8.320   -8.766  1.00 24.47 ? 184 TYR A CE2 1 
ATOM   1429 C CZ  . TYR A 1 182 ? 30.225  9.388   -9.474  1.00 25.27 ? 184 TYR A CZ  1 
ATOM   1430 O OH  . TYR A 1 182 ? 31.575  9.477   -9.720  1.00 28.29 ? 184 TYR A OH  1 
ATOM   1431 N N   . ALA A 1 183 ? 23.642  9.906   -6.251  1.00 24.99 ? 185 ALA A N   1 
ATOM   1432 C CA  . ALA A 1 183 ? 22.294  10.309  -5.853  1.00 25.67 ? 185 ALA A CA  1 
ATOM   1433 C C   . ALA A 1 183 ? 22.211  11.824  -5.702  1.00 24.10 ? 185 ALA A C   1 
ATOM   1434 O O   . ALA A 1 183 ? 21.225  12.441  -6.112  1.00 26.65 ? 185 ALA A O   1 
ATOM   1435 C CB  . ALA A 1 183 ? 21.880  9.622   -4.548  1.00 22.42 ? 185 ALA A CB  1 
ATOM   1436 N N   . THR A 1 184 ? 23.249  12.444  -5.133  1.00 25.85 ? 186 THR A N   1 
ATOM   1437 C CA  . THR A 1 184 ? 23.218  13.891  -4.923  1.00 25.77 ? 186 THR A CA  1 
ATOM   1438 C C   . THR A 1 184 ? 23.381  14.640  -6.232  1.00 26.04 ? 186 THR A C   1 
ATOM   1439 O O   . THR A 1 184 ? 22.679  15.626  -6.478  1.00 26.28 ? 186 THR A O   1 
ATOM   1440 C CB  . THR A 1 184 ? 24.305  14.335  -3.955  1.00 24.23 ? 186 THR A CB  1 
ATOM   1441 O OG1 . THR A 1 184 ? 24.175  13.631  -2.721  1.00 26.00 ? 186 THR A OG1 1 
ATOM   1442 C CG2 . THR A 1 184 ? 24.162  15.852  -3.705  1.00 29.05 ? 186 THR A CG2 1 
ATOM   1443 N N   . SER A 1 185 ? 24.334  14.204  -7.070  1.00 24.26 ? 187 SER A N   1 
ATOM   1444 C CA  . SER A 1 185 ? 24.456  14.773  -8.408  1.00 24.89 ? 187 SER A CA  1 
ATOM   1445 C C   . SER A 1 185 ? 23.132  14.702  -9.145  1.00 25.20 ? 187 SER A C   1 
ATOM   1446 O O   . SER A 1 185 ? 22.712  15.681  -9.769  1.00 25.56 ? 187 SER A O   1 
ATOM   1447 C CB  . SER A 1 185 ? 25.557  14.064  -9.206  1.00 24.34 ? 187 SER A CB  1 
ATOM   1448 O OG  . SER A 1 185 ? 25.733  14.658  -10.489 1.00 21.43 ? 187 SER A OG  1 
ATOM   1449 N N   . SER A 1 186 ? 22.441  13.562  -9.049  1.00 23.78 ? 188 SER A N   1 
ATOM   1450 C CA  . SER A 1 186 ? 21.185  13.409  -9.774  1.00 25.91 ? 188 SER A CA  1 
ATOM   1451 C C   . SER A 1 186 ? 20.108  14.346  -9.243  1.00 26.71 ? 188 SER A C   1 
ATOM   1452 O O   . SER A 1 186 ? 19.248  14.797  -10.009 1.00 26.58 ? 188 SER A O   1 
ATOM   1453 C CB  . SER A 1 186 ? 20.702  11.954  -9.718  1.00 28.93 ? 188 SER A CB  1 
ATOM   1454 O OG  . SER A 1 186 ? 20.123  11.640  -8.462  1.00 29.65 ? 188 SER A OG  1 
ATOM   1455 N N   . ALA A 1 187 ? 20.128  14.638  -7.946  1.00 23.89 ? 189 ALA A N   1 
ATOM   1456 C CA  . ALA A 1 187 ? 19.156  15.571  -7.395  1.00 26.58 ? 189 ALA A CA  1 
ATOM   1457 C C   . ALA A 1 187 ? 19.328  16.948  -8.019  1.00 26.74 ? 189 ALA A C   1 
ATOM   1458 O O   . ALA A 1 187 ? 18.356  17.570  -8.460  1.00 25.97 ? 189 ALA A O   1 
ATOM   1459 C CB  . ALA A 1 187 ? 19.297  15.633  -5.873  1.00 22.94 ? 189 ALA A CB  1 
ATOM   1460 N N   . TYR A 1 188 ? 20.575  17.416  -8.099  1.00 24.99 ? 190 TYR A N   1 
ATOM   1461 C CA  . TYR A 1 188 ? 20.856  18.693  -8.734  1.00 27.52 ? 190 TYR A CA  1 
ATOM   1462 C C   . TYR A 1 188 ? 20.527  18.659  -10.212 1.00 27.59 ? 190 TYR A C   1 
ATOM   1463 O O   . TYR A 1 188 ? 20.098  19.674  -10.770 1.00 24.34 ? 190 TYR A O   1 
ATOM   1464 C CB  . TYR A 1 188 ? 22.320  19.076  -8.527  1.00 27.37 ? 190 TYR A CB  1 
ATOM   1465 C CG  . TYR A 1 188 ? 22.609  19.616  -7.143  1.00 27.56 ? 190 TYR A CG  1 
ATOM   1466 C CD1 . TYR A 1 188 ? 22.205  20.896  -6.775  1.00 26.13 ? 190 TYR A CD1 1 
ATOM   1467 C CD2 . TYR A 1 188 ? 23.262  18.846  -6.200  1.00 26.10 ? 190 TYR A CD2 1 
ATOM   1468 C CE1 . TYR A 1 188 ? 22.461  21.393  -5.515  1.00 24.97 ? 190 TYR A CE1 1 
ATOM   1469 C CE2 . TYR A 1 188 ? 23.536  19.345  -4.931  1.00 28.39 ? 190 TYR A CE2 1 
ATOM   1470 C CZ  . TYR A 1 188 ? 23.128  20.615  -4.594  1.00 30.08 ? 190 TYR A CZ  1 
ATOM   1471 O OH  . TYR A 1 188 ? 23.400  21.100  -3.331  1.00 28.76 ? 190 TYR A OH  1 
ATOM   1472 N N   . PHE A 1 189 ? 20.706  17.505  -10.859 1.00 25.85 ? 191 PHE A N   1 
ATOM   1473 C CA  . PHE A 1 189 ? 20.352  17.408  -12.273 1.00 27.90 ? 191 PHE A CA  1 
ATOM   1474 C C   . PHE A 1 189 ? 18.848  17.542  -12.456 1.00 27.40 ? 191 PHE A C   1 
ATOM   1475 O O   . PHE A 1 189 ? 18.378  18.264  -13.346 1.00 25.77 ? 191 PHE A O   1 
ATOM   1476 C CB  . PHE A 1 189 ? 20.842  16.086  -12.860 1.00 21.91 ? 191 PHE A CB  1 
ATOM   1477 C CG  . PHE A 1 189 ? 19.920  15.515  -13.903 1.00 22.95 ? 191 PHE A CG  1 
ATOM   1478 C CD1 . PHE A 1 189 ? 19.865  16.065  -15.180 1.00 26.44 ? 191 PHE A CD1 1 
ATOM   1479 C CD2 . PHE A 1 189 ? 19.099  14.442  -13.609 1.00 23.43 ? 191 PHE A CD2 1 
ATOM   1480 C CE1 . PHE A 1 189 ? 19.005  15.544  -16.154 1.00 28.58 ? 191 PHE A CE1 1 
ATOM   1481 C CE2 . PHE A 1 189 ? 18.246  13.920  -14.573 1.00 27.80 ? 191 PHE A CE2 1 
ATOM   1482 C CZ  . PHE A 1 189 ? 18.201  14.467  -15.849 1.00 22.80 ? 191 PHE A CZ  1 
ATOM   1483 N N   . PHE A 1 190 ? 18.081  16.824  -11.634 1.00 25.34 ? 192 PHE A N   1 
ATOM   1484 C CA  . PHE A 1 190 ? 16.634  16.997  -11.608 1.00 29.57 ? 192 PHE A CA  1 
ATOM   1485 C C   . PHE A 1 190 ? 16.267  18.476  -11.484 1.00 29.43 ? 192 PHE A C   1 
ATOM   1486 O O   . PHE A 1 190 ? 15.526  19.021  -12.311 1.00 30.91 ? 192 PHE A O   1 
ATOM   1487 C CB  . PHE A 1 190 ? 16.058  16.190  -10.441 1.00 26.76 ? 192 PHE A CB  1 
ATOM   1488 C CG  . PHE A 1 190 ? 14.567  16.185  -10.383 1.00 28.44 ? 192 PHE A CG  1 
ATOM   1489 C CD1 . PHE A 1 190 ? 13.840  15.225  -11.073 1.00 28.27 ? 192 PHE A CD1 1 
ATOM   1490 C CD2 . PHE A 1 190 ? 13.885  17.132  -9.628  1.00 27.96 ? 192 PHE A CD2 1 
ATOM   1491 C CE1 . PHE A 1 190 ? 12.441  15.208  -11.012 1.00 29.06 ? 192 PHE A CE1 1 
ATOM   1492 C CE2 . PHE A 1 190 ? 12.489  17.127  -9.558  1.00 28.53 ? 192 PHE A CE2 1 
ATOM   1493 C CZ  . PHE A 1 190 ? 11.768  16.157  -10.249 1.00 30.02 ? 192 PHE A CZ  1 
ATOM   1494 N N   . TRP A 1 191 ? 16.828  19.140  -10.469 1.00 27.86 ? 193 TRP A N   1 
ATOM   1495 C CA  . TRP A 1 191 ? 16.505  20.529  -10.151 1.00 29.00 ? 193 TRP A CA  1 
ATOM   1496 C C   . TRP A 1 191 ? 16.753  21.452  -11.333 1.00 29.75 ? 193 TRP A C   1 
ATOM   1497 O O   . TRP A 1 191 ? 15.852  22.179  -11.770 1.00 27.38 ? 193 TRP A O   1 
ATOM   1498 C CB  . TRP A 1 191 ? 17.352  20.982  -8.971  1.00 27.72 ? 193 TRP A CB  1 
ATOM   1499 C CG  . TRP A 1 191 ? 16.978  22.309  -8.465  1.00 33.89 ? 193 TRP A CG  1 
ATOM   1500 C CD1 . TRP A 1 191 ? 17.583  23.504  -8.743  1.00 31.29 ? 193 TRP A CD1 1 
ATOM   1501 C CD2 . TRP A 1 191 ? 15.910  22.596  -7.554  1.00 34.07 ? 193 TRP A CD2 1 
ATOM   1502 N NE1 . TRP A 1 191 ? 16.954  24.518  -8.058  1.00 32.88 ? 193 TRP A NE1 1 
ATOM   1503 C CE2 . TRP A 1 191 ? 15.920  23.986  -7.326  1.00 34.99 ? 193 TRP A CE2 1 
ATOM   1504 C CE3 . TRP A 1 191 ? 14.948  21.807  -6.908  1.00 30.50 ? 193 TRP A CE3 1 
ATOM   1505 C CZ2 . TRP A 1 191 ? 14.998  24.608  -6.483  1.00 37.62 ? 193 TRP A CZ2 1 
ATOM   1506 C CZ3 . TRP A 1 191 ? 14.031  22.424  -6.066  1.00 34.02 ? 193 TRP A CZ3 1 
ATOM   1507 C CH2 . TRP A 1 191 ? 14.062  23.813  -5.862  1.00 36.74 ? 193 TRP A CH2 1 
ATOM   1508 N N   . PHE A 1 192 ? 17.982  21.434  -11.858 1.00 28.73 ? 194 PHE A N   1 
ATOM   1509 C CA  . PHE A 1 192 ? 18.456  22.430  -12.812 1.00 34.71 ? 194 PHE A CA  1 
ATOM   1510 C C   . PHE A 1 192 ? 18.211  22.064  -14.265 1.00 31.89 ? 194 PHE A C   1 
ATOM   1511 O O   . PHE A 1 192 ? 18.019  22.963  -15.093 1.00 34.93 ? 194 PHE A O   1 
ATOM   1512 C CB  . PHE A 1 192 ? 19.953  22.655  -12.618 1.00 29.83 ? 194 PHE A CB  1 
ATOM   1513 C CG  . PHE A 1 192 ? 20.276  23.535  -11.472 1.00 29.61 ? 194 PHE A CG  1 
ATOM   1514 C CD1 . PHE A 1 192 ? 19.929  24.879  -11.501 1.00 29.46 ? 194 PHE A CD1 1 
ATOM   1515 C CD2 . PHE A 1 192 ? 20.923  23.029  -10.355 1.00 27.94 ? 194 PHE A CD2 1 
ATOM   1516 C CE1 . PHE A 1 192 ? 20.226  25.717  -10.435 1.00 31.82 ? 194 PHE A CE1 1 
ATOM   1517 C CE2 . PHE A 1 192 ? 21.233  23.866  -9.281  1.00 35.06 ? 194 PHE A CE2 1 
ATOM   1518 C CZ  . PHE A 1 192 ? 20.877  25.214  -9.322  1.00 31.44 ? 194 PHE A CZ  1 
ATOM   1519 N N   . ILE A 1 193 ? 18.228  20.777  -14.601 1.00 32.12 ? 195 ILE A N   1 
ATOM   1520 C CA  . ILE A 1 193 ? 18.211  20.327  -15.992 1.00 29.99 ? 195 ILE A CA  1 
ATOM   1521 C C   . ILE A 1 193 ? 16.920  19.611  -16.325 1.00 31.24 ? 195 ILE A C   1 
ATOM   1522 O O   . ILE A 1 193 ? 16.186  20.022  -17.226 1.00 37.10 ? 195 ILE A O   1 
ATOM   1523 C CB  . ILE A 1 193 ? 19.432  19.434  -16.311 1.00 28.85 ? 195 ILE A CB  1 
ATOM   1524 C CG1 . ILE A 1 193 ? 20.742  20.104  -15.889 1.00 31.60 ? 195 ILE A CG1 1 
ATOM   1525 C CG2 . ILE A 1 193 ? 19.405  19.047  -17.789 1.00 25.10 ? 195 ILE A CG2 1 
ATOM   1526 C CD1 . ILE A 1 193 ? 20.991  21.430  -16.552 1.00 34.42 ? 195 ILE A CD1 1 
ATOM   1527 N N   . TYR A 1 194 ? 16.647  18.495  -15.648 1.00 31.70 ? 196 TYR A N   1 
ATOM   1528 C CA  . TYR A 1 194 ? 15.485  17.687  -15.985 1.00 31.29 ? 196 TYR A CA  1 
ATOM   1529 C C   . TYR A 1 194 ? 14.205  18.516  -16.017 1.00 34.70 ? 196 TYR A C   1 
ATOM   1530 O O   . TYR A 1 194 ? 13.359  18.317  -16.893 1.00 38.95 ? 196 TYR A O   1 
ATOM   1531 C CB  . TYR A 1 194 ? 15.351  16.541  -14.996 1.00 31.74 ? 196 TYR A CB  1 
ATOM   1532 C CG  . TYR A 1 194 ? 14.460  15.440  -15.481 1.00 31.20 ? 196 TYR A CG  1 
ATOM   1533 C CD1 . TYR A 1 194 ? 14.654  14.868  -16.725 1.00 28.11 ? 196 TYR A CD1 1 
ATOM   1534 C CD2 . TYR A 1 194 ? 13.433  14.954  -14.685 1.00 36.71 ? 196 TYR A CD2 1 
ATOM   1535 C CE1 . TYR A 1 194 ? 13.842  13.846  -17.175 1.00 31.50 ? 196 TYR A CE1 1 
ATOM   1536 C CE2 . TYR A 1 194 ? 12.617  13.919  -15.121 1.00 33.67 ? 196 TYR A CE2 1 
ATOM   1537 C CZ  . TYR A 1 194 ? 12.832  13.373  -16.363 1.00 36.30 ? 196 TYR A CZ  1 
ATOM   1538 O OH  . TYR A 1 194 ? 12.027  12.357  -16.804 1.00 44.40 ? 196 TYR A OH  1 
ATOM   1539 N N   . LYS A 1 195 ? 14.048  19.454  -15.081 1.00 32.92 ? 197 LYS A N   1 
ATOM   1540 C CA  . LYS A 1 195 ? 12.843  20.272  -15.001 1.00 33.66 ? 197 LYS A CA  1 
ATOM   1541 C C   . LYS A 1 195 ? 13.079  21.712  -15.444 1.00 32.70 ? 197 LYS A C   1 
ATOM   1542 O O   . LYS A 1 195 ? 12.331  22.610  -15.041 1.00 34.71 ? 197 LYS A O   1 
ATOM   1543 C CB  . LYS A 1 195 ? 12.267  20.245  -13.584 1.00 31.66 ? 197 LYS A CB  1 
ATOM   1544 C CG  . LYS A 1 195 ? 11.769  18.881  -13.181 1.00 37.09 ? 197 LYS A CG  1 
ATOM   1545 C CD  . LYS A 1 195 ? 10.462  18.552  -13.868 1.00 36.79 ? 197 LYS A CD  1 
ATOM   1546 C CE  . LYS A 1 195 ? 10.070  17.122  -13.558 1.00 37.40 ? 197 LYS A CE  1 
ATOM   1547 N NZ  . LYS A 1 195 ? 8.829   16.731  -14.248 1.00 40.51 ? 197 LYS A NZ  1 
ATOM   1548 N N   . LYS A 1 196 ? 14.095  21.951  -16.270 1.00 34.97 ? 198 LYS A N   1 
ATOM   1549 C CA  . LYS A 1 196 ? 14.390  23.316  -16.699 1.00 40.49 ? 198 LYS A CA  1 
ATOM   1550 C C   . LYS A 1 196 ? 13.218  23.915  -17.462 1.00 36.64 ? 198 LYS A C   1 
ATOM   1551 O O   . LYS A 1 196 ? 12.910  25.100  -17.307 1.00 41.06 ? 198 LYS A O   1 
ATOM   1552 C CB  . LYS A 1 196 ? 15.668  23.338  -17.547 1.00 39.25 ? 198 LYS A CB  1 
ATOM   1553 C CG  . LYS A 1 196 ? 16.143  24.717  -18.010 1.00 49.42 ? 198 LYS A CG  1 
ATOM   1554 C CD  . LYS A 1 196 ? 17.451  24.665  -18.810 1.00 56.84 ? 198 LYS A CD  1 
ATOM   1555 C CE  . LYS A 1 196 ? 17.881  26.056  -19.277 1.00 57.72 ? 198 LYS A CE  1 
ATOM   1556 N NZ  . LYS A 1 196 ? 19.154  26.034  -20.060 1.00 63.14 ? 198 LYS A NZ  1 
ATOM   1557 N N   . SER A 1 197 ? 12.532  23.102  -18.262 1.00 36.91 ? 199 SER A N   1 
ATOM   1558 C CA  . SER A 1 197 ? 11.429  23.615  -19.063 1.00 38.19 ? 199 SER A CA  1 
ATOM   1559 C C   . SER A 1 197 ? 10.239  24.034  -18.210 1.00 40.15 ? 199 SER A C   1 
ATOM   1560 O O   . SER A 1 197 ? 9.328   24.684  -18.730 1.00 40.60 ? 199 SER A O   1 
ATOM   1561 C CB  . SER A 1 197 ? 10.987  22.575  -20.093 1.00 40.82 ? 199 SER A CB  1 
ATOM   1562 O OG  . SER A 1 197 ? 10.591  21.369  -19.469 1.00 50.61 ? 199 SER A OG  1 
ATOM   1563 N N   . PHE A 1 198 ? 10.213  23.668  -16.923 1.00 42.90 ? 200 PHE A N   1 
ATOM   1564 C CA  . PHE A 1 198 ? 9.213   24.169  -15.984 1.00 36.96 ? 200 PHE A CA  1 
ATOM   1565 C C   . PHE A 1 198 ? 9.738   25.305  -15.123 1.00 38.90 ? 200 PHE A C   1 
ATOM   1566 O O   . PHE A 1 198 ? 9.012   25.786  -14.250 1.00 43.29 ? 200 PHE A O   1 
ATOM   1567 C CB  . PHE A 1 198 ? 8.711   23.046  -15.070 1.00 38.65 ? 200 PHE A CB  1 
ATOM   1568 C CG  . PHE A 1 198 ? 8.034   21.919  -15.800 1.00 39.76 ? 200 PHE A CG  1 
ATOM   1569 C CD1 . PHE A 1 198 ? 6.700   21.996  -16.144 1.00 42.55 ? 200 PHE A CD1 1 
ATOM   1570 C CD2 . PHE A 1 198 ? 8.741   20.789  -16.151 1.00 40.54 ? 200 PHE A CD2 1 
ATOM   1571 C CE1 . PHE A 1 198 ? 6.084   20.967  -16.817 1.00 40.58 ? 200 PHE A CE1 1 
ATOM   1572 C CE2 . PHE A 1 198 ? 8.133   19.754  -16.827 1.00 43.23 ? 200 PHE A CE2 1 
ATOM   1573 C CZ  . PHE A 1 198 ? 6.805   19.844  -17.161 1.00 46.16 ? 200 PHE A CZ  1 
ATOM   1574 N N   . ASN A 1 199 ? 10.980  25.729  -15.334 1.00 37.11 ? 201 ASN A N   1 
ATOM   1575 C CA  . ASN A 1 199 ? 11.591  26.808  -14.566 1.00 40.74 ? 201 ASN A CA  1 
ATOM   1576 C C   . ASN A 1 199 ? 11.533  26.527  -13.072 1.00 40.60 ? 201 ASN A C   1 
ATOM   1577 O O   . ASN A 1 199 ? 11.190  27.393  -12.267 1.00 42.52 ? 201 ASN A O   1 
ATOM   1578 C CB  . ASN A 1 199 ? 10.944  28.150  -14.887 1.00 42.89 ? 201 ASN A CB  1 
ATOM   1579 C CG  . ASN A 1 199 ? 11.589  28.816  -16.063 1.00 49.60 ? 201 ASN A CG  1 
ATOM   1580 O OD1 . ASN A 1 199 ? 12.766  29.203  -16.013 1.00 59.30 ? 201 ASN A OD1 1 
ATOM   1581 N ND2 . ASN A 1 199 ? 10.837  28.947  -17.140 1.00 42.54 ? 201 ASN A ND2 1 
ATOM   1582 N N   . LEU A 1 200 ? 11.890  25.295  -12.704 1.00 38.91 ? 202 LEU A N   1 
ATOM   1583 C CA  . LEU A 1 200 ? 11.877  24.911  -11.296 1.00 38.12 ? 202 LEU A CA  1 
ATOM   1584 C C   . LEU A 1 200 ? 12.756  25.840  -10.465 1.00 37.15 ? 202 LEU A C   1 
ATOM   1585 O O   . LEU A 1 200 ? 12.329  26.353  -9.425  1.00 37.68 ? 202 LEU A O   1 
ATOM   1586 C CB  . LEU A 1 200 ? 12.324  23.453  -11.150 1.00 33.97 ? 202 LEU A CB  1 
ATOM   1587 C CG  . LEU A 1 200 ? 12.317  22.878  -9.736  1.00 35.34 ? 202 LEU A CG  1 
ATOM   1588 C CD1 . LEU A 1 200 ? 10.961  23.103  -9.078  1.00 35.06 ? 202 LEU A CD1 1 
ATOM   1589 C CD2 . LEU A 1 200 ? 12.673  21.390  -9.744  1.00 32.01 ? 202 LEU A CD2 1 
ATOM   1590 N N   . HIS A 1 201 ? 13.988  26.076  -10.914 1.00 35.65 ? 203 HIS A N   1 
ATOM   1591 C CA  . HIS A 1 201 ? 14.901  26.911  -10.139 1.00 36.86 ? 203 HIS A CA  1 
ATOM   1592 C C   . HIS A 1 201 ? 14.356  28.325  -9.995  1.00 40.29 ? 203 HIS A C   1 
ATOM   1593 O O   . HIS A 1 201 ? 14.381  28.902  -8.904  1.00 44.39 ? 203 HIS A O   1 
ATOM   1594 C CB  . HIS A 1 201 ? 16.287  26.927  -10.792 1.00 37.51 ? 203 HIS A CB  1 
ATOM   1595 C CG  . HIS A 1 201 ? 17.332  27.626  -9.980  1.00 41.76 ? 203 HIS A CG  1 
ATOM   1596 N ND1 . HIS A 1 201 ? 17.713  27.200  -8.724  1.00 39.13 ? 203 HIS A ND1 1 
ATOM   1597 C CD2 . HIS A 1 201 ? 18.078  28.726  -10.246 1.00 42.74 ? 203 HIS A CD2 1 
ATOM   1598 C CE1 . HIS A 1 201 ? 18.654  28.001  -8.256  1.00 40.60 ? 203 HIS A CE1 1 
ATOM   1599 N NE2 . HIS A 1 201 ? 18.896  28.934  -9.161  1.00 45.17 ? 203 HIS A NE2 1 
ATOM   1600 N N   . SER A 1 202 ? 13.860  28.903  -11.088 1.00 42.09 ? 204 SER A N   1 
ATOM   1601 C CA  . SER A 1 202 ? 13.284  30.239  -11.014 1.00 44.46 ? 204 SER A CA  1 
ATOM   1602 C C   . SER A 1 202 ? 12.117  30.266  -10.049 1.00 43.47 ? 204 SER A C   1 
ATOM   1603 O O   . SER A 1 202 ? 12.009  31.164  -9.209  1.00 45.32 ? 204 SER A O   1 
ATOM   1604 C CB  . SER A 1 202 ? 12.824  30.696  -12.395 1.00 42.65 ? 204 SER A CB  1 
ATOM   1605 O OG  . SER A 1 202 ? 13.923  31.145  -13.160 1.00 54.59 ? 204 SER A OG  1 
ATOM   1606 N N   . THR A 1 203 ? 11.229  29.285  -10.160 1.00 43.93 ? 205 THR A N   1 
ATOM   1607 C CA  . THR A 1 203 ? 10.061  29.259  -9.299  1.00 42.13 ? 205 THR A CA  1 
ATOM   1608 C C   . THR A 1 203 ? 10.459  29.163  -7.834  1.00 43.08 ? 205 THR A C   1 
ATOM   1609 O O   . THR A 1 203 ? 9.831   29.785  -6.977  1.00 48.30 ? 205 THR A O   1 
ATOM   1610 C CB  . THR A 1 203 ? 9.159   28.108  -9.714  1.00 39.36 ? 205 THR A CB  1 
ATOM   1611 O OG1 . THR A 1 203 ? 8.826   28.277  -11.095 1.00 38.15 ? 205 THR A OG1 1 
ATOM   1612 C CG2 . THR A 1 203 ? 7.882   28.095  -8.882  1.00 39.27 ? 205 THR A CG2 1 
ATOM   1613 N N   . ALA A 1 204 ? 11.522  28.420  -7.527  1.00 41.98 ? 206 ALA A N   1 
ATOM   1614 C CA  . ALA A 1 204 ? 11.977  28.355  -6.142  1.00 43.30 ? 206 ALA A CA  1 
ATOM   1615 C C   . ALA A 1 204 ? 12.521  29.694  -5.668  1.00 45.60 ? 206 ALA A C   1 
ATOM   1616 O O   . ALA A 1 204 ? 12.481  29.996  -4.469  1.00 44.08 ? 206 ALA A O   1 
ATOM   1617 C CB  . ALA A 1 204 ? 13.045  27.273  -5.986  1.00 36.81 ? 206 ALA A CB  1 
ATOM   1618 N N   . CYS A 1 205 ? 13.042  30.504  -6.592  1.00 46.73 ? 207 CYS A N   1 
ATOM   1619 C CA  . CYS A 1 205 ? 13.695  31.749  -6.207  1.00 46.60 ? 207 CYS A CA  1 
ATOM   1620 C C   . CYS A 1 205 ? 12.687  32.793  -5.735  1.00 43.55 ? 207 CYS A C   1 
ATOM   1621 O O   . CYS A 1 205 ? 12.946  33.517  -4.767  1.00 42.10 ? 207 CYS A O   1 
ATOM   1622 C CB  . CYS A 1 205 ? 14.526  32.279  -7.377  1.00 46.82 ? 207 CYS A CB  1 
ATOM   1623 S SG  . CYS A 1 205 ? 16.223  31.623  -7.428  1.00 48.77 ? 207 CYS A SG  1 
ATOM   1624 N N   . THR A 1 206 ? 11.531  32.878  -6.389  1.00 43.65 ? 208 THR A N   1 
ATOM   1625 C CA  . THR A 1 206 ? 10.551  33.900  -6.050  1.00 50.55 ? 208 THR A CA  1 
ATOM   1626 C C   . THR A 1 206 ? 9.149   33.341  -5.854  1.00 53.24 ? 208 THR A C   1 
ATOM   1627 O O   . THR A 1 206 ? 8.190   34.120  -5.778  1.00 53.28 ? 208 THR A O   1 
ATOM   1628 C CB  . THR A 1 206 ? 10.509  34.981  -7.129  1.00 48.43 ? 208 THR A CB  1 
ATOM   1629 O OG1 . THR A 1 206 ? 10.387  34.360  -8.416  1.00 48.58 ? 208 THR A OG1 1 
ATOM   1630 C CG2 . THR A 1 206 ? 11.776  35.831  -7.077  1.00 49.84 ? 208 THR A CG2 1 
ATOM   1631 N N   . GLY A 1 207 ? 8.993   32.022  -5.764  1.00 49.18 ? 209 GLY A N   1 
ATOM   1632 C CA  . GLY A 1 207 ? 7.695   31.411  -5.739  1.00 43.06 ? 209 GLY A CA  1 
ATOM   1633 C C   . GLY A 1 207 ? 7.357   30.782  -4.406  1.00 42.39 ? 209 GLY A C   1 
ATOM   1634 O O   . GLY A 1 207 ? 7.973   31.059  -3.369  1.00 38.82 ? 209 GLY A O   1 
ATOM   1635 N N   . THR A 1 208 ? 6.393   29.887  -4.446  1.00 43.60 ? 210 THR A N   1 
ATOM   1636 C CA  . THR A 1 208 ? 5.716   29.330  -3.293  1.00 40.47 ? 210 THR A CA  1 
ATOM   1637 C C   . THR A 1 208 ? 6.124   27.868  -3.103  1.00 41.46 ? 210 THR A C   1 
ATOM   1638 O O   . THR A 1 208 ? 6.552   27.203  -4.053  1.00 37.67 ? 210 THR A O   1 
ATOM   1639 C CB  . THR A 1 208 ? 4.210   29.501  -3.543  1.00 38.78 ? 210 THR A CB  1 
ATOM   1640 O OG1 . THR A 1 208 ? 3.825   30.831  -3.199  1.00 50.83 ? 210 THR A OG1 1 
ATOM   1641 C CG2 . THR A 1 208 ? 3.372   28.566  -2.805  1.00 49.55 ? 210 THR A CG2 1 
ATOM   1642 N N   . VAL A 1 209 ? 6.020   27.366  -1.866  1.00 39.60 ? 211 VAL A N   1 
ATOM   1643 C CA  . VAL A 1 209 ? 6.305   25.949  -1.645  1.00 35.03 ? 211 VAL A CA  1 
ATOM   1644 C C   . VAL A 1 209 ? 5.351   25.099  -2.465  1.00 35.24 ? 211 VAL A C   1 
ATOM   1645 O O   . VAL A 1 209 ? 5.745   24.092  -3.069  1.00 36.37 ? 211 VAL A O   1 
ATOM   1646 C CB  . VAL A 1 209 ? 6.234   25.598  -0.148  1.00 38.65 ? 211 VAL A CB  1 
ATOM   1647 C CG1 . VAL A 1 209 ? 6.321   24.087  0.036   1.00 36.65 ? 211 VAL A CG1 1 
ATOM   1648 C CG2 . VAL A 1 209 ? 7.342   26.307  0.614   1.00 34.39 ? 211 VAL A CG2 1 
ATOM   1649 N N   . LYS A 1 210 ? 4.089   25.517  -2.530  1.00 37.24 ? 212 LYS A N   1 
ATOM   1650 C CA  . LYS A 1 210 ? 3.093   24.828  -3.341  1.00 34.60 ? 212 LYS A CA  1 
ATOM   1651 C C   . LYS A 1 210 ? 3.490   24.795  -4.814  1.00 35.29 ? 212 LYS A C   1 
ATOM   1652 O O   . LYS A 1 210 ? 3.348   23.757  -5.476  1.00 33.16 ? 212 LYS A O   1 
ATOM   1653 C CB  . LYS A 1 210 ? 1.731   25.505  -3.161  1.00 34.92 ? 212 LYS A CB  1 
ATOM   1654 C CG  . LYS A 1 210 ? 0.526   24.691  -3.595  1.00 43.76 ? 212 LYS A CG  1 
ATOM   1655 C CD  . LYS A 1 210 ? -0.790  25.400  -3.252  1.00 50.14 ? 212 LYS A CD  1 
ATOM   1656 C CE  . LYS A 1 210 ? -1.955  24.800  -4.038  1.00 50.01 ? 212 LYS A CE  1 
ATOM   1657 N NZ  . LYS A 1 210 ? -3.098  24.371  -3.167  1.00 53.34 ? 212 LYS A NZ  1 
ATOM   1658 N N   . GLU A 1 211 ? 3.973   25.920  -5.352  1.00 34.00 ? 213 GLU A N   1 
ATOM   1659 C CA  . GLU A 1 211 ? 4.354   25.942  -6.765  1.00 39.05 ? 213 GLU A CA  1 
ATOM   1660 C C   . GLU A 1 211 ? 5.588   25.076  -7.017  1.00 35.06 ? 213 GLU A C   1 
ATOM   1661 O O   . GLU A 1 211 ? 5.651   24.343  -8.005  1.00 38.22 ? 213 GLU A O   1 
ATOM   1662 C CB  . GLU A 1 211 ? 4.588   27.380  -7.246  1.00 34.72 ? 213 GLU A CB  1 
ATOM   1663 C CG  . GLU A 1 211 ? 3.537   28.376  -6.794  1.00 47.50 ? 213 GLU A CG  1 
ATOM   1664 C CD  . GLU A 1 211 ? 3.921   29.826  -7.091  1.00 49.56 ? 213 GLU A CD  1 
ATOM   1665 O OE1 . GLU A 1 211 ? 3.169   30.501  -7.819  1.00 53.54 ? 213 GLU A OE1 1 
ATOM   1666 O OE2 . GLU A 1 211 ? 4.974   30.289  -6.610  1.00 48.73 ? 213 GLU A OE2 1 
ATOM   1667 N N   . VAL A 1 212 ? 6.588   25.156  -6.140  1.00 31.23 ? 214 VAL A N   1 
ATOM   1668 C CA  . VAL A 1 212 ? 7.732   24.254  -6.245  1.00 33.02 ? 214 VAL A CA  1 
ATOM   1669 C C   . VAL A 1 212 ? 7.268   22.807  -6.179  1.00 37.23 ? 214 VAL A C   1 
ATOM   1670 O O   . VAL A 1 212 ? 7.713   21.955  -6.961  1.00 36.62 ? 214 VAL A O   1 
ATOM   1671 C CB  . VAL A 1 212 ? 8.764   24.562  -5.148  1.00 31.36 ? 214 VAL A CB  1 
ATOM   1672 C CG1 . VAL A 1 212 ? 9.920   23.567  -5.247  1.00 31.80 ? 214 VAL A CG1 1 
ATOM   1673 C CG2 . VAL A 1 212 ? 9.249   26.010  -5.273  1.00 34.17 ? 214 VAL A CG2 1 
ATOM   1674 N N   . THR A 1 213 ? 6.357   22.509  -5.248  1.00 33.70 ? 215 THR A N   1 
ATOM   1675 C CA  . THR A 1 213 ? 5.867   21.146  -5.085  1.00 31.24 ? 215 THR A CA  1 
ATOM   1676 C C   . THR A 1 213 ? 5.181   20.653  -6.349  1.00 37.71 ? 215 THR A C   1 
ATOM   1677 O O   . THR A 1 213 ? 5.405   19.512  -6.776  1.00 38.80 ? 215 THR A O   1 
ATOM   1678 C CB  . THR A 1 213 ? 4.919   21.075  -3.884  1.00 33.81 ? 215 THR A CB  1 
ATOM   1679 O OG1 . THR A 1 213 ? 5.578   21.580  -2.714  1.00 30.00 ? 215 THR A OG1 1 
ATOM   1680 C CG2 . THR A 1 213 ? 4.453   19.649  -3.631  1.00 30.71 ? 215 THR A CG2 1 
ATOM   1681 N N   . LYS A 1 214 ? 4.360   21.506  -6.981  1.00 38.63 ? 216 LYS A N   1 
ATOM   1682 C CA  . LYS A 1 214 ? 3.663   21.100  -8.202  1.00 40.62 ? 216 LYS A CA  1 
ATOM   1683 C C   . LYS A 1 214 ? 4.638   20.626  -9.273  1.00 34.63 ? 216 LYS A C   1 
ATOM   1684 O O   . LYS A 1 214 ? 4.393   19.617  -9.941  1.00 35.12 ? 216 LYS A O   1 
ATOM   1685 C CB  . LYS A 1 214 ? 2.798   22.246  -8.735  1.00 41.31 ? 216 LYS A CB  1 
ATOM   1686 C CG  . LYS A 1 214 ? 2.002   21.903  -9.999  1.00 40.69 ? 216 LYS A CG  1 
ATOM   1687 C CD  . LYS A 1 214 ? 1.009   20.773  -9.757  1.00 46.84 ? 216 LYS A CD  1 
ATOM   1688 C CE  . LYS A 1 214 ? -0.225  20.874  -10.656 1.00 47.34 ? 216 LYS A CE  1 
ATOM   1689 N NZ  . LYS A 1 214 ? -0.119  20.056  -11.897 1.00 53.04 ? 216 LYS A NZ  1 
ATOM   1690 N N   . ILE A 1 215 ? 5.759   21.325  -9.440  1.00 37.93 ? 217 ILE A N   1 
ATOM   1691 C CA  . ILE A 1 215 ? 6.731   20.925  -10.455 1.00 37.65 ? 217 ILE A CA  1 
ATOM   1692 C C   . ILE A 1 215 ? 7.447   19.644  -10.038 1.00 36.19 ? 217 ILE A C   1 
ATOM   1693 O O   . ILE A 1 215 ? 7.583   18.711  -10.832 1.00 34.87 ? 217 ILE A O   1 
ATOM   1694 C CB  . ILE A 1 215 ? 7.730   22.064  -10.727 1.00 38.16 ? 217 ILE A CB  1 
ATOM   1695 C CG1 . ILE A 1 215 ? 7.011   23.298  -11.279 1.00 39.32 ? 217 ILE A CG1 1 
ATOM   1696 C CG2 . ILE A 1 215 ? 8.781   21.604  -11.702 1.00 35.75 ? 217 ILE A CG2 1 
ATOM   1697 C CD1 . ILE A 1 215 ? 7.826   24.554  -11.180 1.00 31.31 ? 217 ILE A CD1 1 
ATOM   1698 N N   . VAL A 1 216 ? 7.899   19.574  -8.782  1.00 36.59 ? 218 VAL A N   1 
ATOM   1699 C CA  . VAL A 1 216 ? 8.690   18.431  -8.328  1.00 33.63 ? 218 VAL A CA  1 
ATOM   1700 C C   . VAL A 1 216 ? 7.861   17.154  -8.364  1.00 36.27 ? 218 VAL A C   1 
ATOM   1701 O O   . VAL A 1 216 ? 8.314   16.106  -8.848  1.00 30.52 ? 218 VAL A O   1 
ATOM   1702 C CB  . VAL A 1 216 ? 9.246   18.687  -6.914  1.00 35.04 ? 218 VAL A CB  1 
ATOM   1703 C CG1 . VAL A 1 216 ? 9.902   17.443  -6.373  1.00 29.98 ? 218 VAL A CG1 1 
ATOM   1704 C CG2 . VAL A 1 216 ? 10.237  19.850  -6.912  1.00 33.67 ? 218 VAL A CG2 1 
ATOM   1705 N N   . ASN A 1 217 ? 6.632   17.225  -7.854  1.00 36.71 ? 219 ASN A N   1 
ATOM   1706 C CA  . ASN A 1 217 ? 5.797   16.047  -7.660  1.00 34.57 ? 219 ASN A CA  1 
ATOM   1707 C C   . ASN A 1 217 ? 4.821   15.811  -8.803  1.00 34.65 ? 219 ASN A C   1 
ATOM   1708 O O   . ASN A 1 217 ? 4.323   14.689  -8.941  1.00 37.10 ? 219 ASN A O   1 
ATOM   1709 C CB  . ASN A 1 217 ? 5.019   16.166  -6.336  1.00 33.39 ? 219 ASN A CB  1 
ATOM   1710 C CG  . ASN A 1 217 ? 4.119   14.974  -6.062  1.00 36.52 ? 219 ASN A CG  1 
ATOM   1711 O OD1 . ASN A 1 217 ? 2.893   15.111  -6.006  1.00 34.84 ? 219 ASN A OD1 1 
ATOM   1712 N ND2 . ASN A 1 217 ? 4.720   13.800  -5.868  1.00 29.24 ? 219 ASN A ND2 1 
ATOM   1713 N N   . GLY A 1 218 ? 4.568   16.812  -9.647  1.00 33.50 ? 220 GLY A N   1 
ATOM   1714 C CA  . GLY A 1 218 ? 3.473   16.693  -10.593 1.00 34.54 ? 220 GLY A CA  1 
ATOM   1715 C C   . GLY A 1 218 ? 2.135   16.647  -9.891  1.00 40.14 ? 220 GLY A C   1 
ATOM   1716 O O   . GLY A 1 218 ? 1.177   16.065  -10.406 1.00 40.79 ? 220 GLY A O   1 
ATOM   1717 N N   . GLY A 1 219 ? 2.057   17.262  -8.719  1.00 39.62 ? 221 GLY A N   1 
ATOM   1718 C CA  . GLY A 1 219 ? 0.935   17.090  -7.826  1.00 38.10 ? 221 GLY A CA  1 
ATOM   1719 C C   . GLY A 1 219 ? 1.269   17.752  -6.505  1.00 43.20 ? 221 GLY A C   1 
ATOM   1720 O O   . GLY A 1 219 ? 2.219   18.541  -6.410  1.00 41.12 ? 221 GLY A O   1 
ATOM   1721 N N   . TYR A 1 220 ? 0.495   17.397  -5.478  1.00 40.86 ? 222 TYR A N   1 
ATOM   1722 C CA  . TYR A 1 220 ? 0.627   18.045  -4.179  1.00 39.75 ? 222 TYR A CA  1 
ATOM   1723 C C   . TYR A 1 220 ? 0.842   17.040  -3.045  1.00 36.02 ? 222 TYR A C   1 
ATOM   1724 O O   . TYR A 1 220 ? 0.645   17.379  -1.876  1.00 35.77 ? 222 TYR A O   1 
ATOM   1725 C CB  . TYR A 1 220 ? -0.590  18.941  -3.928  1.00 39.22 ? 222 TYR A CB  1 
ATOM   1726 C CG  . TYR A 1 220 ? -0.649  20.098  -4.911  1.00 45.04 ? 222 TYR A CG  1 
ATOM   1727 C CD1 . TYR A 1 220 ? 0.278   21.138  -4.847  1.00 45.73 ? 222 TYR A CD1 1 
ATOM   1728 C CD2 . TYR A 1 220 ? -1.607  20.143  -5.917  1.00 44.58 ? 222 TYR A CD2 1 
ATOM   1729 C CE1 . TYR A 1 220 ? 0.251   22.194  -5.751  1.00 41.29 ? 222 TYR A CE1 1 
ATOM   1730 C CE2 . TYR A 1 220 ? -1.645  21.210  -6.830  1.00 45.14 ? 222 TYR A CE2 1 
ATOM   1731 C CZ  . TYR A 1 220 ? -0.716  22.227  -6.735  1.00 46.78 ? 222 TYR A CZ  1 
ATOM   1732 O OH  . TYR A 1 220 ? -0.746  23.269  -7.634  1.00 48.11 ? 222 TYR A OH  1 
ATOM   1733 N N   . ALA A 1 221 ? 1.289   15.827  -3.372  1.00 33.98 ? 223 ALA A N   1 
ATOM   1734 C CA  . ALA A 1 221 ? 1.611   14.827  -2.359  1.00 33.73 ? 223 ALA A CA  1 
ATOM   1735 C C   . ALA A 1 221 ? 2.685   15.329  -1.393  1.00 35.75 ? 223 ALA A C   1 
ATOM   1736 O O   . ALA A 1 221 ? 3.723   15.859  -1.810  1.00 33.12 ? 223 ALA A O   1 
ATOM   1737 C CB  . ALA A 1 221 ? 2.078   13.542  -3.036  1.00 32.91 ? 223 ALA A CB  1 
ATOM   1738 N N   . GLY A 1 222 ? 2.427   15.152  -0.094  1.00 32.31 ? 224 GLY A N   1 
ATOM   1739 C CA  . GLY A 1 222 ? 3.359   15.555  0.936   1.00 27.11 ? 224 GLY A CA  1 
ATOM   1740 C C   . GLY A 1 222 ? 3.552   17.043  1.064   1.00 30.21 ? 224 GLY A C   1 
ATOM   1741 O O   . GLY A 1 222 ? 4.561   17.477  1.630   1.00 32.53 ? 224 GLY A O   1 
ATOM   1742 N N   . TYR A 1 223 ? 2.608   17.839  0.557   1.00 31.21 ? 225 TYR A N   1 
ATOM   1743 C CA  . TYR A 1 223 ? 2.776   19.293  0.527   1.00 33.92 ? 225 TYR A CA  1 
ATOM   1744 C C   . TYR A 1 223 ? 3.059   19.861  1.918   1.00 33.45 ? 225 TYR A C   1 
ATOM   1745 O O   . TYR A 1 223 ? 4.020   20.614  2.100   1.00 32.34 ? 225 TYR A O   1 
ATOM   1746 C CB  . TYR A 1 223 ? 1.534   19.958  -0.087  1.00 32.45 ? 225 TYR A CB  1 
ATOM   1747 C CG  . TYR A 1 223 ? 1.491   21.467  0.118   1.00 39.43 ? 225 TYR A CG  1 
ATOM   1748 C CD1 . TYR A 1 223 ? 2.602   22.254  -0.156  1.00 36.85 ? 225 TYR A CD1 1 
ATOM   1749 C CD2 . TYR A 1 223 ? 0.351   22.102  0.604   1.00 35.17 ? 225 TYR A CD2 1 
ATOM   1750 C CE1 . TYR A 1 223 ? 2.582   23.619  0.044   1.00 37.24 ? 225 TYR A CE1 1 
ATOM   1751 C CE2 . TYR A 1 223 ? 0.327   23.479  0.800   1.00 36.46 ? 225 TYR A CE2 1 
ATOM   1752 C CZ  . TYR A 1 223 ? 1.443   24.228  0.512   1.00 39.82 ? 225 TYR A CZ  1 
ATOM   1753 O OH  . TYR A 1 223 ? 1.451   25.592  0.695   1.00 43.24 ? 225 TYR A OH  1 
ATOM   1754 N N   . ALA A 1 224 ? 2.232   19.508  2.912   1.00 33.01 ? 226 ALA A N   1 
ATOM   1755 C CA  . ALA A 1 224 ? 2.390   20.057  4.259   1.00 34.24 ? 226 ALA A CA  1 
ATOM   1756 C C   . ALA A 1 224 ? 3.772   19.762  4.837   1.00 33.80 ? 226 ALA A C   1 
ATOM   1757 O O   . ALA A 1 224 ? 4.387   20.625  5.479   1.00 33.62 ? 226 ALA A O   1 
ATOM   1758 C CB  . ALA A 1 224 ? 1.298   19.496  5.180   1.00 31.38 ? 226 ALA A CB  1 
ATOM   1759 N N   . ASP A 1 225 ? 4.279   18.546  4.620   1.00 32.04 ? 227 ASP A N   1 
ATOM   1760 C CA  . ASP A 1 225 ? 5.597   18.184  5.135   1.00 30.92 ? 227 ASP A CA  1 
ATOM   1761 C C   . ASP A 1 225 ? 6.713   18.930  4.410   1.00 30.30 ? 227 ASP A C   1 
ATOM   1762 O O   . ASP A 1 225 ? 7.716   19.306  5.033   1.00 29.31 ? 227 ASP A O   1 
ATOM   1763 C CB  . ASP A 1 225 ? 5.812   16.675  5.021   1.00 29.86 ? 227 ASP A CB  1 
ATOM   1764 C CG  . ASP A 1 225 ? 7.102   16.225  5.673   1.00 29.96 ? 227 ASP A CG  1 
ATOM   1765 O OD1 . ASP A 1 225 ? 7.184   16.258  6.921   1.00 33.23 ? 227 ASP A OD1 1 
ATOM   1766 O OD2 . ASP A 1 225 ? 8.034   15.832  4.942   1.00 30.31 ? 227 ASP A OD2 1 
ATOM   1767 N N   . ARG A 1 226 ? 6.578   19.130  3.093   1.00 30.07 ? 228 ARG A N   1 
ATOM   1768 C CA  . ARG A 1 226 ? 7.577   19.913  2.369   1.00 28.30 ? 228 ARG A CA  1 
ATOM   1769 C C   . ARG A 1 226 ? 7.647   21.342  2.903   1.00 29.09 ? 228 ARG A C   1 
ATOM   1770 O O   . ARG A 1 226 ? 8.739   21.901  3.060   1.00 31.75 ? 228 ARG A O   1 
ATOM   1771 C CB  . ARG A 1 226 ? 7.271   19.905  0.864   1.00 31.49 ? 228 ARG A CB  1 
ATOM   1772 C CG  . ARG A 1 226 ? 7.287   18.523  0.201   1.00 27.15 ? 228 ARG A CG  1 
ATOM   1773 C CD  . ARG A 1 226 ? 6.700   18.585  -1.196  1.00 28.25 ? 228 ARG A CD  1 
ATOM   1774 N NE  . ARG A 1 226 ? 6.242   17.284  -1.677  1.00 28.67 ? 228 ARG A NE  1 
ATOM   1775 C CZ  . ARG A 1 226 ? 6.935   16.483  -2.490  1.00 31.19 ? 228 ARG A CZ  1 
ATOM   1776 N NH1 . ARG A 1 226 ? 8.148   16.833  -2.927  1.00 26.16 ? 228 ARG A NH1 1 
ATOM   1777 N NH2 . ARG A 1 226 ? 6.419   15.318  -2.852  1.00 26.02 ? 228 ARG A NH2 1 
ATOM   1778 N N   . LEU A 1 227 ? 6.488   21.932  3.219   1.00 31.42 ? 229 LEU A N   1 
ATOM   1779 C CA  . LEU A 1 227 ? 6.425   23.286  3.774   1.00 33.37 ? 229 LEU A CA  1 
ATOM   1780 C C   . LEU A 1 227 ? 7.040   23.352  5.168   1.00 32.58 ? 229 LEU A C   1 
ATOM   1781 O O   . LEU A 1 227 ? 7.788   24.285  5.492   1.00 33.77 ? 229 LEU A O   1 
ATOM   1782 C CB  . LEU A 1 227 ? 4.965   23.751  3.812   1.00 34.04 ? 229 LEU A CB  1 
ATOM   1783 C CG  . LEU A 1 227 ? 4.616   25.122  4.387   1.00 34.66 ? 229 LEU A CG  1 
ATOM   1784 C CD1 . LEU A 1 227 ? 5.189   26.209  3.517   1.00 40.65 ? 229 LEU A CD1 1 
ATOM   1785 C CD2 . LEU A 1 227 ? 3.101   25.281  4.519   1.00 34.11 ? 229 LEU A CD2 1 
ATOM   1786 N N   . LYS A 1 228 ? 6.719   22.374  6.015   1.00 30.15 ? 230 LYS A N   1 
ATOM   1787 C CA  . LYS A 1 228 ? 7.336   22.294  7.333   1.00 30.66 ? 230 LYS A CA  1 
ATOM   1788 C C   . LYS A 1 228 ? 8.856   22.241  7.237   1.00 35.10 ? 230 LYS A C   1 
ATOM   1789 O O   . LYS A 1 228 ? 9.562   22.901  8.010   1.00 33.65 ? 230 LYS A O   1 
ATOM   1790 C CB  . LYS A 1 228 ? 6.812   21.061  8.062   1.00 32.70 ? 230 LYS A CB  1 
ATOM   1791 C CG  . LYS A 1 228 ? 7.378   20.868  9.430   1.00 31.80 ? 230 LYS A CG  1 
ATOM   1792 C CD  . LYS A 1 228 ? 6.558   19.829  10.141  1.00 33.79 ? 230 LYS A CD  1 
ATOM   1793 C CE  . LYS A 1 228 ? 7.346   19.127  11.204  1.00 34.09 ? 230 LYS A CE  1 
ATOM   1794 N NZ  . LYS A 1 228 ? 6.928   17.701  11.214  1.00 42.94 ? 230 LYS A NZ  1 
ATOM   1795 N N   . ARG A 1 229 ? 9.380   21.443  6.302   1.00 33.65 ? 231 ARG A N   1 
ATOM   1796 C CA  . ARG A 1 229 ? 10.828  21.354  6.144   1.00 31.87 ? 231 ARG A CA  1 
ATOM   1797 C C   . ARG A 1 229 ? 11.408  22.665  5.634   1.00 31.36 ? 231 ARG A C   1 
ATOM   1798 O O   . ARG A 1 229 ? 12.469  23.100  6.096   1.00 30.01 ? 231 ARG A O   1 
ATOM   1799 C CB  . ARG A 1 229 ? 11.188  20.197  5.206   1.00 31.67 ? 231 ARG A CB  1 
ATOM   1800 C CG  . ARG A 1 229 ? 11.082  18.819  5.843   1.00 30.08 ? 231 ARG A CG  1 
ATOM   1801 C CD  . ARG A 1 229 ? 11.106  17.753  4.765   1.00 32.38 ? 231 ARG A CD  1 
ATOM   1802 N NE  . ARG A 1 229 ? 10.621  16.457  5.228   1.00 32.16 ? 231 ARG A NE  1 
ATOM   1803 C CZ  . ARG A 1 229 ? 11.396  15.469  5.670   1.00 29.23 ? 231 ARG A CZ  1 
ATOM   1804 N NH1 . ARG A 1 229 ? 12.708  15.623  5.734   1.00 26.45 ? 231 ARG A NH1 1 
ATOM   1805 N NH2 . ARG A 1 229 ? 10.851  14.322  6.042   1.00 27.03 ? 231 ARG A NH2 1 
ATOM   1806 N N   . PHE A 1 230 ? 10.724  23.322  4.695   1.00 29.68 ? 232 PHE A N   1 
ATOM   1807 C CA  . PHE A 1 230 ? 11.252  24.578  4.174   1.00 33.38 ? 232 PHE A CA  1 
ATOM   1808 C C   . PHE A 1 230 ? 11.390  25.616  5.281   1.00 35.42 ? 232 PHE A C   1 
ATOM   1809 O O   . PHE A 1 230 ? 12.442  26.248  5.427   1.00 40.26 ? 232 PHE A O   1 
ATOM   1810 C CB  . PHE A 1 230 ? 10.368  25.116  3.052   1.00 34.52 ? 232 PHE A CB  1 
ATOM   1811 C CG  . PHE A 1 230 ? 10.819  26.454  2.534   1.00 38.76 ? 232 PHE A CG  1 
ATOM   1812 C CD1 . PHE A 1 230 ? 11.678  26.536  1.449   1.00 34.58 ? 232 PHE A CD1 1 
ATOM   1813 C CD2 . PHE A 1 230 ? 10.406  27.632  3.150   1.00 40.93 ? 232 PHE A CD2 1 
ATOM   1814 C CE1 . PHE A 1 230 ? 12.100  27.755  0.976   1.00 35.73 ? 232 PHE A CE1 1 
ATOM   1815 C CE2 . PHE A 1 230 ? 10.836  28.859  2.685   1.00 39.20 ? 232 PHE A CE2 1 
ATOM   1816 C CZ  . PHE A 1 230 ? 11.681  28.920  1.595   1.00 41.23 ? 232 PHE A CZ  1 
ATOM   1817 N N   . ASN A 1 231 ? 10.336  25.806  6.074   1.00 36.22 ? 233 ASN A N   1 
ATOM   1818 C CA  . ASN A 1 231 ? 10.394  26.805  7.138   1.00 39.17 ? 233 ASN A CA  1 
ATOM   1819 C C   . ASN A 1 231 ? 11.514  26.507  8.124   1.00 38.03 ? 233 ASN A C   1 
ATOM   1820 O O   . ASN A 1 231 ? 12.246  27.418  8.531   1.00 38.89 ? 233 ASN A O   1 
ATOM   1821 C CB  . ASN A 1 231 ? 9.041   26.899  7.843   1.00 32.49 ? 233 ASN A CB  1 
ATOM   1822 C CG  . ASN A 1 231 ? 8.018   27.583  6.982   1.00 34.25 ? 233 ASN A CG  1 
ATOM   1823 O OD1 . ASN A 1 231 ? 8.376   28.403  6.141   1.00 40.49 ? 233 ASN A OD1 1 
ATOM   1824 N ND2 . ASN A 1 231 ? 6.752   27.256  7.168   1.00 35.70 ? 233 ASN A ND2 1 
ATOM   1825 N N   . ALA A 1 232 ? 11.687  25.236  8.498   1.00 34.97 ? 234 ALA A N   1 
ATOM   1826 C CA  . ALA A 1 232 ? 12.794  24.890  9.377   1.00 31.10 ? 234 ALA A CA  1 
ATOM   1827 C C   . ALA A 1 232 ? 14.124  25.275  8.749   1.00 36.43 ? 234 ALA A C   1 
ATOM   1828 O O   . ALA A 1 232 ? 15.031  25.745  9.444   1.00 40.31 ? 234 ALA A O   1 
ATOM   1829 C CB  . ALA A 1 232 ? 12.766  23.399  9.706   1.00 31.77 ? 234 ALA A CB  1 
ATOM   1830 N N   . VAL A 1 233 ? 14.263  25.093  7.431   1.00 36.44 ? 235 VAL A N   1 
ATOM   1831 C CA  . VAL A 1 233 ? 15.498  25.513  6.779   1.00 36.89 ? 235 VAL A CA  1 
ATOM   1832 C C   . VAL A 1 233 ? 15.588  27.029  6.757   1.00 36.71 ? 235 VAL A C   1 
ATOM   1833 O O   . VAL A 1 233 ? 16.649  27.605  7.032   1.00 36.48 ? 235 VAL A O   1 
ATOM   1834 C CB  . VAL A 1 233 ? 15.614  24.933  5.356   1.00 38.79 ? 235 VAL A CB  1 
ATOM   1835 C CG1 . VAL A 1 233 ? 16.900  25.426  4.717   1.00 38.44 ? 235 VAL A CG1 1 
ATOM   1836 C CG2 . VAL A 1 233 ? 15.631  23.423  5.382   1.00 34.73 ? 235 VAL A CG2 1 
ATOM   1837 N N   . ALA A 1 234 ? 14.483  27.698  6.417   1.00 36.00 ? 236 ALA A N   1 
ATOM   1838 C CA  . ALA A 1 234 ? 14.483  29.155  6.387   1.00 42.18 ? 236 ALA A CA  1 
ATOM   1839 C C   . ALA A 1 234 ? 14.948  29.735  7.719   1.00 42.11 ? 236 ALA A C   1 
ATOM   1840 O O   . ALA A 1 234 ? 15.721  30.703  7.742   1.00 44.62 ? 236 ALA A O   1 
ATOM   1841 C CB  . ALA A 1 234 ? 13.093  29.667  6.026   1.00 39.96 ? 236 ALA A CB  1 
ATOM   1842 N N   . ALA A 1 235 ? 14.520  29.131  8.835   1.00 36.28 ? 237 ALA A N   1 
ATOM   1843 C CA  . ALA A 1 235 ? 14.872  29.647  10.157  1.00 38.83 ? 237 ALA A CA  1 
ATOM   1844 C C   . ALA A 1 235 ? 16.372  29.582  10.396  1.00 43.68 ? 237 ALA A C   1 
ATOM   1845 O O   . ALA A 1 235 ? 16.981  30.560  10.847  1.00 48.59 ? 237 ALA A O   1 
ATOM   1846 C CB  . ALA A 1 235 ? 14.128  28.872  11.242  1.00 35.35 ? 237 ALA A CB  1 
ATOM   1847 N N   . VAL A 1 236 ? 16.985  28.434  10.102  1.00 43.28 ? 238 VAL A N   1 
ATOM   1848 C CA  . VAL A 1 236 ? 18.425  28.280  10.295  1.00 43.60 ? 238 VAL A CA  1 
ATOM   1849 C C   . VAL A 1 236 ? 19.212  29.233  9.395   1.00 45.57 ? 238 VAL A C   1 
ATOM   1850 O O   . VAL A 1 236 ? 20.288  29.716  9.777   1.00 48.97 ? 238 VAL A O   1 
ATOM   1851 C CB  . VAL A 1 236 ? 18.819  26.811  10.048  1.00 41.85 ? 238 VAL A CB  1 
ATOM   1852 C CG1 . VAL A 1 236 ? 20.330  26.644  10.033  1.00 41.25 ? 238 VAL A CG1 1 
ATOM   1853 C CG2 . VAL A 1 236 ? 18.178  25.912  11.095  1.00 36.93 ? 238 VAL A CG2 1 
ATOM   1854 N N   . ILE A 1 237 ? 18.700  29.520  8.199   1.00 42.82 ? 239 ILE A N   1 
ATOM   1855 C CA  . ILE A 1 237 ? 19.416  30.393  7.271   1.00 46.58 ? 239 ILE A CA  1 
ATOM   1856 C C   . ILE A 1 237 ? 19.265  31.863  7.657   1.00 48.26 ? 239 ILE A C   1 
ATOM   1857 O O   . ILE A 1 237 ? 20.186  32.657  7.448   1.00 51.89 ? 239 ILE A O   1 
ATOM   1858 C CB  . ILE A 1 237 ? 18.928  30.169  5.832   1.00 45.51 ? 239 ILE A CB  1 
ATOM   1859 C CG1 . ILE A 1 237 ? 19.182  28.747  5.371   1.00 46.09 ? 239 ILE A CG1 1 
ATOM   1860 C CG2 . ILE A 1 237 ? 19.614  31.119  4.869   1.00 53.02 ? 239 ILE A CG2 1 
ATOM   1861 C CD1 . ILE A 1 237 ? 18.691  28.526  3.952   1.00 45.15 ? 239 ILE A CD1 1 
ATOM   1862 N N   . GLY A 1 238 ? 18.122  32.253  8.212   1.00 47.43 ? 240 GLY A N   1 
ATOM   1863 C CA  . GLY A 1 238 ? 17.816  33.649  8.425   1.00 49.98 ? 240 GLY A CA  1 
ATOM   1864 C C   . GLY A 1 238 ? 16.921  34.262  7.377   1.00 53.42 ? 240 GLY A C   1 
ATOM   1865 O O   . GLY A 1 238 ? 16.863  35.491  7.279   1.00 58.06 ? 240 GLY A O   1 
ATOM   1866 N N   . ILE A 1 239 ? 16.226  33.450  6.608   1.00 47.26 ? 241 ILE A N   1 
ATOM   1867 C CA  . ILE A 1 239 ? 15.385  33.875  5.502   1.00 47.69 ? 241 ILE A CA  1 
ATOM   1868 C C   . ILE A 1 239 ? 13.936  33.870  5.968   1.00 50.18 ? 241 ILE A C   1 
ATOM   1869 O O   . ILE A 1 239 ? 13.562  33.132  6.887   1.00 48.25 ? 241 ILE A O   1 
ATOM   1870 C CB  . ILE A 1 239 ? 15.616  32.925  4.300   1.00 55.42 ? 241 ILE A CB  1 
ATOM   1871 C CG1 . ILE A 1 239 ? 16.996  33.161  3.686   1.00 57.06 ? 241 ILE A CG1 1 
ATOM   1872 C CG2 . ILE A 1 239 ? 14.547  33.053  3.238   1.00 58.03 ? 241 ILE A CG2 1 
ATOM   1873 C CD1 . ILE A 1 239 ? 17.444  34.591  3.697   1.00 49.29 ? 241 ILE A CD1 1 
ATOM   1874 N N   . ASP A 1 240 ? 13.112  34.713  5.350   1.00 48.36 ? 242 ASP A N   1 
ATOM   1875 C CA  . ASP A 1 240 ? 11.677  34.633  5.576   1.00 49.36 ? 242 ASP A CA  1 
ATOM   1876 C C   . ASP A 1 240 ? 11.193  33.207  5.351   1.00 55.09 ? 242 ASP A C   1 
ATOM   1877 O O   . ASP A 1 240 ? 11.610  32.532  4.405   1.00 53.44 ? 242 ASP A O   1 
ATOM   1878 C CB  . ASP A 1 240 ? 10.928  35.586  4.638   1.00 47.10 ? 242 ASP A CB  1 
ATOM   1879 C CG  . ASP A 1 240 ? 10.998  37.031  5.086   1.00 52.08 ? 242 ASP A CG  1 
ATOM   1880 O OD1 . ASP A 1 240 ? 11.419  37.294  6.240   1.00 46.27 ? 242 ASP A OD1 1 
ATOM   1881 O OD2 . ASP A 1 240 ? 10.631  37.907  4.273   1.00 57.28 ? 242 ASP A OD2 1 
ATOM   1882 N N   . GLY A 1 241 ? 10.319  32.740  6.235   1.00 52.50 ? 243 GLY A N   1 
ATOM   1883 C CA  . GLY A 1 241 ? 9.680   31.466  6.002   1.00 41.47 ? 243 GLY A CA  1 
ATOM   1884 C C   . GLY A 1 241 ? 8.692   31.559  4.861   1.00 43.19 ? 243 GLY A C   1 
ATOM   1885 O O   . GLY A 1 241 ? 8.719   32.505  4.072   1.00 45.88 ? 243 GLY A O   1 
ATOM   1886 N N   . ALA A 1 242 ? 7.815   30.576  4.757   1.00 42.38 ? 244 ALA A N   1 
ATOM   1887 C CA  . ALA A 1 242 ? 6.759   30.597  3.765   1.00 45.67 ? 244 ALA A CA  1 
ATOM   1888 C C   . ALA A 1 242 ? 5.462   30.232  4.457   1.00 44.92 ? 244 ALA A C   1 
ATOM   1889 O O   . ALA A 1 242 ? 5.428   29.317  5.283   1.00 46.38 ? 244 ALA A O   1 
ATOM   1890 C CB  . ALA A 1 242 ? 7.034   29.631  2.609   1.00 41.54 ? 244 ALA A CB  1 
ATOM   1891 N N   . ARG A 1 243 ? 4.409   30.978  4.147   1.00 47.78 ? 245 ARG A N   1 
ATOM   1892 C CA  . ARG A 1 243 ? 3.071   30.617  4.575   1.00 46.67 ? 245 ARG A CA  1 
ATOM   1893 C C   . ARG A 1 243 ? 2.389   29.719  3.568   1.00 45.80 ? 245 ARG A C   1 
ATOM   1894 O O   . ARG A 1 243 ? 1.293   29.219  3.840   1.00 50.45 ? 245 ARG A O   1 
ATOM   1895 C CB  . ARG A 1 243 ? 2.229   31.876  4.805   1.00 50.89 ? 245 ARG A CB  1 
ATOM   1896 C CG  . ARG A 1 243 ? 2.859   32.859  5.778   1.00 56.40 ? 245 ARG A CG  1 
ATOM   1897 C CD  . ARG A 1 243 ? 2.216   34.232  5.635   1.00 61.10 ? 245 ARG A CD  1 
ATOM   1898 N NE  . ARG A 1 243 ? 0.773   34.123  5.433   1.00 61.75 ? 245 ARG A NE  1 
ATOM   1899 C CZ  . ARG A 1 243 ? -0.138  34.326  6.382   1.00 64.12 ? 245 ARG A CZ  1 
ATOM   1900 N NH1 . ARG A 1 243 ? -1.429  34.191  6.096   1.00 63.38 ? 245 ARG A NH1 1 
ATOM   1901 N NH2 . ARG A 1 243 ? 0.240   34.665  7.613   1.00 61.99 ? 245 ARG A NH2 1 
ATOM   1902 N N   . GLU A 1 244 ? 3.027   29.492  2.428   1.00 45.11 ? 246 GLU A N   1 
ATOM   1903 C CA  . GLU A 1 244 ? 2.456   28.708  1.353   1.00 44.97 ? 246 GLU A CA  1 
ATOM   1904 C C   . GLU A 1 244 ? 3.572   28.194  0.447   1.00 40.31 ? 246 GLU A C   1 
ATOM   1905 O O   . GLU A 1 244 ? 3.419   27.142  -0.175  1.00 45.17 ? 246 GLU A O   1 
ATOM   1906 C CB  . GLU A 1 244 ? 1.447   29.546  0.562   1.00 45.24 ? 246 GLU A CB  1 
ATOM   1907 C CG  . GLU A 1 244 ? 0.666   28.774  -0.489  1.00 50.35 ? 246 GLU A CG  1 
ATOM   1908 C CD  . GLU A 1 244 ? -0.044  29.693  -1.475  1.00 60.82 ? 246 GLU A CD  1 
ATOM   1909 O OE1 . GLU A 1 244 ? -0.016  29.408  -2.699  1.00 62.11 ? 246 GLU A OE1 1 
ATOM   1910 O OE2 . GLU A 1 244 ? -0.633  30.699  -1.015  1.00 63.61 ? 246 GLU A OE2 1 
HETATM 1911 O O   . HOH B 2 .   ? 30.060  4.017   -20.862 1.00 26.20 ? 301 HOH A O   1 
HETATM 1912 O O   . HOH B 2 .   ? 12.152  11.474  -19.093 1.00 33.15 ? 302 HOH A O   1 
HETATM 1913 O O   . HOH B 2 .   ? 24.039  27.372  9.644   1.00 39.94 ? 303 HOH A O   1 
HETATM 1914 O O   . HOH B 2 .   ? 12.445  12.442  17.093  1.00 51.30 ? 304 HOH A O   1 
HETATM 1915 O O   . HOH B 2 .   ? 5.247   16.221  8.274   1.00 33.95 ? 305 HOH A O   1 
HETATM 1916 O O   . HOH B 2 .   ? 8.866   -9.058  -17.639 1.00 31.87 ? 306 HOH A O   1 
HETATM 1917 O O   . HOH B 2 .   ? 28.337  12.994  -21.520 1.00 25.31 ? 307 HOH A O   1 
HETATM 1918 O O   . HOH B 2 .   ? 9.761   -11.637 -4.377  1.00 29.81 ? 308 HOH A O   1 
HETATM 1919 O O   . HOH B 2 .   ? 13.165  8.157   3.690   1.00 45.74 ? 309 HOH A O   1 
HETATM 1920 O O   . HOH B 2 .   ? 9.778   23.445  -1.110  1.00 30.27 ? 310 HOH A O   1 
HETATM 1921 O O   . HOH B 2 .   ? -12.411 5.353   -19.649 1.00 23.83 ? 311 HOH A O   1 
HETATM 1922 O O   . HOH B 2 .   ? 4.691   -7.221  -23.108 1.00 32.63 ? 312 HOH A O   1 
HETATM 1923 O O   . HOH B 2 .   ? 12.784  20.240  -18.852 1.00 38.78 ? 313 HOH A O   1 
HETATM 1924 O O   . HOH B 2 .   ? 32.588  10.353  -21.112 1.00 34.15 ? 314 HOH A O   1 
HETATM 1925 O O   . HOH B 2 .   ? 16.083  0.570   -25.403 1.00 30.05 ? 315 HOH A O   1 
HETATM 1926 O O   . HOH B 2 .   ? 6.810   0.595   -7.473  1.00 33.40 ? 316 HOH A O   1 
HETATM 1927 O O   . HOH B 2 .   ? -0.410  -6.207  -21.952 1.00 27.07 ? 317 HOH A O   1 
HETATM 1928 O O   . HOH B 2 .   ? -9.653  0.686   -15.527 1.00 26.90 ? 318 HOH A O   1 
HETATM 1929 O O   . HOH B 2 .   ? 17.897  -3.157  -20.822 1.00 32.62 ? 319 HOH A O   1 
HETATM 1930 O O   . HOH B 2 .   ? 33.584  6.619   -16.274 1.00 26.74 ? 320 HOH A O   1 
HETATM 1931 O O   . HOH B 2 .   ? 17.879  12.263  -6.922  1.00 29.21 ? 321 HOH A O   1 
HETATM 1932 O O   . HOH B 2 .   ? 5.956   4.896   -26.225 1.00 31.35 ? 322 HOH A O   1 
HETATM 1933 O O   . HOH B 2 .   ? 23.332  20.014  15.066  1.00 55.29 ? 323 HOH A O   1 
HETATM 1934 O O   . HOH B 2 .   ? -3.791  0.387   -12.056 1.00 25.18 ? 324 HOH A O   1 
HETATM 1935 O O   . HOH B 2 .   ? -3.364  -11.721 -21.045 1.00 34.35 ? 325 HOH A O   1 
HETATM 1936 O O   . HOH B 2 .   ? 9.429   1.772   -4.144  1.00 42.86 ? 326 HOH A O   1 
HETATM 1937 O O   . HOH B 2 .   ? -13.025 -3.421  -16.874 1.00 48.21 ? 327 HOH A O   1 
HETATM 1938 O O   . HOH B 2 .   ? 10.011  5.551   -10.021 1.00 39.81 ? 328 HOH A O   1 
HETATM 1939 O O   . HOH B 2 .   ? 11.153  -2.964  -20.462 1.00 23.23 ? 329 HOH A O   1 
HETATM 1940 O O   . HOH B 2 .   ? 23.048  23.825  -13.866 1.00 34.14 ? 330 HOH A O   1 
HETATM 1941 O O   . HOH B 2 .   ? 31.299  20.966  -19.742 1.00 42.97 ? 331 HOH A O   1 
HETATM 1942 O O   . HOH B 2 .   ? 5.071   -14.110 -18.977 1.00 45.69 ? 332 HOH A O   1 
HETATM 1943 O O   . HOH B 2 .   ? -5.418  6.504   -10.820 1.00 28.48 ? 333 HOH A O   1 
HETATM 1944 O O   . HOH B 2 .   ? 16.475  -5.530  -16.659 1.00 30.06 ? 334 HOH A O   1 
HETATM 1945 O O   . HOH B 2 .   ? 31.578  14.408  -9.944  1.00 28.01 ? 335 HOH A O   1 
HETATM 1946 O O   . HOH B 2 .   ? 0.836   13.487  -6.910  1.00 36.31 ? 336 HOH A O   1 
HETATM 1947 O O   . HOH B 2 .   ? 12.677  8.904   -18.385 1.00 30.43 ? 337 HOH A O   1 
HETATM 1948 O O   . HOH B 2 .   ? 17.401  10.174  7.399   1.00 34.09 ? 338 HOH A O   1 
HETATM 1949 O O   . HOH B 2 .   ? 15.362  -2.120  -5.899  1.00 43.93 ? 339 HOH A O   1 
HETATM 1950 O O   . HOH B 2 .   ? 6.288   18.163  -13.236 1.00 36.20 ? 340 HOH A O   1 
HETATM 1951 O O   . HOH B 2 .   ? 14.979  24.449  -13.141 1.00 31.89 ? 341 HOH A O   1 
HETATM 1952 O O   . HOH B 2 .   ? 12.159  2.036   -16.087 1.00 19.47 ? 342 HOH A O   1 
HETATM 1953 O O   . HOH B 2 .   ? 20.638  -3.788  -10.620 1.00 37.10 ? 343 HOH A O   1 
HETATM 1954 O O   . HOH B 2 .   ? -14.755 -8.989  -12.785 1.00 42.47 ? 344 HOH A O   1 
HETATM 1955 O O   . HOH B 2 .   ? 6.553   -8.134  -8.169  1.00 20.23 ? 345 HOH A O   1 
HETATM 1956 O O   . HOH B 2 .   ? -9.375  4.505   -23.066 1.00 24.65 ? 346 HOH A O   1 
HETATM 1957 O O   . HOH B 2 .   ? -4.689  -13.977 -6.386  1.00 41.22 ? 347 HOH A O   1 
HETATM 1958 O O   . HOH B 2 .   ? -1.564  3.645   -10.375 1.00 28.32 ? 348 HOH A O   1 
HETATM 1959 O O   . HOH B 2 .   ? 13.622  12.795  8.636   1.00 33.04 ? 349 HOH A O   1 
HETATM 1960 O O   . HOH B 2 .   ? 23.212  9.942   3.905   1.00 29.92 ? 350 HOH A O   1 
HETATM 1961 O O   . HOH B 2 .   ? 24.471  19.970  -16.430 1.00 29.46 ? 351 HOH A O   1 
HETATM 1962 O O   . HOH B 2 .   ? 2.194   -5.646  -2.869  1.00 30.20 ? 352 HOH A O   1 
HETATM 1963 O O   . HOH B 2 .   ? -8.384  -7.040  -3.745  1.00 36.16 ? 353 HOH A O   1 
HETATM 1964 O O   . HOH B 2 .   ? 6.398   -5.384  -24.444 1.00 24.97 ? 354 HOH A O   1 
HETATM 1965 O O   . HOH B 2 .   ? -8.892  -12.665 -6.407  1.00 41.10 ? 355 HOH A O   1 
HETATM 1966 O O   . HOH B 2 .   ? -8.800  -13.717 -3.281  1.00 49.48 ? 356 HOH A O   1 
HETATM 1967 O O   . HOH B 2 .   ? 31.776  8.296   -19.282 1.00 29.27 ? 357 HOH A O   1 
HETATM 1968 O O   . HOH B 2 .   ? 30.383  16.170  6.917   1.00 38.59 ? 358 HOH A O   1 
HETATM 1969 O O   . HOH B 2 .   ? 7.861   13.493  -6.353  1.00 30.83 ? 359 HOH A O   1 
HETATM 1970 O O   . HOH B 2 .   ? 7.768   -6.176  -1.155  1.00 42.40 ? 360 HOH A O   1 
HETATM 1971 O O   . HOH B 2 .   ? 28.667  22.577  8.517   1.00 44.15 ? 361 HOH A O   1 
HETATM 1972 O O   . HOH B 2 .   ? 5.061   12.550  -1.260  1.00 33.51 ? 362 HOH A O   1 
HETATM 1973 O O   . HOH B 2 .   ? 20.498  12.337  15.208  1.00 30.27 ? 363 HOH A O   1 
HETATM 1974 O O   . HOH B 2 .   ? 3.312   22.329  7.649   1.00 48.54 ? 364 HOH A O   1 
HETATM 1975 O O   . HOH B 2 .   ? 17.730  33.614  -2.512  1.00 52.48 ? 365 HOH A O   1 
HETATM 1976 O O   . HOH B 2 .   ? 34.826  18.273  -12.637 1.00 35.22 ? 366 HOH A O   1 
HETATM 1977 O O   . HOH B 2 .   ? -3.561  1.856   -1.917  1.00 36.40 ? 367 HOH A O   1 
HETATM 1978 O O   . HOH B 2 .   ? -12.657 5.710   -9.973  1.00 32.01 ? 368 HOH A O   1 
HETATM 1979 O O   . HOH B 2 .   ? 23.746  15.681  -25.072 1.00 49.52 ? 369 HOH A O   1 
HETATM 1980 O O   . HOH B 2 .   ? 16.022  -7.903  -17.444 1.00 28.34 ? 370 HOH A O   1 
HETATM 1981 O O   . HOH B 2 .   ? 11.242  10.516  -5.286  1.00 39.38 ? 371 HOH A O   1 
HETATM 1982 O O   . HOH B 2 .   ? 3.152   -2.137  -20.574 1.00 28.13 ? 372 HOH A O   1 
HETATM 1983 O O   . HOH B 2 .   ? 13.275  -10.915 -10.093 1.00 32.97 ? 373 HOH A O   1 
HETATM 1984 O O   . HOH B 2 .   ? 29.500  28.074  5.995   1.00 55.03 ? 374 HOH A O   1 
HETATM 1985 O O   . HOH B 2 .   ? 12.895  -3.924  -6.581  1.00 32.75 ? 375 HOH A O   1 
HETATM 1986 O O   . HOH B 2 .   ? 9.772   -9.003  -27.597 1.00 39.12 ? 376 HOH A O   1 
HETATM 1987 O O   . HOH B 2 .   ? -14.002 1.153   -20.332 1.00 26.65 ? 377 HOH A O   1 
HETATM 1988 O O   . HOH B 2 .   ? 12.303  10.689  -13.761 1.00 33.84 ? 378 HOH A O   1 
HETATM 1989 O O   . HOH B 2 .   ? 0.336   2.857   -16.181 1.00 44.44 ? 379 HOH A O   1 
HETATM 1990 O O   . HOH B 2 .   ? 20.804  16.690  -20.122 1.00 35.92 ? 380 HOH A O   1 
HETATM 1991 O O   . HOH B 2 .   ? 13.866  15.745  -25.017 1.00 37.40 ? 381 HOH A O   1 
HETATM 1992 O O   . HOH B 2 .   ? 30.634  23.404  -13.762 1.00 44.61 ? 382 HOH A O   1 
HETATM 1993 O O   . HOH B 2 .   ? -2.070  1.379   -13.990 1.00 30.81 ? 383 HOH A O   1 
HETATM 1994 O O   . HOH B 2 .   ? 10.096  7.670   -25.919 1.00 41.23 ? 384 HOH A O   1 
HETATM 1995 O O   . HOH B 2 .   ? 2.123   16.463  3.892   1.00 34.29 ? 385 HOH A O   1 
HETATM 1996 O O   . HOH B 2 .   ? 36.839  11.345  -15.977 1.00 30.24 ? 386 HOH A O   1 
HETATM 1997 O O   . HOH B 2 .   ? -6.399  8.746   -14.666 1.00 32.07 ? 387 HOH A O   1 
HETATM 1998 O O   . HOH B 2 .   ? -2.228  -10.333 -3.096  1.00 30.86 ? 388 HOH A O   1 
HETATM 1999 O O   . HOH B 2 .   ? -6.761  2.304   -5.137  1.00 41.48 ? 389 HOH A O   1 
HETATM 2000 O O   . HOH B 2 .   ? 20.335  0.788   -26.292 1.00 40.76 ? 390 HOH A O   1 
HETATM 2001 O O   . HOH B 2 .   ? 13.038  -2.778  -27.340 1.00 24.96 ? 391 HOH A O   1 
HETATM 2002 O O   . HOH B 2 .   ? 24.510  -0.770  -12.335 1.00 30.68 ? 392 HOH A O   1 
HETATM 2003 O O   . HOH B 2 .   ? -4.580  21.878  -4.418  1.00 56.16 ? 393 HOH A O   1 
HETATM 2004 O O   . HOH B 2 .   ? -0.446  17.858  2.563   1.00 44.63 ? 394 HOH A O   1 
HETATM 2005 O O   . HOH B 2 .   ? 6.492   11.684  -2.976  1.00 41.67 ? 395 HOH A O   1 
HETATM 2006 O O   . HOH B 2 .   ? 15.372  -8.281  -8.147  1.00 46.55 ? 396 HOH A O   1 
HETATM 2007 O O   . HOH B 2 .   ? 11.412  -9.997  -18.360 1.00 33.47 ? 397 HOH A O   1 
HETATM 2008 O O   . HOH B 2 .   ? -2.309  -8.896  -0.995  1.00 40.11 ? 398 HOH A O   1 
HETATM 2009 O O   . HOH B 2 .   ? -3.814  27.535  -3.649  1.00 53.36 ? 399 HOH A O   1 
HETATM 2010 O O   . HOH B 2 .   ? 19.565  -3.138  -12.884 1.00 34.35 ? 400 HOH A O   1 
HETATM 2011 O O   . HOH B 2 .   ? 28.570  16.151  -21.480 1.00 45.24 ? 401 HOH A O   1 
HETATM 2012 O O   . HOH B 2 .   ? 2.867   -10.049 -24.441 1.00 44.70 ? 402 HOH A O   1 
HETATM 2013 O O   . HOH B 2 .   ? 20.898  -3.064  -21.418 1.00 40.13 ? 403 HOH A O   1 
HETATM 2014 O O   . HOH B 2 .   ? 4.636   -13.372 -21.296 1.00 35.59 ? 404 HOH A O   1 
HETATM 2015 O O   . HOH B 2 .   ? 21.631  5.728   11.152  1.00 59.96 ? 405 HOH A O   1 
HETATM 2016 O O   . HOH B 2 .   ? 8.490   -8.367  -25.902 1.00 40.67 ? 406 HOH A O   1 
HETATM 2017 O O   . HOH B 2 .   ? -5.891  -15.833 -7.643  1.00 52.19 ? 407 HOH A O   1 
HETATM 2018 O O   . HOH B 2 .   ? 10.353  -5.517  -0.213  1.00 48.23 ? 408 HOH A O   1 
HETATM 2019 O O   . HOH B 2 .   ? 35.075  12.185  -7.922  1.00 37.90 ? 409 HOH A O   1 
HETATM 2020 O O   . HOH B 2 .   ? -6.921  5.263   -5.529  1.00 47.35 ? 410 HOH A O   1 
HETATM 2021 O O   . HOH B 2 .   ? 17.978  -1.750  -25.233 1.00 49.32 ? 411 HOH A O   1 
HETATM 2022 O O   . HOH B 2 .   ? 36.898  11.628  -9.420  1.00 45.69 ? 412 HOH A O   1 
HETATM 2023 O O   . HOH B 2 .   ? -8.386  -12.253 -10.673 1.00 32.76 ? 413 HOH A O   1 
HETATM 2024 O O   . HOH B 2 .   ? -10.655 -11.983 -11.019 1.00 49.99 ? 414 HOH A O   1 
HETATM 2025 O O   . HOH B 2 .   ? 2.318   15.544  6.568   1.00 32.13 ? 415 HOH A O   1 
HETATM 2026 O O   . HOH B 2 .   ? 10.422  3.300   -2.500  1.00 45.67 ? 416 HOH A O   1 
HETATM 2027 O O   . HOH B 2 .   ? 22.241  16.326  -23.957 0.50 40.15 ? 417 HOH A O   1 
HETATM 2028 O O   . HOH B 2 .   ? 6.515   -10.543 -25.075 1.00 56.36 ? 418 HOH A O   1 
HETATM 2029 O O   . HOH B 2 .   ? 24.977  22.696  -15.415 1.00 46.24 ? 419 HOH A O   1 
HETATM 2030 O O   . HOH B 2 .   ? 18.818  -5.256  -15.106 1.00 42.64 ? 420 HOH A O   1 
HETATM 2031 O O   . HOH B 2 .   ? 22.241  1.472   -23.957 0.50 40.89 ? 421 HOH A O   1 
HETATM 2032 O O   . HOH B 2 .   ? 23.923  20.659  -19.080 1.00 37.52 ? 422 HOH A O   1 
HETATM 2033 O O   . HOH B 2 .   ? -4.847  -7.987  0.384   1.00 45.62 ? 423 HOH A O   1 
# 
