data_9JN5
# 
_entry.id   9JN5 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.399 
_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   9JN5         pdb_00009jn5 10.2210/pdb9jn5/pdb 
WWPDB D_1300051707 ?            ?                   
# 
_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       2025-01-29 
# 
_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                        9JN5 
_pdbx_database_status.recvd_initial_deposition_date   2024-09-22 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBJ 
_pdbx_database_status.process_site                    PDBC 
_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              yunyunyang0219@163.com 
_pdbx_contact_author.name_first         Yunyun 
_pdbx_contact_author.name_last          Yang 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-6042-3617 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Li, Y.L.'     1 ? 
'Yang, Y.Y.'   2 ? 
'Huang, J.-W.' 3 ? 
'Chen, C.-C.'  4 ? 
'Guo, R.-T.'   5 ? 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   US 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'Acs Catalysis' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           2155-5435 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            15 
_citation.language                  ? 
_citation.page_first                1265 
_citation.page_last                 1273 
_citation.title                     
'Structural Insights into the N-N Bond-Formation Mechanism of the Heme-Dependent Piperazate Synthase KtzT' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1021/acscatal.4c06124 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Yang, Y.'    1 ? 
primary 'Li, Y.'      2 ? 
primary 'Yao, L.'     3 ? 
primary 'Dai, K.'     4 ? 
primary 'Fu, X.'      5 ? 
primary 'Ge, A.'      6 ? 
primary 'Huang, J.W.' 7 ? 
primary 'Guo, R.T.'   8 ? 
primary 'Chen, C.C.'  9 ? 
# 
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 'FMN-binding protein'             23249.340 4   ? ? ? ? 
2 non-polymer syn 'PROTOPORPHYRIN IX CONTAINING FE' 616.487   4   ? ? ? ? 
3 non-polymer syn N~5~-hydroxy-L-ornithine          148.160   2   ? ? ? ? 
4 water       nat water                             18.015    744 ? ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        KtzT,Regulator 
# 
_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       
;AGAGAMFVPGPYHAPEDRWLVDLVRGHPLAQLASNGAGGAAPHITHVPIIVDPELDGPVDRLVGITLWGHMNRANPHWAA
LGGAANVVATFAGPNAYVSPAVYRTAPAAPTWNFTSVQVRGELRKVESADDTLATVRATVAALESRFGAGWDMTGSLDYF
RRILPGVGAFRLRVAEADGMFKLSQEQQPAIRRRVRHSFGGAEATRAVAGLMDRLPTE
;
_entity_poly.pdbx_seq_one_letter_code_can   
;AGAGAMFVPGPYHAPEDRWLVDLVRGHPLAQLASNGAGGAAPHITHVPIIVDPELDGPVDRLVGITLWGHMNRANPHWAA
LGGAANVVATFAGPNAYVSPAVYRTAPAAPTWNFTSVQVRGELRKVESADDTLATVRATVAALESRFGAGWDMTGSLDYF
RRILPGVGAFRLRVAEADGMFKLSQEQQPAIRRRVRHSFGGAEATRAVAGLMDRLPTE
;
_entity_poly.pdbx_strand_id                 A,B,C,D 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'PROTOPORPHYRIN IX CONTAINING FE' HEM 
3 N~5~-hydroxy-L-ornithine          ONH 
4 water                             HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   ALA n 
1 2   GLY n 
1 3   ALA n 
1 4   GLY n 
1 5   ALA n 
1 6   MET n 
1 7   PHE n 
1 8   VAL n 
1 9   PRO n 
1 10  GLY n 
1 11  PRO n 
1 12  TYR n 
1 13  HIS n 
1 14  ALA n 
1 15  PRO n 
1 16  GLU n 
1 17  ASP n 
1 18  ARG n 
1 19  TRP n 
1 20  LEU n 
1 21  VAL n 
1 22  ASP n 
1 23  LEU n 
1 24  VAL n 
1 25  ARG n 
1 26  GLY n 
1 27  HIS n 
1 28  PRO n 
1 29  LEU n 
1 30  ALA n 
1 31  GLN n 
1 32  LEU n 
1 33  ALA n 
1 34  SER n 
1 35  ASN n 
1 36  GLY n 
1 37  ALA n 
1 38  GLY n 
1 39  GLY n 
1 40  ALA n 
1 41  ALA n 
1 42  PRO n 
1 43  HIS n 
1 44  ILE n 
1 45  THR n 
1 46  HIS n 
1 47  VAL n 
1 48  PRO n 
1 49  ILE n 
1 50  ILE n 
1 51  VAL n 
1 52  ASP n 
1 53  PRO n 
1 54  GLU n 
1 55  LEU n 
1 56  ASP n 
1 57  GLY n 
1 58  PRO n 
1 59  VAL n 
1 60  ASP n 
1 61  ARG n 
1 62  LEU n 
1 63  VAL n 
1 64  GLY n 
1 65  ILE n 
1 66  THR n 
1 67  LEU n 
1 68  TRP n 
1 69  GLY n 
1 70  HIS n 
1 71  MET n 
1 72  ASN n 
1 73  ARG n 
1 74  ALA n 
1 75  ASN n 
1 76  PRO n 
1 77  HIS n 
1 78  TRP n 
1 79  ALA n 
1 80  ALA n 
1 81  LEU n 
1 82  GLY n 
1 83  GLY n 
1 84  ALA n 
1 85  ALA n 
1 86  ASN n 
1 87  VAL n 
1 88  VAL n 
1 89  ALA n 
1 90  THR n 
1 91  PHE n 
1 92  ALA n 
1 93  GLY n 
1 94  PRO n 
1 95  ASN n 
1 96  ALA n 
1 97  TYR n 
1 98  VAL n 
1 99  SER n 
1 100 PRO n 
1 101 ALA n 
1 102 VAL n 
1 103 TYR n 
1 104 ARG n 
1 105 THR n 
1 106 ALA n 
1 107 PRO n 
1 108 ALA n 
1 109 ALA n 
1 110 PRO n 
1 111 THR n 
1 112 TRP n 
1 113 ASN n 
1 114 PHE n 
1 115 THR n 
1 116 SER n 
1 117 VAL n 
1 118 GLN n 
1 119 VAL n 
1 120 ARG n 
1 121 GLY n 
1 122 GLU n 
1 123 LEU n 
1 124 ARG n 
1 125 LYS n 
1 126 VAL n 
1 127 GLU n 
1 128 SER n 
1 129 ALA n 
1 130 ASP n 
1 131 ASP n 
1 132 THR n 
1 133 LEU n 
1 134 ALA n 
1 135 THR n 
1 136 VAL n 
1 137 ARG n 
1 138 ALA n 
1 139 THR n 
1 140 VAL n 
1 141 ALA n 
1 142 ALA n 
1 143 LEU n 
1 144 GLU n 
1 145 SER n 
1 146 ARG n 
1 147 PHE n 
1 148 GLY n 
1 149 ALA n 
1 150 GLY n 
1 151 TRP n 
1 152 ASP n 
1 153 MET n 
1 154 THR n 
1 155 GLY n 
1 156 SER n 
1 157 LEU n 
1 158 ASP n 
1 159 TYR n 
1 160 PHE n 
1 161 ARG n 
1 162 ARG n 
1 163 ILE n 
1 164 LEU n 
1 165 PRO n 
1 166 GLY n 
1 167 VAL n 
1 168 GLY n 
1 169 ALA n 
1 170 PHE n 
1 171 ARG n 
1 172 LEU n 
1 173 ARG n 
1 174 VAL n 
1 175 ALA n 
1 176 GLU n 
1 177 ALA n 
1 178 ASP n 
1 179 GLY n 
1 180 MET n 
1 181 PHE n 
1 182 LYS n 
1 183 LEU n 
1 184 SER n 
1 185 GLN n 
1 186 GLU n 
1 187 GLN n 
1 188 GLN n 
1 189 PRO n 
1 190 ALA n 
1 191 ILE n 
1 192 ARG n 
1 193 ARG n 
1 194 ARG n 
1 195 VAL n 
1 196 ARG n 
1 197 HIS n 
1 198 SER n 
1 199 PHE n 
1 200 GLY n 
1 201 GLY n 
1 202 ALA n 
1 203 GLU n 
1 204 ALA n 
1 205 THR n 
1 206 ARG n 
1 207 ALA n 
1 208 VAL n 
1 209 ALA n 
1 210 GLY n 
1 211 LEU n 
1 212 MET n 
1 213 ASP n 
1 214 ARG n 
1 215 LEU n 
1 216 PRO n 
1 217 THR n 
1 218 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                   218 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 KUTG_08928 
_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      'Kutzneria sp. 744' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     345341 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli BL21(DE3)' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     469008 
_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  
HEM non-polymer         . 'PROTOPORPHYRIN IX CONTAINING FE' HEME 'C34 H32 Fe N4 O4' 616.487 
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 
ONH 'L-peptide linking' n N~5~-hydroxy-L-ornithine          ?    'C5 H12 N2 O3'     148.160 
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   ALA 1   -4  ?   ?   ?   A . n 
A 1 2   GLY 2   -3  ?   ?   ?   A . n 
A 1 3   ALA 3   -2  ?   ?   ?   A . n 
A 1 4   GLY 4   -1  ?   ?   ?   A . n 
A 1 5   ALA 5   0   ?   ?   ?   A . n 
A 1 6   MET 6   1   1   MET MET A . n 
A 1 7   PHE 7   2   2   PHE PHE A . n 
A 1 8   VAL 8   3   3   VAL VAL A . n 
A 1 9   PRO 9   4   4   PRO PRO A . n 
A 1 10  GLY 10  5   5   GLY GLY A . n 
A 1 11  PRO 11  6   6   PRO PRO A . n 
A 1 12  TYR 12  7   7   TYR TYR A . n 
A 1 13  HIS 13  8   8   HIS HIS A . n 
A 1 14  ALA 14  9   9   ALA ALA A . n 
A 1 15  PRO 15  10  10  PRO PRO A . n 
A 1 16  GLU 16  11  11  GLU GLU A . n 
A 1 17  ASP 17  12  12  ASP ASP A . n 
A 1 18  ARG 18  13  13  ARG ARG A . n 
A 1 19  TRP 19  14  14  TRP TRP A . n 
A 1 20  LEU 20  15  15  LEU LEU A . n 
A 1 21  VAL 21  16  16  VAL VAL A . n 
A 1 22  ASP 22  17  17  ASP ASP A . n 
A 1 23  LEU 23  18  18  LEU LEU A . n 
A 1 24  VAL 24  19  19  VAL VAL A . n 
A 1 25  ARG 25  20  20  ARG ARG A . n 
A 1 26  GLY 26  21  21  GLY GLY A . n 
A 1 27  HIS 27  22  22  HIS HIS A . n 
A 1 28  PRO 28  23  23  PRO PRO A . n 
A 1 29  LEU 29  24  24  LEU LEU A . n 
A 1 30  ALA 30  25  25  ALA ALA A . n 
A 1 31  GLN 31  26  26  GLN GLN A . n 
A 1 32  LEU 32  27  27  LEU LEU A . n 
A 1 33  ALA 33  28  28  ALA ALA A . n 
A 1 34  SER 34  29  29  SER SER A . n 
A 1 35  ASN 35  30  30  ASN ASN A . n 
A 1 36  GLY 36  31  31  GLY GLY A . n 
A 1 37  ALA 37  32  32  ALA ALA A . n 
A 1 38  GLY 38  33  33  GLY GLY A . n 
A 1 39  GLY 39  34  34  GLY GLY A . n 
A 1 40  ALA 40  35  35  ALA ALA A . n 
A 1 41  ALA 41  36  36  ALA ALA A . n 
A 1 42  PRO 42  37  37  PRO PRO A . n 
A 1 43  HIS 43  38  38  HIS HIS A . n 
A 1 44  ILE 44  39  39  ILE ILE A . n 
A 1 45  THR 45  40  40  THR THR A . n 
A 1 46  HIS 46  41  41  HIS HIS A . n 
A 1 47  VAL 47  42  42  VAL VAL A . n 
A 1 48  PRO 48  43  43  PRO PRO A . n 
A 1 49  ILE 49  44  44  ILE ILE A . n 
A 1 50  ILE 50  45  45  ILE ILE A . n 
A 1 51  VAL 51  46  46  VAL VAL A . n 
A 1 52  ASP 52  47  47  ASP ASP A . n 
A 1 53  PRO 53  48  48  PRO PRO A . n 
A 1 54  GLU 54  49  49  GLU GLU A . n 
A 1 55  LEU 55  50  50  LEU LEU A . n 
A 1 56  ASP 56  51  51  ASP ASP A . n 
A 1 57  GLY 57  52  52  GLY GLY A . n 
A 1 58  PRO 58  53  53  PRO PRO A . n 
A 1 59  VAL 59  54  54  VAL VAL A . n 
A 1 60  ASP 60  55  55  ASP ASP A . n 
A 1 61  ARG 61  56  56  ARG ARG A . n 
A 1 62  LEU 62  57  57  LEU LEU A . n 
A 1 63  VAL 63  58  58  VAL VAL A . n 
A 1 64  GLY 64  59  59  GLY GLY A . n 
A 1 65  ILE 65  60  60  ILE ILE A . n 
A 1 66  THR 66  61  61  THR THR A . n 
A 1 67  LEU 67  62  62  LEU LEU A . n 
A 1 68  TRP 68  63  63  TRP TRP A . n 
A 1 69  GLY 69  64  64  GLY GLY A . n 
A 1 70  HIS 70  65  65  HIS HIS A . n 
A 1 71  MET 71  66  66  MET MET A . n 
A 1 72  ASN 72  67  67  ASN ASN A . n 
A 1 73  ARG 73  68  68  ARG ARG A . n 
A 1 74  ALA 74  69  69  ALA ALA A . n 
A 1 75  ASN 75  70  70  ASN ASN A . n 
A 1 76  PRO 76  71  71  PRO PRO A . n 
A 1 77  HIS 77  72  72  HIS HIS A . n 
A 1 78  TRP 78  73  73  TRP TRP A . n 
A 1 79  ALA 79  74  74  ALA ALA A . n 
A 1 80  ALA 80  75  75  ALA ALA A . n 
A 1 81  LEU 81  76  76  LEU LEU A . n 
A 1 82  GLY 82  77  77  GLY GLY A . n 
A 1 83  GLY 83  78  78  GLY GLY A . n 
A 1 84  ALA 84  79  79  ALA ALA A . n 
A 1 85  ALA 85  80  80  ALA ALA A . n 
A 1 86  ASN 86  81  81  ASN ASN A . n 
A 1 87  VAL 87  82  82  VAL VAL A . n 
A 1 88  VAL 88  83  83  VAL VAL A . n 
A 1 89  ALA 89  84  84  ALA ALA A . n 
A 1 90  THR 90  85  85  THR THR A . n 
A 1 91  PHE 91  86  86  PHE PHE A . n 
A 1 92  ALA 92  87  87  ALA ALA A . n 
A 1 93  GLY 93  88  88  GLY GLY A . n 
A 1 94  PRO 94  89  89  PRO PRO A . n 
A 1 95  ASN 95  90  90  ASN ASN A . n 
A 1 96  ALA 96  91  91  ALA ALA A . n 
A 1 97  TYR 97  92  92  TYR TYR A . n 
A 1 98  VAL 98  93  93  VAL VAL A . n 
A 1 99  SER 99  94  94  SER SER A . n 
A 1 100 PRO 100 95  95  PRO PRO A . n 
A 1 101 ALA 101 96  96  ALA ALA A . n 
A 1 102 VAL 102 97  97  VAL VAL A . n 
A 1 103 TYR 103 98  98  TYR TYR A . n 
A 1 104 ARG 104 99  99  ARG ARG A . n 
A 1 105 THR 105 100 100 THR THR A . n 
A 1 106 ALA 106 101 101 ALA ALA A . n 
A 1 107 PRO 107 102 102 PRO PRO A . n 
A 1 108 ALA 108 103 103 ALA ALA A . n 
A 1 109 ALA 109 104 104 ALA ALA A . n 
A 1 110 PRO 110 105 105 PRO PRO A . n 
A 1 111 THR 111 106 106 THR THR A . n 
A 1 112 TRP 112 107 107 TRP TRP A . n 
A 1 113 ASN 113 108 108 ASN ASN A . n 
A 1 114 PHE 114 109 109 PHE PHE A . n 
A 1 115 THR 115 110 110 THR THR A . n 
A 1 116 SER 116 111 111 SER SER A . n 
A 1 117 VAL 117 112 112 VAL VAL A . n 
A 1 118 GLN 118 113 113 GLN GLN A . n 
A 1 119 VAL 119 114 114 VAL VAL A . n 
A 1 120 ARG 120 115 115 ARG ARG A . n 
A 1 121 GLY 121 116 116 GLY GLY A . n 
A 1 122 GLU 122 117 117 GLU GLU A . n 
A 1 123 LEU 123 118 118 LEU LEU A . n 
A 1 124 ARG 124 119 119 ARG ARG A . n 
A 1 125 LYS 125 120 120 LYS LYS A . n 
A 1 126 VAL 126 121 121 VAL VAL A . n 
A 1 127 GLU 127 122 122 GLU GLU A . n 
A 1 128 SER 128 123 123 SER SER A . n 
A 1 129 ALA 129 124 124 ALA ALA A . n 
A 1 130 ASP 130 125 125 ASP ASP A . n 
A 1 131 ASP 131 126 126 ASP ASP A . n 
A 1 132 THR 132 127 127 THR THR A . n 
A 1 133 LEU 133 128 128 LEU LEU A . n 
A 1 134 ALA 134 129 129 ALA ALA A . n 
A 1 135 THR 135 130 130 THR THR A . n 
A 1 136 VAL 136 131 131 VAL VAL A . n 
A 1 137 ARG 137 132 132 ARG ARG A . n 
A 1 138 ALA 138 133 133 ALA ALA A . n 
A 1 139 THR 139 134 134 THR THR A . n 
A 1 140 VAL 140 135 135 VAL VAL A . n 
A 1 141 ALA 141 136 136 ALA ALA A . n 
A 1 142 ALA 142 137 137 ALA ALA A . n 
A 1 143 LEU 143 138 138 LEU LEU A . n 
A 1 144 GLU 144 139 139 GLU GLU A . n 
A 1 145 SER 145 140 140 SER SER A . n 
A 1 146 ARG 146 141 141 ARG ARG A . n 
A 1 147 PHE 147 142 142 PHE PHE A . n 
A 1 148 GLY 148 143 143 GLY GLY A . n 
A 1 149 ALA 149 144 144 ALA ALA A . n 
A 1 150 GLY 150 145 145 GLY GLY A . n 
A 1 151 TRP 151 146 146 TRP TRP A . n 
A 1 152 ASP 152 147 147 ASP ASP A . n 
A 1 153 MET 153 148 148 MET MET A . n 
A 1 154 THR 154 149 149 THR THR A . n 
A 1 155 GLY 155 150 150 GLY GLY A . n 
A 1 156 SER 156 151 151 SER SER A . n 
A 1 157 LEU 157 152 152 LEU LEU A . n 
A 1 158 ASP 158 153 153 ASP ASP A . n 
A 1 159 TYR 159 154 154 TYR TYR A . n 
A 1 160 PHE 160 155 155 PHE PHE A . n 
A 1 161 ARG 161 156 156 ARG ARG A . n 
A 1 162 ARG 162 157 157 ARG ARG A . n 
A 1 163 ILE 163 158 158 ILE ILE A . n 
A 1 164 LEU 164 159 159 LEU LEU A . n 
A 1 165 PRO 165 160 160 PRO PRO A . n 
A 1 166 GLY 166 161 161 GLY GLY A . n 
A 1 167 VAL 167 162 162 VAL VAL A . n 
A 1 168 GLY 168 163 163 GLY GLY A . n 
A 1 169 ALA 169 164 164 ALA ALA A . n 
A 1 170 PHE 170 165 165 PHE PHE A . n 
A 1 171 ARG 171 166 166 ARG ARG A . n 
A 1 172 LEU 172 167 167 LEU LEU A . n 
A 1 173 ARG 173 168 168 ARG ARG A . n 
A 1 174 VAL 174 169 169 VAL VAL A . n 
A 1 175 ALA 175 170 170 ALA ALA A . n 
A 1 176 GLU 176 171 171 GLU GLU A . n 
A 1 177 ALA 177 172 172 ALA ALA A . n 
A 1 178 ASP 178 173 173 ASP ASP A . n 
A 1 179 GLY 179 174 174 GLY GLY A . n 
A 1 180 MET 180 175 175 MET MET A . n 
A 1 181 PHE 181 176 176 PHE PHE A . n 
A 1 182 LYS 182 177 177 LYS LYS A . n 
A 1 183 LEU 183 178 178 LEU LEU A . n 
A 1 184 SER 184 179 179 SER SER A . n 
A 1 185 GLN 185 180 180 GLN GLN A . n 
A 1 186 GLU 186 181 181 GLU GLU A . n 
A 1 187 GLN 187 182 182 GLN GLN A . n 
A 1 188 GLN 188 183 183 GLN GLN A . n 
A 1 189 PRO 189 184 184 PRO PRO A . n 
A 1 190 ALA 190 185 185 ALA ALA A . n 
A 1 191 ILE 191 186 186 ILE ILE A . n 
A 1 192 ARG 192 187 187 ARG ARG A . n 
A 1 193 ARG 193 188 188 ARG ARG A . n 
A 1 194 ARG 194 189 189 ARG ARG A . n 
A 1 195 VAL 195 190 190 VAL VAL A . n 
A 1 196 ARG 196 191 191 ARG ARG A . n 
A 1 197 HIS 197 192 192 HIS HIS A . n 
A 1 198 SER 198 193 193 SER SER A . n 
A 1 199 PHE 199 194 194 PHE PHE A . n 
A 1 200 GLY 200 195 195 GLY GLY A . n 
A 1 201 GLY 201 196 196 GLY GLY A . n 
A 1 202 ALA 202 197 197 ALA ALA A . n 
A 1 203 GLU 203 198 198 GLU GLU A . n 
A 1 204 ALA 204 199 199 ALA ALA A . n 
A 1 205 THR 205 200 200 THR THR A . n 
A 1 206 ARG 206 201 201 ARG ARG A . n 
A 1 207 ALA 207 202 202 ALA ALA A . n 
A 1 208 VAL 208 203 203 VAL VAL A . n 
A 1 209 ALA 209 204 204 ALA ALA A . n 
A 1 210 GLY 210 205 205 GLY GLY A . n 
A 1 211 LEU 211 206 206 LEU LEU A . n 
A 1 212 MET 212 207 207 MET MET A . n 
A 1 213 ASP 213 208 208 ASP ASP A . n 
A 1 214 ARG 214 209 209 ARG ARG A . n 
A 1 215 LEU 215 210 210 LEU LEU A . n 
A 1 216 PRO 216 211 211 PRO PRO A . n 
A 1 217 THR 217 212 ?   ?   ?   A . n 
A 1 218 GLU 218 213 ?   ?   ?   A . n 
B 1 1   ALA 1   -4  ?   ?   ?   B . n 
B 1 2   GLY 2   -3  ?   ?   ?   B . n 
B 1 3   ALA 3   -2  ?   ?   ?   B . n 
B 1 4   GLY 4   -1  ?   ?   ?   B . n 
B 1 5   ALA 5   0   0   ALA ALA B . n 
B 1 6   MET 6   1   1   MET MET B . n 
B 1 7   PHE 7   2   2   PHE PHE B . n 
B 1 8   VAL 8   3   3   VAL VAL B . n 
B 1 9   PRO 9   4   4   PRO PRO B . n 
B 1 10  GLY 10  5   5   GLY GLY B . n 
B 1 11  PRO 11  6   6   PRO PRO B . n 
B 1 12  TYR 12  7   7   TYR TYR B . n 
B 1 13  HIS 13  8   8   HIS HIS B . n 
B 1 14  ALA 14  9   9   ALA ALA B . n 
B 1 15  PRO 15  10  10  PRO PRO B . n 
B 1 16  GLU 16  11  11  GLU GLU B . n 
B 1 17  ASP 17  12  12  ASP ASP B . n 
B 1 18  ARG 18  13  13  ARG ARG B . n 
B 1 19  TRP 19  14  14  TRP TRP B . n 
B 1 20  LEU 20  15  15  LEU LEU B . n 
B 1 21  VAL 21  16  16  VAL VAL B . n 
B 1 22  ASP 22  17  17  ASP ASP B . n 
B 1 23  LEU 23  18  18  LEU LEU B . n 
B 1 24  VAL 24  19  19  VAL VAL B . n 
B 1 25  ARG 25  20  20  ARG ARG B . n 
B 1 26  GLY 26  21  21  GLY GLY B . n 
B 1 27  HIS 27  22  22  HIS HIS B . n 
B 1 28  PRO 28  23  23  PRO PRO B . n 
B 1 29  LEU 29  24  24  LEU LEU B . n 
B 1 30  ALA 30  25  25  ALA ALA B . n 
B 1 31  GLN 31  26  26  GLN GLN B . n 
B 1 32  LEU 32  27  27  LEU LEU B . n 
B 1 33  ALA 33  28  28  ALA ALA B . n 
B 1 34  SER 34  29  29  SER SER B . n 
B 1 35  ASN 35  30  30  ASN ASN B . n 
B 1 36  GLY 36  31  31  GLY GLY B . n 
B 1 37  ALA 37  32  32  ALA ALA B . n 
B 1 38  GLY 38  33  33  GLY GLY B . n 
B 1 39  GLY 39  34  34  GLY GLY B . n 
B 1 40  ALA 40  35  35  ALA ALA B . n 
B 1 41  ALA 41  36  36  ALA ALA B . n 
B 1 42  PRO 42  37  37  PRO PRO B . n 
B 1 43  HIS 43  38  38  HIS HIS B . n 
B 1 44  ILE 44  39  39  ILE ILE B . n 
B 1 45  THR 45  40  40  THR THR B . n 
B 1 46  HIS 46  41  41  HIS HIS B . n 
B 1 47  VAL 47  42  42  VAL VAL B . n 
B 1 48  PRO 48  43  43  PRO PRO B . n 
B 1 49  ILE 49  44  44  ILE ILE B . n 
B 1 50  ILE 50  45  45  ILE ILE B . n 
B 1 51  VAL 51  46  46  VAL VAL B . n 
B 1 52  ASP 52  47  47  ASP ASP B . n 
B 1 53  PRO 53  48  48  PRO PRO B . n 
B 1 54  GLU 54  49  49  GLU GLU B . n 
B 1 55  LEU 55  50  50  LEU LEU B . n 
B 1 56  ASP 56  51  51  ASP ASP B . n 
B 1 57  GLY 57  52  52  GLY GLY B . n 
B 1 58  PRO 58  53  53  PRO PRO B . n 
B 1 59  VAL 59  54  54  VAL VAL B . n 
B 1 60  ASP 60  55  55  ASP ASP B . n 
B 1 61  ARG 61  56  56  ARG ARG B . n 
B 1 62  LEU 62  57  57  LEU LEU B . n 
B 1 63  VAL 63  58  58  VAL VAL B . n 
B 1 64  GLY 64  59  59  GLY GLY B . n 
B 1 65  ILE 65  60  60  ILE ILE B . n 
B 1 66  THR 66  61  61  THR THR B . n 
B 1 67  LEU 67  62  62  LEU LEU B . n 
B 1 68  TRP 68  63  63  TRP TRP B . n 
B 1 69  GLY 69  64  64  GLY GLY B . n 
B 1 70  HIS 70  65  65  HIS HIS B . n 
B 1 71  MET 71  66  66  MET MET B . n 
B 1 72  ASN 72  67  67  ASN ASN B . n 
B 1 73  ARG 73  68  68  ARG ARG B . n 
B 1 74  ALA 74  69  69  ALA ALA B . n 
B 1 75  ASN 75  70  70  ASN ASN B . n 
B 1 76  PRO 76  71  71  PRO PRO B . n 
B 1 77  HIS 77  72  72  HIS HIS B . n 
B 1 78  TRP 78  73  73  TRP TRP B . n 
B 1 79  ALA 79  74  74  ALA ALA B . n 
B 1 80  ALA 80  75  75  ALA ALA B . n 
B 1 81  LEU 81  76  76  LEU LEU B . n 
B 1 82  GLY 82  77  77  GLY GLY B . n 
B 1 83  GLY 83  78  78  GLY GLY B . n 
B 1 84  ALA 84  79  79  ALA ALA B . n 
B 1 85  ALA 85  80  80  ALA ALA B . n 
B 1 86  ASN 86  81  81  ASN ASN B . n 
B 1 87  VAL 87  82  82  VAL VAL B . n 
B 1 88  VAL 88  83  83  VAL VAL B . n 
B 1 89  ALA 89  84  84  ALA ALA B . n 
B 1 90  THR 90  85  85  THR THR B . n 
B 1 91  PHE 91  86  86  PHE PHE B . n 
B 1 92  ALA 92  87  87  ALA ALA B . n 
B 1 93  GLY 93  88  88  GLY GLY B . n 
B 1 94  PRO 94  89  89  PRO PRO B . n 
B 1 95  ASN 95  90  90  ASN ASN B . n 
B 1 96  ALA 96  91  91  ALA ALA B . n 
B 1 97  TYR 97  92  92  TYR TYR B . n 
B 1 98  VAL 98  93  93  VAL VAL B . n 
B 1 99  SER 99  94  94  SER SER B . n 
B 1 100 PRO 100 95  95  PRO PRO B . n 
B 1 101 ALA 101 96  96  ALA ALA B . n 
B 1 102 VAL 102 97  97  VAL VAL B . n 
B 1 103 TYR 103 98  98  TYR TYR B . n 
B 1 104 ARG 104 99  99  ARG ARG B . n 
B 1 105 THR 105 100 100 THR THR B . n 
B 1 106 ALA 106 101 101 ALA ALA B . n 
B 1 107 PRO 107 102 102 PRO PRO B . n 
B 1 108 ALA 108 103 103 ALA ALA B . n 
B 1 109 ALA 109 104 104 ALA ALA B . n 
B 1 110 PRO 110 105 105 PRO PRO B . n 
B 1 111 THR 111 106 106 THR THR B . n 
B 1 112 TRP 112 107 107 TRP TRP B . n 
B 1 113 ASN 113 108 108 ASN ASN B . n 
B 1 114 PHE 114 109 109 PHE PHE B . n 
B 1 115 THR 115 110 110 THR THR B . n 
B 1 116 SER 116 111 111 SER SER B . n 
B 1 117 VAL 117 112 112 VAL VAL B . n 
B 1 118 GLN 118 113 113 GLN GLN B . n 
B 1 119 VAL 119 114 114 VAL VAL B . n 
B 1 120 ARG 120 115 115 ARG ARG B . n 
B 1 121 GLY 121 116 116 GLY GLY B . n 
B 1 122 GLU 122 117 117 GLU GLU B . n 
B 1 123 LEU 123 118 118 LEU LEU B . n 
B 1 124 ARG 124 119 119 ARG ARG B . n 
B 1 125 LYS 125 120 120 LYS LYS B . n 
B 1 126 VAL 126 121 121 VAL VAL B . n 
B 1 127 GLU 127 122 122 GLU GLU B . n 
B 1 128 SER 128 123 123 SER SER B . n 
B 1 129 ALA 129 124 124 ALA ALA B . n 
B 1 130 ASP 130 125 125 ASP ASP B . n 
B 1 131 ASP 131 126 126 ASP ASP B . n 
B 1 132 THR 132 127 127 THR THR B . n 
B 1 133 LEU 133 128 128 LEU LEU B . n 
B 1 134 ALA 134 129 129 ALA ALA B . n 
B 1 135 THR 135 130 130 THR THR B . n 
B 1 136 VAL 136 131 131 VAL VAL B . n 
B 1 137 ARG 137 132 132 ARG ARG B . n 
B 1 138 ALA 138 133 133 ALA ALA B . n 
B 1 139 THR 139 134 134 THR THR B . n 
B 1 140 VAL 140 135 135 VAL VAL B . n 
B 1 141 ALA 141 136 136 ALA ALA B . n 
B 1 142 ALA 142 137 137 ALA ALA B . n 
B 1 143 LEU 143 138 138 LEU LEU B . n 
B 1 144 GLU 144 139 139 GLU GLU B . n 
B 1 145 SER 145 140 140 SER SER B . n 
B 1 146 ARG 146 141 141 ARG ARG B . n 
B 1 147 PHE 147 142 142 PHE PHE B . n 
B 1 148 GLY 148 143 143 GLY GLY B . n 
B 1 149 ALA 149 144 144 ALA ALA B . n 
B 1 150 GLY 150 145 145 GLY GLY B . n 
B 1 151 TRP 151 146 146 TRP TRP B . n 
B 1 152 ASP 152 147 147 ASP ASP B . n 
B 1 153 MET 153 148 148 MET MET B . n 
B 1 154 THR 154 149 149 THR THR B . n 
B 1 155 GLY 155 150 150 GLY GLY B . n 
B 1 156 SER 156 151 151 SER SER B . n 
B 1 157 LEU 157 152 152 LEU LEU B . n 
B 1 158 ASP 158 153 153 ASP ASP B . n 
B 1 159 TYR 159 154 154 TYR TYR B . n 
B 1 160 PHE 160 155 155 PHE PHE B . n 
B 1 161 ARG 161 156 156 ARG ARG B . n 
B 1 162 ARG 162 157 157 ARG ARG B . n 
B 1 163 ILE 163 158 158 ILE ILE B . n 
B 1 164 LEU 164 159 159 LEU LEU B . n 
B 1 165 PRO 165 160 160 PRO PRO B . n 
B 1 166 GLY 166 161 161 GLY GLY B . n 
B 1 167 VAL 167 162 162 VAL VAL B . n 
B 1 168 GLY 168 163 163 GLY GLY B . n 
B 1 169 ALA 169 164 164 ALA ALA B . n 
B 1 170 PHE 170 165 165 PHE PHE B . n 
B 1 171 ARG 171 166 166 ARG ARG B . n 
B 1 172 LEU 172 167 167 LEU LEU B . n 
B 1 173 ARG 173 168 168 ARG ARG B . n 
B 1 174 VAL 174 169 169 VAL VAL B . n 
B 1 175 ALA 175 170 170 ALA ALA B . n 
B 1 176 GLU 176 171 171 GLU GLU B . n 
B 1 177 ALA 177 172 172 ALA ALA B . n 
B 1 178 ASP 178 173 173 ASP ASP B . n 
B 1 179 GLY 179 174 174 GLY GLY B . n 
B 1 180 MET 180 175 175 MET MET B . n 
B 1 181 PHE 181 176 176 PHE PHE B . n 
B 1 182 LYS 182 177 177 LYS LYS B . n 
B 1 183 LEU 183 178 178 LEU LEU B . n 
B 1 184 SER 184 179 179 SER SER B . n 
B 1 185 GLN 185 180 180 GLN GLN B . n 
B 1 186 GLU 186 181 181 GLU GLU B . n 
B 1 187 GLN 187 182 182 GLN GLN B . n 
B 1 188 GLN 188 183 183 GLN GLN B . n 
B 1 189 PRO 189 184 184 PRO PRO B . n 
B 1 190 ALA 190 185 185 ALA ALA B . n 
B 1 191 ILE 191 186 186 ILE ILE B . n 
B 1 192 ARG 192 187 187 ARG ARG B . n 
B 1 193 ARG 193 188 188 ARG ARG B . n 
B 1 194 ARG 194 189 189 ARG ARG B . n 
B 1 195 VAL 195 190 190 VAL VAL B . n 
B 1 196 ARG 196 191 191 ARG ARG B . n 
B 1 197 HIS 197 192 192 HIS HIS B . n 
B 1 198 SER 198 193 193 SER SER B . n 
B 1 199 PHE 199 194 194 PHE PHE B . n 
B 1 200 GLY 200 195 195 GLY GLY B . n 
B 1 201 GLY 201 196 196 GLY GLY B . n 
B 1 202 ALA 202 197 197 ALA ALA B . n 
B 1 203 GLU 203 198 198 GLU GLU B . n 
B 1 204 ALA 204 199 199 ALA ALA B . n 
B 1 205 THR 205 200 200 THR THR B . n 
B 1 206 ARG 206 201 201 ARG ARG B . n 
B 1 207 ALA 207 202 202 ALA ALA B . n 
B 1 208 VAL 208 203 203 VAL VAL B . n 
B 1 209 ALA 209 204 204 ALA ALA B . n 
B 1 210 GLY 210 205 205 GLY GLY B . n 
B 1 211 LEU 211 206 206 LEU LEU B . n 
B 1 212 MET 212 207 207 MET MET B . n 
B 1 213 ASP 213 208 208 ASP ASP B . n 
B 1 214 ARG 214 209 209 ARG ARG B . n 
B 1 215 LEU 215 210 210 LEU LEU B . n 
B 1 216 PRO 216 211 211 PRO PRO B . n 
B 1 217 THR 217 212 ?   ?   ?   B . n 
B 1 218 GLU 218 213 ?   ?   ?   B . n 
C 1 1   ALA 1   -4  ?   ?   ?   C . n 
C 1 2   GLY 2   -3  ?   ?   ?   C . n 
C 1 3   ALA 3   -2  ?   ?   ?   C . n 
C 1 4   GLY 4   -1  -1  GLY GLY C . n 
C 1 5   ALA 5   0   0   ALA ALA C . n 
C 1 6   MET 6   1   1   MET MET C . n 
C 1 7   PHE 7   2   2   PHE PHE C . n 
C 1 8   VAL 8   3   3   VAL VAL C . n 
C 1 9   PRO 9   4   4   PRO PRO C . n 
C 1 10  GLY 10  5   5   GLY GLY C . n 
C 1 11  PRO 11  6   6   PRO PRO C . n 
C 1 12  TYR 12  7   7   TYR TYR C . n 
C 1 13  HIS 13  8   8   HIS HIS C . n 
C 1 14  ALA 14  9   9   ALA ALA C . n 
C 1 15  PRO 15  10  10  PRO PRO C . n 
C 1 16  GLU 16  11  11  GLU GLU C . n 
C 1 17  ASP 17  12  12  ASP ASP C . n 
C 1 18  ARG 18  13  13  ARG ARG C . n 
C 1 19  TRP 19  14  14  TRP TRP C . n 
C 1 20  LEU 20  15  15  LEU LEU C . n 
C 1 21  VAL 21  16  16  VAL VAL C . n 
C 1 22  ASP 22  17  17  ASP ASP C . n 
C 1 23  LEU 23  18  18  LEU LEU C . n 
C 1 24  VAL 24  19  19  VAL VAL C . n 
C 1 25  ARG 25  20  20  ARG ARG C . n 
C 1 26  GLY 26  21  21  GLY GLY C . n 
C 1 27  HIS 27  22  22  HIS HIS C . n 
C 1 28  PRO 28  23  23  PRO PRO C . n 
C 1 29  LEU 29  24  24  LEU LEU C . n 
C 1 30  ALA 30  25  25  ALA ALA C . n 
C 1 31  GLN 31  26  26  GLN GLN C . n 
C 1 32  LEU 32  27  27  LEU LEU C . n 
C 1 33  ALA 33  28  28  ALA ALA C . n 
C 1 34  SER 34  29  29  SER SER C . n 
C 1 35  ASN 35  30  30  ASN ASN C . n 
C 1 36  GLY 36  31  31  GLY GLY C . n 
C 1 37  ALA 37  32  32  ALA ALA C . n 
C 1 38  GLY 38  33  33  GLY GLY C . n 
C 1 39  GLY 39  34  34  GLY GLY C . n 
C 1 40  ALA 40  35  35  ALA ALA C . n 
C 1 41  ALA 41  36  36  ALA ALA C . n 
C 1 42  PRO 42  37  37  PRO PRO C . n 
C 1 43  HIS 43  38  38  HIS HIS C . n 
C 1 44  ILE 44  39  39  ILE ILE C . n 
C 1 45  THR 45  40  40  THR THR C . n 
C 1 46  HIS 46  41  41  HIS HIS C . n 
C 1 47  VAL 47  42  42  VAL VAL C . n 
C 1 48  PRO 48  43  43  PRO PRO C . n 
C 1 49  ILE 49  44  44  ILE ILE C . n 
C 1 50  ILE 50  45  45  ILE ILE C . n 
C 1 51  VAL 51  46  46  VAL VAL C . n 
C 1 52  ASP 52  47  47  ASP ASP C . n 
C 1 53  PRO 53  48  48  PRO PRO C . n 
C 1 54  GLU 54  49  49  GLU GLU C . n 
C 1 55  LEU 55  50  50  LEU LEU C . n 
C 1 56  ASP 56  51  51  ASP ASP C . n 
C 1 57  GLY 57  52  52  GLY GLY C . n 
C 1 58  PRO 58  53  53  PRO PRO C . n 
C 1 59  VAL 59  54  54  VAL VAL C . n 
C 1 60  ASP 60  55  55  ASP ASP C . n 
C 1 61  ARG 61  56  56  ARG ARG C . n 
C 1 62  LEU 62  57  57  LEU LEU C . n 
C 1 63  VAL 63  58  58  VAL VAL C . n 
C 1 64  GLY 64  59  59  GLY GLY C . n 
C 1 65  ILE 65  60  60  ILE ILE C . n 
C 1 66  THR 66  61  61  THR THR C . n 
C 1 67  LEU 67  62  62  LEU LEU C . n 
C 1 68  TRP 68  63  63  TRP TRP C . n 
C 1 69  GLY 69  64  64  GLY GLY C . n 
C 1 70  HIS 70  65  65  HIS HIS C . n 
C 1 71  MET 71  66  66  MET MET C . n 
C 1 72  ASN 72  67  67  ASN ASN C . n 
C 1 73  ARG 73  68  68  ARG ARG C . n 
C 1 74  ALA 74  69  69  ALA ALA C . n 
C 1 75  ASN 75  70  70  ASN ASN C . n 
C 1 76  PRO 76  71  71  PRO PRO C . n 
C 1 77  HIS 77  72  72  HIS HIS C . n 
C 1 78  TRP 78  73  73  TRP TRP C . n 
C 1 79  ALA 79  74  74  ALA ALA C . n 
C 1 80  ALA 80  75  75  ALA ALA C . n 
C 1 81  LEU 81  76  76  LEU LEU C . n 
C 1 82  GLY 82  77  77  GLY GLY C . n 
C 1 83  GLY 83  78  78  GLY GLY C . n 
C 1 84  ALA 84  79  79  ALA ALA C . n 
C 1 85  ALA 85  80  80  ALA ALA C . n 
C 1 86  ASN 86  81  81  ASN ASN C . n 
C 1 87  VAL 87  82  82  VAL VAL C . n 
C 1 88  VAL 88  83  83  VAL VAL C . n 
C 1 89  ALA 89  84  84  ALA ALA C . n 
C 1 90  THR 90  85  85  THR THR C . n 
C 1 91  PHE 91  86  86  PHE PHE C . n 
C 1 92  ALA 92  87  87  ALA ALA C . n 
C 1 93  GLY 93  88  88  GLY GLY C . n 
C 1 94  PRO 94  89  89  PRO PRO C . n 
C 1 95  ASN 95  90  90  ASN ASN C . n 
C 1 96  ALA 96  91  91  ALA ALA C . n 
C 1 97  TYR 97  92  92  TYR TYR C . n 
C 1 98  VAL 98  93  93  VAL VAL C . n 
C 1 99  SER 99  94  94  SER SER C . n 
C 1 100 PRO 100 95  95  PRO PRO C . n 
C 1 101 ALA 101 96  96  ALA ALA C . n 
C 1 102 VAL 102 97  97  VAL VAL C . n 
C 1 103 TYR 103 98  98  TYR TYR C . n 
C 1 104 ARG 104 99  99  ARG ARG C . n 
C 1 105 THR 105 100 100 THR THR C . n 
C 1 106 ALA 106 101 101 ALA ALA C . n 
C 1 107 PRO 107 102 102 PRO PRO C . n 
C 1 108 ALA 108 103 103 ALA ALA C . n 
C 1 109 ALA 109 104 104 ALA ALA C . n 
C 1 110 PRO 110 105 105 PRO PRO C . n 
C 1 111 THR 111 106 106 THR THR C . n 
C 1 112 TRP 112 107 107 TRP TRP C . n 
C 1 113 ASN 113 108 108 ASN ASN C . n 
C 1 114 PHE 114 109 109 PHE PHE C . n 
C 1 115 THR 115 110 110 THR THR C . n 
C 1 116 SER 116 111 111 SER SER C . n 
C 1 117 VAL 117 112 112 VAL VAL C . n 
C 1 118 GLN 118 113 113 GLN GLN C . n 
C 1 119 VAL 119 114 114 VAL VAL C . n 
C 1 120 ARG 120 115 115 ARG ARG C . n 
C 1 121 GLY 121 116 116 GLY GLY C . n 
C 1 122 GLU 122 117 117 GLU GLU C . n 
C 1 123 LEU 123 118 118 LEU LEU C . n 
C 1 124 ARG 124 119 119 ARG ARG C . n 
C 1 125 LYS 125 120 120 LYS LYS C . n 
C 1 126 VAL 126 121 121 VAL VAL C . n 
C 1 127 GLU 127 122 122 GLU GLU C . n 
C 1 128 SER 128 123 123 SER SER C . n 
C 1 129 ALA 129 124 124 ALA ALA C . n 
C 1 130 ASP 130 125 125 ASP ASP C . n 
C 1 131 ASP 131 126 126 ASP ASP C . n 
C 1 132 THR 132 127 127 THR THR C . n 
C 1 133 LEU 133 128 128 LEU LEU C . n 
C 1 134 ALA 134 129 129 ALA ALA C . n 
C 1 135 THR 135 130 130 THR THR C . n 
C 1 136 VAL 136 131 131 VAL VAL C . n 
C 1 137 ARG 137 132 132 ARG ARG C . n 
C 1 138 ALA 138 133 133 ALA ALA C . n 
C 1 139 THR 139 134 134 THR THR C . n 
C 1 140 VAL 140 135 135 VAL VAL C . n 
C 1 141 ALA 141 136 136 ALA ALA C . n 
C 1 142 ALA 142 137 137 ALA ALA C . n 
C 1 143 LEU 143 138 138 LEU LEU C . n 
C 1 144 GLU 144 139 139 GLU GLU C . n 
C 1 145 SER 145 140 140 SER SER C . n 
C 1 146 ARG 146 141 141 ARG ARG C . n 
C 1 147 PHE 147 142 142 PHE PHE C . n 
C 1 148 GLY 148 143 143 GLY GLY C . n 
C 1 149 ALA 149 144 144 ALA ALA C . n 
C 1 150 GLY 150 145 145 GLY GLY C . n 
C 1 151 TRP 151 146 146 TRP TRP C . n 
C 1 152 ASP 152 147 147 ASP ASP C . n 
C 1 153 MET 153 148 148 MET MET C . n 
C 1 154 THR 154 149 149 THR THR C . n 
C 1 155 GLY 155 150 150 GLY GLY C . n 
C 1 156 SER 156 151 151 SER SER C . n 
C 1 157 LEU 157 152 152 LEU LEU C . n 
C 1 158 ASP 158 153 153 ASP ASP C . n 
C 1 159 TYR 159 154 154 TYR TYR C . n 
C 1 160 PHE 160 155 155 PHE PHE C . n 
C 1 161 ARG 161 156 156 ARG ARG C . n 
C 1 162 ARG 162 157 157 ARG ARG C . n 
C 1 163 ILE 163 158 158 ILE ILE C . n 
C 1 164 LEU 164 159 159 LEU LEU C . n 
C 1 165 PRO 165 160 160 PRO PRO C . n 
C 1 166 GLY 166 161 161 GLY GLY C . n 
C 1 167 VAL 167 162 162 VAL VAL C . n 
C 1 168 GLY 168 163 163 GLY GLY C . n 
C 1 169 ALA 169 164 164 ALA ALA C . n 
C 1 170 PHE 170 165 165 PHE PHE C . n 
C 1 171 ARG 171 166 166 ARG ARG C . n 
C 1 172 LEU 172 167 167 LEU LEU C . n 
C 1 173 ARG 173 168 168 ARG ARG C . n 
C 1 174 VAL 174 169 169 VAL VAL C . n 
C 1 175 ALA 175 170 170 ALA ALA C . n 
C 1 176 GLU 176 171 171 GLU GLU C . n 
C 1 177 ALA 177 172 172 ALA ALA C . n 
C 1 178 ASP 178 173 173 ASP ASP C . n 
C 1 179 GLY 179 174 174 GLY GLY C . n 
C 1 180 MET 180 175 175 MET MET C . n 
C 1 181 PHE 181 176 176 PHE PHE C . n 
C 1 182 LYS 182 177 177 LYS LYS C . n 
C 1 183 LEU 183 178 178 LEU LEU C . n 
C 1 184 SER 184 179 179 SER SER C . n 
C 1 185 GLN 185 180 180 GLN GLN C . n 
C 1 186 GLU 186 181 181 GLU GLU C . n 
C 1 187 GLN 187 182 182 GLN GLN C . n 
C 1 188 GLN 188 183 183 GLN GLN C . n 
C 1 189 PRO 189 184 184 PRO PRO C . n 
C 1 190 ALA 190 185 185 ALA ALA C . n 
C 1 191 ILE 191 186 186 ILE ILE C . n 
C 1 192 ARG 192 187 187 ARG ARG C . n 
C 1 193 ARG 193 188 188 ARG ARG C . n 
C 1 194 ARG 194 189 189 ARG ARG C . n 
C 1 195 VAL 195 190 190 VAL VAL C . n 
C 1 196 ARG 196 191 191 ARG ARG C . n 
C 1 197 HIS 197 192 192 HIS HIS C . n 
C 1 198 SER 198 193 193 SER SER C . n 
C 1 199 PHE 199 194 194 PHE PHE C . n 
C 1 200 GLY 200 195 195 GLY GLY C . n 
C 1 201 GLY 201 196 196 GLY GLY C . n 
C 1 202 ALA 202 197 197 ALA ALA C . n 
C 1 203 GLU 203 198 198 GLU GLU C . n 
C 1 204 ALA 204 199 199 ALA ALA C . n 
C 1 205 THR 205 200 200 THR THR C . n 
C 1 206 ARG 206 201 201 ARG ARG C . n 
C 1 207 ALA 207 202 202 ALA ALA C . n 
C 1 208 VAL 208 203 203 VAL VAL C . n 
C 1 209 ALA 209 204 204 ALA ALA C . n 
C 1 210 GLY 210 205 205 GLY GLY C . n 
C 1 211 LEU 211 206 206 LEU LEU C . n 
C 1 212 MET 212 207 207 MET MET C . n 
C 1 213 ASP 213 208 208 ASP ASP C . n 
C 1 214 ARG 214 209 209 ARG ARG C . n 
C 1 215 LEU 215 210 210 LEU LEU C . n 
C 1 216 PRO 216 211 211 PRO PRO C . n 
C 1 217 THR 217 212 ?   ?   ?   C . n 
C 1 218 GLU 218 213 ?   ?   ?   C . n 
D 1 1   ALA 1   -4  ?   ?   ?   D . n 
D 1 2   GLY 2   -3  ?   ?   ?   D . n 
D 1 3   ALA 3   -2  ?   ?   ?   D . n 
D 1 4   GLY 4   -1  -1  GLY GLY D . n 
D 1 5   ALA 5   0   0   ALA ALA D . n 
D 1 6   MET 6   1   1   MET MET D . n 
D 1 7   PHE 7   2   2   PHE PHE D . n 
D 1 8   VAL 8   3   3   VAL VAL D . n 
D 1 9   PRO 9   4   4   PRO PRO D . n 
D 1 10  GLY 10  5   5   GLY GLY D . n 
D 1 11  PRO 11  6   6   PRO PRO D . n 
D 1 12  TYR 12  7   7   TYR TYR D . n 
D 1 13  HIS 13  8   8   HIS HIS D . n 
D 1 14  ALA 14  9   9   ALA ALA D . n 
D 1 15  PRO 15  10  10  PRO PRO D . n 
D 1 16  GLU 16  11  11  GLU GLU D . n 
D 1 17  ASP 17  12  12  ASP ASP D . n 
D 1 18  ARG 18  13  13  ARG ARG D . n 
D 1 19  TRP 19  14  14  TRP TRP D . n 
D 1 20  LEU 20  15  15  LEU LEU D . n 
D 1 21  VAL 21  16  16  VAL VAL D . n 
D 1 22  ASP 22  17  17  ASP ASP D . n 
D 1 23  LEU 23  18  18  LEU LEU D . n 
D 1 24  VAL 24  19  19  VAL VAL D . n 
D 1 25  ARG 25  20  20  ARG ARG D . n 
D 1 26  GLY 26  21  21  GLY GLY D . n 
D 1 27  HIS 27  22  22  HIS HIS D . n 
D 1 28  PRO 28  23  23  PRO PRO D . n 
D 1 29  LEU 29  24  24  LEU LEU D . n 
D 1 30  ALA 30  25  25  ALA ALA D . n 
D 1 31  GLN 31  26  26  GLN GLN D . n 
D 1 32  LEU 32  27  27  LEU LEU D . n 
D 1 33  ALA 33  28  28  ALA ALA D . n 
D 1 34  SER 34  29  29  SER SER D . n 
D 1 35  ASN 35  30  30  ASN ASN D . n 
D 1 36  GLY 36  31  31  GLY GLY D . n 
D 1 37  ALA 37  32  32  ALA ALA D . n 
D 1 38  GLY 38  33  33  GLY GLY D . n 
D 1 39  GLY 39  34  34  GLY GLY D . n 
D 1 40  ALA 40  35  35  ALA ALA D . n 
D 1 41  ALA 41  36  36  ALA ALA D . n 
D 1 42  PRO 42  37  37  PRO PRO D . n 
D 1 43  HIS 43  38  38  HIS HIS D . n 
D 1 44  ILE 44  39  39  ILE ILE D . n 
D 1 45  THR 45  40  40  THR THR D . n 
D 1 46  HIS 46  41  41  HIS HIS D . n 
D 1 47  VAL 47  42  42  VAL VAL D . n 
D 1 48  PRO 48  43  43  PRO PRO D . n 
D 1 49  ILE 49  44  44  ILE ILE D . n 
D 1 50  ILE 50  45  45  ILE ILE D . n 
D 1 51  VAL 51  46  46  VAL VAL D . n 
D 1 52  ASP 52  47  47  ASP ASP D . n 
D 1 53  PRO 53  48  48  PRO PRO D . n 
D 1 54  GLU 54  49  49  GLU GLU D . n 
D 1 55  LEU 55  50  50  LEU LEU D . n 
D 1 56  ASP 56  51  51  ASP ASP D . n 
D 1 57  GLY 57  52  52  GLY GLY D . n 
D 1 58  PRO 58  53  53  PRO PRO D . n 
D 1 59  VAL 59  54  54  VAL VAL D . n 
D 1 60  ASP 60  55  55  ASP ASP D . n 
D 1 61  ARG 61  56  56  ARG ARG D . n 
D 1 62  LEU 62  57  57  LEU LEU D . n 
D 1 63  VAL 63  58  58  VAL VAL D . n 
D 1 64  GLY 64  59  59  GLY GLY D . n 
D 1 65  ILE 65  60  60  ILE ILE D . n 
D 1 66  THR 66  61  61  THR THR D . n 
D 1 67  LEU 67  62  62  LEU LEU D . n 
D 1 68  TRP 68  63  63  TRP TRP D . n 
D 1 69  GLY 69  64  64  GLY GLY D . n 
D 1 70  HIS 70  65  65  HIS HIS D . n 
D 1 71  MET 71  66  66  MET MET D . n 
D 1 72  ASN 72  67  67  ASN ASN D . n 
D 1 73  ARG 73  68  68  ARG ARG D . n 
D 1 74  ALA 74  69  69  ALA ALA D . n 
D 1 75  ASN 75  70  70  ASN ASN D . n 
D 1 76  PRO 76  71  71  PRO PRO D . n 
D 1 77  HIS 77  72  72  HIS HIS D . n 
D 1 78  TRP 78  73  73  TRP TRP D . n 
D 1 79  ALA 79  74  74  ALA ALA D . n 
D 1 80  ALA 80  75  75  ALA ALA D . n 
D 1 81  LEU 81  76  76  LEU LEU D . n 
D 1 82  GLY 82  77  77  GLY GLY D . n 
D 1 83  GLY 83  78  78  GLY GLY D . n 
D 1 84  ALA 84  79  79  ALA ALA D . n 
D 1 85  ALA 85  80  80  ALA ALA D . n 
D 1 86  ASN 86  81  81  ASN ASN D . n 
D 1 87  VAL 87  82  82  VAL VAL D . n 
D 1 88  VAL 88  83  83  VAL VAL D . n 
D 1 89  ALA 89  84  84  ALA ALA D . n 
D 1 90  THR 90  85  85  THR THR D . n 
D 1 91  PHE 91  86  86  PHE PHE D . n 
D 1 92  ALA 92  87  87  ALA ALA D . n 
D 1 93  GLY 93  88  88  GLY GLY D . n 
D 1 94  PRO 94  89  89  PRO PRO D . n 
D 1 95  ASN 95  90  90  ASN ASN D . n 
D 1 96  ALA 96  91  91  ALA ALA D . n 
D 1 97  TYR 97  92  92  TYR TYR D . n 
D 1 98  VAL 98  93  93  VAL VAL D . n 
D 1 99  SER 99  94  94  SER SER D . n 
D 1 100 PRO 100 95  95  PRO PRO D . n 
D 1 101 ALA 101 96  96  ALA ALA D . n 
D 1 102 VAL 102 97  97  VAL VAL D . n 
D 1 103 TYR 103 98  98  TYR TYR D . n 
D 1 104 ARG 104 99  99  ARG ARG D . n 
D 1 105 THR 105 100 100 THR THR D . n 
D 1 106 ALA 106 101 101 ALA ALA D . n 
D 1 107 PRO 107 102 102 PRO PRO D . n 
D 1 108 ALA 108 103 103 ALA ALA D . n 
D 1 109 ALA 109 104 104 ALA ALA D . n 
D 1 110 PRO 110 105 105 PRO PRO D . n 
D 1 111 THR 111 106 106 THR THR D . n 
D 1 112 TRP 112 107 107 TRP TRP D . n 
D 1 113 ASN 113 108 108 ASN ASN D . n 
D 1 114 PHE 114 109 109 PHE PHE D . n 
D 1 115 THR 115 110 110 THR THR D . n 
D 1 116 SER 116 111 111 SER SER D . n 
D 1 117 VAL 117 112 112 VAL VAL D . n 
D 1 118 GLN 118 113 113 GLN GLN D . n 
D 1 119 VAL 119 114 114 VAL VAL D . n 
D 1 120 ARG 120 115 115 ARG ARG D . n 
D 1 121 GLY 121 116 116 GLY GLY D . n 
D 1 122 GLU 122 117 117 GLU GLU D . n 
D 1 123 LEU 123 118 118 LEU LEU D . n 
D 1 124 ARG 124 119 119 ARG ARG D . n 
D 1 125 LYS 125 120 120 LYS LYS D . n 
D 1 126 VAL 126 121 121 VAL VAL D . n 
D 1 127 GLU 127 122 122 GLU GLU D . n 
D 1 128 SER 128 123 123 SER SER D . n 
D 1 129 ALA 129 124 124 ALA ALA D . n 
D 1 130 ASP 130 125 125 ASP ASP D . n 
D 1 131 ASP 131 126 126 ASP ASP D . n 
D 1 132 THR 132 127 127 THR THR D . n 
D 1 133 LEU 133 128 128 LEU LEU D . n 
D 1 134 ALA 134 129 129 ALA ALA D . n 
D 1 135 THR 135 130 130 THR THR D . n 
D 1 136 VAL 136 131 131 VAL VAL D . n 
D 1 137 ARG 137 132 132 ARG ARG D . n 
D 1 138 ALA 138 133 133 ALA ALA D . n 
D 1 139 THR 139 134 134 THR THR D . n 
D 1 140 VAL 140 135 135 VAL VAL D . n 
D 1 141 ALA 141 136 136 ALA ALA D . n 
D 1 142 ALA 142 137 137 ALA ALA D . n 
D 1 143 LEU 143 138 138 LEU LEU D . n 
D 1 144 GLU 144 139 139 GLU GLU D . n 
D 1 145 SER 145 140 140 SER SER D . n 
D 1 146 ARG 146 141 141 ARG ARG D . n 
D 1 147 PHE 147 142 142 PHE PHE D . n 
D 1 148 GLY 148 143 143 GLY GLY D . n 
D 1 149 ALA 149 144 144 ALA ALA D . n 
D 1 150 GLY 150 145 145 GLY GLY D . n 
D 1 151 TRP 151 146 146 TRP TRP D . n 
D 1 152 ASP 152 147 147 ASP ASP D . n 
D 1 153 MET 153 148 148 MET MET D . n 
D 1 154 THR 154 149 149 THR THR D . n 
D 1 155 GLY 155 150 150 GLY GLY D . n 
D 1 156 SER 156 151 151 SER SER D . n 
D 1 157 LEU 157 152 152 LEU LEU D . n 
D 1 158 ASP 158 153 153 ASP ASP D . n 
D 1 159 TYR 159 154 154 TYR TYR D . n 
D 1 160 PHE 160 155 155 PHE PHE D . n 
D 1 161 ARG 161 156 156 ARG ARG D . n 
D 1 162 ARG 162 157 157 ARG ARG D . n 
D 1 163 ILE 163 158 158 ILE ILE D . n 
D 1 164 LEU 164 159 159 LEU LEU D . n 
D 1 165 PRO 165 160 160 PRO PRO D . n 
D 1 166 GLY 166 161 161 GLY GLY D . n 
D 1 167 VAL 167 162 162 VAL VAL D . n 
D 1 168 GLY 168 163 163 GLY GLY D . n 
D 1 169 ALA 169 164 164 ALA ALA D . n 
D 1 170 PHE 170 165 165 PHE PHE D . n 
D 1 171 ARG 171 166 166 ARG ARG D . n 
D 1 172 LEU 172 167 167 LEU LEU D . n 
D 1 173 ARG 173 168 168 ARG ARG D . n 
D 1 174 VAL 174 169 169 VAL VAL D . n 
D 1 175 ALA 175 170 170 ALA ALA D . n 
D 1 176 GLU 176 171 171 GLU GLU D . n 
D 1 177 ALA 177 172 172 ALA ALA D . n 
D 1 178 ASP 178 173 173 ASP ASP D . n 
D 1 179 GLY 179 174 174 GLY GLY D . n 
D 1 180 MET 180 175 175 MET MET D . n 
D 1 181 PHE 181 176 176 PHE PHE D . n 
D 1 182 LYS 182 177 177 LYS LYS D . n 
D 1 183 LEU 183 178 178 LEU LEU D . n 
D 1 184 SER 184 179 179 SER SER D . n 
D 1 185 GLN 185 180 180 GLN GLN D . n 
D 1 186 GLU 186 181 181 GLU GLU D . n 
D 1 187 GLN 187 182 182 GLN GLN D . n 
D 1 188 GLN 188 183 183 GLN GLN D . n 
D 1 189 PRO 189 184 184 PRO PRO D . n 
D 1 190 ALA 190 185 185 ALA ALA D . n 
D 1 191 ILE 191 186 186 ILE ILE D . n 
D 1 192 ARG 192 187 187 ARG ARG D . n 
D 1 193 ARG 193 188 188 ARG ARG D . n 
D 1 194 ARG 194 189 189 ARG ARG D . n 
D 1 195 VAL 195 190 190 VAL VAL D . n 
D 1 196 ARG 196 191 191 ARG ARG D . n 
D 1 197 HIS 197 192 192 HIS HIS D . n 
D 1 198 SER 198 193 193 SER SER D . n 
D 1 199 PHE 199 194 194 PHE PHE D . n 
D 1 200 GLY 200 195 195 GLY GLY D . n 
D 1 201 GLY 201 196 196 GLY GLY D . n 
D 1 202 ALA 202 197 197 ALA ALA D . n 
D 1 203 GLU 203 198 198 GLU GLU D . n 
D 1 204 ALA 204 199 199 ALA ALA D . n 
D 1 205 THR 205 200 200 THR THR D . n 
D 1 206 ARG 206 201 201 ARG ARG D . n 
D 1 207 ALA 207 202 202 ALA ALA D . n 
D 1 208 VAL 208 203 203 VAL VAL D . n 
D 1 209 ALA 209 204 204 ALA ALA D . n 
D 1 210 GLY 210 205 205 GLY GLY D . n 
D 1 211 LEU 211 206 206 LEU LEU D . n 
D 1 212 MET 212 207 207 MET MET D . n 
D 1 213 ASP 213 208 208 ASP ASP D . n 
D 1 214 ARG 214 209 209 ARG ARG D . n 
D 1 215 LEU 215 210 210 LEU LEU D . n 
D 1 216 PRO 216 211 211 PRO PRO D . n 
D 1 217 THR 217 212 ?   ?   ?   D . n 
D 1 218 GLU 218 213 ?   ?   ?   D . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        ONH 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   ONH 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
E 2 HEM 1   301 1   HEM HEM A . 
F 3 ONH 1   302 2   ONH DRG A . 
G 2 HEM 1   301 2   HEM HEM B . 
H 2 HEM 1   301 3   HEM HEM C . 
I 3 ONH 1   302 1   ONH DRG C . 
J 2 HEM 1   301 4   HEM HEM D . 
K 4 HOH 1   401 725 HOH HOH A . 
K 4 HOH 2   402 368 HOH HOH A . 
K 4 HOH 3   403 737 HOH HOH A . 
K 4 HOH 4   404 663 HOH HOH A . 
K 4 HOH 5   405 651 HOH HOH A . 
K 4 HOH 6   406 52  HOH HOH A . 
K 4 HOH 7   407 395 HOH HOH A . 
K 4 HOH 8   408 695 HOH HOH A . 
K 4 HOH 9   409 252 HOH HOH A . 
K 4 HOH 10  410 404 HOH HOH A . 
K 4 HOH 11  411 536 HOH HOH A . 
K 4 HOH 12  412 78  HOH HOH A . 
K 4 HOH 13  413 53  HOH HOH A . 
K 4 HOH 14  414 382 HOH HOH A . 
K 4 HOH 15  415 422 HOH HOH A . 
K 4 HOH 16  416 596 HOH HOH A . 
K 4 HOH 17  417 742 HOH HOH A . 
K 4 HOH 18  418 391 HOH HOH A . 
K 4 HOH 19  419 220 HOH HOH A . 
K 4 HOH 20  420 712 HOH HOH A . 
K 4 HOH 21  421 534 HOH HOH A . 
K 4 HOH 22  422 364 HOH HOH A . 
K 4 HOH 23  423 545 HOH HOH A . 
K 4 HOH 24  424 11  HOH HOH A . 
K 4 HOH 25  425 280 HOH HOH A . 
K 4 HOH 26  426 46  HOH HOH A . 
K 4 HOH 27  427 390 HOH HOH A . 
K 4 HOH 28  428 700 HOH HOH A . 
K 4 HOH 29  429 94  HOH HOH A . 
K 4 HOH 30  430 627 HOH HOH A . 
K 4 HOH 31  431 42  HOH HOH A . 
K 4 HOH 32  432 643 HOH HOH A . 
K 4 HOH 33  433 121 HOH HOH A . 
K 4 HOH 34  434 130 HOH HOH A . 
K 4 HOH 35  435 262 HOH HOH A . 
K 4 HOH 36  436 660 HOH HOH A . 
K 4 HOH 37  437 423 HOH HOH A . 
K 4 HOH 38  438 145 HOH HOH A . 
K 4 HOH 39  439 170 HOH HOH A . 
K 4 HOH 40  440 182 HOH HOH A . 
K 4 HOH 41  441 266 HOH HOH A . 
K 4 HOH 42  442 70  HOH HOH A . 
K 4 HOH 43  443 153 HOH HOH A . 
K 4 HOH 44  444 260 HOH HOH A . 
K 4 HOH 45  445 523 HOH HOH A . 
K 4 HOH 46  446 641 HOH HOH A . 
K 4 HOH 47  447 169 HOH HOH A . 
K 4 HOH 48  448 516 HOH HOH A . 
K 4 HOH 49  449 68  HOH HOH A . 
K 4 HOH 50  450 92  HOH HOH A . 
K 4 HOH 51  451 201 HOH HOH A . 
K 4 HOH 52  452 533 HOH HOH A . 
K 4 HOH 53  453 709 HOH HOH A . 
K 4 HOH 54  454 698 HOH HOH A . 
K 4 HOH 55  455 45  HOH HOH A . 
K 4 HOH 56  456 193 HOH HOH A . 
K 4 HOH 57  457 665 HOH HOH A . 
K 4 HOH 58  458 60  HOH HOH A . 
K 4 HOH 59  459 80  HOH HOH A . 
K 4 HOH 60  460 27  HOH HOH A . 
K 4 HOH 61  461 745 HOH HOH A . 
K 4 HOH 62  462 528 HOH HOH A . 
K 4 HOH 63  463 54  HOH HOH A . 
K 4 HOH 64  464 158 HOH HOH A . 
K 4 HOH 65  465 216 HOH HOH A . 
K 4 HOH 66  466 606 HOH HOH A . 
K 4 HOH 67  467 119 HOH HOH A . 
K 4 HOH 68  468 88  HOH HOH A . 
K 4 HOH 69  469 681 HOH HOH A . 
K 4 HOH 70  470 661 HOH HOH A . 
K 4 HOH 71  471 168 HOH HOH A . 
K 4 HOH 72  472 198 HOH HOH A . 
K 4 HOH 73  473 85  HOH HOH A . 
K 4 HOH 74  474 666 HOH HOH A . 
K 4 HOH 75  475 251 HOH HOH A . 
K 4 HOH 76  476 659 HOH HOH A . 
K 4 HOH 77  477 279 HOH HOH A . 
K 4 HOH 78  478 161 HOH HOH A . 
K 4 HOH 79  479 56  HOH HOH A . 
K 4 HOH 80  480 7   HOH HOH A . 
K 4 HOH 81  481 306 HOH HOH A . 
K 4 HOH 82  482 115 HOH HOH A . 
K 4 HOH 83  483 105 HOH HOH A . 
K 4 HOH 84  484 693 HOH HOH A . 
K 4 HOH 85  485 714 HOH HOH A . 
K 4 HOH 86  486 66  HOH HOH A . 
K 4 HOH 87  487 35  HOH HOH A . 
K 4 HOH 88  488 222 HOH HOH A . 
K 4 HOH 89  489 199 HOH HOH A . 
K 4 HOH 90  490 181 HOH HOH A . 
K 4 HOH 91  491 81  HOH HOH A . 
K 4 HOH 92  492 692 HOH HOH A . 
K 4 HOH 93  493 230 HOH HOH A . 
K 4 HOH 94  494 520 HOH HOH A . 
K 4 HOH 95  495 144 HOH HOH A . 
K 4 HOH 96  496 412 HOH HOH A . 
K 4 HOH 97  497 318 HOH HOH A . 
K 4 HOH 98  498 3   HOH HOH A . 
K 4 HOH 99  499 372 HOH HOH A . 
K 4 HOH 100 500 394 HOH HOH A . 
K 4 HOH 101 501 728 HOH HOH A . 
K 4 HOH 102 502 374 HOH HOH A . 
K 4 HOH 103 503 264 HOH HOH A . 
K 4 HOH 104 504 245 HOH HOH A . 
K 4 HOH 105 505 270 HOH HOH A . 
K 4 HOH 106 506 135 HOH HOH A . 
K 4 HOH 107 507 28  HOH HOH A . 
K 4 HOH 108 508 63  HOH HOH A . 
K 4 HOH 109 509 538 HOH HOH A . 
K 4 HOH 110 510 239 HOH HOH A . 
K 4 HOH 111 511 718 HOH HOH A . 
K 4 HOH 112 512 624 HOH HOH A . 
K 4 HOH 113 513 679 HOH HOH A . 
K 4 HOH 114 514 625 HOH HOH A . 
K 4 HOH 115 515 615 HOH HOH A . 
K 4 HOH 116 516 517 HOH HOH A . 
K 4 HOH 117 517 258 HOH HOH A . 
K 4 HOH 118 518 21  HOH HOH A . 
K 4 HOH 119 519 131 HOH HOH A . 
K 4 HOH 120 520 747 HOH HOH A . 
K 4 HOH 121 521 250 HOH HOH A . 
K 4 HOH 122 522 148 HOH HOH A . 
K 4 HOH 123 523 197 HOH HOH A . 
K 4 HOH 124 524 426 HOH HOH A . 
K 4 HOH 125 525 29  HOH HOH A . 
K 4 HOH 126 526 59  HOH HOH A . 
K 4 HOH 127 527 154 HOH HOH A . 
K 4 HOH 128 528 8   HOH HOH A . 
K 4 HOH 129 529 226 HOH HOH A . 
K 4 HOH 130 530 406 HOH HOH A . 
K 4 HOH 131 531 223 HOH HOH A . 
K 4 HOH 132 532 506 HOH HOH A . 
K 4 HOH 133 533 196 HOH HOH A . 
K 4 HOH 134 534 336 HOH HOH A . 
K 4 HOH 135 535 332 HOH HOH A . 
K 4 HOH 136 536 674 HOH HOH A . 
K 4 HOH 137 537 175 HOH HOH A . 
K 4 HOH 138 538 350 HOH HOH A . 
K 4 HOH 139 539 405 HOH HOH A . 
K 4 HOH 140 540 722 HOH HOH A . 
K 4 HOH 141 541 715 HOH HOH A . 
K 4 HOH 142 542 646 HOH HOH A . 
K 4 HOH 143 543 435 HOH HOH A . 
K 4 HOH 144 544 411 HOH HOH A . 
K 4 HOH 145 545 345 HOH HOH A . 
K 4 HOH 146 546 699 HOH HOH A . 
K 4 HOH 147 547 694 HOH HOH A . 
K 4 HOH 148 548 351 HOH HOH A . 
K 4 HOH 149 549 650 HOH HOH A . 
K 4 HOH 150 550 334 HOH HOH A . 
K 4 HOH 151 551 72  HOH HOH A . 
K 4 HOH 152 552 525 HOH HOH A . 
K 4 HOH 153 553 526 HOH HOH A . 
K 4 HOH 154 554 618 HOH HOH A . 
K 4 HOH 155 555 384 HOH HOH A . 
K 4 HOH 156 556 599 HOH HOH A . 
K 4 HOH 157 557 331 HOH HOH A . 
K 4 HOH 158 558 361 HOH HOH A . 
K 4 HOH 159 559 623 HOH HOH A . 
K 4 HOH 160 560 727 HOH HOH A . 
K 4 HOH 161 561 371 HOH HOH A . 
K 4 HOH 162 562 274 HOH HOH A . 
K 4 HOH 163 563 653 HOH HOH A . 
K 4 HOH 164 564 410 HOH HOH A . 
K 4 HOH 165 565 691 HOH HOH A . 
K 4 HOH 166 566 708 HOH HOH A . 
K 4 HOH 167 567 413 HOH HOH A . 
K 4 HOH 168 568 527 HOH HOH A . 
K 4 HOH 169 569 685 HOH HOH A . 
K 4 HOH 170 570 746 HOH HOH A . 
K 4 HOH 171 571 392 HOH HOH A . 
K 4 HOH 172 572 362 HOH HOH A . 
K 4 HOH 173 573 744 HOH HOH A . 
K 4 HOH 174 574 367 HOH HOH A . 
K 4 HOH 175 575 508 HOH HOH A . 
K 4 HOH 176 576 598 HOH HOH A . 
K 4 HOH 177 577 409 HOH HOH A . 
K 4 HOH 178 578 235 HOH HOH A . 
K 4 HOH 179 579 282 HOH HOH A . 
K 4 HOH 180 580 366 HOH HOH A . 
K 4 HOH 181 581 365 HOH HOH A . 
K 4 HOH 182 582 633 HOH HOH A . 
K 4 HOH 183 583 256 HOH HOH A . 
K 4 HOH 184 584 335 HOH HOH A . 
K 4 HOH 185 585 176 HOH HOH A . 
K 4 HOH 186 586 385 HOH HOH A . 
K 4 HOH 187 587 317 HOH HOH A . 
K 4 HOH 188 588 408 HOH HOH A . 
K 4 HOH 189 589 690 HOH HOH A . 
K 4 HOH 190 590 373 HOH HOH A . 
K 4 HOH 191 591 360 HOH HOH A . 
K 4 HOH 192 592 537 HOH HOH A . 
K 4 HOH 193 593 363 HOH HOH A . 
K 4 HOH 194 594 539 HOH HOH A . 
K 4 HOH 195 595 337 HOH HOH A . 
K 4 HOH 196 596 564 HOH HOH A . 
K 4 HOH 197 597 179 HOH HOH A . 
K 4 HOH 198 598 359 HOH HOH A . 
K 4 HOH 199 599 414 HOH HOH A . 
K 4 HOH 200 600 340 HOH HOH A . 
K 4 HOH 201 601 664 HOH HOH A . 
K 4 HOH 202 602 438 HOH HOH A . 
K 4 HOH 203 603 729 HOH HOH A . 
K 4 HOH 204 604 524 HOH HOH A . 
K 4 HOH 205 605 522 HOH HOH A . 
K 4 HOH 206 606 677 HOH HOH A . 
K 4 HOH 207 607 302 HOH HOH A . 
K 4 HOH 208 608 649 HOH HOH A . 
K 4 HOH 209 609 460 HOH HOH A . 
K 4 HOH 210 610 619 HOH HOH A . 
K 4 HOH 211 611 407 HOH HOH A . 
K 4 HOH 212 612 689 HOH HOH A . 
K 4 HOH 213 613 343 HOH HOH A . 
K 4 HOH 214 614 648 HOH HOH A . 
K 4 HOH 215 615 647 HOH HOH A . 
K 4 HOH 216 616 668 HOH HOH A . 
K 4 HOH 217 617 546 HOH HOH A . 
K 4 HOH 218 618 255 HOH HOH A . 
K 4 HOH 219 619 556 HOH HOH A . 
K 4 HOH 220 620 436 HOH HOH A . 
K 4 HOH 221 621 403 HOH HOH A . 
K 4 HOH 222 622 632 HOH HOH A . 
L 4 HOH 1   401 713 HOH HOH B . 
L 4 HOH 2   402 138 HOH HOH B . 
L 4 HOH 3   403 396 HOH HOH B . 
L 4 HOH 4   404 189 HOH HOH B . 
L 4 HOH 5   405 449 HOH HOH B . 
L 4 HOH 6   406 328 HOH HOH B . 
L 4 HOH 7   407 76  HOH HOH B . 
L 4 HOH 8   408 462 HOH HOH B . 
L 4 HOH 9   409 498 HOH HOH B . 
L 4 HOH 10  410 499 HOH HOH B . 
L 4 HOH 11  411 496 HOH HOH B . 
L 4 HOH 12  412 326 HOH HOH B . 
L 4 HOH 13  413 61  HOH HOH B . 
L 4 HOH 14  414 243 HOH HOH B . 
L 4 HOH 15  415 77  HOH HOH B . 
L 4 HOH 16  416 707 HOH HOH B . 
L 4 HOH 17  417 26  HOH HOH B . 
L 4 HOH 18  418 720 HOH HOH B . 
L 4 HOH 19  419 571 HOH HOH B . 
L 4 HOH 20  420 15  HOH HOH B . 
L 4 HOH 21  421 503 HOH HOH B . 
L 4 HOH 22  422 329 HOH HOH B . 
L 4 HOH 23  423 33  HOH HOH B . 
L 4 HOH 24  424 62  HOH HOH B . 
L 4 HOH 25  425 211 HOH HOH B . 
L 4 HOH 26  426 505 HOH HOH B . 
L 4 HOH 27  427 447 HOH HOH B . 
L 4 HOH 28  428 269 HOH HOH B . 
L 4 HOH 29  429 194 HOH HOH B . 
L 4 HOH 30  430 254 HOH HOH B . 
L 4 HOH 31  431 202 HOH HOH B . 
L 4 HOH 32  432 225 HOH HOH B . 
L 4 HOH 33  433 113 HOH HOH B . 
L 4 HOH 34  434 585 HOH HOH B . 
L 4 HOH 35  435 39  HOH HOH B . 
L 4 HOH 36  436 284 HOH HOH B . 
L 4 HOH 37  437 167 HOH HOH B . 
L 4 HOH 38  438 501 HOH HOH B . 
L 4 HOH 39  439 163 HOH HOH B . 
L 4 HOH 40  440 48  HOH HOH B . 
L 4 HOH 41  441 96  HOH HOH B . 
L 4 HOH 42  442 91  HOH HOH B . 
L 4 HOH 43  443 263 HOH HOH B . 
L 4 HOH 44  444 149 HOH HOH B . 
L 4 HOH 45  445 104 HOH HOH B . 
L 4 HOH 46  446 87  HOH HOH B . 
L 4 HOH 47  447 249 HOH HOH B . 
L 4 HOH 48  448 188 HOH HOH B . 
L 4 HOH 49  449 307 HOH HOH B . 
L 4 HOH 50  450 10  HOH HOH B . 
L 4 HOH 51  451 401 HOH HOH B . 
L 4 HOH 52  452 164 HOH HOH B . 
L 4 HOH 53  453 739 HOH HOH B . 
L 4 HOH 54  454 574 HOH HOH B . 
L 4 HOH 55  455 400 HOH HOH B . 
L 4 HOH 56  456 257 HOH HOH B . 
L 4 HOH 57  457 162 HOH HOH B . 
L 4 HOH 58  458 40  HOH HOH B . 
L 4 HOH 59  459 93  HOH HOH B . 
L 4 HOH 60  460 64  HOH HOH B . 
L 4 HOH 61  461 232 HOH HOH B . 
L 4 HOH 62  462 140 HOH HOH B . 
L 4 HOH 63  463 319 HOH HOH B . 
L 4 HOH 64  464 594 HOH HOH B . 
L 4 HOH 65  465 13  HOH HOH B . 
L 4 HOH 66  466 502 HOH HOH B . 
L 4 HOH 67  467 494 HOH HOH B . 
L 4 HOH 68  468 275 HOH HOH B . 
L 4 HOH 69  469 229 HOH HOH B . 
L 4 HOH 70  470 218 HOH HOH B . 
L 4 HOH 71  471 242 HOH HOH B . 
L 4 HOH 72  472 464 HOH HOH B . 
L 4 HOH 73  473 347 HOH HOH B . 
L 4 HOH 74  474 567 HOH HOH B . 
L 4 HOH 75  475 155 HOH HOH B . 
L 4 HOH 76  476 241 HOH HOH B . 
L 4 HOH 77  477 285 HOH HOH B . 
L 4 HOH 78  478 177 HOH HOH B . 
L 4 HOH 79  479 224 HOH HOH B . 
L 4 HOH 80  480 6   HOH HOH B . 
L 4 HOH 81  481 208 HOH HOH B . 
L 4 HOH 82  482 592 HOH HOH B . 
L 4 HOH 83  483 278 HOH HOH B . 
L 4 HOH 84  484 628 HOH HOH B . 
L 4 HOH 85  485 24  HOH HOH B . 
L 4 HOH 86  486 187 HOH HOH B . 
L 4 HOH 87  487 57  HOH HOH B . 
L 4 HOH 88  488 210 HOH HOH B . 
L 4 HOH 89  489 572 HOH HOH B . 
L 4 HOH 90  490 292 HOH HOH B . 
L 4 HOH 91  491 174 HOH HOH B . 
L 4 HOH 92  492 4   HOH HOH B . 
L 4 HOH 93  493 497 HOH HOH B . 
L 4 HOH 94  494 101 HOH HOH B . 
L 4 HOH 95  495 590 HOH HOH B . 
L 4 HOH 96  496 591 HOH HOH B . 
L 4 HOH 97  497 706 HOH HOH B . 
L 4 HOH 98  498 541 HOH HOH B . 
L 4 HOH 99  499 103 HOH HOH B . 
L 4 HOH 100 500 442 HOH HOH B . 
L 4 HOH 101 501 159 HOH HOH B . 
L 4 HOH 102 502 129 HOH HOH B . 
L 4 HOH 103 503 638 HOH HOH B . 
L 4 HOH 104 504 639 HOH HOH B . 
L 4 HOH 105 505 586 HOH HOH B . 
L 4 HOH 106 506 504 HOH HOH B . 
L 4 HOH 107 507 376 HOH HOH B . 
L 4 HOH 108 508 562 HOH HOH B . 
L 4 HOH 109 509 440 HOH HOH B . 
L 4 HOH 110 510 465 HOH HOH B . 
L 4 HOH 111 511 710 HOH HOH B . 
L 4 HOH 112 512 111 HOH HOH B . 
L 4 HOH 113 513 463 HOH HOH B . 
L 4 HOH 114 514 626 HOH HOH B . 
L 4 HOH 115 515 573 HOH HOH B . 
L 4 HOH 116 516 705 HOH HOH B . 
L 4 HOH 117 517 82  HOH HOH B . 
L 4 HOH 118 518 314 HOH HOH B . 
L 4 HOH 119 519 531 HOH HOH B . 
L 4 HOH 120 520 310 HOH HOH B . 
L 4 HOH 121 521 454 HOH HOH B . 
L 4 HOH 122 522 630 HOH HOH B . 
L 4 HOH 123 523 717 HOH HOH B . 
L 4 HOH 124 524 544 HOH HOH B . 
L 4 HOH 125 525 437 HOH HOH B . 
L 4 HOH 126 526 587 HOH HOH B . 
L 4 HOH 127 527 333 HOH HOH B . 
L 4 HOH 128 528 461 HOH HOH B . 
L 4 HOH 129 529 397 HOH HOH B . 
L 4 HOH 130 530 375 HOH HOH B . 
L 4 HOH 131 531 500 HOH HOH B . 
L 4 HOH 132 532 593 HOH HOH B . 
L 4 HOH 133 533 402 HOH HOH B . 
L 4 HOH 134 534 445 HOH HOH B . 
L 4 HOH 135 535 575 HOH HOH B . 
L 4 HOH 136 536 495 HOH HOH B . 
L 4 HOH 137 537 563 HOH HOH B . 
L 4 HOH 138 538 640 HOH HOH B . 
L 4 HOH 139 539 576 HOH HOH B . 
L 4 HOH 140 540 446 HOH HOH B . 
L 4 HOH 141 541 441 HOH HOH B . 
L 4 HOH 142 542 459 HOH HOH B . 
L 4 HOH 143 543 377 HOH HOH B . 
L 4 HOH 144 544 588 HOH HOH B . 
L 4 HOH 145 545 629 HOH HOH B . 
L 4 HOH 146 546 453 HOH HOH B . 
L 4 HOH 147 547 443 HOH HOH B . 
L 4 HOH 148 548 466 HOH HOH B . 
L 4 HOH 149 549 458 HOH HOH B . 
M 4 HOH 1   401 610 HOH HOH C . 
M 4 HOH 2   402 609 HOH HOH C . 
M 4 HOH 3   403 469 HOH HOH C . 
M 4 HOH 4   404 480 HOH HOH C . 
M 4 HOH 5   405 644 HOH HOH C . 
M 4 HOH 6   406 311 HOH HOH C . 
M 4 HOH 7   407 261 HOH HOH C . 
M 4 HOH 8   408 204 HOH HOH C . 
M 4 HOH 9   409 212 HOH HOH C . 
M 4 HOH 10  410 697 HOH HOH C . 
M 4 HOH 11  411 233 HOH HOH C . 
M 4 HOH 12  412 172 HOH HOH C . 
M 4 HOH 13  413 18  HOH HOH C . 
M 4 HOH 14  414 514 HOH HOH C . 
M 4 HOH 15  415 470 HOH HOH C . 
M 4 HOH 16  416 231 HOH HOH C . 
M 4 HOH 17  417 678 HOH HOH C . 
M 4 HOH 18  418 206 HOH HOH C . 
M 4 HOH 19  419 485 HOH HOH C . 
M 4 HOH 20  420 716 HOH HOH C . 
M 4 HOH 21  421 195 HOH HOH C . 
M 4 HOH 22  422 290 HOH HOH C . 
M 4 HOH 23  423 550 HOH HOH C . 
M 4 HOH 24  424 160 HOH HOH C . 
M 4 HOH 25  425 635 HOH HOH C . 
M 4 HOH 26  426 540 HOH HOH C . 
M 4 HOH 27  427 565 HOH HOH C . 
M 4 HOH 28  428 561 HOH HOH C . 
M 4 HOH 29  429 740 HOH HOH C . 
M 4 HOH 30  430 577 HOH HOH C . 
M 4 HOH 31  431 122 HOH HOH C . 
M 4 HOH 32  432 236 HOH HOH C . 
M 4 HOH 33  433 146 HOH HOH C . 
M 4 HOH 34  434 702 HOH HOH C . 
M 4 HOH 35  435 259 HOH HOH C . 
M 4 HOH 36  436 20  HOH HOH C . 
M 4 HOH 37  437 205 HOH HOH C . 
M 4 HOH 38  438 295 HOH HOH C . 
M 4 HOH 39  439 16  HOH HOH C . 
M 4 HOH 40  440 44  HOH HOH C . 
M 4 HOH 41  441 9   HOH HOH C . 
M 4 HOH 42  442 271 HOH HOH C . 
M 4 HOH 43  443 95  HOH HOH C . 
M 4 HOH 44  444 234 HOH HOH C . 
M 4 HOH 45  445 32  HOH HOH C . 
M 4 HOH 46  446 289 HOH HOH C . 
M 4 HOH 47  447 738 HOH HOH C . 
M 4 HOH 48  448 36  HOH HOH C . 
M 4 HOH 49  449 74  HOH HOH C . 
M 4 HOH 50  450 448 HOH HOH C . 
M 4 HOH 51  451 217 HOH HOH C . 
M 4 HOH 52  452 325 HOH HOH C . 
M 4 HOH 53  453 186 HOH HOH C . 
M 4 HOH 54  454 560 HOH HOH C . 
M 4 HOH 55  455 450 HOH HOH C . 
M 4 HOH 56  456 102 HOH HOH C . 
M 4 HOH 57  457 548 HOH HOH C . 
M 4 HOH 58  458 248 HOH HOH C . 
M 4 HOH 59  459 379 HOH HOH C . 
M 4 HOH 60  460 568 HOH HOH C . 
M 4 HOH 61  461 283 HOH HOH C . 
M 4 HOH 62  462 83  HOH HOH C . 
M 4 HOH 63  463 69  HOH HOH C . 
M 4 HOH 64  464 315 HOH HOH C . 
M 4 HOH 65  465 601 HOH HOH C . 
M 4 HOH 66  466 150 HOH HOH C . 
M 4 HOH 67  467 652 HOH HOH C . 
M 4 HOH 68  468 605 HOH HOH C . 
M 4 HOH 69  469 112 HOH HOH C . 
M 4 HOH 70  470 288 HOH HOH C . 
M 4 HOH 71  471 324 HOH HOH C . 
M 4 HOH 72  472 19  HOH HOH C . 
M 4 HOH 73  473 478 HOH HOH C . 
M 4 HOH 74  474 51  HOH HOH C . 
M 4 HOH 75  475 645 HOH HOH C . 
M 4 HOH 76  476 300 HOH HOH C . 
M 4 HOH 77  477 559 HOH HOH C . 
M 4 HOH 78  478 602 HOH HOH C . 
M 4 HOH 79  479 156 HOH HOH C . 
M 4 HOH 80  480 421 HOH HOH C . 
M 4 HOH 81  481 542 HOH HOH C . 
M 4 HOH 82  482 265 HOH HOH C . 
M 4 HOH 83  483 557 HOH HOH C . 
M 4 HOH 84  484 297 HOH HOH C . 
M 4 HOH 85  485 100 HOH HOH C . 
M 4 HOH 86  486 688 HOH HOH C . 
M 4 HOH 87  487 90  HOH HOH C . 
M 4 HOH 88  488 110 HOH HOH C . 
M 4 HOH 89  489 65  HOH HOH C . 
M 4 HOH 90  490 23  HOH HOH C . 
M 4 HOH 91  491 178 HOH HOH C . 
M 4 HOH 92  492 67  HOH HOH C . 
M 4 HOH 93  493 475 HOH HOH C . 
M 4 HOH 94  494 55  HOH HOH C . 
M 4 HOH 95  495 703 HOH HOH C . 
M 4 HOH 96  496 743 HOH HOH C . 
M 4 HOH 97  497 312 HOH HOH C . 
M 4 HOH 98  498 607 HOH HOH C . 
M 4 HOH 99  499 31  HOH HOH C . 
M 4 HOH 100 500 116 HOH HOH C . 
M 4 HOH 101 501 341 HOH HOH C . 
M 4 HOH 102 502 34  HOH HOH C . 
M 4 HOH 103 503 247 HOH HOH C . 
M 4 HOH 104 504 203 HOH HOH C . 
M 4 HOH 105 505 286 HOH HOH C . 
M 4 HOH 106 506 603 HOH HOH C . 
M 4 HOH 107 507 549 HOH HOH C . 
M 4 HOH 108 508 604 HOH HOH C . 
M 4 HOH 109 509 273 HOH HOH C . 
M 4 HOH 110 510 99  HOH HOH C . 
M 4 HOH 111 511 600 HOH HOH C . 
M 4 HOH 112 512 484 HOH HOH C . 
M 4 HOH 113 513 123 HOH HOH C . 
M 4 HOH 114 514 704 HOH HOH C . 
M 4 HOH 115 515 221 HOH HOH C . 
M 4 HOH 116 516 581 HOH HOH C . 
M 4 HOH 117 517 171 HOH HOH C . 
M 4 HOH 118 518 30  HOH HOH C . 
M 4 HOH 119 519 551 HOH HOH C . 
M 4 HOH 120 520 47  HOH HOH C . 
M 4 HOH 121 521 433 HOH HOH C . 
M 4 HOH 122 522 399 HOH HOH C . 
M 4 HOH 123 523 327 HOH HOH C . 
M 4 HOH 124 524 246 HOH HOH C . 
M 4 HOH 125 525 578 HOH HOH C . 
M 4 HOH 126 526 553 HOH HOH C . 
M 4 HOH 127 527 554 HOH HOH C . 
M 4 HOH 128 528 444 HOH HOH C . 
M 4 HOH 129 529 272 HOH HOH C . 
M 4 HOH 130 530 569 HOH HOH C . 
M 4 HOH 131 531 675 HOH HOH C . 
M 4 HOH 132 532 342 HOH HOH C . 
M 4 HOH 133 533 608 HOH HOH C . 
M 4 HOH 134 534 380 HOH HOH C . 
M 4 HOH 135 535 419 HOH HOH C . 
M 4 HOH 136 536 338 HOH HOH C . 
M 4 HOH 137 537 492 HOH HOH C . 
M 4 HOH 138 538 483 HOH HOH C . 
M 4 HOH 139 539 434 HOH HOH C . 
M 4 HOH 140 540 471 HOH HOH C . 
M 4 HOH 141 541 468 HOH HOH C . 
M 4 HOH 142 542 570 HOH HOH C . 
M 4 HOH 143 543 108 HOH HOH C . 
M 4 HOH 144 544 682 HOH HOH C . 
M 4 HOH 145 545 547 HOH HOH C . 
M 4 HOH 146 546 552 HOH HOH C . 
M 4 HOH 147 547 477 HOH HOH C . 
M 4 HOH 148 548 612 HOH HOH C . 
M 4 HOH 149 549 330 HOH HOH C . 
M 4 HOH 150 550 723 HOH HOH C . 
M 4 HOH 151 551 579 HOH HOH C . 
M 4 HOH 152 552 566 HOH HOH C . 
M 4 HOH 153 553 491 HOH HOH C . 
M 4 HOH 154 554 151 HOH HOH C . 
M 4 HOH 155 555 589 HOH HOH C . 
M 4 HOH 156 556 451 HOH HOH C . 
M 4 HOH 157 557 481 HOH HOH C . 
M 4 HOH 158 558 180 HOH HOH C . 
M 4 HOH 159 559 543 HOH HOH C . 
M 4 HOH 160 560 268 HOH HOH C . 
M 4 HOH 161 561 582 HOH HOH C . 
M 4 HOH 162 562 467 HOH HOH C . 
M 4 HOH 163 563 476 HOH HOH C . 
M 4 HOH 164 564 482 HOH HOH C . 
M 4 HOH 165 565 455 HOH HOH C . 
M 4 HOH 166 566 474 HOH HOH C . 
M 4 HOH 167 567 580 HOH HOH C . 
M 4 HOH 168 568 457 HOH HOH C . 
M 4 HOH 169 569 736 HOH HOH C . 
M 4 HOH 170 570 456 HOH HOH C . 
M 4 HOH 171 571 378 HOH HOH C . 
M 4 HOH 172 572 558 HOH HOH C . 
M 4 HOH 173 573 613 HOH HOH C . 
M 4 HOH 174 574 472 HOH HOH C . 
M 4 HOH 175 575 555 HOH HOH C . 
M 4 HOH 176 576 733 HOH HOH C . 
M 4 HOH 177 577 732 HOH HOH C . 
M 4 HOH 178 578 513 HOH HOH C . 
M 4 HOH 179 579 439 HOH HOH C . 
M 4 HOH 180 580 452 HOH HOH C . 
M 4 HOH 181 581 683 HOH HOH C . 
M 4 HOH 182 582 398 HOH HOH C . 
M 4 HOH 183 583 479 HOH HOH C . 
M 4 HOH 184 584 584 HOH HOH C . 
M 4 HOH 185 585 583 HOH HOH C . 
M 4 HOH 186 586 473 HOH HOH C . 
N 4 HOH 1   401 518 HOH HOH D . 
N 4 HOH 2   402 416 HOH HOH D . 
N 4 HOH 3   403 701 HOH HOH D . 
N 4 HOH 4   404 611 HOH HOH D . 
N 4 HOH 5   405 352 HOH HOH D . 
N 4 HOH 6   406 75  HOH HOH D . 
N 4 HOH 7   407 616 HOH HOH D . 
N 4 HOH 8   408 287 HOH HOH D . 
N 4 HOH 9   409 669 HOH HOH D . 
N 4 HOH 10  410 323 HOH HOH D . 
N 4 HOH 11  411 147 HOH HOH D . 
N 4 HOH 12  412 673 HOH HOH D . 
N 4 HOH 13  413 488 HOH HOH D . 
N 4 HOH 14  414 183 HOH HOH D . 
N 4 HOH 15  415 511 HOH HOH D . 
N 4 HOH 16  416 128 HOH HOH D . 
N 4 HOH 17  417 519 HOH HOH D . 
N 4 HOH 18  418 521 HOH HOH D . 
N 4 HOH 19  419 215 HOH HOH D . 
N 4 HOH 20  420 711 HOH HOH D . 
N 4 HOH 21  421 696 HOH HOH D . 
N 4 HOH 22  422 731 HOH HOH D . 
N 4 HOH 23  423 512 HOH HOH D . 
N 4 HOH 24  424 132 HOH HOH D . 
N 4 HOH 25  425 353 HOH HOH D . 
N 4 HOH 26  426 14  HOH HOH D . 
N 4 HOH 27  427 37  HOH HOH D . 
N 4 HOH 28  428 721 HOH HOH D . 
N 4 HOH 29  429 620 HOH HOH D . 
N 4 HOH 30  430 200 HOH HOH D . 
N 4 HOH 31  431 136 HOH HOH D . 
N 4 HOH 32  432 595 HOH HOH D . 
N 4 HOH 33  433 1   HOH HOH D . 
N 4 HOH 34  434 84  HOH HOH D . 
N 4 HOH 35  435 152 HOH HOH D . 
N 4 HOH 36  436 73  HOH HOH D . 
N 4 HOH 37  437 276 HOH HOH D . 
N 4 HOH 38  438 50  HOH HOH D . 
N 4 HOH 39  439 114 HOH HOH D . 
N 4 HOH 40  440 124 HOH HOH D . 
N 4 HOH 41  441 142 HOH HOH D . 
N 4 HOH 42  442 227 HOH HOH D . 
N 4 HOH 43  443 614 HOH HOH D . 
N 4 HOH 44  444 303 HOH HOH D . 
N 4 HOH 45  445 662 HOH HOH D . 
N 4 HOH 46  446 313 HOH HOH D . 
N 4 HOH 47  447 425 HOH HOH D . 
N 4 HOH 48  448 299 HOH HOH D . 
N 4 HOH 49  449 656 HOH HOH D . 
N 4 HOH 50  450 125 HOH HOH D . 
N 4 HOH 51  451 724 HOH HOH D . 
N 4 HOH 52  452 320 HOH HOH D . 
N 4 HOH 53  453 213 HOH HOH D . 
N 4 HOH 54  454 301 HOH HOH D . 
N 4 HOH 55  455 191 HOH HOH D . 
N 4 HOH 56  456 127 HOH HOH D . 
N 4 HOH 57  457 322 HOH HOH D . 
N 4 HOH 58  458 86  HOH HOH D . 
N 4 HOH 59  459 17  HOH HOH D . 
N 4 HOH 60  460 141 HOH HOH D . 
N 4 HOH 61  461 636 HOH HOH D . 
N 4 HOH 62  462 192 HOH HOH D . 
N 4 HOH 63  463 671 HOH HOH D . 
N 4 HOH 64  464 355 HOH HOH D . 
N 4 HOH 65  465 49  HOH HOH D . 
N 4 HOH 66  466 133 HOH HOH D . 
N 4 HOH 67  467 291 HOH HOH D . 
N 4 HOH 68  468 137 HOH HOH D . 
N 4 HOH 69  469 734 HOH HOH D . 
N 4 HOH 70  470 139 HOH HOH D . 
N 4 HOH 71  471 118 HOH HOH D . 
N 4 HOH 72  472 58  HOH HOH D . 
N 4 HOH 73  473 321 HOH HOH D . 
N 4 HOH 74  474 106 HOH HOH D . 
N 4 HOH 75  475 71  HOH HOH D . 
N 4 HOH 76  476 228 HOH HOH D . 
N 4 HOH 77  477 22  HOH HOH D . 
N 4 HOH 78  478 294 HOH HOH D . 
N 4 HOH 79  479 621 HOH HOH D . 
N 4 HOH 80  480 25  HOH HOH D . 
N 4 HOH 81  481 38  HOH HOH D . 
N 4 HOH 82  482 304 HOH HOH D . 
N 4 HOH 83  483 381 HOH HOH D . 
N 4 HOH 84  484 185 HOH HOH D . 
N 4 HOH 85  485 190 HOH HOH D . 
N 4 HOH 86  486 509 HOH HOH D . 
N 4 HOH 87  487 277 HOH HOH D . 
N 4 HOH 88  488 237 HOH HOH D . 
N 4 HOH 89  489 184 HOH HOH D . 
N 4 HOH 90  490 686 HOH HOH D . 
N 4 HOH 91  491 680 HOH HOH D . 
N 4 HOH 92  492 529 HOH HOH D . 
N 4 HOH 93  493 510 HOH HOH D . 
N 4 HOH 94  494 253 HOH HOH D . 
N 4 HOH 95  495 308 HOH HOH D . 
N 4 HOH 96  496 532 HOH HOH D . 
N 4 HOH 97  497 126 HOH HOH D . 
N 4 HOH 98  498 238 HOH HOH D . 
N 4 HOH 99  499 107 HOH HOH D . 
N 4 HOH 100 500 240 HOH HOH D . 
N 4 HOH 101 501 134 HOH HOH D . 
N 4 HOH 102 502 389 HOH HOH D . 
N 4 HOH 103 503 5   HOH HOH D . 
N 4 HOH 104 504 165 HOH HOH D . 
N 4 HOH 105 505 658 HOH HOH D . 
N 4 HOH 106 506 309 HOH HOH D . 
N 4 HOH 107 507 2   HOH HOH D . 
N 4 HOH 108 508 79  HOH HOH D . 
N 4 HOH 109 509 207 HOH HOH D . 
N 4 HOH 110 510 89  HOH HOH D . 
N 4 HOH 111 511 281 HOH HOH D . 
N 4 HOH 112 512 166 HOH HOH D . 
N 4 HOH 113 513 117 HOH HOH D . 
N 4 HOH 114 514 296 HOH HOH D . 
N 4 HOH 115 515 298 HOH HOH D . 
N 4 HOH 116 516 415 HOH HOH D . 
N 4 HOH 117 517 109 HOH HOH D . 
N 4 HOH 118 518 98  HOH HOH D . 
N 4 HOH 119 519 267 HOH HOH D . 
N 4 HOH 120 520 719 HOH HOH D . 
N 4 HOH 121 521 655 HOH HOH D . 
N 4 HOH 122 522 120 HOH HOH D . 
N 4 HOH 123 523 244 HOH HOH D . 
N 4 HOH 124 524 12  HOH HOH D . 
N 4 HOH 125 525 432 HOH HOH D . 
N 4 HOH 126 526 370 HOH HOH D . 
N 4 HOH 127 527 214 HOH HOH D . 
N 4 HOH 128 528 490 HOH HOH D . 
N 4 HOH 129 529 427 HOH HOH D . 
N 4 HOH 130 530 219 HOH HOH D . 
N 4 HOH 131 531 358 HOH HOH D . 
N 4 HOH 132 532 741 HOH HOH D . 
N 4 HOH 133 533 41  HOH HOH D . 
N 4 HOH 134 534 726 HOH HOH D . 
N 4 HOH 135 535 305 HOH HOH D . 
N 4 HOH 136 536 349 HOH HOH D . 
N 4 HOH 137 537 157 HOH HOH D . 
N 4 HOH 138 538 489 HOH HOH D . 
N 4 HOH 139 539 667 HOH HOH D . 
N 4 HOH 140 540 684 HOH HOH D . 
N 4 HOH 141 541 43  HOH HOH D . 
N 4 HOH 142 542 730 HOH HOH D . 
N 4 HOH 143 543 486 HOH HOH D . 
N 4 HOH 144 544 430 HOH HOH D . 
N 4 HOH 145 545 676 HOH HOH D . 
N 4 HOH 146 546 344 HOH HOH D . 
N 4 HOH 147 547 387 HOH HOH D . 
N 4 HOH 148 548 393 HOH HOH D . 
N 4 HOH 149 549 209 HOH HOH D . 
N 4 HOH 150 550 637 HOH HOH D . 
N 4 HOH 151 551 420 HOH HOH D . 
N 4 HOH 152 552 354 HOH HOH D . 
N 4 HOH 153 553 530 HOH HOH D . 
N 4 HOH 154 554 617 HOH HOH D . 
N 4 HOH 155 555 97  HOH HOH D . 
N 4 HOH 156 556 383 HOH HOH D . 
N 4 HOH 157 557 493 HOH HOH D . 
N 4 HOH 158 558 657 HOH HOH D . 
N 4 HOH 159 559 597 HOH HOH D . 
N 4 HOH 160 560 339 HOH HOH D . 
N 4 HOH 161 561 687 HOH HOH D . 
N 4 HOH 162 562 642 HOH HOH D . 
N 4 HOH 163 563 388 HOH HOH D . 
N 4 HOH 164 564 386 HOH HOH D . 
N 4 HOH 165 565 515 HOH HOH D . 
N 4 HOH 166 566 348 HOH HOH D . 
N 4 HOH 167 567 622 HOH HOH D . 
N 4 HOH 168 568 487 HOH HOH D . 
N 4 HOH 169 569 670 HOH HOH D . 
N 4 HOH 170 570 424 HOH HOH D . 
N 4 HOH 171 571 143 HOH HOH D . 
N 4 HOH 172 572 346 HOH HOH D . 
N 4 HOH 173 573 418 HOH HOH D . 
N 4 HOH 174 574 293 HOH HOH D . 
N 4 HOH 175 575 356 HOH HOH D . 
N 4 HOH 176 576 173 HOH HOH D . 
N 4 HOH 177 577 431 HOH HOH D . 
N 4 HOH 178 578 428 HOH HOH D . 
N 4 HOH 179 579 357 HOH HOH D . 
N 4 HOH 180 580 634 HOH HOH D . 
N 4 HOH 181 581 316 HOH HOH D . 
N 4 HOH 182 582 535 HOH HOH D . 
N 4 HOH 183 583 429 HOH HOH D . 
N 4 HOH 184 584 417 HOH HOH D . 
N 4 HOH 185 585 507 HOH HOH D . 
N 4 HOH 186 586 654 HOH HOH D . 
N 4 HOH 187 587 631 HOH HOH D . 
# 
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       ? ? ? ? ? ? ? ? ? ? ? REFMAC   ? ? ? 5.8.0238 1 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? HKL-2000 ? ? ? .        2 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? HKL-2000 ? ? ? .        3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER   ? ? ? .        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                     9JN5 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     90.688 
_cell.length_a_esd                 ? 
_cell.length_b                     101.088 
_cell.length_b_esd                 ? 
_cell.length_c                     110.977 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        16 
_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                         9JN5 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                19 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 21 21 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                   9JN5 
_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             2.73 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          55.03 
_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' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              7.0 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    
;0.1 M ammonium acetate, 0.1 M Tris pH 8.0,  
1.0 M sodium citrate
;
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            298 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS EIGER X 9M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2023-09-30 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   1.0 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'NSRRC BEAMLINE TPS 05A' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        1.0 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   'TPS 05A' 
_diffrn_source.pdbx_synchrotron_site       NSRRC 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9JN5 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.00 
_reflns.d_resolution_low                               25.00 
_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                                     67091 
_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                           97.6 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                5.4 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          7.4 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               1.152 
_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                                0.125 
_reflns.pdbx_Rpim_I_all                                0.054 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.998 
_reflns.pdbx_CC_star                                   0.999 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.113 
_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 
2.01 2.08  ? ? ? ? ? ? 6509 ? ? ? ? ? ? ? ? ? ? ? 4.4 0.651 ? ? 0.655 0.303 ? 1  1 0.895 0.972 ? 96.1 ? 0.577 ? ? ? ? ? ? ? ? ? 
2.08 2.17  ? ? ? ? ? ? 6621 ? ? ? ? ? ? ? ? ? ? ? 5.1 0.737 ? ? 0.478 0.207 ? 2  1 0.960 0.990 ? 97.3 ? 0.429 ? ? ? ? ? ? ? ? ? 
2.17 2.26  ? ? ? ? ? ? 6664 ? ? ? ? ? ? ? ? ? ? ? 5.7 0.837 ? ? 0.388 0.159 ? 3  1 0.975 0.994 ? 97.8 ? 0.353 ? ? ? ? ? ? ? ? ? 
2.26 2.38  ? ? ? ? ? ? 6606 ? ? ? ? ? ? ? ? ? ? ? 5.7 0.919 ? ? 0.312 0.127 ? 4  1 0.983 0.996 ? 97.3 ? 0.284 ? ? ? ? ? ? ? ? ? 
2.38 2.53  ? ? ? ? ? ? 6632 ? ? ? ? ? ? ? ? ? ? ? 5.6 1.058 ? ? 0.253 0.104 ? 5  1 0.988 0.997 ? 97.0 ? 0.230 ? ? ? ? ? ? ? ? ? 
2.53 2.73  ? ? ? ? ? ? 6639 ? ? ? ? ? ? ? ? ? ? ? 5.3 1.281 ? ? 0.201 0.086 ? 6  1 0.990 0.998 ? 97.3 ? 0.181 ? ? ? ? ? ? ? ? ? 
2.73 3.00  ? ? ? ? ? ? 6777 ? ? ? ? ? ? ? ? ? ? ? 5.5 1.361 ? ? 0.144 0.061 ? 7  1 0.995 0.999 ? 98.6 ? 0.130 ? ? ? ? ? ? ? ? ? 
3.00 3.43  ? ? ? ? ? ? 6833 ? ? ? ? ? ? ? ? ? ? ? 5.6 1.475 ? ? 0.109 0.046 ? 8  1 0.996 0.999 ? 99.6 ? 0.099 ? ? ? ? ? ? ? ? ? 
3.43 4.32  ? ? ? ? ? ? 6850 ? ? ? ? ? ? ? ? ? ? ? 5.5 1.580 ? ? 0.082 0.035 ? 9  1 0.997 0.999 ? 98.3 ? 0.074 ? ? ? ? ? ? ? ? ? 
4.32 25.00 ? ? ? ? ? ? 6960 ? ? ? ? ? ? ? ? ? ? ? 5.2 1.449 ? ? 0.071 0.032 ? 10 1 0.996 0.999 ? 96.4 ? 0.064 ? ? ? ? ? ? ? ? ? 
# 
_refine.aniso_B[1][1]                            1.93 
_refine.aniso_B[1][2]                            0.00 
_refine.aniso_B[1][3]                            -0.00 
_refine.aniso_B[2][2]                            -2.35 
_refine.aniso_B[2][3]                            0.00 
_refine.aniso_B[3][3]                            0.41 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               30.493 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               0.949 
_refine.correlation_coeff_Fo_to_Fc_free          0.919 
_refine.details                                  'HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS' 
_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                                 9JN5 
_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                            2.00 
_refine.ls_d_res_low                             24.95 
_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                     63521 
_refine.ls_number_reflns_R_free                  3309 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    96.59 
_refine.ls_percent_reflns_R_free                 5.0 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.24315 
_refine.ls_R_factor_R_free                       0.30242 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.24008 
_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                    MASK 
_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                          ? 
_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                      ? 
_refine.pdbx_stereochemistry_target_values       'MAXIMUM LIKELIHOOD' 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       0.230 
_refine.pdbx_overall_ESU_R_Free                  0.212 
_refine.pdbx_solvent_vdw_probe_radii             1.20 
_refine.pdbx_solvent_ion_probe_radii             0.80 
_refine.pdbx_solvent_shrinkage_radii             0.80 
_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                 ? 
_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                             6.196 
_refine.overall_SU_ML                            0.167 
_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                         1 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       2.00 
_refine_hist.d_res_low                        24.95 
_refine_hist.number_atoms_solvent             744 
_refine_hist.number_atoms_total               7363 
_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        6427 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         192 
_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' ? 0.010  0.013  6829  ? r_bond_refined_d             ? ? 
'X-RAY DIFFRACTION' ? 0.002  0.017  6281  ? r_bond_other_d               ? ? 
'X-RAY DIFFRACTION' ? 1.659  1.693  9376  ? r_angle_refined_deg          ? ? 
'X-RAY DIFFRACTION' ? 1.360  1.602  14378 ? r_angle_other_deg            ? ? 
'X-RAY DIFFRACTION' ? 6.776  5.000  847   ? r_dihedral_angle_1_deg       ? ? 
'X-RAY DIFFRACTION' ? 31.569 19.130 368   ? r_dihedral_angle_2_deg       ? ? 
'X-RAY DIFFRACTION' ? 14.586 15.000 929   ? r_dihedral_angle_3_deg       ? ? 
'X-RAY DIFFRACTION' ? 17.572 15.000 76    ? r_dihedral_angle_4_deg       ? ? 
'X-RAY DIFFRACTION' ? 0.070  0.200  835   ? r_chiral_restr               ? ? 
'X-RAY DIFFRACTION' ? 0.009  0.020  7913  ? r_gen_planes_refined         ? ? 
'X-RAY DIFFRACTION' ? 0.005  0.020  1643  ? r_gen_planes_other           ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_nbd_refined                ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_nbd_other                  ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_nbtor_refined              ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_nbtor_other                ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_xyhbond_nbd_refined        ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_xyhbond_nbd_other          ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_metal_ion_refined          ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_metal_ion_other            ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_vdw_refined       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_vdw_other         ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_hbond_refined     ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_hbond_other       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_metal_ion_refined ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_metal_ion_other   ? ? 
'X-RAY DIFFRACTION' ? 2.563  3.068  3403  ? r_mcbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 2.562  3.068  3403  ? r_mcbond_other               ? ? 
'X-RAY DIFFRACTION' ? 3.760  4.583  4245  ? r_mcangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 3.760  4.584  4246  ? r_mcangle_other              ? ? 
'X-RAY DIFFRACTION' ? 2.909  3.316  3426  ? r_scbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 2.909  3.316  3426  ? r_scbond_other               ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_scangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 4.524  4.836  5132  ? r_scangle_other              ? ? 
'X-RAY DIFFRACTION' ? 6.900  36.793 8071  ? r_long_range_B_refined       ? ? 
'X-RAY DIFFRACTION' ? 6.900  36.796 8072  ? r_long_range_B_other         ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_rigid_bond_restr           ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_sphericity_free            ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_sphericity_bonded          ? ? 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.d_res_high                       2.004 
_refine_ls_shell.d_res_low                        2.056 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.number_reflns_R_free             219 
_refine_ls_shell.number_reflns_R_work             4204 
_refine_ls_shell.percent_reflns_obs               87.34 
_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                  0.340 
_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   20 
_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                  0.379 
# 
_struct.entry_id                     9JN5 
_struct.title                        'Crystal structure of KtzT-C197A in complex with HEME and substrate' 
_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        9JN5 
_struct_keywords.text            'Heme-dependent piperazate synthase, OXIDOREDUCTASE' 
_struct_keywords.pdbx_keywords   OXIDOREDUCTASE 
# 
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 1 ? 
C N N 1 ? 
D N N 1 ? 
E N N 2 ? 
F N N 3 ? 
G N N 2 ? 
H N N 2 ? 
I N N 3 ? 
J N N 2 ? 
K N N 4 ? 
L N N 4 ? 
M N N 4 ? 
N N N 4 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    A8CF72_KUTS7 
_struct_ref.pdbx_db_accession          A8CF72 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MFVPGPYHAPEDRWLVDLVRGHPLAQLASNGAGGAAPHITHVPIIVDPELDGPVDRLVGITLWGHMNRANPHWAALGGAA
NVVATFAGPNAYVSPAVYRTAPAAPTWNFTSVQVRGELRKVESADDTLATVRATVAALESRFGAGWDMTGSLDYFRRILP
GVGAFRLRVAEADGMFKLSQEQQPAIRRRVRHSFGGCEATRAVAGLMDRLPTE
;
_struct_ref.pdbx_align_begin           1 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 9JN5 A 6 ? 218 ? A8CF72 1 ? 213 ? 1 213 
2 1 9JN5 B 6 ? 218 ? A8CF72 1 ? 213 ? 1 213 
3 1 9JN5 C 6 ? 218 ? A8CF72 1 ? 213 ? 1 213 
4 1 9JN5 D 6 ? 218 ? A8CF72 1 ? 213 ? 1 213 
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
1 9JN5 ALA A 1   ? UNP A8CF72 ?   ?   'expression tag'      -4  1  
1 9JN5 GLY A 2   ? UNP A8CF72 ?   ?   'expression tag'      -3  2  
1 9JN5 ALA A 3   ? UNP A8CF72 ?   ?   'expression tag'      -2  3  
1 9JN5 GLY A 4   ? UNP A8CF72 ?   ?   'expression tag'      -1  4  
1 9JN5 ALA A 5   ? UNP A8CF72 ?   ?   'expression tag'      0   5  
1 9JN5 ALA A 202 ? UNP A8CF72 CYS 197 'engineered mutation' 197 6  
2 9JN5 ALA B 1   ? UNP A8CF72 ?   ?   'expression tag'      -4  7  
2 9JN5 GLY B 2   ? UNP A8CF72 ?   ?   'expression tag'      -3  8  
2 9JN5 ALA B 3   ? UNP A8CF72 ?   ?   'expression tag'      -2  9  
2 9JN5 GLY B 4   ? UNP A8CF72 ?   ?   'expression tag'      -1  10 
2 9JN5 ALA B 5   ? UNP A8CF72 ?   ?   'expression tag'      0   11 
2 9JN5 ALA B 202 ? UNP A8CF72 CYS 197 'engineered mutation' 197 12 
3 9JN5 ALA C 1   ? UNP A8CF72 ?   ?   'expression tag'      -4  13 
3 9JN5 GLY C 2   ? UNP A8CF72 ?   ?   'expression tag'      -3  14 
3 9JN5 ALA C 3   ? UNP A8CF72 ?   ?   'expression tag'      -2  15 
3 9JN5 GLY C 4   ? UNP A8CF72 ?   ?   'expression tag'      -1  16 
3 9JN5 ALA C 5   ? UNP A8CF72 ?   ?   'expression tag'      0   17 
3 9JN5 ALA C 202 ? UNP A8CF72 CYS 197 'engineered mutation' 197 18 
4 9JN5 ALA D 1   ? UNP A8CF72 ?   ?   'expression tag'      -4  19 
4 9JN5 GLY D 2   ? UNP A8CF72 ?   ?   'expression tag'      -3  20 
4 9JN5 ALA D 3   ? UNP A8CF72 ?   ?   'expression tag'      -2  21 
4 9JN5 GLY D 4   ? UNP A8CF72 ?   ?   'expression tag'      -1  22 
4 9JN5 ALA D 5   ? UNP A8CF72 ?   ?   'expression tag'      0   23 
4 9JN5 ALA D 202 ? UNP A8CF72 CYS 197 'engineered mutation' 197 24 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_and_software_defined_assembly PISA dimeric 2 
2 author_and_software_defined_assembly PISA dimeric 2 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 6880  ? 
1 MORE         -74   ? 
1 'SSA (A^2)'  17790 ? 
2 'ABSA (A^2)' 6880  ? 
2 MORE         -74   ? 
2 'SSA (A^2)'  17590 ? 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,D,E,F,J,K,N 
2 1 B,C,G,H,I,L,M 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'light scattering' 
_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 PRO A 9   ? HIS A 13  ? PRO A 4   HIS A 8   5 ? 5  
HELX_P HELX_P2  AA2 ASP A 17  ? HIS A 27  ? ASP A 12  HIS A 22  1 ? 11 
HELX_P HELX_P3  AA3 GLY A 36  ? ALA A 40  ? GLY A 31  ALA A 35  5 ? 5  
HELX_P HELX_P4  AA4 ASN A 75  ? GLY A 82  ? ASN A 70  GLY A 77  1 ? 8  
HELX_P HELX_P5  AA5 SER A 99  ? ARG A 104 ? SER A 94  ARG A 99  1 ? 6  
HELX_P HELX_P6  AA6 SER A 128 ? GLY A 148 ? SER A 123 GLY A 143 1 ? 21 
HELX_P HELX_P7  AA7 MET A 153 ? GLY A 155 ? MET A 148 GLY A 150 5 ? 3  
HELX_P HELX_P8  AA8 SER A 156 ? LEU A 164 ? SER A 151 LEU A 159 1 ? 9  
HELX_P HELX_P9  AA9 GLN A 188 ? GLY A 201 ? GLN A 183 GLY A 196 1 ? 14 
HELX_P HELX_P10 AB1 ALA A 202 ? ARG A 214 ? ALA A 197 ARG A 209 1 ? 13 
HELX_P HELX_P11 AB2 PRO B 9   ? HIS B 13  ? PRO B 4   HIS B 8   5 ? 5  
HELX_P HELX_P12 AB3 ASP B 17  ? HIS B 27  ? ASP B 12  HIS B 22  1 ? 11 
HELX_P HELX_P13 AB4 GLY B 36  ? ALA B 40  ? GLY B 31  ALA B 35  5 ? 5  
HELX_P HELX_P14 AB5 ASN B 75  ? LEU B 81  ? ASN B 70  LEU B 76  1 ? 7  
HELX_P HELX_P15 AB6 SER B 99  ? ARG B 104 ? SER B 94  ARG B 99  1 ? 6  
HELX_P HELX_P16 AB7 SER B 128 ? GLY B 148 ? SER B 123 GLY B 143 1 ? 21 
HELX_P HELX_P17 AB8 MET B 153 ? GLY B 155 ? MET B 148 GLY B 150 5 ? 3  
HELX_P HELX_P18 AB9 SER B 156 ? LEU B 164 ? SER B 151 LEU B 159 1 ? 9  
HELX_P HELX_P19 AC1 GLN B 188 ? GLY B 200 ? GLN B 183 GLY B 195 1 ? 13 
HELX_P HELX_P20 AC2 ALA B 202 ? ARG B 214 ? ALA B 197 ARG B 209 1 ? 13 
HELX_P HELX_P21 AC3 PRO C 9   ? HIS C 13  ? PRO C 4   HIS C 8   5 ? 5  
HELX_P HELX_P22 AC4 ASP C 17  ? HIS C 27  ? ASP C 12  HIS C 22  1 ? 11 
HELX_P HELX_P23 AC5 ASN C 75  ? LEU C 81  ? ASN C 70  LEU C 76  1 ? 7  
HELX_P HELX_P24 AC6 SER C 99  ? ARG C 104 ? SER C 94  ARG C 99  1 ? 6  
HELX_P HELX_P25 AC7 SER C 128 ? GLY C 148 ? SER C 123 GLY C 143 1 ? 21 
HELX_P HELX_P26 AC8 ASP C 152 ? GLY C 155 ? ASP C 147 GLY C 150 5 ? 4  
HELX_P HELX_P27 AC9 SER C 156 ? LEU C 164 ? SER C 151 LEU C 159 1 ? 9  
HELX_P HELX_P28 AD1 GLN C 188 ? GLY C 200 ? GLN C 183 GLY C 195 1 ? 13 
HELX_P HELX_P29 AD2 ALA C 202 ? LEU C 215 ? ALA C 197 LEU C 210 1 ? 14 
HELX_P HELX_P30 AD3 PRO D 9   ? HIS D 13  ? PRO D 4   HIS D 8   5 ? 5  
HELX_P HELX_P31 AD4 ASP D 17  ? HIS D 27  ? ASP D 12  HIS D 22  1 ? 11 
HELX_P HELX_P32 AD5 ASN D 75  ? LEU D 81  ? ASN D 70  LEU D 76  1 ? 7  
HELX_P HELX_P33 AD6 SER D 99  ? ARG D 104 ? SER D 94  ARG D 99  1 ? 6  
HELX_P HELX_P34 AD7 SER D 128 ? GLY D 148 ? SER D 123 GLY D 143 1 ? 21 
HELX_P HELX_P35 AD8 ASP D 152 ? GLY D 155 ? ASP D 147 GLY D 150 5 ? 4  
HELX_P HELX_P36 AD9 SER D 156 ? ILE D 163 ? SER D 151 ILE D 158 1 ? 8  
HELX_P HELX_P37 AE1 GLN D 188 ? GLY D 200 ? GLN D 183 GLY D 195 1 ? 13 
HELX_P HELX_P38 AE2 ALA D 202 ? LEU D 215 ? ALA D 197 LEU D 210 1 ? 14 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
metalc1 metalc ? ? A HIS 70 NE2 ? ? ? 1_555 E HEM . FE ? ? A HIS 65  A HEM 301 1_555 ? ? ? ? ? ? ? 2.166 ? ? 
metalc2 metalc ? ? E HEM .  FE  ? ? ? 1_555 F ONH . NE ? ? A HEM 301 A ONH 302 1_555 ? ? ? ? ? ? ? 2.582 ? ? 
metalc3 metalc ? ? B HIS 70 NE2 ? ? ? 1_555 G HEM . FE ? ? B HIS 65  B HEM 301 1_555 ? ? ? ? ? ? ? 2.098 ? ? 
metalc4 metalc ? ? G HEM .  FE  ? ? ? 1_555 I ONH . OZ ? ? B HEM 301 C ONH 302 1_555 ? ? ? ? ? ? ? 2.747 ? ? 
metalc5 metalc ? ? C HIS 70 NE2 ? ? ? 1_555 H HEM . FE ? ? C HIS 65  C HEM 301 1_555 ? ? ? ? ? ? ? 2.045 ? ? 
metalc6 metalc ? ? H HEM .  FE  ? ? ? 1_555 M HOH . O  ? ? C HEM 301 C HOH 429 1_555 ? ? ? ? ? ? ? 2.000 ? ? 
metalc7 metalc ? ? D HIS 70 NE2 ? ? ? 1_555 J HEM . FE ? ? D HIS 65  D HEM 301 1_555 ? ? ? ? ? ? ? 2.254 ? ? 
# 
_struct_conn_type.id          metalc 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1  NE2 ? A HIS 70 ? A HIS 65  ? 1_555 FE ? E HEM . ? A HEM 301 ? 1_555 NA ? E HEM . ? A HEM 301 ? 1_555 91.5  ? 
2  NE2 ? A HIS 70 ? A HIS 65  ? 1_555 FE ? E HEM . ? A HEM 301 ? 1_555 NB ? E HEM . ? A HEM 301 ? 1_555 84.9  ? 
3  NA  ? E HEM .  ? A HEM 301 ? 1_555 FE ? E HEM . ? A HEM 301 ? 1_555 NB ? E HEM . ? A HEM 301 ? 1_555 92.0  ? 
4  NE2 ? A HIS 70 ? A HIS 65  ? 1_555 FE ? E HEM . ? A HEM 301 ? 1_555 NC ? E HEM . ? A HEM 301 ? 1_555 94.2  ? 
5  NA  ? E HEM .  ? A HEM 301 ? 1_555 FE ? E HEM . ? A HEM 301 ? 1_555 NC ? E HEM . ? A HEM 301 ? 1_555 172.6 ? 
6  NB  ? E HEM .  ? A HEM 301 ? 1_555 FE ? E HEM . ? A HEM 301 ? 1_555 NC ? E HEM . ? A HEM 301 ? 1_555 83.9  ? 
7  NE2 ? A HIS 70 ? A HIS 65  ? 1_555 FE ? E HEM . ? A HEM 301 ? 1_555 ND ? E HEM . ? A HEM 301 ? 1_555 101.0 ? 
8  NA  ? E HEM .  ? A HEM 301 ? 1_555 FE ? E HEM . ? A HEM 301 ? 1_555 ND ? E HEM . ? A HEM 301 ? 1_555 91.7  ? 
9  NB  ? E HEM .  ? A HEM 301 ? 1_555 FE ? E HEM . ? A HEM 301 ? 1_555 ND ? E HEM . ? A HEM 301 ? 1_555 173.0 ? 
10 NC  ? E HEM .  ? A HEM 301 ? 1_555 FE ? E HEM . ? A HEM 301 ? 1_555 ND ? E HEM . ? A HEM 301 ? 1_555 91.9  ? 
11 NE2 ? A HIS 70 ? A HIS 65  ? 1_555 FE ? E HEM . ? A HEM 301 ? 1_555 NE ? F ONH . ? A ONH 302 ? 1_555 173.0 ? 
12 NA  ? E HEM .  ? A HEM 301 ? 1_555 FE ? E HEM . ? A HEM 301 ? 1_555 NE ? F ONH . ? A ONH 302 ? 1_555 85.2  ? 
13 NB  ? E HEM .  ? A HEM 301 ? 1_555 FE ? E HEM . ? A HEM 301 ? 1_555 NE ? F ONH . ? A ONH 302 ? 1_555 89.0  ? 
14 NC  ? E HEM .  ? A HEM 301 ? 1_555 FE ? E HEM . ? A HEM 301 ? 1_555 NE ? F ONH . ? A ONH 302 ? 1_555 88.7  ? 
15 ND  ? E HEM .  ? A HEM 301 ? 1_555 FE ? E HEM . ? A HEM 301 ? 1_555 NE ? F ONH . ? A ONH 302 ? 1_555 85.3  ? 
16 NE2 ? B HIS 70 ? B HIS 65  ? 1_555 FE ? G HEM . ? B HEM 301 ? 1_555 NA ? G HEM . ? B HEM 301 ? 1_555 94.7  ? 
17 NE2 ? B HIS 70 ? B HIS 65  ? 1_555 FE ? G HEM . ? B HEM 301 ? 1_555 NB ? G HEM . ? B HEM 301 ? 1_555 85.8  ? 
18 NA  ? G HEM .  ? B HEM 301 ? 1_555 FE ? G HEM . ? B HEM 301 ? 1_555 NB ? G HEM . ? B HEM 301 ? 1_555 90.9  ? 
19 NE2 ? B HIS 70 ? B HIS 65  ? 1_555 FE ? G HEM . ? B HEM 301 ? 1_555 NC ? G HEM . ? B HEM 301 ? 1_555 93.7  ? 
20 NA  ? G HEM .  ? B HEM 301 ? 1_555 FE ? G HEM . ? B HEM 301 ? 1_555 NC ? G HEM . ? B HEM 301 ? 1_555 170.4 ? 
21 NB  ? G HEM .  ? B HEM 301 ? 1_555 FE ? G HEM . ? B HEM 301 ? 1_555 NC ? G HEM . ? B HEM 301 ? 1_555 84.9  ? 
22 NE2 ? B HIS 70 ? B HIS 65  ? 1_555 FE ? G HEM . ? B HEM 301 ? 1_555 ND ? G HEM . ? B HEM 301 ? 1_555 101.0 ? 
23 NA  ? G HEM .  ? B HEM 301 ? 1_555 FE ? G HEM . ? B HEM 301 ? 1_555 ND ? G HEM . ? B HEM 301 ? 1_555 92.2  ? 
24 NB  ? G HEM .  ? B HEM 301 ? 1_555 FE ? G HEM . ? B HEM 301 ? 1_555 ND ? G HEM . ? B HEM 301 ? 1_555 172.3 ? 
25 NC  ? G HEM .  ? B HEM 301 ? 1_555 FE ? G HEM . ? B HEM 301 ? 1_555 ND ? G HEM . ? B HEM 301 ? 1_555 90.9  ? 
26 NE2 ? B HIS 70 ? B HIS 65  ? 1_555 FE ? G HEM . ? B HEM 301 ? 1_555 OZ ? I ONH . ? C ONH 302 ? 1_555 156.6 ? 
27 NA  ? G HEM .  ? B HEM 301 ? 1_555 FE ? G HEM . ? B HEM 301 ? 1_555 OZ ? I ONH . ? C ONH 302 ? 1_555 104.3 ? 
28 NB  ? G HEM .  ? B HEM 301 ? 1_555 FE ? G HEM . ? B HEM 301 ? 1_555 OZ ? I ONH . ? C ONH 302 ? 1_555 80.4  ? 
29 NC  ? G HEM .  ? B HEM 301 ? 1_555 FE ? G HEM . ? B HEM 301 ? 1_555 OZ ? I ONH . ? C ONH 302 ? 1_555 66.4  ? 
30 ND  ? G HEM .  ? B HEM 301 ? 1_555 FE ? G HEM . ? B HEM 301 ? 1_555 OZ ? I ONH . ? C ONH 302 ? 1_555 91.9  ? 
31 NE2 ? C HIS 70 ? C HIS 65  ? 1_555 FE ? H HEM . ? C HEM 301 ? 1_555 NA ? H HEM . ? C HEM 301 ? 1_555 98.5  ? 
32 NE2 ? C HIS 70 ? C HIS 65  ? 1_555 FE ? H HEM . ? C HEM 301 ? 1_555 NB ? H HEM . ? C HEM 301 ? 1_555 89.1  ? 
33 NA  ? H HEM .  ? C HEM 301 ? 1_555 FE ? H HEM . ? C HEM 301 ? 1_555 NB ? H HEM . ? C HEM 301 ? 1_555 87.6  ? 
34 NE2 ? C HIS 70 ? C HIS 65  ? 1_555 FE ? H HEM . ? C HEM 301 ? 1_555 NC ? H HEM . ? C HEM 301 ? 1_555 94.0  ? 
35 NA  ? H HEM .  ? C HEM 301 ? 1_555 FE ? H HEM . ? C HEM 301 ? 1_555 NC ? H HEM . ? C HEM 301 ? 1_555 167.1 ? 
36 NB  ? H HEM .  ? C HEM 301 ? 1_555 FE ? H HEM . ? C HEM 301 ? 1_555 NC ? H HEM . ? C HEM 301 ? 1_555 89.7  ? 
37 NE2 ? C HIS 70 ? C HIS 65  ? 1_555 FE ? H HEM . ? C HEM 301 ? 1_555 ND ? H HEM . ? C HEM 301 ? 1_555 101.5 ? 
38 NA  ? H HEM .  ? C HEM 301 ? 1_555 FE ? H HEM . ? C HEM 301 ? 1_555 ND ? H HEM . ? C HEM 301 ? 1_555 91.9  ? 
39 NB  ? H HEM .  ? C HEM 301 ? 1_555 FE ? H HEM . ? C HEM 301 ? 1_555 ND ? H HEM . ? C HEM 301 ? 1_555 169.3 ? 
40 NC  ? H HEM .  ? C HEM 301 ? 1_555 FE ? H HEM . ? C HEM 301 ? 1_555 ND ? H HEM . ? C HEM 301 ? 1_555 88.5  ? 
41 NE2 ? C HIS 70 ? C HIS 65  ? 1_555 FE ? H HEM . ? C HEM 301 ? 1_555 O  ? M HOH . ? C HOH 429 ? 1_555 166.6 ? 
42 NA  ? H HEM .  ? C HEM 301 ? 1_555 FE ? H HEM . ? C HEM 301 ? 1_555 O  ? M HOH . ? C HOH 429 ? 1_555 80.7  ? 
43 NB  ? H HEM .  ? C HEM 301 ? 1_555 FE ? H HEM . ? C HEM 301 ? 1_555 O  ? M HOH . ? C HOH 429 ? 1_555 77.5  ? 
44 NC  ? H HEM .  ? C HEM 301 ? 1_555 FE ? H HEM . ? C HEM 301 ? 1_555 O  ? M HOH . ? C HOH 429 ? 1_555 86.5  ? 
45 ND  ? H HEM .  ? C HEM 301 ? 1_555 FE ? H HEM . ? C HEM 301 ? 1_555 O  ? M HOH . ? C HOH 429 ? 1_555 92.0  ? 
46 NE2 ? D HIS 70 ? D HIS 65  ? 1_555 FE ? J HEM . ? D HEM 301 ? 1_555 NA ? J HEM . ? D HEM 301 ? 1_555 99.2  ? 
47 NE2 ? D HIS 70 ? D HIS 65  ? 1_555 FE ? J HEM . ? D HEM 301 ? 1_555 NB ? J HEM . ? D HEM 301 ? 1_555 80.4  ? 
48 NA  ? J HEM .  ? D HEM 301 ? 1_555 FE ? J HEM . ? D HEM 301 ? 1_555 NB ? J HEM . ? D HEM 301 ? 1_555 87.6  ? 
49 NE2 ? D HIS 70 ? D HIS 65  ? 1_555 FE ? J HEM . ? D HEM 301 ? 1_555 NC ? J HEM . ? D HEM 301 ? 1_555 94.9  ? 
50 NA  ? J HEM .  ? D HEM 301 ? 1_555 FE ? J HEM . ? D HEM 301 ? 1_555 NC ? J HEM . ? D HEM 301 ? 1_555 163.4 ? 
51 NB  ? J HEM .  ? D HEM 301 ? 1_555 FE ? J HEM . ? D HEM 301 ? 1_555 NC ? J HEM . ? D HEM 301 ? 1_555 86.3  ? 
52 NE2 ? D HIS 70 ? D HIS 65  ? 1_555 FE ? J HEM . ? D HEM 301 ? 1_555 ND ? J HEM . ? D HEM 301 ? 1_555 111.9 ? 
53 NA  ? J HEM .  ? D HEM 301 ? 1_555 FE ? J HEM . ? D HEM 301 ? 1_555 ND ? J HEM . ? D HEM 301 ? 1_555 91.6  ? 
54 NB  ? J HEM .  ? D HEM 301 ? 1_555 FE ? J HEM . ? D HEM 301 ? 1_555 ND ? J HEM . ? D HEM 301 ? 1_555 167.7 ? 
55 NC  ? J HEM .  ? D HEM 301 ? 1_555 FE ? J HEM . ? D HEM 301 ? 1_555 ND ? J HEM . ? D HEM 301 ? 1_555 91.1  ? 
# 
loop_
_struct_mon_prot_cis.pdbx_id 
_struct_mon_prot_cis.label_comp_id 
_struct_mon_prot_cis.label_seq_id 
_struct_mon_prot_cis.label_asym_id 
_struct_mon_prot_cis.label_alt_id 
_struct_mon_prot_cis.pdbx_PDB_ins_code 
_struct_mon_prot_cis.auth_comp_id 
_struct_mon_prot_cis.auth_seq_id 
_struct_mon_prot_cis.auth_asym_id 
_struct_mon_prot_cis.pdbx_label_comp_id_2 
_struct_mon_prot_cis.pdbx_label_seq_id_2 
_struct_mon_prot_cis.pdbx_label_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2 
_struct_mon_prot_cis.pdbx_auth_comp_id_2 
_struct_mon_prot_cis.pdbx_auth_seq_id_2 
_struct_mon_prot_cis.pdbx_auth_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_model_num 
_struct_mon_prot_cis.pdbx_omega_angle 
1 ALA 106 A . ? ALA 101 A PRO 107 A ? PRO 102 A 1 -3.78 
2 ALA 106 B . ? ALA 101 B PRO 107 B ? PRO 102 B 1 -0.73 
3 ALA 106 C . ? ALA 101 C PRO 107 C ? PRO 102 C 1 -2.72 
4 ALA 106 D . ? ALA 101 D PRO 107 D ? PRO 102 D 1 -1.63 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 8 ? 
AA2 ? 9 ? 
AA3 ? 8 ? 
AA4 ? 8 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA1 3 4 ? anti-parallel 
AA1 4 5 ? anti-parallel 
AA1 5 6 ? anti-parallel 
AA1 6 7 ? anti-parallel 
AA1 7 8 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA2 4 5 ? anti-parallel 
AA2 5 6 ? anti-parallel 
AA2 6 7 ? anti-parallel 
AA2 7 8 ? anti-parallel 
AA2 8 9 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? anti-parallel 
AA3 3 4 ? anti-parallel 
AA3 4 5 ? anti-parallel 
AA3 5 6 ? anti-parallel 
AA3 6 7 ? anti-parallel 
AA3 7 8 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA4 2 3 ? anti-parallel 
AA4 3 4 ? anti-parallel 
AA4 4 5 ? anti-parallel 
AA4 5 6 ? anti-parallel 
AA4 6 7 ? anti-parallel 
AA4 7 8 ? 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 GLU A 176 ? LYS A 182 ? GLU A 171 LYS A 177 
AA1 2 THR A 111 ? LYS A 125 ? THR A 106 LYS A 120 
AA1 3 VAL A 167 ? ARG A 173 ? VAL A 162 ARG A 168 
AA1 4 THR A 66  ? ASN A 72  ? THR A 61  ASN A 67  
AA1 5 HIS A 43  ? VAL A 51  ? HIS A 38  VAL A 46  
AA1 6 LEU A 29  ? SER A 34  ? LEU A 24  SER A 29  
AA1 7 ALA A 85  ? VAL A 98  ? ALA A 80  VAL A 93  
AA1 8 THR A 111 ? LYS A 125 ? THR A 106 LYS A 120 
AA2 1 ALA B 96  ? VAL B 98  ? ALA B 91  VAL B 93  
AA2 2 GLU B 176 ? LYS B 182 ? GLU B 171 LYS B 177 
AA2 3 ALA B 85  ? ALA B 92  ? ALA B 80  ALA B 87  
AA2 4 LEU B 29  ? SER B 34  ? LEU B 24  SER B 29  
AA2 5 HIS B 43  ? VAL B 51  ? HIS B 38  VAL B 46  
AA2 6 THR B 66  ? ASN B 72  ? THR B 61  ASN B 67  
AA2 7 VAL B 167 ? ARG B 173 ? VAL B 162 ARG B 168 
AA2 8 THR B 111 ? LYS B 125 ? THR B 106 LYS B 120 
AA2 9 GLU B 176 ? LYS B 182 ? GLU B 171 LYS B 177 
AA3 1 GLU C 176 ? LYS C 182 ? GLU C 171 LYS C 177 
AA3 2 THR C 111 ? VAL C 126 ? THR C 106 VAL C 121 
AA3 3 VAL C 167 ? ARG C 173 ? VAL C 162 ARG C 168 
AA3 4 THR C 66  ? ASN C 72  ? THR C 61  ASN C 67  
AA3 5 HIS C 43  ? VAL C 51  ? HIS C 38  VAL C 46  
AA3 6 LEU C 29  ? SER C 34  ? LEU C 24  SER C 29  
AA3 7 ASN C 86  ? VAL C 98  ? ASN C 81  VAL C 93  
AA3 8 THR C 111 ? VAL C 126 ? THR C 106 VAL C 121 
AA4 1 GLU D 176 ? LYS D 182 ? GLU D 171 LYS D 177 
AA4 2 THR D 111 ? VAL D 126 ? THR D 106 VAL D 121 
AA4 3 VAL D 167 ? ARG D 173 ? VAL D 162 ARG D 168 
AA4 4 THR D 66  ? ASN D 72  ? THR D 61  ASN D 67  
AA4 5 HIS D 43  ? VAL D 51  ? HIS D 38  VAL D 46  
AA4 6 LEU D 29  ? SER D 34  ? LEU D 24  SER D 29  
AA4 7 ALA D 85  ? VAL D 98  ? ALA D 80  VAL D 93  
AA4 8 THR D 111 ? VAL D 126 ? THR D 106 VAL D 121 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 O ASP A 178 ? O ASP A 173 N GLN A 118 ? N GLN A 113 
AA1 2 3 N ARG A 124 ? N ARG A 119 O ARG A 171 ? O ARG A 166 
AA1 3 4 O GLY A 168 ? O GLY A 163 N MET A 71  ? N MET A 66  
AA1 4 5 O TRP A 68  ? O TRP A 63  N ILE A 50  ? N ILE A 45  
AA1 5 6 O THR A 45  ? O THR A 40  N LEU A 32  ? N LEU A 27  
AA1 6 7 N ALA A 33  ? N ALA A 28  O VAL A 88  ? O VAL A 83  
AA1 7 8 N PHE A 91  ? N PHE A 86  O VAL A 117 ? O VAL A 112 
AA2 3 4 O VAL B 88  ? O VAL B 83  N ALA B 33  ? N ALA B 28  
AA2 4 5 N LEU B 32  ? N LEU B 27  O THR B 45  ? O THR B 40  
AA2 5 6 N ILE B 50  ? N ILE B 45  O TRP B 68  ? O TRP B 63  
AA2 6 7 N MET B 71  ? N MET B 66  O GLY B 168 ? O GLY B 163 
AA2 7 8 O ARG B 171 ? O ARG B 166 N ARG B 124 ? N ARG B 119 
AA2 8 9 N SER B 116 ? N SER B 111 O MET B 180 ? O MET B 175 
AA3 1 2 O MET C 180 ? O MET C 175 N SER C 116 ? N SER C 111 
AA3 2 3 N VAL C 126 ? N VAL C 121 O ALA C 169 ? O ALA C 164 
AA3 3 4 O LEU C 172 ? O LEU C 167 N LEU C 67  ? N LEU C 62  
AA3 4 5 O TRP C 68  ? O TRP C 63  N ILE C 50  ? N ILE C 45  
AA3 5 6 O THR C 45  ? O THR C 40  N LEU C 32  ? N LEU C 27  
AA3 6 7 N ALA C 33  ? N ALA C 28  O VAL C 88  ? O VAL C 83  
AA3 7 8 N PHE C 91  ? N PHE C 86  O VAL C 117 ? O VAL C 112 
AA4 1 2 O MET D 180 ? O MET D 175 N SER D 116 ? N SER D 111 
AA4 2 3 N VAL D 126 ? N VAL D 121 O ALA D 169 ? O ALA D 164 
AA4 3 4 O GLY D 168 ? O GLY D 163 N MET D 71  ? N MET D 66  
AA4 4 5 O TRP D 68  ? O TRP D 63  N ILE D 50  ? N ILE D 45  
AA4 5 6 O THR D 45  ? O THR D 40  N LEU D 32  ? N LEU D 27  
AA4 6 7 N ALA D 33  ? N ALA D 28  O VAL D 88  ? O VAL D 83  
AA4 7 8 N ALA D 85  ? N ALA D 80  O LEU D 123 ? O LEU D 118 
# 
_pdbx_entry_details.entry_id                   9JN5 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1  1 O   C MET 148 ? ? O C HOH 401 ? ? 1.68 
2  1 O   C HOH 415 ? ? O C HOH 540 ? ? 1.98 
3  1 O   B HOH 527 ? ? O C HOH 552 ? ? 1.98 
4  1 O   C HOH 410 ? ? O C HOH 492 ? ? 1.99 
5  1 O   B HOH 516 ? ? O C HOH 496 ? ? 2.01 
6  1 O   B ASN 90  ? ? O B HOH 401 ? ? 2.05 
7  1 O   D HOH 405 ? ? O D HOH 425 ? ? 2.06 
8  1 O   A HOH 446 ? ? O A HOH 501 ? ? 2.06 
9  1 O   A HOH 552 ? ? O D HOH 447 ? ? 2.09 
10 1 O   A HOH 512 ? ? O D HOH 405 ? ? 2.11 
11 1 O   C HOH 405 ? ? O C HOH 490 ? ? 2.12 
12 1 N   A MET 1   ? ? O A HOH 401 ? ? 2.12 
13 1 O   B HOH 482 ? ? O B HOH 526 ? ? 2.13 
14 1 O   C HOH 402 ? ? O C HOH 502 ? ? 2.14 
15 1 O   C HOH 483 ? ? O C HOH 543 ? ? 2.15 
16 1 OD1 A ASP 125 ? ? O A HOH 402 ? ? 2.15 
17 1 OD1 C ASP 126 ? ? O C HOH 402 ? ? 2.15 
18 1 OH  D TYR 154 ? ? O D HOH 401 ? ? 2.15 
19 1 O   A ASN 90  ? ? O A HOH 403 ? ? 2.15 
20 1 CD2 A LEU 159 ? ? O A HOH 408 ? ? 2.16 
21 1 O   C HOH 475 ? ? O D HOH 573 ? ? 2.16 
22 1 O   C HOH 538 ? ? O C HOH 545 ? ? 2.17 
23 1 O   A HOH 559 ? ? O D HOH 534 ? ? 2.17 
24 1 O   B HOH 422 ? ? O B HOH 526 ? ? 2.19 
# 
loop_
_pdbx_validate_symm_contact.id 
_pdbx_validate_symm_contact.PDB_model_num 
_pdbx_validate_symm_contact.auth_atom_id_1 
_pdbx_validate_symm_contact.auth_asym_id_1 
_pdbx_validate_symm_contact.auth_comp_id_1 
_pdbx_validate_symm_contact.auth_seq_id_1 
_pdbx_validate_symm_contact.PDB_ins_code_1 
_pdbx_validate_symm_contact.label_alt_id_1 
_pdbx_validate_symm_contact.site_symmetry_1 
_pdbx_validate_symm_contact.auth_atom_id_2 
_pdbx_validate_symm_contact.auth_asym_id_2 
_pdbx_validate_symm_contact.auth_comp_id_2 
_pdbx_validate_symm_contact.auth_seq_id_2 
_pdbx_validate_symm_contact.PDB_ins_code_2 
_pdbx_validate_symm_contact.label_alt_id_2 
_pdbx_validate_symm_contact.site_symmetry_2 
_pdbx_validate_symm_contact.dist 
1 1 O B HOH 547 ? ? 1_555 O C HOH 570 ? ? 3_545 1.94 
2 1 O B HOH 546 ? ? 1_555 O C HOH 566 ? ? 3_545 2.08 
# 
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 HIS A 22  ? ? -141.16 57.82  
2  1 ASP A 47  ? ? -32.07  108.59 
3  1 ALA A 79  ? ? 83.96   33.73  
4  1 ALA A 144 ? ? -146.02 35.28  
5  1 PHE A 176 ? ? -116.31 75.41  
6  1 HIS B 22  ? ? -145.71 57.60  
7  1 ASP B 47  ? ? -27.07  108.93 
8  1 ALA B 144 ? ? -143.77 38.23  
9  1 PHE B 176 ? ? -113.39 79.33  
10 1 ASP C 47  ? ? -30.71  111.85 
11 1 ALA C 79  ? ? -103.15 57.80  
12 1 ASP D 47  ? ? -29.65  109.04 
13 1 LEU D 178 ? ? -140.26 34.91  
# 
loop_
_pdbx_distant_solvent_atoms.id 
_pdbx_distant_solvent_atoms.PDB_model_num 
_pdbx_distant_solvent_atoms.auth_atom_id 
_pdbx_distant_solvent_atoms.label_alt_id 
_pdbx_distant_solvent_atoms.auth_asym_id 
_pdbx_distant_solvent_atoms.auth_comp_id 
_pdbx_distant_solvent_atoms.auth_seq_id 
_pdbx_distant_solvent_atoms.PDB_ins_code 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance 
1  1 O ? A HOH 612 ? 5.82 . 
2  1 O ? A HOH 613 ? 5.82 . 
3  1 O ? A HOH 614 ? 5.94 . 
4  1 O ? A HOH 615 ? 6.05 . 
5  1 O ? A HOH 616 ? 6.19 . 
6  1 O ? A HOH 617 ? 6.26 . 
7  1 O ? A HOH 618 ? 6.30 . 
8  1 O ? A HOH 619 ? 6.53 . 
9  1 O ? A HOH 620 ? 6.60 . 
10 1 O ? A HOH 621 ? 7.16 . 
11 1 O ? A HOH 622 ? 7.35 . 
12 1 O ? B HOH 544 ? 6.05 . 
13 1 O ? B HOH 545 ? 6.19 . 
14 1 O ? B HOH 546 ? 6.21 . 
15 1 O ? B HOH 547 ? 6.93 . 
16 1 O ? B HOH 548 ? 7.45 . 
17 1 O ? B HOH 549 ? 8.43 . 
18 1 O ? C HOH 576 ? 5.88 . 
19 1 O ? C HOH 577 ? 5.91 . 
20 1 O ? C HOH 578 ? 5.97 . 
21 1 O ? C HOH 579 ? 6.35 . 
22 1 O ? C HOH 580 ? 6.42 . 
23 1 O ? C HOH 581 ? 6.50 . 
24 1 O ? C HOH 582 ? 6.56 . 
25 1 O ? C HOH 583 ? 6.66 . 
26 1 O ? C HOH 584 ? 6.72 . 
27 1 O ? C HOH 585 ? 7.01 . 
28 1 O ? C HOH 586 ? 7.08 . 
29 1 O ? D HOH 584 ? 5.94 . 
30 1 O ? D HOH 585 ? 6.15 . 
31 1 O ? D HOH 586 ? 6.27 . 
32 1 O ? D HOH 587 ? 7.47 . 
# 
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 ALA -4  ? A ALA 1   
2  1 Y 1 A GLY -3  ? A GLY 2   
3  1 Y 1 A ALA -2  ? A ALA 3   
4  1 Y 1 A GLY -1  ? A GLY 4   
5  1 Y 1 A ALA 0   ? A ALA 5   
6  1 Y 1 A THR 212 ? A THR 217 
7  1 Y 1 A GLU 213 ? A GLU 218 
8  1 Y 1 B ALA -4  ? B ALA 1   
9  1 Y 1 B GLY -3  ? B GLY 2   
10 1 Y 1 B ALA -2  ? B ALA 3   
11 1 Y 1 B GLY -1  ? B GLY 4   
12 1 Y 1 B THR 212 ? B THR 217 
13 1 Y 1 B GLU 213 ? B GLU 218 
14 1 Y 1 C ALA -4  ? C ALA 1   
15 1 Y 1 C GLY -3  ? C GLY 2   
16 1 Y 1 C ALA -2  ? C ALA 3   
17 1 Y 1 C THR 212 ? C THR 217 
18 1 Y 1 C GLU 213 ? C GLU 218 
19 1 Y 1 D ALA -4  ? D ALA 1   
20 1 Y 1 D GLY -3  ? D GLY 2   
21 1 Y 1 D ALA -2  ? D ALA 3   
22 1 Y 1 D THR 212 ? D THR 217 
23 1 Y 1 D GLU 213 ? D GLU 218 
# 
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 
HEM CHA  C  N N 137 
HEM CHB  C  N N 138 
HEM CHC  C  N N 139 
HEM CHD  C  N N 140 
HEM C1A  C  Y N 141 
HEM C2A  C  Y N 142 
HEM C3A  C  Y N 143 
HEM C4A  C  Y N 144 
HEM CMA  C  N N 145 
HEM CAA  C  N N 146 
HEM CBA  C  N N 147 
HEM CGA  C  N N 148 
HEM O1A  O  N N 149 
HEM O2A  O  N N 150 
HEM C1B  C  N N 151 
HEM C2B  C  N N 152 
HEM C3B  C  N N 153 
HEM C4B  C  N N 154 
HEM CMB  C  N N 155 
HEM CAB  C  N N 156 
HEM CBB  C  N N 157 
HEM C1C  C  Y N 158 
HEM C2C  C  Y N 159 
HEM C3C  C  Y N 160 
HEM C4C  C  Y N 161 
HEM CMC  C  N N 162 
HEM CAC  C  N N 163 
HEM CBC  C  N N 164 
HEM C1D  C  N N 165 
HEM C2D  C  N N 166 
HEM C3D  C  N N 167 
HEM C4D  C  N N 168 
HEM CMD  C  N N 169 
HEM CAD  C  N N 170 
HEM CBD  C  N N 171 
HEM CGD  C  N N 172 
HEM O1D  O  N N 173 
HEM O2D  O  N N 174 
HEM NA   N  Y N 175 
HEM NB   N  N N 176 
HEM NC   N  Y N 177 
HEM ND   N  N N 178 
HEM FE   FE N N 179 
HEM HHB  H  N N 180 
HEM HHC  H  N N 181 
HEM HHD  H  N N 182 
HEM HMA  H  N N 183 
HEM HMAA H  N N 184 
HEM HMAB H  N N 185 
HEM HAA  H  N N 186 
HEM HAAA H  N N 187 
HEM HBA  H  N N 188 
HEM HBAA H  N N 189 
HEM HMB  H  N N 190 
HEM HMBA H  N N 191 
HEM HMBB H  N N 192 
HEM HAB  H  N N 193 
HEM HBB  H  N N 194 
HEM HBBA H  N N 195 
HEM HMC  H  N N 196 
HEM HMCA H  N N 197 
HEM HMCB H  N N 198 
HEM HAC  H  N N 199 
HEM HBC  H  N N 200 
HEM HBCA H  N N 201 
HEM HMD  H  N N 202 
HEM HMDA H  N N 203 
HEM HMDB H  N N 204 
HEM HAD  H  N N 205 
HEM HADA H  N N 206 
HEM HBD  H  N N 207 
HEM HBDA H  N N 208 
HEM H2A  H  N N 209 
HEM H2D  H  N N 210 
HEM HHA  H  N N 211 
HIS N    N  N N 212 
HIS CA   C  N S 213 
HIS C    C  N N 214 
HIS O    O  N N 215 
HIS CB   C  N N 216 
HIS CG   C  Y N 217 
HIS ND1  N  Y N 218 
HIS CD2  C  Y N 219 
HIS CE1  C  Y N 220 
HIS NE2  N  Y N 221 
HIS OXT  O  N N 222 
HIS H    H  N N 223 
HIS H2   H  N N 224 
HIS HA   H  N N 225 
HIS HB2  H  N N 226 
HIS HB3  H  N N 227 
HIS HD1  H  N N 228 
HIS HD2  H  N N 229 
HIS HE1  H  N N 230 
HIS HE2  H  N N 231 
HIS HXT  H  N N 232 
HOH O    O  N N 233 
HOH H1   H  N N 234 
HOH H2   H  N N 235 
ILE N    N  N N 236 
ILE CA   C  N S 237 
ILE C    C  N N 238 
ILE O    O  N N 239 
ILE CB   C  N S 240 
ILE CG1  C  N N 241 
ILE CG2  C  N N 242 
ILE CD1  C  N N 243 
ILE OXT  O  N N 244 
ILE H    H  N N 245 
ILE H2   H  N N 246 
ILE HA   H  N N 247 
ILE HB   H  N N 248 
ILE HG12 H  N N 249 
ILE HG13 H  N N 250 
ILE HG21 H  N N 251 
ILE HG22 H  N N 252 
ILE HG23 H  N N 253 
ILE HD11 H  N N 254 
ILE HD12 H  N N 255 
ILE HD13 H  N N 256 
ILE HXT  H  N N 257 
LEU N    N  N N 258 
LEU CA   C  N S 259 
LEU C    C  N N 260 
LEU O    O  N N 261 
LEU CB   C  N N 262 
LEU CG   C  N N 263 
LEU CD1  C  N N 264 
LEU CD2  C  N N 265 
LEU OXT  O  N N 266 
LEU H    H  N N 267 
LEU H2   H  N N 268 
LEU HA   H  N N 269 
LEU HB2  H  N N 270 
LEU HB3  H  N N 271 
LEU HG   H  N N 272 
LEU HD11 H  N N 273 
LEU HD12 H  N N 274 
LEU HD13 H  N N 275 
LEU HD21 H  N N 276 
LEU HD22 H  N N 277 
LEU HD23 H  N N 278 
LEU HXT  H  N N 279 
LYS N    N  N N 280 
LYS CA   C  N S 281 
LYS C    C  N N 282 
LYS O    O  N N 283 
LYS CB   C  N N 284 
LYS CG   C  N N 285 
LYS CD   C  N N 286 
LYS CE   C  N N 287 
LYS NZ   N  N N 288 
LYS OXT  O  N N 289 
LYS H    H  N N 290 
LYS H2   H  N N 291 
LYS HA   H  N N 292 
LYS HB2  H  N N 293 
LYS HB3  H  N N 294 
LYS HG2  H  N N 295 
LYS HG3  H  N N 296 
LYS HD2  H  N N 297 
LYS HD3  H  N N 298 
LYS HE2  H  N N 299 
LYS HE3  H  N N 300 
LYS HZ1  H  N N 301 
LYS HZ2  H  N N 302 
LYS HZ3  H  N N 303 
LYS HXT  H  N N 304 
MET N    N  N N 305 
MET CA   C  N S 306 
MET C    C  N N 307 
MET O    O  N N 308 
MET CB   C  N N 309 
MET CG   C  N N 310 
MET SD   S  N N 311 
MET CE   C  N N 312 
MET OXT  O  N N 313 
MET H    H  N N 314 
MET H2   H  N N 315 
MET HA   H  N N 316 
MET HB2  H  N N 317 
MET HB3  H  N N 318 
MET HG2  H  N N 319 
MET HG3  H  N N 320 
MET HE1  H  N N 321 
MET HE2  H  N N 322 
MET HE3  H  N N 323 
MET HXT  H  N N 324 
ONH C    C  N N 325 
ONH N    N  N N 326 
ONH O    O  N N 327 
ONH CA   C  N S 328 
ONH CB   C  N N 329 
ONH CD   C  N N 330 
ONH NE   N  N N 331 
ONH CG   C  N N 332 
ONH OZ   O  N N 333 
ONH OXT  O  N N 334 
ONH HN   H  N N 335 
ONH HNA  H  N N 336 
ONH HA   H  N N 337 
ONH HB   H  N N 338 
ONH HBA  H  N N 339 
ONH HD   H  N N 340 
ONH HDA  H  N N 341 
ONH HG   H  N N 342 
ONH HGA  H  N N 343 
ONH HOXT H  N N 344 
ONH HOZ  H  N N 345 
ONH HNE  H  N N 346 
PHE N    N  N N 347 
PHE CA   C  N S 348 
PHE C    C  N N 349 
PHE O    O  N N 350 
PHE CB   C  N N 351 
PHE CG   C  Y N 352 
PHE CD1  C  Y N 353 
PHE CD2  C  Y N 354 
PHE CE1  C  Y N 355 
PHE CE2  C  Y N 356 
PHE CZ   C  Y N 357 
PHE OXT  O  N N 358 
PHE H    H  N N 359 
PHE H2   H  N N 360 
PHE HA   H  N N 361 
PHE HB2  H  N N 362 
PHE HB3  H  N N 363 
PHE HD1  H  N N 364 
PHE HD2  H  N N 365 
PHE HE1  H  N N 366 
PHE HE2  H  N N 367 
PHE HZ   H  N N 368 
PHE HXT  H  N N 369 
PRO N    N  N N 370 
PRO CA   C  N S 371 
PRO C    C  N N 372 
PRO O    O  N N 373 
PRO CB   C  N N 374 
PRO CG   C  N N 375 
PRO CD   C  N N 376 
PRO OXT  O  N N 377 
PRO H    H  N N 378 
PRO HA   H  N N 379 
PRO HB2  H  N N 380 
PRO HB3  H  N N 381 
PRO HG2  H  N N 382 
PRO HG3  H  N N 383 
PRO HD2  H  N N 384 
PRO HD3  H  N N 385 
PRO HXT  H  N N 386 
SER N    N  N N 387 
SER CA   C  N S 388 
SER C    C  N N 389 
SER O    O  N N 390 
SER CB   C  N N 391 
SER OG   O  N N 392 
SER OXT  O  N N 393 
SER H    H  N N 394 
SER H2   H  N N 395 
SER HA   H  N N 396 
SER HB2  H  N N 397 
SER HB3  H  N N 398 
SER HG   H  N N 399 
SER HXT  H  N N 400 
THR N    N  N N 401 
THR CA   C  N S 402 
THR C    C  N N 403 
THR O    O  N N 404 
THR CB   C  N R 405 
THR OG1  O  N N 406 
THR CG2  C  N N 407 
THR OXT  O  N N 408 
THR H    H  N N 409 
THR H2   H  N N 410 
THR HA   H  N N 411 
THR HB   H  N N 412 
THR HG1  H  N N 413 
THR HG21 H  N N 414 
THR HG22 H  N N 415 
THR HG23 H  N N 416 
THR HXT  H  N N 417 
TRP N    N  N N 418 
TRP CA   C  N S 419 
TRP C    C  N N 420 
TRP O    O  N N 421 
TRP CB   C  N N 422 
TRP CG   C  Y N 423 
TRP CD1  C  Y N 424 
TRP CD2  C  Y N 425 
TRP NE1  N  Y N 426 
TRP CE2  C  Y N 427 
TRP CE3  C  Y N 428 
TRP CZ2  C  Y N 429 
TRP CZ3  C  Y N 430 
TRP CH2  C  Y N 431 
TRP OXT  O  N N 432 
TRP H    H  N N 433 
TRP H2   H  N N 434 
TRP HA   H  N N 435 
TRP HB2  H  N N 436 
TRP HB3  H  N N 437 
TRP HD1  H  N N 438 
TRP HE1  H  N N 439 
TRP HE3  H  N N 440 
TRP HZ2  H  N N 441 
TRP HZ3  H  N N 442 
TRP HH2  H  N N 443 
TRP HXT  H  N N 444 
TYR N    N  N N 445 
TYR CA   C  N S 446 
TYR C    C  N N 447 
TYR O    O  N N 448 
TYR CB   C  N N 449 
TYR CG   C  Y N 450 
TYR CD1  C  Y N 451 
TYR CD2  C  Y N 452 
TYR CE1  C  Y N 453 
TYR CE2  C  Y N 454 
TYR CZ   C  Y N 455 
TYR OH   O  N N 456 
TYR OXT  O  N N 457 
TYR H    H  N N 458 
TYR H2   H  N N 459 
TYR HA   H  N N 460 
TYR HB2  H  N N 461 
TYR HB3  H  N N 462 
TYR HD1  H  N N 463 
TYR HD2  H  N N 464 
TYR HE1  H  N N 465 
TYR HE2  H  N N 466 
TYR HH   H  N N 467 
TYR HXT  H  N N 468 
VAL N    N  N N 469 
VAL CA   C  N S 470 
VAL C    C  N N 471 
VAL O    O  N N 472 
VAL CB   C  N N 473 
VAL CG1  C  N N 474 
VAL CG2  C  N N 475 
VAL OXT  O  N N 476 
VAL H    H  N N 477 
VAL H2   H  N N 478 
VAL HA   H  N N 479 
VAL HB   H  N N 480 
VAL HG11 H  N N 481 
VAL HG12 H  N N 482 
VAL HG13 H  N N 483 
VAL HG21 H  N N 484 
VAL HG22 H  N N 485 
VAL HG23 H  N N 486 
VAL HXT  H  N N 487 
# 
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 
HEM CHA C1A  sing N N 129 
HEM CHA C4D  doub N N 130 
HEM CHA HHA  sing N N 131 
HEM CHB C4A  sing N N 132 
HEM CHB C1B  doub N N 133 
HEM CHB HHB  sing N N 134 
HEM CHC C4B  sing N N 135 
HEM CHC C1C  doub N N 136 
HEM CHC HHC  sing N N 137 
HEM CHD C4C  doub N N 138 
HEM CHD C1D  sing N N 139 
HEM CHD HHD  sing N N 140 
HEM C1A C2A  doub Y N 141 
HEM C1A NA   sing Y N 142 
HEM C2A C3A  sing Y N 143 
HEM C2A CAA  sing N N 144 
HEM C3A C4A  doub Y N 145 
HEM C3A CMA  sing N N 146 
HEM C4A NA   sing Y N 147 
HEM CMA HMA  sing N N 148 
HEM CMA HMAA sing N N 149 
HEM CMA HMAB sing N N 150 
HEM CAA CBA  sing N N 151 
HEM CAA HAA  sing N N 152 
HEM CAA HAAA sing N N 153 
HEM CBA CGA  sing N N 154 
HEM CBA HBA  sing N N 155 
HEM CBA HBAA sing N N 156 
HEM CGA O1A  doub N N 157 
HEM CGA O2A  sing N N 158 
HEM C1B C2B  sing N N 159 
HEM C1B NB   sing N N 160 
HEM C2B C3B  doub N N 161 
HEM C2B CMB  sing N N 162 
HEM C3B C4B  sing N N 163 
HEM C3B CAB  sing N N 164 
HEM C4B NB   doub N N 165 
HEM CMB HMB  sing N N 166 
HEM CMB HMBA sing N N 167 
HEM CMB HMBB sing N N 168 
HEM CAB CBB  doub N N 169 
HEM CAB HAB  sing N N 170 
HEM CBB HBB  sing N N 171 
HEM CBB HBBA sing N N 172 
HEM C1C C2C  sing Y N 173 
HEM C1C NC   sing Y N 174 
HEM C2C C3C  doub Y N 175 
HEM C2C CMC  sing N N 176 
HEM C3C C4C  sing Y N 177 
HEM C3C CAC  sing N N 178 
HEM C4C NC   sing Y N 179 
HEM CMC HMC  sing N N 180 
HEM CMC HMCA sing N N 181 
HEM CMC HMCB sing N N 182 
HEM CAC CBC  doub N N 183 
HEM CAC HAC  sing N N 184 
HEM CBC HBC  sing N N 185 
HEM CBC HBCA sing N N 186 
HEM C1D C2D  sing N N 187 
HEM C1D ND   doub N N 188 
HEM C2D C3D  doub N N 189 
HEM C2D CMD  sing N N 190 
HEM C3D C4D  sing N N 191 
HEM C3D CAD  sing N N 192 
HEM C4D ND   sing N N 193 
HEM CMD HMD  sing N N 194 
HEM CMD HMDA sing N N 195 
HEM CMD HMDB sing N N 196 
HEM CAD CBD  sing N N 197 
HEM CAD HAD  sing N N 198 
HEM CAD HADA sing N N 199 
HEM CBD CGD  sing N N 200 
HEM CBD HBD  sing N N 201 
HEM CBD HBDA sing N N 202 
HEM CGD O1D  doub N N 203 
HEM CGD O2D  sing N N 204 
HEM O2A H2A  sing N N 205 
HEM O2D H2D  sing N N 206 
HEM FE  NA   sing N N 207 
HEM FE  NB   sing N N 208 
HEM FE  NC   sing N N 209 
HEM FE  ND   sing N N 210 
HIS N   CA   sing N N 211 
HIS N   H    sing N N 212 
HIS N   H2   sing N N 213 
HIS CA  C    sing N N 214 
HIS CA  CB   sing N N 215 
HIS CA  HA   sing N N 216 
HIS C   O    doub N N 217 
HIS C   OXT  sing N N 218 
HIS CB  CG   sing N N 219 
HIS CB  HB2  sing N N 220 
HIS CB  HB3  sing N N 221 
HIS CG  ND1  sing Y N 222 
HIS CG  CD2  doub Y N 223 
HIS ND1 CE1  doub Y N 224 
HIS ND1 HD1  sing N N 225 
HIS CD2 NE2  sing Y N 226 
HIS CD2 HD2  sing N N 227 
HIS CE1 NE2  sing Y N 228 
HIS CE1 HE1  sing N N 229 
HIS NE2 HE2  sing N N 230 
HIS OXT HXT  sing N N 231 
HOH O   H1   sing N N 232 
HOH O   H2   sing N N 233 
ILE N   CA   sing N N 234 
ILE N   H    sing N N 235 
ILE N   H2   sing N N 236 
ILE CA  C    sing N N 237 
ILE CA  CB   sing N N 238 
ILE CA  HA   sing N N 239 
ILE C   O    doub N N 240 
ILE C   OXT  sing N N 241 
ILE CB  CG1  sing N N 242 
ILE CB  CG2  sing N N 243 
ILE CB  HB   sing N N 244 
ILE CG1 CD1  sing N N 245 
ILE CG1 HG12 sing N N 246 
ILE CG1 HG13 sing N N 247 
ILE CG2 HG21 sing N N 248 
ILE CG2 HG22 sing N N 249 
ILE CG2 HG23 sing N N 250 
ILE CD1 HD11 sing N N 251 
ILE CD1 HD12 sing N N 252 
ILE CD1 HD13 sing N N 253 
ILE OXT HXT  sing N N 254 
LEU N   CA   sing N N 255 
LEU N   H    sing N N 256 
LEU N   H2   sing N N 257 
LEU CA  C    sing N N 258 
LEU CA  CB   sing N N 259 
LEU CA  HA   sing N N 260 
LEU C   O    doub N N 261 
LEU C   OXT  sing N N 262 
LEU CB  CG   sing N N 263 
LEU CB  HB2  sing N N 264 
LEU CB  HB3  sing N N 265 
LEU CG  CD1  sing N N 266 
LEU CG  CD2  sing N N 267 
LEU CG  HG   sing N N 268 
LEU CD1 HD11 sing N N 269 
LEU CD1 HD12 sing N N 270 
LEU CD1 HD13 sing N N 271 
LEU CD2 HD21 sing N N 272 
LEU CD2 HD22 sing N N 273 
LEU CD2 HD23 sing N N 274 
LEU OXT HXT  sing N N 275 
LYS N   CA   sing N N 276 
LYS N   H    sing N N 277 
LYS N   H2   sing N N 278 
LYS CA  C    sing N N 279 
LYS CA  CB   sing N N 280 
LYS CA  HA   sing N N 281 
LYS C   O    doub N N 282 
LYS C   OXT  sing N N 283 
LYS CB  CG   sing N N 284 
LYS CB  HB2  sing N N 285 
LYS CB  HB3  sing N N 286 
LYS CG  CD   sing N N 287 
LYS CG  HG2  sing N N 288 
LYS CG  HG3  sing N N 289 
LYS CD  CE   sing N N 290 
LYS CD  HD2  sing N N 291 
LYS CD  HD3  sing N N 292 
LYS CE  NZ   sing N N 293 
LYS CE  HE2  sing N N 294 
LYS CE  HE3  sing N N 295 
LYS NZ  HZ1  sing N N 296 
LYS NZ  HZ2  sing N N 297 
LYS NZ  HZ3  sing N N 298 
LYS OXT HXT  sing N N 299 
MET N   CA   sing N N 300 
MET N   H    sing N N 301 
MET N   H2   sing N N 302 
MET CA  C    sing N N 303 
MET CA  CB   sing N N 304 
MET CA  HA   sing N N 305 
MET C   O    doub N N 306 
MET C   OXT  sing N N 307 
MET CB  CG   sing N N 308 
MET CB  HB2  sing N N 309 
MET CB  HB3  sing N N 310 
MET CG  SD   sing N N 311 
MET CG  HG2  sing N N 312 
MET CG  HG3  sing N N 313 
MET SD  CE   sing N N 314 
MET CE  HE1  sing N N 315 
MET CE  HE2  sing N N 316 
MET CE  HE3  sing N N 317 
MET OXT HXT  sing N N 318 
ONH O   C    doub N N 319 
ONH C   OXT  sing N N 320 
ONH C   CA   sing N N 321 
ONH N   CA   sing N N 322 
ONH N   HN   sing N N 323 
ONH N   HNA  sing N N 324 
ONH CB  CA   sing N N 325 
ONH CA  HA   sing N N 326 
ONH CB  CG   sing N N 327 
ONH CB  HB   sing N N 328 
ONH CB  HBA  sing N N 329 
ONH CD  CG   sing N N 330 
ONH CD  NE   sing N N 331 
ONH CD  HD   sing N N 332 
ONH CD  HDA  sing N N 333 
ONH OZ  NE   sing N N 334 
ONH CG  HG   sing N N 335 
ONH CG  HGA  sing N N 336 
ONH OXT HOXT sing N N 337 
ONH OZ  HOZ  sing N N 338 
ONH NE  HNE  sing N N 339 
PHE N   CA   sing N N 340 
PHE N   H    sing N N 341 
PHE N   H2   sing N N 342 
PHE CA  C    sing N N 343 
PHE CA  CB   sing N N 344 
PHE CA  HA   sing N N 345 
PHE C   O    doub N N 346 
PHE C   OXT  sing N N 347 
PHE CB  CG   sing N N 348 
PHE CB  HB2  sing N N 349 
PHE CB  HB3  sing N N 350 
PHE CG  CD1  doub Y N 351 
PHE CG  CD2  sing Y N 352 
PHE CD1 CE1  sing Y N 353 
PHE CD1 HD1  sing N N 354 
PHE CD2 CE2  doub Y N 355 
PHE CD2 HD2  sing N N 356 
PHE CE1 CZ   doub Y N 357 
PHE CE1 HE1  sing N N 358 
PHE CE2 CZ   sing Y N 359 
PHE CE2 HE2  sing N N 360 
PHE CZ  HZ   sing N N 361 
PHE OXT HXT  sing N N 362 
PRO N   CA   sing N N 363 
PRO N   CD   sing N N 364 
PRO N   H    sing N N 365 
PRO CA  C    sing N N 366 
PRO CA  CB   sing N N 367 
PRO CA  HA   sing N N 368 
PRO C   O    doub N N 369 
PRO C   OXT  sing N N 370 
PRO CB  CG   sing N N 371 
PRO CB  HB2  sing N N 372 
PRO CB  HB3  sing N N 373 
PRO CG  CD   sing N N 374 
PRO CG  HG2  sing N N 375 
PRO CG  HG3  sing N N 376 
PRO CD  HD2  sing N N 377 
PRO CD  HD3  sing N N 378 
PRO OXT HXT  sing N N 379 
SER N   CA   sing N N 380 
SER N   H    sing N N 381 
SER N   H2   sing N N 382 
SER CA  C    sing N N 383 
SER CA  CB   sing N N 384 
SER CA  HA   sing N N 385 
SER C   O    doub N N 386 
SER C   OXT  sing N N 387 
SER CB  OG   sing N N 388 
SER CB  HB2  sing N N 389 
SER CB  HB3  sing N N 390 
SER OG  HG   sing N N 391 
SER OXT HXT  sing N N 392 
THR N   CA   sing N N 393 
THR N   H    sing N N 394 
THR N   H2   sing N N 395 
THR CA  C    sing N N 396 
THR CA  CB   sing N N 397 
THR CA  HA   sing N N 398 
THR C   O    doub N N 399 
THR C   OXT  sing N N 400 
THR CB  OG1  sing N N 401 
THR CB  CG2  sing N N 402 
THR CB  HB   sing N N 403 
THR OG1 HG1  sing N N 404 
THR CG2 HG21 sing N N 405 
THR CG2 HG22 sing N N 406 
THR CG2 HG23 sing N N 407 
THR OXT HXT  sing N N 408 
TRP N   CA   sing N N 409 
TRP N   H    sing N N 410 
TRP N   H2   sing N N 411 
TRP CA  C    sing N N 412 
TRP CA  CB   sing N N 413 
TRP CA  HA   sing N N 414 
TRP C   O    doub N N 415 
TRP C   OXT  sing N N 416 
TRP CB  CG   sing N N 417 
TRP CB  HB2  sing N N 418 
TRP CB  HB3  sing N N 419 
TRP CG  CD1  doub Y N 420 
TRP CG  CD2  sing Y N 421 
TRP CD1 NE1  sing Y N 422 
TRP CD1 HD1  sing N N 423 
TRP CD2 CE2  doub Y N 424 
TRP CD2 CE3  sing Y N 425 
TRP NE1 CE2  sing Y N 426 
TRP NE1 HE1  sing N N 427 
TRP CE2 CZ2  sing Y N 428 
TRP CE3 CZ3  doub Y N 429 
TRP CE3 HE3  sing N N 430 
TRP CZ2 CH2  doub Y N 431 
TRP CZ2 HZ2  sing N N 432 
TRP CZ3 CH2  sing Y N 433 
TRP CZ3 HZ3  sing N N 434 
TRP CH2 HH2  sing N N 435 
TRP OXT HXT  sing N N 436 
TYR N   CA   sing N N 437 
TYR N   H    sing N N 438 
TYR N   H2   sing N N 439 
TYR CA  C    sing N N 440 
TYR CA  CB   sing N N 441 
TYR CA  HA   sing N N 442 
TYR C   O    doub N N 443 
TYR C   OXT  sing N N 444 
TYR CB  CG   sing N N 445 
TYR CB  HB2  sing N N 446 
TYR CB  HB3  sing N N 447 
TYR CG  CD1  doub Y N 448 
TYR CG  CD2  sing Y N 449 
TYR CD1 CE1  sing Y N 450 
TYR CD1 HD1  sing N N 451 
TYR CD2 CE2  doub Y N 452 
TYR CD2 HD2  sing N N 453 
TYR CE1 CZ   doub Y N 454 
TYR CE1 HE1  sing N N 455 
TYR CE2 CZ   sing Y N 456 
TYR CE2 HE2  sing N N 457 
TYR CZ  OH   sing N N 458 
TYR OH  HH   sing N N 459 
TYR OXT HXT  sing N N 460 
VAL N   CA   sing N N 461 
VAL N   H    sing N N 462 
VAL N   H2   sing N N 463 
VAL CA  C    sing N N 464 
VAL CA  CB   sing N N 465 
VAL CA  HA   sing N N 466 
VAL C   O    doub N N 467 
VAL C   OXT  sing N N 468 
VAL CB  CG1  sing N N 469 
VAL CB  CG2  sing N N 470 
VAL CB  HB   sing N N 471 
VAL CG1 HG11 sing N N 472 
VAL CG1 HG12 sing N N 473 
VAL CG1 HG13 sing N N 474 
VAL CG2 HG21 sing N N 475 
VAL CG2 HG22 sing N N 476 
VAL CG2 HG23 sing N N 477 
VAL OXT HXT  sing N N 478 
# 
_pdbx_audit_support.funding_organization   'Ministry of Science and Technology (MoST, China)' 
_pdbx_audit_support.country                China 
_pdbx_audit_support.grant_number           2021YFA0911400 
_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                    9JN5 
_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]   0.011027 
_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]   0.009892 
_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]   0.009011 
_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  
FE 
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   . MET A 1 6   ? -15.529 5.504   -24.825 1.00 42.27 ? 1   MET A N   1 
ATOM   2    C  CA  . MET A 1 6   ? -15.077 4.193   -24.228 1.00 41.99 ? 1   MET A CA  1 
ATOM   3    C  C   . MET A 1 6   ? -16.279 3.247   -24.109 1.00 41.31 ? 1   MET A C   1 
ATOM   4    O  O   . MET A 1 6   ? -17.283 3.630   -23.475 1.00 43.88 ? 1   MET A O   1 
ATOM   5    C  CB  . MET A 1 6   ? -14.463 4.352   -22.834 1.00 39.74 ? 1   MET A CB  1 
ATOM   6    C  CG  . MET A 1 6   ? -13.983 3.021   -22.238 1.00 41.51 ? 1   MET A CG  1 
ATOM   7    S  SD  . MET A 1 6   ? -13.298 3.070   -20.540 1.00 41.89 ? 1   MET A SD  1 
ATOM   8    C  CE  . MET A 1 6   ? -12.465 1.480   -20.526 1.00 40.54 ? 1   MET A CE  1 
ATOM   9    N  N   . PHE A 1 7   ? -16.170 2.047   -24.677 1.00 38.63 ? 2   PHE A N   1 
ATOM   10   C  CA  . PHE A 1 7   ? -17.215 0.998   -24.583 1.00 36.64 ? 2   PHE A CA  1 
ATOM   11   C  C   . PHE A 1 7   ? -17.033 0.253   -23.263 1.00 33.81 ? 2   PHE A C   1 
ATOM   12   O  O   . PHE A 1 7   ? -15.963 -0.326  -23.055 1.00 33.18 ? 2   PHE A O   1 
ATOM   13   C  CB  . PHE A 1 7   ? -17.130 0.005   -25.738 1.00 36.95 ? 2   PHE A CB  1 
ATOM   14   C  CG  . PHE A 1 7   ? -18.254 -0.997  -25.740 1.00 37.63 ? 2   PHE A CG  1 
ATOM   15   C  CD1 . PHE A 1 7   ? -19.568 -0.578  -25.894 1.00 39.69 ? 2   PHE A CD1 1 
ATOM   16   C  CD2 . PHE A 1 7   ? -18.005 -2.352  -25.576 1.00 41.10 ? 2   PHE A CD2 1 
ATOM   17   C  CE1 . PHE A 1 7   ? -20.609 -1.497  -25.897 1.00 40.79 ? 2   PHE A CE1 1 
ATOM   18   C  CE2 . PHE A 1 7   ? -19.048 -3.269  -25.579 1.00 42.36 ? 2   PHE A CE2 1 
ATOM   19   C  CZ  . PHE A 1 7   ? -20.347 -2.839  -25.739 1.00 41.81 ? 2   PHE A CZ  1 
ATOM   20   N  N   . VAL A 1 8   ? -18.043 0.302   -22.399 1.00 31.15 ? 3   VAL A N   1 
ATOM   21   C  CA  . VAL A 1 8   ? -18.078 -0.431  -21.101 1.00 29.35 ? 3   VAL A CA  1 
ATOM   22   C  C   . VAL A 1 8   ? -19.426 -1.125  -21.009 1.00 28.73 ? 3   VAL A C   1 
ATOM   23   O  O   . VAL A 1 8   ? -20.441 -0.443  -20.891 1.00 24.78 ? 3   VAL A O   1 
ATOM   24   C  CB  . VAL A 1 8   ? -17.863 0.530   -19.924 1.00 29.00 ? 3   VAL A CB  1 
ATOM   25   C  CG1 . VAL A 1 8   ? -18.003 -0.189  -18.592 1.00 30.85 ? 3   VAL A CG1 1 
ATOM   26   C  CG2 . VAL A 1 8   ? -16.514 1.247   -20.035 1.00 33.02 ? 3   VAL A CG2 1 
ATOM   27   N  N   . PRO A 1 9   ? -19.471 -2.472  -21.063 1.00 30.29 ? 4   PRO A N   1 
ATOM   28   C  CA  . PRO A 1 9   ? -20.717 -3.214  -20.854 1.00 35.05 ? 4   PRO A CA  1 
ATOM   29   C  C   . PRO A 1 9   ? -21.313 -2.973  -19.458 1.00 35.30 ? 4   PRO A C   1 
ATOM   30   O  O   . PRO A 1 9   ? -20.534 -2.873  -18.500 1.00 30.84 ? 4   PRO A O   1 
ATOM   31   C  CB  . PRO A 1 9   ? -20.315 -4.691  -20.992 1.00 32.34 ? 4   PRO A CB  1 
ATOM   32   C  CG  . PRO A 1 9   ? -19.015 -4.650  -21.790 1.00 32.95 ? 4   PRO A CG  1 
ATOM   33   C  CD  . PRO A 1 9   ? -18.338 -3.367  -21.335 1.00 33.53 ? 4   PRO A CD  1 
ATOM   34   N  N   . GLY A 1 10  ? -22.653 -2.934  -19.381 1.00 36.56 ? 5   GLY A N   1 
ATOM   35   C  CA  . GLY A 1 10  ? -23.446 -2.548  -18.191 1.00 37.07 ? 5   GLY A CA  1 
ATOM   36   C  C   . GLY A 1 10  ? -22.934 -3.170  -16.892 1.00 35.19 ? 5   GLY A C   1 
ATOM   37   O  O   . GLY A 1 10  ? -22.669 -2.449  -15.924 1.00 36.48 ? 5   GLY A O   1 
ATOM   38   N  N   . PRO A 1 11  ? -22.724 -4.511  -16.849 1.00 35.16 ? 6   PRO A N   1 
ATOM   39   C  CA  . PRO A 1 11  ? -22.256 -5.184  -15.637 1.00 36.80 ? 6   PRO A CA  1 
ATOM   40   C  C   . PRO A 1 11  ? -20.847 -4.746  -15.174 1.00 32.24 ? 6   PRO A C   1 
ATOM   41   O  O   . PRO A 1 11  ? -20.537 -4.955  -14.020 1.00 34.45 ? 6   PRO A O   1 
ATOM   42   C  CB  . PRO A 1 11  ? -22.245 -6.683  -15.997 1.00 37.18 ? 6   PRO A CB  1 
ATOM   43   C  CG  . PRO A 1 11  ? -23.011 -6.787  -17.295 1.00 38.79 ? 6   PRO A CG  1 
ATOM   44   C  CD  . PRO A 1 11  ? -22.841 -5.445  -17.981 1.00 34.79 ? 6   PRO A CD  1 
ATOM   45   N  N   . TYR A 1 12  ? -20.058 -4.084  -16.021 1.00 28.46 ? 7   TYR A N   1 
ATOM   46   C  CA  . TYR A 1 12  ? -18.654 -3.708  -15.692 1.00 27.34 ? 7   TYR A CA  1 
ATOM   47   C  C   . TYR A 1 12  ? -18.547 -2.224  -15.269 1.00 28.04 ? 7   TYR A C   1 
ATOM   48   O  O   . TYR A 1 12  ? -17.392 -1.691  -15.101 1.00 25.54 ? 7   TYR A O   1 
ATOM   49   C  CB  . TYR A 1 12  ? -17.769 -4.082  -16.880 1.00 28.66 ? 7   TYR A CB  1 
ATOM   50   C  CG  . TYR A 1 12  ? -17.815 -5.541  -17.296 1.00 31.39 ? 7   TYR A CG  1 
ATOM   51   C  CD1 . TYR A 1 12  ? -18.010 -6.542  -16.357 1.00 33.13 ? 7   TYR A CD1 1 
ATOM   52   C  CD2 . TYR A 1 12  ? -17.611 -5.934  -18.614 1.00 32.34 ? 7   TYR A CD2 1 
ATOM   53   C  CE1 . TYR A 1 12  ? -18.046 -7.876  -16.717 1.00 31.41 ? 7   TYR A CE1 1 
ATOM   54   C  CE2 . TYR A 1 12  ? -17.646 -7.269  -19.000 1.00 33.36 ? 7   TYR A CE2 1 
ATOM   55   C  CZ  . TYR A 1 12  ? -17.882 -8.241  -18.039 1.00 33.95 ? 7   TYR A CZ  1 
ATOM   56   O  OH  . TYR A 1 12  ? -17.880 -9.572  -18.328 1.00 36.30 ? 7   TYR A OH  1 
ATOM   57   N  N   . HIS A 1 13  ? -19.676 -1.538  -15.056 1.00 24.87 ? 8   HIS A N   1 
ATOM   58   C  CA  . HIS A 1 13  ? -19.692 -0.143  -14.532 1.00 27.40 ? 8   HIS A CA  1 
ATOM   59   C  C   . HIS A 1 13  ? -19.272 -0.156  -13.069 1.00 24.94 ? 8   HIS A C   1 
ATOM   60   O  O   . HIS A 1 13  ? -19.652 -1.101  -12.381 1.00 25.64 ? 8   HIS A O   1 
ATOM   61   C  CB  . HIS A 1 13  ? -21.076 0.513   -14.692 1.00 30.46 ? 8   HIS A CB  1 
ATOM   62   C  CG  . HIS A 1 13  ? -21.297 0.983   -16.078 1.00 33.62 ? 8   HIS A CG  1 
ATOM   63   N  ND1 . HIS A 1 13  ? -21.440 0.099   -17.129 1.00 36.59 ? 8   HIS A ND1 1 
ATOM   64   C  CD2 . HIS A 1 13  ? -21.291 2.223   -16.611 1.00 38.88 ? 8   HIS A CD2 1 
ATOM   65   C  CE1 . HIS A 1 13  ? -21.557 0.775   -18.253 1.00 35.44 ? 8   HIS A CE1 1 
ATOM   66   N  NE2 . HIS A 1 13  ? -21.487 2.081   -17.961 1.00 42.09 ? 8   HIS A NE2 1 
ATOM   67   N  N   . ALA A 1 14  ? -18.517 0.839   -12.600 1.00 24.95 ? 9   ALA A N   1 
ATOM   68   C  CA  . ALA A 1 14  ? -18.185 0.930   -11.158 1.00 29.77 ? 9   ALA A CA  1 
ATOM   69   C  C   . ALA A 1 14  ? -19.483 1.130   -10.378 1.00 34.33 ? 9   ALA A C   1 
ATOM   70   O  O   . ALA A 1 14  ? -20.435 1.708   -10.902 1.00 30.60 ? 9   ALA A O   1 
ATOM   71   C  CB  . ALA A 1 14  ? -17.212 2.047   -10.907 1.00 31.85 ? 9   ALA A CB  1 
ATOM   72   N  N   . PRO A 1 15  ? -19.584 0.654   -9.117  1.00 35.73 ? 10  PRO A N   1 
ATOM   73   C  CA  . PRO A 1 15  ? -20.767 0.927   -8.301  1.00 36.97 ? 10  PRO A CA  1 
ATOM   74   C  C   . PRO A 1 15  ? -20.989 2.419   -8.012  1.00 36.52 ? 10  PRO A C   1 
ATOM   75   O  O   . PRO A 1 15  ? -22.117 2.802   -7.760  1.00 36.88 ? 10  PRO A O   1 
ATOM   76   C  CB  . PRO A 1 15  ? -20.484 0.228   -6.965  1.00 36.38 ? 10  PRO A CB  1 
ATOM   77   C  CG  . PRO A 1 15  ? -19.385 -0.771  -7.282  1.00 40.41 ? 10  PRO A CG  1 
ATOM   78   C  CD  . PRO A 1 15  ? -18.595 -0.176  -8.428  1.00 36.98 ? 10  PRO A CD  1 
ATOM   79   N  N   . GLU A 1 16  ? -19.910 3.201   -7.966  1.00 36.75 ? 11  GLU A N   1 
ATOM   80   C  CA  . GLU A 1 16  ? -19.905 4.643   -7.584  1.00 40.60 ? 11  GLU A CA  1 
ATOM   81   C  C   . GLU A 1 16  ? -18.805 5.360   -8.370  1.00 38.62 ? 11  GLU A C   1 
ATOM   82   O  O   . GLU A 1 16  ? -17.776 4.702   -8.652  1.00 33.77 ? 11  GLU A O   1 
ATOM   83   C  CB  . GLU A 1 16  ? -19.592 4.844   -6.092  1.00 46.93 ? 11  GLU A CB  1 
ATOM   84   C  CG  . GLU A 1 16  ? -20.651 4.328   -5.126  1.00 52.80 ? 11  GLU A CG  1 
ATOM   85   C  CD  . GLU A 1 16  ? -21.885 5.208   -4.969  1.00 58.69 ? 11  GLU A CD  1 
ATOM   86   O  OE1 . GLU A 1 16  ? -22.783 5.132   -5.839  1.00 63.63 ? 11  GLU A OE1 1 
ATOM   87   O  OE2 . GLU A 1 16  ? -21.947 5.978   -3.987  1.00 59.69 ? 11  GLU A OE2 1 
ATOM   88   N  N   . ASP A 1 17  ? -18.974 6.668   -8.608  1.00 36.62 ? 12  ASP A N   1 
ATOM   89   C  CA  . ASP A 1 17  ? -18.011 7.528   -9.346  1.00 36.31 ? 12  ASP A CA  1 
ATOM   90   C  C   . ASP A 1 17  ? -16.634 7.501   -8.651  1.00 36.33 ? 12  ASP A C   1 
ATOM   91   O  O   . ASP A 1 17  ? -15.600 7.557   -9.382  1.00 31.78 ? 12  ASP A O   1 
ATOM   92   C  CB  . ASP A 1 17  ? -18.558 8.947   -9.518  1.00 39.15 ? 12  ASP A CB  1 
ATOM   93   C  CG  . ASP A 1 17  ? -19.893 9.040   -10.259 1.00 42.00 ? 12  ASP A CG  1 
ATOM   94   O  OD1 . ASP A 1 17  ? -20.058 8.371   -11.285 1.00 38.01 ? 12  ASP A OD1 1 
ATOM   95   O  OD2 . ASP A 1 17  ? -20.773 9.779   -9.787  1.00 48.45 ? 12  ASP A OD2 1 
ATOM   96   N  N   . ARG A 1 18  ? -16.602 7.390   -7.315  1.00 32.88 ? 13  ARG A N   1 
ATOM   97   C  CA  . ARG A 1 18  ? -15.350 7.461   -6.501  1.00 35.52 ? 13  ARG A CA  1 
ATOM   98   C  C   . ARG A 1 18  ? -14.372 6.339   -6.865  1.00 30.33 ? 13  ARG A C   1 
ATOM   99   O  O   . ARG A 1 18  ? -13.149 6.559   -6.700  1.00 30.76 ? 13  ARG A O   1 
ATOM   100  C  CB  . ARG A 1 18  ? -15.651 7.437   -4.997  1.00 39.20 ? 13  ARG A CB  1 
ATOM   101  C  CG  . ARG A 1 18  ? -14.447 7.718   -4.106  1.00 47.00 ? 13  ARG A CG  1 
ATOM   102  C  CD  . ARG A 1 18  ? -14.815 8.459   -2.827  1.00 56.45 ? 13  ARG A CD  1 
ATOM   103  N  NE  . ARG A 1 18  ? -15.671 7.660   -1.955  1.00 62.34 ? 13  ARG A NE  1 
ATOM   104  C  CZ  . ARG A 1 18  ? -17.009 7.639   -1.963  1.00 66.66 ? 13  ARG A CZ  1 
ATOM   105  N  NH1 . ARG A 1 18  ? -17.708 8.383   -2.807  1.00 73.03 ? 13  ARG A NH1 1 
ATOM   106  N  NH2 . ARG A 1 18  ? -17.656 6.854   -1.116  1.00 70.02 ? 13  ARG A NH2 1 
ATOM   107  N  N   . TRP A 1 19  ? -14.858 5.202   -7.370  1.00 31.78 ? 14  TRP A N   1 
ATOM   108  C  CA  . TRP A 1 19  ? -13.981 4.098   -7.849  1.00 33.11 ? 14  TRP A CA  1 
ATOM   109  C  C   . TRP A 1 19  ? -13.096 4.571   -9.010  1.00 28.36 ? 14  TRP A C   1 
ATOM   110  O  O   . TRP A 1 19  ? -11.966 4.070   -9.120  1.00 23.99 ? 14  TRP A O   1 
ATOM   111  C  CB  . TRP A 1 19  ? -14.773 2.871   -8.285  1.00 33.85 ? 14  TRP A CB  1 
ATOM   112  C  CG  . TRP A 1 19  ? -15.384 2.037   -7.203  1.00 35.04 ? 14  TRP A CG  1 
ATOM   113  C  CD1 . TRP A 1 19  ? -16.113 2.456   -6.129  1.00 37.57 ? 14  TRP A CD1 1 
ATOM   114  C  CD2 . TRP A 1 19  ? -15.442 0.601   -7.192  1.00 35.30 ? 14  TRP A CD2 1 
ATOM   115  N  NE1 . TRP A 1 19  ? -16.574 1.377   -5.422  1.00 39.80 ? 14  TRP A NE1 1 
ATOM   116  C  CE2 . TRP A 1 19  ? -16.157 0.225   -6.039  1.00 37.53 ? 14  TRP A CE2 1 
ATOM   117  C  CE3 . TRP A 1 19  ? -14.901 -0.398  -8.007  1.00 34.16 ? 14  TRP A CE3 1 
ATOM   118  C  CZ2 . TRP A 1 19  ? -16.359 -1.111  -5.699  1.00 36.28 ? 14  TRP A CZ2 1 
ATOM   119  C  CZ3 . TRP A 1 19  ? -15.107 -1.715  -7.672  1.00 35.61 ? 14  TRP A CZ3 1 
ATOM   120  C  CH2 . TRP A 1 19  ? -15.832 -2.066  -6.537  1.00 34.68 ? 14  TRP A CH2 1 
ATOM   121  N  N   . LEU A 1 20  ? -13.579 5.464   -9.882  1.00 28.18 ? 15  LEU A N   1 
ATOM   122  C  CA  . LEU A 1 20  ? -12.750 5.922   -11.016 1.00 25.99 ? 15  LEU A CA  1 
ATOM   123  C  C   . LEU A 1 20  ? -11.628 6.775   -10.420 1.00 26.54 ? 15  LEU A C   1 
ATOM   124  O  O   . LEU A 1 20  ? -10.459 6.537   -10.745 1.00 22.33 ? 15  LEU A O   1 
ATOM   125  C  CB  . LEU A 1 20  ? -13.593 6.699   -12.022 1.00 27.25 ? 15  LEU A CB  1 
ATOM   126  C  CG  . LEU A 1 20  ? -14.382 5.830   -12.995 1.00 30.16 ? 15  LEU A CG  1 
ATOM   127  C  CD1 . LEU A 1 20  ? -15.359 4.981   -12.217 1.00 32.48 ? 15  LEU A CD1 1 
ATOM   128  C  CD2 . LEU A 1 20  ? -15.100 6.664   -14.068 1.00 29.17 ? 15  LEU A CD2 1 
ATOM   129  N  N   . VAL A 1 21  ? -11.982 7.680   -9.504  1.00 26.30 ? 16  VAL A N   1 
ATOM   130  C  CA  . VAL A 1 21  ? -11.008 8.556   -8.793  1.00 27.26 ? 16  VAL A CA  1 
ATOM   131  C  C   . VAL A 1 21  ? -9.994  7.670   -8.081  1.00 24.83 ? 16  VAL A C   1 
ATOM   132  O  O   . VAL A 1 21  ? -8.812  7.938   -8.235  1.00 25.49 ? 16  VAL A O   1 
ATOM   133  C  CB  . VAL A 1 21  ? -11.682 9.532   -7.814  1.00 27.67 ? 16  VAL A CB  1 
ATOM   134  C  CG1 . VAL A 1 21  ? -10.659 10.352  -7.045  1.00 28.82 ? 16  VAL A CG1 1 
ATOM   135  C  CG2 . VAL A 1 21  ? -12.653 10.436  -8.531  1.00 29.15 ? 16  VAL A CG2 1 
ATOM   136  N  N   . ASP A 1 22  ? -10.444 6.634   -7.365  1.00 26.97 ? 17  ASP A N   1 
ATOM   137  C  CA  . ASP A 1 22  ? -9.553  5.740   -6.567  1.00 28.85 ? 17  ASP A CA  1 
ATOM   138  C  C   . ASP A 1 22  ? -8.535  5.049   -7.488  1.00 26.86 ? 17  ASP A C   1 
ATOM   139  O  O   . ASP A 1 22  ? -7.345  4.923   -7.105  1.00 19.50 ? 17  ASP A O   1 
ATOM   140  C  CB  . ASP A 1 22  ? -10.361 4.711   -5.756  1.00 32.20 ? 17  ASP A CB  1 
ATOM   141  C  CG  . ASP A 1 22  ? -11.180 5.269   -4.590  1.00 33.60 ? 17  ASP A CG  1 
ATOM   142  O  OD1 . ASP A 1 22  ? -11.926 4.495   -3.985  1.00 46.15 ? 17  ASP A OD1 1 
ATOM   143  O  OD2 . ASP A 1 22  ? -11.092 6.463   -4.300  1.00 35.89 ? 17  ASP A OD2 1 
ATOM   144  N  N   . LEU A 1 23  ? -8.994  4.583   -8.651  1.00 25.02 ? 18  LEU A N   1 
ATOM   145  C  CA  . LEU A 1 23  ? -8.110  3.904   -9.624  1.00 28.33 ? 18  LEU A CA  1 
ATOM   146  C  C   . LEU A 1 23  ? -7.064  4.898   -10.139 1.00 27.64 ? 18  LEU A C   1 
ATOM   147  O  O   . LEU A 1 23  ? -5.898  4.514   -10.154 1.00 23.85 ? 18  LEU A O   1 
ATOM   148  C  CB  . LEU A 1 23  ? -8.928  3.314   -10.768 1.00 30.13 ? 18  LEU A CB  1 
ATOM   149  C  CG  . LEU A 1 23  ? -8.237  2.178   -11.523 1.00 35.36 ? 18  LEU A CG  1 
ATOM   150  C  CD1 . LEU A 1 23  ? -9.245  1.394   -12.342 1.00 37.69 ? 18  LEU A CD1 1 
ATOM   151  C  CD2 . LEU A 1 23  ? -7.132  2.699   -12.423 1.00 37.64 ? 18  LEU A CD2 1 
ATOM   152  N  N   . VAL A 1 24  ? -7.456  6.124   -10.514 1.00 24.57 ? 19  VAL A N   1 
ATOM   153  C  CA  . VAL A 1 24  ? -6.497  7.145   -11.018 1.00 26.24 ? 19  VAL A CA  1 
ATOM   154  C  C   . VAL A 1 24  ? -5.423  7.356   -9.957  1.00 24.96 ? 19  VAL A C   1 
ATOM   155  O  O   . VAL A 1 24  ? -4.275  7.450   -10.342 1.00 25.21 ? 19  VAL A O   1 
ATOM   156  C  CB  . VAL A 1 24  ? -7.144  8.508   -11.303 1.00 27.46 ? 19  VAL A CB  1 
ATOM   157  C  CG1 . VAL A 1 24  ? -6.070  9.576   -11.404 1.00 25.51 ? 19  VAL A CG1 1 
ATOM   158  C  CG2 . VAL A 1 24  ? -8.031  8.475   -12.541 1.00 25.45 ? 19  VAL A CG2 1 
ATOM   159  N  N   . ARG A 1 25  ? -5.832  7.591   -8.706  1.00 25.27 ? 20  ARG A N   1 
ATOM   160  C  CA  . ARG A 1 25  ? -4.928  7.844   -7.556  1.00 29.41 ? 20  ARG A CA  1 
ATOM   161  C  C   . ARG A 1 25  ? -3.982  6.655   -7.352  1.00 27.74 ? 20  ARG A C   1 
ATOM   162  O  O   . ARG A 1 25  ? -2.748  6.876   -7.182  1.00 26.26 ? 20  ARG A O   1 
ATOM   163  C  CB  . ARG A 1 25  ? -5.733  8.115   -6.283  1.00 33.63 ? 20  ARG A CB  1 
ATOM   164  C  CG  . ARG A 1 25  ? -6.413  9.477   -6.247  1.00 36.73 ? 20  ARG A CG  1 
ATOM   165  C  CD  . ARG A 1 25  ? -6.671  9.887   -4.813  1.00 40.05 ? 20  ARG A CD  1 
ATOM   166  N  NE  . ARG A 1 25  ? -7.792  10.793  -4.633  1.00 42.97 ? 20  ARG A NE  1 
ATOM   167  C  CZ  . ARG A 1 25  ? -7.720  12.124  -4.581  1.00 48.70 ? 20  ARG A CZ  1 
ATOM   168  N  NH1 . ARG A 1 25  ? -6.563  12.757  -4.734  1.00 48.91 ? 20  ARG A NH1 1 
ATOM   169  N  NH2 . ARG A 1 25  ? -8.830  12.819  -4.388  1.00 50.04 ? 20  ARG A NH2 1 
ATOM   170  N  N   . GLY A 1 26  ? -4.515  5.436   -7.428  1.00 26.72 ? 21  GLY A N   1 
ATOM   171  C  CA  . GLY A 1 26  ? -3.718  4.208   -7.245  1.00 26.98 ? 21  GLY A CA  1 
ATOM   172  C  C   . GLY A 1 26  ? -2.816  3.863   -8.418  1.00 25.76 ? 21  GLY A C   1 
ATOM   173  O  O   . GLY A 1 26  ? -1.960  2.932   -8.248  1.00 24.62 ? 21  GLY A O   1 
ATOM   174  N  N   . HIS A 1 27  ? -3.015  4.473   -9.590  1.00 23.68 ? 22  HIS A N   1 
ATOM   175  C  CA  . HIS A 1 27  ? -2.348  4.006   -10.840 1.00 25.93 ? 22  HIS A CA  1 
ATOM   176  C  C   . HIS A 1 27  ? -1.913  5.195   -11.705 1.00 25.98 ? 22  HIS A C   1 
ATOM   177  O  O   . HIS A 1 27  ? -2.186  5.219   -12.899 1.00 24.73 ? 22  HIS A O   1 
ATOM   178  C  CB  . HIS A 1 27  ? -3.240  2.963   -11.531 1.00 27.60 ? 22  HIS A CB  1 
ATOM   179  C  CG  . HIS A 1 27  ? -3.571  1.816   -10.639 1.00 25.84 ? 22  HIS A CG  1 
ATOM   180  N  ND1 . HIS A 1 27  ? -2.704  0.765   -10.448 1.00 26.28 ? 22  HIS A ND1 1 
ATOM   181  C  CD2 . HIS A 1 27  ? -4.617  1.595   -9.812  1.00 26.54 ? 22  HIS A CD2 1 
ATOM   182  C  CE1 . HIS A 1 27  ? -3.225  -0.082  -9.584  1.00 27.75 ? 22  HIS A CE1 1 
ATOM   183  N  NE2 . HIS A 1 27  ? -4.399  0.403   -9.173  1.00 26.17 ? 22  HIS A NE2 1 
ATOM   184  N  N   . PRO A 1 28  ? -1.072  6.120   -11.178 1.00 25.95 ? 23  PRO A N   1 
ATOM   185  C  CA  . PRO A 1 28  ? -0.823  7.416   -11.822 1.00 28.08 ? 23  PRO A CA  1 
ATOM   186  C  C   . PRO A 1 28  ? -0.043  7.404   -13.145 1.00 24.81 ? 23  PRO A C   1 
ATOM   187  O  O   . PRO A 1 28  ? -0.101  8.397   -13.859 1.00 23.06 ? 23  PRO A O   1 
ATOM   188  C  CB  . PRO A 1 28  ? 0.034   8.187   -10.810 1.00 26.92 ? 23  PRO A CB  1 
ATOM   189  C  CG  . PRO A 1 28  ? 0.741   7.096   -10.025 1.00 26.70 ? 23  PRO A CG  1 
ATOM   190  C  CD  . PRO A 1 28  ? -0.253  5.947   -9.967  1.00 26.18 ? 23  PRO A CD  1 
ATOM   191  N  N   . LEU A 1 29  ? 0.685   6.330   -13.429 1.00 26.26 ? 24  LEU A N   1 
ATOM   192  C  CA  . LEU A 1 29  ? 1.418   6.214   -14.710 1.00 26.94 ? 24  LEU A CA  1 
ATOM   193  C  C   . LEU A 1 29  ? 0.411   5.837   -15.802 1.00 25.07 ? 24  LEU A C   1 
ATOM   194  O  O   . LEU A 1 29  ? 0.199   4.636   -16.073 1.00 23.51 ? 24  LEU A O   1 
ATOM   195  C  CB  . LEU A 1 29  ? 2.583   5.235   -14.601 1.00 26.99 ? 24  LEU A CB  1 
ATOM   196  C  CG  . LEU A 1 29  ? 3.565   5.353   -15.764 1.00 30.04 ? 24  LEU A CG  1 
ATOM   197  C  CD1 . LEU A 1 29  ? 4.334   6.680   -15.730 1.00 30.68 ? 24  LEU A CD1 1 
ATOM   198  C  CD2 . LEU A 1 29  ? 4.511   4.168   -15.790 1.00 31.88 ? 24  LEU A CD2 1 
ATOM   199  N  N   . ALA A 1 30  ? -0.184  6.870   -16.396 1.00 22.83 ? 25  ALA A N   1 
ATOM   200  C  CA  . ALA A 1 30  ? -1.203  6.777   -17.456 1.00 22.91 ? 25  ALA A CA  1 
ATOM   201  C  C   . ALA A 1 30  ? -0.524  6.586   -18.812 1.00 21.25 ? 25  ALA A C   1 
ATOM   202  O  O   . ALA A 1 30  ? 0.609   7.008   -18.979 1.00 23.13 ? 25  ALA A O   1 
ATOM   203  C  CB  . ALA A 1 30  ? -2.055  8.015   -17.458 1.00 22.43 ? 25  ALA A CB  1 
ATOM   204  N  N   . GLN A 1 31  ? -1.250  6.014   -19.758 1.00 22.11 ? 26  GLN A N   1 
ATOM   205  C  CA  . GLN A 1 31  ? -0.906  6.042   -21.203 1.00 22.65 ? 26  GLN A CA  1 
ATOM   206  C  C   . GLN A 1 31  ? -1.685  7.205   -21.834 1.00 21.37 ? 26  GLN A C   1 
ATOM   207  O  O   . GLN A 1 31  ? -2.929  7.117   -21.923 1.00 19.93 ? 26  GLN A O   1 
ATOM   208  C  CB  . GLN A 1 31  ? -1.203  4.668   -21.817 1.00 22.27 ? 26  GLN A CB  1 
ATOM   209  C  CG  . GLN A 1 31  ? -0.100  3.599   -21.612 1.00 24.80 ? 26  GLN A CG  1 
ATOM   210  C  CD  . GLN A 1 31  ? -0.456  2.274   -22.265 1.00 19.62 ? 26  GLN A CD  1 
ATOM   211  O  OE1 . GLN A 1 31  ? -0.933  2.238   -23.377 1.00 23.02 ? 26  GLN A OE1 1 
ATOM   212  N  NE2 . GLN A 1 31  ? -0.353  1.174   -21.544 1.00 18.88 ? 26  GLN A NE2 1 
ATOM   213  N  N   . LEU A 1 32  ? -0.995  8.290   -22.161 1.00 21.12 ? 27  LEU A N   1 
ATOM   214  C  CA  . LEU A 1 32  ? -1.588  9.505   -22.788 1.00 21.50 ? 27  LEU A CA  1 
ATOM   215  C  C   . LEU A 1 32  ? -1.610  9.286   -24.305 1.00 22.81 ? 27  LEU A C   1 
ATOM   216  O  O   . LEU A 1 32  ? -0.520  9.050   -24.874 1.00 18.64 ? 27  LEU A O   1 
ATOM   217  C  CB  . LEU A 1 32  ? -0.793  10.757  -22.410 1.00 21.96 ? 27  LEU A CB  1 
ATOM   218  C  CG  . LEU A 1 32  ? -1.350  12.090  -22.935 1.00 24.91 ? 27  LEU A CG  1 
ATOM   219  C  CD1 . LEU A 1 32  ? -2.730  12.400  -22.361 1.00 25.42 ? 27  LEU A CD1 1 
ATOM   220  C  CD2 . LEU A 1 32  ? -0.392  13.258  -22.667 1.00 27.59 ? 27  LEU A CD2 1 
ATOM   221  N  N   . ALA A 1 33  ? -2.807  9.305   -24.927 1.00 21.03 ? 28  ALA A N   1 
ATOM   222  C  CA  . ALA A 1 33  ? -2.962  9.075   -26.379 1.00 23.02 ? 28  ALA A CA  1 
ATOM   223  C  C   . ALA A 1 33  ? -3.534  10.320  -27.076 1.00 24.04 ? 28  ALA A C   1 
ATOM   224  O  O   . ALA A 1 33  ? -4.460  10.922  -26.570 1.00 20.51 ? 28  ALA A O   1 
ATOM   225  C  CB  . ALA A 1 33  ? -3.798  7.838   -26.620 1.00 24.38 ? 28  ALA A CB  1 
ATOM   226  N  N   . SER A 1 34  ? -2.984  10.662  -28.237 1.00 28.08 ? 29  SER A N   1 
ATOM   227  C  CA  . SER A 1 34  ? -3.533  11.687  -29.159 1.00 28.19 ? 29  SER A CA  1 
ATOM   228  C  C   . SER A 1 34  ? -3.388  11.197  -30.597 1.00 29.34 ? 29  SER A C   1 
ATOM   229  O  O   . SER A 1 34  ? -2.576  10.272  -30.838 1.00 32.02 ? 29  SER A O   1 
ATOM   230  C  CB  . SER A 1 34  ? -2.854  12.993  -28.959 1.00 27.94 ? 29  SER A CB  1 
ATOM   231  O  OG  . SER A 1 34  ? -1.469  12.849  -29.155 1.00 26.64 ? 29  SER A OG  1 
ATOM   232  N  N   . ASN A 1 35  ? -4.154  11.814  -31.495 1.00 29.05 ? 30  ASN A N   1 
ATOM   233  C  CA  . ASN A 1 35  ? -4.341  11.370  -32.893 1.00 30.04 ? 30  ASN A CA  1 
ATOM   234  C  C   . ASN A 1 35  ? -3.030  11.558  -33.648 1.00 27.74 ? 30  ASN A C   1 
ATOM   235  O  O   . ASN A 1 35  ? -2.335  12.579  -33.414 1.00 25.97 ? 30  ASN A O   1 
ATOM   236  C  CB  . ASN A 1 35  ? -5.488  12.086  -33.603 1.00 29.84 ? 30  ASN A CB  1 
ATOM   237  C  CG  . ASN A 1 35  ? -6.856  11.608  -33.170 1.00 34.88 ? 30  ASN A CG  1 
ATOM   238  O  OD1 . ASN A 1 35  ? -6.989  10.584  -32.503 1.00 34.35 ? 30  ASN A OD1 1 
ATOM   239  N  ND2 . ASN A 1 35  ? -7.882  12.354  -33.557 1.00 34.07 ? 30  ASN A ND2 1 
ATOM   240  N  N   . GLY A 1 36  ? -2.720  10.563  -34.481 1.00 28.57 ? 31  GLY A N   1 
ATOM   241  C  CA  . GLY A 1 36  ? -1.535  10.523  -35.348 1.00 32.43 ? 31  GLY A CA  1 
ATOM   242  C  C   . GLY A 1 36  ? -1.812  11.341  -36.590 1.00 36.56 ? 31  GLY A C   1 
ATOM   243  O  O   . GLY A 1 36  ? -2.958  11.306  -37.059 1.00 40.86 ? 31  GLY A O   1 
ATOM   244  N  N   . ALA A 1 37  ? -0.813  12.072  -37.083 1.00 39.27 ? 32  ALA A N   1 
ATOM   245  C  CA  . ALA A 1 37  ? -0.963  12.998  -38.221 1.00 39.74 ? 32  ALA A CA  1 
ATOM   246  C  C   . ALA A 1 37  ? -1.124  12.150  -39.482 1.00 42.40 ? 32  ALA A C   1 
ATOM   247  O  O   . ALA A 1 37  ? -0.419  11.114  -39.595 1.00 39.59 ? 32  ALA A O   1 
ATOM   248  C  CB  . ALA A 1 37  ? 0.211   13.946  -38.285 1.00 40.50 ? 32  ALA A CB  1 
ATOM   249  N  N   . GLY A 1 38  ? -2.096  12.529  -40.320 1.00 45.16 ? 33  GLY A N   1 
ATOM   250  C  CA  . GLY A 1 38  ? -2.298  12.008  -41.684 1.00 46.88 ? 33  GLY A CA  1 
ATOM   251  C  C   . GLY A 1 38  ? -2.717  10.555  -41.665 1.00 45.60 ? 33  GLY A C   1 
ATOM   252  O  O   . GLY A 1 38  ? -2.200  9.798   -42.477 1.00 45.30 ? 33  GLY A O   1 
ATOM   253  N  N   . GLY A 1 39  ? -3.607  10.193  -40.743 1.00 48.20 ? 34  GLY A N   1 
ATOM   254  C  CA  . GLY A 1 39  ? -4.096  8.815   -40.559 1.00 48.00 ? 34  GLY A CA  1 
ATOM   255  C  C   . GLY A 1 39  ? -3.015  7.875   -40.048 1.00 42.06 ? 34  GLY A C   1 
ATOM   256  O  O   . GLY A 1 39  ? -3.182  6.666   -40.200 1.00 48.75 ? 34  GLY A O   1 
ATOM   257  N  N   . ALA A 1 40  ? -1.944  8.378   -39.451 1.00 38.62 ? 35  ALA A N   1 
ATOM   258  C  CA  . ALA A 1 40  ? -0.941  7.528   -38.765 1.00 40.16 ? 35  ALA A CA  1 
ATOM   259  C  C   . ALA A 1 40  ? -1.551  7.009   -37.450 1.00 36.68 ? 35  ALA A C   1 
ATOM   260  O  O   . ALA A 1 40  ? -2.586  7.527   -37.020 1.00 36.70 ? 35  ALA A O   1 
ATOM   261  C  CB  . ALA A 1 40  ? 0.345   8.288   -38.550 1.00 40.21 ? 35  ALA A CB  1 
ATOM   262  N  N   . ALA A 1 41  ? -0.995  5.948   -36.878 1.00 32.91 ? 36  ALA A N   1 
ATOM   263  C  CA  . ALA A 1 41  ? -1.403  5.445   -35.547 1.00 30.02 ? 36  ALA A CA  1 
ATOM   264  C  C   . ALA A 1 41  ? -1.266  6.570   -34.520 1.00 26.90 ? 36  ALA A C   1 
ATOM   265  O  O   . ALA A 1 41  ? -0.402  7.430   -34.663 1.00 22.74 ? 36  ALA A O   1 
ATOM   266  C  CB  . ALA A 1 41  ? -0.547  4.258   -35.179 1.00 31.05 ? 36  ALA A CB  1 
ATOM   267  N  N   . PRO A 1 42  ? -2.097  6.592   -33.458 1.00 24.08 ? 37  PRO A N   1 
ATOM   268  C  CA  . PRO A 1 42  ? -1.897  7.502   -32.336 1.00 24.41 ? 37  PRO A CA  1 
ATOM   269  C  C   . PRO A 1 42  ? -0.499  7.484   -31.707 1.00 26.00 ? 37  PRO A C   1 
ATOM   270  O  O   . PRO A 1 42  ? 0.169   6.466   -31.750 1.00 23.32 ? 37  PRO A O   1 
ATOM   271  C  CB  . PRO A 1 42  ? -2.965  7.068   -31.332 1.00 22.69 ? 37  PRO A CB  1 
ATOM   272  C  CG  . PRO A 1 42  ? -4.095  6.543   -32.203 1.00 23.80 ? 37  PRO A CG  1 
ATOM   273  C  CD  . PRO A 1 42  ? -3.344  5.824   -33.308 1.00 25.99 ? 37  PRO A CD  1 
ATOM   274  N  N   . HIS A 1 43  ? -0.101  8.649   -31.168 1.00 27.02 ? 38  HIS A N   1 
ATOM   275  C  CA  . HIS A 1 43  ? 1.034   8.824   -30.222 1.00 27.14 ? 38  HIS A CA  1 
ATOM   276  C  C   . HIS A 1 43  ? 0.593   8.307   -28.853 1.00 24.38 ? 38  HIS A C   1 
ATOM   277  O  O   . HIS A 1 43  ? -0.573  8.544   -28.485 1.00 20.42 ? 38  HIS A O   1 
ATOM   278  C  CB  . HIS A 1 43  ? 1.449   10.294  -30.124 1.00 27.75 ? 38  HIS A CB  1 
ATOM   279  C  CG  . HIS A 1 43  ? 1.790   10.915  -31.440 1.00 29.60 ? 38  HIS A CG  1 
ATOM   280  N  ND1 . HIS A 1 43  ? 3.010   10.750  -32.023 1.00 33.28 ? 38  HIS A ND1 1 
ATOM   281  C  CD2 . HIS A 1 43  ? 1.075   11.701  -32.270 1.00 31.27 ? 38  HIS A CD2 1 
ATOM   282  C  CE1 . HIS A 1 43  ? 3.038   11.390  -33.174 1.00 33.44 ? 38  HIS A CE1 1 
ATOM   283  N  NE2 . HIS A 1 43  ? 1.864   11.985  -33.337 1.00 33.14 ? 38  HIS A NE2 1 
ATOM   284  N  N   . ILE A 1 44  ? 1.493   7.601   -28.171 1.00 22.48 ? 39  ILE A N   1 
ATOM   285  C  CA  . ILE A 1 44  ? 1.298   7.015   -26.821 1.00 20.67 ? 39  ILE A CA  1 
ATOM   286  C  C   . ILE A 1 44  ? 2.515   7.331   -25.972 1.00 22.14 ? 39  ILE A C   1 
ATOM   287  O  O   . ILE A 1 44  ? 3.596   6.944   -26.428 1.00 22.04 ? 39  ILE A O   1 
ATOM   288  C  CB  . ILE A 1 44  ? 1.150   5.500   -26.942 1.00 20.99 ? 39  ILE A CB  1 
ATOM   289  C  CG1 . ILE A 1 44  ? 0.092   5.092   -27.954 1.00 20.02 ? 39  ILE A CG1 1 
ATOM   290  C  CG2 . ILE A 1 44  ? 0.901   4.904   -25.587 1.00 19.48 ? 39  ILE A CG2 1 
ATOM   291  C  CD1 . ILE A 1 44  ? -1.297  5.523   -27.571 1.00 23.15 ? 39  ILE A CD1 1 
ATOM   292  N  N   . THR A 1 45  ? 2.338   7.995   -24.814 1.00 21.59 ? 40  THR A N   1 
ATOM   293  C  CA  . THR A 1 45  ? 3.414   8.246   -23.828 1.00 22.84 ? 40  THR A CA  1 
ATOM   294  C  C   . THR A 1 45  ? 2.906   7.885   -22.438 1.00 21.07 ? 40  THR A C   1 
ATOM   295  O  O   . THR A 1 45  ? 1.802   8.317   -22.069 1.00 17.61 ? 40  THR A O   1 
ATOM   296  C  CB  . THR A 1 45  ? 3.922   9.696   -23.837 1.00 24.95 ? 40  THR A CB  1 
ATOM   297  O  OG1 . THR A 1 45  ? 4.208   10.091  -25.192 1.00 30.01 ? 40  THR A OG1 1 
ATOM   298  C  CG2 . THR A 1 45  ? 5.167   9.874   -22.993 1.00 26.16 ? 40  THR A CG2 1 
ATOM   299  N  N   . HIS A 1 46  ? 3.706   7.100   -21.719 1.00 20.96 ? 41  HIS A N   1 
ATOM   300  C  CA  . HIS A 1 46  ? 3.524   6.784   -20.281 1.00 21.11 ? 41  HIS A CA  1 
ATOM   301  C  C   . HIS A 1 46  ? 3.911   8.042   -19.498 1.00 20.75 ? 41  HIS A C   1 
ATOM   302  O  O   . HIS A 1 46  ? 5.059   8.458   -19.548 1.00 18.18 ? 41  HIS A O   1 
ATOM   303  C  CB  . HIS A 1 46  ? 4.305   5.515   -19.871 1.00 23.05 ? 41  HIS A CB  1 
ATOM   304  C  CG  . HIS A 1 46  ? 3.574   4.233   -20.147 1.00 26.72 ? 41  HIS A CG  1 
ATOM   305  N  ND1 . HIS A 1 46  ? 3.668   3.567   -21.354 1.00 29.88 ? 41  HIS A ND1 1 
ATOM   306  C  CD2 . HIS A 1 46  ? 2.741   3.494   -19.385 1.00 29.43 ? 41  HIS A CD2 1 
ATOM   307  C  CE1 . HIS A 1 46  ? 2.903   2.482   -21.336 1.00 30.22 ? 41  HIS A CE1 1 
ATOM   308  N  NE2 . HIS A 1 46  ? 2.355   2.397   -20.132 1.00 33.90 ? 41  HIS A NE2 1 
ATOM   309  N  N   . VAL A 1 47  ? 2.954   8.656   -18.831 1.00 19.78 ? 42  VAL A N   1 
ATOM   310  C  CA  . VAL A 1 47  ? 3.167   9.956   -18.140 1.00 19.65 ? 42  VAL A CA  1 
ATOM   311  C  C   . VAL A 1 47  ? 2.532   9.879   -16.756 1.00 20.45 ? 42  VAL A C   1 
ATOM   312  O  O   . VAL A 1 47  ? 1.436   9.317   -16.616 1.00 21.19 ? 42  VAL A O   1 
ATOM   313  C  CB  . VAL A 1 47  ? 2.601   11.119  -18.977 1.00 19.09 ? 42  VAL A CB  1 
ATOM   314  C  CG1 . VAL A 1 47  ? 3.393   11.341  -20.254 1.00 19.36 ? 42  VAL A CG1 1 
ATOM   315  C  CG2 . VAL A 1 47  ? 1.122   10.930  -19.294 1.00 19.55 ? 42  VAL A CG2 1 
ATOM   316  N  N   . PRO A 1 48  ? 3.159   10.486  -15.714 1.00 20.72 ? 43  PRO A N   1 
ATOM   317  C  CA  . PRO A 1 48  ? 2.571   10.544  -14.386 1.00 20.59 ? 43  PRO A CA  1 
ATOM   318  C  C   . PRO A 1 48  ? 1.495   11.632  -14.305 1.00 20.32 ? 43  PRO A C   1 
ATOM   319  O  O   . PRO A 1 48  ? 1.790   12.789  -14.546 1.00 19.96 ? 43  PRO A O   1 
ATOM   320  C  CB  . PRO A 1 48  ? 3.720   10.873  -13.438 1.00 19.68 ? 43  PRO A CB  1 
ATOM   321  C  CG  . PRO A 1 48  ? 4.709   11.580  -14.297 1.00 21.25 ? 43  PRO A CG  1 
ATOM   322  C  CD  . PRO A 1 48  ? 4.508   11.068  -15.718 1.00 24.97 ? 43  PRO A CD  1 
ATOM   323  N  N   . ILE A 1 49  ? 0.277   11.233  -13.945 1.00 20.69 ? 44  ILE A N   1 
ATOM   324  C  CA  . ILE A 1 49  ? -0.883  12.153  -13.876 1.00 22.19 ? 44  ILE A CA  1 
ATOM   325  C  C   . ILE A 1 49  ? -1.473  12.074  -12.457 1.00 22.26 ? 44  ILE A C   1 
ATOM   326  O  O   . ILE A 1 49  ? -1.612  10.969  -11.921 1.00 21.42 ? 44  ILE A O   1 
ATOM   327  C  CB  . ILE A 1 49  ? -1.897  11.831  -14.992 1.00 24.66 ? 44  ILE A CB  1 
ATOM   328  C  CG1 . ILE A 1 49  ? -1.314  12.153  -16.371 1.00 27.36 ? 44  ILE A CG1 1 
ATOM   329  C  CG2 . ILE A 1 49  ? -3.234  12.541  -14.765 1.00 24.81 ? 44  ILE A CG2 1 
ATOM   330  C  CD1 . ILE A 1 49  ? -2.216  11.808  -17.554 1.00 28.29 ? 44  ILE A CD1 1 
ATOM   331  N  N   . ILE A 1 50  ? -1.859  13.221  -11.891 1.00 22.18 ? 45  ILE A N   1 
ATOM   332  C  CA  . ILE A 1 50  ? -2.475  13.303  -10.530 1.00 23.47 ? 45  ILE A CA  1 
ATOM   333  C  C   . ILE A 1 50  ? -3.723  14.169  -10.627 1.00 20.86 ? 45  ILE A C   1 
ATOM   334  O  O   . ILE A 1 50  ? -3.768  15.005  -11.531 1.00 20.41 ? 45  ILE A O   1 
ATOM   335  C  CB  . ILE A 1 50  ? -1.461  13.891  -9.517  1.00 26.09 ? 45  ILE A CB  1 
ATOM   336  C  CG1 . ILE A 1 50  ? -1.025  15.295  -9.935  1.00 26.93 ? 45  ILE A CG1 1 
ATOM   337  C  CG2 . ILE A 1 50  ? -0.251  12.969  -9.355  1.00 25.16 ? 45  ILE A CG2 1 
ATOM   338  C  CD1 . ILE A 1 50  ? -0.337  16.102  -8.825  1.00 27.73 ? 45  ILE A CD1 1 
ATOM   339  N  N   . VAL A 1 51  ? -4.621  14.033  -9.666  1.00 22.52 ? 46  VAL A N   1 
ATOM   340  C  CA  . VAL A 1 51  ? -5.743  14.985  -9.412  1.00 28.26 ? 46  VAL A CA  1 
ATOM   341  C  C   . VAL A 1 51  ? -5.152  16.331  -8.959  1.00 29.26 ? 46  VAL A C   1 
ATOM   342  O  O   . VAL A 1 51  ? -4.104  16.368  -8.226  1.00 27.37 ? 46  VAL A O   1 
ATOM   343  C  CB  . VAL A 1 51  ? -6.752  14.419  -8.389  1.00 31.62 ? 46  VAL A CB  1 
ATOM   344  C  CG1 . VAL A 1 51  ? -7.700  15.482  -7.829  1.00 34.80 ? 46  VAL A CG1 1 
ATOM   345  C  CG2 . VAL A 1 51  ? -7.527  13.263  -8.996  1.00 32.97 ? 46  VAL A CG2 1 
ATOM   346  N  N   . ASP A 1 52  ? -5.721  17.401  -9.503  1.00 27.69 ? 47  ASP A N   1 
ATOM   347  C  CA  . ASP A 1 52  ? -5.470  18.795  -9.049  1.00 27.81 ? 47  ASP A CA  1 
ATOM   348  C  C   . ASP A 1 52  ? -5.195  18.812  -7.549  1.00 28.93 ? 47  ASP A C   1 
ATOM   349  O  O   . ASP A 1 52  ? -6.136  18.655  -6.776  1.00 28.49 ? 47  ASP A O   1 
ATOM   350  C  CB  . ASP A 1 52  ? -6.738  19.583  -9.343  1.00 30.93 ? 47  ASP A CB  1 
ATOM   351  C  CG  . ASP A 1 52  ? -6.708  21.053  -8.976  1.00 32.13 ? 47  ASP A CG  1 
ATOM   352  O  OD1 . ASP A 1 52  ? -5.770  21.496  -8.282  1.00 30.67 ? 47  ASP A OD1 1 
ATOM   353  O  OD2 . ASP A 1 52  ? -7.645  21.723  -9.394  1.00 32.15 ? 47  ASP A OD2 1 
ATOM   354  N  N   . PRO A 1 53  ? -3.953  19.057  -7.066  1.00 26.74 ? 48  PRO A N   1 
ATOM   355  C  CA  . PRO A 1 53  ? -3.673  19.020  -5.628  1.00 32.60 ? 48  PRO A CA  1 
ATOM   356  C  C   . PRO A 1 53  ? -4.301  20.162  -4.802  1.00 35.99 ? 48  PRO A C   1 
ATOM   357  O  O   . PRO A 1 53  ? -4.159  20.151  -3.575  1.00 35.41 ? 48  PRO A O   1 
ATOM   358  C  CB  . PRO A 1 53  ? -2.137  19.166  -5.575  1.00 32.23 ? 48  PRO A CB  1 
ATOM   359  C  CG  . PRO A 1 53  ? -1.826  20.003  -6.810  1.00 29.96 ? 48  PRO A CG  1 
ATOM   360  C  CD  . PRO A 1 53  ? -2.762  19.412  -7.844  1.00 29.24 ? 48  PRO A CD  1 
ATOM   361  N  N   . GLU A 1 54  ? -4.945  21.131  -5.468  1.00 38.97 ? 49  GLU A N   1 
ATOM   362  C  CA  . GLU A 1 54  ? -5.627  22.282  -4.809  1.00 42.15 ? 49  GLU A CA  1 
ATOM   363  C  C   . GLU A 1 54  ? -7.088  21.917  -4.541  1.00 37.99 ? 49  GLU A C   1 
ATOM   364  O  O   . GLU A 1 54  ? -7.786  22.752  -3.999  1.00 35.13 ? 49  GLU A O   1 
ATOM   365  C  CB  . GLU A 1 54  ? -5.601  23.563  -5.659  1.00 45.10 ? 49  GLU A CB  1 
ATOM   366  C  CG  . GLU A 1 54  ? -4.230  23.933  -6.207  1.00 51.01 ? 49  GLU A CG  1 
ATOM   367  C  CD  . GLU A 1 54  ? -3.130  23.976  -5.163  1.00 55.72 ? 49  GLU A CD  1 
ATOM   368  O  OE1 . GLU A 1 54  ? -3.360  24.582  -4.095  1.00 57.30 ? 49  GLU A OE1 1 
ATOM   369  O  OE2 . GLU A 1 54  ? -2.044  23.395  -5.419  1.00 67.24 ? 49  GLU A OE2 1 
ATOM   370  N  N   . LEU A 1 55  ? -7.551  20.742  -4.960  1.00 40.93 ? 50  LEU A N   1 
ATOM   371  C  CA  . LEU A 1 55  ? -8.915  20.269  -4.598  1.00 44.16 ? 50  LEU A CA  1 
ATOM   372  C  C   . LEU A 1 55  ? -8.866  19.789  -3.141  1.00 48.08 ? 50  LEU A C   1 
ATOM   373  O  O   . LEU A 1 55  ? -8.197  18.773  -2.864  1.00 49.89 ? 50  LEU A O   1 
ATOM   374  C  CB  . LEU A 1 55  ? -9.385  19.169  -5.559  1.00 41.17 ? 50  LEU A CB  1 
ATOM   375  C  CG  . LEU A 1 55  ? -9.783  19.630  -6.963  1.00 39.47 ? 50  LEU A CG  1 
ATOM   376  C  CD1 . LEU A 1 55  ? -10.376 18.468  -7.727  1.00 35.10 ? 50  LEU A CD1 1 
ATOM   377  C  CD2 . LEU A 1 55  ? -10.775 20.796  -6.924  1.00 41.55 ? 50  LEU A CD2 1 
ATOM   378  N  N   . ASP A 1 56  ? -9.508  20.538  -2.242  1.00 55.39 ? 51  ASP A N   1 
ATOM   379  C  CA  . ASP A 1 56  ? -9.659  20.188  -0.805  1.00 63.01 ? 51  ASP A CA  1 
ATOM   380  C  C   . ASP A 1 56  ? -11.078 19.634  -0.612  1.00 62.15 ? 51  ASP A C   1 
ATOM   381  O  O   . ASP A 1 56  ? -12.024 20.221  -1.177  1.00 62.90 ? 51  ASP A O   1 
ATOM   382  C  CB  . ASP A 1 56  ? -9.325  21.392  0.084   1.00 68.51 ? 51  ASP A CB  1 
ATOM   383  C  CG  . ASP A 1 56  ? -7.855  21.797  0.042   1.00 72.23 ? 51  ASP A CG  1 
ATOM   384  O  OD1 . ASP A 1 56  ? -7.004  20.999  0.509   1.00 79.99 ? 51  ASP A OD1 1 
ATOM   385  O  OD2 . ASP A 1 56  ? -7.565  22.901  -0.470  1.00 72.38 ? 51  ASP A OD2 1 
ATOM   386  N  N   . GLY A 1 57  ? -11.205 18.521  0.114   1.00 52.25 ? 52  GLY A N   1 
ATOM   387  C  CA  . GLY A 1 57  ? -12.485 17.827  0.334   1.00 49.74 ? 52  GLY A CA  1 
ATOM   388  C  C   . GLY A 1 57  ? -12.596 16.605  -0.570  1.00 50.30 ? 52  GLY A C   1 
ATOM   389  O  O   . GLY A 1 57  ? -11.872 16.501  -1.560  1.00 49.05 ? 52  GLY A O   1 
ATOM   390  N  N   . PRO A 1 58  ? -13.472 15.630  -0.244  1.00 46.05 ? 53  PRO A N   1 
ATOM   391  C  CA  . PRO A 1 58  ? -13.580 14.411  -1.035  1.00 46.54 ? 53  PRO A CA  1 
ATOM   392  C  C   . PRO A 1 58  ? -13.820 14.720  -2.521  1.00 44.57 ? 53  PRO A C   1 
ATOM   393  O  O   . PRO A 1 58  ? -14.669 15.513  -2.854  1.00 40.33 ? 53  PRO A O   1 
ATOM   394  C  CB  . PRO A 1 58  ? -14.751 13.642  -0.406  1.00 49.23 ? 53  PRO A CB  1 
ATOM   395  C  CG  . PRO A 1 58  ? -14.834 14.175  1.005   1.00 49.83 ? 53  PRO A CG  1 
ATOM   396  C  CD  . PRO A 1 58  ? -14.363 15.615  0.923   1.00 50.54 ? 53  PRO A CD  1 
ATOM   397  N  N   . VAL A 1 59  ? -13.007 14.094  -3.365  1.00 41.11 ? 54  VAL A N   1 
ATOM   398  C  CA  . VAL A 1 59  ? -13.119 14.116  -4.847  1.00 39.21 ? 54  VAL A CA  1 
ATOM   399  C  C   . VAL A 1 59  ? -13.860 12.837  -5.235  1.00 36.77 ? 54  VAL A C   1 
ATOM   400  O  O   . VAL A 1 59  ? -13.240 11.763  -5.188  1.00 35.59 ? 54  VAL A O   1 
ATOM   401  C  CB  . VAL A 1 59  ? -11.720 14.215  -5.483  1.00 37.44 ? 54  VAL A CB  1 
ATOM   402  C  CG1 . VAL A 1 59  ? -11.767 14.054  -6.993  1.00 36.92 ? 54  VAL A CG1 1 
ATOM   403  C  CG2 . VAL A 1 59  ? -11.026 15.523  -5.100  1.00 38.46 ? 54  VAL A CG2 1 
ATOM   404  N  N   . ASP A 1 60  ? -15.140 12.967  -5.581  1.00 36.20 ? 55  ASP A N   1 
ATOM   405  C  CA  . ASP A 1 60  ? -16.064 11.835  -5.809  1.00 37.93 ? 55  ASP A CA  1 
ATOM   406  C  C   . ASP A 1 60  ? -16.153 11.497  -7.293  1.00 36.95 ? 55  ASP A C   1 
ATOM   407  O  O   . ASP A 1 60  ? -16.372 10.324  -7.572  1.00 41.63 ? 55  ASP A O   1 
ATOM   408  C  CB  . ASP A 1 60  ? -17.443 12.152  -5.243  1.00 42.55 ? 55  ASP A CB  1 
ATOM   409  C  CG  . ASP A 1 60  ? -17.563 11.822  -3.762  1.00 51.29 ? 55  ASP A CG  1 
ATOM   410  O  OD1 . ASP A 1 60  ? -16.510 11.536  -3.110  1.00 54.63 ? 55  ASP A OD1 1 
ATOM   411  O  OD2 . ASP A 1 60  ? -18.709 11.851  -3.264  1.00 58.62 ? 55  ASP A OD2 1 
ATOM   412  N  N   . ARG A 1 61  ? -16.009 12.488  -8.178  1.00 36.55 ? 56  ARG A N   1 
ATOM   413  C  CA  . ARG A 1 61  ? -16.268 12.394  -9.650  1.00 35.86 ? 56  ARG A CA  1 
ATOM   414  C  C   . ARG A 1 61  ? -15.055 12.952  -10.399 1.00 33.19 ? 56  ARG A C   1 
ATOM   415  O  O   . ARG A 1 61  ? -14.486 13.946  -9.896  1.00 30.12 ? 56  ARG A O   1 
ATOM   416  C  CB  . ARG A 1 61  ? -17.502 13.218  -10.057 1.00 36.69 ? 56  ARG A CB  1 
ATOM   417  C  CG  . ARG A 1 61  ? -18.798 12.420  -10.113 1.00 40.91 ? 56  ARG A CG  1 
ATOM   418  C  CD  . ARG A 1 61  ? -20.023 13.245  -10.460 1.00 40.77 ? 56  ARG A CD  1 
ATOM   419  N  NE  . ARG A 1 61  ? -20.047 14.459  -9.667  1.00 48.49 ? 56  ARG A NE  1 
ATOM   420  C  CZ  . ARG A 1 61  ? -20.296 14.511  -8.360  1.00 48.23 ? 56  ARG A CZ  1 
ATOM   421  N  NH1 . ARG A 1 61  ? -20.266 15.672  -7.731  1.00 51.14 ? 56  ARG A NH1 1 
ATOM   422  N  NH2 . ARG A 1 61  ? -20.571 13.409  -7.684  1.00 52.01 ? 56  ARG A NH2 1 
ATOM   423  N  N   . LEU A 1 62  ? -14.699 12.387  -11.569 1.00 32.12 ? 57  LEU A N   1 
ATOM   424  C  CA  . LEU A 1 62  ? -13.550 12.867  -12.380 1.00 30.04 ? 57  LEU A CA  1 
ATOM   425  C  C   . LEU A 1 62  ? -14.007 13.976  -13.330 1.00 31.66 ? 57  LEU A C   1 
ATOM   426  O  O   . LEU A 1 62  ? -13.222 14.891  -13.570 1.00 32.90 ? 57  LEU A O   1 
ATOM   427  C  CB  . LEU A 1 62  ? -12.942 11.695  -13.153 1.00 32.88 ? 57  LEU A CB  1 
ATOM   428  C  CG  . LEU A 1 62  ? -11.967 10.815  -12.371 1.00 33.80 ? 57  LEU A CG  1 
ATOM   429  C  CD1 . LEU A 1 62  ? -11.452 9.689   -13.267 1.00 34.72 ? 57  LEU A CD1 1 
ATOM   430  C  CD2 . LEU A 1 62  ? -10.786 11.613  -11.819 1.00 33.85 ? 57  LEU A CD2 1 
ATOM   431  N  N   . VAL A 1 63  ? -15.232 13.907  -13.852 1.00 31.41 ? 58  VAL A N   1 
ATOM   432  C  CA  . VAL A 1 63  ? -15.785 14.926  -14.797 1.00 33.37 ? 58  VAL A CA  1 
ATOM   433  C  C   . VAL A 1 63  ? -15.908 16.289  -14.099 1.00 30.91 ? 58  VAL A C   1 
ATOM   434  O  O   . VAL A 1 63  ? -16.420 16.327  -12.989 1.00 32.49 ? 58  VAL A O   1 
ATOM   435  C  CB  . VAL A 1 63  ? -17.124 14.451  -15.384 1.00 31.56 ? 58  VAL A CB  1 
ATOM   436  C  CG1 . VAL A 1 63  ? -17.830 15.567  -16.141 1.00 33.38 ? 58  VAL A CG1 1 
ATOM   437  C  CG2 . VAL A 1 63  ? -16.879 13.256  -16.301 1.00 33.14 ? 58  VAL A CG2 1 
ATOM   438  N  N   . GLY A 1 64  ? -15.378 17.349  -14.718 1.00 33.09 ? 59  GLY A N   1 
ATOM   439  C  CA  . GLY A 1 64  ? -15.412 18.735  -14.214 1.00 33.67 ? 59  GLY A CA  1 
ATOM   440  C  C   . GLY A 1 64  ? -14.075 19.160  -13.631 1.00 38.49 ? 59  GLY A C   1 
ATOM   441  O  O   . GLY A 1 64  ? -13.805 20.376  -13.561 1.00 39.68 ? 59  GLY A O   1 
ATOM   442  N  N   . ILE A 1 65  ? -13.234 18.188  -13.288 1.00 37.31 ? 60  ILE A N   1 
ATOM   443  C  CA  . ILE A 1 65  ? -11.962 18.386  -12.539 1.00 35.29 ? 60  ILE A CA  1 
ATOM   444  C  C   . ILE A 1 65  ? -10.756 18.440  -13.494 1.00 30.31 ? 60  ILE A C   1 
ATOM   445  O  O   . ILE A 1 65  ? -10.828 17.887  -14.618 1.00 30.39 ? 60  ILE A O   1 
ATOM   446  C  CB  . ILE A 1 65  ? -11.869 17.249  -11.511 1.00 39.94 ? 60  ILE A CB  1 
ATOM   447  C  CG1 . ILE A 1 65  ? -13.030 17.360  -10.521 1.00 39.15 ? 60  ILE A CG1 1 
ATOM   448  C  CG2 . ILE A 1 65  ? -10.514 17.229  -10.834 1.00 46.28 ? 60  ILE A CG2 1 
ATOM   449  C  CD1 . ILE A 1 65  ? -12.922 16.414  -9.361  1.00 42.27 ? 60  ILE A CD1 1 
ATOM   450  N  N   . THR A 1 66  ? -9.663  19.060  -13.045 1.00 28.79 ? 61  THR A N   1 
ATOM   451  C  CA  . THR A 1 66  ? -8.398  19.177  -13.807 1.00 30.52 ? 61  THR A CA  1 
ATOM   452  C  C   . THR A 1 66  ? -7.386  18.186  -13.251 1.00 28.50 ? 61  THR A C   1 
ATOM   453  O  O   . THR A 1 66  ? -7.211  18.154  -12.026 1.00 30.28 ? 61  THR A O   1 
ATOM   454  C  CB  . THR A 1 66  ? -7.898  20.623  -13.901 1.00 30.70 ? 61  THR A CB  1 
ATOM   455  O  OG1 . THR A 1 66  ? -8.947  21.311  -14.587 1.00 33.32 ? 61  THR A OG1 1 
ATOM   456  C  CG2 . THR A 1 66  ? -6.624  20.779  -14.708 1.00 31.12 ? 61  THR A CG2 1 
ATOM   457  N  N   . LEU A 1 67  ? -6.817  17.377  -14.156 1.00 28.51 ? 62  LEU A N   1 
ATOM   458  C  CA  . LEU A 1 67  ? -5.652  16.499  -13.907 1.00 26.32 ? 62  LEU A CA  1 
ATOM   459  C  C   . LEU A 1 67  ? -4.398  17.249  -14.338 1.00 25.64 ? 62  LEU A C   1 
ATOM   460  O  O   . LEU A 1 67  ? -4.495  17.997  -15.289 1.00 26.96 ? 62  LEU A O   1 
ATOM   461  C  CB  . LEU A 1 67  ? -5.830  15.174  -14.656 1.00 27.31 ? 62  LEU A CB  1 
ATOM   462  C  CG  . LEU A 1 67  ? -7.123  14.429  -14.325 1.00 26.01 ? 62  LEU A CG  1 
ATOM   463  C  CD1 . LEU A 1 67  ? -7.146  13.093  -15.005 1.00 27.10 ? 62  LEU A CD1 1 
ATOM   464  C  CD2 . LEU A 1 67  ? -7.318  14.263  -12.827 1.00 26.35 ? 62  LEU A CD2 1 
ATOM   465  N  N   . TRP A 1 68  ? -3.308  17.067  -13.581 1.00 25.13 ? 63  TRP A N   1 
ATOM   466  C  CA  . TRP A 1 68  ? -1.954  17.616  -13.796 1.00 24.51 ? 63  TRP A CA  1 
ATOM   467  C  C   . TRP A 1 68  ? -1.060  16.491  -14.293 1.00 26.33 ? 63  TRP A C   1 
ATOM   468  O  O   . TRP A 1 68  ? -1.173  15.384  -13.743 1.00 27.58 ? 63  TRP A O   1 
ATOM   469  C  CB  . TRP A 1 68  ? -1.369  18.187  -12.501 1.00 26.86 ? 63  TRP A CB  1 
ATOM   470  C  CG  . TRP A 1 68  ? -2.008  19.440  -12.009 1.00 24.69 ? 63  TRP A CG  1 
ATOM   471  C  CD1 . TRP A 1 68  ? -3.280  19.857  -12.260 1.00 26.56 ? 63  TRP A CD1 1 
ATOM   472  C  CD2 . TRP A 1 68  ? -1.433  20.412  -11.122 1.00 25.09 ? 63  TRP A CD2 1 
ATOM   473  N  NE1 . TRP A 1 68  ? -3.532  21.031  -11.613 1.00 28.91 ? 63  TRP A NE1 1 
ATOM   474  C  CE2 . TRP A 1 68  ? -2.430  21.388  -10.884 1.00 27.83 ? 63  TRP A CE2 1 
ATOM   475  C  CE3 . TRP A 1 68  ? -0.201  20.541  -10.491 1.00 24.02 ? 63  TRP A CE3 1 
ATOM   476  C  CZ2 . TRP A 1 68  ? -2.229  22.483  -10.046 1.00 28.37 ? 63  TRP A CZ2 1 
ATOM   477  C  CZ3 . TRP A 1 68  ? 0.004   21.626  -9.664  1.00 27.16 ? 63  TRP A CZ3 1 
ATOM   478  C  CH2 . TRP A 1 68  ? -0.984  22.594  -9.463  1.00 28.97 ? 63  TRP A CH2 1 
ATOM   479  N  N   . GLY A 1 69  ? -0.186  16.762  -15.266 1.00 24.90 ? 64  GLY A N   1 
ATOM   480  C  CA  . GLY A 1 69  ? 0.805   15.761  -15.672 1.00 25.94 ? 64  GLY A CA  1 
ATOM   481  C  C   . GLY A 1 69  ? 2.057   16.418  -16.181 1.00 29.33 ? 64  GLY A C   1 
ATOM   482  O  O   . GLY A 1 69  ? 2.061   17.647  -16.330 1.00 33.96 ? 64  GLY A O   1 
ATOM   483  N  N   . HIS A 1 70  ? 3.104   15.640  -16.426 1.00 25.28 ? 65  HIS A N   1 
ATOM   484  C  CA  . HIS A 1 70  ? 4.235   16.125  -17.252 1.00 25.16 ? 65  HIS A CA  1 
ATOM   485  C  C   . HIS A 1 70  ? 4.770   14.999  -18.114 1.00 24.86 ? 65  HIS A C   1 
ATOM   486  O  O   . HIS A 1 70  ? 4.450   13.827  -17.852 1.00 23.22 ? 65  HIS A O   1 
ATOM   487  C  CB  . HIS A 1 70  ? 5.319   16.766  -16.388 1.00 24.73 ? 65  HIS A CB  1 
ATOM   488  C  CG  . HIS A 1 70  ? 6.100   15.806  -15.563 1.00 22.04 ? 65  HIS A CG  1 
ATOM   489  N  ND1 . HIS A 1 70  ? 5.599   15.290  -14.385 1.00 23.72 ? 65  HIS A ND1 1 
ATOM   490  C  CD2 . HIS A 1 70  ? 7.359   15.309  -15.708 1.00 21.88 ? 65  HIS A CD2 1 
ATOM   491  C  CE1 . HIS A 1 70  ? 6.515   14.502  -13.843 1.00 24.21 ? 65  HIS A CE1 1 
ATOM   492  N  NE2 . HIS A 1 70  ? 7.592   14.489  -14.637 1.00 20.40 ? 65  HIS A NE2 1 
ATOM   493  N  N   . MET A 1 71  ? 5.556   15.389  -19.113 1.00 25.86 ? 66  MET A N   1 
ATOM   494  C  CA  . MET A 1 71  ? 6.289   14.499  -20.013 1.00 23.86 ? 66  MET A CA  1 
ATOM   495  C  C   . MET A 1 71  ? 7.580   15.217  -20.381 1.00 22.82 ? 66  MET A C   1 
ATOM   496  O  O   . MET A 1 71  ? 7.776   16.347  -19.900 1.00 20.54 ? 66  MET A O   1 
ATOM   497  C  CB  . MET A 1 71  ? 5.472   14.183  -21.272 1.00 25.51 ? 66  MET A CB  1 
ATOM   498  C  CG  . MET A 1 71  ? 5.190   15.369  -22.189 1.00 26.96 ? 66  MET A CG  1 
ATOM   499  S  SD  . MET A 1 71  ? 4.610   14.825  -23.790 1.00 35.11 ? 66  MET A SD  1 
ATOM   500  C  CE  . MET A 1 71  ? 2.908   14.534  -23.314 1.00 33.65 ? 66  MET A CE  1 
ATOM   501  N  N   . ASN A 1 72  ? 8.383   14.578  -21.231 1.00 23.01 ? 67  ASN A N   1 
ATOM   502  C  CA  . ASN A 1 72  ? 9.644   15.141  -21.762 1.00 24.16 ? 67  ASN A CA  1 
ATOM   503  C  C   . ASN A 1 72  ? 9.318   16.095  -22.917 1.00 24.40 ? 67  ASN A C   1 
ATOM   504  O  O   . ASN A 1 72  ? 8.760   15.633  -23.910 1.00 24.78 ? 67  ASN A O   1 
ATOM   505  C  CB  . ASN A 1 72  ? 10.609  14.071  -22.234 1.00 23.76 ? 67  ASN A CB  1 
ATOM   506  C  CG  . ASN A 1 72  ? 11.972  14.671  -22.464 1.00 28.23 ? 67  ASN A CG  1 
ATOM   507  O  OD1 . ASN A 1 72  ? 12.066  15.892  -22.670 1.00 26.23 ? 67  ASN A OD1 1 
ATOM   508  N  ND2 . ASN A 1 72  ? 13.003  13.839  -22.364 1.00 25.34 ? 67  ASN A ND2 1 
ATOM   509  N  N   . ARG A 1 73  ? 9.695   17.371  -22.794 1.00 23.16 ? 68  ARG A N   1 
ATOM   510  C  CA  . ARG A 1 73  ? 9.560   18.371  -23.892 1.00 26.19 ? 68  ARG A CA  1 
ATOM   511  C  C   . ARG A 1 73  ? 10.226  17.912  -25.189 1.00 26.59 ? 68  ARG A C   1 
ATOM   512  O  O   . ARG A 1 73  ? 9.722   18.277  -26.235 1.00 31.61 ? 68  ARG A O   1 
ATOM   513  C  CB  . ARG A 1 73  ? 10.145  19.710  -23.462 1.00 26.71 ? 68  ARG A CB  1 
ATOM   514  C  CG  . ARG A 1 73  ? 9.051   20.648  -23.010 1.00 25.78 ? 68  ARG A CG  1 
ATOM   515  C  CD  . ARG A 1 73  ? 9.567   22.021  -22.713 1.00 23.09 ? 68  ARG A CD  1 
ATOM   516  N  NE  . ARG A 1 73  ? 8.593   22.574  -21.808 1.00 19.35 ? 68  ARG A NE  1 
ATOM   517  C  CZ  . ARG A 1 73  ? 7.785   23.543  -22.103 1.00 19.34 ? 68  ARG A CZ  1 
ATOM   518  N  NH1 . ARG A 1 73  ? 7.789   24.068  -23.314 1.00 23.70 ? 68  ARG A NH1 1 
ATOM   519  N  NH2 . ARG A 1 73  ? 6.943   23.967  -21.194 1.00 21.75 ? 68  ARG A NH2 1 
ATOM   520  N  N   . ALA A 1 74  ? 11.309  17.136  -25.109 1.00 28.05 ? 69  ALA A N   1 
ATOM   521  C  CA  . ALA A 1 74  ? 12.070  16.618  -26.266 1.00 28.82 ? 69  ALA A CA  1 
ATOM   522  C  C   . ALA A 1 74  ? 11.348  15.394  -26.859 1.00 28.85 ? 69  ALA A C   1 
ATOM   523  O  O   . ALA A 1 74  ? 11.649  15.000  -27.993 1.00 29.56 ? 69  ALA A O   1 
ATOM   524  C  CB  . ALA A 1 74  ? 13.478  16.288  -25.831 1.00 27.92 ? 69  ALA A CB  1 
ATOM   525  N  N   . ASN A 1 75  ? 10.411  14.801  -26.121 1.00 29.36 ? 70  ASN A N   1 
ATOM   526  C  CA  . ASN A 1 75  ? 9.453   13.801  -26.669 1.00 26.98 ? 70  ASN A CA  1 
ATOM   527  C  C   . ASN A 1 75  ? 8.689   14.425  -27.840 1.00 24.41 ? 70  ASN A C   1 
ATOM   528  O  O   . ASN A 1 75  ? 7.915   15.359  -27.626 1.00 20.59 ? 70  ASN A O   1 
ATOM   529  C  CB  . ASN A 1 75  ? 8.496   13.318  -25.579 1.00 27.69 ? 70  ASN A CB  1 
ATOM   530  C  CG  . ASN A 1 75  ? 7.696   12.105  -25.978 1.00 26.60 ? 70  ASN A CG  1 
ATOM   531  O  OD1 . ASN A 1 75  ? 7.393   11.957  -27.158 1.00 27.57 ? 70  ASN A OD1 1 
ATOM   532  N  ND2 . ASN A 1 75  ? 7.348   11.259  -25.004 1.00 25.02 ? 70  ASN A ND2 1 
ATOM   533  N  N   . PRO A 1 76  ? 8.776   13.861  -29.075 1.00 25.45 ? 71  PRO A N   1 
ATOM   534  C  CA  . PRO A 1 76  ? 8.058   14.427  -30.223 1.00 26.48 ? 71  PRO A CA  1 
ATOM   535  C  C   . PRO A 1 76  ? 6.524   14.469  -30.019 1.00 26.81 ? 71  PRO A C   1 
ATOM   536  O  O   . PRO A 1 76  ? 5.862   15.185  -30.742 1.00 27.92 ? 71  PRO A O   1 
ATOM   537  C  CB  . PRO A 1 76  ? 8.465   13.518  -31.407 1.00 27.93 ? 71  PRO A CB  1 
ATOM   538  C  CG  . PRO A 1 76  ? 9.718   12.782  -30.924 1.00 28.82 ? 71  PRO A CG  1 
ATOM   539  C  CD  . PRO A 1 76  ? 9.525   12.641  -29.432 1.00 25.27 ? 71  PRO A CD  1 
ATOM   540  N  N   . HIS A 1 77  ? 5.970   13.699  -29.064 1.00 25.52 ? 72  HIS A N   1 
ATOM   541  C  CA  . HIS A 1 77  ? 4.525   13.722  -28.695 1.00 22.44 ? 72  HIS A CA  1 
ATOM   542  C  C   . HIS A 1 77  ? 4.173   15.132  -28.192 1.00 21.80 ? 72  HIS A C   1 
ATOM   543  O  O   . HIS A 1 77  ? 3.108   15.601  -28.459 1.00 22.31 ? 72  HIS A O   1 
ATOM   544  C  CB  . HIS A 1 77  ? 4.213   12.642  -27.664 1.00 22.14 ? 72  HIS A CB  1 
ATOM   545  C  CG  . HIS A 1 77  ? 2.752   12.401  -27.429 1.00 20.52 ? 72  HIS A CG  1 
ATOM   546  N  ND1 . HIS A 1 77  ? 2.313   11.399  -26.604 1.00 19.73 ? 72  HIS A ND1 1 
ATOM   547  C  CD2 . HIS A 1 77  ? 1.630   12.993  -27.916 1.00 21.36 ? 72  HIS A CD2 1 
ATOM   548  C  CE1 . HIS A 1 77  ? 0.984   11.377  -26.562 1.00 19.87 ? 72  HIS A CE1 1 
ATOM   549  N  NE2 . HIS A 1 77  ? 0.539   12.382  -27.333 1.00 21.92 ? 72  HIS A NE2 1 
ATOM   550  N  N   . TRP A 1 78  ? 5.070   15.785  -27.492 1.00 21.96 ? 73  TRP A N   1 
ATOM   551  C  CA  . TRP A 1 78  ? 4.871   17.162  -26.986 1.00 26.60 ? 73  TRP A CA  1 
ATOM   552  C  C   . TRP A 1 78  ? 4.618   18.090  -28.187 1.00 26.71 ? 73  TRP A C   1 
ATOM   553  O  O   . TRP A 1 78  ? 3.528   18.715  -28.240 1.00 25.62 ? 73  TRP A O   1 
ATOM   554  C  CB  . TRP A 1 78  ? 6.064   17.615  -26.137 1.00 26.36 ? 73  TRP A CB  1 
ATOM   555  C  CG  . TRP A 1 78  ? 5.907   19.013  -25.621 1.00 27.41 ? 73  TRP A CG  1 
ATOM   556  C  CD1 . TRP A 1 78  ? 6.409   20.147  -26.190 1.00 24.47 ? 73  TRP A CD1 1 
ATOM   557  C  CD2 . TRP A 1 78  ? 5.146   19.432  -24.471 1.00 26.28 ? 73  TRP A CD2 1 
ATOM   558  N  NE1 . TRP A 1 78  ? 6.037   21.229  -25.461 1.00 27.40 ? 73  TRP A NE1 1 
ATOM   559  C  CE2 . TRP A 1 78  ? 5.283   20.832  -24.390 1.00 28.99 ? 73  TRP A CE2 1 
ATOM   560  C  CE3 . TRP A 1 78  ? 4.375   18.776  -23.506 1.00 29.64 ? 73  TRP A CE3 1 
ATOM   561  C  CZ2 . TRP A 1 78  ? 4.702   21.582  -23.370 1.00 27.15 ? 73  TRP A CZ2 1 
ATOM   562  C  CZ3 . TRP A 1 78  ? 3.778   19.516  -22.505 1.00 26.85 ? 73  TRP A CZ3 1 
ATOM   563  C  CH2 . TRP A 1 78  ? 3.941   20.898  -22.456 1.00 30.37 ? 73  TRP A CH2 1 
ATOM   564  N  N   . ALA A 1 79  ? 5.521   18.110  -29.169 1.00 26.53 ? 74  ALA A N   1 
ATOM   565  C  CA  . ALA A 1 79  ? 5.354   18.949  -30.387 1.00 29.73 ? 74  ALA A CA  1 
ATOM   566  C  C   . ALA A 1 79  ? 4.035   18.582  -31.093 1.00 32.76 ? 74  ALA A C   1 
ATOM   567  O  O   . ALA A 1 79  ? 3.354   19.506  -31.569 1.00 34.40 ? 74  ALA A O   1 
ATOM   568  C  CB  . ALA A 1 79  ? 6.550   18.829  -31.304 1.00 29.23 ? 74  ALA A CB  1 
ATOM   569  N  N   . ALA A 1 80  ? 3.673   17.294  -31.178 1.00 30.95 ? 75  ALA A N   1 
ATOM   570  C  CA  . ALA A 1 80  ? 2.522   16.847  -31.977 1.00 29.14 ? 75  ALA A CA  1 
ATOM   571  C  C   . ALA A 1 80  ? 1.230   17.185  -31.230 1.00 34.97 ? 75  ALA A C   1 
ATOM   572  O  O   . ALA A 1 80  ? 0.190   17.356  -31.897 1.00 35.14 ? 75  ALA A O   1 
ATOM   573  C  CB  . ALA A 1 80  ? 2.649   15.395  -32.312 1.00 35.23 ? 75  ALA A CB  1 
ATOM   574  N  N   . LEU A 1 81  ? 1.275   17.364  -29.910 1.00 34.55 ? 76  LEU A N   1 
ATOM   575  C  CA  . LEU A 1 81  ? 0.056   17.737  -29.151 1.00 37.90 ? 76  LEU A CA  1 
ATOM   576  C  C   . LEU A 1 81  ? -0.429  19.097  -29.654 1.00 51.54 ? 76  LEU A C   1 
ATOM   577  O  O   . LEU A 1 81  ? -1.665  19.235  -29.868 1.00 53.36 ? 76  LEU A O   1 
ATOM   578  C  CB  . LEU A 1 81  ? 0.321   17.743  -27.646 1.00 35.05 ? 76  LEU A CB  1 
ATOM   579  C  CG  . LEU A 1 81  ? 0.336   16.356  -27.003 1.00 34.16 ? 76  LEU A CG  1 
ATOM   580  C  CD1 . LEU A 1 81  ? 0.870   16.442  -25.577 1.00 31.24 ? 76  LEU A CD1 1 
ATOM   581  C  CD2 . LEU A 1 81  ? -1.056  15.736  -27.031 1.00 34.68 ? 76  LEU A CD2 1 
ATOM   582  N  N   . GLY A 1 82  ? 0.505   20.021  -29.914 1.00 54.79 ? 77  GLY A N   1 
ATOM   583  C  CA  . GLY A 1 82  ? 0.170   21.430  -30.156 1.00 58.07 ? 77  GLY A CA  1 
ATOM   584  C  C   . GLY A 1 82  ? -0.712  21.889  -29.016 1.00 61.86 ? 77  GLY A C   1 
ATOM   585  O  O   . GLY A 1 82  ? -0.726  21.172  -27.987 1.00 51.15 ? 77  GLY A O   1 
ATOM   586  N  N   . GLY A 1 83  ? -1.440  22.996  -29.189 1.00 63.49 ? 78  GLY A N   1 
ATOM   587  C  CA  . GLY A 1 83  ? -2.383  23.513  -28.180 1.00 59.91 ? 78  GLY A CA  1 
ATOM   588  C  C   . GLY A 1 83  ? -3.799  23.183  -28.574 1.00 58.13 ? 78  GLY A C   1 
ATOM   589  O  O   . GLY A 1 83  ? -4.108  23.369  -29.767 1.00 64.03 ? 78  GLY A O   1 
ATOM   590  N  N   . ALA A 1 84  ? -4.611  22.693  -27.629 1.00 57.06 ? 79  ALA A N   1 
ATOM   591  C  CA  . ALA A 1 84  ? -6.061  22.404  -27.802 1.00 56.09 ? 79  ALA A CA  1 
ATOM   592  C  C   . ALA A 1 84  ? -6.297  21.021  -28.426 1.00 50.62 ? 79  ALA A C   1 
ATOM   593  O  O   . ALA A 1 84  ? -7.290  20.877  -29.178 1.00 53.45 ? 79  ALA A O   1 
ATOM   594  C  CB  . ALA A 1 84  ? -6.715  23.476  -28.646 1.00 52.42 ? 79  ALA A CB  1 
ATOM   595  N  N   . ALA A 1 85  ? -5.442  20.039  -28.120 1.00 48.63 ? 80  ALA A N   1 
ATOM   596  C  CA  . ALA A 1 85  ? -5.556  18.643  -28.620 1.00 45.23 ? 80  ALA A CA  1 
ATOM   597  C  C   . ALA A 1 85  ? -6.570  17.881  -27.769 1.00 36.23 ? 80  ALA A C   1 
ATOM   598  O  O   . ALA A 1 85  ? -6.514  17.996  -26.541 1.00 33.92 ? 80  ALA A O   1 
ATOM   599  C  CB  . ALA A 1 85  ? -4.221  17.949  -28.604 1.00 44.03 ? 80  ALA A CB  1 
ATOM   600  N  N   . ASN A 1 86  ? -7.424  17.086  -28.406 1.00 35.79 ? 81  ASN A N   1 
ATOM   601  C  CA  . ASN A 1 86  ? -8.374  16.211  -27.665 1.00 35.79 ? 81  ASN A CA  1 
ATOM   602  C  C   . ASN A 1 86  ? -7.648  14.916  -27.327 1.00 28.63 ? 81  ASN A C   1 
ATOM   603  O  O   . ASN A 1 86  ? -7.239  14.219  -28.252 1.00 30.21 ? 81  ASN A O   1 
ATOM   604  C  CB  . ASN A 1 86  ? -9.687  16.021  -28.385 1.00 34.10 ? 81  ASN A CB  1 
ATOM   605  C  CG  . ASN A 1 86  ? -10.225 17.356  -28.820 1.00 37.94 ? 81  ASN A CG  1 
ATOM   606  O  OD1 . ASN A 1 86  ? -10.162 18.317  -28.075 1.00 44.84 ? 81  ASN A OD1 1 
ATOM   607  N  ND2 . ASN A 1 86  ? -10.701 17.430  -30.039 1.00 39.41 ? 81  ASN A ND2 1 
ATOM   608  N  N   . VAL A 1 87  ? -7.513  14.639  -26.041 1.00 24.48 ? 82  VAL A N   1 
ATOM   609  C  CA  . VAL A 1 87  ? -6.680  13.478  -25.625 1.00 24.95 ? 82  VAL A CA  1 
ATOM   610  C  C   . VAL A 1 87  ? -7.492  12.521  -24.772 1.00 23.98 ? 82  VAL A C   1 
ATOM   611  O  O   . VAL A 1 87  ? -8.598  12.872  -24.340 1.00 25.47 ? 82  VAL A O   1 
ATOM   612  C  CB  . VAL A 1 87  ? -5.355  13.890  -24.964 1.00 25.61 ? 82  VAL A CB  1 
ATOM   613  C  CG1 . VAL A 1 87  ? -4.590  14.845  -25.854 1.00 27.86 ? 82  VAL A CG1 1 
ATOM   614  C  CG2 . VAL A 1 87  ? -5.521  14.468  -23.571 1.00 26.05 ? 82  VAL A CG2 1 
ATOM   615  N  N   . VAL A 1 88  ? -6.973  11.304  -24.654 1.00 23.01 ? 83  VAL A N   1 
ATOM   616  C  CA  . VAL A 1 88  ? -7.469  10.270  -23.707 1.00 22.61 ? 83  VAL A CA  1 
ATOM   617  C  C   . VAL A 1 88  ? -6.261  9.897   -22.862 1.00 21.93 ? 83  VAL A C   1 
ATOM   618  O  O   . VAL A 1 88  ? -5.180  9.762   -23.418 1.00 21.46 ? 83  VAL A O   1 
ATOM   619  C  CB  . VAL A 1 88  ? -8.122  9.070   -24.413 1.00 22.51 ? 83  VAL A CB  1 
ATOM   620  C  CG1 . VAL A 1 88  ? -7.275  8.549   -25.561 1.00 26.98 ? 83  VAL A CG1 1 
ATOM   621  C  CG2 . VAL A 1 88  ? -8.437  7.948   -23.454 1.00 23.13 ? 83  VAL A CG2 1 
ATOM   622  N  N   . ALA A 1 89  ? -6.442  9.810   -21.552 1.00 20.77 ? 84  ALA A N   1 
ATOM   623  C  CA  . ALA A 1 89  ? -5.421  9.265   -20.642 1.00 21.53 ? 84  ALA A CA  1 
ATOM   624  C  C   . ALA A 1 89  ? -6.017  8.015   -20.006 1.00 22.30 ? 84  ALA A C   1 
ATOM   625  O  O   . ALA A 1 89  ? -7.168  8.093   -19.512 1.00 18.64 ? 84  ALA A O   1 
ATOM   626  C  CB  . ALA A 1 89  ? -5.026  10.308  -19.635 1.00 23.08 ? 84  ALA A CB  1 
ATOM   627  N  N   . THR A 1 90  ? -5.354  6.877   -20.180 1.00 20.70 ? 85  THR A N   1 
ATOM   628  C  CA  . THR A 1 90  ? -5.864  5.563   -19.722 1.00 19.99 ? 85  THR A CA  1 
ATOM   629  C  C   . THR A 1 90  ? -5.047  5.123   -18.496 1.00 18.92 ? 85  THR A C   1 
ATOM   630  O  O   . THR A 1 90  ? -3.766  5.053   -18.543 1.00 19.84 ? 85  THR A O   1 
ATOM   631  C  CB  . THR A 1 90  ? -5.840  4.531   -20.849 1.00 19.76 ? 85  THR A CB  1 
ATOM   632  O  OG1 . THR A 1 90  ? -6.664  4.956   -21.928 1.00 20.12 ? 85  THR A OG1 1 
ATOM   633  C  CG2 . THR A 1 90  ? -6.340  3.192   -20.366 1.00 19.92 ? 85  THR A CG2 1 
ATOM   634  N  N   . PHE A 1 91  ? -5.737  4.901   -17.406 1.00 18.24 ? 86  PHE A N   1 
ATOM   635  C  CA  . PHE A 1 91  ? -5.140  4.370   -16.165 1.00 20.32 ? 86  PHE A CA  1 
ATOM   636  C  C   . PHE A 1 91  ? -5.533  2.893   -16.117 1.00 20.64 ? 86  PHE A C   1 
ATOM   637  O  O   . PHE A 1 91  ? -6.735  2.570   -16.276 1.00 22.64 ? 86  PHE A O   1 
ATOM   638  C  CB  . PHE A 1 91  ? -5.630  5.195   -14.981 1.00 18.46 ? 86  PHE A CB  1 
ATOM   639  C  CG  . PHE A 1 91  ? -5.376  6.681   -15.077 1.00 18.39 ? 86  PHE A CG  1 
ATOM   640  C  CD1 . PHE A 1 91  ? -6.161  7.508   -15.883 1.00 17.76 ? 86  PHE A CD1 1 
ATOM   641  C  CD2 . PHE A 1 91  ? -4.389  7.269   -14.299 1.00 19.00 ? 86  PHE A CD2 1 
ATOM   642  C  CE1 . PHE A 1 91  ? -5.962  8.876   -15.910 1.00 17.01 ? 86  PHE A CE1 1 
ATOM   643  C  CE2 . PHE A 1 91  ? -4.244  8.649   -14.268 1.00 18.06 ? 86  PHE A CE2 1 
ATOM   644  C  CZ  . PHE A 1 91  ? -4.975  9.435   -15.135 1.00 19.74 ? 86  PHE A CZ  1 
ATOM   645  N  N   . ALA A 1 92  ? -4.565  2.039   -15.854 1.00 20.48 ? 87  ALA A N   1 
ATOM   646  C  CA  . ALA A 1 92  ? -4.745  0.578   -15.789 1.00 24.36 ? 87  ALA A CA  1 
ATOM   647  C  C   . ALA A 1 92  ? -4.501  0.083   -14.352 1.00 26.85 ? 87  ALA A C   1 
ATOM   648  O  O   . ALA A 1 92  ? -3.365  0.178   -13.853 1.00 23.76 ? 87  ALA A O   1 
ATOM   649  C  CB  . ALA A 1 92  ? -3.824  -0.055  -16.792 1.00 26.01 ? 87  ALA A CB  1 
ATOM   650  N  N   . GLY A 1 93  ? -5.532  -0.494  -13.732 1.00 25.10 ? 88  GLY A N   1 
ATOM   651  C  CA  . GLY A 1 93  ? -5.474  -1.053  -12.373 1.00 23.92 ? 88  GLY A CA  1 
ATOM   652  C  C   . GLY A 1 93  ? -5.154  -2.553  -12.310 1.00 23.98 ? 88  GLY A C   1 
ATOM   653  O  O   . GLY A 1 93  ? -4.538  -3.152  -13.198 1.00 18.67 ? 88  GLY A O   1 
ATOM   654  N  N   . PRO A 1 94  ? -5.538  -3.200  -11.187 1.00 23.63 ? 89  PRO A N   1 
ATOM   655  C  CA  . PRO A 1 94  ? -5.328  -4.633  -11.004 1.00 24.01 ? 89  PRO A CA  1 
ATOM   656  C  C   . PRO A 1 94  ? -6.020  -5.460  -12.106 1.00 24.27 ? 89  PRO A C   1 
ATOM   657  O  O   . PRO A 1 94  ? -7.063  -5.066  -12.675 1.00 22.35 ? 89  PRO A O   1 
ATOM   658  C  CB  . PRO A 1 94  ? -5.974  -4.913  -9.643  1.00 25.86 ? 89  PRO A CB  1 
ATOM   659  C  CG  . PRO A 1 94  ? -6.004  -3.567  -8.942  1.00 24.65 ? 89  PRO A CG  1 
ATOM   660  C  CD  . PRO A 1 94  ? -6.220  -2.571  -10.046 1.00 24.95 ? 89  PRO A CD  1 
ATOM   661  N  N   . ASN A 1 95  ? -5.435  -6.615  -12.394 1.00 23.17 ? 90  ASN A N   1 
ATOM   662  C  CA  . ASN A 1 95  ? -5.885  -7.467  -13.510 1.00 22.11 ? 90  ASN A CA  1 
ATOM   663  C  C   . ASN A 1 95  ? -5.334  -8.871  -13.289 1.00 22.91 ? 90  ASN A C   1 
ATOM   664  O  O   . ASN A 1 95  ? -4.219  -9.027  -12.706 1.00 22.45 ? 90  ASN A O   1 
ATOM   665  C  CB  . ASN A 1 95  ? -5.462  -6.849  -14.842 1.00 22.86 ? 90  ASN A CB  1 
ATOM   666  C  CG  . ASN A 1 95  ? -3.974  -6.973  -15.089 1.00 25.20 ? 90  ASN A CG  1 
ATOM   667  O  OD1 . ASN A 1 95  ? -3.514  -7.988  -15.592 1.00 26.62 ? 90  ASN A OD1 1 
ATOM   668  N  ND2 . ASN A 1 95  ? -3.233  -5.929  -14.788 1.00 24.14 ? 90  ASN A ND2 1 
ATOM   669  N  N   . ALA A 1 96  ? -6.061  -9.869  -13.769 1.00 20.64 ? 91  ALA A N   1 
ATOM   670  C  CA  . ALA A 1 96  ? -5.618  -11.274 -13.710 1.00 19.34 ? 91  ALA A CA  1 
ATOM   671  C  C   . ALA A 1 96  ? -6.360  -12.092 -14.739 1.00 21.59 ? 91  ALA A C   1 
ATOM   672  O  O   . ALA A 1 96  ? -7.609  -11.877 -14.879 1.00 19.44 ? 91  ALA A O   1 
ATOM   673  C  CB  . ALA A 1 96  ? -5.874  -11.813 -12.327 1.00 19.09 ? 91  ALA A CB  1 
ATOM   674  N  N   . TYR A 1 97  ? -5.658  -13.046 -15.349 1.00 21.53 ? 92  TYR A N   1 
ATOM   675  C  CA  . TYR A 1 97  ? -6.269  -14.033 -16.259 1.00 23.14 ? 92  TYR A CA  1 
ATOM   676  C  C   . TYR A 1 97  ? -7.231  -14.930 -15.491 1.00 22.81 ? 92  TYR A C   1 
ATOM   677  O  O   . TYR A 1 97  ? -6.888  -15.336 -14.381 1.00 21.93 ? 92  TYR A O   1 
ATOM   678  C  CB  . TYR A 1 97  ? -5.194  -14.898 -16.884 1.00 23.42 ? 92  TYR A CB  1 
ATOM   679  C  CG  . TYR A 1 97  ? -5.734  -16.005 -17.740 1.00 23.12 ? 92  TYR A CG  1 
ATOM   680  C  CD1 . TYR A 1 97  ? -6.192  -15.745 -19.011 1.00 23.15 ? 92  TYR A CD1 1 
ATOM   681  C  CD2 . TYR A 1 97  ? -5.706  -17.320 -17.309 1.00 23.50 ? 92  TYR A CD2 1 
ATOM   682  C  CE1 . TYR A 1 97  ? -6.597  -16.766 -19.851 1.00 25.48 ? 92  TYR A CE1 1 
ATOM   683  C  CE2 . TYR A 1 97  ? -6.155  -18.348 -18.116 1.00 24.92 ? 92  TYR A CE2 1 
ATOM   684  C  CZ  . TYR A 1 97  ? -6.611  -18.072 -19.395 1.00 25.56 ? 92  TYR A CZ  1 
ATOM   685  O  OH  . TYR A 1 97  ? -7.055  -19.064 -20.218 1.00 23.61 ? 92  TYR A OH  1 
ATOM   686  N  N   . VAL A 1 98  ? -8.414  -15.197 -16.055 1.00 23.68 ? 93  VAL A N   1 
ATOM   687  C  CA  . VAL A 1 98  ? -9.457  -16.050 -15.404 1.00 22.59 ? 93  VAL A CA  1 
ATOM   688  C  C   . VAL A 1 98  ? -9.489  -17.385 -16.152 1.00 23.30 ? 93  VAL A C   1 
ATOM   689  O  O   . VAL A 1 98  ? -9.978  -17.394 -17.331 1.00 26.14 ? 93  VAL A O   1 
ATOM   690  C  CB  . VAL A 1 98  ? -10.841 -15.386 -15.416 1.00 24.14 ? 93  VAL A CB  1 
ATOM   691  C  CG1 . VAL A 1 98  ? -11.895 -16.279 -14.779 1.00 26.32 ? 93  VAL A CG1 1 
ATOM   692  C  CG2 . VAL A 1 98  ? -10.817 -14.014 -14.771 1.00 25.46 ? 93  VAL A CG2 1 
ATOM   693  N  N   . SER A 1 99  ? -8.960  -18.437 -15.526 1.00 21.48 ? 94  SER A N   1 
ATOM   694  C  CA  . SER A 1 99  ? -9.030  -19.842 -16.006 1.00 23.75 ? 94  SER A CA  1 
ATOM   695  C  C   . SER A 1 99  ? -10.422 -20.381 -15.707 1.00 22.91 ? 94  SER A C   1 
ATOM   696  O  O   . SER A 1 99  ? -10.863 -20.365 -14.568 1.00 25.13 ? 94  SER A O   1 
ATOM   697  C  CB  . SER A 1 99  ? -8.009  -20.720 -15.361 1.00 23.72 ? 94  SER A CB  1 
ATOM   698  O  OG  . SER A 1 99  ? -8.190  -22.087 -15.759 1.00 26.03 ? 94  SER A OG  1 
ATOM   699  N  N   . PRO A 1 100 ? -11.147 -20.903 -16.702 1.00 26.43 ? 95  PRO A N   1 
ATOM   700  C  CA  . PRO A 1 100 ? -12.420 -21.573 -16.425 1.00 26.87 ? 95  PRO A CA  1 
ATOM   701  C  C   . PRO A 1 100 ? -12.269 -22.786 -15.487 1.00 25.85 ? 95  PRO A C   1 
ATOM   702  O  O   . PRO A 1 100 ? -13.277 -23.238 -14.959 1.00 23.08 ? 95  PRO A O   1 
ATOM   703  C  CB  . PRO A 1 100 ? -12.934 -21.976 -17.815 1.00 27.83 ? 95  PRO A CB  1 
ATOM   704  C  CG  . PRO A 1 100 ? -12.151 -21.118 -18.787 1.00 27.01 ? 95  PRO A CG  1 
ATOM   705  C  CD  . PRO A 1 100 ? -10.806 -20.869 -18.133 1.00 26.12 ? 95  PRO A CD  1 
ATOM   706  N  N   . ALA A 1 101 ? -11.044 -23.261 -15.228 1.00 25.79 ? 96  ALA A N   1 
ATOM   707  C  CA  . ALA A 1 101 ? -10.834 -24.355 -14.251 1.00 29.66 ? 96  ALA A CA  1 
ATOM   708  C  C   . ALA A 1 101 ? -11.354 -23.859 -12.895 1.00 30.95 ? 96  ALA A C   1 
ATOM   709  O  O   . ALA A 1 101 ? -11.923 -24.656 -12.131 1.00 27.50 ? 96  ALA A O   1 
ATOM   710  C  CB  . ALA A 1 101 ? -9.377  -24.773 -14.192 1.00 30.01 ? 96  ALA A CB  1 
ATOM   711  N  N   . VAL A 1 102 ? -11.188 -22.561 -12.622 1.00 31.00 ? 97  VAL A N   1 
ATOM   712  C  CA  . VAL A 1 102 ? -11.645 -21.919 -11.358 1.00 33.58 ? 97  VAL A CA  1 
ATOM   713  C  C   . VAL A 1 102 ? -13.185 -21.980 -11.287 1.00 32.62 ? 97  VAL A C   1 
ATOM   714  O  O   . VAL A 1 102 ? -13.706 -22.140 -10.182 1.00 32.62 ? 97  VAL A O   1 
ATOM   715  C  CB  . VAL A 1 102 ? -11.110 -20.482 -11.242 1.00 35.24 ? 97  VAL A CB  1 
ATOM   716  C  CG1 . VAL A 1 102 ? -11.706 -19.755 -10.061 1.00 37.47 ? 97  VAL A CG1 1 
ATOM   717  C  CG2 . VAL A 1 102 ? -9.592  -20.468 -11.152 1.00 38.42 ? 97  VAL A CG2 1 
ATOM   718  N  N   . TYR A 1 103 ? -13.891 -21.893 -12.415 1.00 33.37 ? 98  TYR A N   1 
ATOM   719  C  CA  . TYR A 1 103 ? -15.382 -21.871 -12.433 1.00 33.73 ? 98  TYR A CA  1 
ATOM   720  C  C   . TYR A 1 103 ? -15.937 -23.224 -11.983 1.00 36.40 ? 98  TYR A C   1 
ATOM   721  O  O   . TYR A 1 103 ? -17.042 -23.230 -11.424 1.00 35.82 ? 98  TYR A O   1 
ATOM   722  C  CB  . TYR A 1 103 ? -15.940 -21.604 -13.828 1.00 31.30 ? 98  TYR A CB  1 
ATOM   723  C  CG  . TYR A 1 103 ? -15.654 -20.267 -14.459 1.00 29.35 ? 98  TYR A CG  1 
ATOM   724  C  CD1 . TYR A 1 103 ? -15.226 -19.151 -13.744 1.00 29.38 ? 98  TYR A CD1 1 
ATOM   725  C  CD2 . TYR A 1 103 ? -15.877 -20.113 -15.813 1.00 29.13 ? 98  TYR A CD2 1 
ATOM   726  C  CE1 . TYR A 1 103 ? -15.009 -17.927 -14.374 1.00 28.48 ? 98  TYR A CE1 1 
ATOM   727  C  CE2 . TYR A 1 103 ? -15.659 -18.904 -16.454 1.00 29.98 ? 98  TYR A CE2 1 
ATOM   728  C  CZ  . TYR A 1 103 ? -15.216 -17.811 -15.738 1.00 29.18 ? 98  TYR A CZ  1 
ATOM   729  O  OH  . TYR A 1 103 ? -15.068 -16.644 -16.425 1.00 28.11 ? 98  TYR A OH  1 
ATOM   730  N  N   . ARG A 1 104 ? -15.215 -24.320 -12.268 1.00 36.33 ? 99  ARG A N   1 
ATOM   731  C  CA  . ARG A 1 104 ? -15.686 -25.718 -12.067 1.00 43.36 ? 99  ARG A CA  1 
ATOM   732  C  C   . ARG A 1 104 ? -17.030 -25.921 -12.787 1.00 40.75 ? 99  ARG A C   1 
ATOM   733  O  O   . ARG A 1 104 ? -17.826 -26.732 -12.320 1.00 43.09 ? 99  ARG A O   1 
ATOM   734  C  CB  . ARG A 1 104 ? -15.810 -26.048 -10.571 1.00 45.50 ? 99  ARG A CB  1 
ATOM   735  C  CG  . ARG A 1 104 ? -14.519 -25.876 -9.781  1.00 50.88 ? 99  ARG A CG  1 
ATOM   736  C  CD  . ARG A 1 104 ? -14.504 -26.557 -8.421  1.00 54.63 ? 99  ARG A CD  1 
ATOM   737  N  NE  . ARG A 1 104 ? -15.635 -26.257 -7.542  1.00 56.87 ? 99  ARG A NE  1 
ATOM   738  C  CZ  . ARG A 1 104 ? -15.670 -25.298 -6.612  1.00 63.28 ? 99  ARG A CZ  1 
ATOM   739  N  NH1 . ARG A 1 104 ? -14.644 -24.478 -6.436  1.00 65.05 ? 99  ARG A NH1 1 
ATOM   740  N  NH2 . ARG A 1 104 ? -16.754 -25.146 -5.867  1.00 63.87 ? 99  ARG A NH2 1 
ATOM   741  N  N   . THR A 1 105 ? -17.281 -25.223 -13.893 1.00 40.98 ? 100 THR A N   1 
ATOM   742  C  CA  . THR A 1 105 ? -18.497 -25.427 -14.732 1.00 38.22 ? 100 THR A CA  1 
ATOM   743  C  C   . THR A 1 105 ? -18.067 -25.674 -16.178 1.00 35.28 ? 100 THR A C   1 
ATOM   744  O  O   . THR A 1 105 ? -16.858 -25.549 -16.486 1.00 31.96 ? 100 THR A O   1 
ATOM   745  C  CB  . THR A 1 105 ? -19.475 -24.248 -14.637 1.00 40.05 ? 100 THR A CB  1 
ATOM   746  O  OG1 . THR A 1 105 ? -18.786 -23.097 -15.115 1.00 37.20 ? 100 THR A OG1 1 
ATOM   747  C  CG2 . THR A 1 105 ? -19.982 -23.993 -13.234 1.00 45.74 ? 100 THR A CG2 1 
ATOM   748  N  N   . ALA A 1 106 ? -19.029 -26.064 -17.012 1.00 33.10 ? 101 ALA A N   1 
ATOM   749  C  CA  . ALA A 1 106 ? -18.839 -26.393 -18.437 1.00 34.33 ? 101 ALA A CA  1 
ATOM   750  C  C   . ALA A 1 106 ? -20.189 -26.267 -19.138 1.00 34.90 ? 101 ALA A C   1 
ATOM   751  O  O   . ALA A 1 106 ? -21.224 -26.568 -18.546 1.00 33.38 ? 101 ALA A O   1 
ATOM   752  C  CB  . ALA A 1 106 ? -18.258 -27.782 -18.571 1.00 36.27 ? 101 ALA A CB  1 
ATOM   753  N  N   . PRO A 1 107 ? -20.228 -25.758 -20.384 1.00 31.88 ? 102 PRO A N   1 
ATOM   754  C  CA  . PRO A 1 107 ? -19.033 -25.249 -21.053 1.00 31.12 ? 102 PRO A CA  1 
ATOM   755  C  C   . PRO A 1 107 ? -18.689 -23.826 -20.578 1.00 30.74 ? 102 PRO A C   1 
ATOM   756  O  O   . PRO A 1 107 ? -19.388 -23.263 -19.765 1.00 28.07 ? 102 PRO A O   1 
ATOM   757  C  CB  . PRO A 1 107 ? -19.454 -25.275 -22.524 1.00 31.65 ? 102 PRO A CB  1 
ATOM   758  C  CG  . PRO A 1 107 ? -20.947 -24.931 -22.464 1.00 30.85 ? 102 PRO A CG  1 
ATOM   759  C  CD  . PRO A 1 107 ? -21.447 -25.596 -21.197 1.00 31.94 ? 102 PRO A CD  1 
ATOM   760  N  N   . ALA A 1 108 ? -17.576 -23.283 -21.061 1.00 28.11 ? 103 ALA A N   1 
ATOM   761  C  CA  . ALA A 1 108 ? -17.024 -22.010 -20.566 1.00 27.24 ? 103 ALA A CA  1 
ATOM   762  C  C   . ALA A 1 108 ? -15.974 -21.499 -21.547 1.00 24.50 ? 103 ALA A C   1 
ATOM   763  O  O   . ALA A 1 108 ? -15.553 -22.240 -22.431 1.00 24.37 ? 103 ALA A O   1 
ATOM   764  C  CB  . ALA A 1 108 ? -16.456 -22.206 -19.178 1.00 26.67 ? 103 ALA A CB  1 
ATOM   765  N  N   . ALA A 1 109 ? -15.599 -20.242 -21.398 1.00 26.65 ? 104 ALA A N   1 
ATOM   766  C  CA  . ALA A 1 109 ? -14.460 -19.643 -22.115 1.00 25.29 ? 104 ALA A CA  1 
ATOM   767  C  C   . ALA A 1 109 ? -13.672 -18.823 -21.108 1.00 23.26 ? 104 ALA A C   1 
ATOM   768  O  O   . ALA A 1 109 ? -14.254 -18.319 -20.155 1.00 21.04 ? 104 ALA A O   1 
ATOM   769  C  CB  . ALA A 1 109 ? -14.963 -18.839 -23.280 1.00 25.48 ? 104 ALA A CB  1 
ATOM   770  N  N   . PRO A 1 110 ? -12.328 -18.737 -21.248 1.00 24.21 ? 105 PRO A N   1 
ATOM   771  C  CA  . PRO A 1 110 ? -11.523 -17.908 -20.361 1.00 22.14 ? 105 PRO A CA  1 
ATOM   772  C  C   . PRO A 1 110 ? -11.794 -16.418 -20.594 1.00 22.83 ? 105 PRO A C   1 
ATOM   773  O  O   . PRO A 1 110 ? -12.244 -16.029 -21.646 1.00 24.29 ? 105 PRO A O   1 
ATOM   774  C  CB  . PRO A 1 110 ? -10.061 -18.186 -20.746 1.00 22.50 ? 105 PRO A CB  1 
ATOM   775  C  CG  . PRO A 1 110 ? -10.105 -19.355 -21.725 1.00 23.83 ? 105 PRO A CG  1 
ATOM   776  C  CD  . PRO A 1 110 ? -11.516 -19.397 -22.286 1.00 23.38 ? 105 PRO A CD  1 
ATOM   777  N  N   . THR A 1 111 ? -11.445 -15.582 -19.631 1.00 22.95 ? 106 THR A N   1 
ATOM   778  C  CA  . THR A 1 111 ? -11.411 -14.114 -19.860 1.00 22.38 ? 106 THR A CA  1 
ATOM   779  C  C   . THR A 1 111 ? -10.207 -13.522 -19.130 1.00 21.45 ? 106 THR A C   1 
ATOM   780  O  O   . THR A 1 111 ? -9.308  -14.283 -18.629 1.00 22.29 ? 106 THR A O   1 
ATOM   781  C  CB  . THR A 1 111 ? -12.751 -13.478 -19.477 1.00 19.17 ? 106 THR A CB  1 
ATOM   782  O  OG1 . THR A 1 111 ? -12.780 -12.200 -20.105 1.00 21.03 ? 106 THR A OG1 1 
ATOM   783  C  CG2 . THR A 1 111 ? -12.910 -13.323 -17.984 1.00 21.31 ? 106 THR A CG2 1 
ATOM   784  N  N   . TRP A 1 112 ? -10.154 -12.209 -19.134 1.00 21.50 ? 107 TRP A N   1 
ATOM   785  C  CA  . TRP A 1 112 ? -9.169  -11.450 -18.329 1.00 22.03 ? 107 TRP A CA  1 
ATOM   786  C  C   . TRP A 1 112 ? -9.941  -10.398 -17.536 1.00 23.18 ? 107 TRP A C   1 
ATOM   787  O  O   . TRP A 1 112 ? -10.623 -9.534  -18.141 1.00 23.43 ? 107 TRP A O   1 
ATOM   788  C  CB  . TRP A 1 112 ? -8.095  -10.840 -19.232 1.00 22.48 ? 107 TRP A CB  1 
ATOM   789  C  CG  . TRP A 1 112 ? -6.773  -10.607 -18.568 1.00 18.96 ? 107 TRP A CG  1 
ATOM   790  C  CD1 . TRP A 1 112 ? -6.489  -9.745  -17.576 1.00 20.39 ? 107 TRP A CD1 1 
ATOM   791  C  CD2 . TRP A 1 112 ? -5.562  -11.300 -18.845 1.00 20.26 ? 107 TRP A CD2 1 
ATOM   792  N  NE1 . TRP A 1 112 ? -5.167  -9.832  -17.216 1.00 21.09 ? 107 TRP A NE1 1 
ATOM   793  C  CE2 . TRP A 1 112 ? -4.575  -10.794 -17.968 1.00 21.78 ? 107 TRP A CE2 1 
ATOM   794  C  CE3 . TRP A 1 112 ? -5.217  -12.318 -19.741 1.00 21.58 ? 107 TRP A CE3 1 
ATOM   795  C  CZ2 . TRP A 1 112 ? -3.251  -11.238 -17.980 1.00 21.61 ? 107 TRP A CZ2 1 
ATOM   796  C  CZ3 . TRP A 1 112 ? -3.911  -12.765 -19.745 1.00 22.88 ? 107 TRP A CZ3 1 
ATOM   797  C  CH2 . TRP A 1 112 ? -2.955  -12.251 -18.854 1.00 22.21 ? 107 TRP A CH2 1 
ATOM   798  N  N   . ASN A 1 113 ? -9.927  -10.517 -16.214 1.00 24.20 ? 108 ASN A N   1 
ATOM   799  C  CA  . ASN A 1 113 ? -10.499 -9.459  -15.345 1.00 24.85 ? 108 ASN A CA  1 
ATOM   800  C  C   . ASN A 1 113 ? -9.491  -8.328  -15.318 1.00 25.23 ? 108 ASN A C   1 
ATOM   801  O  O   . ASN A 1 113 ? -8.257  -8.596  -15.256 1.00 25.50 ? 108 ASN A O   1 
ATOM   802  C  CB  . ASN A 1 113 ? -10.853 -10.006 -13.964 1.00 23.20 ? 108 ASN A CB  1 
ATOM   803  C  CG  . ASN A 1 113 ? -12.092 -10.868 -14.004 1.00 26.06 ? 108 ASN A CG  1 
ATOM   804  O  OD1 . ASN A 1 113 ? -12.725 -11.040 -15.072 1.00 21.79 ? 108 ASN A OD1 1 
ATOM   805  N  ND2 . ASN A 1 113 ? -12.410 -11.426 -12.843 1.00 26.07 ? 108 ASN A ND2 1 
ATOM   806  N  N   . PHE A 1 114 ? -9.993  -7.112  -15.351 1.00 24.39 ? 109 PHE A N   1 
ATOM   807  C  CA  . PHE A 1 114 ? -9.150  -5.919  -15.492 1.00 22.87 ? 109 PHE A CA  1 
ATOM   808  C  C   . PHE A 1 114 ? -9.963  -4.694  -15.111 1.00 23.60 ? 109 PHE A C   1 
ATOM   809  O  O   . PHE A 1 114 ? -11.268 -4.709  -15.044 1.00 21.32 ? 109 PHE A O   1 
ATOM   810  C  CB  . PHE A 1 114 ? -8.575  -5.877  -16.905 1.00 24.37 ? 109 PHE A CB  1 
ATOM   811  C  CG  . PHE A 1 114 ? -9.449  -5.306  -17.988 1.00 21.84 ? 109 PHE A CG  1 
ATOM   812  C  CD1 . PHE A 1 114 ? -9.448  -3.944  -18.247 1.00 25.05 ? 109 PHE A CD1 1 
ATOM   813  C  CD2 . PHE A 1 114 ? -10.166 -6.130  -18.837 1.00 24.66 ? 109 PHE A CD2 1 
ATOM   814  C  CE1 . PHE A 1 114 ? -10.226 -3.419  -19.270 1.00 25.07 ? 109 PHE A CE1 1 
ATOM   815  C  CE2 . PHE A 1 114 ? -10.916 -5.605  -19.886 1.00 23.57 ? 109 PHE A CE2 1 
ATOM   816  C  CZ  . PHE A 1 114 ? -10.982 -4.248  -20.071 1.00 23.50 ? 109 PHE A CZ  1 
ATOM   817  N  N   . THR A 1 115 ? -9.206  -3.670  -14.776 1.00 24.15 ? 110 THR A N   1 
ATOM   818  C  CA  . THR A 1 115 ? -9.719  -2.333  -14.388 1.00 25.49 ? 110 THR A CA  1 
ATOM   819  C  C   . THR A 1 115 ? -9.008  -1.306  -15.250 1.00 25.58 ? 110 THR A C   1 
ATOM   820  O  O   . THR A 1 115 ? -7.768  -1.398  -15.360 1.00 27.13 ? 110 THR A O   1 
ATOM   821  C  CB  . THR A 1 115 ? -9.564  -2.118  -12.876 1.00 25.42 ? 110 THR A CB  1 
ATOM   822  O  OG1 . THR A 1 115 ? -8.202  -2.279  -12.481 1.00 23.10 ? 110 THR A OG1 1 
ATOM   823  C  CG2 . THR A 1 115 ? -10.455 -3.073  -12.119 1.00 26.42 ? 110 THR A CG2 1 
ATOM   824  N  N   . SER A 1 116 ? -9.768  -0.409  -15.887 1.00 24.98 ? 111 SER A N   1 
ATOM   825  C  CA  . SER A 1 116 ? -9.194  0.773   -16.572 1.00 22.21 ? 111 SER A CA  1 
ATOM   826  C  C   . SER A 1 116 ? -10.053 1.996   -16.289 1.00 20.20 ? 111 SER A C   1 
ATOM   827  O  O   . SER A 1 116 ? -11.262 1.871   -16.067 1.00 22.24 ? 111 SER A O   1 
ATOM   828  C  CB  . SER A 1 116 ? -8.952  0.546   -18.058 1.00 22.52 ? 111 SER A CB  1 
ATOM   829  O  OG  . SER A 1 116 ? -10.110 0.077   -18.722 1.00 29.24 ? 111 SER A OG  1 
ATOM   830  N  N   . VAL A 1 117 ? -9.433  3.154   -16.236 1.00 19.76 ? 112 VAL A N   1 
ATOM   831  C  CA  . VAL A 1 117 ? -10.183 4.429   -16.386 1.00 19.23 ? 112 VAL A CA  1 
ATOM   832  C  C   . VAL A 1 117 ? -9.626  5.130   -17.627 1.00 19.15 ? 112 VAL A C   1 
ATOM   833  O  O   . VAL A 1 117 ? -8.393  5.238   -17.757 1.00 16.57 ? 112 VAL A O   1 
ATOM   834  C  CB  . VAL A 1 117 ? -10.125 5.304   -15.140 1.00 18.70 ? 112 VAL A CB  1 
ATOM   835  C  CG1 . VAL A 1 117 ? -10.677 6.704   -15.395 1.00 18.18 ? 112 VAL A CG1 1 
ATOM   836  C  CG2 . VAL A 1 117 ? -10.870 4.634   -13.999 1.00 23.10 ? 112 VAL A CG2 1 
ATOM   837  N  N   . GLN A 1 118 ? -10.532 5.566   -18.483 1.00 16.56 ? 113 GLN A N   1 
ATOM   838  C  CA  . GLN A 1 118 ? -10.230 6.431   -19.633 1.00 19.88 ? 113 GLN A CA  1 
ATOM   839  C  C   . GLN A 1 118 ? -10.802 7.802   -19.375 1.00 21.71 ? 113 GLN A C   1 
ATOM   840  O  O   . GLN A 1 118 ? -12.031 7.884   -19.206 1.00 22.30 ? 113 GLN A O   1 
ATOM   841  C  CB  . GLN A 1 118 ? -10.809 5.849   -20.909 1.00 19.36 ? 113 GLN A CB  1 
ATOM   842  C  CG  . GLN A 1 118 ? -10.061 4.600   -21.333 1.00 22.64 ? 113 GLN A CG  1 
ATOM   843  C  CD  . GLN A 1 118 ? -10.490 4.009   -22.651 1.00 21.56 ? 113 GLN A CD  1 
ATOM   844  O  OE1 . GLN A 1 118 ? -11.131 4.661   -23.448 1.00 20.46 ? 113 GLN A OE1 1 
ATOM   845  N  NE2 . GLN A 1 118 ? -10.147 2.744   -22.855 1.00 21.45 ? 113 GLN A NE2 1 
ATOM   846  N  N   . VAL A 1 119 ? -9.947  8.817   -19.326 1.00 21.80 ? 114 VAL A N   1 
ATOM   847  C  CA  . VAL A 1 119 ? -10.394 10.246  -19.286 1.00 23.85 ? 114 VAL A CA  1 
ATOM   848  C  C   . VAL A 1 119 ? -10.084 10.912  -20.619 1.00 24.60 ? 114 VAL A C   1 
ATOM   849  O  O   . VAL A 1 119 ? -8.994  10.679  -21.194 1.00 27.38 ? 114 VAL A O   1 
ATOM   850  C  CB  . VAL A 1 119 ? -9.765  11.053  -18.150 1.00 26.03 ? 114 VAL A CB  1 
ATOM   851  C  CG1 . VAL A 1 119 ? -10.286 10.604  -16.798 1.00 25.95 ? 114 VAL A CG1 1 
ATOM   852  C  CG2 . VAL A 1 119 ? -8.243  11.004  -18.206 1.00 27.51 ? 114 VAL A CG2 1 
ATOM   853  N  N   . ARG A 1 120 ? -10.980 11.794  -21.037 1.00 24.86 ? 115 ARG A N   1 
ATOM   854  C  CA  . ARG A 1 120 ? -10.868 12.552  -22.305 1.00 24.71 ? 115 ARG A CA  1 
ATOM   855  C  C   . ARG A 1 120 ? -11.159 14.026  -22.018 1.00 25.01 ? 115 ARG A C   1 
ATOM   856  O  O   . ARG A 1 120 ? -12.069 14.331  -21.158 1.00 24.34 ? 115 ARG A O   1 
ATOM   857  C  CB  . ARG A 1 120 ? -11.827 11.958  -23.350 1.00 26.65 ? 115 ARG A CB  1 
ATOM   858  C  CG  . ARG A 1 120 ? -11.638 10.469  -23.620 1.00 25.24 ? 115 ARG A CG  1 
ATOM   859  C  CD  . ARG A 1 120 ? -12.622 9.988   -24.695 1.00 25.70 ? 115 ARG A CD  1 
ATOM   860  N  NE  . ARG A 1 120 ? -12.070 8.885   -25.483 1.00 26.08 ? 115 ARG A NE  1 
ATOM   861  C  CZ  . ARG A 1 120 ? -11.844 7.649   -25.024 1.00 27.77 ? 115 ARG A CZ  1 
ATOM   862  N  NH1 . ARG A 1 120 ? -12.088 7.317   -23.758 1.00 23.47 ? 115 ARG A NH1 1 
ATOM   863  N  NH2 . ARG A 1 120 ? -11.346 6.744   -25.852 1.00 26.99 ? 115 ARG A NH2 1 
ATOM   864  N  N   . GLY A 1 121 ? -10.403 14.892  -22.686 1.00 21.28 ? 116 GLY A N   1 
ATOM   865  C  CA  . GLY A 1 121 ? -10.704 16.322  -22.804 1.00 24.33 ? 116 GLY A CA  1 
ATOM   866  C  C   . GLY A 1 121 ? -9.585  17.028  -23.539 1.00 27.60 ? 116 GLY A C   1 
ATOM   867  O  O   . GLY A 1 121 ? -8.773  16.326  -24.222 1.00 27.12 ? 116 GLY A O   1 
ATOM   868  N  N   . GLU A 1 122 ? -9.515  18.351  -23.393 1.00 25.30 ? 117 GLU A N   1 
ATOM   869  C  CA  . GLU A 1 122 ? -8.465  19.177  -24.013 1.00 28.50 ? 117 GLU A CA  1 
ATOM   870  C  C   . GLU A 1 122 ? -7.243  19.151  -23.116 1.00 26.57 ? 117 GLU A C   1 
ATOM   871  O  O   . GLU A 1 122 ? -7.408  19.295  -21.913 1.00 30.07 ? 117 GLU A O   1 
ATOM   872  C  CB  . GLU A 1 122 ? -8.892  20.624  -24.216 1.00 33.44 ? 117 GLU A CB  1 
ATOM   873  C  CG  . GLU A 1 122 ? -9.345  20.896  -25.633 1.00 43.18 ? 117 GLU A CG  1 
ATOM   874  C  CD  . GLU A 1 122 ? -10.413 21.970  -25.756 1.00 49.31 ? 117 GLU A CD  1 
ATOM   875  O  OE1 . GLU A 1 122 ? -11.640 21.636  -25.627 1.00 48.49 ? 117 GLU A OE1 1 
ATOM   876  O  OE2 . GLU A 1 122 ? -10.014 23.134  -25.948 1.00 53.59 ? 117 GLU A OE2 1 
ATOM   877  N  N   . LEU A 1 123 ? -6.082  18.915  -23.709 1.00 27.79 ? 118 LEU A N   1 
ATOM   878  C  CA  . LEU A 1 123 ? -4.783  19.069  -23.039 1.00 26.21 ? 118 LEU A CA  1 
ATOM   879  C  C   . LEU A 1 123 ? -4.299  20.494  -23.290 1.00 28.71 ? 118 LEU A C   1 
ATOM   880  O  O   . LEU A 1 123 ? -4.159  20.843  -24.465 1.00 31.07 ? 118 LEU A O   1 
ATOM   881  C  CB  . LEU A 1 123 ? -3.797  18.042  -23.573 1.00 26.27 ? 118 LEU A CB  1 
ATOM   882  C  CG  . LEU A 1 123 ? -2.449  18.088  -22.849 1.00 28.30 ? 118 LEU A CG  1 
ATOM   883  C  CD1 . LEU A 1 123 ? -1.849  16.700  -22.684 1.00 27.99 ? 118 LEU A CD1 1 
ATOM   884  C  CD2 . LEU A 1 123 ? -1.470  18.974  -23.585 1.00 29.79 ? 118 LEU A CD2 1 
ATOM   885  N  N   . ARG A 1 124 ? -4.039  21.266  -22.228 1.00 29.08 ? 119 ARG A N   1 
ATOM   886  C  CA  . ARG A 1 124 ? -3.334  22.563  -22.351 1.00 29.29 ? 119 ARG A CA  1 
ATOM   887  C  C   . ARG A 1 124 ? -1.896  22.401  -21.858 1.00 26.81 ? 119 ARG A C   1 
ATOM   888  O  O   . ARG A 1 124 ? -1.691  21.929  -20.719 1.00 28.74 ? 119 ARG A O   1 
ATOM   889  C  CB  . ARG A 1 124 ? -3.983  23.707  -21.572 1.00 31.34 ? 119 ARG A CB  1 
ATOM   890  C  CG  . ARG A 1 124 ? -3.143  24.967  -21.711 1.00 35.75 ? 119 ARG A CG  1 
ATOM   891  C  CD  . ARG A 1 124 ? -3.747  26.167  -21.040 1.00 39.42 ? 119 ARG A CD  1 
ATOM   892  N  NE  . ARG A 1 124 ? -3.868  25.965  -19.612 1.00 42.58 ? 119 ARG A NE  1 
ATOM   893  C  CZ  . ARG A 1 124 ? -2.858  25.988  -18.751 1.00 47.27 ? 119 ARG A CZ  1 
ATOM   894  N  NH1 . ARG A 1 124 ? -1.607  26.153  -19.164 1.00 52.11 ? 119 ARG A NH1 1 
ATOM   895  N  NH2 . ARG A 1 124 ? -3.112  25.837  -17.465 1.00 45.78 ? 119 ARG A NH2 1 
ATOM   896  N  N   . LYS A 1 125 ? -0.950  22.849  -22.662 1.00 22.77 ? 120 LYS A N   1 
ATOM   897  C  CA  . LYS A 1 125 ? 0.474   22.873  -22.263 1.00 25.94 ? 120 LYS A CA  1 
ATOM   898  C  C   . LYS A 1 125 ? 0.659   24.009  -21.265 1.00 27.93 ? 120 LYS A C   1 
ATOM   899  O  O   . LYS A 1 125 ? 0.146   25.134  -21.506 1.00 28.55 ? 120 LYS A O   1 
ATOM   900  C  CB  . LYS A 1 125 ? 1.395   23.061  -23.463 1.00 25.03 ? 120 LYS A CB  1 
ATOM   901  C  CG  . LYS A 1 125 ? 1.279   21.953  -24.486 1.00 27.31 ? 120 LYS A CG  1 
ATOM   902  C  CD  . LYS A 1 125 ? 1.861   22.315  -25.826 1.00 28.60 ? 120 LYS A CD  1 
ATOM   903  C  CE  . LYS A 1 125 ? 2.205   21.079  -26.621 1.00 26.32 ? 120 LYS A CE  1 
ATOM   904  N  NZ  . LYS A 1 125 ? 2.931   21.448  -27.858 1.00 25.64 ? 120 LYS A NZ  1 
ATOM   905  N  N   . VAL A 1 126 ? 1.315   23.687  -20.158 1.00 31.19 ? 121 VAL A N   1 
ATOM   906  C  CA  . VAL A 1 126 ? 1.865   24.679  -19.205 1.00 29.77 ? 121 VAL A CA  1 
ATOM   907  C  C   . VAL A 1 126 ? 3.161   25.215  -19.824 1.00 29.30 ? 121 VAL A C   1 
ATOM   908  O  O   . VAL A 1 126 ? 4.012   24.386  -20.301 1.00 25.08 ? 121 VAL A O   1 
ATOM   909  C  CB  . VAL A 1 126 ? 2.093   24.017  -17.837 1.00 32.52 ? 121 VAL A CB  1 
ATOM   910  C  CG1 . VAL A 1 126 ? 2.611   25.007  -16.811 1.00 33.29 ? 121 VAL A CG1 1 
ATOM   911  C  CG2 . VAL A 1 126 ? 0.828   23.349  -17.320 1.00 34.30 ? 121 VAL A CG2 1 
ATOM   912  N  N   . GLU A 1 127 ? 3.325   26.535  -19.838 1.00 28.11 ? 122 GLU A N   1 
ATOM   913  C  CA  . GLU A 1 127 ? 4.611   27.169  -20.244 1.00 29.26 ? 122 GLU A CA  1 
ATOM   914  C  C   . GLU A 1 127 ? 5.297   27.790  -19.029 1.00 26.01 ? 122 GLU A C   1 
ATOM   915  O  O   . GLU A 1 127 ? 6.544   27.837  -19.048 1.00 28.71 ? 122 GLU A O   1 
ATOM   916  C  CB  . GLU A 1 127 ? 4.385   28.208  -21.336 1.00 28.24 ? 122 GLU A CB  1 
ATOM   917  C  CG  . GLU A 1 127 ? 3.809   27.623  -22.603 1.00 29.09 ? 122 GLU A CG  1 
ATOM   918  C  CD  . GLU A 1 127 ? 4.702   26.654  -23.336 1.00 27.75 ? 122 GLU A CD  1 
ATOM   919  O  OE1 . GLU A 1 127 ? 5.809   26.374  -22.853 1.00 32.59 ? 122 GLU A OE1 1 
ATOM   920  O  OE2 . GLU A 1 127 ? 4.283   26.160  -24.367 1.00 29.47 ? 122 GLU A OE2 1 
ATOM   921  N  N   . SER A 1 128 ? 4.506   28.261  -18.067 1.00 27.71 ? 123 SER A N   1 
ATOM   922  C  CA  . SER A 1 128 ? 4.921   28.993  -16.841 1.00 29.33 ? 123 SER A CA  1 
ATOM   923  C  C   . SER A 1 128 ? 5.888   28.161  -16.005 1.00 32.10 ? 123 SER A C   1 
ATOM   924  O  O   . SER A 1 128 ? 5.535   27.046  -15.635 1.00 32.50 ? 123 SER A O   1 
ATOM   925  C  CB  . SER A 1 128 ? 3.723   29.362  -16.011 1.00 33.09 ? 123 SER A CB  1 
ATOM   926  O  OG  . SER A 1 128 ? 4.124   29.630  -14.681 1.00 31.52 ? 123 SER A OG  1 
ATOM   927  N  N   . ALA A 1 129 ? 7.066   28.706  -15.730 1.00 35.09 ? 124 ALA A N   1 
ATOM   928  C  CA  . ALA A 1 129 ? 8.067   28.136  -14.808 1.00 37.95 ? 124 ALA A CA  1 
ATOM   929  C  C   . ALA A 1 129 ? 7.391   27.716  -13.497 1.00 38.49 ? 124 ALA A C   1 
ATOM   930  O  O   . ALA A 1 129 ? 7.471   26.538  -13.161 1.00 35.01 ? 124 ALA A O   1 
ATOM   931  C  CB  . ALA A 1 129 ? 9.122   29.169  -14.546 1.00 36.76 ? 124 ALA A CB  1 
ATOM   932  N  N   . ASP A 1 130 ? 6.740   28.659  -12.811 1.00 35.07 ? 125 ASP A N   1 
ATOM   933  C  CA  . ASP A 1 130 ? 6.031   28.449  -11.516 1.00 39.77 ? 125 ASP A CA  1 
ATOM   934  C  C   . ASP A 1 130 ? 5.040   27.282  -11.603 1.00 36.19 ? 125 ASP A C   1 
ATOM   935  O  O   . ASP A 1 130 ? 5.014   26.477  -10.649 1.00 35.24 ? 125 ASP A O   1 
ATOM   936  C  CB  . ASP A 1 130 ? 5.259   29.688  -11.049 1.00 45.84 ? 125 ASP A CB  1 
ATOM   937  C  CG  . ASP A 1 130 ? 6.094   30.957  -10.991 1.00 52.58 ? 125 ASP A CG  1 
ATOM   938  O  OD1 . ASP A 1 130 ? 5.496   32.035  -10.773 1.00 61.11 ? 125 ASP A OD1 1 
ATOM   939  O  OD2 . ASP A 1 130 ? 7.333   30.864  -11.187 1.00 56.38 ? 125 ASP A OD2 1 
ATOM   940  N  N   . ASP A 1 131 ? 4.203   27.215  -12.650 1.00 35.50 ? 126 ASP A N   1 
ATOM   941  C  CA  . ASP A 1 131 ? 3.172   26.150  -12.763 1.00 33.07 ? 126 ASP A CA  1 
ATOM   942  C  C   . ASP A 1 131 ? 3.884   24.809  -13.068 1.00 29.33 ? 126 ASP A C   1 
ATOM   943  O  O   . ASP A 1 131 ? 3.352   23.745  -12.693 1.00 29.09 ? 126 ASP A O   1 
ATOM   944  C  CB  . ASP A 1 131 ? 2.039   26.564  -13.710 1.00 38.28 ? 126 ASP A CB  1 
ATOM   945  C  CG  . ASP A 1 131 ? 1.048   27.581  -13.120 1.00 46.65 ? 126 ASP A CG  1 
ATOM   946  O  OD1 . ASP A 1 131 ? -0.066  27.799  -13.712 1.00 52.66 ? 126 ASP A OD1 1 
ATOM   947  O  OD2 . ASP A 1 131 ? 1.365   28.151  -12.066 1.00 49.32 ? 126 ASP A OD2 1 
ATOM   948  N  N   . THR A 1 132 ? 5.021   24.825  -13.762 1.00 28.41 ? 127 THR A N   1 
ATOM   949  C  CA  . THR A 1 132 ? 5.797   23.608  -14.114 1.00 28.86 ? 127 THR A CA  1 
ATOM   950  C  C   . THR A 1 132 ? 6.422   23.003  -12.848 1.00 28.39 ? 127 THR A C   1 
ATOM   951  O  O   . THR A 1 132 ? 6.269   21.786  -12.624 1.00 27.16 ? 127 THR A O   1 
ATOM   952  C  CB  . THR A 1 132 ? 6.890   23.916  -15.139 1.00 29.22 ? 127 THR A CB  1 
ATOM   953  O  OG1 . THR A 1 132 ? 6.257   24.477  -16.292 1.00 27.33 ? 127 THR A OG1 1 
ATOM   954  C  CG2 . THR A 1 132 ? 7.708   22.685  -15.500 1.00 28.10 ? 127 THR A CG2 1 
ATOM   955  N  N   . LEU A 1 133 ? 7.126   23.824  -12.065 1.00 28.37 ? 128 LEU A N   1 
ATOM   956  C  CA  . LEU A 1 133 ? 7.649   23.424  -10.744 1.00 26.40 ? 128 LEU A CA  1 
ATOM   957  C  C   . LEU A 1 133 ? 6.499   23.027  -9.804  1.00 26.05 ? 128 LEU A C   1 
ATOM   958  O  O   . LEU A 1 133 ? 6.614   22.005  -9.140  1.00 23.23 ? 128 LEU A O   1 
ATOM   959  C  CB  . LEU A 1 133 ? 8.493   24.564  -10.184 1.00 30.28 ? 128 LEU A CB  1 
ATOM   960  C  CG  . LEU A 1 133 ? 9.305   24.177  -8.950  1.00 31.01 ? 128 LEU A CG  1 
ATOM   961  C  CD1 . LEU A 1 133 ? 10.453  23.221  -9.305  1.00 31.47 ? 128 LEU A CD1 1 
ATOM   962  C  CD2 . LEU A 1 133 ? 9.830   25.411  -8.254  1.00 32.26 ? 128 LEU A CD2 1 
ATOM   963  N  N   . ALA A 1 134 ? 5.367   23.731  -9.795  1.00 27.40 ? 129 ALA A N   1 
ATOM   964  C  CA  . ALA A 1 134 ? 4.180   23.327  -9.004  1.00 26.65 ? 129 ALA A CA  1 
ATOM   965  C  C   . ALA A 1 134 ? 3.739   21.898  -9.367  1.00 24.68 ? 129 ALA A C   1 
ATOM   966  O  O   . ALA A 1 134 ? 3.380   21.130  -8.446  1.00 21.69 ? 129 ALA A O   1 
ATOM   967  C  CB  . ALA A 1 134 ? 3.050   24.313  -9.195  1.00 29.27 ? 129 ALA A CB  1 
ATOM   968  N  N   . THR A 1 135 ? 3.750   21.557  -10.657 1.00 25.07 ? 130 THR A N   1 
ATOM   969  C  CA  . THR A 1 135 ? 3.363   20.221  -11.207 1.00 24.98 ? 130 THR A CA  1 
ATOM   970  C  C   . THR A 1 135 ? 4.306   19.114  -10.696 1.00 23.64 ? 130 THR A C   1 
ATOM   971  O  O   . THR A 1 135 ? 3.820   18.108  -10.137 1.00 22.13 ? 130 THR A O   1 
ATOM   972  C  CB  . THR A 1 135 ? 3.327   20.255  -12.747 1.00 26.82 ? 130 THR A CB  1 
ATOM   973  O  OG1 . THR A 1 135 ? 2.570   21.381  -13.211 1.00 30.48 ? 130 THR A OG1 1 
ATOM   974  C  CG2 . THR A 1 135 ? 2.750   18.991  -13.350 1.00 27.13 ? 130 THR A CG2 1 
ATOM   975  N  N   . VAL A 1 136 ? 5.623   19.238  -10.860 1.00 24.63 ? 131 VAL A N   1 
ATOM   976  C  CA  . VAL A 1 136 ? 6.509   18.124  -10.408 1.00 25.96 ? 131 VAL A CA  1 
ATOM   977  C  C   . VAL A 1 136 ? 6.503   18.009  -8.871  1.00 24.00 ? 131 VAL A C   1 
ATOM   978  O  O   . VAL A 1 136 ? 6.528   16.866  -8.408  1.00 25.10 ? 131 VAL A O   1 
ATOM   979  C  CB  . VAL A 1 136 ? 7.931   18.123  -11.022 1.00 27.97 ? 131 VAL A CB  1 
ATOM   980  C  CG1 . VAL A 1 136 ? 7.856   18.038  -12.531 1.00 28.48 ? 131 VAL A CG1 1 
ATOM   981  C  CG2 . VAL A 1 136 ? 8.817   19.274  -10.567 1.00 29.69 ? 131 VAL A CG2 1 
ATOM   982  N  N   . ARG A 1 137 ? 6.389   19.099  -8.101  1.00 25.27 ? 132 ARG A N   1 
ATOM   983  C  CA  . ARG A 1 137 ? 6.345   19.050  -6.616  1.00 25.08 ? 132 ARG A CA  1 
ATOM   984  C  C   . ARG A 1 137 ? 5.043   18.391  -6.102  1.00 25.40 ? 132 ARG A C   1 
ATOM   985  O  O   . ARG A 1 137 ? 5.130   17.590  -5.119  1.00 25.30 ? 132 ARG A O   1 
ATOM   986  C  CB  . ARG A 1 137 ? 6.486   20.442  -5.990  1.00 27.33 ? 132 ARG A CB  1 
ATOM   987  C  CG  . ARG A 1 137 ? 7.816   21.119  -6.264  1.00 30.62 ? 132 ARG A CG  1 
ATOM   988  C  CD  . ARG A 1 137 ? 8.470   21.744  -5.063  1.00 35.61 ? 132 ARG A CD  1 
ATOM   989  N  NE  . ARG A 1 137 ? 7.682   22.662  -4.261  1.00 42.48 ? 132 ARG A NE  1 
ATOM   990  C  CZ  . ARG A 1 137 ? 7.741   22.753  -2.923  1.00 50.75 ? 132 ARG A CZ  1 
ATOM   991  N  NH1 . ARG A 1 137 ? 8.509   21.943  -2.205  1.00 55.09 ? 132 ARG A NH1 1 
ATOM   992  N  NH2 . ARG A 1 137 ? 6.980   23.627  -2.296  1.00 51.67 ? 132 ARG A NH2 1 
ATOM   993  N  N   . ALA A 1 138 ? 3.870   18.709  -6.652  1.00 22.45 ? 133 ALA A N   1 
ATOM   994  C  CA  . ALA A 1 138 ? 2.608   18.006  -6.277  1.00 22.34 ? 133 ALA A CA  1 
ATOM   995  C  C   . ALA A 1 138 ? 2.671   16.517  -6.691  1.00 22.85 ? 133 ALA A C   1 
ATOM   996  O  O   . ALA A 1 138 ? 2.156   15.683  -5.932  1.00 21.52 ? 133 ALA A O   1 
ATOM   997  C  CB  . ALA A 1 138 ? 1.420   18.707  -6.893  1.00 22.22 ? 133 ALA A CB  1 
ATOM   998  N  N   . THR A 1 139 ? 3.264   16.190  -7.860  1.00 24.13 ? 134 THR A N   1 
ATOM   999  C  CA  . THR A 1 139 ? 3.563   14.794  -8.302  1.00 24.83 ? 134 THR A CA  1 
ATOM   1000 C  C   . THR A 1 139 ? 4.468   14.075  -7.286  1.00 25.09 ? 134 THR A C   1 
ATOM   1001 O  O   . THR A 1 139 ? 4.195   12.911  -6.968  1.00 22.33 ? 134 THR A O   1 
ATOM   1002 C  CB  . THR A 1 139 ? 4.188   14.774  -9.703  1.00 24.20 ? 134 THR A CB  1 
ATOM   1003 O  OG1 . THR A 1 139 ? 3.278   15.500  -10.501 1.00 21.51 ? 134 THR A OG1 1 
ATOM   1004 C  CG2 . THR A 1 139 ? 4.369   13.396  -10.297 1.00 25.47 ? 134 THR A CG2 1 
ATOM   1005 N  N   . VAL A 1 140 ? 5.533   14.725  -6.808  1.00 25.91 ? 135 VAL A N   1 
ATOM   1006 C  CA  . VAL A 1 140 ? 6.356   14.114  -5.730  1.00 25.74 ? 135 VAL A CA  1 
ATOM   1007 C  C   . VAL A 1 140 ? 5.457   13.945  -4.491  1.00 23.51 ? 135 VAL A C   1 
ATOM   1008 O  O   . VAL A 1 140 ? 5.396   12.851  -3.965  1.00 20.42 ? 135 VAL A O   1 
ATOM   1009 C  CB  . VAL A 1 140 ? 7.661   14.888  -5.452  1.00 24.30 ? 135 VAL A CB  1 
ATOM   1010 C  CG1 . VAL A 1 140 ? 8.304   14.357  -4.186  1.00 26.63 ? 135 VAL A CG1 1 
ATOM   1011 C  CG2 . VAL A 1 140 ? 8.651   14.811  -6.615  1.00 21.66 ? 135 VAL A CG2 1 
ATOM   1012 N  N   . ALA A 1 141 ? 4.744   14.988  -4.083  1.00 26.99 ? 136 ALA A N   1 
ATOM   1013 C  CA  . ALA A 1 141 ? 3.919   14.989  -2.857  1.00 29.01 ? 136 ALA A CA  1 
ATOM   1014 C  C   . ALA A 1 141 ? 2.930   13.815  -2.900  1.00 30.13 ? 136 ALA A C   1 
ATOM   1015 O  O   . ALA A 1 141 ? 2.863   13.073  -1.909  1.00 26.66 ? 136 ALA A O   1 
ATOM   1016 C  CB  . ALA A 1 141 ? 3.241   16.336  -2.702  1.00 32.17 ? 136 ALA A CB  1 
ATOM   1017 N  N   . ALA A 1 142 ? 2.193   13.648  -4.009  1.00 29.96 ? 137 ALA A N   1 
ATOM   1018 C  CA  . ALA A 1 142 ? 1.125   12.630  -4.180  1.00 27.11 ? 137 ALA A CA  1 
ATOM   1019 C  C   . ALA A 1 142 ? 1.728   11.228  -4.276  1.00 24.29 ? 137 ALA A C   1 
ATOM   1020 O  O   . ALA A 1 142 ? 1.240   10.329  -3.583  1.00 24.54 ? 137 ALA A O   1 
ATOM   1021 C  CB  . ALA A 1 142 ? 0.283   12.923  -5.397  1.00 28.04 ? 137 ALA A CB  1 
ATOM   1022 N  N   . LEU A 1 143 ? 2.732   11.021  -5.118  1.00 25.83 ? 138 LEU A N   1 
ATOM   1023 C  CA  . LEU A 1 143 ? 3.228   9.640   -5.378  1.00 23.66 ? 138 LEU A CA  1 
ATOM   1024 C  C   . LEU A 1 143 ? 4.122   9.155   -4.228  1.00 23.44 ? 138 LEU A C   1 
ATOM   1025 O  O   . LEU A 1 143 ? 4.028   7.931   -3.900  1.00 21.72 ? 138 LEU A O   1 
ATOM   1026 C  CB  . LEU A 1 143 ? 3.966   9.519   -6.713  1.00 22.18 ? 138 LEU A CB  1 
ATOM   1027 C  CG  . LEU A 1 143 ? 3.277   10.007  -7.976  1.00 21.95 ? 138 LEU A CG  1 
ATOM   1028 C  CD1 . LEU A 1 143 ? 3.826   9.283   -9.173  1.00 20.54 ? 138 LEU A CD1 1 
ATOM   1029 C  CD2 . LEU A 1 143 ? 1.755   9.956   -7.915  1.00 22.75 ? 138 LEU A CD2 1 
ATOM   1030 N  N   . GLU A 1 144 ? 4.975   10.007  -3.641  1.00 24.23 ? 139 GLU A N   1 
ATOM   1031 C  CA  . GLU A 1 144 ? 5.875   9.552   -2.536  1.00 25.62 ? 139 GLU A CA  1 
ATOM   1032 C  C   . GLU A 1 144 ? 4.987   9.159   -1.342  1.00 27.83 ? 139 GLU A C   1 
ATOM   1033 O  O   . GLU A 1 144 ? 5.216   8.098   -0.692  1.00 23.75 ? 139 GLU A O   1 
ATOM   1034 C  CB  . GLU A 1 144 ? 6.910   10.630  -2.213  1.00 27.58 ? 139 GLU A CB  1 
ATOM   1035 C  CG  . GLU A 1 144 ? 7.943   10.202  -1.183  1.00 26.93 ? 139 GLU A CG  1 
ATOM   1036 C  CD  . GLU A 1 144 ? 8.970   9.174   -1.631  1.00 27.12 ? 139 GLU A CD  1 
ATOM   1037 O  OE1 . GLU A 1 144 ? 9.153   9.003   -2.858  1.00 23.25 ? 139 GLU A OE1 1 
ATOM   1038 O  OE2 . GLU A 1 144 ? 9.578   8.526   -0.736  1.00 26.41 ? 139 GLU A OE2 1 
ATOM   1039 N  N   . SER A 1 145 ? 3.915   9.914   -1.117  1.00 27.45 ? 140 SER A N   1 
ATOM   1040 C  CA  . SER A 1 145 ? 2.947   9.610   -0.037  1.00 30.66 ? 140 SER A CA  1 
ATOM   1041 C  C   . SER A 1 145 ? 2.384   8.198   -0.224  1.00 28.68 ? 140 SER A C   1 
ATOM   1042 O  O   . SER A 1 145 ? 2.248   7.445   0.773   1.00 31.74 ? 140 SER A O   1 
ATOM   1043 C  CB  . SER A 1 145 ? 1.824   10.629  0.024   1.00 31.17 ? 140 SER A CB  1 
ATOM   1044 O  OG  . SER A 1 145 ? 0.822   10.166  0.922   1.00 30.69 ? 140 SER A OG  1 
ATOM   1045 N  N   . ARG A 1 146 ? 2.041   7.839   -1.451  1.00 30.12 ? 141 ARG A N   1 
ATOM   1046 C  CA  . ARG A 1 146 ? 1.209   6.643   -1.743  1.00 31.70 ? 141 ARG A CA  1 
ATOM   1047 C  C   . ARG A 1 146 ? 2.097   5.426   -2.018  1.00 28.47 ? 141 ARG A C   1 
ATOM   1048 O  O   . ARG A 1 146 ? 1.653   4.307   -1.692  1.00 32.12 ? 141 ARG A O   1 
ATOM   1049 C  CB  . ARG A 1 146 ? 0.300   6.979   -2.921  1.00 36.34 ? 141 ARG A CB  1 
ATOM   1050 C  CG  . ARG A 1 146 ? -1.066  6.317   -2.871  1.00 42.38 ? 141 ARG A CG  1 
ATOM   1051 C  CD  . ARG A 1 146 ? -1.982  7.021   -3.851  1.00 43.37 ? 141 ARG A CD  1 
ATOM   1052 N  NE  . ARG A 1 146 ? -2.816  8.033   -3.213  1.00 46.51 ? 141 ARG A NE  1 
ATOM   1053 C  CZ  . ARG A 1 146 ? -4.009  7.807   -2.660  1.00 47.16 ? 141 ARG A CZ  1 
ATOM   1054 N  NH1 . ARG A 1 146 ? -4.515  6.586   -2.625  1.00 45.16 ? 141 ARG A NH1 1 
ATOM   1055 N  NH2 . ARG A 1 146 ? -4.678  8.805   -2.115  1.00 54.20 ? 141 ARG A NH2 1 
ATOM   1056 N  N   . PHE A 1 147 ? 3.293   5.632   -2.577  1.00 24.57 ? 142 PHE A N   1 
ATOM   1057 C  CA  . PHE A 1 147 ? 4.170   4.573   -3.171  1.00 25.00 ? 142 PHE A CA  1 
ATOM   1058 C  C   . PHE A 1 147 ? 5.594   4.589   -2.587  1.00 22.76 ? 142 PHE A C   1 
ATOM   1059 O  O   . PHE A 1 147 ? 6.411   3.631   -2.859  1.00 22.02 ? 142 PHE A O   1 
ATOM   1060 C  CB  . PHE A 1 147 ? 4.209   4.747   -4.698  1.00 26.10 ? 142 PHE A CB  1 
ATOM   1061 C  CG  . PHE A 1 147 ? 2.838   4.738   -5.358  1.00 25.80 ? 142 PHE A CG  1 
ATOM   1062 C  CD1 . PHE A 1 147 ? 2.080   3.577   -5.414  1.00 25.55 ? 142 PHE A CD1 1 
ATOM   1063 C  CD2 . PHE A 1 147 ? 2.291   5.900   -5.896  1.00 27.77 ? 142 PHE A CD2 1 
ATOM   1064 C  CE1 . PHE A 1 147 ? 0.807   3.584   -5.972  1.00 26.27 ? 142 PHE A CE1 1 
ATOM   1065 C  CE2 . PHE A 1 147 ? 1.020   5.911   -6.462  1.00 26.32 ? 142 PHE A CE2 1 
ATOM   1066 C  CZ  . PHE A 1 147 ? 0.287   4.744   -6.510  1.00 26.76 ? 142 PHE A CZ  1 
ATOM   1067 N  N   . GLY A 1 148 ? 5.929   5.643   -1.840  1.00 23.92 ? 143 GLY A N   1 
ATOM   1068 C  CA  . GLY A 1 148 ? 7.318   5.933   -1.435  1.00 23.88 ? 143 GLY A CA  1 
ATOM   1069 C  C   . GLY A 1 148 ? 7.627   5.511   0.002   1.00 25.75 ? 143 GLY A C   1 
ATOM   1070 O  O   . GLY A 1 148 ? 7.070   4.494   0.527   1.00 23.58 ? 143 GLY A O   1 
ATOM   1071 N  N   . ALA A 1 149 ? 8.593   6.208   0.587   1.00 25.47 ? 144 ALA A N   1 
ATOM   1072 C  CA  . ALA A 1 149 ? 9.280   5.809   1.825   1.00 26.98 ? 144 ALA A CA  1 
ATOM   1073 C  C   . ALA A 1 149 ? 9.626   7.076   2.609   1.00 28.20 ? 144 ALA A C   1 
ATOM   1074 O  O   . ALA A 1 149 ? 10.715  7.141   3.153   1.00 32.94 ? 144 ALA A O   1 
ATOM   1075 C  CB  . ALA A 1 149 ? 10.502  4.997   1.425   1.00 29.55 ? 144 ALA A CB  1 
ATOM   1076 N  N   . GLY A 1 150 ? 8.763   8.091   2.556   1.00 26.32 ? 145 GLY A N   1 
ATOM   1077 C  CA  . GLY A 1 150 ? 8.881   9.304   3.381   1.00 26.48 ? 145 GLY A CA  1 
ATOM   1078 C  C   . GLY A 1 150 ? 9.984   10.233  2.915   1.00 27.51 ? 145 GLY A C   1 
ATOM   1079 O  O   . GLY A 1 150 ? 10.420  11.042  3.740   1.00 26.11 ? 145 GLY A O   1 
ATOM   1080 N  N   . TRP A 1 151 ? 10.429  10.126  1.658   1.00 25.29 ? 146 TRP A N   1 
ATOM   1081 C  CA  . TRP A 1 151 ? 11.497  10.979  1.085   1.00 26.45 ? 146 TRP A CA  1 
ATOM   1082 C  C   . TRP A 1 151 ? 11.100  12.467  1.124   1.00 27.51 ? 146 TRP A C   1 
ATOM   1083 O  O   . TRP A 1 151 ? 9.963   12.818  0.752   1.00 23.54 ? 146 TRP A O   1 
ATOM   1084 C  CB  . TRP A 1 151 ? 11.854  10.560  -0.337  1.00 26.61 ? 146 TRP A CB  1 
ATOM   1085 C  CG  . TRP A 1 151 ? 12.953  11.401  -0.901  1.00 27.34 ? 146 TRP A CG  1 
ATOM   1086 C  CD1 . TRP A 1 151 ? 14.252  11.434  -0.491  1.00 28.64 ? 146 TRP A CD1 1 
ATOM   1087 C  CD2 . TRP A 1 151 ? 12.832  12.390  -1.940  1.00 26.49 ? 146 TRP A CD2 1 
ATOM   1088 N  NE1 . TRP A 1 151 ? 14.949  12.361  -1.213  1.00 27.11 ? 146 TRP A NE1 1 
ATOM   1089 C  CE2 . TRP A 1 151 ? 14.116  12.958  -2.114  1.00 26.76 ? 146 TRP A CE2 1 
ATOM   1090 C  CE3 . TRP A 1 151 ? 11.771  12.841  -2.736  1.00 23.14 ? 146 TRP A CE3 1 
ATOM   1091 C  CZ2 . TRP A 1 151 ? 14.379  13.928  -3.080  1.00 25.41 ? 146 TRP A CZ2 1 
ATOM   1092 C  CZ3 . TRP A 1 151 ? 12.037  13.784  -3.705  1.00 26.02 ? 146 TRP A CZ3 1 
ATOM   1093 C  CH2 . TRP A 1 151 ? 13.322  14.316  -3.868  1.00 27.04 ? 146 TRP A CH2 1 
ATOM   1094 N  N   . ASP A 1 152 ? 12.033  13.305  1.559   1.00 25.25 ? 147 ASP A N   1 
ATOM   1095 C  CA  . ASP A 1 152 ? 11.839  14.774  1.710   1.00 28.16 ? 147 ASP A CA  1 
ATOM   1096 C  C   . ASP A 1 152 ? 12.437  15.448  0.476   1.00 25.49 ? 147 ASP A C   1 
ATOM   1097 O  O   . ASP A 1 152 ? 13.672  15.381  0.323   1.00 24.43 ? 147 ASP A O   1 
ATOM   1098 C  CB  . ASP A 1 152 ? 12.462  15.251  3.032   1.00 29.75 ? 147 ASP A CB  1 
ATOM   1099 C  CG  . ASP A 1 152 ? 12.177  16.703  3.407   1.00 34.56 ? 147 ASP A CG  1 
ATOM   1100 O  OD1 . ASP A 1 152 ? 11.485  17.419  2.631   1.00 31.40 ? 147 ASP A OD1 1 
ATOM   1101 O  OD2 . ASP A 1 152 ? 12.687  17.129  4.476   1.00 39.30 ? 147 ASP A OD2 1 
ATOM   1102 N  N   . MET A 1 153 ? 11.604  16.077  -0.369  1.00 26.79 ? 148 MET A N   1 
ATOM   1103 C  CA  . MET A 1 153 ? 12.049  16.770  -1.616  1.00 28.54 ? 148 MET A CA  1 
ATOM   1104 C  C   . MET A 1 153 ? 12.779  18.097  -1.326  1.00 30.14 ? 148 MET A C   1 
ATOM   1105 O  O   . MET A 1 153 ? 13.389  18.637  -2.312  1.00 30.68 ? 148 MET A O   1 
ATOM   1106 C  CB  . MET A 1 153 ? 10.872  17.055  -2.556  1.00 29.55 ? 148 MET A CB  1 
ATOM   1107 C  CG  . MET A 1 153 ? 10.094  18.291  -2.260  1.00 28.71 ? 148 MET A CG  1 
ATOM   1108 S  SD  . MET A 1 153 ? 8.595   18.389  -3.303  1.00 31.80 ? 148 MET A SD  1 
ATOM   1109 C  CE  . MET A 1 153 ? 7.339   17.746  -2.200  1.00 31.16 ? 148 MET A CE  1 
ATOM   1110 N  N   . THR A 1 154 ? 12.752  18.588  -0.069  1.00 31.53 ? 149 THR A N   1 
ATOM   1111 C  CA  . THR A 1 154 ? 13.237  19.946  0.328   1.00 33.49 ? 149 THR A CA  1 
ATOM   1112 C  C   . THR A 1 154 ? 14.673  20.100  -0.157  1.00 31.76 ? 149 THR A C   1 
ATOM   1113 O  O   . THR A 1 154 ? 14.896  21.003  -0.971  1.00 36.42 ? 149 THR A O   1 
ATOM   1114 C  CB  . THR A 1 154 ? 13.107  20.246  1.827   1.00 32.70 ? 149 THR A CB  1 
ATOM   1115 O  OG1 . THR A 1 154 ? 11.720  20.202  2.153   1.00 32.47 ? 149 THR A OG1 1 
ATOM   1116 C  CG2 . THR A 1 154 ? 13.646  21.607  2.222   1.00 32.63 ? 149 THR A CG2 1 
ATOM   1117 N  N   . GLY A 1 155 ? 15.565  19.189  0.233   1.00 32.40 ? 150 GLY A N   1 
ATOM   1118 C  CA  . GLY A 1 155 ? 17.005  19.251  -0.097  1.00 33.12 ? 150 GLY A CA  1 
ATOM   1119 C  C   . GLY A 1 155 ? 17.285  19.234  -1.600  1.00 34.25 ? 150 GLY A C   1 
ATOM   1120 O  O   . GLY A 1 155 ? 18.467  19.375  -1.994  1.00 38.28 ? 150 GLY A O   1 
ATOM   1121 N  N   . SER A 1 156 ? 16.270  18.978  -2.424  1.00 30.69 ? 151 SER A N   1 
ATOM   1122 C  CA  . SER A 1 156 ? 16.445  18.728  -3.876  1.00 31.08 ? 151 SER A CA  1 
ATOM   1123 C  C   . SER A 1 156 ? 15.735  19.797  -4.720  1.00 29.24 ? 151 SER A C   1 
ATOM   1124 O  O   . SER A 1 156 ? 15.829  19.694  -5.956  1.00 31.96 ? 151 SER A O   1 
ATOM   1125 C  CB  . SER A 1 156 ? 15.986  17.317  -4.236  1.00 32.90 ? 151 SER A CB  1 
ATOM   1126 O  OG  . SER A 1 156 ? 16.813  16.341  -3.621  1.00 36.44 ? 151 SER A OG  1 
ATOM   1127 N  N   . LEU A 1 157 ? 15.046  20.776  -4.114  1.00 31.12 ? 152 LEU A N   1 
ATOM   1128 C  CA  . LEU A 1 157 ? 14.275  21.815  -4.867  1.00 33.66 ? 152 LEU A CA  1 
ATOM   1129 C  C   . LEU A 1 157 ? 15.175  22.579  -5.859  1.00 33.98 ? 152 LEU A C   1 
ATOM   1130 O  O   . LEU A 1 157 ? 14.764  22.769  -7.014  1.00 35.95 ? 152 LEU A O   1 
ATOM   1131 C  CB  . LEU A 1 157 ? 13.612  22.737  -3.854  1.00 32.56 ? 152 LEU A CB  1 
ATOM   1132 C  CG  . LEU A 1 157 ? 12.528  22.048  -3.039  1.00 35.00 ? 152 LEU A CG  1 
ATOM   1133 C  CD1 . LEU A 1 157 ? 11.775  23.033  -2.155  1.00 36.06 ? 152 LEU A CD1 1 
ATOM   1134 C  CD2 . LEU A 1 157 ? 11.571  21.323  -3.965  1.00 36.43 ? 152 LEU A CD2 1 
ATOM   1135 N  N   . ASP A 1 158 ? 16.385  22.968  -5.459  1.00 32.93 ? 153 ASP A N   1 
ATOM   1136 C  CA  . ASP A 1 158 ? 17.376  23.601  -6.366  1.00 33.50 ? 153 ASP A CA  1 
ATOM   1137 C  C   . ASP A 1 158 ? 17.597  22.689  -7.579  1.00 31.19 ? 153 ASP A C   1 
ATOM   1138 O  O   . ASP A 1 158 ? 17.578  23.214  -8.735  1.00 27.19 ? 153 ASP A O   1 
ATOM   1139 C  CB  . ASP A 1 158 ? 18.686  23.901  -5.631  1.00 39.85 ? 153 ASP A CB  1 
ATOM   1140 C  CG  . ASP A 1 158 ? 18.737  25.266  -4.964  1.00 42.94 ? 153 ASP A CG  1 
ATOM   1141 O  OD1 . ASP A 1 158 ? 17.684  25.929  -4.898  1.00 43.47 ? 153 ASP A OD1 1 
ATOM   1142 O  OD2 . ASP A 1 158 ? 19.845  25.664  -4.545  1.00 47.94 ? 153 ASP A OD2 1 
ATOM   1143 N  N   . TYR A 1 159 ? 17.770  21.376  -7.346  1.00 28.58 ? 154 TYR A N   1 
ATOM   1144 C  CA  . TYR A 1 159 ? 18.006  20.377  -8.417  1.00 27.42 ? 154 TYR A CA  1 
ATOM   1145 C  C   . TYR A 1 159 ? 16.780  20.323  -9.337  1.00 26.58 ? 154 TYR A C   1 
ATOM   1146 O  O   . TYR A 1 159 ? 16.951  20.329  -10.572 1.00 26.15 ? 154 TYR A O   1 
ATOM   1147 C  CB  . TYR A 1 159 ? 18.330  18.999  -7.835  1.00 28.53 ? 154 TYR A CB  1 
ATOM   1148 C  CG  . TYR A 1 159 ? 18.403  17.913  -8.872  1.00 27.10 ? 154 TYR A CG  1 
ATOM   1149 C  CD1 . TYR A 1 159 ? 19.389  17.908  -9.860  1.00 28.09 ? 154 TYR A CD1 1 
ATOM   1150 C  CD2 . TYR A 1 159 ? 17.474  16.885  -8.870  1.00 27.03 ? 154 TYR A CD2 1 
ATOM   1151 C  CE1 . TYR A 1 159 ? 19.444  16.901  -10.813 1.00 30.93 ? 154 TYR A CE1 1 
ATOM   1152 C  CE2 . TYR A 1 159 ? 17.516  15.881  -9.819  1.00 26.46 ? 154 TYR A CE2 1 
ATOM   1153 C  CZ  . TYR A 1 159 ? 18.489  15.891  -10.797 1.00 28.60 ? 154 TYR A CZ  1 
ATOM   1154 O  OH  . TYR A 1 159 ? 18.461  14.885  -11.717 1.00 32.66 ? 154 TYR A OH  1 
ATOM   1155 N  N   . PHE A 1 160 ? 15.576  20.297  -8.768  1.00 25.91 ? 155 PHE A N   1 
ATOM   1156 C  CA  . PHE A 1 160 ? 14.317  20.344  -9.556  1.00 25.74 ? 155 PHE A CA  1 
ATOM   1157 C  C   . PHE A 1 160 ? 14.431  21.546  -10.514 1.00 28.36 ? 155 PHE A C   1 
ATOM   1158 O  O   . PHE A 1 160 ? 14.151  21.426  -11.712 1.00 29.27 ? 155 PHE A O   1 
ATOM   1159 C  CB  . PHE A 1 160 ? 13.050  20.418  -8.683  1.00 22.75 ? 155 PHE A CB  1 
ATOM   1160 C  CG  . PHE A 1 160 ? 12.629  19.210  -7.859  1.00 22.33 ? 155 PHE A CG  1 
ATOM   1161 C  CD1 . PHE A 1 160 ? 13.413  18.067  -7.765  1.00 23.20 ? 155 PHE A CD1 1 
ATOM   1162 C  CD2 . PHE A 1 160 ? 11.469  19.266  -7.092  1.00 19.75 ? 155 PHE A CD2 1 
ATOM   1163 C  CE1 . PHE A 1 160 ? 13.031  17.001  -6.967  1.00 21.91 ? 155 PHE A CE1 1 
ATOM   1164 C  CE2 . PHE A 1 160 ? 11.098  18.219  -6.278  1.00 20.38 ? 155 PHE A CE2 1 
ATOM   1165 C  CZ  . PHE A 1 160 ? 11.866  17.074  -6.229  1.00 21.86 ? 155 PHE A CZ  1 
ATOM   1166 N  N   . ARG A 1 161 ? 14.865  22.694  -10.000 1.00 29.92 ? 156 ARG A N   1 
ATOM   1167 C  CA  . ARG A 1 161 ? 14.848  23.966  -10.772 1.00 32.25 ? 156 ARG A CA  1 
ATOM   1168 C  C   . ARG A 1 161 ? 15.851  23.884  -11.923 1.00 29.55 ? 156 ARG A C   1 
ATOM   1169 O  O   . ARG A 1 161 ? 15.562  24.406  -12.993 1.00 29.89 ? 156 ARG A O   1 
ATOM   1170 C  CB  . ARG A 1 161 ? 15.149  25.136  -9.835  1.00 35.78 ? 156 ARG A CB  1 
ATOM   1171 C  CG  . ARG A 1 161 ? 13.975  25.526  -8.952  1.00 38.53 ? 156 ARG A CG  1 
ATOM   1172 C  CD  . ARG A 1 161 ? 14.408  26.718  -8.134  1.00 44.58 ? 156 ARG A CD  1 
ATOM   1173 N  NE  . ARG A 1 161 ? 13.291  27.322  -7.451  1.00 48.42 ? 156 ARG A NE  1 
ATOM   1174 C  CZ  . ARG A 1 161 ? 12.941  27.076  -6.192  1.00 58.32 ? 156 ARG A CZ  1 
ATOM   1175 N  NH1 . ARG A 1 161 ? 13.630  26.225  -5.443  1.00 56.41 ? 156 ARG A NH1 1 
ATOM   1176 N  NH2 . ARG A 1 161 ? 11.889  27.703  -5.688  1.00 58.85 ? 156 ARG A NH2 1 
ATOM   1177 N  N   . ARG A 1 162 ? 16.991  23.245  -11.683 1.00 29.31 ? 157 ARG A N   1 
ATOM   1178 C  CA  . ARG A 1 162 ? 18.095  23.097  -12.651 1.00 31.52 ? 157 ARG A CA  1 
ATOM   1179 C  C   . ARG A 1 162 ? 17.626  22.249  -13.845 1.00 28.96 ? 157 ARG A C   1 
ATOM   1180 O  O   . ARG A 1 162 ? 18.046  22.534  -14.968 1.00 30.59 ? 157 ARG A O   1 
ATOM   1181 C  CB  . ARG A 1 162 ? 19.286  22.470  -11.920 1.00 35.16 ? 157 ARG A CB  1 
ATOM   1182 C  CG  . ARG A 1 162 ? 20.656  22.936  -12.377 1.00 40.49 ? 157 ARG A CG  1 
ATOM   1183 C  CD  . ARG A 1 162 ? 21.615  23.071  -11.188 1.00 47.27 ? 157 ARG A CD  1 
ATOM   1184 N  NE  . ARG A 1 162 ? 21.877  21.824  -10.453 1.00 47.79 ? 157 ARG A NE  1 
ATOM   1185 C  CZ  . ARG A 1 162 ? 21.636  21.598  -9.157  1.00 50.66 ? 157 ARG A CZ  1 
ATOM   1186 N  NH1 . ARG A 1 162 ? 21.102  22.528  -8.376  1.00 55.43 ? 157 ARG A NH1 1 
ATOM   1187 N  NH2 . ARG A 1 162 ? 21.923  20.415  -8.642  1.00 49.75 ? 157 ARG A NH2 1 
ATOM   1188 N  N   . ILE A 1 163 ? 16.804  21.224  -13.635 1.00 28.36 ? 158 ILE A N   1 
ATOM   1189 C  CA  . ILE A 1 163 ? 16.413  20.287  -14.738 1.00 27.27 ? 158 ILE A CA  1 
ATOM   1190 C  C   . ILE A 1 163 ? 15.035  20.672  -15.311 1.00 26.50 ? 158 ILE A C   1 
ATOM   1191 O  O   . ILE A 1 163 ? 14.656  20.124  -16.344 1.00 25.85 ? 158 ILE A O   1 
ATOM   1192 C  CB  . ILE A 1 163 ? 16.455  18.822  -14.273 1.00 24.77 ? 158 ILE A CB  1 
ATOM   1193 C  CG1 . ILE A 1 163 ? 15.439  18.525  -13.179 1.00 26.45 ? 158 ILE A CG1 1 
ATOM   1194 C  CG2 . ILE A 1 163 ? 17.860  18.432  -13.862 1.00 26.96 ? 158 ILE A CG2 1 
ATOM   1195 C  CD1 . ILE A 1 163 ? 15.089  17.051  -13.072 1.00 27.62 ? 158 ILE A CD1 1 
ATOM   1196 N  N   . LEU A 1 164 ? 14.357  21.630  -14.695 1.00 27.61 ? 159 LEU A N   1 
ATOM   1197 C  CA  . LEU A 1 164 ? 12.975  22.080  -15.040 1.00 27.69 ? 159 LEU A CA  1 
ATOM   1198 C  C   . LEU A 1 164 ? 12.780  22.447  -16.523 1.00 28.45 ? 159 LEU A C   1 
ATOM   1199 O  O   . LEU A 1 164 ? 11.685  22.278  -17.073 1.00 28.69 ? 159 LEU A O   1 
ATOM   1200 C  CB  . LEU A 1 164 ? 12.708  23.301  -14.171 1.00 28.69 ? 159 LEU A CB  1 
ATOM   1201 C  CG  . LEU A 1 164 ? 11.245  23.660  -13.957 1.00 27.41 ? 159 LEU A CG  1 
ATOM   1202 C  CD1 . LEU A 1 164 ? 10.496  22.494  -13.318 1.00 29.15 ? 159 LEU A CD1 1 
ATOM   1203 C  CD2 . LEU A 1 164 ? 11.207  24.892  -13.088 1.00 29.18 ? 159 LEU A CD2 1 
ATOM   1204 N  N   . PRO A 1 165 ? 13.769  23.022  -17.241 1.00 29.61 ? 160 PRO A N   1 
ATOM   1205 C  CA  . PRO A 1 165 ? 13.542  23.407  -18.640 1.00 27.28 ? 160 PRO A CA  1 
ATOM   1206 C  C   . PRO A 1 165 ? 13.064  22.262  -19.555 1.00 29.84 ? 160 PRO A C   1 
ATOM   1207 O  O   . PRO A 1 165 ? 12.332  22.532  -20.531 1.00 26.03 ? 160 PRO A O   1 
ATOM   1208 C  CB  . PRO A 1 165 ? 14.927  23.942  -19.029 1.00 27.77 ? 160 PRO A CB  1 
ATOM   1209 C  CG  . PRO A 1 165 ? 15.406  24.566  -17.741 1.00 28.48 ? 160 PRO A CG  1 
ATOM   1210 C  CD  . PRO A 1 165 ? 15.085  23.473  -16.741 1.00 29.51 ? 160 PRO A CD  1 
ATOM   1211 N  N   . GLY A 1 166 ? 13.440  21.012  -19.240 1.00 27.32 ? 161 GLY A N   1 
ATOM   1212 C  CA  . GLY A 1 166 ? 13.039  19.840  -20.047 1.00 27.87 ? 161 GLY A CA  1 
ATOM   1213 C  C   . GLY A 1 166 ? 11.634  19.352  -19.710 1.00 24.92 ? 161 GLY A C   1 
ATOM   1214 O  O   . GLY A 1 166 ? 11.140  18.456  -20.352 1.00 28.68 ? 161 GLY A O   1 
ATOM   1215 N  N   . VAL A 1 167 ? 11.005  19.904  -18.704 1.00 25.17 ? 162 VAL A N   1 
ATOM   1216 C  CA  . VAL A 1 167 ? 9.646   19.464  -18.295 1.00 26.31 ? 162 VAL A CA  1 
ATOM   1217 C  C   . VAL A 1 167 ? 8.625   20.075  -19.256 1.00 28.02 ? 162 VAL A C   1 
ATOM   1218 O  O   . VAL A 1 167 ? 8.622   21.319  -19.407 1.00 28.00 ? 162 VAL A O   1 
ATOM   1219 C  CB  . VAL A 1 167 ? 9.357   19.850  -16.836 1.00 27.09 ? 162 VAL A CB  1 
ATOM   1220 C  CG1 . VAL A 1 167 ? 7.966   19.400  -16.408 1.00 29.17 ? 162 VAL A CG1 1 
ATOM   1221 C  CG2 . VAL A 1 167 ? 10.443  19.326  -15.888 1.00 27.43 ? 162 VAL A CG2 1 
ATOM   1222 N  N   . GLY A 1 168 ? 7.813   19.215  -19.871 1.00 26.72 ? 163 GLY A N   1 
ATOM   1223 C  CA  . GLY A 1 168 ? 6.566   19.580  -20.550 1.00 23.59 ? 163 GLY A CA  1 
ATOM   1224 C  C   . GLY A 1 168 ? 5.369   19.256  -19.678 1.00 24.05 ? 163 GLY A C   1 
ATOM   1225 O  O   . GLY A 1 168 ? 4.836   18.121  -19.732 1.00 22.78 ? 163 GLY A O   1 
ATOM   1226 N  N   . ALA A 1 169 ? 4.917   20.228  -18.909 1.00 20.78 ? 164 ALA A N   1 
ATOM   1227 C  CA  . ALA A 1 169 ? 3.885   19.991  -17.893 1.00 20.19 ? 164 ALA A CA  1 
ATOM   1228 C  C   . ALA A 1 169 ? 2.559   20.352  -18.537 1.00 19.82 ? 164 ALA A C   1 
ATOM   1229 O  O   . ALA A 1 169 ? 2.582   21.187  -19.409 1.00 21.37 ? 164 ALA A O   1 
ATOM   1230 C  CB  . ALA A 1 169 ? 4.165   20.789  -16.653 1.00 21.83 ? 164 ALA A CB  1 
ATOM   1231 N  N   . PHE A 1 170 ? 1.466   19.694  -18.153 1.00 22.83 ? 165 PHE A N   1 
ATOM   1232 C  CA  . PHE A 1 170 ? 0.141   19.887  -18.789 1.00 22.98 ? 165 PHE A CA  1 
ATOM   1233 C  C   . PHE A 1 170 ? -1.003  19.764  -17.785 1.00 23.91 ? 165 PHE A C   1 
ATOM   1234 O  O   . PHE A 1 170 ? -0.818  19.286  -16.635 1.00 21.15 ? 165 PHE A O   1 
ATOM   1235 C  CB  . PHE A 1 170 ? -0.033  18.944  -19.975 1.00 26.00 ? 165 PHE A CB  1 
ATOM   1236 C  CG  . PHE A 1 170 ? 0.020   17.475  -19.645 1.00 31.40 ? 165 PHE A CG  1 
ATOM   1237 C  CD1 . PHE A 1 170 ? -1.137  16.780  -19.346 1.00 29.93 ? 165 PHE A CD1 1 
ATOM   1238 C  CD2 . PHE A 1 170 ? 1.221   16.772  -19.706 1.00 29.36 ? 165 PHE A CD2 1 
ATOM   1239 C  CE1 . PHE A 1 170 ? -1.091  15.419  -19.071 1.00 31.81 ? 165 PHE A CE1 1 
ATOM   1240 C  CE2 . PHE A 1 170 ? 1.267   15.415  -19.420 1.00 31.37 ? 165 PHE A CE2 1 
ATOM   1241 C  CZ  . PHE A 1 170 ? 0.108   14.738  -19.104 1.00 30.74 ? 165 PHE A CZ  1 
ATOM   1242 N  N   . ARG A 1 171 ? -2.149  20.262  -18.260 1.00 24.89 ? 166 ARG A N   1 
ATOM   1243 C  CA  . ARG A 1 171 ? -3.463  20.315  -17.594 1.00 27.00 ? 166 ARG A CA  1 
ATOM   1244 C  C   . ARG A 1 171 ? -4.487  19.624  -18.502 1.00 28.87 ? 166 ARG A C   1 
ATOM   1245 O  O   . ARG A 1 171 ? -4.618  19.989  -19.701 1.00 33.23 ? 166 ARG A O   1 
ATOM   1246 C  CB  . ARG A 1 171 ? -3.872  21.771  -17.335 1.00 28.77 ? 166 ARG A CB  1 
ATOM   1247 C  CG  . ARG A 1 171 ? -2.936  22.539  -16.407 1.00 31.02 ? 166 ARG A CG  1 
ATOM   1248 C  CD  . ARG A 1 171 ? -2.880  21.982  -14.989 1.00 30.82 ? 166 ARG A CD  1 
ATOM   1249 N  NE  . ARG A 1 171 ? -1.944  22.703  -14.148 1.00 34.00 ? 166 ARG A NE  1 
ATOM   1250 C  CZ  . ARG A 1 171 ? -0.683  22.344  -13.860 1.00 31.01 ? 166 ARG A CZ  1 
ATOM   1251 N  NH1 . ARG A 1 171 ? -0.137  21.227  -14.324 1.00 27.22 ? 166 ARG A NH1 1 
ATOM   1252 N  NH2 . ARG A 1 171 ? 0.034   23.147  -13.108 1.00 29.87 ? 166 ARG A NH2 1 
ATOM   1253 N  N   . LEU A 1 172 ? -5.201  18.642  -17.966 1.00 28.43 ? 167 LEU A N   1 
ATOM   1254 C  CA  . LEU A 1 172 ? -6.275  17.957  -18.714 1.00 28.07 ? 167 LEU A CA  1 
ATOM   1255 C  C   . LEU A 1 172 ? -7.607  18.194  -17.990 1.00 28.13 ? 167 LEU A C   1 
ATOM   1256 O  O   . LEU A 1 172 ? -7.877  17.576  -16.971 1.00 23.67 ? 167 LEU A O   1 
ATOM   1257 C  CB  . LEU A 1 172 ? -5.910  16.476  -18.809 1.00 29.78 ? 167 LEU A CB  1 
ATOM   1258 C  CG  . LEU A 1 172 ? -6.766  15.633  -19.749 1.00 30.63 ? 167 LEU A CG  1 
ATOM   1259 C  CD1 . LEU A 1 172 ? -6.728  16.199  -21.154 1.00 35.32 ? 167 LEU A CD1 1 
ATOM   1260 C  CD2 . LEU A 1 172 ? -6.278  14.200  -19.753 1.00 29.52 ? 167 LEU A CD2 1 
ATOM   1261 N  N   . ARG A 1 173 ? -8.407  19.088  -18.532 1.00 32.41 ? 168 ARG A N   1 
ATOM   1262 C  CA  . ARG A 1 173 ? -9.819  19.303  -18.139 1.00 32.15 ? 168 ARG A CA  1 
ATOM   1263 C  C   . ARG A 1 173 ? -10.598 18.062  -18.583 1.00 27.30 ? 168 ARG A C   1 
ATOM   1264 O  O   . ARG A 1 173 ? -10.758 17.848  -19.773 1.00 28.29 ? 168 ARG A O   1 
ATOM   1265 C  CB  . ARG A 1 173 ? -10.300 20.657  -18.694 1.00 40.73 ? 168 ARG A CB  1 
ATOM   1266 C  CG  . ARG A 1 173 ? -10.003 20.896  -20.168 1.00 50.44 ? 168 ARG A CG  1 
ATOM   1267 C  CD  . ARG A 1 173 ? -9.775  22.344  -20.596 1.00 56.52 ? 168 ARG A CD  1 
ATOM   1268 N  NE  . ARG A 1 173 ? -10.821 23.238  -20.112 1.00 65.46 ? 168 ARG A NE  1 
ATOM   1269 C  CZ  . ARG A 1 173 ? -11.222 24.370  -20.699 1.00 74.28 ? 168 ARG A CZ  1 
ATOM   1270 N  NH1 . ARG A 1 173 ? -12.183 25.089  -20.140 1.00 79.47 ? 168 ARG A NH1 1 
ATOM   1271 N  NH2 . ARG A 1 173 ? -10.684 24.783  -21.837 1.00 72.13 ? 168 ARG A NH2 1 
ATOM   1272 N  N   . VAL A 1 174 ? -10.995 17.215  -17.633 1.00 27.87 ? 169 VAL A N   1 
ATOM   1273 C  CA  . VAL A 1 174 ? -11.774 15.974  -17.914 1.00 29.67 ? 169 VAL A CA  1 
ATOM   1274 C  C   . VAL A 1 174 ? -13.195 16.362  -18.348 1.00 27.03 ? 169 VAL A C   1 
ATOM   1275 O  O   . VAL A 1 174 ? -13.940 16.890  -17.509 1.00 22.91 ? 169 VAL A O   1 
ATOM   1276 C  CB  . VAL A 1 174 ? -11.781 15.011  -16.715 1.00 27.48 ? 169 VAL A CB  1 
ATOM   1277 C  CG1 . VAL A 1 174 ? -12.510 13.735  -17.074 1.00 28.23 ? 169 VAL A CG1 1 
ATOM   1278 C  CG2 . VAL A 1 174 ? -10.361 14.715  -16.241 1.00 25.92 ? 169 VAL A CG2 1 
ATOM   1279 N  N   . ALA A 1 175 ? -13.514 16.136  -19.626 1.00 27.09 ? 170 ALA A N   1 
ATOM   1280 C  CA  . ALA A 1 175 ? -14.867 16.321  -20.207 1.00 30.39 ? 170 ALA A CA  1 
ATOM   1281 C  C   . ALA A 1 175 ? -15.679 15.026  -20.043 1.00 31.28 ? 170 ALA A C   1 
ATOM   1282 O  O   . ALA A 1 175 ? -16.901 15.113  -19.825 1.00 28.77 ? 170 ALA A O   1 
ATOM   1283 C  CB  . ALA A 1 175 ? -14.753 16.715  -21.659 1.00 27.97 ? 170 ALA A CB  1 
ATOM   1284 N  N   . GLU A 1 176 ? -15.020 13.878  -20.224 1.00 30.71 ? 171 GLU A N   1 
ATOM   1285 C  CA  . GLU A 1 176 ? -15.617 12.519  -20.172 1.00 32.77 ? 171 GLU A CA  1 
ATOM   1286 C  C   . GLU A 1 176 ? -14.715 11.619  -19.318 1.00 30.87 ? 171 GLU A C   1 
ATOM   1287 O  O   . GLU A 1 176 ? -13.463 11.710  -19.428 1.00 27.86 ? 171 GLU A O   1 
ATOM   1288 C  CB  . GLU A 1 176 ? -15.751 11.924  -21.583 1.00 39.94 ? 171 GLU A CB  1 
ATOM   1289 C  CG  . GLU A 1 176 ? -16.806 12.590  -22.458 1.00 46.23 ? 171 GLU A CG  1 
ATOM   1290 C  CD  . GLU A 1 176 ? -16.804 12.144  -23.908 1.00 48.22 ? 171 GLU A CD  1 
ATOM   1291 O  OE1 . GLU A 1 176 ? -16.492 12.973  -24.783 1.00 56.64 ? 171 GLU A OE1 1 
ATOM   1292 O  OE2 . GLU A 1 176 ? -17.130 10.975  -24.163 1.00 54.60 ? 171 GLU A OE2 1 
ATOM   1293 N  N   . ALA A 1 177 ? -15.313 10.748  -18.513 1.00 28.45 ? 172 ALA A N   1 
ATOM   1294 C  CA  . ALA A 1 177 ? -14.577 9.728   -17.738 1.00 30.16 ? 172 ALA A CA  1 
ATOM   1295 C  C   . ALA A 1 177 ? -15.382 8.430   -17.774 1.00 27.97 ? 172 ALA A C   1 
ATOM   1296 O  O   . ALA A 1 177 ? -16.577 8.440   -17.442 1.00 30.89 ? 172 ALA A O   1 
ATOM   1297 C  CB  . ALA A 1 177 ? -14.310 10.213  -16.334 1.00 28.63 ? 172 ALA A CB  1 
ATOM   1298 N  N   . ASP A 1 178 ? -14.769 7.364   -18.252 1.00 29.28 ? 173 ASP A N   1 
ATOM   1299 C  CA  . ASP A 1 178 ? -15.393 6.015   -18.264 1.00 29.94 ? 173 ASP A CA  1 
ATOM   1300 C  C   . ASP A 1 178 ? -14.480 5.052   -17.511 1.00 26.49 ? 173 ASP A C   1 
ATOM   1301 O  O   . ASP A 1 178 ? -13.257 5.232   -17.567 1.00 23.01 ? 173 ASP A O   1 
ATOM   1302 C  CB  . ASP A 1 178 ? -15.678 5.592   -19.702 1.00 34.90 ? 173 ASP A CB  1 
ATOM   1303 C  CG  . ASP A 1 178 ? -16.832 6.358   -20.329 1.00 40.85 ? 173 ASP A CG  1 
ATOM   1304 O  OD1 . ASP A 1 178 ? -17.999 6.085   -19.924 1.00 46.78 ? 173 ASP A OD1 1 
ATOM   1305 O  OD2 . ASP A 1 178 ? -16.556 7.234   -21.207 1.00 42.20 ? 173 ASP A OD2 1 
ATOM   1306 N  N   . GLY A 1 179 ? -15.077 4.079   -16.830 1.00 26.31 ? 174 GLY A N   1 
ATOM   1307 C  CA  . GLY A 1 179 ? -14.362 3.046   -16.060 1.00 25.66 ? 174 GLY A CA  1 
ATOM   1308 C  C   . GLY A 1 179 ? -14.877 1.657   -16.350 1.00 24.13 ? 174 GLY A C   1 
ATOM   1309 O  O   . GLY A 1 179 ? -16.075 1.431   -16.218 1.00 23.76 ? 174 GLY A O   1 
ATOM   1310 N  N   . MET A 1 180 ? -13.981 0.796   -16.819 1.00 27.60 ? 175 MET A N   1 
ATOM   1311 C  CA  . MET A 1 180 ? -14.144 -0.667  -16.970 1.00 24.85 ? 175 MET A CA  1 
ATOM   1312 C  C   . MET A 1 180 ? -13.751 -1.341  -15.649 1.00 24.58 ? 175 MET A C   1 
ATOM   1313 O  O   . MET A 1 180 ? -12.510 -1.300  -15.279 1.00 22.65 ? 175 MET A O   1 
ATOM   1314 C  CB  . MET A 1 180 ? -13.224 -1.160  -18.090 1.00 26.80 ? 175 MET A CB  1 
ATOM   1315 C  CG  . MET A 1 180 ? -13.315 -2.649  -18.358 1.00 28.68 ? 175 MET A CG  1 
ATOM   1316 S  SD  . MET A 1 180 ? -14.832 -3.176  -19.203 1.00 32.23 ? 175 MET A SD  1 
ATOM   1317 C  CE  . MET A 1 180 ? -14.442 -2.657  -20.874 1.00 28.53 ? 175 MET A CE  1 
ATOM   1318 N  N   . PHE A 1 181 ? -14.718 -1.938  -14.955 1.00 20.25 ? 176 PHE A N   1 
ATOM   1319 C  CA  . PHE A 1 181 ? -14.452 -2.813  -13.785 1.00 24.10 ? 176 PHE A CA  1 
ATOM   1320 C  C   . PHE A 1 181 ? -14.933 -4.216  -14.147 1.00 27.05 ? 176 PHE A C   1 
ATOM   1321 O  O   . PHE A 1 181 ? -16.019 -4.648  -13.761 1.00 22.70 ? 176 PHE A O   1 
ATOM   1322 C  CB  . PHE A 1 181 ? -15.037 -2.213  -12.506 1.00 23.49 ? 176 PHE A CB  1 
ATOM   1323 C  CG  . PHE A 1 181 ? -14.349 -0.934  -12.143 1.00 24.45 ? 176 PHE A CG  1 
ATOM   1324 C  CD1 . PHE A 1 181 ? -14.625 0.231   -12.829 1.00 27.09 ? 176 PHE A CD1 1 
ATOM   1325 C  CD2 . PHE A 1 181 ? -13.322 -0.926  -11.215 1.00 26.90 ? 176 PHE A CD2 1 
ATOM   1326 C  CE1 . PHE A 1 181 ? -13.932 1.400   -12.542 1.00 26.01 ? 176 PHE A CE1 1 
ATOM   1327 C  CE2 . PHE A 1 181 ? -12.639 0.249   -10.922 1.00 29.14 ? 176 PHE A CE2 1 
ATOM   1328 C  CZ  . PHE A 1 181 ? -12.954 1.413   -11.589 1.00 26.09 ? 176 PHE A CZ  1 
ATOM   1329 N  N   . LYS A 1 182 ? -14.144 -4.878  -14.977 1.00 27.57 ? 177 LYS A N   1 
ATOM   1330 C  CA  . LYS A 1 182 ? -14.495 -6.202  -15.510 1.00 27.60 ? 177 LYS A CA  1 
ATOM   1331 C  C   . LYS A 1 182 ? -14.069 -7.200  -14.436 1.00 26.07 ? 177 LYS A C   1 
ATOM   1332 O  O   . LYS A 1 182 ? -12.852 -7.516  -14.306 1.00 24.94 ? 177 LYS A O   1 
ATOM   1333 C  CB  . LYS A 1 182 ? -13.839 -6.414  -16.870 1.00 30.76 ? 177 LYS A CB  1 
ATOM   1334 C  CG  . LYS A 1 182 ? -14.189 -7.743  -17.515 1.00 32.89 ? 177 LYS A CG  1 
ATOM   1335 C  CD  . LYS A 1 182 ? -13.640 -7.899  -18.909 1.00 35.97 ? 177 LYS A CD  1 
ATOM   1336 C  CE  . LYS A 1 182 ? -13.587 -9.342  -19.343 1.00 38.08 ? 177 LYS A CE  1 
ATOM   1337 N  NZ  . LYS A 1 182 ? -14.879 -10.025 -19.086 1.00 40.74 ? 177 LYS A NZ  1 
ATOM   1338 N  N   . LEU A 1 183 ? -15.010 -7.588  -13.602 1.00 23.08 ? 178 LEU A N   1 
ATOM   1339 C  CA  . LEU A 1 183 ? -14.686 -8.318  -12.356 1.00 26.17 ? 178 LEU A CA  1 
ATOM   1340 C  C   . LEU A 1 183 ? -15.635 -9.514  -12.182 1.00 26.46 ? 178 LEU A C   1 
ATOM   1341 O  O   . LEU A 1 183 ? -16.079 -9.741  -11.062 1.00 26.97 ? 178 LEU A O   1 
ATOM   1342 C  CB  . LEU A 1 183 ? -14.770 -7.308  -11.202 1.00 26.19 ? 178 LEU A CB  1 
ATOM   1343 C  CG  . LEU A 1 183 ? -13.689 -6.223  -11.179 1.00 26.42 ? 178 LEU A CG  1 
ATOM   1344 C  CD1 . LEU A 1 183 ? -14.022 -5.134  -10.161 1.00 28.36 ? 178 LEU A CD1 1 
ATOM   1345 C  CD2 . LEU A 1 183 ? -12.332 -6.841  -10.858 1.00 26.15 ? 178 LEU A CD2 1 
ATOM   1346 N  N   . SER A 1 184 ? -15.920 -10.256 -13.249 1.00 27.44 ? 179 SER A N   1 
ATOM   1347 C  CA  . SER A 1 184 ? -16.762 -11.491 -13.232 1.00 27.97 ? 179 SER A CA  1 
ATOM   1348 C  C   . SER A 1 184 ? -18.237 -11.213 -12.856 1.00 28.66 ? 179 SER A C   1 
ATOM   1349 O  O   . SER A 1 184 ? -18.956 -12.195 -12.550 1.00 27.36 ? 179 SER A O   1 
ATOM   1350 C  CB  . SER A 1 184 ? -16.182 -12.511 -12.330 1.00 25.70 ? 179 SER A CB  1 
ATOM   1351 O  OG  . SER A 1 184 ? -14.865 -12.820 -12.719 1.00 22.57 ? 179 SER A OG  1 
ATOM   1352 N  N   . GLN A 1 185 ? -18.708 -9.966  -12.926 1.00 28.11 ? 180 GLN A N   1 
ATOM   1353 C  CA  . GLN A 1 185 ? -20.126 -9.614  -12.612 1.00 30.63 ? 180 GLN A CA  1 
ATOM   1354 C  C   . GLN A 1 185 ? -21.079 -10.349 -13.577 1.00 32.94 ? 180 GLN A C   1 
ATOM   1355 O  O   . GLN A 1 185 ? -22.245 -10.490 -13.206 1.00 38.63 ? 180 GLN A O   1 
ATOM   1356 C  CB  . GLN A 1 185 ? -20.372 -8.100  -12.670 1.00 28.90 ? 180 GLN A CB  1 
ATOM   1357 C  CG  . GLN A 1 185 ? -19.557 -7.282  -11.666 1.00 28.92 ? 180 GLN A CG  1 
ATOM   1358 C  CD  . GLN A 1 185 ? -18.328 -6.686  -12.312 1.00 27.66 ? 180 GLN A CD  1 
ATOM   1359 O  OE1 . GLN A 1 185 ? -17.587 -7.368  -13.002 1.00 25.01 ? 180 GLN A OE1 1 
ATOM   1360 N  NE2 . GLN A 1 185 ? -18.118 -5.393  -12.131 1.00 27.10 ? 180 GLN A NE2 1 
ATOM   1361 N  N   . GLU A 1 186 ? -20.617 -10.785 -14.764 1.00 35.70 ? 181 GLU A N   1 
ATOM   1362 C  CA  . GLU A 1 186 ? -21.433 -11.527 -15.770 1.00 36.84 ? 181 GLU A CA  1 
ATOM   1363 C  C   . GLU A 1 186 ? -21.680 -12.978 -15.322 1.00 40.55 ? 181 GLU A C   1 
ATOM   1364 O  O   . GLU A 1 186 ? -22.570 -13.613 -15.923 1.00 41.85 ? 181 GLU A O   1 
ATOM   1365 C  CB  . GLU A 1 186 ? -20.799 -11.510 -17.171 1.00 37.47 ? 181 GLU A CB  1 
ATOM   1366 C  CG  . GLU A 1 186 ? -19.668 -12.519 -17.417 1.00 39.36 ? 181 GLU A CG  1 
ATOM   1367 C  CD  . GLU A 1 186 ? -18.344 -12.248 -16.706 1.00 42.16 ? 181 GLU A CD  1 
ATOM   1368 O  OE1 . GLU A 1 186 ? -18.267 -11.214 -15.982 1.00 35.57 ? 181 GLU A OE1 1 
ATOM   1369 O  OE2 . GLU A 1 186 ? -17.390 -13.063 -16.881 1.00 33.42 ? 181 GLU A OE2 1 
ATOM   1370 N  N   . GLN A 1 187 ? -20.907 -13.502 -14.358 1.00 39.14 ? 182 GLN A N   1 
ATOM   1371 C  CA  . GLN A 1 187 ? -21.012 -14.906 -13.874 1.00 38.09 ? 182 GLN A CA  1 
ATOM   1372 C  C   . GLN A 1 187 ? -22.077 -14.978 -12.774 1.00 36.70 ? 182 GLN A C   1 
ATOM   1373 O  O   . GLN A 1 187 ? -22.344 -13.943 -12.151 1.00 36.79 ? 182 GLN A O   1 
ATOM   1374 C  CB  . GLN A 1 187 ? -19.653 -15.402 -13.373 1.00 38.08 ? 182 GLN A CB  1 
ATOM   1375 C  CG  . GLN A 1 187 ? -18.568 -15.400 -14.433 1.00 38.98 ? 182 GLN A CG  1 
ATOM   1376 C  CD  . GLN A 1 187 ? -18.944 -16.279 -15.600 1.00 42.24 ? 182 GLN A CD  1 
ATOM   1377 O  OE1 . GLN A 1 187 ? -19.716 -17.226 -15.474 1.00 42.28 ? 182 GLN A OE1 1 
ATOM   1378 N  NE2 . GLN A 1 187 ? -18.418 -15.949 -16.762 1.00 45.13 ? 182 GLN A NE2 1 
ATOM   1379 N  N   . GLN A 1 188 ? -22.657 -16.158 -12.553 1.00 38.87 ? 183 GLN A N   1 
ATOM   1380 C  CA  . GLN A 1 188 ? -23.600 -16.443 -11.433 1.00 41.66 ? 183 GLN A CA  1 
ATOM   1381 C  C   . GLN A 1 188 ? -22.882 -16.225 -10.099 1.00 40.18 ? 183 GLN A C   1 
ATOM   1382 O  O   . GLN A 1 188 ? -21.660 -16.311 -10.044 1.00 37.72 ? 183 GLN A O   1 
ATOM   1383 C  CB  . GLN A 1 188 ? -24.117 -17.877 -11.542 1.00 42.65 ? 183 GLN A CB  1 
ATOM   1384 C  CG  . GLN A 1 188 ? -24.931 -18.128 -12.803 1.00 45.81 ? 183 GLN A CG  1 
ATOM   1385 C  CD  . GLN A 1 188 ? -26.315 -17.530 -12.716 1.00 47.63 ? 183 GLN A CD  1 
ATOM   1386 O  OE1 . GLN A 1 188 ? -26.845 -17.268 -11.637 1.00 49.25 ? 183 GLN A OE1 1 
ATOM   1387 N  NE2 . GLN A 1 188 ? -26.928 -17.334 -13.870 1.00 60.29 ? 183 GLN A NE2 1 
ATOM   1388 N  N   . PRO A 1 189 ? -23.599 -15.945 -8.985  1.00 44.92 ? 184 PRO A N   1 
ATOM   1389 C  CA  . PRO A 1 189 ? -22.952 -15.635 -7.701  1.00 43.35 ? 184 PRO A CA  1 
ATOM   1390 C  C   . PRO A 1 189 ? -21.899 -16.626 -7.181  1.00 42.39 ? 184 PRO A C   1 
ATOM   1391 O  O   . PRO A 1 189 ? -20.860 -16.159 -6.770  1.00 42.14 ? 184 PRO A O   1 
ATOM   1392 C  CB  . PRO A 1 189 ? -24.127 -15.544 -6.714  1.00 46.19 ? 184 PRO A CB  1 
ATOM   1393 C  CG  . PRO A 1 189 ? -25.285 -15.099 -7.589  1.00 47.42 ? 184 PRO A CG  1 
ATOM   1394 C  CD  . PRO A 1 189 ? -25.066 -15.816 -8.912  1.00 46.87 ? 184 PRO A CD  1 
ATOM   1395 N  N   . ALA A 1 190 ? -22.162 -17.937 -7.205  1.00 39.61 ? 185 ALA A N   1 
ATOM   1396 C  CA  . ALA A 1 190 ? -21.241 -18.965 -6.661  1.00 40.01 ? 185 ALA A CA  1 
ATOM   1397 C  C   . ALA A 1 190 ? -19.952 -19.030 -7.498  1.00 40.27 ? 185 ALA A C   1 
ATOM   1398 O  O   . ALA A 1 190 ? -18.896 -19.372 -6.919  1.00 40.15 ? 185 ALA A O   1 
ATOM   1399 C  CB  . ALA A 1 190 ? -21.912 -20.311 -6.591  1.00 41.71 ? 185 ALA A CB  1 
ATOM   1400 N  N   . ILE A 1 191 ? -20.036 -18.737 -8.802  1.00 39.41 ? 186 ILE A N   1 
ATOM   1401 C  CA  . ILE A 1 191 ? -18.870 -18.689 -9.728  1.00 38.83 ? 186 ILE A CA  1 
ATOM   1402 C  C   . ILE A 1 191 ? -18.030 -17.440 -9.422  1.00 36.26 ? 186 ILE A C   1 
ATOM   1403 O  O   . ILE A 1 191 ? -16.807 -17.575 -9.328  1.00 35.68 ? 186 ILE A O   1 
ATOM   1404 C  CB  . ILE A 1 191 ? -19.293 -18.712 -11.207 1.00 39.32 ? 186 ILE A CB  1 
ATOM   1405 C  CG1 . ILE A 1 191 ? -20.265 -19.846 -11.564 1.00 43.60 ? 186 ILE A CG1 1 
ATOM   1406 C  CG2 . ILE A 1 191 ? -18.048 -18.744 -12.078 1.00 38.75 ? 186 ILE A CG2 1 
ATOM   1407 C  CD1 . ILE A 1 191 ? -20.190 -21.083 -10.685 1.00 43.45 ? 186 ILE A CD1 1 
ATOM   1408 N  N   . ARG A 1 192 ? -18.649 -16.268 -9.290  1.00 35.43 ? 187 ARG A N   1 
ATOM   1409 C  CA  . ARG A 1 192 ? -17.949 -15.022 -8.851  1.00 40.08 ? 187 ARG A CA  1 
ATOM   1410 C  C   . ARG A 1 192 ? -17.206 -15.308 -7.539  1.00 36.28 ? 187 ARG A C   1 
ATOM   1411 O  O   . ARG A 1 192 ? -16.047 -14.870 -7.395  1.00 31.36 ? 187 ARG A O   1 
ATOM   1412 C  CB  . ARG A 1 192 ? -18.917 -13.847 -8.666  1.00 44.23 ? 187 ARG A CB  1 
ATOM   1413 C  CG  . ARG A 1 192 ? -19.642 -13.435 -9.941  1.00 49.77 ? 187 ARG A CG  1 
ATOM   1414 C  CD  . ARG A 1 192 ? -20.273 -12.061 -9.864  1.00 53.62 ? 187 ARG A CD  1 
ATOM   1415 N  NE  . ARG A 1 192 ? -21.070 -11.938 -8.654  1.00 62.57 ? 187 ARG A NE  1 
ATOM   1416 C  CZ  . ARG A 1 192 ? -22.391 -12.119 -8.570  1.00 69.50 ? 187 ARG A CZ  1 
ATOM   1417 N  NH1 . ARG A 1 192 ? -22.996 -11.991 -7.397  1.00 70.82 ? 187 ARG A NH1 1 
ATOM   1418 N  NH2 . ARG A 1 192 ? -23.105 -12.436 -9.639  1.00 68.64 ? 187 ARG A NH2 1 
ATOM   1419 N  N   . ARG A 1 193 ? -17.850 -16.047 -6.640  1.00 34.86 ? 188 ARG A N   1 
ATOM   1420 C  CA  . ARG A 1 193 ? -17.298 -16.450 -5.319  1.00 37.28 ? 188 ARG A CA  1 
ATOM   1421 C  C   . ARG A 1 193 ? -16.089 -17.379 -5.506  1.00 36.52 ? 188 ARG A C   1 
ATOM   1422 O  O   . ARG A 1 193 ? -15.083 -17.179 -4.787  1.00 31.43 ? 188 ARG A O   1 
ATOM   1423 C  CB  . ARG A 1 193 ? -18.402 -17.097 -4.480  1.00 41.92 ? 188 ARG A CB  1 
ATOM   1424 C  CG  . ARG A 1 193 ? -17.963 -17.528 -3.090  1.00 48.88 ? 188 ARG A CG  1 
ATOM   1425 C  CD  . ARG A 1 193 ? -19.148 -17.599 -2.136  1.00 58.24 ? 188 ARG A CD  1 
ATOM   1426 N  NE  . ARG A 1 193 ? -18.755 -17.909 -0.765  1.00 64.91 ? 188 ARG A NE  1 
ATOM   1427 C  CZ  . ARG A 1 193 ? -18.547 -19.131 -0.278  1.00 69.47 ? 188 ARG A CZ  1 
ATOM   1428 N  NH1 . ARG A 1 193 ? -18.679 -20.198 -1.055  1.00 74.01 ? 188 ARG A NH1 1 
ATOM   1429 N  NH2 . ARG A 1 193 ? -18.205 -19.279 0.992   1.00 66.89 ? 188 ARG A NH2 1 
ATOM   1430 N  N   . ARG A 1 194 ? -16.165 -18.354 -6.421  1.00 31.68 ? 189 ARG A N   1 
ATOM   1431 C  CA  . ARG A 1 194 ? -15.028 -19.277 -6.677  1.00 32.19 ? 189 ARG A CA  1 
ATOM   1432 C  C   . ARG A 1 194 ? -13.848 -18.482 -7.240  1.00 29.31 ? 189 ARG A C   1 
ATOM   1433 O  O   . ARG A 1 194 ? -12.708 -18.760 -6.837  1.00 29.46 ? 189 ARG A O   1 
ATOM   1434 C  CB  . ARG A 1 194 ? -15.429 -20.406 -7.628  1.00 34.57 ? 189 ARG A CB  1 
ATOM   1435 C  CG  . ARG A 1 194 ? -16.362 -21.433 -7.009  1.00 36.15 ? 189 ARG A CG  1 
ATOM   1436 C  CD  . ARG A 1 194 ? -16.892 -22.476 -7.984  1.00 38.78 ? 189 ARG A CD  1 
ATOM   1437 N  NE  . ARG A 1 194 ? -18.079 -23.086 -7.393  1.00 39.93 ? 189 ARG A NE  1 
ATOM   1438 C  CZ  . ARG A 1 194 ? -19.065 -23.672 -8.061  1.00 47.31 ? 189 ARG A CZ  1 
ATOM   1439 N  NH1 . ARG A 1 194 ? -19.014 -23.783 -9.378  1.00 51.77 ? 189 ARG A NH1 1 
ATOM   1440 N  NH2 . ARG A 1 194 ? -20.103 -24.165 -7.404  1.00 47.04 ? 189 ARG A NH2 1 
ATOM   1441 N  N   . VAL A 1 195 ? -14.109 -17.570 -8.183  1.00 30.12 ? 190 VAL A N   1 
ATOM   1442 C  CA  . VAL A 1 195 ? -13.071 -16.698 -8.802  1.00 29.67 ? 190 VAL A CA  1 
ATOM   1443 C  C   . VAL A 1 195 ? -12.409 -15.878 -7.687  1.00 29.93 ? 190 VAL A C   1 
ATOM   1444 O  O   . VAL A 1 195 ? -11.153 -15.886 -7.602  1.00 30.07 ? 190 VAL A O   1 
ATOM   1445 C  CB  . VAL A 1 195 ? -13.643 -15.797 -9.917  1.00 31.31 ? 190 VAL A CB  1 
ATOM   1446 C  CG1 . VAL A 1 195 ? -12.596 -14.793 -10.378 1.00 31.36 ? 190 VAL A CG1 1 
ATOM   1447 C  CG2 . VAL A 1 195 ? -14.176 -16.584 -11.120 1.00 32.83 ? 190 VAL A CG2 1 
ATOM   1448 N  N   . ARG A 1 196 ? -13.203 -15.184 -6.866  1.00 31.20 ? 191 ARG A N   1 
ATOM   1449 C  CA  . ARG A 1 196 ? -12.675 -14.309 -5.780  1.00 35.62 ? 191 ARG A CA  1 
ATOM   1450 C  C   . ARG A 1 196 ? -11.769 -15.128 -4.854  1.00 35.36 ? 191 ARG A C   1 
ATOM   1451 O  O   . ARG A 1 196 ? -10.699 -14.618 -4.454  1.00 32.72 ? 191 ARG A O   1 
ATOM   1452 C  CB  . ARG A 1 196 ? -13.801 -13.657 -4.975  1.00 38.71 ? 191 ARG A CB  1 
ATOM   1453 C  CG  . ARG A 1 196 ? -13.308 -12.752 -3.852  1.00 46.12 ? 191 ARG A CG  1 
ATOM   1454 C  CD  . ARG A 1 196 ? -14.317 -12.620 -2.732  1.00 57.53 ? 191 ARG A CD  1 
ATOM   1455 N  NE  . ARG A 1 196 ? -15.671 -12.471 -3.256  1.00 65.01 ? 191 ARG A NE  1 
ATOM   1456 C  CZ  . ARG A 1 196 ? -16.779 -12.887 -2.648  1.00 69.83 ? 191 ARG A CZ  1 
ATOM   1457 N  NH1 . ARG A 1 196 ? -16.718 -13.471 -1.461  1.00 70.96 ? 191 ARG A NH1 1 
ATOM   1458 N  NH2 . ARG A 1 196 ? -17.949 -12.722 -3.244  1.00 72.19 ? 191 ARG A NH2 1 
ATOM   1459 N  N   . HIS A 1 197 ? -12.192 -16.350 -4.521  1.00 37.84 ? 192 HIS A N   1 
ATOM   1460 C  CA  . HIS A 1 197 ? -11.458 -17.279 -3.625  1.00 35.88 ? 192 HIS A CA  1 
ATOM   1461 C  C   . HIS A 1 197 ? -10.101 -17.649 -4.252  1.00 36.42 ? 192 HIS A C   1 
ATOM   1462 O  O   . HIS A 1 197 ? -9.075  -17.532 -3.533  1.00 30.66 ? 192 HIS A O   1 
ATOM   1463 C  CB  . HIS A 1 197 ? -12.321 -18.496 -3.295  1.00 39.26 ? 192 HIS A CB  1 
ATOM   1464 C  CG  . HIS A 1 197 ? -11.554 -19.538 -2.558  1.00 45.19 ? 192 HIS A CG  1 
ATOM   1465 N  ND1 . HIS A 1 197 ? -11.171 -19.372 -1.242  1.00 50.43 ? 192 HIS A ND1 1 
ATOM   1466 C  CD2 . HIS A 1 197 ? -11.025 -20.714 -2.962  1.00 50.01 ? 192 HIS A CD2 1 
ATOM   1467 C  CE1 . HIS A 1 197 ? -10.458 -20.413 -0.858  1.00 50.02 ? 192 HIS A CE1 1 
ATOM   1468 N  NE2 . HIS A 1 197 ? -10.355 -21.251 -1.895  1.00 50.97 ? 192 HIS A NE2 1 
ATOM   1469 N  N   . SER A 1 198 ? -10.079 -18.064 -5.530  1.00 35.21 ? 193 SER A N   1 
ATOM   1470 C  CA  . SER A 1 198 ? -8.848  -18.483 -6.258  1.00 33.77 ? 193 SER A CA  1 
ATOM   1471 C  C   . SER A 1 198 ? -7.840  -17.322 -6.323  1.00 32.26 ? 193 SER A C   1 
ATOM   1472 O  O   . SER A 1 198 ? -6.623  -17.586 -6.187  1.00 36.23 ? 193 SER A O   1 
ATOM   1473 C  CB  . SER A 1 198 ? -9.161  -19.009 -7.633  1.00 33.85 ? 193 SER A CB  1 
ATOM   1474 O  OG  . SER A 1 198 ? -9.412  -17.937 -8.525  1.00 37.83 ? 193 SER A OG  1 
ATOM   1475 N  N   . PHE A 1 199 ? -8.314  -16.083 -6.487  1.00 33.29 ? 194 PHE A N   1 
ATOM   1476 C  CA  . PHE A 1 199 ? -7.473  -14.853 -6.566  1.00 33.21 ? 194 PHE A CA  1 
ATOM   1477 C  C   . PHE A 1 199 ? -6.954  -14.466 -5.166  1.00 35.38 ? 194 PHE A C   1 
ATOM   1478 O  O   . PHE A 1 199 ? -5.875  -13.806 -5.067  1.00 32.31 ? 194 PHE A O   1 
ATOM   1479 C  CB  . PHE A 1 199 ? -8.249  -13.717 -7.238  1.00 29.91 ? 194 PHE A CB  1 
ATOM   1480 C  CG  . PHE A 1 199 ? -8.412  -13.825 -8.737  1.00 30.21 ? 194 PHE A CG  1 
ATOM   1481 C  CD1 . PHE A 1 199 ? -7.630  -14.685 -9.499  1.00 30.04 ? 194 PHE A CD1 1 
ATOM   1482 C  CD2 . PHE A 1 199 ? -9.331  -13.020 -9.400  1.00 29.66 ? 194 PHE A CD2 1 
ATOM   1483 C  CE1 . PHE A 1 199 ? -7.794  -14.763 -10.877 1.00 29.89 ? 194 PHE A CE1 1 
ATOM   1484 C  CE2 . PHE A 1 199 ? -9.477  -13.088 -10.777 1.00 27.80 ? 194 PHE A CE2 1 
ATOM   1485 C  CZ  . PHE A 1 199 ? -8.710  -13.960 -11.512 1.00 28.03 ? 194 PHE A CZ  1 
ATOM   1486 N  N   . GLY A 1 200 ? -7.666  -14.888 -4.116  1.00 34.97 ? 195 GLY A N   1 
ATOM   1487 C  CA  . GLY A 1 200 ? -7.336  -14.617 -2.704  1.00 39.97 ? 195 GLY A CA  1 
ATOM   1488 C  C   . GLY A 1 200 ? -5.966  -15.135 -2.292  1.00 45.07 ? 195 GLY A C   1 
ATOM   1489 O  O   . GLY A 1 200 ? -5.366  -14.512 -1.393  1.00 46.82 ? 195 GLY A O   1 
ATOM   1490 N  N   . GLY A 1 201 ? -5.477  -16.209 -2.927  1.00 49.06 ? 196 GLY A N   1 
ATOM   1491 C  CA  . GLY A 1 201 ? -4.342  -17.016 -2.434  1.00 53.18 ? 196 GLY A CA  1 
ATOM   1492 C  C   . GLY A 1 201 ? -3.045  -16.820 -3.206  1.00 52.29 ? 196 GLY A C   1 
ATOM   1493 O  O   . GLY A 1 201 ? -2.271  -17.797 -3.288  1.00 57.43 ? 196 GLY A O   1 
ATOM   1494 N  N   . ALA A 1 202 ? -2.771  -15.610 -3.708  1.00 52.06 ? 197 ALA A N   1 
ATOM   1495 C  CA  . ALA A 1 202 ? -1.466  -15.234 -4.313  1.00 49.38 ? 197 ALA A CA  1 
ATOM   1496 C  C   . ALA A 1 202 ? -1.417  -13.725 -4.546  1.00 45.66 ? 197 ALA A C   1 
ATOM   1497 O  O   . ALA A 1 202 ? -2.475  -13.175 -4.882  1.00 46.50 ? 197 ALA A O   1 
ATOM   1498 C  CB  . ALA A 1 202 ? -1.253  -15.998 -5.598  1.00 52.29 ? 197 ALA A CB  1 
ATOM   1499 N  N   . GLU A 1 203 ? -0.243  -13.090 -4.398  1.00 44.88 ? 198 GLU A N   1 
ATOM   1500 C  CA  . GLU A 1 203 ? -0.096  -11.604 -4.434  1.00 48.57 ? 198 GLU A CA  1 
ATOM   1501 C  C   . GLU A 1 203 ? -0.519  -11.053 -5.802  1.00 46.90 ? 198 GLU A C   1 
ATOM   1502 O  O   . GLU A 1 203 ? -1.244  -10.056 -5.820  1.00 48.76 ? 198 GLU A O   1 
ATOM   1503 C  CB  . GLU A 1 203 ? 1.329   -11.138 -4.118  1.00 54.72 ? 198 GLU A CB  1 
ATOM   1504 C  CG  . GLU A 1 203 ? 1.611   -10.956 -2.628  1.00 63.89 ? 198 GLU A CG  1 
ATOM   1505 C  CD  . GLU A 1 203 ? 0.867   -9.844  -1.888  1.00 64.50 ? 198 GLU A CD  1 
ATOM   1506 O  OE1 . GLU A 1 203 ? 1.526   -8.848  -1.496  1.00 62.75 ? 198 GLU A OE1 1 
ATOM   1507 O  OE2 . GLU A 1 203 ? -0.362  -9.992  -1.657  1.00 57.59 ? 198 GLU A OE2 1 
ATOM   1508 N  N   . ALA A 1 204 ? -0.081  -11.676 -6.902  1.00 45.95 ? 199 ALA A N   1 
ATOM   1509 C  CA  . ALA A 1 204 ? -0.377  -11.252 -8.294  1.00 40.65 ? 199 ALA A CA  1 
ATOM   1510 C  C   . ALA A 1 204 ? -1.873  -10.913 -8.459  1.00 37.69 ? 199 ALA A C   1 
ATOM   1511 O  O   . ALA A 1 204 ? -2.179  -10.046 -9.298  1.00 36.96 ? 199 ALA A O   1 
ATOM   1512 C  CB  . ALA A 1 204 ? 0.052   -12.329 -9.262  1.00 37.37 ? 199 ALA A CB  1 
ATOM   1513 N  N   . THR A 1 205 ? -2.763  -11.527 -7.669  1.00 35.27 ? 200 THR A N   1 
ATOM   1514 C  CA  . THR A 1 205 ? -4.237  -11.564 -7.910  1.00 33.52 ? 200 THR A CA  1 
ATOM   1515 C  C   . THR A 1 205 ? -5.059  -11.021 -6.725  1.00 33.04 ? 200 THR A C   1 
ATOM   1516 O  O   . THR A 1 205 ? -6.296  -10.861 -6.899  1.00 29.19 ? 200 THR A O   1 
ATOM   1517 C  CB  . THR A 1 205 ? -4.639  -12.993 -8.301  1.00 36.45 ? 200 THR A CB  1 
ATOM   1518 O  OG1 . THR A 1 205 ? -4.312  -13.917 -7.263  1.00 35.76 ? 200 THR A OG1 1 
ATOM   1519 C  CG2 . THR A 1 205 ? -3.939  -13.449 -9.563  1.00 36.77 ? 200 THR A CG2 1 
ATOM   1520 N  N   . ARG A 1 206 ? -4.449  -10.725 -5.569  1.00 31.25 ? 201 ARG A N   1 
ATOM   1521 C  CA  . ARG A 1 206 ? -5.193  -10.354 -4.327  1.00 36.42 ? 201 ARG A CA  1 
ATOM   1522 C  C   . ARG A 1 206 ? -5.881  -8.989  -4.495  1.00 33.97 ? 201 ARG A C   1 
ATOM   1523 O  O   . ARG A 1 206 ? -7.024  -8.809  -3.974  1.00 30.88 ? 201 ARG A O   1 
ATOM   1524 C  CB  . ARG A 1 206 ? -4.278  -10.383 -3.094  1.00 41.34 ? 201 ARG A CB  1 
ATOM   1525 C  CG  . ARG A 1 206 ? -4.481  -11.612 -2.219  1.00 50.05 ? 201 ARG A CG  1 
ATOM   1526 C  CD  . ARG A 1 206 ? -3.695  -11.604 -0.912  1.00 52.42 ? 201 ARG A CD  1 
ATOM   1527 N  NE  . ARG A 1 206 ? -2.327  -12.099 -1.061  1.00 55.83 ? 201 ARG A NE  1 
ATOM   1528 C  CZ  . ARG A 1 206 ? -1.950  -13.384 -1.076  1.00 53.58 ? 201 ARG A CZ  1 
ATOM   1529 N  NH1 . ARG A 1 206 ? -2.833  -14.362 -0.939  1.00 54.47 ? 201 ARG A NH1 1 
ATOM   1530 N  NH2 . ARG A 1 206 ? -0.670  -13.687 -1.222  1.00 51.70 ? 201 ARG A NH2 1 
ATOM   1531 N  N   . ALA A 1 207 ? -5.260  -8.069  -5.236  1.00 30.91 ? 202 ALA A N   1 
ATOM   1532 C  CA  . ALA A 1 207 ? -5.813  -6.720  -5.493  1.00 29.70 ? 202 ALA A CA  1 
ATOM   1533 C  C   . ALA A 1 207 ? -7.127  -6.852  -6.275  1.00 28.71 ? 202 ALA A C   1 
ATOM   1534 O  O   . ALA A 1 207 ? -8.022  -6.039  -6.053  1.00 31.08 ? 202 ALA A O   1 
ATOM   1535 C  CB  . ALA A 1 207 ? -4.791  -5.869  -6.212  1.00 31.60 ? 202 ALA A CB  1 
ATOM   1536 N  N   . VAL A 1 208 ? -7.221  -7.838  -7.174  1.00 27.96 ? 203 VAL A N   1 
ATOM   1537 C  CA  . VAL A 1 208 ? -8.453  -8.109  -7.970  1.00 27.33 ? 203 VAL A CA  1 
ATOM   1538 C  C   . VAL A 1 208 ? -9.474  -8.700  -7.002  1.00 25.65 ? 203 VAL A C   1 
ATOM   1539 O  O   . VAL A 1 208 ? -10.572 -8.168  -6.935  1.00 27.76 ? 203 VAL A O   1 
ATOM   1540 C  CB  . VAL A 1 208 ? -8.181  -9.025  -9.177  1.00 29.26 ? 203 VAL A CB  1 
ATOM   1541 C  CG1 . VAL A 1 208 ? -9.463  -9.423  -9.895  1.00 30.31 ? 203 VAL A CG1 1 
ATOM   1542 C  CG2 . VAL A 1 208 ? -7.222  -8.370  -10.162 1.00 29.63 ? 203 VAL A CG2 1 
ATOM   1543 N  N   . ALA A 1 209 ? -9.099  -9.720  -6.227  1.00 25.03 ? 204 ALA A N   1 
ATOM   1544 C  CA  . ALA A 1 209 ? -9.961  -10.283 -5.163  1.00 28.10 ? 204 ALA A CA  1 
ATOM   1545 C  C   . ALA A 1 209 ? -10.457 -9.135  -4.259  1.00 29.19 ? 204 ALA A C   1 
ATOM   1546 O  O   . ALA A 1 209 ? -11.674 -9.079  -3.942  1.00 27.77 ? 204 ALA A O   1 
ATOM   1547 C  CB  . ALA A 1 209 ? -9.225  -11.368 -4.402  1.00 26.88 ? 204 ALA A CB  1 
ATOM   1548 N  N   . GLY A 1 210 ? -9.563  -8.227  -3.884  1.00 31.82 ? 205 GLY A N   1 
ATOM   1549 C  CA  . GLY A 1 210 ? -9.895  -6.975  -3.162  1.00 34.00 ? 205 GLY A CA  1 
ATOM   1550 C  C   . GLY A 1 210 ? -11.079 -6.220  -3.769  1.00 33.64 ? 205 GLY A C   1 
ATOM   1551 O  O   . GLY A 1 210 ? -12.047 -5.921  -3.024  1.00 33.20 ? 205 GLY A O   1 
ATOM   1552 N  N   . LEU A 1 211 ? -11.036 -5.881  -5.055  1.00 29.42 ? 206 LEU A N   1 
ATOM   1553 C  CA  . LEU A 1 211 ? -12.143 -5.102  -5.684  1.00 28.87 ? 206 LEU A CA  1 
ATOM   1554 C  C   . LEU A 1 211 ? -13.422 -5.956  -5.799  1.00 31.41 ? 206 LEU A C   1 
ATOM   1555 O  O   . LEU A 1 211 ? -14.564 -5.367  -5.663  1.00 26.60 ? 206 LEU A O   1 
ATOM   1556 C  CB  . LEU A 1 211 ? -11.681 -4.605  -7.060  1.00 32.76 ? 206 LEU A CB  1 
ATOM   1557 C  CG  . LEU A 1 211 ? -10.550 -3.584  -7.009  1.00 38.29 ? 206 LEU A CG  1 
ATOM   1558 C  CD1 . LEU A 1 211 ? -9.829  -3.490  -8.337  1.00 41.50 ? 206 LEU A CD1 1 
ATOM   1559 C  CD2 . LEU A 1 211 ? -11.078 -2.222  -6.570  1.00 42.52 ? 206 LEU A CD2 1 
ATOM   1560 N  N   . MET A 1 212 ? -13.284 -7.270  -6.064  1.00 31.58 ? 207 MET A N   1 
ATOM   1561 C  CA  . MET A 1 212 ? -14.441 -8.212  -6.173  1.00 34.11 ? 207 MET A CA  1 
ATOM   1562 C  C   . MET A 1 212 ? -15.167 -8.295  -4.822  1.00 38.90 ? 207 MET A C   1 
ATOM   1563 O  O   . MET A 1 212 ? -16.413 -8.322  -4.843  1.00 38.22 ? 207 MET A O   1 
ATOM   1564 C  CB  . MET A 1 212 ? -14.023 -9.618  -6.623  1.00 33.79 ? 207 MET A CB  1 
ATOM   1565 C  CG  . MET A 1 212 ? -13.480 -9.657  -8.048  1.00 32.53 ? 207 MET A CG  1 
ATOM   1566 S  SD  . MET A 1 212 ? -12.939 -11.293 -8.626  1.00 28.48 ? 207 MET A SD  1 
ATOM   1567 C  CE  . MET A 1 212 ? -14.560 -12.035 -8.883  1.00 33.78 ? 207 MET A CE  1 
ATOM   1568 N  N   . ASP A 1 213 ? -14.428 -8.324  -3.703  1.00 43.11 ? 208 ASP A N   1 
ATOM   1569 C  CA  . ASP A 1 213 ? -14.963 -8.158  -2.313  1.00 49.96 ? 208 ASP A CA  1 
ATOM   1570 C  C   . ASP A 1 213 ? -15.850 -6.902  -2.223  1.00 53.01 ? 208 ASP A C   1 
ATOM   1571 O  O   . ASP A 1 213 ? -17.015 -7.036  -1.790  1.00 58.63 ? 208 ASP A O   1 
ATOM   1572 C  CB  . ASP A 1 213 ? -13.853 -8.039  -1.255  1.00 51.76 ? 208 ASP A CB  1 
ATOM   1573 C  CG  . ASP A 1 213 ? -13.615 -9.276  -0.401  1.00 51.74 ? 208 ASP A CG  1 
ATOM   1574 O  OD1 . ASP A 1 213 ? -13.588 -10.369 -0.960  1.00 54.31 ? 208 ASP A OD1 1 
ATOM   1575 O  OD2 . ASP A 1 213 ? -13.451 -9.127  0.826   1.00 52.68 ? 208 ASP A OD2 1 
ATOM   1576 N  N   . ARG A 1 214 ? -15.323 -5.730  -2.614  1.00 53.68 ? 209 ARG A N   1 
ATOM   1577 C  CA  . ARG A 1 214 ? -15.975 -4.402  -2.431  1.00 52.99 ? 209 ARG A CA  1 
ATOM   1578 C  C   . ARG A 1 214 ? -17.193 -4.233  -3.354  1.00 51.66 ? 209 ARG A C   1 
ATOM   1579 O  O   . ARG A 1 214 ? -17.867 -3.210  -3.197  1.00 53.61 ? 209 ARG A O   1 
ATOM   1580 C  CB  . ARG A 1 214 ? -14.993 -3.248  -2.665  1.00 56.45 ? 209 ARG A CB  1 
ATOM   1581 C  CG  . ARG A 1 214 ? -13.707 -3.348  -1.856  1.00 62.30 ? 209 ARG A CG  1 
ATOM   1582 C  CD  . ARG A 1 214 ? -13.120 -2.012  -1.437  1.00 66.40 ? 209 ARG A CD  1 
ATOM   1583 N  NE  . ARG A 1 214 ? -12.942 -1.081  -2.550  1.00 73.87 ? 209 ARG A NE  1 
ATOM   1584 C  CZ  . ARG A 1 214 ? -13.756 -0.071  -2.861  1.00 71.32 ? 209 ARG A CZ  1 
ATOM   1585 N  NH1 . ARG A 1 214 ? -14.847 0.167   -2.152  1.00 71.81 ? 209 ARG A NH1 1 
ATOM   1586 N  NH2 . ARG A 1 214 ? -13.473 0.699   -3.896  1.00 75.38 ? 209 ARG A NH2 1 
ATOM   1587 N  N   . LEU A 1 215 ? -17.470 -5.148  -4.292  1.00 47.99 ? 210 LEU A N   1 
ATOM   1588 C  CA  . LEU A 1 215 ? -18.699 -5.052  -5.118  1.00 51.13 ? 210 LEU A CA  1 
ATOM   1589 C  C   . LEU A 1 215 ? -19.878 -5.376  -4.202  1.00 58.22 ? 210 LEU A C   1 
ATOM   1590 O  O   . LEU A 1 215 ? -19.752 -6.223  -3.322  1.00 68.79 ? 210 LEU A O   1 
ATOM   1591 C  CB  . LEU A 1 215 ? -18.630 -5.985  -6.334  1.00 48.77 ? 210 LEU A CB  1 
ATOM   1592 C  CG  . LEU A 1 215 ? -17.643 -5.591  -7.438  1.00 47.92 ? 210 LEU A CG  1 
ATOM   1593 C  CD1 . LEU A 1 215 ? -17.687 -6.582  -8.590  1.00 48.10 ? 210 LEU A CD1 1 
ATOM   1594 C  CD2 . LEU A 1 215 ? -17.920 -4.203  -7.978  1.00 44.86 ? 210 LEU A CD2 1 
ATOM   1595 N  N   . PRO A 1 216 ? -21.031 -4.676  -4.331  1.00 61.17 ? 211 PRO A N   1 
ATOM   1596 C  CA  . PRO A 1 216 ? -22.198 -4.931  -3.480  1.00 61.88 ? 211 PRO A CA  1 
ATOM   1597 C  C   . PRO A 1 216 ? -22.603 -6.409  -3.361  1.00 61.71 ? 211 PRO A C   1 
ATOM   1598 O  O   . PRO A 1 216 ? -23.135 -6.985  -4.297  1.00 66.62 ? 211 PRO A O   1 
ATOM   1599 C  CB  . PRO A 1 216 ? -23.306 -4.128  -4.179  1.00 61.54 ? 211 PRO A CB  1 
ATOM   1600 C  CG  . PRO A 1 216 ? -22.569 -2.969  -4.808  1.00 61.50 ? 211 PRO A CG  1 
ATOM   1601 C  CD  . PRO A 1 216 ? -21.254 -3.561  -5.267  1.00 60.26 ? 211 PRO A CD  1 
ATOM   1602 N  N   . ALA B 1 5   ? -17.421 -13.240 25.646  1.00 40.18 ? 0   ALA B N   1 
ATOM   1603 C  CA  . ALA B 1 5   ? -16.038 -13.306 26.244  1.00 39.32 ? 0   ALA B CA  1 
ATOM   1604 C  C   . ALA B 1 5   ? -15.174 -12.124 25.778  1.00 38.45 ? 0   ALA B C   1 
ATOM   1605 O  O   . ALA B 1 5   ? -14.092 -11.929 26.372  1.00 40.23 ? 0   ALA B O   1 
ATOM   1606 C  CB  . ALA B 1 5   ? -15.386 -14.626 25.928  1.00 37.48 ? 0   ALA B CB  1 
ATOM   1607 N  N   . MET B 1 6   ? -15.612 -11.402 24.741  1.00 36.97 ? 1   MET B N   1 
ATOM   1608 C  CA  . MET B 1 6   ? -15.071 -10.088 24.300  1.00 37.80 ? 1   MET B CA  1 
ATOM   1609 C  C   . MET B 1 6   ? -16.236 -9.097  24.280  1.00 36.61 ? 1   MET B C   1 
ATOM   1610 O  O   . MET B 1 6   ? -17.257 -9.442  23.692  1.00 38.42 ? 1   MET B O   1 
ATOM   1611 C  CB  . MET B 1 6   ? -14.481 -10.172 22.888  1.00 38.46 ? 1   MET B CB  1 
ATOM   1612 C  CG  . MET B 1 6   ? -13.881 -8.865  22.408  1.00 40.25 ? 1   MET B CG  1 
ATOM   1613 S  SD  . MET B 1 6   ? -13.084 -8.987  20.776  1.00 43.16 ? 1   MET B SD  1 
ATOM   1614 C  CE  . MET B 1 6   ? -12.353 -7.358  20.698  1.00 38.76 ? 1   MET B CE  1 
ATOM   1615 N  N   . PHE B 1 7   ? -16.101 -7.927  24.907  1.00 37.38 ? 2   PHE B N   1 
ATOM   1616 C  CA  . PHE B 1 7   ? -17.116 -6.849  24.836  1.00 35.28 ? 2   PHE B CA  1 
ATOM   1617 C  C   . PHE B 1 7   ? -16.967 -6.141  23.488  1.00 31.77 ? 2   PHE B C   1 
ATOM   1618 O  O   . PHE B 1 7   ? -15.926 -5.519  23.245  1.00 31.85 ? 2   PHE B O   1 
ATOM   1619 C  CB  . PHE B 1 7   ? -16.982 -5.846  25.984  1.00 35.40 ? 2   PHE B CB  1 
ATOM   1620 C  CG  . PHE B 1 7   ? -18.079 -4.806  26.006  1.00 35.34 ? 2   PHE B CG  1 
ATOM   1621 C  CD1 . PHE B 1 7   ? -19.409 -5.181  26.142  1.00 36.81 ? 2   PHE B CD1 1 
ATOM   1622 C  CD2 . PHE B 1 7   ? -17.786 -3.454  25.915  1.00 37.45 ? 2   PHE B CD2 1 
ATOM   1623 C  CE1 . PHE B 1 7   ? -20.421 -4.232  26.160  1.00 37.58 ? 2   PHE B CE1 1 
ATOM   1624 C  CE2 . PHE B 1 7   ? -18.800 -2.503  25.937  1.00 38.79 ? 2   PHE B CE2 1 
ATOM   1625 C  CZ  . PHE B 1 7   ? -20.116 -2.894  26.059  1.00 36.63 ? 2   PHE B CZ  1 
ATOM   1626 N  N   . VAL B 1 8   ? -17.961 -6.300  22.618  1.00 32.49 ? 3   VAL B N   1 
ATOM   1627 C  CA  . VAL B 1 8   ? -18.063 -5.568  21.322  1.00 29.99 ? 3   VAL B CA  1 
ATOM   1628 C  C   . VAL B 1 8   ? -19.442 -4.928  21.215  1.00 29.65 ? 3   VAL B C   1 
ATOM   1629 O  O   . VAL B 1 8   ? -20.428 -5.626  20.982  1.00 28.05 ? 3   VAL B O   1 
ATOM   1630 C  CB  . VAL B 1 8   ? -17.802 -6.479  20.117  1.00 29.79 ? 3   VAL B CB  1 
ATOM   1631 C  CG1 . VAL B 1 8   ? -18.007 -5.674  18.825  1.00 29.36 ? 3   VAL B CG1 1 
ATOM   1632 C  CG2 . VAL B 1 8   ? -16.404 -7.118  20.187  1.00 32.71 ? 3   VAL B CG2 1 
ATOM   1633 N  N   . PRO B 1 9   ? -19.547 -3.590  21.349  1.00 31.08 ? 4   PRO B N   1 
ATOM   1634 C  CA  . PRO B 1 9   ? -20.829 -2.899  21.185  1.00 34.07 ? 4   PRO B CA  1 
ATOM   1635 C  C   . PRO B 1 9   ? -21.381 -3.136  19.771  1.00 33.90 ? 4   PRO B C   1 
ATOM   1636 O  O   . PRO B 1 9   ? -20.594 -3.216  18.843  1.00 32.86 ? 4   PRO B O   1 
ATOM   1637 C  CB  . PRO B 1 9   ? -20.503 -1.417  21.433  1.00 33.23 ? 4   PRO B CB  1 
ATOM   1638 C  CG  . PRO B 1 9   ? -19.172 -1.425  22.180  1.00 33.74 ? 4   PRO B CG  1 
ATOM   1639 C  CD  . PRO B 1 9   ? -18.452 -2.667  21.686  1.00 32.78 ? 4   PRO B CD  1 
ATOM   1640 N  N   . GLY B 1 10  ? -22.706 -3.225  19.642  1.00 34.31 ? 5   GLY B N   1 
ATOM   1641 C  CA  . GLY B 1 10  ? -23.418 -3.659  18.416  1.00 36.58 ? 5   GLY B CA  1 
ATOM   1642 C  C   . GLY B 1 10  ? -22.917 -2.976  17.139  1.00 33.04 ? 5   GLY B C   1 
ATOM   1643 O  O   . GLY B 1 10  ? -22.636 -3.649  16.141  1.00 31.09 ? 5   GLY B O   1 
ATOM   1644 N  N   . PRO B 1 11  ? -22.750 -1.631  17.148  1.00 31.05 ? 6   PRO B N   1 
ATOM   1645 C  CA  . PRO B 1 11  ? -22.353 -0.889  15.953  1.00 33.62 ? 6   PRO B CA  1 
ATOM   1646 C  C   . PRO B 1 11  ? -20.929 -1.234  15.472  1.00 28.53 ? 6   PRO B C   1 
ATOM   1647 O  O   . PRO B 1 11  ? -20.644 -0.932  14.380  1.00 29.93 ? 6   PRO B O   1 
ATOM   1648 C  CB  . PRO B 1 11  ? -22.440 0.592   16.376  1.00 34.82 ? 6   PRO B CB  1 
ATOM   1649 C  CG  . PRO B 1 11  ? -23.232 0.576   17.668  1.00 36.69 ? 6   PRO B CG  1 
ATOM   1650 C  CD  . PRO B 1 11  ? -22.884 -0.748  18.318  1.00 34.72 ? 6   PRO B CD  1 
ATOM   1651 N  N   . TYR B 1 12  ? -20.107 -1.918  16.268  1.00 30.41 ? 7   TYR B N   1 
ATOM   1652 C  CA  . TYR B 1 12  ? -18.701 -2.263  15.902  1.00 28.78 ? 7   TYR B CA  1 
ATOM   1653 C  C   . TYR B 1 12  ? -18.567 -3.748  15.524  1.00 28.43 ? 7   TYR B C   1 
ATOM   1654 O  O   . TYR B 1 12  ? -17.417 -4.254  15.389  1.00 24.84 ? 7   TYR B O   1 
ATOM   1655 C  CB  . TYR B 1 12  ? -17.778 -1.879  17.052  1.00 28.35 ? 7   TYR B CB  1 
ATOM   1656 C  CG  . TYR B 1 12  ? -17.860 -0.428  17.458  1.00 28.72 ? 7   TYR B CG  1 
ATOM   1657 C  CD1 . TYR B 1 12  ? -18.021 0.557   16.504  1.00 27.70 ? 7   TYR B CD1 1 
ATOM   1658 C  CD2 . TYR B 1 12  ? -17.750 -0.029  18.783  1.00 31.42 ? 7   TYR B CD2 1 
ATOM   1659 C  CE1 . TYR B 1 12  ? -18.059 1.894   16.836  1.00 25.88 ? 7   TYR B CE1 1 
ATOM   1660 C  CE2 . TYR B 1 12  ? -17.823 1.313   19.144  1.00 30.26 ? 7   TYR B CE2 1 
ATOM   1661 C  CZ  . TYR B 1 12  ? -17.963 2.273   18.157  1.00 30.10 ? 7   TYR B CZ  1 
ATOM   1662 O  OH  . TYR B 1 12  ? -18.022 3.604   18.435  1.00 36.14 ? 7   TYR B OH  1 
ATOM   1663 N  N   . HIS B 1 13  ? -19.691 -4.443  15.351  1.00 25.91 ? 8   HIS B N   1 
ATOM   1664 C  CA  . HIS B 1 13  ? -19.748 -5.820  14.790  1.00 29.67 ? 8   HIS B CA  1 
ATOM   1665 C  C   . HIS B 1 13  ? -19.370 -5.782  13.316  1.00 28.86 ? 8   HIS B C   1 
ATOM   1666 O  O   . HIS B 1 13  ? -19.783 -4.814  12.629  1.00 25.95 ? 8   HIS B O   1 
ATOM   1667 C  CB  . HIS B 1 13  ? -21.151 -6.438  14.956  1.00 33.46 ? 8   HIS B CB  1 
ATOM   1668 C  CG  . HIS B 1 13  ? -21.371 -6.978  16.321  1.00 36.38 ? 8   HIS B CG  1 
ATOM   1669 N  ND1 . HIS B 1 13  ? -21.422 -6.161  17.429  1.00 40.57 ? 8   HIS B ND1 1 
ATOM   1670 C  CD2 . HIS B 1 13  ? -21.464 -8.244  16.767  1.00 42.55 ? 8   HIS B CD2 1 
ATOM   1671 C  CE1 . HIS B 1 13  ? -21.575 -6.899  18.506  1.00 40.47 ? 8   HIS B CE1 1 
ATOM   1672 N  NE2 . HIS B 1 13  ? -21.609 -8.183  18.125  1.00 48.13 ? 8   HIS B NE2 1 
ATOM   1673 N  N   . ALA B 1 14  ? -18.607 -6.773  12.845  1.00 31.70 ? 9   ALA B N   1 
ATOM   1674 C  CA  . ALA B 1 14  ? -18.257 -6.898  11.408  1.00 35.72 ? 9   ALA B CA  1 
ATOM   1675 C  C   . ALA B 1 14  ? -19.539 -7.069  10.606  1.00 36.43 ? 9   ALA B C   1 
ATOM   1676 O  O   . ALA B 1 14  ? -20.481 -7.691  11.078  1.00 34.00 ? 9   ALA B O   1 
ATOM   1677 C  CB  . ALA B 1 14  ? -17.343 -8.063  11.175  1.00 35.84 ? 9   ALA B CB  1 
ATOM   1678 N  N   . PRO B 1 15  ? -19.619 -6.540  9.370   1.00 38.65 ? 10  PRO B N   1 
ATOM   1679 C  CA  . PRO B 1 15  ? -20.785 -6.788  8.521   1.00 40.39 ? 10  PRO B CA  1 
ATOM   1680 C  C   . PRO B 1 15  ? -21.024 -8.276  8.225   1.00 37.79 ? 10  PRO B C   1 
ATOM   1681 O  O   . PRO B 1 15  ? -22.152 -8.642  7.963   1.00 39.11 ? 10  PRO B O   1 
ATOM   1682 C  CB  . PRO B 1 15  ? -20.461 -6.055  7.206   1.00 39.65 ? 10  PRO B CB  1 
ATOM   1683 C  CG  . PRO B 1 15  ? -19.388 -5.049  7.582   1.00 39.25 ? 10  PRO B CG  1 
ATOM   1684 C  CD  . PRO B 1 15  ? -18.633 -5.651  8.746   1.00 36.36 ? 10  PRO B CD  1 
ATOM   1685 N  N   . GLU B 1 16  ? -19.967 -9.081  8.229   1.00 35.17 ? 11  GLU B N   1 
ATOM   1686 C  CA  . GLU B 1 16  ? -19.974 -10.485 7.732   1.00 38.42 ? 11  GLU B CA  1 
ATOM   1687 C  C   . GLU B 1 16  ? -18.892 -11.253 8.493   1.00 37.61 ? 11  GLU B C   1 
ATOM   1688 O  O   . GLU B 1 16  ? -17.849 -10.633 8.753   1.00 35.86 ? 11  GLU B O   1 
ATOM   1689 C  CB  . GLU B 1 16  ? -19.644 -10.549 6.233   1.00 42.98 ? 11  GLU B CB  1 
ATOM   1690 C  CG  . GLU B 1 16  ? -20.714 -10.008 5.291   1.00 49.42 ? 11  GLU B CG  1 
ATOM   1691 C  CD  . GLU B 1 16  ? -21.975 -10.852 5.098   1.00 59.06 ? 11  GLU B CD  1 
ATOM   1692 O  OE1 . GLU B 1 16  ? -22.997 -10.548 5.758   1.00 63.95 ? 11  GLU B OE1 1 
ATOM   1693 O  OE2 . GLU B 1 16  ? -21.958 -11.783 4.247   1.00 63.90 ? 11  GLU B OE2 1 
ATOM   1694 N  N   . ASP B 1 17  ? -19.101 -12.545 8.776   1.00 35.68 ? 12  ASP B N   1 
ATOM   1695 C  CA  . ASP B 1 17  ? -18.133 -13.406 9.515   1.00 37.79 ? 12  ASP B CA  1 
ATOM   1696 C  C   . ASP B 1 17  ? -16.763 -13.413 8.808   1.00 36.26 ? 12  ASP B C   1 
ATOM   1697 O  O   . ASP B 1 17  ? -15.705 -13.511 9.521   1.00 32.75 ? 12  ASP B O   1 
ATOM   1698 C  CB  . ASP B 1 17  ? -18.666 -14.828 9.688   1.00 41.03 ? 12  ASP B CB  1 
ATOM   1699 C  CG  . ASP B 1 17  ? -19.988 -14.924 10.441  1.00 44.04 ? 12  ASP B CG  1 
ATOM   1700 O  OD1 . ASP B 1 17  ? -20.073 -14.383 11.554  1.00 44.97 ? 12  ASP B OD1 1 
ATOM   1701 O  OD2 . ASP B 1 17  ? -20.926 -15.546 9.903   1.00 51.65 ? 12  ASP B OD2 1 
ATOM   1702 N  N   . ARG B 1 18  ? -16.755 -13.321 7.473   1.00 35.20 ? 13  ARG B N   1 
ATOM   1703 C  CA  . ARG B 1 18  ? -15.520 -13.375 6.637   1.00 37.82 ? 13  ARG B CA  1 
ATOM   1704 C  C   . ARG B 1 18  ? -14.553 -12.253 7.040   1.00 30.89 ? 13  ARG B C   1 
ATOM   1705 O  O   . ARG B 1 18  ? -13.369 -12.435 6.812   1.00 29.13 ? 13  ARG B O   1 
ATOM   1706 C  CB  . ARG B 1 18  ? -15.850 -13.299 5.142   1.00 44.91 ? 13  ARG B CB  1 
ATOM   1707 C  CG  . ARG B 1 18  ? -14.694 -13.650 4.208   1.00 53.13 ? 13  ARG B CG  1 
ATOM   1708 C  CD  . ARG B 1 18  ? -15.013 -13.380 2.741   1.00 61.31 ? 13  ARG B CD  1 
ATOM   1709 N  NE  . ARG B 1 18  ? -16.179 -14.141 2.304   1.00 68.85 ? 13  ARG B NE  1 
ATOM   1710 C  CZ  . ARG B 1 18  ? -17.439 -13.697 2.264   1.00 79.22 ? 13  ARG B CZ  1 
ATOM   1711 N  NH1 . ARG B 1 18  ? -17.743 -12.457 2.620   1.00 85.47 ? 13  ARG B NH1 1 
ATOM   1712 N  NH2 . ARG B 1 18  ? -18.406 -14.508 1.864   1.00 86.66 ? 13  ARG B NH2 1 
ATOM   1713 N  N   . TRP B 1 19  ? -15.028 -11.148 7.630   1.00 30.96 ? 14  TRP B N   1 
ATOM   1714 C  CA  . TRP B 1 19  ? -14.158 -10.018 8.061   1.00 30.90 ? 14  TRP B CA  1 
ATOM   1715 C  C   . TRP B 1 19  ? -13.184 -10.479 9.156   1.00 27.65 ? 14  TRP B C   1 
ATOM   1716 O  O   . TRP B 1 19  ? -12.056 -9.961  9.195   1.00 25.61 ? 14  TRP B O   1 
ATOM   1717 C  CB  . TRP B 1 19  ? -14.981 -8.814  8.524   1.00 32.15 ? 14  TRP B CB  1 
ATOM   1718 C  CG  . TRP B 1 19  ? -15.541 -7.968  7.419   1.00 34.75 ? 14  TRP B CG  1 
ATOM   1719 C  CD1 . TRP B 1 19  ? -16.174 -8.388  6.285   1.00 34.96 ? 14  TRP B CD1 1 
ATOM   1720 C  CD2 . TRP B 1 19  ? -15.568 -6.534  7.377   1.00 32.27 ? 14  TRP B CD2 1 
ATOM   1721 N  NE1 . TRP B 1 19  ? -16.557 -7.311  5.530   1.00 35.26 ? 14  TRP B NE1 1 
ATOM   1722 C  CE2 . TRP B 1 19  ? -16.196 -6.162  6.174   1.00 34.29 ? 14  TRP B CE2 1 
ATOM   1723 C  CE3 . TRP B 1 19  ? -15.107 -5.534  8.227   1.00 35.43 ? 14  TRP B CE3 1 
ATOM   1724 C  CZ2 . TRP B 1 19  ? -16.371 -4.831  5.802   1.00 34.38 ? 14  TRP B CZ2 1 
ATOM   1725 C  CZ3 . TRP B 1 19  ? -15.280 -4.218  7.860   1.00 36.53 ? 14  TRP B CZ3 1 
ATOM   1726 C  CH2 . TRP B 1 19  ? -15.902 -3.873  6.661   1.00 34.94 ? 14  TRP B CH2 1 
ATOM   1727 N  N   . LEU B 1 20  ? -13.625 -11.364 10.050  1.00 27.05 ? 15  LEU B N   1 
ATOM   1728 C  CA  . LEU B 1 20  ? -12.805 -11.869 11.165  1.00 26.16 ? 15  LEU B CA  1 
ATOM   1729 C  C   . LEU B 1 20  ? -11.701 -12.726 10.549  1.00 26.74 ? 15  LEU B C   1 
ATOM   1730 O  O   . LEU B 1 20  ? -10.524 -12.463 10.837  1.00 25.75 ? 15  LEU B O   1 
ATOM   1731 C  CB  . LEU B 1 20  ? -13.688 -12.619 12.163  1.00 27.66 ? 15  LEU B CB  1 
ATOM   1732 C  CG  . LEU B 1 20  ? -14.530 -11.762 13.119  1.00 28.73 ? 15  LEU B CG  1 
ATOM   1733 C  CD1 . LEU B 1 20  ? -15.721 -11.121 12.411  1.00 32.46 ? 15  LEU B CD1 1 
ATOM   1734 C  CD2 . LEU B 1 20  ? -15.048 -12.564 14.312  1.00 25.90 ? 15  LEU B CD2 1 
ATOM   1735 N  N   . VAL B 1 21  ? -12.059 -13.586 9.589   1.00 27.41 ? 16  VAL B N   1 
ATOM   1736 C  CA  . VAL B 1 21  ? -11.096 -14.466 8.859   1.00 27.88 ? 16  VAL B CA  1 
ATOM   1737 C  C   . VAL B 1 21  ? -10.070 -13.591 8.122   1.00 27.22 ? 16  VAL B C   1 
ATOM   1738 O  O   . VAL B 1 21  ? -8.847  -13.861 8.262   1.00 24.61 ? 16  VAL B O   1 
ATOM   1739 C  CB  . VAL B 1 21  ? -11.778 -15.453 7.893   1.00 28.56 ? 16  VAL B CB  1 
ATOM   1740 C  CG1 . VAL B 1 21  ? -10.743 -16.323 7.202   1.00 30.73 ? 16  VAL B CG1 1 
ATOM   1741 C  CG2 . VAL B 1 21  ? -12.838 -16.318 8.569   1.00 28.24 ? 16  VAL B CG2 1 
ATOM   1742 N  N   . ASP B 1 22  ? -10.530 -12.545 7.435   1.00 26.26 ? 17  ASP B N   1 
ATOM   1743 C  CA  . ASP B 1 22  ? -9.652  -11.633 6.660   1.00 29.97 ? 17  ASP B CA  1 
ATOM   1744 C  C   . ASP B 1 22  ? -8.615  -11.028 7.606   1.00 27.90 ? 17  ASP B C   1 
ATOM   1745 O  O   . ASP B 1 22  ? -7.433  -10.952 7.211   1.00 23.80 ? 17  ASP B O   1 
ATOM   1746 C  CB  . ASP B 1 22  ? -10.434 -10.530 5.939   1.00 33.74 ? 17  ASP B CB  1 
ATOM   1747 C  CG  . ASP B 1 22  ? -11.258 -11.005 4.750   1.00 39.38 ? 17  ASP B CG  1 
ATOM   1748 O  OD1 . ASP B 1 22  ? -11.094 -12.196 4.333   1.00 41.18 ? 17  ASP B OD1 1 
ATOM   1749 O  OD2 . ASP B 1 22  ? -12.089 -10.199 4.273   1.00 46.29 ? 17  ASP B OD2 1 
ATOM   1750 N  N   . LEU B 1 23  ? -9.048  -10.585 8.787   1.00 29.02 ? 18  LEU B N   1 
ATOM   1751 C  CA  . LEU B 1 23  ? -8.140  -9.917  9.756   1.00 29.44 ? 18  LEU B CA  1 
ATOM   1752 C  C   . LEU B 1 23  ? -7.093  -10.929 10.242  1.00 27.11 ? 18  LEU B C   1 
ATOM   1753 O  O   . LEU B 1 23  ? -5.902  -10.596 10.160  1.00 24.07 ? 18  LEU B O   1 
ATOM   1754 C  CB  . LEU B 1 23  ? -8.941  -9.313  10.907  1.00 30.57 ? 18  LEU B CB  1 
ATOM   1755 C  CG  . LEU B 1 23  ? -8.265  -8.132  11.607  1.00 33.33 ? 18  LEU B CG  1 
ATOM   1756 C  CD1 . LEU B 1 23  ? -9.299  -7.217  12.230  1.00 36.03 ? 18  LEU B CD1 1 
ATOM   1757 C  CD2 . LEU B 1 23  ? -7.289  -8.616  12.665  1.00 34.51 ? 18  LEU B CD2 1 
ATOM   1758 N  N   . VAL B 1 24  ? -7.518  -12.131 10.651  1.00 24.96 ? 19  VAL B N   1 
ATOM   1759 C  CA  . VAL B 1 24  ? -6.588  -13.221 11.062  1.00 28.14 ? 19  VAL B CA  1 
ATOM   1760 C  C   . VAL B 1 24  ? -5.564  -13.437 9.938   1.00 26.57 ? 19  VAL B C   1 
ATOM   1761 O  O   . VAL B 1 24  ? -4.369  -13.455 10.232  1.00 24.30 ? 19  VAL B O   1 
ATOM   1762 C  CB  . VAL B 1 24  ? -7.322  -14.531 11.410  1.00 30.82 ? 19  VAL B CB  1 
ATOM   1763 C  CG1 . VAL B 1 24  ? -6.344  -15.699 11.527  1.00 31.60 ? 19  VAL B CG1 1 
ATOM   1764 C  CG2 . VAL B 1 24  ? -8.165  -14.395 12.675  1.00 28.57 ? 19  VAL B CG2 1 
ATOM   1765 N  N   . ARG B 1 25  ? -6.002  -13.625 8.697   1.00 26.72 ? 20  ARG B N   1 
ATOM   1766 C  CA  . ARG B 1 25  ? -5.058  -13.854 7.575   1.00 30.35 ? 20  ARG B CA  1 
ATOM   1767 C  C   . ARG B 1 25  ? -4.137  -12.651 7.422   1.00 29.44 ? 20  ARG B C   1 
ATOM   1768 O  O   . ARG B 1 25  ? -2.938  -12.876 7.227   1.00 29.20 ? 20  ARG B O   1 
ATOM   1769 C  CB  . ARG B 1 25  ? -5.774  -14.092 6.249   1.00 32.74 ? 20  ARG B CB  1 
ATOM   1770 C  CG  . ARG B 1 25  ? -6.505  -15.418 6.151   1.00 34.03 ? 20  ARG B CG  1 
ATOM   1771 C  CD  . ARG B 1 25  ? -6.939  -15.628 4.710   1.00 34.41 ? 20  ARG B CD  1 
ATOM   1772 N  NE  . ARG B 1 25  ? -7.988  -16.611 4.545   1.00 35.14 ? 20  ARG B NE  1 
ATOM   1773 C  CZ  . ARG B 1 25  ? -7.839  -17.926 4.672   1.00 41.42 ? 20  ARG B CZ  1 
ATOM   1774 N  NH1 . ARG B 1 25  ? -6.652  -18.443 4.965   1.00 40.72 ? 20  ARG B NH1 1 
ATOM   1775 N  NH2 . ARG B 1 25  ? -8.887  -18.721 4.494   1.00 40.93 ? 20  ARG B NH2 1 
ATOM   1776 N  N   . GLY B 1 26  ? -4.672  -11.432 7.569   1.00 27.61 ? 21  GLY B N   1 
ATOM   1777 C  CA  . GLY B 1 26  ? -3.913  -10.186 7.338   1.00 25.55 ? 21  GLY B CA  1 
ATOM   1778 C  C   . GLY B 1 26  ? -2.941  -9.861  8.456   1.00 24.77 ? 21  GLY B C   1 
ATOM   1779 O  O   . GLY B 1 26  ? -2.038  -9.029  8.239   1.00 23.35 ? 21  GLY B O   1 
ATOM   1780 N  N   . HIS B 1 27  ? -3.076  -10.485 9.625   1.00 23.76 ? 22  HIS B N   1 
ATOM   1781 C  CA  . HIS B 1 27  ? -2.420  -10.012 10.876  1.00 24.09 ? 22  HIS B CA  1 
ATOM   1782 C  C   . HIS B 1 27  ? -2.011  -11.194 11.766  1.00 26.18 ? 22  HIS B C   1 
ATOM   1783 O  O   . HIS B 1 27  ? -2.357  -11.248 12.953  1.00 25.78 ? 22  HIS B O   1 
ATOM   1784 C  CB  . HIS B 1 27  ? -3.380  -9.010  11.535  1.00 20.79 ? 22  HIS B CB  1 
ATOM   1785 C  CG  . HIS B 1 27  ? -3.637  -7.856  10.645  1.00 20.45 ? 22  HIS B CG  1 
ATOM   1786 N  ND1 . HIS B 1 27  ? -2.710  -6.844  10.482  1.00 22.02 ? 22  HIS B ND1 1 
ATOM   1787 C  CD2 . HIS B 1 27  ? -4.643  -7.584  9.793   1.00 22.30 ? 22  HIS B CD2 1 
ATOM   1788 C  CE1 . HIS B 1 27  ? -3.178  -5.963  9.623   1.00 23.82 ? 22  HIS B CE1 1 
ATOM   1789 N  NE2 . HIS B 1 27  ? -4.352  -6.398  9.168   1.00 22.30 ? 22  HIS B NE2 1 
ATOM   1790 N  N   . PRO B 1 28  ? -1.181  -12.123 11.242  1.00 25.30 ? 23  PRO B N   1 
ATOM   1791 C  CA  . PRO B 1 28  ? -0.994  -13.438 11.857  1.00 26.20 ? 23  PRO B CA  1 
ATOM   1792 C  C   . PRO B 1 28  ? -0.145  -13.462 13.134  1.00 24.77 ? 23  PRO B C   1 
ATOM   1793 O  O   . PRO B 1 28  ? -0.163  -14.475 13.831  1.00 20.03 ? 23  PRO B O   1 
ATOM   1794 C  CB  . PRO B 1 28  ? -0.288  -14.238 10.757  1.00 24.37 ? 23  PRO B CB  1 
ATOM   1795 C  CG  . PRO B 1 28  ? 0.526   -13.206 10.026  1.00 25.88 ? 23  PRO B CG  1 
ATOM   1796 C  CD  . PRO B 1 28  ? -0.354  -11.958 10.029  1.00 26.38 ? 23  PRO B CD  1 
ATOM   1797 N  N   . LEU B 1 29  ? 0.563   -12.373 13.434  1.00 27.03 ? 24  LEU B N   1 
ATOM   1798 C  CA  . LEU B 1 29  ? 1.322   -12.303 14.702  1.00 27.32 ? 24  LEU B CA  1 
ATOM   1799 C  C   . LEU B 1 29  ? 0.319   -11.872 15.760  1.00 25.16 ? 24  LEU B C   1 
ATOM   1800 O  O   . LEU B 1 29  ? 0.043   -10.656 15.845  1.00 22.08 ? 24  LEU B O   1 
ATOM   1801 C  CB  . LEU B 1 29  ? 2.529   -11.370 14.621  1.00 28.85 ? 24  LEU B CB  1 
ATOM   1802 C  CG  . LEU B 1 29  ? 3.530   -11.612 15.752  1.00 31.31 ? 24  LEU B CG  1 
ATOM   1803 C  CD1 . LEU B 1 29  ? 4.286   -12.900 15.509  1.00 28.88 ? 24  LEU B CD1 1 
ATOM   1804 C  CD2 . LEU B 1 29  ? 4.511   -10.461 15.927  1.00 34.43 ? 24  LEU B CD2 1 
ATOM   1805 N  N   . ALA B 1 30  ? -0.300  -12.881 16.377  1.00 21.94 ? 25  ALA B N   1 
ATOM   1806 C  CA  . ALA B 1 30  ? -1.267  -12.795 17.484  1.00 22.56 ? 25  ALA B CA  1 
ATOM   1807 C  C   . ALA B 1 30  ? -0.536  -12.645 18.824  1.00 23.08 ? 25  ALA B C   1 
ATOM   1808 O  O   . ALA B 1 30  ? 0.590   -13.102 18.958  1.00 21.15 ? 25  ALA B O   1 
ATOM   1809 C  CB  . ALA B 1 30  ? -2.117  -14.042 17.487  1.00 23.67 ? 25  ALA B CB  1 
ATOM   1810 N  N   . GLN B 1 31  ? -1.212  -12.030 19.780  1.00 23.90 ? 26  GLN B N   1 
ATOM   1811 C  CA  . GLN B 1 31  ? -0.912  -12.101 21.231  1.00 23.39 ? 26  GLN B CA  1 
ATOM   1812 C  C   . GLN B 1 31  ? -1.718  -13.258 21.824  1.00 23.13 ? 26  GLN B C   1 
ATOM   1813 O  O   . GLN B 1 31  ? -2.963  -13.154 21.872  1.00 22.63 ? 26  GLN B O   1 
ATOM   1814 C  CB  . GLN B 1 31  ? -1.242  -10.750 21.866  1.00 22.76 ? 26  GLN B CB  1 
ATOM   1815 C  CG  . GLN B 1 31  ? -0.312  -9.648  21.383  1.00 26.44 ? 26  GLN B CG  1 
ATOM   1816 C  CD  . GLN B 1 31  ? -0.489  -8.325  22.094  1.00 24.77 ? 26  GLN B CD  1 
ATOM   1817 O  OE1 . GLN B 1 31  ? -0.849  -8.274  23.261  1.00 28.20 ? 26  GLN B OE1 1 
ATOM   1818 N  NE2 . GLN B 1 31  ? -0.241  -7.245  21.377  1.00 24.26 ? 26  GLN B NE2 1 
ATOM   1819 N  N   . LEU B 1 32  ? -1.033  -14.341 22.187  1.00 22.01 ? 27  LEU B N   1 
ATOM   1820 C  CA  . LEU B 1 32  ? -1.635  -15.548 22.813  1.00 22.87 ? 27  LEU B CA  1 
ATOM   1821 C  C   . LEU B 1 32  ? -1.622  -15.329 24.325  1.00 23.37 ? 27  LEU B C   1 
ATOM   1822 O  O   . LEU B 1 32  ? -0.523  -15.057 24.882  1.00 21.12 ? 27  LEU B O   1 
ATOM   1823 C  CB  . LEU B 1 32  ? -0.826  -16.777 22.422  1.00 21.28 ? 27  LEU B CB  1 
ATOM   1824 C  CG  . LEU B 1 32  ? -1.314  -18.126 22.956  1.00 23.65 ? 27  LEU B CG  1 
ATOM   1825 C  CD1 . LEU B 1 32  ? -2.689  -18.506 22.406  1.00 22.61 ? 27  LEU B CD1 1 
ATOM   1826 C  CD2 . LEU B 1 32  ? -0.291  -19.207 22.624  1.00 25.13 ? 27  LEU B CD2 1 
ATOM   1827 N  N   . ALA B 1 33  ? -2.789  -15.370 24.973  1.00 22.52 ? 28  ALA B N   1 
ATOM   1828 C  CA  . ALA B 1 33  ? -2.876  -15.149 26.429  1.00 22.54 ? 28  ALA B CA  1 
ATOM   1829 C  C   . ALA B 1 33  ? -3.482  -16.377 27.112  1.00 22.64 ? 28  ALA B C   1 
ATOM   1830 O  O   . ALA B 1 33  ? -4.478  -16.923 26.627  1.00 22.59 ? 28  ALA B O   1 
ATOM   1831 C  CB  . ALA B 1 33  ? -3.653  -13.887 26.706  1.00 23.35 ? 28  ALA B CB  1 
ATOM   1832 N  N   . SER B 1 34  ? -2.895  -16.774 28.227  1.00 24.86 ? 29  SER B N   1 
ATOM   1833 C  CA  . SER B 1 34  ? -3.447  -17.798 29.141  1.00 28.52 ? 29  SER B CA  1 
ATOM   1834 C  C   . SER B 1 34  ? -3.290  -17.278 30.565  1.00 30.15 ? 29  SER B C   1 
ATOM   1835 O  O   . SER B 1 34  ? -2.399  -16.421 30.787  1.00 30.79 ? 29  SER B O   1 
ATOM   1836 C  CB  . SER B 1 34  ? -2.768  -19.114 28.948  1.00 27.32 ? 29  SER B CB  1 
ATOM   1837 O  OG  . SER B 1 34  ? -1.377  -18.991 29.171  1.00 27.73 ? 29  SER B OG  1 
ATOM   1838 N  N   . ASN B 1 35  ? -4.112  -17.801 31.475  1.00 30.09 ? 30  ASN B N   1 
ATOM   1839 C  CA  . ASN B 1 35  ? -4.192  -17.352 32.887  1.00 29.98 ? 30  ASN B CA  1 
ATOM   1840 C  C   . ASN B 1 35  ? -2.849  -17.567 33.566  1.00 27.89 ? 30  ASN B C   1 
ATOM   1841 O  O   . ASN B 1 35  ? -2.226  -18.609 33.318  1.00 26.32 ? 30  ASN B O   1 
ATOM   1842 C  CB  . ASN B 1 35  ? -5.264  -18.110 33.666  1.00 31.34 ? 30  ASN B CB  1 
ATOM   1843 C  CG  . ASN B 1 35  ? -6.656  -17.693 33.276  1.00 34.31 ? 30  ASN B CG  1 
ATOM   1844 O  OD1 . ASN B 1 35  ? -6.842  -16.655 32.641  1.00 29.95 ? 30  ASN B OD1 1 
ATOM   1845 N  ND2 . ASN B 1 35  ? -7.632  -18.507 33.655  1.00 37.56 ? 30  ASN B ND2 1 
ATOM   1846 N  N   . GLY B 1 36  ? -2.453  -16.606 34.396  1.00 30.45 ? 31  GLY B N   1 
ATOM   1847 C  CA  . GLY B 1 36  ? -1.278  -16.699 35.276  1.00 35.78 ? 31  GLY B CA  1 
ATOM   1848 C  C   . GLY B 1 36  ? -1.600  -17.541 36.493  1.00 37.30 ? 31  GLY B C   1 
ATOM   1849 O  O   . GLY B 1 36  ? -2.776  -17.535 36.915  1.00 39.12 ? 31  GLY B O   1 
ATOM   1850 N  N   . ALA B 1 37  ? -0.611  -18.269 37.006  1.00 41.65 ? 32  ALA B N   1 
ATOM   1851 C  CA  . ALA B 1 37  ? -0.779  -19.222 38.125  1.00 43.99 ? 32  ALA B CA  1 
ATOM   1852 C  C   . ALA B 1 37  ? -0.922  -18.424 39.418  1.00 47.39 ? 32  ALA B C   1 
ATOM   1853 O  O   . ALA B 1 37  ? -0.155  -17.457 39.582  1.00 48.02 ? 32  ALA B O   1 
ATOM   1854 C  CB  . ALA B 1 37  ? 0.395   -20.165 38.182  1.00 45.56 ? 32  ALA B CB  1 
ATOM   1855 N  N   . GLY B 1 38  ? -1.884  -18.809 40.265  1.00 51.48 ? 33  GLY B N   1 
ATOM   1856 C  CA  . GLY B 1 38  ? -2.094  -18.272 41.626  1.00 50.94 ? 33  GLY B CA  1 
ATOM   1857 C  C   . GLY B 1 38  ? -2.463  -16.797 41.616  1.00 51.79 ? 33  GLY B C   1 
ATOM   1858 O  O   . GLY B 1 38  ? -1.915  -16.048 42.437  1.00 54.59 ? 33  GLY B O   1 
ATOM   1859 N  N   . GLY B 1 39  ? -3.342  -16.383 40.704  1.00 50.09 ? 34  GLY B N   1 
ATOM   1860 C  CA  . GLY B 1 39  ? -3.810  -14.989 40.595  1.00 48.96 ? 34  GLY B CA  1 
ATOM   1861 C  C   . GLY B 1 39  ? -2.771  -14.046 39.994  1.00 45.08 ? 34  GLY B C   1 
ATOM   1862 O  O   . GLY B 1 39  ? -3.017  -12.835 40.022  1.00 48.14 ? 34  GLY B O   1 
ATOM   1863 N  N   . ALA B 1 40  ? -1.648  -14.542 39.468  1.00 44.29 ? 35  ALA B N   1 
ATOM   1864 C  CA  . ALA B 1 40  ? -0.661  -13.698 38.749  1.00 42.09 ? 35  ALA B CA  1 
ATOM   1865 C  C   . ALA B 1 40  ? -1.311  -13.183 37.451  1.00 38.92 ? 35  ALA B C   1 
ATOM   1866 O  O   . ALA B 1 40  ? -2.350  -13.716 37.031  1.00 37.18 ? 35  ALA B O   1 
ATOM   1867 C  CB  . ALA B 1 40  ? 0.612   -14.465 38.492  1.00 42.79 ? 35  ALA B CB  1 
ATOM   1868 N  N   . ALA B 1 41  ? -0.756  -12.132 36.861  1.00 36.56 ? 36  ALA B N   1 
ATOM   1869 C  CA  . ALA B 1 41  ? -1.223  -11.585 35.566  1.00 33.41 ? 36  ALA B CA  1 
ATOM   1870 C  C   . ALA B 1 41  ? -1.100  -12.665 34.487  1.00 30.44 ? 36  ALA B C   1 
ATOM   1871 O  O   . ALA B 1 41  ? -0.278  -13.584 34.595  1.00 24.28 ? 36  ALA B O   1 
ATOM   1872 C  CB  . ALA B 1 41  ? -0.421  -10.355 35.226  1.00 32.12 ? 36  ALA B CB  1 
ATOM   1873 N  N   . PRO B 1 42  ? -1.924  -12.608 33.420  1.00 27.19 ? 37  PRO B N   1 
ATOM   1874 C  CA  . PRO B 1 42  ? -1.771  -13.533 32.300  1.00 26.72 ? 37  PRO B CA  1 
ATOM   1875 C  C   . PRO B 1 42  ? -0.366  -13.515 31.688  1.00 26.83 ? 37  PRO B C   1 
ATOM   1876 O  O   . PRO B 1 42  ? 0.309   -12.478 31.750  1.00 24.76 ? 37  PRO B O   1 
ATOM   1877 C  CB  . PRO B 1 42  ? -2.849  -13.066 31.320  1.00 24.99 ? 37  PRO B CB  1 
ATOM   1878 C  CG  . PRO B 1 42  ? -3.926  -12.497 32.231  1.00 24.75 ? 37  PRO B CG  1 
ATOM   1879 C  CD  . PRO B 1 42  ? -3.109  -11.748 33.264  1.00 25.96 ? 37  PRO B CD  1 
ATOM   1880 N  N   . HIS B 1 43  ? 0.036   -14.684 31.167  1.00 27.15 ? 38  HIS B N   1 
ATOM   1881 C  CA  . HIS B 1 43  ? 1.131   -14.863 30.176  1.00 26.79 ? 38  HIS B CA  1 
ATOM   1882 C  C   . HIS B 1 43  ? 0.640   -14.344 28.823  1.00 24.27 ? 38  HIS B C   1 
ATOM   1883 O  O   . HIS B 1 43  ? -0.531  -14.600 28.466  1.00 22.21 ? 38  HIS B O   1 
ATOM   1884 C  CB  . HIS B 1 43  ? 1.579   -16.330 30.056  1.00 28.66 ? 38  HIS B CB  1 
ATOM   1885 C  CG  . HIS B 1 43  ? 1.982   -16.966 31.344  1.00 31.44 ? 38  HIS B CG  1 
ATOM   1886 N  ND1 . HIS B 1 43  ? 3.274   -16.934 31.808  1.00 39.97 ? 38  HIS B ND1 1 
ATOM   1887 C  CD2 . HIS B 1 43  ? 1.275   -17.698 32.234  1.00 35.70 ? 38  HIS B CD2 1 
ATOM   1888 C  CE1 . HIS B 1 43  ? 3.345   -17.582 32.961  1.00 40.65 ? 38  HIS B CE1 1 
ATOM   1889 N  NE2 . HIS B 1 43  ? 2.125   -18.068 33.239  1.00 37.24 ? 38  HIS B NE2 1 
ATOM   1890 N  N   . ILE B 1 44  ? 1.522   -13.643 28.113  1.00 22.52 ? 39  ILE B N   1 
ATOM   1891 C  CA  . ILE B 1 44  ? 1.316   -13.018 26.775  1.00 20.15 ? 39  ILE B CA  1 
ATOM   1892 C  C   . ILE B 1 44  ? 2.547   -13.370 25.937  1.00 22.18 ? 39  ILE B C   1 
ATOM   1893 O  O   . ILE B 1 44  ? 3.666   -13.050 26.412  1.00 20.46 ? 39  ILE B O   1 
ATOM   1894 C  CB  . ILE B 1 44  ? 1.168   -11.481 26.883  1.00 21.31 ? 39  ILE B CB  1 
ATOM   1895 C  CG1 . ILE B 1 44  ? 0.114   -11.068 27.903  1.00 20.32 ? 39  ILE B CG1 1 
ATOM   1896 C  CG2 . ILE B 1 44  ? 0.910   -10.855 25.516  1.00 21.10 ? 39  ILE B CG2 1 
ATOM   1897 C  CD1 . ILE B 1 44  ? -1.268  -11.441 27.499  1.00 25.04 ? 39  ILE B CD1 1 
ATOM   1898 N  N   . THR B 1 45  ? 2.353   -14.021 24.784  1.00 20.82 ? 40  THR B N   1 
ATOM   1899 C  CA  . THR B 1 45  ? 3.422   -14.252 23.778  1.00 23.99 ? 40  THR B CA  1 
ATOM   1900 C  C   . THR B 1 45  ? 2.894   -13.924 22.392  1.00 22.18 ? 40  THR B C   1 
ATOM   1901 O  O   . THR B 1 45  ? 1.758   -14.363 22.059  1.00 21.73 ? 40  THR B O   1 
ATOM   1902 C  CB  . THR B 1 45  ? 3.962   -15.685 23.779  1.00 24.41 ? 40  THR B CB  1 
ATOM   1903 O  OG1 . THR B 1 45  ? 4.327   -16.034 25.121  1.00 25.49 ? 40  THR B OG1 1 
ATOM   1904 C  CG2 . THR B 1 45  ? 5.157   -15.819 22.872  1.00 24.57 ? 40  THR B CG2 1 
ATOM   1905 N  N   . HIS B 1 46  ? 3.681   -13.135 21.666  1.00 22.60 ? 41  HIS B N   1 
ATOM   1906 C  CA  . HIS B 1 46  ? 3.549   -12.861 20.212  1.00 24.50 ? 41  HIS B CA  1 
ATOM   1907 C  C   . HIS B 1 46  ? 3.927   -14.115 19.435  1.00 23.65 ? 41  HIS B C   1 
ATOM   1908 O  O   . HIS B 1 46  ? 5.126   -14.448 19.466  1.00 19.22 ? 41  HIS B O   1 
ATOM   1909 C  CB  . HIS B 1 46  ? 4.413   -11.662 19.790  1.00 25.28 ? 41  HIS B CB  1 
ATOM   1910 C  CG  . HIS B 1 46  ? 3.759   -10.385 20.168  1.00 29.76 ? 41  HIS B CG  1 
ATOM   1911 N  ND1 . HIS B 1 46  ? 4.048   -9.730  21.349  1.00 32.44 ? 41  HIS B ND1 1 
ATOM   1912 C  CD2 . HIS B 1 46  ? 2.758   -9.695  19.573  1.00 35.53 ? 41  HIS B CD2 1 
ATOM   1913 C  CE1 . HIS B 1 46  ? 3.272   -8.664  21.446  1.00 35.52 ? 41  HIS B CE1 1 
ATOM   1914 N  NE2 . HIS B 1 46  ? 2.488   -8.607  20.357  1.00 34.08 ? 41  HIS B NE2 1 
ATOM   1915 N  N   . VAL B 1 47  ? 2.942   -14.770 18.808  1.00 21.91 ? 42  VAL B N   1 
ATOM   1916 C  CA  . VAL B 1 47  ? 3.141   -16.049 18.062  1.00 23.66 ? 42  VAL B CA  1 
ATOM   1917 C  C   . VAL B 1 47  ? 2.549   -15.929 16.661  1.00 24.32 ? 42  VAL B C   1 
ATOM   1918 O  O   . VAL B 1 47  ? 1.492   -15.318 16.487  1.00 26.92 ? 42  VAL B O   1 
ATOM   1919 C  CB  . VAL B 1 47  ? 2.564   -17.263 18.818  1.00 23.60 ? 42  VAL B CB  1 
ATOM   1920 C  CG1 . VAL B 1 47  ? 3.428   -17.594 20.023  1.00 25.21 ? 42  VAL B CG1 1 
ATOM   1921 C  CG2 . VAL B 1 47  ? 1.116   -17.091 19.252  1.00 23.04 ? 42  VAL B CG2 1 
ATOM   1922 N  N   . PRO B 1 48  ? 3.159   -16.561 15.625  1.00 23.67 ? 43  PRO B N   1 
ATOM   1923 C  CA  . PRO B 1 48  ? 2.531   -16.639 14.311  1.00 23.98 ? 43  PRO B CA  1 
ATOM   1924 C  C   . PRO B 1 48  ? 1.410   -17.687 14.258  1.00 22.40 ? 43  PRO B C   1 
ATOM   1925 O  O   . PRO B 1 48  ? 1.689   -18.843 14.465  1.00 21.18 ? 43  PRO B O   1 
ATOM   1926 C  CB  . PRO B 1 48  ? 3.659   -17.035 13.357  1.00 22.94 ? 43  PRO B CB  1 
ATOM   1927 C  CG  . PRO B 1 48  ? 4.622   -17.801 14.238  1.00 24.12 ? 43  PRO B CG  1 
ATOM   1928 C  CD  . PRO B 1 48  ? 4.505   -17.157 15.614  1.00 25.31 ? 43  PRO B CD  1 
ATOM   1929 N  N   . ILE B 1 49  ? 0.193   -17.257 13.899  1.00 22.62 ? 44  ILE B N   1 
ATOM   1930 C  CA  . ILE B 1 49  ? -0.984  -18.150 13.825  1.00 23.74 ? 44  ILE B CA  1 
ATOM   1931 C  C   . ILE B 1 49  ? -1.581  -18.015 12.420  1.00 24.85 ? 44  ILE B C   1 
ATOM   1932 O  O   . ILE B 1 49  ? -1.719  -16.869 11.949  1.00 27.49 ? 44  ILE B O   1 
ATOM   1933 C  CB  . ILE B 1 49  ? -1.997  -17.833 14.935  1.00 25.02 ? 44  ILE B CB  1 
ATOM   1934 C  CG1 . ILE B 1 49  ? -1.399  -18.090 16.324  1.00 27.07 ? 44  ILE B CG1 1 
ATOM   1935 C  CG2 . ILE B 1 49  ? -3.269  -18.641 14.708  1.00 24.97 ? 44  ILE B CG2 1 
ATOM   1936 C  CD1 . ILE B 1 49  ? -2.321  -17.740 17.488  1.00 26.39 ? 44  ILE B CD1 1 
ATOM   1937 N  N   . ILE B 1 50  ? -1.926  -19.155 11.810  1.00 22.08 ? 45  ILE B N   1 
ATOM   1938 C  CA  . ILE B 1 50  ? -2.578  -19.279 10.469  1.00 23.56 ? 45  ILE B CA  1 
ATOM   1939 C  C   . ILE B 1 50  ? -3.833  -20.152 10.589  1.00 23.48 ? 45  ILE B C   1 
ATOM   1940 O  O   . ILE B 1 50  ? -3.924  -21.000 11.500  1.00 20.97 ? 45  ILE B O   1 
ATOM   1941 C  CB  . ILE B 1 50  ? -1.590  -19.853 9.437   1.00 23.47 ? 45  ILE B CB  1 
ATOM   1942 C  CG1 . ILE B 1 50  ? -1.179  -21.281 9.808   1.00 25.87 ? 45  ILE B CG1 1 
ATOM   1943 C  CG2 . ILE B 1 50  ? -0.378  -18.930 9.309   1.00 23.84 ? 45  ILE B CG2 1 
ATOM   1944 C  CD1 . ILE B 1 50  ? -0.400  -22.014 8.742   1.00 26.73 ? 45  ILE B CD1 1 
ATOM   1945 N  N   . VAL B 1 51  ? -4.758  -19.969 9.660   1.00 25.00 ? 46  VAL B N   1 
ATOM   1946 C  CA  . VAL B 1 51  ? -5.914  -20.890 9.459   1.00 27.84 ? 46  VAL B CA  1 
ATOM   1947 C  C   . VAL B 1 51  ? -5.363  -22.238 8.984   1.00 26.67 ? 46  VAL B C   1 
ATOM   1948 O  O   . VAL B 1 51  ? -4.354  -22.250 8.235   1.00 30.19 ? 46  VAL B O   1 
ATOM   1949 C  CB  . VAL B 1 51  ? -6.940  -20.297 8.474   1.00 29.83 ? 46  VAL B CB  1 
ATOM   1950 C  CG1 . VAL B 1 51  ? -7.994  -21.323 8.072   1.00 30.90 ? 46  VAL B CG1 1 
ATOM   1951 C  CG2 . VAL B 1 51  ? -7.580  -19.042 9.053   1.00 29.56 ? 46  VAL B CG2 1 
ATOM   1952 N  N   . ASP B 1 52  ? -5.899  -23.326 9.543   1.00 27.35 ? 47  ASP B N   1 
ATOM   1953 C  CA  . ASP B 1 52  ? -5.721  -24.719 9.051   1.00 29.64 ? 47  ASP B CA  1 
ATOM   1954 C  C   . ASP B 1 52  ? -5.452  -24.695 7.544   1.00 29.23 ? 47  ASP B C   1 
ATOM   1955 O  O   . ASP B 1 52  ? -6.353  -24.402 6.760   1.00 24.94 ? 47  ASP B O   1 
ATOM   1956 C  CB  . ASP B 1 52  ? -6.988  -25.516 9.398   1.00 32.25 ? 47  ASP B CB  1 
ATOM   1957 C  CG  . ASP B 1 52  ? -6.957  -27.003 9.064   1.00 34.19 ? 47  ASP B CG  1 
ATOM   1958 O  OD1 . ASP B 1 52  ? -5.952  -27.479 8.501   1.00 30.09 ? 47  ASP B OD1 1 
ATOM   1959 O  OD2 . ASP B 1 52  ? -7.959  -27.665 9.371   1.00 34.51 ? 47  ASP B OD2 1 
ATOM   1960 N  N   . PRO B 1 53  ? -4.217  -24.995 7.082   1.00 30.31 ? 48  PRO B N   1 
ATOM   1961 C  CA  . PRO B 1 53  ? -3.903  -24.932 5.659   1.00 33.83 ? 48  PRO B CA  1 
ATOM   1962 C  C   . PRO B 1 53  ? -4.485  -26.112 4.868   1.00 36.19 ? 48  PRO B C   1 
ATOM   1963 O  O   . PRO B 1 53  ? -4.460  -26.041 3.658   1.00 36.91 ? 48  PRO B O   1 
ATOM   1964 C  CB  . PRO B 1 53  ? -2.372  -25.014 5.648   1.00 36.20 ? 48  PRO B CB  1 
ATOM   1965 C  CG  . PRO B 1 53  ? -2.067  -25.891 6.840   1.00 32.90 ? 48  PRO B CG  1 
ATOM   1966 C  CD  . PRO B 1 53  ? -3.069  -25.439 7.880   1.00 32.35 ? 48  PRO B CD  1 
ATOM   1967 N  N   . GLU B 1 54  ? -4.987  -27.149 5.549   1.00 38.59 ? 49  GLU B N   1 
ATOM   1968 C  CA  . GLU B 1 54  ? -5.673  -28.306 4.902   1.00 43.91 ? 49  GLU B CA  1 
ATOM   1969 C  C   . GLU B 1 54  ? -7.110  -27.922 4.527   1.00 44.85 ? 49  GLU B C   1 
ATOM   1970 O  O   . GLU B 1 54  ? -7.753  -28.737 3.853   1.00 44.49 ? 49  GLU B O   1 
ATOM   1971 C  CB  . GLU B 1 54  ? -5.734  -29.557 5.791   1.00 46.97 ? 49  GLU B CB  1 
ATOM   1972 C  CG  . GLU B 1 54  ? -4.400  -30.033 6.351   1.00 53.64 ? 49  GLU B CG  1 
ATOM   1973 C  CD  . GLU B 1 54  ? -3.348  -30.458 5.341   1.00 58.05 ? 49  GLU B CD  1 
ATOM   1974 O  OE1 . GLU B 1 54  ? -2.151  -30.421 5.703   1.00 68.90 ? 49  GLU B OE1 1 
ATOM   1975 O  OE2 . GLU B 1 54  ? -3.718  -30.829 4.207   1.00 59.15 ? 49  GLU B OE2 1 
ATOM   1976 N  N   . LEU B 1 55  ? -7.618  -26.765 4.972   1.00 47.33 ? 50  LEU B N   1 
ATOM   1977 C  CA  . LEU B 1 55  ? -8.976  -26.287 4.589   1.00 48.96 ? 50  LEU B CA  1 
ATOM   1978 C  C   . LEU B 1 55  ? -8.948  -25.848 3.121   1.00 54.44 ? 50  LEU B C   1 
ATOM   1979 O  O   . LEU B 1 55  ? -8.208  -24.900 2.788   1.00 54.08 ? 50  LEU B O   1 
ATOM   1980 C  CB  . LEU B 1 55  ? -9.440  -25.138 5.494   1.00 48.85 ? 50  LEU B CB  1 
ATOM   1981 C  CG  . LEU B 1 55  ? -9.950  -25.530 6.881   1.00 47.36 ? 50  LEU B CG  1 
ATOM   1982 C  CD1 . LEU B 1 55  ? -10.523 -24.310 7.592   1.00 45.96 ? 50  LEU B CD1 1 
ATOM   1983 C  CD2 . LEU B 1 55  ? -11.000 -26.632 6.805   1.00 47.55 ? 50  LEU B CD2 1 
ATOM   1984 N  N   . ASP B 1 56  ? -9.732  -26.530 2.287   1.00 59.94 ? 51  ASP B N   1 
ATOM   1985 C  CA  . ASP B 1 56  ? -9.920  -26.226 0.845   1.00 63.63 ? 51  ASP B CA  1 
ATOM   1986 C  C   . ASP B 1 56  ? -11.282 -25.540 0.679   1.00 64.49 ? 51  ASP B C   1 
ATOM   1987 O  O   . ASP B 1 56  ? -12.262 -25.986 1.319   1.00 70.42 ? 51  ASP B O   1 
ATOM   1988 C  CB  . ASP B 1 56  ? -9.782  -27.496 -0.002  1.00 66.17 ? 51  ASP B CB  1 
ATOM   1989 C  CG  . ASP B 1 56  ? -8.349  -27.997 -0.129  1.00 69.11 ? 51  ASP B CG  1 
ATOM   1990 O  OD1 . ASP B 1 56  ? -7.857  -28.641 0.828   1.00 67.10 ? 51  ASP B OD1 1 
ATOM   1991 O  OD2 . ASP B 1 56  ? -7.726  -27.730 -1.179  1.00 71.78 ? 51  ASP B OD2 1 
ATOM   1992 N  N   . GLY B 1 57  ? -11.327 -24.481 -0.127  1.00 60.28 ? 52  GLY B N   1 
ATOM   1993 C  CA  . GLY B 1 57  ? -12.543 -23.686 -0.370  1.00 59.03 ? 52  GLY B CA  1 
ATOM   1994 C  C   . GLY B 1 57  ? -12.656 -22.532 0.620   1.00 55.71 ? 52  GLY B C   1 
ATOM   1995 O  O   . GLY B 1 57  ? -11.941 -22.491 1.624   1.00 53.10 ? 52  GLY B O   1 
ATOM   1996 N  N   . PRO B 1 58  ? -13.547 -21.553 0.352   1.00 52.88 ? 53  PRO B N   1 
ATOM   1997 C  CA  . PRO B 1 58  ? -13.651 -20.354 1.187   1.00 49.80 ? 53  PRO B CA  1 
ATOM   1998 C  C   . PRO B 1 58  ? -13.881 -20.677 2.672   1.00 46.70 ? 53  PRO B C   1 
ATOM   1999 O  O   . PRO B 1 58  ? -14.675 -21.537 2.980   1.00 43.87 ? 53  PRO B O   1 
ATOM   2000 C  CB  . PRO B 1 58  ? -14.849 -19.589 0.601   1.00 52.36 ? 53  PRO B CB  1 
ATOM   2001 C  CG  . PRO B 1 58  ? -14.946 -20.092 -0.834  1.00 53.13 ? 53  PRO B CG  1 
ATOM   2002 C  CD  . PRO B 1 58  ? -14.485 -21.536 -0.783  1.00 51.85 ? 53  PRO B CD  1 
ATOM   2003 N  N   . VAL B 1 59  ? -13.132 -19.996 3.542   1.00 42.57 ? 54  VAL B N   1 
ATOM   2004 C  CA  . VAL B 1 59  ? -13.272 -20.039 5.026   1.00 41.90 ? 54  VAL B CA  1 
ATOM   2005 C  C   . VAL B 1 59  ? -14.035 -18.770 5.409   1.00 41.91 ? 54  VAL B C   1 
ATOM   2006 O  O   . VAL B 1 59  ? -13.424 -17.689 5.398   1.00 43.02 ? 54  VAL B O   1 
ATOM   2007 C  CB  . VAL B 1 59  ? -11.891 -20.138 5.711   1.00 39.81 ? 54  VAL B CB  1 
ATOM   2008 C  CG1 . VAL B 1 59  ? -11.992 -20.216 7.226   1.00 38.25 ? 54  VAL B CG1 1 
ATOM   2009 C  CG2 . VAL B 1 59  ? -11.087 -21.316 5.180   1.00 40.90 ? 54  VAL B CG2 1 
ATOM   2010 N  N   . ASP B 1 60  ? -15.334 -18.897 5.680   1.00 45.92 ? 55  ASP B N   1 
ATOM   2011 C  CA  . ASP B 1 60  ? -16.246 -17.751 5.939   1.00 45.76 ? 55  ASP B CA  1 
ATOM   2012 C  C   . ASP B 1 60  ? -16.290 -17.446 7.442   1.00 44.05 ? 55  ASP B C   1 
ATOM   2013 O  O   . ASP B 1 60  ? -16.448 -16.261 7.770   1.00 44.99 ? 55  ASP B O   1 
ATOM   2014 C  CB  . ASP B 1 60  ? -17.640 -18.026 5.369   1.00 51.09 ? 55  ASP B CB  1 
ATOM   2015 C  CG  . ASP B 1 60  ? -17.757 -17.742 3.878   1.00 55.52 ? 55  ASP B CG  1 
ATOM   2016 O  OD1 . ASP B 1 60  ? -16.716 -17.475 3.242   1.00 56.71 ? 55  ASP B OD1 1 
ATOM   2017 O  OD2 . ASP B 1 60  ? -18.893 -17.779 3.365   1.00 61.87 ? 55  ASP B OD2 1 
ATOM   2018 N  N   . ARG B 1 61  ? -16.135 -18.462 8.304   1.00 40.41 ? 56  ARG B N   1 
ATOM   2019 C  CA  . ARG B 1 61  ? -16.310 -18.359 9.783   1.00 41.09 ? 56  ARG B CA  1 
ATOM   2020 C  C   . ARG B 1 61  ? -15.105 -18.956 10.517  1.00 35.40 ? 56  ARG B C   1 
ATOM   2021 O  O   . ARG B 1 61  ? -14.609 -20.022 10.103  1.00 32.74 ? 56  ARG B O   1 
ATOM   2022 C  CB  . ARG B 1 61  ? -17.562 -19.113 10.238  1.00 43.41 ? 56  ARG B CB  1 
ATOM   2023 C  CG  . ARG B 1 61  ? -18.816 -18.257 10.233  1.00 50.77 ? 56  ARG B CG  1 
ATOM   2024 C  CD  . ARG B 1 61  ? -20.056 -19.069 10.546  1.00 55.20 ? 56  ARG B CD  1 
ATOM   2025 N  NE  . ARG B 1 61  ? -20.094 -20.296 9.761   1.00 62.69 ? 56  ARG B NE  1 
ATOM   2026 C  CZ  . ARG B 1 61  ? -20.389 -20.385 8.460   1.00 61.67 ? 56  ARG B CZ  1 
ATOM   2027 N  NH1 . ARG B 1 61  ? -20.384 -21.570 7.869   1.00 66.58 ? 56  ARG B NH1 1 
ATOM   2028 N  NH2 . ARG B 1 61  ? -20.688 -19.310 7.752   1.00 62.52 ? 56  ARG B NH2 1 
ATOM   2029 N  N   . LEU B 1 62  ? -14.694 -18.325 11.616  1.00 32.44 ? 57  LEU B N   1 
ATOM   2030 C  CA  . LEU B 1 62  ? -13.605 -18.840 12.479  1.00 31.54 ? 57  LEU B CA  1 
ATOM   2031 C  C   . LEU B 1 62  ? -14.152 -19.904 13.448  1.00 31.03 ? 57  LEU B C   1 
ATOM   2032 O  O   . LEU B 1 62  ? -13.401 -20.810 13.742  1.00 31.71 ? 57  LEU B O   1 
ATOM   2033 C  CB  . LEU B 1 62  ? -12.956 -17.675 13.231  1.00 30.91 ? 57  LEU B CB  1 
ATOM   2034 C  CG  . LEU B 1 62  ? -12.009 -16.808 12.409  1.00 30.29 ? 57  LEU B CG  1 
ATOM   2035 C  CD1 . LEU B 1 62  ? -11.500 -15.651 13.247  1.00 29.38 ? 57  LEU B CD1 1 
ATOM   2036 C  CD2 . LEU B 1 62  ? -10.843 -17.610 11.853  1.00 31.14 ? 57  LEU B CD2 1 
ATOM   2037 N  N   . VAL B 1 63  ? -15.396 -19.807 13.936  1.00 30.94 ? 58  VAL B N   1 
ATOM   2038 C  CA  . VAL B 1 63  ? -15.956 -20.805 14.909  1.00 32.40 ? 58  VAL B CA  1 
ATOM   2039 C  C   . VAL B 1 63  ? -16.055 -22.173 14.223  1.00 30.44 ? 58  VAL B C   1 
ATOM   2040 O  O   . VAL B 1 63  ? -16.569 -22.236 13.102  1.00 32.86 ? 58  VAL B O   1 
ATOM   2041 C  CB  . VAL B 1 63  ? -17.308 -20.363 15.505  1.00 32.18 ? 58  VAL B CB  1 
ATOM   2042 C  CG1 . VAL B 1 63  ? -18.042 -21.514 16.182  1.00 32.59 ? 58  VAL B CG1 1 
ATOM   2043 C  CG2 . VAL B 1 63  ? -17.127 -19.221 16.490  1.00 33.75 ? 58  VAL B CG2 1 
ATOM   2044 N  N   . GLY B 1 64  ? -15.541 -23.222 14.862  1.00 34.44 ? 59  GLY B N   1 
ATOM   2045 C  CA  . GLY B 1 64  ? -15.556 -24.604 14.329  1.00 36.78 ? 59  GLY B CA  1 
ATOM   2046 C  C   . GLY B 1 64  ? -14.229 -25.030 13.702  1.00 38.38 ? 59  GLY B C   1 
ATOM   2047 O  O   . GLY B 1 64  ? -13.982 -26.241 13.645  1.00 46.92 ? 59  GLY B O   1 
ATOM   2048 N  N   . ILE B 1 65  ? -13.395 -24.096 13.235  1.00 37.91 ? 60  ILE B N   1 
ATOM   2049 C  CA  . ILE B 1 65  ? -12.131 -24.427 12.511  1.00 37.37 ? 60  ILE B CA  1 
ATOM   2050 C  C   . ILE B 1 65  ? -10.962 -24.428 13.505  1.00 32.70 ? 60  ILE B C   1 
ATOM   2051 O  O   . ILE B 1 65  ? -11.115 -23.938 14.646  1.00 31.86 ? 60  ILE B O   1 
ATOM   2052 C  CB  . ILE B 1 65  ? -11.909 -23.489 11.298  1.00 42.78 ? 60  ILE B CB  1 
ATOM   2053 C  CG1 . ILE B 1 65  ? -11.558 -22.053 11.701  1.00 42.84 ? 60  ILE B CG1 1 
ATOM   2054 C  CG2 . ILE B 1 65  ? -13.113 -23.517 10.362  1.00 44.42 ? 60  ILE B CG2 1 
ATOM   2055 C  CD1 . ILE B 1 65  ? -10.096 -21.720 11.573  1.00 47.43 ? 60  ILE B CD1 1 
ATOM   2056 N  N   . THR B 1 66  ? -9.824  -24.971 13.080  1.00 30.01 ? 61  THR B N   1 
ATOM   2057 C  CA  . THR B 1 66  ? -8.607  -25.128 13.906  1.00 30.59 ? 61  THR B CA  1 
ATOM   2058 C  C   . THR B 1 66  ? -7.548  -24.165 13.383  1.00 30.16 ? 61  THR B C   1 
ATOM   2059 O  O   . THR B 1 66  ? -7.384  -24.096 12.156  1.00 25.90 ? 61  THR B O   1 
ATOM   2060 C  CB  . THR B 1 66  ? -8.131  -26.584 13.918  1.00 31.51 ? 61  THR B CB  1 
ATOM   2061 O  OG1 . THR B 1 66  ? -9.139  -27.285 14.644  1.00 32.13 ? 61  THR B OG1 1 
ATOM   2062 C  CG2 . THR B 1 66  ? -6.791  -26.780 14.587  1.00 30.96 ? 61  THR B CG2 1 
ATOM   2063 N  N   . LEU B 1 67  ? -6.921  -23.408 14.291  1.00 28.05 ? 62  LEU B N   1 
ATOM   2064 C  CA  . LEU B 1 67  ? -5.797  -22.513 13.945  1.00 27.46 ? 62  LEU B CA  1 
ATOM   2065 C  C   . LEU B 1 67  ? -4.514  -23.245 14.332  1.00 27.04 ? 62  LEU B C   1 
ATOM   2066 O  O   . LEU B 1 67  ? -4.558  -24.041 15.281  1.00 28.86 ? 62  LEU B O   1 
ATOM   2067 C  CB  . LEU B 1 67  ? -5.931  -21.158 14.643  1.00 26.60 ? 62  LEU B CB  1 
ATOM   2068 C  CG  . LEU B 1 67  ? -7.211  -20.366 14.368  1.00 27.99 ? 62  LEU B CG  1 
ATOM   2069 C  CD1 . LEU B 1 67  ? -7.148  -19.019 15.061  1.00 30.54 ? 62  LEU B CD1 1 
ATOM   2070 C  CD2 . LEU B 1 67  ? -7.445  -20.154 12.892  1.00 28.30 ? 62  LEU B CD2 1 
ATOM   2071 N  N   . TRP B 1 68  ? -3.454  -23.017 13.558  1.00 26.14 ? 63  TRP B N   1 
ATOM   2072 C  CA  . TRP B 1 68  ? -2.099  -23.593 13.740  1.00 26.80 ? 63  TRP B CA  1 
ATOM   2073 C  C   . TRP B 1 68  ? -1.169  -22.477 14.178  1.00 25.82 ? 63  TRP B C   1 
ATOM   2074 O  O   . TRP B 1 68  ? -1.243  -21.400 13.567  1.00 25.38 ? 63  TRP B O   1 
ATOM   2075 C  CB  . TRP B 1 68  ? -1.558  -24.177 12.442  1.00 27.42 ? 63  TRP B CB  1 
ATOM   2076 C  CG  . TRP B 1 68  ? -2.237  -25.405 11.945  1.00 29.26 ? 63  TRP B CG  1 
ATOM   2077 C  CD1 . TRP B 1 68  ? -3.520  -25.802 12.166  1.00 31.10 ? 63  TRP B CD1 1 
ATOM   2078 C  CD2 . TRP B 1 68  ? -1.663  -26.367 11.044  1.00 30.06 ? 63  TRP B CD2 1 
ATOM   2079 N  NE1 . TRP B 1 68  ? -3.773  -26.958 11.486  1.00 33.04 ? 63  TRP B NE1 1 
ATOM   2080 C  CE2 . TRP B 1 68  ? -2.657  -27.335 10.790  1.00 32.46 ? 63  TRP B CE2 1 
ATOM   2081 C  CE3 . TRP B 1 68  ? -0.412  -26.505 10.443  1.00 28.74 ? 63  TRP B CE3 1 
ATOM   2082 C  CZ2 . TRP B 1 68  ? -2.429  -28.442 9.968   1.00 33.73 ? 63  TRP B CZ2 1 
ATOM   2083 C  CZ3 . TRP B 1 68  ? -0.182  -27.593 9.629   1.00 31.80 ? 63  TRP B CZ3 1 
ATOM   2084 C  CH2 . TRP B 1 68  ? -1.177  -28.548 9.397   1.00 33.91 ? 63  TRP B CH2 1 
ATOM   2085 N  N   . GLY B 1 69  ? -0.298  -22.750 15.144  1.00 25.59 ? 64  GLY B N   1 
ATOM   2086 C  CA  . GLY B 1 69  ? 0.710   -21.774 15.594  1.00 26.15 ? 64  GLY B CA  1 
ATOM   2087 C  C   . GLY B 1 69  ? 1.957   -22.460 16.097  1.00 25.07 ? 64  GLY B C   1 
ATOM   2088 O  O   . GLY B 1 69  ? 1.956   -23.704 16.238  1.00 30.26 ? 64  GLY B O   1 
ATOM   2089 N  N   . HIS B 1 70  ? 3.024   -21.700 16.324  1.00 24.76 ? 65  HIS B N   1 
ATOM   2090 C  CA  . HIS B 1 70  ? 4.169   -22.184 17.136  1.00 23.12 ? 65  HIS B CA  1 
ATOM   2091 C  C   . HIS B 1 70  ? 4.693   -21.085 18.027  1.00 23.24 ? 65  HIS B C   1 
ATOM   2092 O  O   . HIS B 1 70  ? 4.453   -19.898 17.771  1.00 21.25 ? 65  HIS B O   1 
ATOM   2093 C  CB  . HIS B 1 70  ? 5.309   -22.756 16.296  1.00 23.21 ? 65  HIS B CB  1 
ATOM   2094 C  CG  . HIS B 1 70  ? 6.081   -21.771 15.492  1.00 19.58 ? 65  HIS B CG  1 
ATOM   2095 N  ND1 . HIS B 1 70  ? 5.562   -21.210 14.345  1.00 22.42 ? 65  HIS B ND1 1 
ATOM   2096 C  CD2 . HIS B 1 70  ? 7.387   -21.399 15.533  1.00 22.11 ? 65  HIS B CD2 1 
ATOM   2097 C  CE1 . HIS B 1 70  ? 6.489   -20.455 13.755  1.00 23.36 ? 65  HIS B CE1 1 
ATOM   2098 N  NE2 . HIS B 1 70  ? 7.627   -20.550 14.458  1.00 20.12 ? 65  HIS B NE2 1 
ATOM   2099 N  N   . MET B 1 71  ? 5.441   -21.516 19.020  1.00 23.86 ? 66  MET B N   1 
ATOM   2100 C  CA  . MET B 1 71  ? 6.205   -20.616 19.896  1.00 24.85 ? 66  MET B CA  1 
ATOM   2101 C  C   . MET B 1 71  ? 7.487   -21.346 20.270  1.00 22.77 ? 66  MET B C   1 
ATOM   2102 O  O   . MET B 1 71  ? 7.696   -22.449 19.747  1.00 23.34 ? 66  MET B O   1 
ATOM   2103 C  CB  . MET B 1 71  ? 5.398   -20.285 21.155  1.00 26.79 ? 66  MET B CB  1 
ATOM   2104 C  CG  . MET B 1 71  ? 4.994   -21.480 21.977  1.00 29.00 ? 66  MET B CG  1 
ATOM   2105 S  SD  . MET B 1 71  ? 4.214   -20.975 23.515  1.00 36.54 ? 66  MET B SD  1 
ATOM   2106 C  CE  . MET B 1 71  ? 5.180   -19.569 24.019  1.00 41.34 ? 66  MET B CE  1 
ATOM   2107 N  N   . ASN B 1 72  ? 8.276   -20.728 21.125  1.00 20.58 ? 67  ASN B N   1 
ATOM   2108 C  CA  . ASN B 1 72  ? 9.571   -21.252 21.620  1.00 24.56 ? 67  ASN B CA  1 
ATOM   2109 C  C   . ASN B 1 72  ? 9.298   -22.204 22.782  1.00 23.41 ? 67  ASN B C   1 
ATOM   2110 O  O   . ASN B 1 72  ? 8.708   -21.768 23.804  1.00 22.66 ? 67  ASN B O   1 
ATOM   2111 C  CB  . ASN B 1 72  ? 10.517  -20.115 22.016  1.00 23.43 ? 67  ASN B CB  1 
ATOM   2112 C  CG  . ASN B 1 72  ? 11.914  -20.618 22.275  1.00 28.59 ? 67  ASN B CG  1 
ATOM   2113 O  OD1 . ASN B 1 72  ? 12.122  -21.829 22.457  1.00 26.14 ? 67  ASN B OD1 1 
ATOM   2114 N  ND2 . ASN B 1 72  ? 12.869  -19.697 22.259  1.00 25.82 ? 67  ASN B ND2 1 
ATOM   2115 N  N   . ARG B 1 73  ? 9.747   -23.454 22.653  1.00 26.58 ? 68  ARG B N   1 
ATOM   2116 C  CA  . ARG B 1 73  ? 9.592   -24.481 23.715  1.00 27.92 ? 68  ARG B CA  1 
ATOM   2117 C  C   . ARG B 1 73  ? 10.202  -23.991 25.020  1.00 31.04 ? 68  ARG B C   1 
ATOM   2118 O  O   . ARG B 1 73  ? 9.702   -24.445 26.042  1.00 32.68 ? 68  ARG B O   1 
ATOM   2119 C  CB  . ARG B 1 73  ? 10.175  -25.828 23.286  1.00 28.88 ? 68  ARG B CB  1 
ATOM   2120 C  CG  . ARG B 1 73  ? 9.068   -26.809 22.976  1.00 27.42 ? 68  ARG B CG  1 
ATOM   2121 C  CD  . ARG B 1 73  ? 9.550   -28.159 22.563  1.00 26.54 ? 68  ARG B CD  1 
ATOM   2122 N  NE  . ARG B 1 73  ? 8.581   -28.673 21.628  1.00 21.66 ? 68  ARG B NE  1 
ATOM   2123 C  CZ  . ARG B 1 73  ? 7.740   -29.640 21.892  1.00 24.53 ? 68  ARG B CZ  1 
ATOM   2124 N  NH1 . ARG B 1 73  ? 7.754   -30.224 23.081  1.00 23.02 ? 68  ARG B NH1 1 
ATOM   2125 N  NH2 . ARG B 1 73  ? 6.904   -30.049 20.950  1.00 26.90 ? 68  ARG B NH2 1 
ATOM   2126 N  N   . ALA B 1 74  ? 11.237  -23.128 24.946  1.00 34.28 ? 69  ALA B N   1 
ATOM   2127 C  CA  . ALA B 1 74  ? 12.047  -22.609 26.079  1.00 34.63 ? 69  ALA B CA  1 
ATOM   2128 C  C   . ALA B 1 74  ? 11.367  -21.384 26.686  1.00 30.95 ? 69  ALA B C   1 
ATOM   2129 O  O   . ALA B 1 74  ? 11.761  -20.987 27.777  1.00 28.38 ? 69  ALA B O   1 
ATOM   2130 C  CB  . ALA B 1 74  ? 13.459  -22.249 25.662  1.00 36.16 ? 69  ALA B CB  1 
ATOM   2131 N  N   . ASN B 1 75  ? 10.388  -20.823 25.989  1.00 28.39 ? 70  ASN B N   1 
ATOM   2132 C  CA  . ASN B 1 75  ? 9.506   -19.771 26.550  1.00 26.69 ? 70  ASN B CA  1 
ATOM   2133 C  C   . ASN B 1 75  ? 8.772   -20.385 27.742  1.00 23.32 ? 70  ASN B C   1 
ATOM   2134 O  O   . ASN B 1 75  ? 8.069   -21.387 27.602  1.00 22.89 ? 70  ASN B O   1 
ATOM   2135 C  CB  . ASN B 1 75  ? 8.603   -19.223 25.448  1.00 26.59 ? 70  ASN B CB  1 
ATOM   2136 C  CG  . ASN B 1 75  ? 7.725   -18.074 25.873  1.00 27.24 ? 70  ASN B CG  1 
ATOM   2137 O  OD1 . ASN B 1 75  ? 7.455   -17.898 27.055  1.00 25.29 ? 70  ASN B OD1 1 
ATOM   2138 N  ND2 . ASN B 1 75  ? 7.263   -17.308 24.894  1.00 27.94 ? 70  ASN B ND2 1 
ATOM   2139 N  N   . PRO B 1 76  ? 8.857   -19.803 28.946  1.00 21.07 ? 71  PRO B N   1 
ATOM   2140 C  CA  . PRO B 1 76  ? 8.189   -20.413 30.092  1.00 24.52 ? 71  PRO B CA  1 
ATOM   2141 C  C   . PRO B 1 76  ? 6.660   -20.470 29.916  1.00 24.99 ? 71  PRO B C   1 
ATOM   2142 O  O   . PRO B 1 76  ? 6.030   -21.233 30.619  1.00 26.66 ? 71  PRO B O   1 
ATOM   2143 C  CB  . PRO B 1 76  ? 8.621   -19.533 31.284  1.00 24.75 ? 71  PRO B CB  1 
ATOM   2144 C  CG  . PRO B 1 76  ? 9.879   -18.818 30.795  1.00 24.49 ? 71  PRO B CG  1 
ATOM   2145 C  CD  . PRO B 1 76  ? 9.609   -18.591 29.319  1.00 23.18 ? 71  PRO B CD  1 
ATOM   2146 N  N   . HIS B 1 77  ? 6.091   -19.686 28.990  1.00 26.16 ? 72  HIS B N   1 
ATOM   2147 C  CA  . HIS B 1 77  ? 4.646   -19.721 28.611  1.00 23.94 ? 72  HIS B CA  1 
ATOM   2148 C  C   . HIS B 1 77  ? 4.304   -21.120 28.064  1.00 23.62 ? 72  HIS B C   1 
ATOM   2149 O  O   . HIS B 1 77  ? 3.238   -21.622 28.351  1.00 19.91 ? 72  HIS B O   1 
ATOM   2150 C  CB  . HIS B 1 77  ? 4.293   -18.611 27.599  1.00 25.34 ? 72  HIS B CB  1 
ATOM   2151 C  CG  . HIS B 1 77  ? 2.818   -18.414 27.377  1.00 24.25 ? 72  HIS B CG  1 
ATOM   2152 N  ND1 . HIS B 1 77  ? 2.329   -17.412 26.591  1.00 24.60 ? 72  HIS B ND1 1 
ATOM   2153 C  CD2 . HIS B 1 77  ? 1.733   -19.068 27.857  1.00 26.47 ? 72  HIS B CD2 1 
ATOM   2154 C  CE1 . HIS B 1 77  ? 1.009   -17.450 26.585  1.00 25.36 ? 72  HIS B CE1 1 
ATOM   2155 N  NE2 . HIS B 1 77  ? 0.619   -18.481 27.329  1.00 25.67 ? 72  HIS B NE2 1 
ATOM   2156 N  N   . TRP B 1 78  ? 5.208   -21.735 27.316  1.00 25.69 ? 73  TRP B N   1 
ATOM   2157 C  CA  . TRP B 1 78  ? 5.031   -23.121 26.808  1.00 28.33 ? 73  TRP B CA  1 
ATOM   2158 C  C   . TRP B 1 78  ? 4.766   -24.074 27.991  1.00 28.41 ? 73  TRP B C   1 
ATOM   2159 O  O   . TRP B 1 78  ? 3.727   -24.769 27.967  1.00 25.69 ? 73  TRP B O   1 
ATOM   2160 C  CB  . TRP B 1 78  ? 6.222   -23.551 25.939  1.00 26.70 ? 73  TRP B CB  1 
ATOM   2161 C  CG  . TRP B 1 78  ? 6.069   -24.954 25.435  1.00 25.42 ? 73  TRP B CG  1 
ATOM   2162 C  CD1 . TRP B 1 78  ? 6.607   -26.062 26.004  1.00 26.69 ? 73  TRP B CD1 1 
ATOM   2163 C  CD2 . TRP B 1 78  ? 5.244   -25.425 24.356  1.00 25.54 ? 73  TRP B CD2 1 
ATOM   2164 N  NE1 . TRP B 1 78  ? 6.275   -27.175 25.293  1.00 28.58 ? 73  TRP B NE1 1 
ATOM   2165 C  CE2 . TRP B 1 78  ? 5.432   -26.818 24.278  1.00 28.19 ? 73  TRP B CE2 1 
ATOM   2166 C  CE3 . TRP B 1 78  ? 4.409   -24.812 23.423  1.00 24.74 ? 73  TRP B CE3 1 
ATOM   2167 C  CZ2 . TRP B 1 78  ? 4.806   -27.611 23.316  1.00 29.47 ? 73  TRP B CZ2 1 
ATOM   2168 C  CZ3 . TRP B 1 78  ? 3.807   -25.590 22.455  1.00 26.25 ? 73  TRP B CZ3 1 
ATOM   2169 C  CH2 . TRP B 1 78  ? 3.993   -26.973 22.414  1.00 28.09 ? 73  TRP B CH2 1 
ATOM   2170 N  N   . ALA B 1 79  ? 5.626   -24.071 29.009  1.00 28.97 ? 74  ALA B N   1 
ATOM   2171 C  CA  . ALA B 1 79  ? 5.497   -24.927 30.219  1.00 35.70 ? 74  ALA B CA  1 
ATOM   2172 C  C   . ALA B 1 79  ? 4.163   -24.646 30.947  1.00 37.90 ? 74  ALA B C   1 
ATOM   2173 O  O   . ALA B 1 79  ? 3.456   -25.617 31.378  1.00 36.07 ? 74  ALA B O   1 
ATOM   2174 C  CB  . ALA B 1 79  ? 6.668   -24.660 31.125  1.00 34.63 ? 74  ALA B CB  1 
ATOM   2175 N  N   . ALA B 1 80  ? 3.817   -23.365 31.087  1.00 39.70 ? 75  ALA B N   1 
ATOM   2176 C  CA  . ALA B 1 80  ? 2.599   -22.887 31.780  1.00 36.90 ? 75  ALA B CA  1 
ATOM   2177 C  C   . ALA B 1 80  ? 1.349   -23.373 31.055  1.00 40.22 ? 75  ALA B C   1 
ATOM   2178 O  O   . ALA B 1 80  ? 0.349   -23.636 31.742  1.00 40.94 ? 75  ALA B O   1 
ATOM   2179 C  CB  . ALA B 1 80  ? 2.615   -21.393 31.915  1.00 38.00 ? 75  ALA B CB  1 
ATOM   2180 N  N   . LEU B 1 81  ? 1.392   -23.551 29.736  1.00 43.75 ? 76  LEU B N   1 
ATOM   2181 C  CA  . LEU B 1 81  ? 0.190   -24.027 28.999  1.00 45.58 ? 76  LEU B CA  1 
ATOM   2182 C  C   . LEU B 1 81  ? -0.086  -25.475 29.423  1.00 57.92 ? 76  LEU B C   1 
ATOM   2183 O  O   . LEU B 1 81  ? 0.803   -26.341 29.229  1.00 50.72 ? 76  LEU B O   1 
ATOM   2184 C  CB  . LEU B 1 81  ? 0.374   -23.898 27.484  1.00 42.36 ? 76  LEU B CB  1 
ATOM   2185 C  CG  . LEU B 1 81  ? 0.388   -22.467 26.933  1.00 39.12 ? 76  LEU B CG  1 
ATOM   2186 C  CD1 . LEU B 1 81  ? 0.921   -22.456 25.506  1.00 34.26 ? 76  LEU B CD1 1 
ATOM   2187 C  CD2 . LEU B 1 81  ? -0.996  -21.837 27.008  1.00 38.48 ? 76  LEU B CD2 1 
ATOM   2188 N  N   . GLY B 1 82  ? -1.248  -25.701 30.047  1.00 64.66 ? 77  GLY B N   1 
ATOM   2189 C  CA  . GLY B 1 82  ? -1.722  -27.041 30.434  1.00 69.25 ? 77  GLY B CA  1 
ATOM   2190 C  C   . GLY B 1 82  ? -1.964  -27.883 29.202  1.00 74.08 ? 77  GLY B C   1 
ATOM   2191 O  O   . GLY B 1 82  ? -1.993  -27.311 28.080  1.00 81.04 ? 77  GLY B O   1 
ATOM   2192 N  N   . GLY B 1 83  ? -2.101  -29.193 29.393  1.00 75.67 ? 78  GLY B N   1 
ATOM   2193 C  CA  . GLY B 1 83  ? -2.587  -30.111 28.349  1.00 75.42 ? 78  GLY B CA  1 
ATOM   2194 C  C   . GLY B 1 83  ? -3.779  -29.506 27.625  1.00 79.59 ? 78  GLY B C   1 
ATOM   2195 O  O   . GLY B 1 83  ? -3.748  -29.480 26.372  1.00 89.87 ? 78  GLY B O   1 
ATOM   2196 N  N   . ALA B 1 84  ? -4.767  -28.999 28.379  1.00 71.28 ? 79  ALA B N   1 
ATOM   2197 C  CA  . ALA B 1 84  ? -6.054  -28.477 27.860  1.00 58.73 ? 79  ALA B CA  1 
ATOM   2198 C  C   . ALA B 1 84  ? -6.308  -27.052 28.364  1.00 55.56 ? 79  ALA B C   1 
ATOM   2199 O  O   . ALA B 1 84  ? -7.407  -26.807 28.911  1.00 55.85 ? 79  ALA B O   1 
ATOM   2200 C  CB  . ALA B 1 84  ? -7.154  -29.403 28.286  1.00 57.45 ? 79  ALA B CB  1 
ATOM   2201 N  N   . ALA B 1 85  ? -5.343  -26.145 28.173  1.00 48.56 ? 80  ALA B N   1 
ATOM   2202 C  CA  . ALA B 1 85  ? -5.413  -24.726 28.612  1.00 45.95 ? 80  ALA B CA  1 
ATOM   2203 C  C   . ALA B 1 85  ? -6.444  -23.972 27.757  1.00 39.83 ? 80  ALA B C   1 
ATOM   2204 O  O   . ALA B 1 85  ? -6.433  -24.145 26.526  1.00 35.33 ? 80  ALA B O   1 
ATOM   2205 C  CB  . ALA B 1 85  ? -4.051  -24.087 28.525  1.00 44.05 ? 80  ALA B CB  1 
ATOM   2206 N  N   . ASN B 1 86  ? -7.334  -23.196 28.380  1.00 39.79 ? 81  ASN B N   1 
ATOM   2207 C  CA  . ASN B 1 86  ? -8.265  -22.298 27.640  1.00 38.54 ? 81  ASN B CA  1 
ATOM   2208 C  C   . ASN B 1 86  ? -7.566  -20.966 27.385  1.00 32.05 ? 81  ASN B C   1 
ATOM   2209 O  O   . ASN B 1 86  ? -7.188  -20.310 28.363  1.00 35.43 ? 81  ASN B O   1 
ATOM   2210 C  CB  . ASN B 1 86  ? -9.613  -22.125 28.332  1.00 41.33 ? 81  ASN B CB  1 
ATOM   2211 C  CG  . ASN B 1 86  ? -10.566 -23.212 27.890  1.00 45.36 ? 81  ASN B CG  1 
ATOM   2212 O  OD1 . ASN B 1 86  ? -10.407 -24.342 28.316  1.00 44.45 ? 81  ASN B OD1 1 
ATOM   2213 N  ND2 . ASN B 1 86  ? -11.462 -22.910 26.957  1.00 43.29 ? 81  ASN B ND2 1 
ATOM   2214 N  N   . VAL B 1 87  ? -7.454  -20.576 26.116  1.00 26.60 ? 82  VAL B N   1 
ATOM   2215 C  CA  . VAL B 1 87  ? -6.616  -19.424 25.694  1.00 26.27 ? 82  VAL B CA  1 
ATOM   2216 C  C   . VAL B 1 87  ? -7.436  -18.482 24.822  1.00 24.95 ? 82  VAL B C   1 
ATOM   2217 O  O   . VAL B 1 87  ? -8.545  -18.849 24.377  1.00 24.83 ? 82  VAL B O   1 
ATOM   2218 C  CB  . VAL B 1 87  ? -5.335  -19.892 24.981  1.00 27.10 ? 82  VAL B CB  1 
ATOM   2219 C  CG1 . VAL B 1 87  ? -4.514  -20.809 25.872  1.00 29.55 ? 82  VAL B CG1 1 
ATOM   2220 C  CG2 . VAL B 1 87  ? -5.640  -20.572 23.657  1.00 26.00 ? 82  VAL B CG2 1 
ATOM   2221 N  N   . VAL B 1 88  ? -6.910  -17.270 24.679  1.00 24.95 ? 83  VAL B N   1 
ATOM   2222 C  CA  . VAL B 1 88  ? -7.410  -16.226 23.751  1.00 23.58 ? 83  VAL B CA  1 
ATOM   2223 C  C   . VAL B 1 88  ? -6.190  -15.854 22.919  1.00 23.32 ? 83  VAL B C   1 
ATOM   2224 O  O   . VAL B 1 88  ? -5.082  -15.743 23.507  1.00 20.75 ? 83  VAL B O   1 
ATOM   2225 C  CB  . VAL B 1 88  ? -8.059  -15.035 24.487  1.00 25.70 ? 83  VAL B CB  1 
ATOM   2226 C  CG1 . VAL B 1 88  ? -7.167  -14.426 25.555  1.00 27.46 ? 83  VAL B CG1 1 
ATOM   2227 C  CG2 . VAL B 1 88  ? -8.528  -13.952 23.547  1.00 24.51 ? 83  VAL B CG2 1 
ATOM   2228 N  N   . ALA B 1 89  ? -6.368  -15.814 21.597  1.00 22.97 ? 84  ALA B N   1 
ATOM   2229 C  CA  . ALA B 1 89  ? -5.395  -15.230 20.652  1.00 25.25 ? 84  ALA B CA  1 
ATOM   2230 C  C   . ALA B 1 89  ? -6.058  -14.003 20.045  1.00 24.31 ? 84  ALA B C   1 
ATOM   2231 O  O   . ALA B 1 89  ? -7.238  -14.126 19.595  1.00 23.35 ? 84  ALA B O   1 
ATOM   2232 C  CB  . ALA B 1 89  ? -4.979  -16.249 19.624  1.00 25.71 ? 84  ALA B CB  1 
ATOM   2233 N  N   . THR B 1 90  ? -5.418  -12.848 20.172  1.00 22.85 ? 85  THR B N   1 
ATOM   2234 C  CA  . THR B 1 90  ? -5.977  -11.535 19.723  1.00 21.70 ? 85  THR B CA  1 
ATOM   2235 C  C   . THR B 1 90  ? -5.185  -11.081 18.502  1.00 21.95 ? 85  THR B C   1 
ATOM   2236 O  O   . THR B 1 90  ? -3.903  -11.055 18.553  1.00 22.66 ? 85  THR B O   1 
ATOM   2237 C  CB  . THR B 1 90  ? -5.914  -10.452 20.815  1.00 22.26 ? 85  THR B CB  1 
ATOM   2238 O  OG1 . THR B 1 90  ? -6.653  -10.867 21.963  1.00 21.59 ? 85  THR B OG1 1 
ATOM   2239 C  CG2 . THR B 1 90  ? -6.465  -9.120  20.350  1.00 21.59 ? 85  THR B CG2 1 
ATOM   2240 N  N   . PHE B 1 91  ? -5.883  -10.733 17.443  1.00 23.35 ? 86  PHE B N   1 
ATOM   2241 C  CA  . PHE B 1 91  ? -5.253  -10.251 16.193  1.00 23.83 ? 86  PHE B CA  1 
ATOM   2242 C  C   . PHE B 1 91  ? -5.590  -8.773  16.065  1.00 24.16 ? 86  PHE B C   1 
ATOM   2243 O  O   . PHE B 1 91  ? -6.781  -8.425  16.121  1.00 25.98 ? 86  PHE B O   1 
ATOM   2244 C  CB  . PHE B 1 91  ? -5.667  -11.088 14.985  1.00 22.27 ? 86  PHE B CB  1 
ATOM   2245 C  CG  . PHE B 1 91  ? -5.423  -12.566 15.112  1.00 21.25 ? 86  PHE B CG  1 
ATOM   2246 C  CD1 . PHE B 1 91  ? -6.291  -13.364 15.840  1.00 22.14 ? 86  PHE B CD1 1 
ATOM   2247 C  CD2 . PHE B 1 91  ? -4.399  -13.179 14.429  1.00 21.10 ? 86  PHE B CD2 1 
ATOM   2248 C  CE1 . PHE B 1 91  ? -6.097  -14.729 15.940  1.00 22.63 ? 86  PHE B CE1 1 
ATOM   2249 C  CE2 . PHE B 1 91  ? -4.218  -14.554 14.493  1.00 22.87 ? 86  PHE B CE2 1 
ATOM   2250 C  CZ  . PHE B 1 91  ? -5.051  -15.327 15.274  1.00 23.29 ? 86  PHE B CZ  1 
ATOM   2251 N  N   . ALA B 1 92  ? -4.549  -7.936  15.981  1.00 23.69 ? 87  ALA B N   1 
ATOM   2252 C  CA  . ALA B 1 92  ? -4.665  -6.465  15.877  1.00 26.42 ? 87  ALA B CA  1 
ATOM   2253 C  C   . ALA B 1 92  ? -4.475  -6.063  14.409  1.00 27.90 ? 87  ALA B C   1 
ATOM   2254 O  O   . ALA B 1 92  ? -3.387  -6.301  13.880  1.00 22.16 ? 87  ALA B O   1 
ATOM   2255 C  CB  . ALA B 1 92  ? -3.652  -5.782  16.764  1.00 28.53 ? 87  ALA B CB  1 
ATOM   2256 N  N   . GLY B 1 93  ? -5.528  -5.503  13.805  1.00 24.90 ? 88  GLY B N   1 
ATOM   2257 C  CA  . GLY B 1 93  ? -5.559  -4.962  12.436  1.00 26.03 ? 88  GLY B CA  1 
ATOM   2258 C  C   . GLY B 1 93  ? -5.264  -3.471  12.360  1.00 23.00 ? 88  GLY B C   1 
ATOM   2259 O  O   . GLY B 1 93  ? -4.676  -2.876  13.280  1.00 21.17 ? 88  GLY B O   1 
ATOM   2260 N  N   . PRO B 1 94  ? -5.627  -2.834  11.224  1.00 23.67 ? 89  PRO B N   1 
ATOM   2261 C  CA  . PRO B 1 94  ? -5.323  -1.422  11.021  1.00 23.39 ? 89  PRO B CA  1 
ATOM   2262 C  C   . PRO B 1 94  ? -6.057  -0.581  12.089  1.00 23.31 ? 89  PRO B C   1 
ATOM   2263 O  O   . PRO B 1 94  ? -7.123  -0.970  12.550  1.00 24.63 ? 89  PRO B O   1 
ATOM   2264 C  CB  . PRO B 1 94  ? -5.769  -1.136  9.582   1.00 23.93 ? 89  PRO B CB  1 
ATOM   2265 C  CG  . PRO B 1 94  ? -5.828  -2.493  8.925   1.00 24.03 ? 89  PRO B CG  1 
ATOM   2266 C  CD  . PRO B 1 94  ? -6.245  -3.442  10.040  1.00 24.64 ? 89  PRO B CD  1 
ATOM   2267 N  N   . ASN B 1 95  ? -5.452  0.540   12.481  1.00 24.92 ? 90  ASN B N   1 
ATOM   2268 C  CA  . ASN B 1 95  ? -5.942  1.406   13.594  1.00 25.24 ? 90  ASN B CA  1 
ATOM   2269 C  C   . ASN B 1 95  ? -5.390  2.814   13.384  1.00 25.73 ? 90  ASN B C   1 
ATOM   2270 O  O   . ASN B 1 95  ? -4.233  2.938   12.863  1.00 24.58 ? 90  ASN B O   1 
ATOM   2271 C  CB  . ASN B 1 95  ? -5.554  0.837   14.966  1.00 24.34 ? 90  ASN B CB  1 
ATOM   2272 C  CG  . ASN B 1 95  ? -4.059  0.885   15.168  1.00 28.35 ? 90  ASN B CG  1 
ATOM   2273 O  OD1 . ASN B 1 95  ? -3.518  1.931   15.528  1.00 25.60 ? 90  ASN B OD1 1 
ATOM   2274 N  ND2 . ASN B 1 95  ? -3.377  -0.202  14.835  1.00 28.02 ? 90  ASN B ND2 1 
ATOM   2275 N  N   . ALA B 1 96  ? -6.138  3.834   13.812  1.00 23.19 ? 91  ALA B N   1 
ATOM   2276 C  CA  . ALA B 1 96  ? -5.693  5.248   13.781  1.00 23.08 ? 91  ALA B CA  1 
ATOM   2277 C  C   . ALA B 1 96  ? -6.422  6.064   14.844  1.00 23.84 ? 91  ALA B C   1 
ATOM   2278 O  O   . ALA B 1 96  ? -7.656  5.871   15.045  1.00 23.85 ? 91  ALA B O   1 
ATOM   2279 C  CB  . ALA B 1 96  ? -5.878  5.846   12.404  1.00 21.20 ? 91  ALA B CB  1 
ATOM   2280 N  N   . TYR B 1 97  ? -5.681  6.955   15.492  1.00 25.54 ? 92  TYR B N   1 
ATOM   2281 C  CA  . TYR B 1 97  ? -6.232  7.987   16.403  1.00 26.26 ? 92  TYR B CA  1 
ATOM   2282 C  C   . TYR B 1 97  ? -7.172  8.903   15.631  1.00 25.61 ? 92  TYR B C   1 
ATOM   2283 O  O   . TYR B 1 97  ? -6.771  9.380   14.577  1.00 25.41 ? 92  TYR B O   1 
ATOM   2284 C  CB  . TYR B 1 97  ? -5.129  8.858   16.990  1.00 27.45 ? 92  TYR B CB  1 
ATOM   2285 C  CG  . TYR B 1 97  ? -5.633  9.958   17.889  1.00 26.38 ? 92  TYR B CG  1 
ATOM   2286 C  CD1 . TYR B 1 97  ? -6.136  9.678   19.147  1.00 26.77 ? 92  TYR B CD1 1 
ATOM   2287 C  CD2 . TYR B 1 97  ? -5.639  11.275  17.469  1.00 25.78 ? 92  TYR B CD2 1 
ATOM   2288 C  CE1 . TYR B 1 97  ? -6.567  10.691  19.997  1.00 28.71 ? 92  TYR B CE1 1 
ATOM   2289 C  CE2 . TYR B 1 97  ? -6.118  12.289  18.279  1.00 25.80 ? 92  TYR B CE2 1 
ATOM   2290 C  CZ  . TYR B 1 97  ? -6.581  12.000  19.552  1.00 27.14 ? 92  TYR B CZ  1 
ATOM   2291 O  OH  . TYR B 1 97  ? -7.008  12.991  20.379  1.00 24.43 ? 92  TYR B OH  1 
ATOM   2292 N  N   . VAL B 1 98  ? -8.388  9.128   16.136  1.00 25.52 ? 93  VAL B N   1 
ATOM   2293 C  CA  . VAL B 1 98  ? -9.353  10.080  15.515  1.00 22.88 ? 93  VAL B CA  1 
ATOM   2294 C  C   . VAL B 1 98  ? -9.350  11.396  16.308  1.00 23.64 ? 93  VAL B C   1 
ATOM   2295 O  O   . VAL B 1 98  ? -9.720  11.417  17.536  1.00 24.32 ? 93  VAL B O   1 
ATOM   2296 C  CB  . VAL B 1 98  ? -10.762 9.495   15.494  1.00 24.41 ? 93  VAL B CB  1 
ATOM   2297 C  CG1 . VAL B 1 98  ? -11.732 10.521  14.934  1.00 23.25 ? 93  VAL B CG1 1 
ATOM   2298 C  CG2 . VAL B 1 98  ? -10.782 8.190   14.722  1.00 24.46 ? 93  VAL B CG2 1 
ATOM   2299 N  N   . SER B 1 99  ? -8.976  12.462  15.632  1.00 21.06 ? 94  SER B N   1 
ATOM   2300 C  CA  . SER B 1 99  ? -9.048  13.850  16.130  1.00 22.24 ? 94  SER B CA  1 
ATOM   2301 C  C   . SER B 1 99  ? -10.454 14.367  15.917  1.00 21.31 ? 94  SER B C   1 
ATOM   2302 O  O   . SER B 1 99  ? -10.856 14.523  14.779  1.00 25.49 ? 94  SER B O   1 
ATOM   2303 C  CB  . SER B 1 99  ? -8.120  14.772  15.420  1.00 20.20 ? 94  SER B CB  1 
ATOM   2304 O  OG  . SER B 1 99  ? -8.340  16.118  15.862  1.00 24.98 ? 94  SER B OG  1 
ATOM   2305 N  N   . PRO B 1 100 ? -11.132 14.915  16.939  1.00 23.32 ? 95  PRO B N   1 
ATOM   2306 C  CA  . PRO B 1 100 ? -12.437 15.542  16.699  1.00 25.76 ? 95  PRO B CA  1 
ATOM   2307 C  C   . PRO B 1 100 ? -12.289 16.769  15.776  1.00 26.65 ? 95  PRO B C   1 
ATOM   2308 O  O   . PRO B 1 100 ? -13.268 17.227  15.242  1.00 23.59 ? 95  PRO B O   1 
ATOM   2309 C  CB  . PRO B 1 100 ? -12.932 15.887  18.110  1.00 25.72 ? 95  PRO B CB  1 
ATOM   2310 C  CG  . PRO B 1 100 ? -12.063 15.053  19.026  1.00 23.87 ? 95  PRO B CG  1 
ATOM   2311 C  CD  . PRO B 1 100 ? -10.713 15.014  18.340  1.00 21.30 ? 95  PRO B CD  1 
ATOM   2312 N  N   . ALA B 1 101 ? -11.070 17.269  15.547  1.00 29.09 ? 96  ALA B N   1 
ATOM   2313 C  CA  . ALA B 1 101 ? -10.897 18.392  14.592  1.00 30.95 ? 96  ALA B CA  1 
ATOM   2314 C  C   . ALA B 1 101 ? -11.467 17.920  13.250  1.00 32.01 ? 96  ALA B C   1 
ATOM   2315 O  O   . ALA B 1 101 ? -12.006 18.728  12.514  1.00 32.94 ? 96  ALA B O   1 
ATOM   2316 C  CB  . ALA B 1 101 ? -9.443  18.805  14.466  1.00 31.24 ? 96  ALA B CB  1 
ATOM   2317 N  N   . VAL B 1 102 ? -11.331 16.630  12.956  1.00 31.34 ? 97  VAL B N   1 
ATOM   2318 C  CA  . VAL B 1 102 ? -11.747 16.016  11.663  1.00 34.09 ? 97  VAL B CA  1 
ATOM   2319 C  C   . VAL B 1 102 ? -13.277 16.105  11.529  1.00 34.14 ? 97  VAL B C   1 
ATOM   2320 O  O   . VAL B 1 102 ? -13.754 16.397  10.422  1.00 36.91 ? 97  VAL B O   1 
ATOM   2321 C  CB  . VAL B 1 102 ? -11.221 14.570  11.582  1.00 34.60 ? 97  VAL B CB  1 
ATOM   2322 C  CG1 . VAL B 1 102 ? -11.911 13.743  10.511  1.00 38.04 ? 97  VAL B CG1 1 
ATOM   2323 C  CG2 . VAL B 1 102 ? -9.712  14.555  11.378  1.00 35.06 ? 97  VAL B CG2 1 
ATOM   2324 N  N   . TYR B 1 103 ? -14.016 15.886  12.617  1.00 34.39 ? 98  TYR B N   1 
ATOM   2325 C  CA  . TYR B 1 103 ? -15.506 15.896  12.650  1.00 31.08 ? 98  TYR B CA  1 
ATOM   2326 C  C   . TYR B 1 103 ? -16.068 17.266  12.274  1.00 34.44 ? 98  TYR B C   1 
ATOM   2327 O  O   . TYR B 1 103 ? -17.200 17.298  11.774  1.00 35.50 ? 98  TYR B O   1 
ATOM   2328 C  CB  . TYR B 1 103 ? -16.017 15.635  14.062  1.00 28.92 ? 98  TYR B CB  1 
ATOM   2329 C  CG  . TYR B 1 103 ? -15.668 14.307  14.675  1.00 28.87 ? 98  TYR B CG  1 
ATOM   2330 C  CD1 . TYR B 1 103 ? -15.176 13.242  13.927  1.00 27.54 ? 98  TYR B CD1 1 
ATOM   2331 C  CD2 . TYR B 1 103 ? -15.873 14.112  16.029  1.00 29.62 ? 98  TYR B CD2 1 
ATOM   2332 C  CE1 . TYR B 1 103 ? -14.918 12.006  14.511  1.00 28.91 ? 98  TYR B CE1 1 
ATOM   2333 C  CE2 . TYR B 1 103 ? -15.585 12.900  16.633  1.00 31.25 ? 98  TYR B CE2 1 
ATOM   2334 C  CZ  . TYR B 1 103 ? -15.098 11.850  15.875  1.00 29.38 ? 98  TYR B CZ  1 
ATOM   2335 O  OH  . TYR B 1 103 ? -14.886 10.662  16.496  1.00 31.06 ? 98  TYR B OH  1 
ATOM   2336 N  N   . ARG B 1 104 ? -15.335 18.351  12.575  1.00 35.43 ? 99  ARG B N   1 
ATOM   2337 C  CA  . ARG B 1 104 ? -15.820 19.745  12.427  1.00 42.04 ? 99  ARG B CA  1 
ATOM   2338 C  C   . ARG B 1 104 ? -17.152 19.915  13.188  1.00 41.95 ? 99  ARG B C   1 
ATOM   2339 O  O   . ARG B 1 104 ? -17.952 20.762  12.780  1.00 43.92 ? 99  ARG B O   1 
ATOM   2340 C  CB  . ARG B 1 104 ? -15.994 20.104  10.942  1.00 45.62 ? 99  ARG B CB  1 
ATOM   2341 C  CG  . ARG B 1 104 ? -14.714 20.091  10.114  1.00 50.10 ? 99  ARG B CG  1 
ATOM   2342 C  CD  . ARG B 1 104 ? -14.825 20.873  8.807   1.00 55.50 ? 99  ARG B CD  1 
ATOM   2343 N  NE  . ARG B 1 104 ? -15.882 20.434  7.882   1.00 55.75 ? 99  ARG B NE  1 
ATOM   2344 C  CZ  . ARG B 1 104 ? -15.735 19.541  6.894   1.00 59.69 ? 99  ARG B CZ  1 
ATOM   2345 N  NH1 . ARG B 1 104 ? -14.571 18.950  6.678   1.00 62.68 ? 99  ARG B NH1 1 
ATOM   2346 N  NH2 . ARG B 1 104 ? -16.766 19.228  6.123   1.00 60.70 ? 99  ARG B NH2 1 
ATOM   2347 N  N   . THR B 1 105 ? -17.403 19.150  14.256  1.00 40.91 ? 100 THR B N   1 
ATOM   2348 C  CA  . THR B 1 105 ? -18.595 19.338  15.135  1.00 39.49 ? 100 THR B CA  1 
ATOM   2349 C  C   . THR B 1 105 ? -18.124 19.587  16.566  1.00 37.23 ? 100 THR B C   1 
ATOM   2350 O  O   . THR B 1 105 ? -16.933 19.369  16.833  1.00 31.15 ? 100 THR B O   1 
ATOM   2351 C  CB  . THR B 1 105 ? -19.547 18.139  15.102  1.00 42.92 ? 100 THR B CB  1 
ATOM   2352 O  OG1 . THR B 1 105 ? -18.756 17.041  15.559  1.00 36.71 ? 100 THR B OG1 1 
ATOM   2353 C  CG2 . THR B 1 105 ? -20.144 17.890  13.735  1.00 46.43 ? 100 THR B CG2 1 
ATOM   2354 N  N   . ALA B 1 106 ? -19.030 20.091  17.406  1.00 33.54 ? 101 ALA B N   1 
ATOM   2355 C  CA  . ALA B 1 106 ? -18.847 20.366  18.848  1.00 34.35 ? 101 ALA B CA  1 
ATOM   2356 C  C   . ALA B 1 106 ? -20.185 20.145  19.533  1.00 32.41 ? 101 ALA B C   1 
ATOM   2357 O  O   . ALA B 1 106 ? -21.223 20.422  18.939  1.00 33.49 ? 101 ALA B O   1 
ATOM   2358 C  CB  . ALA B 1 106 ? -18.361 21.776  19.070  1.00 36.79 ? 101 ALA B CB  1 
ATOM   2359 N  N   . PRO B 1 107 ? -20.223 19.539  20.734  1.00 30.75 ? 102 PRO B N   1 
ATOM   2360 C  CA  . PRO B 1 107 ? -19.026 19.060  21.420  1.00 30.52 ? 102 PRO B CA  1 
ATOM   2361 C  C   . PRO B 1 107 ? -18.670 17.661  20.907  1.00 30.23 ? 102 PRO B C   1 
ATOM   2362 O  O   . PRO B 1 107 ? -19.456 17.053  20.224  1.00 28.15 ? 102 PRO B O   1 
ATOM   2363 C  CB  . PRO B 1 107 ? -19.477 19.023  22.885  1.00 30.31 ? 102 PRO B CB  1 
ATOM   2364 C  CG  . PRO B 1 107 ? -20.954 18.621  22.783  1.00 28.57 ? 102 PRO B CG  1 
ATOM   2365 C  CD  . PRO B 1 107 ? -21.448 19.176  21.457  1.00 29.46 ? 102 PRO B CD  1 
ATOM   2366 N  N   . ALA B 1 108 ? -17.476 17.193  21.229  1.00 28.12 ? 103 ALA B N   1 
ATOM   2367 C  CA  . ALA B 1 108 ? -16.973 15.885  20.783  1.00 25.99 ? 103 ALA B CA  1 
ATOM   2368 C  C   . ALA B 1 108 ? -15.962 15.350  21.801  1.00 25.41 ? 103 ALA B C   1 
ATOM   2369 O  O   . ALA B 1 108 ? -15.605 16.065  22.765  1.00 20.78 ? 103 ALA B O   1 
ATOM   2370 C  CB  . ALA B 1 108 ? -16.375 16.050  19.417  1.00 28.66 ? 103 ALA B CB  1 
ATOM   2371 N  N   . ALA B 1 109 ? -15.547 14.102  21.609  1.00 24.40 ? 104 ALA B N   1 
ATOM   2372 C  CA  . ALA B 1 109 ? -14.405 13.508  22.317  1.00 24.41 ? 104 ALA B CA  1 
ATOM   2373 C  C   . ALA B 1 109 ? -13.606 12.694  21.315  1.00 21.80 ? 104 ALA B C   1 
ATOM   2374 O  O   . ALA B 1 109 ? -14.167 12.184  20.365  1.00 19.67 ? 104 ALA B O   1 
ATOM   2375 C  CB  . ALA B 1 109 ? -14.892 12.677  23.474  1.00 25.13 ? 104 ALA B CB  1 
ATOM   2376 N  N   . PRO B 1 110 ? -12.266 12.646  21.440  1.00 21.28 ? 105 PRO B N   1 
ATOM   2377 C  CA  . PRO B 1 110 ? -11.451 11.873  20.517  1.00 21.53 ? 105 PRO B CA  1 
ATOM   2378 C  C   . PRO B 1 110 ? -11.763 10.402  20.753  1.00 21.57 ? 105 PRO B C   1 
ATOM   2379 O  O   . PRO B 1 110 ? -12.358 10.044  21.804  1.00 24.82 ? 105 PRO B O   1 
ATOM   2380 C  CB  . PRO B 1 110 ? -9.999  12.124  20.923  1.00 21.42 ? 105 PRO B CB  1 
ATOM   2381 C  CG  . PRO B 1 110 ? -10.066 13.266  21.911  1.00 22.11 ? 105 PRO B CG  1 
ATOM   2382 C  CD  . PRO B 1 110 ? -11.469 13.297  22.481  1.00 21.63 ? 105 PRO B CD  1 
ATOM   2383 N  N   A THR B 1 111 ? -11.355 9.556   19.816  0.50 20.04 ? 106 THR B N   1 
ATOM   2384 N  N   B THR B 1 111 ? -11.353 9.571   19.804  0.50 22.52 ? 106 THR B N   1 
ATOM   2385 C  CA  A THR B 1 111 ? -11.389 8.080   19.983  0.50 18.69 ? 106 THR B CA  1 
ATOM   2386 C  CA  B THR B 1 111 ? -11.469 8.094   19.891  0.50 22.60 ? 106 THR B CA  1 
ATOM   2387 C  C   A THR B 1 111 ? -10.188 7.487   19.260  0.50 20.17 ? 106 THR B C   1 
ATOM   2388 C  C   B THR B 1 111 ? -10.246 7.491   19.197  0.50 22.64 ? 106 THR B C   1 
ATOM   2389 O  O   A THR B 1 111 ? -9.325  8.265   18.814  0.50 22.24 ? 106 THR B O   1 
ATOM   2390 O  O   B THR B 1 111 ? -9.411  8.276   18.699  0.50 24.87 ? 106 THR B O   1 
ATOM   2391 C  CB  A THR B 1 111 ? -12.718 7.451   19.536  0.50 16.96 ? 106 THR B CB  1 
ATOM   2392 C  CB  B THR B 1 111 ? -12.811 7.590   19.335  0.50 23.52 ? 106 THR B CB  1 
ATOM   2393 O  OG1 A THR B 1 111 ? -12.695 6.147   20.114  0.50 16.98 ? 106 THR B OG1 1 
ATOM   2394 O  OG1 B THR B 1 111 ? -13.938 8.391   19.720  0.50 25.89 ? 106 THR B OG1 1 
ATOM   2395 C  CG2 A THR B 1 111 ? -12.928 7.393   18.038  0.50 15.46 ? 106 THR B CG2 1 
ATOM   2396 C  CG2 B THR B 1 111 ? -13.102 6.205   19.846  0.50 24.49 ? 106 THR B CG2 1 
ATOM   2397 N  N   . TRP B 1 112 ? -10.152 6.160   19.168  1.00 20.56 ? 107 TRP B N   1 
ATOM   2398 C  CA  . TRP B 1 112 ? -9.137  5.427   18.392  1.00 21.03 ? 107 TRP B CA  1 
ATOM   2399 C  C   . TRP B 1 112 ? -9.885  4.354   17.643  1.00 24.26 ? 107 TRP B C   1 
ATOM   2400 O  O   . TRP B 1 112 ? -10.524 3.523   18.298  1.00 28.29 ? 107 TRP B O   1 
ATOM   2401 C  CB  . TRP B 1 112 ? -8.076  4.855   19.303  1.00 22.00 ? 107 TRP B CB  1 
ATOM   2402 C  CG  . TRP B 1 112 ? -6.789  4.571   18.603  1.00 22.48 ? 107 TRP B CG  1 
ATOM   2403 C  CD1 . TRP B 1 112 ? -6.561  3.684   17.597  1.00 22.23 ? 107 TRP B CD1 1 
ATOM   2404 C  CD2 . TRP B 1 112 ? -5.543  5.221   18.872  1.00 22.70 ? 107 TRP B CD2 1 
ATOM   2405 N  NE1 . TRP B 1 112 ? -5.247  3.747   17.215  1.00 24.31 ? 107 TRP B NE1 1 
ATOM   2406 C  CE2 . TRP B 1 112 ? -4.596  4.665   17.991  1.00 24.65 ? 107 TRP B CE2 1 
ATOM   2407 C  CE3 . TRP B 1 112 ? -5.141  6.207   19.781  1.00 23.74 ? 107 TRP B CE3 1 
ATOM   2408 C  CZ2 . TRP B 1 112 ? -3.263  5.075   17.983  1.00 25.09 ? 107 TRP B CZ2 1 
ATOM   2409 C  CZ3 . TRP B 1 112 ? -3.815  6.596   19.784  1.00 24.59 ? 107 TRP B CZ3 1 
ATOM   2410 C  CH2 . TRP B 1 112 ? -2.906  6.059   18.877  1.00 24.19 ? 107 TRP B CH2 1 
ATOM   2411 N  N   . ASN B 1 113 ? -9.935  4.505   16.336  1.00 22.63 ? 108 ASN B N   1 
ATOM   2412 C  CA  . ASN B 1 113 ? -10.557 3.518   15.455  1.00 23.76 ? 108 ASN B CA  1 
ATOM   2413 C  C   . ASN B 1 113 ? -9.579  2.358   15.424  1.00 22.76 ? 108 ASN B C   1 
ATOM   2414 O  O   . ASN B 1 113 ? -8.365  2.581   15.263  1.00 23.17 ? 108 ASN B O   1 
ATOM   2415 C  CB  . ASN B 1 113 ? -10.880 4.104   14.075  1.00 24.10 ? 108 ASN B CB  1 
ATOM   2416 C  CG  . ASN B 1 113 ? -12.166 4.901   14.078  1.00 26.50 ? 108 ASN B CG  1 
ATOM   2417 O  OD1 . ASN B 1 113 ? -12.711 5.166   15.141  1.00 27.99 ? 108 ASN B OD1 1 
ATOM   2418 N  ND2 . ASN B 1 113 ? -12.669 5.268   12.905  1.00 28.32 ? 108 ASN B ND2 1 
ATOM   2419 N  N   . PHE B 1 114 ? -10.076 1.145   15.518  1.00 21.51 ? 109 PHE B N   1 
ATOM   2420 C  CA  . PHE B 1 114 ? -9.159  -0.005  15.567  1.00 21.95 ? 109 PHE B CA  1 
ATOM   2421 C  C   . PHE B 1 114 ? -9.957  -1.227  15.180  1.00 23.22 ? 109 PHE B C   1 
ATOM   2422 O  O   . PHE B 1 114 ? -11.238 -1.178  15.134  1.00 21.02 ? 109 PHE B O   1 
ATOM   2423 C  CB  . PHE B 1 114 ? -8.468  -0.086  16.935  1.00 21.75 ? 109 PHE B CB  1 
ATOM   2424 C  CG  . PHE B 1 114 ? -9.326  -0.654  18.034  1.00 21.82 ? 109 PHE B CG  1 
ATOM   2425 C  CD1 . PHE B 1 114 ? -10.112 0.170   18.809  1.00 21.78 ? 109 PHE B CD1 1 
ATOM   2426 C  CD2 . PHE B 1 114 ? -9.358  -2.028  18.272  1.00 22.02 ? 109 PHE B CD2 1 
ATOM   2427 C  CE1 . PHE B 1 114 ? -10.863 -0.343  19.847  1.00 23.12 ? 109 PHE B CE1 1 
ATOM   2428 C  CE2 . PHE B 1 114 ? -10.139 -2.548  19.291  1.00 22.17 ? 109 PHE B CE2 1 
ATOM   2429 C  CZ  . PHE B 1 114 ? -10.916 -1.699  20.053  1.00 23.44 ? 109 PHE B CZ  1 
ATOM   2430 N  N   . THR B 1 115 ? -9.203  -2.277  14.877  1.00 22.90 ? 110 THR B N   1 
ATOM   2431 C  CA  . THR B 1 115 ? -9.736  -3.587  14.470  1.00 24.19 ? 110 THR B CA  1 
ATOM   2432 C  C   . THR B 1 115 ? -9.073  -4.658  15.321  1.00 23.47 ? 110 THR B C   1 
ATOM   2433 O  O   . THR B 1 115 ? -7.820  -4.641  15.493  1.00 22.36 ? 110 THR B O   1 
ATOM   2434 C  CB  . THR B 1 115 ? -9.572  -3.802  12.960  1.00 25.19 ? 110 THR B CB  1 
ATOM   2435 O  OG1 . THR B 1 115 ? -8.234  -3.461  12.569  1.00 26.24 ? 110 THR B OG1 1 
ATOM   2436 C  CG2 . THR B 1 115 ? -10.621 -3.015  12.208  1.00 25.56 ? 110 THR B CG2 1 
ATOM   2437 N  N   . SER B 1 116 ? -9.874  -5.561  15.850  1.00 22.64 ? 111 SER B N   1 
ATOM   2438 C  CA  . SER B 1 116 ? -9.297  -6.743  16.530  1.00 24.02 ? 111 SER B CA  1 
ATOM   2439 C  C   . SER B 1 116 ? -10.226 -7.946  16.399  1.00 23.06 ? 111 SER B C   1 
ATOM   2440 O  O   . SER B 1 116 ? -11.472 -7.810  16.316  1.00 22.39 ? 111 SER B O   1 
ATOM   2441 C  CB  . SER B 1 116 ? -8.954  -6.427  17.954  1.00 25.16 ? 111 SER B CB  1 
ATOM   2442 O  OG  . SER B 1 116 ? -10.124 -6.101  18.665  1.00 34.00 ? 111 SER B OG  1 
ATOM   2443 N  N   . VAL B 1 117 ? -9.609  -9.106  16.389  1.00 23.00 ? 112 VAL B N   1 
ATOM   2444 C  CA  . VAL B 1 117 ? -10.321 -10.408 16.467  1.00 23.93 ? 112 VAL B CA  1 
ATOM   2445 C  C   . VAL B 1 117 ? -9.723  -11.114 17.674  1.00 24.20 ? 112 VAL B C   1 
ATOM   2446 O  O   . VAL B 1 117 ? -8.411  -11.198 17.772  1.00 19.45 ? 112 VAL B O   1 
ATOM   2447 C  CB  . VAL B 1 117 ? -10.184 -11.232 15.174  1.00 21.36 ? 112 VAL B CB  1 
ATOM   2448 C  CG1 . VAL B 1 117 ? -10.664 -12.648 15.345  1.00 22.02 ? 112 VAL B CG1 1 
ATOM   2449 C  CG2 . VAL B 1 117 ? -10.902 -10.582 14.009  1.00 25.12 ? 112 VAL B CG2 1 
ATOM   2450 N  N   . GLN B 1 118 ? -10.627 -11.562 18.539  1.00 18.71 ? 113 GLN B N   1 
ATOM   2451 C  CA  . GLN B 1 118 ? -10.289 -12.407 19.693  1.00 21.21 ? 113 GLN B CA  1 
ATOM   2452 C  C   . GLN B 1 118 ? -10.844 -13.814 19.476  1.00 22.82 ? 113 GLN B C   1 
ATOM   2453 O  O   . GLN B 1 118 ? -12.070 -13.959 19.305  1.00 23.56 ? 113 GLN B O   1 
ATOM   2454 C  CB  . GLN B 1 118 ? -10.827 -11.759 20.951  1.00 20.64 ? 113 GLN B CB  1 
ATOM   2455 C  CG  . GLN B 1 118 ? -10.083 -10.487 21.307  1.00 22.12 ? 113 GLN B CG  1 
ATOM   2456 C  CD  . GLN B 1 118 ? -10.484 -9.983  22.657  1.00 20.06 ? 113 GLN B CD  1 
ATOM   2457 O  OE1 . GLN B 1 118 ? -11.008 -10.742 23.454  1.00 21.84 ? 113 GLN B OE1 1 
ATOM   2458 N  NE2 . GLN B 1 118 ? -10.230 -8.711  22.899  1.00 19.12 ? 113 GLN B NE2 1 
ATOM   2459 N  N   . VAL B 1 119 ? -9.982  -14.814 19.418  1.00 22.61 ? 114 VAL B N   1 
ATOM   2460 C  CA  . VAL B 1 119 ? -10.445 -16.235 19.326  1.00 24.58 ? 114 VAL B CA  1 
ATOM   2461 C  C   . VAL B 1 119 ? -10.117 -16.923 20.649  1.00 24.50 ? 114 VAL B C   1 
ATOM   2462 O  O   . VAL B 1 119 ? -9.035  -16.672 21.222  1.00 27.43 ? 114 VAL B O   1 
ATOM   2463 C  CB  . VAL B 1 119 ? -9.857  -17.002 18.135  1.00 24.33 ? 114 VAL B CB  1 
ATOM   2464 C  CG1 . VAL B 1 119 ? -10.419 -16.519 16.812  1.00 26.12 ? 114 VAL B CG1 1 
ATOM   2465 C  CG2 . VAL B 1 119 ? -8.340  -16.998 18.131  1.00 25.88 ? 114 VAL B CG2 1 
ATOM   2466 N  N   . ARG B 1 120 ? -11.024 -17.759 21.119  1.00 24.05 ? 115 ARG B N   1 
ATOM   2467 C  CA  . ARG B 1 120 ? -10.881 -18.486 22.398  1.00 24.26 ? 115 ARG B CA  1 
ATOM   2468 C  C   . ARG B 1 120 ? -11.167 -19.960 22.125  1.00 24.85 ? 115 ARG B C   1 
ATOM   2469 O  O   . ARG B 1 120 ? -12.057 -20.257 21.299  1.00 25.16 ? 115 ARG B O   1 
ATOM   2470 C  CB  . ARG B 1 120 ? -11.836 -17.919 23.463  1.00 25.92 ? 115 ARG B CB  1 
ATOM   2471 C  CG  . ARG B 1 120 ? -11.459 -16.534 23.962  1.00 26.89 ? 115 ARG B CG  1 
ATOM   2472 C  CD  . ARG B 1 120 ? -12.481 -15.951 24.922  1.00 28.96 ? 115 ARG B CD  1 
ATOM   2473 N  NE  . ARG B 1 120 ? -11.947 -14.809 25.657  1.00 28.73 ? 115 ARG B NE  1 
ATOM   2474 C  CZ  . ARG B 1 120 ? -11.754 -13.579 25.160  1.00 29.07 ? 115 ARG B CZ  1 
ATOM   2475 N  NH1 . ARG B 1 120 ? -12.076 -13.279 23.910  1.00 27.76 ? 115 ARG B NH1 1 
ATOM   2476 N  NH2 . ARG B 1 120 ? -11.241 -12.635 25.933  1.00 31.39 ? 115 ARG B NH2 1 
ATOM   2477 N  N   . GLY B 1 121 ? -10.455 -20.832 22.821  1.00 24.79 ? 116 GLY B N   1 
ATOM   2478 C  CA  . GLY B 1 121 ? -10.685 -22.278 22.818  1.00 27.58 ? 116 GLY B CA  1 
ATOM   2479 C  C   . GLY B 1 121 ? -9.558  -22.977 23.551  1.00 30.91 ? 116 GLY B C   1 
ATOM   2480 O  O   . GLY B 1 121 ? -8.765  -22.277 24.264  1.00 27.14 ? 116 GLY B O   1 
ATOM   2481 N  N   . GLU B 1 122 ? -9.483  -24.297 23.383  1.00 30.30 ? 117 GLU B N   1 
ATOM   2482 C  CA  . GLU B 1 122 ? -8.462  -25.167 24.009  1.00 34.39 ? 117 GLU B CA  1 
ATOM   2483 C  C   . GLU B 1 122 ? -7.222  -25.149 23.127  1.00 28.58 ? 117 GLU B C   1 
ATOM   2484 O  O   . GLU B 1 122 ? -7.361  -25.406 21.927  1.00 31.58 ? 117 GLU B O   1 
ATOM   2485 C  CB  . GLU B 1 122 ? -8.921  -26.624 24.114  1.00 39.81 ? 117 GLU B CB  1 
ATOM   2486 C  CG  . GLU B 1 122 ? -10.112 -26.852 25.021  1.00 47.65 ? 117 GLU B CG  1 
ATOM   2487 C  CD  . GLU B 1 122 ? -10.372 -28.332 25.284  1.00 52.07 ? 117 GLU B CD  1 
ATOM   2488 O  OE1 . GLU B 1 122 ? -10.858 -29.032 24.347  1.00 55.48 ? 117 GLU B OE1 1 
ATOM   2489 O  OE2 . GLU B 1 122 ? -10.044 -28.793 26.412  1.00 46.76 ? 117 GLU B OE2 1 
ATOM   2490 N  N   . LEU B 1 123 ? -6.062  -24.858 23.696  1.00 29.60 ? 118 LEU B N   1 
ATOM   2491 C  CA  . LEU B 1 123 ? -4.769  -25.057 23.002  1.00 28.76 ? 118 LEU B CA  1 
ATOM   2492 C  C   . LEU B 1 123 ? -4.305  -26.494 23.256  1.00 30.53 ? 118 LEU B C   1 
ATOM   2493 O  O   . LEU B 1 123 ? -4.285  -26.882 24.436  1.00 28.88 ? 118 LEU B O   1 
ATOM   2494 C  CB  . LEU B 1 123 ? -3.755  -24.048 23.524  1.00 27.73 ? 118 LEU B CB  1 
ATOM   2495 C  CG  . LEU B 1 123 ? -2.458  -24.015 22.723  1.00 29.21 ? 118 LEU B CG  1 
ATOM   2496 C  CD1 . LEU B 1 123 ? -1.989  -22.595 22.520  1.00 29.32 ? 118 LEU B CD1 1 
ATOM   2497 C  CD2 . LEU B 1 123 ? -1.377  -24.856 23.375  1.00 30.09 ? 118 LEU B CD2 1 
ATOM   2498 N  N   . ARG B 1 124 ? -3.963  -27.246 22.198  1.00 31.36 ? 119 ARG B N   1 
ATOM   2499 C  CA  . ARG B 1 124 ? -3.353  -28.594 22.302  1.00 28.29 ? 119 ARG B CA  1 
ATOM   2500 C  C   . ARG B 1 124 ? -1.906  -28.526 21.812  1.00 29.49 ? 119 ARG B C   1 
ATOM   2501 O  O   . ARG B 1 124 ? -1.684  -28.089 20.674  1.00 28.23 ? 119 ARG B O   1 
ATOM   2502 C  CB  . ARG B 1 124 ? -4.081  -29.672 21.507  1.00 32.85 ? 119 ARG B CB  1 
ATOM   2503 C  CG  . ARG B 1 124 ? -3.381  -31.022 21.640  1.00 37.03 ? 119 ARG B CG  1 
ATOM   2504 C  CD  . ARG B 1 124 ? -4.048  -32.174 20.929  1.00 41.59 ? 119 ARG B CD  1 
ATOM   2505 N  NE  . ARG B 1 124 ? -4.037  -32.022 19.483  1.00 44.65 ? 119 ARG B NE  1 
ATOM   2506 C  CZ  . ARG B 1 124 ? -2.949  -32.062 18.716  1.00 45.93 ? 119 ARG B CZ  1 
ATOM   2507 N  NH1 . ARG B 1 124 ? -1.737  -32.213 19.243  1.00 42.07 ? 119 ARG B NH1 1 
ATOM   2508 N  NH2 . ARG B 1 124 ? -3.091  -31.937 17.409  1.00 47.21 ? 119 ARG B NH2 1 
ATOM   2509 N  N   . LYS B 1 125 ? -0.963  -28.932 22.654  1.00 24.26 ? 120 LYS B N   1 
ATOM   2510 C  CA  . LYS B 1 125 ? 0.454   -28.952 22.233  1.00 30.20 ? 120 LYS B CA  1 
ATOM   2511 C  C   . LYS B 1 125 ? 0.623   -30.062 21.201  1.00 31.06 ? 120 LYS B C   1 
ATOM   2512 O  O   . LYS B 1 125 ? 0.171   -31.179 21.452  1.00 33.64 ? 120 LYS B O   1 
ATOM   2513 C  CB  . LYS B 1 125 ? 1.389   -29.168 23.416  1.00 29.71 ? 120 LYS B CB  1 
ATOM   2514 C  CG  . LYS B 1 125 ? 1.429   -27.999 24.383  1.00 30.47 ? 120 LYS B CG  1 
ATOM   2515 C  CD  . LYS B 1 125 ? 2.185   -28.374 25.605  1.00 31.40 ? 120 LYS B CD  1 
ATOM   2516 C  CE  . LYS B 1 125 ? 2.401   -27.194 26.515  1.00 32.63 ? 120 LYS B CE  1 
ATOM   2517 N  NZ  . LYS B 1 125 ? 3.181   -27.560 27.718  1.00 32.04 ? 120 LYS B NZ  1 
ATOM   2518 N  N   . VAL B 1 126 ? 1.222   -29.733 20.064  1.00 33.52 ? 121 VAL B N   1 
ATOM   2519 C  CA  . VAL B 1 126 ? 1.764   -30.715 19.096  1.00 30.31 ? 121 VAL B CA  1 
ATOM   2520 C  C   . VAL B 1 126 ? 3.062   -31.237 19.707  1.00 29.56 ? 121 VAL B C   1 
ATOM   2521 O  O   . VAL B 1 126 ? 3.817   -30.409 20.241  1.00 26.09 ? 121 VAL B O   1 
ATOM   2522 C  CB  . VAL B 1 126 ? 2.004   -30.046 17.732  1.00 32.96 ? 121 VAL B CB  1 
ATOM   2523 C  CG1 . VAL B 1 126 ? 2.780   -30.959 16.792  1.00 36.39 ? 121 VAL B CG1 1 
ATOM   2524 C  CG2 . VAL B 1 126 ? 0.706   -29.591 17.074  1.00 31.72 ? 121 VAL B CG2 1 
ATOM   2525 N  N   . GLU B 1 127 ? 3.282   -32.556 19.646  1.00 31.47 ? 122 GLU B N   1 
ATOM   2526 C  CA  . GLU B 1 127 ? 4.549   -33.220 20.064  1.00 33.82 ? 122 GLU B CA  1 
ATOM   2527 C  C   . GLU B 1 127 ? 5.184   -33.920 18.862  1.00 30.21 ? 122 GLU B C   1 
ATOM   2528 O  O   . GLU B 1 127 ? 6.420   -34.070 18.887  1.00 29.04 ? 122 GLU B O   1 
ATOM   2529 C  CB  . GLU B 1 127 ? 4.297   -34.266 21.161  1.00 34.24 ? 122 GLU B CB  1 
ATOM   2530 C  CG  . GLU B 1 127 ? 3.636   -33.690 22.386  1.00 35.24 ? 122 GLU B CG  1 
ATOM   2531 C  CD  . GLU B 1 127 ? 4.509   -32.760 23.207  1.00 33.26 ? 122 GLU B CD  1 
ATOM   2532 O  OE1 . GLU B 1 127 ? 5.615   -32.450 22.770  1.00 31.78 ? 122 GLU B OE1 1 
ATOM   2533 O  OE2 . GLU B 1 127 ? 4.080   -32.376 24.301  1.00 29.75 ? 122 GLU B OE2 1 
ATOM   2534 N  N   . SER B 1 128 ? 4.355   -34.374 17.914  1.00 28.48 ? 123 SER B N   1 
ATOM   2535 C  CA  . SER B 1 128 ? 4.762   -35.097 16.683  1.00 31.98 ? 123 SER B CA  1 
ATOM   2536 C  C   . SER B 1 128 ? 5.736   -34.241 15.879  1.00 35.18 ? 123 SER B C   1 
ATOM   2537 O  O   . SER B 1 128 ? 5.475   -33.010 15.786  1.00 30.83 ? 123 SER B O   1 
ATOM   2538 C  CB  . SER B 1 128 ? 3.583   -35.441 15.846  1.00 33.72 ? 123 SER B CB  1 
ATOM   2539 O  OG  . SER B 1 128 ? 3.974   -35.550 14.490  1.00 36.03 ? 123 SER B OG  1 
ATOM   2540 N  N   . ALA B 1 129 ? 6.780   -34.862 15.309  1.00 33.81 ? 124 ALA B N   1 
ATOM   2541 C  CA  . ALA B 1 129 ? 7.812   -34.183 14.493  1.00 36.01 ? 124 ALA B CA  1 
ATOM   2542 C  C   . ALA B 1 129 ? 7.196   -33.820 13.143  1.00 39.62 ? 124 ALA B C   1 
ATOM   2543 O  O   . ALA B 1 129 ? 7.393   -32.671 12.685  1.00 35.29 ? 124 ALA B O   1 
ATOM   2544 C  CB  . ALA B 1 129 ? 9.043   -35.046 14.328  1.00 38.79 ? 124 ALA B CB  1 
ATOM   2545 N  N   . ASP B 1 130 ? 6.430   -34.749 12.571  1.00 39.69 ? 125 ASP B N   1 
ATOM   2546 C  CA  . ASP B 1 130 ? 5.717   -34.568 11.281  1.00 41.72 ? 125 ASP B CA  1 
ATOM   2547 C  C   . ASP B 1 130 ? 4.795   -33.345 11.379  1.00 40.45 ? 125 ASP B C   1 
ATOM   2548 O  O   . ASP B 1 130 ? 4.823   -32.505 10.458  1.00 37.42 ? 125 ASP B O   1 
ATOM   2549 C  CB  . ASP B 1 130 ? 4.922   -35.818 10.900  1.00 47.29 ? 125 ASP B CB  1 
ATOM   2550 C  CG  . ASP B 1 130 ? 5.698   -37.125 11.019  1.00 55.99 ? 125 ASP B CG  1 
ATOM   2551 O  OD1 . ASP B 1 130 ? 5.035   -38.184 11.097  1.00 64.95 ? 125 ASP B OD1 1 
ATOM   2552 O  OD2 . ASP B 1 130 ? 6.957   -37.083 11.034  1.00 60.71 ? 125 ASP B OD2 1 
ATOM   2553 N  N   . ASP B 1 131 ? 3.987   -33.251 12.437  1.00 35.55 ? 126 ASP B N   1 
ATOM   2554 C  CA  . ASP B 1 131 ? 2.975   -32.175 12.563  1.00 35.20 ? 126 ASP B CA  1 
ATOM   2555 C  C   . ASP B 1 131 ? 3.667   -30.850 12.902  1.00 32.13 ? 126 ASP B C   1 
ATOM   2556 O  O   . ASP B 1 131 ? 3.122   -29.788 12.535  1.00 32.01 ? 126 ASP B O   1 
ATOM   2557 C  CB  . ASP B 1 131 ? 1.900   -32.552 13.575  1.00 40.93 ? 126 ASP B CB  1 
ATOM   2558 C  CG  . ASP B 1 131 ? 0.973   -33.642 13.060  1.00 45.14 ? 126 ASP B CG  1 
ATOM   2559 O  OD1 . ASP B 1 131 ? 0.977   -33.886 11.836  1.00 48.95 ? 126 ASP B OD1 1 
ATOM   2560 O  OD2 . ASP B 1 131 ? 0.249   -34.225 13.882  1.00 51.68 ? 126 ASP B OD2 1 
ATOM   2561 N  N   . THR B 1 132 ? 4.802   -30.906 13.596  1.00 29.19 ? 127 THR B N   1 
ATOM   2562 C  CA  . THR B 1 132 ? 5.594   -29.719 13.976  1.00 28.36 ? 127 THR B CA  1 
ATOM   2563 C  C   . THR B 1 132 ? 6.206   -29.120 12.695  1.00 29.65 ? 127 THR B C   1 
ATOM   2564 O  O   . THR B 1 132 ? 6.120   -27.880 12.505  1.00 27.22 ? 127 THR B O   1 
ATOM   2565 C  CB  . THR B 1 132 ? 6.624   -30.067 15.057  1.00 26.83 ? 127 THR B CB  1 
ATOM   2566 O  OG1 . THR B 1 132 ? 5.980   -30.384 16.298  1.00 28.79 ? 127 THR B OG1 1 
ATOM   2567 C  CG2 . THR B 1 132 ? 7.567   -28.910 15.288  1.00 26.82 ? 127 THR B CG2 1 
ATOM   2568 N  N   . LEU B 1 133 ? 6.811   -29.949 11.839  1.00 29.64 ? 128 LEU B N   1 
ATOM   2569 C  CA  . LEU B 1 133 ? 7.366   -29.485 10.537  1.00 30.53 ? 128 LEU B CA  1 
ATOM   2570 C  C   . LEU B 1 133 ? 6.232   -28.989 9.636   1.00 27.84 ? 128 LEU B C   1 
ATOM   2571 O  O   . LEU B 1 133 ? 6.404   -27.919 9.011   1.00 24.28 ? 128 LEU B O   1 
ATOM   2572 C  CB  . LEU B 1 133 ? 8.134   -30.618 9.861   1.00 33.05 ? 128 LEU B CB  1 
ATOM   2573 C  CG  . LEU B 1 133 ? 8.879   -30.234 8.582   1.00 34.75 ? 128 LEU B CG  1 
ATOM   2574 C  CD1 . LEU B 1 133 ? 10.074  -29.344 8.887   1.00 35.70 ? 128 LEU B CD1 1 
ATOM   2575 C  CD2 . LEU B 1 133 ? 9.317   -31.483 7.819   1.00 36.81 ? 128 LEU B CD2 1 
ATOM   2576 N  N   . ALA B 1 134 ? 5.127   -29.746 9.544   1.00 25.97 ? 129 ALA B N   1 
ATOM   2577 C  CA  . ALA B 1 134 ? 3.919   -29.328 8.794   1.00 27.53 ? 129 ALA B CA  1 
ATOM   2578 C  C   . ALA B 1 134 ? 3.535   -27.903 9.210   1.00 25.95 ? 129 ALA B C   1 
ATOM   2579 O  O   . ALA B 1 134 ? 3.156   -27.106 8.323   1.00 26.34 ? 129 ALA B O   1 
ATOM   2580 C  CB  . ALA B 1 134 ? 2.761   -30.289 8.993   1.00 27.67 ? 129 ALA B CB  1 
ATOM   2581 N  N   . THR B 1 135 ? 3.630   -27.582 10.503  1.00 27.41 ? 130 THR B N   1 
ATOM   2582 C  CA  . THR B 1 135 ? 3.215   -26.272 11.058  1.00 26.38 ? 130 THR B CA  1 
ATOM   2583 C  C   . THR B 1 135 ? 4.129   -25.168 10.513  1.00 27.73 ? 130 THR B C   1 
ATOM   2584 O  O   . THR B 1 135 ? 3.602   -24.175 9.982   1.00 27.02 ? 130 THR B O   1 
ATOM   2585 C  CB  . THR B 1 135 ? 3.197   -26.272 12.594  1.00 27.79 ? 130 THR B CB  1 
ATOM   2586 O  OG1 . THR B 1 135 ? 2.412   -27.364 13.097  1.00 30.46 ? 130 THR B OG1 1 
ATOM   2587 C  CG2 . THR B 1 135 ? 2.651   -24.972 13.143  1.00 26.37 ? 130 THR B CG2 1 
ATOM   2588 N  N   . VAL B 1 136 ? 5.444   -25.268 10.700  1.00 26.20 ? 131 VAL B N   1 
ATOM   2589 C  CA  . VAL B 1 136 ? 6.337   -24.159 10.264  1.00 27.57 ? 131 VAL B CA  1 
ATOM   2590 C  C   . VAL B 1 136 ? 6.283   -24.017 8.731   1.00 26.01 ? 131 VAL B C   1 
ATOM   2591 O  O   . VAL B 1 136 ? 6.271   -22.856 8.253   1.00 25.11 ? 131 VAL B O   1 
ATOM   2592 C  CB  . VAL B 1 136 ? 7.764   -24.321 10.800  1.00 28.58 ? 131 VAL B CB  1 
ATOM   2593 C  CG1 . VAL B 1 136 ? 7.769   -24.194 12.318  1.00 29.79 ? 131 VAL B CG1 1 
ATOM   2594 C  CG2 . VAL B 1 136 ? 8.420   -25.611 10.332  1.00 30.41 ? 131 VAL B CG2 1 
ATOM   2595 N  N   . ARG B 1 137 ? 6.181   -25.121 7.982   1.00 25.19 ? 132 ARG B N   1 
ATOM   2596 C  CA  . ARG B 1 137 ? 6.133   -25.099 6.496   1.00 25.27 ? 132 ARG B CA  1 
ATOM   2597 C  C   . ARG B 1 137 ? 4.838   -24.418 6.018   1.00 25.88 ? 132 ARG B C   1 
ATOM   2598 O  O   . ARG B 1 137 ? 4.911   -23.622 5.051   1.00 25.12 ? 132 ARG B O   1 
ATOM   2599 C  CB  . ARG B 1 137 ? 6.290   -26.502 5.899   1.00 26.94 ? 132 ARG B CB  1 
ATOM   2600 C  CG  . ARG B 1 137 ? 7.709   -27.051 5.990   1.00 29.14 ? 132 ARG B CG  1 
ATOM   2601 C  CD  . ARG B 1 137 ? 7.894   -28.368 5.259   1.00 33.58 ? 132 ARG B CD  1 
ATOM   2602 N  NE  . ARG B 1 137 ? 7.633   -28.262 3.828   1.00 37.07 ? 132 ARG B NE  1 
ATOM   2603 C  CZ  . ARG B 1 137 ? 7.675   -29.276 2.965   1.00 42.68 ? 132 ARG B CZ  1 
ATOM   2604 N  NH1 . ARG B 1 137 ? 7.993   -30.494 3.370   1.00 44.86 ? 132 ARG B NH1 1 
ATOM   2605 N  NH2 . ARG B 1 137 ? 7.417   -29.068 1.689   1.00 47.41 ? 132 ARG B NH2 1 
ATOM   2606 N  N   . ALA B 1 138 ? 3.698   -24.684 6.648   1.00 23.12 ? 133 ALA B N   1 
ATOM   2607 C  CA  . ALA B 1 138 ? 2.427   -24.014 6.261   1.00 23.64 ? 133 ALA B CA  1 
ATOM   2608 C  C   . ALA B 1 138 ? 2.518   -22.531 6.634   1.00 23.38 ? 133 ALA B C   1 
ATOM   2609 O  O   . ALA B 1 138 ? 1.970   -21.698 5.913   1.00 23.76 ? 133 ALA B O   1 
ATOM   2610 C  CB  . ALA B 1 138 ? 1.239   -24.687 6.903   1.00 22.31 ? 133 ALA B CB  1 
ATOM   2611 N  N   . THR B 1 139 ? 3.212   -22.211 7.721   1.00 23.23 ? 134 THR B N   1 
ATOM   2612 C  CA  . THR B 1 139 ? 3.410   -20.810 8.171   1.00 26.28 ? 134 THR B CA  1 
ATOM   2613 C  C   . THR B 1 139 ? 4.271   -20.045 7.151   1.00 26.18 ? 134 THR B C   1 
ATOM   2614 O  O   . THR B 1 139 ? 3.935   -18.886 6.852   1.00 25.57 ? 134 THR B O   1 
ATOM   2615 C  CB  . THR B 1 139 ? 3.985   -20.796 9.589   1.00 26.16 ? 134 THR B CB  1 
ATOM   2616 O  OG1 . THR B 1 139 ? 3.023   -21.525 10.364  1.00 23.85 ? 134 THR B OG1 1 
ATOM   2617 C  CG2 . THR B 1 139 ? 4.215   -19.398 10.118  1.00 25.71 ? 134 THR B CG2 1 
ATOM   2618 N  N   . VAL B 1 140 ? 5.374   -20.633 6.684   1.00 25.11 ? 135 VAL B N   1 
ATOM   2619 C  CA  . VAL B 1 140 ? 6.186   -20.022 5.604   1.00 25.24 ? 135 VAL B CA  1 
ATOM   2620 C  C   . VAL B 1 140 ? 5.295   -19.887 4.362   1.00 25.16 ? 135 VAL B C   1 
ATOM   2621 O  O   . VAL B 1 140 ? 5.249   -18.773 3.789   1.00 23.68 ? 135 VAL B O   1 
ATOM   2622 C  CB  . VAL B 1 140 ? 7.447   -20.840 5.295   1.00 26.21 ? 135 VAL B CB  1 
ATOM   2623 C  CG1 . VAL B 1 140 ? 8.117   -20.347 4.021   1.00 26.15 ? 135 VAL B CG1 1 
ATOM   2624 C  CG2 . VAL B 1 140 ? 8.397   -20.818 6.472   1.00 24.88 ? 135 VAL B CG2 1 
ATOM   2625 N  N   . ALA B 1 141 ? 4.570   -20.943 3.991   1.00 23.61 ? 136 ALA B N   1 
ATOM   2626 C  CA  . ALA B 1 141 ? 3.736   -20.918 2.771   1.00 27.80 ? 136 ALA B CA  1 
ATOM   2627 C  C   . ALA B 1 141 ? 2.728   -19.761 2.858   1.00 28.53 ? 136 ALA B C   1 
ATOM   2628 O  O   . ALA B 1 141 ? 2.568   -19.056 1.848   1.00 28.01 ? 136 ALA B O   1 
ATOM   2629 C  CB  . ALA B 1 141 ? 3.058   -22.242 2.532   1.00 28.65 ? 136 ALA B CB  1 
ATOM   2630 N  N   . ALA B 1 142 ? 2.062   -19.562 4.001   1.00 27.54 ? 137 ALA B N   1 
ATOM   2631 C  CA  . ALA B 1 142 ? 0.986   -18.553 4.136   1.00 27.61 ? 137 ALA B CA  1 
ATOM   2632 C  C   . ALA B 1 142 ? 1.591   -17.146 4.209   1.00 23.81 ? 137 ALA B C   1 
ATOM   2633 O  O   . ALA B 1 142 ? 1.108   -16.249 3.520   1.00 22.98 ? 137 ALA B O   1 
ATOM   2634 C  CB  . ALA B 1 142 ? 0.145   -18.829 5.354   1.00 31.35 ? 137 ALA B CB  1 
ATOM   2635 N  N   . LEU B 1 143 ? 2.586   -16.930 5.062   1.00 23.44 ? 138 LEU B N   1 
ATOM   2636 C  CA  . LEU B 1 143 ? 3.103   -15.558 5.301   1.00 21.91 ? 138 LEU B CA  1 
ATOM   2637 C  C   . LEU B 1 143 ? 3.991   -15.094 4.130   1.00 22.44 ? 138 LEU B C   1 
ATOM   2638 O  O   . LEU B 1 143 ? 3.913   -13.911 3.793   1.00 19.26 ? 138 LEU B O   1 
ATOM   2639 C  CB  . LEU B 1 143 ? 3.842   -15.462 6.636   1.00 21.18 ? 138 LEU B CB  1 
ATOM   2640 C  CG  . LEU B 1 143 ? 3.160   -15.984 7.896   1.00 21.34 ? 138 LEU B CG  1 
ATOM   2641 C  CD1 . LEU B 1 143 ? 3.606   -15.209 9.101   1.00 18.62 ? 138 LEU B CD1 1 
ATOM   2642 C  CD2 . LEU B 1 143 ? 1.640   -16.062 7.782   1.00 22.57 ? 138 LEU B CD2 1 
ATOM   2643 N  N   . GLU B 1 144 ? 4.808   -15.958 3.515   1.00 23.84 ? 139 GLU B N   1 
ATOM   2644 C  CA  . GLU B 1 144 ? 5.733   -15.529 2.419   1.00 25.78 ? 139 GLU B CA  1 
ATOM   2645 C  C   . GLU B 1 144 ? 4.874   -15.117 1.215   1.00 27.73 ? 139 GLU B C   1 
ATOM   2646 O  O   . GLU B 1 144 ? 5.111   -14.052 0.612   1.00 22.74 ? 139 GLU B O   1 
ATOM   2647 C  CB  . GLU B 1 144 ? 6.740   -16.636 2.101   1.00 28.76 ? 139 GLU B CB  1 
ATOM   2648 C  CG  . GLU B 1 144 ? 7.799   -16.256 1.088   1.00 27.31 ? 139 GLU B CG  1 
ATOM   2649 C  CD  . GLU B 1 144 ? 8.825   -15.212 1.506   1.00 28.17 ? 139 GLU B CD  1 
ATOM   2650 O  OE1 . GLU B 1 144 ? 9.063   -15.037 2.718   1.00 26.02 ? 139 GLU B OE1 1 
ATOM   2651 O  OE2 . GLU B 1 144 ? 9.371   -14.558 0.590   1.00 26.19 ? 139 GLU B OE2 1 
ATOM   2652 N  N   . SER B 1 145 ? 3.825   -15.883 0.931   1.00 29.31 ? 140 SER B N   1 
ATOM   2653 C  CA  . SER B 1 145 ? 2.838   -15.532 -0.114  1.00 30.96 ? 140 SER B CA  1 
ATOM   2654 C  C   . SER B 1 145 ? 2.316   -14.102 0.085   1.00 29.50 ? 140 SER B C   1 
ATOM   2655 O  O   . SER B 1 145 ? 2.233   -13.340 -0.885  1.00 34.34 ? 140 SER B O   1 
ATOM   2656 C  CB  . SER B 1 145 ? 1.684   -16.500 -0.119  1.00 32.39 ? 140 SER B CB  1 
ATOM   2657 O  OG  . SER B 1 145 ? 0.733   -16.044 -1.069  1.00 32.64 ? 140 SER B OG  1 
ATOM   2658 N  N   . ARG B 1 146 ? 1.958   -13.759 1.310   1.00 31.46 ? 141 ARG B N   1 
ATOM   2659 C  CA  . ARG B 1 146 ? 1.155   -12.557 1.647   1.00 30.55 ? 141 ARG B CA  1 
ATOM   2660 C  C   . ARG B 1 146 ? 2.042   -11.343 1.952   1.00 28.20 ? 141 ARG B C   1 
ATOM   2661 O  O   . ARG B 1 146 ? 1.598   -10.243 1.641   1.00 29.40 ? 141 ARG B O   1 
ATOM   2662 C  CB  . ARG B 1 146 ? 0.258   -12.911 2.834   1.00 34.35 ? 141 ARG B CB  1 
ATOM   2663 C  CG  . ARG B 1 146 ? -1.110  -12.256 2.793   1.00 41.72 ? 141 ARG B CG  1 
ATOM   2664 C  CD  . ARG B 1 146 ? -1.986  -12.778 3.916   1.00 44.57 ? 141 ARG B CD  1 
ATOM   2665 N  NE  . ARG B 1 146 ? -2.863  -13.851 3.465   1.00 47.31 ? 141 ARG B NE  1 
ATOM   2666 C  CZ  . ARG B 1 146 ? -4.033  -13.677 2.862   1.00 47.31 ? 141 ARG B CZ  1 
ATOM   2667 N  NH1 . ARG B 1 146 ? -4.497  -12.461 2.603   1.00 46.28 ? 141 ARG B NH1 1 
ATOM   2668 N  NH2 . ARG B 1 146 ? -4.725  -14.738 2.502   1.00 53.59 ? 141 ARG B NH2 1 
ATOM   2669 N  N   . PHE B 1 147 ? 3.216   -11.516 2.574   1.00 25.69 ? 142 PHE B N   1 
ATOM   2670 C  CA  . PHE B 1 147 ? 4.086   -10.417 3.093   1.00 26.21 ? 142 PHE B CA  1 
ATOM   2671 C  C   . PHE B 1 147 ? 5.516   -10.522 2.520   1.00 26.40 ? 142 PHE B C   1 
ATOM   2672 O  O   . PHE B 1 147 ? 6.383   -9.681  2.855   1.00 25.65 ? 142 PHE B O   1 
ATOM   2673 C  CB  . PHE B 1 147 ? 4.121   -10.463 4.631   1.00 26.04 ? 142 PHE B CB  1 
ATOM   2674 C  CG  . PHE B 1 147 ? 2.760   -10.618 5.290   1.00 25.60 ? 142 PHE B CG  1 
ATOM   2675 C  CD1 . PHE B 1 147 ? 1.893   -9.547  5.396   1.00 23.45 ? 142 PHE B CD1 1 
ATOM   2676 C  CD2 . PHE B 1 147 ? 2.338   -11.856 5.769   1.00 26.19 ? 142 PHE B CD2 1 
ATOM   2677 C  CE1 . PHE B 1 147 ? 0.618   -9.714  5.917   1.00 27.34 ? 142 PHE B CE1 1 
ATOM   2678 C  CE2 . PHE B 1 147 ? 1.075   -12.018 6.332   1.00 24.99 ? 142 PHE B CE2 1 
ATOM   2679 C  CZ  . PHE B 1 147 ? 0.204   -10.954 6.375   1.00 25.12 ? 142 PHE B CZ  1 
ATOM   2680 N  N   . GLY B 1 148 ? 5.792   -11.521 1.686   1.00 26.29 ? 143 GLY B N   1 
ATOM   2681 C  CA  . GLY B 1 148 ? 7.168   -11.873 1.309   1.00 27.55 ? 143 GLY B CA  1 
ATOM   2682 C  C   . GLY B 1 148 ? 7.541   -11.438 -0.098  1.00 29.36 ? 143 GLY B C   1 
ATOM   2683 O  O   . GLY B 1 148 ? 6.953   -10.476 -0.645  1.00 23.19 ? 143 GLY B O   1 
ATOM   2684 N  N   . ALA B 1 149 ? 8.517   -12.142 -0.663  1.00 30.53 ? 144 ALA B N   1 
ATOM   2685 C  CA  . ALA B 1 149 ? 9.207   -11.773 -1.910  1.00 30.65 ? 144 ALA B CA  1 
ATOM   2686 C  C   . ALA B 1 149 ? 9.523   -13.052 -2.695  1.00 29.44 ? 144 ALA B C   1 
ATOM   2687 O  O   . ALA B 1 149 ? 10.597  -13.132 -3.266  1.00 31.23 ? 144 ALA B O   1 
ATOM   2688 C  CB  . ALA B 1 149 ? 10.439  -10.971 -1.561  1.00 30.85 ? 144 ALA B CB  1 
ATOM   2689 N  N   . GLY B 1 150 ? 8.606   -14.023 -2.680  1.00 30.53 ? 145 GLY B N   1 
ATOM   2690 C  CA  . GLY B 1 150 ? 8.705   -15.284 -3.440  1.00 29.36 ? 145 GLY B CA  1 
ATOM   2691 C  C   . GLY B 1 150 ? 9.840   -16.175 -2.971  1.00 30.07 ? 145 GLY B C   1 
ATOM   2692 O  O   . GLY B 1 150 ? 10.302  -16.978 -3.754  1.00 29.97 ? 145 GLY B O   1 
ATOM   2693 N  N   . TRP B 1 151 ? 10.264  -16.078 -1.713  1.00 28.58 ? 146 TRP B N   1 
ATOM   2694 C  CA  . TRP B 1 151 ? 11.305  -16.984 -1.174  1.00 27.65 ? 146 TRP B CA  1 
ATOM   2695 C  C   . TRP B 1 151 ? 10.848  -18.446 -1.233  1.00 28.39 ? 146 TRP B C   1 
ATOM   2696 O  O   . TRP B 1 151 ? 9.693   -18.743 -0.877  1.00 24.87 ? 146 TRP B O   1 
ATOM   2697 C  CB  . TRP B 1 151 ? 11.693  -16.601 0.243   1.00 26.64 ? 146 TRP B CB  1 
ATOM   2698 C  CG  . TRP B 1 151 ? 12.790  -17.459 0.786   1.00 26.56 ? 146 TRP B CG  1 
ATOM   2699 C  CD1 . TRP B 1 151 ? 14.099  -17.464 0.408   1.00 24.80 ? 146 TRP B CD1 1 
ATOM   2700 C  CD2 . TRP B 1 151 ? 12.661  -18.454 1.820   1.00 24.61 ? 146 TRP B CD2 1 
ATOM   2701 N  NE1 . TRP B 1 151 ? 14.794  -18.382 1.148   1.00 26.14 ? 146 TRP B NE1 1 
ATOM   2702 C  CE2 . TRP B 1 151 ? 13.948  -19.007 2.020   1.00 24.38 ? 146 TRP B CE2 1 
ATOM   2703 C  CE3 . TRP B 1 151 ? 11.601  -18.904 2.610   1.00 24.45 ? 146 TRP B CE3 1 
ATOM   2704 C  CZ2 . TRP B 1 151 ? 14.205  -19.960 3.004   1.00 23.47 ? 146 TRP B CZ2 1 
ATOM   2705 C  CZ3 . TRP B 1 151 ? 11.853  -19.855 3.575   1.00 24.30 ? 146 TRP B CZ3 1 
ATOM   2706 C  CH2 . TRP B 1 151 ? 13.135  -20.383 3.758   1.00 25.66 ? 146 TRP B CH2 1 
ATOM   2707 N  N   . ASP B 1 152 ? 11.746  -19.315 -1.698  1.00 27.99 ? 147 ASP B N   1 
ATOM   2708 C  CA  . ASP B 1 152 ? 11.511  -20.770 -1.879  1.00 31.58 ? 147 ASP B CA  1 
ATOM   2709 C  C   . ASP B 1 152 ? 12.160  -21.484 -0.694  1.00 29.02 ? 147 ASP B C   1 
ATOM   2710 O  O   . ASP B 1 152 ? 13.397  -21.430 -0.558  1.00 27.83 ? 147 ASP B O   1 
ATOM   2711 C  CB  . ASP B 1 152 ? 12.058  -21.237 -3.229  1.00 34.48 ? 147 ASP B CB  1 
ATOM   2712 C  CG  . ASP B 1 152 ? 11.883  -22.718 -3.534  1.00 37.26 ? 147 ASP B CG  1 
ATOM   2713 O  OD1 . ASP B 1 152 ? 11.194  -23.430 -2.747  1.00 35.85 ? 147 ASP B OD1 1 
ATOM   2714 O  OD2 . ASP B 1 152 ? 12.468  -23.155 -4.546  1.00 42.85 ? 147 ASP B OD2 1 
ATOM   2715 N  N   . MET B 1 153 ? 11.347  -22.102 0.155   1.00 29.18 ? 148 MET B N   1 
ATOM   2716 C  CA  . MET B 1 153 ? 11.842  -22.793 1.372   1.00 29.56 ? 148 MET B CA  1 
ATOM   2717 C  C   . MET B 1 153 ? 12.595  -24.091 1.040   1.00 27.62 ? 148 MET B C   1 
ATOM   2718 O  O   . MET B 1 153 ? 13.196  -24.634 1.981   1.00 23.05 ? 148 MET B O   1 
ATOM   2719 C  CB  . MET B 1 153 ? 10.689  -23.102 2.319   1.00 28.95 ? 148 MET B CB  1 
ATOM   2720 C  CG  . MET B 1 153 ? 9.755   -24.170 1.848   1.00 29.75 ? 148 MET B CG  1 
ATOM   2721 S  SD  . MET B 1 153 ? 8.425   -24.325 3.068   1.00 29.88 ? 148 MET B SD  1 
ATOM   2722 C  CE  . MET B 1 153 ? 7.026   -23.692 2.145   1.00 28.47 ? 148 MET B CE  1 
ATOM   2723 N  N   . THR B 1 154 ? 12.566  -24.568 -0.220  1.00 31.96 ? 149 THR B N   1 
ATOM   2724 C  CA  . THR B 1 154 ? 12.977  -25.956 -0.611  1.00 33.67 ? 149 THR B CA  1 
ATOM   2725 C  C   . THR B 1 154 ? 14.395  -26.238 -0.108  1.00 32.16 ? 149 THR B C   1 
ATOM   2726 O  O   . THR B 1 154 ? 14.559  -27.255 0.568   1.00 36.36 ? 149 THR B O   1 
ATOM   2727 C  CB  . THR B 1 154 ? 12.884  -26.224 -2.121  1.00 35.59 ? 149 THR B CB  1 
ATOM   2728 O  OG1 . THR B 1 154 ? 11.525  -26.047 -2.524  1.00 34.73 ? 149 THR B OG1 1 
ATOM   2729 C  CG2 . THR B 1 154 ? 13.357  -27.620 -2.490  1.00 36.84 ? 149 THR B CG2 1 
ATOM   2730 N  N   . GLY B 1 155 ? 15.346  -25.347 -0.395  1.00 31.84 ? 150 GLY B N   1 
ATOM   2731 C  CA  . GLY B 1 155 ? 16.769  -25.463 -0.008  1.00 31.51 ? 150 GLY B CA  1 
ATOM   2732 C  C   . GLY B 1 155 ? 16.999  -25.289 1.490   1.00 32.09 ? 150 GLY B C   1 
ATOM   2733 O  O   . GLY B 1 155 ? 18.139  -25.494 1.953   1.00 33.10 ? 150 GLY B O   1 
ATOM   2734 N  N   . SER B 1 156 ? 15.991  -24.901 2.272   1.00 29.59 ? 151 SER B N   1 
ATOM   2735 C  CA  . SER B 1 156 ? 16.181  -24.715 3.736   1.00 30.12 ? 151 SER B CA  1 
ATOM   2736 C  C   . SER B 1 156 ? 15.470  -25.817 4.550   1.00 28.66 ? 151 SER B C   1 
ATOM   2737 O  O   . SER B 1 156 ? 15.510  -25.738 5.781   1.00 30.34 ? 151 SER B O   1 
ATOM   2738 C  CB  . SER B 1 156 ? 15.764  -23.313 4.144   1.00 30.39 ? 151 SER B CB  1 
ATOM   2739 O  OG  . SER B 1 156 ? 16.631  -22.348 3.567   1.00 33.10 ? 151 SER B OG  1 
ATOM   2740 N  N   . LEU B 1 157 ? 14.846  -26.813 3.917   1.00 32.49 ? 152 LEU B N   1 
ATOM   2741 C  CA  . LEU B 1 157 ? 14.015  -27.820 4.638   1.00 32.79 ? 152 LEU B CA  1 
ATOM   2742 C  C   . LEU B 1 157 ? 14.888  -28.631 5.609   1.00 35.50 ? 152 LEU B C   1 
ATOM   2743 O  O   . LEU B 1 157 ? 14.432  -28.875 6.747   1.00 35.19 ? 152 LEU B O   1 
ATOM   2744 C  CB  . LEU B 1 157 ? 13.291  -28.709 3.629   1.00 35.06 ? 152 LEU B CB  1 
ATOM   2745 C  CG  . LEU B 1 157 ? 12.140  -28.056 2.871   1.00 36.19 ? 152 LEU B CG  1 
ATOM   2746 C  CD1 . LEU B 1 157 ? 11.510  -29.055 1.909   1.00 36.69 ? 152 LEU B CD1 1 
ATOM   2747 C  CD2 . LEU B 1 157 ? 11.090  -27.498 3.821   1.00 38.52 ? 152 LEU B CD2 1 
ATOM   2748 N  N   . ASP B 1 158 ? 16.124  -28.972 5.235   1.00 33.90 ? 153 ASP B N   1 
ATOM   2749 C  CA  . ASP B 1 158 ? 17.075  -29.657 6.147   1.00 33.75 ? 153 ASP B CA  1 
ATOM   2750 C  C   . ASP B 1 158 ? 17.379  -28.758 7.342   1.00 32.08 ? 153 ASP B C   1 
ATOM   2751 O  O   . ASP B 1 158 ? 17.497  -29.287 8.461   1.00 31.20 ? 153 ASP B O   1 
ATOM   2752 C  CB  . ASP B 1 158 ? 18.386  -30.038 5.453   1.00 39.05 ? 153 ASP B CB  1 
ATOM   2753 C  CG  . ASP B 1 158 ? 18.330  -31.363 4.709   1.00 41.83 ? 153 ASP B CG  1 
ATOM   2754 O  OD1 . ASP B 1 158 ? 17.200  -31.869 4.475   1.00 45.13 ? 153 ASP B OD1 1 
ATOM   2755 O  OD2 . ASP B 1 158 ? 19.420  -31.876 4.368   1.00 47.52 ? 153 ASP B OD2 1 
ATOM   2756 N  N   . TYR B 1 159 ? 17.519  -27.449 7.120   1.00 28.99 ? 154 TYR B N   1 
ATOM   2757 C  CA  . TYR B 1 159 ? 17.765  -26.467 8.202   1.00 26.61 ? 154 TYR B CA  1 
ATOM   2758 C  C   . TYR B 1 159 ? 16.550  -26.448 9.141   1.00 25.62 ? 154 TYR B C   1 
ATOM   2759 O  O   . TYR B 1 159 ? 16.758  -26.459 10.366  1.00 24.01 ? 154 TYR B O   1 
ATOM   2760 C  CB  . TYR B 1 159 ? 18.117  -25.093 7.619   1.00 28.44 ? 154 TYR B CB  1 
ATOM   2761 C  CG  . TYR B 1 159 ? 18.224  -24.005 8.652   1.00 27.72 ? 154 TYR B CG  1 
ATOM   2762 C  CD1 . TYR B 1 159 ? 19.202  -24.061 9.634   1.00 29.23 ? 154 TYR B CD1 1 
ATOM   2763 C  CD2 . TYR B 1 159 ? 17.351  -22.922 8.651   1.00 27.55 ? 154 TYR B CD2 1 
ATOM   2764 C  CE1 . TYR B 1 159 ? 19.299  -23.084 10.606  1.00 32.14 ? 154 TYR B CE1 1 
ATOM   2765 C  CE2 . TYR B 1 159 ? 17.433  -21.937 9.620   1.00 26.96 ? 154 TYR B CE2 1 
ATOM   2766 C  CZ  . TYR B 1 159 ? 18.407  -22.021 10.606  1.00 29.83 ? 154 TYR B CZ  1 
ATOM   2767 O  OH  . TYR B 1 159 ? 18.527  -21.069 11.573  1.00 28.06 ? 154 TYR B OH  1 
ATOM   2768 N  N   . PHE B 1 160 ? 15.327  -26.446 8.600   1.00 25.35 ? 155 PHE B N   1 
ATOM   2769 C  CA  . PHE B 1 160 ? 14.085  -26.490 9.416   1.00 26.61 ? 155 PHE B CA  1 
ATOM   2770 C  C   . PHE B 1 160 ? 14.172  -27.708 10.352  1.00 29.57 ? 155 PHE B C   1 
ATOM   2771 O  O   . PHE B 1 160 ? 13.945  -27.551 11.571  1.00 31.68 ? 155 PHE B O   1 
ATOM   2772 C  CB  . PHE B 1 160 ? 12.815  -26.537 8.557   1.00 24.42 ? 155 PHE B CB  1 
ATOM   2773 C  CG  . PHE B 1 160 ? 12.444  -25.322 7.736   1.00 23.26 ? 155 PHE B CG  1 
ATOM   2774 C  CD1 . PHE B 1 160 ? 13.261  -24.212 7.640   1.00 22.77 ? 155 PHE B CD1 1 
ATOM   2775 C  CD2 . PHE B 1 160 ? 11.267  -25.331 6.995   1.00 24.92 ? 155 PHE B CD2 1 
ATOM   2776 C  CE1 . PHE B 1 160 ? 12.900  -23.131 6.850   1.00 24.87 ? 155 PHE B CE1 1 
ATOM   2777 C  CE2 . PHE B 1 160 ? 10.911  -24.258 6.192   1.00 24.85 ? 155 PHE B CE2 1 
ATOM   2778 C  CZ  . PHE B 1 160 ? 11.731  -23.156 6.114   1.00 24.17 ? 155 PHE B CZ  1 
ATOM   2779 N  N   . ARG B 1 161 ? 14.563  -28.871 9.809   1.00 32.17 ? 156 ARG B N   1 
ATOM   2780 C  CA  . ARG B 1 161 ? 14.637  -30.161 10.551  1.00 35.01 ? 156 ARG B CA  1 
ATOM   2781 C  C   . ARG B 1 161 ? 15.665  -30.012 11.667  1.00 31.49 ? 156 ARG B C   1 
ATOM   2782 O  O   . ARG B 1 161 ? 15.385  -30.420 12.803  1.00 32.65 ? 156 ARG B O   1 
ATOM   2783 C  CB  . ARG B 1 161 ? 14.976  -31.329 9.619   1.00 34.65 ? 156 ARG B CB  1 
ATOM   2784 C  CG  . ARG B 1 161 ? 13.841  -31.706 8.685   1.00 40.52 ? 156 ARG B CG  1 
ATOM   2785 C  CD  . ARG B 1 161 ? 14.157  -32.924 7.828   1.00 42.76 ? 156 ARG B CD  1 
ATOM   2786 N  NE  . ARG B 1 161 ? 12.991  -33.215 7.023   1.00 44.39 ? 156 ARG B NE  1 
ATOM   2787 C  CZ  . ARG B 1 161 ? 12.819  -32.880 5.746   1.00 48.83 ? 156 ARG B CZ  1 
ATOM   2788 N  NH1 . ARG B 1 161 ? 13.773  -32.259 5.066   1.00 51.06 ? 156 ARG B NH1 1 
ATOM   2789 N  NH2 . ARG B 1 161 ? 11.682  -33.189 5.145   1.00 47.02 ? 156 ARG B NH2 1 
ATOM   2790 N  N   . ARG B 1 162 ? 16.775  -29.364 11.353  1.00 32.23 ? 157 ARG B N   1 
ATOM   2791 C  CA  . ARG B 1 162 ? 17.911  -29.173 12.282  1.00 32.94 ? 157 ARG B CA  1 
ATOM   2792 C  C   . ARG B 1 162 ? 17.485  -28.363 13.518  1.00 31.39 ? 157 ARG B C   1 
ATOM   2793 O  O   . ARG B 1 162 ? 17.931  -28.710 14.616  1.00 30.43 ? 157 ARG B O   1 
ATOM   2794 C  CB  . ARG B 1 162 ? 19.055  -28.493 11.534  1.00 37.74 ? 157 ARG B CB  1 
ATOM   2795 C  CG  . ARG B 1 162 ? 20.432  -28.694 12.146  1.00 44.11 ? 157 ARG B CG  1 
ATOM   2796 C  CD  . ARG B 1 162 ? 21.468  -28.926 11.047  1.00 47.28 ? 157 ARG B CD  1 
ATOM   2797 N  NE  . ARG B 1 162 ? 21.640  -27.778 10.156  1.00 50.07 ? 157 ARG B NE  1 
ATOM   2798 C  CZ  . ARG B 1 162 ? 21.360  -27.730 8.844   1.00 52.31 ? 157 ARG B CZ  1 
ATOM   2799 N  NH1 . ARG B 1 162 ? 21.583  -26.607 8.186   1.00 51.00 ? 157 ARG B NH1 1 
ATOM   2800 N  NH2 . ARG B 1 162 ? 20.867  -28.771 8.185   1.00 56.70 ? 157 ARG B NH2 1 
ATOM   2801 N  N   . ILE B 1 163 ? 16.674  -27.314 13.367  1.00 31.40 ? 158 ILE B N   1 
ATOM   2802 C  CA  . ILE B 1 163 ? 16.308  -26.412 14.505  1.00 29.65 ? 158 ILE B CA  1 
ATOM   2803 C  C   . ILE B 1 163 ? 14.931  -26.815 15.047  1.00 28.24 ? 158 ILE B C   1 
ATOM   2804 O  O   . ILE B 1 163 ? 14.496  -26.181 16.022  1.00 28.56 ? 158 ILE B O   1 
ATOM   2805 C  CB  . ILE B 1 163 ? 16.342  -24.921 14.090  1.00 28.33 ? 158 ILE B CB  1 
ATOM   2806 C  CG1 . ILE B 1 163 ? 15.329  -24.619 12.992  1.00 28.46 ? 158 ILE B CG1 1 
ATOM   2807 C  CG2 . ILE B 1 163 ? 17.746  -24.488 13.691  1.00 30.55 ? 158 ILE B CG2 1 
ATOM   2808 C  CD1 . ILE B 1 163 ? 15.162  -23.151 12.671  1.00 31.27 ? 158 ILE B CD1 1 
ATOM   2809 N  N   . LEU B 1 164 ? 14.289  -27.831 14.462  1.00 31.09 ? 159 LEU B N   1 
ATOM   2810 C  CA  . LEU B 1 164 ? 12.877  -28.209 14.765  1.00 31.73 ? 159 LEU B CA  1 
ATOM   2811 C  C   . LEU B 1 164 ? 12.652  -28.502 16.261  1.00 31.49 ? 159 LEU B C   1 
ATOM   2812 O  O   . LEU B 1 164 ? 11.557  -28.246 16.794  1.00 33.74 ? 159 LEU B O   1 
ATOM   2813 C  CB  . LEU B 1 164 ? 12.461  -29.418 13.917  1.00 31.53 ? 159 LEU B CB  1 
ATOM   2814 C  CG  . LEU B 1 164 ? 10.947  -29.636 13.831  1.00 29.56 ? 159 LEU B CG  1 
ATOM   2815 C  CD1 . LEU B 1 164 ? 10.285  -28.483 13.099  1.00 29.33 ? 159 LEU B CD1 1 
ATOM   2816 C  CD2 . LEU B 1 164 ? 10.616  -30.961 13.166  1.00 33.61 ? 159 LEU B CD2 1 
ATOM   2817 N  N   . PRO B 1 165 ? 13.636  -29.035 17.017  1.00 29.63 ? 160 PRO B N   1 
ATOM   2818 C  CA  . PRO B 1 165 ? 13.400  -29.375 18.437  1.00 27.82 ? 160 PRO B CA  1 
ATOM   2819 C  C   . PRO B 1 165 ? 12.968  -28.231 19.369  1.00 26.25 ? 160 PRO B C   1 
ATOM   2820 O  O   . PRO B 1 165 ? 12.309  -28.479 20.354  1.00 29.94 ? 160 PRO B O   1 
ATOM   2821 C  CB  . PRO B 1 165 ? 14.747  -29.937 18.876  1.00 25.51 ? 160 PRO B CB  1 
ATOM   2822 C  CG  . PRO B 1 165 ? 15.286  -30.523 17.591  1.00 28.97 ? 160 PRO B CG  1 
ATOM   2823 C  CD  . PRO B 1 165 ? 14.970  -29.452 16.561  1.00 29.88 ? 160 PRO B CD  1 
ATOM   2824 N  N   . GLY B 1 166 ? 13.304  -26.983 19.058  1.00 26.81 ? 161 GLY B N   1 
ATOM   2825 C  CA  . GLY B 1 166 ? 12.874  -25.851 19.892  1.00 22.93 ? 161 GLY B CA  1 
ATOM   2826 C  C   . GLY B 1 166 ? 11.444  -25.438 19.576  1.00 23.76 ? 161 GLY B C   1 
ATOM   2827 O  O   . GLY B 1 166 ? 10.909  -24.633 20.327  1.00 24.94 ? 161 GLY B O   1 
ATOM   2828 N  N   . VAL B 1 167 ? 10.848  -25.940 18.501  1.00 24.80 ? 162 VAL B N   1 
ATOM   2829 C  CA  . VAL B 1 167 ? 9.506   -25.476 18.046  1.00 28.89 ? 162 VAL B CA  1 
ATOM   2830 C  C   . VAL B 1 167 ? 8.456   -26.045 19.000  1.00 29.52 ? 162 VAL B C   1 
ATOM   2831 O  O   . VAL B 1 167 ? 8.390   -27.268 19.145  1.00 30.57 ? 162 VAL B O   1 
ATOM   2832 C  CB  . VAL B 1 167 ? 9.186   -25.852 16.587  1.00 28.38 ? 162 VAL B CB  1 
ATOM   2833 C  CG1 . VAL B 1 167 ? 7.835   -25.295 16.153  1.00 24.89 ? 162 VAL B CG1 1 
ATOM   2834 C  CG2 . VAL B 1 167 ? 10.297  -25.392 15.634  1.00 32.06 ? 162 VAL B CG2 1 
ATOM   2835 N  N   . GLY B 1 168 ? 7.700   -25.162 19.639  1.00 25.77 ? 163 GLY B N   1 
ATOM   2836 C  CA  . GLY B 1 168 ? 6.474   -25.532 20.356  1.00 24.75 ? 163 GLY B CA  1 
ATOM   2837 C  C   . GLY B 1 168 ? 5.268   -25.247 19.506  1.00 22.58 ? 163 GLY B C   1 
ATOM   2838 O  O   . GLY B 1 168 ? 4.785   -24.110 19.536  1.00 27.26 ? 163 GLY B O   1 
ATOM   2839 N  N   . ALA B 1 169 ? 4.868   -26.210 18.701  1.00 20.78 ? 164 ALA B N   1 
ATOM   2840 C  CA  . ALA B 1 169 ? 3.783   -26.046 17.728  1.00 21.54 ? 164 ALA B CA  1 
ATOM   2841 C  C   . ALA B 1 169 ? 2.501   -26.386 18.461  1.00 21.36 ? 164 ALA B C   1 
ATOM   2842 O  O   . ALA B 1 169 ? 2.579   -27.248 19.316  1.00 23.18 ? 164 ALA B O   1 
ATOM   2843 C  CB  . ALA B 1 169 ? 4.000   -26.939 16.547  1.00 22.01 ? 164 ALA B CB  1 
ATOM   2844 N  N   . PHE B 1 170 ? 1.374   -25.767 18.104  1.00 23.56 ? 165 PHE B N   1 
ATOM   2845 C  CA  . PHE B 1 170 ? 0.071   -26.022 18.776  1.00 22.55 ? 165 PHE B CA  1 
ATOM   2846 C  C   . PHE B 1 170 ? -1.081  -25.898 17.801  1.00 23.92 ? 165 PHE B C   1 
ATOM   2847 O  O   . PHE B 1 170 ? -0.915  -25.345 16.676  1.00 23.43 ? 165 PHE B O   1 
ATOM   2848 C  CB  . PHE B 1 170 ? -0.127  -25.059 19.940  1.00 24.10 ? 165 PHE B CB  1 
ATOM   2849 C  CG  . PHE B 1 170 ? -0.064  -23.591 19.591  1.00 25.39 ? 165 PHE B CG  1 
ATOM   2850 C  CD1 . PHE B 1 170 ? 1.144   -22.904 19.624  1.00 24.29 ? 165 PHE B CD1 1 
ATOM   2851 C  CD2 . PHE B 1 170 ? -1.213  -22.891 19.264  1.00 26.39 ? 165 PHE B CD2 1 
ATOM   2852 C  CE1 . PHE B 1 170 ? 1.194   -21.549 19.328  1.00 28.14 ? 165 PHE B CE1 1 
ATOM   2853 C  CE2 . PHE B 1 170 ? -1.160  -21.534 18.960  1.00 26.99 ? 165 PHE B CE2 1 
ATOM   2854 C  CZ  . PHE B 1 170 ? 0.041   -20.861 18.993  1.00 25.21 ? 165 PHE B CZ  1 
ATOM   2855 N  N   . ARG B 1 171 ? -2.242  -26.329 18.278  1.00 25.18 ? 166 ARG B N   1 
ATOM   2856 C  CA  . ARG B 1 171 ? -3.538  -26.270 17.571  1.00 25.11 ? 166 ARG B CA  1 
ATOM   2857 C  C   . ARG B 1 171 ? -4.569  -25.621 18.506  1.00 27.53 ? 166 ARG B C   1 
ATOM   2858 O  O   . ARG B 1 171 ? -4.711  -26.059 19.647  1.00 28.53 ? 166 ARG B O   1 
ATOM   2859 C  CB  . ARG B 1 171 ? -3.950  -27.693 17.184  1.00 27.63 ? 166 ARG B CB  1 
ATOM   2860 C  CG  . ARG B 1 171 ? -2.931  -28.434 16.328  1.00 28.16 ? 166 ARG B CG  1 
ATOM   2861 C  CD  . ARG B 1 171 ? -2.940  -27.882 14.917  1.00 27.71 ? 166 ARG B CD  1 
ATOM   2862 N  NE  . ARG B 1 171 ? -2.094  -28.577 13.961  1.00 28.72 ? 166 ARG B NE  1 
ATOM   2863 C  CZ  . ARG B 1 171 ? -0.829  -28.268 13.677  1.00 28.01 ? 166 ARG B CZ  1 
ATOM   2864 N  NH1 . ARG B 1 171 ? -0.220  -27.277 14.302  1.00 26.17 ? 166 ARG B NH1 1 
ATOM   2865 N  NH2 . ARG B 1 171 ? -0.165  -28.980 12.781  1.00 30.78 ? 166 ARG B NH2 1 
ATOM   2866 N  N   . LEU B 1 172 ? -5.278  -24.612 18.029  1.00 28.58 ? 167 LEU B N   1 
ATOM   2867 C  CA  . LEU B 1 172 ? -6.370  -23.951 18.782  1.00 28.86 ? 167 LEU B CA  1 
ATOM   2868 C  C   . LEU B 1 172 ? -7.675  -24.191 18.021  1.00 29.96 ? 167 LEU B C   1 
ATOM   2869 O  O   . LEU B 1 172 ? -7.834  -23.666 16.915  1.00 28.93 ? 167 LEU B O   1 
ATOM   2870 C  CB  . LEU B 1 172 ? -6.027  -22.471 18.904  1.00 32.35 ? 167 LEU B CB  1 
ATOM   2871 C  CG  . LEU B 1 172 ? -7.026  -21.607 19.657  1.00 35.17 ? 167 LEU B CG  1 
ATOM   2872 C  CD1 . LEU B 1 172 ? -7.287  -22.175 21.044  1.00 38.69 ? 167 LEU B CD1 1 
ATOM   2873 C  CD2 . LEU B 1 172 ? -6.483  -20.194 19.738  1.00 36.59 ? 167 LEU B CD2 1 
ATOM   2874 N  N   . ARG B 1 173 ? -8.513  -25.064 18.561  1.00 33.78 ? 168 ARG B N   1 
ATOM   2875 C  CA  . ARG B 1 173 ? -9.914  -25.258 18.131  1.00 33.80 ? 168 ARG B CA  1 
ATOM   2876 C  C   . ARG B 1 173 ? -10.677 -24.006 18.585  1.00 29.36 ? 168 ARG B C   1 
ATOM   2877 O  O   . ARG B 1 173 ? -10.786 -23.760 19.791  1.00 32.16 ? 168 ARG B O   1 
ATOM   2878 C  CB  . ARG B 1 173 ? -10.481 -26.593 18.643  1.00 40.30 ? 168 ARG B CB  1 
ATOM   2879 C  CG  . ARG B 1 173 ? -9.927  -27.073 19.980  1.00 50.11 ? 168 ARG B CG  1 
ATOM   2880 C  CD  . ARG B 1 173 ? -10.760 -28.085 20.782  1.00 57.76 ? 168 ARG B CD  1 
ATOM   2881 N  NE  . ARG B 1 173 ? -12.194 -27.799 20.957  1.00 61.47 ? 168 ARG B NE  1 
ATOM   2882 C  CZ  . ARG B 1 173 ? -12.742 -26.700 21.507  1.00 64.37 ? 168 ARG B CZ  1 
ATOM   2883 N  NH1 . ARG B 1 173 ? -14.060 -26.611 21.580  1.00 67.85 ? 168 ARG B NH1 1 
ATOM   2884 N  NH2 . ARG B 1 173 ? -12.008 -25.686 21.946  1.00 54.65 ? 168 ARG B NH2 1 
ATOM   2885 N  N   . VAL B 1 174 ? -11.116 -23.181 17.634  1.00 28.54 ? 169 VAL B N   1 
ATOM   2886 C  CA  . VAL B 1 174 ? -11.877 -21.935 17.930  1.00 28.82 ? 169 VAL B CA  1 
ATOM   2887 C  C   . VAL B 1 174 ? -13.285 -22.326 18.406  1.00 29.25 ? 169 VAL B C   1 
ATOM   2888 O  O   . VAL B 1 174 ? -14.039 -22.854 17.587  1.00 28.13 ? 169 VAL B O   1 
ATOM   2889 C  CB  . VAL B 1 174 ? -11.946 -20.980 16.730  1.00 27.46 ? 169 VAL B CB  1 
ATOM   2890 C  CG1 . VAL B 1 174 ? -12.711 -19.727 17.104  1.00 27.90 ? 169 VAL B CG1 1 
ATOM   2891 C  CG2 . VAL B 1 174 ? -10.556 -20.639 16.193  1.00 27.36 ? 169 VAL B CG2 1 
ATOM   2892 N  N   . ALA B 1 175 ? -13.584 -22.074 19.687  1.00 27.11 ? 170 ALA B N   1 
ATOM   2893 C  CA  . ALA B 1 175 ? -14.906 -22.272 20.310  1.00 29.01 ? 170 ALA B CA  1 
ATOM   2894 C  C   . ALA B 1 175 ? -15.721 -20.973 20.210  1.00 30.34 ? 170 ALA B C   1 
ATOM   2895 O  O   . ALA B 1 175 ? -16.942 -21.058 20.049  1.00 29.80 ? 170 ALA B O   1 
ATOM   2896 C  CB  . ALA B 1 175 ? -14.710 -22.727 21.731  1.00 28.48 ? 170 ALA B CB  1 
ATOM   2897 N  N   . GLU B 1 176 ? -15.062 -19.820 20.324  1.00 28.78 ? 171 GLU B N   1 
ATOM   2898 C  CA  . GLU B 1 176 ? -15.676 -18.466 20.298  1.00 31.11 ? 171 GLU B CA  1 
ATOM   2899 C  C   . GLU B 1 176 ? -14.783 -17.567 19.441  1.00 29.28 ? 171 GLU B C   1 
ATOM   2900 O  O   . GLU B 1 176 ? -13.538 -17.680 19.569  1.00 26.16 ? 171 GLU B O   1 
ATOM   2901 C  CB  . GLU B 1 176 ? -15.765 -17.839 21.693  1.00 35.88 ? 171 GLU B CB  1 
ATOM   2902 C  CG  . GLU B 1 176 ? -16.709 -18.533 22.663  1.00 45.74 ? 171 GLU B CG  1 
ATOM   2903 C  CD  . GLU B 1 176 ? -16.625 -18.057 24.111  1.00 52.82 ? 171 GLU B CD  1 
ATOM   2904 O  OE1 . GLU B 1 176 ? -17.228 -16.999 24.441  1.00 52.35 ? 171 GLU B OE1 1 
ATOM   2905 O  OE2 . GLU B 1 176 ? -15.942 -18.737 24.915  1.00 56.77 ? 171 GLU B OE2 1 
ATOM   2906 N  N   . ALA B 1 177 ? -15.380 -16.714 18.611  1.00 26.47 ? 172 ALA B N   1 
ATOM   2907 C  CA  . ALA B 1 177 ? -14.654 -15.712 17.789  1.00 28.32 ? 172 ALA B CA  1 
ATOM   2908 C  C   . ALA B 1 177 ? -15.428 -14.405 17.868  1.00 26.00 ? 172 ALA B C   1 
ATOM   2909 O  O   . ALA B 1 177 ? -16.640 -14.436 17.656  1.00 27.18 ? 172 ALA B O   1 
ATOM   2910 C  CB  . ALA B 1 177 ? -14.498 -16.163 16.368  1.00 27.29 ? 172 ALA B CB  1 
ATOM   2911 N  N   . ASP B 1 178 ? -14.773 -13.336 18.285  1.00 29.24 ? 173 ASP B N   1 
ATOM   2912 C  CA  . ASP B 1 178 ? -15.384 -11.988 18.414  1.00 29.23 ? 173 ASP B CA  1 
ATOM   2913 C  C   . ASP B 1 178 ? -14.508 -10.989 17.653  1.00 27.10 ? 173 ASP B C   1 
ATOM   2914 O  O   . ASP B 1 178 ? -13.304 -11.034 17.798  1.00 23.29 ? 173 ASP B O   1 
ATOM   2915 C  CB  . ASP B 1 178 ? -15.573 -11.624 19.888  1.00 34.30 ? 173 ASP B CB  1 
ATOM   2916 C  CG  . ASP B 1 178 ? -16.652 -12.439 20.601  1.00 41.21 ? 173 ASP B CG  1 
ATOM   2917 O  OD1 . ASP B 1 178 ? -17.867 -12.229 20.278  1.00 41.71 ? 173 ASP B OD1 1 
ATOM   2918 O  OD2 . ASP B 1 178 ? -16.275 -13.292 21.469  1.00 45.18 ? 173 ASP B OD2 1 
ATOM   2919 N  N   . GLY B 1 179 ? -15.149 -10.088 16.922  1.00 26.04 ? 174 GLY B N   1 
ATOM   2920 C  CA  . GLY B 1 179 ? -14.511 -9.044  16.117  1.00 27.56 ? 174 GLY B CA  1 
ATOM   2921 C  C   . GLY B 1 179 ? -14.965 -7.665  16.532  1.00 25.72 ? 174 GLY B C   1 
ATOM   2922 O  O   . GLY B 1 179 ? -16.208 -7.391  16.520  1.00 25.37 ? 174 GLY B O   1 
ATOM   2923 N  N   . MET B 1 180 ? -13.994 -6.817  16.853  1.00 24.68 ? 175 MET B N   1 
ATOM   2924 C  CA  . MET B 1 180 ? -14.203 -5.364  17.079  1.00 26.30 ? 175 MET B CA  1 
ATOM   2925 C  C   . MET B 1 180 ? -13.786 -4.619  15.820  1.00 22.85 ? 175 MET B C   1 
ATOM   2926 O  O   . MET B 1 180 ? -12.577 -4.682  15.448  1.00 22.95 ? 175 MET B O   1 
ATOM   2927 C  CB  . MET B 1 180 ? -13.378 -4.897  18.278  1.00 30.68 ? 175 MET B CB  1 
ATOM   2928 C  CG  . MET B 1 180 ? -13.388 -3.395  18.479  1.00 33.90 ? 175 MET B CG  1 
ATOM   2929 S  SD  . MET B 1 180 ? -14.841 -2.855  19.404  1.00 36.68 ? 175 MET B SD  1 
ATOM   2930 C  CE  . MET B 1 180 ? -14.344 -3.273  21.075  1.00 32.59 ? 175 MET B CE  1 
ATOM   2931 N  N   . PHE B 1 181 ? -14.744 -4.038  15.116  1.00 21.08 ? 176 PHE B N   1 
ATOM   2932 C  CA  . PHE B 1 181 ? -14.483 -3.150  13.951  1.00 23.18 ? 176 PHE B CA  1 
ATOM   2933 C  C   . PHE B 1 181 ? -14.935 -1.742  14.353  1.00 23.52 ? 176 PHE B C   1 
ATOM   2934 O  O   . PHE B 1 181 ? -16.018 -1.317  14.002  1.00 21.86 ? 176 PHE B O   1 
ATOM   2935 C  CB  . PHE B 1 181 ? -15.056 -3.727  12.650  1.00 22.68 ? 176 PHE B CB  1 
ATOM   2936 C  CG  . PHE B 1 181 ? -14.350 -4.999  12.244  1.00 27.00 ? 176 PHE B CG  1 
ATOM   2937 C  CD1 . PHE B 1 181 ? -14.639 -6.199  12.875  1.00 28.15 ? 176 PHE B CD1 1 
ATOM   2938 C  CD2 . PHE B 1 181 ? -13.314 -4.973  11.325  1.00 28.20 ? 176 PHE B CD2 1 
ATOM   2939 C  CE1 . PHE B 1 181 ? -13.977 -7.365  12.542  1.00 27.54 ? 176 PHE B CE1 1 
ATOM   2940 C  CE2 . PHE B 1 181 ? -12.639 -6.142  11.005  1.00 30.15 ? 176 PHE B CE2 1 
ATOM   2941 C  CZ  . PHE B 1 181 ? -12.976 -7.330  11.610  1.00 27.87 ? 176 PHE B CZ  1 
ATOM   2942 N  N   . LYS B 1 182 ? -14.086 -1.064  15.118  1.00 23.58 ? 177 LYS B N   1 
ATOM   2943 C  CA  . LYS B 1 182 ? -14.372 0.273   15.680  1.00 26.74 ? 177 LYS B CA  1 
ATOM   2944 C  C   . LYS B 1 182 ? -13.982 1.290   14.606  1.00 26.65 ? 177 LYS B C   1 
ATOM   2945 O  O   . LYS B 1 182 ? -12.802 1.678   14.536  1.00 25.64 ? 177 LYS B O   1 
ATOM   2946 C  CB  . LYS B 1 182 ? -13.677 0.452   17.023  1.00 26.15 ? 177 LYS B CB  1 
ATOM   2947 C  CG  . LYS B 1 182 ? -14.030 1.758   17.710  1.00 29.80 ? 177 LYS B CG  1 
ATOM   2948 C  CD  . LYS B 1 182 ? -13.669 1.754   19.175  1.00 34.01 ? 177 LYS B CD  1 
ATOM   2949 C  CE  . LYS B 1 182 ? -13.684 3.130   19.801  1.00 36.44 ? 177 LYS B CE  1 
ATOM   2950 N  NZ  . LYS B 1 182 ? -14.794 3.965   19.265  1.00 41.45 ? 177 LYS B NZ  1 
ATOM   2951 N  N   . LEU B 1 183 ? -14.945 1.637   13.753  1.00 25.20 ? 178 LEU B N   1 
ATOM   2952 C  CA  . LEU B 1 183 ? -14.681 2.376   12.495  1.00 27.41 ? 178 LEU B CA  1 
ATOM   2953 C  C   . LEU B 1 183 ? -15.709 3.514   12.339  1.00 27.25 ? 178 LEU B C   1 
ATOM   2954 O  O   . LEU B 1 183 ? -16.211 3.695   11.228  1.00 28.05 ? 178 LEU B O   1 
ATOM   2955 C  CB  . LEU B 1 183 ? -14.726 1.363   11.347  1.00 24.61 ? 178 LEU B CB  1 
ATOM   2956 C  CG  . LEU B 1 183 ? -13.672 0.249   11.374  1.00 23.87 ? 178 LEU B CG  1 
ATOM   2957 C  CD1 . LEU B 1 183 ? -13.984 -0.786  10.321  1.00 26.77 ? 178 LEU B CD1 1 
ATOM   2958 C  CD2 . LEU B 1 183 ? -12.280 0.802   11.141  1.00 23.96 ? 178 LEU B CD2 1 
ATOM   2959 N  N   . SER B 1 184 ? -16.004 4.243   13.418  1.00 27.73 ? 179 SER B N   1 
ATOM   2960 C  CA  . SER B 1 184 ? -16.831 5.486   13.427  1.00 28.95 ? 179 SER B CA  1 
ATOM   2961 C  C   . SER B 1 184 ? -18.308 5.197   13.038  1.00 25.84 ? 179 SER B C   1 
ATOM   2962 O  O   . SER B 1 184 ? -19.043 6.152   12.722  1.00 24.33 ? 179 SER B O   1 
ATOM   2963 C  CB  . SER B 1 184 ? -16.209 6.553   12.557  1.00 28.92 ? 179 SER B CB  1 
ATOM   2964 O  OG  . SER B 1 184 ? -14.819 6.737   12.836  1.00 27.82 ? 179 SER B OG  1 
ATOM   2965 N  N   . GLN B 1 185 ? -18.773 3.963   13.175  1.00 25.95 ? 180 GLN B N   1 
ATOM   2966 C  CA  . GLN B 1 185 ? -20.181 3.606   12.829  1.00 30.05 ? 180 GLN B CA  1 
ATOM   2967 C  C   . GLN B 1 185 ? -21.170 4.367   13.728  1.00 30.67 ? 180 GLN B C   1 
ATOM   2968 O  O   . GLN B 1 185 ? -22.315 4.504   13.296  1.00 37.08 ? 180 GLN B O   1 
ATOM   2969 C  CB  . GLN B 1 185 ? -20.436 2.103   12.924  1.00 31.71 ? 180 GLN B CB  1 
ATOM   2970 C  CG  . GLN B 1 185 ? -19.644 1.264   11.918  1.00 32.48 ? 180 GLN B CG  1 
ATOM   2971 C  CD  . GLN B 1 185 ? -18.446 0.618   12.569  1.00 32.74 ? 180 GLN B CD  1 
ATOM   2972 O  OE1 . GLN B 1 185 ? -17.686 1.280   13.282  1.00 29.76 ? 180 GLN B OE1 1 
ATOM   2973 N  NE2 . GLN B 1 185 ? -18.286 -0.683  12.349  1.00 32.46 ? 180 GLN B NE2 1 
ATOM   2974 N  N   . GLU B 1 186 ? -20.762 4.800   14.930  1.00 32.72 ? 181 GLU B N   1 
ATOM   2975 C  CA  . GLU B 1 186 ? -21.597 5.523   15.935  1.00 33.71 ? 181 GLU B CA  1 
ATOM   2976 C  C   . GLU B 1 186 ? -21.829 6.980   15.504  1.00 35.80 ? 181 GLU B C   1 
ATOM   2977 O  O   . GLU B 1 186 ? -22.689 7.657   16.126  1.00 37.12 ? 181 GLU B O   1 
ATOM   2978 C  CB  . GLU B 1 186 ? -20.948 5.489   17.324  1.00 35.66 ? 181 GLU B CB  1 
ATOM   2979 C  CG  . GLU B 1 186 ? -19.813 6.509   17.548  1.00 41.88 ? 181 GLU B CG  1 
ATOM   2980 C  CD  . GLU B 1 186 ? -18.437 6.254   16.917  1.00 50.34 ? 181 GLU B CD  1 
ATOM   2981 O  OE1 . GLU B 1 186 ? -18.281 5.225   16.216  1.00 50.20 ? 181 GLU B OE1 1 
ATOM   2982 O  OE2 . GLU B 1 186 ? -17.501 7.096   17.113  1.00 47.80 ? 181 GLU B OE2 1 
ATOM   2983 N  N   . GLN B 1 187 ? -21.054 7.485   14.539  1.00 36.54 ? 182 GLN B N   1 
ATOM   2984 C  CA  . GLN B 1 187 ? -21.157 8.887   14.037  1.00 36.24 ? 182 GLN B CA  1 
ATOM   2985 C  C   . GLN B 1 187 ? -22.205 8.982   12.912  1.00 34.52 ? 182 GLN B C   1 
ATOM   2986 O  O   . GLN B 1 187 ? -22.488 7.959   12.258  1.00 30.82 ? 182 GLN B O   1 
ATOM   2987 C  CB  . GLN B 1 187 ? -19.786 9.384   13.578  1.00 36.19 ? 182 GLN B CB  1 
ATOM   2988 C  CG  . GLN B 1 187 ? -18.725 9.313   14.670  1.00 35.26 ? 182 GLN B CG  1 
ATOM   2989 C  CD  . GLN B 1 187 ? -19.067 10.248  15.799  1.00 37.30 ? 182 GLN B CD  1 
ATOM   2990 O  OE1 . GLN B 1 187 ? -20.066 10.960  15.749  1.00 38.58 ? 182 GLN B OE1 1 
ATOM   2991 N  NE2 . GLN B 1 187 ? -18.218 10.270  16.810  1.00 38.17 ? 182 GLN B NE2 1 
ATOM   2992 N  N   . GLN B 1 188 ? -22.754 10.185  12.703  1.00 36.26 ? 183 GLN B N   1 
ATOM   2993 C  CA  . GLN B 1 188 ? -23.642 10.526  11.558  1.00 38.69 ? 183 GLN B CA  1 
ATOM   2994 C  C   . GLN B 1 188 ? -22.857 10.297  10.264  1.00 38.68 ? 183 GLN B C   1 
ATOM   2995 O  O   . GLN B 1 188 ? -21.633 10.407  10.259  1.00 35.93 ? 183 GLN B O   1 
ATOM   2996 C  CB  . GLN B 1 188 ? -24.158 11.969  11.686  1.00 41.35 ? 183 GLN B CB  1 
ATOM   2997 C  CG  . GLN B 1 188 ? -24.992 12.244  12.940  1.00 41.90 ? 183 GLN B CG  1 
ATOM   2998 C  CD  . GLN B 1 188 ? -26.133 11.271  13.108  1.00 43.63 ? 183 GLN B CD  1 
ATOM   2999 O  OE1 . GLN B 1 188 ? -26.380 10.750  14.196  1.00 50.72 ? 183 GLN B OE1 1 
ATOM   3000 N  NE2 . GLN B 1 188 ? -26.815 10.979  12.014  1.00 43.03 ? 183 GLN B NE2 1 
ATOM   3001 N  N   . PRO B 1 189 ? -23.525 9.942   9.143   1.00 45.03 ? 184 PRO B N   1 
ATOM   3002 C  CA  . PRO B 1 189 ? -22.842 9.716   7.861   1.00 45.19 ? 184 PRO B CA  1 
ATOM   3003 C  C   . PRO B 1 189 ? -21.849 10.806  7.414   1.00 40.63 ? 184 PRO B C   1 
ATOM   3004 O  O   . PRO B 1 189 ? -20.797 10.443  6.915   1.00 36.48 ? 184 PRO B O   1 
ATOM   3005 C  CB  . PRO B 1 189 ? -24.011 9.642   6.864   1.00 48.63 ? 184 PRO B CB  1 
ATOM   3006 C  CG  . PRO B 1 189 ? -25.154 9.063   7.689   1.00 47.77 ? 184 PRO B CG  1 
ATOM   3007 C  CD  . PRO B 1 189 ? -24.975 9.679   9.062   1.00 46.84 ? 184 PRO B CD  1 
ATOM   3008 N  N   . ALA B 1 190 ? -22.201 12.085  7.593   1.00 41.42 ? 185 ALA B N   1 
ATOM   3009 C  CA  . ALA B 1 190 ? -21.396 13.271  7.206   1.00 39.27 ? 185 ALA B CA  1 
ATOM   3010 C  C   . ALA B 1 190 ? -20.045 13.217  7.924   1.00 40.13 ? 185 ALA B C   1 
ATOM   3011 O  O   . ALA B 1 190 ? -19.009 13.502  7.294   1.00 36.49 ? 185 ALA B O   1 
ATOM   3012 C  CB  . ALA B 1 190 ? -22.120 14.541  7.559   1.00 39.26 ? 185 ALA B CB  1 
ATOM   3013 N  N   . ILE B 1 191 ? -20.071 12.856  9.207   1.00 38.18 ? 186 ILE B N   1 
ATOM   3014 C  CA  . ILE B 1 191 ? -18.863 12.815  10.069  1.00 37.99 ? 186 ILE B CA  1 
ATOM   3015 C  C   . ILE B 1 191 ? -18.049 11.575  9.691   1.00 36.87 ? 186 ILE B C   1 
ATOM   3016 O  O   . ILE B 1 191 ? -16.826 11.717  9.586   1.00 35.98 ? 186 ILE B O   1 
ATOM   3017 C  CB  . ILE B 1 191 ? -19.248 12.892  11.557  1.00 37.18 ? 186 ILE B CB  1 
ATOM   3018 C  CG1 . ILE B 1 191 ? -19.790 14.293  11.865  1.00 41.04 ? 186 ILE B CG1 1 
ATOM   3019 C  CG2 . ILE B 1 191 ? -18.075 12.522  12.460  1.00 32.02 ? 186 ILE B CG2 1 
ATOM   3020 C  CD1 . ILE B 1 191 ? -20.816 14.326  12.966  1.00 44.71 ? 186 ILE B CD1 1 
ATOM   3021 N  N   . ARG B 1 192 ? -18.704 10.432  9.471   1.00 36.48 ? 187 ARG B N   1 
ATOM   3022 C  CA  . ARG B 1 192 ? -18.057 9.185   8.970   1.00 39.38 ? 187 ARG B CA  1 
ATOM   3023 C  C   . ARG B 1 192 ? -17.296 9.515   7.677   1.00 35.91 ? 187 ARG B C   1 
ATOM   3024 O  O   . ARG B 1 192 ? -16.153 9.044   7.502   1.00 32.61 ? 187 ARG B O   1 
ATOM   3025 C  CB  . ARG B 1 192 ? -19.081 8.067   8.725   1.00 41.09 ? 187 ARG B CB  1 
ATOM   3026 C  CG  . ARG B 1 192 ? -19.851 7.625   9.966   1.00 46.58 ? 187 ARG B CG  1 
ATOM   3027 C  CD  . ARG B 1 192 ? -20.696 6.370   9.783   1.00 50.92 ? 187 ARG B CD  1 
ATOM   3028 N  NE  . ARG B 1 192 ? -20.059 5.453   8.854   1.00 58.32 ? 187 ARG B NE  1 
ATOM   3029 C  CZ  . ARG B 1 192 ? -18.859 4.884   9.031   1.00 67.71 ? 187 ARG B CZ  1 
ATOM   3030 N  NH1 . ARG B 1 192 ? -18.362 4.079   8.106   1.00 77.84 ? 187 ARG B NH1 1 
ATOM   3031 N  NH2 . ARG B 1 192 ? -18.143 5.117   10.116  1.00 71.08 ? 187 ARG B NH2 1 
ATOM   3032 N  N   . ARG B 1 193 ? -17.913 10.287  6.792   1.00 33.52 ? 188 ARG B N   1 
ATOM   3033 C  CA  . ARG B 1 193 ? -17.303 10.639  5.487   1.00 36.44 ? 188 ARG B CA  1 
ATOM   3034 C  C   . ARG B 1 193 ? -16.084 11.543  5.731   1.00 35.00 ? 188 ARG B C   1 
ATOM   3035 O  O   . ARG B 1 193 ? -15.014 11.301  5.108   1.00 28.03 ? 188 ARG B O   1 
ATOM   3036 C  CB  . ARG B 1 193 ? -18.364 11.277  4.594   1.00 42.26 ? 188 ARG B CB  1 
ATOM   3037 C  CG  . ARG B 1 193 ? -17.918 11.474  3.157   1.00 50.16 ? 188 ARG B CG  1 
ATOM   3038 C  CD  . ARG B 1 193 ? -19.109 11.652  2.230   1.00 57.44 ? 188 ARG B CD  1 
ATOM   3039 N  NE  . ARG B 1 193 ? -18.698 12.040  0.884   1.00 62.77 ? 188 ARG B NE  1 
ATOM   3040 C  CZ  . ARG B 1 193 ? -18.516 13.290  0.461   1.00 66.23 ? 188 ARG B CZ  1 
ATOM   3041 N  NH1 . ARG B 1 193 ? -18.695 14.319  1.275   1.00 70.14 ? 188 ARG B NH1 1 
ATOM   3042 N  NH2 . ARG B 1 193 ? -18.144 13.507  -0.788  1.00 68.04 ? 188 ARG B NH2 1 
ATOM   3043 N  N   . ARG B 1 194 ? -16.208 12.523  6.630   1.00 31.63 ? 189 ARG B N   1 
ATOM   3044 C  CA  . ARG B 1 194 ? -15.083 13.440  6.961   1.00 32.62 ? 189 ARG B CA  1 
ATOM   3045 C  C   . ARG B 1 194 ? -13.891 12.619  7.470   1.00 30.73 ? 189 ARG B C   1 
ATOM   3046 O  O   . ARG B 1 194 ? -12.796 12.857  6.980   1.00 27.93 ? 189 ARG B O   1 
ATOM   3047 C  CB  . ARG B 1 194 ? -15.530 14.497  7.967   1.00 32.83 ? 189 ARG B CB  1 
ATOM   3048 C  CG  . ARG B 1 194 ? -16.386 15.588  7.345   1.00 36.46 ? 189 ARG B CG  1 
ATOM   3049 C  CD  . ARG B 1 194 ? -16.988 16.529  8.368   1.00 38.51 ? 189 ARG B CD  1 
ATOM   3050 N  NE  . ARG B 1 194 ? -18.137 17.197  7.782   1.00 43.01 ? 189 ARG B NE  1 
ATOM   3051 C  CZ  . ARG B 1 194 ? -19.144 17.753  8.456   1.00 47.67 ? 189 ARG B CZ  1 
ATOM   3052 N  NH1 . ARG B 1 194 ? -19.170 17.752  9.778   1.00 50.02 ? 189 ARG B NH1 1 
ATOM   3053 N  NH2 . ARG B 1 194 ? -20.137 18.313  7.788   1.00 47.41 ? 189 ARG B NH2 1 
ATOM   3054 N  N   . VAL B 1 195 ? -14.115 11.685  8.410   1.00 29.91 ? 190 VAL B N   1 
ATOM   3055 C  CA  . VAL B 1 195 ? -13.067 10.772  8.955   1.00 31.30 ? 190 VAL B CA  1 
ATOM   3056 C  C   . VAL B 1 195 ? -12.432 9.974   7.801   1.00 30.05 ? 190 VAL B C   1 
ATOM   3057 O  O   . VAL B 1 195 ? -11.186 9.977   7.673   1.00 29.17 ? 190 VAL B O   1 
ATOM   3058 C  CB  . VAL B 1 195 ? -13.640 9.832   10.034  1.00 29.33 ? 190 VAL B CB  1 
ATOM   3059 C  CG1 . VAL B 1 195 ? -12.619 8.778   10.449  1.00 30.27 ? 190 VAL B CG1 1 
ATOM   3060 C  CG2 . VAL B 1 195 ? -14.152 10.587  11.243  1.00 30.74 ? 190 VAL B CG2 1 
ATOM   3061 N  N   . ARG B 1 196 ? -13.249 9.240   7.043   1.00 32.96 ? 191 ARG B N   1 
ATOM   3062 C  CA  . ARG B 1 196 ? -12.769 8.369   5.932   1.00 37.46 ? 191 ARG B CA  1 
ATOM   3063 C  C   . ARG B 1 196 ? -11.864 9.213   5.022   1.00 35.73 ? 191 ARG B C   1 
ATOM   3064 O  O   . ARG B 1 196 ? -10.786 8.719   4.619   1.00 32.58 ? 191 ARG B O   1 
ATOM   3065 C  CB  . ARG B 1 196 ? -13.950 7.760   5.162   1.00 43.71 ? 191 ARG B CB  1 
ATOM   3066 C  CG  . ARG B 1 196 ? -13.569 6.676   4.160   1.00 51.22 ? 191 ARG B CG  1 
ATOM   3067 C  CD  . ARG B 1 196 ? -14.627 6.471   3.082   1.00 60.21 ? 191 ARG B CD  1 
ATOM   3068 N  NE  . ARG B 1 196 ? -15.037 7.743   2.497   1.00 66.21 ? 191 ARG B NE  1 
ATOM   3069 C  CZ  . ARG B 1 196 ? -14.289 8.490   1.681   1.00 72.89 ? 191 ARG B CZ  1 
ATOM   3070 N  NH1 . ARG B 1 196 ? -13.088 8.077   1.306   1.00 74.40 ? 191 ARG B NH1 1 
ATOM   3071 N  NH2 . ARG B 1 196 ? -14.747 9.654   1.242   1.00 76.36 ? 191 ARG B NH2 1 
ATOM   3072 N  N   . HIS B 1 197 ? -12.260 10.462  4.751   1.00 35.78 ? 192 HIS B N   1 
ATOM   3073 C  CA  . HIS B 1 197 ? -11.550 11.356  3.802   1.00 34.69 ? 192 HIS B CA  1 
ATOM   3074 C  C   . HIS B 1 197 ? -10.212 11.772  4.405   1.00 36.24 ? 192 HIS B C   1 
ATOM   3075 O  O   . HIS B 1 197 ? -9.195  11.676  3.685   1.00 36.87 ? 192 HIS B O   1 
ATOM   3076 C  CB  . HIS B 1 197 ? -12.394 12.558  3.408   1.00 36.93 ? 192 HIS B CB  1 
ATOM   3077 C  CG  . HIS B 1 197 ? -11.588 13.579  2.683   1.00 43.80 ? 192 HIS B CG  1 
ATOM   3078 N  ND1 . HIS B 1 197 ? -11.301 14.829  3.229   1.00 45.51 ? 192 HIS B ND1 1 
ATOM   3079 C  CD2 . HIS B 1 197 ? -10.956 13.524  1.490   1.00 43.80 ? 192 HIS B CD2 1 
ATOM   3080 C  CE1 . HIS B 1 197 ? -10.549 15.508  2.381   1.00 49.29 ? 192 HIS B CE1 1 
ATOM   3081 N  NE2 . HIS B 1 197 ? -10.325 14.727  1.305   1.00 47.24 ? 192 HIS B NE2 1 
ATOM   3082 N  N   . SER B 1 198 ? -10.190 12.153  5.686   1.00 36.04 ? 193 SER B N   1 
ATOM   3083 C  CA  . SER B 1 198 ? -8.952  12.567  6.402   1.00 34.68 ? 193 SER B CA  1 
ATOM   3084 C  C   . SER B 1 198 ? -7.954  11.408  6.463   1.00 33.00 ? 193 SER B C   1 
ATOM   3085 O  O   . SER B 1 198 ? -6.769  11.689  6.321   1.00 37.41 ? 193 SER B O   1 
ATOM   3086 C  CB  . SER B 1 198 ? -9.234  13.109  7.771   1.00 36.30 ? 193 SER B CB  1 
ATOM   3087 O  OG  . SER B 1 198 ? -9.491  12.050  8.679   1.00 37.32 ? 193 SER B OG  1 
ATOM   3088 N  N   . PHE B 1 199 ? -8.404  10.164  6.678   1.00 34.42 ? 194 PHE B N   1 
ATOM   3089 C  CA  . PHE B 1 199 ? -7.524  8.958   6.716   1.00 32.14 ? 194 PHE B CA  1 
ATOM   3090 C  C   . PHE B 1 199 ? -7.053  8.582   5.295   1.00 34.58 ? 194 PHE B C   1 
ATOM   3091 O  O   . PHE B 1 199 ? -5.986  7.924   5.146   1.00 29.80 ? 194 PHE B O   1 
ATOM   3092 C  CB  . PHE B 1 199 ? -8.212  7.786   7.418   1.00 29.38 ? 194 PHE B CB  1 
ATOM   3093 C  CG  . PHE B 1 199 ? -8.369  7.901   8.916   1.00 29.53 ? 194 PHE B CG  1 
ATOM   3094 C  CD1 . PHE B 1 199 ? -7.518  8.684   9.688   1.00 29.52 ? 194 PHE B CD1 1 
ATOM   3095 C  CD2 . PHE B 1 199 ? -9.354  7.180   9.571   1.00 29.14 ? 194 PHE B CD2 1 
ATOM   3096 C  CE1 . PHE B 1 199 ? -7.682  8.775   11.062  1.00 29.43 ? 194 PHE B CE1 1 
ATOM   3097 C  CE2 . PHE B 1 199 ? -9.515  7.272   10.948  1.00 29.20 ? 194 PHE B CE2 1 
ATOM   3098 C  CZ  . PHE B 1 199 ? -8.673  8.065   11.697  1.00 28.02 ? 194 PHE B CZ  1 
ATOM   3099 N  N   . GLY B 1 200 ? -7.773  9.032   4.263   1.00 36.40 ? 195 GLY B N   1 
ATOM   3100 C  CA  . GLY B 1 200 ? -7.431  8.779   2.847   1.00 41.04 ? 195 GLY B CA  1 
ATOM   3101 C  C   . GLY B 1 200 ? -6.025  9.237   2.464   1.00 44.04 ? 195 GLY B C   1 
ATOM   3102 O  O   . GLY B 1 200 ? -5.415  8.575   1.603   1.00 51.74 ? 195 GLY B O   1 
ATOM   3103 N  N   . GLY B 1 201 ? -5.499  10.297  3.083   1.00 47.91 ? 196 GLY B N   1 
ATOM   3104 C  CA  . GLY B 1 201 ? -4.316  11.023  2.575   1.00 52.10 ? 196 GLY B CA  1 
ATOM   3105 C  C   . GLY B 1 201 ? -3.044  10.812  3.380   1.00 51.48 ? 196 GLY B C   1 
ATOM   3106 O  O   . GLY B 1 201 ? -2.285  11.790  3.504   1.00 56.50 ? 196 GLY B O   1 
ATOM   3107 N  N   . ALA B 1 202 ? -2.787  9.596   3.879   1.00 49.14 ? 197 ALA B N   1 
ATOM   3108 C  CA  . ALA B 1 202 ? -1.473  9.189   4.438   1.00 47.70 ? 197 ALA B CA  1 
ATOM   3109 C  C   . ALA B 1 202 ? -1.403  7.668   4.587   1.00 48.54 ? 197 ALA B C   1 
ATOM   3110 O  O   . ALA B 1 202 ? -2.450  7.044   4.895   1.00 46.60 ? 197 ALA B O   1 
ATOM   3111 C  CB  . ALA B 1 202 ? -1.212  9.883   5.751   1.00 51.88 ? 197 ALA B CB  1 
ATOM   3112 N  N   . GLU B 1 203 ? -0.211  7.095   4.370   1.00 48.94 ? 198 GLU B N   1 
ATOM   3113 C  CA  . GLU B 1 203 ? 0.018   5.628   4.385   1.00 51.65 ? 198 GLU B CA  1 
ATOM   3114 C  C   . GLU B 1 203 ? -0.413  5.076   5.747   1.00 49.98 ? 198 GLU B C   1 
ATOM   3115 O  O   . GLU B 1 203 ? -1.183  4.104   5.751   1.00 47.91 ? 198 GLU B O   1 
ATOM   3116 C  CB  . GLU B 1 203 ? 1.466   5.254   4.047   1.00 58.40 ? 198 GLU B CB  1 
ATOM   3117 C  CG  . GLU B 1 203 ? 1.683   4.854   2.586   1.00 62.93 ? 198 GLU B CG  1 
ATOM   3118 C  CD  . GLU B 1 203 ? 0.739   3.815   1.987   1.00 61.87 ? 198 GLU B CD  1 
ATOM   3119 O  OE1 . GLU B 1 203 ? 1.177   2.657   1.770   1.00 63.98 ? 198 GLU B OE1 1 
ATOM   3120 O  OE2 . GLU B 1 203 ? -0.422  4.167   1.698   1.00 56.95 ? 198 GLU B OE2 1 
ATOM   3121 N  N   . ALA B 1 204 ? -0.005  5.712   6.851   1.00 46.60 ? 199 ALA B N   1 
ATOM   3122 C  CA  . ALA B 1 204 ? -0.327  5.263   8.230   1.00 44.86 ? 199 ALA B CA  1 
ATOM   3123 C  C   . ALA B 1 204 ? -1.822  4.908   8.353   1.00 44.44 ? 199 ALA B C   1 
ATOM   3124 O  O   . ALA B 1 204 ? -2.122  3.940   9.071   1.00 45.64 ? 199 ALA B O   1 
ATOM   3125 C  CB  . ALA B 1 204 ? 0.080   6.318   9.236   1.00 46.74 ? 199 ALA B CB  1 
ATOM   3126 N  N   . THR B 1 205 ? -2.729  5.607   7.650   1.00 39.44 ? 200 THR B N   1 
ATOM   3127 C  CA  . THR B 1 205 ? -4.194  5.563   7.931   1.00 35.82 ? 200 THR B CA  1 
ATOM   3128 C  C   . THR B 1 205 ? -5.023  5.046   6.742   1.00 33.86 ? 200 THR B C   1 
ATOM   3129 O  O   . THR B 1 205 ? -6.262  4.934   6.899   1.00 30.11 ? 200 THR B O   1 
ATOM   3130 C  CB  . THR B 1 205 ? -4.653  6.951   8.390   1.00 37.19 ? 200 THR B CB  1 
ATOM   3131 O  OG1 . THR B 1 205 ? -4.376  7.912   7.371   1.00 33.80 ? 200 THR B OG1 1 
ATOM   3132 C  CG2 . THR B 1 205 ? -3.959  7.365   9.667   1.00 37.77 ? 200 THR B CG2 1 
ATOM   3133 N  N   . ARG B 1 206 ? -4.413  4.694   5.610   1.00 31.48 ? 201 ARG B N   1 
ATOM   3134 C  CA  . ARG B 1 206 ? -5.170  4.351   4.371   1.00 34.50 ? 201 ARG B CA  1 
ATOM   3135 C  C   . ARG B 1 206 ? -5.905  3.012   4.530   1.00 31.38 ? 201 ARG B C   1 
ATOM   3136 O  O   . ARG B 1 206 ? -7.040  2.897   4.023   1.00 29.24 ? 201 ARG B O   1 
ATOM   3137 C  CB  . ARG B 1 206 ? -4.267  4.398   3.133   1.00 38.95 ? 201 ARG B CB  1 
ATOM   3138 C  CG  . ARG B 1 206 ? -4.290  5.754   2.439   1.00 44.87 ? 201 ARG B CG  1 
ATOM   3139 C  CD  . ARG B 1 206 ? -3.661  5.776   1.052   1.00 49.01 ? 201 ARG B CD  1 
ATOM   3140 N  NE  . ARG B 1 206 ? -2.256  6.171   1.100   1.00 52.73 ? 201 ARG B NE  1 
ATOM   3141 C  CZ  . ARG B 1 206 ? -1.806  7.427   1.098   1.00 52.12 ? 201 ARG B CZ  1 
ATOM   3142 N  NH1 . ARG B 1 206 ? -0.504  7.654   1.159   1.00 50.69 ? 201 ARG B NH1 1 
ATOM   3143 N  NH2 . ARG B 1 206 ? -2.645  8.446   1.021   1.00 50.66 ? 201 ARG B NH2 1 
ATOM   3144 N  N   . ALA B 1 207 ? -5.344  2.074   5.286   1.00 29.37 ? 202 ALA B N   1 
ATOM   3145 C  CA  . ALA B 1 207 ? -5.945  0.755   5.609   1.00 28.39 ? 202 ALA B CA  1 
ATOM   3146 C  C   . ALA B 1 207 ? -7.256  0.919   6.410   1.00 25.16 ? 202 ALA B C   1 
ATOM   3147 O  O   . ALA B 1 207 ? -8.260  0.247   6.106   1.00 30.03 ? 202 ALA B O   1 
ATOM   3148 C  CB  . ALA B 1 207 ? -4.908  -0.064  6.346   1.00 31.36 ? 202 ALA B CB  1 
ATOM   3149 N  N   . VAL B 1 208 ? -7.284  1.823   7.374   1.00 26.42 ? 203 VAL B N   1 
ATOM   3150 C  CA  . VAL B 1 208 ? -8.523  2.160   8.131   1.00 24.75 ? 203 VAL B CA  1 
ATOM   3151 C  C   . VAL B 1 208 ? -9.484  2.775   7.116   1.00 24.46 ? 203 VAL B C   1 
ATOM   3152 O  O   . VAL B 1 208 ? -10.593 2.234   6.980   1.00 29.79 ? 203 VAL B O   1 
ATOM   3153 C  CB  . VAL B 1 208 ? -8.230  3.091   9.321   1.00 26.55 ? 203 VAL B CB  1 
ATOM   3154 C  CG1 . VAL B 1 208 ? -9.467  3.364   10.145  1.00 28.19 ? 203 VAL B CG1 1 
ATOM   3155 C  CG2 . VAL B 1 208 ? -7.157  2.529   10.229  1.00 28.07 ? 203 VAL B CG2 1 
ATOM   3156 N  N   . ALA B 1 209 ? -9.069  3.796   6.355   1.00 24.19 ? 204 ALA B N   1 
ATOM   3157 C  CA  . ALA B 1 209 ? -9.934  4.391   5.297   1.00 27.69 ? 204 ALA B CA  1 
ATOM   3158 C  C   . ALA B 1 209 ? -10.532 3.279   4.420   1.00 28.97 ? 204 ALA B C   1 
ATOM   3159 O  O   . ALA B 1 209 ? -11.784 3.293   4.177   1.00 28.13 ? 204 ALA B O   1 
ATOM   3160 C  CB  . ALA B 1 209 ? -9.198  5.420   4.473   1.00 26.21 ? 204 ALA B CB  1 
ATOM   3161 N  N   . GLY B 1 210 ? -9.685  2.343   3.993   1.00 30.02 ? 205 GLY B N   1 
ATOM   3162 C  CA  . GLY B 1 210 ? -10.055 1.164   3.174   1.00 33.62 ? 205 GLY B CA  1 
ATOM   3163 C  C   . GLY B 1 210 ? -11.165 0.324   3.806   1.00 32.31 ? 205 GLY B C   1 
ATOM   3164 O  O   . GLY B 1 210 ? -12.103 -0.039  3.091   1.00 34.86 ? 205 GLY B O   1 
ATOM   3165 N  N   . LEU B 1 211 ? -11.087 0.043   5.106   1.00 30.45 ? 206 LEU B N   1 
ATOM   3166 C  CA  . LEU B 1 211 ? -12.129 -0.728  5.844   1.00 30.20 ? 206 LEU B CA  1 
ATOM   3167 C  C   . LEU B 1 211 ? -13.432 0.079   5.990   1.00 29.03 ? 206 LEU B C   1 
ATOM   3168 O  O   . LEU B 1 211 ? -14.526 -0.518  5.869   1.00 32.39 ? 206 LEU B O   1 
ATOM   3169 C  CB  . LEU B 1 211 ? -11.548 -1.117  7.211   1.00 33.03 ? 206 LEU B CB  1 
ATOM   3170 C  CG  . LEU B 1 211 ? -10.523 -2.251  7.182   1.00 33.59 ? 206 LEU B CG  1 
ATOM   3171 C  CD1 . LEU B 1 211 ? -9.467  -2.093  8.264   1.00 31.25 ? 206 LEU B CD1 1 
ATOM   3172 C  CD2 . LEU B 1 211 ? -11.213 -3.597  7.288   1.00 36.16 ? 206 LEU B CD2 1 
ATOM   3173 N  N   . MET B 1 212 ? -13.341 1.386   6.258   1.00 32.00 ? 207 MET B N   1 
ATOM   3174 C  CA  . MET B 1 212 ? -14.526 2.270   6.411   1.00 33.87 ? 207 MET B CA  1 
ATOM   3175 C  C   . MET B 1 212 ? -15.187 2.454   5.039   1.00 37.30 ? 207 MET B C   1 
ATOM   3176 O  O   . MET B 1 212 ? -16.410 2.657   5.010   1.00 37.43 ? 207 MET B O   1 
ATOM   3177 C  CB  . MET B 1 212 ? -14.167 3.649   6.961   1.00 32.86 ? 207 MET B CB  1 
ATOM   3178 C  CG  . MET B 1 212 ? -13.512 3.625   8.332   1.00 33.31 ? 207 MET B CG  1 
ATOM   3179 S  SD  . MET B 1 212 ? -12.966 5.285   8.859   1.00 31.79 ? 207 MET B SD  1 
ATOM   3180 C  CE  . MET B 1 212 ? -14.580 6.064   8.996   1.00 33.79 ? 207 MET B CE  1 
ATOM   3181 N  N   . ASP B 1 213 ? -14.394 2.415   3.966   1.00 35.35 ? 208 ASP B N   1 
ATOM   3182 C  CA  . ASP B 1 213 ? -14.868 2.274   2.563   1.00 42.63 ? 208 ASP B CA  1 
ATOM   3183 C  C   . ASP B 1 213 ? -15.796 1.056   2.392   1.00 45.04 ? 208 ASP B C   1 
ATOM   3184 O  O   . ASP B 1 213 ? -16.767 1.210   1.650   1.00 48.71 ? 208 ASP B O   1 
ATOM   3185 C  CB  . ASP B 1 213 ? -13.704 2.160   1.572   1.00 43.30 ? 208 ASP B CB  1 
ATOM   3186 C  CG  . ASP B 1 213 ? -13.530 3.370   0.677   1.00 48.43 ? 208 ASP B CG  1 
ATOM   3187 O  OD1 . ASP B 1 213 ? -13.677 4.490   1.198   1.00 55.80 ? 208 ASP B OD1 1 
ATOM   3188 O  OD2 . ASP B 1 213 ? -13.260 3.177   -0.544  1.00 53.82 ? 208 ASP B OD2 1 
ATOM   3189 N  N   . ARG B 1 214 ? -15.508 -0.102  3.009   1.00 50.22 ? 209 ARG B N   1 
ATOM   3190 C  CA  . ARG B 1 214 ? -16.246 -1.383  2.780   1.00 49.78 ? 209 ARG B CA  1 
ATOM   3191 C  C   . ARG B 1 214 ? -17.514 -1.494  3.645   1.00 50.34 ? 209 ARG B C   1 
ATOM   3192 O  O   . ARG B 1 214 ? -18.213 -2.517  3.499   1.00 46.43 ? 209 ARG B O   1 
ATOM   3193 C  CB  . ARG B 1 214 ? -15.373 -2.606  3.079   1.00 50.75 ? 209 ARG B CB  1 
ATOM   3194 C  CG  . ARG B 1 214 ? -14.046 -2.652  2.336   1.00 55.63 ? 209 ARG B CG  1 
ATOM   3195 C  CD  . ARG B 1 214 ? -13.666 -4.040  1.834   1.00 56.78 ? 209 ARG B CD  1 
ATOM   3196 N  NE  . ARG B 1 214 ? -13.360 -5.043  2.863   1.00 63.37 ? 209 ARG B NE  1 
ATOM   3197 C  CZ  . ARG B 1 214 ? -14.121 -6.098  3.189   1.00 63.56 ? 209 ARG B CZ  1 
ATOM   3198 N  NH1 . ARG B 1 214 ? -13.721 -6.932  4.137   1.00 67.34 ? 209 ARG B NH1 1 
ATOM   3199 N  NH2 . ARG B 1 214 ? -15.285 -6.312  2.594   1.00 61.06 ? 209 ARG B NH2 1 
ATOM   3200 N  N   . LEU B 1 215 ? -17.801 -0.533  4.531   1.00 48.60 ? 210 LEU B N   1 
ATOM   3201 C  CA  . LEU B 1 215 ? -18.993 -0.592  5.424   1.00 51.88 ? 210 LEU B CA  1 
ATOM   3202 C  C   . LEU B 1 215 ? -20.238 -0.191  4.637   1.00 62.11 ? 210 LEU B C   1 
ATOM   3203 O  O   . LEU B 1 215 ? -20.334 0.947   4.179   1.00 66.34 ? 210 LEU B O   1 
ATOM   3204 C  CB  . LEU B 1 215 ? -18.813 0.333   6.630   1.00 47.14 ? 210 LEU B CB  1 
ATOM   3205 C  CG  . LEU B 1 215 ? -17.795 -0.120  7.679   1.00 46.26 ? 210 LEU B CG  1 
ATOM   3206 C  CD1 . LEU B 1 215 ? -17.661 0.939   8.753   1.00 40.91 ? 210 LEU B CD1 1 
ATOM   3207 C  CD2 . LEU B 1 215 ? -18.164 -1.453  8.310   1.00 43.06 ? 210 LEU B CD2 1 
ATOM   3208 N  N   . PRO B 1 216 ? -21.245 -1.092  4.508   1.00 69.16 ? 211 PRO B N   1 
ATOM   3209 C  CA  . PRO B 1 216 ? -22.452 -0.818  3.720   1.00 68.62 ? 211 PRO B CA  1 
ATOM   3210 C  C   . PRO B 1 216 ? -23.075 0.564   3.962   1.00 65.96 ? 211 PRO B C   1 
ATOM   3211 O  O   . PRO B 1 216 ? -22.927 1.099   5.058   1.00 65.18 ? 211 PRO B O   1 
ATOM   3212 C  CB  . PRO B 1 216 ? -23.425 -1.907  4.195   1.00 71.09 ? 211 PRO B CB  1 
ATOM   3213 C  CG  . PRO B 1 216 ? -22.526 -3.069  4.563   1.00 71.21 ? 211 PRO B CG  1 
ATOM   3214 C  CD  . PRO B 1 216 ? -21.275 -2.428  5.128   1.00 68.50 ? 211 PRO B CD  1 
ATOM   3215 N  N   . GLY C 1 4   ? 11.869  -13.598 33.999  1.00 48.96 ? -1  GLY C N   1 
ATOM   3216 C  CA  . GLY C 1 4   ? 10.770  -12.615 34.266  1.00 45.71 ? -1  GLY C CA  1 
ATOM   3217 C  C   . GLY C 1 4   ? 9.424   -13.152 33.820  1.00 41.75 ? -1  GLY C C   1 
ATOM   3218 O  O   . GLY C 1 4   ? 9.340   -14.341 33.498  1.00 38.08 ? -1  GLY C O   1 
ATOM   3219 N  N   . ALA C 1 5   ? 8.389   -12.307 33.794  1.00 42.17 ? 0   ALA C N   1 
ATOM   3220 C  CA  . ALA C 1 5   ? 7.004   -12.719 33.455  1.00 40.14 ? 0   ALA C CA  1 
ATOM   3221 C  C   . ALA C 1 5   ? 6.811   -12.657 31.935  1.00 35.25 ? 0   ALA C C   1 
ATOM   3222 O  O   . ALA C 1 5   ? 5.740   -13.017 31.451  1.00 36.44 ? 0   ALA C O   1 
ATOM   3223 C  CB  . ALA C 1 5   ? 6.010   -11.856 34.183  1.00 39.31 ? 0   ALA C CB  1 
ATOM   3224 N  N   . MET C 1 6   ? 7.817   -12.159 31.223  1.00 37.05 ? 1   MET C N   1 
ATOM   3225 C  CA  . MET C 1 6   ? 7.844   -12.074 29.740  1.00 35.41 ? 1   MET C CA  1 
ATOM   3226 C  C   . MET C 1 6   ? 9.109   -12.769 29.236  1.00 31.79 ? 1   MET C C   1 
ATOM   3227 O  O   . MET C 1 6   ? 10.213  -12.472 29.743  1.00 30.93 ? 1   MET C O   1 
ATOM   3228 C  CB  . MET C 1 6   ? 7.811   -10.614 29.276  1.00 35.86 ? 1   MET C CB  1 
ATOM   3229 C  CG  . MET C 1 6   ? 7.535   -10.455 27.798  1.00 36.64 ? 1   MET C CG  1 
ATOM   3230 S  SD  . MET C 1 6   ? 7.799   -8.773  27.183  1.00 42.34 ? 1   MET C SD  1 
ATOM   3231 C  CE  . MET C 1 6   ? 7.655   -9.098  25.428  1.00 42.50 ? 1   MET C CE  1 
ATOM   3232 N  N   . PHE C 1 7   ? 8.966   -13.688 28.281  1.00 31.88 ? 2   PHE C N   1 
ATOM   3233 C  CA  . PHE C 1 7   ? 10.138  -14.312 27.639  1.00 31.62 ? 2   PHE C CA  1 
ATOM   3234 C  C   . PHE C 1 7   ? 10.717  -13.318 26.629  1.00 30.26 ? 2   PHE C C   1 
ATOM   3235 O  O   . PHE C 1 7   ? 10.045  -12.926 25.643  1.00 29.95 ? 2   PHE C O   1 
ATOM   3236 C  CB  . PHE C 1 7   ? 9.803   -15.643 26.977  1.00 34.93 ? 2   PHE C CB  1 
ATOM   3237 C  CG  . PHE C 1 7   ? 11.036  -16.363 26.485  1.00 36.17 ? 2   PHE C CG  1 
ATOM   3238 C  CD1 . PHE C 1 7   ? 12.044  -16.716 27.369  1.00 36.20 ? 2   PHE C CD1 1 
ATOM   3239 C  CD2 . PHE C 1 7   ? 11.183  -16.700 25.149  1.00 36.99 ? 2   PHE C CD2 1 
ATOM   3240 C  CE1 . PHE C 1 7   ? 13.171  -17.390 26.938  1.00 37.19 ? 2   PHE C CE1 1 
ATOM   3241 C  CE2 . PHE C 1 7   ? 12.315  -17.376 24.722  1.00 39.26 ? 2   PHE C CE2 1 
ATOM   3242 C  CZ  . PHE C 1 7   ? 13.301  -17.725 25.614  1.00 40.35 ? 2   PHE C CZ  1 
ATOM   3243 N  N   . VAL C 1 8   ? 11.950  -12.887 26.884  1.00 27.84 ? 3   VAL C N   1 
ATOM   3244 C  CA  . VAL C 1 8   ? 12.693  -12.030 25.927  1.00 28.14 ? 3   VAL C CA  1 
ATOM   3245 C  C   . VAL C 1 8   ? 14.100  -12.606 25.796  1.00 31.24 ? 3   VAL C C   1 
ATOM   3246 O  O   . VAL C 1 8   ? 14.903  -12.537 26.732  1.00 31.52 ? 3   VAL C O   1 
ATOM   3247 C  CB  . VAL C 1 8   ? 12.665  -10.553 26.356  1.00 25.91 ? 3   VAL C CB  1 
ATOM   3248 C  CG1 . VAL C 1 8   ? 13.509  -9.704  25.439  1.00 24.15 ? 3   VAL C CG1 1 
ATOM   3249 C  CG2 . VAL C 1 8   ? 11.253  -9.991  26.439  1.00 25.75 ? 3   VAL C CG2 1 
ATOM   3250 N  N   . PRO C 1 9   ? 14.416  -13.250 24.651  1.00 32.14 ? 4   PRO C N   1 
ATOM   3251 C  CA  . PRO C 1 9   ? 15.769  -13.737 24.391  1.00 33.83 ? 4   PRO C CA  1 
ATOM   3252 C  C   . PRO C 1 9   ? 16.795  -12.605 24.464  1.00 34.78 ? 4   PRO C C   1 
ATOM   3253 O  O   . PRO C 1 9   ? 16.462  -11.475 24.139  1.00 34.85 ? 4   PRO C O   1 
ATOM   3254 C  CB  . PRO C 1 9   ? 15.674  -14.298 22.968  1.00 35.89 ? 4   PRO C CB  1 
ATOM   3255 C  CG  . PRO C 1 9   ? 14.216  -14.716 22.855  1.00 35.28 ? 4   PRO C CG  1 
ATOM   3256 C  CD  . PRO C 1 9   ? 13.477  -13.607 23.575  1.00 33.44 ? 4   PRO C CD  1 
ATOM   3257 N  N   . GLY C 1 10  ? 18.022  -12.954 24.844  1.00 38.75 ? 5   GLY C N   1 
ATOM   3258 C  CA  . GLY C 1 10  ? 19.131  -12.018 25.126  1.00 36.49 ? 5   GLY C CA  1 
ATOM   3259 C  C   . GLY C 1 10  ? 19.323  -10.963 24.038  1.00 32.62 ? 5   GLY C C   1 
ATOM   3260 O  O   . GLY C 1 10  ? 19.443  -9.786  24.344  1.00 32.35 ? 5   GLY C O   1 
ATOM   3261 N  N   . PRO C 1 11  ? 19.374  -11.333 22.738  1.00 33.05 ? 6   PRO C N   1 
ATOM   3262 C  CA  . PRO C 1 11  ? 19.645  -10.352 21.685  1.00 31.52 ? 6   PRO C CA  1 
ATOM   3263 C  C   . PRO C 1 11  ? 18.545  -9.287  21.486  1.00 32.49 ? 6   PRO C C   1 
ATOM   3264 O  O   . PRO C 1 11  ? 18.840  -8.263  20.907  1.00 33.19 ? 6   PRO C O   1 
ATOM   3265 C  CB  . PRO C 1 11  ? 19.807  -11.205 20.413  1.00 33.96 ? 6   PRO C CB  1 
ATOM   3266 C  CG  . PRO C 1 11  ? 20.020  -12.627 20.921  1.00 34.92 ? 6   PRO C CG  1 
ATOM   3267 C  CD  . PRO C 1 11  ? 19.236  -12.700 22.216  1.00 34.75 ? 6   PRO C CD  1 
ATOM   3268 N  N   . TYR C 1 12  ? 17.324  -9.521  21.976  1.00 32.16 ? 7   TYR C N   1 
ATOM   3269 C  CA  . TYR C 1 12  ? 16.127  -8.670  21.731  1.00 29.85 ? 7   TYR C CA  1 
ATOM   3270 C  C   . TYR C 1 12  ? 15.795  -7.736  22.903  1.00 30.78 ? 7   TYR C C   1 
ATOM   3271 O  O   . TYR C 1 12  ? 14.696  -7.142  22.876  1.00 34.77 ? 7   TYR C O   1 
ATOM   3272 C  CB  . TYR C 1 12  ? 14.952  -9.589  21.389  1.00 28.47 ? 7   TYR C CB  1 
ATOM   3273 C  CG  . TYR C 1 12  ? 15.271  -10.491 20.235  1.00 31.32 ? 7   TYR C CG  1 
ATOM   3274 C  CD1 . TYR C 1 12  ? 16.089  -10.049 19.206  1.00 31.76 ? 7   TYR C CD1 1 
ATOM   3275 C  CD2 . TYR C 1 12  ? 14.781  -11.776 20.178  1.00 32.29 ? 7   TYR C CD2 1 
ATOM   3276 C  CE1 . TYR C 1 12  ? 16.431  -10.877 18.160  1.00 32.96 ? 7   TYR C CE1 1 
ATOM   3277 C  CE2 . TYR C 1 12  ? 15.101  -12.613 19.128  1.00 34.51 ? 7   TYR C CE2 1 
ATOM   3278 C  CZ  . TYR C 1 12  ? 15.932  -12.161 18.125  1.00 30.78 ? 7   TYR C CZ  1 
ATOM   3279 O  OH  . TYR C 1 12  ? 16.196  -12.940 17.065  1.00 32.75 ? 7   TYR C OH  1 
ATOM   3280 N  N   . HIS C 1 13  ? 16.695  -7.536  23.869  1.00 33.45 ? 8   HIS C N   1 
ATOM   3281 C  CA  . HIS C 1 13  ? 16.532  -6.506  24.934  1.00 33.21 ? 8   HIS C CA  1 
ATOM   3282 C  C   . HIS C 1 13  ? 16.790  -5.121  24.332  1.00 32.80 ? 8   HIS C C   1 
ATOM   3283 O  O   . HIS C 1 13  ? 17.683  -5.009  23.478  1.00 32.03 ? 8   HIS C O   1 
ATOM   3284 C  CB  . HIS C 1 13  ? 17.452  -6.792  26.126  1.00 37.35 ? 8   HIS C CB  1 
ATOM   3285 C  CG  . HIS C 1 13  ? 17.079  -8.006  26.898  1.00 39.72 ? 8   HIS C CG  1 
ATOM   3286 N  ND1 . HIS C 1 13  ? 16.561  -7.932  28.172  1.00 45.37 ? 8   HIS C ND1 1 
ATOM   3287 C  CD2 . HIS C 1 13  ? 17.137  -9.316  26.585  1.00 42.50 ? 8   HIS C CD2 1 
ATOM   3288 C  CE1 . HIS C 1 13  ? 16.322  -9.151  28.617  1.00 45.61 ? 8   HIS C CE1 1 
ATOM   3289 N  NE2 . HIS C 1 13  ? 16.660  -10.016 27.659  1.00 44.19 ? 8   HIS C NE2 1 
ATOM   3290 N  N   . ALA C 1 14  ? 16.020  -4.103  24.734  1.00 33.83 ? 9   ALA C N   1 
ATOM   3291 C  CA  . ALA C 1 14  ? 16.261  -2.697  24.339  1.00 33.97 ? 9   ALA C CA  1 
ATOM   3292 C  C   . ALA C 1 14  ? 17.684  -2.309  24.749  1.00 36.42 ? 9   ALA C C   1 
ATOM   3293 O  O   . ALA C 1 14  ? 18.182  -2.797  25.766  1.00 34.40 ? 9   ALA C O   1 
ATOM   3294 C  CB  . ALA C 1 14  ? 15.240  -1.795  24.970  1.00 35.34 ? 9   ALA C CB  1 
ATOM   3295 N  N   . PRO C 1 15  ? 18.379  -1.462  23.950  1.00 38.32 ? 10  PRO C N   1 
ATOM   3296 C  CA  . PRO C 1 15  ? 19.578  -0.739  24.389  1.00 39.59 ? 10  PRO C CA  1 
ATOM   3297 C  C   . PRO C 1 15  ? 19.505  0.011   25.729  1.00 38.32 ? 10  PRO C C   1 
ATOM   3298 O  O   . PRO C 1 15  ? 20.482  0.043   26.443  1.00 40.84 ? 10  PRO C O   1 
ATOM   3299 C  CB  . PRO C 1 15  ? 19.692  0.361   23.316  1.00 37.07 ? 10  PRO C CB  1 
ATOM   3300 C  CG  . PRO C 1 15  ? 19.232  -0.321  22.075  1.00 37.81 ? 10  PRO C CG  1 
ATOM   3301 C  CD  . PRO C 1 15  ? 18.069  -1.173  22.537  1.00 38.35 ? 10  PRO C CD  1 
ATOM   3302 N  N   . GLU C 1 16  ? 18.378  0.674   25.969  1.00 38.79 ? 11  GLU C N   1 
ATOM   3303 C  CA  . GLU C 1 16  ? 18.136  1.613   27.094  1.00 41.77 ? 11  GLU C CA  1 
ATOM   3304 C  C   . GLU C 1 16  ? 16.731  1.338   27.615  1.00 38.61 ? 11  GLU C C   1 
ATOM   3305 O  O   . GLU C 1 16  ? 15.876  0.968   26.793  1.00 32.65 ? 11  GLU C O   1 
ATOM   3306 C  CB  . GLU C 1 16  ? 18.177  3.086   26.657  1.00 45.48 ? 11  GLU C CB  1 
ATOM   3307 C  CG  . GLU C 1 16  ? 19.301  3.444   25.692  1.00 51.33 ? 11  GLU C CG  1 
ATOM   3308 C  CD  . GLU C 1 16  ? 20.693  3.555   26.304  1.00 56.35 ? 11  GLU C CD  1 
ATOM   3309 O  OE1 . GLU C 1 16  ? 20.891  3.027   27.427  1.00 58.57 ? 11  GLU C OE1 1 
ATOM   3310 O  OE2 . GLU C 1 16  ? 21.587  4.171   25.659  1.00 55.64 ? 11  GLU C OE2 1 
ATOM   3311 N  N   . ASP C 1 17  ? 16.499  1.579   28.903  1.00 33.95 ? 12  ASP C N   1 
ATOM   3312 C  CA  . ASP C 1 17  ? 15.161  1.433   29.524  1.00 35.52 ? 12  ASP C CA  1 
ATOM   3313 C  C   . ASP C 1 17  ? 14.209  2.410   28.835  1.00 32.60 ? 12  ASP C C   1 
ATOM   3314 O  O   . ASP C 1 17  ? 13.012  2.104   28.770  1.00 30.68 ? 12  ASP C O   1 
ATOM   3315 C  CB  . ASP C 1 17  ? 15.230  1.657   31.034  1.00 40.04 ? 12  ASP C CB  1 
ATOM   3316 C  CG  . ASP C 1 17  ? 15.964  0.532   31.746  1.00 42.35 ? 12  ASP C CG  1 
ATOM   3317 O  OD1 . ASP C 1 17  ? 15.700  -0.631  31.406  1.00 47.23 ? 12  ASP C OD1 1 
ATOM   3318 O  OD2 . ASP C 1 17  ? 16.808  0.832   32.612  1.00 48.82 ? 12  ASP C OD2 1 
ATOM   3319 N  N   . ARG C 1 18  ? 14.743  3.536   28.357  1.00 30.97 ? 13  ARG C N   1 
ATOM   3320 C  CA  . ARG C 1 18  ? 13.971  4.660   27.751  1.00 33.39 ? 13  ARG C CA  1 
ATOM   3321 C  C   . ARG C 1 18  ? 13.219  4.188   26.488  1.00 29.47 ? 13  ARG C C   1 
ATOM   3322 O  O   . ARG C 1 18  ? 12.153  4.819   26.162  1.00 23.84 ? 13  ARG C O   1 
ATOM   3323 C  CB  . ARG C 1 18  ? 14.906  5.844   27.473  1.00 35.32 ? 13  ARG C CB  1 
ATOM   3324 C  CG  . ARG C 1 18  ? 14.339  6.888   26.517  1.00 37.89 ? 13  ARG C CG  1 
ATOM   3325 C  CD  . ARG C 1 18  ? 13.235  7.733   27.104  1.00 41.79 ? 13  ARG C CD  1 
ATOM   3326 N  NE  . ARG C 1 18  ? 13.839  8.882   27.760  1.00 51.69 ? 13  ARG C NE  1 
ATOM   3327 C  CZ  . ARG C 1 18  ? 13.310  10.100  27.861  1.00 57.47 ? 13  ARG C CZ  1 
ATOM   3328 N  NH1 . ARG C 1 18  ? 12.121  10.382  27.345  1.00 57.74 ? 13  ARG C NH1 1 
ATOM   3329 N  NH2 . ARG C 1 18  ? 13.990  11.041  28.495  1.00 62.65 ? 13  ARG C NH2 1 
ATOM   3330 N  N   . TRP C 1 19  ? 13.725  3.153   25.800  1.00 27.81 ? 14  TRP C N   1 
ATOM   3331 C  CA  . TRP C 1 19  ? 13.071  2.577   24.597  1.00 27.85 ? 14  TRP C CA  1 
ATOM   3332 C  C   . TRP C 1 19  ? 11.699  2.038   25.007  1.00 29.37 ? 14  TRP C C   1 
ATOM   3333 O  O   . TRP C 1 19  ? 10.777  2.115   24.172  1.00 30.10 ? 14  TRP C O   1 
ATOM   3334 C  CB  . TRP C 1 19  ? 13.902  1.486   23.927  1.00 28.71 ? 14  TRP C CB  1 
ATOM   3335 C  CG  . TRP C 1 19  ? 15.010  1.956   23.028  1.00 31.89 ? 14  TRP C CG  1 
ATOM   3336 C  CD1 . TRP C 1 19  ? 15.948  2.914   23.289  1.00 33.06 ? 14  TRP C CD1 1 
ATOM   3337 C  CD2 . TRP C 1 19  ? 15.339  1.426   21.729  1.00 30.28 ? 14  TRP C CD2 1 
ATOM   3338 N  NE1 . TRP C 1 19  ? 16.836  3.006   22.248  1.00 33.77 ? 14  TRP C NE1 1 
ATOM   3339 C  CE2 . TRP C 1 19  ? 16.481  2.112   21.275  1.00 33.92 ? 14  TRP C CE2 1 
ATOM   3340 C  CE3 . TRP C 1 19  ? 14.791  0.431   20.914  1.00 30.68 ? 14  TRP C CE3 1 
ATOM   3341 C  CZ2 . TRP C 1 19  ? 17.058  1.853   20.032  1.00 32.67 ? 14  TRP C CZ2 1 
ATOM   3342 C  CZ3 . TRP C 1 19  ? 15.368  0.166   19.692  1.00 29.83 ? 14  TRP C CZ3 1 
ATOM   3343 C  CH2 . TRP C 1 19  ? 16.479  0.881   19.255  1.00 30.32 ? 14  TRP C CH2 1 
ATOM   3344 N  N   . LEU C 1 20  ? 11.557  1.518   26.226  1.00 25.68 ? 15  LEU C N   1 
ATOM   3345 C  CA  . LEU C 1 20  ? 10.255  0.941   26.646  1.00 28.73 ? 15  LEU C CA  1 
ATOM   3346 C  C   . LEU C 1 20  ? 9.259   2.077   26.879  1.00 30.48 ? 15  LEU C C   1 
ATOM   3347 O  O   . LEU C 1 20  ? 8.095   1.949   26.446  1.00 27.45 ? 15  LEU C O   1 
ATOM   3348 C  CB  . LEU C 1 20  ? 10.421  0.069   27.893  1.00 28.93 ? 15  LEU C CB  1 
ATOM   3349 C  CG  . LEU C 1 20  ? 11.014  -1.307  27.628  1.00 25.37 ? 15  LEU C CG  1 
ATOM   3350 C  CD1 . LEU C 1 20  ? 12.514  -1.205  27.507  1.00 27.36 ? 15  LEU C CD1 1 
ATOM   3351 C  CD2 . LEU C 1 20  ? 10.622  -2.272  28.738  1.00 24.81 ? 15  LEU C CD2 1 
ATOM   3352 N  N   . VAL C 1 21  ? 9.702   3.140   27.562  1.00 29.98 ? 16  VAL C N   1 
ATOM   3353 C  CA  . VAL C 1 21  ? 8.869   4.351   27.812  1.00 27.79 ? 16  VAL C CA  1 
ATOM   3354 C  C   . VAL C 1 21  ? 8.439   4.887   26.448  1.00 28.21 ? 16  VAL C C   1 
ATOM   3355 O  O   . VAL C 1 21  ? 7.226   5.219   26.293  1.00 25.22 ? 16  VAL C O   1 
ATOM   3356 C  CB  . VAL C 1 21  ? 9.604   5.412   28.656  1.00 23.64 ? 16  VAL C CB  1 
ATOM   3357 C  CG1 . VAL C 1 21  ? 8.802   6.697   28.744  1.00 23.14 ? 16  VAL C CG1 1 
ATOM   3358 C  CG2 . VAL C 1 21  ? 9.901   4.884   30.056  1.00 24.99 ? 16  VAL C CG2 1 
ATOM   3359 N  N   . ASP C 1 22  ? 9.386   4.948   25.499  1.00 27.28 ? 17  ASP C N   1 
ATOM   3360 C  CA  . ASP C 1 22  ? 9.150   5.475   24.127  1.00 30.40 ? 17  ASP C CA  1 
ATOM   3361 C  C   . ASP C 1 22  ? 7.978   4.703   23.483  1.00 28.46 ? 17  ASP C C   1 
ATOM   3362 O  O   . ASP C 1 22  ? 7.048   5.349   22.960  1.00 25.51 ? 17  ASP C O   1 
ATOM   3363 C  CB  . ASP C 1 22  ? 10.414  5.371   23.276  1.00 33.37 ? 17  ASP C CB  1 
ATOM   3364 C  CG  . ASP C 1 22  ? 11.461  6.436   23.560  1.00 39.10 ? 17  ASP C CG  1 
ATOM   3365 O  OD1 . ASP C 1 22  ? 11.177  7.367   24.348  1.00 39.54 ? 17  ASP C OD1 1 
ATOM   3366 O  OD2 . ASP C 1 22  ? 12.555  6.339   22.972  1.00 45.10 ? 17  ASP C OD2 1 
ATOM   3367 N  N   . LEU C 1 23  ? 8.013   3.365   23.528  1.00 30.70 ? 18  LEU C N   1 
ATOM   3368 C  CA  . LEU C 1 23  ? 6.982   2.503   22.869  1.00 27.57 ? 18  LEU C CA  1 
ATOM   3369 C  C   . LEU C 1 23  ? 5.605   2.739   23.517  1.00 24.81 ? 18  LEU C C   1 
ATOM   3370 O  O   . LEU C 1 23  ? 4.635   2.854   22.766  1.00 21.98 ? 18  LEU C O   1 
ATOM   3371 C  CB  . LEU C 1 23  ? 7.389   1.027   22.914  1.00 29.95 ? 18  LEU C CB  1 
ATOM   3372 C  CG  . LEU C 1 23  ? 6.658   0.122   21.912  1.00 28.94 ? 18  LEU C CG  1 
ATOM   3373 C  CD1 . LEU C 1 23  ? 7.419   -1.149  21.594  1.00 31.58 ? 18  LEU C CD1 1 
ATOM   3374 C  CD2 . LEU C 1 23  ? 5.273   -0.242  22.401  1.00 33.55 ? 18  LEU C CD2 1 
ATOM   3375 N  N   . VAL C 1 24  ? 5.536   2.884   24.846  1.00 25.12 ? 19  VAL C N   1 
ATOM   3376 C  CA  . VAL C 1 24  ? 4.264   3.126   25.596  1.00 24.99 ? 19  VAL C CA  1 
ATOM   3377 C  C   . VAL C 1 24  ? 3.664   4.451   25.110  1.00 26.96 ? 19  VAL C C   1 
ATOM   3378 O  O   . VAL C 1 24  ? 2.416   4.502   24.846  1.00 22.00 ? 19  VAL C O   1 
ATOM   3379 C  CB  . VAL C 1 24  ? 4.475   3.109   27.123  1.00 23.50 ? 19  VAL C CB  1 
ATOM   3380 C  CG1 . VAL C 1 24  ? 3.434   3.898   27.886  1.00 23.47 ? 19  VAL C CG1 1 
ATOM   3381 C  CG2 . VAL C 1 24  ? 4.531   1.716   27.657  1.00 23.70 ? 19  VAL C CG2 1 
ATOM   3382 N  N   . ARG C 1 25  ? 4.518   5.478   24.979  1.00 26.59 ? 20  ARG C N   1 
ATOM   3383 C  CA  . ARG C 1 25  ? 4.136   6.832   24.506  1.00 26.60 ? 20  ARG C CA  1 
ATOM   3384 C  C   . ARG C 1 25  ? 3.638   6.762   23.058  1.00 28.11 ? 20  ARG C C   1 
ATOM   3385 O  O   . ARG C 1 25  ? 2.656   7.447   22.761  1.00 28.61 ? 20  ARG C O   1 
ATOM   3386 C  CB  . ARG C 1 25  ? 5.310   7.821   24.637  1.00 26.28 ? 20  ARG C CB  1 
ATOM   3387 C  CG  . ARG C 1 25  ? 5.589   8.203   26.079  1.00 28.02 ? 20  ARG C CG  1 
ATOM   3388 C  CD  . ARG C 1 25  ? 6.279   9.536   26.076  1.00 29.04 ? 20  ARG C CD  1 
ATOM   3389 N  NE  . ARG C 1 25  ? 6.995   9.732   27.302  1.00 31.85 ? 20  ARG C NE  1 
ATOM   3390 C  CZ  . ARG C 1 25  ? 6.517   10.275  28.402  1.00 31.68 ? 20  ARG C CZ  1 
ATOM   3391 N  NH1 . ARG C 1 25  ? 5.270   10.690  28.465  1.00 33.94 ? 20  ARG C NH1 1 
ATOM   3392 N  NH2 . ARG C 1 25  ? 7.305   10.414  29.451  1.00 35.25 ? 20  ARG C NH2 1 
ATOM   3393 N  N   . GLY C 1 26  ? 4.308   5.987   22.198  1.00 28.81 ? 21  GLY C N   1 
ATOM   3394 C  CA  . GLY C 1 26  ? 4.032   5.938   20.739  1.00 26.72 ? 21  GLY C CA  1 
ATOM   3395 C  C   . GLY C 1 26  ? 2.809   5.100   20.391  1.00 25.61 ? 21  GLY C C   1 
ATOM   3396 O  O   . GLY C 1 26  ? 2.252   5.312   19.302  1.00 25.79 ? 21  GLY C O   1 
ATOM   3397 N  N   . HIS C 1 27  ? 2.442   4.138   21.239  1.00 22.28 ? 22  HIS C N   1 
ATOM   3398 C  CA  . HIS C 1 27  ? 1.358   3.154   20.973  1.00 24.87 ? 22  HIS C CA  1 
ATOM   3399 C  C   . HIS C 1 27  ? 0.460   3.007   22.192  1.00 22.41 ? 22  HIS C C   1 
ATOM   3400 O  O   . HIS C 1 27  ? 0.478   1.985   22.860  1.00 22.63 ? 22  HIS C O   1 
ATOM   3401 C  CB  . HIS C 1 27  ? 2.031   1.854   20.564  1.00 24.38 ? 22  HIS C CB  1 
ATOM   3402 C  CG  . HIS C 1 27  ? 3.041   2.136   19.530  1.00 22.78 ? 22  HIS C CG  1 
ATOM   3403 N  ND1 . HIS C 1 27  ? 2.691   2.261   18.189  1.00 24.57 ? 22  HIS C ND1 1 
ATOM   3404 C  CD2 . HIS C 1 27  ? 4.368   2.354   19.616  1.00 25.91 ? 22  HIS C CD2 1 
ATOM   3405 C  CE1 . HIS C 1 27  ? 3.783   2.536   17.488  1.00 25.81 ? 22  HIS C CE1 1 
ATOM   3406 N  NE2 . HIS C 1 27  ? 4.823   2.611   18.340  1.00 24.84 ? 22  HIS C NE2 1 
ATOM   3407 N  N   . PRO C 1 28  ? -0.324  4.042   22.549  1.00 19.71 ? 23  PRO C N   1 
ATOM   3408 C  CA  . PRO C 1 28  ? -1.038  4.042   23.821  1.00 20.05 ? 23  PRO C CA  1 
ATOM   3409 C  C   . PRO C 1 28  ? -2.220  3.067   23.886  1.00 21.73 ? 23  PRO C C   1 
ATOM   3410 O  O   . PRO C 1 28  ? -2.752  2.869   24.955  1.00 18.94 ? 23  PRO C O   1 
ATOM   3411 C  CB  . PRO C 1 28  ? -1.592  5.464   23.956  1.00 20.00 ? 23  PRO C CB  1 
ATOM   3412 C  CG  . PRO C 1 28  ? -1.501  6.079   22.578  1.00 19.59 ? 23  PRO C CG  1 
ATOM   3413 C  CD  . PRO C 1 28  ? -0.529  5.251   21.769  1.00 18.90 ? 23  PRO C CD  1 
ATOM   3414 N  N   . LEU C 1 29  ? -2.622  2.503   22.748  1.00 22.83 ? 24  LEU C N   1 
ATOM   3415 C  CA  . LEU C 1 29  ? -3.809  1.606   22.700  1.00 21.83 ? 24  LEU C CA  1 
ATOM   3416 C  C   . LEU C 1 29  ? -3.348  0.185   23.003  1.00 20.71 ? 24  LEU C C   1 
ATOM   3417 O  O   . LEU C 1 29  ? -2.941  -0.564  22.068  1.00 18.54 ? 24  LEU C O   1 
ATOM   3418 C  CB  . LEU C 1 29  ? -4.536  1.690   21.367  1.00 21.01 ? 24  LEU C CB  1 
ATOM   3419 C  CG  . LEU C 1 29  ? -5.898  1.004   21.406  1.00 20.30 ? 24  LEU C CG  1 
ATOM   3420 C  CD1 . LEU C 1 29  ? -6.859  1.782   22.260  1.00 18.83 ? 24  LEU C CD1 1 
ATOM   3421 C  CD2 . LEU C 1 29  ? -6.420  0.801   20.003  1.00 20.97 ? 24  LEU C CD2 1 
ATOM   3422 N  N   . ALA C 1 30  ? -3.349  -0.109  24.307  1.00 21.28 ? 25  ALA C N   1 
ATOM   3423 C  CA  . ALA C 1 30  ? -2.692  -1.264  24.926  1.00 22.22 ? 25  ALA C CA  1 
ATOM   3424 C  C   . ALA C 1 30  ? -3.710  -2.382  24.931  1.00 24.45 ? 25  ALA C C   1 
ATOM   3425 O  O   . ALA C 1 30  ? -4.961  -2.053  24.839  1.00 21.38 ? 25  ALA C O   1 
ATOM   3426 C  CB  . ALA C 1 30  ? -2.268  -0.937  26.326  1.00 25.38 ? 25  ALA C CB  1 
ATOM   3427 N  N   . GLN C 1 31  ? -3.233  -3.622  24.998  1.00 19.45 ? 26  GLN C N   1 
ATOM   3428 C  CA  . GLN C 1 31  ? -4.161  -4.749  25.305  1.00 21.77 ? 26  GLN C CA  1 
ATOM   3429 C  C   . GLN C 1 31  ? -4.112  -4.992  26.815  1.00 20.30 ? 26  GLN C C   1 
ATOM   3430 O  O   . GLN C 1 31  ? -3.032  -5.235  27.380  1.00 26.35 ? 26  GLN C O   1 
ATOM   3431 C  CB  . GLN C 1 31  ? -3.855  -5.967  24.431  1.00 19.80 ? 26  GLN C CB  1 
ATOM   3432 C  CG  . GLN C 1 31  ? -4.006  -5.698  22.930  1.00 21.93 ? 26  GLN C CG  1 
ATOM   3433 C  CD  . GLN C 1 31  ? -3.840  -6.950  22.087  1.00 23.79 ? 26  GLN C CD  1 
ATOM   3434 O  OE1 . GLN C 1 31  ? -4.063  -8.074  22.555  1.00 28.30 ? 26  GLN C OE1 1 
ATOM   3435 N  NE2 . GLN C 1 31  ? -3.482  -6.773  20.829  1.00 22.23 ? 26  GLN C NE2 1 
ATOM   3436 N  N   . LEU C 1 32  ? -5.215  -4.784  27.499  1.00 23.12 ? 27  LEU C N   1 
ATOM   3437 C  CA  . LEU C 1 32  ? -5.291  -5.063  28.957  1.00 23.32 ? 27  LEU C CA  1 
ATOM   3438 C  C   . LEU C 1 32  ? -5.771  -6.500  29.164  1.00 24.85 ? 27  LEU C C   1 
ATOM   3439 O  O   . LEU C 1 32  ? -6.817  -6.853  28.596  1.00 26.42 ? 27  LEU C O   1 
ATOM   3440 C  CB  . LEU C 1 32  ? -6.238  -4.076  29.640  1.00 23.74 ? 27  LEU C CB  1 
ATOM   3441 C  CG  . LEU C 1 32  ? -6.309  -4.220  31.164  1.00 24.45 ? 27  LEU C CG  1 
ATOM   3442 C  CD1 . LEU C 1 32  ? -4.995  -3.829  31.808  1.00 25.97 ? 27  LEU C CD1 1 
ATOM   3443 C  CD2 . LEU C 1 32  ? -7.450  -3.406  31.747  1.00 26.00 ? 27  LEU C CD2 1 
ATOM   3444 N  N   . ALA C 1 33  ? -5.021  -7.296  29.936  1.00 21.77 ? 28  ALA C N   1 
ATOM   3445 C  CA  . ALA C 1 33  ? -5.322  -8.723  30.186  1.00 23.63 ? 28  ALA C CA  1 
ATOM   3446 C  C   . ALA C 1 33  ? -5.337  -8.981  31.691  1.00 22.67 ? 28  ALA C C   1 
ATOM   3447 O  O   . ALA C 1 33  ? -4.487  -8.431  32.445  1.00 24.63 ? 28  ALA C O   1 
ATOM   3448 C  CB  . ALA C 1 33  ? -4.338  -9.621  29.482  1.00 23.03 ? 28  ALA C CB  1 
ATOM   3449 N  N   . SER C 1 34  ? -6.316  -9.768  32.095  1.00 23.20 ? 29  SER C N   1 
ATOM   3450 C  CA  . SER C 1 34  ? -6.523  -10.254 33.476  1.00 23.76 ? 29  SER C CA  1 
ATOM   3451 C  C   . SER C 1 34  ? -7.073  -11.689 33.385  1.00 22.51 ? 29  SER C C   1 
ATOM   3452 O  O   . SER C 1 34  ? -7.612  -12.050 32.334  1.00 24.81 ? 29  SER C O   1 
ATOM   3453 C  CB  . SER C 1 34  ? -7.429  -9.297  34.213  1.00 24.29 ? 29  SER C CB  1 
ATOM   3454 O  OG  . SER C 1 34  ? -8.751  -9.298  33.659  1.00 26.66 ? 29  SER C OG  1 
ATOM   3455 N  N   . ASN C 1 35  ? -6.901  -12.497 34.423  1.00 23.67 ? 30  ASN C N   1 
ATOM   3456 C  CA  . ASN C 1 35  ? -7.267  -13.937 34.411  1.00 25.62 ? 30  ASN C CA  1 
ATOM   3457 C  C   . ASN C 1 35  ? -8.784  -14.089 34.227  1.00 29.09 ? 30  ASN C C   1 
ATOM   3458 O  O   . ASN C 1 35  ? -9.536  -13.292 34.805  1.00 26.60 ? 30  ASN C O   1 
ATOM   3459 C  CB  . ASN C 1 35  ? -6.818  -14.648 35.678  1.00 26.48 ? 30  ASN C CB  1 
ATOM   3460 C  CG  . ASN C 1 35  ? -5.322  -14.822 35.732  1.00 29.13 ? 30  ASN C CG  1 
ATOM   3461 O  OD1 . ASN C 1 35  ? -4.625  -14.571 34.754  1.00 26.62 ? 30  ASN C OD1 1 
ATOM   3462 N  ND2 . ASN C 1 35  ? -4.827  -15.252 36.880  1.00 33.18 ? 30  ASN C ND2 1 
ATOM   3463 N  N   . GLY C 1 36  ? -9.192  -15.028 33.371  1.00 29.59 ? 31  GLY C N   1 
ATOM   3464 C  CA  . GLY C 1 36  ? -10.576 -15.519 33.272  1.00 33.08 ? 31  GLY C CA  1 
ATOM   3465 C  C   . GLY C 1 36  ? -10.961 -16.277 34.533  1.00 36.74 ? 31  GLY C C   1 
ATOM   3466 O  O   . GLY C 1 36  ? -10.064 -16.814 35.203  1.00 33.96 ? 31  GLY C O   1 
ATOM   3467 N  N   . ALA C 1 37  ? -12.249 -16.273 34.866  1.00 40.42 ? 32  ALA C N   1 
ATOM   3468 C  CA  . ALA C 1 37  ? -12.811 -16.971 36.041  1.00 45.36 ? 32  ALA C CA  1 
ATOM   3469 C  C   . ALA C 1 37  ? -12.958 -18.458 35.707  1.00 45.60 ? 32  ALA C C   1 
ATOM   3470 O  O   . ALA C 1 37  ? -13.494 -18.771 34.609  1.00 47.02 ? 32  ALA C O   1 
ATOM   3471 C  CB  . ALA C 1 37  ? -14.127 -16.339 36.431  1.00 45.33 ? 32  ALA C CB  1 
ATOM   3472 N  N   . GLY C 1 38  ? -12.453 -19.317 36.603  1.00 47.95 ? 33  GLY C N   1 
ATOM   3473 C  CA  . GLY C 1 38  ? -12.685 -20.774 36.627  1.00 51.87 ? 33  GLY C CA  1 
ATOM   3474 C  C   . GLY C 1 38  ? -12.223 -21.425 35.340  1.00 56.58 ? 33  GLY C C   1 
ATOM   3475 O  O   . GLY C 1 38  ? -13.074 -22.014 34.641  1.00 62.28 ? 33  GLY C O   1 
ATOM   3476 N  N   . GLY C 1 39  ? -10.937 -21.259 35.018  1.00 54.96 ? 34  GLY C N   1 
ATOM   3477 C  CA  . GLY C 1 39  ? -10.284 -21.815 33.817  1.00 56.04 ? 34  GLY C CA  1 
ATOM   3478 C  C   . GLY C 1 39  ? -10.819 -21.252 32.505  1.00 54.51 ? 34  GLY C C   1 
ATOM   3479 O  O   . GLY C 1 39  ? -10.617 -21.902 31.462  1.00 63.70 ? 34  GLY C O   1 
ATOM   3480 N  N   . ALA C 1 40  ? -11.458 -20.082 32.507  1.00 49.17 ? 35  ALA C N   1 
ATOM   3481 C  CA  . ALA C 1 40  ? -11.806 -19.386 31.248  1.00 43.94 ? 35  ALA C CA  1 
ATOM   3482 C  C   . ALA C 1 40  ? -10.541 -18.692 30.734  1.00 39.15 ? 35  ALA C C   1 
ATOM   3483 O  O   . ALA C 1 40  ? -9.599  -18.480 31.539  1.00 41.74 ? 35  ALA C O   1 
ATOM   3484 C  CB  . ALA C 1 40  ? -12.963 -18.436 31.423  1.00 38.72 ? 35  ALA C CB  1 
ATOM   3485 N  N   . ALA C 1 41  ? -10.489 -18.439 29.423  1.00 36.74 ? 36  ALA C N   1 
ATOM   3486 C  CA  . ALA C 1 41  ? -9.444  -17.616 28.760  1.00 33.89 ? 36  ALA C CA  1 
ATOM   3487 C  C   . ALA C 1 41  ? -9.375  -16.270 29.478  1.00 31.01 ? 36  ALA C C   1 
ATOM   3488 O  O   . ALA C 1 41  ? -10.407 -15.798 29.953  1.00 31.51 ? 36  ALA C O   1 
ATOM   3489 C  CB  . ALA C 1 41  ? -9.778  -17.443 27.285  1.00 31.25 ? 36  ALA C CB  1 
ATOM   3490 N  N   . PRO C 1 42  ? -8.198  -15.599 29.561  1.00 27.43 ? 37  PRO C N   1 
ATOM   3491 C  CA  . PRO C 1 42  ? -8.147  -14.203 29.990  1.00 27.23 ? 37  PRO C CA  1 
ATOM   3492 C  C   . PRO C 1 42  ? -9.135  -13.259 29.291  1.00 27.53 ? 37  PRO C C   1 
ATOM   3493 O  O   . PRO C 1 42  ? -9.461  -13.468 28.127  1.00 27.89 ? 37  PRO C O   1 
ATOM   3494 C  CB  . PRO C 1 42  ? -6.705  -13.805 29.625  1.00 28.49 ? 37  PRO C CB  1 
ATOM   3495 C  CG  . PRO C 1 42  ? -5.934  -15.079 29.821  1.00 27.93 ? 37  PRO C CG  1 
ATOM   3496 C  CD  . PRO C 1 42  ? -6.859  -16.144 29.285  1.00 26.96 ? 37  PRO C CD  1 
ATOM   3497 N  N   . HIS C 1 43  ? -9.581  -12.226 30.020  1.00 29.31 ? 38  HIS C N   1 
ATOM   3498 C  CA  . HIS C 1 43  ? -10.286 -11.043 29.471  1.00 27.53 ? 38  HIS C CA  1 
ATOM   3499 C  C   . HIS C 1 43  ? -9.237  -10.157 28.796  1.00 25.51 ? 38  HIS C C   1 
ATOM   3500 O  O   . HIS C 1 43  ? -8.149  -9.956  29.380  1.00 26.44 ? 38  HIS C O   1 
ATOM   3501 C  CB  . HIS C 1 43  ? -11.024 -10.248 30.563  1.00 32.13 ? 38  HIS C CB  1 
ATOM   3502 C  CG  . HIS C 1 43  ? -12.046 -11.018 31.333  1.00 32.81 ? 38  HIS C CG  1 
ATOM   3503 N  ND1 . HIS C 1 43  ? -13.403 -10.936 31.057  1.00 38.18 ? 38  HIS C ND1 1 
ATOM   3504 C  CD2 . HIS C 1 43  ? -11.923 -11.824 32.407  1.00 32.77 ? 38  HIS C CD2 1 
ATOM   3505 C  CE1 . HIS C 1 43  ? -14.061 -11.696 31.909  1.00 37.34 ? 38  HIS C CE1 1 
ATOM   3506 N  NE2 . HIS C 1 43  ? -13.173 -12.249 32.743  1.00 36.64 ? 38  HIS C NE2 1 
ATOM   3507 N  N   . ILE C 1 44  ? -9.522  -9.685  27.588  1.00 25.06 ? 39  ILE C N   1 
ATOM   3508 C  CA  . ILE C 1 44  ? -8.607  -8.776  26.826  1.00 26.20 ? 39  ILE C CA  1 
ATOM   3509 C  C   . ILE C 1 44  ? -9.457  -7.569  26.409  1.00 23.72 ? 39  ILE C C   1 
ATOM   3510 O  O   . ILE C 1 44  ? -10.504 -7.788  25.752  1.00 20.07 ? 39  ILE C O   1 
ATOM   3511 C  CB  . ILE C 1 44  ? -8.017  -9.486  25.590  1.00 26.88 ? 39  ILE C CB  1 
ATOM   3512 C  CG1 . ILE C 1 44  ? -7.455  -10.879 25.894  1.00 28.20 ? 39  ILE C CG1 1 
ATOM   3513 C  CG2 . ILE C 1 44  ? -7.017  -8.588  24.905  1.00 28.42 ? 39  ILE C CG2 1 
ATOM   3514 C  CD1 . ILE C 1 44  ? -6.153  -10.889 26.648  1.00 27.02 ? 39  ILE C CD1 1 
ATOM   3515 N  N   . THR C 1 45  ? -9.035  -6.364  26.771  1.00 22.15 ? 40  THR C N   1 
ATOM   3516 C  CA  . THR C 1 45  ? -9.629  -5.092  26.297  1.00 24.19 ? 40  THR C CA  1 
ATOM   3517 C  C   . THR C 1 45  ? -8.535  -4.168  25.760  1.00 23.43 ? 40  THR C C   1 
ATOM   3518 O  O   . THR C 1 45  ? -7.509  -4.004  26.434  1.00 23.56 ? 40  THR C O   1 
ATOM   3519 C  CB  . THR C 1 45  ? -10.434 -4.400  27.398  1.00 24.64 ? 40  THR C CB  1 
ATOM   3520 O  OG1 . THR C 1 45  ? -11.190 -5.384  28.096  1.00 25.98 ? 40  THR C OG1 1 
ATOM   3521 C  CG2 . THR C 1 45  ? -11.346 -3.327  26.852  1.00 24.37 ? 40  THR C CG2 1 
ATOM   3522 N  N   . HIS C 1 46  ? -8.746  -3.634  24.553  1.00 23.00 ? 41  HIS C N   1 
ATOM   3523 C  CA  . HIS C 1 46  ? -7.988  -2.486  24.012  1.00 21.95 ? 41  HIS C CA  1 
ATOM   3524 C  C   . HIS C 1 46  ? -8.438  -1.225  24.727  1.00 23.52 ? 41  HIS C C   1 
ATOM   3525 O  O   . HIS C 1 46  ? -9.637  -0.857  24.651  1.00 23.33 ? 41  HIS C O   1 
ATOM   3526 C  CB  . HIS C 1 46  ? -8.137  -2.354  22.510  1.00 23.44 ? 41  HIS C CB  1 
ATOM   3527 C  CG  . HIS C 1 46  ? -7.429  -3.424  21.757  1.00 25.18 ? 41  HIS C CG  1 
ATOM   3528 N  ND1 . HIS C 1 46  ? -8.061  -4.614  21.424  1.00 27.79 ? 41  HIS C ND1 1 
ATOM   3529 C  CD2 . HIS C 1 46  ? -6.195  -3.459  21.225  1.00 26.82 ? 41  HIS C CD2 1 
ATOM   3530 C  CE1 . HIS C 1 46  ? -7.206  -5.363  20.762  1.00 29.60 ? 41  HIS C CE1 1 
ATOM   3531 N  NE2 . HIS C 1 46  ? -6.062  -4.651  20.594  1.00 29.99 ? 41  HIS C NE2 1 
ATOM   3532 N  N   . VAL C 1 47  ? -7.489  -0.581  25.382  1.00 23.59 ? 42  VAL C N   1 
ATOM   3533 C  CA  . VAL C 1 47  ? -7.780  0.546   26.310  1.00 22.15 ? 42  VAL C CA  1 
ATOM   3534 C  C   . VAL C 1 47  ? -6.695  1.577   26.145  1.00 22.86 ? 42  VAL C C   1 
ATOM   3535 O  O   . VAL C 1 47  ? -5.518  1.217   26.087  1.00 20.16 ? 42  VAL C O   1 
ATOM   3536 C  CB  . VAL C 1 47  ? -7.831  0.070   27.771  1.00 21.37 ? 42  VAL C CB  1 
ATOM   3537 C  CG1 . VAL C 1 47  ? -9.055  -0.794  28.092  1.00 21.74 ? 42  VAL C CG1 1 
ATOM   3538 C  CG2 . VAL C 1 47  ? -6.566  -0.653  28.138  1.00 21.18 ? 42  VAL C CG2 1 
ATOM   3539 N  N   . PRO C 1 48  ? -7.066  2.879   26.151  1.00 23.61 ? 43  PRO C N   1 
ATOM   3540 C  CA  . PRO C 1 48  ? -6.072  3.950   26.076  1.00 24.56 ? 43  PRO C CA  1 
ATOM   3541 C  C   . PRO C 1 48  ? -5.331  4.153   27.409  1.00 27.18 ? 43  PRO C C   1 
ATOM   3542 O  O   . PRO C 1 48  ? -6.008  4.479   28.424  1.00 26.91 ? 43  PRO C O   1 
ATOM   3543 C  CB  . PRO C 1 48  ? -6.939  5.176   25.747  1.00 25.14 ? 43  PRO C CB  1 
ATOM   3544 C  CG  . PRO C 1 48  ? -8.317  4.872   26.412  1.00 23.04 ? 43  PRO C CG  1 
ATOM   3545 C  CD  . PRO C 1 48  ? -8.436  3.366   26.345  1.00 22.03 ? 43  PRO C CD  1 
ATOM   3546 N  N   . ILE C 1 49  ? -3.989  4.049   27.387  1.00 25.88 ? 44  ILE C N   1 
ATOM   3547 C  CA  . ILE C 1 49  ? -3.135  4.150   28.604  1.00 26.86 ? 44  ILE C CA  1 
ATOM   3548 C  C   . ILE C 1 49  ? -2.003  5.165   28.385  1.00 28.35 ? 44  ILE C C   1 
ATOM   3549 O  O   . ILE C 1 49  ? -1.338  5.131   27.338  1.00 28.74 ? 44  ILE C O   1 
ATOM   3550 C  CB  . ILE C 1 49  ? -2.597  2.775   29.053  1.00 26.19 ? 44  ILE C CB  1 
ATOM   3551 C  CG1 . ILE C 1 49  ? -3.733  1.809   29.396  1.00 25.76 ? 44  ILE C CG1 1 
ATOM   3552 C  CG2 . ILE C 1 49  ? -1.633  2.911   30.236  1.00 23.70 ? 44  ILE C CG2 1 
ATOM   3553 C  CD1 . ILE C 1 49  ? -3.225  0.453   29.907  1.00 28.57 ? 44  ILE C CD1 1 
ATOM   3554 N  N   . ILE C 1 50  ? -1.794  6.036   29.375  1.00 25.77 ? 45  ILE C N   1 
ATOM   3555 C  CA  . ILE C 1 50  ? -0.736  7.075   29.340  1.00 26.96 ? 45  ILE C CA  1 
ATOM   3556 C  C   . ILE C 1 50  ? 0.050   6.988   30.632  1.00 28.18 ? 45  ILE C C   1 
ATOM   3557 O  O   . ILE C 1 50  ? -0.503  6.473   31.624  1.00 26.12 ? 45  ILE C O   1 
ATOM   3558 C  CB  . ILE C 1 50  ? -1.339  8.476   29.154  1.00 28.16 ? 45  ILE C CB  1 
ATOM   3559 C  CG1 . ILE C 1 50  ? -2.318  8.815   30.273  1.00 27.70 ? 45  ILE C CG1 1 
ATOM   3560 C  CG2 . ILE C 1 50  ? -1.974  8.597   27.770  1.00 28.84 ? 45  ILE C CG2 1 
ATOM   3561 C  CD1 . ILE C 1 50  ? -2.589  10.295  30.424  1.00 30.55 ? 45  ILE C CD1 1 
ATOM   3562 N  N   . VAL C 1 51  ? 1.300   7.453   30.551  1.00 31.15 ? 46  VAL C N   1 
ATOM   3563 C  CA  . VAL C 1 51  ? 2.216   7.706   31.690  1.00 26.94 ? 46  VAL C CA  1 
ATOM   3564 C  C   . VAL C 1 51  ? 1.593   8.787   32.568  1.00 28.38 ? 46  VAL C C   1 
ATOM   3565 O  O   . VAL C 1 51  ? 1.132   9.789   32.004  1.00 27.41 ? 46  VAL C O   1 
ATOM   3566 C  CB  . VAL C 1 51  ? 3.581   8.183   31.160  1.00 24.42 ? 46  VAL C CB  1 
ATOM   3567 C  CG1 . VAL C 1 51  ? 4.364   8.886   32.245  1.00 25.68 ? 46  VAL C CG1 1 
ATOM   3568 C  CG2 . VAL C 1 51  ? 4.387   7.055   30.546  1.00 24.27 ? 46  VAL C CG2 1 
ATOM   3569 N  N   . ASP C 1 52  ? 1.664   8.622   33.895  1.00 28.92 ? 47  ASP C N   1 
ATOM   3570 C  CA  . ASP C 1 52  ? 1.344   9.662   34.902  1.00 27.94 ? 47  ASP C CA  1 
ATOM   3571 C  C   . ASP C 1 52  ? 1.664   11.044  34.336  1.00 27.08 ? 47  ASP C C   1 
ATOM   3572 O  O   . ASP C 1 52  ? 2.827   11.386  34.140  1.00 27.24 ? 47  ASP C O   1 
ATOM   3573 C  CB  . ASP C 1 52  ? 2.116   9.447   36.200  1.00 32.01 ? 47  ASP C CB  1 
ATOM   3574 C  CG  . ASP C 1 52  ? 1.693   10.374  37.337  1.00 33.46 ? 47  ASP C CG  1 
ATOM   3575 O  OD1 . ASP C 1 52  ? 0.787   11.217  37.132  1.00 34.76 ? 47  ASP C OD1 1 
ATOM   3576 O  OD2 . ASP C 1 52  ? 2.219   10.201  38.437  1.00 36.86 ? 47  ASP C OD2 1 
ATOM   3577 N  N   . PRO C 1 53  ? 0.648   11.890  34.072  1.00 26.47 ? 48  PRO C N   1 
ATOM   3578 C  CA  . PRO C 1 53  ? 0.895   13.224  33.521  1.00 28.50 ? 48  PRO C CA  1 
ATOM   3579 C  C   . PRO C 1 53  ? 1.584   14.176  34.501  1.00 30.98 ? 48  PRO C C   1 
ATOM   3580 O  O   . PRO C 1 53  ? 2.129   15.149  34.052  1.00 31.49 ? 48  PRO C O   1 
ATOM   3581 C  CB  . PRO C 1 53  ? -0.505  13.800  33.285  1.00 30.07 ? 48  PRO C CB  1 
ATOM   3582 C  CG  . PRO C 1 53  ? -1.417  13.011  34.201  1.00 29.10 ? 48  PRO C CG  1 
ATOM   3583 C  CD  . PRO C 1 53  ? -0.783  11.628  34.317  1.00 28.98 ? 48  PRO C CD  1 
ATOM   3584 N  N   . GLU C 1 54  ? 1.481   13.893  35.806  1.00 35.08 ? 49  GLU C N   1 
ATOM   3585 C  CA  . GLU C 1 54  ? 2.051   14.743  36.884  1.00 35.19 ? 49  GLU C CA  1 
ATOM   3586 C  C   . GLU C 1 54  ? 3.568   14.518  36.975  1.00 35.99 ? 49  GLU C C   1 
ATOM   3587 O  O   . GLU C 1 54  ? 4.206   15.316  37.629  1.00 30.57 ? 49  GLU C O   1 
ATOM   3588 C  CB  . GLU C 1 54  ? 1.323   14.491  38.205  1.00 37.28 ? 49  GLU C CB  1 
ATOM   3589 C  CG  . GLU C 1 54  ? -0.192  14.677  38.114  1.00 40.61 ? 49  GLU C CG  1 
ATOM   3590 C  CD  . GLU C 1 54  ? -0.665  16.066  37.683  1.00 43.11 ? 49  GLU C CD  1 
ATOM   3591 O  OE1 . GLU C 1 54  ? -0.030  17.068  38.103  1.00 49.81 ? 49  GLU C OE1 1 
ATOM   3592 O  OE2 . GLU C 1 54  ? -1.683  16.158  36.943  1.00 44.36 ? 49  GLU C OE2 1 
ATOM   3593 N  N   . LEU C 1 55  ? 4.122   13.498  36.302  1.00 40.06 ? 50  LEU C N   1 
ATOM   3594 C  CA  . LEU C 1 55  ? 5.573   13.161  36.360  1.00 42.12 ? 50  LEU C CA  1 
ATOM   3595 C  C   . LEU C 1 55  ? 6.402   14.295  35.762  1.00 42.14 ? 50  LEU C C   1 
ATOM   3596 O  O   . LEU C 1 55  ? 6.283   14.540  34.576  1.00 45.49 ? 50  LEU C O   1 
ATOM   3597 C  CB  . LEU C 1 55  ? 5.846   11.867  35.586  1.00 42.62 ? 50  LEU C CB  1 
ATOM   3598 C  CG  . LEU C 1 55  ? 5.427   10.577  36.277  1.00 45.66 ? 50  LEU C CG  1 
ATOM   3599 C  CD1 . LEU C 1 55  ? 6.165   9.390   35.674  1.00 44.72 ? 50  LEU C CD1 1 
ATOM   3600 C  CD2 . LEU C 1 55  ? 5.637   10.652  37.791  1.00 45.67 ? 50  LEU C CD2 1 
ATOM   3601 N  N   . ASP C 1 56  ? 7.231   14.943  36.562  1.00 48.69 ? 51  ASP C N   1 
ATOM   3602 C  CA  . ASP C 1 56  ? 8.181   15.965  36.058  1.00 57.64 ? 51  ASP C CA  1 
ATOM   3603 C  C   . ASP C 1 56  ? 9.513   15.262  35.780  1.00 67.69 ? 51  ASP C C   1 
ATOM   3604 O  O   . ASP C 1 56  ? 9.676   14.095  36.224  1.00 71.20 ? 51  ASP C O   1 
ATOM   3605 C  CB  . ASP C 1 56  ? 8.273   17.149  37.027  1.00 57.60 ? 51  ASP C CB  1 
ATOM   3606 C  CG  . ASP C 1 56  ? 6.974   17.932  37.158  1.00 58.34 ? 51  ASP C CG  1 
ATOM   3607 O  OD1 . ASP C 1 56  ? 6.649   18.681  36.224  1.00 55.15 ? 51  ASP C OD1 1 
ATOM   3608 O  OD2 . ASP C 1 56  ? 6.282   17.768  38.185  1.00 64.09 ? 51  ASP C OD2 1 
ATOM   3609 N  N   . GLY C 1 57  ? 10.395  15.938  35.037  1.00 68.78 ? 52  GLY C N   1 
ATOM   3610 C  CA  . GLY C 1 57  ? 11.759  15.479  34.721  1.00 68.03 ? 52  GLY C CA  1 
ATOM   3611 C  C   . GLY C 1 57  ? 11.706  14.354  33.702  1.00 70.17 ? 52  GLY C C   1 
ATOM   3612 O  O   . GLY C 1 57  ? 10.607  13.931  33.335  1.00 69.28 ? 52  GLY C O   1 
ATOM   3613 N  N   . PRO C 1 58  ? 12.873  13.849  33.229  1.00 63.50 ? 53  PRO C N   1 
ATOM   3614 C  CA  . PRO C 1 58  ? 12.901  12.733  32.280  1.00 60.37 ? 53  PRO C CA  1 
ATOM   3615 C  C   . PRO C 1 58  ? 12.338  11.445  32.906  1.00 55.23 ? 53  PRO C C   1 
ATOM   3616 O  O   . PRO C 1 58  ? 12.619  11.186  34.065  1.00 57.99 ? 53  PRO C O   1 
ATOM   3617 C  CB  . PRO C 1 58  ? 14.387  12.579  31.900  1.00 61.13 ? 53  PRO C CB  1 
ATOM   3618 C  CG  . PRO C 1 58  ? 15.163  13.289  32.996  1.00 61.48 ? 53  PRO C CG  1 
ATOM   3619 C  CD  . PRO C 1 58  ? 14.219  14.318  33.591  1.00 61.78 ? 53  PRO C CD  1 
ATOM   3620 N  N   . VAL C 1 59  ? 11.528  10.691  32.150  1.00 47.86 ? 54  VAL C N   1 
ATOM   3621 C  CA  . VAL C 1 59  ? 11.041  9.331   32.537  1.00 43.66 ? 54  VAL C CA  1 
ATOM   3622 C  C   . VAL C 1 59  ? 11.863  8.340   31.713  1.00 39.08 ? 54  VAL C C   1 
ATOM   3623 O  O   . VAL C 1 59  ? 11.642  8.273   30.494  1.00 36.79 ? 54  VAL C O   1 
ATOM   3624 C  CB  . VAL C 1 59  ? 9.524   9.166   32.296  1.00 43.97 ? 54  VAL C CB  1 
ATOM   3625 C  CG1 . VAL C 1 59  ? 8.988   7.883   32.901  1.00 44.38 ? 54  VAL C CG1 1 
ATOM   3626 C  CG2 . VAL C 1 59  ? 8.737   10.361  32.807  1.00 45.48 ? 54  VAL C CG2 1 
ATOM   3627 N  N   . ASP C 1 60  ? 12.829  7.659   32.328  1.00 41.05 ? 55  ASP C N   1 
ATOM   3628 C  CA  . ASP C 1 60  ? 13.717  6.688   31.628  1.00 42.20 ? 55  ASP C CA  1 
ATOM   3629 C  C   . ASP C 1 60  ? 13.293  5.250   31.935  1.00 39.77 ? 55  ASP C C   1 
ATOM   3630 O  O   . ASP C 1 60  ? 13.722  4.352   31.192  1.00 41.57 ? 55  ASP C O   1 
ATOM   3631 C  CB  . ASP C 1 60  ? 15.186  6.934   31.975  1.00 47.35 ? 55  ASP C CB  1 
ATOM   3632 C  CG  . ASP C 1 60  ? 15.645  8.309   31.527  1.00 51.63 ? 55  ASP C CG  1 
ATOM   3633 O  OD1 . ASP C 1 60  ? 15.447  8.635   30.340  1.00 53.41 ? 55  ASP C OD1 1 
ATOM   3634 O  OD2 . ASP C 1 60  ? 16.143  9.064   32.379  1.00 60.75 ? 55  ASP C OD2 1 
ATOM   3635 N  N   . ARG C 1 61  ? 12.483  5.033   32.971  1.00 39.52 ? 56  ARG C N   1 
ATOM   3636 C  CA  . ARG C 1 61  ? 12.114  3.675   33.446  1.00 41.50 ? 56  ARG C CA  1 
ATOM   3637 C  C   . ARG C 1 61  ? 10.624  3.641   33.761  1.00 36.24 ? 56  ARG C C   1 
ATOM   3638 O  O   . ARG C 1 61  ? 10.164  4.528   34.496  1.00 37.02 ? 56  ARG C O   1 
ATOM   3639 C  CB  . ARG C 1 61  ? 12.938  3.288   34.676  1.00 47.29 ? 56  ARG C CB  1 
ATOM   3640 C  CG  . ARG C 1 61  ? 14.367  2.873   34.351  1.00 55.33 ? 56  ARG C CG  1 
ATOM   3641 C  CD  . ARG C 1 61  ? 15.232  2.738   35.591  1.00 61.35 ? 56  ARG C CD  1 
ATOM   3642 N  NE  . ARG C 1 61  ? 15.115  3.914   36.449  1.00 71.31 ? 56  ARG C NE  1 
ATOM   3643 C  CZ  . ARG C 1 61  ? 15.746  5.083   36.270  1.00 78.43 ? 56  ARG C CZ  1 
ATOM   3644 N  NH1 . ARG C 1 61  ? 16.585  5.262   35.260  1.00 75.87 ? 56  ARG C NH1 1 
ATOM   3645 N  NH2 . ARG C 1 61  ? 15.533  6.078   37.117  1.00 81.92 ? 56  ARG C NH2 1 
ATOM   3646 N  N   . LEU C 1 62  ? 9.921   2.633   33.246  1.00 30.79 ? 57  LEU C N   1 
ATOM   3647 C  CA  . LEU C 1 62  ? 8.484   2.382   33.538  1.00 30.75 ? 57  LEU C CA  1 
ATOM   3648 C  C   . LEU C 1 62  ? 8.344   1.814   34.953  1.00 30.30 ? 57  LEU C C   1 
ATOM   3649 O  O   . LEU C 1 62  ? 7.308   2.055   35.589  1.00 28.83 ? 57  LEU C O   1 
ATOM   3650 C  CB  . LEU C 1 62  ? 7.912   1.382   32.523  1.00 30.27 ? 57  LEU C CB  1 
ATOM   3651 C  CG  . LEU C 1 62  ? 7.817   1.876   31.082  1.00 27.49 ? 57  LEU C CG  1 
ATOM   3652 C  CD1 . LEU C 1 62  ? 7.531   0.711   30.148  1.00 26.55 ? 57  LEU C CD1 1 
ATOM   3653 C  CD2 . LEU C 1 62  ? 6.746   2.945   30.949  1.00 26.58 ? 57  LEU C CD2 1 
ATOM   3654 N  N   . VAL C 1 63  ? 9.301   1.011   35.425  1.00 34.22 ? 58  VAL C N   1 
ATOM   3655 C  CA  . VAL C 1 63  ? 9.124   0.340   36.749  1.00 35.03 ? 58  VAL C CA  1 
ATOM   3656 C  C   . VAL C 1 63  ? 9.083   1.423   37.832  1.00 32.76 ? 58  VAL C C   1 
ATOM   3657 O  O   . VAL C 1 63  ? 10.036  2.206   37.905  1.00 30.73 ? 58  VAL C O   1 
ATOM   3658 C  CB  . VAL C 1 63  ? 10.184  -0.733  37.056  1.00 36.39 ? 58  VAL C CB  1 
ATOM   3659 C  CG1 . VAL C 1 63  ? 10.123  -1.162  38.522  1.00 37.36 ? 58  VAL C CG1 1 
ATOM   3660 C  CG2 . VAL C 1 63  ? 10.035  -1.939  36.136  1.00 35.65 ? 58  VAL C CG2 1 
ATOM   3661 N  N   . GLY C 1 64  ? 8.012   1.446   38.629  1.00 33.10 ? 59  GLY C N   1 
ATOM   3662 C  CA  . GLY C 1 64  ? 7.826   2.429   39.710  1.00 38.67 ? 59  GLY C CA  1 
ATOM   3663 C  C   . GLY C 1 64  ? 6.803   3.496   39.345  1.00 39.05 ? 59  GLY C C   1 
ATOM   3664 O  O   . GLY C 1 64  ? 6.190   4.066   40.276  1.00 41.52 ? 59  GLY C O   1 
ATOM   3665 N  N   . ILE C 1 65  ? 6.588   3.786   38.058  1.00 33.73 ? 60  ILE C N   1 
ATOM   3666 C  CA  . ILE C 1 65  ? 5.654   4.897   37.713  1.00 32.15 ? 60  ILE C CA  1 
ATOM   3667 C  C   . ILE C 1 65  ? 4.236   4.330   37.712  1.00 29.07 ? 60  ILE C C   1 
ATOM   3668 O  O   . ILE C 1 65  ? 4.072   3.095   37.706  1.00 28.05 ? 60  ILE C O   1 
ATOM   3669 C  CB  . ILE C 1 65  ? 6.021   5.626   36.406  1.00 33.52 ? 60  ILE C CB  1 
ATOM   3670 C  CG1 . ILE C 1 65  ? 5.806   4.762   35.169  1.00 33.44 ? 60  ILE C CG1 1 
ATOM   3671 C  CG2 . ILE C 1 65  ? 7.436   6.186   36.455  1.00 33.58 ? 60  ILE C CG2 1 
ATOM   3672 C  CD1 . ILE C 1 65  ? 5.949   5.538   33.881  1.00 35.92 ? 60  ILE C CD1 1 
ATOM   3673 N  N   . THR C 1 66  ? 3.254   5.212   37.783  1.00 26.73 ? 61  THR C N   1 
ATOM   3674 C  CA  . THR C 1 66  ? 1.821   4.852   37.694  1.00 30.56 ? 61  THR C CA  1 
ATOM   3675 C  C   . THR C 1 66  ? 1.326   5.227   36.305  1.00 30.38 ? 61  THR C C   1 
ATOM   3676 O  O   . THR C 1 66  ? 1.512   6.411   35.926  1.00 26.33 ? 61  THR C O   1 
ATOM   3677 C  CB  . THR C 1 66  ? 0.954   5.544   38.747  1.00 33.56 ? 61  THR C CB  1 
ATOM   3678 O  OG1 . THR C 1 66  ? 1.506   5.222   40.021  1.00 34.27 ? 61  THR C OG1 1 
ATOM   3679 C  CG2 . THR C 1 66  ? -0.505  5.135   38.650  1.00 32.04 ? 61  THR C CG2 1 
ATOM   3680 N  N   . LEU C 1 67  ? 0.683   4.267   35.621  1.00 26.76 ? 62  LEU C N   1 
ATOM   3681 C  CA  . LEU C 1 67  ? 0.002   4.511   34.330  1.00 26.16 ? 62  LEU C CA  1 
ATOM   3682 C  C   . LEU C 1 67  ? -1.478  4.805   34.574  1.00 21.71 ? 62  LEU C C   1 
ATOM   3683 O  O   . LEU C 1 67  ? -2.082  4.289   35.532  1.00 20.63 ? 62  LEU C O   1 
ATOM   3684 C  CB  . LEU C 1 67  ? 0.208   3.327   33.370  1.00 25.11 ? 62  LEU C CB  1 
ATOM   3685 C  CG  . LEU C 1 67  ? 1.630   2.783   33.263  1.00 24.89 ? 62  LEU C CG  1 
ATOM   3686 C  CD1 . LEU C 1 67  ? 1.725   1.636   32.252  1.00 25.00 ? 62  LEU C CD1 1 
ATOM   3687 C  CD2 . LEU C 1 67  ? 2.592   3.882   32.907  1.00 24.75 ? 62  LEU C CD2 1 
ATOM   3688 N  N   . TRP C 1 68  ? -2.048  5.607   33.698  1.00 21.30 ? 63  TRP C N   1 
ATOM   3689 C  CA  . TRP C 1 68  ? -3.470  6.029   33.772  1.00 23.84 ? 63  TRP C CA  1 
ATOM   3690 C  C   . TRP C 1 68  ? -4.174  5.487   32.527  1.00 24.43 ? 63  TRP C C   1 
ATOM   3691 O  O   . TRP C 1 68  ? -3.575  5.591   31.423  1.00 23.57 ? 63  TRP C O   1 
ATOM   3692 C  CB  . TRP C 1 68  ? -3.581  7.552   33.801  1.00 26.59 ? 63  TRP C CB  1 
ATOM   3693 C  CG  . TRP C 1 68  ? -3.134  8.277   35.028  1.00 26.73 ? 63  TRP C CG  1 
ATOM   3694 C  CD1 . TRP C 1 68  ? -2.209  7.909   35.957  1.00 28.26 ? 63  TRP C CD1 1 
ATOM   3695 C  CD2 . TRP C 1 68  ? -3.557  9.605   35.383  1.00 26.53 ? 63  TRP C CD2 1 
ATOM   3696 N  NE1 . TRP C 1 68  ? -2.045  8.909   36.880  1.00 29.81 ? 63  TRP C NE1 1 
ATOM   3697 C  CE2 . TRP C 1 68  ? -2.873  9.954   36.563  1.00 28.92 ? 63  TRP C CE2 1 
ATOM   3698 C  CE3 . TRP C 1 68  ? -4.451  10.524  34.813  1.00 28.41 ? 63  TRP C CE3 1 
ATOM   3699 C  CZ2 . TRP C 1 68  ? -3.075  11.182  37.195  1.00 29.01 ? 63  TRP C CZ2 1 
ATOM   3700 C  CZ3 . TRP C 1 68  ? -4.665  11.731  35.443  1.00 29.05 ? 63  TRP C CZ3 1 
ATOM   3701 C  CH2 . TRP C 1 68  ? -3.987  12.048  36.622  1.00 31.98 ? 63  TRP C CH2 1 
ATOM   3702 N  N   . GLY C 1 69  ? -5.378  4.933   32.692  1.00 23.19 ? 64  GLY C N   1 
ATOM   3703 C  CA  . GLY C 1 69  ? -6.174  4.385   31.579  1.00 22.90 ? 64  GLY C CA  1 
ATOM   3704 C  C   . GLY C 1 69  ? -7.654  4.441   31.890  1.00 21.62 ? 64  GLY C C   1 
ATOM   3705 O  O   . GLY C 1 69  ? -8.018  4.747   33.052  1.00 23.96 ? 64  GLY C O   1 
ATOM   3706 N  N   . HIS C 1 70  ? -8.485  4.161   30.901  1.00 21.68 ? 65  HIS C N   1 
ATOM   3707 C  CA  . HIS C 1 70  ? -9.947  3.975   31.084  1.00 22.71 ? 65  HIS C CA  1 
ATOM   3708 C  C   . HIS C 1 70  ? -10.450 2.875   30.146  1.00 25.29 ? 65  HIS C C   1 
ATOM   3709 O  O   . HIS C 1 70  ? -9.721  2.513   29.170  1.00 24.66 ? 65  HIS C O   1 
ATOM   3710 C  CB  . HIS C 1 70  ? -10.694 5.296   30.958  1.00 22.56 ? 65  HIS C CB  1 
ATOM   3711 C  CG  . HIS C 1 70  ? -10.836 5.862   29.583  1.00 22.24 ? 65  HIS C CG  1 
ATOM   3712 N  ND1 . HIS C 1 70  ? -9.840  6.582   28.957  1.00 24.55 ? 65  HIS C ND1 1 
ATOM   3713 C  CD2 . HIS C 1 70  ? -11.903 5.916   28.756  1.00 24.36 ? 65  HIS C CD2 1 
ATOM   3714 C  CE1 . HIS C 1 70  ? -10.287 7.009   27.769  1.00 24.07 ? 65  HIS C CE1 1 
ATOM   3715 N  NE2 . HIS C 1 70  ? -11.557 6.608   27.624  1.00 21.13 ? 65  HIS C NE2 1 
ATOM   3716 N  N   . MET C 1 71  ? -11.626 2.341   30.487  1.00 23.21 ? 66  MET C N   1 
ATOM   3717 C  CA  . MET C 1 71  ? -12.376 1.380   29.666  1.00 27.51 ? 66  MET C CA  1 
ATOM   3718 C  C   . MET C 1 71  ? -13.870 1.656   29.869  1.00 28.57 ? 66  MET C C   1 
ATOM   3719 O  O   . MET C 1 71  ? -14.209 2.593   30.618  1.00 25.38 ? 66  MET C O   1 
ATOM   3720 C  CB  . MET C 1 71  ? -12.017 -0.060  30.042  1.00 31.52 ? 66  MET C CB  1 
ATOM   3721 C  CG  . MET C 1 71  ? -12.418 -0.474  31.438  1.00 33.98 ? 66  MET C CG  1 
ATOM   3722 S  SD  . MET C 1 71  ? -12.311 -2.273  31.641  1.00 39.24 ? 66  MET C SD  1 
ATOM   3723 C  CE  . MET C 1 71  ? -10.564 -2.464  32.002  1.00 39.84 ? 66  MET C CE  1 
ATOM   3724 N  N   . ASN C 1 72  ? -14.724 0.921   29.168  1.00 27.65 ? 67  ASN C N   1 
ATOM   3725 C  CA  . ASN C 1 72  ? -16.201 1.020   29.306  1.00 26.81 ? 67  ASN C CA  1 
ATOM   3726 C  C   . ASN C 1 72  ? -16.587 0.293   30.607  1.00 30.92 ? 67  ASN C C   1 
ATOM   3727 O  O   . ASN C 1 72  ? -16.172 -0.855  30.818  1.00 29.80 ? 67  ASN C O   1 
ATOM   3728 C  CB  . ASN C 1 72  ? -16.864 0.523   28.026  1.00 25.99 ? 67  ASN C CB  1 
ATOM   3729 C  CG  . ASN C 1 72  ? -18.354 0.788   27.969  1.00 26.02 ? 67  ASN C CG  1 
ATOM   3730 O  OD1 . ASN C 1 72  ? -18.973 1.121   28.977  1.00 25.32 ? 67  ASN C OD1 1 
ATOM   3731 N  ND2 . ASN C 1 72  ? -18.921 0.659   26.790  1.00 23.53 ? 67  ASN C ND2 1 
ATOM   3732 N  N   . ARG C 1 73  ? -17.271 0.978   31.519  1.00 38.81 ? 68  ARG C N   1 
ATOM   3733 C  CA  . ARG C 1 73  ? -17.775 0.368   32.785  1.00 38.79 ? 68  ARG C CA  1 
ATOM   3734 C  C   . ARG C 1 73  ? -18.737 -0.768  32.474  1.00 36.20 ? 68  ARG C C   1 
ATOM   3735 O  O   . ARG C 1 73  ? -18.875 -1.651  33.330  1.00 41.62 ? 68  ARG C O   1 
ATOM   3736 C  CB  . ARG C 1 73  ? -18.554 1.358   33.654  1.00 42.01 ? 68  ARG C CB  1 
ATOM   3737 C  CG  . ARG C 1 73  ? -17.778 1.846   34.857  1.00 42.84 ? 68  ARG C CG  1 
ATOM   3738 C  CD  . ARG C 1 73  ? -18.481 3.001   35.515  1.00 45.80 ? 68  ARG C CD  1 
ATOM   3739 N  NE  . ARG C 1 73  ? -17.488 3.735   36.261  1.00 44.62 ? 68  ARG C NE  1 
ATOM   3740 C  CZ  . ARG C 1 73  ? -17.111 3.443   37.492  1.00 47.42 ? 68  ARG C CZ  1 
ATOM   3741 N  NH1 . ARG C 1 73  ? -17.700 2.441   38.125  1.00 46.60 ? 68  ARG C NH1 1 
ATOM   3742 N  NH2 . ARG C 1 73  ? -16.172 4.176   38.089  1.00 41.60 ? 68  ARG C NH2 1 
ATOM   3743 N  N   . ALA C 1 74  ? -19.400 -0.720  31.323  1.00 33.21 ? 69  ALA C N   1 
ATOM   3744 C  CA  . ALA C 1 74  ? -20.409 -1.723  30.927  1.00 35.74 ? 69  ALA C CA  1 
ATOM   3745 C  C   . ALA C 1 74  ? -19.681 -2.939  30.348  1.00 35.51 ? 69  ALA C C   1 
ATOM   3746 O  O   . ALA C 1 74  ? -20.338 -3.954  30.133  1.00 35.08 ? 69  ALA C O   1 
ATOM   3747 C  CB  . ALA C 1 74  ? -21.396 -1.137  29.952  1.00 35.31 ? 69  ALA C CB  1 
ATOM   3748 N  N   . ASN C 1 75  ? -18.372 -2.818  30.086  1.00 33.93 ? 70  ASN C N   1 
ATOM   3749 C  CA  . ASN C 1 75  ? -17.503 -3.958  29.695  1.00 30.05 ? 70  ASN C CA  1 
ATOM   3750 C  C   . ASN C 1 75  ? -17.483 -4.920  30.881  1.00 27.72 ? 70  ASN C C   1 
ATOM   3751 O  O   . ASN C 1 75  ? -17.058 -4.532  31.959  1.00 29.59 ? 70  ASN C O   1 
ATOM   3752 C  CB  . ASN C 1 75  ? -16.099 -3.478  29.292  1.00 32.75 ? 70  ASN C CB  1 
ATOM   3753 C  CG  . ASN C 1 75  ? -15.226 -4.570  28.703  1.00 31.90 ? 70  ASN C CG  1 
ATOM   3754 O  OD1 . ASN C 1 75  ? -15.468 -5.752  28.936  1.00 35.55 ? 70  ASN C OD1 1 
ATOM   3755 N  ND2 . ASN C 1 75  ? -14.210 -4.191  27.949  1.00 31.51 ? 70  ASN C ND2 1 
ATOM   3756 N  N   . PRO C 1 76  ? -17.939 -6.186  30.740  1.00 26.40 ? 71  PRO C N   1 
ATOM   3757 C  CA  . PRO C 1 76  ? -17.847 -7.175  31.817  1.00 24.48 ? 71  PRO C CA  1 
ATOM   3758 C  C   . PRO C 1 76  ? -16.444 -7.277  32.426  1.00 24.51 ? 71  PRO C C   1 
ATOM   3759 O  O   . PRO C 1 76  ? -16.301 -7.591  33.579  1.00 26.30 ? 71  PRO C O   1 
ATOM   3760 C  CB  . PRO C 1 76  ? -18.147 -8.516  31.121  1.00 27.67 ? 71  PRO C CB  1 
ATOM   3761 C  CG  . PRO C 1 76  ? -18.967 -8.143  29.924  1.00 29.80 ? 71  PRO C CG  1 
ATOM   3762 C  CD  . PRO C 1 76  ? -18.520 -6.751  29.514  1.00 27.36 ? 71  PRO C CD  1 
ATOM   3763 N  N   . HIS C 1 77  ? -15.417 -7.016  31.626  1.00 23.25 ? 72  HIS C N   1 
ATOM   3764 C  CA  . HIS C 1 77  ? -14.002 -7.004  32.102  1.00 24.17 ? 72  HIS C CA  1 
ATOM   3765 C  C   . HIS C 1 77  ? -13.882 -6.092  33.340  1.00 25.79 ? 72  HIS C C   1 
ATOM   3766 O  O   . HIS C 1 77  ? -13.198 -6.481  34.328  1.00 27.73 ? 72  HIS C O   1 
ATOM   3767 C  CB  . HIS C 1 77  ? -13.112 -6.593  30.937  1.00 21.20 ? 72  HIS C CB  1 
ATOM   3768 C  CG  . HIS C 1 77  ? -11.670 -6.805  31.208  1.00 21.90 ? 72  HIS C CG  1 
ATOM   3769 N  ND1 . HIS C 1 77  ? -10.718 -6.528  30.261  1.00 19.61 ? 72  HIS C ND1 1 
ATOM   3770 C  CD2 . HIS C 1 77  ? -11.032 -7.294  32.278  1.00 19.92 ? 72  HIS C CD2 1 
ATOM   3771 C  CE1 . HIS C 1 77  ? -9.539  -6.761  30.765  1.00 21.32 ? 72  HIS C CE1 1 
ATOM   3772 N  NE2 . HIS C 1 77  ? -9.694  -7.209  32.003  1.00 22.53 ? 72  HIS C NE2 1 
ATOM   3773 N  N   . TRP C 1 78  ? -14.580 -4.950  33.334  1.00 28.48 ? 73  TRP C N   1 
ATOM   3774 C  CA  . TRP C 1 78  ? -14.525 -3.955  34.446  1.00 30.56 ? 73  TRP C CA  1 
ATOM   3775 C  C   . TRP C 1 78  ? -14.898 -4.647  35.762  1.00 31.03 ? 73  TRP C C   1 
ATOM   3776 O  O   . TRP C 1 78  ? -14.081 -4.607  36.676  1.00 28.43 ? 73  TRP C O   1 
ATOM   3777 C  CB  . TRP C 1 78  ? -15.421 -2.751  34.149  1.00 31.97 ? 73  TRP C CB  1 
ATOM   3778 C  CG  . TRP C 1 78  ? -15.520 -1.755  35.265  1.00 33.17 ? 73  TRP C CG  1 
ATOM   3779 C  CD1 . TRP C 1 78  ? -16.616 -1.512  36.044  1.00 33.15 ? 73  TRP C CD1 1 
ATOM   3780 C  CD2 . TRP C 1 78  ? -14.488 -0.871  35.744  1.00 31.14 ? 73  TRP C CD2 1 
ATOM   3781 N  NE1 . TRP C 1 78  ? -16.342 -0.531  36.957  1.00 33.11 ? 73  TRP C NE1 1 
ATOM   3782 C  CE2 . TRP C 1 78  ? -15.049 -0.117  36.798  1.00 31.17 ? 73  TRP C CE2 1 
ATOM   3783 C  CE3 . TRP C 1 78  ? -13.161 -0.625  35.380  1.00 31.17 ? 73  TRP C CE3 1 
ATOM   3784 C  CZ2 . TRP C 1 78  ? -14.331 0.860   37.480  1.00 30.30 ? 73  TRP C CZ2 1 
ATOM   3785 C  CZ3 . TRP C 1 78  ? -12.457 0.359   36.037  1.00 31.57 ? 73  TRP C CZ3 1 
ATOM   3786 C  CH2 . TRP C 1 78  ? -13.026 1.074   37.090  1.00 31.03 ? 73  TRP C CH2 1 
ATOM   3787 N  N   . ALA C 1 79  ? -16.065 -5.308  35.811  1.00 34.17 ? 74  ALA C N   1 
ATOM   3788 C  CA  . ALA C 1 79  ? -16.609 -5.969  37.022  1.00 36.96 ? 74  ALA C CA  1 
ATOM   3789 C  C   . ALA C 1 79  ? -15.747 -7.187  37.367  1.00 36.47 ? 74  ALA C C   1 
ATOM   3790 O  O   . ALA C 1 79  ? -15.607 -7.459  38.552  1.00 35.49 ? 74  ALA C O   1 
ATOM   3791 C  CB  . ALA C 1 79  ? -18.070 -6.331  36.836  1.00 36.99 ? 74  ALA C CB  1 
ATOM   3792 N  N   . ALA C 1 80  ? -15.153 -7.850  36.366  1.00 37.30 ? 75  ALA C N   1 
ATOM   3793 C  CA  . ALA C 1 80  ? -14.245 -9.006  36.551  1.00 38.74 ? 75  ALA C CA  1 
ATOM   3794 C  C   . ALA C 1 80  ? -12.927 -8.545  37.191  1.00 38.75 ? 75  ALA C C   1 
ATOM   3795 O  O   . ALA C 1 80  ? -12.292 -9.351  37.892  1.00 37.26 ? 75  ALA C O   1 
ATOM   3796 C  CB  . ALA C 1 80  ? -14.012 -9.727  35.240  1.00 38.47 ? 75  ALA C CB  1 
ATOM   3797 N  N   . LEU C 1 81  ? -12.515 -7.295  37.011  1.00 38.03 ? 76  LEU C N   1 
ATOM   3798 C  CA  . LEU C 1 81  ? -11.222 -6.848  37.602  1.00 39.82 ? 76  LEU C CA  1 
ATOM   3799 C  C   . LEU C 1 81  ? -11.349 -6.743  39.130  1.00 45.25 ? 76  LEU C C   1 
ATOM   3800 O  O   . LEU C 1 81  ? -10.292 -6.703  39.800  1.00 42.99 ? 76  LEU C O   1 
ATOM   3801 C  CB  . LEU C 1 81  ? -10.809 -5.513  36.979  1.00 37.91 ? 76  LEU C CB  1 
ATOM   3802 C  CG  . LEU C 1 81  ? -10.253 -5.622  35.562  1.00 32.44 ? 76  LEU C CG  1 
ATOM   3803 C  CD1 . LEU C 1 81  ? -10.305 -4.286  34.864  1.00 32.30 ? 76  LEU C CD1 1 
ATOM   3804 C  CD2 . LEU C 1 81  ? -8.839  -6.186  35.582  1.00 32.84 ? 76  LEU C CD2 1 
ATOM   3805 N  N   . GLY C 1 82  ? -12.586 -6.676  39.646  1.00 47.08 ? 77  GLY C N   1 
ATOM   3806 C  CA  . GLY C 1 82  ? -12.890 -6.674  41.090  1.00 55.93 ? 77  GLY C CA  1 
ATOM   3807 C  C   . GLY C 1 82  ? -12.028 -5.667  41.834  1.00 66.00 ? 77  GLY C C   1 
ATOM   3808 O  O   . GLY C 1 82  ? -12.034 -4.484  41.436  1.00 75.51 ? 77  GLY C O   1 
ATOM   3809 N  N   . GLY C 1 83  ? -11.282 -6.117  42.848  1.00 68.48 ? 78  GLY C N   1 
ATOM   3810 C  CA  . GLY C 1 83  ? -10.486 -5.236  43.724  1.00 71.01 ? 78  GLY C CA  1 
ATOM   3811 C  C   . GLY C 1 83  ? -9.146  -4.882  43.106  1.00 72.52 ? 78  GLY C C   1 
ATOM   3812 O  O   . GLY C 1 83  ? -9.112  -4.030  42.192  1.00 83.94 ? 78  GLY C O   1 
ATOM   3813 N  N   . ALA C 1 84  ? -8.080  -5.521  43.588  1.00 70.29 ? 79  ALA C N   1 
ATOM   3814 C  CA  . ALA C 1 84  ? -6.671  -5.232  43.238  1.00 65.09 ? 79  ALA C CA  1 
ATOM   3815 C  C   . ALA C 1 84  ? -6.168  -6.300  42.259  1.00 59.12 ? 79  ALA C C   1 
ATOM   3816 O  O   . ALA C 1 84  ? -5.157  -6.974  42.577  1.00 59.39 ? 79  ALA C O   1 
ATOM   3817 C  CB  . ALA C 1 84  ? -5.843  -5.190  44.501  1.00 67.18 ? 79  ALA C CB  1 
ATOM   3818 N  N   . ALA C 1 85  ? -6.852  -6.435  41.115  1.00 52.60 ? 80  ALA C N   1 
ATOM   3819 C  CA  . ALA C 1 85  ? -6.560  -7.424  40.048  1.00 46.69 ? 80  ALA C CA  1 
ATOM   3820 C  C   . ALA C 1 85  ? -5.114  -7.256  39.561  1.00 41.42 ? 80  ALA C C   1 
ATOM   3821 O  O   . ALA C 1 85  ? -4.705  -6.111  39.269  1.00 37.90 ? 80  ALA C O   1 
ATOM   3822 C  CB  . ALA C 1 85  ? -7.544  -7.283  38.918  1.00 45.02 ? 80  ALA C CB  1 
ATOM   3823 N  N   . ASN C 1 86  ? -4.363  -8.359  39.505  1.00 34.38 ? 81  ASN C N   1 
ATOM   3824 C  CA  . ASN C 1 86  ? -3.022  -8.410  38.867  1.00 37.44 ? 81  ASN C CA  1 
ATOM   3825 C  C   . ASN C 1 86  ? -3.200  -8.514  37.353  1.00 33.45 ? 81  ASN C C   1 
ATOM   3826 O  O   . ASN C 1 86  ? -3.792  -9.500  36.882  1.00 32.72 ? 81  ASN C O   1 
ATOM   3827 C  CB  . ASN C 1 86  ? -2.172  -9.560  39.387  1.00 38.89 ? 81  ASN C CB  1 
ATOM   3828 C  CG  . ASN C 1 86  ? -1.784  -9.357  40.832  1.00 43.42 ? 81  ASN C CG  1 
ATOM   3829 O  OD1 . ASN C 1 86  ? -1.957  -10.260 41.648  1.00 47.45 ? 81  ASN C OD1 1 
ATOM   3830 N  ND2 . ASN C 1 86  ? -1.281  -8.175  41.149  1.00 42.57 ? 81  ASN C ND2 1 
ATOM   3831 N  N   . VAL C 1 87  ? -2.696  -7.530  36.616  1.00 30.91 ? 82  VAL C N   1 
ATOM   3832 C  CA  . VAL C 1 87  ? -2.989  -7.403  35.161  1.00 28.74 ? 82  VAL C CA  1 
ATOM   3833 C  C   . VAL C 1 87  ? -1.684  -7.328  34.385  1.00 27.09 ? 82  VAL C C   1 
ATOM   3834 O  O   . VAL C 1 87  ? -0.586  -7.131  34.991  1.00 24.85 ? 82  VAL C O   1 
ATOM   3835 C  CB  . VAL C 1 87  ? -3.868  -6.185  34.837  1.00 28.37 ? 82  VAL C CB  1 
ATOM   3836 C  CG1 . VAL C 1 87  ? -5.195  -6.230  35.558  1.00 28.92 ? 82  VAL C CG1 1 
ATOM   3837 C  CG2 . VAL C 1 87  ? -3.146  -4.881  35.078  1.00 27.09 ? 82  VAL C CG2 1 
ATOM   3838 N  N   . VAL C 1 88  ? -1.800  -7.518  33.080  1.00 26.25 ? 83  VAL C N   1 
ATOM   3839 C  CA  . VAL C 1 88  ? -0.711  -7.149  32.142  1.00 27.77 ? 83  VAL C CA  1 
ATOM   3840 C  C   . VAL C 1 88  ? -1.327  -6.243  31.083  1.00 28.41 ? 83  VAL C C   1 
ATOM   3841 O  O   . VAL C 1 88  ? -2.459  -6.525  30.613  1.00 29.02 ? 83  VAL C O   1 
ATOM   3842 C  CB  . VAL C 1 88  ? -0.012  -8.353  31.509  1.00 29.30 ? 83  VAL C CB  1 
ATOM   3843 C  CG1 . VAL C 1 88  ? -1.016  -9.354  30.952  1.00 26.96 ? 83  VAL C CG1 1 
ATOM   3844 C  CG2 . VAL C 1 88  ? 0.958   -7.898  30.426  1.00 28.23 ? 83  VAL C CG2 1 
ATOM   3845 N  N   . ALA C 1 89  ? -0.615  -5.163  30.785  1.00 28.99 ? 84  ALA C N   1 
ATOM   3846 C  CA  . ALA C 1 89  ? -0.914  -4.235  29.679  1.00 29.10 ? 84  ALA C CA  1 
ATOM   3847 C  C   . ALA C 1 89  ? 0.214   -4.398  28.678  1.00 27.58 ? 84  ALA C C   1 
ATOM   3848 O  O   . ALA C 1 89  ? 1.381   -4.171  29.080  1.00 26.67 ? 84  ALA C O   1 
ATOM   3849 C  CB  . ALA C 1 89  ? -1.025  -2.823  30.176  1.00 29.51 ? 84  ALA C CB  1 
ATOM   3850 N  N   . THR C 1 90  ? -0.134  -4.836  27.467  1.00 25.38 ? 85  THR C N   1 
ATOM   3851 C  CA  . THR C 1 90  ? 0.801   -5.062  26.345  1.00 23.60 ? 85  THR C CA  1 
ATOM   3852 C  C   . THR C 1 90  ? 0.637   -3.926  25.318  1.00 22.46 ? 85  THR C C   1 
ATOM   3853 O  O   . THR C 1 90  ? -0.510  -3.589  24.877  1.00 18.05 ? 85  THR C O   1 
ATOM   3854 C  CB  . THR C 1 90  ? 0.613   -6.468  25.765  1.00 22.31 ? 85  THR C CB  1 
ATOM   3855 O  OG1 . THR C 1 90  ? 0.754   -7.403  26.845  1.00 22.26 ? 85  THR C OG1 1 
ATOM   3856 C  CG2 . THR C 1 90  ? 1.602   -6.742  24.652  1.00 23.51 ? 85  THR C CG2 1 
ATOM   3857 N  N   . PHE C 1 91  ? 1.769   -3.330  24.967  1.00 21.12 ? 86  PHE C N   1 
ATOM   3858 C  CA  . PHE C 1 91  ? 1.891   -2.189  24.031  1.00 21.88 ? 86  PHE C CA  1 
ATOM   3859 C  C   . PHE C 1 91  ? 2.665   -2.685  22.822  1.00 22.52 ? 86  PHE C C   1 
ATOM   3860 O  O   . PHE C 1 91  ? 3.781   -3.216  23.091  1.00 27.30 ? 86  PHE C O   1 
ATOM   3861 C  CB  . PHE C 1 91  ? 2.623   -1.055  24.723  1.00 20.22 ? 86  PHE C CB  1 
ATOM   3862 C  CG  . PHE C 1 91  ? 1.918   -0.463  25.907  1.00 22.11 ? 86  PHE C CG  1 
ATOM   3863 C  CD1 . PHE C 1 91  ? 1.993   -1.074  27.152  1.00 21.78 ? 86  PHE C CD1 1 
ATOM   3864 C  CD2 . PHE C 1 91  ? 1.229   0.736   25.793  1.00 18.54 ? 86  PHE C CD2 1 
ATOM   3865 C  CE1 . PHE C 1 91  ? 1.366   -0.513  28.239  1.00 20.55 ? 86  PHE C CE1 1 
ATOM   3866 C  CE2 . PHE C 1 91  ? 0.618   1.298   26.892  1.00 20.67 ? 86  PHE C CE2 1 
ATOM   3867 C  CZ  . PHE C 1 91  ? 0.691   0.681   28.116  1.00 21.63 ? 86  PHE C CZ  1 
ATOM   3868 N  N   . ALA C 1 92  ? 2.089   -2.632  21.613  1.00 20.00 ? 87  ALA C N   1 
ATOM   3869 C  CA  . ALA C 1 92  ? 2.673   -3.205  20.367  1.00 25.42 ? 87  ALA C CA  1 
ATOM   3870 C  C   . ALA C 1 92  ? 3.180   -2.088  19.439  1.00 24.45 ? 87  ALA C C   1 
ATOM   3871 O  O   . ALA C 1 92  ? 2.348   -1.288  18.972  1.00 24.12 ? 87  ALA C O   1 
ATOM   3872 C  CB  . ALA C 1 92  ? 1.685   -4.105  19.639  1.00 24.07 ? 87  ALA C CB  1 
ATOM   3873 N  N   . GLY C 1 93  ? 4.490   -2.054  19.184  1.00 22.63 ? 88  GLY C N   1 
ATOM   3874 C  CA  . GLY C 1 93  ? 5.142   -1.022  18.357  1.00 26.57 ? 88  GLY C CA  1 
ATOM   3875 C  C   . GLY C 1 93  ? 5.323   -1.401  16.872  1.00 26.42 ? 88  GLY C C   1 
ATOM   3876 O  O   . GLY C 1 93  ? 4.654   -2.267  16.317  1.00 21.69 ? 88  GLY C O   1 
ATOM   3877 N  N   . PRO C 1 94  ? 6.239   -0.725  16.145  1.00 26.17 ? 89  PRO C N   1 
ATOM   3878 C  CA  . PRO C 1 94  ? 6.521   -1.081  14.750  1.00 26.73 ? 89  PRO C CA  1 
ATOM   3879 C  C   . PRO C 1 94  ? 6.869   -2.570  14.597  1.00 25.29 ? 89  PRO C C   1 
ATOM   3880 O  O   . PRO C 1 94  ? 7.511   -3.124  15.489  1.00 23.66 ? 89  PRO C O   1 
ATOM   3881 C  CB  . PRO C 1 94  ? 7.725   -0.211  14.379  1.00 27.56 ? 89  PRO C CB  1 
ATOM   3882 C  CG  . PRO C 1 94  ? 7.629   0.974   15.327  1.00 28.88 ? 89  PRO C CG  1 
ATOM   3883 C  CD  . PRO C 1 94  ? 7.044   0.412   16.615  1.00 28.01 ? 89  PRO C CD  1 
ATOM   3884 N  N   . ASN C 1 95  ? 6.441   -3.169  13.477  1.00 23.05 ? 90  ASN C N   1 
ATOM   3885 C  CA  . ASN C 1 95  ? 6.677   -4.597  13.184  1.00 23.40 ? 90  ASN C CA  1 
ATOM   3886 C  C   . ASN C 1 95  ? 6.727   -4.765  11.672  1.00 22.42 ? 90  ASN C C   1 
ATOM   3887 O  O   . ASN C 1 95  ? 6.089   -3.965  10.993  1.00 22.59 ? 90  ASN C O   1 
ATOM   3888 C  CB  . ASN C 1 95  ? 5.615   -5.473  13.860  1.00 22.47 ? 90  ASN C CB  1 
ATOM   3889 C  CG  . ASN C 1 95  ? 4.221   -5.217  13.339  1.00 22.15 ? 90  ASN C CG  1 
ATOM   3890 O  OD1 . ASN C 1 95  ? 3.744   -5.971  12.505  1.00 23.27 ? 90  ASN C OD1 1 
ATOM   3891 N  ND2 . ASN C 1 95  ? 3.568   -4.170  13.811  1.00 19.65 ? 90  ASN C ND2 1 
ATOM   3892 N  N   . ALA C 1 96  ? 7.488   -5.732  11.173  1.00 21.65 ? 91  ALA C N   1 
ATOM   3893 C  CA  . ALA C 1 96  ? 7.400   -6.171  9.762   1.00 20.89 ? 91  ALA C CA  1 
ATOM   3894 C  C   . ALA C 1 96  ? 7.901   -7.604  9.607   1.00 22.80 ? 91  ALA C C   1 
ATOM   3895 O  O   . ALA C 1 96  ? 8.946   -7.962  10.238  1.00 22.83 ? 91  ALA C O   1 
ATOM   3896 C  CB  . ALA C 1 96  ? 8.166   -5.253  8.883   1.00 20.16 ? 91  ALA C CB  1 
ATOM   3897 N  N   . TYR C 1 97  ? 7.197   -8.363  8.760   1.00 23.32 ? 92  TYR C N   1 
ATOM   3898 C  CA  . TYR C 1 97  ? 7.617   -9.691  8.251   1.00 21.04 ? 92  TYR C CA  1 
ATOM   3899 C  C   . TYR C 1 97  ? 8.986   -9.559  7.568   1.00 20.42 ? 92  TYR C C   1 
ATOM   3900 O  O   . TYR C 1 97  ? 9.183   -8.587  6.801   1.00 19.88 ? 92  TYR C O   1 
ATOM   3901 C  CB  . TYR C 1 97  ? 6.575   -10.259 7.301   1.00 21.98 ? 92  TYR C CB  1 
ATOM   3902 C  CG  . TYR C 1 97  ? 6.960   -11.594 6.729   1.00 24.10 ? 92  TYR C CG  1 
ATOM   3903 C  CD1 . TYR C 1 97  ? 6.772   -12.760 7.459   1.00 21.19 ? 92  TYR C CD1 1 
ATOM   3904 C  CD2 . TYR C 1 97  ? 7.517   -11.697 5.460   1.00 24.67 ? 92  TYR C CD2 1 
ATOM   3905 C  CE1 . TYR C 1 97  ? 7.105   -13.995 6.920   1.00 21.90 ? 92  TYR C CE1 1 
ATOM   3906 C  CE2 . TYR C 1 97  ? 7.850   -12.928 4.911   1.00 24.64 ? 92  TYR C CE2 1 
ATOM   3907 C  CZ  . TYR C 1 97  ? 7.668   -14.088 5.661   1.00 23.04 ? 92  TYR C CZ  1 
ATOM   3908 O  OH  . TYR C 1 97  ? 7.993   -15.337 5.169   1.00 21.70 ? 92  TYR C OH  1 
ATOM   3909 N  N   . VAL C 1 98  ? 9.884   -10.508 7.848   1.00 19.80 ? 93  VAL C N   1 
ATOM   3910 C  CA  . VAL C 1 98  ? 11.225  -10.632 7.204   1.00 21.07 ? 93  VAL C CA  1 
ATOM   3911 C  C   . VAL C 1 98  ? 11.283  -11.868 6.312   1.00 19.59 ? 93  VAL C C   1 
ATOM   3912 O  O   . VAL C 1 98  ? 11.398  -12.987 6.844   1.00 18.50 ? 93  VAL C O   1 
ATOM   3913 C  CB  . VAL C 1 98  ? 12.332  -10.732 8.246   1.00 20.25 ? 93  VAL C CB  1 
ATOM   3914 C  CG1 . VAL C 1 98  ? 13.679  -10.726 7.547   1.00 18.78 ? 93  VAL C CG1 1 
ATOM   3915 C  CG2 . VAL C 1 98  ? 12.202  -9.625  9.266   1.00 20.19 ? 93  VAL C CG2 1 
ATOM   3916 N  N   . SER C 1 99  ? 11.252  -11.644 5.003   1.00 23.21 ? 94  SER C N   1 
ATOM   3917 C  CA  . SER C 1 99  ? 11.488  -12.661 3.952   1.00 23.20 ? 94  SER C CA  1 
ATOM   3918 C  C   . SER C 1 99  ? 12.980  -12.974 3.895   1.00 24.23 ? 94  SER C C   1 
ATOM   3919 O  O   . SER C 1 99  ? 13.779  -12.052 3.897   1.00 24.08 ? 94  SER C O   1 
ATOM   3920 C  CB  . SER C 1 99  ? 11.001  -12.172 2.614   1.00 24.37 ? 94  SER C CB  1 
ATOM   3921 O  OG  . SER C 1 99  ? 11.247  -13.177 1.631   1.00 27.89 ? 94  SER C OG  1 
ATOM   3922 N  N   . PRO C 1 100 ? 13.412  -14.255 3.824   1.00 26.28 ? 95  PRO C N   1 
ATOM   3923 C  CA  . PRO C 1 100 ? 14.835  -14.576 3.656   1.00 24.41 ? 95  PRO C CA  1 
ATOM   3924 C  C   . PRO C 1 100 ? 15.408  -14.149 2.293   1.00 27.17 ? 95  PRO C C   1 
ATOM   3925 O  O   . PRO C 1 100 ? 16.618  -13.953 2.182   1.00 30.47 ? 95  PRO C O   1 
ATOM   3926 C  CB  . PRO C 1 100 ? 14.845  -16.095 3.824   1.00 23.72 ? 95  PRO C CB  1 
ATOM   3927 C  CG  . PRO C 1 100 ? 13.604  -16.397 4.580   1.00 22.66 ? 95  PRO C CG  1 
ATOM   3928 C  CD  . PRO C 1 100 ? 12.585  -15.464 3.975   1.00 25.02 ? 95  PRO C CD  1 
ATOM   3929 N  N   . ALA C 1 101 ? 14.540  -13.922 1.304   1.00 26.40 ? 96  ALA C N   1 
ATOM   3930 C  CA  . ALA C 1 101 ? 14.901  -13.233 0.044   1.00 28.43 ? 96  ALA C CA  1 
ATOM   3931 C  C   . ALA C 1 101 ? 15.782  -12.017 0.365   1.00 28.43 ? 96  ALA C C   1 
ATOM   3932 O  O   . ALA C 1 101 ? 16.830  -11.901 -0.274  1.00 33.31 ? 96  ALA C O   1 
ATOM   3933 C  CB  . ALA C 1 101 ? 13.662  -12.843 -0.729  1.00 28.47 ? 96  ALA C CB  1 
ATOM   3934 N  N   . VAL C 1 102 ? 15.398  -11.197 1.356   1.00 25.64 ? 97  VAL C N   1 
ATOM   3935 C  CA  . VAL C 1 102 ? 16.082  -9.938  1.759   1.00 25.71 ? 97  VAL C CA  1 
ATOM   3936 C  C   . VAL C 1 102 ? 17.486  -10.287 2.276   1.00 29.63 ? 97  VAL C C   1 
ATOM   3937 O  O   . VAL C 1 102 ? 18.418  -9.519  2.006   1.00 29.84 ? 97  VAL C O   1 
ATOM   3938 C  CB  . VAL C 1 102 ? 15.287  -9.159  2.824   1.00 28.87 ? 97  VAL C CB  1 
ATOM   3939 C  CG1 . VAL C 1 102 ? 16.064  -7.963  3.329   1.00 30.52 ? 97  VAL C CG1 1 
ATOM   3940 C  CG2 . VAL C 1 102 ? 13.902  -8.710  2.356   1.00 27.63 ? 97  VAL C CG2 1 
ATOM   3941 N  N   . TYR C 1 103 ? 17.633  -11.376 3.029   1.00 28.50 ? 98  TYR C N   1 
ATOM   3942 C  CA  . TYR C 1 103 ? 18.947  -11.847 3.547   1.00 30.75 ? 98  TYR C CA  1 
ATOM   3943 C  C   . TYR C 1 103 ? 19.914  -12.115 2.388   1.00 33.20 ? 98  TYR C C   1 
ATOM   3944 O  O   . TYR C 1 103 ? 21.108  -11.763 2.525   1.00 32.24 ? 98  TYR C O   1 
ATOM   3945 C  CB  . TYR C 1 103 ? 18.834  -13.164 4.321   1.00 29.25 ? 98  TYR C CB  1 
ATOM   3946 C  CG  . TYR C 1 103 ? 18.014  -13.131 5.583   1.00 31.57 ? 98  TYR C CG  1 
ATOM   3947 C  CD1 . TYR C 1 103 ? 17.768  -11.954 6.278   1.00 29.20 ? 98  TYR C CD1 1 
ATOM   3948 C  CD2 . TYR C 1 103 ? 17.550  -14.319 6.132   1.00 33.29 ? 98  TYR C CD2 1 
ATOM   3949 C  CE1 . TYR C 1 103 ? 17.045  -11.958 7.460   1.00 30.36 ? 98  TYR C CE1 1 
ATOM   3950 C  CE2 . TYR C 1 103 ? 16.837  -14.339 7.320   1.00 33.16 ? 98  TYR C CE2 1 
ATOM   3951 C  CZ  . TYR C 1 103 ? 16.584  -13.158 7.989   1.00 30.33 ? 98  TYR C CZ  1 
ATOM   3952 O  OH  . TYR C 1 103 ? 15.844  -13.187 9.136   1.00 28.83 ? 98  TYR C OH  1 
ATOM   3953 N  N   . ARG C 1 104 ? 19.418  -12.794 1.340   1.00 33.02 ? 99  ARG C N   1 
ATOM   3954 C  CA  . ARG C 1 104 ? 20.177  -13.289 0.159   1.00 35.69 ? 99  ARG C CA  1 
ATOM   3955 C  C   . ARG C 1 104 ? 21.168  -14.375 0.600   1.00 37.82 ? 99  ARG C C   1 
ATOM   3956 O  O   . ARG C 1 104 ? 22.197  -14.551 -0.094  1.00 37.12 ? 99  ARG C O   1 
ATOM   3957 C  CB  . ARG C 1 104 ? 20.900  -12.151 -0.571  1.00 34.82 ? 99  ARG C CB  1 
ATOM   3958 C  CG  . ARG C 1 104 ? 20.060  -10.891 -0.733  1.00 33.15 ? 99  ARG C CG  1 
ATOM   3959 C  CD  . ARG C 1 104 ? 20.482  -10.069 -1.926  1.00 31.76 ? 99  ARG C CD  1 
ATOM   3960 N  NE  . ARG C 1 104 ? 21.850  -9.541  -1.879  1.00 33.15 ? 99  ARG C NE  1 
ATOM   3961 C  CZ  . ARG C 1 104 ? 22.230  -8.381  -1.325  1.00 32.78 ? 99  ARG C CZ  1 
ATOM   3962 N  NH1 . ARG C 1 104 ? 21.364  -7.618  -0.678  1.00 29.87 ? 99  ARG C NH1 1 
ATOM   3963 N  NH2 . ARG C 1 104 ? 23.497  -8.002  -1.395  1.00 32.91 ? 99  ARG C NH2 1 
ATOM   3964 N  N   . THR C 1 105 ? 20.867  -15.079 1.696   1.00 38.23 ? 100 THR C N   1 
ATOM   3965 C  CA  . THR C 1 105 ? 21.675  -16.204 2.237   1.00 37.44 ? 100 THR C CA  1 
ATOM   3966 C  C   . THR C 1 105 ? 20.833  -17.481 2.187   1.00 37.37 ? 100 THR C C   1 
ATOM   3967 O  O   . THR C 1 105 ? 19.597  -17.395 2.012   1.00 34.69 ? 100 THR C O   1 
ATOM   3968 C  CB  . THR C 1 105 ? 22.171  -15.930 3.666   1.00 39.67 ? 100 THR C CB  1 
ATOM   3969 O  OG1 . THR C 1 105 ? 21.044  -15.716 4.520   1.00 36.52 ? 100 THR C OG1 1 
ATOM   3970 C  CG2 . THR C 1 105 ? 23.112  -14.748 3.753   1.00 41.43 ? 100 THR C CG2 1 
ATOM   3971 N  N   . ALA C 1 106 ? 21.493  -18.624 2.328   1.00 35.07 ? 101 ALA C N   1 
ATOM   3972 C  CA  . ALA C 1 106 ? 20.889  -19.976 2.307   1.00 35.65 ? 101 ALA C CA  1 
ATOM   3973 C  C   . ALA C 1 106 ? 21.767  -20.862 3.178   1.00 34.99 ? 101 ALA C C   1 
ATOM   3974 O  O   . ALA C 1 106 ? 22.988  -20.731 3.129   1.00 33.95 ? 101 ALA C O   1 
ATOM   3975 C  CB  . ALA C 1 106 ? 20.768  -20.518 0.894   1.00 32.81 ? 101 ALA C CB  1 
ATOM   3976 N  N   . PRO C 1 107 ? 21.181  -21.716 4.050   1.00 35.00 ? 102 PRO C N   1 
ATOM   3977 C  CA  . PRO C 1 107 ? 19.733  -21.780 4.230   1.00 31.64 ? 102 PRO C CA  1 
ATOM   3978 C  C   . PRO C 1 107 ? 19.273  -20.681 5.198   1.00 30.81 ? 102 PRO C C   1 
ATOM   3979 O  O   . PRO C 1 107 ? 20.100  -19.997 5.778   1.00 34.64 ? 102 PRO C O   1 
ATOM   3980 C  CB  . PRO C 1 107 ? 19.546  -23.184 4.815   1.00 31.83 ? 102 PRO C CB  1 
ATOM   3981 C  CG  . PRO C 1 107 ? 20.774  -23.337 5.699   1.00 34.92 ? 102 PRO C CG  1 
ATOM   3982 C  CD  . PRO C 1 107 ? 21.891  -22.676 4.910   1.00 34.73 ? 102 PRO C CD  1 
ATOM   3983 N  N   . ALA C 1 108 ? 17.965  -20.559 5.394   1.00 26.27 ? 103 ALA C N   1 
ATOM   3984 C  CA  . ALA C 1 108 ? 17.382  -19.557 6.302   1.00 27.18 ? 103 ALA C CA  1 
ATOM   3985 C  C   . ALA C 1 108 ? 15.939  -19.943 6.617   1.00 26.26 ? 103 ALA C C   1 
ATOM   3986 O  O   . ALA C 1 108 ? 15.398  -20.877 5.978   1.00 27.92 ? 103 ALA C O   1 
ATOM   3987 C  CB  . ALA C 1 108 ? 17.468  -18.181 5.672   1.00 27.57 ? 103 ALA C CB  1 
ATOM   3988 N  N   . ALA C 1 109 ? 15.350  -19.233 7.571   1.00 26.58 ? 104 ALA C N   1 
ATOM   3989 C  CA  . ALA C 1 109 ? 13.905  -19.289 7.875   1.00 27.66 ? 104 ALA C CA  1 
ATOM   3990 C  C   . ALA C 1 109 ? 13.412  -17.852 7.967   1.00 26.07 ? 104 ALA C C   1 
ATOM   3991 O  O   . ALA C 1 109 ? 14.195  -16.966 8.298   1.00 29.78 ? 104 ALA C O   1 
ATOM   3992 C  CB  . ALA C 1 109 ? 13.677  -20.040 9.157   1.00 25.91 ? 104 ALA C CB  1 
ATOM   3993 N  N   . PRO C 1 110 ? 12.137  -17.575 7.615   1.00 25.26 ? 105 PRO C N   1 
ATOM   3994 C  CA  . PRO C 1 110 ? 11.547  -16.263 7.819   1.00 25.82 ? 105 PRO C CA  1 
ATOM   3995 C  C   . PRO C 1 110 ? 11.333  -15.972 9.310   1.00 27.30 ? 105 PRO C C   1 
ATOM   3996 O  O   . PRO C 1 110 ? 11.321  -16.904 10.119  1.00 27.76 ? 105 PRO C O   1 
ATOM   3997 C  CB  . PRO C 1 110 ? 10.173  -16.338 7.139   1.00 26.05 ? 105 PRO C CB  1 
ATOM   3998 C  CG  . PRO C 1 110 ? 10.213  -17.585 6.300   1.00 26.88 ? 105 PRO C CG  1 
ATOM   3999 C  CD  . PRO C 1 110 ? 11.180  -18.508 7.013   1.00 26.62 ? 105 PRO C CD  1 
ATOM   4000 N  N   . THR C 1 111 ? 11.148  -14.696 9.641   1.00 23.96 ? 106 THR C N   1 
ATOM   4001 C  CA  . THR C 1 111 ? 10.772  -14.250 11.002  1.00 23.72 ? 106 THR C CA  1 
ATOM   4002 C  C   . THR C 1 111 ? 9.820   -13.078 10.859  1.00 22.06 ? 106 THR C C   1 
ATOM   4003 O  O   . THR C 1 111 ? 9.525   -12.698 9.709   1.00 20.37 ? 106 THR C O   1 
ATOM   4004 C  CB  . THR C 1 111 ? 11.989  -13.896 11.864  1.00 25.80 ? 106 THR C CB  1 
ATOM   4005 O  OG1 . THR C 1 111 ? 11.534  -14.092 13.198  1.00 28.49 ? 106 THR C OG1 1 
ATOM   4006 C  CG2 . THR C 1 111 ? 12.491  -12.491 11.635  1.00 25.06 ? 106 THR C CG2 1 
ATOM   4007 N  N   . TRP C 1 112 ? 9.392   -12.542 11.994  1.00 21.09 ? 107 TRP C N   1 
ATOM   4008 C  CA  . TRP C 1 112 ? 8.628   -11.282 12.072  1.00 22.35 ? 107 TRP C CA  1 
ATOM   4009 C  C   . TRP C 1 112 ? 9.392   -10.343 12.995  1.00 21.74 ? 107 TRP C C   1 
ATOM   4010 O  O   . TRP C 1 112 ? 9.494   -10.719 14.207  1.00 24.19 ? 107 TRP C O   1 
ATOM   4011 C  CB  . TRP C 1 112 ? 7.211   -11.553 12.576  1.00 23.35 ? 107 TRP C CB  1 
ATOM   4012 C  CG  . TRP C 1 112 ? 6.247   -10.517 12.072  1.00 23.05 ? 107 TRP C CG  1 
ATOM   4013 C  CD1 . TRP C 1 112 ? 6.195   -9.203  12.437  1.00 22.94 ? 107 TRP C CD1 1 
ATOM   4014 C  CD2 . TRP C 1 112 ? 5.222   -10.702 11.080  1.00 21.66 ? 107 TRP C CD2 1 
ATOM   4015 N  NE1 . TRP C 1 112 ? 5.186   -8.563  11.764  1.00 21.63 ? 107 TRP C NE1 1 
ATOM   4016 C  CE2 . TRP C 1 112 ? 4.581   -9.449  10.915  1.00 22.09 ? 107 TRP C CE2 1 
ATOM   4017 C  CE3 . TRP C 1 112 ? 4.754   -11.803 10.356  1.00 20.75 ? 107 TRP C CE3 1 
ATOM   4018 C  CZ2 . TRP C 1 112 ? 3.527   -9.264  10.028  1.00 20.76 ? 107 TRP C CZ2 1 
ATOM   4019 C  CZ3 . TRP C 1 112 ? 3.712   -11.620 9.486   1.00 20.11 ? 107 TRP C CZ3 1 
ATOM   4020 C  CH2 . TRP C 1 112 ? 3.121   -10.360 9.310   1.00 20.89 ? 107 TRP C CH2 1 
ATOM   4021 N  N   . ASN C 1 113 ? 9.955   -9.235  12.482  1.00 17.19 ? 108 ASN C N   1 
ATOM   4022 C  CA  . ASN C 1 113 ? 10.574  -8.249  13.391  1.00 16.86 ? 108 ASN C CA  1 
ATOM   4023 C  C   . ASN C 1 113 ? 9.469   -7.488  14.082  1.00 14.06 ? 108 ASN C C   1 
ATOM   4024 O  O   . ASN C 1 113 ? 8.582   -6.962  13.393  1.00 22.79 ? 108 ASN C O   1 
ATOM   4025 C  CB  . ASN C 1 113 ? 11.519  -7.275  12.698  1.00 16.98 ? 108 ASN C CB  1 
ATOM   4026 C  CG  . ASN C 1 113 ? 12.900  -7.853  12.538  1.00 21.77 ? 108 ASN C CG  1 
ATOM   4027 O  OD1 . ASN C 1 113 ? 13.119  -9.001  12.912  1.00 21.91 ? 108 ASN C OD1 1 
ATOM   4028 N  ND2 . ASN C 1 113 ? 13.818  -7.071  11.985  1.00 22.87 ? 108 ASN C ND2 1 
ATOM   4029 N  N   . PHE C 1 114 ? 9.551   -7.314  15.352  1.00 14.42 ? 109 PHE C N   1 
ATOM   4030 C  CA  . PHE C 1 114 ? 8.480   -6.628  16.095  1.00 17.69 ? 109 PHE C CA  1 
ATOM   4031 C  C   . PHE C 1 114 ? 9.041   -6.068  17.380  1.00 18.88 ? 109 PHE C C   1 
ATOM   4032 O  O   . PHE C 1 114 ? 10.063  -6.541  17.875  1.00 20.62 ? 109 PHE C O   1 
ATOM   4033 C  CB  . PHE C 1 114 ? 7.272   -7.573  16.336  1.00 18.97 ? 109 PHE C CB  1 
ATOM   4034 C  CG  . PHE C 1 114 ? 7.379   -8.572  17.482  1.00 18.83 ? 109 PHE C CG  1 
ATOM   4035 C  CD1 . PHE C 1 114 ? 7.995   -9.799  17.320  1.00 20.38 ? 109 PHE C CD1 1 
ATOM   4036 C  CD2 . PHE C 1 114 ? 6.858   -8.284  18.742  1.00 21.91 ? 109 PHE C CD2 1 
ATOM   4037 C  CE1 . PHE C 1 114 ? 8.100   -10.698 18.388  1.00 21.42 ? 109 PHE C CE1 1 
ATOM   4038 C  CE2 . PHE C 1 114 ? 6.939   -9.192  19.794  1.00 22.31 ? 109 PHE C CE2 1 
ATOM   4039 C  CZ  . PHE C 1 114 ? 7.577   -10.397 19.624  1.00 19.61 ? 109 PHE C CZ  1 
ATOM   4040 N  N   . THR C 1 115 ? 8.322   -5.089  17.916  1.00 21.14 ? 110 THR C N   1 
ATOM   4041 C  CA  . THR C 1 115 ? 8.581   -4.469  19.234  1.00 19.91 ? 110 THR C CA  1 
ATOM   4042 C  C   . THR C 1 115 ? 7.355   -4.647  20.136  1.00 22.77 ? 110 THR C C   1 
ATOM   4043 O  O   . THR C 1 115 ? 6.197   -4.373  19.657  1.00 18.78 ? 110 THR C O   1 
ATOM   4044 C  CB  . THR C 1 115 ? 8.881   -2.991  19.017  1.00 23.15 ? 110 THR C CB  1 
ATOM   4045 O  OG1 . THR C 1 115 ? 7.810   -2.471  18.228  1.00 23.45 ? 110 THR C OG1 1 
ATOM   4046 C  CG2 . THR C 1 115 ? 10.204  -2.760  18.327  1.00 23.10 ? 110 THR C CG2 1 
ATOM   4047 N  N   . SER C 1 116 ? 7.571   -5.027  21.396  1.00 23.16 ? 111 SER C N   1 
ATOM   4048 C  CA  . SER C 1 116 ? 6.471   -5.195  22.376  1.00 28.86 ? 111 SER C CA  1 
ATOM   4049 C  C   . SER C 1 116 ? 6.943   -4.767  23.762  1.00 25.18 ? 111 SER C C   1 
ATOM   4050 O  O   . SER C 1 116 ? 8.055   -5.095  24.098  1.00 26.05 ? 111 SER C O   1 
ATOM   4051 C  CB  . SER C 1 116 ? 5.981   -6.618  22.410  1.00 31.57 ? 111 SER C CB  1 
ATOM   4052 O  OG  . SER C 1 116 ? 5.060   -6.778  23.468  1.00 41.64 ? 111 SER C OG  1 
ATOM   4053 N  N   . VAL C 1 117 ? 6.093   -4.068  24.504  1.00 24.66 ? 112 VAL C N   1 
ATOM   4054 C  CA  . VAL C 1 117 ? 6.290   -3.771  25.949  1.00 21.45 ? 112 VAL C CA  1 
ATOM   4055 C  C   . VAL C 1 117 ? 5.112   -4.341  26.726  1.00 22.46 ? 112 VAL C C   1 
ATOM   4056 O  O   . VAL C 1 117 ? 3.969   -3.972  26.351  1.00 21.72 ? 112 VAL C O   1 
ATOM   4057 C  CB  . VAL C 1 117 ? 6.406   -2.267  26.185  1.00 19.29 ? 112 VAL C CB  1 
ATOM   4058 C  CG1 . VAL C 1 117 ? 6.319   -1.960  27.644  1.00 19.46 ? 112 VAL C CG1 1 
ATOM   4059 C  CG2 . VAL C 1 117 ? 7.677   -1.708  25.570  1.00 20.14 ? 112 VAL C CG2 1 
ATOM   4060 N  N   . GLN C 1 118 ? 5.414   -5.155  27.750  1.00 19.87 ? 113 GLN C N   1 
ATOM   4061 C  CA  . GLN C 1 118 ? 4.485   -5.789  28.726  1.00 21.35 ? 113 GLN C CA  1 
ATOM   4062 C  C   . GLN C 1 118 ? 4.747   -5.215  30.127  1.00 21.52 ? 113 GLN C C   1 
ATOM   4063 O  O   . GLN C 1 118 ? 5.867   -5.333  30.669  1.00 22.26 ? 113 GLN C O   1 
ATOM   4064 C  CB  . GLN C 1 118 ? 4.662   -7.312  28.719  1.00 21.77 ? 113 GLN C CB  1 
ATOM   4065 C  CG  . GLN C 1 118 ? 4.191   -7.930  27.407  1.00 22.50 ? 113 GLN C CG  1 
ATOM   4066 C  CD  . GLN C 1 118 ? 4.289   -9.429  27.419  1.00 22.54 ? 113 GLN C CD  1 
ATOM   4067 O  OE1 . GLN C 1 118 ? 4.166   -10.047 28.460  1.00 21.87 ? 113 GLN C OE1 1 
ATOM   4068 N  NE2 . GLN C 1 118 ? 4.389   -10.023 26.241  1.00 22.15 ? 113 GLN C NE2 1 
ATOM   4069 N  N   . VAL C 1 119 ? 3.775   -4.502  30.670  1.00 24.93 ? 114 VAL C N   1 
ATOM   4070 C  CA  . VAL C 1 119 ? 3.877   -3.992  32.065  1.00 24.37 ? 114 VAL C CA  1 
ATOM   4071 C  C   . VAL C 1 119 ? 2.908   -4.800  32.903  1.00 22.80 ? 114 VAL C C   1 
ATOM   4072 O  O   . VAL C 1 119 ? 1.798   -5.087  32.430  1.00 20.77 ? 114 VAL C O   1 
ATOM   4073 C  CB  . VAL C 1 119 ? 3.661   -2.470  32.210  1.00 23.96 ? 114 VAL C CB  1 
ATOM   4074 C  CG1 . VAL C 1 119 ? 4.763   -1.699  31.496  1.00 26.51 ? 114 VAL C CG1 1 
ATOM   4075 C  CG2 . VAL C 1 119 ? 2.299   -2.037  31.716  1.00 27.31 ? 114 VAL C CG2 1 
ATOM   4076 N  N   . ARG C 1 120 ? 3.353   -5.146  34.105  1.00 23.45 ? 115 ARG C N   1 
ATOM   4077 C  CA  . ARG C 1 120 ? 2.526   -5.891  35.070  1.00 26.31 ? 115 ARG C CA  1 
ATOM   4078 C  C   . ARG C 1 120 ? 2.519   -5.118  36.382  1.00 26.69 ? 115 ARG C C   1 
ATOM   4079 O  O   . ARG C 1 120 ? 3.577   -4.540  36.790  1.00 25.01 ? 115 ARG C O   1 
ATOM   4080 C  CB  . ARG C 1 120 ? 3.024   -7.329  35.236  1.00 27.66 ? 115 ARG C CB  1 
ATOM   4081 C  CG  . ARG C 1 120 ? 2.825   -8.183  33.994  1.00 29.55 ? 115 ARG C CG  1 
ATOM   4082 C  CD  . ARG C 1 120 ? 3.462   -9.565  34.062  1.00 31.58 ? 115 ARG C CD  1 
ATOM   4083 N  NE  . ARG C 1 120 ? 2.897   -10.451 33.053  1.00 31.18 ? 115 ARG C NE  1 
ATOM   4084 C  CZ  . ARG C 1 120 ? 3.281   -10.523 31.784  1.00 30.14 ? 115 ARG C CZ  1 
ATOM   4085 N  NH1 . ARG C 1 120 ? 4.302   -9.812  31.316  1.00 31.64 ? 115 ARG C NH1 1 
ATOM   4086 N  NH2 . ARG C 1 120 ? 2.670   -11.373 30.999  1.00 31.56 ? 115 ARG C NH2 1 
ATOM   4087 N  N   . GLY C 1 121 ? 1.353   -5.154  37.007  1.00 24.40 ? 116 GLY C N   1 
ATOM   4088 C  CA  . GLY C 1 121 ? 1.155   -4.755  38.401  1.00 26.30 ? 116 GLY C CA  1 
ATOM   4089 C  C   . GLY C 1 121 ? -0.294  -4.876  38.752  1.00 28.32 ? 116 GLY C C   1 
ATOM   4090 O  O   . GLY C 1 121 ? -1.046  -5.619  38.048  1.00 27.97 ? 116 GLY C O   1 
ATOM   4091 N  N   . GLU C 1 122 ? -0.659  -4.129  39.773  1.00 28.72 ? 117 GLU C N   1 
ATOM   4092 C  CA  . GLU C 1 122 ? -1.985  -4.177  40.419  1.00 35.37 ? 117 GLU C CA  1 
ATOM   4093 C  C   . GLU C 1 122 ? -2.824  -3.071  39.790  1.00 31.46 ? 117 GLU C C   1 
ATOM   4094 O  O   . GLU C 1 122 ? -2.396  -1.904  39.791  1.00 31.13 ? 117 GLU C O   1 
ATOM   4095 C  CB  . GLU C 1 122 ? -1.772  -4.056  41.929  1.00 38.02 ? 117 GLU C CB  1 
ATOM   4096 C  CG  . GLU C 1 122 ? -3.036  -4.100  42.741  1.00 46.12 ? 117 GLU C CG  1 
ATOM   4097 C  CD  . GLU C 1 122 ? -2.768  -3.937  44.233  1.00 54.54 ? 117 GLU C CD  1 
ATOM   4098 O  OE1 . GLU C 1 122 ? -3.536  -3.196  44.898  1.00 58.34 ? 117 GLU C OE1 1 
ATOM   4099 O  OE2 . GLU C 1 122 ? -1.782  -4.551  44.725  1.00 57.76 ? 117 GLU C OE2 1 
ATOM   4100 N  N   . LEU C 1 123 ? -3.943  -3.435  39.191  1.00 34.06 ? 118 LEU C N   1 
ATOM   4101 C  CA  . LEU C 1 123 ? -4.871  -2.425  38.630  1.00 36.61 ? 118 LEU C CA  1 
ATOM   4102 C  C   . LEU C 1 123 ? -5.725  -1.903  39.788  1.00 39.07 ? 118 LEU C C   1 
ATOM   4103 O  O   . LEU C 1 123 ? -6.270  -2.739  40.555  1.00 38.30 ? 118 LEU C O   1 
ATOM   4104 C  CB  . LEU C 1 123 ? -5.717  -3.036  37.513  1.00 34.93 ? 118 LEU C CB  1 
ATOM   4105 C  CG  . LEU C 1 123 ? -6.608  -2.037  36.778  1.00 34.29 ? 118 LEU C CG  1 
ATOM   4106 C  CD1 . LEU C 1 123 ? -6.665  -2.377  35.310  1.00 33.32 ? 118 LEU C CD1 1 
ATOM   4107 C  CD2 . LEU C 1 123 ? -8.014  -1.976  37.383  1.00 36.86 ? 118 LEU C CD2 1 
ATOM   4108 N  N   . ARG C 1 124 ? -5.780  -0.581  39.932  1.00 38.03 ? 119 ARG C N   1 
ATOM   4109 C  CA  . ARG C 1 124 ? -6.461  0.125   41.035  1.00 37.18 ? 119 ARG C CA  1 
ATOM   4110 C  C   . ARG C 1 124 ? -7.610  0.904   40.395  1.00 36.54 ? 119 ARG C C   1 
ATOM   4111 O  O   . ARG C 1 124 ? -7.320  1.812   39.632  1.00 34.01 ? 119 ARG C O   1 
ATOM   4112 C  CB  . ARG C 1 124 ? -5.433  1.005   41.751  1.00 44.29 ? 119 ARG C CB  1 
ATOM   4113 C  CG  . ARG C 1 124 ? -5.809  1.392   43.175  1.00 52.23 ? 119 ARG C CG  1 
ATOM   4114 C  CD  . ARG C 1 124 ? -5.094  2.634   43.718  1.00 58.14 ? 119 ARG C CD  1 
ATOM   4115 N  NE  . ARG C 1 124 ? -5.344  3.886   42.996  1.00 57.76 ? 119 ARG C NE  1 
ATOM   4116 C  CZ  . ARG C 1 124 ? -6.495  4.571   42.996  1.00 66.55 ? 119 ARG C CZ  1 
ATOM   4117 N  NH1 . ARG C 1 124 ? -7.553  4.135   43.664  1.00 72.26 ? 119 ARG C NH1 1 
ATOM   4118 N  NH2 . ARG C 1 124 ? -6.597  5.694   42.305  1.00 68.32 ? 119 ARG C NH2 1 
ATOM   4119 N  N   . LYS C 1 125 ? -8.861  0.507   40.622  1.00 31.79 ? 120 LYS C N   1 
ATOM   4120 C  CA  . LYS C 1 125 ? -10.036 1.236   40.083  1.00 34.53 ? 120 LYS C CA  1 
ATOM   4121 C  C   . LYS C 1 125 ? -10.088 2.654   40.688  1.00 35.29 ? 120 LYS C C   1 
ATOM   4122 O  O   . LYS C 1 125 ? -9.729  2.829   41.872  1.00 38.21 ? 120 LYS C O   1 
ATOM   4123 C  CB  . LYS C 1 125 ? -11.316 0.440   40.347  1.00 35.04 ? 120 LYS C CB  1 
ATOM   4124 C  CG  . LYS C 1 125 ? -11.501 -0.804  39.493  1.00 34.70 ? 120 LYS C CG  1 
ATOM   4125 C  CD  . LYS C 1 125 ? -12.861 -1.415  39.703  1.00 36.32 ? 120 LYS C CD  1 
ATOM   4126 C  CE  . LYS C 1 125 ? -13.040 -2.746  39.007  1.00 38.22 ? 120 LYS C CE  1 
ATOM   4127 N  NZ  . LYS C 1 125 ? -14.393 -3.308  39.236  1.00 39.41 ? 120 LYS C NZ  1 
ATOM   4128 N  N   . VAL C 1 126 ? -10.485 3.637   39.881  1.00 37.24 ? 121 VAL C N   1 
ATOM   4129 C  CA  . VAL C 1 126 ? -10.836 5.020   40.306  1.00 39.48 ? 121 VAL C CA  1 
ATOM   4130 C  C   . VAL C 1 126 ? -12.360 5.116   40.378  1.00 43.82 ? 121 VAL C C   1 
ATOM   4131 O  O   . VAL C 1 126 ? -13.002 4.998   39.323  1.00 41.39 ? 121 VAL C O   1 
ATOM   4132 C  CB  . VAL C 1 126 ? -10.273 6.049   39.317  1.00 43.23 ? 121 VAL C CB  1 
ATOM   4133 C  CG1 . VAL C 1 126 ? -10.953 7.397   39.465  1.00 46.14 ? 121 VAL C CG1 1 
ATOM   4134 C  CG2 . VAL C 1 126 ? -8.768  6.176   39.440  1.00 46.70 ? 121 VAL C CG2 1 
ATOM   4135 N  N   . GLU C 1 127 ? -12.936 5.354   41.555  1.00 45.43 ? 122 GLU C N   1 
ATOM   4136 C  CA  . GLU C 1 127 ? -14.421 5.422   41.658  1.00 52.29 ? 122 GLU C CA  1 
ATOM   4137 C  C   . GLU C 1 127 ? -14.876 6.887   41.727  1.00 54.52 ? 122 GLU C C   1 
ATOM   4138 O  O   . GLU C 1 127 ? -16.059 7.144   41.411  1.00 60.90 ? 122 GLU C O   1 
ATOM   4139 C  CB  . GLU C 1 127 ? -14.915 4.545   42.812  1.00 53.65 ? 122 GLU C CB  1 
ATOM   4140 C  CG  . GLU C 1 127 ? -14.493 3.082   42.677  1.00 53.74 ? 122 GLU C CG  1 
ATOM   4141 C  CD  . GLU C 1 127 ? -15.150 2.280   41.556  1.00 55.80 ? 122 GLU C CD  1 
ATOM   4142 O  OE1 . GLU C 1 127 ? -14.765 1.109   41.369  1.00 61.99 ? 122 GLU C OE1 1 
ATOM   4143 O  OE2 . GLU C 1 127 ? -16.055 2.808   40.882  1.00 54.05 ? 122 GLU C OE2 1 
ATOM   4144 N  N   . SER C 1 128 ? -13.979 7.818   42.057  1.00 47.09 ? 123 SER C N   1 
ATOM   4145 C  CA  . SER C 1 128 ? -14.313 9.257   42.220  1.00 46.31 ? 123 SER C CA  1 
ATOM   4146 C  C   . SER C 1 128 ? -14.463 9.926   40.849  1.00 42.46 ? 123 SER C C   1 
ATOM   4147 O  O   . SER C 1 128 ? -13.529 9.803   40.031  1.00 35.54 ? 123 SER C O   1 
ATOM   4148 C  CB  . SER C 1 128 ? -13.270 9.942   43.045  1.00 46.47 ? 123 SER C CB  1 
ATOM   4149 O  OG  . SER C 1 128 ? -12.948 9.152   44.171  1.00 53.65 ? 123 SER C OG  1 
ATOM   4150 N  N   . ALA C 1 129 ? -15.586 10.622  40.631  1.00 37.17 ? 124 ALA C N   1 
ATOM   4151 C  CA  . ALA C 1 129 ? -15.888 11.449  39.434  1.00 41.56 ? 124 ALA C CA  1 
ATOM   4152 C  C   . ALA C 1 129 ? -14.738 12.419  39.104  1.00 39.33 ? 124 ALA C C   1 
ATOM   4153 O  O   . ALA C 1 129 ? -14.459 12.613  37.912  1.00 37.68 ? 124 ALA C O   1 
ATOM   4154 C  CB  . ALA C 1 129 ? -17.173 12.208  39.654  1.00 40.56 ? 124 ALA C CB  1 
ATOM   4155 N  N   . ASP C 1 130 ? -14.123 13.030  40.117  1.00 40.97 ? 125 ASP C N   1 
ATOM   4156 C  CA  . ASP C 1 130 ? -12.991 13.994  39.974  1.00 45.93 ? 125 ASP C CA  1 
ATOM   4157 C  C   . ASP C 1 130 ? -11.800 13.309  39.287  1.00 36.94 ? 125 ASP C C   1 
ATOM   4158 O  O   . ASP C 1 130 ? -11.199 13.905  38.361  1.00 34.39 ? 125 ASP C O   1 
ATOM   4159 C  CB  . ASP C 1 130 ? -12.561 14.596  41.328  1.00 50.98 ? 125 ASP C CB  1 
ATOM   4160 C  CG  . ASP C 1 130 ? -12.010 13.630  42.384  1.00 64.10 ? 125 ASP C CG  1 
ATOM   4161 O  OD1 . ASP C 1 130 ? -11.330 14.112  43.321  1.00 72.19 ? 125 ASP C OD1 1 
ATOM   4162 O  OD2 . ASP C 1 130 ? -12.269 12.403  42.291  1.00 67.56 ? 125 ASP C OD2 1 
ATOM   4163 N  N   . ASP C 1 131 ? -11.441 12.128  39.762  1.00 31.79 ? 126 ASP C N   1 
ATOM   4164 C  CA  . ASP C 1 131 ? -10.236 11.401  39.290  1.00 38.72 ? 126 ASP C CA  1 
ATOM   4165 C  C   . ASP C 1 131 ? -10.534 10.742  37.933  1.00 35.03 ? 126 ASP C C   1 
ATOM   4166 O  O   . ASP C 1 131 ? -9.542  10.509  37.188  1.00 37.34 ? 126 ASP C O   1 
ATOM   4167 C  CB  . ASP C 1 131 ? -9.753  10.408  40.345  1.00 41.31 ? 126 ASP C CB  1 
ATOM   4168 C  CG  . ASP C 1 131 ? -9.261  11.074  41.616  1.00 48.20 ? 126 ASP C CG  1 
ATOM   4169 O  OD1 . ASP C 1 131 ? -8.495  12.063  41.507  1.00 53.07 ? 126 ASP C OD1 1 
ATOM   4170 O  OD2 . ASP C 1 131 ? -9.655  10.600  42.701  1.00 46.97 ? 126 ASP C OD2 1 
ATOM   4171 N  N   . THR C 1 132 ? -11.816 10.483  37.626  1.00 31.66 ? 127 THR C N   1 
ATOM   4172 C  CA  . THR C 1 132 ? -12.313 9.924   36.330  1.00 31.57 ? 127 THR C CA  1 
ATOM   4173 C  C   . THR C 1 132 ? -12.199 11.019  35.269  1.00 31.02 ? 127 THR C C   1 
ATOM   4174 O  O   . THR C 1 132 ? -11.575 10.779  34.201  1.00 28.80 ? 127 THR C O   1 
ATOM   4175 C  CB  . THR C 1 132 ? -13.749 9.377   36.446  1.00 31.33 ? 127 THR C CB  1 
ATOM   4176 O  OG1 . THR C 1 132 ? -13.763 8.323   37.399  1.00 30.88 ? 127 THR C OG1 1 
ATOM   4177 C  CG2 . THR C 1 132 ? -14.310 8.782   35.174  1.00 33.23 ? 127 THR C CG2 1 
ATOM   4178 N  N   . LEU C 1 133 ? -12.755 12.193  35.569  1.00 27.01 ? 128 LEU C N   1 
ATOM   4179 C  CA  . LEU C 1 133 ? -12.625 13.377  34.707  1.00 27.67 ? 128 LEU C CA  1 
ATOM   4180 C  C   . LEU C 1 133 ? -11.137 13.657  34.444  1.00 25.28 ? 128 LEU C C   1 
ATOM   4181 O  O   . LEU C 1 133 ? -10.796 13.813  33.286  1.00 26.28 ? 128 LEU C O   1 
ATOM   4182 C  CB  . LEU C 1 133 ? -13.330 14.581  35.341  1.00 28.75 ? 128 LEU C CB  1 
ATOM   4183 C  CG  . LEU C 1 133 ? -13.381 15.829  34.449  1.00 25.94 ? 128 LEU C CG  1 
ATOM   4184 C  CD1 . LEU C 1 133 ? -14.229 15.587  33.200  1.00 26.92 ? 128 LEU C CD1 1 
ATOM   4185 C  CD2 . LEU C 1 133 ? -13.906 17.026  35.225  1.00 28.45 ? 128 LEU C CD2 1 
ATOM   4186 N  N   . ALA C 1 134 ? -10.278 13.731  35.463  1.00 25.40 ? 129 ALA C N   1 
ATOM   4187 C  CA  . ALA C 1 134 ? -8.820  14.008  35.280  1.00 24.43 ? 129 ALA C CA  1 
ATOM   4188 C  C   . ALA C 1 134 ? -8.162  13.020  34.313  1.00 25.86 ? 129 ALA C C   1 
ATOM   4189 O  O   . ALA C 1 134 ? -7.227  13.429  33.582  1.00 27.31 ? 129 ALA C O   1 
ATOM   4190 C  CB  . ALA C 1 134 ? -8.120  13.938  36.577  1.00 22.26 ? 129 ALA C CB  1 
ATOM   4191 N  N   . THR C 1 135 ? -8.548  11.741  34.404  1.00 27.83 ? 130 THR C N   1 
ATOM   4192 C  CA  . THR C 1 135 ? -8.003  10.637  33.575  1.00 27.24 ? 130 THR C CA  1 
ATOM   4193 C  C   . THR C 1 135 ? -8.282  10.948  32.103  1.00 26.39 ? 130 THR C C   1 
ATOM   4194 O  O   . THR C 1 135 ? -7.315  10.865  31.299  1.00 26.08 ? 130 THR C O   1 
ATOM   4195 C  CB  . THR C 1 135 ? -8.565  9.260   33.966  1.00 26.03 ? 130 THR C CB  1 
ATOM   4196 O  OG1 . THR C 1 135 ? -8.288  8.997   35.344  1.00 23.18 ? 130 THR C OG1 1 
ATOM   4197 C  CG2 . THR C 1 135 ? -7.959  8.157   33.124  1.00 26.57 ? 130 THR C CG2 1 
ATOM   4198 N  N   . VAL C 1 136 ? -9.542  11.257  31.759  1.00 23.08 ? 131 VAL C N   1 
ATOM   4199 C  CA  . VAL C 1 136 ? -9.987  11.440  30.346  1.00 23.60 ? 131 VAL C CA  1 
ATOM   4200 C  C   . VAL C 1 136 ? -9.422  12.758  29.783  1.00 23.95 ? 131 VAL C C   1 
ATOM   4201 O  O   . VAL C 1 136 ? -9.015  12.762  28.573  1.00 25.54 ? 131 VAL C O   1 
ATOM   4202 C  CB  . VAL C 1 136 ? -11.520 11.299  30.172  1.00 24.97 ? 131 VAL C CB  1 
ATOM   4203 C  CG1 . VAL C 1 136 ? -12.026 9.964   30.734  1.00 24.33 ? 131 VAL C CG1 1 
ATOM   4204 C  CG2 . VAL C 1 136 ? -12.315 12.455  30.733  1.00 23.79 ? 131 VAL C CG2 1 
ATOM   4205 N  N   . ARG C 1 137 ? -9.339  13.823  30.591  1.00 23.16 ? 132 ARG C N   1 
ATOM   4206 C  CA  . ARG C 1 137 ? -8.780  15.133  30.125  1.00 23.39 ? 132 ARG C CA  1 
ATOM   4207 C  C   . ARG C 1 137 ? -7.261  14.982  29.945  1.00 24.24 ? 132 ARG C C   1 
ATOM   4208 O  O   . ARG C 1 137 ? -6.689  15.584  28.975  1.00 22.68 ? 132 ARG C O   1 
ATOM   4209 C  CB  . ARG C 1 137 ? -9.120  16.266  31.092  1.00 21.27 ? 132 ARG C CB  1 
ATOM   4210 C  CG  . ARG C 1 137 ? -10.619 16.553  31.136  1.00 22.42 ? 132 ARG C CG  1 
ATOM   4211 C  CD  . ARG C 1 137 ? -10.962 17.851  31.827  1.00 22.55 ? 132 ARG C CD  1 
ATOM   4212 N  NE  . ARG C 1 137 ? -10.438 17.994  33.196  1.00 23.87 ? 132 ARG C NE  1 
ATOM   4213 C  CZ  . ARG C 1 137 ? -10.812 18.927  34.079  1.00 25.61 ? 132 ARG C CZ  1 
ATOM   4214 N  NH1 . ARG C 1 137 ? -11.757 19.803  33.776  1.00 30.47 ? 132 ARG C NH1 1 
ATOM   4215 N  NH2 . ARG C 1 137 ? -10.265 18.975  35.277  1.00 23.33 ? 132 ARG C NH2 1 
ATOM   4216 N  N   . ALA C 1 138 ? -6.603  14.210  30.814  1.00 23.50 ? 133 ALA C N   1 
ATOM   4217 C  CA  . ALA C 1 138 ? -5.128  14.034  30.719  1.00 22.78 ? 133 ALA C CA  1 
ATOM   4218 C  C   . ALA C 1 138 ? -4.845  13.194  29.475  1.00 24.41 ? 133 ALA C C   1 
ATOM   4219 O  O   . ALA C 1 138 ? -3.812  13.413  28.853  1.00 22.31 ? 133 ALA C O   1 
ATOM   4220 C  CB  . ALA C 1 138 ? -4.559  13.407  31.968  1.00 24.79 ? 133 ALA C CB  1 
ATOM   4221 N  N   . THR C 1 139 ? -5.763  12.275  29.138  1.00 23.53 ? 134 THR C N   1 
ATOM   4222 C  CA  . THR C 1 139 ? -5.642  11.392  27.953  1.00 23.35 ? 134 THR C CA  1 
ATOM   4223 C  C   . THR C 1 139 ? -5.777  12.273  26.696  1.00 25.00 ? 134 THR C C   1 
ATOM   4224 O  O   . THR C 1 139 ? -4.886  12.198  25.823  1.00 25.66 ? 134 THR C O   1 
ATOM   4225 C  CB  . THR C 1 139 ? -6.598  10.196  28.021  1.00 21.36 ? 134 THR C CB  1 
ATOM   4226 O  OG1 . THR C 1 139 ? -6.321  9.396   29.185  1.00 21.19 ? 134 THR C OG1 1 
ATOM   4227 C  CG2 . THR C 1 139 ? -6.484  9.310   26.793  1.00 20.43 ? 134 THR C CG2 1 
ATOM   4228 N  N   . VAL C 1 140 ? -6.820  13.091  26.622  1.00 24.55 ? 135 VAL C N   1 
ATOM   4229 C  CA  . VAL C 1 140 ? -6.964  14.105  25.554  1.00 24.09 ? 135 VAL C CA  1 
ATOM   4230 C  C   . VAL C 1 140 ? -5.659  14.875  25.438  1.00 25.30 ? 135 VAL C C   1 
ATOM   4231 O  O   . VAL C 1 140 ? -5.129  14.936  24.302  1.00 25.94 ? 135 VAL C O   1 
ATOM   4232 C  CB  . VAL C 1 140 ? -8.137  15.069  25.770  1.00 24.39 ? 135 VAL C CB  1 
ATOM   4233 C  CG1 . VAL C 1 140 ? -8.169  16.075  24.649  1.00 26.86 ? 135 VAL C CG1 1 
ATOM   4234 C  CG2 . VAL C 1 140 ? -9.471  14.345  25.795  1.00 26.87 ? 135 VAL C CG2 1 
ATOM   4235 N  N   . ALA C 1 141 ? -5.186  15.515  26.504  1.00 24.28 ? 136 ALA C N   1 
ATOM   4236 C  CA  . ALA C 1 141 ? -3.985  16.371  26.379  1.00 25.03 ? 136 ALA C CA  1 
ATOM   4237 C  C   . ALA C 1 141 ? -2.883  15.548  25.679  1.00 24.38 ? 136 ALA C C   1 
ATOM   4238 O  O   . ALA C 1 141 ? -2.361  15.956  24.614  1.00 26.12 ? 136 ALA C O   1 
ATOM   4239 C  CB  . ALA C 1 141 ? -3.582  16.881  27.724  1.00 28.73 ? 136 ALA C CB  1 
ATOM   4240 N  N   . ALA C 1 142 ? -2.582  14.378  26.221  1.00 23.23 ? 137 ALA C N   1 
ATOM   4241 C  CA  . ALA C 1 142 ? -1.461  13.514  25.778  1.00 24.43 ? 137 ALA C CA  1 
ATOM   4242 C  C   . ALA C 1 142 ? -1.690  13.016  24.338  1.00 22.41 ? 137 ALA C C   1 
ATOM   4243 O  O   . ALA C 1 142 ? -0.705  13.155  23.535  1.00 21.94 ? 137 ALA C O   1 
ATOM   4244 C  CB  . ALA C 1 142 ? -1.265  12.373  26.747  1.00 25.73 ? 137 ALA C CB  1 
ATOM   4245 N  N   . LEU C 1 143 ? -2.876  12.471  23.981  1.00 20.43 ? 138 LEU C N   1 
ATOM   4246 C  CA  . LEU C 1 143 ? -3.020  11.845  22.641  1.00 20.87 ? 138 LEU C CA  1 
ATOM   4247 C  C   . LEU C 1 143 ? -3.224  12.895  21.547  1.00 24.77 ? 138 LEU C C   1 
ATOM   4248 O  O   . LEU C 1 143 ? -2.646  12.670  20.451  1.00 22.48 ? 138 LEU C O   1 
ATOM   4249 C  CB  . LEU C 1 143 ? -4.131  10.799  22.601  1.00 24.58 ? 138 LEU C CB  1 
ATOM   4250 C  CG  . LEU C 1 143 ? -4.060  9.639   23.599  1.00 27.87 ? 138 LEU C CG  1 
ATOM   4251 C  CD1 . LEU C 1 143 ? -4.644  8.380   22.978  1.00 28.19 ? 138 LEU C CD1 1 
ATOM   4252 C  CD2 . LEU C 1 143 ? -2.653  9.390   24.114  1.00 29.53 ? 138 LEU C CD2 1 
ATOM   4253 N  N   . GLU C 1 144 ? -4.066  13.921  21.746  1.00 21.84 ? 139 GLU C N   1 
ATOM   4254 C  CA  . GLU C 1 144 ? -4.319  14.949  20.697  1.00 24.00 ? 139 GLU C CA  1 
ATOM   4255 C  C   . GLU C 1 144 ? -2.980  15.620  20.317  1.00 26.75 ? 139 GLU C C   1 
ATOM   4256 O  O   . GLU C 1 144 ? -2.700  15.757  19.132  1.00 25.04 ? 139 GLU C O   1 
ATOM   4257 C  CB  . GLU C 1 144 ? -5.388  15.939  21.153  1.00 25.68 ? 139 GLU C CB  1 
ATOM   4258 C  CG  . GLU C 1 144 ? -5.836  16.922  20.072  1.00 26.08 ? 139 GLU C CG  1 
ATOM   4259 C  CD  . GLU C 1 144 ? -6.466  16.292  18.843  1.00 24.62 ? 139 GLU C CD  1 
ATOM   4260 O  OE1 . GLU C 1 144 ? -7.030  15.187  18.953  1.00 22.97 ? 139 GLU C OE1 1 
ATOM   4261 O  OE2 . GLU C 1 144 ? -6.341  16.888  17.761  1.00 26.69 ? 139 GLU C OE2 1 
ATOM   4262 N  N   . SER C 1 145 ? -2.112  15.931  21.271  1.00 29.43 ? 140 SER C N   1 
ATOM   4263 C  CA  . SER C 1 145 ? -0.816  16.602  20.982  1.00 30.97 ? 140 SER C CA  1 
ATOM   4264 C  C   . SER C 1 145 ? 0.049   15.667  20.124  1.00 33.51 ? 140 SER C C   1 
ATOM   4265 O  O   . SER C 1 145 ? 0.539   16.115  19.080  1.00 35.23 ? 140 SER C O   1 
ATOM   4266 C  CB  . SER C 1 145 ? -0.149  16.997  22.228  1.00 29.72 ? 140 SER C CB  1 
ATOM   4267 O  OG  . SER C 1 145 ? -0.158  15.895  23.095  1.00 37.06 ? 140 SER C OG  1 
ATOM   4268 N  N   . ARG C 1 146 ? 0.135   14.384  20.477  1.00 38.03 ? 141 ARG C N   1 
ATOM   4269 C  CA  . ARG C 1 146 ? 1.024   13.405  19.785  1.00 34.38 ? 141 ARG C CA  1 
ATOM   4270 C  C   . ARG C 1 146 ? 0.407   12.907  18.464  1.00 29.76 ? 141 ARG C C   1 
ATOM   4271 O  O   . ARG C 1 146 ? 1.183   12.788  17.518  1.00 25.83 ? 141 ARG C O   1 
ATOM   4272 C  CB  . ARG C 1 146 ? 1.391   12.252  20.720  1.00 36.64 ? 141 ARG C CB  1 
ATOM   4273 C  CG  . ARG C 1 146 ? 2.409   11.270  20.147  1.00 38.53 ? 141 ARG C CG  1 
ATOM   4274 C  CD  . ARG C 1 146 ? 2.746   10.232  21.203  1.00 43.89 ? 141 ARG C CD  1 
ATOM   4275 N  NE  . ARG C 1 146 ? 3.579   10.817  22.244  1.00 48.36 ? 141 ARG C NE  1 
ATOM   4276 C  CZ  . ARG C 1 146 ? 4.914   10.826  22.265  1.00 47.83 ? 141 ARG C CZ  1 
ATOM   4277 N  NH1 . ARG C 1 146 ? 5.622   10.244  21.307  1.00 47.79 ? 141 ARG C NH1 1 
ATOM   4278 N  NH2 . ARG C 1 146 ? 5.537   11.408  23.272  1.00 48.23 ? 141 ARG C NH2 1 
ATOM   4279 N  N   . PHE C 1 147 ? -0.902  12.625  18.373  1.00 26.10 ? 142 PHE C N   1 
ATOM   4280 C  CA  . PHE C 1 147 ? -1.506  11.906  17.217  1.00 28.01 ? 142 PHE C CA  1 
ATOM   4281 C  C   . PHE C 1 147 ? -2.546  12.748  16.456  1.00 28.11 ? 142 PHE C C   1 
ATOM   4282 O  O   . PHE C 1 147 ? -2.981  12.317  15.371  1.00 27.66 ? 142 PHE C O   1 
ATOM   4283 C  CB  . PHE C 1 147 ? -2.113  10.577  17.678  1.00 26.59 ? 142 PHE C CB  1 
ATOM   4284 C  CG  . PHE C 1 147 ? -1.141  9.716   18.445  1.00 27.59 ? 142 PHE C CG  1 
ATOM   4285 C  CD1 . PHE C 1 147 ? -0.158  9.005   17.779  1.00 26.98 ? 142 PHE C CD1 1 
ATOM   4286 C  CD2 . PHE C 1 147 ? -1.166  9.672   19.839  1.00 26.57 ? 142 PHE C CD2 1 
ATOM   4287 C  CE1 . PHE C 1 147 ? 0.774   8.255   18.476  1.00 27.92 ? 142 PHE C CE1 1 
ATOM   4288 C  CE2 . PHE C 1 147 ? -0.244  8.904   20.534  1.00 28.93 ? 142 PHE C CE2 1 
ATOM   4289 C  CZ  . PHE C 1 147 ? 0.739   8.208   19.852  1.00 27.31 ? 142 PHE C CZ  1 
ATOM   4290 N  N   . GLY C 1 148 ? -2.914  13.925  16.954  1.00 28.20 ? 143 GLY C N   1 
ATOM   4291 C  CA  . GLY C 1 148 ? -4.151  14.603  16.522  1.00 28.67 ? 143 GLY C CA  1 
ATOM   4292 C  C   . GLY C 1 148 ? -3.877  15.762  15.593  1.00 29.89 ? 143 GLY C C   1 
ATOM   4293 O  O   . GLY C 1 148 ? -2.728  15.845  15.071  1.00 27.93 ? 143 GLY C O   1 
ATOM   4294 N  N   . ALA C 1 149 ? -4.894  16.616  15.403  1.00 30.43 ? 144 ALA C N   1 
ATOM   4295 C  CA  . ALA C 1 149 ? -4.893  17.753  14.448  1.00 30.92 ? 144 ALA C CA  1 
ATOM   4296 C  C   . ALA C 1 149 ? -5.306  19.051  15.164  1.00 30.08 ? 144 ALA C C   1 
ATOM   4297 O  O   . ALA C 1 149 ? -6.097  19.807  14.619  1.00 35.43 ? 144 ALA C O   1 
ATOM   4298 C  CB  . ALA C 1 149 ? -5.761  17.428  13.257  1.00 30.52 ? 144 ALA C CB  1 
ATOM   4299 N  N   . GLY C 1 150 ? -4.747  19.290  16.352  1.00 30.58 ? 145 GLY C N   1 
ATOM   4300 C  CA  . GLY C 1 150 ? -4.806  20.568  17.083  1.00 30.75 ? 145 GLY C CA  1 
ATOM   4301 C  C   . GLY C 1 150 ? -6.186  20.877  17.629  1.00 34.15 ? 145 GLY C C   1 
ATOM   4302 O  O   . GLY C 1 150 ? -6.421  22.068  17.896  1.00 31.88 ? 145 GLY C O   1 
ATOM   4303 N  N   . TRP C 1 151 ? -7.045  19.856  17.839  1.00 32.34 ? 146 TRP C N   1 
ATOM   4304 C  CA  . TRP C 1 151 ? -8.403  20.018  18.444  1.00 28.88 ? 146 TRP C CA  1 
ATOM   4305 C  C   . TRP C 1 151 ? -8.277  20.568  19.866  1.00 31.62 ? 146 TRP C C   1 
ATOM   4306 O  O   . TRP C 1 151 ? -7.469  20.047  20.668  1.00 27.38 ? 146 TRP C O   1 
ATOM   4307 C  CB  . TRP C 1 151 ? -9.158  18.685  18.456  1.00 27.89 ? 146 TRP C CB  1 
ATOM   4308 C  CG  . TRP C 1 151 ? -10.537 18.756  19.024  1.00 22.95 ? 146 TRP C CG  1 
ATOM   4309 C  CD1 . TRP C 1 151 ? -11.645 19.304  18.434  1.00 25.72 ? 146 TRP C CD1 1 
ATOM   4310 C  CD2 . TRP C 1 151 ? -10.991 18.175  20.256  1.00 25.45 ? 146 TRP C CD2 1 
ATOM   4311 N  NE1 . TRP C 1 151 ? -12.743 19.158  19.243  1.00 22.63 ? 146 TRP C NE1 1 
ATOM   4312 C  CE2 . TRP C 1 151 ? -12.380 18.452  20.356  1.00 23.85 ? 146 TRP C CE2 1 
ATOM   4313 C  CE3 . TRP C 1 151 ? -10.370 17.463  21.295  1.00 24.12 ? 146 TRP C CE3 1 
ATOM   4314 C  CZ2 . TRP C 1 151 ? -13.137 18.022  21.441  1.00 24.16 ? 146 TRP C CZ2 1 
ATOM   4315 C  CZ3 . TRP C 1 151 ? -11.116 17.066  22.384  1.00 23.86 ? 146 TRP C CZ3 1 
ATOM   4316 C  CH2 . TRP C 1 151 ? -12.492 17.326  22.440  1.00 23.68 ? 146 TRP C CH2 1 
ATOM   4317 N  N   . ASP C 1 152 ? -9.123  21.541  20.183  1.00 31.97 ? 147 ASP C N   1 
ATOM   4318 C  CA  . ASP C 1 152 ? -9.224  22.192  21.505  1.00 31.11 ? 147 ASP C CA  1 
ATOM   4319 C  C   . ASP C 1 152 ? -10.413 21.565  22.229  1.00 28.17 ? 147 ASP C C   1 
ATOM   4320 O  O   . ASP C 1 152 ? -11.592 21.785  21.780  1.00 28.64 ? 147 ASP C O   1 
ATOM   4321 C  CB  . ASP C 1 152 ? -9.375  23.701  21.291  1.00 35.95 ? 147 ASP C CB  1 
ATOM   4322 C  CG  . ASP C 1 152 ? -9.689  24.491  22.540  1.00 40.07 ? 147 ASP C CG  1 
ATOM   4323 O  OD1 . ASP C 1 152 ? -9.432  23.968  23.661  1.00 42.76 ? 147 ASP C OD1 1 
ATOM   4324 O  OD2 . ASP C 1 152 ? -10.207 25.612  22.376  1.00 43.98 ? 147 ASP C OD2 1 
ATOM   4325 N  N   . MET C 1 153 ? -10.134 20.870  23.333  1.00 26.82 ? 148 MET C N   1 
ATOM   4326 C  CA  . MET C 1 153 ? -11.166 20.171  24.136  1.00 26.39 ? 148 MET C CA  1 
ATOM   4327 C  C   . MET C 1 153 ? -12.055 21.148  24.948  1.00 26.85 ? 148 MET C C   1 
ATOM   4328 O  O   . MET C 1 153 ? -13.104 20.698  25.513  1.00 22.51 ? 148 MET C O   1 
ATOM   4329 C  CB  . MET C 1 153 ? -10.476 19.178  25.057  1.00 29.64 ? 148 MET C CB  1 
ATOM   4330 C  CG  . MET C 1 153 ? -9.946  19.826  26.321  1.00 32.10 ? 148 MET C CG  1 
ATOM   4331 S  SD  . MET C 1 153 ? -9.550  18.589  27.560  1.00 34.91 ? 148 MET C SD  1 
ATOM   4332 C  CE  . MET C 1 153 ? -7.835  18.312  27.105  1.00 34.82 ? 148 MET C CE  1 
ATOM   4333 N  N   . THR C 1 154 ? -11.719 22.434  25.016  1.00 23.57 ? 149 THR C N   1 
ATOM   4334 C  CA  . THR C 1 154 ? -12.372 23.398  25.943  1.00 27.99 ? 149 THR C CA  1 
ATOM   4335 C  C   . THR C 1 154 ? -13.896 23.333  25.861  1.00 29.51 ? 149 THR C C   1 
ATOM   4336 O  O   . THR C 1 154 ? -14.530 23.230  26.922  1.00 35.04 ? 149 THR C O   1 
ATOM   4337 C  CB  . THR C 1 154 ? -11.959 24.834  25.625  1.00 29.62 ? 149 THR C CB  1 
ATOM   4338 O  OG1 . THR C 1 154 ? -10.522 24.868  25.632  1.00 35.15 ? 149 THR C OG1 1 
ATOM   4339 C  CG2 . THR C 1 154 ? -12.587 25.814  26.587  1.00 28.38 ? 149 THR C CG2 1 
ATOM   4340 N  N   . GLY C 1 155 ? -14.455 23.402  24.652  1.00 31.35 ? 150 GLY C N   1 
ATOM   4341 C  CA  . GLY C 1 155 ? -15.916 23.501  24.427  1.00 32.50 ? 150 GLY C CA  1 
ATOM   4342 C  C   . GLY C 1 155 ? -16.641 22.188  24.680  1.00 29.91 ? 150 GLY C C   1 
ATOM   4343 O  O   . GLY C 1 155 ? -17.872 22.168  24.596  1.00 35.98 ? 150 GLY C O   1 
ATOM   4344 N  N   . SER C 1 156 ? -15.909 21.115  24.983  1.00 27.91 ? 151 SER C N   1 
ATOM   4345 C  CA  . SER C 1 156 ? -16.470 19.771  25.247  1.00 24.69 ? 151 SER C CA  1 
ATOM   4346 C  C   . SER C 1 156 ? -16.295 19.376  26.707  1.00 23.41 ? 151 SER C C   1 
ATOM   4347 O  O   . SER C 1 156 ? -16.692 18.215  27.065  1.00 22.47 ? 151 SER C O   1 
ATOM   4348 C  CB  . SER C 1 156 ? -15.881 18.751  24.304  1.00 24.66 ? 151 SER C CB  1 
ATOM   4349 O  OG  . SER C 1 156 ? -16.199 19.077  22.967  1.00 24.32 ? 151 SER C OG  1 
ATOM   4350 N  N   . LEU C 1 157 ? -15.776 20.282  27.538  1.00 25.22 ? 152 LEU C N   1 
ATOM   4351 C  CA  . LEU C 1 157 ? -15.509 19.979  28.984  1.00 28.93 ? 152 LEU C CA  1 
ATOM   4352 C  C   . LEU C 1 157 ? -16.803 19.572  29.706  1.00 29.79 ? 152 LEU C C   1 
ATOM   4353 O  O   . LEU C 1 157 ? -16.784 18.565  30.478  1.00 31.53 ? 152 LEU C O   1 
ATOM   4354 C  CB  . LEU C 1 157 ? -14.802 21.168  29.641  1.00 33.53 ? 152 LEU C CB  1 
ATOM   4355 C  CG  . LEU C 1 157 ? -13.346 21.394  29.201  1.00 37.10 ? 152 LEU C CG  1 
ATOM   4356 C  CD1 . LEU C 1 157 ? -12.684 22.515  29.996  1.00 37.30 ? 152 LEU C CD1 1 
ATOM   4357 C  CD2 . LEU C 1 157 ? -12.519 20.127  29.317  1.00 35.73 ? 152 LEU C CD2 1 
ATOM   4358 N  N   . ASP C 1 158 ? -17.927 20.226  29.412  1.00 29.89 ? 153 ASP C N   1 
ATOM   4359 C  CA  . ASP C 1 158 ? -19.240 19.865  30.026  1.00 31.24 ? 153 ASP C CA  1 
ATOM   4360 C  C   . ASP C 1 158 ? -19.714 18.518  29.490  1.00 29.37 ? 153 ASP C C   1 
ATOM   4361 O  O   . ASP C 1 158 ? -20.234 17.711  30.272  1.00 28.44 ? 153 ASP C O   1 
ATOM   4362 C  CB  . ASP C 1 158 ? -20.301 20.927  29.753  1.00 32.13 ? 153 ASP C CB  1 
ATOM   4363 C  CG  . ASP C 1 158 ? -20.093 22.169  30.581  1.00 34.09 ? 153 ASP C CG  1 
ATOM   4364 O  OD1 . ASP C 1 158 ? -19.495 22.057  31.691  1.00 37.74 ? 153 ASP C OD1 1 
ATOM   4365 O  OD2 . ASP C 1 158 ? -20.549 23.209  30.131  1.00 34.29 ? 153 ASP C OD2 1 
ATOM   4366 N  N   . TYR C 1 159 ? -19.535 18.296  28.188  1.00 30.65 ? 154 TYR C N   1 
ATOM   4367 C  CA  . TYR C 1 159 ? -19.895 17.035  27.500  1.00 29.31 ? 154 TYR C CA  1 
ATOM   4368 C  C   . TYR C 1 159 ? -19.167 15.876  28.195  1.00 29.19 ? 154 TYR C C   1 
ATOM   4369 O  O   . TYR C 1 159 ? -19.846 14.872  28.553  1.00 26.58 ? 154 TYR C O   1 
ATOM   4370 C  CB  . TYR C 1 159 ? -19.583 17.135  26.003  1.00 30.70 ? 154 TYR C CB  1 
ATOM   4371 C  CG  . TYR C 1 159 ? -19.715 15.819  25.277  1.00 36.10 ? 154 TYR C CG  1 
ATOM   4372 C  CD1 . TYR C 1 159 ? -20.923 15.140  25.245  1.00 34.56 ? 154 TYR C CD1 1 
ATOM   4373 C  CD2 . TYR C 1 159 ? -18.635 15.246  24.624  1.00 34.66 ? 154 TYR C CD2 1 
ATOM   4374 C  CE1 . TYR C 1 159 ? -21.053 13.929  24.586  1.00 35.97 ? 154 TYR C CE1 1 
ATOM   4375 C  CE2 . TYR C 1 159 ? -18.759 14.048  23.943  1.00 32.50 ? 154 TYR C CE2 1 
ATOM   4376 C  CZ  . TYR C 1 159 ? -19.972 13.393  23.918  1.00 34.00 ? 154 TYR C CZ  1 
ATOM   4377 O  OH  . TYR C 1 159 ? -20.084 12.203  23.276  1.00 36.22 ? 154 TYR C OH  1 
ATOM   4378 N  N   . PHE C 1 160 ? -17.847 16.019  28.420  1.00 24.96 ? 155 PHE C N   1 
ATOM   4379 C  CA  . PHE C 1 160 ? -17.011 15.012  29.119  1.00 24.47 ? 155 PHE C CA  1 
ATOM   4380 C  C   . PHE C 1 160 ? -17.666 14.706  30.476  1.00 26.34 ? 155 PHE C C   1 
ATOM   4381 O  O   . PHE C 1 160 ? -17.633 13.522  30.963  1.00 22.03 ? 155 PHE C O   1 
ATOM   4382 C  CB  . PHE C 1 160 ? -15.571 15.489  29.390  1.00 23.21 ? 155 PHE C CB  1 
ATOM   4383 C  CG  . PHE C 1 160 ? -14.642 15.655  28.212  1.00 23.94 ? 155 PHE C CG  1 
ATOM   4384 C  CD1 . PHE C 1 160 ? -15.082 15.547  26.901  1.00 22.90 ? 155 PHE C CD1 1 
ATOM   4385 C  CD2 . PHE C 1 160 ? -13.303 15.947  28.426  1.00 26.36 ? 155 PHE C CD2 1 
ATOM   4386 C  CE1 . PHE C 1 160 ? -14.222 15.741  25.829  1.00 25.36 ? 155 PHE C CE1 1 
ATOM   4387 C  CE2 . PHE C 1 160 ? -12.432 16.123  27.354  1.00 29.02 ? 155 PHE C CE2 1 
ATOM   4388 C  CZ  . PHE C 1 160 ? -12.893 16.015  26.050  1.00 27.46 ? 155 PHE C CZ  1 
ATOM   4389 N  N   . ARG C 1 161 ? -18.171 15.750  31.133  1.00 26.16 ? 156 ARG C N   1 
ATOM   4390 C  CA  . ARG C 1 161 ? -18.660 15.592  32.520  1.00 35.41 ? 156 ARG C CA  1 
ATOM   4391 C  C   . ARG C 1 161 ? -19.956 14.768  32.480  1.00 34.34 ? 156 ARG C C   1 
ATOM   4392 O  O   . ARG C 1 161 ? -20.111 13.922  33.354  1.00 34.14 ? 156 ARG C O   1 
ATOM   4393 C  CB  . ARG C 1 161 ? -18.742 16.945  33.232  1.00 38.21 ? 156 ARG C CB  1 
ATOM   4394 C  CG  . ARG C 1 161 ? -17.387 17.648  33.284  1.00 46.79 ? 156 ARG C CG  1 
ATOM   4395 C  CD  . ARG C 1 161 ? -17.019 18.188  34.648  1.00 48.20 ? 156 ARG C CD  1 
ATOM   4396 N  NE  . ARG C 1 161 ? -17.917 19.251  35.077  1.00 44.80 ? 156 ARG C NE  1 
ATOM   4397 C  CZ  . ARG C 1 161 ? -18.781 19.210  36.101  1.00 53.85 ? 156 ARG C CZ  1 
ATOM   4398 N  NH1 . ARG C 1 161 ? -18.936 18.125  36.846  1.00 57.15 ? 156 ARG C NH1 1 
ATOM   4399 N  NH2 . ARG C 1 161 ? -19.510 20.280  36.375  1.00 52.02 ? 156 ARG C NH2 1 
ATOM   4400 N  N   . ARG C 1 162 ? -20.804 14.956  31.477  1.00 34.71 ? 157 ARG C N   1 
ATOM   4401 C  CA  . ARG C 1 162 ? -22.115 14.272  31.436  1.00 37.56 ? 157 ARG C CA  1 
ATOM   4402 C  C   . ARG C 1 162 ? -21.924 12.786  31.131  1.00 40.37 ? 157 ARG C C   1 
ATOM   4403 O  O   . ARG C 1 162 ? -22.681 11.974  31.706  1.00 39.78 ? 157 ARG C O   1 
ATOM   4404 C  CB  . ARG C 1 162 ? -23.036 14.880  30.386  1.00 37.13 ? 157 ARG C CB  1 
ATOM   4405 C  CG  . ARG C 1 162 ? -24.437 14.285  30.431  1.00 40.72 ? 157 ARG C CG  1 
ATOM   4406 C  CD  . ARG C 1 162 ? -25.291 14.753  31.601  1.00 40.42 ? 157 ARG C CD  1 
ATOM   4407 N  NE  . ARG C 1 162 ? -26.518 13.959  31.705  1.00 41.37 ? 157 ARG C NE  1 
ATOM   4408 C  CZ  . ARG C 1 162 ? -27.749 14.424  31.951  1.00 39.72 ? 157 ARG C CZ  1 
ATOM   4409 N  NH1 . ARG C 1 162 ? -27.955 15.720  32.113  1.00 39.31 ? 157 ARG C NH1 1 
ATOM   4410 N  NH2 . ARG C 1 162 ? -28.777 13.583  32.015  1.00 37.74 ? 157 ARG C NH2 1 
ATOM   4411 N  N   . ILE C 1 163 ? -20.988 12.444  30.234  1.00 39.96 ? 158 ILE C N   1 
ATOM   4412 C  CA  . ILE C 1 163 ? -20.786 11.046  29.758  1.00 35.37 ? 158 ILE C CA  1 
ATOM   4413 C  C   . ILE C 1 163 ? -19.865 10.324  30.736  1.00 36.37 ? 158 ILE C C   1 
ATOM   4414 O  O   . ILE C 1 163 ? -19.669 9.111   30.573  1.00 35.81 ? 158 ILE C O   1 
ATOM   4415 C  CB  . ILE C 1 163 ? -20.263 11.001  28.312  1.00 38.96 ? 158 ILE C CB  1 
ATOM   4416 C  CG1 . ILE C 1 163 ? -18.925 11.725  28.120  1.00 41.34 ? 158 ILE C CG1 1 
ATOM   4417 C  CG2 . ILE C 1 163 ? -21.314 11.538  27.371  1.00 35.84 ? 158 ILE C CG2 1 
ATOM   4418 C  CD1 . ILE C 1 163 ? -18.274 11.437  26.787  1.00 39.35 ? 158 ILE C CD1 1 
ATOM   4419 N  N   . LEU C 1 164 ? -19.383 11.023  31.761  1.00 30.73 ? 159 LEU C N   1 
ATOM   4420 C  CA  . LEU C 1 164 ? -18.397 10.474  32.717  1.00 33.15 ? 159 LEU C CA  1 
ATOM   4421 C  C   . LEU C 1 164 ? -18.896 9.204   33.426  1.00 34.83 ? 159 LEU C C   1 
ATOM   4422 O  O   . LEU C 1 164 ? -18.081 8.350   33.794  1.00 32.29 ? 159 LEU C O   1 
ATOM   4423 C  CB  . LEU C 1 164 ? -18.042 11.590  33.694  1.00 33.17 ? 159 LEU C CB  1 
ATOM   4424 C  CG  . LEU C 1 164 ? -16.745 11.408  34.466  1.00 36.19 ? 159 LEU C CG  1 
ATOM   4425 C  CD1 . LEU C 1 164 ? -15.543 11.548  33.550  1.00 37.13 ? 159 LEU C CD1 1 
ATOM   4426 C  CD2 . LEU C 1 164 ? -16.665 12.427  35.588  1.00 38.30 ? 159 LEU C CD2 1 
ATOM   4427 N  N   . PRO C 1 165 ? -20.209 9.001   33.700  1.00 34.42 ? 160 PRO C N   1 
ATOM   4428 C  CA  . PRO C 1 165 ? -20.649 7.782   34.386  1.00 35.42 ? 160 PRO C CA  1 
ATOM   4429 C  C   . PRO C 1 165 ? -20.265 6.466   33.680  1.00 31.74 ? 160 PRO C C   1 
ATOM   4430 O  O   . PRO C 1 165 ? -20.105 5.480   34.351  1.00 29.30 ? 160 PRO C O   1 
ATOM   4431 C  CB  . PRO C 1 165 ? -22.187 7.938   34.440  1.00 35.25 ? 160 PRO C CB  1 
ATOM   4432 C  CG  . PRO C 1 165 ? -22.397 9.423   34.439  1.00 34.16 ? 160 PRO C CG  1 
ATOM   4433 C  CD  . PRO C 1 165 ? -21.328 9.936   33.488  1.00 36.46 ? 160 PRO C CD  1 
ATOM   4434 N  N   . GLY C 1 166 ? -20.168 6.477   32.352  1.00 28.00 ? 161 GLY C N   1 
ATOM   4435 C  CA  . GLY C 1 166 ? -19.794 5.310   31.525  1.00 29.43 ? 161 GLY C CA  1 
ATOM   4436 C  C   . GLY C 1 166 ? -18.307 4.977   31.576  1.00 25.61 ? 161 GLY C C   1 
ATOM   4437 O  O   . GLY C 1 166 ? -17.959 3.914   31.116  1.00 23.55 ? 161 GLY C O   1 
ATOM   4438 N  N   . VAL C 1 167 ? -17.456 5.835   32.140  1.00 26.32 ? 162 VAL C N   1 
ATOM   4439 C  CA  . VAL C 1 167 ? -15.984 5.586   32.172  1.00 24.65 ? 162 VAL C CA  1 
ATOM   4440 C  C   . VAL C 1 167 ? -15.645 4.705   33.364  1.00 25.50 ? 162 VAL C C   1 
ATOM   4441 O  O   . VAL C 1 167 ? -15.958 5.101   34.486  1.00 27.21 ? 162 VAL C O   1 
ATOM   4442 C  CB  . VAL C 1 167 ? -15.203 6.900   32.283  1.00 24.44 ? 162 VAL C CB  1 
ATOM   4443 C  CG1 . VAL C 1 167 ? -13.711 6.659   32.313  1.00 25.51 ? 162 VAL C CG1 1 
ATOM   4444 C  CG2 . VAL C 1 167 ? -15.589 7.866   31.175  1.00 27.88 ? 162 VAL C CG2 1 
ATOM   4445 N  N   . GLY C 1 168 ? -14.876 3.637   33.139  1.00 26.74 ? 163 GLY C N   1 
ATOM   4446 C  CA  . GLY C 1 168 ? -14.117 2.960   34.198  1.00 24.05 ? 163 GLY C CA  1 
ATOM   4447 C  C   . GLY C 1 168 ? -12.665 3.401   34.127  1.00 25.60 ? 163 GLY C C   1 
ATOM   4448 O  O   . GLY C 1 168 ? -11.957 2.841   33.300  1.00 21.49 ? 163 GLY C O   1 
ATOM   4449 N  N   . ALA C 1 169 ? -12.235 4.358   34.966  1.00 25.36 ? 164 ALA C N   1 
ATOM   4450 C  CA  . ALA C 1 169 ? -10.833 4.845   35.011  1.00 23.43 ? 164 ALA C CA  1 
ATOM   4451 C  C   . ALA C 1 169 ? -10.050 4.040   36.039  1.00 26.27 ? 164 ALA C C   1 
ATOM   4452 O  O   . ALA C 1 169 ? -10.662 3.574   37.074  1.00 29.19 ? 164 ALA C O   1 
ATOM   4453 C  CB  . ALA C 1 169 ? -10.784 6.319   35.327  1.00 21.85 ? 164 ALA C CB  1 
ATOM   4454 N  N   . PHE C 1 170 ? -8.736  3.958   35.823  1.00 24.34 ? 165 PHE C N   1 
ATOM   4455 C  CA  . PHE C 1 170 ? -7.849  3.083   36.610  1.00 24.84 ? 165 PHE C CA  1 
ATOM   4456 C  C   . PHE C 1 170 ? -6.410  3.604   36.609  1.00 25.98 ? 165 PHE C C   1 
ATOM   4457 O  O   . PHE C 1 170 ? -6.015  4.464   35.809  1.00 26.88 ? 165 PHE C O   1 
ATOM   4458 C  CB  . PHE C 1 170 ? -7.962  1.637   36.118  1.00 25.46 ? 165 PHE C CB  1 
ATOM   4459 C  CG  . PHE C 1 170 ? -7.596  1.376   34.686  1.00 25.58 ? 165 PHE C CG  1 
ATOM   4460 C  CD1 . PHE C 1 170 ? -6.275  1.333   34.289  1.00 25.74 ? 165 PHE C CD1 1 
ATOM   4461 C  CD2 . PHE C 1 170 ? -8.570  1.107   33.754  1.00 26.03 ? 165 PHE C CD2 1 
ATOM   4462 C  CE1 . PHE C 1 170 ? -5.960  1.089   32.969  1.00 28.28 ? 165 PHE C CE1 1 
ATOM   4463 C  CE2 . PHE C 1 170 ? -8.240  0.780   32.455  1.00 24.53 ? 165 PHE C CE2 1 
ATOM   4464 C  CZ  . PHE C 1 170 ? -6.942  0.825   32.056  1.00 25.18 ? 165 PHE C CZ  1 
ATOM   4465 N  N   . ARG C 1 171 ? -5.653  3.084   37.566  1.00 26.20 ? 166 ARG C N   1 
ATOM   4466 C  CA  . ARG C 1 171 ? -4.234  3.394   37.813  1.00 26.69 ? 166 ARG C CA  1 
ATOM   4467 C  C   . ARG C 1 171 ? -3.541  2.052   37.818  1.00 29.26 ? 166 ARG C C   1 
ATOM   4468 O  O   . ARG C 1 171 ? -4.158  1.083   38.306  1.00 31.07 ? 166 ARG C O   1 
ATOM   4469 C  CB  . ARG C 1 171 ? -4.119  4.154   39.136  1.00 28.39 ? 166 ARG C CB  1 
ATOM   4470 C  CG  . ARG C 1 171 ? -4.865  5.485   39.156  1.00 26.95 ? 166 ARG C CG  1 
ATOM   4471 C  CD  . ARG C 1 171 ? -4.300  6.493   38.172  1.00 29.53 ? 166 ARG C CD  1 
ATOM   4472 N  NE  . ARG C 1 171 ? -4.858  7.855   38.237  1.00 30.29 ? 166 ARG C NE  1 
ATOM   4473 C  CZ  . ARG C 1 171 ? -5.903  8.296   37.517  1.00 33.88 ? 166 ARG C CZ  1 
ATOM   4474 N  NH1 . ARG C 1 171 ? -6.526  7.502   36.656  1.00 34.21 ? 166 ARG C NH1 1 
ATOM   4475 N  NH2 . ARG C 1 171 ? -6.331  9.539   37.661  1.00 34.67 ? 166 ARG C NH2 1 
ATOM   4476 N  N   . LEU C 1 172 ? -2.367  1.987   37.212  1.00 32.07 ? 167 LEU C N   1 
ATOM   4477 C  CA  . LEU C 1 172 ? -1.564  0.752   37.108  1.00 31.20 ? 167 LEU C CA  1 
ATOM   4478 C  C   . LEU C 1 172 ? -0.163  1.136   37.552  1.00 30.91 ? 167 LEU C C   1 
ATOM   4479 O  O   . LEU C 1 172 ? 0.550   1.836   36.797  1.00 31.43 ? 167 LEU C O   1 
ATOM   4480 C  CB  . LEU C 1 172 ? -1.593  0.223   35.672  1.00 29.08 ? 167 LEU C CB  1 
ATOM   4481 C  CG  . LEU C 1 172 ? -0.812  -1.065  35.433  1.00 29.63 ? 167 LEU C CG  1 
ATOM   4482 C  CD1 . LEU C 1 172 ? -1.208  -2.132  36.446  1.00 34.21 ? 167 LEU C CD1 1 
ATOM   4483 C  CD2 . LEU C 1 172 ? -1.062  -1.572  34.025  1.00 29.70 ? 167 LEU C CD2 1 
ATOM   4484 N  N   . ARG C 1 173 ? 0.154   0.779   38.783  1.00 30.36 ? 168 ARG C N   1 
ATOM   4485 C  CA  . ARG C 1 173 ? 1.502   0.932   39.361  1.00 35.36 ? 168 ARG C CA  1 
ATOM   4486 C  C   . ARG C 1 173 ? 2.362   -0.146  38.695  1.00 30.53 ? 168 ARG C C   1 
ATOM   4487 O  O   . ARG C 1 173 ? 2.098   -1.342  38.911  1.00 33.61 ? 168 ARG C O   1 
ATOM   4488 C  CB  . ARG C 1 173 ? 1.367   0.866   40.894  1.00 41.64 ? 168 ARG C CB  1 
ATOM   4489 C  CG  . ARG C 1 173 ? 2.673   0.761   41.664  1.00 52.45 ? 168 ARG C CG  1 
ATOM   4490 C  CD  . ARG C 1 173 ? 3.581   1.966   41.497  1.00 59.69 ? 168 ARG C CD  1 
ATOM   4491 N  NE  . ARG C 1 173 ? 4.570   2.029   42.568  1.00 68.64 ? 168 ARG C NE  1 
ATOM   4492 C  CZ  . ARG C 1 173 ? 5.606   1.193   42.722  1.00 75.50 ? 168 ARG C CZ  1 
ATOM   4493 N  NH1 . ARG C 1 173 ? 5.817   0.200   41.869  1.00 76.60 ? 168 ARG C NH1 1 
ATOM   4494 N  NH2 . ARG C 1 173 ? 6.434   1.357   43.742  1.00 75.86 ? 168 ARG C NH2 1 
ATOM   4495 N  N   . VAL C 1 174 ? 3.331   0.243   37.880  1.00 29.52 ? 169 VAL C N   1 
ATOM   4496 C  CA  . VAL C 1 174 ? 4.178   -0.750  37.169  1.00 31.00 ? 169 VAL C CA  1 
ATOM   4497 C  C   . VAL C 1 174 ? 5.135   -1.405  38.172  1.00 31.64 ? 169 VAL C C   1 
ATOM   4498 O  O   . VAL C 1 174 ? 6.085   -0.732  38.594  1.00 32.30 ? 169 VAL C O   1 
ATOM   4499 C  CB  . VAL C 1 174 ? 4.948   -0.141  35.990  1.00 31.41 ? 169 VAL C CB  1 
ATOM   4500 C  CG1 . VAL C 1 174 ? 5.772   -1.212  35.313  1.00 31.42 ? 169 VAL C CG1 1 
ATOM   4501 C  CG2 . VAL C 1 174 ? 4.036   0.567   34.995  1.00 30.25 ? 169 VAL C CG2 1 
ATOM   4502 N  N   . ALA C 1 175 ? 4.906   -2.691  38.472  1.00 31.81 ? 170 ALA C N   1 
ATOM   4503 C  CA  . ALA C 1 175 ? 5.764   -3.559  39.310  1.00 31.20 ? 170 ALA C CA  1 
ATOM   4504 C  C   . ALA C 1 175 ? 6.855   -4.180  38.449  1.00 33.21 ? 170 ALA C C   1 
ATOM   4505 O  O   . ALA C 1 175 ? 7.992   -4.236  38.915  1.00 32.19 ? 170 ALA C O   1 
ATOM   4506 C  CB  . ALA C 1 175 ? 4.934   -4.629  39.970  1.00 34.22 ? 170 ALA C CB  1 
ATOM   4507 N  N   . GLU C 1 176 ? 6.515   -4.576  37.217  1.00 33.71 ? 171 GLU C N   1 
ATOM   4508 C  CA  . GLU C 1 176 ? 7.429   -5.283  36.294  1.00 36.09 ? 171 GLU C CA  1 
ATOM   4509 C  C   . GLU C 1 176 ? 7.223   -4.768  34.857  1.00 32.85 ? 171 GLU C C   1 
ATOM   4510 O  O   . GLU C 1 176 ? 6.086   -4.543  34.437  1.00 25.43 ? 171 GLU C O   1 
ATOM   4511 C  CB  . GLU C 1 176 ? 7.179   -6.790  36.431  1.00 42.75 ? 171 GLU C CB  1 
ATOM   4512 C  CG  . GLU C 1 176 ? 8.349   -7.609  35.926  1.00 51.66 ? 171 GLU C CG  1 
ATOM   4513 C  CD  . GLU C 1 176 ? 8.240   -9.122  36.061  1.00 58.24 ? 171 GLU C CD  1 
ATOM   4514 O  OE1 . GLU C 1 176 ? 7.269   -9.605  36.717  1.00 55.60 ? 171 GLU C OE1 1 
ATOM   4515 O  OE2 . GLU C 1 176 ? 9.129   -9.813  35.490  1.00 62.34 ? 171 GLU C OE2 1 
ATOM   4516 N  N   . ALA C 1 177 ? 8.301   -4.590  34.109  1.00 28.68 ? 172 ALA C N   1 
ATOM   4517 C  CA  . ALA C 1 177 ? 8.237   -4.095  32.722  1.00 30.18 ? 172 ALA C CA  1 
ATOM   4518 C  C   . ALA C 1 177 ? 9.229   -4.889  31.880  1.00 32.04 ? 172 ALA C C   1 
ATOM   4519 O  O   . ALA C 1 177 ? 10.355  -5.110  32.352  1.00 32.39 ? 172 ALA C O   1 
ATOM   4520 C  CB  . ALA C 1 177 ? 8.536   -2.620  32.695  1.00 27.62 ? 172 ALA C CB  1 
ATOM   4521 N  N   . ASP C 1 178 ? 8.805   -5.334  30.704  1.00 30.97 ? 173 ASP C N   1 
ATOM   4522 C  CA  . ASP C 1 178 ? 9.631   -6.178  29.813  1.00 28.34 ? 173 ASP C CA  1 
ATOM   4523 C  C   . ASP C 1 178 ? 9.466   -5.636  28.398  1.00 27.89 ? 173 ASP C C   1 
ATOM   4524 O  O   . ASP C 1 178 ? 8.289   -5.349  27.985  1.00 23.46 ? 173 ASP C O   1 
ATOM   4525 C  CB  . ASP C 1 178 ? 9.229   -7.642  29.958  1.00 31.01 ? 173 ASP C CB  1 
ATOM   4526 C  CG  . ASP C 1 178 ? 9.471   -8.139  31.375  1.00 36.82 ? 173 ASP C CG  1 
ATOM   4527 O  OD1 . ASP C 1 178 ? 10.678  -8.328  31.723  1.00 35.87 ? 173 ASP C OD1 1 
ATOM   4528 O  OD2 . ASP C 1 178 ? 8.476   -8.269  32.140  1.00 31.91 ? 173 ASP C OD2 1 
ATOM   4529 N  N   . GLY C 1 179 ? 10.587  -5.499  27.693  1.00 27.00 ? 174 GLY C N   1 
ATOM   4530 C  CA  . GLY C 1 179 ? 10.636  -5.003  26.302  1.00 28.63 ? 174 GLY C CA  1 
ATOM   4531 C  C   . GLY C 1 179 ? 11.149  -6.063  25.347  1.00 27.66 ? 174 GLY C C   1 
ATOM   4532 O  O   . GLY C 1 179 ? 12.291  -6.497  25.558  1.00 25.89 ? 174 GLY C O   1 
ATOM   4533 N  N   . MET C 1 180 ? 10.339  -6.492  24.366  1.00 26.93 ? 175 MET C N   1 
ATOM   4534 C  CA  . MET C 1 180 ? 10.815  -7.316  23.222  1.00 26.70 ? 175 MET C CA  1 
ATOM   4535 C  C   . MET C 1 180 ? 11.136  -6.389  22.054  1.00 26.78 ? 175 MET C C   1 
ATOM   4536 O  O   . MET C 1 180 ? 10.200  -5.828  21.473  1.00 24.32 ? 175 MET C O   1 
ATOM   4537 C  CB  . MET C 1 180 ? 9.770   -8.325  22.760  1.00 29.16 ? 175 MET C CB  1 
ATOM   4538 C  CG  . MET C 1 180 ? 10.194  -9.099  21.536  1.00 31.04 ? 175 MET C CG  1 
ATOM   4539 S  SD  . MET C 1 180 ? 11.263  -10.510 21.922  1.00 33.39 ? 175 MET C SD  1 
ATOM   4540 C  CE  . MET C 1 180 ? 9.989   -11.597 22.582  1.00 29.46 ? 175 MET C CE  1 
ATOM   4541 N  N   . PHE C 1 181 ? 12.407  -6.241  21.703  1.00 25.52 ? 176 PHE C N   1 
ATOM   4542 C  CA  . PHE C 1 181 ? 12.819  -5.436  20.531  1.00 26.71 ? 176 PHE C CA  1 
ATOM   4543 C  C   . PHE C 1 181 ? 13.486  -6.364  19.514  1.00 27.04 ? 176 PHE C C   1 
ATOM   4544 O  O   . PHE C 1 181 ? 14.728  -6.435  19.459  1.00 25.20 ? 176 PHE C O   1 
ATOM   4545 C  CB  . PHE C 1 181 ? 13.694  -4.261  20.959  1.00 26.99 ? 176 PHE C CB  1 
ATOM   4546 C  CG  . PHE C 1 181 ? 12.918  -3.251  21.743  1.00 29.76 ? 176 PHE C CG  1 
ATOM   4547 C  CD1 . PHE C 1 181 ? 12.677  -3.443  23.092  1.00 30.52 ? 176 PHE C CD1 1 
ATOM   4548 C  CD2 . PHE C 1 181 ? 12.351  -2.155  21.108  1.00 32.16 ? 176 PHE C CD2 1 
ATOM   4549 C  CE1 . PHE C 1 181 ? 11.894  -2.539  23.794  1.00 33.03 ? 176 PHE C CE1 1 
ATOM   4550 C  CE2 . PHE C 1 181 ? 11.583  -1.249  21.817  1.00 30.68 ? 176 PHE C CE2 1 
ATOM   4551 C  CZ  . PHE C 1 181 ? 11.373  -1.435  23.159  1.00 31.71 ? 176 PHE C CZ  1 
ATOM   4552 N  N   . LYS C 1 182 ? 12.663  -7.055  18.736  1.00 23.80 ? 177 LYS C N   1 
ATOM   4553 C  CA  . LYS C 1 182 ? 13.134  -8.119  17.809  1.00 24.54 ? 177 LYS C CA  1 
ATOM   4554 C  C   . LYS C 1 182 ? 13.377  -7.466  16.443  1.00 23.17 ? 177 LYS C C   1 
ATOM   4555 O  O   . LYS C 1 182 ? 12.387  -7.150  15.744  1.00 19.56 ? 177 LYS C O   1 
ATOM   4556 C  CB  . LYS C 1 182 ? 12.130  -9.266  17.801  1.00 24.09 ? 177 LYS C CB  1 
ATOM   4557 C  CG  . LYS C 1 182 ? 12.497  -10.421 16.895  1.00 24.91 ? 177 LYS C CG  1 
ATOM   4558 C  CD  . LYS C 1 182 ? 11.582  -11.607 17.100  1.00 29.11 ? 177 LYS C CD  1 
ATOM   4559 C  CE  . LYS C 1 182 ? 11.624  -12.636 15.990  1.00 30.57 ? 177 LYS C CE  1 
ATOM   4560 N  NZ  . LYS C 1 182 ? 13.001  -12.802 15.447  1.00 35.64 ? 177 LYS C NZ  1 
ATOM   4561 N  N   . LEU C 1 183 ? 14.646  -7.143  16.170  1.00 21.56 ? 178 LEU C N   1 
ATOM   4562 C  CA  . LEU C 1 183 ? 15.088  -6.197  15.114  1.00 23.34 ? 178 LEU C CA  1 
ATOM   4563 C  C   . LEU C 1 183 ? 16.320  -6.758  14.386  1.00 24.97 ? 178 LEU C C   1 
ATOM   4564 O  O   . LEU C 1 183 ? 17.200  -5.957  14.078  1.00 26.85 ? 178 LEU C O   1 
ATOM   4565 C  CB  . LEU C 1 183 ? 15.432  -4.863  15.776  1.00 24.90 ? 178 LEU C CB  1 
ATOM   4566 C  CG  . LEU C 1 183 ? 14.266  -4.118  16.428  1.00 25.27 ? 178 LEU C CG  1 
ATOM   4567 C  CD1 . LEU C 1 183 ? 14.803  -2.896  17.162  1.00 26.95 ? 178 LEU C CD1 1 
ATOM   4568 C  CD2 . LEU C 1 183 ? 13.219  -3.707  15.393  1.00 23.73 ? 178 LEU C CD2 1 
ATOM   4569 N  N   . SER C 1 184 ? 16.366  -8.080  14.155  1.00 25.93 ? 179 SER C N   1 
ATOM   4570 C  CA  . SER C 1 184 ? 17.421  -8.838  13.428  1.00 27.15 ? 179 SER C CA  1 
ATOM   4571 C  C   . SER C 1 184 ? 18.762  -8.799  14.178  1.00 27.56 ? 179 SER C C   1 
ATOM   4572 O  O   . SER C 1 184 ? 19.804  -8.932  13.513  1.00 28.05 ? 179 SER C O   1 
ATOM   4573 C  CB  . SER C 1 184 ? 17.579  -8.347  11.989  1.00 29.17 ? 179 SER C CB  1 
ATOM   4574 O  OG  . SER C 1 184 ? 16.359  -8.481  11.261  1.00 28.24 ? 179 SER C OG  1 
ATOM   4575 N  N   . GLN C 1 185 ? 18.773  -8.698  15.510  1.00 27.46 ? 180 GLN C N   1 
ATOM   4576 C  CA  . GLN C 1 185 ? 20.055  -8.676  16.278  1.00 29.78 ? 180 GLN C CA  1 
ATOM   4577 C  C   . GLN C 1 185 ? 20.761  -10.037 16.146  1.00 31.00 ? 180 GLN C C   1 
ATOM   4578 O  O   . GLN C 1 185 ? 22.009  -10.086 16.217  1.00 31.01 ? 180 GLN C O   1 
ATOM   4579 C  CB  . GLN C 1 185 ? 19.855  -8.299  17.747  1.00 27.81 ? 180 GLN C CB  1 
ATOM   4580 C  CG  . GLN C 1 185 ? 19.392  -6.870  17.983  1.00 25.94 ? 180 GLN C CG  1 
ATOM   4581 C  CD  . GLN C 1 185 ? 17.883  -6.804  18.069  1.00 25.34 ? 180 GLN C CD  1 
ATOM   4582 O  OE1 . GLN C 1 185 ? 17.187  -7.485  17.329  1.00 26.09 ? 180 GLN C OE1 1 
ATOM   4583 N  NE2 . GLN C 1 185 ? 17.371  -5.984  18.965  1.00 22.84 ? 180 GLN C NE2 1 
ATOM   4584 N  N   . GLU C 1 186 ? 19.995  -11.095 15.894  1.00 33.16 ? 181 GLU C N   1 
ATOM   4585 C  CA  . GLU C 1 186 ? 20.490  -12.485 15.836  1.00 33.01 ? 181 GLU C CA  1 
ATOM   4586 C  C   . GLU C 1 186 ? 21.273  -12.698 14.533  1.00 34.66 ? 181 GLU C C   1 
ATOM   4587 O  O   . GLU C 1 186 ? 21.943  -13.723 14.430  1.00 31.19 ? 181 GLU C O   1 
ATOM   4588 C  CB  . GLU C 1 186 ? 19.291  -13.433 15.940  1.00 37.82 ? 181 GLU C CB  1 
ATOM   4589 C  CG  . GLU C 1 186 ? 18.513  -13.623 14.629  1.00 39.77 ? 181 GLU C CG  1 
ATOM   4590 C  CD  . GLU C 1 186 ? 17.391  -12.649 14.287  1.00 41.10 ? 181 GLU C CD  1 
ATOM   4591 O  OE1 . GLU C 1 186 ? 17.218  -11.658 15.025  1.00 40.38 ? 181 GLU C OE1 1 
ATOM   4592 O  OE2 . GLU C 1 186 ? 16.678  -12.900 13.286  1.00 39.33 ? 181 GLU C OE2 1 
ATOM   4593 N  N   . GLN C 1 187 ? 21.129  -11.811 13.541  1.00 32.63 ? 182 GLN C N   1 
ATOM   4594 C  CA  . GLN C 1 187 ? 21.743  -11.970 12.196  1.00 31.62 ? 182 GLN C CA  1 
ATOM   4595 C  C   . GLN C 1 187 ? 23.182  -11.442 12.268  1.00 29.93 ? 182 GLN C C   1 
ATOM   4596 O  O   . GLN C 1 187 ? 23.465  -10.616 13.148  1.00 27.68 ? 182 GLN C O   1 
ATOM   4597 C  CB  . GLN C 1 187 ? 20.925  -11.222 11.128  1.00 33.06 ? 182 GLN C CB  1 
ATOM   4598 C  CG  . GLN C 1 187 ? 19.524  -11.770 10.862  1.00 31.27 ? 182 GLN C CG  1 
ATOM   4599 C  CD  . GLN C 1 187 ? 19.527  -13.203 10.386  1.00 35.82 ? 182 GLN C CD  1 
ATOM   4600 O  OE1 . GLN C 1 187 ? 20.459  -13.644 9.722   1.00 35.14 ? 182 GLN C OE1 1 
ATOM   4601 N  NE2 . GLN C 1 187 ? 18.481  -13.948 10.731  1.00 41.75 ? 182 GLN C NE2 1 
ATOM   4602 N  N   . GLN C 1 188 ? 24.053  -11.890 11.371  1.00 30.67 ? 183 GLN C N   1 
ATOM   4603 C  CA  . GLN C 1 188 ? 25.390  -11.282 11.159  1.00 35.36 ? 183 GLN C CA  1 
ATOM   4604 C  C   . GLN C 1 188 ? 25.177  -9.835  10.705  1.00 39.55 ? 183 GLN C C   1 
ATOM   4605 O  O   . GLN C 1 188 ? 24.141  -9.513  10.113  1.00 36.98 ? 183 GLN C O   1 
ATOM   4606 C  CB  . GLN C 1 188 ? 26.184  -12.121 10.159  1.00 37.68 ? 183 GLN C CB  1 
ATOM   4607 C  CG  . GLN C 1 188 ? 26.697  -13.437 10.739  1.00 44.08 ? 183 GLN C CG  1 
ATOM   4608 C  CD  . GLN C 1 188 ? 27.994  -13.293 11.510  1.00 51.69 ? 183 GLN C CD  1 
ATOM   4609 O  OE1 . GLN C 1 188 ? 28.055  -12.667 12.571  1.00 54.61 ? 183 GLN C OE1 1 
ATOM   4610 N  NE2 . GLN C 1 188 ? 29.055  -13.890 10.987  1.00 55.09 ? 183 GLN C NE2 1 
ATOM   4611 N  N   . PRO C 1 189 ? 26.136  -8.916  10.963  1.00 38.92 ? 184 PRO C N   1 
ATOM   4612 C  CA  . PRO C 1 189 ? 25.911  -7.485  10.746  1.00 40.46 ? 184 PRO C CA  1 
ATOM   4613 C  C   . PRO C 1 189 ? 25.582  -7.098  9.289   1.00 40.17 ? 184 PRO C C   1 
ATOM   4614 O  O   . PRO C 1 189 ? 24.749  -6.217  9.083   1.00 35.20 ? 184 PRO C O   1 
ATOM   4615 C  CB  . PRO C 1 189 ? 27.235  -6.854  11.217  1.00 41.60 ? 184 PRO C CB  1 
ATOM   4616 C  CG  . PRO C 1 189 ? 27.816  -7.880  12.162  1.00 39.20 ? 184 PRO C CG  1 
ATOM   4617 C  CD  . PRO C 1 189 ? 27.480  -9.197  11.497  1.00 39.72 ? 184 PRO C CD  1 
ATOM   4618 N  N   . ALA C 1 190 ? 26.231  -7.752  8.325   1.00 38.69 ? 185 ALA C N   1 
ATOM   4619 C  CA  . ALA C 1 190 ? 25.997  -7.592  6.872   1.00 38.20 ? 185 ALA C CA  1 
ATOM   4620 C  C   . ALA C 1 190 ? 24.520  -7.862  6.528   1.00 35.77 ? 185 ALA C C   1 
ATOM   4621 O  O   . ALA C 1 190 ? 23.940  -7.088  5.748   1.00 36.49 ? 185 ALA C O   1 
ATOM   4622 C  CB  . ALA C 1 190 ? 26.912  -8.523  6.126   1.00 38.75 ? 185 ALA C CB  1 
ATOM   4623 N  N   . ILE C 1 191 ? 23.930  -8.902  7.109   1.00 31.23 ? 186 ILE C N   1 
ATOM   4624 C  CA  . ILE C 1 191 ? 22.529  -9.350  6.836   1.00 32.63 ? 186 ILE C CA  1 
ATOM   4625 C  C   . ILE C 1 191 ? 21.571  -8.360  7.501   1.00 29.93 ? 186 ILE C C   1 
ATOM   4626 O  O   . ILE C 1 191 ? 20.584  -7.977  6.840   1.00 32.31 ? 186 ILE C O   1 
ATOM   4627 C  CB  . ILE C 1 191 ? 22.262  -10.790 7.334   1.00 32.98 ? 186 ILE C CB  1 
ATOM   4628 C  CG1 . ILE C 1 191 ? 23.358  -11.775 6.921   1.00 34.71 ? 186 ILE C CG1 1 
ATOM   4629 C  CG2 . ILE C 1 191 ? 20.873  -11.263 6.920   1.00 28.84 ? 186 ILE C CG2 1 
ATOM   4630 C  CD1 . ILE C 1 191 ? 23.609  -11.819 5.448   1.00 37.47 ? 186 ILE C CD1 1 
ATOM   4631 N  N   . ARG C 1 192 ? 21.882  -7.947  8.734   1.00 30.15 ? 187 ARG C N   1 
ATOM   4632 C  CA  . ARG C 1 192 ? 21.135  -6.919  9.509   1.00 32.08 ? 187 ARG C CA  1 
ATOM   4633 C  C   . ARG C 1 192 ? 21.057  -5.636  8.684   1.00 32.76 ? 187 ARG C C   1 
ATOM   4634 O  O   . ARG C 1 192 ? 19.979  -5.007  8.674   1.00 27.77 ? 187 ARG C O   1 
ATOM   4635 C  CB  . ARG C 1 192 ? 21.798  -6.599  10.850  1.00 36.41 ? 187 ARG C CB  1 
ATOM   4636 C  CG  . ARG C 1 192 ? 21.867  -7.788  11.795  1.00 42.45 ? 187 ARG C CG  1 
ATOM   4637 C  CD  . ARG C 1 192 ? 22.880  -7.621  12.901  1.00 48.66 ? 187 ARG C CD  1 
ATOM   4638 N  NE  . ARG C 1 192 ? 22.462  -6.680  13.919  1.00 54.06 ? 187 ARG C NE  1 
ATOM   4639 C  CZ  . ARG C 1 192 ? 23.267  -6.168  14.846  1.00 62.17 ? 187 ARG C CZ  1 
ATOM   4640 N  NH1 . ARG C 1 192 ? 24.551  -6.498  14.872  1.00 59.80 ? 187 ARG C NH1 1 
ATOM   4641 N  NH2 . ARG C 1 192 ? 22.780  -5.319  15.738  1.00 62.89 ? 187 ARG C NH2 1 
ATOM   4642 N  N   . ARG C 1 193 ? 22.172  -5.253  8.053   1.00 32.90 ? 188 ARG C N   1 
ATOM   4643 C  CA  . ARG C 1 193 ? 22.248  -4.107  7.099   1.00 33.05 ? 188 ARG C CA  1 
ATOM   4644 C  C   . ARG C 1 193 ? 21.254  -4.322  5.947   1.00 28.34 ? 188 ARG C C   1 
ATOM   4645 O  O   . ARG C 1 193 ? 20.570  -3.373  5.563   1.00 24.98 ? 188 ARG C O   1 
ATOM   4646 C  CB  . ARG C 1 193 ? 23.665  -4.002  6.533   1.00 37.90 ? 188 ARG C CB  1 
ATOM   4647 C  CG  . ARG C 1 193 ? 24.221  -2.594  6.405   1.00 46.41 ? 188 ARG C CG  1 
ATOM   4648 C  CD  . ARG C 1 193 ? 25.639  -2.630  5.839   1.00 50.20 ? 188 ARG C CD  1 
ATOM   4649 N  NE  . ARG C 1 193 ? 26.053  -1.322  5.340   1.00 59.16 ? 188 ARG C NE  1 
ATOM   4650 C  CZ  . ARG C 1 193 ? 26.249  -0.980  4.060   1.00 63.82 ? 188 ARG C CZ  1 
ATOM   4651 N  NH1 . ARG C 1 193 ? 26.614  0.261   3.776   1.00 62.48 ? 188 ARG C NH1 1 
ATOM   4652 N  NH2 . ARG C 1 193 ? 26.094  -1.852  3.073   1.00 65.12 ? 188 ARG C NH2 1 
ATOM   4653 N  N   . ARG C 1 194 ? 21.213  -5.514  5.354   1.00 27.63 ? 189 ARG C N   1 
ATOM   4654 C  CA  . ARG C 1 194 ? 20.330  -5.748  4.182   1.00 28.43 ? 189 ARG C CA  1 
ATOM   4655 C  C   . ARG C 1 194 ? 18.862  -5.597  4.585   1.00 27.01 ? 189 ARG C C   1 
ATOM   4656 O  O   . ARG C 1 194 ? 18.098  -5.024  3.791   1.00 27.60 ? 189 ARG C O   1 
ATOM   4657 C  CB  . ARG C 1 194 ? 20.571  -7.113  3.559   1.00 29.10 ? 189 ARG C CB  1 
ATOM   4658 C  CG  . ARG C 1 194 ? 21.912  -7.214  2.868   1.00 27.00 ? 189 ARG C CG  1 
ATOM   4659 C  CD  . ARG C 1 194 ? 22.258  -8.673  2.703   1.00 28.48 ? 189 ARG C CD  1 
ATOM   4660 N  NE  . ARG C 1 194 ? 23.579  -8.750  2.116   1.00 28.14 ? 189 ARG C NE  1 
ATOM   4661 C  CZ  . ARG C 1 194 ? 24.226  -9.861  1.784   1.00 33.09 ? 189 ARG C CZ  1 
ATOM   4662 N  NH1 . ARG C 1 194 ? 23.679  -11.055 1.960   1.00 30.34 ? 189 ARG C NH1 1 
ATOM   4663 N  NH2 . ARG C 1 194 ? 25.441  -9.762  1.265   1.00 35.54 ? 189 ARG C NH2 1 
ATOM   4664 N  N   . VAL C 1 195 ? 18.482  -6.081  5.764   1.00 26.39 ? 190 VAL C N   1 
ATOM   4665 C  CA  . VAL C 1 195 ? 17.098  -5.961  6.289   1.00 24.38 ? 190 VAL C CA  1 
ATOM   4666 C  C   . VAL C 1 195 ? 16.804  -4.485  6.598   1.00 24.13 ? 190 VAL C C   1 
ATOM   4667 O  O   . VAL C 1 195 ? 15.666  -4.023  6.333   1.00 21.52 ? 190 VAL C O   1 
ATOM   4668 C  CB  . VAL C 1 195 ? 16.877  -6.898  7.493   1.00 25.80 ? 190 VAL C CB  1 
ATOM   4669 C  CG1 . VAL C 1 195 ? 15.511  -6.694  8.139   1.00 25.23 ? 190 VAL C CG1 1 
ATOM   4670 C  CG2 . VAL C 1 195 ? 17.055  -8.348  7.078   1.00 26.28 ? 190 VAL C CG2 1 
ATOM   4671 N  N   . ARG C 1 196 ? 17.765  -3.732  7.126   1.00 24.33 ? 191 ARG C N   1 
ATOM   4672 C  CA  . ARG C 1 196 ? 17.547  -2.300  7.462   1.00 24.38 ? 191 ARG C CA  1 
ATOM   4673 C  C   . ARG C 1 196 ? 17.398  -1.487  6.171   1.00 24.78 ? 191 ARG C C   1 
ATOM   4674 O  O   . ARG C 1 196 ? 16.505  -0.614  6.144   1.00 25.39 ? 191 ARG C O   1 
ATOM   4675 C  CB  . ARG C 1 196 ? 18.660  -1.752  8.362   1.00 26.66 ? 191 ARG C CB  1 
ATOM   4676 C  CG  . ARG C 1 196 ? 18.548  -0.268  8.693   1.00 27.93 ? 191 ARG C CG  1 
ATOM   4677 C  CD  . ARG C 1 196 ? 19.651  0.147   9.648   1.00 31.78 ? 191 ARG C CD  1 
ATOM   4678 N  NE  . ARG C 1 196 ? 20.990  -0.017  9.068   1.00 34.91 ? 191 ARG C NE  1 
ATOM   4679 C  CZ  . ARG C 1 196 ? 21.646  0.893   8.333   1.00 35.71 ? 191 ARG C CZ  1 
ATOM   4680 N  NH1 . ARG C 1 196 ? 21.113  2.071   8.064   1.00 36.68 ? 191 ARG C NH1 1 
ATOM   4681 N  NH2 . ARG C 1 196 ? 22.865  0.635   7.890   1.00 36.00 ? 191 ARG C NH2 1 
ATOM   4682 N  N   . HIS C 1 197 ? 18.224  -1.714  5.152   1.00 26.17 ? 192 HIS C N   1 
ATOM   4683 C  CA  . HIS C 1 197 ? 18.076  -1.055  3.816   1.00 28.23 ? 192 HIS C CA  1 
ATOM   4684 C  C   . HIS C 1 197 ? 16.750  -1.461  3.132   1.00 24.18 ? 192 HIS C C   1 
ATOM   4685 O  O   . HIS C 1 197 ? 16.065  -0.578  2.703   1.00 28.86 ? 192 HIS C O   1 
ATOM   4686 C  CB  . HIS C 1 197 ? 19.306  -1.272  2.931   1.00 29.72 ? 192 HIS C CB  1 
ATOM   4687 C  CG  . HIS C 1 197 ? 20.463  -0.466  3.400   1.00 30.72 ? 192 HIS C CG  1 
ATOM   4688 N  ND1 . HIS C 1 197 ? 20.284  0.775   3.993   1.00 32.28 ? 192 HIS C ND1 1 
ATOM   4689 C  CD2 . HIS C 1 197 ? 21.789  -0.723  3.422   1.00 30.03 ? 192 HIS C CD2 1 
ATOM   4690 C  CE1 . HIS C 1 197 ? 21.456  1.254   4.364   1.00 31.79 ? 192 HIS C CE1 1 
ATOM   4691 N  NE2 . HIS C 1 197 ? 22.391  0.345   4.044   1.00 33.84 ? 192 HIS C NE2 1 
ATOM   4692 N  N   . SER C 1 198 ? 16.356  -2.727  3.120   1.00 25.69 ? 193 SER C N   1 
ATOM   4693 C  CA  . SER C 1 198 ? 15.035  -3.192  2.603   1.00 27.42 ? 193 SER C CA  1 
ATOM   4694 C  C   . SER C 1 198 ? 13.916  -2.403  3.278   1.00 27.46 ? 193 SER C C   1 
ATOM   4695 O  O   . SER C 1 198 ? 13.115  -1.807  2.572   1.00 30.25 ? 193 SER C O   1 
ATOM   4696 C  CB  . SER C 1 198 ? 14.807  -4.670  2.779   1.00 27.48 ? 193 SER C CB  1 
ATOM   4697 O  OG  . SER C 1 198 ? 13.740  -5.145  1.943   1.00 29.69 ? 193 SER C OG  1 
ATOM   4698 N  N   . PHE C 1 199 ? 13.851  -2.416  4.598   1.00 23.73 ? 194 PHE C N   1 
ATOM   4699 C  CA  . PHE C 1 199 ? 12.716  -1.831  5.352   1.00 26.03 ? 194 PHE C CA  1 
ATOM   4700 C  C   . PHE C 1 199 ? 12.686  -0.316  5.113   1.00 25.27 ? 194 PHE C C   1 
ATOM   4701 O  O   . PHE C 1 199 ? 11.602  0.303   5.270   1.00 21.21 ? 194 PHE C O   1 
ATOM   4702 C  CB  . PHE C 1 199 ? 12.786  -2.257  6.830   1.00 24.55 ? 194 PHE C CB  1 
ATOM   4703 C  CG  . PHE C 1 199 ? 12.347  -3.671  7.099   1.00 25.43 ? 194 PHE C CG  1 
ATOM   4704 C  CD1 . PHE C 1 199 ? 11.402  -4.293  6.290   1.00 28.39 ? 194 PHE C CD1 1 
ATOM   4705 C  CD2 . PHE C 1 199 ? 12.801  -4.359  8.207   1.00 25.72 ? 194 PHE C CD2 1 
ATOM   4706 C  CE1 . PHE C 1 199 ? 10.985  -5.593  6.533   1.00 27.31 ? 194 PHE C CE1 1 
ATOM   4707 C  CE2 . PHE C 1 199 ? 12.388  -5.654  8.441   1.00 24.44 ? 194 PHE C CE2 1 
ATOM   4708 C  CZ  . PHE C 1 199 ? 11.471  -6.265  7.619   1.00 25.05 ? 194 PHE C CZ  1 
ATOM   4709 N  N   . GLY C 1 200 ? 13.840  0.255   4.718   1.00 23.44 ? 195 GLY C N   1 
ATOM   4710 C  CA  . GLY C 1 200 ? 14.002  1.691   4.439   1.00 24.50 ? 195 GLY C CA  1 
ATOM   4711 C  C   . GLY C 1 200 ? 13.309  2.121   3.145   1.00 25.60 ? 195 GLY C C   1 
ATOM   4712 O  O   . GLY C 1 200 ? 13.234  3.341   2.899   1.00 26.05 ? 195 GLY C O   1 
ATOM   4713 N  N   . GLY C 1 201 ? 12.873  1.165   2.314   1.00 26.16 ? 196 GLY C N   1 
ATOM   4714 C  CA  . GLY C 1 201 ? 12.437  1.378   0.922   1.00 25.88 ? 196 GLY C CA  1 
ATOM   4715 C  C   . GLY C 1 201 ? 10.924  1.457   0.763   1.00 24.57 ? 196 GLY C C   1 
ATOM   4716 O  O   . GLY C 1 201 ? 10.474  1.539   -0.419  1.00 24.37 ? 196 GLY C O   1 
ATOM   4717 N  N   . ALA C 1 202 ? 10.172  1.386   1.865   1.00 23.75 ? 197 ALA C N   1 
ATOM   4718 C  CA  . ALA C 1 202 ? 8.697   1.547   1.896   1.00 26.50 ? 197 ALA C CA  1 
ATOM   4719 C  C   . ALA C 1 202 ? 8.237   2.126   3.236   1.00 28.93 ? 197 ALA C C   1 
ATOM   4720 O  O   . ALA C 1 202 ? 8.808   1.782   4.317   1.00 25.40 ? 197 ALA C O   1 
ATOM   4721 C  CB  . ALA C 1 202 ? 7.986   0.240   1.613   1.00 28.47 ? 197 ALA C CB  1 
ATOM   4722 N  N   . GLU C 1 203 ? 7.190   2.955   3.182   1.00 29.30 ? 198 GLU C N   1 
ATOM   4723 C  CA  . GLU C 1 203 ? 6.693   3.702   4.372   1.00 30.90 ? 198 GLU C CA  1 
ATOM   4724 C  C   . GLU C 1 203 ? 6.210   2.686   5.426   1.00 28.18 ? 198 GLU C C   1 
ATOM   4725 O  O   . GLU C 1 203 ? 6.479   2.909   6.604   1.00 26.69 ? 198 GLU C O   1 
ATOM   4726 C  CB  . GLU C 1 203 ? 5.632   4.708   3.917   1.00 28.19 ? 198 GLU C CB  1 
ATOM   4727 C  CG  . GLU C 1 203 ? 5.130   5.624   5.003   1.00 33.11 ? 198 GLU C CG  1 
ATOM   4728 C  CD  . GLU C 1 203 ? 6.164   6.438   5.759   1.00 35.91 ? 198 GLU C CD  1 
ATOM   4729 O  OE1 . GLU C 1 203 ? 7.346   6.455   5.357   1.00 34.08 ? 198 GLU C OE1 1 
ATOM   4730 O  OE2 . GLU C 1 203 ? 5.774   7.024   6.779   1.00 39.64 ? 198 GLU C OE2 1 
ATOM   4731 N  N   . ALA C 1 204 ? 5.512   1.616   5.020   1.00 28.21 ? 199 ALA C N   1 
ATOM   4732 C  CA  . ALA C 1 204 ? 4.958   0.590   5.938   1.00 29.78 ? 199 ALA C CA  1 
ATOM   4733 C  C   . ALA C 1 204 ? 6.061   0.078   6.888   1.00 28.88 ? 199 ALA C C   1 
ATOM   4734 O  O   . ALA C 1 204 ? 5.765   -0.220  8.055   1.00 27.42 ? 199 ALA C O   1 
ATOM   4735 C  CB  . ALA C 1 204 ? 4.330   -0.537  5.151   1.00 31.82 ? 199 ALA C CB  1 
ATOM   4736 N  N   . THR C 1 205 ? 7.309   0.023   6.431   1.00 26.02 ? 200 THR C N   1 
ATOM   4737 C  CA  . THR C 1 205 ? 8.386   -0.675  7.166   1.00 25.93 ? 200 THR C CA  1 
ATOM   4738 C  C   . THR C 1 205 ? 9.444   0.321   7.683   1.00 24.31 ? 200 THR C C   1 
ATOM   4739 O  O   . THR C 1 205 ? 10.321  -0.121  8.401   1.00 24.49 ? 200 THR C O   1 
ATOM   4740 C  CB  . THR C 1 205 ? 8.943   -1.796  6.272   1.00 23.58 ? 200 THR C CB  1 
ATOM   4741 O  OG1 . THR C 1 205 ? 9.384   -1.177  5.065   1.00 21.80 ? 200 THR C OG1 1 
ATOM   4742 C  CG2 . THR C 1 205 ? 7.940   -2.876  5.931   1.00 21.24 ? 200 THR C CG2 1 
ATOM   4743 N  N   . ARG C 1 206 ? 9.289   1.620   7.426   1.00 25.16 ? 201 ARG C N   1 
ATOM   4744 C  CA  . ARG C 1 206 ? 10.326  2.631   7.703   1.00 27.67 ? 201 ARG C CA  1 
ATOM   4745 C  C   . ARG C 1 206 ? 10.534  2.802   9.222   1.00 26.53 ? 201 ARG C C   1 
ATOM   4746 O  O   . ARG C 1 206 ? 11.720  2.947   9.609   1.00 19.58 ? 201 ARG C O   1 
ATOM   4747 C  CB  . ARG C 1 206 ? 9.986   3.969   7.044   1.00 28.64 ? 201 ARG C CB  1 
ATOM   4748 C  CG  . ARG C 1 206 ? 10.925  5.083   7.500   1.00 30.78 ? 201 ARG C CG  1 
ATOM   4749 C  CD  . ARG C 1 206 ? 11.134  6.180   6.488   1.00 33.21 ? 201 ARG C CD  1 
ATOM   4750 N  NE  . ARG C 1 206 ? 9.952   6.997   6.460   1.00 36.84 ? 201 ARG C NE  1 
ATOM   4751 C  CZ  . ARG C 1 206 ? 9.674   7.971   7.327   1.00 46.04 ? 201 ARG C CZ  1 
ATOM   4752 N  NH1 . ARG C 1 206 ? 8.544   8.657   7.199   1.00 47.44 ? 201 ARG C NH1 1 
ATOM   4753 N  NH2 . ARG C 1 206 ? 10.520  8.257   8.309   1.00 47.85 ? 201 ARG C NH2 1 
ATOM   4754 N  N   . ALA C 1 207 ? 9.461   2.800   10.044  1.00 25.87 ? 202 ALA C N   1 
ATOM   4755 C  CA  . ALA C 1 207 ? 9.552   2.890   11.529  1.00 28.58 ? 202 ALA C CA  1 
ATOM   4756 C  C   . ALA C 1 207 ? 10.375  1.725   12.074  1.00 30.79 ? 202 ALA C C   1 
ATOM   4757 O  O   . ALA C 1 207 ? 11.102  1.972   13.033  1.00 34.09 ? 202 ALA C O   1 
ATOM   4758 C  CB  . ALA C 1 207 ? 8.190   2.907   12.171  1.00 32.93 ? 202 ALA C CB  1 
ATOM   4759 N  N   . VAL C 1 208 ? 10.283  0.516   11.486  1.00 28.79 ? 203 VAL C N   1 
ATOM   4760 C  CA  . VAL C 1 208 ? 11.138  -0.647  11.889  1.00 29.19 ? 203 VAL C CA  1 
ATOM   4761 C  C   . VAL C 1 208 ? 12.611  -0.358  11.538  1.00 24.03 ? 203 VAL C C   1 
ATOM   4762 O  O   . VAL C 1 208 ? 13.469  -0.632  12.353  1.00 24.08 ? 203 VAL C O   1 
ATOM   4763 C  CB  . VAL C 1 208 ? 10.678  -1.967  11.253  1.00 27.86 ? 203 VAL C CB  1 
ATOM   4764 C  CG1 . VAL C 1 208 ? 11.662  -3.070  11.590  1.00 31.68 ? 203 VAL C CG1 1 
ATOM   4765 C  CG2 . VAL C 1 208 ? 9.272   -2.327  11.715  1.00 28.35 ? 203 VAL C CG2 1 
ATOM   4766 N  N   . ALA C 1 209 ? 12.889  0.169   10.351  1.00 24.68 ? 204 ALA C N   1 
ATOM   4767 C  CA  . ALA C 1 209 ? 14.261  0.539   9.899   1.00 26.40 ? 204 ALA C CA  1 
ATOM   4768 C  C   . ALA C 1 209 ? 14.873  1.588   10.841  1.00 25.56 ? 204 ALA C C   1 
ATOM   4769 O  O   . ALA C 1 209 ? 16.103  1.490   11.118  1.00 25.79 ? 204 ALA C O   1 
ATOM   4770 C  CB  . ALA C 1 209 ? 14.198  1.034   8.472   1.00 25.78 ? 204 ALA C CB  1 
ATOM   4771 N  N   . GLY C 1 210 ? 14.053  2.541   11.310  1.00 27.30 ? 205 GLY C N   1 
ATOM   4772 C  CA  . GLY C 1 210 ? 14.380  3.610   12.289  1.00 27.53 ? 205 GLY C CA  1 
ATOM   4773 C  C   . GLY C 1 210 ? 14.981  3.047   13.581  1.00 29.54 ? 205 GLY C C   1 
ATOM   4774 O  O   . GLY C 1 210 ? 16.095  3.536   14.055  1.00 23.70 ? 205 GLY C O   1 
ATOM   4775 N  N   . LEU C 1 211 ? 14.306  2.052   14.153  1.00 27.16 ? 206 LEU C N   1 
ATOM   4776 C  CA  . LEU C 1 211 ? 14.757  1.385   15.400  1.00 26.10 ? 206 LEU C CA  1 
ATOM   4777 C  C   . LEU C 1 211 ? 16.020  0.579   15.074  1.00 26.46 ? 206 LEU C C   1 
ATOM   4778 O  O   . LEU C 1 211 ? 17.034  0.747   15.770  1.00 24.37 ? 206 LEU C O   1 
ATOM   4779 C  CB  . LEU C 1 211 ? 13.618  0.545   15.987  1.00 27.21 ? 206 LEU C CB  1 
ATOM   4780 C  CG  . LEU C 1 211 ? 12.356  1.312   16.391  1.00 27.21 ? 206 LEU C CG  1 
ATOM   4781 C  CD1 . LEU C 1 211 ? 11.177  0.383   16.498  1.00 27.23 ? 206 LEU C CD1 1 
ATOM   4782 C  CD2 . LEU C 1 211 ? 12.523  2.066   17.700  1.00 26.64 ? 206 LEU C CD2 1 
ATOM   4783 N  N   . MET C 1 212 ? 16.035  -0.162  13.965  1.00 25.20 ? 207 MET C N   1 
ATOM   4784 C  CA  . MET C 1 212 ? 17.231  -0.938  13.602  1.00 25.21 ? 207 MET C CA  1 
ATOM   4785 C  C   . MET C 1 212 ? 18.417  0.024   13.526  1.00 27.82 ? 207 MET C C   1 
ATOM   4786 O  O   . MET C 1 212 ? 19.496  -0.341  14.006  1.00 30.78 ? 207 MET C O   1 
ATOM   4787 C  CB  . MET C 1 212 ? 17.027  -1.695  12.289  1.00 24.93 ? 207 MET C CB  1 
ATOM   4788 C  CG  . MET C 1 212 ? 16.033  -2.842  12.435  1.00 23.02 ? 207 MET C CG  1 
ATOM   4789 S  SD  . MET C 1 212 ? 15.712  -3.664  10.878  1.00 22.49 ? 207 MET C SD  1 
ATOM   4790 C  CE  . MET C 1 212 ? 17.238  -4.602  10.737  1.00 23.14 ? 207 MET C CE  1 
ATOM   4791 N  N   . ASP C 1 213 ? 18.213  1.224   12.988  1.00 30.24 ? 208 ASP C N   1 
ATOM   4792 C  CA  . ASP C 1 213 ? 19.301  2.199   12.733  1.00 32.41 ? 208 ASP C CA  1 
ATOM   4793 C  C   . ASP C 1 213 ? 19.760  2.823   14.056  1.00 30.61 ? 208 ASP C C   1 
ATOM   4794 O  O   . ASP C 1 213 ? 20.920  3.182   14.122  1.00 34.78 ? 208 ASP C O   1 
ATOM   4795 C  CB  . ASP C 1 213 ? 18.898  3.262   11.703  1.00 37.63 ? 208 ASP C CB  1 
ATOM   4796 C  CG  . ASP C 1 213 ? 20.109  3.962   11.092  1.00 44.42 ? 208 ASP C CG  1 
ATOM   4797 O  OD1 . ASP C 1 213 ? 21.103  3.261   10.805  1.00 54.49 ? 208 ASP C OD1 1 
ATOM   4798 O  OD2 . ASP C 1 213 ? 20.078  5.204   10.948  1.00 49.00 ? 208 ASP C OD2 1 
ATOM   4799 N  N   . ARG C 1 214 ? 18.910  2.946   15.071  1.00 29.49 ? 209 ARG C N   1 
ATOM   4800 C  CA  . ARG C 1 214 ? 19.331  3.486   16.392  1.00 34.06 ? 209 ARG C CA  1 
ATOM   4801 C  C   . ARG C 1 214 ? 20.019  2.394   17.232  1.00 39.75 ? 209 ARG C C   1 
ATOM   4802 O  O   . ARG C 1 214 ? 20.461  2.741   18.353  1.00 43.77 ? 209 ARG C O   1 
ATOM   4803 C  CB  . ARG C 1 214 ? 18.135  4.105   17.125  1.00 37.61 ? 209 ARG C CB  1 
ATOM   4804 C  CG  . ARG C 1 214 ? 17.688  5.452   16.572  1.00 39.69 ? 209 ARG C CG  1 
ATOM   4805 C  CD  . ARG C 1 214 ? 16.335  5.918   17.094  1.00 42.81 ? 209 ARG C CD  1 
ATOM   4806 N  NE  . ARG C 1 214 ? 15.209  5.630   16.187  1.00 45.81 ? 209 ARG C NE  1 
ATOM   4807 C  CZ  . ARG C 1 214 ? 13.961  5.310   16.570  1.00 50.83 ? 209 ARG C CZ  1 
ATOM   4808 N  NH1 . ARG C 1 214 ? 13.642  5.236   17.854  1.00 60.64 ? 209 ARG C NH1 1 
ATOM   4809 N  NH2 . ARG C 1 214 ? 13.019  5.065   15.673  1.00 43.94 ? 209 ARG C NH2 1 
ATOM   4810 N  N   . LEU C 1 215 ? 20.088  1.131   16.771  1.00 35.53 ? 210 LEU C N   1 
ATOM   4811 C  CA  . LEU C 1 215 ? 20.704  0.029   17.562  1.00 39.68 ? 210 LEU C CA  1 
ATOM   4812 C  C   . LEU C 1 215 ? 22.221  0.224   17.594  1.00 45.50 ? 210 LEU C C   1 
ATOM   4813 O  O   . LEU C 1 215 ? 22.816  0.575   16.577  1.00 40.99 ? 210 LEU C O   1 
ATOM   4814 C  CB  . LEU C 1 215 ? 20.377  -1.339  16.950  1.00 39.86 ? 210 LEU C CB  1 
ATOM   4815 C  CG  . LEU C 1 215 ? 18.962  -1.877  17.170  1.00 37.20 ? 210 LEU C CG  1 
ATOM   4816 C  CD1 . LEU C 1 215 ? 18.762  -3.156  16.383  1.00 39.54 ? 210 LEU C CD1 1 
ATOM   4817 C  CD2 . LEU C 1 215 ? 18.681  -2.143  18.636  1.00 36.93 ? 210 LEU C CD2 1 
ATOM   4818 N  N   . PRO C 1 216 ? 22.903  -0.060  18.730  1.00 48.07 ? 211 PRO C N   1 
ATOM   4819 C  CA  . PRO C 1 216 ? 24.354  0.151   18.845  1.00 51.02 ? 211 PRO C CA  1 
ATOM   4820 C  C   . PRO C 1 216 ? 25.207  -0.636  17.837  1.00 48.60 ? 211 PRO C C   1 
ATOM   4821 O  O   . PRO C 1 216 ? 24.849  -1.780  17.568  1.00 51.01 ? 211 PRO C O   1 
ATOM   4822 C  CB  . PRO C 1 216 ? 24.685  -0.343  20.261  1.00 52.59 ? 211 PRO C CB  1 
ATOM   4823 C  CG  . PRO C 1 216 ? 23.532  -1.263  20.624  1.00 53.62 ? 211 PRO C CG  1 
ATOM   4824 C  CD  . PRO C 1 216 ? 22.326  -0.645  19.948  1.00 51.46 ? 211 PRO C CD  1 
ATOM   4825 N  N   . GLY D 1 4   ? 11.729  7.424   -34.518 1.00 48.71 ? -1  GLY D N   1 
ATOM   4826 C  CA  . GLY D 1 4   ? 10.649  6.415   -34.391 1.00 45.10 ? -1  GLY D CA  1 
ATOM   4827 C  C   . GLY D 1 4   ? 9.322   7.058   -34.025 1.00 42.96 ? -1  GLY D C   1 
ATOM   4828 O  O   . GLY D 1 4   ? 9.307   8.282   -33.800 1.00 47.20 ? -1  GLY D O   1 
ATOM   4829 N  N   . ALA D 1 5   ? 8.254   6.256   -33.939 1.00 39.56 ? 0   ALA D N   1 
ATOM   4830 C  CA  . ALA D 1 5   ? 6.887   6.673   -33.546 1.00 36.40 ? 0   ALA D CA  1 
ATOM   4831 C  C   . ALA D 1 5   ? 6.714   6.593   -32.019 1.00 35.96 ? 0   ALA D C   1 
ATOM   4832 O  O   . ALA D 1 5   ? 5.696   7.106   -31.517 1.00 34.69 ? 0   ALA D O   1 
ATOM   4833 C  CB  . ALA D 1 5   ? 5.872   5.815   -34.251 1.00 38.37 ? 0   ALA D CB  1 
ATOM   4834 N  N   . MET D 1 6   ? 7.654   5.955   -31.312 1.00 38.39 ? 1   MET D N   1 
ATOM   4835 C  CA  . MET D 1 6   ? 7.735   5.970   -29.828 1.00 38.03 ? 1   MET D CA  1 
ATOM   4836 C  C   . MET D 1 6   ? 9.061   6.601   -29.368 1.00 34.76 ? 1   MET D C   1 
ATOM   4837 O  O   . MET D 1 6   ? 10.142  6.193   -29.835 1.00 36.64 ? 1   MET D O   1 
ATOM   4838 C  CB  . MET D 1 6   ? 7.623   4.550   -29.280 1.00 41.34 ? 1   MET D CB  1 
ATOM   4839 C  CG  . MET D 1 6   ? 7.655   4.468   -27.761 1.00 41.09 ? 1   MET D CG  1 
ATOM   4840 S  SD  . MET D 1 6   ? 7.650   2.747   -27.189 1.00 42.79 ? 1   MET D SD  1 
ATOM   4841 C  CE  . MET D 1 6   ? 7.639   3.042   -25.422 1.00 43.00 ? 1   MET D CE  1 
ATOM   4842 N  N   . PHE D 1 7   ? 8.983   7.551   -28.448 1.00 33.15 ? 2   PHE D N   1 
ATOM   4843 C  CA  . PHE D 1 7   ? 10.172  8.213   -27.858 1.00 32.94 ? 2   PHE D CA  1 
ATOM   4844 C  C   . PHE D 1 7   ? 10.774  7.307   -26.777 1.00 30.99 ? 2   PHE D C   1 
ATOM   4845 O  O   . PHE D 1 7   ? 10.131  7.054   -25.731 1.00 28.33 ? 2   PHE D O   1 
ATOM   4846 C  CB  . PHE D 1 7   ? 9.780   9.573   -27.289 1.00 34.07 ? 2   PHE D CB  1 
ATOM   4847 C  CG  . PHE D 1 7   ? 10.958  10.354  -26.772 1.00 33.28 ? 2   PHE D CG  1 
ATOM   4848 C  CD1 . PHE D 1 7   ? 12.015  10.654  -27.609 1.00 35.47 ? 2   PHE D CD1 1 
ATOM   4849 C  CD2 . PHE D 1 7   ? 11.015  10.764  -25.454 1.00 32.82 ? 2   PHE D CD2 1 
ATOM   4850 C  CE1 . PHE D 1 7   ? 13.124  11.334  -27.132 1.00 37.82 ? 2   PHE D CE1 1 
ATOM   4851 C  CE2 . PHE D 1 7   ? 12.111  11.466  -24.986 1.00 34.42 ? 2   PHE D CE2 1 
ATOM   4852 C  CZ  . PHE D 1 7   ? 13.160  11.750  -25.824 1.00 37.43 ? 2   PHE D CZ  1 
ATOM   4853 N  N   . VAL D 1 8   ? 11.993  6.830   -26.993 1.00 28.57 ? 3   VAL D N   1 
ATOM   4854 C  CA  . VAL D 1 8   ? 12.688  5.972   -25.991 1.00 29.13 ? 3   VAL D CA  1 
ATOM   4855 C  C   . VAL D 1 8   ? 14.120  6.477   -25.911 1.00 33.33 ? 3   VAL D C   1 
ATOM   4856 O  O   . VAL D 1 8   ? 14.878  6.296   -26.868 1.00 33.51 ? 3   VAL D O   1 
ATOM   4857 C  CB  . VAL D 1 8   ? 12.606  4.478   -26.360 1.00 28.73 ? 3   VAL D CB  1 
ATOM   4858 C  CG1 . VAL D 1 8   ? 13.358  3.565   -25.384 1.00 26.67 ? 3   VAL D CG1 1 
ATOM   4859 C  CG2 . VAL D 1 8   ? 11.169  4.031   -26.504 1.00 28.16 ? 3   VAL D CG2 1 
ATOM   4860 N  N   . PRO D 1 9   ? 14.498  7.161   -24.803 1.00 33.22 ? 4   PRO D N   1 
ATOM   4861 C  CA  . PRO D 1 9   ? 15.853  7.684   -24.633 1.00 36.24 ? 4   PRO D CA  1 
ATOM   4862 C  C   . PRO D 1 9   ? 16.880  6.546   -24.686 1.00 37.14 ? 4   PRO D C   1 
ATOM   4863 O  O   . PRO D 1 9   ? 16.530  5.442   -24.306 1.00 35.26 ? 4   PRO D O   1 
ATOM   4864 C  CB  . PRO D 1 9   ? 15.840  8.348   -23.245 1.00 37.97 ? 4   PRO D CB  1 
ATOM   4865 C  CG  . PRO D 1 9   ? 14.367  8.634   -22.960 1.00 38.35 ? 4   PRO D CG  1 
ATOM   4866 C  CD  . PRO D 1 9   ? 13.605  7.545   -23.693 1.00 38.20 ? 4   PRO D CD  1 
ATOM   4867 N  N   . GLY D 1 10  ? 18.118  6.857   -25.087 1.00 39.96 ? 5   GLY D N   1 
ATOM   4868 C  CA  . GLY D 1 10  ? 19.203  5.889   -25.360 1.00 35.05 ? 5   GLY D CA  1 
ATOM   4869 C  C   . GLY D 1 10  ? 19.352  4.819   -24.276 1.00 34.03 ? 5   GLY D C   1 
ATOM   4870 O  O   . GLY D 1 10  ? 19.413  3.630   -24.585 1.00 38.16 ? 5   GLY D O   1 
ATOM   4871 N  N   . PRO D 1 11  ? 19.416  5.175   -22.973 1.00 32.00 ? 6   PRO D N   1 
ATOM   4872 C  CA  . PRO D 1 11  ? 19.671  4.173   -21.928 1.00 30.77 ? 6   PRO D CA  1 
ATOM   4873 C  C   . PRO D 1 11  ? 18.555  3.125   -21.699 1.00 31.66 ? 6   PRO D C   1 
ATOM   4874 O  O   . PRO D 1 11  ? 18.812  2.096   -21.093 1.00 32.37 ? 6   PRO D O   1 
ATOM   4875 C  CB  . PRO D 1 11  ? 19.866  5.018   -20.655 1.00 31.01 ? 6   PRO D CB  1 
ATOM   4876 C  CG  . PRO D 1 11  ? 19.966  6.468   -21.119 1.00 30.36 ? 6   PRO D CG  1 
ATOM   4877 C  CD  . PRO D 1 11  ? 19.254  6.538   -22.448 1.00 30.80 ? 6   PRO D CD  1 
ATOM   4878 N  N   . TYR D 1 12  ? 17.355  3.384   -22.216 1.00 29.28 ? 7   TYR D N   1 
ATOM   4879 C  CA  . TYR D 1 12  ? 16.111  2.624   -21.978 1.00 26.27 ? 7   TYR D CA  1 
ATOM   4880 C  C   . TYR D 1 12  ? 15.757  1.681   -23.125 1.00 29.56 ? 7   TYR D C   1 
ATOM   4881 O  O   . TYR D 1 12  ? 14.697  1.047   -23.052 1.00 29.40 ? 7   TYR D O   1 
ATOM   4882 C  CB  . TYR D 1 12  ? 15.014  3.644   -21.733 1.00 28.98 ? 7   TYR D CB  1 
ATOM   4883 C  CG  . TYR D 1 12  ? 15.299  4.496   -20.528 1.00 31.29 ? 7   TYR D CG  1 
ATOM   4884 C  CD1 . TYR D 1 12  ? 16.063  4.000   -19.475 1.00 30.78 ? 7   TYR D CD1 1 
ATOM   4885 C  CD2 . TYR D 1 12  ? 14.795  5.778   -20.426 1.00 30.25 ? 7   TYR D CD2 1 
ATOM   4886 C  CE1 . TYR D 1 12  ? 16.338  4.768   -18.366 1.00 30.74 ? 7   TYR D CE1 1 
ATOM   4887 C  CE2 . TYR D 1 12  ? 15.040  6.550   -19.303 1.00 31.98 ? 7   TYR D CE2 1 
ATOM   4888 C  CZ  . TYR D 1 12  ? 15.816  6.041   -18.277 1.00 29.75 ? 7   TYR D CZ  1 
ATOM   4889 O  OH  . TYR D 1 12  ? 16.044  6.769   -17.157 1.00 30.90 ? 7   TYR D OH  1 
ATOM   4890 N  N   . HIS D 1 13  ? 16.650  1.481   -24.092 1.00 32.52 ? 8   HIS D N   1 
ATOM   4891 C  CA  . HIS D 1 13  ? 16.483  0.465   -25.169 1.00 32.83 ? 8   HIS D CA  1 
ATOM   4892 C  C   . HIS D 1 13  ? 16.744  -0.916  -24.558 1.00 33.43 ? 8   HIS D C   1 
ATOM   4893 O  O   . HIS D 1 13  ? 17.631  -1.012  -23.705 1.00 36.99 ? 8   HIS D O   1 
ATOM   4894 C  CB  . HIS D 1 13  ? 17.368  0.818   -26.383 1.00 37.07 ? 8   HIS D CB  1 
ATOM   4895 C  CG  . HIS D 1 13  ? 16.897  2.018   -27.143 1.00 40.23 ? 8   HIS D CG  1 
ATOM   4896 N  ND1 . HIS D 1 13  ? 17.481  3.267   -26.997 1.00 46.93 ? 8   HIS D ND1 1 
ATOM   4897 C  CD2 . HIS D 1 13  ? 15.873  2.179   -28.018 1.00 45.08 ? 8   HIS D CD2 1 
ATOM   4898 C  CE1 . HIS D 1 13  ? 16.849  4.143   -27.760 1.00 46.10 ? 8   HIS D CE1 1 
ATOM   4899 N  NE2 . HIS D 1 13  ? 15.860  3.495   -28.402 1.00 47.25 ? 8   HIS D NE2 1 
ATOM   4900 N  N   . ALA D 1 14  ? 15.971  -1.942  -24.923 1.00 30.96 ? 9   ALA D N   1 
ATOM   4901 C  CA  . ALA D 1 14  ? 16.211  -3.335  -24.482 1.00 32.50 ? 9   ALA D CA  1 
ATOM   4902 C  C   . ALA D 1 14  ? 17.623  -3.768  -24.885 1.00 33.58 ? 9   ALA D C   1 
ATOM   4903 O  O   . ALA D 1 14  ? 18.132  -3.371  -25.923 1.00 32.84 ? 9   ALA D O   1 
ATOM   4904 C  CB  . ALA D 1 14  ? 15.179  -4.251  -25.068 1.00 32.49 ? 9   ALA D CB  1 
ATOM   4905 N  N   . PRO D 1 15  ? 18.309  -4.609  -24.086 1.00 37.79 ? 10  PRO D N   1 
ATOM   4906 C  CA  . PRO D 1 15  ? 19.544  -5.251  -24.539 1.00 40.27 ? 10  PRO D CA  1 
ATOM   4907 C  C   . PRO D 1 15  ? 19.439  -5.964  -25.897 1.00 41.71 ? 10  PRO D C   1 
ATOM   4908 O  O   . PRO D 1 15  ? 20.378  -5.916  -26.656 1.00 43.34 ? 10  PRO D O   1 
ATOM   4909 C  CB  . PRO D 1 15  ? 19.779  -6.314  -23.459 1.00 39.91 ? 10  PRO D CB  1 
ATOM   4910 C  CG  . PRO D 1 15  ? 19.156  -5.731  -22.222 1.00 40.15 ? 10  PRO D CG  1 
ATOM   4911 C  CD  . PRO D 1 15  ? 17.933  -4.988  -22.716 1.00 39.20 ? 10  PRO D CD  1 
ATOM   4912 N  N   . GLU D 1 16  ? 18.312  -6.644  -26.140 1.00 43.02 ? 11  GLU D N   1 
ATOM   4913 C  CA  . GLU D 1 16  ? 18.077  -7.520  -27.315 1.00 43.86 ? 11  GLU D CA  1 
ATOM   4914 C  C   . GLU D 1 16  ? 16.624  -7.384  -27.773 1.00 40.43 ? 11  GLU D C   1 
ATOM   4915 O  O   . GLU D 1 16  ? 15.746  -7.116  -26.929 1.00 32.27 ? 11  GLU D O   1 
ATOM   4916 C  CB  . GLU D 1 16  ? 18.395  -8.975  -26.967 1.00 51.82 ? 11  GLU D CB  1 
ATOM   4917 C  CG  . GLU D 1 16  ? 19.888  -9.252  -26.933 1.00 62.58 ? 11  GLU D CG  1 
ATOM   4918 C  CD  . GLU D 1 16  ? 20.267  -10.644 -26.463 1.00 74.08 ? 11  GLU D CD  1 
ATOM   4919 O  OE1 . GLU D 1 16  ? 19.464  -11.584 -26.691 1.00 82.51 ? 11  GLU D OE1 1 
ATOM   4920 O  OE2 . GLU D 1 16  ? 21.364  -10.786 -25.864 1.00 82.59 ? 11  GLU D OE2 1 
ATOM   4921 N  N   . ASP D 1 17  ? 16.400  -7.581  -29.069 1.00 34.57 ? 12  ASP D N   1 
ATOM   4922 C  CA  . ASP D 1 17  ? 15.063  -7.543  -29.698 1.00 38.41 ? 12  ASP D CA  1 
ATOM   4923 C  C   . ASP D 1 17  ? 14.133  -8.496  -28.943 1.00 34.08 ? 12  ASP D C   1 
ATOM   4924 O  O   . ASP D 1 17  ? 12.953  -8.146  -28.816 1.00 30.25 ? 12  ASP D O   1 
ATOM   4925 C  CB  . ASP D 1 17  ? 15.153  -7.888  -31.182 1.00 42.98 ? 12  ASP D CB  1 
ATOM   4926 C  CG  . ASP D 1 17  ? 15.875  -6.818  -31.977 1.00 47.84 ? 12  ASP D CG  1 
ATOM   4927 O  OD1 . ASP D 1 17  ? 15.538  -5.641  -31.790 1.00 49.28 ? 12  ASP D OD1 1 
ATOM   4928 O  OD2 . ASP D 1 17  ? 16.776  -7.174  -32.749 1.00 55.86 ? 12  ASP D OD2 1 
ATOM   4929 N  N   . ARG D 1 18  ? 14.665  -9.624  -28.457 1.00 32.18 ? 13  ARG D N   1 
ATOM   4930 C  CA  . ARG D 1 18  ? 13.899  -10.734 -27.829 1.00 34.86 ? 13  ARG D CA  1 
ATOM   4931 C  C   . ARG D 1 18  ? 13.114  -10.233 -26.606 1.00 30.27 ? 13  ARG D C   1 
ATOM   4932 O  O   . ARG D 1 18  ? 12.072  -10.835 -26.314 1.00 27.20 ? 13  ARG D O   1 
ATOM   4933 C  CB  . ARG D 1 18  ? 14.828  -11.885 -27.432 1.00 40.21 ? 13  ARG D CB  1 
ATOM   4934 C  CG  . ARG D 1 18  ? 14.183  -12.925 -26.521 1.00 45.98 ? 13  ARG D CG  1 
ATOM   4935 C  CD  . ARG D 1 18  ? 13.191  -13.851 -27.213 1.00 50.85 ? 13  ARG D CD  1 
ATOM   4936 N  NE  . ARG D 1 18  ? 13.943  -14.962 -27.787 1.00 62.29 ? 13  ARG D NE  1 
ATOM   4937 C  CZ  . ARG D 1 18  ? 13.479  -16.188 -28.031 1.00 62.60 ? 13  ARG D CZ  1 
ATOM   4938 N  NH1 . ARG D 1 18  ? 12.223  -16.510 -27.762 1.00 64.33 ? 13  ARG D NH1 1 
ATOM   4939 N  NH2 . ARG D 1 18  ? 14.291  -17.091 -28.557 1.00 62.11 ? 13  ARG D NH2 1 
ATOM   4940 N  N   . TRP D 1 19  ? 13.613  -9.210  -25.902 1.00 28.63 ? 14  TRP D N   1 
ATOM   4941 C  CA  . TRP D 1 19  ? 12.973  -8.646  -24.686 1.00 27.55 ? 14  TRP D CA  1 
ATOM   4942 C  C   . TRP D 1 19  ? 11.584  -8.128  -25.058 1.00 28.26 ? 14  TRP D C   1 
ATOM   4943 O  O   . TRP D 1 19  ? 10.695  -8.199  -24.200 1.00 27.92 ? 14  TRP D O   1 
ATOM   4944 C  CB  . TRP D 1 19  ? 13.823  -7.544  -24.054 1.00 29.41 ? 14  TRP D CB  1 
ATOM   4945 C  CG  . TRP D 1 19  ? 14.971  -8.038  -23.229 1.00 31.17 ? 14  TRP D CG  1 
ATOM   4946 C  CD1 . TRP D 1 19  ? 15.863  -9.020  -23.559 1.00 34.07 ? 14  TRP D CD1 1 
ATOM   4947 C  CD2 . TRP D 1 19  ? 15.378  -7.541  -21.945 1.00 30.84 ? 14  TRP D CD2 1 
ATOM   4948 N  NE1 . TRP D 1 19  ? 16.783  -9.181  -22.556 1.00 35.38 ? 14  TRP D NE1 1 
ATOM   4949 C  CE2 . TRP D 1 19  ? 16.512  -8.287  -21.554 1.00 34.27 ? 14  TRP D CE2 1 
ATOM   4950 C  CE3 . TRP D 1 19  ? 14.890  -6.551  -21.084 1.00 32.80 ? 14  TRP D CE3 1 
ATOM   4951 C  CZ2 . TRP D 1 19  ? 17.158  -8.071  -20.336 1.00 33.69 ? 14  TRP D CZ2 1 
ATOM   4952 C  CZ3 . TRP D 1 19  ? 15.525  -6.340  -19.876 1.00 32.63 ? 14  TRP D CZ3 1 
ATOM   4953 C  CH2 . TRP D 1 19  ? 16.654  -7.079  -19.520 1.00 32.61 ? 14  TRP D CH2 1 
ATOM   4954 N  N   . LEU D 1 20  ? 11.432  -7.596  -26.275 1.00 28.14 ? 15  LEU D N   1 
ATOM   4955 C  CA  . LEU D 1 20  ? 10.166  -6.991  -26.738 1.00 27.21 ? 15  LEU D CA  1 
ATOM   4956 C  C   . LEU D 1 20  ? 9.148   -8.122  -26.957 1.00 28.41 ? 15  LEU D C   1 
ATOM   4957 O  O   . LEU D 1 20  ? 8.015   -7.992  -26.474 1.00 26.47 ? 15  LEU D O   1 
ATOM   4958 C  CB  . LEU D 1 20  ? 10.420  -6.170  -28.001 1.00 27.41 ? 15  LEU D CB  1 
ATOM   4959 C  CG  . LEU D 1 20  ? 11.020  -4.778  -27.784 1.00 25.11 ? 15  LEU D CG  1 
ATOM   4960 C  CD1 . LEU D 1 20  ? 12.535  -4.825  -27.758 1.00 26.08 ? 15  LEU D CD1 1 
ATOM   4961 C  CD2 . LEU D 1 20  ? 10.547  -3.816  -28.858 1.00 23.88 ? 15  LEU D CD2 1 
ATOM   4962 N  N   . VAL D 1 21  ? 9.576   -9.216  -27.598 1.00 29.33 ? 16  VAL D N   1 
ATOM   4963 C  CA  . VAL D 1 21  ? 8.745   -10.436 -27.836 1.00 27.22 ? 16  VAL D CA  1 
ATOM   4964 C  C   . VAL D 1 21  ? 8.335   -11.006 -26.478 1.00 26.24 ? 16  VAL D C   1 
ATOM   4965 O  O   . VAL D 1 21  ? 7.132   -11.314 -26.292 1.00 22.67 ? 16  VAL D O   1 
ATOM   4966 C  CB  . VAL D 1 21  ? 9.493   -11.483 -28.682 1.00 28.30 ? 16  VAL D CB  1 
ATOM   4967 C  CG1 . VAL D 1 21  ? 8.647   -12.730 -28.890 1.00 28.65 ? 16  VAL D CG1 1 
ATOM   4968 C  CG2 . VAL D 1 21  ? 9.956   -10.921 -30.019 1.00 28.37 ? 16  VAL D CG2 1 
ATOM   4969 N  N   . ASP D 1 22  ? 9.288   -11.095 -25.547 1.00 25.95 ? 17  ASP D N   1 
ATOM   4970 C  CA  . ASP D 1 22  ? 9.035   -11.614 -24.175 1.00 28.32 ? 17  ASP D CA  1 
ATOM   4971 C  C   . ASP D 1 22  ? 7.890   -10.816 -23.539 1.00 27.09 ? 17  ASP D C   1 
ATOM   4972 O  O   . ASP D 1 22  ? 6.984   -11.469 -22.993 1.00 25.42 ? 17  ASP D O   1 
ATOM   4973 C  CB  . ASP D 1 22  ? 10.281  -11.574 -23.281 1.00 31.27 ? 17  ASP D CB  1 
ATOM   4974 C  CG  . ASP D 1 22  ? 11.381  -12.575 -23.616 1.00 32.78 ? 17  ASP D CG  1 
ATOM   4975 O  OD1 . ASP D 1 22  ? 11.124  -13.522 -24.394 1.00 30.19 ? 17  ASP D OD1 1 
ATOM   4976 O  OD2 . ASP D 1 22  ? 12.516  -12.377 -23.110 1.00 37.20 ? 17  ASP D OD2 1 
ATOM   4977 N  N   . LEU D 1 23  ? 7.925   -9.471  -23.602 1.00 25.14 ? 18  LEU D N   1 
ATOM   4978 C  CA  . LEU D 1 23  ? 6.938   -8.617  -22.878 1.00 25.82 ? 18  LEU D CA  1 
ATOM   4979 C  C   . LEU D 1 23  ? 5.557   -8.825  -23.510 1.00 24.27 ? 18  LEU D C   1 
ATOM   4980 O  O   . LEU D 1 23  ? 4.579   -8.975  -22.764 1.00 22.36 ? 18  LEU D O   1 
ATOM   4981 C  CB  . LEU D 1 23  ? 7.362   -7.139  -22.897 1.00 26.65 ? 18  LEU D CB  1 
ATOM   4982 C  CG  . LEU D 1 23  ? 6.573   -6.212  -21.966 1.00 28.44 ? 18  LEU D CG  1 
ATOM   4983 C  CD1 . LEU D 1 23  ? 7.241   -4.859  -21.834 1.00 30.98 ? 18  LEU D CD1 1 
ATOM   4984 C  CD2 . LEU D 1 23  ? 5.134   -6.000  -22.447 1.00 31.27 ? 18  LEU D CD2 1 
ATOM   4985 N  N   . VAL D 1 24  ? 5.491   -8.928  -24.835 1.00 24.02 ? 19  VAL D N   1 
ATOM   4986 C  CA  . VAL D 1 24  ? 4.220   -9.200  -25.571 1.00 23.81 ? 19  VAL D CA  1 
ATOM   4987 C  C   . VAL D 1 24  ? 3.630   -10.544 -25.108 1.00 25.45 ? 19  VAL D C   1 
ATOM   4988 O  O   . VAL D 1 24  ? 2.365   -10.612 -24.909 1.00 22.69 ? 19  VAL D O   1 
ATOM   4989 C  CB  . VAL D 1 24  ? 4.439   -9.141  -27.099 1.00 23.75 ? 19  VAL D CB  1 
ATOM   4990 C  CG1 . VAL D 1 24  ? 3.378   -9.885  -27.875 1.00 23.13 ? 19  VAL D CG1 1 
ATOM   4991 C  CG2 . VAL D 1 24  ? 4.541   -7.708  -27.580 1.00 22.70 ? 19  VAL D CG2 1 
ATOM   4992 N  N   . ARG D 1 25  ? 4.463   -11.574 -24.938 1.00 23.06 ? 20  ARG D N   1 
ATOM   4993 C  CA  . ARG D 1 25  ? 3.998   -12.899 -24.449 1.00 25.58 ? 20  ARG D CA  1 
ATOM   4994 C  C   . ARG D 1 25  ? 3.560   -12.804 -22.979 1.00 24.69 ? 20  ARG D C   1 
ATOM   4995 O  O   . ARG D 1 25  ? 2.540   -13.411 -22.638 1.00 24.86 ? 20  ARG D O   1 
ATOM   4996 C  CB  . ARG D 1 25  ? 5.073   -13.980 -24.631 1.00 28.26 ? 20  ARG D CB  1 
ATOM   4997 C  CG  . ARG D 1 25  ? 5.363   -14.328 -26.088 1.00 31.43 ? 20  ARG D CG  1 
ATOM   4998 C  CD  . ARG D 1 25  ? 6.283   -15.533 -26.126 1.00 35.82 ? 20  ARG D CD  1 
ATOM   4999 N  NE  . ARG D 1 25  ? 6.976   -15.716 -27.385 1.00 34.97 ? 20  ARG D NE  1 
ATOM   5000 C  CZ  . ARG D 1 25  ? 6.481   -16.332 -28.447 1.00 37.04 ? 20  ARG D CZ  1 
ATOM   5001 N  NH1 . ARG D 1 25  ? 5.252   -16.810 -28.416 1.00 37.24 ? 20  ARG D NH1 1 
ATOM   5002 N  NH2 . ARG D 1 25  ? 7.211   -16.453 -29.545 1.00 35.74 ? 20  ARG D NH2 1 
ATOM   5003 N  N   . GLY D 1 26  ? 4.304   -12.077 -22.146 1.00 24.18 ? 21  GLY D N   1 
ATOM   5004 C  CA  . GLY D 1 26  ? 4.025   -11.919 -20.703 1.00 25.63 ? 21  GLY D CA  1 
ATOM   5005 C  C   . GLY D 1 26  ? 2.779   -11.092 -20.407 1.00 22.81 ? 21  GLY D C   1 
ATOM   5006 O  O   . GLY D 1 26  ? 2.243   -11.247 -19.311 1.00 23.10 ? 21  GLY D O   1 
ATOM   5007 N  N   . HIS D 1 27  ? 2.368   -10.194 -21.302 1.00 23.89 ? 22  HIS D N   1 
ATOM   5008 C  CA  . HIS D 1 27  ? 1.328   -9.148  -21.035 1.00 24.38 ? 22  HIS D CA  1 
ATOM   5009 C  C   . HIS D 1 27  ? 0.440   -8.997  -22.263 1.00 22.11 ? 22  HIS D C   1 
ATOM   5010 O  O   . HIS D 1 27  ? 0.368   -7.966  -22.919 1.00 21.67 ? 22  HIS D O   1 
ATOM   5011 C  CB  . HIS D 1 27  ? 2.022   -7.880  -20.554 1.00 22.85 ? 22  HIS D CB  1 
ATOM   5012 C  CG  . HIS D 1 27  ? 3.055   -8.191  -19.534 1.00 20.87 ? 22  HIS D CG  1 
ATOM   5013 N  ND1 . HIS D 1 27  ? 2.749   -8.287  -18.189 1.00 20.56 ? 22  HIS D ND1 1 
ATOM   5014 C  CD2 . HIS D 1 27  ? 4.373   -8.450  -19.643 1.00 21.05 ? 22  HIS D CD2 1 
ATOM   5015 C  CE1 . HIS D 1 27  ? 3.842   -8.576  -17.518 1.00 21.44 ? 22  HIS D CE1 1 
ATOM   5016 N  NE2 . HIS D 1 27  ? 4.846   -8.681  -18.377 1.00 20.05 ? 22  HIS D NE2 1 
ATOM   5017 N  N   . PRO D 1 28  ? -0.285  -10.071 -22.593 1.00 21.21 ? 23  PRO D N   1 
ATOM   5018 C  CA  . PRO D 1 28  ? -1.022  -10.149 -23.846 1.00 22.67 ? 23  PRO D CA  1 
ATOM   5019 C  C   . PRO D 1 28  ? -2.227  -9.207  -23.913 1.00 20.95 ? 23  PRO D C   1 
ATOM   5020 O  O   . PRO D 1 28  ? -2.754  -9.059  -25.017 1.00 21.95 ? 23  PRO D O   1 
ATOM   5021 C  CB  . PRO D 1 28  ? -1.547  -11.577 -23.896 1.00 21.92 ? 23  PRO D CB  1 
ATOM   5022 C  CG  . PRO D 1 28  ? -1.487  -12.074 -22.482 1.00 20.87 ? 23  PRO D CG  1 
ATOM   5023 C  CD  . PRO D 1 28  ? -0.462  -11.245 -21.749 1.00 20.61 ? 23  PRO D CD  1 
ATOM   5024 N  N   . LEU D 1 29  ? -2.619  -8.625  -22.776 1.00 18.91 ? 24  LEU D N   1 
ATOM   5025 C  CA  . LEU D 1 29  ? -3.812  -7.725  -22.701 1.00 19.08 ? 24  LEU D CA  1 
ATOM   5026 C  C   . LEU D 1 29  ? -3.354  -6.290  -23.034 1.00 19.07 ? 24  LEU D C   1 
ATOM   5027 O  O   . LEU D 1 29  ? -2.987  -5.548  -22.159 1.00 18.09 ? 24  LEU D O   1 
ATOM   5028 C  CB  . LEU D 1 29  ? -4.543  -7.847  -21.371 1.00 19.83 ? 24  LEU D CB  1 
ATOM   5029 C  CG  . LEU D 1 29  ? -5.919  -7.164  -21.404 1.00 22.94 ? 24  LEU D CG  1 
ATOM   5030 C  CD1 . LEU D 1 29  ? -6.935  -8.020  -22.151 1.00 23.62 ? 24  LEU D CD1 1 
ATOM   5031 C  CD2 . LEU D 1 29  ? -6.440  -6.753  -20.029 1.00 20.82 ? 24  LEU D CD2 1 
ATOM   5032 N  N   . ALA D 1 30  ? -3.313  -5.983  -24.328 1.00 18.38 ? 25  ALA D N   1 
ATOM   5033 C  CA  . ALA D 1 30  ? -2.734  -4.756  -24.895 1.00 21.47 ? 25  ALA D CA  1 
ATOM   5034 C  C   . ALA D 1 30  ? -3.777  -3.656  -24.859 1.00 22.96 ? 25  ALA D C   1 
ATOM   5035 O  O   . ALA D 1 30  ? -5.006  -3.967  -24.802 1.00 23.31 ? 25  ALA D O   1 
ATOM   5036 C  CB  . ALA D 1 30  ? -2.273  -5.021  -26.302 1.00 22.93 ? 25  ALA D CB  1 
ATOM   5037 N  N   . GLN D 1 31  ? -3.317  -2.417  -24.939 1.00 21.22 ? 26  GLN D N   1 
ATOM   5038 C  CA  . GLN D 1 31  ? -4.219  -1.272  -25.218 1.00 23.10 ? 26  GLN D CA  1 
ATOM   5039 C  C   . GLN D 1 31  ? -4.132  -0.966  -26.716 1.00 22.87 ? 26  GLN D C   1 
ATOM   5040 O  O   . GLN D 1 31  ? -3.023  -0.665  -27.226 1.00 21.01 ? 26  GLN D O   1 
ATOM   5041 C  CB  . GLN D 1 31  ? -3.890  -0.057  -24.354 1.00 22.59 ? 26  GLN D CB  1 
ATOM   5042 C  CG  . GLN D 1 31  ? -4.066  -0.273  -22.855 1.00 25.58 ? 26  GLN D CG  1 
ATOM   5043 C  CD  . GLN D 1 31  ? -3.830  1.015   -22.081 1.00 25.06 ? 26  GLN D CD  1 
ATOM   5044 O  OE1 . GLN D 1 31  ? -3.987  2.121   -22.610 1.00 29.69 ? 26  GLN D OE1 1 
ATOM   5045 N  NE2 . GLN D 1 31  ? -3.438  0.882   -20.827 1.00 22.71 ? 26  GLN D NE2 1 
ATOM   5046 N  N   . LEU D 1 32  ? -5.243  -1.171  -27.414 1.00 23.55 ? 27  LEU D N   1 
ATOM   5047 C  CA  . LEU D 1 32  ? -5.325  -0.974  -28.882 1.00 25.18 ? 27  LEU D CA  1 
ATOM   5048 C  C   . LEU D 1 32  ? -5.847  0.440   -29.150 1.00 23.24 ? 27  LEU D C   1 
ATOM   5049 O  O   . LEU D 1 32  ? -6.957  0.728   -28.728 1.00 24.27 ? 27  LEU D O   1 
ATOM   5050 C  CB  . LEU D 1 32  ? -6.242  -2.034  -29.500 1.00 27.09 ? 27  LEU D CB  1 
ATOM   5051 C  CG  . LEU D 1 32  ? -6.440  -1.891  -31.011 1.00 28.68 ? 27  LEU D CG  1 
ATOM   5052 C  CD1 . LEU D 1 32  ? -5.174  -2.241  -31.765 1.00 26.74 ? 27  LEU D CD1 1 
ATOM   5053 C  CD2 . LEU D 1 32  ? -7.601  -2.750  -31.506 1.00 28.35 ? 27  LEU D CD2 1 
ATOM   5054 N  N   . ALA D 1 33  ? -5.062  1.281   -29.820 1.00 21.98 ? 28  ALA D N   1 
ATOM   5055 C  CA  . ALA D 1 33  ? -5.406  2.701   -30.088 1.00 24.46 ? 28  ALA D CA  1 
ATOM   5056 C  C   . ALA D 1 33  ? -5.484  2.945   -31.601 1.00 23.19 ? 28  ALA D C   1 
ATOM   5057 O  O   . ALA D 1 33  ? -4.604  2.476   -32.324 1.00 25.68 ? 28  ALA D O   1 
ATOM   5058 C  CB  . ALA D 1 33  ? -4.399  3.631   -29.440 1.00 23.89 ? 28  ALA D CB  1 
ATOM   5059 N  N   . SER D 1 34  ? -6.481  3.707   -32.035 1.00 23.47 ? 29  SER D N   1 
ATOM   5060 C  CA  . SER D 1 34  ? -6.629  4.231   -33.412 1.00 24.53 ? 29  SER D CA  1 
ATOM   5061 C  C   . SER D 1 34  ? -7.205  5.646   -33.289 1.00 26.25 ? 29  SER D C   1 
ATOM   5062 O  O   . SER D 1 34  ? -7.782  5.955   -32.255 1.00 27.02 ? 29  SER D O   1 
ATOM   5063 C  CB  . SER D 1 34  ? -7.502  3.335   -34.223 1.00 26.54 ? 29  SER D CB  1 
ATOM   5064 O  OG  . SER D 1 34  ? -8.831  3.312   -33.687 1.00 25.41 ? 29  SER D OG  1 
ATOM   5065 N  N   . ASN D 1 35  ? -7.017  6.474   -34.304 1.00 25.26 ? 30  ASN D N   1 
ATOM   5066 C  CA  . ASN D 1 35  ? -7.465  7.885   -34.325 1.00 26.69 ? 30  ASN D CA  1 
ATOM   5067 C  C   . ASN D 1 35  ? -8.979  7.957   -34.120 1.00 28.01 ? 30  ASN D C   1 
ATOM   5068 O  O   . ASN D 1 35  ? -9.676  7.093   -34.650 1.00 27.51 ? 30  ASN D O   1 
ATOM   5069 C  CB  . ASN D 1 35  ? -7.115  8.562   -35.640 1.00 25.41 ? 30  ASN D CB  1 
ATOM   5070 C  CG  . ASN D 1 35  ? -5.640  8.823   -35.750 1.00 28.53 ? 30  ASN D CG  1 
ATOM   5071 O  OD1 . ASN D 1 35  ? -4.897  8.576   -34.798 1.00 27.21 ? 30  ASN D OD1 1 
ATOM   5072 N  ND2 . ASN D 1 35  ? -5.228  9.361   -36.891 1.00 32.76 ? 30  ASN D ND2 1 
ATOM   5073 N  N   . GLY D 1 36  ? -9.435  8.947   -33.356 1.00 26.23 ? 31  GLY D N   1 
ATOM   5074 C  CA  . GLY D 1 36  ? -10.852 9.319   -33.252 1.00 31.16 ? 31  GLY D CA  1 
ATOM   5075 C  C   . GLY D 1 36  ? -11.282 10.082  -34.495 1.00 31.95 ? 31  GLY D C   1 
ATOM   5076 O  O   . GLY D 1 36  ? -10.386 10.662  -35.155 1.00 28.89 ? 31  GLY D O   1 
ATOM   5077 N  N   . ALA D 1 37  ? -12.587 10.053  -34.810 1.00 34.73 ? 32  ALA D N   1 
ATOM   5078 C  CA  . ALA D 1 37  ? -13.194 10.769  -35.961 1.00 38.60 ? 32  ALA D CA  1 
ATOM   5079 C  C   . ALA D 1 37  ? -13.188 12.274  -35.661 1.00 41.02 ? 32  ALA D C   1 
ATOM   5080 O  O   . ALA D 1 37  ? -13.521 12.656  -34.484 1.00 37.55 ? 32  ALA D O   1 
ATOM   5081 C  CB  . ALA D 1 37  ? -14.588 10.275  -36.245 1.00 34.82 ? 32  ALA D CB  1 
ATOM   5082 N  N   . GLY D 1 38  ? -12.759 13.054  -36.667 1.00 43.35 ? 33  GLY D N   1 
ATOM   5083 C  CA  . GLY D 1 38  ? -12.839 14.524  -36.747 1.00 48.67 ? 33  GLY D CA  1 
ATOM   5084 C  C   . GLY D 1 38  ? -12.405 15.171  -35.448 1.00 52.65 ? 33  GLY D C   1 
ATOM   5085 O  O   . GLY D 1 38  ? -13.285 15.726  -34.748 1.00 49.69 ? 33  GLY D O   1 
ATOM   5086 N  N   . GLY D 1 39  ? -11.111 15.046  -35.125 1.00 47.09 ? 34  GLY D N   1 
ATOM   5087 C  CA  . GLY D 1 39  ? -10.472 15.657  -33.944 1.00 52.13 ? 34  GLY D CA  1 
ATOM   5088 C  C   . GLY D 1 39  ? -11.014 15.140  -32.615 1.00 49.72 ? 34  GLY D C   1 
ATOM   5089 O  O   . GLY D 1 39  ? -10.841 15.836  -31.590 1.00 54.01 ? 34  GLY D O   1 
ATOM   5090 N  N   . ALA D 1 40  ? -11.644 13.966  -32.585 1.00 44.08 ? 35  ALA D N   1 
ATOM   5091 C  CA  . ALA D 1 40  ? -11.973 13.271  -31.317 1.00 38.81 ? 35  ALA D CA  1 
ATOM   5092 C  C   . ALA D 1 40  ? -10.696 12.582  -30.833 1.00 32.73 ? 35  ALA D C   1 
ATOM   5093 O  O   . ALA D 1 40  ? -9.784  12.379  -31.670 1.00 32.72 ? 35  ALA D O   1 
ATOM   5094 C  CB  . ALA D 1 40  ? -13.117 12.301  -31.485 1.00 35.90 ? 35  ALA D CB  1 
ATOM   5095 N  N   . ALA D 1 41  ? -10.618 12.308  -29.528 1.00 30.46 ? 36  ALA D N   1 
ATOM   5096 C  CA  . ALA D 1 41  ? -9.541  11.529  -28.869 1.00 31.37 ? 36  ALA D CA  1 
ATOM   5097 C  C   . ALA D 1 41  ? -9.461  10.139  -29.507 1.00 30.76 ? 36  ALA D C   1 
ATOM   5098 O  O   . ALA D 1 41  ? -10.497 9.634   -29.977 1.00 26.84 ? 36  ALA D O   1 
ATOM   5099 C  CB  . ALA D 1 41  ? -9.835  11.449  -27.373 1.00 29.63 ? 36  ALA D CB  1 
ATOM   5100 N  N   . PRO D 1 42  ? -8.265  9.478   -29.549 1.00 26.83 ? 37  PRO D N   1 
ATOM   5101 C  CA  . PRO D 1 42  ? -8.194  8.082   -29.965 1.00 26.14 ? 37  PRO D CA  1 
ATOM   5102 C  C   . PRO D 1 42  ? -9.204  7.187   -29.234 1.00 25.92 ? 37  PRO D C   1 
ATOM   5103 O  O   . PRO D 1 42  ? -9.452  7.444   -28.067 1.00 24.31 ? 37  PRO D O   1 
ATOM   5104 C  CB  . PRO D 1 42  ? -6.754  7.699   -29.588 1.00 26.85 ? 37  PRO D CB  1 
ATOM   5105 C  CG  . PRO D 1 42  ? -5.980  8.993   -29.807 1.00 26.01 ? 37  PRO D CG  1 
ATOM   5106 C  CD  . PRO D 1 42  ? -6.925  10.057  -29.318 1.00 25.31 ? 37  PRO D CD  1 
ATOM   5107 N  N   . HIS D 1 43  ? -9.729  6.167   -29.928 1.00 27.03 ? 38  HIS D N   1 
ATOM   5108 C  CA  . HIS D 1 43  ? -10.399 4.976   -29.329 1.00 28.13 ? 38  HIS D CA  1 
ATOM   5109 C  C   . HIS D 1 43  ? -9.342  4.086   -28.701 1.00 25.36 ? 38  HIS D C   1 
ATOM   5110 O  O   . HIS D 1 43  ? -8.276  3.903   -29.324 1.00 26.99 ? 38  HIS D O   1 
ATOM   5111 C  CB  . HIS D 1 43  ? -11.133 4.092   -30.335 1.00 29.27 ? 38  HIS D CB  1 
ATOM   5112 C  CG  . HIS D 1 43  ? -12.154 4.821   -31.116 1.00 33.72 ? 38  HIS D CG  1 
ATOM   5113 N  ND1 . HIS D 1 43  ? -13.502 4.637   -30.902 1.00 39.79 ? 38  HIS D ND1 1 
ATOM   5114 C  CD2 . HIS D 1 43  ? -12.022 5.712   -32.123 1.00 33.09 ? 38  HIS D CD2 1 
ATOM   5115 C  CE1 . HIS D 1 43  ? -14.157 5.406   -31.749 1.00 39.45 ? 38  HIS D CE1 1 
ATOM   5116 N  NE2 . HIS D 1 43  ? -13.266 6.078   -32.501 1.00 33.40 ? 38  HIS D NE2 1 
ATOM   5117 N  N   . ILE D 1 44  ? -9.600  3.611   -27.489 1.00 25.35 ? 39  ILE D N   1 
ATOM   5118 C  CA  . ILE D 1 44  ? -8.666  2.700   -26.774 1.00 25.28 ? 39  ILE D CA  1 
ATOM   5119 C  C   . ILE D 1 44  ? -9.485  1.509   -26.274 1.00 25.29 ? 39  ILE D C   1 
ATOM   5120 O  O   . ILE D 1 44  ? -10.529 1.718   -25.604 1.00 22.58 ? 39  ILE D O   1 
ATOM   5121 C  CB  . ILE D 1 44  ? -7.958  3.403   -25.609 1.00 26.96 ? 39  ILE D CB  1 
ATOM   5122 C  CG1 . ILE D 1 44  ? -7.305  4.729   -25.997 1.00 25.69 ? 39  ILE D CG1 1 
ATOM   5123 C  CG2 . ILE D 1 44  ? -6.991  2.423   -24.978 1.00 29.92 ? 39  ILE D CG2 1 
ATOM   5124 C  CD1 . ILE D 1 44  ? -5.892  4.608   -26.455 1.00 24.42 ? 39  ILE D CD1 1 
ATOM   5125 N  N   . THR D 1 45  ? -9.057  0.298   -26.609 1.00 23.67 ? 40  THR D N   1 
ATOM   5126 C  CA  . THR D 1 45  ? -9.730  -0.944  -26.163 1.00 24.17 ? 40  THR D CA  1 
ATOM   5127 C  C   . THR D 1 45  ? -8.665  -1.893  -25.632 1.00 23.20 ? 40  THR D C   1 
ATOM   5128 O  O   . THR D 1 45  ? -7.691  -2.072  -26.352 1.00 21.70 ? 40  THR D O   1 
ATOM   5129 C  CB  . THR D 1 45  ? -10.540 -1.598  -27.285 1.00 24.23 ? 40  THR D CB  1 
ATOM   5130 O  OG1 . THR D 1 45  ? -11.375 -0.608  -27.873 1.00 22.91 ? 40  THR D OG1 1 
ATOM   5131 C  CG2 . THR D 1 45  ? -11.377 -2.746  -26.761 1.00 26.66 ? 40  THR D CG2 1 
ATOM   5132 N  N   . HIS D 1 46  ? -8.868  -2.430  -24.419 1.00 23.01 ? 41  HIS D N   1 
ATOM   5133 C  CA  . HIS D 1 46  ? -8.071  -3.548  -23.859 1.00 22.84 ? 41  HIS D CA  1 
ATOM   5134 C  C   . HIS D 1 46  ? -8.448  -4.814  -24.597 1.00 21.04 ? 41  HIS D C   1 
ATOM   5135 O  O   . HIS D 1 46  ? -9.604  -5.231  -24.534 1.00 22.29 ? 41  HIS D O   1 
ATOM   5136 C  CB  . HIS D 1 46  ? -8.248  -3.679  -22.359 1.00 27.13 ? 41  HIS D CB  1 
ATOM   5137 C  CG  . HIS D 1 46  ? -7.533  -2.612  -21.614 1.00 28.34 ? 41  HIS D CG  1 
ATOM   5138 N  ND1 . HIS D 1 46  ? -8.097  -1.372  -21.407 1.00 31.62 ? 41  HIS D ND1 1 
ATOM   5139 C  CD2 . HIS D 1 46  ? -6.304  -2.587  -21.058 1.00 32.81 ? 41  HIS D CD2 1 
ATOM   5140 C  CE1 . HIS D 1 46  ? -7.238  -0.627  -20.740 1.00 32.95 ? 41  HIS D CE1 1 
ATOM   5141 N  NE2 . HIS D 1 46  ? -6.137  -1.349  -20.503 1.00 33.11 ? 41  HIS D NE2 1 
ATOM   5142 N  N   . VAL D 1 47  ? -7.503  -5.345  -25.339 1.00 22.52 ? 42  VAL D N   1 
ATOM   5143 C  CA  . VAL D 1 47  ? -7.718  -6.539  -26.216 1.00 23.90 ? 42  VAL D CA  1 
ATOM   5144 C  C   . VAL D 1 47  ? -6.618  -7.533  -25.965 1.00 21.00 ? 42  VAL D C   1 
ATOM   5145 O  O   . VAL D 1 47  ? -5.452  -7.161  -25.906 1.00 23.57 ? 42  VAL D O   1 
ATOM   5146 C  CB  . VAL D 1 47  ? -7.749  -6.201  -27.717 1.00 25.17 ? 42  VAL D CB  1 
ATOM   5147 C  CG1 . VAL D 1 47  ? -9.023  -5.464  -28.090 1.00 26.81 ? 42  VAL D CG1 1 
ATOM   5148 C  CG2 . VAL D 1 47  ? -6.507  -5.445  -28.174 1.00 24.57 ? 42  VAL D CG2 1 
ATOM   5149 N  N   . PRO D 1 48  ? -6.986  -8.821  -25.920 1.00 22.70 ? 43  PRO D N   1 
ATOM   5150 C  CA  . PRO D 1 48  ? -6.008  -9.905  -25.899 1.00 20.14 ? 43  PRO D CA  1 
ATOM   5151 C  C   . PRO D 1 48  ? -5.322  -10.116 -27.240 1.00 20.99 ? 43  PRO D C   1 
ATOM   5152 O  O   . PRO D 1 48  ? -6.020  -10.330 -28.245 1.00 22.41 ? 43  PRO D O   1 
ATOM   5153 C  CB  . PRO D 1 48  ? -6.868  -11.124 -25.555 1.00 21.58 ? 43  PRO D CB  1 
ATOM   5154 C  CG  . PRO D 1 48  ? -8.240  -10.784 -26.159 1.00 22.22 ? 43  PRO D CG  1 
ATOM   5155 C  CD  . PRO D 1 48  ? -8.376  -9.301  -25.973 1.00 20.72 ? 43  PRO D CD  1 
ATOM   5156 N  N   . ILE D 1 49  ? -3.989  -10.161 -27.233 1.00 19.09 ? 44  ILE D N   1 
ATOM   5157 C  CA  . ILE D 1 49  ? -3.198  -10.243 -28.487 1.00 19.97 ? 44  ILE D CA  1 
ATOM   5158 C  C   . ILE D 1 49  ? -2.049  -11.241 -28.309 1.00 21.77 ? 44  ILE D C   1 
ATOM   5159 O  O   . ILE D 1 49  ? -1.346  -11.135 -27.318 1.00 25.48 ? 44  ILE D O   1 
ATOM   5160 C  CB  . ILE D 1 49  ? -2.684  -8.844  -28.910 1.00 19.70 ? 44  ILE D CB  1 
ATOM   5161 C  CG1 . ILE D 1 49  ? -3.845  -7.852  -29.104 1.00 18.71 ? 44  ILE D CG1 1 
ATOM   5162 C  CG2 . ILE D 1 49  ? -1.807  -8.962  -30.142 1.00 18.84 ? 44  ILE D CG2 1 
ATOM   5163 C  CD1 . ILE D 1 49  ? -3.429  -6.572  -29.734 1.00 20.58 ? 44  ILE D CD1 1 
ATOM   5164 N  N   . ILE D 1 50  ? -1.833  -12.127 -29.288 1.00 20.49 ? 45  ILE D N   1 
ATOM   5165 C  CA  . ILE D 1 50  ? -0.763  -13.157 -29.239 1.00 21.69 ? 45  ILE D CA  1 
ATOM   5166 C  C   . ILE D 1 50  ? 0.033   -13.118 -30.549 1.00 24.00 ? 45  ILE D C   1 
ATOM   5167 O  O   . ILE D 1 50  ? -0.462  -12.628 -31.570 1.00 23.84 ? 45  ILE D O   1 
ATOM   5168 C  CB  . ILE D 1 50  ? -1.390  -14.539 -28.994 1.00 23.72 ? 45  ILE D CB  1 
ATOM   5169 C  CG1 . ILE D 1 50  ? -2.335  -14.945 -30.132 1.00 25.08 ? 45  ILE D CG1 1 
ATOM   5170 C  CG2 . ILE D 1 50  ? -2.097  -14.590 -27.650 1.00 23.19 ? 45  ILE D CG2 1 
ATOM   5171 C  CD1 . ILE D 1 50  ? -2.463  -16.431 -30.298 1.00 25.33 ? 45  ILE D CD1 1 
ATOM   5172 N  N   . VAL D 1 51  ? 1.263   -13.600 -30.495 1.00 27.10 ? 46  VAL D N   1 
ATOM   5173 C  CA  . VAL D 1 51  ? 2.115   -13.839 -31.681 1.00 26.04 ? 46  VAL D CA  1 
ATOM   5174 C  C   . VAL D 1 51  ? 1.436   -14.889 -32.575 1.00 26.27 ? 46  VAL D C   1 
ATOM   5175 O  O   . VAL D 1 51  ? 0.845   -15.816 -32.062 1.00 27.54 ? 46  VAL D O   1 
ATOM   5176 C  CB  . VAL D 1 51  ? 3.503   -14.276 -31.180 1.00 28.34 ? 46  VAL D CB  1 
ATOM   5177 C  CG1 . VAL D 1 51  ? 4.310   -14.992 -32.242 1.00 29.13 ? 46  VAL D CG1 1 
ATOM   5178 C  CG2 . VAL D 1 51  ? 4.263   -13.094 -30.601 1.00 27.58 ? 46  VAL D CG2 1 
ATOM   5179 N  N   . ASP D 1 52  ? 1.514   -14.715 -33.890 1.00 29.12 ? 47  ASP D N   1 
ATOM   5180 C  CA  . ASP D 1 52  ? 1.232   -15.749 -34.917 1.00 27.20 ? 47  ASP D CA  1 
ATOM   5181 C  C   . ASP D 1 52  ? 1.562   -17.112 -34.337 1.00 25.11 ? 47  ASP D C   1 
ATOM   5182 O  O   . ASP D 1 52  ? 2.735   -17.430 -34.131 1.00 26.57 ? 47  ASP D O   1 
ATOM   5183 C  CB  . ASP D 1 52  ? 2.039   -15.484 -36.185 1.00 30.80 ? 47  ASP D CB  1 
ATOM   5184 C  CG  . ASP D 1 52  ? 1.680   -16.388 -37.353 1.00 35.57 ? 47  ASP D CG  1 
ATOM   5185 O  OD1 . ASP D 1 52  ? 0.794   -17.279 -37.170 1.00 32.68 ? 47  ASP D OD1 1 
ATOM   5186 O  OD2 . ASP D 1 52  ? 2.280   -16.180 -38.448 1.00 36.12 ? 47  ASP D OD2 1 
ATOM   5187 N  N   . PRO D 1 53  ? 0.548   -17.950 -34.042 1.00 24.97 ? 48  PRO D N   1 
ATOM   5188 C  CA  . PRO D 1 53  ? 0.801   -19.276 -33.476 1.00 27.58 ? 48  PRO D CA  1 
ATOM   5189 C  C   . PRO D 1 53  ? 1.441   -20.270 -34.450 1.00 30.36 ? 48  PRO D C   1 
ATOM   5190 O  O   . PRO D 1 53  ? 2.030   -21.226 -33.982 1.00 33.52 ? 48  PRO D O   1 
ATOM   5191 C  CB  . PRO D 1 53  ? -0.592  -19.826 -33.168 1.00 27.09 ? 48  PRO D CB  1 
ATOM   5192 C  CG  . PRO D 1 53  ? -1.530  -19.053 -34.056 1.00 27.33 ? 48  PRO D CG  1 
ATOM   5193 C  CD  . PRO D 1 53  ? -0.894  -17.684 -34.216 1.00 25.30 ? 48  PRO D CD  1 
ATOM   5194 N  N   . GLU D 1 54  ? 1.263   -20.017 -35.750 1.00 32.40 ? 49  GLU D N   1 
ATOM   5195 C  CA  . GLU D 1 54  ? 1.825   -20.813 -36.874 1.00 34.30 ? 49  GLU D CA  1 
ATOM   5196 C  C   . GLU D 1 54  ? 3.340   -20.570 -36.994 1.00 36.95 ? 49  GLU D C   1 
ATOM   5197 O  O   . GLU D 1 54  ? 4.000   -21.306 -37.753 1.00 37.52 ? 49  GLU D O   1 
ATOM   5198 C  CB  . GLU D 1 54  ? 1.075   -20.482 -38.169 1.00 36.62 ? 49  GLU D CB  1 
ATOM   5199 C  CG  . GLU D 1 54  ? -0.431  -20.723 -38.071 1.00 38.93 ? 49  GLU D CG  1 
ATOM   5200 C  CD  . GLU D 1 54  ? -0.794  -22.050 -37.418 1.00 41.57 ? 49  GLU D CD  1 
ATOM   5201 O  OE1 . GLU D 1 54  ? -0.032  -23.016 -37.619 1.00 47.21 ? 49  GLU D OE1 1 
ATOM   5202 O  OE2 . GLU D 1 54  ? -1.825  -22.128 -36.709 1.00 40.50 ? 49  GLU D OE2 1 
ATOM   5203 N  N   . LEU D 1 55  ? 3.899   -19.603 -36.267 1.00 36.25 ? 50  LEU D N   1 
ATOM   5204 C  CA  . LEU D 1 55  ? 5.346   -19.298 -36.354 1.00 37.69 ? 50  LEU D CA  1 
ATOM   5205 C  C   . LEU D 1 55  ? 6.126   -20.456 -35.733 1.00 41.55 ? 50  LEU D C   1 
ATOM   5206 O  O   . LEU D 1 55  ? 5.868   -20.782 -34.556 1.00 41.93 ? 50  LEU D O   1 
ATOM   5207 C  CB  . LEU D 1 55  ? 5.657   -17.986 -35.628 1.00 39.47 ? 50  LEU D CB  1 
ATOM   5208 C  CG  . LEU D 1 55  ? 5.552   -16.710 -36.465 1.00 40.41 ? 50  LEU D CG  1 
ATOM   5209 C  CD1 . LEU D 1 55  ? 6.190   -15.548 -35.725 1.00 40.36 ? 50  LEU D CD1 1 
ATOM   5210 C  CD2 . LEU D 1 55  ? 6.195   -16.874 -37.833 1.00 42.97 ? 50  LEU D CD2 1 
ATOM   5211 N  N   . ASP D 1 56  ? 7.006   -21.075 -36.514 1.00 45.62 ? 51  ASP D N   1 
ATOM   5212 C  CA  . ASP D 1 56  ? 8.091   -21.947 -35.989 1.00 54.89 ? 51  ASP D CA  1 
ATOM   5213 C  C   . ASP D 1 56  ? 9.392   -21.133 -36.023 1.00 63.16 ? 51  ASP D C   1 
ATOM   5214 O  O   . ASP D 1 56  ? 9.391   -19.995 -36.559 1.00 63.66 ? 51  ASP D O   1 
ATOM   5215 C  CB  . ASP D 1 56  ? 8.228   -23.254 -36.784 1.00 57.83 ? 51  ASP D CB  1 
ATOM   5216 C  CG  . ASP D 1 56  ? 6.954   -24.078 -36.898 1.00 58.90 ? 51  ASP D CG  1 
ATOM   5217 O  OD1 . ASP D 1 56  ? 6.451   -24.216 -38.025 1.00 59.66 ? 51  ASP D OD1 1 
ATOM   5218 O  OD2 . ASP D 1 56  ? 6.476   -24.584 -35.865 1.00 61.13 ? 51  ASP D OD2 1 
ATOM   5219 N  N   . GLY D 1 57  ? 10.472  -21.715 -35.509 1.00 64.01 ? 52  GLY D N   1 
ATOM   5220 C  CA  . GLY D 1 57  ? 11.745  -21.020 -35.285 1.00 63.87 ? 52  GLY D CA  1 
ATOM   5221 C  C   . GLY D 1 57  ? 11.631  -20.162 -34.033 1.00 66.03 ? 52  GLY D C   1 
ATOM   5222 O  O   . GLY D 1 57  ? 10.515  -19.906 -33.570 1.00 64.77 ? 52  GLY D O   1 
ATOM   5223 N  N   . PRO D 1 58  ? 12.768  -19.735 -33.434 1.00 64.13 ? 53  PRO D N   1 
ATOM   5224 C  CA  . PRO D 1 58  ? 12.740  -18.752 -32.354 1.00 60.62 ? 53  PRO D CA  1 
ATOM   5225 C  C   . PRO D 1 58  ? 12.257  -17.414 -32.933 1.00 53.07 ? 53  PRO D C   1 
ATOM   5226 O  O   . PRO D 1 58  ? 12.702  -17.065 -34.015 1.00 55.23 ? 53  PRO D O   1 
ATOM   5227 C  CB  . PRO D 1 58  ? 14.191  -18.655 -31.849 1.00 60.73 ? 53  PRO D CB  1 
ATOM   5228 C  CG  . PRO D 1 58  ? 14.907  -19.834 -32.488 1.00 62.88 ? 53  PRO D CG  1 
ATOM   5229 C  CD  . PRO D 1 58  ? 14.137  -20.167 -33.753 1.00 62.45 ? 53  PRO D CD  1 
ATOM   5230 N  N   . VAL D 1 59  ? 11.363  -16.721 -32.219 1.00 45.46 ? 54  VAL D N   1 
ATOM   5231 C  CA  . VAL D 1 59  ? 10.880  -15.357 -32.581 1.00 39.79 ? 54  VAL D CA  1 
ATOM   5232 C  C   . VAL D 1 59  ? 11.742  -14.355 -31.814 1.00 37.62 ? 54  VAL D C   1 
ATOM   5233 O  O   . VAL D 1 59  ? 11.570  -14.238 -30.591 1.00 37.49 ? 54  VAL D O   1 
ATOM   5234 C  CB  . VAL D 1 59  ? 9.381   -15.176 -32.276 1.00 37.42 ? 54  VAL D CB  1 
ATOM   5235 C  CG1 . VAL D 1 59  ? 8.824   -13.962 -32.989 1.00 36.75 ? 54  VAL D CG1 1 
ATOM   5236 C  CG2 . VAL D 1 59  ? 8.581   -16.423 -32.631 1.00 39.48 ? 54  VAL D CG2 1 
ATOM   5237 N  N   . ASP D 1 60  ? 12.661  -13.682 -32.501 1.00 38.80 ? 55  ASP D N   1 
ATOM   5238 C  CA  . ASP D 1 60  ? 13.608  -12.740 -31.853 1.00 39.07 ? 55  ASP D CA  1 
ATOM   5239 C  C   . ASP D 1 60  ? 13.187  -11.291 -32.128 1.00 38.48 ? 55  ASP D C   1 
ATOM   5240 O  O   . ASP D 1 60  ? 13.595  -10.418 -31.343 1.00 40.44 ? 55  ASP D O   1 
ATOM   5241 C  CB  . ASP D 1 60  ? 15.047  -13.026 -32.283 1.00 44.10 ? 55  ASP D CB  1 
ATOM   5242 C  CG  . ASP D 1 60  ? 15.603  -14.314 -31.702 1.00 48.74 ? 55  ASP D CG  1 
ATOM   5243 O  OD1 . ASP D 1 60  ? 15.498  -14.501 -30.475 1.00 50.82 ? 55  ASP D OD1 1 
ATOM   5244 O  OD2 . ASP D 1 60  ? 16.106  -15.131 -32.485 1.00 54.68 ? 55  ASP D OD2 1 
ATOM   5245 N  N   . ARG D 1 61  ? 12.412  -11.027 -33.180 1.00 36.21 ? 56  ARG D N   1 
ATOM   5246 C  CA  . ARG D 1 61  ? 11.996  -9.643  -33.544 1.00 38.34 ? 56  ARG D CA  1 
ATOM   5247 C  C   . ARG D 1 61  ? 10.489  -9.630  -33.780 1.00 32.08 ? 56  ARG D C   1 
ATOM   5248 O  O   . ARG D 1 61  ? 9.962   -10.601 -34.315 1.00 33.57 ? 56  ARG D O   1 
ATOM   5249 C  CB  . ARG D 1 61  ? 12.756  -9.124  -34.770 1.00 44.04 ? 56  ARG D CB  1 
ATOM   5250 C  CG  . ARG D 1 61  ? 14.147  -8.581  -34.457 1.00 51.81 ? 56  ARG D CG  1 
ATOM   5251 C  CD  . ARG D 1 61  ? 15.077  -8.459  -35.655 1.00 55.93 ? 56  ARG D CD  1 
ATOM   5252 N  NE  . ARG D 1 61  ? 14.899  -9.512  -36.654 1.00 64.50 ? 56  ARG D NE  1 
ATOM   5253 C  CZ  . ARG D 1 61  ? 15.322  -10.776 -36.547 1.00 67.04 ? 56  ARG D CZ  1 
ATOM   5254 N  NH1 . ARG D 1 61  ? 15.971  -11.197 -35.472 1.00 69.50 ? 56  ARG D NH1 1 
ATOM   5255 N  NH2 . ARG D 1 61  ? 15.080  -11.630 -37.527 1.00 71.80 ? 56  ARG D NH2 1 
ATOM   5256 N  N   . LEU D 1 62  ? 9.822   -8.563  -33.377 1.00 28.09 ? 57  LEU D N   1 
ATOM   5257 C  CA  . LEU D 1 62  ? 8.365   -8.411  -33.619 1.00 28.22 ? 57  LEU D CA  1 
ATOM   5258 C  C   . LEU D 1 62  ? 8.132   -7.907  -35.041 1.00 28.55 ? 57  LEU D C   1 
ATOM   5259 O  O   . LEU D 1 62  ? 7.058   -8.242  -35.602 1.00 27.71 ? 57  LEU D O   1 
ATOM   5260 C  CB  . LEU D 1 62  ? 7.773   -7.426  -32.617 1.00 26.12 ? 57  LEU D CB  1 
ATOM   5261 C  CG  . LEU D 1 62  ? 7.622   -7.969  -31.207 1.00 24.58 ? 57  LEU D CG  1 
ATOM   5262 C  CD1 . LEU D 1 62  ? 7.299   -6.818  -30.268 1.00 24.78 ? 57  LEU D CD1 1 
ATOM   5263 C  CD2 . LEU D 1 62  ? 6.543   -9.041  -31.170 1.00 24.48 ? 57  LEU D CD2 1 
ATOM   5264 N  N   . VAL D 1 63  ? 9.060   -7.107  -35.575 1.00 30.75 ? 58  VAL D N   1 
ATOM   5265 C  CA  . VAL D 1 63  ? 8.912   -6.484  -36.926 1.00 32.66 ? 58  VAL D CA  1 
ATOM   5266 C  C   . VAL D 1 63  ? 8.854   -7.612  -37.957 1.00 30.87 ? 58  VAL D C   1 
ATOM   5267 O  O   . VAL D 1 63  ? 9.760   -8.425  -37.956 1.00 33.07 ? 58  VAL D O   1 
ATOM   5268 C  CB  . VAL D 1 63  ? 10.011  -5.458  -37.256 1.00 33.40 ? 58  VAL D CB  1 
ATOM   5269 C  CG1 . VAL D 1 63  ? 9.932   -4.995  -38.703 1.00 34.66 ? 58  VAL D CG1 1 
ATOM   5270 C  CG2 . VAL D 1 63  ? 9.935   -4.250  -36.339 1.00 35.28 ? 58  VAL D CG2 1 
ATOM   5271 N  N   . GLY D 1 64  ? 7.793   -7.644  -38.763 1.00 33.81 ? 59  GLY D N   1 
ATOM   5272 C  CA  . GLY D 1 64  ? 7.576   -8.621  -39.839 1.00 36.76 ? 59  GLY D CA  1 
ATOM   5273 C  C   . GLY D 1 64  ? 6.595   -9.713  -39.438 1.00 38.17 ? 59  GLY D C   1 
ATOM   5274 O  O   . GLY D 1 64  ? 6.073   -10.408 -40.327 1.00 38.47 ? 59  GLY D O   1 
ATOM   5275 N  N   . ILE D 1 65  ? 6.340   -9.918  -38.147 1.00 35.83 ? 60  ILE D N   1 
ATOM   5276 C  CA  . ILE D 1 65  ? 5.408   -11.010 -37.761 1.00 30.74 ? 60  ILE D CA  1 
ATOM   5277 C  C   . ILE D 1 65  ? 4.004   -10.416 -37.727 1.00 27.86 ? 60  ILE D C   1 
ATOM   5278 O  O   . ILE D 1 65  ? 3.866   -9.183  -37.595 1.00 24.00 ? 60  ILE D O   1 
ATOM   5279 C  CB  . ILE D 1 65  ? 5.815   -11.718 -36.452 1.00 33.16 ? 60  ILE D CB  1 
ATOM   5280 C  CG1 . ILE D 1 65  ? 5.430   -10.927 -35.202 1.00 30.53 ? 60  ILE D CG1 1 
ATOM   5281 C  CG2 . ILE D 1 65  ? 7.288   -12.096 -36.474 1.00 32.05 ? 60  ILE D CG2 1 
ATOM   5282 C  CD1 . ILE D 1 65  ? 5.833   -11.596 -33.917 1.00 33.09 ? 60  ILE D CD1 1 
ATOM   5283 N  N   . THR D 1 66  ? 3.008   -11.285 -37.848 1.00 26.28 ? 61  THR D N   1 
ATOM   5284 C  CA  . THR D 1 66  ? 1.576   -10.943 -37.654 1.00 28.99 ? 61  THR D CA  1 
ATOM   5285 C  C   . THR D 1 66  ? 1.176   -11.318 -36.225 1.00 28.91 ? 61  THR D C   1 
ATOM   5286 O  O   . THR D 1 66  ? 1.529   -12.416 -35.787 1.00 33.92 ? 61  THR D O   1 
ATOM   5287 C  CB  . THR D 1 66  ? 0.689   -11.602 -38.711 1.00 29.11 ? 61  THR D CB  1 
ATOM   5288 O  OG1 . THR D 1 66  ? 1.237   -11.201 -39.968 1.00 28.42 ? 61  THR D OG1 1 
ATOM   5289 C  CG2 . THR D 1 66  ? -0.765  -11.207 -38.579 1.00 30.13 ? 61  THR D CG2 1 
ATOM   5290 N  N   . LEU D 1 67  ? 0.496   -10.399 -35.542 1.00 23.66 ? 62  LEU D N   1 
ATOM   5291 C  CA  . LEU D 1 67  ? -0.167  -10.596 -34.240 1.00 24.35 ? 62  LEU D CA  1 
ATOM   5292 C  C   . LEU D 1 67  ? -1.633  -10.906 -34.517 1.00 22.49 ? 62  LEU D C   1 
ATOM   5293 O  O   . LEU D 1 67  ? -2.153  -10.397 -35.519 1.00 21.80 ? 62  LEU D O   1 
ATOM   5294 C  CB  . LEU D 1 67  ? -0.012  -9.324  -33.391 1.00 24.63 ? 62  LEU D CB  1 
ATOM   5295 C  CG  . LEU D 1 67  ? 1.424   -8.840  -33.212 1.00 24.88 ? 62  LEU D CG  1 
ATOM   5296 C  CD1 . LEU D 1 67  ? 1.461   -7.627  -32.292 1.00 23.85 ? 62  LEU D CD1 1 
ATOM   5297 C  CD2 . LEU D 1 67  ? 2.280   -9.971  -32.660 1.00 25.12 ? 62  LEU D CD2 1 
ATOM   5298 N  N   . TRP D 1 68  ? -2.241  -11.723 -33.658 1.00 20.68 ? 63  TRP D N   1 
ATOM   5299 C  CA  . TRP D 1 68  ? -3.673  -12.102 -33.709 1.00 23.60 ? 63  TRP D CA  1 
ATOM   5300 C  C   . TRP D 1 68  ? -4.398  -11.529 -32.499 1.00 21.59 ? 63  TRP D C   1 
ATOM   5301 O  O   . TRP D 1 68  ? -3.862  -11.603 -31.389 1.00 23.05 ? 63  TRP D O   1 
ATOM   5302 C  CB  . TRP D 1 68  ? -3.792  -13.623 -33.693 1.00 25.66 ? 63  TRP D CB  1 
ATOM   5303 C  CG  . TRP D 1 68  ? -3.334  -14.360 -34.910 1.00 24.45 ? 63  TRP D CG  1 
ATOM   5304 C  CD1 . TRP D 1 68  ? -2.435  -13.969 -35.863 1.00 27.35 ? 63  TRP D CD1 1 
ATOM   5305 C  CD2 . TRP D 1 68  ? -3.741  -15.694 -35.254 1.00 25.70 ? 63  TRP D CD2 1 
ATOM   5306 N  NE1 . TRP D 1 68  ? -2.266  -14.972 -36.786 1.00 31.22 ? 63  TRP D NE1 1 
ATOM   5307 C  CE2 . TRP D 1 68  ? -3.058  -16.044 -36.440 1.00 27.04 ? 63  TRP D CE2 1 
ATOM   5308 C  CE3 . TRP D 1 68  ? -4.599  -16.633 -34.657 1.00 27.84 ? 63  TRP D CE3 1 
ATOM   5309 C  CZ2 . TRP D 1 68  ? -3.221  -17.292 -37.036 1.00 26.63 ? 63  TRP D CZ2 1 
ATOM   5310 C  CZ3 . TRP D 1 68  ? -4.798  -17.849 -35.277 1.00 28.49 ? 63  TRP D CZ3 1 
ATOM   5311 C  CH2 . TRP D 1 68  ? -4.137  -18.157 -36.471 1.00 27.49 ? 63  TRP D CH2 1 
ATOM   5312 N  N   . GLY D 1 69  ? -5.627  -11.075 -32.672 1.00 21.89 ? 64  GLY D N   1 
ATOM   5313 C  CA  . GLY D 1 69  ? -6.399  -10.526 -31.550 1.00 21.04 ? 64  GLY D CA  1 
ATOM   5314 C  C   . GLY D 1 69  ? -7.890  -10.567 -31.814 1.00 21.07 ? 64  GLY D C   1 
ATOM   5315 O  O   . GLY D 1 69  ? -8.290  -10.898 -32.952 1.00 23.33 ? 64  GLY D O   1 
ATOM   5316 N  N   . HIS D 1 70  ? -8.676  -10.281 -30.792 1.00 19.68 ? 65  HIS D N   1 
ATOM   5317 C  CA  . HIS D 1 70  ? -10.138 -10.109 -30.936 1.00 21.68 ? 65  HIS D CA  1 
ATOM   5318 C  C   . HIS D 1 70  ? -10.623 -8.997  -30.023 1.00 23.76 ? 65  HIS D C   1 
ATOM   5319 O  O   . HIS D 1 70  ? -9.879  -8.536  -29.134 1.00 23.91 ? 65  HIS D O   1 
ATOM   5320 C  CB  . HIS D 1 70  ? -10.896 -11.427 -30.765 1.00 20.83 ? 65  HIS D CB  1 
ATOM   5321 C  CG  . HIS D 1 70  ? -10.848 -12.039 -29.405 1.00 22.73 ? 65  HIS D CG  1 
ATOM   5322 N  ND1 . HIS D 1 70  ? -9.715  -12.663 -28.906 1.00 22.52 ? 65  HIS D ND1 1 
ATOM   5323 C  CD2 . HIS D 1 70  ? -11.817 -12.243 -28.489 1.00 26.06 ? 65  HIS D CD2 1 
ATOM   5324 C  CE1 . HIS D 1 70  ? -9.965  -13.125 -27.692 1.00 24.47 ? 65  HIS D CE1 1 
ATOM   5325 N  NE2 . HIS D 1 70  ? -11.268 -12.927 -27.429 1.00 26.54 ? 65  HIS D NE2 1 
ATOM   5326 N  N   . MET D 1 71  ? -11.859 -8.568  -30.279 1.00 23.72 ? 66  MET D N   1 
ATOM   5327 C  CA  . MET D 1 71  ? -12.558 -7.565  -29.466 1.00 24.94 ? 66  MET D CA  1 
ATOM   5328 C  C   . MET D 1 71  ? -14.057 -7.836  -29.643 1.00 25.39 ? 66  MET D C   1 
ATOM   5329 O  O   . MET D 1 71  ? -14.412 -8.800  -30.360 1.00 23.49 ? 66  MET D O   1 
ATOM   5330 C  CB  . MET D 1 71  ? -12.168 -6.134  -29.878 1.00 26.18 ? 66  MET D CB  1 
ATOM   5331 C  CG  . MET D 1 71  ? -12.541 -5.713  -31.262 1.00 29.71 ? 66  MET D CG  1 
ATOM   5332 S  SD  . MET D 1 71  ? -12.297 -3.888  -31.458 1.00 36.55 ? 66  MET D SD  1 
ATOM   5333 C  CE  . MET D 1 71  ? -10.550 -3.887  -31.833 1.00 35.69 ? 66  MET D CE  1 
ATOM   5334 N  N   . ASN D 1 72  ? -14.899 -7.044  -29.002 1.00 25.80 ? 67  ASN D N   1 
ATOM   5335 C  CA  . ASN D 1 72  ? -16.372 -7.183  -29.130 1.00 25.16 ? 67  ASN D CA  1 
ATOM   5336 C  C   . ASN D 1 72  ? -16.795 -6.451  -30.415 1.00 28.99 ? 67  ASN D C   1 
ATOM   5337 O  O   . ASN D 1 72  ? -16.429 -5.276  -30.553 1.00 27.34 ? 67  ASN D O   1 
ATOM   5338 C  CB  . ASN D 1 72  ? -16.994 -6.655  -27.858 1.00 24.64 ? 67  ASN D CB  1 
ATOM   5339 C  CG  . ASN D 1 72  ? -18.489 -6.856  -27.789 1.00 24.50 ? 67  ASN D CG  1 
ATOM   5340 O  OD1 . ASN D 1 72  ? -19.125 -7.264  -28.757 1.00 25.12 ? 67  ASN D OD1 1 
ATOM   5341 N  ND2 . ASN D 1 72  ? -19.016 -6.631  -26.609 1.00 23.55 ? 67  ASN D ND2 1 
ATOM   5342 N  N   . ARG D 1 73  ? -17.500 -7.114  -31.337 1.00 28.66 ? 68  ARG D N   1 
ATOM   5343 C  CA  . ARG D 1 73  ? -18.077 -6.446  -32.553 1.00 33.48 ? 68  ARG D CA  1 
ATOM   5344 C  C   . ARG D 1 73  ? -18.966 -5.253  -32.184 1.00 30.29 ? 68  ARG D C   1 
ATOM   5345 O  O   . ARG D 1 73  ? -19.007 -4.283  -32.966 1.00 35.81 ? 68  ARG D O   1 
ATOM   5346 C  CB  . ARG D 1 73  ? -18.869 -7.435  -33.413 1.00 36.56 ? 68  ARG D CB  1 
ATOM   5347 C  CG  . ARG D 1 73  ? -17.949 -8.258  -34.300 1.00 35.83 ? 68  ARG D CG  1 
ATOM   5348 C  CD  . ARG D 1 73  ? -18.684 -9.219  -35.207 1.00 35.43 ? 68  ARG D CD  1 
ATOM   5349 N  NE  . ARG D 1 73  ? -17.647 -9.893  -35.956 1.00 33.35 ? 68  ARG D NE  1 
ATOM   5350 C  CZ  . ARG D 1 73  ? -17.334 -9.636  -37.210 1.00 38.55 ? 68  ARG D CZ  1 
ATOM   5351 N  NH1 . ARG D 1 73  ? -18.015 -8.733  -37.903 1.00 37.10 ? 68  ARG D NH1 1 
ATOM   5352 N  NH2 . ARG D 1 73  ? -16.342 -10.303 -37.777 1.00 41.07 ? 68  ARG D NH2 1 
ATOM   5353 N  N   . ALA D 1 74  ? -19.611 -5.309  -31.026 1.00 31.58 ? 69  ALA D N   1 
ATOM   5354 C  CA  . ALA D 1 74  ? -20.621 -4.330  -30.575 1.00 32.10 ? 69  ALA D CA  1 
ATOM   5355 C  C   . ALA D 1 74  ? -19.925 -3.079  -30.044 1.00 32.18 ? 69  ALA D C   1 
ATOM   5356 O  O   . ALA D 1 74  ? -20.626 -2.087  -29.744 1.00 31.20 ? 69  ALA D O   1 
ATOM   5357 C  CB  . ALA D 1 74  ? -21.479 -4.944  -29.504 1.00 31.66 ? 69  ALA D CB  1 
ATOM   5358 N  N   . ASN D 1 75  ? -18.620 -3.194  -29.791 1.00 32.63 ? 70  ASN D N   1 
ATOM   5359 C  CA  . ASN D 1 75  ? -17.719 -2.073  -29.412 1.00 31.03 ? 70  ASN D CA  1 
ATOM   5360 C  C   . ASN D 1 75  ? -17.637 -1.129  -30.619 1.00 28.68 ? 70  ASN D C   1 
ATOM   5361 O  O   . ASN D 1 75  ? -17.140 -1.522  -31.668 1.00 32.19 ? 70  ASN D O   1 
ATOM   5362 C  CB  . ASN D 1 75  ? -16.371 -2.654  -28.948 1.00 32.96 ? 70  ASN D CB  1 
ATOM   5363 C  CG  . ASN D 1 75  ? -15.415 -1.640  -28.358 1.00 34.17 ? 70  ASN D CG  1 
ATOM   5364 O  OD1 . ASN D 1 75  ? -15.587 -0.432  -28.547 1.00 36.50 ? 70  ASN D OD1 1 
ATOM   5365 N  ND2 . ASN D 1 75  ? -14.387 -2.133  -27.689 1.00 33.07 ? 70  ASN D ND2 1 
ATOM   5366 N  N   . PRO D 1 76  ? -18.074 0.154   -30.524 1.00 26.58 ? 71  PRO D N   1 
ATOM   5367 C  CA  . PRO D 1 76  ? -17.937 1.111   -31.623 1.00 23.67 ? 71  PRO D CA  1 
ATOM   5368 C  C   . PRO D 1 76  ? -16.530 1.136   -32.231 1.00 25.47 ? 71  PRO D C   1 
ATOM   5369 O  O   . PRO D 1 76  ? -16.325 1.456   -33.408 1.00 26.63 ? 71  PRO D O   1 
ATOM   5370 C  CB  . PRO D 1 76  ? -18.133 2.466   -30.940 1.00 25.21 ? 71  PRO D CB  1 
ATOM   5371 C  CG  . PRO D 1 76  ? -18.984 2.174   -29.740 1.00 29.91 ? 71  PRO D CG  1 
ATOM   5372 C  CD  . PRO D 1 76  ? -18.614 0.773   -29.307 1.00 29.45 ? 71  PRO D CD  1 
ATOM   5373 N  N   . HIS D 1 77  ? -15.546 0.841   -31.394 1.00 24.14 ? 72  HIS D N   1 
ATOM   5374 C  CA  . HIS D 1 77  ? -14.127 0.790   -31.830 1.00 26.19 ? 72  HIS D CA  1 
ATOM   5375 C  C   . HIS D 1 77  ? -14.041 -0.148  -33.041 1.00 26.39 ? 72  HIS D C   1 
ATOM   5376 O  O   . HIS D 1 77  ? -13.329 0.181   -34.018 1.00 24.25 ? 72  HIS D O   1 
ATOM   5377 C  CB  . HIS D 1 77  ? -13.234 0.417   -30.647 1.00 23.43 ? 72  HIS D CB  1 
ATOM   5378 C  CG  . HIS D 1 77  ? -11.794 0.678   -30.910 1.00 25.13 ? 72  HIS D CG  1 
ATOM   5379 N  ND1 . HIS D 1 77  ? -10.833 0.449   -29.965 1.00 21.96 ? 72  HIS D ND1 1 
ATOM   5380 C  CD2 . HIS D 1 77  ? -11.161 1.172   -31.988 1.00 21.61 ? 72  HIS D CD2 1 
ATOM   5381 C  CE1 . HIS D 1 77  ? -9.665  0.748   -30.464 1.00 23.51 ? 72  HIS D CE1 1 
ATOM   5382 N  NE2 . HIS D 1 77  ? -9.842  1.235   -31.668 1.00 25.97 ? 72  HIS D NE2 1 
ATOM   5383 N  N   . TRP D 1 78  ? -14.808 -1.235  -33.039 1.00 28.15 ? 73  TRP D N   1 
ATOM   5384 C  CA  . TRP D 1 78  ? -14.772 -2.215  -34.165 1.00 30.53 ? 73  TRP D CA  1 
ATOM   5385 C  C   . TRP D 1 78  ? -15.161 -1.540  -35.491 1.00 31.48 ? 73  TRP D C   1 
ATOM   5386 O  O   . TRP D 1 78  ? -14.339 -1.612  -36.436 1.00 29.55 ? 73  TRP D O   1 
ATOM   5387 C  CB  . TRP D 1 78  ? -15.635 -3.429  -33.828 1.00 32.61 ? 73  TRP D CB  1 
ATOM   5388 C  CG  . TRP D 1 78  ? -15.725 -4.446  -34.914 1.00 31.58 ? 73  TRP D CG  1 
ATOM   5389 C  CD1 . TRP D 1 78  ? -16.821 -4.699  -35.674 1.00 31.90 ? 73  TRP D CD1 1 
ATOM   5390 C  CD2 . TRP D 1 78  ? -14.685 -5.325  -35.384 1.00 33.41 ? 73  TRP D CD2 1 
ATOM   5391 N  NE1 . TRP D 1 78  ? -16.547 -5.679  -36.584 1.00 33.08 ? 73  TRP D NE1 1 
ATOM   5392 C  CE2 . TRP D 1 78  ? -15.249 -6.090  -36.430 1.00 33.88 ? 73  TRP D CE2 1 
ATOM   5393 C  CE3 . TRP D 1 78  ? -13.347 -5.561  -35.024 1.00 31.01 ? 73  TRP D CE3 1 
ATOM   5394 C  CZ2 . TRP D 1 78  ? -14.524 -7.074  -37.105 1.00 31.84 ? 73  TRP D CZ2 1 
ATOM   5395 C  CZ3 . TRP D 1 78  ? -12.629 -6.518  -35.694 1.00 27.27 ? 73  TRP D CZ3 1 
ATOM   5396 C  CH2 . TRP D 1 78  ? -13.213 -7.273  -36.714 1.00 32.08 ? 73  TRP D CH2 1 
ATOM   5397 N  N   . ALA D 1 79  ? -16.343 -0.896  -35.562 1.00 32.67 ? 74  ALA D N   1 
ATOM   5398 C  CA  . ALA D 1 79  ? -16.856 -0.193  -36.766 1.00 35.23 ? 74  ALA D CA  1 
ATOM   5399 C  C   . ALA D 1 79  ? -15.970 1.016   -37.119 1.00 35.07 ? 74  ALA D C   1 
ATOM   5400 O  O   . ALA D 1 79  ? -15.853 1.346   -38.321 1.00 29.50 ? 74  ALA D O   1 
ATOM   5401 C  CB  . ALA D 1 79  ? -18.299 0.232   -36.560 1.00 35.85 ? 74  ALA D CB  1 
ATOM   5402 N  N   . ALA D 1 80  ? -15.398 1.685   -36.111 1.00 36.85 ? 75  ALA D N   1 
ATOM   5403 C  CA  . ALA D 1 80  ? -14.508 2.865   -36.273 1.00 36.67 ? 75  ALA D CA  1 
ATOM   5404 C  C   . ALA D 1 80  ? -13.251 2.456   -37.047 1.00 41.77 ? 75  ALA D C   1 
ATOM   5405 O  O   . ALA D 1 80  ? -12.655 3.325   -37.750 1.00 36.52 ? 75  ALA D O   1 
ATOM   5406 C  CB  . ALA D 1 80  ? -14.145 3.454   -34.925 1.00 35.87 ? 75  ALA D CB  1 
ATOM   5407 N  N   . LEU D 1 81  ? -12.840 1.190   -36.937 1.00 39.06 ? 76  LEU D N   1 
ATOM   5408 C  CA  . LEU D 1 81  ? -11.552 0.747   -37.536 1.00 39.46 ? 76  LEU D CA  1 
ATOM   5409 C  C   . LEU D 1 81  ? -11.703 0.596   -39.059 1.00 46.20 ? 76  LEU D C   1 
ATOM   5410 O  O   . LEU D 1 81  ? -10.653 0.510   -39.753 1.00 43.14 ? 76  LEU D O   1 
ATOM   5411 C  CB  . LEU D 1 81  ? -11.107 -0.543  -36.841 1.00 37.88 ? 76  LEU D CB  1 
ATOM   5412 C  CG  . LEU D 1 81  ? -10.457 -0.306  -35.483 1.00 31.31 ? 76  LEU D CG  1 
ATOM   5413 C  CD1 . LEU D 1 81  ? -10.543 -1.543  -34.627 1.00 35.82 ? 76  LEU D CD1 1 
ATOM   5414 C  CD2 . LEU D 1 81  ? -9.017  0.126   -35.659 1.00 32.50 ? 76  LEU D CD2 1 
ATOM   5415 N  N   . GLY D 1 82  ? -12.952 0.591   -39.546 1.00 45.50 ? 77  GLY D N   1 
ATOM   5416 C  CA  . GLY D 1 82  ? -13.313 0.767   -40.968 1.00 51.38 ? 77  GLY D CA  1 
ATOM   5417 C  C   . GLY D 1 82  ? -12.734 -0.326  -41.845 1.00 60.48 ? 77  GLY D C   1 
ATOM   5418 O  O   . GLY D 1 82  ? -13.363 -1.420  -41.928 1.00 63.53 ? 77  GLY D O   1 
ATOM   5419 N  N   . GLY D 1 83  ? -11.583 -0.021  -42.455 1.00 62.96 ? 78  GLY D N   1 
ATOM   5420 C  CA  . GLY D 1 83  ? -10.835 -0.902  -43.367 1.00 62.76 ? 78  GLY D CA  1 
ATOM   5421 C  C   . GLY D 1 83  ? -9.398  -1.054  -42.923 1.00 67.26 ? 78  GLY D C   1 
ATOM   5422 O  O   . GLY D 1 83  ? -9.193  -1.464  -41.788 1.00 83.00 ? 78  GLY D O   1 
ATOM   5423 N  N   . ALA D 1 84  ? -8.413  -0.696  -43.735 1.00 61.89 ? 79  ALA D N   1 
ATOM   5424 C  CA  . ALA D 1 84  ? -7.046  -0.920  -43.220 1.00 59.90 ? 79  ALA D CA  1 
ATOM   5425 C  C   . ALA D 1 84  ? -6.621  0.251   -42.333 1.00 58.01 ? 79  ALA D C   1 
ATOM   5426 O  O   . ALA D 1 84  ? -6.022  1.199   -42.847 1.00 62.24 ? 79  ALA D O   1 
ATOM   5427 C  CB  . ALA D 1 84  ? -6.075  -1.143  -44.336 1.00 62.29 ? 79  ALA D CB  1 
ATOM   5428 N  N   . ALA D 1 85  ? -6.917  0.148   -41.039 1.00 49.15 ? 80  ALA D N   1 
ATOM   5429 C  CA  . ALA D 1 85  ? -6.602  1.222   -40.072 1.00 42.33 ? 80  ALA D CA  1 
ATOM   5430 C  C   . ALA D 1 85  ? -5.190  1.073   -39.497 1.00 34.18 ? 80  ALA D C   1 
ATOM   5431 O  O   . ALA D 1 85  ? -4.808  -0.010  -39.112 1.00 34.10 ? 80  ALA D O   1 
ATOM   5432 C  CB  . ALA D 1 85  ? -7.642  1.255   -38.992 1.00 38.39 ? 80  ALA D CB  1 
ATOM   5433 N  N   . ASN D 1 86  ? -4.473  2.179   -39.471 1.00 29.17 ? 81  ASN D N   1 
ATOM   5434 C  CA  . ASN D 1 86  ? -3.134  2.231   -38.869 1.00 33.02 ? 81  ASN D CA  1 
ATOM   5435 C  C   . ASN D 1 86  ? -3.381  2.309   -37.373 1.00 32.13 ? 81  ASN D C   1 
ATOM   5436 O  O   . ASN D 1 86  ? -4.171  3.151   -36.976 1.00 35.53 ? 81  ASN D O   1 
ATOM   5437 C  CB  . ASN D 1 86  ? -2.344  3.399   -39.427 1.00 37.02 ? 81  ASN D CB  1 
ATOM   5438 C  CG  . ASN D 1 86  ? -2.077  3.215   -40.896 1.00 39.44 ? 81  ASN D CG  1 
ATOM   5439 O  OD1 . ASN D 1 86  ? -1.604  2.170   -41.295 1.00 40.43 ? 81  ASN D OD1 1 
ATOM   5440 N  ND2 . ASN D 1 86  ? -2.379  4.214   -41.689 1.00 41.22 ? 81  ASN D ND2 1 
ATOM   5441 N  N   . VAL D 1 87  ? -2.750  1.424   -36.616 1.00 28.06 ? 82  VAL D N   1 
ATOM   5442 C  CA  . VAL D 1 87  ? -3.024  1.294   -35.161 1.00 25.60 ? 82  VAL D CA  1 
ATOM   5443 C  C   . VAL D 1 87  ? -1.712  1.175   -34.414 1.00 23.83 ? 82  VAL D C   1 
ATOM   5444 O  O   . VAL D 1 87  ? -0.658  0.953   -35.026 1.00 23.55 ? 82  VAL D O   1 
ATOM   5445 C  CB  . VAL D 1 87  ? -3.985  0.137   -34.818 1.00 24.63 ? 82  VAL D CB  1 
ATOM   5446 C  CG1 . VAL D 1 87  ? -5.307  0.269   -35.573 1.00 26.07 ? 82  VAL D CG1 1 
ATOM   5447 C  CG2 . VAL D 1 87  ? -3.352  -1.237  -34.990 1.00 24.27 ? 82  VAL D CG2 1 
ATOM   5448 N  N   . VAL D 1 88  ? -1.809  1.383   -33.114 1.00 23.94 ? 83  VAL D N   1 
ATOM   5449 C  CA  . VAL D 1 88  ? -0.737  1.038   -32.145 1.00 25.05 ? 83  VAL D CA  1 
ATOM   5450 C  C   . VAL D 1 88  ? -1.396  0.127   -31.129 1.00 23.66 ? 83  VAL D C   1 
ATOM   5451 O  O   . VAL D 1 88  ? -2.612  0.361   -30.783 1.00 24.89 ? 83  VAL D O   1 
ATOM   5452 C  CB  . VAL D 1 88  ? -0.118  2.272   -31.474 1.00 26.02 ? 83  VAL D CB  1 
ATOM   5453 C  CG1 . VAL D 1 88  ? -1.181  3.175   -30.863 1.00 24.58 ? 83  VAL D CG1 1 
ATOM   5454 C  CG2 . VAL D 1 88  ? 0.891   1.851   -30.421 1.00 26.52 ? 83  VAL D CG2 1 
ATOM   5455 N  N   . ALA D 1 89  ? -0.690  -0.923  -30.753 1.00 22.60 ? 84  ALA D N   1 
ATOM   5456 C  CA  . ALA D 1 89  ? -1.088  -1.759  -29.603 1.00 20.76 ? 84  ALA D CA  1 
ATOM   5457 C  C   . ALA D 1 89  ? 0.038   -1.627  -28.601 1.00 21.23 ? 84  ALA D C   1 
ATOM   5458 O  O   . ALA D 1 89  ? 1.194   -1.837  -29.031 1.00 24.17 ? 84  ALA D O   1 
ATOM   5459 C  CB  . ALA D 1 89  ? -1.334  -3.176  -30.049 1.00 21.18 ? 84  ALA D CB  1 
ATOM   5460 N  N   . THR D 1 90  ? -0.263  -1.220  -27.361 1.00 21.82 ? 85  THR D N   1 
ATOM   5461 C  CA  . THR D 1 90  ? 0.736   -1.005  -26.282 1.00 20.43 ? 85  THR D CA  1 
ATOM   5462 C  C   . THR D 1 90  ? 0.597   -2.114  -25.231 1.00 20.87 ? 85  THR D C   1 
ATOM   5463 O  O   . THR D 1 90  ? -0.509  -2.388  -24.762 1.00 20.21 ? 85  THR D O   1 
ATOM   5464 C  CB  . THR D 1 90  ? 0.601   0.374   -25.650 1.00 19.81 ? 85  THR D CB  1 
ATOM   5465 O  OG1 . THR D 1 90  ? 0.613   1.338   -26.709 1.00 22.93 ? 85  THR D OG1 1 
ATOM   5466 C  CG2 . THR D 1 90  ? 1.696   0.679   -24.644 1.00 22.56 ? 85  THR D CG2 1 
ATOM   5467 N  N   . PHE D 1 91  ? 1.704   -2.731  -24.903 1.00 19.15 ? 86  PHE D N   1 
ATOM   5468 C  CA  . PHE D 1 91  ? 1.797   -3.868  -23.973 1.00 20.65 ? 86  PHE D CA  1 
ATOM   5469 C  C   . PHE D 1 91  ? 2.594   -3.373  -22.772 1.00 22.08 ? 86  PHE D C   1 
ATOM   5470 O  O   . PHE D 1 91  ? 3.703   -2.897  -23.000 1.00 24.39 ? 86  PHE D O   1 
ATOM   5471 C  CB  . PHE D 1 91  ? 2.519   -5.028  -24.637 1.00 19.51 ? 86  PHE D CB  1 
ATOM   5472 C  CG  . PHE D 1 91  ? 1.851   -5.603  -25.846 1.00 21.64 ? 86  PHE D CG  1 
ATOM   5473 C  CD1 . PHE D 1 91  ? 2.050   -5.043  -27.106 1.00 21.95 ? 86  PHE D CD1 1 
ATOM   5474 C  CD2 . PHE D 1 91  ? 1.133   -6.781  -25.748 1.00 21.53 ? 86  PHE D CD2 1 
ATOM   5475 C  CE1 . PHE D 1 91  ? 1.458   -5.608  -28.222 1.00 22.13 ? 86  PHE D CE1 1 
ATOM   5476 C  CE2 . PHE D 1 91  ? 0.540   -7.340  -26.867 1.00 22.89 ? 86  PHE D CE2 1 
ATOM   5477 C  CZ  . PHE D 1 91  ? 0.706   -6.755  -28.100 1.00 23.49 ? 86  PHE D CZ  1 
ATOM   5478 N  N   . ALA D 1 92  ? 2.060   -3.489  -21.568 1.00 20.55 ? 87  ALA D N   1 
ATOM   5479 C  CA  . ALA D 1 92  ? 2.637   -2.878  -20.349 1.00 25.03 ? 87  ALA D CA  1 
ATOM   5480 C  C   . ALA D 1 92  ? 3.137   -4.010  -19.448 1.00 23.11 ? 87  ALA D C   1 
ATOM   5481 O  O   . ALA D 1 92  ? 2.325   -4.830  -19.071 1.00 21.94 ? 87  ALA D O   1 
ATOM   5482 C  CB  . ALA D 1 92  ? 1.595   -1.987  -19.690 1.00 23.92 ? 87  ALA D CB  1 
ATOM   5483 N  N   . GLY D 1 93  ? 4.445   -4.058  -19.186 1.00 22.73 ? 88  GLY D N   1 
ATOM   5484 C  CA  . GLY D 1 93  ? 5.091   -5.096  -18.372 1.00 24.49 ? 88  GLY D CA  1 
ATOM   5485 C  C   . GLY D 1 93  ? 5.318   -4.642  -16.924 1.00 25.53 ? 88  GLY D C   1 
ATOM   5486 O  O   . GLY D 1 93  ? 4.672   -3.712  -16.430 1.00 24.77 ? 88  GLY D O   1 
ATOM   5487 N  N   . PRO D 1 94  ? 6.260   -5.285  -16.201 1.00 24.07 ? 89  PRO D N   1 
ATOM   5488 C  CA  . PRO D 1 94  ? 6.528   -4.940  -14.800 1.00 24.07 ? 89  PRO D CA  1 
ATOM   5489 C  C   . PRO D 1 94  ? 6.882   -3.452  -14.647 1.00 22.88 ? 89  PRO D C   1 
ATOM   5490 O  O   . PRO D 1 94  ? 7.440   -2.848  -15.587 1.00 21.19 ? 89  PRO D O   1 
ATOM   5491 C  CB  . PRO D 1 94  ? 7.709   -5.858  -14.441 1.00 24.17 ? 89  PRO D CB  1 
ATOM   5492 C  CG  . PRO D 1 94  ? 7.566   -7.045  -15.398 1.00 24.59 ? 89  PRO D CG  1 
ATOM   5493 C  CD  . PRO D 1 94  ? 7.114   -6.385  -16.682 1.00 25.73 ? 89  PRO D CD  1 
ATOM   5494 N  N   . ASN D 1 95  ? 6.494   -2.869  -13.513 1.00 22.79 ? 90  ASN D N   1 
ATOM   5495 C  CA  . ASN D 1 95  ? 6.693   -1.426  -13.234 1.00 23.04 ? 90  ASN D CA  1 
ATOM   5496 C  C   . ASN D 1 95  ? 6.678   -1.211  -11.718 1.00 23.39 ? 90  ASN D C   1 
ATOM   5497 O  O   . ASN D 1 95  ? 5.952   -1.963  -11.037 1.00 23.45 ? 90  ASN D O   1 
ATOM   5498 C  CB  . ASN D 1 95  ? 5.635   -0.586  -13.948 1.00 22.30 ? 90  ASN D CB  1 
ATOM   5499 C  CG  . ASN D 1 95  ? 4.249   -0.772  -13.374 1.00 22.87 ? 90  ASN D CG  1 
ATOM   5500 O  OD1 . ASN D 1 95  ? 3.839   0.010   -12.524 1.00 24.37 ? 90  ASN D OD1 1 
ATOM   5501 N  ND2 . ASN D 1 95  ? 3.561   -1.839  -13.756 1.00 22.08 ? 90  ASN D ND2 1 
ATOM   5502 N  N   . ALA D 1 96  ? 7.440   -0.238  -11.211 1.00 23.26 ? 91  ALA D N   1 
ATOM   5503 C  CA  . ALA D 1 96  ? 7.369   0.212   -9.799  1.00 22.02 ? 91  ALA D CA  1 
ATOM   5504 C  C   . ALA D 1 96  ? 7.853   1.661   -9.620  1.00 22.14 ? 91  ALA D C   1 
ATOM   5505 O  O   . ALA D 1 96  ? 8.942   2.070   -10.197 1.00 20.97 ? 91  ALA D O   1 
ATOM   5506 C  CB  . ALA D 1 96  ? 8.135   -0.745  -8.932  1.00 21.45 ? 91  ALA D CB  1 
ATOM   5507 N  N   . TYR D 1 97  ? 7.114   2.412   -8.796  1.00 20.49 ? 92  TYR D N   1 
ATOM   5508 C  CA  . TYR D 1 97  ? 7.559   3.716   -8.234  1.00 21.71 ? 92  TYR D CA  1 
ATOM   5509 C  C   . TYR D 1 97  ? 8.991   3.599   -7.675  1.00 20.69 ? 92  TYR D C   1 
ATOM   5510 O  O   . TYR D 1 97  ? 9.360   2.583   -7.018  1.00 22.04 ? 92  TYR D O   1 
ATOM   5511 C  CB  . TYR D 1 97  ? 6.644   4.186   -7.116  1.00 23.67 ? 92  TYR D CB  1 
ATOM   5512 C  CG  . TYR D 1 97  ? 7.051   5.542   -6.604  1.00 24.23 ? 92  TYR D CG  1 
ATOM   5513 C  CD1 . TYR D 1 97  ? 6.848   6.663   -7.384  1.00 23.80 ? 92  TYR D CD1 1 
ATOM   5514 C  CD2 . TYR D 1 97  ? 7.634   5.711   -5.362  1.00 23.65 ? 92  TYR D CD2 1 
ATOM   5515 C  CE1 . TYR D 1 97  ? 7.251   7.915   -6.959  1.00 26.58 ? 92  TYR D CE1 1 
ATOM   5516 C  CE2 . TYR D 1 97  ? 8.017   6.968   -4.909  1.00 26.87 ? 92  TYR D CE2 1 
ATOM   5517 C  CZ  . TYR D 1 97  ? 7.825   8.083   -5.713  1.00 27.41 ? 92  TYR D CZ  1 
ATOM   5518 O  OH  . TYR D 1 97  ? 8.102   9.363   -5.307  1.00 20.68 ? 92  TYR D OH  1 
ATOM   5519 N  N   . VAL D 1 98  ? 9.812   4.604   -7.911  1.00 19.39 ? 93  VAL D N   1 
ATOM   5520 C  CA  . VAL D 1 98  ? 11.214  4.590   -7.395  1.00 20.55 ? 93  VAL D CA  1 
ATOM   5521 C  C   . VAL D 1 98  ? 11.401  5.788   -6.452  1.00 19.93 ? 93  VAL D C   1 
ATOM   5522 O  O   . VAL D 1 98  ? 11.493  6.959   -6.977  1.00 19.35 ? 93  VAL D O   1 
ATOM   5523 C  CB  . VAL D 1 98  ? 12.234  4.629   -8.537  1.00 19.72 ? 93  VAL D CB  1 
ATOM   5524 C  CG1 . VAL D 1 98  ? 13.666  4.657   -7.986  1.00 18.71 ? 93  VAL D CG1 1 
ATOM   5525 C  CG2 . VAL D 1 98  ? 12.009  3.483   -9.513  1.00 18.66 ? 93  VAL D CG2 1 
ATOM   5526 N  N   . SER D 1 99  ? 11.388  5.532   -5.144  1.00 17.72 ? 94  SER D N   1 
ATOM   5527 C  CA  . SER D 1 99  ? 11.621  6.565   -4.105  1.00 20.58 ? 94  SER D CA  1 
ATOM   5528 C  C   . SER D 1 99  ? 13.114  6.861   -4.085  1.00 23.25 ? 94  SER D C   1 
ATOM   5529 O  O   . SER D 1 99  ? 13.899  5.912   -4.127  1.00 21.47 ? 94  SER D O   1 
ATOM   5530 C  CB  . SER D 1 99  ? 11.142  6.111   -2.736  1.00 20.55 ? 94  SER D CB  1 
ATOM   5531 O  OG  . SER D 1 99  ? 11.388  7.108   -1.749  1.00 22.49 ? 94  SER D OG  1 
ATOM   5532 N  N   . PRO D 1 100 ? 13.520  8.153   -4.084  1.00 22.21 ? 95  PRO D N   1 
ATOM   5533 C  CA  . PRO D 1 100 ? 14.893  8.556   -3.830  1.00 24.69 ? 95  PRO D CA  1 
ATOM   5534 C  C   . PRO D 1 100 ? 15.450  8.118   -2.473  1.00 27.61 ? 95  PRO D C   1 
ATOM   5535 O  O   . PRO D 1 100 ? 16.661  7.977   -2.386  1.00 25.64 ? 95  PRO D O   1 
ATOM   5536 C  CB  . PRO D 1 100 ? 14.836  10.076  -3.823  1.00 23.09 ? 95  PRO D CB  1 
ATOM   5537 C  CG  . PRO D 1 100 ? 13.682  10.378  -4.721  1.00 22.91 ? 95  PRO D CG  1 
ATOM   5538 C  CD  . PRO D 1 100 ? 12.677  9.313   -4.379  1.00 23.92 ? 95  PRO D CD  1 
ATOM   5539 N  N   . ALA D 1 101 ? 14.566  7.840   -1.505  1.00 26.09 ? 96  ALA D N   1 
ATOM   5540 C  CA  . ALA D 1 101 ? 14.938  7.198   -0.225  1.00 26.66 ? 96  ALA D CA  1 
ATOM   5541 C  C   . ALA D 1 101 ? 15.764  5.938   -0.510  1.00 28.50 ? 96  ALA D C   1 
ATOM   5542 O  O   . ALA D 1 101 ? 16.762  5.725   0.182   1.00 33.99 ? 96  ALA D O   1 
ATOM   5543 C  CB  . ALA D 1 101 ? 13.718  6.925   0.607   1.00 27.81 ? 96  ALA D CB  1 
ATOM   5544 N  N   . VAL D 1 102 ? 15.448  5.202   -1.573  1.00 28.42 ? 97  VAL D N   1 
ATOM   5545 C  CA  . VAL D 1 102 ? 16.129  3.928   -1.929  1.00 25.30 ? 97  VAL D CA  1 
ATOM   5546 C  C   . VAL D 1 102 ? 17.557  4.266   -2.382  1.00 28.13 ? 97  VAL D C   1 
ATOM   5547 O  O   . VAL D 1 102 ? 18.477  3.519   -2.029  1.00 29.79 ? 97  VAL D O   1 
ATOM   5548 C  CB  . VAL D 1 102 ? 15.342  3.164   -3.012  1.00 27.41 ? 97  VAL D CB  1 
ATOM   5549 C  CG1 . VAL D 1 102 ? 16.119  1.960   -3.513  1.00 27.51 ? 97  VAL D CG1 1 
ATOM   5550 C  CG2 . VAL D 1 102 ? 13.925  2.770   -2.571  1.00 25.43 ? 97  VAL D CG2 1 
ATOM   5551 N  N   . TYR D 1 103 ? 17.725  5.345   -3.149  1.00 27.13 ? 98  TYR D N   1 
ATOM   5552 C  CA  . TYR D 1 103 ? 19.023  5.792   -3.722  1.00 28.24 ? 98  TYR D CA  1 
ATOM   5553 C  C   . TYR D 1 103 ? 20.039  6.065   -2.613  1.00 30.22 ? 98  TYR D C   1 
ATOM   5554 O  O   . TYR D 1 103 ? 21.245  5.831   -2.845  1.00 29.09 ? 98  TYR D O   1 
ATOM   5555 C  CB  . TYR D 1 103 ? 18.867  7.116   -4.469  1.00 26.88 ? 98  TYR D CB  1 
ATOM   5556 C  CG  . TYR D 1 103 ? 18.070  7.075   -5.743  1.00 29.07 ? 98  TYR D CG  1 
ATOM   5557 C  CD1 . TYR D 1 103 ? 17.750  5.881   -6.361  1.00 30.09 ? 98  TYR D CD1 1 
ATOM   5558 C  CD2 . TYR D 1 103 ? 17.720  8.251   -6.378  1.00 28.58 ? 98  TYR D CD2 1 
ATOM   5559 C  CE1 . TYR D 1 103 ? 17.051  5.856   -7.552  1.00 33.69 ? 98  TYR D CE1 1 
ATOM   5560 C  CE2 . TYR D 1 103 ? 17.025  8.244   -7.568  1.00 30.46 ? 98  TYR D CE2 1 
ATOM   5561 C  CZ  . TYR D 1 103 ? 16.673  7.045   -8.157  1.00 31.54 ? 98  TYR D CZ  1 
ATOM   5562 O  OH  . TYR D 1 103 ? 15.961  7.023   -9.331  1.00 29.39 ? 98  TYR D OH  1 
ATOM   5563 N  N   . ARG D 1 104 ? 19.546  6.671   -1.527  1.00 30.08 ? 99  ARG D N   1 
ATOM   5564 C  CA  . ARG D 1 104 ? 20.290  7.144   -0.329  1.00 35.75 ? 99  ARG D CA  1 
ATOM   5565 C  C   . ARG D 1 104 ? 21.217  8.306   -0.714  1.00 39.06 ? 99  ARG D C   1 
ATOM   5566 O  O   . ARG D 1 104 ? 22.187  8.551   0.015   1.00 39.14 ? 99  ARG D O   1 
ATOM   5567 C  CB  . ARG D 1 104 ? 21.068  5.998   0.322   1.00 36.10 ? 99  ARG D CB  1 
ATOM   5568 C  CG  . ARG D 1 104 ? 20.211  4.781   0.646   1.00 35.51 ? 99  ARG D CG  1 
ATOM   5569 C  CD  . ARG D 1 104 ? 20.688  4.093   1.907   1.00 35.74 ? 99  ARG D CD  1 
ATOM   5570 N  NE  . ARG D 1 104 ? 22.052  3.556   1.884   1.00 35.06 ? 99  ARG D NE  1 
ATOM   5571 C  CZ  . ARG D 1 104 ? 22.419  2.405   1.301   1.00 36.13 ? 99  ARG D CZ  1 
ATOM   5572 N  NH1 . ARG D 1 104 ? 21.537  1.669   0.633   1.00 33.80 ? 99  ARG D NH1 1 
ATOM   5573 N  NH2 . ARG D 1 104 ? 23.673  1.992   1.406   1.00 34.33 ? 99  ARG D NH2 1 
ATOM   5574 N  N   . THR D 1 105 ? 20.912  8.992   -1.813  1.00 37.58 ? 100 THR D N   1 
ATOM   5575 C  CA  . THR D 1 105 ? 21.741  10.071  -2.399  1.00 36.53 ? 100 THR D CA  1 
ATOM   5576 C  C   . THR D 1 105 ? 20.958  11.383  -2.346  1.00 35.29 ? 100 THR D C   1 
ATOM   5577 O  O   . THR D 1 105 ? 19.717  11.362  -2.127  1.00 34.14 ? 100 THR D O   1 
ATOM   5578 C  CB  . THR D 1 105 ? 22.143  9.776   -3.853  1.00 37.21 ? 100 THR D CB  1 
ATOM   5579 O  OG1 . THR D 1 105 ? 20.987  9.426   -4.631  1.00 34.30 ? 100 THR D OG1 1 
ATOM   5580 C  CG2 . THR D 1 105 ? 23.214  8.716   -3.962  1.00 37.21 ? 100 THR D CG2 1 
ATOM   5581 N  N   . ALA D 1 106 ? 21.668  12.479  -2.553  1.00 32.52 ? 101 ALA D N   1 
ATOM   5582 C  CA  . ALA D 1 106 ? 21.121  13.848  -2.522  1.00 33.97 ? 101 ALA D CA  1 
ATOM   5583 C  C   . ALA D 1 106 ? 22.018  14.719  -3.379  1.00 32.23 ? 101 ALA D C   1 
ATOM   5584 O  O   . ALA D 1 106 ? 23.226  14.592  -3.270  1.00 33.65 ? 101 ALA D O   1 
ATOM   5585 C  CB  . ALA D 1 106 ? 21.046  14.360  -1.097  1.00 35.36 ? 101 ALA D CB  1 
ATOM   5586 N  N   . PRO D 1 107 ? 21.471  15.584  -4.269  1.00 31.80 ? 102 PRO D N   1 
ATOM   5587 C  CA  . PRO D 1 107 ? 20.034  15.690  -4.465  1.00 29.95 ? 102 PRO D CA  1 
ATOM   5588 C  C   . PRO D 1 107 ? 19.569  14.580  -5.420  1.00 28.58 ? 102 PRO D C   1 
ATOM   5589 O  O   . PRO D 1 107 ? 20.418  13.926  -6.057  1.00 26.87 ? 102 PRO D O   1 
ATOM   5590 C  CB  . PRO D 1 107 ? 19.896  17.086  -5.084  1.00 30.54 ? 102 PRO D CB  1 
ATOM   5591 C  CG  . PRO D 1 107 ? 21.120  17.173  -5.982  1.00 31.51 ? 102 PRO D CG  1 
ATOM   5592 C  CD  . PRO D 1 107 ? 22.210  16.464  -5.196  1.00 31.20 ? 102 PRO D CD  1 
ATOM   5593 N  N   . ALA D 1 108 ? 18.250  14.440  -5.579  1.00 25.15 ? 103 ALA D N   1 
ATOM   5594 C  CA  . ALA D 1 108 ? 17.662  13.407  -6.452  1.00 25.77 ? 103 ALA D CA  1 
ATOM   5595 C  C   . ALA D 1 108 ? 16.254  13.812  -6.842  1.00 25.68 ? 103 ALA D C   1 
ATOM   5596 O  O   . ALA D 1 108 ? 15.703  14.715  -6.202  1.00 25.48 ? 103 ALA D O   1 
ATOM   5597 C  CB  . ALA D 1 108 ? 17.632  12.081  -5.741  1.00 24.22 ? 103 ALA D CB  1 
ATOM   5598 N  N   . ALA D 1 109 ? 15.670  13.089  -7.792  1.00 25.93 ? 104 ALA D N   1 
ATOM   5599 C  CA  . ALA D 1 109 ? 14.213  13.146  -8.048  1.00 27.92 ? 104 ALA D CA  1 
ATOM   5600 C  C   . ALA D 1 109 ? 13.675  11.728  -8.185  1.00 26.52 ? 104 ALA D C   1 
ATOM   5601 O  O   . ALA D 1 109 ? 14.403  10.815  -8.580  1.00 27.22 ? 104 ALA D O   1 
ATOM   5602 C  CB  . ALA D 1 109 ? 13.933  13.970  -9.272  1.00 27.25 ? 104 ALA D CB  1 
ATOM   5603 N  N   . PRO D 1 110 ? 12.380  11.497  -7.888  1.00 23.32 ? 105 PRO D N   1 
ATOM   5604 C  CA  . PRO D 1 110 ? 11.839  10.155  -7.952  1.00 25.99 ? 105 PRO D CA  1 
ATOM   5605 C  C   . PRO D 1 110 ? 11.531  9.843   -9.413  1.00 26.22 ? 105 PRO D C   1 
ATOM   5606 O  O   . PRO D 1 110 ? 11.512  10.748  -10.225 1.00 28.44 ? 105 PRO D O   1 
ATOM   5607 C  CB  . PRO D 1 110 ? 10.553  10.235  -7.120  1.00 25.66 ? 105 PRO D CB  1 
ATOM   5608 C  CG  . PRO D 1 110 ? 10.601  11.603  -6.468  1.00 24.20 ? 105 PRO D CG  1 
ATOM   5609 C  CD  . PRO D 1 110 ? 11.372  12.454  -7.439  1.00 23.06 ? 105 PRO D CD  1 
ATOM   5610 N  N   . THR D 1 111 ? 11.278  8.578   -9.722  1.00 24.59 ? 106 THR D N   1 
ATOM   5611 C  CA  . THR D 1 111 ? 10.845  8.183   -11.069 1.00 22.93 ? 106 THR D CA  1 
ATOM   5612 C  C   . THR D 1 111 ? 9.929   6.989   -10.898 1.00 22.26 ? 106 THR D C   1 
ATOM   5613 O  O   . THR D 1 111 ? 9.584   6.647   -9.736  1.00 21.60 ? 106 THR D O   1 
ATOM   5614 C  CB  . THR D 1 111 ? 12.043  7.906   -11.988 1.00 26.49 ? 106 THR D CB  1 
ATOM   5615 O  OG1 . THR D 1 111 ? 11.543  7.930   -13.325 1.00 27.83 ? 106 THR D OG1 1 
ATOM   5616 C  CG2 . THR D 1 111 ? 12.731  6.581   -11.713 1.00 22.95 ? 106 THR D CG2 1 
ATOM   5617 N  N   . TRP D 1 112 ? 9.581   6.396   -12.027 1.00 22.10 ? 107 TRP D N   1 
ATOM   5618 C  CA  . TRP D 1 112 ? 8.737   5.189   -12.132 1.00 23.03 ? 107 TRP D CA  1 
ATOM   5619 C  C   . TRP D 1 112 ? 9.440   4.278   -13.112 1.00 24.07 ? 107 TRP D C   1 
ATOM   5620 O  O   . TRP D 1 112 ? 9.506   4.678   -14.281 1.00 24.91 ? 107 TRP D O   1 
ATOM   5621 C  CB  . TRP D 1 112 ? 7.313   5.521   -12.596 1.00 21.78 ? 107 TRP D CB  1 
ATOM   5622 C  CG  . TRP D 1 112 ? 6.326   4.493   -12.122 1.00 21.36 ? 107 TRP D CG  1 
ATOM   5623 C  CD1 . TRP D 1 112 ? 6.262   3.191   -12.522 1.00 21.26 ? 107 TRP D CD1 1 
ATOM   5624 C  CD2 . TRP D 1 112 ? 5.287   4.660   -11.140 1.00 21.26 ? 107 TRP D CD2 1 
ATOM   5625 N  NE1 . TRP D 1 112 ? 5.252   2.541   -11.867 1.00 21.39 ? 107 TRP D NE1 1 
ATOM   5626 C  CE2 . TRP D 1 112 ? 4.644   3.410   -11.005 1.00 20.69 ? 107 TRP D CE2 1 
ATOM   5627 C  CE3 . TRP D 1 112 ? 4.823   5.741   -10.376 1.00 22.07 ? 107 TRP D CE3 1 
ATOM   5628 C  CZ2 . TRP D 1 112 ? 3.586   3.207   -10.127 1.00 20.81 ? 107 TRP D CZ2 1 
ATOM   5629 C  CZ3 . TRP D 1 112 ? 3.786   5.541   -9.493  1.00 20.43 ? 107 TRP D CZ3 1 
ATOM   5630 C  CH2 . TRP D 1 112 ? 3.181   4.290   -9.372  1.00 21.49 ? 107 TRP D CH2 1 
ATOM   5631 N  N   . ASN D 1 113 ? 9.982   3.160   -12.639 1.00 22.99 ? 108 ASN D N   1 
ATOM   5632 C  CA  . ASN D 1 113 ? 10.616  2.143   -13.506 1.00 20.97 ? 108 ASN D CA  1 
ATOM   5633 C  C   . ASN D 1 113 ? 9.463   1.393   -14.176 1.00 22.99 ? 108 ASN D C   1 
ATOM   5634 O  O   . ASN D 1 113 ? 8.474   1.070   -13.464 1.00 27.25 ? 108 ASN D O   1 
ATOM   5635 C  CB  . ASN D 1 113 ? 11.574  1.281   -12.690 1.00 19.54 ? 108 ASN D CB  1 
ATOM   5636 C  CG  . ASN D 1 113 ? 12.953  1.900   -12.556 1.00 22.47 ? 108 ASN D CG  1 
ATOM   5637 O  OD1 . ASN D 1 113 ? 13.196  3.032   -12.974 1.00 24.35 ? 108 ASN D OD1 1 
ATOM   5638 N  ND2 . ASN D 1 113 ? 13.867  1.157   -11.980 1.00 19.57 ? 108 ASN D ND2 1 
ATOM   5639 N  N   . PHE D 1 114 ? 9.523   1.182   -15.481 1.00 21.23 ? 109 PHE D N   1 
ATOM   5640 C  CA  . PHE D 1 114 ? 8.427   0.532   -16.224 1.00 21.64 ? 109 PHE D CA  1 
ATOM   5641 C  C   . PHE D 1 114 ? 8.951   0.005   -17.556 1.00 22.06 ? 109 PHE D C   1 
ATOM   5642 O  O   . PHE D 1 114 ? 10.009  0.424   -18.071 1.00 21.33 ? 109 PHE D O   1 
ATOM   5643 C  CB  . PHE D 1 114 ? 7.237   1.489   -16.406 1.00 21.14 ? 109 PHE D CB  1 
ATOM   5644 C  CG  . PHE D 1 114 ? 7.396   2.520   -17.495 1.00 19.23 ? 109 PHE D CG  1 
ATOM   5645 C  CD1 . PHE D 1 114 ? 8.007   3.737   -17.235 1.00 21.33 ? 109 PHE D CD1 1 
ATOM   5646 C  CD2 . PHE D 1 114 ? 6.945   2.276   -18.784 1.00 21.78 ? 109 PHE D CD2 1 
ATOM   5647 C  CE1 . PHE D 1 114 ? 8.167   4.690   -18.238 1.00 23.21 ? 109 PHE D CE1 1 
ATOM   5648 C  CE2 . PHE D 1 114 ? 7.087   3.241   -19.779 1.00 22.64 ? 109 PHE D CE2 1 
ATOM   5649 C  CZ  . PHE D 1 114 ? 7.697   4.447   -19.505 1.00 22.04 ? 109 PHE D CZ  1 
ATOM   5650 N  N   . THR D 1 115 ? 8.199   -0.951  -18.083 1.00 21.82 ? 110 THR D N   1 
ATOM   5651 C  CA  . THR D 1 115 ? 8.469   -1.635  -19.360 1.00 21.16 ? 110 THR D CA  1 
ATOM   5652 C  C   . THR D 1 115 ? 7.234   -1.448  -20.232 1.00 23.10 ? 110 THR D C   1 
ATOM   5653 O  O   . THR D 1 115 ? 6.093   -1.599  -19.703 1.00 18.76 ? 110 THR D O   1 
ATOM   5654 C  CB  . THR D 1 115 ? 8.788   -3.109  -19.110 1.00 23.45 ? 110 THR D CB  1 
ATOM   5655 O  OG1 . THR D 1 115 ? 7.674   -3.616  -18.372 1.00 24.96 ? 110 THR D OG1 1 
ATOM   5656 C  CG2 . THR D 1 115 ? 10.077  -3.309  -18.352 1.00 24.10 ? 110 THR D CG2 1 
ATOM   5657 N  N   . SER D 1 116 ? 7.427   -1.091  -21.495 1.00 22.10 ? 111 SER D N   1 
ATOM   5658 C  CA  . SER D 1 116 ? 6.304   -0.977  -22.463 1.00 25.33 ? 111 SER D CA  1 
ATOM   5659 C  C   . SER D 1 116 ? 6.807   -1.420  -23.829 1.00 22.70 ? 111 SER D C   1 
ATOM   5660 O  O   . SER D 1 116 ? 7.974   -1.100  -24.146 1.00 25.29 ? 111 SER D O   1 
ATOM   5661 C  CB  . SER D 1 116 ? 5.773   0.442   -22.559 1.00 25.52 ? 111 SER D CB  1 
ATOM   5662 O  OG  . SER D 1 116 ? 6.845   1.278   -22.991 1.00 30.43 ? 111 SER D OG  1 
ATOM   5663 N  N   . VAL D 1 117 ? 5.942   -2.035  -24.623 1.00 20.16 ? 112 VAL D N   1 
ATOM   5664 C  CA  . VAL D 1 117 ? 6.198   -2.292  -26.061 1.00 20.36 ? 112 VAL D CA  1 
ATOM   5665 C  C   . VAL D 1 117 ? 5.024   -1.692  -26.808 1.00 21.99 ? 112 VAL D C   1 
ATOM   5666 O  O   . VAL D 1 117 ? 3.862   -2.009  -26.433 1.00 24.76 ? 112 VAL D O   1 
ATOM   5667 C  CB  . VAL D 1 117 ? 6.366   -3.784  -26.370 1.00 20.70 ? 112 VAL D CB  1 
ATOM   5668 C  CG1 . VAL D 1 117 ? 6.296   -4.080  -27.864 1.00 21.66 ? 112 VAL D CG1 1 
ATOM   5669 C  CG2 . VAL D 1 117 ? 7.655   -4.333  -25.774 1.00 22.40 ? 112 VAL D CG2 1 
ATOM   5670 N  N   . GLN D 1 118 ? 5.330   -0.876  -27.813 1.00 22.46 ? 113 GLN D N   1 
ATOM   5671 C  CA  . GLN D 1 118 ? 4.344   -0.306  -28.764 1.00 23.32 ? 113 GLN D CA  1 
ATOM   5672 C  C   . GLN D 1 118 ? 4.568   -0.905  -30.162 1.00 21.03 ? 113 GLN D C   1 
ATOM   5673 O  O   . GLN D 1 118 ? 5.636   -0.720  -30.729 1.00 23.64 ? 113 GLN D O   1 
ATOM   5674 C  CB  . GLN D 1 118 ? 4.478   1.218   -28.740 1.00 23.68 ? 113 GLN D CB  1 
ATOM   5675 C  CG  . GLN D 1 118 ? 3.992   1.827   -27.434 1.00 23.11 ? 113 GLN D CG  1 
ATOM   5676 C  CD  . GLN D 1 118 ? 4.211   3.306   -27.352 1.00 22.69 ? 113 GLN D CD  1 
ATOM   5677 O  OE1 . GLN D 1 118 ? 4.198   3.997   -28.350 1.00 22.89 ? 113 GLN D OE1 1 
ATOM   5678 N  NE2 . GLN D 1 118 ? 4.338   3.803   -26.140 1.00 26.01 ? 113 GLN D NE2 1 
ATOM   5679 N  N   . VAL D 1 119 ? 3.595   -1.608  -30.710 1.00 21.68 ? 114 VAL D N   1 
ATOM   5680 C  CA  . VAL D 1 119 ? 3.724   -2.155  -32.082 1.00 24.20 ? 114 VAL D CA  1 
ATOM   5681 C  C   . VAL D 1 119 ? 2.766   -1.346  -32.938 1.00 24.42 ? 114 VAL D C   1 
ATOM   5682 O  O   . VAL D 1 119 ? 1.685   -1.053  -32.432 1.00 26.93 ? 114 VAL D O   1 
ATOM   5683 C  CB  . VAL D 1 119 ? 3.445   -3.666  -32.166 1.00 26.38 ? 114 VAL D CB  1 
ATOM   5684 C  CG1 . VAL D 1 119 ? 4.502   -4.457  -31.408 1.00 26.00 ? 114 VAL D CG1 1 
ATOM   5685 C  CG2 . VAL D 1 119 ? 2.030   -4.011  -31.716 1.00 27.09 ? 114 VAL D CG2 1 
ATOM   5686 N  N   . ARG D 1 120 ? 3.174   -0.999  -34.157 1.00 25.28 ? 115 ARG D N   1 
ATOM   5687 C  CA  . ARG D 1 120 ? 2.282   -0.302  -35.118 1.00 27.19 ? 115 ARG D CA  1 
ATOM   5688 C  C   . ARG D 1 120 ? 2.290   -1.040  -36.451 1.00 26.87 ? 115 ARG D C   1 
ATOM   5689 O  O   . ARG D 1 120 ? 3.353   -1.595  -36.856 1.00 24.25 ? 115 ARG D O   1 
ATOM   5690 C  CB  . ARG D 1 120 ? 2.693   1.152   -35.307 1.00 29.69 ? 115 ARG D CB  1 
ATOM   5691 C  CG  . ARG D 1 120 ? 2.672   1.974   -34.026 1.00 30.49 ? 115 ARG D CG  1 
ATOM   5692 C  CD  . ARG D 1 120 ? 3.143   3.392   -34.274 1.00 30.73 ? 115 ARG D CD  1 
ATOM   5693 N  NE  . ARG D 1 120 ? 2.578   4.284   -33.274 1.00 31.07 ? 115 ARG D NE  1 
ATOM   5694 C  CZ  . ARG D 1 120 ? 3.045   4.442   -32.049 1.00 31.00 ? 115 ARG D CZ  1 
ATOM   5695 N  NH1 . ARG D 1 120 ? 4.124   3.785   -31.636 1.00 32.24 ? 115 ARG D NH1 1 
ATOM   5696 N  NH2 . ARG D 1 120 ? 2.439   5.285   -31.245 1.00 29.88 ? 115 ARG D NH2 1 
ATOM   5697 N  N   . GLY D 1 121 ? 1.132   -1.022  -37.090 1.00 23.83 ? 116 GLY D N   1 
ATOM   5698 C  CA  . GLY D 1 121 ? 0.937   -1.472  -38.473 1.00 26.62 ? 116 GLY D CA  1 
ATOM   5699 C  C   . GLY D 1 121 ? -0.523  -1.392  -38.799 1.00 30.81 ? 116 GLY D C   1 
ATOM   5700 O  O   . GLY D 1 121 ? -1.266  -0.697  -38.028 1.00 29.94 ? 116 GLY D O   1 
ATOM   5701 N  N   . GLU D 1 122 ? -0.960  -2.056  -39.858 1.00 30.19 ? 117 GLU D N   1 
ATOM   5702 C  CA  . GLU D 1 122 ? -2.359  -1.850  -40.306 1.00 36.91 ? 117 GLU D CA  1 
ATOM   5703 C  C   . GLU D 1 122 ? -3.179  -2.997  -39.724 1.00 34.80 ? 117 GLU D C   1 
ATOM   5704 O  O   . GLU D 1 122 ? -2.735  -4.140  -39.822 1.00 36.14 ? 117 GLU D O   1 
ATOM   5705 C  CB  . GLU D 1 122 ? -2.417  -1.607  -41.815 1.00 41.91 ? 117 GLU D CB  1 
ATOM   5706 C  CG  . GLU D 1 122 ? -2.339  -2.835  -42.688 1.00 52.36 ? 117 GLU D CG  1 
ATOM   5707 C  CD  . GLU D 1 122 ? -2.729  -2.522  -44.128 1.00 57.82 ? 117 GLU D CD  1 
ATOM   5708 O  OE1 . GLU D 1 122 ? -3.374  -3.390  -44.775 1.00 63.84 ? 117 GLU D OE1 1 
ATOM   5709 O  OE2 . GLU D 1 122 ? -2.422  -1.388  -44.586 1.00 54.04 ? 117 GLU D OE2 1 
ATOM   5710 N  N   . LEU D 1 123 ? -4.252  -2.682  -39.002 1.00 33.88 ? 118 LEU D N   1 
ATOM   5711 C  CA  . LEU D 1 123 ? -5.163  -3.735  -38.512 1.00 33.57 ? 118 LEU D CA  1 
ATOM   5712 C  C   . LEU D 1 123 ? -5.975  -4.227  -39.709 1.00 35.08 ? 118 LEU D C   1 
ATOM   5713 O  O   . LEU D 1 123 ? -6.572  -3.370  -40.401 1.00 37.10 ? 118 LEU D O   1 
ATOM   5714 C  CB  . LEU D 1 123 ? -6.057  -3.182  -37.411 1.00 32.90 ? 118 LEU D CB  1 
ATOM   5715 C  CG  . LEU D 1 123 ? -6.936  -4.222  -36.714 1.00 34.14 ? 118 LEU D CG  1 
ATOM   5716 C  CD1 . LEU D 1 123 ? -7.063  -3.908  -35.228 1.00 34.60 ? 118 LEU D CD1 1 
ATOM   5717 C  CD2 . LEU D 1 123 ? -8.331  -4.290  -37.350 1.00 36.81 ? 118 LEU D CD2 1 
ATOM   5718 N  N   . ARG D 1 124 ? -5.977  -5.543  -39.939 1.00 35.04 ? 119 ARG D N   1 
ATOM   5719 C  CA  . ARG D 1 124 ? -6.801  -6.219  -40.970 1.00 37.70 ? 119 ARG D CA  1 
ATOM   5720 C  C   . ARG D 1 124 ? -7.869  -7.044  -40.257 1.00 33.36 ? 119 ARG D C   1 
ATOM   5721 O  O   . ARG D 1 124 ? -7.489  -7.955  -39.556 1.00 31.74 ? 119 ARG D O   1 
ATOM   5722 C  CB  . ARG D 1 124 ? -5.914  -7.101  -41.851 1.00 44.17 ? 119 ARG D CB  1 
ATOM   5723 C  CG  . ARG D 1 124 ? -6.695  -8.062  -42.740 1.00 53.57 ? 119 ARG D CG  1 
ATOM   5724 C  CD  . ARG D 1 124 ? -5.838  -8.772  -43.776 1.00 57.11 ? 119 ARG D CD  1 
ATOM   5725 N  NE  . ARG D 1 124 ? -5.334  -10.074 -43.355 1.00 56.52 ? 119 ARG D NE  1 
ATOM   5726 C  CZ  . ARG D 1 124 ? -4.189  -10.287 -42.696 1.00 59.32 ? 119 ARG D CZ  1 
ATOM   5727 N  NH1 . ARG D 1 124 ? -3.418  -9.273  -42.329 1.00 61.25 ? 119 ARG D NH1 1 
ATOM   5728 N  NH2 . ARG D 1 124 ? -3.815  -11.524 -42.401 1.00 56.96 ? 119 ARG D NH2 1 
ATOM   5729 N  N   . LYS D 1 125 ? -9.155  -6.735  -40.436 1.00 35.11 ? 120 LYS D N   1 
ATOM   5730 C  CA  . LYS D 1 125 ? -10.263 -7.475  -39.777 1.00 32.84 ? 120 LYS D CA  1 
ATOM   5731 C  C   . LYS D 1 125 ? -10.345 -8.867  -40.419 1.00 38.85 ? 120 LYS D C   1 
ATOM   5732 O  O   . LYS D 1 125 ? -10.013 -8.996  -41.616 1.00 37.55 ? 120 LYS D O   1 
ATOM   5733 C  CB  . LYS D 1 125 ? -11.576 -6.700  -39.894 1.00 32.02 ? 120 LYS D CB  1 
ATOM   5734 C  CG  . LYS D 1 125 ? -11.617 -5.350  -39.198 1.00 33.05 ? 120 LYS D CG  1 
ATOM   5735 C  CD  . LYS D 1 125 ? -12.847 -4.557  -39.603 1.00 36.09 ? 120 LYS D CD  1 
ATOM   5736 C  CE  . LYS D 1 125 ? -13.114 -3.353  -38.736 1.00 36.75 ? 120 LYS D CE  1 
ATOM   5737 N  NZ  . LYS D 1 125 ? -14.514 -2.895  -38.878 1.00 36.84 ? 120 LYS D NZ  1 
ATOM   5738 N  N   . VAL D 1 126 ? -10.692 -9.882  -39.620 1.00 40.81 ? 121 VAL D N   1 
ATOM   5739 C  CA  . VAL D 1 126 ? -11.017 -11.265 -40.067 1.00 40.90 ? 121 VAL D CA  1 
ATOM   5740 C  C   . VAL D 1 126 ? -12.548 -11.397 -40.134 1.00 41.27 ? 121 VAL D C   1 
ATOM   5741 O  O   . VAL D 1 126 ? -13.179 -11.268 -39.072 1.00 44.76 ? 121 VAL D O   1 
ATOM   5742 C  CB  . VAL D 1 126 ? -10.427 -12.270 -39.065 1.00 43.02 ? 121 VAL D CB  1 
ATOM   5743 C  CG1 . VAL D 1 126 ? -10.851 -13.676 -39.409 1.00 43.84 ? 121 VAL D CG1 1 
ATOM   5744 C  CG2 . VAL D 1 126 ? -8.911  -12.163 -38.939 1.00 39.37 ? 121 VAL D CG2 1 
ATOM   5745 N  N   . GLU D 1 127 ? -13.140 -11.662 -41.300 1.00 39.58 ? 122 GLU D N   1 
ATOM   5746 C  CA  . GLU D 1 127 ? -14.623 -11.730 -41.417 1.00 44.26 ? 122 GLU D CA  1 
ATOM   5747 C  C   . GLU D 1 127 ? -15.118 -13.173 -41.603 1.00 49.33 ? 122 GLU D C   1 
ATOM   5748 O  O   . GLU D 1 127 ? -16.340 -13.364 -41.483 1.00 57.21 ? 122 GLU D O   1 
ATOM   5749 C  CB  . GLU D 1 127 ? -15.125 -10.816 -42.537 1.00 46.73 ? 122 GLU D CB  1 
ATOM   5750 C  CG  . GLU D 1 127 ? -14.872 -9.334  -42.285 1.00 45.49 ? 122 GLU D CG  1 
ATOM   5751 C  CD  . GLU D 1 127 ? -15.651 -8.704  -41.141 1.00 46.66 ? 122 GLU D CD  1 
ATOM   5752 O  OE1 . GLU D 1 127 ? -16.518 -9.385  -40.557 1.00 50.35 ? 122 GLU D OE1 1 
ATOM   5753 O  OE2 . GLU D 1 127 ? -15.376 -7.531  -40.824 1.00 54.09 ? 122 GLU D OE2 1 
ATOM   5754 N  N   . SER D 1 128 ? -14.246 -14.148 -41.878 1.00 45.02 ? 123 SER D N   1 
ATOM   5755 C  CA  . SER D 1 128 ? -14.630 -15.584 -41.948 1.00 44.66 ? 123 SER D CA  1 
ATOM   5756 C  C   . SER D 1 128 ? -14.716 -16.159 -40.534 1.00 42.97 ? 123 SER D C   1 
ATOM   5757 O  O   . SER D 1 128 ? -13.780 -15.920 -39.736 1.00 37.20 ? 123 SER D O   1 
ATOM   5758 C  CB  . SER D 1 128 ? -13.671 -16.388 -42.765 1.00 48.49 ? 123 SER D CB  1 
ATOM   5759 O  OG  . SER D 1 128 ? -12.708 -16.991 -41.915 1.00 53.90 ? 123 SER D OG  1 
ATOM   5760 N  N   . ALA D 1 129 ? -15.787 -16.901 -40.259 1.00 39.13 ? 124 ALA D N   1 
ATOM   5761 C  CA  . ALA D 1 129 ? -16.041 -17.576 -38.970 1.00 43.80 ? 124 ALA D CA  1 
ATOM   5762 C  C   . ALA D 1 129 ? -14.938 -18.604 -38.701 1.00 38.91 ? 124 ALA D C   1 
ATOM   5763 O  O   . ALA D 1 129 ? -14.683 -18.876 -37.531 1.00 39.58 ? 124 ALA D O   1 
ATOM   5764 C  CB  . ALA D 1 129 ? -17.401 -18.237 -38.968 1.00 43.37 ? 124 ALA D CB  1 
ATOM   5765 N  N   . ASP D 1 130 ? -14.362 -19.199 -39.736 1.00 34.95 ? 125 ASP D N   1 
ATOM   5766 C  CA  . ASP D 1 130 ? -13.291 -20.224 -39.577 1.00 41.12 ? 125 ASP D CA  1 
ATOM   5767 C  C   . ASP D 1 130 ? -12.078 -19.528 -38.944 1.00 36.03 ? 125 ASP D C   1 
ATOM   5768 O  O   . ASP D 1 130 ? -11.532 -20.052 -37.951 1.00 38.96 ? 125 ASP D O   1 
ATOM   5769 C  CB  . ASP D 1 130 ? -12.970 -20.891 -40.922 1.00 47.21 ? 125 ASP D CB  1 
ATOM   5770 C  CG  . ASP D 1 130 ? -11.913 -21.995 -40.898 1.00 58.68 ? 125 ASP D CG  1 
ATOM   5771 O  OD1 . ASP D 1 130 ? -11.344 -22.290 -41.994 1.00 66.13 ? 125 ASP D OD1 1 
ATOM   5772 O  OD2 . ASP D 1 130 ? -11.653 -22.572 -39.804 1.00 66.57 ? 125 ASP D OD2 1 
ATOM   5773 N  N   . ASP D 1 131 ? -11.696 -18.370 -39.483 1.00 35.33 ? 126 ASP D N   1 
ATOM   5774 C  CA  . ASP D 1 131 ? -10.523 -17.580 -39.015 1.00 38.48 ? 126 ASP D CA  1 
ATOM   5775 C  C   . ASP D 1 131 ? -10.798 -16.940 -37.650 1.00 32.49 ? 126 ASP D C   1 
ATOM   5776 O  O   . ASP D 1 131 ? -9.793  -16.688 -36.907 1.00 32.81 ? 126 ASP D O   1 
ATOM   5777 C  CB  . ASP D 1 131 ? -10.158 -16.493 -40.012 1.00 38.67 ? 126 ASP D CB  1 
ATOM   5778 C  CG  . ASP D 1 131 ? -9.637  -17.038 -41.318 1.00 42.25 ? 126 ASP D CG  1 
ATOM   5779 O  OD1 . ASP D 1 131 ? -9.993  -16.448 -42.364 1.00 38.25 ? 126 ASP D OD1 1 
ATOM   5780 O  OD2 . ASP D 1 131 ? -8.898  -18.047 -41.270 1.00 45.73 ? 126 ASP D OD2 1 
ATOM   5781 N  N   . THR D 1 132 ? -12.072 -16.674 -37.344 1.00 29.16 ? 127 THR D N   1 
ATOM   5782 C  CA  . THR D 1 132 ? -12.531 -16.091 -36.056 1.00 26.44 ? 127 THR D CA  1 
ATOM   5783 C  C   . THR D 1 132 ? -12.366 -17.166 -34.988 1.00 28.08 ? 127 THR D C   1 
ATOM   5784 O  O   . THR D 1 132 ? -11.720 -16.915 -33.951 1.00 26.43 ? 127 THR D O   1 
ATOM   5785 C  CB  . THR D 1 132 ? -13.980 -15.585 -36.158 1.00 27.99 ? 127 THR D CB  1 
ATOM   5786 O  OG1 . THR D 1 132 ? -14.082 -14.499 -37.078 1.00 25.96 ? 127 THR D OG1 1 
ATOM   5787 C  CG2 . THR D 1 132 ? -14.492 -15.074 -34.833 1.00 29.76 ? 127 THR D CG2 1 
ATOM   5788 N  N   . LEU D 1 133 ? -12.870 -18.364 -35.274 1.00 24.47 ? 128 LEU D N   1 
ATOM   5789 C  CA  . LEU D 1 133 ? -12.715 -19.523 -34.370 1.00 27.43 ? 128 LEU D CA  1 
ATOM   5790 C  C   . LEU D 1 133 ? -11.225 -19.832 -34.164 1.00 24.11 ? 128 LEU D C   1 
ATOM   5791 O  O   . LEU D 1 133 ? -10.808 -19.944 -33.012 1.00 25.76 ? 128 LEU D O   1 
ATOM   5792 C  CB  . LEU D 1 133 ? -13.484 -20.706 -34.950 1.00 28.94 ? 128 LEU D CB  1 
ATOM   5793 C  CG  . LEU D 1 133 ? -13.623 -21.914 -34.035 1.00 28.59 ? 128 LEU D CG  1 
ATOM   5794 C  CD1 . LEU D 1 133 ? -14.426 -21.576 -32.788 1.00 28.53 ? 128 LEU D CD1 1 
ATOM   5795 C  CD2 . LEU D 1 133 ? -14.266 -23.055 -34.802 1.00 28.22 ? 128 LEU D CD2 1 
ATOM   5796 N  N   . ALA D 1 134 ? -10.434 -19.938 -35.212 1.00 23.52 ? 129 ALA D N   1 
ATOM   5797 C  CA  . ALA D 1 134 ? -8.954  -20.091 -35.084 1.00 25.55 ? 129 ALA D CA  1 
ATOM   5798 C  C   . ALA D 1 134 ? -8.373  -19.073 -34.093 1.00 28.14 ? 129 ALA D C   1 
ATOM   5799 O  O   . ALA D 1 134 ? -7.483  -19.473 -33.304 1.00 27.22 ? 129 ALA D O   1 
ATOM   5800 C  CB  . ALA D 1 134 ? -8.269  -19.927 -36.408 1.00 24.42 ? 129 ALA D CB  1 
ATOM   5801 N  N   . THR D 1 135 ? -8.807  -17.799 -34.160 1.00 26.73 ? 130 THR D N   1 
ATOM   5802 C  CA  . THR D 1 135 ? -8.240  -16.723 -33.319 1.00 23.97 ? 130 THR D CA  1 
ATOM   5803 C  C   . THR D 1 135 ? -8.488  -17.046 -31.845 1.00 25.24 ? 130 THR D C   1 
ATOM   5804 O  O   . THR D 1 135 ? -7.495  -16.951 -31.054 1.00 25.11 ? 130 THR D O   1 
ATOM   5805 C  CB  . THR D 1 135 ? -8.769  -15.337 -33.666 1.00 22.65 ? 130 THR D CB  1 
ATOM   5806 O  OG1 . THR D 1 135 ? -8.461  -15.139 -35.039 1.00 21.40 ? 130 THR D OG1 1 
ATOM   5807 C  CG2 . THR D 1 135 ? -8.134  -14.242 -32.819 1.00 21.27 ? 130 THR D CG2 1 
ATOM   5808 N  N   . VAL D 1 136 ? -9.732  -17.395 -31.482 1.00 23.12 ? 131 VAL D N   1 
ATOM   5809 C  CA  . VAL D 1 136 ? -10.125 -17.584 -30.053 1.00 23.60 ? 131 VAL D CA  1 
ATOM   5810 C  C   . VAL D 1 136 ? -9.544  -18.904 -29.509 1.00 23.50 ? 131 VAL D C   1 
ATOM   5811 O  O   . VAL D 1 136 ? -9.107  -18.858 -28.361 1.00 23.04 ? 131 VAL D O   1 
ATOM   5812 C  CB  . VAL D 1 136 ? -11.643 -17.471 -29.798 1.00 26.44 ? 131 VAL D CB  1 
ATOM   5813 C  CG1 . VAL D 1 136 ? -12.201 -16.108 -30.166 1.00 27.07 ? 131 VAL D CG1 1 
ATOM   5814 C  CG2 . VAL D 1 136 ? -12.432 -18.569 -30.460 1.00 26.38 ? 131 VAL D CG2 1 
ATOM   5815 N  N   . ARG D 1 137 ? -9.526  -20.004 -30.287 1.00 19.83 ? 132 ARG D N   1 
ATOM   5816 C  CA  . ARG D 1 137 ? -8.849  -21.279 -29.927 1.00 21.89 ? 132 ARG D CA  1 
ATOM   5817 C  C   . ARG D 1 137 ? -7.331  -21.064 -29.739 1.00 22.74 ? 132 ARG D C   1 
ATOM   5818 O  O   . ARG D 1 137 ? -6.764  -21.672 -28.815 1.00 24.85 ? 132 ARG D O   1 
ATOM   5819 C  CB  . ARG D 1 137 ? -9.167  -22.368 -30.966 1.00 21.34 ? 132 ARG D CB  1 
ATOM   5820 C  CG  . ARG D 1 137 ? -10.659 -22.680 -30.961 1.00 22.86 ? 132 ARG D CG  1 
ATOM   5821 C  CD  . ARG D 1 137 ? -11.067 -23.921 -31.693 1.00 23.38 ? 132 ARG D CD  1 
ATOM   5822 N  NE  . ARG D 1 137 ? -10.515 -24.110 -33.025 1.00 22.17 ? 132 ARG D NE  1 
ATOM   5823 C  CZ  . ARG D 1 137 ? -10.920 -25.063 -33.854 1.00 25.72 ? 132 ARG D CZ  1 
ATOM   5824 N  NH1 . ARG D 1 137 ? -11.948 -25.838 -33.527 1.00 27.30 ? 132 ARG D NH1 1 
ATOM   5825 N  NH2 . ARG D 1 137 ? -10.328 -25.210 -35.025 1.00 24.33 ? 132 ARG D NH2 1 
ATOM   5826 N  N   . ALA D 1 138 ? -6.692  -20.266 -30.587 1.00 21.46 ? 133 ALA D N   1 
ATOM   5827 C  CA  . ALA D 1 138 ? -5.229  -20.024 -30.552 1.00 22.06 ? 133 ALA D CA  1 
ATOM   5828 C  C   . ALA D 1 138 ? -4.938  -19.230 -29.293 1.00 23.42 ? 133 ALA D C   1 
ATOM   5829 O  O   . ALA D 1 138 ? -3.962  -19.547 -28.567 1.00 21.57 ? 133 ALA D O   1 
ATOM   5830 C  CB  . ALA D 1 138 ? -4.763  -19.306 -31.791 1.00 20.27 ? 133 ALA D CB  1 
ATOM   5831 N  N   . THR D 1 139 ? -5.813  -18.269 -29.010 1.00 22.83 ? 134 THR D N   1 
ATOM   5832 C  CA  . THR D 1 139 ? -5.678  -17.418 -27.803 1.00 23.26 ? 134 THR D CA  1 
ATOM   5833 C  C   . THR D 1 139 ? -5.798  -18.291 -26.542 1.00 23.91 ? 134 THR D C   1 
ATOM   5834 O  O   . THR D 1 139 ? -4.955  -18.137 -25.631 1.00 24.72 ? 134 THR D O   1 
ATOM   5835 C  CB  . THR D 1 139 ? -6.650  -16.237 -27.850 1.00 22.03 ? 134 THR D CB  1 
ATOM   5836 O  OG1 . THR D 1 139 ? -6.377  -15.546 -29.073 1.00 22.48 ? 134 THR D OG1 1 
ATOM   5837 C  CG2 . THR D 1 139 ? -6.503  -15.314 -26.661 1.00 21.88 ? 134 THR D CG2 1 
ATOM   5838 N  N   . VAL D 1 140 ? -6.807  -19.150 -26.460 1.00 23.74 ? 135 VAL D N   1 
ATOM   5839 C  CA  . VAL D 1 140 ? -6.965  -20.067 -25.297 1.00 23.75 ? 135 VAL D CA  1 
ATOM   5840 C  C   . VAL D 1 140 ? -5.671  -20.869 -25.181 1.00 25.45 ? 135 VAL D C   1 
ATOM   5841 O  O   . VAL D 1 140 ? -5.159  -21.020 -24.048 1.00 27.74 ? 135 VAL D O   1 
ATOM   5842 C  CB  . VAL D 1 140 ? -8.194  -20.987 -25.428 1.00 24.40 ? 135 VAL D CB  1 
ATOM   5843 C  CG1 . VAL D 1 140 ? -8.220  -22.021 -24.320 1.00 23.42 ? 135 VAL D CG1 1 
ATOM   5844 C  CG2 . VAL D 1 140 ? -9.508  -20.205 -25.432 1.00 24.97 ? 135 VAL D CG2 1 
ATOM   5845 N  N   . ALA D 1 141 ? -5.178  -21.448 -26.270 1.00 23.47 ? 136 ALA D N   1 
ATOM   5846 C  CA  . ALA D 1 141 ? -4.036  -22.391 -26.134 1.00 24.44 ? 136 ALA D CA  1 
ATOM   5847 C  C   . ALA D 1 141 ? -2.839  -21.636 -25.530 1.00 26.32 ? 136 ALA D C   1 
ATOM   5848 O  O   . ALA D 1 141 ? -2.271  -22.103 -24.487 1.00 27.81 ? 136 ALA D O   1 
ATOM   5849 C  CB  . ALA D 1 141 ? -3.733  -23.041 -27.438 1.00 22.66 ? 136 ALA D CB  1 
ATOM   5850 N  N   . ALA D 1 142 ? -2.558  -20.446 -26.060 1.00 26.36 ? 137 ALA D N   1 
ATOM   5851 C  CA  . ALA D 1 142 ? -1.422  -19.593 -25.640 1.00 26.31 ? 137 ALA D CA  1 
ATOM   5852 C  C   . ALA D 1 142 ? -1.667  -19.059 -24.215 1.00 25.99 ? 137 ALA D C   1 
ATOM   5853 O  O   . ALA D 1 142 ? -0.719  -19.158 -23.411 1.00 24.56 ? 137 ALA D O   1 
ATOM   5854 C  CB  . ALA D 1 142 ? -1.205  -18.476 -26.636 1.00 26.39 ? 137 ALA D CB  1 
ATOM   5855 N  N   . LEU D 1 143 ? -2.862  -18.557 -23.866 1.00 22.08 ? 138 LEU D N   1 
ATOM   5856 C  CA  . LEU D 1 143 ? -3.016  -17.907 -22.528 1.00 25.08 ? 138 LEU D CA  1 
ATOM   5857 C  C   . LEU D 1 143 ? -3.236  -18.942 -21.408 1.00 26.22 ? 138 LEU D C   1 
ATOM   5858 O  O   . LEU D 1 143 ? -2.641  -18.747 -20.336 1.00 23.16 ? 138 LEU D O   1 
ATOM   5859 C  CB  . LEU D 1 143 ? -4.105  -16.826 -22.520 1.00 24.98 ? 138 LEU D CB  1 
ATOM   5860 C  CG  . LEU D 1 143 ? -3.942  -15.678 -23.514 1.00 26.41 ? 138 LEU D CG  1 
ATOM   5861 C  CD1 . LEU D 1 143 ? -4.700  -14.459 -23.033 1.00 25.12 ? 138 LEU D CD1 1 
ATOM   5862 C  CD2 . LEU D 1 143 ? -2.485  -15.358 -23.813 1.00 28.83 ? 138 LEU D CD2 1 
ATOM   5863 N  N   . GLU D 1 144 ? -4.050  -19.988 -21.612 1.00 24.84 ? 139 GLU D N   1 
ATOM   5864 C  CA  . GLU D 1 144 ? -4.337  -20.976 -20.549 1.00 24.10 ? 139 GLU D CA  1 
ATOM   5865 C  C   . GLU D 1 144 ? -3.026  -21.642 -20.101 1.00 26.65 ? 139 GLU D C   1 
ATOM   5866 O  O   . GLU D 1 144 ? -2.828  -21.795 -18.884 1.00 25.07 ? 139 GLU D O   1 
ATOM   5867 C  CB  . GLU D 1 144 ? -5.366  -22.001 -21.018 1.00 25.39 ? 139 GLU D CB  1 
ATOM   5868 C  CG  . GLU D 1 144 ? -5.789  -22.948 -19.900 1.00 25.90 ? 139 GLU D CG  1 
ATOM   5869 C  CD  . GLU D 1 144 ? -6.428  -22.299 -18.679 1.00 25.71 ? 139 GLU D CD  1 
ATOM   5870 O  OE1 . GLU D 1 144 ? -7.029  -21.190 -18.812 1.00 24.03 ? 139 GLU D OE1 1 
ATOM   5871 O  OE2 . GLU D 1 144 ? -6.348  -22.911 -17.598 1.00 25.16 ? 139 GLU D OE2 1 
ATOM   5872 N  N   . SER D 1 145 ? -2.149  -22.008 -21.040 1.00 30.56 ? 140 SER D N   1 
ATOM   5873 C  CA  . SER D 1 145 ? -0.844  -22.655 -20.737 1.00 33.70 ? 140 SER D CA  1 
ATOM   5874 C  C   . SER D 1 145 ? 0.052   -21.704 -19.919 1.00 35.68 ? 140 SER D C   1 
ATOM   5875 O  O   . SER D 1 145 ? 0.658   -22.180 -18.957 1.00 37.68 ? 140 SER D O   1 
ATOM   5876 C  CB  . SER D 1 145 ? -0.158  -23.122 -21.988 1.00 35.16 ? 140 SER D CB  1 
ATOM   5877 O  OG  . SER D 1 145 ? 0.154   -22.018 -22.816 1.00 43.32 ? 140 SER D OG  1 
ATOM   5878 N  N   . ARG D 1 146 ? 0.096   -20.404 -20.240 1.00 35.30 ? 141 ARG D N   1 
ATOM   5879 C  CA  . ARG D 1 146 ? 1.024   -19.429 -19.595 1.00 34.79 ? 141 ARG D CA  1 
ATOM   5880 C  C   . ARG D 1 146 ? 0.437   -18.915 -18.274 1.00 31.22 ? 141 ARG D C   1 
ATOM   5881 O  O   . ARG D 1 146 ? 1.197   -18.738 -17.319 1.00 29.01 ? 141 ARG D O   1 
ATOM   5882 C  CB  . ARG D 1 146 ? 1.338   -18.285 -20.560 1.00 38.18 ? 141 ARG D CB  1 
ATOM   5883 C  CG  . ARG D 1 146 ? 2.419   -17.328 -20.081 1.00 40.68 ? 141 ARG D CG  1 
ATOM   5884 C  CD  . ARG D 1 146 ? 2.744   -16.359 -21.206 1.00 44.73 ? 141 ARG D CD  1 
ATOM   5885 N  NE  . ARG D 1 146 ? 3.470   -17.038 -22.271 1.00 48.31 ? 141 ARG D NE  1 
ATOM   5886 C  CZ  . ARG D 1 146 ? 4.798   -17.062 -22.415 1.00 50.00 ? 141 ARG D CZ  1 
ATOM   5887 N  NH1 . ARG D 1 146 ? 5.587   -16.400 -21.583 1.00 50.92 ? 141 ARG D NH1 1 
ATOM   5888 N  NH2 . ARG D 1 146 ? 5.334   -17.736 -23.418 1.00 50.79 ? 141 ARG D NH2 1 
ATOM   5889 N  N   . PHE D 1 147 ? -0.868  -18.681 -18.196 1.00 27.01 ? 142 PHE D N   1 
ATOM   5890 C  CA  . PHE D 1 147 ? -1.464  -17.920 -17.073 1.00 27.51 ? 142 PHE D CA  1 
ATOM   5891 C  C   . PHE D 1 147 ? -2.521  -18.748 -16.327 1.00 28.02 ? 142 PHE D C   1 
ATOM   5892 O  O   . PHE D 1 147 ? -2.985  -18.271 -15.298 1.00 27.86 ? 142 PHE D O   1 
ATOM   5893 C  CB  . PHE D 1 147 ? -2.054  -16.617 -17.615 1.00 26.42 ? 142 PHE D CB  1 
ATOM   5894 C  CG  . PHE D 1 147 ? -1.079  -15.755 -18.378 1.00 26.11 ? 142 PHE D CG  1 
ATOM   5895 C  CD1 . PHE D 1 147 ? -0.150  -14.974 -17.708 1.00 25.40 ? 142 PHE D CD1 1 
ATOM   5896 C  CD2 . PHE D 1 147 ? -1.115  -15.692 -19.766 1.00 25.23 ? 142 PHE D CD2 1 
ATOM   5897 C  CE1 . PHE D 1 147 ? 0.733   -14.168 -18.413 1.00 25.96 ? 142 PHE D CE1 1 
ATOM   5898 C  CE2 . PHE D 1 147 ? -0.216  -14.899 -20.469 1.00 25.47 ? 142 PHE D CE2 1 
ATOM   5899 C  CZ  . PHE D 1 147 ? 0.691   -14.118 -19.791 1.00 24.90 ? 142 PHE D CZ  1 
ATOM   5900 N  N   . GLY D 1 148 ? -2.923  -19.909 -16.847 1.00 27.15 ? 143 GLY D N   1 
ATOM   5901 C  CA  . GLY D 1 148 ? -4.171  -20.573 -16.432 1.00 29.60 ? 143 GLY D CA  1 
ATOM   5902 C  C   . GLY D 1 148 ? -3.922  -21.686 -15.438 1.00 31.00 ? 143 GLY D C   1 
ATOM   5903 O  O   . GLY D 1 148 ? -2.836  -21.709 -14.854 1.00 29.24 ? 143 GLY D O   1 
ATOM   5904 N  N   . ALA D 1 149 ? -4.896  -22.587 -15.269 1.00 33.28 ? 144 ALA D N   1 
ATOM   5905 C  CA  . ALA D 1 149 ? -4.890  -23.639 -14.227 1.00 34.23 ? 144 ALA D CA  1 
ATOM   5906 C  C   . ALA D 1 149 ? -5.226  -24.986 -14.878 1.00 36.01 ? 144 ALA D C   1 
ATOM   5907 O  O   . ALA D 1 149 ? -6.088  -25.687 -14.351 1.00 35.50 ? 144 ALA D O   1 
ATOM   5908 C  CB  . ALA D 1 149 ? -5.859  -23.262 -13.128 1.00 35.04 ? 144 ALA D CB  1 
ATOM   5909 N  N   . GLY D 1 150 ? -4.612  -25.265 -16.034 1.00 36.03 ? 145 GLY D N   1 
ATOM   5910 C  CA  . GLY D 1 150 ? -4.717  -26.539 -16.770 1.00 35.36 ? 145 GLY D CA  1 
ATOM   5911 C  C   . GLY D 1 150 ? -6.131  -26.835 -17.244 1.00 36.64 ? 145 GLY D C   1 
ATOM   5912 O  O   . GLY D 1 150 ? -6.460  -28.033 -17.393 1.00 34.43 ? 145 GLY D O   1 
ATOM   5913 N  N   . TRP D 1 151 ? -6.943  -25.805 -17.514 1.00 33.47 ? 146 TRP D N   1 
ATOM   5914 C  CA  . TRP D 1 151 ? -8.303  -26.003 -18.076 1.00 31.14 ? 146 TRP D CA  1 
ATOM   5915 C  C   . TRP D 1 151 ? -8.172  -26.599 -19.474 1.00 30.50 ? 146 TRP D C   1 
ATOM   5916 O  O   . TRP D 1 151 ? -7.255  -26.205 -20.207 1.00 27.85 ? 146 TRP D O   1 
ATOM   5917 C  CB  . TRP D 1 151 ? -9.084  -24.696 -18.117 1.00 29.53 ? 146 TRP D CB  1 
ATOM   5918 C  CG  . TRP D 1 151 ? -10.465 -24.796 -18.689 1.00 27.78 ? 146 TRP D CG  1 
ATOM   5919 C  CD1 . TRP D 1 151 ? -11.567 -25.351 -18.099 1.00 26.86 ? 146 TRP D CD1 1 
ATOM   5920 C  CD2 . TRP D 1 151 ? -10.914 -24.255 -19.943 1.00 25.88 ? 146 TRP D CD2 1 
ATOM   5921 N  NE1 . TRP D 1 151 ? -12.660 -25.207 -18.915 1.00 25.80 ? 146 TRP D NE1 1 
ATOM   5922 C  CE2 . TRP D 1 151 ? -12.300 -24.528 -20.039 1.00 24.81 ? 146 TRP D CE2 1 
ATOM   5923 C  CE3 . TRP D 1 151 ? -10.299 -23.534 -20.974 1.00 25.30 ? 146 TRP D CE3 1 
ATOM   5924 C  CZ2 . TRP D 1 151 ? -13.072 -24.106 -21.119 1.00 26.27 ? 146 TRP D CZ2 1 
ATOM   5925 C  CZ3 . TRP D 1 151 ? -11.064 -23.116 -22.039 1.00 26.33 ? 146 TRP D CZ3 1 
ATOM   5926 C  CH2 . TRP D 1 151 ? -12.436 -23.395 -22.109 1.00 24.67 ? 146 TRP D CH2 1 
ATOM   5927 N  N   . ASP D 1 152 ? -9.073  -27.513 -19.821 1.00 29.42 ? 147 ASP D N   1 
ATOM   5928 C  CA  . ASP D 1 152 ? -9.118  -28.178 -21.149 1.00 26.93 ? 147 ASP D CA  1 
ATOM   5929 C  C   . ASP D 1 152 ? -10.325 -27.609 -21.894 1.00 26.84 ? 147 ASP D C   1 
ATOM   5930 O  O   . ASP D 1 152 ? -11.462 -27.798 -21.422 1.00 26.68 ? 147 ASP D O   1 
ATOM   5931 C  CB  . ASP D 1 152 ? -9.156  -29.696 -20.947 1.00 29.83 ? 147 ASP D CB  1 
ATOM   5932 C  CG  . ASP D 1 152 ? -9.409  -30.529 -22.189 1.00 29.74 ? 147 ASP D CG  1 
ATOM   5933 O  OD1 . ASP D 1 152 ? -9.334  -29.988 -23.288 1.00 32.98 ? 147 ASP D OD1 1 
ATOM   5934 O  OD2 . ASP D 1 152 ? -9.676  -31.725 -22.031 1.00 33.88 ? 147 ASP D OD2 1 
ATOM   5935 N  N   . MET D 1 153 ? -10.072 -26.944 -23.021 1.00 27.69 ? 148 MET D N   1 
ATOM   5936 C  CA  . MET D 1 153 ? -11.098 -26.277 -23.857 1.00 27.50 ? 148 MET D CA  1 
ATOM   5937 C  C   . MET D 1 153 ? -11.966 -27.305 -24.611 1.00 29.52 ? 148 MET D C   1 
ATOM   5938 O  O   . MET D 1 153 ? -13.010 -26.864 -25.180 1.00 24.14 ? 148 MET D O   1 
ATOM   5939 C  CB  . MET D 1 153 ? -10.421 -25.328 -24.841 1.00 27.85 ? 148 MET D CB  1 
ATOM   5940 C  CG  . MET D 1 153 ? -9.823  -25.989 -26.071 1.00 26.13 ? 148 MET D CG  1 
ATOM   5941 S  SD  . MET D 1 153 ? -9.187  -24.722 -27.166 1.00 27.77 ? 148 MET D SD  1 
ATOM   5942 C  CE  . MET D 1 153 ? -7.520  -24.582 -26.510 1.00 28.36 ? 148 MET D CE  1 
ATOM   5943 N  N   . THR D 1 154 ? -11.599 -28.605 -24.596 1.00 28.71 ? 149 THR D N   1 
ATOM   5944 C  CA  . THR D 1 154 ? -12.229 -29.638 -25.465 1.00 31.57 ? 149 THR D CA  1 
ATOM   5945 C  C   . THR D 1 154 ? -13.755 -29.661 -25.261 1.00 31.10 ? 149 THR D C   1 
ATOM   5946 O  O   . THR D 1 154 ? -14.490 -29.671 -26.272 1.00 35.27 ? 149 THR D O   1 
ATOM   5947 C  CB  . THR D 1 154 ? -11.622 -31.026 -25.261 1.00 33.92 ? 149 THR D CB  1 
ATOM   5948 O  OG1 . THR D 1 154 ? -10.221 -30.979 -25.564 1.00 34.06 ? 149 THR D OG1 1 
ATOM   5949 C  CG2 . THR D 1 154 ? -12.313 -32.048 -26.137 1.00 34.17 ? 149 THR D CG2 1 
ATOM   5950 N  N   . GLY D 1 155 ? -14.232 -29.618 -24.016 1.00 31.59 ? 150 GLY D N   1 
ATOM   5951 C  CA  . GLY D 1 155 ? -15.672 -29.723 -23.715 1.00 30.22 ? 150 GLY D CA  1 
ATOM   5952 C  C   . GLY D 1 155 ? -16.442 -28.502 -24.191 1.00 30.00 ? 150 GLY D C   1 
ATOM   5953 O  O   . GLY D 1 155 ? -17.658 -28.581 -24.241 1.00 32.92 ? 150 GLY D O   1 
ATOM   5954 N  N   . SER D 1 156 ? -15.746 -27.411 -24.533 1.00 28.56 ? 151 SER D N   1 
ATOM   5955 C  CA  . SER D 1 156 ? -16.320 -26.070 -24.822 1.00 28.01 ? 151 SER D CA  1 
ATOM   5956 C  C   . SER D 1 156 ? -16.160 -25.689 -26.301 1.00 27.47 ? 151 SER D C   1 
ATOM   5957 O  O   . SER D 1 156 ? -16.593 -24.570 -26.707 1.00 25.86 ? 151 SER D O   1 
ATOM   5958 C  CB  . SER D 1 156 ? -15.704 -25.058 -23.895 1.00 26.45 ? 151 SER D CB  1 
ATOM   5959 O  OG  . SER D 1 156 ? -16.073 -25.319 -22.546 1.00 26.03 ? 151 SER D OG  1 
ATOM   5960 N  N   . LEU D 1 157 ? -15.584 -26.585 -27.105 1.00 28.99 ? 152 LEU D N   1 
ATOM   5961 C  CA  . LEU D 1 157 ? -15.302 -26.283 -28.532 1.00 30.60 ? 152 LEU D CA  1 
ATOM   5962 C  C   . LEU D 1 157 ? -16.609 -25.954 -29.255 1.00 31.30 ? 152 LEU D C   1 
ATOM   5963 O  O   . LEU D 1 157 ? -16.631 -24.965 -30.029 1.00 29.46 ? 152 LEU D O   1 
ATOM   5964 C  CB  . LEU D 1 157 ? -14.546 -27.452 -29.163 1.00 31.34 ? 152 LEU D CB  1 
ATOM   5965 C  CG  . LEU D 1 157 ? -13.068 -27.542 -28.766 1.00 31.79 ? 152 LEU D CG  1 
ATOM   5966 C  CD1 . LEU D 1 157 ? -12.402 -28.757 -29.392 1.00 35.41 ? 152 LEU D CD1 1 
ATOM   5967 C  CD2 . LEU D 1 157 ? -12.334 -26.286 -29.163 1.00 31.39 ? 152 LEU D CD2 1 
ATOM   5968 N  N   . ASP D 1 158 ? -17.684 -26.698 -28.999 1.00 30.20 ? 153 ASP D N   1 
ATOM   5969 C  CA  . ASP D 1 158 ? -18.989 -26.372 -29.637 1.00 32.87 ? 153 ASP D CA  1 
ATOM   5970 C  C   . ASP D 1 158 ? -19.513 -25.051 -29.075 1.00 29.78 ? 153 ASP D C   1 
ATOM   5971 O  O   . ASP D 1 158 ? -20.030 -24.255 -29.850 1.00 28.71 ? 153 ASP D O   1 
ATOM   5972 C  CB  . ASP D 1 158 ? -19.999 -27.509 -29.499 1.00 37.66 ? 153 ASP D CB  1 
ATOM   5973 C  CG  . ASP D 1 158 ? -19.720 -28.615 -30.503 1.00 45.92 ? 153 ASP D CG  1 
ATOM   5974 O  OD1 . ASP D 1 158 ? -19.193 -28.295 -31.611 1.00 41.95 ? 153 ASP D OD1 1 
ATOM   5975 O  OD2 . ASP D 1 158 ? -20.006 -29.785 -30.170 1.00 54.05 ? 153 ASP D OD2 1 
ATOM   5976 N  N   . TYR D 1 159 ? -19.398 -24.850 -27.766 1.00 29.78 ? 154 TYR D N   1 
ATOM   5977 C  CA  . TYR D 1 159 ? -19.816 -23.597 -27.094 1.00 30.26 ? 154 TYR D CA  1 
ATOM   5978 C  C   . TYR D 1 159 ? -19.169 -22.381 -27.774 1.00 28.57 ? 154 TYR D C   1 
ATOM   5979 O  O   . TYR D 1 159 ? -19.874 -21.440 -28.110 1.00 27.37 ? 154 TYR D O   1 
ATOM   5980 C  CB  . TYR D 1 159 ? -19.460 -23.668 -25.615 1.00 30.33 ? 154 TYR D CB  1 
ATOM   5981 C  CG  . TYR D 1 159 ? -19.774 -22.393 -24.883 1.00 33.09 ? 154 TYR D CG  1 
ATOM   5982 C  CD1 . TYR D 1 159 ? -21.089 -21.972 -24.714 1.00 34.85 ? 154 TYR D CD1 1 
ATOM   5983 C  CD2 . TYR D 1 159 ? -18.755 -21.609 -24.362 1.00 31.50 ? 154 TYR D CD2 1 
ATOM   5984 C  CE1 . TYR D 1 159 ? -21.376 -20.789 -24.052 1.00 35.09 ? 154 TYR D CE1 1 
ATOM   5985 C  CE2 . TYR D 1 159 ? -19.029 -20.438 -23.682 1.00 32.55 ? 154 TYR D CE2 1 
ATOM   5986 C  CZ  . TYR D 1 159 ? -20.342 -20.038 -23.516 1.00 33.08 ? 154 TYR D CZ  1 
ATOM   5987 O  OH  . TYR D 1 159 ? -20.586 -18.873 -22.860 1.00 35.24 ? 154 TYR D OH  1 
ATOM   5988 N  N   . PHE D 1 160 ? -17.853 -22.418 -27.999 1.00 28.19 ? 155 PHE D N   1 
ATOM   5989 C  CA  . PHE D 1 160 ? -17.102 -21.351 -28.699 1.00 28.16 ? 155 PHE D CA  1 
ATOM   5990 C  C   . PHE D 1 160 ? -17.821 -21.032 -30.004 1.00 33.75 ? 155 PHE D C   1 
ATOM   5991 O  O   . PHE D 1 160 ? -17.888 -19.838 -30.362 1.00 31.08 ? 155 PHE D O   1 
ATOM   5992 C  CB  . PHE D 1 160 ? -15.682 -21.783 -29.069 1.00 28.28 ? 155 PHE D CB  1 
ATOM   5993 C  CG  . PHE D 1 160 ? -14.704 -21.952 -27.935 1.00 25.04 ? 155 PHE D CG  1 
ATOM   5994 C  CD1 . PHE D 1 160 ? -15.096 -21.867 -26.617 1.00 23.95 ? 155 PHE D CD1 1 
ATOM   5995 C  CD2 . PHE D 1 160 ? -13.370 -22.214 -28.211 1.00 26.66 ? 155 PHE D CD2 1 
ATOM   5996 C  CE1 . PHE D 1 160 ? -14.181 -22.049 -25.592 1.00 25.50 ? 155 PHE D CE1 1 
ATOM   5997 C  CE2 . PHE D 1 160 ? -12.455 -22.403 -27.186 1.00 26.47 ? 155 PHE D CE2 1 
ATOM   5998 C  CZ  . PHE D 1 160 ? -12.855 -22.282 -25.874 1.00 24.12 ? 155 PHE D CZ  1 
ATOM   5999 N  N   . ARG D 1 161 ? -18.263 -22.075 -30.724 1.00 29.36 ? 156 ARG D N   1 
ATOM   6000 C  CA  . ARG D 1 161 ? -18.937 -21.909 -32.032 1.00 33.05 ? 156 ARG D CA  1 
ATOM   6001 C  C   . ARG D 1 161 ? -20.329 -21.322 -31.751 1.00 32.44 ? 156 ARG D C   1 
ATOM   6002 O  O   . ARG D 1 161 ? -20.699 -20.401 -32.449 1.00 29.78 ? 156 ARG D O   1 
ATOM   6003 C  CB  . ARG D 1 161 ? -18.966 -23.226 -32.825 1.00 35.88 ? 156 ARG D CB  1 
ATOM   6004 C  CG  . ARG D 1 161 ? -17.590 -23.756 -33.218 1.00 40.12 ? 156 ARG D CG  1 
ATOM   6005 C  CD  . ARG D 1 161 ? -17.663 -25.038 -34.050 1.00 41.74 ? 156 ARG D CD  1 
ATOM   6006 N  NE  . ARG D 1 161 ? -18.414 -24.829 -35.283 1.00 44.59 ? 156 ARG D NE  1 
ATOM   6007 C  CZ  . ARG D 1 161 ? -18.885 -25.791 -36.079 1.00 48.00 ? 156 ARG D CZ  1 
ATOM   6008 N  NH1 . ARG D 1 161 ? -18.689 -27.070 -35.798 1.00 49.60 ? 156 ARG D NH1 1 
ATOM   6009 N  NH2 . ARG D 1 161 ? -19.560 -25.460 -37.166 1.00 48.42 ? 156 ARG D NH2 1 
ATOM   6010 N  N   . ARG D 1 162 ? -21.006 -21.774 -30.687 1.00 33.46 ? 157 ARG D N   1 
ATOM   6011 C  CA  . ARG D 1 162 ? -22.374 -21.323 -30.295 1.00 33.42 ? 157 ARG D CA  1 
ATOM   6012 C  C   . ARG D 1 162 ? -22.353 -19.861 -29.779 1.00 32.58 ? 157 ARG D C   1 
ATOM   6013 O  O   . ARG D 1 162 ? -23.454 -19.338 -29.577 1.00 27.90 ? 157 ARG D O   1 
ATOM   6014 C  CB  . ARG D 1 162 ? -22.969 -22.228 -29.201 1.00 38.90 ? 157 ARG D CB  1 
ATOM   6015 C  CG  . ARG D 1 162 ? -23.430 -23.617 -29.637 1.00 40.81 ? 157 ARG D CG  1 
ATOM   6016 C  CD  . ARG D 1 162 ? -24.496 -24.215 -28.707 1.00 40.03 ? 157 ARG D CD  1 
ATOM   6017 N  NE  . ARG D 1 162 ? -24.055 -24.454 -27.326 1.00 42.24 ? 157 ARG D NE  1 
ATOM   6018 C  CZ  . ARG D 1 162 ? -23.257 -25.459 -26.930 1.00 45.37 ? 157 ARG D CZ  1 
ATOM   6019 N  NH1 . ARG D 1 162 ? -22.909 -25.585 -25.658 1.00 40.18 ? 157 ARG D NH1 1 
ATOM   6020 N  NH2 . ARG D 1 162 ? -22.810 -26.340 -27.814 1.00 45.25 ? 157 ARG D NH2 1 
ATOM   6021 N  N   . ILE D 1 163 ? -21.193 -19.212 -29.573 1.00 30.89 ? 158 ILE D N   1 
ATOM   6022 C  CA  . ILE D 1 163 ? -21.122 -17.794 -29.070 1.00 32.72 ? 158 ILE D CA  1 
ATOM   6023 C  C   . ILE D 1 163 ? -20.251 -16.893 -29.974 1.00 31.06 ? 158 ILE D C   1 
ATOM   6024 O  O   . ILE D 1 163 ? -19.946 -15.764 -29.565 1.00 38.32 ? 158 ILE D O   1 
ATOM   6025 C  CB  . ILE D 1 163 ? -20.661 -17.711 -27.593 1.00 30.55 ? 158 ILE D CB  1 
ATOM   6026 C  CG1 . ILE D 1 163 ? -19.313 -18.387 -27.337 1.00 32.97 ? 158 ILE D CG1 1 
ATOM   6027 C  CG2 . ILE D 1 163 ? -21.711 -18.201 -26.621 1.00 34.29 ? 158 ILE D CG2 1 
ATOM   6028 C  CD1 . ILE D 1 163 ? -18.503 -17.680 -26.298 1.00 31.46 ? 158 ILE D CD1 1 
ATOM   6029 N  N   . LEU D 1 164 ? -19.936 -17.314 -31.195 1.00 34.57 ? 159 LEU D N   1 
ATOM   6030 C  CA  . LEU D 1 164 ? -18.849 -16.759 -32.052 1.00 32.08 ? 159 LEU D CA  1 
ATOM   6031 C  C   . LEU D 1 164 ? -19.209 -15.441 -32.730 1.00 32.73 ? 159 LEU D C   1 
ATOM   6032 O  O   . LEU D 1 164 ? -18.307 -14.707 -33.118 1.00 31.80 ? 159 LEU D O   1 
ATOM   6033 C  CB  . LEU D 1 164 ? -18.504 -17.780 -33.135 1.00 33.57 ? 159 LEU D CB  1 
ATOM   6034 C  CG  . LEU D 1 164 ? -17.131 -17.619 -33.784 1.00 36.31 ? 159 LEU D CG  1 
ATOM   6035 C  CD1 . LEU D 1 164 ? -16.002 -17.805 -32.763 1.00 40.95 ? 159 LEU D CD1 1 
ATOM   6036 C  CD2 . LEU D 1 164 ? -16.965 -18.599 -34.921 1.00 36.56 ? 159 LEU D CD2 1 
ATOM   6037 N  N   . PRO D 1 165 ? -20.485 -15.148 -33.060 1.00 32.31 ? 160 PRO D N   1 
ATOM   6038 C  CA  . PRO D 1 165 ? -20.803 -13.923 -33.795 1.00 31.42 ? 160 PRO D CA  1 
ATOM   6039 C  C   . PRO D 1 165 ? -20.345 -12.594 -33.154 1.00 30.16 ? 160 PRO D C   1 
ATOM   6040 O  O   . PRO D 1 165 ? -20.022 -11.687 -33.917 1.00 29.76 ? 160 PRO D O   1 
ATOM   6041 C  CB  . PRO D 1 165 ? -22.345 -13.932 -33.885 1.00 33.32 ? 160 PRO D CB  1 
ATOM   6042 C  CG  . PRO D 1 165 ? -22.747 -15.381 -33.696 1.00 33.47 ? 160 PRO D CG  1 
ATOM   6043 C  CD  . PRO D 1 165 ? -21.655 -16.024 -32.863 1.00 32.56 ? 160 PRO D CD  1 
ATOM   6044 N  N   . GLY D 1 166 ? -20.295 -12.512 -31.813 1.00 27.68 ? 161 GLY D N   1 
ATOM   6045 C  CA  . GLY D 1 166 ? -19.884 -11.324 -31.036 1.00 25.58 ? 161 GLY D CA  1 
ATOM   6046 C  C   . GLY D 1 166 ? -18.403 -10.997 -31.249 1.00 24.91 ? 161 GLY D C   1 
ATOM   6047 O  O   . GLY D 1 166 ? -18.036 -9.840  -31.078 1.00 23.01 ? 161 GLY D O   1 
ATOM   6048 N  N   . VAL D 1 167 ? -17.586 -11.981 -31.655 1.00 25.54 ? 162 VAL D N   1 
ATOM   6049 C  CA  . VAL D 1 167 ? -16.102 -11.835 -31.788 1.00 25.15 ? 162 VAL D CA  1 
ATOM   6050 C  C   . VAL D 1 167 ? -15.778 -11.013 -33.041 1.00 25.90 ? 162 VAL D C   1 
ATOM   6051 O  O   . VAL D 1 167 ? -16.174 -11.435 -34.140 1.00 26.24 ? 162 VAL D O   1 
ATOM   6052 C  CB  . VAL D 1 167 ? -15.391 -13.201 -31.872 1.00 23.25 ? 162 VAL D CB  1 
ATOM   6053 C  CG1 . VAL D 1 167 ? -13.891 -13.041 -32.047 1.00 22.84 ? 162 VAL D CG1 1 
ATOM   6054 C  CG2 . VAL D 1 167 ? -15.689 -14.063 -30.673 1.00 24.68 ? 162 VAL D CG2 1 
ATOM   6055 N  N   . GLY D 1 168 ? -15.021 -9.920  -32.878 1.00 27.11 ? 163 GLY D N   1 
ATOM   6056 C  CA  . GLY D 1 168 ? -14.333 -9.205  -33.968 1.00 24.81 ? 163 GLY D CA  1 
ATOM   6057 C  C   . GLY D 1 168 ? -12.859 -9.555  -33.971 1.00 25.94 ? 163 GLY D C   1 
ATOM   6058 O  O   . GLY D 1 168 ? -12.110 -8.930  -33.193 1.00 23.65 ? 163 GLY D O   1 
ATOM   6059 N  N   . ALA D 1 169 ? -12.443 -10.515 -34.802 1.00 25.95 ? 164 ALA D N   1 
ATOM   6060 C  CA  . ALA D 1 169 ? -11.039 -11.000 -34.864 1.00 25.20 ? 164 ALA D CA  1 
ATOM   6061 C  C   . ALA D 1 169 ? -10.265 -10.137 -35.851 1.00 23.82 ? 164 ALA D C   1 
ATOM   6062 O  O   . ALA D 1 169 ? -10.872 -9.674  -36.862 1.00 23.94 ? 164 ALA D O   1 
ATOM   6063 C  CB  . ALA D 1 169 ? -10.951 -12.488 -35.215 1.00 24.05 ? 164 ALA D CB  1 
ATOM   6064 N  N   . PHE D 1 170 ? -8.954  -10.001 -35.628 1.00 21.58 ? 165 PHE D N   1 
ATOM   6065 C  CA  . PHE D 1 170 ? -8.086  -9.139  -36.455 1.00 22.83 ? 165 PHE D CA  1 
ATOM   6066 C  C   . PHE D 1 170 ? -6.662  -9.711  -36.487 1.00 22.39 ? 165 PHE D C   1 
ATOM   6067 O  O   . PHE D 1 170 ? -6.287  -10.581 -35.721 1.00 23.41 ? 165 PHE D O   1 
ATOM   6068 C  CB  . PHE D 1 170 ? -8.161  -7.685  -35.977 1.00 23.56 ? 165 PHE D CB  1 
ATOM   6069 C  CG  . PHE D 1 170 ? -7.862  -7.425  -34.518 1.00 22.93 ? 165 PHE D CG  1 
ATOM   6070 C  CD1 . PHE D 1 170 ? -6.566  -7.337  -34.073 1.00 23.93 ? 165 PHE D CD1 1 
ATOM   6071 C  CD2 . PHE D 1 170 ? -8.878  -7.242  -33.600 1.00 27.82 ? 165 PHE D CD2 1 
ATOM   6072 C  CE1 . PHE D 1 170 ? -6.291  -7.083  -32.741 1.00 24.84 ? 165 PHE D CE1 1 
ATOM   6073 C  CE2 . PHE D 1 170 ? -8.607  -6.998  -32.263 1.00 26.03 ? 165 PHE D CE2 1 
ATOM   6074 C  CZ  . PHE D 1 170 ? -7.307  -6.937  -31.836 1.00 24.52 ? 165 PHE D CZ  1 
ATOM   6075 N  N   . ARG D 1 171 ? -5.912  -9.215  -37.446 1.00 24.42 ? 166 ARG D N   1 
ATOM   6076 C  CA  . ARG D 1 171 ? -4.505  -9.549  -37.714 1.00 25.66 ? 166 ARG D CA  1 
ATOM   6077 C  C   . ARG D 1 171 ? -3.823  -8.201  -37.758 1.00 29.21 ? 166 ARG D C   1 
ATOM   6078 O  O   . ARG D 1 171 ? -4.451  -7.227  -38.274 1.00 30.51 ? 166 ARG D O   1 
ATOM   6079 C  CB  . ARG D 1 171 ? -4.380  -10.289 -39.045 1.00 26.29 ? 166 ARG D CB  1 
ATOM   6080 C  CG  . ARG D 1 171 ? -5.182  -11.578 -39.116 1.00 25.81 ? 166 ARG D CG  1 
ATOM   6081 C  CD  . ARG D 1 171 ? -4.554  -12.553 -38.131 1.00 27.42 ? 166 ARG D CD  1 
ATOM   6082 N  NE  . ARG D 1 171 ? -5.076  -13.908 -38.095 1.00 28.74 ? 166 ARG D NE  1 
ATOM   6083 C  CZ  . ARG D 1 171 ? -6.105  -14.322 -37.359 1.00 29.85 ? 166 ARG D CZ  1 
ATOM   6084 N  NH1 . ARG D 1 171 ? -6.801  -13.481 -36.604 1.00 29.33 ? 166 ARG D NH1 1 
ATOM   6085 N  NH2 . ARG D 1 171 ? -6.423  -15.599 -37.361 1.00 30.13 ? 166 ARG D NH2 1 
ATOM   6086 N  N   . LEU D 1 172 ? -2.629  -8.130  -37.199 1.00 29.25 ? 167 LEU D N   1 
ATOM   6087 C  CA  . LEU D 1 172 ? -1.837  -6.886  -37.178 1.00 30.74 ? 167 LEU D CA  1 
ATOM   6088 C  C   . LEU D 1 172 ? -0.416  -7.225  -37.616 1.00 29.68 ? 167 LEU D C   1 
ATOM   6089 O  O   . LEU D 1 172 ? 0.306   -7.865  -36.834 1.00 30.30 ? 167 LEU D O   1 
ATOM   6090 C  CB  . LEU D 1 172 ? -1.869  -6.283  -35.766 1.00 32.91 ? 167 LEU D CB  1 
ATOM   6091 C  CG  . LEU D 1 172 ? -1.021  -5.027  -35.590 1.00 31.34 ? 167 LEU D CG  1 
ATOM   6092 C  CD1 . LEU D 1 172 ? -1.580  -3.899  -36.443 1.00 36.80 ? 167 LEU D CD1 1 
ATOM   6093 C  CD2 . LEU D 1 172 ? -0.964  -4.617  -34.135 1.00 34.25 ? 167 LEU D CD2 1 
ATOM   6094 N  N   . ARG D 1 173 ? -0.053  -6.830  -38.832 1.00 31.49 ? 168 ARG D N   1 
ATOM   6095 C  CA  . ARG D 1 173 ? 1.320   -6.985  -39.371 1.00 38.13 ? 168 ARG D CA  1 
ATOM   6096 C  C   . ARG D 1 173 ? 2.184   -5.906  -38.723 1.00 34.15 ? 168 ARG D C   1 
ATOM   6097 O  O   . ARG D 1 173 ? 1.890   -4.686  -38.927 1.00 35.58 ? 168 ARG D O   1 
ATOM   6098 C  CB  . ARG D 1 173 ? 1.337   -6.877  -40.902 1.00 46.27 ? 168 ARG D CB  1 
ATOM   6099 C  CG  . ARG D 1 173 ? 0.968   -8.165  -41.625 1.00 58.06 ? 168 ARG D CG  1 
ATOM   6100 C  CD  . ARG D 1 173 ? 1.527   -8.289  -43.039 1.00 65.89 ? 168 ARG D CD  1 
ATOM   6101 N  NE  . ARG D 1 173 ? 2.840   -7.665  -43.166 1.00 76.46 ? 168 ARG D NE  1 
ATOM   6102 C  CZ  . ARG D 1 173 ? 3.974   -8.124  -42.634 1.00 77.41 ? 168 ARG D CZ  1 
ATOM   6103 N  NH1 . ARG D 1 173 ? 3.987   -9.241  -41.927 1.00 77.90 ? 168 ARG D NH1 1 
ATOM   6104 N  NH2 . ARG D 1 173 ? 5.101   -7.454  -42.815 1.00 80.16 ? 168 ARG D NH2 1 
ATOM   6105 N  N   . VAL D 1 174 ? 3.196   -6.313  -37.963 1.00 29.49 ? 169 VAL D N   1 
ATOM   6106 C  CA  . VAL D 1 174 ? 4.026   -5.338  -37.211 1.00 31.24 ? 169 VAL D CA  1 
ATOM   6107 C  C   . VAL D 1 174 ? 4.982   -4.670  -38.209 1.00 32.33 ? 169 VAL D C   1 
ATOM   6108 O  O   . VAL D 1 174 ? 5.965   -5.323  -38.631 1.00 33.25 ? 169 VAL D O   1 
ATOM   6109 C  CB  . VAL D 1 174 ? 4.767   -5.974  -36.027 1.00 28.54 ? 169 VAL D CB  1 
ATOM   6110 C  CG1 . VAL D 1 174 ? 5.678   -4.943  -35.392 1.00 26.33 ? 169 VAL D CG1 1 
ATOM   6111 C  CG2 . VAL D 1 174 ? 3.803   -6.564  -35.017 1.00 26.30 ? 169 VAL D CG2 1 
ATOM   6112 N  N   . ALA D 1 175 ? 4.660   -3.424  -38.571 1.00 32.63 ? 170 ALA D N   1 
ATOM   6113 C  CA  . ALA D 1 175 ? 5.473   -2.492  -39.385 1.00 33.02 ? 170 ALA D CA  1 
ATOM   6114 C  C   . ALA D 1 175 ? 6.590   -1.901  -38.531 1.00 32.05 ? 170 ALA D C   1 
ATOM   6115 O  O   . ALA D 1 175 ? 7.665   -1.732  -39.055 1.00 29.55 ? 170 ALA D O   1 
ATOM   6116 C  CB  . ALA D 1 175 ? 4.597   -1.398  -39.948 1.00 33.45 ? 170 ALA D CB  1 
ATOM   6117 N  N   . GLU D 1 176 ? 6.335   -1.597  -37.254 1.00 31.21 ? 171 GLU D N   1 
ATOM   6118 C  CA  . GLU D 1 176 ? 7.371   -1.032  -36.352 1.00 31.81 ? 171 GLU D CA  1 
ATOM   6119 C  C   . GLU D 1 176 ? 7.097   -1.477  -34.916 1.00 29.36 ? 171 GLU D C   1 
ATOM   6120 O  O   . GLU D 1 176 ? 5.921   -1.653  -34.550 1.00 25.77 ? 171 GLU D O   1 
ATOM   6121 C  CB  . GLU D 1 176 ? 7.390   0.495   -36.458 1.00 36.11 ? 171 GLU D CB  1 
ATOM   6122 C  CG  . GLU D 1 176 ? 6.007   1.106   -36.560 1.00 43.41 ? 171 GLU D CG  1 
ATOM   6123 C  CD  . GLU D 1 176 ? 5.851   2.270   -37.531 1.00 54.06 ? 171 GLU D CD  1 
ATOM   6124 O  OE1 . GLU D 1 176 ? 4.669   2.652   -37.833 1.00 52.71 ? 171 GLU D OE1 1 
ATOM   6125 O  OE2 . GLU D 1 176 ? 6.900   2.807   -37.977 1.00 57.77 ? 171 GLU D OE2 1 
ATOM   6126 N  N   . ALA D 1 177 ? 8.162   -1.637  -34.143 1.00 27.31 ? 172 ALA D N   1 
ATOM   6127 C  CA  . ALA D 1 177 ? 8.118   -2.084  -32.738 1.00 29.59 ? 172 ALA D CA  1 
ATOM   6128 C  C   . ALA D 1 177 ? 9.134   -1.263  -31.955 1.00 32.07 ? 172 ALA D C   1 
ATOM   6129 O  O   . ALA D 1 177 ? 10.279  -1.132  -32.426 1.00 33.87 ? 172 ALA D O   1 
ATOM   6130 C  CB  . ALA D 1 177 ? 8.425   -3.552  -32.644 1.00 28.84 ? 172 ALA D CB  1 
ATOM   6131 N  N   . ASP D 1 178 ? 8.710   -0.669  -30.847 1.00 29.93 ? 173 ASP D N   1 
ATOM   6132 C  CA  . ASP D 1 178 ? 9.625   0.115   -29.981 1.00 30.79 ? 173 ASP D CA  1 
ATOM   6133 C  C   . ASP D 1 178 ? 9.378   -0.378  -28.567 1.00 25.43 ? 173 ASP D C   1 
ATOM   6134 O  O   . ASP D 1 178 ? 8.248   -0.799  -28.279 1.00 23.39 ? 173 ASP D O   1 
ATOM   6135 C  CB  . ASP D 1 178 ? 9.431   1.617   -30.190 1.00 33.92 ? 173 ASP D CB  1 
ATOM   6136 C  CG  . ASP D 1 178 ? 9.575   2.030   -31.648 1.00 38.88 ? 173 ASP D CG  1 
ATOM   6137 O  OD1 . ASP D 1 178 ? 10.745  2.174   -32.095 1.00 42.27 ? 173 ASP D OD1 1 
ATOM   6138 O  OD2 . ASP D 1 178 ? 8.514   2.152   -32.351 1.00 35.70 ? 173 ASP D OD2 1 
ATOM   6139 N  N   . GLY D 1 179 ? 10.442  -0.439  -27.787 1.00 25.29 ? 174 GLY D N   1 
ATOM   6140 C  CA  . GLY D 1 179 ? 10.435  -0.959  -26.409 1.00 27.08 ? 174 GLY D CA  1 
ATOM   6141 C  C   . GLY D 1 179 ? 11.008  0.062   -25.465 1.00 25.42 ? 174 GLY D C   1 
ATOM   6142 O  O   . GLY D 1 179 ? 12.141  0.536   -25.755 1.00 21.82 ? 174 GLY D O   1 
ATOM   6143 N  N   . MET D 1 180 ? 10.229  0.456   -24.453 1.00 24.72 ? 175 MET D N   1 
ATOM   6144 C  CA  . MET D 1 180 ? 10.753  1.220   -23.297 1.00 24.92 ? 175 MET D CA  1 
ATOM   6145 C  C   . MET D 1 180 ? 11.080  0.241   -22.172 1.00 25.25 ? 175 MET D C   1 
ATOM   6146 O  O   . MET D 1 180 ? 10.158  -0.369  -21.629 1.00 22.07 ? 175 MET D O   1 
ATOM   6147 C  CB  . MET D 1 180 ? 9.752   2.257   -22.788 1.00 26.98 ? 175 MET D CB  1 
ATOM   6148 C  CG  . MET D 1 180 ? 10.274  3.045   -21.565 1.00 28.11 ? 175 MET D CG  1 
ATOM   6149 S  SD  . MET D 1 180 ? 11.247  4.495   -21.985 1.00 30.50 ? 175 MET D SD  1 
ATOM   6150 C  CE  . MET D 1 180 ? 9.967   5.533   -22.707 1.00 29.17 ? 175 MET D CE  1 
ATOM   6151 N  N   . PHE D 1 181 ? 12.356  0.093   -21.822 1.00 24.02 ? 176 PHE D N   1 
ATOM   6152 C  CA  . PHE D 1 181 ? 12.760  -0.642  -20.603 1.00 25.52 ? 176 PHE D CA  1 
ATOM   6153 C  C   . PHE D 1 181 ? 13.418  0.331   -19.619 1.00 25.54 ? 176 PHE D C   1 
ATOM   6154 O  O   . PHE D 1 181 ? 14.676  0.474   -19.551 1.00 23.87 ? 176 PHE D O   1 
ATOM   6155 C  CB  . PHE D 1 181 ? 13.607  -1.857  -20.969 1.00 26.27 ? 176 PHE D CB  1 
ATOM   6156 C  CG  . PHE D 1 181 ? 12.836  -2.845  -21.789 1.00 28.74 ? 176 PHE D CG  1 
ATOM   6157 C  CD1 . PHE D 1 181 ? 12.594  -2.603  -23.129 1.00 27.67 ? 176 PHE D CD1 1 
ATOM   6158 C  CD2 . PHE D 1 181 ? 12.288  -3.975  -21.205 1.00 30.20 ? 176 PHE D CD2 1 
ATOM   6159 C  CE1 . PHE D 1 181 ? 11.869  -3.507  -23.882 1.00 29.29 ? 176 PHE D CE1 1 
ATOM   6160 C  CE2 . PHE D 1 181 ? 11.544  -4.867  -21.960 1.00 28.45 ? 176 PHE D CE2 1 
ATOM   6161 C  CZ  . PHE D 1 181 ? 11.345  -4.632  -23.295 1.00 29.89 ? 176 PHE D CZ  1 
ATOM   6162 N  N   . LYS D 1 182 ? 12.583  0.987   -18.826 1.00 23.25 ? 177 LYS D N   1 
ATOM   6163 C  CA  . LYS D 1 182 ? 13.068  2.037   -17.893 1.00 24.45 ? 177 LYS D CA  1 
ATOM   6164 C  C   . LYS D 1 182 ? 13.337  1.410   -16.514 1.00 23.90 ? 177 LYS D C   1 
ATOM   6165 O  O   . LYS D 1 182 ? 12.375  1.183   -15.743 1.00 20.58 ? 177 LYS D O   1 
ATOM   6166 C  CB  . LYS D 1 182 ? 12.066  3.191   -17.891 1.00 24.84 ? 177 LYS D CB  1 
ATOM   6167 C  CG  . LYS D 1 182 ? 12.436  4.322   -16.963 1.00 25.69 ? 177 LYS D CG  1 
ATOM   6168 C  CD  . LYS D 1 182 ? 11.601  5.542   -17.199 1.00 28.35 ? 177 LYS D CD  1 
ATOM   6169 C  CE  . LYS D 1 182 ? 11.686  6.502   -16.042 1.00 30.61 ? 177 LYS D CE  1 
ATOM   6170 N  NZ  . LYS D 1 182 ? 13.074  6.579   -15.515 1.00 32.31 ? 177 LYS D NZ  1 
ATOM   6171 N  N   . LEU D 1 183 ? 14.614  1.117   -16.242 1.00 22.10 ? 178 LEU D N   1 
ATOM   6172 C  CA  . LEU D 1 183 ? 15.069  0.152   -15.206 1.00 24.24 ? 178 LEU D CA  1 
ATOM   6173 C  C   . LEU D 1 183 ? 16.308  0.711   -14.493 1.00 25.05 ? 178 LEU D C   1 
ATOM   6174 O  O   . LEU D 1 183 ? 17.170  -0.127  -14.131 1.00 22.68 ? 178 LEU D O   1 
ATOM   6175 C  CB  . LEU D 1 183 ? 15.407  -1.183  -15.883 1.00 25.89 ? 178 LEU D CB  1 
ATOM   6176 C  CG  . LEU D 1 183 ? 14.268  -1.915  -16.592 1.00 26.72 ? 178 LEU D CG  1 
ATOM   6177 C  CD1 . LEU D 1 183 ? 14.818  -3.148  -17.296 1.00 27.76 ? 178 LEU D CD1 1 
ATOM   6178 C  CD2 . LEU D 1 183 ? 13.145  -2.305  -15.635 1.00 26.80 ? 178 LEU D CD2 1 
ATOM   6179 N  N   . SER D 1 184 ? 16.371  2.047   -14.305 1.00 23.11 ? 179 SER D N   1 
ATOM   6180 C  CA  . SER D 1 184 ? 17.431  2.798   -13.588 1.00 26.78 ? 179 SER D CA  1 
ATOM   6181 C  C   . SER D 1 184 ? 18.780  2.805   -14.347 1.00 28.26 ? 179 SER D C   1 
ATOM   6182 O  O   . SER D 1 184 ? 19.813  3.063   -13.690 1.00 27.21 ? 179 SER D O   1 
ATOM   6183 C  CB  . SER D 1 184 ? 17.597  2.246   -12.180 1.00 28.59 ? 179 SER D CB  1 
ATOM   6184 O  OG  . SER D 1 184 ? 16.361  2.305   -11.479 1.00 30.23 ? 179 SER D OG  1 
ATOM   6185 N  N   . GLN D 1 185 ? 18.799  2.606   -15.667 1.00 26.55 ? 180 GLN D N   1 
ATOM   6186 C  CA  . GLN D 1 185 ? 20.069  2.576   -16.445 1.00 29.95 ? 180 GLN D CA  1 
ATOM   6187 C  C   . GLN D 1 185 ? 20.782  3.936   -16.350 1.00 30.11 ? 180 GLN D C   1 
ATOM   6188 O  O   . GLN D 1 185 ? 22.025  3.964   -16.393 1.00 31.13 ? 180 GLN D O   1 
ATOM   6189 C  CB  . GLN D 1 185 ? 19.838  2.189   -17.903 1.00 28.26 ? 180 GLN D CB  1 
ATOM   6190 C  CG  . GLN D 1 185 ? 19.371  0.753   -18.095 1.00 28.58 ? 180 GLN D CG  1 
ATOM   6191 C  CD  . GLN D 1 185 ? 17.864  0.691   -18.191 1.00 25.42 ? 180 GLN D CD  1 
ATOM   6192 O  OE1 . GLN D 1 185 ? 17.167  1.411   -17.497 1.00 24.14 ? 180 GLN D OE1 1 
ATOM   6193 N  NE2 . GLN D 1 185 ? 17.359  -0.134  -19.083 1.00 24.19 ? 180 GLN D NE2 1 
ATOM   6194 N  N   . GLU D 1 186 ? 20.024  5.011   -16.175 1.00 33.33 ? 181 GLU D N   1 
ATOM   6195 C  CA  . GLU D 1 186 ? 20.520  6.407   -16.073 1.00 35.64 ? 181 GLU D CA  1 
ATOM   6196 C  C   . GLU D 1 186 ? 21.326  6.584   -14.771 1.00 39.02 ? 181 GLU D C   1 
ATOM   6197 O  O   . GLU D 1 186 ? 22.133  7.493   -14.721 1.00 35.65 ? 181 GLU D O   1 
ATOM   6198 C  CB  . GLU D 1 186 ? 19.331  7.366   -16.149 1.00 37.97 ? 181 GLU D CB  1 
ATOM   6199 C  CG  . GLU D 1 186 ? 18.609  7.573   -14.818 1.00 39.18 ? 181 GLU D CG  1 
ATOM   6200 C  CD  . GLU D 1 186 ? 17.531  6.584   -14.383 1.00 39.20 ? 181 GLU D CD  1 
ATOM   6201 O  OE1 . GLU D 1 186 ? 17.260  5.580   -15.110 1.00 33.04 ? 181 GLU D OE1 1 
ATOM   6202 O  OE2 . GLU D 1 186 ? 16.935  6.845   -13.308 1.00 34.24 ? 181 GLU D OE2 1 
ATOM   6203 N  N   . GLN D 1 187 ? 21.120  5.737   -13.751 1.00 37.86 ? 182 GLN D N   1 
ATOM   6204 C  CA  . GLN D 1 187 ? 21.776  5.865   -12.414 1.00 33.20 ? 182 GLN D CA  1 
ATOM   6205 C  C   . GLN D 1 187 ? 23.196  5.271   -12.451 1.00 32.75 ? 182 GLN D C   1 
ATOM   6206 O  O   . GLN D 1 187 ? 23.436  4.403   -13.290 1.00 27.62 ? 182 GLN D O   1 
ATOM   6207 C  CB  . GLN D 1 187 ? 20.947  5.143   -11.343 1.00 31.94 ? 182 GLN D CB  1 
ATOM   6208 C  CG  . GLN D 1 187 ? 19.578  5.750   -11.083 1.00 31.58 ? 182 GLN D CG  1 
ATOM   6209 C  CD  . GLN D 1 187 ? 19.673  7.185   -10.635 1.00 33.29 ? 182 GLN D CD  1 
ATOM   6210 O  OE1 . GLN D 1 187 ? 20.518  7.549   -9.815  1.00 36.53 ? 182 GLN D OE1 1 
ATOM   6211 N  NE2 . GLN D 1 187 ? 18.804  8.012   -11.187 1.00 33.35 ? 182 GLN D NE2 1 
ATOM   6212 N  N   . GLN D 1 188 ? 24.079  5.708   -11.541 1.00 33.60 ? 183 GLN D N   1 
ATOM   6213 C  CA  . GLN D 1 188 ? 25.424  5.118   -11.287 1.00 35.69 ? 183 GLN D CA  1 
ATOM   6214 C  C   . GLN D 1 188 ? 25.240  3.686   -10.798 1.00 38.49 ? 183 GLN D C   1 
ATOM   6215 O  O   . GLN D 1 188 ? 24.277  3.405   -10.091 1.00 38.00 ? 183 GLN D O   1 
ATOM   6216 C  CB  . GLN D 1 188 ? 26.160  5.918   -10.213 1.00 38.95 ? 183 GLN D CB  1 
ATOM   6217 C  CG  . GLN D 1 188 ? 26.564  7.319   -10.648 1.00 41.86 ? 183 GLN D CG  1 
ATOM   6218 C  CD  . GLN D 1 188 ? 27.842  7.293   -11.456 1.00 49.79 ? 183 GLN D CD  1 
ATOM   6219 O  OE1 . GLN D 1 188 ? 27.854  6.949   -12.640 1.00 51.77 ? 183 GLN D OE1 1 
ATOM   6220 N  NE2 . GLN D 1 188 ? 28.942  7.665   -10.820 1.00 51.28 ? 183 GLN D NE2 1 
ATOM   6221 N  N   . PRO D 1 189 ? 26.158  2.744   -11.107 1.00 38.69 ? 184 PRO D N   1 
ATOM   6222 C  CA  . PRO D 1 189 ? 25.917  1.322   -10.859 1.00 37.91 ? 184 PRO D CA  1 
ATOM   6223 C  C   . PRO D 1 189 ? 25.588  0.958   -9.403  1.00 36.71 ? 184 PRO D C   1 
ATOM   6224 O  O   . PRO D 1 189 ? 24.792  0.056   -9.204  1.00 34.61 ? 184 PRO D O   1 
ATOM   6225 C  CB  . PRO D 1 189 ? 27.246  0.679   -11.269 1.00 38.83 ? 184 PRO D CB  1 
ATOM   6226 C  CG  . PRO D 1 189 ? 27.782  1.634   -12.302 1.00 38.90 ? 184 PRO D CG  1 
ATOM   6227 C  CD  . PRO D 1 189 ? 27.477  2.988   -11.704 1.00 38.08 ? 184 PRO D CD  1 
ATOM   6228 N  N   . ALA D 1 190 ? 26.216  1.637   -8.438  1.00 38.40 ? 185 ALA D N   1 
ATOM   6229 C  CA  . ALA D 1 190 ? 26.008  1.420   -6.988  1.00 37.21 ? 185 ALA D CA  1 
ATOM   6230 C  C   . ALA D 1 190 ? 24.560  1.785   -6.623  1.00 35.23 ? 185 ALA D C   1 
ATOM   6231 O  O   . ALA D 1 190 ? 23.982  1.116   -5.763  1.00 34.00 ? 185 ALA D O   1 
ATOM   6232 C  CB  . ALA D 1 190 ? 27.010  2.212   -6.190  1.00 36.95 ? 185 ALA D CB  1 
ATOM   6233 N  N   . ILE D 1 191 ? 23.988  2.798   -7.275  1.00 31.37 ? 186 ILE D N   1 
ATOM   6234 C  CA  . ILE D 1 191 ? 22.577  3.242   -7.064  1.00 31.26 ? 186 ILE D CA  1 
ATOM   6235 C  C   . ILE D 1 191 ? 21.640  2.238   -7.730  1.00 29.57 ? 186 ILE D C   1 
ATOM   6236 O  O   . ILE D 1 191 ? 20.578  1.940   -7.164  1.00 32.36 ? 186 ILE D O   1 
ATOM   6237 C  CB  . ILE D 1 191 ? 22.342  4.652   -7.633  1.00 30.91 ? 186 ILE D CB  1 
ATOM   6238 C  CG1 . ILE D 1 191 ? 23.369  5.660   -7.121  1.00 33.94 ? 186 ILE D CG1 1 
ATOM   6239 C  CG2 . ILE D 1 191 ? 20.912  5.092   -7.365  1.00 30.06 ? 186 ILE D CG2 1 
ATOM   6240 C  CD1 . ILE D 1 191 ? 23.470  5.730   -5.620  1.00 37.77 ? 186 ILE D CD1 1 
ATOM   6241 N  N   . ARG D 1 192 ? 22.013  1.741   -8.901  1.00 29.70 ? 187 ARG D N   1 
ATOM   6242 C  CA  . ARG D 1 192 ? 21.177  0.769   -9.648  1.00 33.72 ? 187 ARG D CA  1 
ATOM   6243 C  C   . ARG D 1 192 ? 21.073  -0.504  -8.807  1.00 31.34 ? 187 ARG D C   1 
ATOM   6244 O  O   . ARG D 1 192 ? 19.942  -1.041  -8.722  1.00 25.56 ? 187 ARG D O   1 
ATOM   6245 C  CB  . ARG D 1 192 ? 21.748  0.506   -11.043 1.00 38.05 ? 187 ARG D CB  1 
ATOM   6246 C  CG  . ARG D 1 192 ? 21.752  1.757   -11.903 1.00 42.41 ? 187 ARG D CG  1 
ATOM   6247 C  CD  . ARG D 1 192 ? 22.684  1.707   -13.088 1.00 47.89 ? 187 ARG D CD  1 
ATOM   6248 N  NE  . ARG D 1 192 ? 22.604  0.482   -13.864 1.00 48.51 ? 187 ARG D NE  1 
ATOM   6249 C  CZ  . ARG D 1 192 ? 23.640  -0.086  -14.465 1.00 53.71 ? 187 ARG D CZ  1 
ATOM   6250 N  NH1 . ARG D 1 192 ? 24.854  0.440   -14.362 1.00 53.81 ? 187 ARG D NH1 1 
ATOM   6251 N  NH2 . ARG D 1 192 ? 23.455  -1.197  -15.157 1.00 57.97 ? 187 ARG D NH2 1 
ATOM   6252 N  N   . ARG D 1 193 ? 22.190  -0.933  -8.199  1.00 28.56 ? 188 ARG D N   1 
ATOM   6253 C  CA  . ARG D 1 193 ? 22.237  -2.084  -7.250  1.00 30.58 ? 188 ARG D CA  1 
ATOM   6254 C  C   . ARG D 1 193 ? 21.237  -1.867  -6.109  1.00 27.73 ? 188 ARG D C   1 
ATOM   6255 O  O   . ARG D 1 193 ? 20.502  -2.792  -5.797  1.00 26.76 ? 188 ARG D O   1 
ATOM   6256 C  CB  . ARG D 1 193 ? 23.622  -2.256  -6.626  1.00 36.48 ? 188 ARG D CB  1 
ATOM   6257 C  CG  . ARG D 1 193 ? 24.394  -3.474  -7.109  1.00 45.59 ? 188 ARG D CG  1 
ATOM   6258 C  CD  . ARG D 1 193 ? 25.801  -3.518  -6.532  1.00 48.17 ? 188 ARG D CD  1 
ATOM   6259 N  NE  . ARG D 1 193 ? 25.872  -4.097  -5.191  1.00 53.63 ? 188 ARG D NE  1 
ATOM   6260 C  CZ  . ARG D 1 193 ? 25.851  -5.404  -4.904  1.00 58.59 ? 188 ARG D CZ  1 
ATOM   6261 N  NH1 . ARG D 1 193 ? 25.715  -6.311  -5.861  1.00 62.70 ? 188 ARG D NH1 1 
ATOM   6262 N  NH2 . ARG D 1 193 ? 25.943  -5.802  -3.646  1.00 58.62 ? 188 ARG D NH2 1 
ATOM   6263 N  N   . ARG D 1 194 ? 21.264  -0.695  -5.473  1.00 26.13 ? 189 ARG D N   1 
ATOM   6264 C  CA  . ARG D 1 194 ? 20.350  -0.378  -4.348  1.00 28.18 ? 189 ARG D CA  1 
ATOM   6265 C  C   . ARG D 1 194 ? 18.885  -0.536  -4.783  1.00 27.40 ? 189 ARG D C   1 
ATOM   6266 O  O   . ARG D 1 194 ? 18.093  -1.084  -3.991  1.00 26.21 ? 189 ARG D O   1 
ATOM   6267 C  CB  . ARG D 1 194 ? 20.626  1.028   -3.821  1.00 29.51 ? 189 ARG D CB  1 
ATOM   6268 C  CG  . ARG D 1 194 ? 21.961  1.138   -3.109  1.00 29.79 ? 189 ARG D CG  1 
ATOM   6269 C  CD  . ARG D 1 194 ? 22.229  2.554   -2.652  1.00 31.99 ? 189 ARG D CD  1 
ATOM   6270 N  NE  . ARG D 1 194 ? 23.603  2.636   -2.195  1.00 34.02 ? 189 ARG D NE  1 
ATOM   6271 C  CZ  . ARG D 1 194 ? 24.234  3.750   -1.871  1.00 33.60 ? 189 ARG D CZ  1 
ATOM   6272 N  NH1 . ARG D 1 194 ? 23.619  4.913   -1.952  1.00 32.19 ? 189 ARG D NH1 1 
ATOM   6273 N  NH2 . ARG D 1 194 ? 25.493  3.691   -1.473  1.00 35.99 ? 189 ARG D NH2 1 
ATOM   6274 N  N   . VAL D 1 195 ? 18.516  -0.053  -5.969  1.00 26.86 ? 190 VAL D N   1 
ATOM   6275 C  CA  . VAL D 1 195 ? 17.108  -0.167  -6.463  1.00 27.22 ? 190 VAL D CA  1 
ATOM   6276 C  C   . VAL D 1 195 ? 16.788  -1.657  -6.678  1.00 26.63 ? 190 VAL D C   1 
ATOM   6277 O  O   . VAL D 1 195 ? 15.674  -2.107  -6.298  1.00 23.57 ? 190 VAL D O   1 
ATOM   6278 C  CB  . VAL D 1 195 ? 16.881  0.647   -7.749  1.00 28.06 ? 190 VAL D CB  1 
ATOM   6279 C  CG1 . VAL D 1 195 ? 15.460  0.450   -8.277  1.00 29.65 ? 190 VAL D CG1 1 
ATOM   6280 C  CG2 . VAL D 1 195 ? 17.210  2.136   -7.557  1.00 27.63 ? 190 VAL D CG2 1 
ATOM   6281 N  N   . ARG D 1 196 ? 17.710  -2.399  -7.291  1.00 25.18 ? 191 ARG D N   1 
ATOM   6282 C  CA  . ARG D 1 196 ? 17.501  -3.827  -7.641  1.00 28.01 ? 191 ARG D CA  1 
ATOM   6283 C  C   . ARG D 1 196 ? 17.239  -4.608  -6.352  1.00 28.55 ? 191 ARG D C   1 
ATOM   6284 O  O   . ARG D 1 196 ? 16.300  -5.439  -6.344  1.00 27.92 ? 191 ARG D O   1 
ATOM   6285 C  CB  . ARG D 1 196 ? 18.703  -4.401  -8.387  1.00 28.97 ? 191 ARG D CB  1 
ATOM   6286 C  CG  . ARG D 1 196 ? 18.580  -5.887  -8.681  1.00 31.06 ? 191 ARG D CG  1 
ATOM   6287 C  CD  . ARG D 1 196 ? 19.607  -6.318  -9.689  1.00 33.80 ? 191 ARG D CD  1 
ATOM   6288 N  NE  . ARG D 1 196 ? 20.963  -6.049  -9.226  1.00 35.76 ? 191 ARG D NE  1 
ATOM   6289 C  CZ  . ARG D 1 196 ? 21.713  -6.877  -8.501  1.00 37.97 ? 191 ARG D CZ  1 
ATOM   6290 N  NH1 . ARG D 1 196 ? 21.249  -8.053  -8.116  1.00 38.18 ? 191 ARG D NH1 1 
ATOM   6291 N  NH2 . ARG D 1 196 ? 22.947  -6.523  -8.176  1.00 40.50 ? 191 ARG D NH2 1 
ATOM   6292 N  N   . HIS D 1 197 ? 18.043  -4.333  -5.320  1.00 27.87 ? 192 HIS D N   1 
ATOM   6293 C  CA  . HIS D 1 197 ? 18.008  -5.015  -3.999  1.00 29.09 ? 192 HIS D CA  1 
ATOM   6294 C  C   . HIS D 1 197 ? 16.739  -4.603  -3.245  1.00 28.29 ? 192 HIS D C   1 
ATOM   6295 O  O   . HIS D 1 197 ? 16.078  -5.499  -2.721  1.00 27.24 ? 192 HIS D O   1 
ATOM   6296 C  CB  . HIS D 1 197 ? 19.309  -4.767  -3.225  1.00 31.00 ? 192 HIS D CB  1 
ATOM   6297 C  CG  . HIS D 1 197 ? 20.433  -5.605  -3.736  1.00 32.50 ? 192 HIS D CG  1 
ATOM   6298 N  ND1 . HIS D 1 197 ? 20.231  -6.879  -4.212  1.00 30.87 ? 192 HIS D ND1 1 
ATOM   6299 C  CD2 . HIS D 1 197 ? 21.759  -5.367  -3.848  1.00 34.89 ? 192 HIS D CD2 1 
ATOM   6300 C  CE1 . HIS D 1 197 ? 21.381  -7.396  -4.596  1.00 32.13 ? 192 HIS D CE1 1 
ATOM   6301 N  NE2 . HIS D 1 197 ? 22.324  -6.481  -4.421  1.00 30.36 ? 192 HIS D NE2 1 
ATOM   6302 N  N   . SER D 1 198 ? 16.369  -3.315  -3.264  1.00 26.21 ? 193 SER D N   1 
ATOM   6303 C  CA  . SER D 1 198 ? 15.080  -2.838  -2.696  1.00 27.79 ? 193 SER D CA  1 
ATOM   6304 C  C   . SER D 1 198 ? 13.942  -3.620  -3.353  1.00 27.19 ? 193 SER D C   1 
ATOM   6305 O  O   . SER D 1 198 ? 13.137  -4.200  -2.626  1.00 28.88 ? 193 SER D O   1 
ATOM   6306 C  CB  . SER D 1 198 ? 14.879  -1.340  -2.836  1.00 29.22 ? 193 SER D CB  1 
ATOM   6307 O  OG  . SER D 1 198 ? 13.898  -0.874  -1.903  1.00 29.47 ? 193 SER D OG  1 
ATOM   6308 N  N   . PHE D 1 199 ? 13.887  -3.656  -4.681  1.00 25.27 ? 194 PHE D N   1 
ATOM   6309 C  CA  . PHE D 1 199 ? 12.731  -4.226  -5.423  1.00 24.67 ? 194 PHE D CA  1 
ATOM   6310 C  C   . PHE D 1 199 ? 12.690  -5.748  -5.212  1.00 23.62 ? 194 PHE D C   1 
ATOM   6311 O  O   . PHE D 1 199 ? 11.585  -6.337  -5.302  1.00 23.26 ? 194 PHE D O   1 
ATOM   6312 C  CB  . PHE D 1 199 ? 12.779  -3.769  -6.884  1.00 26.54 ? 194 PHE D CB  1 
ATOM   6313 C  CG  . PHE D 1 199 ? 12.357  -2.341  -7.155  1.00 27.69 ? 194 PHE D CG  1 
ATOM   6314 C  CD1 . PHE D 1 199 ? 11.536  -1.637  -6.276  1.00 31.29 ? 194 PHE D CD1 1 
ATOM   6315 C  CD2 . PHE D 1 199 ? 12.663  -1.741  -8.366  1.00 28.48 ? 194 PHE D CD2 1 
ATOM   6316 C  CE1 . PHE D 1 199 ? 11.108  -0.344  -6.557  1.00 30.01 ? 194 PHE D CE1 1 
ATOM   6317 C  CE2 . PHE D 1 199 ? 12.232  -0.453  -8.646  1.00 29.09 ? 194 PHE D CE2 1 
ATOM   6318 C  CZ  . PHE D 1 199 ? 11.458  0.248   -7.739  1.00 27.98 ? 194 PHE D CZ  1 
ATOM   6319 N  N   . GLY D 1 200 ? 13.843  -6.368  -4.925  1.00 22.55 ? 195 GLY D N   1 
ATOM   6320 C  CA  . GLY D 1 200 ? 13.963  -7.798  -4.608  1.00 24.91 ? 195 GLY D CA  1 
ATOM   6321 C  C   . GLY D 1 200 ? 13.260  -8.176  -3.312  1.00 24.63 ? 195 GLY D C   1 
ATOM   6322 O  O   . GLY D 1 200 ? 12.999  -9.360  -3.145  1.00 24.64 ? 195 GLY D O   1 
ATOM   6323 N  N   . GLY D 1 201 ? 12.952  -7.209  -2.436  1.00 27.88 ? 196 GLY D N   1 
ATOM   6324 C  CA  . GLY D 1 201 ? 12.466  -7.450  -1.066  1.00 27.32 ? 196 GLY D CA  1 
ATOM   6325 C  C   . GLY D 1 201 ? 10.957  -7.446  -0.946  1.00 27.73 ? 196 GLY D C   1 
ATOM   6326 O  O   . GLY D 1 201 ? 10.483  -7.525  0.169   1.00 30.53 ? 196 GLY D O   1 
ATOM   6327 N  N   . ALA D 1 202 ? 10.215  -7.408  -2.043  1.00 28.61 ? 197 ALA D N   1 
ATOM   6328 C  CA  . ALA D 1 202 ? 8.731   -7.464  -2.039  1.00 27.17 ? 197 ALA D CA  1 
ATOM   6329 C  C   . ALA D 1 202 ? 8.255   -8.074  -3.347  1.00 26.26 ? 197 ALA D C   1 
ATOM   6330 O  O   . ALA D 1 202 ? 8.783   -7.710  -4.412  1.00 25.84 ? 197 ALA D O   1 
ATOM   6331 C  CB  . ALA D 1 202 ? 8.114   -6.096  -1.819  1.00 27.06 ? 197 ALA D CB  1 
ATOM   6332 N  N   . GLU D 1 203 ? 7.243   -8.937  -3.267  1.00 27.31 ? 198 GLU D N   1 
ATOM   6333 C  CA  . GLU D 1 203 ? 6.730   -9.679  -4.442  1.00 28.24 ? 198 GLU D CA  1 
ATOM   6334 C  C   . GLU D 1 203 ? 6.222   -8.692  -5.504  1.00 28.17 ? 198 GLU D C   1 
ATOM   6335 O  O   . GLU D 1 203 ? 6.439   -8.964  -6.708  1.00 27.38 ? 198 GLU D O   1 
ATOM   6336 C  CB  . GLU D 1 203 ? 5.664   -10.682 -3.996  1.00 29.81 ? 198 GLU D CB  1 
ATOM   6337 C  CG  . GLU D 1 203 ? 5.230   -11.617 -5.103  1.00 32.99 ? 198 GLU D CG  1 
ATOM   6338 C  CD  . GLU D 1 203 ? 6.332   -12.451 -5.736  1.00 38.08 ? 198 GLU D CD  1 
ATOM   6339 O  OE1 . GLU D 1 203 ? 7.410   -12.560 -5.130  1.00 40.62 ? 198 GLU D OE1 1 
ATOM   6340 O  OE2 . GLU D 1 203 ? 6.119   -12.973 -6.850  1.00 39.23 ? 198 GLU D OE2 1 
ATOM   6341 N  N   . ALA D 1 204 ? 5.536   -7.613  -5.097  1.00 28.99 ? 199 ALA D N   1 
ATOM   6342 C  CA  . ALA D 1 204 ? 4.962   -6.600  -6.016  1.00 28.50 ? 199 ALA D CA  1 
ATOM   6343 C  C   . ALA D 1 204 ? 6.067   -5.998  -6.892  1.00 27.74 ? 199 ALA D C   1 
ATOM   6344 O  O   . ALA D 1 204 ? 5.765   -5.556  -7.979  1.00 29.24 ? 199 ALA D O   1 
ATOM   6345 C  CB  . ALA D 1 204 ? 4.222   -5.535  -5.241  1.00 30.86 ? 199 ALA D CB  1 
ATOM   6346 N  N   . THR D 1 205 ? 7.327   -5.990  -6.461  1.00 27.84 ? 200 THR D N   1 
ATOM   6347 C  CA  . THR D 1 205 ? 8.409   -5.316  -7.232  1.00 27.20 ? 200 THR D CA  1 
ATOM   6348 C  C   . THR D 1 205 ? 9.449   -6.322  -7.752  1.00 27.28 ? 200 THR D C   1 
ATOM   6349 O  O   . THR D 1 205 ? 10.351  -5.875  -8.470  1.00 27.89 ? 200 THR D O   1 
ATOM   6350 C  CB  . THR D 1 205 ? 9.033   -4.202  -6.386  1.00 28.12 ? 200 THR D CB  1 
ATOM   6351 O  OG1 . THR D 1 205 ? 9.500   -4.798  -5.174  1.00 27.19 ? 200 THR D OG1 1 
ATOM   6352 C  CG2 . THR D 1 205 ? 8.066   -3.064  -6.107  1.00 27.51 ? 200 THR D CG2 1 
ATOM   6353 N  N   . ARG D 1 206 ? 9.275   -7.621  -7.497  1.00 26.67 ? 201 ARG D N   1 
ATOM   6354 C  CA  . ARG D 1 206 ? 10.310  -8.646  -7.782  1.00 29.29 ? 201 ARG D CA  1 
ATOM   6355 C  C   . ARG D 1 206 ? 10.505  -8.805  -9.295  1.00 26.47 ? 201 ARG D C   1 
ATOM   6356 O  O   . ARG D 1 206 ? 11.665  -8.976  -9.689  1.00 21.41 ? 201 ARG D O   1 
ATOM   6357 C  CB  . ARG D 1 206 ? 9.985   -9.998  -7.146  1.00 31.12 ? 201 ARG D CB  1 
ATOM   6358 C  CG  . ARG D 1 206 ? 11.039  -11.057 -7.444  1.00 32.57 ? 201 ARG D CG  1 
ATOM   6359 C  CD  . ARG D 1 206 ? 11.021  -12.200 -6.452  1.00 36.04 ? 201 ARG D CD  1 
ATOM   6360 N  NE  . ARG D 1 206 ? 9.804   -12.949 -6.650  1.00 38.82 ? 201 ARG D NE  1 
ATOM   6361 C  CZ  . ARG D 1 206 ? 9.614   -13.839 -7.615  1.00 41.69 ? 201 ARG D CZ  1 
ATOM   6362 N  NH1 . ARG D 1 206 ? 10.581  -14.107 -8.475  1.00 40.71 ? 201 ARG D NH1 1 
ATOM   6363 N  NH2 . ARG D 1 206 ? 8.452   -14.462 -7.711  1.00 44.02 ? 201 ARG D NH2 1 
ATOM   6364 N  N   . ALA D 1 207 ? 9.441   -8.746  -10.104 1.00 24.30 ? 202 ALA D N   1 
ATOM   6365 C  CA  . ALA D 1 207 ? 9.563   -8.862  -11.583 1.00 27.10 ? 202 ALA D CA  1 
ATOM   6366 C  C   . ALA D 1 207 ? 10.427  -7.717  -12.121 1.00 26.99 ? 202 ALA D C   1 
ATOM   6367 O  O   . ALA D 1 207 ? 11.235  -7.991  -13.034 1.00 29.21 ? 202 ALA D O   1 
ATOM   6368 C  CB  . ALA D 1 207 ? 8.216   -8.921  -12.266 1.00 28.28 ? 202 ALA D CB  1 
ATOM   6369 N  N   . VAL D 1 208 ? 10.313  -6.497  -11.575 1.00 25.83 ? 203 VAL D N   1 
ATOM   6370 C  CA  . VAL D 1 208 ? 11.175  -5.364  -12.016 1.00 26.13 ? 203 VAL D CA  1 
ATOM   6371 C  C   . VAL D 1 208 ? 12.631  -5.687  -11.666 1.00 25.87 ? 203 VAL D C   1 
ATOM   6372 O  O   . VAL D 1 208 ? 13.491  -5.464  -12.534 1.00 27.06 ? 203 VAL D O   1 
ATOM   6373 C  CB  . VAL D 1 208 ? 10.734  -4.010  -11.438 1.00 26.38 ? 203 VAL D CB  1 
ATOM   6374 C  CG1 . VAL D 1 208 ? 11.732  -2.926  -11.836 1.00 27.66 ? 203 VAL D CG1 1 
ATOM   6375 C  CG2 . VAL D 1 208 ? 9.313   -3.657  -11.888 1.00 25.13 ? 203 VAL D CG2 1 
ATOM   6376 N  N   . ALA D 1 209 ? 12.892  -6.195  -10.458 1.00 24.70 ? 204 ALA D N   1 
ATOM   6377 C  CA  . ALA D 1 209 ? 14.246  -6.597  -9.988  1.00 25.45 ? 204 ALA D CA  1 
ATOM   6378 C  C   . ALA D 1 209 ? 14.833  -7.649  -10.926 1.00 27.15 ? 204 ALA D C   1 
ATOM   6379 O  O   . ALA D 1 209 ? 16.068  -7.570  -11.224 1.00 27.80 ? 204 ALA D O   1 
ATOM   6380 C  CB  . ALA D 1 209 ? 14.185  -7.142  -8.590  1.00 25.36 ? 204 ALA D CB  1 
ATOM   6381 N  N   . GLY D 1 210 ? 13.997  -8.593  -11.368 1.00 25.96 ? 205 GLY D N   1 
ATOM   6382 C  CA  . GLY D 1 210 ? 14.367  -9.680  -12.303 1.00 28.38 ? 205 GLY D CA  1 
ATOM   6383 C  C   . GLY D 1 210 ? 14.866  -9.151  -13.653 1.00 30.28 ? 205 GLY D C   1 
ATOM   6384 O  O   . GLY D 1 210 ? 15.857  -9.695  -14.191 1.00 27.10 ? 205 GLY D O   1 
ATOM   6385 N  N   . LEU D 1 211 ? 14.225  -8.116  -14.199 1.00 29.31 ? 206 LEU D N   1 
ATOM   6386 C  CA  . LEU D 1 211 ? 14.677  -7.482  -15.472 1.00 28.07 ? 206 LEU D CA  1 
ATOM   6387 C  C   . LEU D 1 211 ? 15.958  -6.680  -15.197 1.00 28.84 ? 206 LEU D C   1 
ATOM   6388 O  O   . LEU D 1 211 ? 16.916  -6.825  -15.972 1.00 29.28 ? 206 LEU D O   1 
ATOM   6389 C  CB  . LEU D 1 211 ? 13.545  -6.633  -16.051 1.00 27.06 ? 206 LEU D CB  1 
ATOM   6390 C  CG  . LEU D 1 211 ? 12.292  -7.425  -16.430 1.00 27.90 ? 206 LEU D CG  1 
ATOM   6391 C  CD1 . LEU D 1 211 ? 11.070  -6.538  -16.455 1.00 28.47 ? 206 LEU D CD1 1 
ATOM   6392 C  CD2 . LEU D 1 211 ? 12.459  -8.122  -17.772 1.00 28.01 ? 206 LEU D CD2 1 
ATOM   6393 N  N   . MET D 1 212 ? 16.014  -5.924  -14.095 1.00 27.94 ? 207 MET D N   1 
ATOM   6394 C  CA  . MET D 1 212 ? 17.236  -5.166  -13.707 1.00 28.81 ? 207 MET D CA  1 
ATOM   6395 C  C   . MET D 1 212 ? 18.430  -6.138  -13.613 1.00 30.63 ? 207 MET D C   1 
ATOM   6396 O  O   . MET D 1 212 ? 19.511  -5.815  -14.143 1.00 32.57 ? 207 MET D O   1 
ATOM   6397 C  CB  . MET D 1 212 ? 17.030  -4.394  -12.403 1.00 26.02 ? 207 MET D CB  1 
ATOM   6398 C  CG  . MET D 1 212 ? 16.024  -3.263  -12.573 1.00 26.71 ? 207 MET D CG  1 
ATOM   6399 S  SD  . MET D 1 212 ? 15.672  -2.341  -11.074 1.00 26.70 ? 207 MET D SD  1 
ATOM   6400 C  CE  . MET D 1 212 ? 17.228  -1.451  -10.936 1.00 27.33 ? 207 MET D CE  1 
ATOM   6401 N  N   . ASP D 1 213 ? 18.209  -7.335  -13.079 1.00 30.69 ? 208 ASP D N   1 
ATOM   6402 C  CA  . ASP D 1 213 ? 19.266  -8.345  -12.837 1.00 32.61 ? 208 ASP D CA  1 
ATOM   6403 C  C   . ASP D 1 213 ? 19.776  -8.928  -14.166 1.00 35.15 ? 208 ASP D C   1 
ATOM   6404 O  O   . ASP D 1 213 ? 20.912  -9.424  -14.179 1.00 36.17 ? 208 ASP D O   1 
ATOM   6405 C  CB  . ASP D 1 213 ? 18.742  -9.441  -11.910 1.00 35.77 ? 208 ASP D CB  1 
ATOM   6406 C  CG  . ASP D 1 213 ? 19.859  -10.166 -11.179 1.00 42.28 ? 208 ASP D CG  1 
ATOM   6407 O  OD1 . ASP D 1 213 ? 20.712  -9.475  -10.568 1.00 50.17 ? 208 ASP D OD1 1 
ATOM   6408 O  OD2 . ASP D 1 213 ? 19.874  -11.402 -11.231 1.00 44.01 ? 208 ASP D OD2 1 
ATOM   6409 N  N   . ARG D 1 214 ? 18.973  -8.899  -15.234 1.00 36.09 ? 209 ARG D N   1 
ATOM   6410 C  CA  . ARG D 1 214 ? 19.333  -9.449  -16.572 1.00 38.72 ? 209 ARG D CA  1 
ATOM   6411 C  C   . ARG D 1 214 ? 19.946  -8.370  -17.482 1.00 39.83 ? 209 ARG D C   1 
ATOM   6412 O  O   . ARG D 1 214 ? 20.413  -8.750  -18.583 1.00 39.40 ? 209 ARG D O   1 
ATOM   6413 C  CB  . ARG D 1 214 ? 18.112  -10.113 -17.210 1.00 40.32 ? 209 ARG D CB  1 
ATOM   6414 C  CG  . ARG D 1 214 ? 17.636  -11.337 -16.439 1.00 42.54 ? 209 ARG D CG  1 
ATOM   6415 C  CD  . ARG D 1 214 ? 16.301  -11.880 -16.913 1.00 46.57 ? 209 ARG D CD  1 
ATOM   6416 N  NE  . ARG D 1 214 ? 16.411  -12.231 -18.322 1.00 54.69 ? 209 ARG D NE  1 
ATOM   6417 C  CZ  . ARG D 1 214 ? 15.624  -11.788 -19.312 1.00 59.62 ? 209 ARG D CZ  1 
ATOM   6418 N  NH1 . ARG D 1 214 ? 15.851  -12.181 -20.557 1.00 58.58 ? 209 ARG D NH1 1 
ATOM   6419 N  NH2 . ARG D 1 214 ? 14.608  -10.975 -19.069 1.00 58.28 ? 209 ARG D NH2 1 
ATOM   6420 N  N   . LEU D 1 215 ? 19.996  -7.098  -17.060 1.00 36.75 ? 210 LEU D N   1 
ATOM   6421 C  CA  . LEU D 1 215 ? 20.711  -6.037  -17.826 1.00 40.01 ? 210 LEU D CA  1 
ATOM   6422 C  C   . LEU D 1 215 ? 22.222  -6.291  -17.764 1.00 45.18 ? 210 LEU D C   1 
ATOM   6423 O  O   . LEU D 1 215 ? 22.735  -6.693  -16.719 1.00 41.98 ? 210 LEU D O   1 
ATOM   6424 C  CB  . LEU D 1 215 ? 20.375  -4.659  -17.248 1.00 39.21 ? 210 LEU D CB  1 
ATOM   6425 C  CG  . LEU D 1 215 ? 18.941  -4.178  -17.464 1.00 36.33 ? 210 LEU D CG  1 
ATOM   6426 C  CD1 . LEU D 1 215 ? 18.655  -2.945  -16.634 1.00 36.62 ? 210 LEU D CD1 1 
ATOM   6427 C  CD2 . LEU D 1 215 ? 18.687  -3.890  -18.927 1.00 40.35 ? 210 LEU D CD2 1 
ATOM   6428 N  N   . PRO D 1 216 ? 22.988  -6.016  -18.850 1.00 50.20 ? 211 PRO D N   1 
ATOM   6429 C  CA  . PRO D 1 216 ? 24.427  -6.309  -18.894 1.00 54.56 ? 211 PRO D CA  1 
ATOM   6430 C  C   . PRO D 1 216 ? 25.248  -5.671  -17.765 1.00 53.09 ? 211 PRO D C   1 
ATOM   6431 O  O   . PRO D 1 216 ? 25.119  -4.463  -17.610 1.00 58.35 ? 211 PRO D O   1 
ATOM   6432 C  CB  . PRO D 1 216 ? 24.899  -5.712  -20.233 1.00 55.10 ? 211 PRO D CB  1 
ATOM   6433 C  CG  . PRO D 1 216 ? 23.794  -4.756  -20.638 1.00 56.08 ? 211 PRO D CG  1 
ATOM   6434 C  CD  . PRO D 1 216 ? 22.523  -5.374  -20.088 1.00 52.88 ? 211 PRO D CD  1 
HETATM 6435 C  CHA . HEM E 2 .   ? 10.089  13.252  -17.791 1.00 21.94 ? 301 HEM A CHA 1 
HETATM 6436 C  CHB . HEM E 2 .   ? 7.978   10.547  -14.489 1.00 21.27 ? 301 HEM A CHB 1 
HETATM 6437 C  CHC . HEM E 2 .   ? 8.976   13.835  -10.901 1.00 20.96 ? 301 HEM A CHC 1 
HETATM 6438 C  CHD . HEM E 2 .   ? 11.603  16.207  -14.187 1.00 24.89 ? 301 HEM A CHD 1 
HETATM 6439 C  C1A . HEM E 2 .   ? 9.383   12.258  -17.200 1.00 19.77 ? 301 HEM A C1A 1 
HETATM 6440 C  C2A . HEM E 2 .   ? 8.880   11.102  -17.876 1.00 19.26 ? 301 HEM A C2A 1 
HETATM 6441 C  C3A . HEM E 2 .   ? 8.351   10.322  -16.917 1.00 21.80 ? 301 HEM A C3A 1 
HETATM 6442 C  C4A . HEM E 2 .   ? 8.470   11.004  -15.685 1.00 20.61 ? 301 HEM A C4A 1 
HETATM 6443 C  CMA . HEM E 2 .   ? 7.691   8.957   -17.135 1.00 22.86 ? 301 HEM A CMA 1 
HETATM 6444 C  CAA . HEM E 2 .   ? 9.034   10.692  -19.328 1.00 19.43 ? 301 HEM A CAA 1 
HETATM 6445 C  CBA . HEM E 2 .   ? 7.811   11.126  -20.170 1.00 19.09 ? 301 HEM A CBA 1 
HETATM 6446 C  CGA . HEM E 2 .   ? 8.038   10.918  -21.612 1.00 19.20 ? 301 HEM A CGA 1 
HETATM 6447 O  O1A . HEM E 2 .   ? 7.873   11.853  -22.445 1.00 22.10 ? 301 HEM A O1A 1 
HETATM 6448 O  O2A . HEM E 2 .   ? 8.532   9.833   -22.004 1.00 21.47 ? 301 HEM A O2A 1 
HETATM 6449 C  C1B . HEM E 2 .   ? 8.110   11.228  -13.265 1.00 20.85 ? 301 HEM A C1B 1 
HETATM 6450 C  C2B . HEM E 2 .   ? 7.554   10.720  -12.072 1.00 21.54 ? 301 HEM A C2B 1 
HETATM 6451 C  C3B . HEM E 2 .   ? 7.798   11.603  -11.077 1.00 18.83 ? 301 HEM A C3B 1 
HETATM 6452 C  C4B . HEM E 2 .   ? 8.541   12.729  -11.652 1.00 21.06 ? 301 HEM A C4B 1 
HETATM 6453 C  CMB . HEM E 2 .   ? 6.795   9.405   -11.931 1.00 22.68 ? 301 HEM A CMB 1 
HETATM 6454 C  CAB . HEM E 2 .   ? 7.393   11.323  -9.696  1.00 21.10 ? 301 HEM A CAB 1 
HETATM 6455 C  CBB . HEM E 2 .   ? 7.507   12.096  -8.654  1.00 19.90 ? 301 HEM A CBB 1 
HETATM 6456 C  C1C . HEM E 2 .   ? 9.775   14.778  -11.533 1.00 22.59 ? 301 HEM A C1C 1 
HETATM 6457 C  C2C . HEM E 2 .   ? 10.432  15.801  -10.888 1.00 22.81 ? 301 HEM A C2C 1 
HETATM 6458 C  C3C . HEM E 2 .   ? 11.182  16.521  -11.787 1.00 24.13 ? 301 HEM A C3C 1 
HETATM 6459 C  C4C . HEM E 2 .   ? 10.987  15.845  -13.022 1.00 25.54 ? 301 HEM A C4C 1 
HETATM 6460 C  CMC . HEM E 2 .   ? 10.316  16.138  -9.425  1.00 25.20 ? 301 HEM A CMC 1 
HETATM 6461 C  CAC . HEM E 2 .   ? 11.901  17.778  -11.397 1.00 24.07 ? 301 HEM A CAC 1 
HETATM 6462 C  CBC . HEM E 2 .   ? 12.213  18.781  -12.219 1.00 26.58 ? 301 HEM A CBC 1 
HETATM 6463 C  C1D . HEM E 2 .   ? 11.397  15.569  -15.387 1.00 24.15 ? 301 HEM A C1D 1 
HETATM 6464 C  C2D . HEM E 2 .   ? 12.118  15.998  -16.590 1.00 25.70 ? 301 HEM A C2D 1 
HETATM 6465 C  C3D . HEM E 2 .   ? 11.718  15.198  -17.564 1.00 26.29 ? 301 HEM A C3D 1 
HETATM 6466 C  C4D . HEM E 2 .   ? 10.703  14.299  -17.004 1.00 23.86 ? 301 HEM A C4D 1 
HETATM 6467 C  CMD . HEM E 2 .   ? 13.123  17.081  -16.765 1.00 25.86 ? 301 HEM A CMD 1 
HETATM 6468 C  CAD . HEM E 2 .   ? 12.192  15.256  -18.971 1.00 28.88 ? 301 HEM A CAD 1 
HETATM 6469 C  CBD . HEM E 2 .   ? 12.751  13.862  -19.198 1.00 34.72 ? 301 HEM A CBD 1 
HETATM 6470 C  CGD . HEM E 2 .   ? 14.175  13.764  -18.808 1.00 44.04 ? 301 HEM A CGD 1 
HETATM 6471 O  O1D . HEM E 2 .   ? 14.620  12.596  -18.732 1.00 48.01 ? 301 HEM A O1D 1 
HETATM 6472 O  O2D . HEM E 2 .   ? 14.876  14.791  -18.574 1.00 48.44 ? 301 HEM A O2D 1 
HETATM 6473 N  NA  . HEM E 2 .   ? 9.100   12.222  -15.841 1.00 19.32 ? 301 HEM A NA  1 
HETATM 6474 N  NB  . HEM E 2 .   ? 8.664   12.436  -12.976 1.00 21.74 ? 301 HEM A NB  1 
HETATM 6475 N  NC  . HEM E 2 .   ? 10.129  14.779  -12.853 1.00 22.14 ? 301 HEM A NC  1 
HETATM 6476 N  ND  . HEM E 2 .   ? 10.543  14.588  -15.672 1.00 23.07 ? 301 HEM A ND  1 
HETATM 6477 FE FE  . HEM E 2 .   ? 9.543   13.567  -14.447 1.00 21.24 ? 301 HEM A FE  1 
HETATM 6478 C  C   . ONH F 3 .   ? 16.627  12.558  -13.872 1.00 56.65 ? 302 ONH A C   1 
HETATM 6479 N  N   . ONH F 3 .   ? 15.074  11.557  -15.519 1.00 51.89 ? 302 ONH A N   1 
HETATM 6480 O  O   . ONH F 3 .   ? 17.029  13.746  -13.777 1.00 61.26 ? 302 ONH A O   1 
HETATM 6481 C  CA  . ONH F 3 .   ? 15.168  12.402  -14.319 1.00 53.71 ? 302 ONH A CA  1 
HETATM 6482 C  CB  . ONH F 3 .   ? 14.378  11.836  -13.150 1.00 53.54 ? 302 ONH A CB  1 
HETATM 6483 C  CD  . ONH F 3 .   ? 12.057  12.554  -12.747 1.00 50.05 ? 302 ONH A CD  1 
HETATM 6484 N  NE  . ONH F 3 .   ? 11.714  12.206  -14.132 1.00 54.63 ? 302 ONH A NE  1 
HETATM 6485 C  CG  . ONH F 3 .   ? 13.519  12.974  -12.615 1.00 51.31 ? 302 ONH A CG  1 
HETATM 6486 O  OZ  . ONH F 3 .   ? 12.627  12.799  -15.178 1.00 54.55 ? 302 ONH A OZ  1 
HETATM 6487 O  OXT . ONH F 3 .   ? 17.293  11.508  -13.626 1.00 55.96 ? 302 ONH A OXT 1 
HETATM 6488 C  CHA . HEM G 2 .   ? 10.205  -19.370 17.575  1.00 24.20 ? 301 HEM B CHA 1 
HETATM 6489 C  CHB . HEM G 2 .   ? 7.869   -16.563 14.408  1.00 24.36 ? 301 HEM B CHB 1 
HETATM 6490 C  CHC . HEM G 2 .   ? 8.923   -19.745 10.779  1.00 23.47 ? 301 HEM B CHC 1 
HETATM 6491 C  CHD . HEM G 2 .   ? 11.487  -22.273 13.975  1.00 24.22 ? 301 HEM B CHD 1 
HETATM 6492 C  C1A . HEM G 2 .   ? 9.478   -18.331 17.034  1.00 24.60 ? 301 HEM B C1A 1 
HETATM 6493 C  C2A . HEM G 2 .   ? 9.043   -17.160 17.747  1.00 24.79 ? 301 HEM B C2A 1 
HETATM 6494 C  C3A . HEM G 2 .   ? 8.390   -16.358 16.819  1.00 23.99 ? 301 HEM B C3A 1 
HETATM 6495 C  C4A . HEM G 2 .   ? 8.414   -17.021 15.581  1.00 22.58 ? 301 HEM B C4A 1 
HETATM 6496 C  CMA . HEM G 2 .   ? 7.728   -15.013 17.104  1.00 24.31 ? 301 HEM B CMA 1 
HETATM 6497 C  CAA . HEM G 2 .   ? 9.228   -16.811 19.222  1.00 22.93 ? 301 HEM B CAA 1 
HETATM 6498 C  CBA . HEM G 2 .   ? 7.972   -17.231 20.072  1.00 22.81 ? 301 HEM B CBA 1 
HETATM 6499 C  CGA . HEM G 2 .   ? 8.146   -16.995 21.550  1.00 19.47 ? 301 HEM B CGA 1 
HETATM 6500 O  O1A . HEM G 2 .   ? 8.638   -15.935 21.993  1.00 19.52 ? 301 HEM B O1A 1 
HETATM 6501 O  O2A . HEM G 2 .   ? 7.842   -17.925 22.324  1.00 18.76 ? 301 HEM B O2A 1 
HETATM 6502 C  C1B . HEM G 2 .   ? 7.978   -17.239 13.156  1.00 23.96 ? 301 HEM B C1B 1 
HETATM 6503 C  C2B . HEM G 2 .   ? 7.418   -16.706 11.991  1.00 23.45 ? 301 HEM B C2B 1 
HETATM 6504 C  C3B . HEM G 2 .   ? 7.696   -17.508 10.940  1.00 21.77 ? 301 HEM B C3B 1 
HETATM 6505 C  C4B . HEM G 2 .   ? 8.444   -18.653 11.494  1.00 24.04 ? 301 HEM B C4B 1 
HETATM 6506 C  CMB . HEM G 2 .   ? 6.681   -15.382 11.933  1.00 22.37 ? 301 HEM B CMB 1 
HETATM 6507 C  CAB . HEM G 2 .   ? 7.211   -17.174 9.584   1.00 23.64 ? 301 HEM B CAB 1 
HETATM 6508 C  CBB . HEM G 2 .   ? 7.331   -17.993 8.535   1.00 23.76 ? 301 HEM B CBB 1 
HETATM 6509 C  C1C . HEM G 2 .   ? 9.714   -20.735 11.353  1.00 25.06 ? 301 HEM B C1C 1 
HETATM 6510 C  C2C . HEM G 2 .   ? 10.299  -21.838 10.703  1.00 25.24 ? 301 HEM B C2C 1 
HETATM 6511 C  C3C . HEM G 2 .   ? 11.052  -22.560 11.603  1.00 25.69 ? 301 HEM B C3C 1 
HETATM 6512 C  C4C . HEM G 2 .   ? 10.893  -21.871 12.834  1.00 24.86 ? 301 HEM B C4C 1 
HETATM 6513 C  CMC . HEM G 2 .   ? 10.201  -22.201 9.241   1.00 26.83 ? 301 HEM B CMC 1 
HETATM 6514 C  CAC . HEM G 2 .   ? 11.737  -23.840 11.275  1.00 25.81 ? 301 HEM B CAC 1 
HETATM 6515 C  CBC . HEM G 2 .   ? 12.004  -24.811 12.170  1.00 26.47 ? 301 HEM B CBC 1 
HETATM 6516 C  C1D . HEM G 2 .   ? 11.322  -21.651 15.171  1.00 24.05 ? 301 HEM B C1D 1 
HETATM 6517 C  C2D . HEM G 2 .   ? 12.089  -22.120 16.312  1.00 26.13 ? 301 HEM B C2D 1 
HETATM 6518 C  C3D . HEM G 2 .   ? 11.729  -21.319 17.326  1.00 26.17 ? 301 HEM B C3D 1 
HETATM 6519 C  C4D . HEM G 2 .   ? 10.758  -20.375 16.792  1.00 25.72 ? 301 HEM B C4D 1 
HETATM 6520 C  CMD . HEM G 2 .   ? 13.064  -23.278 16.369  1.00 24.01 ? 301 HEM B CMD 1 
HETATM 6521 C  CAD . HEM G 2 .   ? 12.244  -21.390 18.719  1.00 28.13 ? 301 HEM B CAD 1 
HETATM 6522 C  CBD . HEM G 2 .   ? 13.169  -20.202 19.067  1.00 33.44 ? 301 HEM B CBD 1 
HETATM 6523 C  CGD . HEM G 2 .   ? 14.360  -19.940 18.153  1.00 41.54 ? 301 HEM B CGD 1 
HETATM 6524 O  O1D . HEM G 2 .   ? 14.629  -18.765 17.719  1.00 48.65 ? 301 HEM B O1D 1 
HETATM 6525 O  O2D . HEM G 2 .   ? 15.131  -20.889 17.870  1.00 42.74 ? 301 HEM B O2D 1 
HETATM 6526 N  NA  . HEM G 2 .   ? 9.093   -18.220 15.695  1.00 23.66 ? 301 HEM B NA  1 
HETATM 6527 N  NB  . HEM G 2 .   ? 8.560   -18.403 12.833  1.00 25.23 ? 301 HEM B NB  1 
HETATM 6528 N  NC  . HEM G 2 .   ? 10.093  -20.767 12.666  1.00 25.21 ? 301 HEM B NC  1 
HETATM 6529 N  ND  . HEM G 2 .   ? 10.541  -20.622 15.474  1.00 24.96 ? 301 HEM B ND  1 
HETATM 6530 FE FE  . HEM G 2 .   ? 9.484   -19.589 14.283  1.00 24.12 ? 301 HEM B FE  1 
HETATM 6531 C  CHA . HEM H 2 .   ? -14.604 4.055   26.291  1.00 30.14 ? 301 HEM C CHA 1 
HETATM 6532 C  CHB . HEM H 2 .   ? -10.590 5.267   23.825  1.00 28.05 ? 301 HEM C CHB 1 
HETATM 6533 C  CHC . HEM H 2 .   ? -11.093 9.782   25.491  1.00 24.22 ? 301 HEM C CHC 1 
HETATM 6534 C  CHD . HEM H 2 .   ? -15.321 8.669   27.511  1.00 27.21 ? 301 HEM C CHD 1 
HETATM 6535 C  C1A . HEM H 2 .   ? -13.448 4.015   25.521  1.00 28.21 ? 301 HEM C C1A 1 
HETATM 6536 C  C2A . HEM H 2 .   ? -12.994 2.827   24.860  1.00 28.03 ? 301 HEM C C2A 1 
HETATM 6537 C  C3A . HEM H 2 .   ? -11.875 3.139   24.142  1.00 26.95 ? 301 HEM C C3A 1 
HETATM 6538 C  C4A . HEM H 2 .   ? -11.643 4.534   24.373  1.00 28.89 ? 301 HEM C C4A 1 
HETATM 6539 C  CMA . HEM H 2 .   ? -11.036 2.142   23.314  1.00 24.22 ? 301 HEM C CMA 1 
HETATM 6540 C  CAA . HEM H 2 .   ? -13.663 1.441   24.916  1.00 27.02 ? 301 HEM C CAA 1 
HETATM 6541 C  CBA . HEM H 2 .   ? -13.126 0.671   26.113  1.00 25.54 ? 301 HEM C CBA 1 
HETATM 6542 C  CGA . HEM H 2 .   ? -13.785 -0.699  26.314  1.00 25.79 ? 301 HEM C CGA 1 
HETATM 6543 O  O1A . HEM H 2 .   ? -14.031 -1.164  27.478  1.00 23.26 ? 301 HEM C O1A 1 
HETATM 6544 O  O2A . HEM H 2 .   ? -13.986 -1.429  25.305  1.00 26.73 ? 301 HEM C O2A 1 
HETATM 6545 C  C1B . HEM H 2 .   ? -10.391 6.643   24.042  1.00 29.12 ? 301 HEM C C1B 1 
HETATM 6546 C  C2B . HEM H 2 .   ? -9.312  7.395   23.465  1.00 29.97 ? 301 HEM C C2B 1 
HETATM 6547 C  C3B . HEM H 2 .   ? -9.408  8.666   23.927  1.00 25.81 ? 301 HEM C C3B 1 
HETATM 6548 C  C4B . HEM H 2 .   ? -10.605 8.679   24.805  1.00 26.86 ? 301 HEM C C4B 1 
HETATM 6549 C  CMB . HEM H 2 .   ? -8.249  6.909   22.495  1.00 27.89 ? 301 HEM C CMB 1 
HETATM 6550 C  CAB . HEM H 2 .   ? -8.474  9.732   23.538  1.00 24.51 ? 301 HEM C CAB 1 
HETATM 6551 C  CBB . HEM H 2 .   ? -8.466  10.885  24.145  1.00 23.82 ? 301 HEM C CBB 1 
HETATM 6552 C  C1C . HEM H 2 .   ? -12.266 9.904   26.175  1.00 26.19 ? 301 HEM C C1C 1 
HETATM 6553 C  C2C . HEM H 2 .   ? -12.865 11.109  26.645  1.00 26.71 ? 301 HEM C C2C 1 
HETATM 6554 C  C3C . HEM H 2 .   ? -14.070 10.793  27.209  1.00 26.44 ? 301 HEM C C3C 1 
HETATM 6555 C  C4C . HEM H 2 .   ? -14.223 9.388   27.092  1.00 26.67 ? 301 HEM C C4C 1 
HETATM 6556 C  CMC . HEM H 2 .   ? -12.302 12.493  26.571  1.00 23.73 ? 301 HEM C CMC 1 
HETATM 6557 C  CAC . HEM H 2 .   ? -14.883 11.779  27.942  1.00 31.23 ? 301 HEM C CAC 1 
HETATM 6558 C  CBC . HEM H 2 .   ? -15.670 11.458  28.993  1.00 32.74 ? 301 HEM C CBC 1 
HETATM 6559 C  C1D . HEM H 2 .   ? -15.432 7.313   27.298  1.00 27.30 ? 301 HEM C C1D 1 
HETATM 6560 C  C2D . HEM H 2 .   ? -16.665 6.614   27.697  1.00 30.07 ? 301 HEM C C2D 1 
HETATM 6561 C  C3D . HEM H 2 .   ? -16.476 5.342   27.363  1.00 32.96 ? 301 HEM C C3D 1 
HETATM 6562 C  C4D . HEM H 2 .   ? -15.107 5.255   26.788  1.00 32.26 ? 301 HEM C C4D 1 
HETATM 6563 C  CMD . HEM H 2 .   ? -17.924 7.204   28.350  1.00 30.03 ? 301 HEM C CMD 1 
HETATM 6564 C  CAD . HEM H 2 .   ? -17.464 4.215   27.600  1.00 35.75 ? 301 HEM C CAD 1 
HETATM 6565 C  CBD . HEM H 2 .   ? -18.092 3.735   26.287  1.00 38.90 ? 301 HEM C CBD 1 
HETATM 6566 C  CGD . HEM H 2 .   ? -18.638 4.899   25.500  1.00 47.40 ? 301 HEM C CGD 1 
HETATM 6567 O  O1D . HEM H 2 .   ? -17.992 5.238   24.463  1.00 50.29 ? 301 HEM C O1D 1 
HETATM 6568 O  O2D . HEM H 2 .   ? -19.709 5.493   25.885  1.00 41.26 ? 301 HEM C O2D 1 
HETATM 6569 N  NA  . HEM H 2 .   ? -12.617 5.064   25.196  1.00 27.28 ? 301 HEM C NA  1 
HETATM 6570 N  NB  . HEM H 2 .   ? -11.072 7.436   24.867  1.00 29.36 ? 301 HEM C NB  1 
HETATM 6571 N  NC  . HEM H 2 .   ? -13.117 8.896   26.429  1.00 28.02 ? 301 HEM C NC  1 
HETATM 6572 N  ND  . HEM H 2 .   ? -14.518 6.480   26.752  1.00 30.07 ? 301 HEM C ND  1 
HETATM 6573 FE FE  . HEM H 2 .   ? -12.771 6.889   26.003  1.00 24.78 ? 301 HEM C FE  1 
HETATM 6574 C  C   . ONH I 3 .   ? 17.102  -17.089 12.808  1.00 57.40 ? 302 ONH C C   1 
HETATM 6575 N  N   . ONH I 3 .   ? 16.100  -19.338 12.557  1.00 64.33 ? 302 ONH C N   1 
HETATM 6576 O  O   . ONH I 3 .   ? 17.681  -16.683 13.832  1.00 54.75 ? 302 ONH C O   1 
HETATM 6577 C  CA  . ONH I 3 .   ? 15.828  -17.956 12.984  1.00 58.97 ? 302 ONH C CA  1 
HETATM 6578 C  CB  . ONH I 3 .   ? 15.380  -17.881 14.424  1.00 58.09 ? 302 ONH C CB  1 
HETATM 6579 C  CD  . ONH I 3 .   ? 13.031  -17.250 14.367  1.00 55.30 ? 302 ONH C CD  1 
HETATM 6580 N  NE  . ONH I 3 .   ? 11.707  -17.856 14.198  1.00 51.57 ? 302 ONH C NE  1 
HETATM 6581 C  CG  . ONH I 3 .   ? 13.973  -18.434 14.417  1.00 58.96 ? 302 ONH C CG  1 
HETATM 6582 O  OZ  . ONH I 3 .   ? 11.711  -18.622 12.997  1.00 43.34 ? 302 ONH C OZ  1 
HETATM 6583 O  OXT . ONH I 3 .   ? 17.491  -16.867 11.651  1.00 52.36 ? 302 ONH C OXT 1 
HETATM 6584 C  CHA . HEM J 2 .   ? -14.623 -10.119 -26.234 1.00 26.26 ? 301 HEM D CHA 1 
HETATM 6585 C  CHB . HEM J 2 .   ? -10.655 -11.355 -23.677 1.00 27.91 ? 301 HEM D CHB 1 
HETATM 6586 C  CHC . HEM J 2 .   ? -11.167 -15.952 -25.185 1.00 22.85 ? 301 HEM D CHC 1 
HETATM 6587 C  CHD . HEM J 2 .   ? -15.476 -14.783 -27.108 1.00 23.86 ? 301 HEM D CHD 1 
HETATM 6588 C  C1A . HEM J 2 .   ? -13.469 -10.077 -25.458 1.00 25.81 ? 301 HEM D C1A 1 
HETATM 6589 C  C2A . HEM J 2 .   ? -13.021 -8.887  -24.805 1.00 27.56 ? 301 HEM D C2A 1 
HETATM 6590 C  C3A . HEM J 2 .   ? -11.920 -9.213  -24.053 1.00 27.49 ? 301 HEM D C3A 1 
HETATM 6591 C  C4A . HEM J 2 .   ? -11.685 -10.622 -24.251 1.00 27.76 ? 301 HEM D C4A 1 
HETATM 6592 C  CMA . HEM J 2 .   ? -11.113 -8.222  -23.203 1.00 25.49 ? 301 HEM D CMA 1 
HETATM 6593 C  CAA . HEM J 2 .   ? -13.651 -7.482  -24.883 1.00 27.18 ? 301 HEM D CAA 1 
HETATM 6594 C  CBA . HEM J 2 .   ? -13.020 -6.639  -26.004 1.00 24.23 ? 301 HEM D CBA 1 
HETATM 6595 C  CGA . HEM J 2 .   ? -13.706 -5.290  -26.207 1.00 24.88 ? 301 HEM D CGA 1 
HETATM 6596 O  O1A . HEM J 2 .   ? -13.960 -4.610  -25.177 1.00 25.66 ? 301 HEM D O1A 1 
HETATM 6597 O  O2A . HEM J 2 .   ? -13.983 -4.801  -27.355 1.00 22.98 ? 301 HEM D O2A 1 
HETATM 6598 C  C1B . HEM J 2 .   ? -10.473 -12.742 -23.887 1.00 27.44 ? 301 HEM D C1B 1 
HETATM 6599 C  C2B . HEM J 2 .   ? -9.438  -13.490 -23.276 1.00 27.85 ? 301 HEM D C2B 1 
HETATM 6600 C  C3B . HEM J 2 .   ? -9.548  -14.772 -23.664 1.00 24.64 ? 301 HEM D C3B 1 
HETATM 6601 C  C4B . HEM J 2 .   ? -10.696 -14.795 -24.562 1.00 25.97 ? 301 HEM D C4B 1 
HETATM 6602 C  CMB . HEM J 2 .   ? -8.384  -12.973 -22.341 1.00 27.19 ? 301 HEM D CMB 1 
HETATM 6603 C  CAB . HEM J 2 .   ? -8.595  -15.811 -23.270 1.00 27.91 ? 301 HEM D CAB 1 
HETATM 6604 C  CBB . HEM J 2 .   ? -8.487  -17.028 -23.782 1.00 27.23 ? 301 HEM D CBB 1 
HETATM 6605 C  C1C . HEM J 2 .   ? -12.354 -16.036 -25.804 1.00 23.02 ? 301 HEM D C1C 1 
HETATM 6606 C  C2C . HEM J 2 .   ? -12.912 -17.223 -26.312 1.00 23.56 ? 301 HEM D C2C 1 
HETATM 6607 C  C3C . HEM J 2 .   ? -14.153 -16.906 -26.846 1.00 22.78 ? 301 HEM D C3C 1 
HETATM 6608 C  C4C . HEM J 2 .   ? -14.340 -15.504 -26.690 1.00 23.65 ? 301 HEM D C4C 1 
HETATM 6609 C  CMC . HEM J 2 .   ? -12.269 -18.582 -26.286 1.00 24.33 ? 301 HEM D CMC 1 
HETATM 6610 C  CAC . HEM J 2 .   ? -14.959 -17.894 -27.581 1.00 26.15 ? 301 HEM D CAC 1 
HETATM 6611 C  CBC . HEM J 2 .   ? -15.746 -17.585 -28.611 1.00 25.58 ? 301 HEM D CBC 1 
HETATM 6612 C  C1D . HEM J 2 .   ? -15.578 -13.408 -27.012 1.00 23.36 ? 301 HEM D C1D 1 
HETATM 6613 C  C2D . HEM J 2 .   ? -16.803 -12.704 -27.399 1.00 23.66 ? 301 HEM D C2D 1 
HETATM 6614 C  C3D . HEM J 2 .   ? -16.585 -11.431 -27.164 1.00 26.14 ? 301 HEM D C3D 1 
HETATM 6615 C  C4D . HEM J 2 .   ? -15.192 -11.331 -26.626 1.00 27.73 ? 301 HEM D C4D 1 
HETATM 6616 C  CMD . HEM J 2 .   ? -18.082 -13.295 -28.019 1.00 26.90 ? 301 HEM D CMD 1 
HETATM 6617 C  CAD . HEM J 2 .   ? -17.557 -10.298 -27.499 1.00 30.37 ? 301 HEM D CAD 1 
HETATM 6618 C  CBD . HEM J 2 .   ? -18.038 -9.635  -26.203 1.00 36.02 ? 301 HEM D CBD 1 
HETATM 6619 C  CGD . HEM J 2 .   ? -18.706 -10.660 -25.348 1.00 40.70 ? 301 HEM D CGD 1 
HETATM 6620 O  O1D . HEM J 2 .   ? -18.230 -10.856 -24.186 1.00 40.69 ? 301 HEM D O1D 1 
HETATM 6621 O  O2D . HEM J 2 .   ? -19.700 -11.268 -25.866 1.00 37.67 ? 301 HEM D O2D 1 
HETATM 6622 N  NA  . HEM J 2 .   ? -12.641 -11.140 -25.094 1.00 26.69 ? 301 HEM D NA  1 
HETATM 6623 N  NB  . HEM J 2 .   ? -11.160 -13.547 -24.673 1.00 26.48 ? 301 HEM D NB  1 
HETATM 6624 N  NC  . HEM J 2 .   ? -13.220 -15.004 -26.021 1.00 21.56 ? 301 HEM D NC  1 
HETATM 6625 N  ND  . HEM J 2 .   ? -14.620 -12.562 -26.539 1.00 26.25 ? 301 HEM D ND  1 
HETATM 6626 FE FE  . HEM J 2 .   ? -12.854 -12.989 -25.829 1.00 24.78 ? 301 HEM D FE  1 
HETATM 6627 O  O   . HOH K 4 .   ? -14.102 6.279   -26.194 1.00 34.24 ? 401 HOH A O   1 
HETATM 6628 O  O   . HOH K 4 .   ? 3.605   33.017  -11.040 1.00 43.22 ? 402 HOH A O   1 
HETATM 6629 O  O   . HOH K 4 .   ? -2.343  -9.660  -11.868 1.00 40.01 ? 403 HOH A O   1 
HETATM 6630 O  O   . HOH K 4 .   ? -0.235  26.633  -23.129 1.00 32.42 ? 404 HOH A O   1 
HETATM 6631 O  O   . HOH K 4 .   ? 0.197   16.291  -4.961  1.00 42.90 ? 405 HOH A O   1 
HETATM 6632 O  O   . HOH K 4 .   ? 9.300   17.720  2.096   1.00 39.35 ? 406 HOH A O   1 
HETATM 6633 O  O   . HOH K 4 .   ? 4.854   3.250   -23.341 1.00 33.69 ? 407 HOH A O   1 
HETATM 6634 O  O   . HOH K 4 .   ? 9.403   25.559  -14.065 1.00 18.09 ? 408 HOH A O   1 
HETATM 6635 O  O   . HOH K 4 .   ? 7.902   12.360  1.857   1.00 36.63 ? 409 HOH A O   1 
HETATM 6636 O  O   . HOH K 4 .   ? 3.206   21.863  -6.160  1.00 27.17 ? 410 HOH A O   1 
HETATM 6637 O  O   . HOH K 4 .   ? -11.654 23.152  -23.754 1.00 43.31 ? 411 HOH A O   1 
HETATM 6638 O  O   . HOH K 4 .   ? -15.573 -16.422 -18.779 1.00 26.41 ? 412 HOH A O   1 
HETATM 6639 O  O   . HOH K 4 .   ? -14.378 -9.624  3.004   1.00 37.05 ? 413 HOH A O   1 
HETATM 6640 O  O   . HOH K 4 .   ? -6.263  -3.328  -15.541 1.00 25.71 ? 414 HOH A O   1 
HETATM 6641 O  O   . HOH K 4 .   ? -2.926  20.573  -26.583 1.00 34.58 ? 415 HOH A O   1 
HETATM 6642 O  O   . HOH K 4 .   ? -2.219  -7.271  -17.566 1.00 44.22 ? 416 HOH A O   1 
HETATM 6643 O  O   . HOH K 4 .   ? -11.825 -12.042 -0.522  1.00 49.26 ? 417 HOH A O   1 
HETATM 6644 O  O   . HOH K 4 .   ? 5.212   11.006  -30.901 1.00 36.81 ? 418 HOH A O   1 
HETATM 6645 O  O   . HOH K 4 .   ? -12.773 -23.257 -8.162  1.00 30.99 ? 419 HOH A O   1 
HETATM 6646 O  O   . HOH K 4 .   ? 12.933  7.997   3.909   1.00 30.74 ? 420 HOH A O   1 
HETATM 6647 O  O   . HOH K 4 .   ? -4.658  11.836  -39.172 1.00 36.35 ? 421 HOH A O   1 
HETATM 6648 O  O   . HOH K 4 .   ? -15.056 15.378  -7.914  1.00 47.53 ? 422 HOH A O   1 
HETATM 6649 O  O   . HOH K 4 .   ? -16.568 14.946  -6.198  1.00 46.44 ? 423 HOH A O   1 
HETATM 6650 O  O   . HOH K 4 .   ? 15.986  18.749  -18.017 1.00 31.25 ? 424 HOH A O   1 
HETATM 6651 O  O   . HOH K 4 .   ? -0.112  2.571   -2.285  1.00 43.73 ? 425 HOH A O   1 
HETATM 6652 O  O   . HOH K 4 .   ? 7.989   27.332  -21.085 1.00 22.98 ? 426 HOH A O   1 
HETATM 6653 O  O   . HOH K 4 .   ? 3.602   8.329   -32.603 1.00 39.16 ? 427 HOH A O   1 
HETATM 6654 O  O   . HOH K 4 .   ? -18.609 8.589   -15.877 1.00 49.50 ? 428 HOH A O   1 
HETATM 6655 O  O   . HOH K 4 .   ? -4.159  5.994   -23.882 1.00 27.52 ? 429 HOH A O   1 
HETATM 6656 O  O   . HOH K 4 .   ? 13.135  9.883   -15.145 1.00 43.26 ? 430 HOH A O   1 
HETATM 6657 O  O   . HOH K 4 .   ? 0.869   4.889   -38.331 1.00 31.53 ? 431 HOH A O   1 
HETATM 6658 O  O   . HOH K 4 .   ? 9.711   23.432  -18.373 1.00 24.26 ? 432 HOH A O   1 
HETATM 6659 O  O   . HOH K 4 .   ? -1.682  -9.282  -14.284 1.00 27.68 ? 433 HOH A O   1 
HETATM 6660 O  O   . HOH K 4 .   ? -6.388  4.463   -4.733  1.00 39.69 ? 434 HOH A O   1 
HETATM 6661 O  O   . HOH K 4 .   ? -19.948 -3.342  -11.085 1.00 41.17 ? 435 HOH A O   1 
HETATM 6662 O  O   . HOH K 4 .   ? -3.115  4.460   -3.184  1.00 52.44 ? 436 HOH A O   1 
HETATM 6663 O  O   . HOH K 4 .   ? 15.265  16.973  -19.947 1.00 44.35 ? 437 HOH A O   1 
HETATM 6664 O  O   . HOH K 4 .   ? 1.866   26.596  -25.253 1.00 25.90 ? 438 HOH A O   1 
HETATM 6665 O  O   . HOH K 4 .   ? 2.139   6.911   -34.358 1.00 26.06 ? 439 HOH A O   1 
HETATM 6666 O  O   . HOH K 4 .   ? 4.853   3.160   0.173   1.00 32.15 ? 440 HOH A O   1 
HETATM 6667 O  O   . HOH K 4 .   ? -12.053 -21.207 -6.184  1.00 36.87 ? 441 HOH A O   1 
HETATM 6668 O  O   . HOH K 4 .   ? -2.777  3.390   -24.835 1.00 19.01 ? 442 HOH A O   1 
HETATM 6669 O  O   . HOH K 4 .   ? 3.177   15.032  -13.420 1.00 20.38 ? 443 HOH A O   1 
HETATM 6670 O  O   . HOH K 4 .   ? -9.768  20.868  -10.672 1.00 36.28 ? 444 HOH A O   1 
HETATM 6671 O  O   . HOH K 4 .   ? 14.169  17.420  -22.326 1.00 29.06 ? 445 HOH A O   1 
HETATM 6672 O  O   . HOH K 4 .   ? -11.837 19.137  -21.787 1.00 34.68 ? 446 HOH A O   1 
HETATM 6673 O  O   . HOH K 4 .   ? -4.149  11.773  -8.411  1.00 29.52 ? 447 HOH A O   1 
HETATM 6674 O  O   . HOH K 4 .   ? -3.703  -16.291 -8.224  1.00 34.77 ? 448 HOH A O   1 
HETATM 6675 O  O   . HOH K 4 .   ? 15.752  16.258  -1.208  1.00 36.98 ? 449 HOH A O   1 
HETATM 6676 O  O   . HOH K 4 .   ? -14.448 -25.589 -15.247 1.00 32.50 ? 450 HOH A O   1 
HETATM 6677 O  O   . HOH K 4 .   ? -22.738 -4.767  -12.557 1.00 45.15 ? 451 HOH A O   1 
HETATM 6678 O  O   . HOH K 4 .   ? -1.382  14.367  -31.326 1.00 40.87 ? 452 HOH A O   1 
HETATM 6679 O  O   . HOH K 4 .   ? -5.700  14.062  -30.407 1.00 34.93 ? 453 HOH A O   1 
HETATM 6680 O  O   . HOH K 4 .   ? 0.261   1.834   -9.200  1.00 42.37 ? 454 HOH A O   1 
HETATM 6681 O  O   . HOH K 4 .   ? 7.435   7.754   -20.765 1.00 23.56 ? 455 HOH A O   1 
HETATM 6682 O  O   . HOH K 4 .   ? -10.407 14.177  -25.785 1.00 27.87 ? 456 HOH A O   1 
HETATM 6683 O  O   . HOH K 4 .   ? 13.810  12.452  3.344   1.00 37.58 ? 457 HOH A O   1 
HETATM 6684 O  O   . HOH K 4 .   ? 8.501   17.505  -29.085 1.00 34.60 ? 458 HOH A O   1 
HETATM 6685 O  O   . HOH K 4 .   ? -15.032 -14.008 -15.101 1.00 32.83 ? 459 HOH A O   1 
HETATM 6686 O  O   . HOH K 4 .   ? -2.146  3.479   -14.930 1.00 22.07 ? 460 HOH A O   1 
HETATM 6687 O  O   . HOH K 4 .   ? -15.244 19.145  -18.118 1.00 34.64 ? 461 HOH A O   1 
HETATM 6688 O  O   . HOH K 4 .   ? -0.903  0.925   -14.595 1.00 35.63 ? 462 HOH A O   1 
HETATM 6689 O  O   . HOH K 4 .   ? 15.639  14.181  -22.714 1.00 36.33 ? 463 HOH A O   1 
HETATM 6690 O  O   . HOH K 4 .   ? -5.631  5.607   -39.929 1.00 55.54 ? 464 HOH A O   1 
HETATM 6691 O  O   . HOH K 4 .   ? 5.945   23.131  -18.595 1.00 23.57 ? 465 HOH A O   1 
HETATM 6692 O  O   . HOH K 4 .   ? -14.328 3.675   -3.104  1.00 37.12 ? 466 HOH A O   1 
HETATM 6693 O  O   . HOH K 4 .   ? -2.844  9.798   -9.832  1.00 25.73 ? 467 HOH A O   1 
HETATM 6694 O  O   . HOH K 4 .   ? -1.227  9.099   -7.293  1.00 30.92 ? 468 HOH A O   1 
HETATM 6695 O  O   . HOH K 4 .   ? 1.229   10.466  3.572   1.00 42.08 ? 469 HOH A O   1 
HETATM 6696 O  O   . HOH K 4 .   ? -2.072  -2.186  -13.717 1.00 51.86 ? 470 HOH A O   1 
HETATM 6697 O  O   . HOH K 4 .   ? -1.792  1.480   -5.975  1.00 40.17 ? 471 HOH A O   1 
HETATM 6698 O  O   . HOH K 4 .   ? -4.656  -15.291 -12.854 1.00 28.21 ? 472 HOH A O   1 
HETATM 6699 O  O   . HOH K 4 .   ? -12.278 4.241   -26.298 1.00 37.40 ? 473 HOH A O   1 
HETATM 6700 O  O   . HOH K 4 .   ? 12.703  11.444  5.148   1.00 44.31 ? 474 HOH A O   1 
HETATM 6701 O  O   . HOH K 4 .   ? 6.440   34.041  -9.195  1.00 36.34 ? 475 HOH A O   1 
HETATM 6702 O  O   . HOH K 4 .   ? -4.449  -0.937  -6.805  1.00 55.17 ? 476 HOH A O   1 
HETATM 6703 O  O   . HOH K 4 .   ? -17.586 2.751   -14.372 1.00 35.88 ? 477 HOH A O   1 
HETATM 6704 O  O   . HOH K 4 .   ? -15.208 -10.701 -16.155 1.00 28.08 ? 478 HOH A O   1 
HETATM 6705 O  O   . HOH K 4 .   ? -7.189  -17.765 -13.171 1.00 22.02 ? 479 HOH A O   1 
HETATM 6706 O  O   . HOH K 4 .   ? 18.968  14.858  -15.346 1.00 44.12 ? 480 HOH A O   1 
HETATM 6707 O  O   . HOH K 4 .   ? 4.032   7.214   -29.115 1.00 37.31 ? 481 HOH A O   1 
HETATM 6708 O  O   . HOH K 4 .   ? -2.590  2.600   -18.837 1.00 25.31 ? 482 HOH A O   1 
HETATM 6709 O  O   . HOH K 4 .   ? -7.787  -3.822  -4.454  1.00 27.86 ? 483 HOH A O   1 
HETATM 6710 O  O   . HOH K 4 .   ? 4.978   24.483  -4.001  1.00 38.49 ? 484 HOH A O   1 
HETATM 6711 O  O   . HOH K 4 .   ? 8.978   20.416  2.506   1.00 54.51 ? 485 HOH A O   1 
HETATM 6712 O  O   . HOH K 4 .   ? 5.995   7.939   1.976   1.00 31.96 ? 486 HOH A O   1 
HETATM 6713 O  O   . HOH K 4 .   ? 8.094   23.758  -26.071 1.00 30.02 ? 487 HOH A O   1 
HETATM 6714 O  O   . HOH K 4 .   ? 9.102   3.428   -2.042  1.00 35.78 ? 488 HOH A O   1 
HETATM 6715 O  O   . HOH K 4 .   ? -21.596 7.548   -8.058  1.00 38.92 ? 489 HOH A O   1 
HETATM 6716 O  O   . HOH K 4 .   ? 8.883   15.313  -0.429  1.00 33.07 ? 490 HOH A O   1 
HETATM 6717 O  O   . HOH K 4 .   ? -18.111 11.059  -18.803 1.00 28.53 ? 491 HOH A O   1 
HETATM 6718 O  O   . HOH K 4 .   ? 5.162   21.477  -2.584  1.00 55.33 ? 492 HOH A O   1 
HETATM 6719 O  O   . HOH K 4 .   ? -2.791  14.269  -35.640 1.00 48.11 ? 493 HOH A O   1 
HETATM 6720 O  O   . HOH K 4 .   ? 1.730   23.890  -28.645 1.00 43.72 ? 494 HOH A O   1 
HETATM 6721 O  O   . HOH K 4 .   ? -20.342 3.385   -13.185 1.00 53.76 ? 495 HOH A O   1 
HETATM 6722 O  O   . HOH K 4 .   ? 20.904  23.678  -2.815  1.00 65.69 ? 496 HOH A O   1 
HETATM 6723 O  O   . HOH K 4 .   ? -6.025  22.635  -11.556 1.00 40.46 ? 497 HOH A O   1 
HETATM 6724 O  O   . HOH K 4 .   ? 6.179   8.062   -26.908 1.00 20.01 ? 498 HOH A O   1 
HETATM 6725 O  O   . HOH K 4 .   ? -18.688 8.092   -5.492  1.00 38.41 ? 499 HOH A O   1 
HETATM 6726 O  O   . HOH K 4 .   ? 11.307  9.140   -22.090 1.00 38.58 ? 500 HOH A O   1 
HETATM 6727 O  O   . HOH K 4 .   ? -12.282 18.990  -23.797 1.00 33.13 ? 501 HOH A O   1 
HETATM 6728 O  O   . HOH K 4 .   ? 5.540   1.305   -4.306  1.00 22.85 ? 502 HOH A O   1 
HETATM 6729 O  O   . HOH K 4 .   ? -11.304 1.604   -7.786  1.00 29.70 ? 503 HOH A O   1 
HETATM 6730 O  O   . HOH K 4 .   ? -7.234  -18.128 -10.402 1.00 29.57 ? 504 HOH A O   1 
HETATM 6731 O  O   . HOH K 4 .   ? -11.837 16.676  -26.399 1.00 40.48 ? 505 HOH A O   1 
HETATM 6732 O  O   . HOH K 4 .   ? -1.641  23.929  -25.249 1.00 23.75 ? 506 HOH A O   1 
HETATM 6733 O  O   . HOH K 4 .   ? 18.736  20.513  -4.754  1.00 33.08 ? 507 HOH A O   1 
HETATM 6734 O  O   . HOH K 4 .   ? 6.318   6.266   -22.658 1.00 22.58 ? 508 HOH A O   1 
HETATM 6735 O  O   . HOH K 4 .   ? 13.097  30.203  -7.806  1.00 40.37 ? 509 HOH A O   1 
HETATM 6736 O  O   . HOH K 4 .   ? -2.803  -13.082 -14.733 1.00 25.55 ? 510 HOH A O   1 
HETATM 6737 O  O   . HOH K 4 .   ? 6.161   34.477  -12.246 1.00 50.48 ? 511 HOH A O   1 
HETATM 6738 O  O   . HOH K 4 .   ? -13.800 -1.720  -24.456 1.00 37.33 ? 512 HOH A O   1 
HETATM 6739 O  O   . HOH K 4 .   ? 5.788   24.291  -26.064 1.00 39.05 ? 513 HOH A O   1 
HETATM 6740 O  O   . HOH K 4 .   ? -20.649 1.413   -23.195 1.00 45.73 ? 514 HOH A O   1 
HETATM 6741 O  O   . HOH K 4 .   ? 6.395   9.860   -28.968 1.00 29.99 ? 515 HOH A O   1 
HETATM 6742 O  O   . HOH K 4 .   ? -18.975 -19.288 -17.441 1.00 37.32 ? 516 HOH A O   1 
HETATM 6743 O  O   . HOH K 4 .   ? -4.396  14.259  -39.678 1.00 41.76 ? 517 HOH A O   1 
HETATM 6744 O  O   . HOH K 4 .   ? -1.876  25.026  -11.863 1.00 36.94 ? 518 HOH A O   1 
HETATM 6745 O  O   . HOH K 4 .   ? -2.926  -7.047  -10.892 1.00 30.70 ? 519 HOH A O   1 
HETATM 6746 O  O   . HOH K 4 .   ? 20.059  10.750  -12.866 1.00 42.27 ? 520 HOH A O   1 
HETATM 6747 O  O   . HOH K 4 .   ? -0.019  1.509   -18.587 1.00 26.88 ? 521 HOH A O   1 
HETATM 6748 O  O   . HOH K 4 .   ? -13.759 8.648   -21.694 1.00 27.14 ? 522 HOH A O   1 
HETATM 6749 O  O   . HOH K 4 .   ? -15.364 9.480   -11.639 1.00 30.28 ? 523 HOH A O   1 
HETATM 6750 O  O   . HOH K 4 .   ? -10.669 -23.819 -3.388  1.00 49.12 ? 524 HOH A O   1 
HETATM 6751 O  O   . HOH K 4 .   ? 12.462  11.190  -21.084 1.00 32.36 ? 525 HOH A O   1 
HETATM 6752 O  O   . HOH K 4 .   ? 0.798   3.692   -12.018 1.00 21.63 ? 526 HOH A O   1 
HETATM 6753 O  O   . HOH K 4 .   ? -17.479 -18.656 -19.653 1.00 28.81 ? 527 HOH A O   1 
HETATM 6754 O  O   . HOH K 4 .   ? -18.102 4.284   -16.872 1.00 32.03 ? 528 HOH A O   1 
HETATM 6755 O  O   . HOH K 4 .   ? 15.401  17.108  2.443   1.00 41.17 ? 529 HOH A O   1 
HETATM 6756 O  O   . HOH K 4 .   ? 14.111  25.898  -2.430  1.00 42.24 ? 530 HOH A O   1 
HETATM 6757 O  O   . HOH K 4 .   ? 3.126   1.606   -1.591  1.00 33.42 ? 531 HOH A O   1 
HETATM 6758 O  O   . HOH K 4 .   ? -1.678  29.764  -11.910 1.00 43.51 ? 532 HOH A O   1 
HETATM 6759 O  O   . HOH K 4 .   ? -0.616  16.898  -34.879 1.00 47.95 ? 533 HOH A O   1 
HETATM 6760 O  O   . HOH K 4 .   ? -22.518 -2.374  -12.547 1.00 46.02 ? 534 HOH A O   1 
HETATM 6761 O  O   . HOH K 4 .   ? -0.640  19.400  -34.214 1.00 35.44 ? 535 HOH A O   1 
HETATM 6762 O  O   . HOH K 4 .   ? 14.568  22.212  -22.802 1.00 40.67 ? 536 HOH A O   1 
HETATM 6763 O  O   . HOH K 4 .   ? -18.957 18.124  -9.337  1.00 48.20 ? 537 HOH A O   1 
HETATM 6764 O  O   . HOH K 4 .   ? -29.459 -15.324 -13.846 1.00 46.19 ? 538 HOH A O   1 
HETATM 6765 O  O   . HOH K 4 .   ? 3.554   20.456  -3.930  1.00 25.32 ? 539 HOH A O   1 
HETATM 6766 O  O   . HOH K 4 .   ? -15.222 26.221  -19.866 1.00 50.01 ? 540 HOH A O   1 
HETATM 6767 O  O   . HOH K 4 .   ? 21.014  21.424  -1.703  1.00 49.65 ? 541 HOH A O   1 
HETATM 6768 O  O   . HOH K 4 .   ? 8.636   13.788  4.205   1.00 33.46 ? 542 HOH A O   1 
HETATM 6769 O  O   . HOH K 4 .   ? 22.316  26.883  -2.653  1.00 46.69 ? 543 HOH A O   1 
HETATM 6770 O  O   . HOH K 4 .   ? 20.211  17.582  0.263   1.00 54.45 ? 544 HOH A O   1 
HETATM 6771 O  O   . HOH K 4 .   ? -9.007  1.899   -6.568  1.00 35.39 ? 545 HOH A O   1 
HETATM 6772 O  O   . HOH K 4 .   ? -6.897  23.714  -24.610 1.00 49.13 ? 546 HOH A O   1 
HETATM 6773 O  O   . HOH K 4 .   ? 6.123   29.791  -8.100  1.00 50.00 ? 547 HOH A O   1 
HETATM 6774 O  O   . HOH K 4 .   ? -13.903 7.020   -28.296 1.00 30.21 ? 548 HOH A O   1 
HETATM 6775 O  O   . HOH K 4 .   ? -0.252  14.873  -1.628  1.00 48.92 ? 549 HOH A O   1 
HETATM 6776 O  O   . HOH K 4 .   ? -4.492  1.253   -5.648  1.00 37.52 ? 550 HOH A O   1 
HETATM 6777 O  O   . HOH K 4 .   ? 6.097   25.351  -6.153  1.00 39.77 ? 551 HOH A O   1 
HETATM 6778 O  O   . HOH K 4 .   ? 21.202  13.098  -10.032 1.00 46.34 ? 552 HOH A O   1 
HETATM 6779 O  O   . HOH K 4 .   ? 21.023  21.331  -4.856  1.00 40.95 ? 553 HOH A O   1 
HETATM 6780 O  O   . HOH K 4 .   ? 6.899   22.019  -29.008 1.00 35.06 ? 554 HOH A O   1 
HETATM 6781 O  O   . HOH K 4 .   ? -6.811  22.525  -32.520 1.00 38.63 ? 555 HOH A O   1 
HETATM 6782 O  O   . HOH K 4 .   ? -9.234  -21.762 -6.028  1.00 46.74 ? 556 HOH A O   1 
HETATM 6783 O  O   . HOH K 4 .   ? 0.920   25.392  -27.141 1.00 28.37 ? 557 HOH A O   1 
HETATM 6784 O  O   . HOH K 4 .   ? -19.667 9.997   -21.245 1.00 49.49 ? 558 HOH A O   1 
HETATM 6785 O  O   . HOH K 4 .   ? -14.295 10.950  -28.189 1.00 46.70 ? 559 HOH A O   1 
HETATM 6786 O  O   . HOH K 4 .   ? -16.075 24.289  -21.070 1.00 51.22 ? 560 HOH A O   1 
HETATM 6787 O  O   . HOH K 4 .   ? -9.446  0.890   -4.567  1.00 39.16 ? 561 HOH A O   1 
HETATM 6788 O  O   . HOH K 4 .   ? 1.389   22.895  -3.240  1.00 45.66 ? 562 HOH A O   1 
HETATM 6789 O  O   . HOH K 4 .   ? 10.817  29.223  -2.012  1.00 47.01 ? 563 HOH A O   1 
HETATM 6790 O  O   . HOH K 4 .   ? 14.422  9.678   2.720   1.00 42.57 ? 564 HOH A O   1 
HETATM 6791 O  O   . HOH K 4 .   ? 5.040   20.118  -0.772  1.00 35.13 ? 565 HOH A O   1 
HETATM 6792 O  O   . HOH K 4 .   ? -6.086  16.016  -32.222 1.00 40.62 ? 566 HOH A O   1 
HETATM 6793 O  O   . HOH K 4 .   ? 18.568  27.147  -11.838 1.00 39.73 ? 567 HOH A O   1 
HETATM 6794 O  O   . HOH K 4 .   ? -20.835 7.406   -15.321 1.00 45.84 ? 568 HOH A O   1 
HETATM 6795 O  O   . HOH K 4 .   ? 14.424  19.750  -23.911 1.00 43.65 ? 569 HOH A O   1 
HETATM 6796 O  O   . HOH K 4 .   ? -14.654 21.601  -17.537 1.00 46.66 ? 570 HOH A O   1 
HETATM 6797 O  O   . HOH K 4 .   ? 3.564   10.256  -36.857 1.00 37.30 ? 571 HOH A O   1 
HETATM 6798 O  O   . HOH K 4 .   ? -19.510 10.963  -15.611 1.00 43.98 ? 572 HOH A O   1 
HETATM 6799 O  O   . HOH K 4 .   ? -19.215 12.349  -13.319 1.00 52.94 ? 573 HOH A O   1 
HETATM 6800 O  O   . HOH K 4 .   ? 2.963   28.223  -7.289  1.00 36.90 ? 574 HOH A O   1 
HETATM 6801 O  O   . HOH K 4 .   ? -7.572  26.694  -26.343 1.00 41.27 ? 575 HOH A O   1 
HETATM 6802 O  O   . HOH K 4 .   ? -6.325  -2.069  -5.557  1.00 38.88 ? 576 HOH A O   1 
HETATM 6803 O  O   . HOH K 4 .   ? 10.132  24.664  0.921   1.00 42.48 ? 577 HOH A O   1 
HETATM 6804 O  O   . HOH K 4 .   ? 0.593   0.546   -3.839  1.00 47.46 ? 578 HOH A O   1 
HETATM 6805 O  O   . HOH K 4 .   ? -22.075 -3.964  -9.928  1.00 43.52 ? 579 HOH A O   1 
HETATM 6806 O  O   . HOH K 4 .   ? -1.561  26.038  -9.072  1.00 51.50 ? 580 HOH A O   1 
HETATM 6807 O  O   . HOH K 4 .   ? 7.162   16.563  0.478   1.00 45.71 ? 581 HOH A O   1 
HETATM 6808 O  O   . HOH K 4 .   ? 23.435  27.153  -6.959  1.00 49.81 ? 582 HOH A O   1 
HETATM 6809 O  O   . HOH K 4 .   ? 1.928   25.048  -3.844  1.00 47.75 ? 583 HOH A O   1 
HETATM 6810 O  O   . HOH K 4 .   ? 6.312   31.742  -6.266  1.00 45.86 ? 584 HOH A O   1 
HETATM 6811 O  O   . HOH K 4 .   ? 4.322   27.078  -3.761  1.00 47.78 ? 585 HOH A O   1 
HETATM 6812 O  O   . HOH K 4 .   ? -2.495  22.540  -34.019 1.00 52.20 ? 586 HOH A O   1 
HETATM 6813 O  O   . HOH K 4 .   ? -4.992  -17.168 -10.512 1.00 38.30 ? 587 HOH A O   1 
HETATM 6814 O  O   . HOH K 4 .   ? 15.892  30.015  -3.383  1.00 52.86 ? 588 HOH A O   1 
HETATM 6815 O  O   . HOH K 4 .   ? 0.663   18.998  -2.747  1.00 35.41 ? 589 HOH A O   1 
HETATM 6816 O  O   . HOH K 4 .   ? 2.388   0.648   -7.811  1.00 32.88 ? 590 HOH A O   1 
HETATM 6817 O  O   . HOH K 4 .   ? -21.744 9.291   -19.737 1.00 46.07 ? 591 HOH A O   1 
HETATM 6818 O  O   . HOH K 4 .   ? -3.759  26.142  -10.763 1.00 40.94 ? 592 HOH A O   1 
HETATM 6819 O  O   . HOH K 4 .   ? -14.098 18.204  -7.041  1.00 35.60 ? 593 HOH A O   1 
HETATM 6820 O  O   . HOH K 4 .   ? 8.452   30.262  -3.088  1.00 38.64 ? 594 HOH A O   1 
HETATM 6821 O  O   . HOH K 4 .   ? 10.019  19.389  8.081   1.00 47.95 ? 595 HOH A O   1 
HETATM 6822 O  O   . HOH K 4 .   ? -22.541 7.367   -18.203 1.00 46.91 ? 596 HOH A O   1 
HETATM 6823 O  O   . HOH K 4 .   ? -5.686  -3.536  -2.317  1.00 52.47 ? 597 HOH A O   1 
HETATM 6824 O  O   . HOH K 4 .   ? -18.511 13.251  -29.465 1.00 43.52 ? 598 HOH A O   1 
HETATM 6825 O  O   . HOH K 4 .   ? 17.606  28.189  -10.044 1.00 45.83 ? 599 HOH A O   1 
HETATM 6826 O  O   . HOH K 4 .   ? -21.296 12.948  -18.234 1.00 51.13 ? 600 HOH A O   1 
HETATM 6827 O  O   . HOH K 4 .   ? -0.861  32.629  -10.741 1.00 47.84 ? 601 HOH A O   1 
HETATM 6828 O  O   . HOH K 4 .   ? 23.887  15.765  -9.923  1.00 44.58 ? 602 HOH A O   1 
HETATM 6829 O  O   . HOH K 4 .   ? 12.933  30.638  -1.434  1.00 40.11 ? 603 HOH A O   1 
HETATM 6830 O  O   . HOH K 4 .   ? 23.218  16.718  -13.120 1.00 45.64 ? 604 HOH A O   1 
HETATM 6831 O  O   . HOH K 4 .   ? 16.698  13.664  -26.776 1.00 48.91 ? 605 HOH A O   1 
HETATM 6832 O  O   . HOH K 4 .   ? 20.595  17.400  -15.988 1.00 51.53 ? 606 HOH A O   1 
HETATM 6833 O  O   . HOH K 4 .   ? 4.435   30.100  -5.778  1.00 49.11 ? 607 HOH A O   1 
HETATM 6834 O  O   . HOH K 4 .   ? 6.697   15.402  4.372   1.00 48.40 ? 608 HOH A O   1 
HETATM 6835 O  O   . HOH K 4 .   ? 25.713  25.577  -8.515  1.00 43.57 ? 609 HOH A O   1 
HETATM 6836 O  O   . HOH K 4 .   ? 0.851   17.222  -38.297 1.00 45.26 ? 610 HOH A O   1 
HETATM 6837 O  O   . HOH K 4 .   ? 15.046  32.258  -4.233  1.00 41.48 ? 611 HOH A O   1 
HETATM 6838 O  O   . HOH K 4 .   ? 2.116   19.495  -0.525  1.00 39.72 ? 612 HOH A O   1 
HETATM 6839 O  O   . HOH K 4 .   ? -2.025  19.832  -36.675 1.00 41.85 ? 613 HOH A O   1 
HETATM 6840 O  O   . HOH K 4 .   ? 10.989  14.578  9.565   1.00 41.56 ? 614 HOH A O   1 
HETATM 6841 O  O   . HOH K 4 .   ? 6.354   14.583  6.486   1.00 35.99 ? 615 HOH A O   1 
HETATM 6842 O  O   . HOH K 4 .   ? -22.722 9.287   -16.792 1.00 49.29 ? 616 HOH A O   1 
HETATM 6843 O  O   . HOH K 4 .   ? -13.879 26.634  -13.464 1.00 48.03 ? 617 HOH A O   1 
HETATM 6844 O  O   . HOH K 4 .   ? -1.789  -2.887  -4.327  1.00 53.65 ? 618 HOH A O   1 
HETATM 6845 O  O   . HOH K 4 .   ? 16.340  11.602  6.447   1.00 34.30 ? 619 HOH A O   1 
HETATM 6846 O  O   . HOH K 4 .   ? 17.403  31.713  -1.725  1.00 45.98 ? 620 HOH A O   1 
HETATM 6847 O  O   . HOH K 4 .   ? -5.585  29.000  -9.311  1.00 49.01 ? 621 HOH A O   1 
HETATM 6848 O  O   . HOH K 4 .   ? 28.162  18.886  -12.873 1.00 39.89 ? 622 HOH A O   1 
HETATM 6849 O  O   . HOH L 4 .   ? -2.923  3.681   11.470  1.00 43.55 ? 401 HOH B O   1 
HETATM 6850 O  O   . HOH L 4 .   ? -1.832  3.043   14.449  1.00 25.71 ? 402 HOH B O   1 
HETATM 6851 O  O   . HOH L 4 .   ? -12.907 17.290  8.487   1.00 16.45 ? 403 HOH B O   1 
HETATM 6852 O  O   . HOH L 4 .   ? 15.712  -25.119 17.732  1.00 31.46 ? 404 HOH B O   1 
HETATM 6853 O  O   . HOH L 4 .   ? 4.838   -9.265  23.518  1.00 34.99 ? 405 HOH B O   1 
HETATM 6854 O  O   . HOH L 4 .   ? 2.623   0.917   2.519   1.00 33.33 ? 406 HOH B O   1 
HETATM 6855 O  O   . HOH L 4 .   ? 4.024   -12.989 28.775  1.00 30.18 ? 407 HOH B O   1 
HETATM 6856 O  O   . HOH L 4 .   ? 5.845   -29.275 18.446  1.00 21.20 ? 408 HOH B O   1 
HETATM 6857 O  O   . HOH L 4 .   ? -17.377 -8.679  14.799  1.00 33.50 ? 409 HOH B O   1 
HETATM 6858 O  O   . HOH L 4 .   ? -11.982 -7.685  5.691   1.00 48.28 ? 410 HOH B O   1 
HETATM 6859 O  O   . HOH L 4 .   ? -1.032  -5.775  11.913  1.00 41.55 ? 411 HOH B O   1 
HETATM 6860 O  O   . HOH L 4 .   ? 12.791  -13.852 -4.113  1.00 28.97 ? 412 HOH B O   1 
HETATM 6861 O  O   . HOH L 4 .   ? 14.084  -23.220 21.933  1.00 30.16 ? 413 HOH B O   1 
HETATM 6862 O  O   . HOH L 4 .   ? 9.596   -26.681 27.070  1.00 37.19 ? 414 HOH B O   1 
HETATM 6863 O  O   . HOH L 4 .   ? -1.500  -14.883 7.171   1.00 27.97 ? 415 HOH B O   1 
HETATM 6864 O  O   . HOH L 4 .   ? -3.508  1.948   8.555   1.00 41.74 ? 416 HOH B O   1 
HETATM 6865 O  O   . HOH L 4 .   ? -0.941  -6.725  13.980  1.00 23.47 ? 417 HOH B O   1 
HETATM 6866 O  O   . HOH L 4 .   ? -20.777 3.078   8.541   1.00 42.01 ? 418 HOH B O   1 
HETATM 6867 O  O   . HOH L 4 .   ? -3.650  10.156  8.205   1.00 34.19 ? 419 HOH B O   1 
HETATM 6868 O  O   . HOH L 4 .   ? -15.508 10.271  18.896  1.00 26.08 ? 420 HOH B O   1 
HETATM 6869 O  O   . HOH L 4 .   ? -0.140  -22.354 4.716   1.00 35.95 ? 421 HOH B O   1 
HETATM 6870 O  O   . HOH L 4 .   ? 1.893   -32.568 25.533  1.00 27.74 ? 422 HOH B O   1 
HETATM 6871 O  O   . HOH L 4 .   ? 7.284   -13.741 20.555  1.00 23.92 ? 423 HOH B O   1 
HETATM 6872 O  O   . HOH L 4 .   ? 8.726   -23.511 28.796  1.00 27.12 ? 424 HOH B O   1 
HETATM 6873 O  O   . HOH L 4 .   ? -22.288 12.003  15.151  1.00 44.50 ? 425 HOH B O   1 
HETATM 6874 O  O   . HOH L 4 .   ? 2.721   -27.922 5.965   1.00 37.60 ? 426 HOH B O   1 
HETATM 6875 O  O   . HOH L 4 .   ? 11.089  -15.234 21.979  1.00 33.76 ? 427 HOH B O   1 
HETATM 6876 O  O   . HOH L 4 .   ? -1.411  -20.212 31.484  1.00 41.23 ? 428 HOH B O   1 
HETATM 6877 O  O   . HOH L 4 .   ? -5.924  -19.632 30.496  1.00 37.62 ? 429 HOH B O   1 
HETATM 6878 O  O   . HOH L 4 .   ? -0.009  -32.382 23.720  1.00 35.67 ? 430 HOH B O   1 
HETATM 6879 O  O   . HOH L 4 .   ? -13.981 -12.973 28.726  1.00 37.36 ? 431 HOH B O   1 
HETATM 6880 O  O   . HOH L 4 .   ? -0.436  -8.725  2.129   1.00 34.61 ? 432 HOH B O   1 
HETATM 6881 O  O   . HOH L 4 .   ? -2.117  -9.533  14.873  1.00 23.89 ? 433 HOH B O   1 
HETATM 6882 O  O   . HOH L 4 .   ? -4.653  -17.896 39.063  1.00 41.20 ? 434 HOH B O   1 
HETATM 6883 O  O   . HOH L 4 .   ? -12.173 -10.194 26.581  1.00 26.20 ? 435 HOH B O   1 
HETATM 6884 O  O   . HOH L 4 .   ? -3.474  -21.033 6.110   1.00 40.15 ? 436 HOH B O   1 
HETATM 6885 O  O   . HOH L 4 .   ? -16.414 7.566   19.561  1.00 43.34 ? 437 HOH B O   1 
HETATM 6886 O  O   . HOH L 4 .   ? -3.137  -10.294 3.160   1.00 45.17 ? 438 HOH B O   1 
HETATM 6887 O  O   . HOH L 4 .   ? 2.275   -13.020 34.431  1.00 31.98 ? 439 HOH B O   1 
HETATM 6888 O  O   . HOH L 4 .   ? -1.588  -30.150 25.040  1.00 29.17 ? 440 HOH B O   1 
HETATM 6889 O  O   . HOH L 4 .   ? -19.863 -2.582  11.249  1.00 32.63 ? 441 HOH B O   1 
HETATM 6890 O  O   . HOH L 4 .   ? 5.578   -13.513 -1.922  1.00 33.09 ? 442 HOH B O   1 
HETATM 6891 O  O   . HOH L 4 .   ? 1.185   -11.023 38.267  1.00 33.70 ? 443 HOH B O   1 
HETATM 6892 O  O   . HOH L 4 .   ? 9.700   -29.560 18.146  1.00 26.29 ? 444 HOH B O   1 
HETATM 6893 O  O   . HOH L 4 .   ? 3.139   -20.911 13.321  1.00 19.10 ? 445 HOH B O   1 
HETATM 6894 O  O   . HOH L 4 .   ? -2.869  -15.894 9.757   1.00 24.87 ? 446 HOH B O   1 
HETATM 6895 O  O   . HOH L 4 .   ? -10.046 -26.711 10.719  1.00 36.61 ? 447 HOH B O   1 
HETATM 6896 O  O   . HOH L 4 .   ? -14.589 19.535  15.408  1.00 32.25 ? 448 HOH B O   1 
HETATM 6897 O  O   . HOH L 4 .   ? 7.466   -18.061 -2.174  1.00 50.46 ? 449 HOH B O   1 
HETATM 6898 O  O   . HOH L 4 .   ? 6.177   -13.893 26.737  1.00 22.62 ? 450 HOH B O   1 
HETATM 6899 O  O   . HOH L 4 .   ? -4.652  9.359   12.950  1.00 17.53 ? 451 HOH B O   1 
HETATM 6900 O  O   . HOH L 4 .   ? 7.783   -33.527 21.139  1.00 32.27 ? 452 HOH B O   1 
HETATM 6901 O  O   . HOH L 4 .   ? 15.619  -22.168 0.782   1.00 39.63 ? 453 HOH B O   1 
HETATM 6902 O  O   . HOH L 4 .   ? -7.933  -1.908  4.500   1.00 36.01 ? 454 HOH B O   1 
HETATM 6903 O  O   . HOH L 4 .   ? -7.208  11.733  13.298  1.00 24.28 ? 455 HOH B O   1 
HETATM 6904 O  O   . HOH L 4 .   ? 1.402   -16.373 -3.684  1.00 41.31 ? 456 HOH B O   1 
HETATM 6905 O  O   . HOH L 4 .   ? 21.973  -25.796 11.990  1.00 51.66 ? 457 HOH B O   1 
HETATM 6906 O  O   . HOH L 4 .   ? -15.011 8.173   15.152  1.00 26.86 ? 458 HOH B O   1 
HETATM 6907 O  O   . HOH L 4 .   ? -4.452  -12.009 23.857  1.00 24.23 ? 459 HOH B O   1 
HETATM 6908 O  O   . HOH L 4 .   ? -0.003  -7.450  9.170   1.00 34.06 ? 460 HOH B O   1 
HETATM 6909 O  O   . HOH L 4 .   ? 8.739   -21.104 0.143   1.00 39.00 ? 461 HOH B O   1 
HETATM 6910 O  O   . HOH L 4 .   ? -0.107  -7.410  18.642  1.00 31.23 ? 462 HOH B O   1 
HETATM 6911 O  O   . HOH L 4 .   ? -2.848  -9.357  24.797  1.00 24.97 ? 463 HOH B O   1 
HETATM 6912 O  O   . HOH L 4 .   ? 4.880   -8.675  -0.365  1.00 37.39 ? 464 HOH B O   1 
HETATM 6913 O  O   . HOH L 4 .   ? -6.020  -2.560  15.766  1.00 18.73 ? 465 HOH B O   1 
HETATM 6914 O  O   . HOH L 4 .   ? -4.251  -17.673 8.192   1.00 33.40 ? 466 HOH B O   1 
HETATM 6915 O  O   . HOH L 4 .   ? 9.040   -9.253  2.132   1.00 31.68 ? 467 HOH B O   1 
HETATM 6916 O  O   . HOH L 4 .   ? 13.798  -18.396 -3.352  1.00 33.65 ? 468 HOH B O   1 
HETATM 6917 O  O   . HOH L 4 .   ? -24.459 -2.679  21.751  1.00 38.23 ? 469 HOH B O   1 
HETATM 6918 O  O   . HOH L 4 .   ? -2.667  -8.538  18.609  1.00 29.75 ? 470 HOH B O   1 
HETATM 6919 O  O   . HOH L 4 .   ? -17.953 -10.217 16.664  1.00 38.63 ? 471 HOH B O   1 
HETATM 6920 O  O   . HOH L 4 .   ? 18.663  -26.782 4.420   1.00 32.04 ? 472 HOH B O   1 
HETATM 6921 O  O   . HOH L 4 .   ? 13.822  -32.595 13.742  1.00 44.17 ? 473 HOH B O   1 
HETATM 6922 O  O   . HOH L 4 .   ? -22.902 10.427  16.719  1.00 48.53 ? 474 HOH B O   1 
HETATM 6923 O  O   . HOH L 4 .   ? 6.626   -15.995 28.999  1.00 25.83 ? 475 HOH B O   1 
HETATM 6924 O  O   . HOH L 4 .   ? -15.527 -15.421 11.623  1.00 28.17 ? 476 HOH B O   1 
HETATM 6925 O  O   . HOH L 4 .   ? -16.875 -21.279 5.963   1.00 47.84 ? 477 HOH B O   1 
HETATM 6926 O  O   . HOH L 4 .   ? -21.790 -13.440 8.155   1.00 37.21 ? 478 HOH B O   1 
HETATM 6927 O  O   . HOH L 4 .   ? -18.226 -16.890 18.944  1.00 32.61 ? 479 HOH B O   1 
HETATM 6928 O  O   . HOH L 4 .   ? -15.289 4.708   16.331  1.00 19.17 ? 480 HOH B O   1 
HETATM 6929 O  O   . HOH L 4 .   ? 20.518  -31.618 7.932   1.00 45.94 ? 481 HOH B O   1 
HETATM 6930 O  O   . HOH L 4 .   ? 1.695   -29.992 28.228  1.00 36.29 ? 482 HOH B O   1 
HETATM 6931 O  O   . HOH L 4 .   ? -6.461  -10.674 4.487   1.00 43.77 ? 483 HOH B O   1 
HETATM 6932 O  O   . HOH L 4 .   ? -20.501 -7.324  23.618  1.00 45.81 ? 484 HOH B O   1 
HETATM 6933 O  O   . HOH L 4 .   ? -13.662 -14.615 21.830  1.00 26.60 ? 485 HOH B O   1 
HETATM 6934 O  O   . HOH L 4 .   ? 6.404   -12.413 22.550  1.00 23.66 ? 486 HOH B O   1 
HETATM 6935 O  O   . HOH L 4 .   ? -11.417 -7.435  7.805   1.00 32.02 ? 487 HOH B O   1 
HETATM 6936 O  O   . HOH L 4 .   ? -7.532  -23.663 31.299  1.00 42.27 ? 488 HOH B O   1 
HETATM 6937 O  O   . HOH L 4 .   ? -7.148  12.118  10.503  1.00 29.46 ? 489 HOH B O   1 
HETATM 6938 O  O   . HOH L 4 .   ? -6.042  -28.853 11.783  1.00 35.38 ? 490 HOH B O   1 
HETATM 6939 O  O   . HOH L 4 .   ? -18.932 -14.145 5.608   1.00 38.02 ? 491 HOH B O   1 
HETATM 6940 O  O   . HOH L 4 .   ? 5.453   -7.257  4.351   1.00 20.75 ? 492 HOH B O   1 
HETATM 6941 O  O   . HOH L 4 .   ? -13.471 -4.566  24.692  1.00 32.59 ? 493 HOH B O   1 
HETATM 6942 O  O   . HOH L 4 .   ? -2.736  7.105   14.877  1.00 26.05 ? 494 HOH B O   1 
HETATM 6943 O  O   . HOH L 4 .   ? 8.414   -29.562 25.949  1.00 28.97 ? 495 HOH B O   1 
HETATM 6944 O  O   . HOH L 4 .   ? 5.822   -30.046 26.122  1.00 39.06 ? 496 HOH B O   1 
HETATM 6945 O  O   . HOH L 4 .   ? -2.912  1.190   10.725  1.00 28.11 ? 497 HOH B O   1 
HETATM 6946 O  O   . HOH L 4 .   ? 16.808  -28.618 2.180   1.00 42.91 ? 498 HOH B O   1 
HETATM 6947 O  O   . HOH L 4 .   ? -17.377 12.712  19.540  1.00 29.99 ? 499 HOH B O   1 
HETATM 6948 O  O   . HOH L 4 .   ? 2.914   -25.867 34.441  1.00 45.05 ? 500 HOH B O   1 
HETATM 6949 O  O   . HOH L 4 .   ? -3.605  -17.719 5.408   1.00 47.04 ? 501 HOH B O   1 
HETATM 6950 O  O   . HOH L 4 .   ? 0.648   -9.558  11.946  1.00 17.39 ? 502 HOH B O   1 
HETATM 6951 O  O   . HOH L 4 .   ? -18.622 13.400  17.340  1.00 52.92 ? 503 HOH B O   1 
HETATM 6952 O  O   . HOH L 4 .   ? -16.774 23.229  6.521   1.00 48.86 ? 504 HOH B O   1 
HETATM 6953 O  O   . HOH L 4 .   ? 6.558   -28.438 28.280  1.00 46.30 ? 505 HOH B O   1 
HETATM 6954 O  O   . HOH L 4 .   ? 3.446   -26.277 3.736   1.00 42.45 ? 506 HOH B O   1 
HETATM 6955 O  O   . HOH L 4 .   ? 3.095   -7.279  1.886   1.00 29.80 ? 507 HOH B O   1 
HETATM 6956 O  O   . HOH L 4 .   ? 12.370  -16.837 20.582  1.00 30.22 ? 508 HOH B O   1 
HETATM 6957 O  O   . HOH L 4 .   ? 4.273   -23.882 34.459  1.00 33.61 ? 509 HOH B O   1 
HETATM 6958 O  O   . HOH L 4 .   ? 21.074  -27.345 4.851   1.00 33.72 ? 510 HOH B O   1 
HETATM 6959 O  O   . HOH L 4 .   ? 1.843   2.370   5.640   1.00 47.81 ? 511 HOH B O   1 
HETATM 6960 O  O   . HOH L 4 .   ? -14.319 16.180  4.450   1.00 50.06 ? 512 HOH B O   1 
HETATM 6961 O  O   . HOH L 4 .   ? -1.268  -37.438 13.815  1.00 42.28 ? 513 HOH B O   1 
HETATM 6962 O  O   . HOH L 4 .   ? -4.545  -2.054  17.721  1.00 28.45 ? 514 HOH B O   1 
HETATM 6963 O  O   . HOH L 4 .   ? -21.906 11.604  3.624   1.00 52.15 ? 515 HOH B O   1 
HETATM 6964 O  O   . HOH L 4 .   ? 0.218   0.091   15.485  1.00 37.03 ? 516 HOH B O   1 
HETATM 6965 O  O   . HOH L 4 .   ? -9.055  15.732  6.245   1.00 27.95 ? 517 HOH B O   1 
HETATM 6966 O  O   . HOH L 4 .   ? -1.942  -2.427  17.734  1.00 36.96 ? 518 HOH B O   1 
HETATM 6967 O  O   . HOH L 4 .   ? -15.662 -29.419 24.017  1.00 52.53 ? 519 HOH B O   1 
HETATM 6968 O  O   . HOH L 4 .   ? 3.263   -11.667 37.048  1.00 42.72 ? 520 HOH B O   1 
HETATM 6969 O  O   . HOH L 4 .   ? -2.954  -31.538 32.698  1.00 36.45 ? 521 HOH B O   1 
HETATM 6970 O  O   . HOH L 4 .   ? 5.882   -5.863  1.305   1.00 42.54 ? 522 HOH B O   1 
HETATM 6971 O  O   . HOH L 4 .   ? 0.451   -0.808  13.321  1.00 39.35 ? 523 HOH B O   1 
HETATM 6972 O  O   . HOH L 4 .   ? 10.960  -13.068 19.762  1.00 41.86 ? 524 HOH B O   1 
HETATM 6973 O  O   . HOH L 4 .   ? -22.217 20.667  12.149  1.00 46.11 ? 525 HOH B O   1 
HETATM 6974 O  O   . HOH L 4 .   ? 0.712   -31.324 26.889  1.00 29.82 ? 526 HOH B O   1 
HETATM 6975 O  O   . HOH L 4 .   ? -19.456 8.536   20.754  1.00 36.47 ? 527 HOH B O   1 
HETATM 6976 O  O   . HOH L 4 .   ? -15.264 23.317  15.199  1.00 46.31 ? 528 HOH B O   1 
HETATM 6977 O  O   . HOH L 4 .   ? -11.325 21.233  4.688   1.00 44.42 ? 529 HOH B O   1 
HETATM 6978 O  O   . HOH L 4 .   ? 2.108   -1.685  0.955   1.00 45.08 ? 530 HOH B O   1 
HETATM 6979 O  O   . HOH L 4 .   ? -6.414  -3.859  5.760   1.00 38.55 ? 531 HOH B O   1 
HETATM 6980 O  O   . HOH L 4 .   ? 0.832   -24.932 2.971   1.00 42.28 ? 532 HOH B O   1 
HETATM 6981 O  O   . HOH L 4 .   ? -5.153  11.086  10.684  1.00 35.96 ? 533 HOH B O   1 
HETATM 6982 O  O   . HOH L 4 .   ? 12.783  -17.585 30.621  1.00 33.06 ? 534 HOH B O   1 
HETATM 6983 O  O   . HOH L 4 .   ? -1.840  -2.784  7.387   1.00 53.56 ? 535 HOH B O   1 
HETATM 6984 O  O   . HOH L 4 .   ? 2.230   -6.926  7.707   1.00 26.31 ? 536 HOH B O   1 
HETATM 6985 O  O   . HOH L 4 .   ? 16.304  -19.582 25.759  1.00 43.14 ? 537 HOH B O   1 
HETATM 6986 O  O   . HOH L 4 .   ? -18.935 25.008  17.851  1.00 52.57 ? 538 HOH B O   1 
HETATM 6987 O  O   . HOH L 4 .   ? 0.873   1.897   12.440  1.00 43.45 ? 539 HOH B O   1 
HETATM 6988 O  O   . HOH L 4 .   ? 16.509  -19.990 28.970  1.00 41.50 ? 540 HOH B O   1 
HETATM 6989 O  O   . HOH L 4 .   ? 2.895   -22.858 36.045  1.00 43.17 ? 541 HOH B O   1 
HETATM 6990 O  O   . HOH L 4 .   ? -22.549 22.293  10.258  1.00 55.76 ? 542 HOH B O   1 
HETATM 6991 O  O   . HOH L 4 .   ? 2.164   -5.629  4.755   1.00 40.89 ? 543 HOH B O   1 
HETATM 6992 O  O   . HOH L 4 .   ? -15.773 26.271  14.013  1.00 54.32 ? 544 HOH B O   1 
HETATM 6993 O  O   . HOH L 4 .   ? -11.244 -31.646 31.778  1.00 51.97 ? 545 HOH B O   1 
HETATM 6994 O  O   . HOH L 4 .   ? -7.086  -33.119 32.406  1.00 47.13 ? 546 HOH B O   1 
HETATM 6995 O  O   . HOH L 4 .   ? 6.206   -21.555 37.616  1.00 38.37 ? 547 HOH B O   1 
HETATM 6996 O  O   . HOH L 4 .   ? -27.729 17.085  7.538   1.00 46.44 ? 548 HOH B O   1 
HETATM 6997 O  O   . HOH L 4 .   ? -9.017  25.330  7.720   1.00 43.94 ? 549 HOH B O   1 
HETATM 6998 O  O   . HOH M 4 .   ? -12.884 19.046  25.706  1.00 19.40 ? 401 HOH C O   1 
HETATM 6999 O  O   . HOH M 4 .   ? -7.288  12.960  39.973  1.00 36.73 ? 402 HOH C O   1 
HETATM 7000 O  O   . HOH M 4 .   ? 14.791  4.938   19.722  1.00 36.80 ? 403 HOH C O   1 
HETATM 7001 O  O   . HOH M 4 .   ? -5.713  24.198  17.411  1.00 41.72 ? 404 HOH C O   1 
HETATM 7002 O  O   . HOH M 4 .   ? 2.439   17.416  19.290  1.00 39.68 ? 405 HOH C O   1 
HETATM 7003 O  O   . HOH M 4 .   ? -21.061 7.497   29.622  1.00 29.80 ? 406 HOH C O   1 
HETATM 7004 O  O   . HOH M 4 .   ? -13.572 5.460   37.090  1.00 27.88 ? 407 HOH C O   1 
HETATM 7005 O  O   . HOH M 4 .   ? -17.073 6.813   35.656  1.00 35.85 ? 408 HOH C O   1 
HETATM 7006 O  O   . HOH M 4 .   ? 12.427  9.291   23.658  1.00 43.77 ? 409 HOH C O   1 
HETATM 7007 O  O   . HOH M 4 .   ? 16.036  0.960   0.858   1.00 39.79 ? 410 HOH C O   1 
HETATM 7008 O  O   . HOH M 4 .   ? 3.552   0.167   8.954   1.00 34.93 ? 411 HOH C O   1 
HETATM 7009 O  O   . HOH M 4 .   ? 10.674  6.571   35.701  1.00 32.27 ? 412 HOH C O   1 
HETATM 7010 O  O   . HOH M 4 .   ? -0.042  -0.862  18.956  1.00 24.19 ? 413 HOH C O   1 
HETATM 7011 O  O   . HOH M 4 .   ? 22.921  -13.755 9.686   1.00 44.22 ? 414 HOH C O   1 
HETATM 7012 O  O   . HOH M 4 .   ? 10.820  4.051   14.350  1.00 25.63 ? 415 HOH C O   1 
HETATM 7013 O  O   . HOH M 4 .   ? -5.027  -11.613 36.497  1.00 37.12 ? 416 HOH C O   1 
HETATM 7014 O  O   . HOH M 4 .   ? -10.197 -5.885  21.480  1.00 42.34 ? 417 HOH C O   1 
HETATM 7015 O  O   . HOH M 4 .   ? 21.991  -0.233  13.930  1.00 42.40 ? 418 HOH C O   1 
HETATM 7016 O  O   . HOH M 4 .   ? 6.018   -7.812  32.349  1.00 28.98 ? 419 HOH C O   1 
HETATM 7017 O  O   . HOH M 4 .   ? 21.975  4.556   8.839   1.00 46.78 ? 420 HOH C O   1 
HETATM 7018 O  O   . HOH M 4 .   ? 1.440   17.647  40.074  1.00 44.85 ? 421 HOH C O   1 
HETATM 7019 O  O   . HOH M 4 .   ? -0.416  -0.652  21.841  1.00 23.51 ? 422 HOH C O   1 
HETATM 7020 O  O   . HOH M 4 .   ? 11.373  0.725   -2.651  1.00 33.93 ? 423 HOH C O   1 
HETATM 7021 O  O   . HOH M 4 .   ? 10.153  9.551   28.721  1.00 32.88 ? 424 HOH C O   1 
HETATM 7022 O  O   . HOH M 4 .   ? -30.746 15.054  32.691  1.00 37.54 ? 425 HOH C O   1 
HETATM 7023 O  O   . HOH M 4 .   ? 17.612  -18.920 1.531   1.00 46.16 ? 426 HOH C O   1 
HETATM 7024 O  O   . HOH M 4 .   ? -16.074 -1.300  23.844  1.00 37.57 ? 427 HOH C O   1 
HETATM 7025 O  O   . HOH M 4 .   ? -21.179 3.182   33.907  1.00 44.30 ? 428 HOH C O   1 
HETATM 7026 O  O   . HOH M 4 .   ? -13.555 7.264   24.202  1.00 39.55 ? 429 HOH C O   1 
HETATM 7027 O  O   . HOH M 4 .   ? 6.777   2.967   9.174   1.00 18.45 ? 430 HOH C O   1 
HETATM 7028 O  O   . HOH M 4 .   ? 17.370  -17.313 9.104   1.00 24.02 ? 431 HOH C O   1 
HETATM 7029 O  O   . HOH M 4 .   ? -14.830 -8.173  28.258  1.00 38.46 ? 432 HOH C O   1 
HETATM 7030 O  O   . HOH M 4 .   ? 18.616  -4.878  1.252   1.00 28.86 ? 433 HOH C O   1 
HETATM 7031 O  O   . HOH M 4 .   ? 19.944  -16.690 12.559  1.00 29.74 ? 434 HOH C O   1 
HETATM 7032 O  O   . HOH M 4 .   ? -6.885  6.782   29.257  1.00 26.75 ? 435 HOH C O   1 
HETATM 7033 O  O   . HOH M 4 .   ? 15.212  -15.617 10.278  1.00 31.99 ? 436 HOH C O   1 
HETATM 7034 O  O   . HOH M 4 .   ? -2.334  10.141  14.089  1.00 38.13 ? 437 HOH C O   1 
HETATM 7035 O  O   . HOH M 4 .   ? 13.875  -4.720  26.635  1.00 33.22 ? 438 HOH C O   1 
HETATM 7036 O  O   . HOH M 4 .   ? 11.072  2.078   21.569  1.00 22.75 ? 439 HOH C O   1 
HETATM 7037 O  O   . HOH M 4 .   ? 0.120   4.497   18.015  1.00 24.05 ? 440 HOH C O   1 
HETATM 7038 O  O   . HOH M 4 .   ? -11.969 -1.374  23.568  1.00 19.27 ? 441 HOH C O   1 
HETATM 7039 O  O   . HOH M 4 .   ? 4.214   9.681   19.165  1.00 39.01 ? 442 HOH C O   1 
HETATM 7040 O  O   . HOH M 4 .   ? 16.765  1.987   6.380   1.00 31.76 ? 443 HOH C O   1 
HETATM 7041 O  O   . HOH M 4 .   ? -12.261 -19.613 27.878  1.00 43.91 ? 444 HOH C O   1 
HETATM 7042 O  O   . HOH M 4 .   ? -1.799  14.693  29.956  1.00 26.88 ? 445 HOH C O   1 
HETATM 7043 O  O   . HOH M 4 .   ? 14.216  5.379   4.262   1.00 33.00 ? 446 HOH C O   1 
HETATM 7044 O  O   . HOH M 4 .   ? 14.211  -15.093 14.896  1.00 40.47 ? 447 HOH C O   1 
HETATM 7045 O  O   . HOH M 4 .   ? 7.401   7.638   21.669  1.00 28.91 ? 448 HOH C O   1 
HETATM 7046 O  O   . HOH M 4 .   ? 8.042   14.017  38.917  1.00 40.68 ? 449 HOH C O   1 
HETATM 7047 O  O   . HOH M 4 .   ? -1.786  -8.163  27.033  1.00 22.75 ? 450 HOH C O   1 
HETATM 7048 O  O   . HOH M 4 .   ? 5.049   -4.986  17.338  1.00 21.37 ? 451 HOH C O   1 
HETATM 7049 O  O   . HOH M 4 .   ? -11.018 16.431  37.539  1.00 27.07 ? 452 HOH C O   1 
HETATM 7050 O  O   . HOH M 4 .   ? -12.654 -15.375 28.585  1.00 41.32 ? 453 HOH C O   1 
HETATM 7051 O  O   . HOH M 4 .   ? -18.635 -4.313  34.100  1.00 40.66 ? 454 HOH C O   1 
HETATM 7052 O  O   . HOH M 4 .   ? -9.492  27.283  24.335  1.00 44.00 ? 455 HOH C O   1 
HETATM 7053 O  O   . HOH M 4 .   ? -17.817 -9.606  34.480  1.00 34.18 ? 456 HOH C O   1 
HETATM 7054 O  O   . HOH M 4 .   ? 9.827   11.460  36.734  1.00 45.12 ? 457 HOH C O   1 
HETATM 7055 O  O   . HOH M 4 .   ? 1.624   -6.966  13.827  1.00 32.28 ? 458 HOH C O   1 
HETATM 7056 O  O   . HOH M 4 .   ? 4.797   1.342   2.442   1.00 26.43 ? 459 HOH C O   1 
HETATM 7057 O  O   . HOH M 4 .   ? -16.080 6.598   23.147  1.00 42.07 ? 460 HOH C O   1 
HETATM 7058 O  O   . HOH M 4 .   ? 16.624  6.132   13.556  1.00 41.51 ? 461 HOH C O   1 
HETATM 7059 O  O   . HOH M 4 .   ? 14.681  -10.757 14.251  1.00 25.30 ? 462 HOH C O   1 
HETATM 7060 O  O   . HOH M 4 .   ? 5.061   -2.745  8.729   1.00 36.58 ? 463 HOH C O   1 
HETATM 7061 O  O   . HOH M 4 .   ? -9.301  -1.380  42.713  1.00 34.79 ? 464 HOH C O   1 
HETATM 7062 O  O   . HOH M 4 .   ? 0.803   6.266   26.123  1.00 18.01 ? 465 HOH C O   1 
HETATM 7063 O  O   . HOH M 4 .   ? -13.129 -7.048  25.791  1.00 32.61 ? 466 HOH C O   1 
HETATM 7064 O  O   . HOH M 4 .   ? 7.412   0.187   10.200  1.00 36.95 ? 467 HOH C O   1 
HETATM 7065 O  O   . HOH M 4 .   ? 3.915   8.065   38.646  1.00 33.88 ? 468 HOH C O   1 
HETATM 7066 O  O   . HOH M 4 .   ? -2.657  18.312  18.134  1.00 27.61 ? 469 HOH C O   1 
HETATM 7067 O  O   . HOH M 4 .   ? 17.909  -15.819 0.529   1.00 35.65 ? 470 HOH C O   1 
HETATM 7068 O  O   . HOH M 4 .   ? 16.011  -11.309 11.151  1.00 32.35 ? 471 HOH C O   1 
HETATM 7069 O  O   . HOH M 4 .   ? -0.874  -4.321  22.253  1.00 21.74 ? 472 HOH C O   1 
HETATM 7070 O  O   . HOH M 4 .   ? 18.627  -7.651  -0.006  1.00 26.25 ? 473 HOH C O   1 
HETATM 7071 O  O   . HOH M 4 .   ? 11.582  -6.681  2.712   1.00 28.26 ? 474 HOH C O   1 
HETATM 7072 O  O   . HOH M 4 .   ? 23.133  3.096   6.483   1.00 52.02 ? 475 HOH C O   1 
HETATM 7073 O  O   . HOH M 4 .   ? 25.361  -5.636  3.873   1.00 38.87 ? 476 HOH C O   1 
HETATM 7074 O  O   . HOH M 4 .   ? 1.424   11.498  29.850  1.00 29.77 ? 477 HOH C O   1 
HETATM 7075 O  O   . HOH M 4 .   ? 0.783   8.504   24.501  1.00 28.88 ? 478 HOH C O   1 
HETATM 7076 O  O   . HOH M 4 .   ? 1.310   -2.616  41.243  1.00 36.10 ? 479 HOH C O   1 
HETATM 7077 O  O   . HOH M 4 .   ? 7.656   -6.714  5.436   1.00 22.05 ? 480 HOH C O   1 
HETATM 7078 O  O   . HOH M 4 .   ? 3.941   -14.420 33.074  1.00 43.35 ? 481 HOH C O   1 
HETATM 7079 O  O   . HOH M 4 .   ? -14.328 21.284  22.122  1.00 28.74 ? 482 HOH C O   1 
HETATM 7080 O  O   . HOH M 4 .   ? 3.500   14.371  17.585  1.00 47.67 ? 483 HOH C O   1 
HETATM 7081 O  O   . HOH M 4 .   ? 11.628  1.267   31.079  1.00 33.36 ? 484 HOH C O   1 
HETATM 7082 O  O   . HOH M 4 .   ? -19.220 23.466  22.478  1.00 35.61 ? 485 HOH C O   1 
HETATM 7083 O  O   . HOH M 4 .   ? 9.473   8.952   26.137  1.00 43.65 ? 486 HOH C O   1 
HETATM 7084 O  O   . HOH M 4 .   ? 3.948   6.492   17.343  1.00 33.51 ? 487 HOH C O   1 
HETATM 7085 O  O   . HOH M 4 .   ? -14.665 19.381  32.200  1.00 30.53 ? 488 HOH C O   1 
HETATM 7086 O  O   . HOH M 4 .   ? 7.299   3.550   17.282  1.00 28.27 ? 489 HOH C O   1 
HETATM 7087 O  O   . HOH M 4 .   ? 2.542   16.325  21.109  1.00 42.85 ? 490 HOH C O   1 
HETATM 7088 O  O   . HOH M 4 .   ? 24.306  -18.215 1.809   1.00 37.72 ? 491 HOH C O   1 
HETATM 7089 O  O   . HOH M 4 .   ? 17.304  1.953   2.030   1.00 39.84 ? 492 HOH C O   1 
HETATM 7090 O  O   . HOH M 4 .   ? 13.407  13.902  28.612  1.00 42.68 ? 493 HOH C O   1 
HETATM 7091 O  O   . HOH M 4 .   ? 9.198   -2.896  2.700   1.00 21.01 ? 494 HOH C O   1 
HETATM 7092 O  O   . HOH M 4 .   ? 10.872  -5.234  35.391  1.00 33.79 ? 495 HOH C O   1 
HETATM 7093 O  O   . HOH M 4 .   ? 0.227   1.720   16.670  1.00 36.30 ? 496 HOH C O   1 
HETATM 7094 O  O   . HOH M 4 .   ? 5.149   -1.156  11.752  1.00 32.43 ? 497 HOH C O   1 
HETATM 7095 O  O   . HOH M 4 .   ? 17.120  4.649   29.715  1.00 39.27 ? 498 HOH C O   1 
HETATM 7096 O  O   . HOH M 4 .   ? 7.557   1.396   -0.897  1.00 31.26 ? 499 HOH C O   1 
HETATM 7097 O  O   . HOH M 4 .   ? -13.034 24.376  21.678  1.00 41.58 ? 500 HOH C O   1 
HETATM 7098 O  O   . HOH M 4 .   ? 13.230  8.628   21.200  1.00 47.21 ? 501 HOH C O   1 
HETATM 7099 O  O   . HOH M 4 .   ? -5.948  11.295  40.033  1.00 35.32 ? 502 HOH C O   1 
HETATM 7100 O  O   . HOH M 4 .   ? 10.741  -8.822  4.207   1.00 29.03 ? 503 HOH C O   1 
HETATM 7101 O  O   . HOH M 4 .   ? -20.777 19.977  33.395  1.00 54.38 ? 504 HOH C O   1 
HETATM 7102 O  O   . HOH M 4 .   ? 2.193   8.334   27.831  1.00 32.81 ? 505 HOH C O   1 
HETATM 7103 O  O   . HOH M 4 .   ? 1.972   10.863  24.776  1.00 34.65 ? 506 HOH C O   1 
HETATM 7104 O  O   . HOH M 4 .   ? -1.824  2.860   19.874  1.00 32.84 ? 507 HOH C O   1 
HETATM 7105 O  O   . HOH M 4 .   ? 2.492   10.757  27.303  1.00 29.20 ? 508 HOH C O   1 
HETATM 7106 O  O   . HOH M 4 .   ? -0.658  8.524   39.535  1.00 32.23 ? 509 HOH C O   1 
HETATM 7107 O  O   . HOH M 4 .   ? -11.415 -4.194  23.254  1.00 25.65 ? 510 HOH C O   1 
HETATM 7108 O  O   . HOH M 4 .   ? 21.436  -20.359 8.472   1.00 39.84 ? 511 HOH C O   1 
HETATM 7109 O  O   . HOH M 4 .   ? -10.486 22.920  17.853  1.00 31.72 ? 512 HOH C O   1 
HETATM 7110 O  O   . HOH M 4 .   ? 19.083  4.950   21.608  1.00 50.32 ? 513 HOH C O   1 
HETATM 7111 O  O   . HOH M 4 .   ? -16.958 15.819  36.946  1.00 43.17 ? 514 HOH C O   1 
HETATM 7112 O  O   . HOH M 4 .   ? 11.737  -0.100  33.984  1.00 32.09 ? 515 HOH C O   1 
HETATM 7113 O  O   . HOH M 4 .   ? 16.069  13.197  29.157  1.00 45.18 ? 516 HOH C O   1 
HETATM 7114 O  O   . HOH M 4 .   ? -8.994  18.186  37.964  1.00 47.79 ? 517 HOH C O   1 
HETATM 7115 O  O   . HOH M 4 .   ? -2.831  8.461   40.499  1.00 36.18 ? 518 HOH C O   1 
HETATM 7116 O  O   . HOH M 4 .   ? 22.756  -2.336  10.224  1.00 36.09 ? 519 HOH C O   1 
HETATM 7117 O  O   . HOH M 4 .   ? 23.319  1.546   12.349  1.00 43.20 ? 520 HOH C O   1 
HETATM 7118 O  O   . HOH M 4 .   ? -24.519 12.714  34.221  1.00 44.98 ? 521 HOH C O   1 
HETATM 7119 O  O   . HOH M 4 .   ? -5.358  13.272  13.354  1.00 29.47 ? 522 HOH C O   1 
HETATM 7120 O  O   . HOH M 4 .   ? 4.548   -7.211  7.191   1.00 16.97 ? 523 HOH C O   1 
HETATM 7121 O  O   . HOH M 4 .   ? 17.121  -3.108  -0.056  1.00 30.25 ? 524 HOH C O   1 
HETATM 7122 O  O   . HOH M 4 .   ? 7.386   5.521   9.229   1.00 42.11 ? 525 HOH C O   1 
HETATM 7123 O  O   . HOH M 4 .   ? 5.094   9.598   9.030   1.00 45.75 ? 526 HOH C O   1 
HETATM 7124 O  O   . HOH M 4 .   ? 10.522  10.442  11.079  1.00 55.01 ? 527 HOH C O   1 
HETATM 7125 O  O   . HOH M 4 .   ? 11.548  -15.568 30.791  1.00 31.65 ? 528 HOH C O   1 
HETATM 7126 O  O   . HOH M 4 .   ? -2.282  2.761   41.568  1.00 44.64 ? 529 HOH C O   1 
HETATM 7127 O  O   . HOH M 4 .   ? -17.143 8.654   23.750  1.00 51.34 ? 530 HOH C O   1 
HETATM 7128 O  O   . HOH M 4 .   ? -22.572 16.291  34.598  1.00 45.35 ? 531 HOH C O   1 
HETATM 7129 O  O   . HOH M 4 .   ? 9.994   5.586   18.315  1.00 34.79 ? 532 HOH C O   1 
HETATM 7130 O  O   . HOH M 4 .   ? 2.823   -6.435  16.681  1.00 38.06 ? 533 HOH C O   1 
HETATM 7131 O  O   . HOH M 4 .   ? 9.467   -0.551  -3.359  1.00 36.60 ? 534 HOH C O   1 
HETATM 7132 O  O   . HOH M 4 .   ? 21.510  -4.153  0.741   1.00 38.04 ? 535 HOH C O   1 
HETATM 7133 O  O   . HOH M 4 .   ? 17.080  6.085   24.456  1.00 43.07 ? 536 HOH C O   1 
HETATM 7134 O  O   . HOH M 4 .   ? 10.091  -2.481  0.349   1.00 36.76 ? 537 HOH C O   1 
HETATM 7135 O  O   . HOH M 4 .   ? -9.032  24.219  16.083  1.00 41.08 ? 538 HOH C O   1 
HETATM 7136 O  O   . HOH M 4 .   ? 10.224  12.083  8.549   1.00 40.13 ? 539 HOH C O   1 
HETATM 7137 O  O   . HOH M 4 .   ? 9.216   4.952   15.085  1.00 39.13 ? 540 HOH C O   1 
HETATM 7138 O  O   . HOH M 4 .   ? 15.980  8.822   24.559  1.00 49.83 ? 541 HOH C O   1 
HETATM 7139 O  O   . HOH M 4 .   ? -8.025  20.153  11.300  1.00 44.94 ? 542 HOH C O   1 
HETATM 7140 O  O   . HOH M 4 .   ? 4.274   15.067  19.461  1.00 51.51 ? 543 HOH C O   1 
HETATM 7141 O  O   . HOH M 4 .   ? 6.679   7.831   39.199  1.00 51.37 ? 544 HOH C O   1 
HETATM 7142 O  O   . HOH M 4 .   ? -9.646  22.207  15.568  1.00 33.17 ? 545 HOH C O   1 
HETATM 7143 O  O   . HOH M 4 .   ? 6.012   11.842  7.380   1.00 43.29 ? 546 HOH C O   1 
HETATM 7144 O  O   . HOH M 4 .   ? 13.000  18.101  32.700  1.00 53.25 ? 547 HOH C O   1 
HETATM 7145 O  O   . HOH M 4 .   ? 25.630  0.897   11.016  1.00 50.13 ? 548 HOH C O   1 
HETATM 7146 O  O   . HOH M 4 .   ? 5.226   2.484   11.223  1.00 43.58 ? 549 HOH C O   1 
HETATM 7147 O  O   . HOH M 4 .   ? 22.113  7.454   7.739   1.00 47.10 ? 550 HOH C O   1 
HETATM 7148 O  O   . HOH M 4 .   ? 7.092   6.293   11.512  1.00 36.83 ? 551 HOH C O   1 
HETATM 7149 O  O   . HOH M 4 .   ? -20.230 6.714   20.867  1.00 39.35 ? 552 HOH C O   1 
HETATM 7150 O  O   . HOH M 4 .   ? 6.224   -3.008  2.442   1.00 34.97 ? 553 HOH C O   1 
HETATM 7151 O  O   . HOH M 4 .   ? 4.991   -4.505  6.660   1.00 43.81 ? 554 HOH C O   1 
HETATM 7152 O  O   . HOH M 4 .   ? -20.120 26.024  23.628  1.00 38.21 ? 555 HOH C O   1 
HETATM 7153 O  O   . HOH M 4 .   ? -12.211 29.745  22.181  1.00 43.83 ? 556 HOH C O   1 
HETATM 7154 O  O   . HOH M 4 .   ? 0.285   20.550  20.291  1.00 42.96 ? 557 HOH C O   1 
HETATM 7155 O  O   . HOH M 4 .   ? 0.694   13.870  29.796  1.00 34.59 ? 558 HOH C O   1 
HETATM 7156 O  O   . HOH M 4 .   ? 7.436   -18.344 34.935  1.00 47.58 ? 559 HOH C O   1 
HETATM 7157 O  O   . HOH M 4 .   ? -0.487  6.194   15.615  1.00 37.55 ? 560 HOH C O   1 
HETATM 7158 O  O   . HOH M 4 .   ? 13.338  14.638  25.449  1.00 53.14 ? 561 HOH C O   1 
HETATM 7159 O  O   . HOH M 4 .   ? 18.041  9.675   25.633  1.00 41.16 ? 562 HOH C O   1 
HETATM 7160 O  O   . HOH M 4 .   ? 14.553  15.812  28.242  1.00 47.45 ? 563 HOH C O   1 
HETATM 7161 O  O   . HOH M 4 .   ? -1.660  22.778  18.076  1.00 57.44 ? 564 HOH C O   1 
HETATM 7162 O  O   . HOH M 4 .   ? -3.231  25.705  16.669  1.00 43.02 ? 565 HOH C O   1 
HETATM 7163 O  O   . HOH M 4 .   ? 8.140   15.743  23.700  1.00 42.15 ? 566 HOH C O   1 
HETATM 7164 O  O   . HOH M 4 .   ? 8.341   7.224   18.229  1.00 45.18 ? 567 HOH C O   1 
HETATM 7165 O  O   . HOH M 4 .   ? -16.029 27.192  21.623  1.00 39.54 ? 568 HOH C O   1 
HETATM 7166 O  O   . HOH M 4 .   ? 5.079   -1.534  0.913   1.00 33.45 ? 569 HOH C O   1 
HETATM 7167 O  O   . HOH M 4 .   ? -6.898  27.299  18.536  1.00 34.95 ? 570 HOH C O   1 
HETATM 7168 O  O   . HOH M 4 .   ? 4.728   -3.993  4.088   1.00 26.01 ? 571 HOH C O   1 
HETATM 7169 O  O   . HOH M 4 .   ? 6.599   11.912  16.256  1.00 43.49 ? 572 HOH C O   1 
HETATM 7170 O  O   . HOH M 4 .   ? 26.493  4.164   10.816  1.00 48.06 ? 573 HOH C O   1 
HETATM 7171 O  O   . HOH M 4 .   ? 15.549  8.406   11.293  1.00 37.12 ? 574 HOH C O   1 
HETATM 7172 O  O   . HOH M 4 .   ? 10.467  12.885  11.653  1.00 50.69 ? 575 HOH C O   1 
HETATM 7173 O  O   . HOH M 4 .   ? 12.869  11.588  12.545  1.00 46.07 ? 576 HOH C O   1 
HETATM 7174 O  O   . HOH M 4 .   ? 13.341  12.974  10.481  1.00 49.89 ? 577 HOH C O   1 
HETATM 7175 O  O   . HOH M 4 .   ? 16.877  -16.108 31.089  1.00 47.50 ? 578 HOH C O   1 
HETATM 7176 O  O   . HOH M 4 .   ? 6.468   -16.904 38.548  1.00 46.34 ? 579 HOH C O   1 
HETATM 7177 O  O   . HOH M 4 .   ? 12.172  -19.468 36.576  1.00 48.30 ? 580 HOH C O   1 
HETATM 7178 O  O   . HOH M 4 .   ? 17.109  10.751  12.578  1.00 42.56 ? 581 HOH C O   1 
HETATM 7179 O  O   . HOH M 4 .   ? -2.129  16.410  8.560   1.00 43.02 ? 582 HOH C O   1 
HETATM 7180 O  O   . HOH M 4 .   ? -3.813  27.633  15.319  1.00 44.61 ? 583 HOH C O   1 
HETATM 7181 O  O   . HOH M 4 .   ? 19.300  11.604  24.423  1.00 48.93 ? 584 HOH C O   1 
HETATM 7182 O  O   . HOH M 4 .   ? 15.583  14.311  22.502  1.00 51.83 ? 585 HOH C O   1 
HETATM 7183 O  O   . HOH M 4 .   ? 6.659   9.446   14.347  1.00 43.21 ? 586 HOH C O   1 
HETATM 7184 O  O   . HOH N 4 .   ? -19.139 -17.420 -22.215 1.00 47.58 ? 401 HOH D O   1 
HETATM 7185 O  O   . HOH N 4 .   ? 21.115  11.209  -6.032  1.00 43.01 ? 402 HOH D O   1 
HETATM 7186 O  O   . HOH N 4 .   ? -7.171  -11.176 -42.575 1.00 49.57 ? 403 HOH D O   1 
HETATM 7187 O  O   . HOH N 4 .   ? 14.688  -1.279  0.217   1.00 52.24 ? 404 HOH D O   1 
HETATM 7188 O  O   . HOH N 4 .   ? -12.734 -0.753  -25.996 1.00 17.75 ? 405 HOH D O   1 
HETATM 7189 O  O   . HOH N 4 .   ? 12.256  -2.186  -31.718 1.00 43.32 ? 406 HOH D O   1 
HETATM 7190 O  O   . HOH N 4 .   ? 11.469  4.869   -31.304 1.00 38.02 ? 407 HOH D O   1 
HETATM 7191 O  O   . HOH N 4 .   ? -14.030 -11.577 -36.868 1.00 24.06 ? 408 HOH D O   1 
HETATM 7192 O  O   . HOH N 4 .   ? -5.415  -30.207 -17.311 1.00 47.79 ? 409 HOH D O   1 
HETATM 7193 O  O   . HOH N 4 .   ? 2.870   -17.599 -40.311 1.00 47.73 ? 410 HOH D O   1 
HETATM 7194 O  O   . HOH N 4 .   ? -7.637  -19.140 -39.496 1.00 24.43 ? 411 HOH D O   1 
HETATM 7195 O  O   . HOH N 4 .   ? -11.473 -22.741 -37.380 1.00 29.92 ? 412 HOH D O   1 
HETATM 7196 O  O   . HOH N 4 .   ? 7.979   -20.086 -38.543 1.00 42.63 ? 413 HOH D O   1 
HETATM 7197 O  O   . HOH N 4 .   ? -20.203 -20.435 -34.840 1.00 35.91 ? 414 HOH D O   1 
HETATM 7198 O  O   . HOH N 4 .   ? 9.197   3.679   -34.132 1.00 43.84 ? 415 HOH D O   1 
HETATM 7199 O  O   . HOH N 4 .   ? 10.827  -9.956  -14.443 1.00 26.56 ? 416 HOH D O   1 
HETATM 7200 O  O   . HOH N 4 .   ? -21.198 -13.660 -29.391 1.00 35.18 ? 417 HOH D O   1 
HETATM 7201 O  O   . HOH N 4 .   ? -9.623  -33.632 -23.582 1.00 32.38 ? 418 HOH D O   1 
HETATM 7202 O  O   . HOH N 4 .   ? 0.490   1.293   -40.347 1.00 42.64 ? 419 HOH D O   1 
HETATM 7203 O  O   . HOH N 4 .   ? 15.811  8.954   -12.703 1.00 47.24 ? 420 HOH D O   1 
HETATM 7204 O  O   . HOH N 4 .   ? -10.284 -22.598 -44.200 1.00 40.98 ? 421 HOH D O   1 
HETATM 7205 O  O   . HOH N 4 .   ? -10.355 2.870   -40.408 1.00 48.46 ? 422 HOH D O   1 
HETATM 7206 O  O   . HOH N 4 .   ? 12.967  1.106   -31.996 1.00 50.81 ? 423 HOH D O   1 
HETATM 7207 O  O   . HOH N 4 .   ? 22.976  7.777   -9.882  1.00 31.98 ? 424 HOH D O   1 
HETATM 7208 O  O   . HOH N 4 .   ? -12.981 1.234   -25.513 1.00 23.49 ? 425 HOH D O   1 
HETATM 7209 O  O   . HOH N 4 .   ? -18.844 -1.894  -33.702 1.00 33.54 ? 426 HOH D O   1 
HETATM 7210 O  O   . HOH N 4 .   ? 14.686  4.527   -14.339 1.00 21.96 ? 427 HOH D O   1 
HETATM 7211 O  O   . HOH N 4 .   ? 7.719   3.678   -35.758 1.00 38.63 ? 428 HOH D O   1 
HETATM 7212 O  O   . HOH N 4 .   ? 7.334   -13.590 -21.661 1.00 39.45 ? 429 HOH D O   1 
HETATM 7213 O  O   . HOH N 4 .   ? -19.463 -26.867 -26.235 1.00 49.10 ? 430 HOH D O   1 
HETATM 7214 O  O   . HOH N 4 .   ? 1.084   -3.550  -41.052 1.00 33.96 ? 431 HOH D O   1 
HETATM 7215 O  O   . HOH N 4 .   ? -0.196  -5.214  -18.835 1.00 34.75 ? 432 HOH D O   1 
HETATM 7216 O  O   . HOH N 4 .   ? 15.565  9.551   -10.487 1.00 20.16 ? 433 HOH D O   1 
HETATM 7217 O  O   . HOH N 4 .   ? 10.106  -17.523 -36.595 1.00 36.62 ? 434 HOH D O   1 
HETATM 7218 O  O   . HOH N 4 .   ? 9.994   -15.685 -28.771 1.00 32.96 ? 435 HOH D O   1 
HETATM 7219 O  O   . HOH N 4 .   ? 0.765   -12.305 -26.023 1.00 21.87 ? 436 HOH D O   1 
HETATM 7220 O  O   . HOH N 4 .   ? 3.804   -12.302 -7.794  1.00 44.21 ? 437 HOH D O   1 
HETATM 7221 O  O   . HOH N 4 .   ? -17.695 -13.224 -35.275 1.00 32.28 ? 438 HOH D O   1 
HETATM 7222 O  O   . HOH N 4 .   ? 5.209   -3.114  -8.718  1.00 34.89 ? 439 HOH D O   1 
HETATM 7223 O  O   . HOH N 4 .   ? 6.727   -8.842  -9.301  1.00 23.23 ? 440 HOH D O   1 
HETATM 7224 O  O   . HOH N 4 .   ? 18.636  -1.127  -1.427  1.00 25.08 ? 441 HOH D O   1 
HETATM 7225 O  O   . HOH N 4 .   ? 3.696   -13.995 -38.776 1.00 31.31 ? 442 HOH D O   1 
HETATM 7226 O  O   . HOH N 4 .   ? 7.776   7.968   -25.018 1.00 29.05 ? 443 HOH D O   1 
HETATM 7227 O  O   . HOH N 4 .   ? 18.510  9.329   -25.895 1.00 40.31 ? 444 HOH D O   1 
HETATM 7228 O  O   . HOH N 4 .   ? 0.332   -7.481  -17.533 1.00 43.79 ? 445 HOH D O   1 
HETATM 7229 O  O   . HOH N 4 .   ? 9.637   -14.679 -26.249 1.00 41.74 ? 446 HOH D O   1 
HETATM 7230 O  O   . HOH N 4 .   ? 21.679  14.255  -8.360  1.00 39.17 ? 447 HOH D O   1 
HETATM 7231 O  O   . HOH N 4 .   ? 5.967   1.442   -32.478 1.00 25.32 ? 448 HOH D O   1 
HETATM 7232 O  O   . HOH N 4 .   ? -12.660 9.121   -28.539 1.00 40.62 ? 449 HOH D O   1 
HETATM 7233 O  O   . HOH N 4 .   ? 4.231   -18.860 -32.477 1.00 42.77 ? 450 HOH D O   1 
HETATM 7234 O  O   . HOH N 4 .   ? -2.858  -1.563  -19.986 1.00 37.60 ? 451 HOH D O   1 
HETATM 7235 O  O   . HOH N 4 .   ? -7.082  -12.883 -29.165 1.00 25.50 ? 452 HOH D O   1 
HETATM 7236 O  O   . HOH N 4 .   ? 17.633  12.895  -1.529  1.00 43.04 ? 453 HOH D O   1 
HETATM 7237 O  O   . HOH N 4 .   ? 22.168  -5.875  -14.007 1.00 44.89 ? 454 HOH D O   1 
HETATM 7238 O  O   . HOH N 4 .   ? -2.362  -15.931 -14.165 1.00 29.82 ? 455 HOH D O   1 
HETATM 7239 O  O   . HOH N 4 .   ? -4.601  -26.443 -19.985 1.00 33.05 ? 456 HOH D O   1 
HETATM 7240 O  O   . HOH N 4 .   ? -1.966  1.980   -27.008 1.00 28.25 ? 457 HOH D O   1 
HETATM 7241 O  O   . HOH N 4 .   ? -1.847  -20.670 -29.759 1.00 27.91 ? 458 HOH D O   1 
HETATM 7242 O  O   . HOH N 4 .   ? 4.833   -0.962  -17.427 1.00 22.29 ? 459 HOH D O   1 
HETATM 7243 O  O   . HOH N 4 .   ? -1.011  -1.672  -22.227 1.00 26.21 ? 460 HOH D O   1 
HETATM 7244 O  O   . HOH N 4 .   ? -21.179 -9.431  -24.576 1.00 41.42 ? 461 HOH D O   1 
HETATM 7245 O  O   . HOH N 4 .   ? 17.871  9.822   -0.846  1.00 30.80 ? 462 HOH D O   1 
HETATM 7246 O  O   . HOH N 4 .   ? -14.117 -27.367 -21.586 1.00 30.49 ? 463 HOH D O   1 
HETATM 7247 O  O   . HOH N 4 .   ? -17.930 3.369   -34.435 1.00 33.74 ? 464 HOH D O   1 
HETATM 7248 O  O   . HOH N 4 .   ? 0.129   -10.469 -17.820 1.00 25.98 ? 465 HOH D O   1 
HETATM 7249 O  O   . HOH N 4 .   ? -9.594  -29.892 -27.960 1.00 29.38 ? 466 HOH D O   1 
HETATM 7250 O  O   . HOH N 4 .   ? -0.303  -5.397  -21.855 1.00 20.84 ? 467 HOH D O   1 
HETATM 7251 O  O   . HOH N 4 .   ? 0.763   -14.487 -24.376 1.00 32.59 ? 468 HOH D O   1 
HETATM 7252 O  O   . HOH N 4 .   ? 12.716  -10.200 -21.502 1.00 46.16 ? 469 HOH D O   1 
HETATM 7253 O  O   . HOH N 4 .   ? 18.797  1.607   -0.129  1.00 29.50 ? 470 HOH D O   1 
HETATM 7254 O  O   . HOH N 4 .   ? -25.969 -20.290 -29.173 1.00 36.56 ? 471 HOH D O   1 
HETATM 7255 O  O   . HOH N 4 .   ? 16.652  -8.134  -6.473  1.00 35.87 ? 472 HOH D O   1 
HETATM 7256 O  O   . HOH N 4 .   ? -22.575 -30.546 -30.646 1.00 56.09 ? 473 HOH D O   1 
HETATM 7257 O  O   . HOH N 4 .   ? -11.976 -4.564  -23.305 1.00 26.35 ? 474 HOH D O   1 
HETATM 7258 O  O   . HOH N 4 .   ? 11.102  -8.315  -21.504 1.00 26.93 ? 475 HOH D O   1 
HETATM 7259 O  O   . HOH N 4 .   ? 14.042  -11.525 -4.462  1.00 31.35 ? 476 HOH D O   1 
HETATM 7260 O  O   . HOH N 4 .   ? 13.867  -1.375  -26.693 1.00 29.61 ? 477 HOH D O   1 
HETATM 7261 O  O   . HOH N 4 .   ? -5.300  5.632   -36.686 1.00 31.38 ? 478 HOH D O   1 
HETATM 7262 O  O   . HOH N 4 .   ? 4.436   -15.649 -19.208 1.00 48.67 ? 479 HOH D O   1 
HETATM 7263 O  O   . HOH N 4 .   ? 17.085  -7.914  -1.873  1.00 34.39 ? 480 HOH D O   1 
HETATM 7264 O  O   . HOH N 4 .   ? 16.008  5.026   -11.258 1.00 25.98 ? 481 HOH D O   1 
HETATM 7265 O  O   . HOH N 4 .   ? 0.850   -2.068  -13.255 1.00 39.41 ? 482 HOH D O   1 
HETATM 7266 O  O   . HOH N 4 .   ? 9.083   -3.106  -3.023  1.00 27.49 ? 483 HOH D O   1 
HETATM 7267 O  O   . HOH N 4 .   ? 3.861   -12.274 -17.309 1.00 32.99 ? 484 HOH D O   1 
HETATM 7268 O  O   . HOH N 4 .   ? 2.758   -16.609 -27.223 1.00 31.52 ? 485 HOH D O   1 
HETATM 7269 O  O   . HOH N 4 .   ? 10.273  -18.285 -30.201 1.00 48.74 ? 486 HOH D O   1 
HETATM 7270 O  O   . HOH N 4 .   ? 4.725   -7.263  -2.455  1.00 30.54 ? 487 HOH D O   1 
HETATM 7271 O  O   . HOH N 4 .   ? -18.262 -22.156 -36.056 1.00 55.65 ? 488 HOH D O   1 
HETATM 7272 O  O   . HOH N 4 .   ? -15.862 -19.708 -42.040 1.00 37.29 ? 489 HOH D O   1 
HETATM 7273 O  O   . HOH N 4 .   ? 25.376  -0.546  -3.981  1.00 37.12 ? 490 HOH D O   1 
HETATM 7274 O  O   . HOH N 4 .   ? 19.913  -0.686  -13.871 1.00 37.33 ? 491 HOH D O   1 
HETATM 7275 O  O   . HOH N 4 .   ? 3.349   -1.119  -9.995  1.00 41.42 ? 492 HOH D O   1 
HETATM 7276 O  O   . HOH N 4 .   ? 11.545  -7.227  -31.085 1.00 39.60 ? 493 HOH D O   1 
HETATM 7277 O  O   . HOH N 4 .   ? -0.877  -15.025 -39.247 1.00 33.30 ? 494 HOH D O   1 
HETATM 7278 O  O   . HOH N 4 .   ? -10.653 -28.837 -17.865 1.00 35.57 ? 495 HOH D O   1 
HETATM 7279 O  O   . HOH N 4 .   ? 7.494   -9.536  -17.719 1.00 37.18 ? 496 HOH D O   1 
HETATM 7280 O  O   . HOH N 4 .   ? -22.070 -6.599  -31.784 1.00 44.58 ? 497 HOH D O   1 
HETATM 7281 O  O   . HOH N 4 .   ? 25.232  0.301   -1.685  1.00 45.28 ? 498 HOH D O   1 
HETATM 7282 O  O   . HOH N 4 .   ? 5.126   -4.728  -11.754 1.00 30.78 ? 499 HOH D O   1 
HETATM 7283 O  O   . HOH N 4 .   ? 1.281   -17.496 -29.727 1.00 31.35 ? 500 HOH D O   1 
HETATM 7284 O  O   . HOH N 4 .   ? 24.426  12.057  -1.726  1.00 38.77 ? 501 HOH D O   1 
HETATM 7285 O  O   . HOH N 4 .   ? -21.206 -3.473  -34.714 1.00 58.23 ? 502 HOH D O   1 
HETATM 7286 O  O   . HOH N 4 .   ? 10.497  -4.013  -1.353  1.00 41.24 ? 503 HOH D O   1 
HETATM 7287 O  O   . HOH N 4 .   ? 2.200   -14.153 -27.767 1.00 27.96 ? 504 HOH D O   1 
HETATM 7288 O  O   . HOH N 4 .   ? 10.541  -22.720 -32.707 1.00 56.99 ? 505 HOH D O   1 
HETATM 7289 O  O   . HOH N 4 .   ? 7.491   -6.121  -10.296 1.00 28.16 ? 506 HOH D O   1 
HETATM 7290 O  O   . HOH N 4 .   ? 7.669   0.632   -5.602  1.00 22.00 ? 507 HOH D O   1 
HETATM 7291 O  O   . HOH N 4 .   ? 4.586   -20.127 -40.387 1.00 45.51 ? 508 HOH D O   1 
HETATM 7292 O  O   . HOH N 4 .   ? -14.608 -25.623 -32.067 1.00 40.39 ? 509 HOH D O   1 
HETATM 7293 O  O   . HOH N 4 .   ? 10.711  2.711   -4.401  1.00 22.99 ? 510 HOH D O   1 
HETATM 7294 O  O   . HOH N 4 .   ? 7.710   -7.485  1.175   1.00 39.05 ? 511 HOH D O   1 
HETATM 7295 O  O   . HOH N 4 .   ? -12.455 -30.585 -21.637 1.00 47.40 ? 512 HOH D O   1 
HETATM 7296 O  O   . HOH N 4 .   ? -9.604  -4.602  -42.450 1.00 35.23 ? 513 HOH D O   1 
HETATM 7297 O  O   . HOH N 4 .   ? 16.913  -11.052 -29.784 1.00 40.74 ? 514 HOH D O   1 
HETATM 7298 O  O   . HOH N 4 .   ? 22.322  -3.747  -10.550 1.00 37.84 ? 515 HOH D O   1 
HETATM 7299 O  O   . HOH N 4 .   ? 17.261  11.077  -9.483  1.00 25.24 ? 516 HOH D O   1 
HETATM 7300 O  O   . HOH N 4 .   ? 10.705  -0.813  -35.577 1.00 31.36 ? 517 HOH D O   1 
HETATM 7301 O  O   . HOH N 4 .   ? -1.721  -8.681  -19.870 1.00 30.55 ? 518 HOH D O   1 
HETATM 7302 O  O   . HOH N 4 .   ? -5.102  -19.135 -13.288 1.00 31.27 ? 519 HOH D O   1 
HETATM 7303 O  O   . HOH N 4 .   ? -11.740 -19.375 -43.564 1.00 45.37 ? 520 HOH D O   1 
HETATM 7304 O  O   . HOH N 4 .   ? -0.672  -10.699 -42.309 1.00 42.58 ? 521 HOH D O   1 
HETATM 7305 O  O   . HOH N 4 .   ? -22.029 -28.532 -25.674 1.00 46.44 ? 522 HOH D O   1 
HETATM 7306 O  O   . HOH N 4 .   ? -11.534 -1.914  -22.950 1.00 27.46 ? 523 HOH D O   1 
HETATM 7307 O  O   . HOH N 4 .   ? 4.839   1.188   -7.101  1.00 30.08 ? 524 HOH D O   1 
HETATM 7308 O  O   . HOH N 4 .   ? -18.534 -11.535 -21.174 1.00 40.90 ? 525 HOH D O   1 
HETATM 7309 O  O   . HOH N 4 .   ? -15.617 -9.814  -22.804 1.00 31.28 ? 526 HOH D O   1 
HETATM 7310 O  O   . HOH N 4 .   ? 1.762   -16.829 -24.917 1.00 37.64 ? 527 HOH D O   1 
HETATM 7311 O  O   . HOH N 4 .   ? 11.640  -5.975  -34.115 1.00 33.29 ? 528 HOH D O   1 
HETATM 7312 O  O   . HOH N 4 .   ? -24.885 -26.511 -23.345 1.00 43.83 ? 529 HOH D O   1 
HETATM 7313 O  O   . HOH N 4 .   ? 17.755  -8.945  -4.041  1.00 41.20 ? 530 HOH D O   1 
HETATM 7314 O  O   . HOH N 4 .   ? -16.441 13.670  -33.547 1.00 37.79 ? 531 HOH D O   1 
HETATM 7315 O  O   . HOH N 4 .   ? 19.924  10.578  -8.806  1.00 32.97 ? 532 HOH D O   1 
HETATM 7316 O  O   . HOH N 4 .   ? -13.475 6.994   -35.614 1.00 44.69 ? 533 HOH D O   1 
HETATM 7317 O  O   . HOH N 4 .   ? -12.986 12.439  -27.300 1.00 48.78 ? 534 HOH D O   1 
HETATM 7318 O  O   . HOH N 4 .   ? 23.435  -9.347  -6.078  1.00 53.93 ? 535 HOH D O   1 
HETATM 7319 O  O   . HOH N 4 .   ? -25.838 -27.544 -27.581 1.00 46.19 ? 536 HOH D O   1 
HETATM 7320 O  O   . HOH N 4 .   ? 1.660   -4.823  -15.822 1.00 44.42 ? 537 HOH D O   1 
HETATM 7321 O  O   . HOH N 4 .   ? 12.310  -5.073  -31.896 1.00 43.25 ? 538 HOH D O   1 
HETATM 7322 O  O   . HOH N 4 .   ? 23.151  -7.810  -12.086 1.00 43.00 ? 539 HOH D O   1 
HETATM 7323 O  O   . HOH N 4 .   ? 0.858   -25.503 -18.298 1.00 52.10 ? 540 HOH D O   1 
HETATM 7324 O  O   . HOH N 4 .   ? 3.142   5.665   -37.413 1.00 35.93 ? 541 HOH D O   1 
HETATM 7325 O  O   . HOH N 4 .   ? -9.719  -25.059 -38.420 1.00 49.54 ? 542 HOH D O   1 
HETATM 7326 O  O   . HOH N 4 .   ? -15.729 13.519  -38.408 1.00 44.46 ? 543 HOH D O   1 
HETATM 7327 O  O   . HOH N 4 .   ? -19.165 -31.726 -24.238 1.00 55.87 ? 544 HOH D O   1 
HETATM 7328 O  O   . HOH N 4 .   ? 11.349  9.301   -30.913 1.00 40.65 ? 545 HOH D O   1 
HETATM 7329 O  O   . HOH N 4 .   ? 6.013   -13.907 -39.824 1.00 41.37 ? 546 HOH D O   1 
HETATM 7330 O  O   . HOH N 4 .   ? -18.128 3.794   -36.956 1.00 42.05 ? 547 HOH D O   1 
HETATM 7331 O  O   . HOH N 4 .   ? 6.659   10.645  -34.150 1.00 41.35 ? 548 HOH D O   1 
HETATM 7332 O  O   . HOH N 4 .   ? -16.655 -30.859 -30.824 1.00 43.05 ? 549 HOH D O   1 
HETATM 7333 O  O   . HOH N 4 .   ? -16.577 -15.193 -44.606 1.00 49.37 ? 550 HOH D O   1 
HETATM 7334 O  O   . HOH N 4 .   ? 21.538  -1.815  -0.601  1.00 33.91 ? 551 HOH D O   1 
HETATM 7335 O  O   . HOH N 4 .   ? -17.068 5.621   -30.941 1.00 47.27 ? 552 HOH D O   1 
HETATM 7336 O  O   . HOH N 4 .   ? 2.960   0.431   -16.657 1.00 29.93 ? 553 HOH D O   1 
HETATM 7337 O  O   . HOH N 4 .   ? -11.740 -34.515 -23.480 1.00 35.04 ? 554 HOH D O   1 
HETATM 7338 O  O   . HOH N 4 .   ? 8.840   -22.068 -30.987 1.00 41.81 ? 555 HOH D O   1 
HETATM 7339 O  O   . HOH N 4 .   ? -5.100  -3.890  -17.652 1.00 38.01 ? 556 HOH D O   1 
HETATM 7340 O  O   . HOH N 4 .   ? 9.354   -5.630  3.492   1.00 32.85 ? 557 HOH D O   1 
HETATM 7341 O  O   . HOH N 4 .   ? 0.795   -16.747 -42.108 1.00 48.92 ? 558 HOH D O   1 
HETATM 7342 O  O   . HOH N 4 .   ? -0.899  -2.800  -17.664 1.00 45.70 ? 559 HOH D O   1 
HETATM 7343 O  O   . HOH N 4 .   ? -13.713 -5.816  -21.285 1.00 32.19 ? 560 HOH D O   1 
HETATM 7344 O  O   . HOH N 4 .   ? -14.246 -16.706 -45.754 1.00 58.76 ? 561 HOH D O   1 
HETATM 7345 O  O   . HOH N 4 .   ? 7.554   -23.912 -42.020 1.00 46.26 ? 562 HOH D O   1 
HETATM 7346 O  O   . HOH N 4 .   ? -20.462 0.158   -33.929 1.00 40.42 ? 563 HOH D O   1 
HETATM 7347 O  O   . HOH N 4 .   ? -12.052 7.005   -39.619 1.00 46.88 ? 564 HOH D O   1 
HETATM 7348 O  O   . HOH N 4 .   ? 15.055  -10.120 -6.701  1.00 38.07 ? 565 HOH D O   1 
HETATM 7349 O  O   . HOH N 4 .   ? -22.526 -32.341 -27.929 1.00 46.81 ? 566 HOH D O   1 
HETATM 7350 O  O   . HOH N 4 .   ? -15.467 6.494   -36.953 1.00 38.29 ? 567 HOH D O   1 
HETATM 7351 O  O   . HOH N 4 .   ? -9.425  18.997  -34.743 1.00 40.79 ? 568 HOH D O   1 
HETATM 7352 O  O   . HOH N 4 .   ? -10.172 -27.927 -15.197 1.00 39.02 ? 569 HOH D O   1 
HETATM 7353 O  O   . HOH N 4 .   ? -19.205 -33.067 -33.070 1.00 41.96 ? 570 HOH D O   1 
HETATM 7354 O  O   . HOH N 4 .   ? 0.660   -20.079 -29.861 1.00 30.20 ? 571 HOH D O   1 
HETATM 7355 O  O   . HOH N 4 .   ? 6.315   -3.039  -2.524  1.00 33.96 ? 572 HOH D O   1 
HETATM 7356 O  O   . HOH N 4 .   ? 24.382  4.641   5.638   1.00 44.11 ? 573 HOH D O   1 
HETATM 7357 O  O   . HOH N 4 .   ? 5.340   -1.221  -6.584  1.00 40.97 ? 574 HOH D O   1 
HETATM 7358 O  O   . HOH N 4 .   ? -18.144 5.683   -32.996 1.00 54.17 ? 575 HOH D O   1 
HETATM 7359 O  O   . HOH N 4 .   ? -0.570  -12.028 -15.556 1.00 35.57 ? 576 HOH D O   1 
HETATM 7360 O  O   . HOH N 4 .   ? -19.234 -34.365 -31.207 1.00 44.93 ? 577 HOH D O   1 
HETATM 7361 O  O   . HOH N 4 .   ? -26.489 -28.499 -24.377 1.00 41.95 ? 578 HOH D O   1 
HETATM 7362 O  O   . HOH N 4 .   ? -16.934 10.538  -31.497 1.00 37.57 ? 579 HOH D O   1 
HETATM 7363 O  O   . HOH N 4 .   ? -16.557 -17.765 -45.259 1.00 41.70 ? 580 HOH D O   1 
HETATM 7364 O  O   . HOH N 4 .   ? 4.837   -1.907  -4.265  1.00 29.44 ? 581 HOH D O   1 
HETATM 7365 O  O   . HOH N 4 .   ? -7.050  18.548  -34.346 1.00 35.06 ? 582 HOH D O   1 
HETATM 7366 O  O   . HOH N 4 .   ? -25.413 -30.715 -25.730 1.00 46.05 ? 583 HOH D O   1 
HETATM 7367 O  O   . HOH N 4 .   ? 20.608  8.335   5.740   1.00 44.01 ? 584 HOH D O   1 
HETATM 7368 O  O   . HOH N 4 .   ? 3.023   -17.109 -44.485 1.00 48.23 ? 585 HOH D O   1 
HETATM 7369 O  O   . HOH N 4 .   ? 7.734   -20.770 -43.107 1.00 46.97 ? 586 HOH D O   1 
HETATM 7370 O  O   . HOH N 4 .   ? 26.290  14.644  -10.801 1.00 50.00 ? 587 HOH D O   1 
# 
